CNRS Nantes University UFIP UFIP
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***  PELD  ***

elNémo ID: 220403081755100004

Job options:

ID        	=	 220403081755100004
JOBID     	=	 PELD
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER PELD

HEADER    SIGNALING PROTEIN                       24-APR-12   4ETX              
TITLE     CRYSTAL STRUCTURE OF PELD 158-CT FROM PSEUDOMONAS AERUGINOSA PAO1     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PELD;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 155-454;                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 GENE: PA3061, PELD;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA(DE3);                         
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    C-DI-GMP, SIGNALING PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.LI,J.CHEN,S.K.NAIR                                                  
REVDAT   2   19-SEP-12 4ETX    1       JRNL                                     
REVDAT   1   25-JUL-12 4ETX    0                                                
JRNL        AUTH   Z.LI,J.H.CHEN,Y.HAO,S.K.NAIR                                 
JRNL        TITL   STRUCTURES OF THE PELD CYCLIC DIGUANYLATE EFFECTOR INVOLVED  
JRNL        TITL 2 IN PELLICLE FORMATION IN PSEUDOMONAS AERUGINOSA PAO1.        
JRNL        REF    J.BIOL.CHEM.                  V. 287 30191 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22810222                                                     
JRNL        DOI    10.1074/JBC.M112.378273                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 19298                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 965                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1309                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2370                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 86                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.35000                                             
REMARK   3    B22 (A**2) : -1.47000                                             
REMARK   3    B33 (A**2) : 2.29000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.67000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.254         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.015        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2401 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3245 ; 1.351 ; 1.997       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   299 ; 6.198 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   127 ;33.722 ;23.071       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   424 ;17.575 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ;18.013 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   369 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1847 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1487 ; 0.711 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2363 ; 1.292 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   914 ; 1.848 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   882 ; 3.060 ; 4.500       
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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   155        A   454                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2278   1.5679  15.0848              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1383 T22:   0.1471                                     
REMARK   3      T33:   0.0997 T12:  -0.0060                                     
REMARK   3      T13:   0.0607 T23:   0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0490 L22:   0.9291                                     
REMARK   3      L33:   2.4631 L12:   0.3477                                     
REMARK   3      L13:   2.3666 L23:   0.6564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0412 S12:  -0.1508 S13:  -0.0585                       
REMARK   3      S21:   0.0602 S22:  -0.0805 S23:   0.1604                       
REMARK   3      S31:   0.0115 S32:  -0.3187 S33:   0.0393                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 4ETX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072064.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19307                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 24.6900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.040                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS, PH 8, 200 MM MGCL2, 10%     
REMARK 280  (V/V) PEG 8000, HANGING DROP, TEMPERATURE 298K                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       21.22000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CB   THR A   391     O    HOH A   583              2.10            
REMARK 500   OE1  GLN A   401     O    HOH A   579              2.14            
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    LEU A 226     -115.61    -66.50                                   
REMARK 500    ASP A 227     -136.38   -144.12                                   
REMARK 500    ALA A 228      -25.58   -146.30                                   
REMARK 500    ASP A 229       51.73    176.56                                   
REMARK 500    HIS A 258      -15.62     72.18                                   
REMARK 500    SER A 259       54.69     34.06                                   
REMARK 500    GLN A 308       15.99    -50.93                                   
REMARK 500    SER A 309       31.56    -71.77                                   
REMARK 500    ARG A 311       -6.00     59.69                                   
REMARK 500    LEU A 314       -9.48   -140.55                                   
REMARK 500    LEU A 369      -24.15     80.97                                   
REMARK 500    PHE A 411     -169.54   -115.03                                   
REMARK 500    ASN A 444      -80.34    108.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ETZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EU0   RELATED DB: PDB                                   
DBREF  4ETX A  155   454  UNP    Q9HZE7   Q9HZE7_PSEAE   155    454             
SEQRES   1 A  300  GLY ASN ASP GLN SER LEU ARG SER SER LEU LEU GLY LEU          
SEQRES   2 A  300  ARG GLN LEU LEU ARG GLU LEU PRO GLY ASP GLU ALA PRO          
SEQRES   3 A  300  LEU ASP ALA LEU ALA GLU THR VAL LEU ALA LEU LEU ALA          
SEQRES   4 A  300  GLN TYR GLY SER LEU ARG ILE ALA GLY LEU TYR ARG VAL          
SEQRES   5 A  300  ARG TYR ASP ARG THR PRO GLU PRO GLN PRO LEU ALA THR          
SEQRES   6 A  300  LEU GLY GLU MET PRO ALA LEU ASP ALA ASP ASP LEU LEU          
SEQRES   7 A  300  VAL ARG THR CYS LEU GLU ARG GLY GLU LEU VAL SER VAL          
SEQRES   8 A  300  ARG GLN GLU LEU LEU GLU ARG GLY GLU GLN ARG ALA HIS          
SEQRES   9 A  300  SER ALA LEU GLN VAL CYS VAL PRO LEU VAL ASP THR ASP          
SEQRES  10 A  300  GLY ARG ILE LEU ALA LEU LEU ALA VAL GLU GLN MET PRO          
SEQRES  11 A  300  PHE PHE VAL PHE ASN GLU ARG THR PHE SER LEU LEU ALA          
SEQRES  12 A  300  ILE LEU ALA GLY HIS ILE ALA ASP LEU LEU GLN SER ASP          
SEQRES  13 A  300  ARG ARG ALA LEU GLN LEU ALA ASP ILE ASP ALA GLN ARG          
SEQRES  14 A  300  PHE SER GLN TYR LEU LYS ARG SER LEU LEU ASP ALA ARG          
SEQRES  15 A  300  ASP HIS GLY LEU PRO ALA CYS LEU TYR ALA PHE GLU LEU          
SEQRES  16 A  300  THR ASP ALA ARG TYR GLY GLU GLU VAL GLN ARG LEU LEU          
SEQRES  17 A  300  GLU GLY SER GLN ARG GLY LEU ASP VAL GLN LEU ARG LEU          
SEQRES  18 A  300  ARG ASN ASP GLU GLY ARG ARG VAL LEU LEU VAL LEU LEU          
SEQRES  19 A  300  PRO LEU THR SER ALA GLU GLY SER GLN GLY TYR LEU GLN          
SEQRES  20 A  300  ARG LEU ARG ILE LEU PHE ALA GLU ARG PHE GLY GLN ALA          
SEQRES  21 A  300  ARG GLU LEU GLU SER LEU GLY VAL ARG ILE ARG GLN TYR          
SEQRES  22 A  300  GLU LEU ASP ALA GLY ASN ASP ARG GLN ALA LEU GLY HIS          
SEQRES  23 A  300  PHE LEU PHE ASN GLU CYS GLY LEU ASN ASP GLN GLN VAL          
SEQRES  24 A  300  ALA                                                          
FORMUL   2  HOH   *86(H2 O)                                                     
HELIX    1   1 GLY A  155  GLU A  173  1                                  19    
HELIX    2   2 ALA A  179  LEU A  184  1                                   6    
HELIX    3   3 LEU A  184  GLY A  196  1                                  13    
HELIX    4   4 ASP A  230  GLY A  240  1                                  11    
HELIX    5   5 ARG A  246  GLY A  253  1                                   8    
HELIX    6   6 ARG A  256  ALA A  260  5                                   5    
HELIX    7   7 PRO A  284  PHE A  288  5                                   5    
HELIX    8   8 ASN A  289  GLN A  308  1                                  20    
HELIX    9   9 ASP A  318  GLY A  339  1                                  22    
HELIX   10  10 TYR A  354  SER A  365  1                                  12    
HELIX   11  11 SER A  392  PHE A  411  1                                  20    
HELIX   12  12 GLU A  416  LEU A  420  5                                   5    
HELIX   13  13 GLN A  436  PHE A  443  1                                   8    
SHEET    1   A 5 ALA A 218  LEU A 220  0                                        
SHEET    2   A 5 ILE A 200  ARG A 205 -1  N  ALA A 201   O  LEU A 220           
SHEET    3   A 5 ILE A 274  GLN A 282 -1  O  LEU A 277   N  TYR A 204           
SHEET    4   A 5 VAL A 263  VAL A 268 -1  N  VAL A 263   O  VAL A 280           
SHEET    5   A 5 VAL A 243  SER A 244 -1  N  VAL A 243   O  CYS A 264           
SHEET    1   B 4 VAL A 371  ARG A 376  0                                        
SHEET    2   B 4 ARG A 382  LEU A 388 -1  O  VAL A 383   N  LEU A 375           
SHEET    3   B 4 ALA A 342  LEU A 349 -1  N  TYR A 345   O  VAL A 386           
SHEET    4   B 4 VAL A 422  LEU A 429 -1  O  ARG A 425   N  ALA A 346           
CRYST1   60.290   42.440   60.470  90.00 112.78  90.00 P 1 21 1      2          
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      0.016586  0.000000  0.006967        0.00000                         
SCALE2      0.000000  0.023563  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017937        0.00000                         
ATOM      1  N   GLY A 155       8.161  -3.481   7.694  1.00 46.59           N  
ANISOU    1  N   GLY A 155     5566   6804   5331    338    258   -719       N  
ATOM      2  CA  GLY A 155       8.173  -3.881   6.242  1.00 47.62           C  
ANISOU    2  CA  GLY A 155     5560   7177   5358    402    240   -880       C  
ATOM      3  C   GLY A 155       6.825  -3.534   5.641  1.00 47.11           C  
ANISOU    3  C   GLY A 155     5546   7080   5275    346    271   -774       C  
ATOM      4  O   GLY A 155       6.633  -2.451   5.083  1.00 46.82           O  
ANISOU    4  O   GLY A 155     5497   7181   5112    245    358   -642       O  
ATOM      5  N   ASN A 156       5.875  -4.451   5.774  1.00 46.83           N  
ANISOU    5  N   ASN A 156     5570   6850   5374    404    181   -822       N  
ATOM      6  CA  ASN A 156       4.476  -4.124   5.517  1.00 46.18           C  
ANISOU    6  CA  ASN A 156     5553   6683   5310    345    207   -703       C  
ATOM      7  C   ASN A 156       3.964  -3.166   6.580  1.00 43.68           C  
ANISOU    7  C   ASN A 156     5354   6210   5034    239    282   -486       C  
ATOM      8  O   ASN A 156       3.175  -2.272   6.288  1.00 43.50           O  
ANISOU    8  O   ASN A 156     5360   6205   4965    173    339   -365       O  
ATOM      9  CB  ASN A 156       3.618  -5.391   5.492  1.00 47.15           C  
ANISOU    9  CB  ASN A 156     5704   6633   5577    415     79   -801       C  
ATOM     10  CG  ASN A 156       3.775  -6.167   4.211  1.00 50.36           C  
ANISOU   10  CG  ASN A 156     5995   7204   5937    528     -4  -1022       C  
ATOM     11  OD1 ASN A 156       4.192  -7.330   4.218  1.00 54.04           O  
ANISOU   11  OD1 ASN A 156     6428   7606   6498    644   -148  -1212       O  
ATOM     12  ND2 ASN A 156       3.437  -5.532   3.091  1.00 53.05           N  
ANISOU   12  ND2 ASN A 156     6271   7756   6130    501     67  -1007       N  
ATOM     13  N   ASP A 157       4.440  -3.360   7.806  1.00 42.00           N  
ANISOU   13  N   ASP A 157     5201   5852   4904    235    267   -456       N  
ATOM     14  CA  ASP A 157       4.047  -2.534   8.941  1.00 40.31           C  
ANISOU   14  CA  ASP A 157     5086   5507   4722    154    328   -285       C  
ATOM     15  C   ASP A 157       4.367  -1.043   8.707  1.00 38.34           C  
ANISOU   15  C   ASP A 157     4832   5374   4362     83    416   -173       C  
ATOM     16  O   ASP A 157       3.547  -0.215   9.006  1.00 37.02           O  
ANISOU   16  O   ASP A 157     4723   5140   4203     34    449    -58       O  
ATOM     17  CB  ASP A 157       4.674  -3.044  10.257  1.00 39.96           C  
ANISOU   17  CB  ASP A 157     5099   5320   4764    162    287   -283       C  
ATOM     18  CG  ASP A 157       4.037  -4.353  10.776  1.00 42.02           C  
ANISOU   18  CG  ASP A 157     5408   5401   5156    179    175   -313       C  
ATOM     19  OD1 ASP A 157       2.801  -4.556  10.725  1.00 42.66           O  
ANISOU   19  OD1 ASP A 157     5514   5418   5277    140    168   -260       O  
ATOM     20  OD2 ASP A 157       4.800  -5.185  11.298  1.00 46.06           O  
ANISOU   20  OD2 ASP A 157     5935   5829   5737    221     77   -382       O  
ATOM     21  N   GLN A 158       5.533  -0.703   8.150  1.00 38.46           N  
ANISOU   21  N   GLN A 158     4770   5570   4273     74    436   -209       N  
ATOM     22  CA  GLN A 158       5.854   0.723   7.932  1.00 37.73           C  
ANISOU   22  CA  GLN A 158     4683   5571   4083    -26    489    -71       C  
ATOM     23  C   GLN A 158       5.017   1.410   6.853  1.00 37.19           C  
ANISOU   23  C   GLN A 158     4607   5586   3937    -79    493      5       C  
ATOM     24  O   GLN A 158       4.748   2.607   6.969  1.00 36.39           O  
ANISOU   24  O   GLN A 158     4565   5440   3820   -158    494    151       O  
ATOM     25  CB  GLN A 158       7.351   0.976   7.696  1.00 39.35           C  
ANISOU   25  CB  GLN A 158     4797   5968   4185    -59    509   -100       C  
ATOM     26  CG  GLN A 158       7.942   0.338   6.478  1.00 42.76           C  
ANISOU   26  CG  GLN A 158     5080   6668   4500    -20    505   -248       C  
ATOM     27  CD  GLN A 158       9.461   0.441   6.449  1.00 47.34           C  
ANISOU   27  CD  GLN A 158     5546   7455   4986    -41    526   -308       C  
ATOM     28  OE1 GLN A 158      10.121   0.464   7.496  1.00 50.48           O  
ANISOU   28  OE1 GLN A 158     5982   7740   5459    -31    520   -301       O  
ATOM     29  NE2 GLN A 158      10.024   0.485   5.250  1.00 47.76           N  
ANISOU   29  NE2 GLN A 158     5446   7836   4865    -73    550   -373       N  
ATOM     30  N   SER A 159       4.625   0.667   5.816  1.00 36.04           N  
ANISOU   30  N   SER A 159     4392   5551   3750    -30    473    -98       N  
ATOM     31  CA  SER A 159       3.713   1.196   4.803  1.00 36.50           C  
ANISOU   31  CA  SER A 159     4450   5675   3743    -72    464    -33       C  
ATOM     32  C   SER A 159       2.418   1.638   5.473  1.00 33.70           C  
ANISOU   32  C   SER A 159     4203   5095   3506    -73    449     59       C  
ATOM     33  O   SER A 159       1.998   2.774   5.305  1.00 33.32           O  
ANISOU   33  O   SER A 159     4204   5023   3434   -137    433    186       O  
ATOM     34  CB  SER A 159       3.407   0.165   3.710  1.00 36.93           C  
ANISOU   34  CB  SER A 159     4415   5863   3753      4    435   -188       C  
ATOM     35  OG  SER A 159       4.447   0.134   2.749  1.00 42.31           O  
ANISOU   35  OG  SER A 159     4970   6843   4264    -15    452   -259       O  
ATOM     36  N   LEU A 160       1.835   0.737   6.265  1.00 32.83           N  
ANISOU   36  N   LEU A 160     4124   4828   3522     -5    440    -10       N  
ATOM     37  CA  LEU A 160       0.566   0.975   6.965  1.00 31.55           C  
ANISOU   37  CA  LEU A 160     4028   4500   3458     -3    436     47       C  
ATOM     38  C   LEU A 160       0.680   2.170   7.898  1.00 29.93           C  
ANISOU   38  C   LEU A 160     3891   4211   3270    -43    453    155       C  
ATOM     39  O   LEU A 160      -0.196   3.043   7.897  1.00 28.20           O  
ANISOU   39  O   LEU A 160     3706   3938   3069    -51    431    216       O  
ATOM     40  CB  LEU A 160       0.149  -0.243   7.809  1.00 31.96           C  
ANISOU   40  CB  LEU A 160     4092   4429   3624     37    421    -21       C  
ATOM     41  CG  LEU A 160      -0.661  -1.425   7.261  1.00 34.98           C  
ANISOU   41  CG  LEU A 160     4439   4790   4061     75    367   -110       C  
ATOM     42  CD1 LEU A 160       0.096  -2.176   6.203  1.00 38.43           C  
ANISOU   42  CD1 LEU A 160     4806   5348   4448    130    322   -239       C  
ATOM     43  CD2 LEU A 160      -0.995  -2.376   8.430  1.00 35.95           C  
ANISOU   43  CD2 LEU A 160     4598   4763   4299     63    336   -110       C  
ATOM     44  N   ARG A 161       1.746   2.169   8.713  1.00 28.42           N  
ANISOU   44  N   ARG A 161     3715   4000   3082    -53    474    160       N  
ATOM     45  CA  ARG A 161       2.024   3.261   9.642  1.00 27.57           C  
ANISOU   45  CA  ARG A 161     3670   3814   2993    -83    477    244       C  
ATOM     46  C   ARG A 161       2.146   4.586   8.885  1.00 27.26           C  
ANISOU   46  C   ARG A 161     3646   3820   2890   -147    432    346       C  
ATOM     47  O   ARG A 161       1.575   5.573   9.304  1.00 27.93           O  
ANISOU   47  O   ARG A 161     3788   3803   3021   -147    387    403       O  
ATOM     48  CB  ARG A 161       3.316   3.010  10.450  1.00 26.73           C  
ANISOU   48  CB  ARG A 161     3566   3702   2886    -89    497    228       C  
ATOM     49  CG  ARG A 161       3.251   1.891  11.475  1.00 27.33           C  
ANISOU   49  CG  ARG A 161     3658   3689   3036    -45    507    165       C  
ATOM     50  CD  ARG A 161       4.333   2.022  12.615  1.00 29.92           C  
ANISOU   50  CD  ARG A 161     4021   3969   3378    -51    513    177       C  
ATOM     51  NE  ARG A 161       5.702   2.191  12.113  1.00 30.69           N  
ANISOU   51  NE  ARG A 161     4071   4175   3416    -70    511    160       N  
ATOM     52  CZ  ARG A 161       6.517   1.209  11.729  1.00 33.49           C  
ANISOU   52  CZ  ARG A 161     4360   4608   3757    -34    495     58       C  
ATOM     53  NH1 ARG A 161       6.150  -0.063  11.783  1.00 33.74           N  
ANISOU   53  NH1 ARG A 161     4387   4583   3852     26    455    -31       N  
ATOM     54  NH2 ARG A 161       7.727   1.506  11.266  1.00 37.49           N  
ANISOU   54  NH2 ARG A 161     4797   5260   4189    -58    502     37       N  
ATOM     55  N   SER A 162       2.917   4.592   7.796  1.00 27.54           N  
ANISOU   55  N   SER A 162     3625   4020   2819   -204    430    365       N  
ATOM     56  CA  SER A 162       3.088   5.773   6.923  1.00 28.11           C  
ANISOU   56  CA  SER A 162     3709   4164   2808   -306    370    495       C  
ATOM     57  C   SER A 162       1.766   6.302   6.343  1.00 27.04           C  
ANISOU   57  C   SER A 162     3614   3962   2698   -296    300    539       C  
ATOM     58  O   SER A 162       1.512   7.508   6.352  1.00 27.19           O  
ANISOU   58  O   SER A 162     3701   3889   2741   -343    205    649       O  
ATOM     59  CB  SER A 162       4.096   5.485   5.795  1.00 29.15           C  
ANISOU   59  CB  SER A 162     3739   4554   2782   -381    396    495       C  
ATOM     60  OG  SER A 162       5.363   5.186   6.375  1.00 33.66           O  
ANISOU   60  OG  SER A 162     4266   5187   3336   -389    442    453       O  
ATOM     61  N   SER A 163       0.931   5.402   5.839  1.00 26.57           N  
ANISOU   61  N   SER A 163     3513   3937   2645   -230    326    447       N  
ATOM     62  CA  SER A 163      -0.403   5.777   5.361  1.00 27.15           C  
ANISOU   62  CA  SER A 163     3613   3945   2756   -202    262    463       C  
ATOM     63  C   SER A 163      -1.229   6.455   6.474  1.00 26.10           C  
ANISOU   63  C   SER A 163     3546   3619   2752   -143    222    463       C  
ATOM     64  O   SER A 163      -1.854   7.505   6.272  1.00 25.75           O  
ANISOU   64  O   SER A 163     3552   3493   2741   -145    115    524       O  
ATOM     65  CB  SER A 163      -1.151   4.540   4.855  1.00 26.55           C  
ANISOU   65  CB  SER A 163     3475   3922   2689   -133    301    344       C  
ATOM     66  OG  SER A 163      -0.534   4.020   3.695  1.00 30.54           O  
ANISOU   66  OG  SER A 163     3910   4626   3067   -165    314    315       O  
ATOM     67  N   LEU A 164      -1.232   5.829   7.642  1.00 24.97           N  
ANISOU   67  N   LEU A 164     3396   3416   2676    -87    293    386       N  
ATOM     68  CA  LEU A 164      -1.990   6.335   8.784  1.00 25.00           C  
ANISOU   68  CA  LEU A 164     3430   3296   2773    -23    274    354       C  
ATOM     69  C   LEU A 164      -1.447   7.665   9.302  1.00 25.78           C  
ANISOU   69  C   LEU A 164     3598   3304   2895    -41    192    422       C  
ATOM     70  O   LEU A 164      -2.218   8.546   9.685  1.00 26.11           O  
ANISOU   70  O   LEU A 164     3668   3248   3004     17    105    401       O  
ATOM     71  CB  LEU A 164      -2.049   5.292   9.904  1.00 24.32           C  
ANISOU   71  CB  LEU A 164     3315   3202   2722     11    368    277       C  
ATOM     72  CG  LEU A 164      -2.938   4.070   9.605  1.00 25.20           C  
ANISOU   72  CG  LEU A 164     3367   3355   2852     29    408    211       C  
ATOM     73  CD1 LEU A 164      -2.773   3.035  10.704  1.00 24.40           C  
ANISOU   73  CD1 LEU A 164     3254   3238   2780     22    470    177       C  
ATOM     74  CD2 LEU A 164      -4.431   4.496   9.466  1.00 25.61           C  
ANISOU   74  CD2 LEU A 164     3390   3392   2947     77    369    177       C  
ATOM     75  N   LEU A 165      -0.123   7.818   9.282  1.00 25.89           N  
ANISOU   75  N   LEU A 165     3630   3352   2856   -118    202    491       N  
ATOM     76  CA  LEU A 165       0.482   9.082   9.675  1.00 26.06           C  
ANISOU   76  CA  LEU A 165     3719   3279   2903   -158    101    573       C  
ATOM     77  C   LEU A 165       0.116  10.217   8.716  1.00 27.57           C  
ANISOU   77  C   LEU A 165     3960   3419   3095   -212    -58    680       C  
ATOM     78  O   LEU A 165      -0.171  11.326   9.172  1.00 27.54           O  
ANISOU   78  O   LEU A 165     4024   3263   3178   -181   -198    697       O  
ATOM     79  CB  LEU A 165       1.995   8.938   9.828  1.00 26.37           C  
ANISOU   79  CB  LEU A 165     3750   3388   2882   -244    149    627       C  
ATOM     80  CG  LEU A 165       2.386   8.182  11.109  1.00 24.78           C  
ANISOU   80  CG  LEU A 165     3536   3165   2714   -181    247    534       C  
ATOM     81  CD1 LEU A 165       3.847   7.706  11.040  1.00 26.26           C  
ANISOU   81  CD1 LEU A 165     3686   3456   2834   -250    305    555       C  
ATOM     82  CD2 LEU A 165       2.118   9.024  12.351  1.00 29.08           C  
ANISOU   82  CD2 LEU A 165     4139   3567   3344   -119    188    506       C  
ATOM     83  N   GLY A 166       0.133   9.923   7.407  1.00 27.65           N  
ANISOU   83  N   GLY A 166     3938   3557   3009   -289    -55    744       N  
ATOM     84  CA  GLY A 166      -0.362  10.831   6.364  1.00 29.17           C  
ANISOU   84  CA  GLY A 166     4177   3719   3187   -351   -212    857       C  
ATOM     85  C   GLY A 166      -1.798  11.301   6.582  1.00 30.28           C  
ANISOU   85  C   GLY A 166     4351   3706   3448   -225   -318    779       C  
ATOM     86  O   GLY A 166      -2.090  12.516   6.511  1.00 31.03           O  
ANISOU   86  O   GLY A 166     4526   3648   3615   -231   -517    847       O  
ATOM     87  N   LEU A 167      -2.697  10.342   6.826  1.00 28.63           N  
ANISOU   87  N   LEU A 167     4074   3538   3264   -114   -206    635       N  
ATOM     88  CA  LEU A 167      -4.083  10.644   7.189  1.00 29.16           C  
ANISOU   88  CA  LEU A 167     4134   3507   3438     18   -276    523       C  
ATOM     89  C   LEU A 167      -4.220  11.503   8.454  1.00 29.88           C  
ANISOU   89  C   LEU A 167     4259   3457   3637    111   -356    449       C  
ATOM     90  O   LEU A 167      -5.001  12.474   8.456  1.00 29.54           O  
ANISOU   90  O   LEU A 167     4249   3290   3685    192   -532    410       O  
ATOM     91  CB  LEU A 167      -4.922   9.361   7.334  1.00 28.31           C  
ANISOU   91  CB  LEU A 167     3931   3499   3328     89   -128    394       C  
ATOM     92  CG  LEU A 167      -6.435   9.556   7.500  1.00 29.61           C  
ANISOU   92  CG  LEU A 167     4051   3623   3577    209   -186    276       C  
ATOM     93  CD1 LEU A 167      -7.023  10.284   6.258  1.00 32.83           C  
ANISOU   93  CD1 LEU A 167     4499   3982   3993    202   -356    337       C  
ATOM     94  CD2 LEU A 167      -7.114   8.213   7.724  1.00 29.33           C  
ANISOU   94  CD2 LEU A 167     3916   3698   3531    237    -35    177       C  
ATOM     95  N   ARG A 168      -3.486  11.146   9.517  1.00 28.38           N  
ANISOU   95  N   ARG A 168     4057   3287   3439    114   -245    414       N  
ATOM     96  CA  ARG A 168      -3.525  11.923  10.762  1.00 29.70           C  
ANISOU   96  CA  ARG A 168     4248   3347   3689    206   -315    328       C  
ATOM     97  C   ARG A 168      -3.087  13.366  10.530  1.00 31.70           C  
ANISOU   97  C   ARG A 168     4606   3430   4008    175   -547    421       C  
ATOM     98  O   ARG A 168      -3.650  14.294  11.124  1.00 32.18           O  
ANISOU   98  O   ARG A 168     4691   3360   4175    293   -705    321       O  
ATOM     99  CB  ARG A 168      -2.672  11.266  11.869  1.00 29.09           C  
ANISOU   99  CB  ARG A 168     4150   3329   3574    192   -163    299       C  
ATOM    100  CG  ARG A 168      -2.882  11.825  13.278  1.00 29.94           C  
ANISOU  100  CG  ARG A 168     4252   3381   3741    306   -198    171       C  
ATOM    101  CD  ARG A 168      -2.076  11.021  14.335  1.00 30.70           C  
ANISOU  101  CD  ARG A 168     4328   3554   3782    279    -40    156       C  
ATOM    102  NE  ARG A 168      -0.635  11.273  14.232  1.00 29.82           N  
ANISOU  102  NE  ARG A 168     4286   3392   3653    177    -61    276       N  
ATOM    103  CZ  ARG A 168       0.274  10.859  15.106  1.00 28.97           C  
ANISOU  103  CZ  ARG A 168     4182   3311   3514    153     25    275       C  
ATOM    104  NH1 ARG A 168      -0.088  10.155  16.169  1.00 28.32           N  
ANISOU  104  NH1 ARG A 168     4050   3302   3407    211    133    178       N  
ATOM    105  NH2 ARG A 168       1.550  11.174  14.929  1.00 27.97           N  
ANISOU  105  NH2 ARG A 168     4104   3148   3376     60     -8    379       N  
ATOM    106  N   GLN A 169      -2.100  13.551   9.651  1.00 32.03           N  
ANISOU  106  N   GLN A 169     4701   3483   3985     11   -584    607       N  
ATOM    107  CA  GLN A 169      -1.608  14.886   9.318  1.00 34.91           C  
ANISOU  107  CA  GLN A 169     5173   3687   4404    -72   -825    747       C  
ATOM    108  C   GLN A 169      -2.690  15.765   8.670  1.00 36.44           C  
ANISOU  108  C   GLN A 169     5418   3739   4688    -15  -1062    747       C  
ATOM    109  O   GLN A 169      -2.866  16.931   9.045  1.00 37.34           O  
ANISOU  109  O   GLN A 169     5612   3645   4932     45  -1306    729       O  
ATOM    110  CB  GLN A 169      -0.375  14.778   8.417  1.00 35.05           C  
ANISOU  110  CB  GLN A 169     5206   3815   4296   -291   -793    959       C  
ATOM    111  CG  GLN A 169       0.135  16.114   7.892  1.00 40.10           C  
ANISOU  111  CG  GLN A 169     5955   4312   4970   -437  -1056   1159       C  
ATOM    112  CD  GLN A 169       1.634  16.131   7.724  1.00 43.58           C  
ANISOU  112  CD  GLN A 169     6390   4862   5305   -639  -1005   1327       C  
ATOM    113  OE1 GLN A 169       2.146  16.374   6.633  1.00 46.51           O  
ANISOU  113  OE1 GLN A 169     6769   5337   5564   -838  -1063   1528       O  
ATOM    114  NE2 GLN A 169       2.354  15.866   8.812  1.00 45.53           N  
ANISOU  114  NE2 GLN A 169     6613   5110   5574   -595   -897   1244       N  
ATOM    115  N   LEU A 170      -3.397  15.193   7.696  1.00 36.65           N  
ANISOU  115  N   LEU A 170     5403   3870   4654    -24  -1009    758       N  
ATOM    116  CA  LEU A 170      -4.483  15.867   6.997  1.00 39.11           C  
ANISOU  116  CA  LEU A 170     5753   4067   5041     35  -1222    752       C  
ATOM    117  C   LEU A 170      -5.607  16.237   7.967  1.00 39.56           C  
ANISOU  117  C   LEU A 170     5772   4015   5243    269  -1303    509       C  
ATOM    118  O   LEU A 170      -6.150  17.350   7.931  1.00 40.97           O  
ANISOU  118  O   LEU A 170     6017   3995   5553    353  -1583    474       O  
ATOM    119  CB  LEU A 170      -5.009  14.966   5.874  1.00 38.51           C  
ANISOU  119  CB  LEU A 170     5615   4161   4857     -7  -1104    780       C  
ATOM    120  CG  LEU A 170      -4.427  15.031   4.450  1.00 41.39           C  
ANISOU  120  CG  LEU A 170     6022   4617   5086   -213  -1154   1012       C  
ATOM    121  CD1 LEU A 170      -3.245  15.985   4.255  1.00 44.28           C  
ANISOU  121  CD1 LEU A 170     6486   4914   5423   -403  -1307   1236       C  
ATOM    122  CD2 LEU A 170      -4.099  13.637   3.933  1.00 40.91           C  
ANISOU  122  CD2 LEU A 170     5857   4819   4867   -268   -888    997       C  
ATOM    123  N   LEU A 171      -5.921  15.295   8.847  1.00 38.54           N  
ANISOU  123  N   LEU A 171     5530   4029   5086    370  -1071    339       N  
ATOM    124  CA  LEU A 171      -6.912  15.478   9.892  1.00 40.11           C  
ANISOU  124  CA  LEU A 171     5650   4215   5375    577  -1091     93       C  
ATOM    125  C   LEU A 171      -6.530  16.651  10.789  1.00 41.72           C  
ANISOU  125  C   LEU A 171     5922   4241   5691    659  -1290     28       C  
ATOM    126  O   LEU A 171      -7.353  17.526  11.064  1.00 42.60           O  
ANISOU  126  O   LEU A 171     6029   4230   5926    826  -1507   -130       O  
ATOM    127  CB  LEU A 171      -6.982  14.206  10.722  1.00 38.79           C  
ANISOU  127  CB  LEU A 171     5362   4256   5120    598   -795    -10       C  
ATOM    128  CG  LEU A 171      -8.307  13.537  11.103  1.00 41.45           C  
ANISOU  128  CG  LEU A 171     5552   4743   5452    721   -684   -200       C  
ATOM    129  CD1 LEU A 171      -9.520  14.031  10.308  1.00 41.11           C  
ANISOU  129  CD1 LEU A 171     5484   4650   5484    816   -853   -273       C  
ATOM    130  CD2 LEU A 171      -8.137  12.017  10.981  1.00 39.55           C  
ANISOU  130  CD2 LEU A 171     5245   4682   5099    612   -423   -142       C  
ATOM    131  N   ARG A 172      -5.277  16.658  11.234  1.00 41.50           N  
ANISOU  131  N   ARG A 172     5949   4197   5623    551  -1231    135       N  
ATOM    132  CA  ARG A 172      -4.780  17.697  12.133  1.00 44.00           C  
ANISOU  132  CA  ARG A 172     6331   4345   6042    616  -1413     79       C  
ATOM    133  C   ARG A 172      -4.826  19.084  11.466  1.00 46.43           C  
ANISOU  133  C   ARG A 172     6771   4382   6488    602  -1788    170       C  
ATOM    134  O   ARG A 172      -5.068  20.078  12.136  1.00 48.96           O  
ANISOU  134  O   ARG A 172     7127   4526   6949    749  -2027     27       O  
ATOM    135  CB  ARG A 172      -3.376  17.338  12.642  1.00 42.35           C  
ANISOU  135  CB  ARG A 172     6151   4184   5757    482  -1266    195       C  
ATOM    136  CG  ARG A 172      -3.371  16.325  13.803  1.00 42.72           C  
ANISOU  136  CG  ARG A 172     6087   4421   5722    555   -995     47       C  
ATOM    137  CD  ARG A 172      -1.971  15.733  14.064  1.00 42.71           C  
ANISOU  137  CD  ARG A 172     6111   4487   5631    404   -832    182       C  
ATOM    138  NE  ARG A 172      -1.978  14.771  15.169  1.00 44.53           N  
ANISOU  138  NE  ARG A 172     6252   4878   5789    463   -607     60       N  
ATOM    139  CZ  ARG A 172      -0.899  14.366  15.840  1.00 44.27           C  
ANISOU  139  CZ  ARG A 172     6231   4885   5704    397   -495    104       C  
ATOM    140  NH1 ARG A 172       0.307  14.824  15.535  1.00 45.19           N  
ANISOU  140  NH1 ARG A 172     6429   4911   5830    273   -570    255       N  
ATOM    141  NH2 ARG A 172      -1.028  13.495  16.827  1.00 44.53           N  
ANISOU  141  NH2 ARG A 172     6191   5058   5670    444   -317      4       N  
ATOM    142  N   GLU A 173      -4.644  19.137  10.147  1.00 47.00           N  
ANISOU  142  N   GLU A 173     6913   4428   6517    429  -1859    399       N  
ATOM    143  CA  GLU A 173      -4.664  20.407   9.393  1.00 50.17           C  
ANISOU  143  CA  GLU A 173     7455   4570   7035    367  -2237    542       C  
ATOM    144  C   GLU A 173      -6.061  20.897   8.973  1.00 51.47           C  
ANISOU  144  C   GLU A 173     7617   4622   7318    538  -2460    403       C  
ATOM    145  O   GLU A 173      -6.195  21.980   8.406  1.00 53.76           O  
ANISOU  145  O   GLU A 173     8032   4666   7730    511  -2818    502       O  
ATOM    146  CB  GLU A 173      -3.762  20.323   8.152  1.00 50.36           C  
ANISOU  146  CB  GLU A 173     7554   4645   6934     71  -2233    878       C  
ATOM    147  CG  GLU A 173      -2.272  20.272   8.455  1.00 51.06           C  
ANISOU  147  CG  GLU A 173     7670   4785   6944   -116  -2136   1041       C  
ATOM    148  CD  GLU A 173      -1.438  19.766   7.284  1.00 52.42           C  
ANISOU  148  CD  GLU A 173     7837   5154   6926   -389  -2009   1312       C  
ATOM    149  OE1 GLU A 173      -1.972  19.666   6.155  1.00 51.54           O  
ANISOU  149  OE1 GLU A 173     7733   5100   6751   -455  -2054   1409       O  
ATOM    150  OE2 GLU A 173      -0.241  19.464   7.503  1.00 51.51           O  
ANISOU  150  OE2 GLU A 173     7699   5156   6715   -530  -1866   1412       O  
ATOM    151  N   LEU A 174      -7.087  20.097   9.249  1.00 50.65           N  
ANISOU  151  N   LEU A 174     7368   4697   7180    704  -2263    183       N  
ATOM    152  CA  LEU A 174      -8.457  20.381   8.822  1.00 52.44           C  
ANISOU  152  CA  LEU A 174     7556   4871   7498    870  -2428     31       C  
ATOM    153  C   LEU A 174      -9.022  21.616   9.547  1.00 55.22           C  
ANISOU  153  C   LEU A 174     7934   4989   8059   1105  -2773   -198       C  
ATOM    154  O   LEU A 174      -8.843  21.743  10.756  1.00 55.42           O  
ANISOU  154  O   LEU A 174     7903   5038   8117   1234  -2729   -387       O  
ATOM    155  CB  LEU A 174      -9.328  19.157   9.094  1.00 50.45           C  
ANISOU  155  CB  LEU A 174     7120   4900   7149    972  -2109   -152       C  
ATOM    156  CG  LEU A 174     -10.281  18.621   8.025  1.00 50.92           C  
ANISOU  156  CG  LEU A 174     7128   5052   7168    966  -2073   -135       C  
ATOM    157  CD1 LEU A 174      -9.699  18.697   6.601  1.00 49.10           C  
ANISOU  157  CD1 LEU A 174     7028   4762   6867    734  -2155    178       C  
ATOM    158  CD2 LEU A 174     -10.657  17.181   8.394  1.00 47.88           C  
ANISOU  158  CD2 LEU A 174     6575   4962   6654    976  -1698   -238       C  
ATOM    159  N   PRO A 175      -9.707  22.518   8.813  1.00 58.07           N  
ANISOU  159  N   PRO A 175     8377   5126   8561   1169  -3134   -195       N  
ATOM    160  CA  PRO A 175     -10.173  23.789   9.376  1.00 61.36           C  
ANISOU  160  CA  PRO A 175     8840   5272   9203   1395  -3537   -410       C  
ATOM    161  C   PRO A 175     -10.714  23.696  10.810  1.00 62.15           C  
ANISOU  161  C   PRO A 175     8766   5511   9337   1680  -3433   -807       C  
ATOM    162  O   PRO A 175     -10.095  24.252  11.724  1.00 63.08           O  
ANISOU  162  O   PRO A 175     8920   5526   9521   1738  -3530   -887       O  
ATOM    163  CB  PRO A 175     -11.255  24.226   8.394  1.00 63.03           C  
ANISOU  163  CB  PRO A 175     9080   5353   9517   1477  -3812   -434       C  
ATOM    164  CG  PRO A 175     -10.759  23.714   7.087  1.00 61.68           C  
ANISOU  164  CG  PRO A 175     8998   5241   9196   1174  -3701    -63       C  
ATOM    165  CD  PRO A 175     -10.070  22.401   7.385  1.00 58.19           C  
ANISOU  165  CD  PRO A 175     8453   5124   8534   1035  -3210      9       C  
ATOM    166  N   GLY A 176     -11.821  22.981  11.014  1.00 61.90           N  
ANISOU  166  N   GLY A 176     8540   5735   9244   1838  -3231  -1043       N  
ATOM    167  CA  GLY A 176     -12.420  22.877  12.353  1.00 62.30           C  
ANISOU  167  CA  GLY A 176     8395   5983   9292   2094  -3124  -1422       C  
ATOM    168  C   GLY A 176     -13.930  23.006  12.336  1.00 64.00           C  
ANISOU  168  C   GLY A 176     8444   6297   9577   2352  -3228  -1741       C  
ATOM    169  O   GLY A 176     -14.612  22.553  13.253  1.00 64.39           O  
ANISOU  169  O   GLY A 176     8273   6641   9552   2518  -3033  -2032       O  
ATOM    170  N   ASP A 177     -14.443  23.636  11.287  1.00 65.10           N  
ANISOU  170  N   ASP A 177     8682   6202   9852   2377  -3545  -1681       N  
ATOM    171  CA  ASP A 177     -15.870  23.702  11.028  1.00 66.76           C  
ANISOU  171  CA  ASP A 177     8743   6494  10129   2597  -3653  -1946       C  
ATOM    172  C   ASP A 177     -16.262  22.533  10.130  1.00 64.19           C  
ANISOU  172  C   ASP A 177     8357   6383   9648   2425  -3350  -1768       C  
ATOM    173  O   ASP A 177     -17.438  22.354   9.815  1.00 64.93           O  
ANISOU  173  O   ASP A 177     8312   6592   9766   2562  -3372  -1948       O  
ATOM    174  CB  ASP A 177     -16.205  25.014  10.314  1.00 70.28           C  
ANISOU  174  CB  ASP A 177     9347   6538  10818   2712  -4198  -1962       C  
ATOM    175  CG  ASP A 177     -15.397  25.200   9.038  1.00 71.02           C  
ANISOU  175  CG  ASP A 177     9700   6371  10913   2407  -4333  -1505       C  
ATOM    176  OD1 ASP A 177     -15.983  25.120   7.937  1.00 72.83           O  
ANISOU  176  OD1 ASP A 177     9967   6551  11153   2356  -4430  -1392       O  
ATOM    177  OD2 ASP A 177     -14.167  25.406   9.145  1.00 71.83           O  
ANISOU  177  OD2 ASP A 177     9956   6346  10990   2210  -4334  -1258       O  
ATOM    178  N   GLU A 178     -15.263  21.753   9.721  1.00 60.77           N  
ANISOU  178  N   GLU A 178     8022   6005   9065   2133  -3085  -1432       N  
ATOM    179  CA  GLU A 178     -15.433  20.714   8.703  1.00 58.77           C  
ANISOU  179  CA  GLU A 178     7755   5899   8676   1947  -2851  -1224       C  
ATOM    180  C   GLU A 178     -15.518  19.318   9.310  1.00 55.42           C  
ANISOU  180  C   GLU A 178     7149   5839   8069   1887  -2395  -1275       C  
ATOM    181  O   GLU A 178     -14.661  18.934  10.106  1.00 53.56           O  
ANISOU  181  O   GLU A 178     6913   5693   7745   1805  -2192  -1226       O  
ATOM    182  CB  GLU A 178     -14.285  20.772   7.685  1.00 58.06           C  
ANISOU  182  CB  GLU A 178     7886   5640   8533   1661  -2894   -821       C  
ATOM    183  CG  GLU A 178     -14.153  22.133   7.005  1.00 62.07           C  
ANISOU  183  CG  GLU A 178     8593   5779   9212   1660  -3368   -706       C  
ATOM    184  CD  GLU A 178     -13.510  22.069   5.632  1.00 63.21           C  
ANISOU  184  CD  GLU A 178     8906   5840   9271   1374  -3417   -315       C  
ATOM    185  OE1 GLU A 178     -13.111  20.966   5.198  1.00 60.92           O  
ANISOU  185  OE1 GLU A 178     8574   5782   8791   1194  -3079   -157       O  
ATOM    186  OE2 GLU A 178     -13.404  23.138   4.991  1.00 66.11           O  
ANISOU  186  OE2 GLU A 178     9445   5914   9760   1329  -3815   -172       O  
ATOM    187  N   ALA A 179     -16.562  18.580   8.934  1.00 54.20           N  
ANISOU  187  N   ALA A 179     6846   5882   7867   1924  -2261  -1367       N  
ATOM    188  CA  ALA A 179     -16.740  17.206   9.378  1.00 52.01           C  
ANISOU  188  CA  ALA A 179     6405   5931   7428   1839  -1867  -1385       C  
ATOM    189  C   ALA A 179     -15.683  16.321   8.709  1.00 49.34           C  
ANISOU  189  C   ALA A 179     6189   5594   6963   1566  -1660  -1057       C  
ATOM    190  O   ALA A 179     -15.625  16.251   7.479  1.00 48.64           O  
ANISOU  190  O   ALA A 179     6201   5410   6869   1458  -1734   -874       O  
ATOM    191  CB  ALA A 179     -18.145  16.718   9.052  1.00 52.55           C  
ANISOU  191  CB  ALA A 179     6288   6184   7495   1935  -1821  -1555       C  
ATOM    192  N   PRO A 180     -14.840  15.653   9.518  1.00 47.72           N  
ANISOU  192  N   PRO A 180     5969   5510   6651   1462  -1412   -995       N  
ATOM    193  CA  PRO A 180     -13.688  14.927   8.992  1.00 45.85           C  
ANISOU  193  CA  PRO A 180     5847   5264   6309   1231  -1248   -719       C  
ATOM    194  C   PRO A 180     -14.075  13.847   7.987  1.00 44.97           C  
ANISOU  194  C   PRO A 180     5697   5271   6119   1119  -1103   -618       C  
ATOM    195  O   PRO A 180     -13.413  13.700   6.960  1.00 43.67           O  
ANISOU  195  O   PRO A 180     5650   5037   5907    974  -1119   -406       O  
ATOM    196  CB  PRO A 180     -13.069  14.305  10.244  1.00 44.86           C  
ANISOU  196  CB  PRO A 180     5661   5287   6099   1195  -1013   -754       C  
ATOM    197  CG  PRO A 180     -13.524  15.188  11.350  1.00 45.76           C  
ANISOU  197  CG  PRO A 180     5699   5400   6289   1396  -1138  -1001       C  
ATOM    198  CD  PRO A 180     -14.903  15.568  10.990  1.00 47.76           C  
ANISOU  198  CD  PRO A 180     5844   5680   6624   1562  -1287  -1194       C  
ATOM    199  N   LEU A 181     -15.155  13.121   8.276  1.00 45.20           N  
ANISOU  199  N   LEU A 181     5553   5494   6130   1185   -974   -776       N  
ATOM    200  CA  LEU A 181     -15.619  12.077   7.381  1.00 44.63           C  
ANISOU  200  CA  LEU A 181     5433   5525   6000   1092   -855   -705       C  
ATOM    201  C   LEU A 181     -16.049  12.657   6.033  1.00 45.57           C  
ANISOU  201  C   LEU A 181     5632   5504   6176   1112  -1076   -644       C  
ATOM    202  O   LEU A 181     -15.764  12.060   5.006  1.00 45.17           O  
ANISOU  202  O   LEU A 181     5640   5464   6059    985  -1027   -488       O  
ATOM    203  CB  LEU A 181     -16.737  11.243   8.027  1.00 45.21           C  
ANISOU  203  CB  LEU A 181     5292   5835   6049   1143   -695   -880       C  
ATOM    204  CG  LEU A 181     -17.167   9.959   7.303  1.00 44.24           C  
ANISOU  204  CG  LEU A 181     5109   5830   5870   1027   -551   -809       C  
ATOM    205  CD1 LEU A 181     -15.986   9.077   6.949  1.00 41.44           C  
ANISOU  205  CD1 LEU A 181     4863   5450   5431    850   -413   -605       C  
ATOM    206  CD2 LEU A 181     -18.201   9.196   8.123  1.00 44.63           C  
ANISOU  206  CD2 LEU A 181     4943   6123   5893   1044   -403   -961       C  
ATOM    207  N   ASP A 182     -16.692  13.827   6.041  1.00 46.73           N  
ANISOU  207  N   ASP A 182     5787   5522   6445   1275  -1337   -773       N  
ATOM    208  CA  ASP A 182     -17.044  14.529   4.803  1.00 48.01           C  
ANISOU  208  CA  ASP A 182     6053   5516   6673   1291  -1599   -697       C  
ATOM    209  C   ASP A 182     -15.804  15.064   4.093  1.00 46.77           C  
ANISOU  209  C   ASP A 182     6109   5182   6481   1130  -1717   -425       C  
ATOM    210  O   ASP A 182     -15.626  14.843   2.889  1.00 46.87           O  
ANISOU  210  O   ASP A 182     6200   5185   6425   1003  -1748   -246       O  
ATOM    211  CB  ASP A 182     -18.033  15.684   5.062  1.00 50.75           C  
ANISOU  211  CB  ASP A 182     6357   5744   7181   1523  -1891   -922       C  
ATOM    212  CG  ASP A 182     -19.265  15.248   5.850  1.00 53.97           C  
ANISOU  212  CG  ASP A 182     6519   6379   7608   1687  -1776  -1217       C  
ATOM    213  OD1 ASP A 182     -19.253  14.154   6.462  1.00 55.58           O  
ANISOU  213  OD1 ASP A 182     6596   6817   7704   1610  -1474  -1237       O  
ATOM    214  OD2 ASP A 182     -20.249  16.017   5.882  1.00 59.51           O  
ANISOU  214  OD2 ASP A 182     7146   7032   8432   1890  -2004  -1434       O  
ATOM    215  N   ALA A 183     -14.948  15.749   4.852  1.00 45.35           N  
ANISOU  215  N   ALA A 183     6008   4890   6334   1128  -1780   -398       N  
ATOM    216  CA  ALA A 183     -13.759  16.412   4.305  1.00 44.59           C  
ANISOU  216  CA  ALA A 183     6103   4627   6214    966  -1921   -141       C  
ATOM    217  C   ALA A 183     -12.735  15.443   3.687  1.00 41.85           C  
ANISOU  217  C   ALA A 183     5788   4425   5689    739  -1684     82       C  
ATOM    218  O   ALA A 183     -12.186  15.712   2.621  1.00 41.82           O  
ANISOU  218  O   ALA A 183     5897   4375   5617    583  -1788    304       O  
ATOM    219  CB  ALA A 183     -13.091  17.282   5.374  1.00 44.75           C  
ANISOU  219  CB  ALA A 183     6180   4504   6317   1020  -2030   -185       C  
ATOM    220  N   LEU A 184     -12.471  14.326   4.355  1.00 39.00           N  
ANISOU  220  N   LEU A 184     5322   4249   5246    718  -1382     19       N  
ATOM    221  CA  LEU A 184     -11.397  13.437   3.900  1.00 37.33           C  
ANISOU  221  CA  LEU A 184     5136   4165   4884    533  -1180    191       C  
ATOM    222  C   LEU A 184     -11.879  12.150   3.225  1.00 35.66           C  
ANISOU  222  C   LEU A 184     4830   4134   4585    500  -1000    167       C  
ATOM    223  O   LEU A 184     -11.086  11.234   3.031  1.00 33.64           O  
ANISOU  223  O   LEU A 184     4561   4002   4217    389   -819    243       O  
ATOM    224  CB  LEU A 184     -10.424  13.124   5.056  1.00 36.44           C  
ANISOU  224  CB  LEU A 184     5010   4093   4743    503  -1009    179       C  
ATOM    225  CG  LEU A 184      -9.725  14.385   5.624  1.00 38.68           C  
ANISOU  225  CG  LEU A 184     5402   4191   5102    507  -1197    230       C  
ATOM    226  CD1 LEU A 184      -8.742  14.033   6.703  1.00 40.11           C  
ANISOU  226  CD1 LEU A 184     5571   4424   5247    473  -1026    222       C  
ATOM    227  CD2 LEU A 184      -9.035  15.198   4.526  1.00 42.46           C  
ANISOU  227  CD2 LEU A 184     6023   4559   5549    350  -1400    471       C  
ATOM    228  N   ALA A 185     -13.165  12.099   2.866  1.00 35.30           N  
ANISOU  228  N   ALA A 185     4716   4097   4601    606  -1071     50       N  
ATOM    229  CA  ALA A 185     -13.795  10.872   2.327  1.00 34.53           C  
ANISOU  229  CA  ALA A 185     4517   4157   4448    593   -920     -2       C  
ATOM    230  C   ALA A 185     -13.025  10.278   1.146  1.00 33.78           C  
ANISOU  230  C   ALA A 185     4475   4148   4213    442   -864    161       C  
ATOM    231  O   ALA A 185     -12.748   9.076   1.115  1.00 32.20           O  
ANISOU  231  O   ALA A 185     4211   4081   3942    392   -674    142       O  
ATOM    232  CB  ALA A 185     -15.252  11.143   1.928  1.00 34.27           C  
ANISOU  232  CB  ALA A 185     4416   4100   4505    720  -1058   -131       C  
ATOM    233  N   GLU A 186     -12.689  11.125   0.170  1.00 35.10           N  
ANISOU  233  N   GLU A 186     4754   4249   4336    367  -1047    317       N  
ATOM    234  CA  GLU A 186     -11.930  10.665  -1.000  1.00 35.23           C  
ANISOU  234  CA  GLU A 186     4804   4400   4184    217  -1002    468       C  
ATOM    235  C   GLU A 186     -10.572  10.096  -0.590  1.00 33.57           C  
ANISOU  235  C   GLU A 186     4587   4294   3874    115   -818    525       C  
ATOM    236  O   GLU A 186     -10.137   9.069  -1.118  1.00 32.59           O  
ANISOU  236  O   GLU A 186     4408   4339   3634     59   -676    520       O  
ATOM    237  CB  GLU A 186     -11.769  11.781  -2.035  1.00 37.54           C  
ANISOU  237  CB  GLU A 186     5217   4620   4427    122  -1246    656       C  
ATOM    238  CG  GLU A 186     -12.927  11.873  -3.027  1.00 41.42           C  
ANISOU  238  CG  GLU A 186     5703   5099   4935    175  -1394    631       C  
ATOM    239  CD  GLU A 186     -12.798  13.051  -3.970  1.00 48.07           C  
ANISOU  239  CD  GLU A 186     6683   5845   5738     69  -1674    839       C  
ATOM    240  OE1 GLU A 186     -11.710  13.675  -4.019  1.00 50.78           O  
ANISOU  240  OE1 GLU A 186     7116   6172   6006    -84  -1733   1030       O  
ATOM    241  OE2 GLU A 186     -13.787  13.361  -4.663  1.00 51.08           O  
ANISOU  241  OE2 GLU A 186     7082   6163   6163    128  -1850    822       O  
ATOM    242  N   THR A 187      -9.914  10.745   0.367  1.00 32.32           N  
ANISOU  242  N   THR A 187     4479   4033   3769    107   -834    558       N  
ATOM    243  CA  THR A 187      -8.641  10.230   0.901  1.00 31.11           C  
ANISOU  243  CA  THR A 187     4314   3968   3540     27   -665    594       C  
ATOM    244  C   THR A 187      -8.794   8.853   1.557  1.00 29.37           C  
ANISOU  244  C   THR A 187     3987   3840   3334     92   -450    440       C  
ATOM    245  O   THR A 187      -7.960   7.951   1.335  1.00 28.68           O  
ANISOU  245  O   THR A 187     3864   3886   3147     28   -316    449       O  
ATOM    246  CB  THR A 187      -7.974  11.280   1.830  1.00 31.27           C  
ANISOU  246  CB  THR A 187     4413   3839   3629     12   -751    655       C  
ATOM    247  OG1 THR A 187      -7.633  12.427   1.033  1.00 33.52           O  
ANISOU  247  OG1 THR A 187     4806   4050   3881   -100   -968    844       O  
ATOM    248  CG2 THR A 187      -6.711  10.747   2.514  1.00 30.62           C  
ANISOU  248  CG2 THR A 187     4311   3838   3485    -53   -579    672       C  
ATOM    249  N   VAL A 188      -9.866   8.687   2.332  1.00 28.75           N  
ANISOU  249  N   VAL A 188     3850   3700   3373    214   -434    297       N  
ATOM    250  CA  VAL A 188     -10.158   7.429   3.013  1.00 28.04           C  
ANISOU  250  CA  VAL A 188     3664   3685   3306    250   -261    177       C  
ATOM    251  C   VAL A 188     -10.462   6.308   2.014  1.00 27.94           C  
ANISOU  251  C   VAL A 188     3595   3786   3236    226   -209    148       C  
ATOM    252  O   VAL A 188      -9.946   5.192   2.131  1.00 27.65           O  
ANISOU  252  O   VAL A 188     3519   3823   3163    193    -90    118       O  
ATOM    253  CB  VAL A 188     -11.344   7.597   3.991  1.00 28.74           C  
ANISOU  253  CB  VAL A 188     3680   3729   3510    364   -269     40       C  
ATOM    254  CG1 VAL A 188     -11.829   6.222   4.510  1.00 26.62           C  
ANISOU  254  CG1 VAL A 188     3304   3559   3253    361   -114    -52       C  
ATOM    255  CG2 VAL A 188     -10.939   8.513   5.145  1.00 28.06           C  
ANISOU  255  CG2 VAL A 188     3632   3556   3473    405   -301     27       C  
ATOM    256  N   LEU A 189     -11.286   6.619   1.023  1.00 29.06           N  
ANISOU  256  N   LEU A 189     3736   3929   3376    250   -322    150       N  
ATOM    257  CA  LEU A 189     -11.572   5.677  -0.046  1.00 28.71           C  
ANISOU  257  CA  LEU A 189     3645   3993   3271    233   -300    120       C  
ATOM    258  C   LEU A 189     -10.312   5.305  -0.852  1.00 29.32           C  
ANISOU  258  C   LEU A 189     3746   4199   3196    140   -258    196       C  
ATOM    259  O   LEU A 189     -10.047   4.127  -1.089  1.00 27.11           O  
ANISOU  259  O   LEU A 189     3408   4013   2879    139   -171    121       O  
ATOM    260  CB  LEU A 189     -12.698   6.210  -0.936  1.00 30.01           C  
ANISOU  260  CB  LEU A 189     3810   4133   3460    280   -448    111       C  
ATOM    261  CG  LEU A 189     -13.163   5.245  -2.034  1.00 28.11           C  
ANISOU  261  CG  LEU A 189     3513   4002   3166    278   -440     58       C  
ATOM    262  CD1 LEU A 189     -13.513   3.864  -1.461  1.00 25.63           C  
ANISOU  262  CD1 LEU A 189     3102   3717   2918    304   -314    -68       C  
ATOM    263  CD2 LEU A 189     -14.380   5.825  -2.716  1.00 27.39           C  
ANISOU  263  CD2 LEU A 189     3419   3866   3122    338   -592     38       C  
ATOM    264  N   ALA A 190      -9.513   6.302  -1.231  1.00 30.60           N  
ANISOU  264  N   ALA A 190     3985   4373   3270     61   -330    337       N  
ATOM    265  CA  ALA A 190      -8.244   6.018  -1.901  1.00 31.35           C  
ANISOU  265  CA  ALA A 190     4074   4639   3197    -40   -276    405       C  
ATOM    266  C   ALA A 190      -7.339   5.079  -1.075  1.00 30.55           C  
ANISOU  266  C   ALA A 190     3927   4579   3104    -31   -125    326       C  
ATOM    267  O   ALA A 190      -6.742   4.142  -1.626  1.00 30.08           O  
ANISOU  267  O   ALA A 190     3804   4677   2949    -40    -59    260       O  
ATOM    268  CB  ALA A 190      -7.508   7.307  -2.270  1.00 32.73           C  
ANISOU  268  CB  ALA A 190     4335   4821   3281   -161   -384    597       C  
ATOM    269  N   LEU A 191      -7.235   5.323   0.230  1.00 29.81           N  
ANISOU  269  N   LEU A 191     3860   4347   3120     -3    -86    319       N  
ATOM    270  CA  LEU A 191      -6.373   4.496   1.071  1.00 28.98           C  
ANISOU  270  CA  LEU A 191     3724   4260   3026      0     35    259       C  
ATOM    271  C   LEU A 191      -6.877   3.053   1.095  1.00 28.30           C  
ANISOU  271  C   LEU A 191     3565   4194   2993     61     93    119       C  
ATOM    272  O   LEU A 191      -6.083   2.121   0.941  1.00 27.87           O  
ANISOU  272  O   LEU A 191     3472   4227   2893     59    144     54       O  
ATOM    273  CB  LEU A 191      -6.277   5.046   2.494  1.00 29.53           C  
ANISOU  273  CB  LEU A 191     3837   4186   3198     18     56    277       C  
ATOM    274  CG  LEU A 191      -5.346   6.212   2.820  1.00 32.82           C  
ANISOU  274  CG  LEU A 191     4326   4562   3583    -47     12    399       C  
ATOM    275  CD1 LEU A 191      -5.361   6.429   4.332  1.00 32.91           C  
ANISOU  275  CD1 LEU A 191     4358   4445   3702      3     48    361       C  
ATOM    276  CD2 LEU A 191      -3.912   5.952   2.364  1.00 35.95           C  
ANISOU  276  CD2 LEU A 191     4705   5109   3847   -137     66    451       C  
ATOM    277  N   LEU A 192      -8.190   2.879   1.298  1.00 27.83           N  
ANISOU  277  N   LEU A 192     3484   4055   3037    114     67     65       N  
ATOM    278  CA  LEU A 192      -8.831   1.567   1.264  1.00 28.26           C  
ANISOU  278  CA  LEU A 192     3472   4110   3154    149     88    -46       C  
ATOM    279  C   LEU A 192      -8.673   0.854  -0.089  1.00 29.58           C  
ANISOU  279  C   LEU A 192     3600   4402   3236    159     52   -109       C  
ATOM    280  O   LEU A 192      -8.439  -0.376  -0.141  1.00 29.09           O  
ANISOU  280  O   LEU A 192     3495   4358   3198    181     63   -210       O  
ATOM    281  CB  LEU A 192     -10.316   1.657   1.705  1.00 29.04           C  
ANISOU  281  CB  LEU A 192     3536   4133   3365    186     63    -81       C  
ATOM    282  CG  LEU A 192     -10.538   1.976   3.198  1.00 27.98           C  
ANISOU  282  CG  LEU A 192     3399   3923   3308    187    117    -72       C  
ATOM    283  CD1 LEU A 192     -11.992   2.362   3.528  1.00 29.42           C  
ANISOU  283  CD1 LEU A 192     3521   4090   3569    232     85   -120       C  
ATOM    284  CD2 LEU A 192     -10.135   0.800   4.051  1.00 30.37           C  
ANISOU  284  CD2 LEU A 192     3679   4210   3648    148    189    -97       C  
ATOM    285  N   ALA A 193      -8.779   1.627  -1.171  1.00 30.15           N  
ANISOU  285  N   ALA A 193     3689   4561   3206    143    -11    -53       N  
ATOM    286  CA  ALA A 193      -8.628   1.121  -2.530  1.00 31.68           C  
ANISOU  286  CA  ALA A 193     3839   4919   3281    149    -49   -110       C  
ATOM    287  C   ALA A 193      -7.215   0.627  -2.795  1.00 32.23           C  
ANISOU  287  C   ALA A 193     3873   5146   3229    130      3   -152       C  
ATOM    288  O   ALA A 193      -7.026  -0.370  -3.493  1.00 33.39           O  
ANISOU  288  O   ALA A 193     3950   5408   3327    178    -10   -287       O  
ATOM    289  CB  ALA A 193      -8.993   2.200  -3.560  1.00 32.23           C  
ANISOU  289  CB  ALA A 193     3943   5058   3245    109   -138     -4       C  
ATOM    290  N   GLN A 194      -6.234   1.342  -2.259  1.00 31.64           N  
ANISOU  290  N   GLN A 194     3835   5083   3104     68     49    -51       N  
ATOM    291  CA  GLN A 194      -4.828   1.021  -2.483  1.00 34.06           C  
ANISOU  291  CA  GLN A 194     4091   5568   3283     43    100    -88       C  
ATOM    292  C   GLN A 194      -4.492  -0.304  -1.770  1.00 32.98           C  
ANISOU  292  C   GLN A 194     3914   5361   3255    125    134   -247       C  
ATOM    293  O   GLN A 194      -3.859  -1.177  -2.359  1.00 34.56           O  
ANISOU  293  O   GLN A 194     4033   5711   3385    176    126   -391       O  
ATOM    294  CB  GLN A 194      -3.934   2.192  -2.030  1.00 33.85           C  
ANISOU  294  CB  GLN A 194     4117   5553   3193    -60    125     76       C  
ATOM    295  CG  GLN A 194      -2.459   1.884  -1.897  1.00 37.41           C  
ANISOU  295  CG  GLN A 194     4509   6161   3546    -87    193     37       C  
ATOM    296  CD  GLN A 194      -1.700   2.873  -1.000  1.00 40.83           C  
ANISOU  296  CD  GLN A 194     5005   6516   3992   -172    218    183       C  
ATOM    297  OE1 GLN A 194      -2.211   3.929  -0.629  1.00 43.29           O  
ANISOU  297  OE1 GLN A 194     5408   6676   4364   -219    166    323       O  
ATOM    298  NE2 GLN A 194      -0.467   2.524  -0.661  1.00 41.45           N  
ANISOU  298  NE2 GLN A 194     5030   6700   4021   -181    279    133       N  
ATOM    299  N   TYR A 195      -4.957  -0.462  -0.532  1.00 31.43           N  
ANISOU  299  N   TYR A 195     3769   4946   3227    139    151   -228       N  
ATOM    300  CA  TYR A 195      -4.699  -1.681   0.242  1.00 31.46           C  
ANISOU  300  CA  TYR A 195     3756   4851   3347    190    154   -340       C  
ATOM    301  C   TYR A 195      -5.478  -2.930  -0.194  1.00 31.91           C  
ANISOU  301  C   TYR A 195     3769   4862   3491    256     75   -478       C  
ATOM    302  O   TYR A 195      -4.957  -4.053  -0.120  1.00 32.45           O  
ANISOU  302  O   TYR A 195     3806   4914   3610    312     27   -610       O  
ATOM    303  CB  TYR A 195      -4.779  -1.409   1.754  1.00 30.42           C  
ANISOU  303  CB  TYR A 195     3688   4539   3330    157    199   -253       C  
ATOM    304  CG  TYR A 195      -3.538  -0.682   2.242  1.00 30.56           C  
ANISOU  304  CG  TYR A 195     3733   4603   3277    117    256   -181       C  
ATOM    305  CD1 TYR A 195      -2.403  -1.394   2.642  1.00 34.13           C  
ANISOU  305  CD1 TYR A 195     4162   5076   3730    140    268   -257       C  
ATOM    306  CD2 TYR A 195      -3.468   0.714   2.241  1.00 29.82           C  
ANISOU  306  CD2 TYR A 195     3684   4527   3121     57    272    -45       C  
ATOM    307  CE1 TYR A 195      -1.246  -0.739   3.084  1.00 32.80           C  
ANISOU  307  CE1 TYR A 195     4007   4958   3497    100    317   -196       C  
ATOM    308  CE2 TYR A 195      -2.299   1.387   2.660  1.00 30.55           C  
ANISOU  308  CE2 TYR A 195     3799   4658   3152      5    308     28       C  
ATOM    309  CZ  TYR A 195      -1.206   0.646   3.092  1.00 32.80           C  
ANISOU  309  CZ  TYR A 195     4051   4977   3433     25    342    -48       C  
ATOM    310  OH  TYR A 195      -0.054   1.272   3.507  1.00 35.50           O  
ANISOU  310  OH  TYR A 195     4404   5366   3719    -27    376     16       O  
ATOM    311  N   GLY A 196      -6.676  -2.734  -0.737  1.00 32.16           N  
ANISOU  311  N   GLY A 196     3799   4878   3544    256     38   -461       N  
ATOM    312  CA  GLY A 196      -7.460  -3.859  -1.218  1.00 32.44           C  
ANISOU  312  CA  GLY A 196     3792   4870   3665    308    -50   -586       C  
ATOM    313  C   GLY A 196      -7.451  -4.042  -2.712  1.00 34.08           C  
ANISOU  313  C   GLY A 196     3939   5260   3750    363   -107   -692       C  
ATOM    314  O   GLY A 196      -8.249  -4.816  -3.230  1.00 35.10           O  
ANISOU  314  O   GLY A 196     4035   5353   3946    408   -193   -792       O  
ATOM    315  N   SER A 197      -6.545  -3.351  -3.407  1.00 34.52           N  
ANISOU  315  N   SER A 197     3973   5527   3616    348    -65   -670       N  
ATOM    316  CA  SER A 197      -6.528  -3.318  -4.879  1.00 35.74           C  
ANISOU  316  CA  SER A 197     4062   5917   3600    376   -106   -744       C  
ATOM    317  C   SER A 197      -7.949  -3.210  -5.459  1.00 35.65           C  
ANISOU  317  C   SER A 197     4064   5845   3637    383   -172   -726       C  
ATOM    318  O   SER A 197      -8.314  -3.929  -6.378  1.00 36.47           O  
ANISOU  318  O   SER A 197     4110   6032   3716    451   -249   -868       O  
ATOM    319  CB  SER A 197      -5.784  -4.541  -5.461  1.00 36.92           C  
ANISOU  319  CB  SER A 197     4114   6206   3708    484   -161   -984       C  
ATOM    320  OG  SER A 197      -4.487  -4.662  -4.899  1.00 37.81           O  
ANISOU  320  OG  SER A 197     4204   6375   3788    490   -111  -1019       O  
ATOM    321  N   LEU A 198      -8.753  -2.305  -4.910  1.00 34.67           N  
ANISOU  321  N   LEU A 198     4009   5580   3586    324   -154   -569       N  
ATOM    322  CA  LEU A 198     -10.156  -2.204  -5.303  1.00 34.86           C  
ANISOU  322  CA  LEU A 198     4035   5529   3680    339   -221   -562       C  
ATOM    323  C   LEU A 198     -10.271  -1.469  -6.642  1.00 36.03           C  
ANISOU  323  C   LEU A 198     4179   5863   3646    321   -270   -517       C  
ATOM    324  O   LEU A 198      -9.505  -0.545  -6.918  1.00 37.32           O  
ANISOU  324  O   LEU A 198     4370   6154   3655    250   -243   -397       O  
ATOM    325  CB  LEU A 198     -10.989  -1.493  -4.211  1.00 33.26           C  
ANISOU  325  CB  LEU A 198     3885   5135   3618    303   -196   -444       C  
ATOM    326  CG  LEU A 198     -10.894  -1.911  -2.715  1.00 32.88           C  
ANISOU  326  CG  LEU A 198     3849   4927   3716    285   -134   -435       C  
ATOM    327  CD1 LEU A 198     -11.691  -0.965  -1.819  1.00 30.45           C  
ANISOU  327  CD1 LEU A 198     3570   4511   3490    260   -109   -335       C  
ATOM    328  CD2 LEU A 198     -11.357  -3.338  -2.457  1.00 32.22           C  
ANISOU  328  CD2 LEU A 198     3720   4755   3768    308   -177   -549       C  
ATOM    329  N   ARG A 199     -11.228  -1.876  -7.461  1.00 37.19           N  
ANISOU  329  N   ARG A 199     4292   6028   3809    369   -354   -598       N  
ATOM    330  CA  ARG A 199     -11.476  -1.221  -8.764  1.00 39.15           C  
ANISOU  330  CA  ARG A 199     4541   6452   3883    348   -420   -550       C  
ATOM    331  C   ARG A 199     -12.736  -0.350  -8.750  1.00 38.32           C  
ANISOU  331  C   ARG A 199     4489   6205   3864    333   -491   -442       C  
ATOM    332  O   ARG A 199     -12.719   0.768  -9.266  1.00 39.75           O  
ANISOU  332  O   ARG A 199     4725   6446   3930    271   -541   -296       O  
ATOM    333  CB  ARG A 199     -11.560  -2.253  -9.900  1.00 40.47           C  
ANISOU  333  CB  ARG A 199     4622   6786   3968    427   -483   -740       C  
ATOM    334  CG  ARG A 199     -10.317  -2.369 -10.769  1.00 44.52           C  
ANISOU  334  CG  ARG A 199     5069   7617   4229    419   -456   -802       C  
ATOM    335  CD  ARG A 199     -10.311  -1.349 -11.937  1.00 48.85           C  
ANISOU  335  CD  ARG A 199     5629   8401   4530    330   -494   -664       C  
ATOM    336  NE  ARG A 199     -11.247  -1.692 -13.018  1.00 51.15           N  
ANISOU  336  NE  ARG A 199     5887   8767   4780    388   -599   -757       N  
ATOM    337  CZ  ARG A 199     -10.898  -2.069 -14.250  1.00 53.93           C  
ANISOU  337  CZ  ARG A 199     6151   9435   4903    414   -633   -875       C  
ATOM    338  NH1 ARG A 199      -9.620  -2.158 -14.604  1.00 55.21           N  
ANISOU  338  NH1 ARG A 199     6230   9904   4843    386   -565   -923       N  
ATOM    339  NH2 ARG A 199     -11.841  -2.353 -15.145  1.00 55.88           N  
ANISOU  339  NH2 ARG A 199     6379   9719   5135    472   -738   -956       N  
ATOM    340  N   ILE A 200     -13.818  -0.870  -8.179  1.00 37.11           N  
ANISOU  340  N   ILE A 200     4315   5875   3912    386   -512   -514       N  
ATOM    341  CA  ILE A 200     -15.094  -0.162  -8.131  1.00 37.17           C  
ANISOU  341  CA  ILE A 200     4342   5765   4016    397   -585   -459       C  
ATOM    342  C   ILE A 200     -15.647  -0.245  -6.712  1.00 36.23           C  
ANISOU  342  C   ILE A 200     4209   5462   4095    403   -529   -462       C  
ATOM    343  O   ILE A 200     -15.941  -1.326  -6.235  1.00 36.42           O  
ANISOU  343  O   ILE A 200     4176   5429   4233    417   -502   -559       O  
ATOM    344  CB  ILE A 200     -16.158  -0.730  -9.147  1.00 38.49           C  
ANISOU  344  CB  ILE A 200     4455   5970   4199    455   -689   -568       C  
ATOM    345  CG1 ILE A 200     -15.592  -0.764 -10.575  1.00 38.66           C  
ANISOU  345  CG1 ILE A 200     4474   6220   3996    451   -741   -586       C  
ATOM    346  CG2 ILE A 200     -17.458   0.077  -9.074  1.00 38.68           C  
ANISOU  346  CG2 ILE A 200     4489   5880   4326    476   -774   -522       C  
ATOM    347  CD1 ILE A 200     -16.611  -1.184 -11.680  1.00 40.35           C  
ANISOU  347  CD1 ILE A 200     4644   6488   4201    510   -860   -688       C  
ATOM    348  N   ALA A 201     -15.764   0.898  -6.036  1.00 34.95           N  
ANISOU  348  N   ALA A 201     4097   5217   3966    387   -526   -357       N  
ATOM    349  CA  ALA A 201     -16.199   0.910  -4.634  1.00 33.53           C  
ANISOU  349  CA  ALA A 201     3889   4913   3939    393   -461   -369       C  
ATOM    350  C   ALA A 201     -16.866   2.211  -4.209  1.00 33.21           C  
ANISOU  350  C   ALA A 201     3872   4792   3955    425   -523   -317       C  
ATOM    351  O   ALA A 201     -16.772   3.218  -4.920  1.00 33.46           O  
ANISOU  351  O   ALA A 201     3974   4825   3913    427   -627   -235       O  
ATOM    352  CB  ALA A 201     -15.007   0.602  -3.705  1.00 31.34           C  
ANISOU  352  CB  ALA A 201     3637   4623   3647    348   -346   -337       C  
ATOM    353  N   GLY A 202     -17.525   2.168  -3.043  1.00 32.96           N  
ANISOU  353  N   GLY A 202     3776   4699   4050    447   -473   -368       N  
ATOM    354  CA  GLY A 202     -18.116   3.354  -2.403  1.00 33.58           C  
ANISOU  354  CA  GLY A 202     3853   4711   4196    506   -529   -367       C  
ATOM    355  C   GLY A 202     -17.936   3.468  -0.884  1.00 32.15           C  
ANISOU  355  C   GLY A 202     3637   4505   4074    502   -425   -384       C  
ATOM    356  O   GLY A 202     -17.901   2.464  -0.171  1.00 31.54           O  
ANISOU  356  O   GLY A 202     3496   4463   4024    450   -311   -413       O  
ATOM    357  N   LEU A 203     -17.818   4.702  -0.396  1.00 32.36           N  
ANISOU  357  N   LEU A 203     3711   4466   4118    553   -485   -362       N  
ATOM    358  CA  LEU A 203     -17.804   4.976   1.054  1.00 31.76           C  
ANISOU  358  CA  LEU A 203     3588   4386   4093    575   -408   -407       C  
ATOM    359  C   LEU A 203     -19.080   5.687   1.511  1.00 33.40           C  
ANISOU  359  C   LEU A 203     3691   4606   4394    692   -490   -541       C  
ATOM    360  O   LEU A 203     -19.477   6.696   0.930  1.00 34.51           O  
ANISOU  360  O   LEU A 203     3874   4670   4568    778   -661   -558       O  
ATOM    361  CB  LEU A 203     -16.548   5.775   1.449  1.00 30.88           C  
ANISOU  361  CB  LEU A 203     3599   4199   3936    553   -411   -308       C  
ATOM    362  CG  LEU A 203     -16.216   5.970   2.940  1.00 29.36           C  
ANISOU  362  CG  LEU A 203     3379   4006   3769    564   -319   -342       C  
ATOM    363  CD1 LEU A 203     -15.660   4.692   3.588  1.00 28.73           C  
ANISOU  363  CD1 LEU A 203     3265   3996   3655    467   -146   -319       C  
ATOM    364  CD2 LEU A 203     -15.233   7.117   3.127  1.00 28.16           C  
ANISOU  364  CD2 LEU A 203     3353   3748   3601    572   -397   -259       C  
ATOM    365  N   TYR A 204     -19.734   5.145   2.538  1.00 34.00           N  
ANISOU  365  N   TYR A 204     3622   4793   4505    689   -381   -638       N  
ATOM    366  CA  TYR A 204     -21.016   5.688   2.989  1.00 36.04           C  
ANISOU  366  CA  TYR A 204     3733   5127   4834    803   -442   -801       C  
ATOM    367  C   TYR A 204     -20.992   6.035   4.471  1.00 36.25           C  
ANISOU  367  C   TYR A 204     3675   5241   4858    837   -360   -883       C  
ATOM    368  O   TYR A 204     -20.400   5.309   5.265  1.00 34.83           O  
ANISOU  368  O   TYR A 204     3487   5122   4625    729   -207   -821       O  
ATOM    369  CB  TYR A 204     -22.176   4.731   2.678  1.00 37.44           C  
ANISOU  369  CB  TYR A 204     3756   5429   5041    769   -408   -872       C  
ATOM    370  CG  TYR A 204     -22.198   4.304   1.226  1.00 39.31           C  
ANISOU  370  CG  TYR A 204     4070   5595   5273    741   -489   -807       C  
ATOM    371  CD1 TYR A 204     -23.051   4.913   0.299  1.00 41.02           C  
ANISOU  371  CD1 TYR A 204     4273   5777   5537    843   -655   -875       C  
ATOM    372  CD2 TYR A 204     -21.322   3.321   0.771  1.00 38.13           C  
ANISOU  372  CD2 TYR A 204     4006   5415   5065    623   -415   -692       C  
ATOM    373  CE1 TYR A 204     -23.023   4.530  -1.059  1.00 41.76           C  
ANISOU  373  CE1 TYR A 204     4442   5824   5603    814   -730   -812       C  
ATOM    374  CE2 TYR A 204     -21.296   2.937  -0.548  1.00 40.41           C  
ANISOU  374  CE2 TYR A 204     4354   5669   5330    610   -489   -656       C  
ATOM    375  CZ  TYR A 204     -22.146   3.522  -1.456  1.00 41.48           C  
ANISOU  375  CZ  TYR A 204     4478   5788   5496    697   -638   -709       C  
ATOM    376  OH  TYR A 204     -22.057   3.105  -2.756  1.00 43.27           O  
ANISOU  376  OH  TYR A 204     4762   6002   5675    675   -706   -671       O  
ATOM    377  N   ARG A 205     -21.614   7.159   4.827  1.00 37.27           N  
ANISOU  377  N   ARG A 205     3742   5374   5043    995   -481  -1033       N  
ATOM    378  CA  ARG A 205     -21.782   7.521   6.233  1.00 38.62           C  
ANISOU  378  CA  ARG A 205     3793   5679   5202   1056   -414  -1164       C  
ATOM    379  C   ARG A 205     -22.744   6.519   6.865  1.00 38.57           C  
ANISOU  379  C   ARG A 205     3561   5936   5157    980   -261  -1243       C  
ATOM    380  O   ARG A 205     -23.676   6.059   6.212  1.00 39.51           O  
ANISOU  380  O   ARG A 205     3584   6121   5309    969   -286  -1283       O  
ATOM    381  CB  ARG A 205     -22.339   8.946   6.397  1.00 40.41           C  
ANISOU  381  CB  ARG A 205     3984   5857   5513   1274   -616  -1353       C  
ATOM    382  CG  ARG A 205     -22.662   9.279   7.857  1.00 43.16           C  
ANISOU  382  CG  ARG A 205     4164   6402   5834   1361   -548  -1542       C  
ATOM    383  CD  ARG A 205     -23.054  10.729   8.082  1.00 48.64           C  
ANISOU  383  CD  ARG A 205     4836   7022   6623   1604   -779  -1757       C  
ATOM    384  NE  ARG A 205     -21.942  11.655   7.891  1.00 50.71           N  
ANISOU  384  NE  ARG A 205     5332   7002   6935   1636   -933  -1650       N  
ATOM    385  CZ  ARG A 205     -21.031  11.951   8.813  1.00 53.04           C  
ANISOU  385  CZ  ARG A 205     5688   7272   7194   1626   -882  -1629       C  
ATOM    386  NH1 ARG A 205     -21.071  11.387  10.021  1.00 55.57           N  
ANISOU  386  NH1 ARG A 205     5858   7841   7414   1586   -674  -1704       N  
ATOM    387  NH2 ARG A 205     -20.078  12.826   8.530  1.00 53.47           N  
ANISOU  387  NH2 ARG A 205     5952   7059   7305   1643  -1049  -1522       N  
ATOM    388  N   VAL A 206     -22.504   6.176   8.119  1.00 38.21           N  
ANISOU  388  N   VAL A 206     3433   6048   5037    911   -110  -1251       N  
ATOM    389  CA  VAL A 206     -23.407   5.321   8.850  1.00 39.70           C  
ANISOU  389  CA  VAL A 206     3395   6522   5168    812     27  -1308       C  
ATOM    390  C   VAL A 206     -24.005   6.126  10.007  1.00 42.18           C  
ANISOU  390  C   VAL A 206     3517   7068   5440    945     35  -1530       C  
ATOM    391  O   VAL A 206     -23.281   6.707  10.827  1.00 41.71           O  
ANISOU  391  O   VAL A 206     3513   6993   5343    998     51  -1554       O  
ATOM    392  CB  VAL A 206     -22.721   4.027   9.352  1.00 38.99           C  
ANISOU  392  CB  VAL A 206     3346   6468   5001    578    192  -1112       C  
ATOM    393  CG1 VAL A 206     -23.662   3.216  10.232  1.00 39.18           C  
ANISOU  393  CG1 VAL A 206     3130   6807   4950    442    317  -1145       C  
ATOM    394  CG2 VAL A 206     -22.233   3.173   8.164  1.00 37.11           C  
ANISOU  394  CG2 VAL A 206     3266   6026   4810    475    162   -945       C  
ATOM    395  N   ARG A 207     -25.333   6.166  10.039  1.00 44.29           N  
ANISOU  395  N   ARG A 207     3549   7563   5714   1007     17  -1710       N  
ATOM    396  CA  ARG A 207     -26.075   6.895  11.062  1.00 47.82           C  
ANISOU  396  CA  ARG A 207     3762   8294   6113   1155     17  -1973       C  
ATOM    397  C   ARG A 207     -25.970   6.212  12.427  1.00 48.85           C  
ANISOU  397  C   ARG A 207     3746   8735   6078    988    229  -1935       C  
ATOM    398  O   ARG A 207     -25.497   5.081  12.525  1.00 47.48           O  
ANISOU  398  O   ARG A 207     3641   8551   5848    745    358  -1699       O  
ATOM    399  CB  ARG A 207     -27.538   7.048  10.638  1.00 49.56           C  
ANISOU  399  CB  ARG A 207     3750   8700   6381   1262    -62  -2182       C  
ATOM    400  CG  ARG A 207     -27.715   7.690   9.265  1.00 50.45           C  
ANISOU  400  CG  ARG A 207     4006   8511   6652   1416   -289  -2210       C  
ATOM    401  CD  ARG A 207     -29.162   8.126   9.032  1.00 54.43           C  
ANISOU  401  CD  ARG A 207     4264   9205   7214   1587   -404  -2483       C  
ATOM    402  NE  ARG A 207     -29.922   7.106   8.321  1.00 57.98           N  
ANISOU  402  NE  ARG A 207     4621   9739   7670   1437   -348  -2400       N  
ATOM    403  CZ  ARG A 207     -30.239   7.155   7.028  1.00 58.45           C  
ANISOU  403  CZ  ARG A 207     4779   9589   7842   1486   -500  -2368       C  
ATOM    404  NH1 ARG A 207     -29.879   8.186   6.276  1.00 59.57           N  
ANISOU  404  NH1 ARG A 207     5118   9426   8092   1667   -724  -2393       N  
ATOM    405  NH2 ARG A 207     -30.924   6.166   6.485  1.00 59.93           N  
ANISOU  405  NH2 ARG A 207     4869   9871   8030   1342   -441  -2301       N  
ATOM    406  N   TYR A 208     -26.419   6.902  13.474  1.00 51.75           N  
ANISOU  406  N   TYR A 208     3911   9386   6367   1121    245  -2175       N  
ATOM    407  CA  TYR A 208     -26.331   6.396  14.846  1.00 53.61           C  
ANISOU  407  CA  TYR A 208     3993   9962   6416    972    437  -2156       C  
ATOM    408  C   TYR A 208     -27.125   5.090  15.097  1.00 54.48           C  
ANISOU  408  C   TYR A 208     3896  10391   6411    695    599  -2036       C  
ATOM    409  O   TYR A 208     -26.836   4.366  16.058  1.00 55.00           O  
ANISOU  409  O   TYR A 208     3909  10664   6325    479    755  -1897       O  
ATOM    410  CB  TYR A 208     -26.738   7.506  15.830  1.00 56.19           C  
ANISOU  410  CB  TYR A 208     4117  10557   6675   1210    397  -2489       C  
ATOM    411  CG  TYR A 208     -26.780   7.105  17.290  1.00 60.07           C  
ANISOU  411  CG  TYR A 208     4406  11478   6939   1076    590  -2512       C  
ATOM    412  CD1 TYR A 208     -25.663   7.251  18.108  1.00 61.59           C  
ANISOU  412  CD1 TYR A 208     4743  11601   7059   1047    644  -2426       C  
ATOM    413  CD2 TYR A 208     -27.954   6.602  17.859  1.00 63.97           C  
ANISOU  413  CD2 TYR A 208     4552  12476   7279    971    715  -2620       C  
ATOM    414  CE1 TYR A 208     -25.711   6.896  19.457  1.00 63.34           C  
ANISOU  414  CE1 TYR A 208     4777  12236   7053    919    814  -2443       C  
ATOM    415  CE2 TYR A 208     -28.006   6.236  19.192  1.00 66.81           C  
ANISOU  415  CE2 TYR A 208     4715  13269   7400    823    891  -2624       C  
ATOM    416  CZ  TYR A 208     -26.885   6.384  19.984  1.00 66.43           C  
ANISOU  416  CZ  TYR A 208     4826  13136   7279    800    938  -2534       C  
ATOM    417  OH  TYR A 208     -26.949   6.029  21.313  1.00 69.46           O  
ANISOU  417  OH  TYR A 208     5013  13970   7408    647   1105  -2534       O  
ATOM    418  N   ASP A 209     -28.094   4.784  14.234  1.00 54.88           N  
ANISOU  418  N   ASP A 209     3843  10469   6538    685    547  -2072       N  
ATOM    419  CA  ASP A 209     -28.873   3.536  14.351  1.00 56.14           C  
ANISOU  419  CA  ASP A 209     3818  10897   6616    405    668  -1940       C  
ATOM    420  C   ASP A 209     -28.397   2.368  13.448  1.00 54.43           C  
ANISOU  420  C   ASP A 209     3820  10368   6491    183    659  -1630       C  
ATOM    421  O   ASP A 209     -29.116   1.376  13.288  1.00 55.27           O  
ANISOU  421  O   ASP A 209     3797  10621   6581    -30    701  -1528       O  
ATOM    422  CB  ASP A 209     -30.374   3.812  14.150  1.00 58.70           C  
ANISOU  422  CB  ASP A 209     3825  11537   6943    505    631  -2194       C  
ATOM    423  CG  ASP A 209     -30.698   4.346  12.759  1.00 57.71           C  
ANISOU  423  CG  ASP A 209     3808  11099   7019    713    437  -2290       C  
ATOM    424  OD1 ASP A 209     -29.765   4.504  11.937  1.00 52.60           O  
ANISOU  424  OD1 ASP A 209     3478  10015   6494    765    339  -2151       O  
ATOM    425  OD2 ASP A 209     -31.895   4.602  12.492  1.00 58.89           O  
ANISOU  425  OD2 ASP A 209     3717  11465   7195    818    381  -2506       O  
ATOM    426  N   ARG A 210     -27.187   2.488  12.888  1.00 52.21           N  
ANISOU  426  N   ARG A 210     3856   9677   6303    231    594  -1495       N  
ATOM    427  CA  ARG A 210     -26.568   1.453  12.011  1.00 51.10           C  
ANISOU  427  CA  ARG A 210     3937   9229   6250     65    567  -1239       C  
ATOM    428  C   ARG A 210     -27.201   1.327  10.609  1.00 50.89           C  
ANISOU  428  C   ARG A 210     3931   9043   6359    126    444  -1270       C  
ATOM    429  O   ARG A 210     -27.155   0.265   9.976  1.00 50.74           O  
ANISOU  429  O   ARG A 210     3988   8897   6395    -40    427  -1105       O  
ATOM    430  CB  ARG A 210     -26.481   0.084  12.707  1.00 51.60           C  
ANISOU  430  CB  ARG A 210     3956   9425   6224   -259    678  -1013       C  
ATOM    431  CG  ARG A 210     -25.444   0.004  13.839  1.00 52.84           C  
ANISOU  431  CG  ARG A 210     4205   9603   6270   -347    770   -900       C  
ATOM    432  CD  ARG A 210     -25.567  -1.338  14.583  1.00 57.51           C  
ANISOU  432  CD  ARG A 210     4721  10362   6766   -687    851   -674       C  
ATOM    433  NE  ARG A 210     -24.502  -1.555  15.561  1.00 58.25           N  
ANISOU  433  NE  ARG A 210     4937  10428   6767   -790    914   -533       N  
ATOM    434  CZ  ARG A 210     -23.527  -2.457  15.436  1.00 58.21           C  
ANISOU  434  CZ  ARG A 210     5151  10147   6817   -937    874   -307       C  
ATOM    435  NH1 ARG A 210     -23.469  -3.255  14.369  1.00 56.99           N  
ANISOU  435  NH1 ARG A 210     5119   9727   6809   -996    770   -205       N  
ATOM    436  NH2 ARG A 210     -22.606  -2.566  16.383  1.00 56.95           N  
ANISOU  436  NH2 ARG A 210     5086   9982   6569  -1013    926   -199       N  
ATOM    437  N   THR A 211     -27.782   2.418  10.124  1.00 51.26           N  
ANISOU  437  N   THR A 211     3919   9089   6470    373    335  -1490       N  
ATOM    438  CA  THR A 211     -28.282   2.472   8.756  1.00 50.93           C  
ANISOU  438  CA  THR A 211     3927   8870   6555    460    197  -1525       C  
ATOM    439  C   THR A 211     -27.354   3.378   7.952  1.00 49.00           C  
ANISOU  439  C   THR A 211     3949   8278   6390    643     63  -1515       C  
ATOM    440  O   THR A 211     -26.778   4.317   8.514  1.00 48.83           O  
ANISOU  440  O   THR A 211     3989   8218   6348    773     44  -1584       O  
ATOM    441  CB  THR A 211     -29.741   2.983   8.680  1.00 53.43           C  
ANISOU  441  CB  THR A 211     3968   9439   6892    592    138  -1775       C  
ATOM    442  OG1 THR A 211     -29.857   4.231   9.379  1.00 54.17           O  
ANISOU  442  OG1 THR A 211     3969   9654   6957    818    100  -2008       O  
ATOM    443  CG2 THR A 211     -30.694   1.973   9.294  1.00 55.71           C  
ANISOU  443  CG2 THR A 211     3984  10087   7096    367    264  -1751       C  
ATOM    444  N   PRO A 212     -27.163   3.071   6.653  1.00 47.67           N  
ANISOU  444  N   PRO A 212     3940   7868   6304    635    -34  -1417       N  
ATOM    445  CA  PRO A 212     -26.297   3.888   5.814  1.00 46.19           C  
ANISOU  445  CA  PRO A 212     3994   7386   6168    769   -163  -1378       C  
ATOM    446  C   PRO A 212     -27.053   5.006   5.089  1.00 47.41           C  
ANISOU  446  C   PRO A 212     4121   7485   6409    989   -356  -1550       C  
ATOM    447  O   PRO A 212     -28.243   4.856   4.757  1.00 49.05           O  
ANISOU  447  O   PRO A 212     4155   7824   6658   1025   -402  -1672       O  
ATOM    448  CB  PRO A 212     -25.743   2.870   4.808  1.00 44.87           C  
ANISOU  448  CB  PRO A 212     3984   7047   6017    632   -162  -1192       C  
ATOM    449  CG  PRO A 212     -26.857   1.861   4.660  1.00 46.07           C  
ANISOU  449  CG  PRO A 212     3953   7360   6192    517   -132  -1215       C  
ATOM    450  CD  PRO A 212     -27.643   1.865   5.940  1.00 47.33           C  
ANISOU  450  CD  PRO A 212     3864   7824   6296    476    -26  -1319       C  
ATOM    451  N   GLU A 213     -26.370   6.124   4.862  1.00 46.90           N  
ANISOU  451  N   GLU A 213     4226   7220   6376   1129   -486  -1557       N  
ATOM    452  CA  GLU A 213     -26.898   7.197   4.014  1.00 47.68           C  
ANISOU  452  CA  GLU A 213     4360   7185   6569   1323   -723  -1672       C  
ATOM    453  C   GLU A 213     -26.540   6.823   2.579  1.00 46.57           C  
ANISOU  453  C   GLU A 213     4402   6849   6443   1251   -800  -1501       C  
ATOM    454  O   GLU A 213     -25.352   6.631   2.261  1.00 44.58           O  
ANISOU  454  O   GLU A 213     4346   6451   6139   1153   -762  -1313       O  
ATOM    455  CB  GLU A 213     -26.293   8.550   4.403  1.00 48.16           C  
ANISOU  455  CB  GLU A 213     4537   7097   6666   1480   -863  -1730       C  
ATOM    456  CG  GLU A 213     -26.378   8.846   5.904  1.00 49.43           C  
ANISOU  456  CG  GLU A 213     4539   7459   6785   1541   -765  -1890       C  
ATOM    457  CD  GLU A 213     -26.037  10.283   6.269  1.00 52.61           C  
ANISOU  457  CD  GLU A 213     5021   7713   7255   1743   -961  -2013       C  
ATOM    458  OE1 GLU A 213     -25.208  10.904   5.566  1.00 53.02           O  
ANISOU  458  OE1 GLU A 213     5315   7473   7355   1752  -1115  -1871       O  
ATOM    459  OE2 GLU A 213     -26.586  10.781   7.281  1.00 53.24           O  
ANISOU  459  OE2 GLU A 213     4913   7982   7335   1885   -967  -2256       O  
ATOM    460  N   PRO A 214     -27.562   6.688   1.716  1.00 47.46           N  
ANISOU  460  N   PRO A 214     4434   6987   6612   1299   -904  -1577       N  
ATOM    461  CA  PRO A 214     -27.432   6.145   0.360  1.00 46.60           C  
ANISOU  461  CA  PRO A 214     4449   6758   6499   1225   -962  -1444       C  
ATOM    462  C   PRO A 214     -26.512   6.935  -0.563  1.00 46.00           C  
ANISOU  462  C   PRO A 214     4624   6446   6408   1256  -1118  -1307       C  
ATOM    463  O   PRO A 214     -25.847   6.346  -1.424  1.00 45.48           O  
ANISOU  463  O   PRO A 214     4689   6313   6278   1144  -1091  -1149       O  
ATOM    464  CB  PRO A 214     -28.870   6.190  -0.176  1.00 48.22           C  
ANISOU  464  CB  PRO A 214     4488   7049   6784   1323  -1081  -1609       C  
ATOM    465  CG  PRO A 214     -29.581   7.173   0.702  1.00 50.16           C  
ANISOU  465  CG  PRO A 214     4575   7394   7088   1501  -1155  -1833       C  
ATOM    466  CD  PRO A 214     -28.966   7.007   2.040  1.00 49.40           C  
ANISOU  466  CD  PRO A 214     4434   7415   6922   1433   -967  -1820       C  
ATOM    467  N   GLN A 215     -26.482   8.249  -0.396  1.00 46.44           N  
ANISOU  467  N   GLN A 215     4739   6387   6519   1401  -1294  -1370       N  
ATOM    468  CA  GLN A 215     -25.646   9.103  -1.220  1.00 46.45           C  
ANISOU  468  CA  GLN A 215     4976   6168   6506   1404  -1472  -1216       C  
ATOM    469  C   GLN A 215     -24.197   8.981  -0.758  1.00 44.43           C  
ANISOU  469  C   GLN A 215     4857   5865   6161   1280  -1336  -1047       C  
ATOM    470  O   GLN A 215     -23.882   9.309   0.389  1.00 44.13           O  
ANISOU  470  O   GLN A 215     4783   5848   6135   1314  -1270  -1105       O  
ATOM    471  CB  GLN A 215     -26.125  10.549  -1.154  1.00 48.54           C  
ANISOU  471  CB  GLN A 215     5263   6295   6885   1596  -1750  -1339       C  
ATOM    472  CG  GLN A 215     -27.589  10.699  -1.542  1.00 51.43           C  
ANISOU  472  CG  GLN A 215     5473   6718   7350   1744  -1898  -1540       C  
ATOM    473  CD  GLN A 215     -28.018  12.136  -1.649  1.00 55.88           C  
ANISOU  473  CD  GLN A 215     6085   7103   8043   1946  -2230  -1660       C  
ATOM    474  OE1 GLN A 215     -27.896  12.917  -0.693  1.00 57.05           O  
ANISOU  474  OE1 GLN A 215     6206   7217   8254   2066  -2294  -1787       O  
ATOM    475  NE2 GLN A 215     -28.536  12.504  -2.816  1.00 57.22           N  
ANISOU  475  NE2 GLN A 215     6330   7149   8261   1994  -2468  -1632       N  
ATOM    476  N   PRO A 216     -23.316   8.488  -1.648  1.00 42.92           N  
ANISOU  476  N   PRO A 216     4807   5631   5869   1140  -1295   -853       N  
ATOM    477  CA  PRO A 216     -21.930   8.234  -1.268  1.00 41.08           C  
ANISOU  477  CA  PRO A 216     4682   5384   5545   1018  -1154   -705       C  
ATOM    478  C   PRO A 216     -21.123   9.487  -0.954  1.00 41.00           C  
ANISOU  478  C   PRO A 216     4812   5221   5546   1045  -1283   -628       C  
ATOM    479  O   PRO A 216     -21.208  10.491  -1.672  1.00 42.07           O  
ANISOU  479  O   PRO A 216     5056   5217   5713   1089  -1521   -574       O  
ATOM    480  CB  PRO A 216     -21.343   7.511  -2.496  1.00 40.96           C  
ANISOU  480  CB  PRO A 216     4757   5390   5417    894  -1124   -558       C  
ATOM    481  CG  PRO A 216     -22.243   7.856  -3.635  1.00 42.50           C  
ANISOU  481  CG  PRO A 216     4959   5553   5638    956  -1316   -582       C  
ATOM    482  CD  PRO A 216     -23.611   8.034  -3.023  1.00 43.66           C  
ANISOU  482  CD  PRO A 216     4938   5730   5919   1096  -1364   -790       C  
ATOM    483  N   LEU A 217     -20.344   9.407   0.127  1.00 39.49           N  
ANISOU  483  N   LEU A 217     4622   5049   5334   1009  -1142   -616       N  
ATOM    484  CA  LEU A 217     -19.340  10.399   0.447  1.00 38.69           C  
ANISOU  484  CA  LEU A 217     4662   4810   5230    997  -1233   -516       C  
ATOM    485  C   LEU A 217     -18.266  10.434  -0.627  1.00 37.88           C  
ANISOU  485  C   LEU A 217     4722   4656   5013    848  -1270   -285       C  
ATOM    486  O   LEU A 217     -17.737  11.495  -0.960  1.00 38.51           O  
ANISOU  486  O   LEU A 217     4941   4595   5097    825  -1458   -164       O  
ATOM    487  CB  LEU A 217     -18.697  10.082   1.799  1.00 37.50           C  
ANISOU  487  CB  LEU A 217     4466   4721   5061    973  -1043   -549       C  
ATOM    488  CG  LEU A 217     -19.619   9.916   3.003  1.00 38.78           C  
ANISOU  488  CG  LEU A 217     4442   5007   5286   1084   -959   -765       C  
ATOM    489  CD1 LEU A 217     -18.866   9.278   4.157  1.00 39.17           C  
ANISOU  489  CD1 LEU A 217     4460   5151   5273   1004   -739   -745       C  
ATOM    490  CD2 LEU A 217     -20.212  11.261   3.408  1.00 40.03           C  
ANISOU  490  CD2 LEU A 217     4582   5067   5558   1270  -1184   -921       C  
ATOM    491  N   ALA A 218     -17.927   9.261  -1.149  1.00 36.74           N  
ANISOU  491  N   ALA A 218     4553   4643   4764    741  -1100   -228       N  
ATOM    492  CA  ALA A 218     -16.967   9.149  -2.251  1.00 36.90           C  
ANISOU  492  CA  ALA A 218     4687   4691   4644    605  -1114    -43       C  
ATOM    493  C   ALA A 218     -17.202   7.860  -3.040  1.00 36.32           C  
ANISOU  493  C   ALA A 218     4542   4766   4494    562   -997    -73       C  
ATOM    494  O   ALA A 218     -17.808   6.918  -2.534  1.00 35.10           O  
ANISOU  494  O   ALA A 218     4266   4676   4395    600   -870   -202       O  
ATOM    495  CB  ALA A 218     -15.527   9.208  -1.719  1.00 35.09           C  
ANISOU  495  CB  ALA A 218     4529   4466   4339    502  -1009     73       C  
ATOM    496  N   THR A 219     -16.729   7.833  -4.288  1.00 38.04           N  
ANISOU  496  N   THR A 219     4829   5045   4578    474  -1055     49       N  
ATOM    497  CA  THR A 219     -16.790   6.630  -5.117  1.00 38.75           C  
ANISOU  497  CA  THR A 219     4859   5285   4581    441   -963      8       C  
ATOM    498  C   THR A 219     -15.468   6.406  -5.837  1.00 39.11           C  
ANISOU  498  C   THR A 219     4962   5462   4437    316   -909    135       C  
ATOM    499  O   THR A 219     -14.657   7.326  -5.972  1.00 39.85           O  
ANISOU  499  O   THR A 219     5151   5536   4452    233   -980    290       O  
ATOM    500  CB  THR A 219     -17.939   6.690  -6.183  1.00 40.32           C  
ANISOU  500  CB  THR A 219     5036   5492   4792    495  -1113    -34       C  
ATOM    501  OG1 THR A 219     -17.764   7.837  -7.019  1.00 42.96           O  
ANISOU  501  OG1 THR A 219     5490   5777   5055    450  -1314    118       O  
ATOM    502  CG2 THR A 219     -19.309   6.730  -5.524  1.00 39.42           C  
ANISOU  502  CG2 THR A 219     4822   5300   4858    623  -1150   -194       C  
ATOM    503  N   LEU A 220     -15.257   5.167  -6.277  1.00 39.45           N  
ANISOU  503  N   LEU A 220     4935   5646   4409    303   -795     57       N  
ATOM    504  CA  LEU A 220     -14.101   4.780  -7.072  1.00 40.21           C  
ANISOU  504  CA  LEU A 220     5042   5926   4309    212   -741    118       C  
ATOM    505  C   LEU A 220     -14.615   3.983  -8.260  1.00 41.54           C  
ANISOU  505  C   LEU A 220     5153   6231   4400    239   -775     31       C  
ATOM    506  O   LEU A 220     -15.451   3.084  -8.097  1.00 40.12           O  
ANISOU  506  O   LEU A 220     4896   6012   4336    320   -748   -118       O  
ATOM    507  CB  LEU A 220     -13.132   3.900  -6.260  1.00 39.51           C  
ANISOU  507  CB  LEU A 220     4910   5880   4223    200   -568     56       C  
ATOM    508  CG  LEU A 220     -11.963   3.292  -7.047  1.00 40.93           C  
ANISOU  508  CG  LEU A 220     5060   6284   4208    139   -504     53       C  
ATOM    509  CD1 LEU A 220     -10.853   4.324  -7.253  1.00 42.91           C  
ANISOU  509  CD1 LEU A 220     5378   6622   4305     15   -523    236       C  
ATOM    510  CD2 LEU A 220     -11.426   2.034  -6.372  1.00 40.40           C  
ANISOU  510  CD2 LEU A 220     4924   6230   4196    182   -374    -87       C  
ATOM    511  N   GLY A 221     -14.109   4.326  -9.445  1.00 43.16           N  
ANISOU  511  N   GLY A 221     5390   6608   4401    159   -842    130       N  
ATOM    512  CA  GLY A 221     -14.503   3.655 -10.666  1.00 45.13           C  
ANISOU  512  CA  GLY A 221     5585   7021   4541    183   -885     47       C  
ATOM    513  C   GLY A 221     -15.948   3.941 -10.989  1.00 46.39           C  
ANISOU  513  C   GLY A 221     5753   7055   4819    256  -1026     15       C  
ATOM    514  O   GLY A 221     -16.470   5.005 -10.656  1.00 47.10           O  
ANISOU  514  O   GLY A 221     5913   6980   5003    260  -1139    109       O  
ATOM    515  N   GLU A 222     -16.598   2.984 -11.639  1.00 47.16           N  
ANISOU  515  N   GLU A 222     5773   7225   4919    325  -1036   -133       N  
ATOM    516  CA  GLU A 222     -17.975   3.155 -12.062  1.00 48.28           C  
ANISOU  516  CA  GLU A 222     5906   7276   5162    396  -1172   -180       C  
ATOM    517  C   GLU A 222     -18.936   2.594 -11.021  1.00 46.80           C  
ANISOU  517  C   GLU A 222     5643   6918   5222    488  -1122   -321       C  
ATOM    518  O   GLU A 222     -19.697   1.674 -11.311  1.00 46.10           O  
ANISOU  518  O   GLU A 222     5472   6843   5203    546  -1131   -462       O  
ATOM    519  CB  GLU A 222     -18.203   2.499 -13.433  1.00 49.66           C  
ANISOU  519  CB  GLU A 222     6038   7640   5192    411  -1233   -257       C  
ATOM    520  CG  GLU A 222     -17.386   3.125 -14.560  1.00 53.37           C  
ANISOU  520  CG  GLU A 222     6566   8333   5380    300  -1295   -105       C  
ATOM    521  CD  GLU A 222     -16.132   2.345 -14.884  1.00 55.70           C  
ANISOU  521  CD  GLU A 222     6797   8886   5481    259  -1164   -165       C  
ATOM    522  OE1 GLU A 222     -15.288   2.145 -13.972  1.00 56.03           O  
ANISOU  522  OE1 GLU A 222     6827   8896   5565    242  -1033   -172       O  
ATOM    523  OE2 GLU A 222     -15.997   1.942 -16.066  1.00 58.41           O  
ANISOU  523  OE2 GLU A 222     7092   9478   5623    253  -1201   -220       O  
ATOM    524  N   MET A 223     -18.889   3.151  -9.808  1.00 46.33           N  
ANISOU  524  N   MET A 223     5602   6716   5284    491  -1074   -281       N  
ATOM    525  CA  MET A 223     -19.784   2.723  -8.736  1.00 45.95           C  
ANISOU  525  CA  MET A 223     5465   6552   5441    555  -1019   -398       C  
ATOM    526  C   MET A 223     -21.245   2.972  -9.063  1.00 47.70           C  
ANISOU  526  C   MET A 223     5633   6719   5772    636  -1151   -474       C  
ATOM    527  O   MET A 223     -21.635   4.112  -9.380  1.00 48.08           O  
ANISOU  527  O   MET A 223     5742   6703   5823    667  -1301   -411       O  
ATOM    528  CB  MET A 223     -19.453   3.404  -7.399  1.00 45.28           C  
ANISOU  528  CB  MET A 223     5404   6360   5439    550   -955   -349       C  
ATOM    529  CG  MET A 223     -20.115   2.728  -6.189  1.00 43.29           C  
ANISOU  529  CG  MET A 223     5040   6062   5348    581   -851   -464       C  
ATOM    530  SD  MET A 223     -19.537   1.028  -5.976  1.00 42.86           S  
ANISOU  530  SD  MET A 223     4928   6069   5287    521   -708   -528       S  
ATOM    531  CE  MET A 223     -20.691   0.373  -4.785  1.00 34.95           C  
ANISOU  531  CE  MET A 223     3788   5025   4466    522   -648   -624       C  
ATOM    532  N   PRO A 224     -22.065   1.912  -8.959  1.00 48.71           N  
ANISOU  532  N   PRO A 224     5644   6861   6001    666  -1114   -611       N  
ATOM    533  CA  PRO A 224     -23.499   2.038  -9.136  1.00 50.44           C  
ANISOU  533  CA  PRO A 224     5780   7046   6339    740  -1221   -704       C  
ATOM    534  C   PRO A 224     -24.078   2.793  -7.948  1.00 51.03           C  
ANISOU  534  C   PRO A 224     5802   7041   6547    789  -1212   -733       C  
ATOM    535  O   PRO A 224     -23.385   2.969  -6.941  1.00 49.34           O  
ANISOU  535  O   PRO A 224     5608   6801   6338    756  -1103   -690       O  
ATOM    536  CB  PRO A 224     -23.966   0.579  -9.090  1.00 50.46           C  
ANISOU  536  CB  PRO A 224     5668   7089   6416    720  -1156   -822       C  
ATOM    537  CG  PRO A 224     -23.012  -0.063  -8.129  1.00 48.72           C  
ANISOU  537  CG  PRO A 224     5453   6862   6198    649   -998   -795       C  
ATOM    538  CD  PRO A 224     -21.692   0.546  -8.527  1.00 48.51           C  
ANISOU  538  CD  PRO A 224     5557   6868   6007    624   -984   -682       C  
ATOM    539  N   ALA A 225     -25.331   3.239  -8.067  1.00 53.00           N  
ANISOU  539  N   ALA A 225     5974   7267   6897    877  -1333   -824       N  
ATOM    540  CA  ALA A 225     -26.118   3.635  -6.897  1.00 54.20           C  
ANISOU  540  CA  ALA A 225     6005   7405   7183    940  -1309   -923       C  
ATOM    541  C   ALA A 225     -26.242   2.388  -6.009  1.00 54.25           C  
ANISOU  541  C   ALA A 225     5880   7493   7238    857  -1125   -978       C  
ATOM    542  O   ALA A 225     -26.032   1.270  -6.492  1.00 53.00           O  
ANISOU  542  O   ALA A 225     5720   7366   7053    783  -1080   -968       O  
ATOM    543  CB  ALA A 225     -27.495   4.127  -7.328  1.00 55.61           C  
ANISOU  543  CB  ALA A 225     6092   7579   7457   1056  -1478  -1043       C  
ATOM    544  N   LEU A 226     -26.562   2.560  -4.724  1.00 55.41           N  
ANISOU  544  N   LEU A 226     5918   7680   7454    865  -1037  -1035       N  
ATOM    545  CA  LEU A 226     -26.717   1.387  -3.844  1.00 56.37           C  
ANISOU  545  CA  LEU A 226     5915   7890   7612    753   -880  -1056       C  
ATOM    546  C   LEU A 226     -27.912   0.509  -4.221  1.00 58.18           C  
ANISOU  546  C   LEU A 226     5992   8196   7918    722   -915  -1145       C  
ATOM    547  O   LEU A 226     -27.949  -0.044  -5.322  1.00 59.12           O  
ANISOU  547  O   LEU A 226     6159   8277   8025    713   -993  -1138       O  
ATOM    548  CB  LEU A 226     -26.731   1.746  -2.349  1.00 56.45           C  
ANISOU  548  CB  LEU A 226     5837   7970   7643    745   -766  -1084       C  
ATOM    549  CG  LEU A 226     -25.395   1.883  -1.605  1.00 55.26           C  
ANISOU  549  CG  LEU A 226     5805   7767   7423    693   -657   -976       C  
ATOM    550  CD1 LEU A 226     -25.625   2.178  -0.131  1.00 55.16           C  
ANISOU  550  CD1 LEU A 226     5673   7859   7427    691   -554  -1031       C  
ATOM    551  CD2 LEU A 226     -24.477   0.652  -1.752  1.00 54.61           C  
ANISOU  551  CD2 LEU A 226     5800   7651   7298    560   -569   -873       C  
ATOM    552  N   ASP A 227     -28.902   0.411  -3.337  1.00 59.84           N  
ANISOU  552  N   ASP A 227     6006   8532   8197    706   -866  -1236       N  
ATOM    553  CA  ASP A 227     -29.833  -0.723  -3.352  1.00 60.79           C  
ANISOU  553  CA  ASP A 227     5965   8746   8385    601   -853  -1278       C  
ATOM    554  C   ASP A 227     -31.275  -0.373  -2.979  1.00 63.03           C  
ANISOU  554  C   ASP A 227     6015   9196   8737    652   -883  -1425       C  
ATOM    555  O   ASP A 227     -31.828   0.622  -3.456  1.00 64.06           O  
ANISOU  555  O   ASP A 227     6129   9318   8893    815  -1006  -1531       O  
ATOM    556  CB  ASP A 227     -29.311  -1.768  -2.366  1.00 60.30           C  
ANISOU  556  CB  ASP A 227     5880   8718   8314    419   -709  -1181       C  
ATOM    557  CG  ASP A 227     -28.907  -1.158  -1.033  1.00 58.34           C  
ANISOU  557  CG  ASP A 227     5603   8548   8017    413   -584  -1162       C  
ATOM    558  OD1 ASP A 227     -29.339  -0.031  -0.715  1.00 57.49           O  
ANISOU  558  OD1 ASP A 227     5428   8509   7905    546   -606  -1264       O  
ATOM    559  OD2 ASP A 227     -28.154  -1.802  -0.294  1.00 58.51           O  
ANISOU  559  OD2 ASP A 227     5667   8556   8007    285   -480  -1058       O  
ATOM    560  N   ALA A 228     -31.871  -1.233  -2.145  1.00 63.98           N  
ANISOU  560  N   ALA A 228     5949   9474   8885    500   -784  -1428       N  
ATOM    561  CA  ALA A 228     -33.160  -1.000  -1.481  1.00 65.85           C  
ANISOU  561  CA  ALA A 228     5915   9950   9156    508   -764  -1566       C  
ATOM    562  C   ALA A 228     -33.148  -1.658  -0.088  1.00 66.18           C  
ANISOU  562  C   ALA A 228     5815  10180   9152    311   -594  -1498       C  
ATOM    563  O   ALA A 228     -33.878  -1.235   0.813  1.00 67.73           O  
ANISOU  563  O   ALA A 228     5790  10625   9319    323   -528  -1608       O  
ATOM    564  CB  ALA A 228     -34.311  -1.532  -2.325  1.00 67.30           C  
ANISOU  564  CB  ALA A 228     5969  10180   9423    493   -873  -1643       C  
ATOM    565  N   ASP A 229     -32.313  -2.694   0.056  1.00 64.78           N  
ANISOU  565  N   ASP A 229     5760   9891   8961    134   -538  -1325       N  
ATOM    566  CA  ASP A 229     -32.005  -3.391   1.327  1.00 64.33           C  
ANISOU  566  CA  ASP A 229     5639   9952   8852    -77   -399  -1203       C  
ATOM    567  C   ASP A 229     -31.067  -4.574   1.028  1.00 62.65           C  
ANISOU  567  C   ASP A 229     5614   9522   8670   -226   -425  -1031       C  
ATOM    568  O   ASP A 229     -31.334  -5.713   1.416  1.00 63.41           O  
ANISOU  568  O   ASP A 229     5637   9656   8800   -449   -424   -927       O  
ATOM    569  CB  ASP A 229     -33.282  -3.873   2.054  1.00 66.61           C  
ANISOU  569  CB  ASP A 229     5626  10545   9140   -242   -348  -1237       C  
ATOM    570  CG  ASP A 229     -33.021  -4.338   3.498  1.00 67.49           C  
ANISOU  570  CG  ASP A 229     5649  10839   9157   -458   -200  -1113       C  
ATOM    571  OD1 ASP A 229     -31.995  -4.998   3.781  1.00 67.29           O  
ANISOU  571  OD1 ASP A 229     5798  10649   9120   -581   -176   -941       O  
ATOM    572  OD2 ASP A 229     -33.865  -4.054   4.368  1.00 70.02           O  
ANISOU  572  OD2 ASP A 229     5709  11489   9405   -507   -113  -1193       O  
ATOM    573  N   ASP A 230     -29.974  -4.297   0.321  1.00 60.34           N  
ANISOU  573  N   ASP A 230     5556   9007   8365   -104   -468  -1007       N  
ATOM    574  CA  ASP A 230     -28.992  -5.326  -0.027  1.00 58.85           C  
ANISOU  574  CA  ASP A 230     5541   8619   8201   -196   -508   -891       C  
ATOM    575  C   ASP A 230     -28.574  -6.141   1.204  1.00 58.31           C  
ANISOU  575  C   ASP A 230     5455   8582   8119   -408   -425   -750       C  
ATOM    576  O   ASP A 230     -28.217  -5.583   2.241  1.00 57.95           O  
ANISOU  576  O   ASP A 230     5390   8637   7992   -417   -303   -719       O  
ATOM    577  CB  ASP A 230     -27.771  -4.689  -0.705  1.00 57.60           C  
ANISOU  577  CB  ASP A 230     5603   8296   7986    -34   -525   -893       C  
ATOM    578  CG  ASP A 230     -26.857  -5.710  -1.342  1.00 57.37           C  
ANISOU  578  CG  ASP A 230     5727   8089   7982    -78   -595   -837       C  
ATOM    579  OD1 ASP A 230     -25.948  -6.202  -0.645  1.00 56.29           O  
ANISOU  579  OD1 ASP A 230     5668   7891   7830   -166   -543   -744       O  
ATOM    580  OD2 ASP A 230     -27.044  -6.011  -2.544  1.00 59.14           O  
ANISOU  580  OD2 ASP A 230     5989   8244   8239    -12   -714   -901       O  
ATOM    581  N   LEU A 231     -28.643  -7.463   1.075  1.00 58.20           N  
ANISOU  581  N   LEU A 231     5449   8476   8189   -580   -513   -665       N  
ATOM    582  CA  LEU A 231     -28.358  -8.389   2.177  1.00 57.84           C  
ANISOU  582  CA  LEU A 231     5391   8439   8149   -818   -484   -504       C  
ATOM    583  C   LEU A 231     -26.919  -8.288   2.715  1.00 55.55           C  
ANISOU  583  C   LEU A 231     5282   8027   7799   -791   -423   -428       C  
ATOM    584  O   LEU A 231     -26.696  -8.389   3.925  1.00 55.39           O  
ANISOU  584  O   LEU A 231     5227   8099   7721   -930   -332   -319       O  
ATOM    585  CB  LEU A 231     -28.674  -9.828   1.745  1.00 59.21           C  
ANISOU  585  CB  LEU A 231     5569   8473   8456   -990   -654   -435       C  
ATOM    586  CG  LEU A 231     -28.456 -10.994   2.717  1.00 60.82           C  
ANISOU  586  CG  LEU A 231     5779   8629   8702  -1271   -701   -241       C  
ATOM    587  CD1 LEU A 231     -29.190 -10.807   4.044  1.00 62.69           C  
ANISOU  587  CD1 LEU A 231     5812   9165   8843  -1475   -566   -139       C  
ATOM    588  CD2 LEU A 231     -28.886 -12.297   2.049  1.00 62.74           C  
ANISOU  588  CD2 LEU A 231     6031   8699   9108  -1403   -924   -207       C  
ATOM    589  N   LEU A 232     -25.952  -8.085   1.823  1.00 52.78           N  
ANISOU  589  N   LEU A 232     5111   7493   7450   -620   -471   -485       N  
ATOM    590  CA  LEU A 232     -24.565  -7.945   2.256  1.00 50.93           C  
ANISOU  590  CA  LEU A 232     5037   7157   7160   -582   -416   -429       C  
ATOM    591  C   LEU A 232     -24.396  -6.664   3.090  1.00 49.46           C  
ANISOU  591  C   LEU A 232     4818   7117   6857   -506   -256   -439       C  
ATOM    592  O   LEU A 232     -23.784  -6.697   4.160  1.00 48.79           O  
ANISOU  592  O   LEU A 232     4762   7056   6722   -588   -174   -349       O  
ATOM    593  CB  LEU A 232     -23.600  -7.969   1.064  1.00 49.70           C  
ANISOU  593  CB  LEU A 232     5046   6829   7008   -419   -499   -504       C  
ATOM    594  CG  LEU A 232     -22.155  -8.382   1.364  1.00 49.29           C  
ANISOU  594  CG  LEU A 232     5148   6641   6939   -420   -501   -451       C  
ATOM    595  CD1 LEU A 232     -22.078  -9.783   1.975  1.00 50.19           C  
ANISOU  595  CD1 LEU A 232     5271   6640   7157   -610   -605   -353       C  
ATOM    596  CD2 LEU A 232     -21.304  -8.302   0.106  1.00 49.38           C  
ANISOU  596  CD2 LEU A 232     5278   6562   6923   -250   -569   -554       C  
ATOM    597  N   VAL A 233     -24.973  -5.565   2.593  1.00 48.38           N  
ANISOU  597  N   VAL A 233     4623   7070   6688   -348   -237   -554       N  
ATOM    598  CA  VAL A 233     -24.946  -4.256   3.257  1.00 47.18           C  
ANISOU  598  CA  VAL A 233     4434   7042   6452   -241   -132   -603       C  
ATOM    599  C   VAL A 233     -25.591  -4.387   4.630  1.00 48.24           C  
ANISOU  599  C   VAL A 233     4391   7394   6544   -387    -31   -568       C  
ATOM    600  O   VAL A 233     -24.997  -4.021   5.632  1.00 47.92           O  
ANISOU  600  O   VAL A 233     4372   7409   6428   -404     66   -526       O  
ATOM    601  CB  VAL A 233     -25.668  -3.172   2.398  1.00 47.40           C  
ANISOU  601  CB  VAL A 233     4417   7108   6486    -53   -189   -744       C  
ATOM    602  CG1 VAL A 233     -25.969  -1.909   3.207  1.00 47.20           C  
ANISOU  602  CG1 VAL A 233     4302   7227   6405     53   -121   -829       C  
ATOM    603  CG2 VAL A 233     -24.851  -2.837   1.154  1.00 46.13           C  
ANISOU  603  CG2 VAL A 233     4443   6768   6318     79   -274   -753       C  
ATOM    604  N   ARG A 234     -26.807  -4.930   4.658  1.00 50.11           N  
ANISOU  604  N   ARG A 234     4445   7776   6820   -502    -55   -583       N  
ATOM    605  CA  ARG A 234     -27.542  -5.180   5.900  1.00 51.60           C  
ANISOU  605  CA  ARG A 234     4427   8233   6946   -682     38   -539       C  
ATOM    606  C   ARG A 234     -26.782  -6.078   6.894  1.00 51.19           C  
ANISOU  606  C   ARG A 234     4444   8150   6858   -901     79   -348       C  
ATOM    607  O   ARG A 234     -26.663  -5.739   8.071  1.00 51.26           O  
ANISOU  607  O   ARG A 234     4380   8342   6756   -960    196   -316       O  
ATOM    608  CB  ARG A 234     -28.928  -5.750   5.570  1.00 53.77           C  
ANISOU  608  CB  ARG A 234     4499   8655   7277   -795    -18   -570       C  
ATOM    609  CG  ARG A 234     -29.749  -6.228   6.769  1.00 57.13           C  
ANISOU  609  CG  ARG A 234     4686   9395   7625  -1043     67   -493       C  
ATOM    610  CD  ARG A 234     -30.981  -6.962   6.270  1.00 61.07           C  
ANISOU  610  CD  ARG A 234     5012   9989   8202  -1182    -18   -493       C  
ATOM    611  NE  ARG A 234     -31.533  -7.880   7.261  1.00 65.05           N  
ANISOU  611  NE  ARG A 234     5344  10719   8651  -1515     18   -327       N  
ATOM    612  CZ  ARG A 234     -32.173  -9.007   6.961  1.00 68.59           C  
ANISOU  612  CZ  ARG A 234     5728  11142   9191  -1746    -97   -211       C  
ATOM    613  NH1 ARG A 234     -32.333  -9.373   5.691  1.00 68.84           N  
ANISOU  613  NH1 ARG A 234     5852  10928   9376  -1657   -251   -267       N  
ATOM    614  NH2 ARG A 234     -32.647  -9.775   7.934  1.00 70.86           N  
ANISOU  614  NH2 ARG A 234     5857  11654   9411  -2078    -71    -32       N  
ATOM    615  N   THR A 235     -26.274  -7.214   6.416  1.00 50.81           N  
ANISOU  615  N   THR A 235     4535   7868   6904  -1010    -36   -233       N  
ATOM    616  CA  THR A 235     -25.514  -8.163   7.255  1.00 51.11           C  
ANISOU  616  CA  THR A 235     4664   7820   6937  -1214    -51    -47       C  
ATOM    617  C   THR A 235     -24.269  -7.547   7.913  1.00 49.91           C  
ANISOU  617  C   THR A 235     4649   7614   6699  -1121     43    -27       C  
ATOM    618  O   THR A 235     -23.974  -7.797   9.090  1.00 50.23           O  
ANISOU  618  O   THR A 235     4673   7748   6664  -1277    105     96       O  
ATOM    619  CB  THR A 235     -25.096  -9.410   6.436  1.00 50.90           C  
ANISOU  619  CB  THR A 235     4783   7499   7058  -1282   -240     20       C  
ATOM    620  OG1 THR A 235     -26.264  -9.998   5.843  1.00 52.17           O  
ANISOU  620  OG1 THR A 235     4817   7700   7307  -1376   -342      5       O  
ATOM    621  CG2 THR A 235     -24.390 -10.443   7.318  1.00 50.89           C  
ANISOU  621  CG2 THR A 235     4875   7384   7075  -1499   -303    214       C  
ATOM    622  N   CYS A 236     -23.543  -6.749   7.136  1.00 48.44           N  
ANISOU  622  N   CYS A 236     4597   7288   6521   -881     43   -139       N  
ATOM    623  CA  CYS A 236     -22.332  -6.085   7.609  1.00 47.21           C  
ANISOU  623  CA  CYS A 236     4575   7068   6295   -779    118   -132       C  
ATOM    624  C   CYS A 236     -22.632  -5.126   8.765  1.00 48.09           C  
ANISOU  624  C   CYS A 236     4563   7427   6283   -764    260   -166       C  
ATOM    625  O   CYS A 236     -21.969  -5.179   9.813  1.00 48.00           O  
ANISOU  625  O   CYS A 236     4589   7450   6200   -843    328    -79       O  
ATOM    626  CB  CYS A 236     -21.669  -5.348   6.446  1.00 45.45           C  
ANISOU  626  CB  CYS A 236     4489   6688   6093   -548     79   -239       C  
ATOM    627  SG  CYS A 236     -20.458  -4.098   6.896  1.00 43.23           S  
ANISOU  627  SG  CYS A 236     4328   6378   5720   -395    172   -262       S  
ATOM    628  N   LEU A 237     -23.640  -4.269   8.579  1.00 48.70           N  
ANISOU  628  N   LEU A 237     4486   7680   6339   -654    291   -308       N  
ATOM    629  CA  LEU A 237     -23.963  -3.236   9.569  1.00 49.39           C  
ANISOU  629  CA  LEU A 237     4439   8011   6315   -585    402   -403       C  
ATOM    630  C   LEU A 237     -24.598  -3.823  10.803  1.00 51.46           C  
ANISOU  630  C   LEU A 237     4513   8558   6480   -812    487   -322       C  
ATOM    631  O   LEU A 237     -24.313  -3.384  11.913  1.00 51.06           O  
ANISOU  631  O   LEU A 237     4417   8671   6312   -825    586   -324       O  
ATOM    632  CB  LEU A 237     -24.867  -2.158   8.976  1.00 50.03           C  
ANISOU  632  CB  LEU A 237     4405   8187   6417   -379    373   -605       C  
ATOM    633  CG  LEU A 237     -24.152  -1.212   8.018  1.00 48.73           C  
ANISOU  633  CG  LEU A 237     4424   7785   6305   -150    295   -677       C  
ATOM    634  CD1 LEU A 237     -25.142  -0.258   7.400  1.00 50.40           C  
ANISOU  634  CD1 LEU A 237     4526   8067   6555     33    223   -861       C  
ATOM    635  CD2 LEU A 237     -23.035  -0.464   8.729  1.00 48.45           C  
ANISOU  635  CD2 LEU A 237     4509   7692   6207    -73    348   -664       C  
ATOM    636  N   GLU A 238     -25.473  -4.809  10.590  1.00 53.81           N  
ANISOU  636  N   GLU A 238     4696   8930   6820  -1002    440   -247       N  
ATOM    637  CA  GLU A 238     -26.024  -5.627  11.670  1.00 56.62           C  
ANISOU  637  CA  GLU A 238     4889   9541   7083  -1294    494   -104       C  
ATOM    638  C   GLU A 238     -24.903  -6.200  12.542  1.00 56.05           C  
ANISOU  638  C   GLU A 238     4971   9365   6961  -1444    509     87       C  
ATOM    639  O   GLU A 238     -24.906  -6.021  13.763  1.00 57.23           O  
ANISOU  639  O   GLU A 238     5019   9768   6958  -1548    617    132       O  
ATOM    640  CB  GLU A 238     -26.914  -6.739  11.081  1.00 58.56           C  
ANISOU  640  CB  GLU A 238     5051   9774   7424  -1492    388    -14       C  
ATOM    641  CG  GLU A 238     -26.713  -8.160  11.642  1.00 61.67           C  
ANISOU  641  CG  GLU A 238     5490  10110   7832  -1831    315    254       C  
ATOM    642  CD  GLU A 238     -27.680  -8.521  12.753  1.00 66.30           C  
ANISOU  642  CD  GLU A 238     5816  11102   8273  -2121    394    363       C  
ATOM    643  OE1 GLU A 238     -28.903  -8.433  12.520  1.00 69.06           O  
ANISOU  643  OE1 GLU A 238     5934  11696   8611  -2158    412    277       O  
ATOM    644  OE2 GLU A 238     -27.216  -8.913  13.851  1.00 68.55           O  
ANISOU  644  OE2 GLU A 238     6120  11478   8448  -2322    434    539       O  
ATOM    645  N   ARG A 239     -23.933  -6.846  11.892  1.00 54.47           N  
ANISOU  645  N   ARG A 239     5009   8803   6884  -1435    393    179       N  
ATOM    646  CA  ARG A 239     -22.915  -7.631  12.572  1.00 54.70           C  
ANISOU  646  CA  ARG A 239     5193   8684   6906  -1592    355    368       C  
ATOM    647  C   ARG A 239     -21.712  -6.796  13.033  1.00 52.64           C  
ANISOU  647  C   ARG A 239     5070   8352   6580  -1423    435    321       C  
ATOM    648  O   ARG A 239     -20.948  -7.236  13.894  1.00 52.66           O  
ANISOU  648  O   ARG A 239     5159   8314   6534  -1549    437    462       O  
ATOM    649  CB  ARG A 239     -22.457  -8.771  11.653  1.00 54.56           C  
ANISOU  649  CB  ARG A 239     5346   8320   7063  -1644    166    453       C  
ATOM    650  CG  ARG A 239     -22.282 -10.129  12.337  1.00 57.96           C  
ANISOU  650  CG  ARG A 239     5825   8669   7526  -1950     45    693       C  
ATOM    651  CD  ARG A 239     -21.601 -11.136  11.395  1.00 60.34           C  
ANISOU  651  CD  ARG A 239     6324   8582   8021  -1927   -172    720       C  
ATOM    652  NE  ARG A 239     -22.555 -11.896  10.582  1.00 63.29           N  
ANISOU  652  NE  ARG A 239     6627   8901   8520  -2021   -314    723       N  
ATOM    653  CZ  ARG A 239     -22.228 -12.695   9.561  1.00 64.09           C  
ANISOU  653  CZ  ARG A 239     6857   8699   8794  -1964   -514    685       C  
ATOM    654  NH1 ARG A 239     -20.958 -12.853   9.190  1.00 63.29           N  
ANISOU  654  NH1 ARG A 239     6952   8339   8757  -1808   -593    630       N  
ATOM    655  NH2 ARG A 239     -23.177 -13.342   8.900  1.00 65.34           N  
ANISOU  655  NH2 ARG A 239     6937   8829   9061  -2057   -644    686       N  
ATOM    656  N   GLY A 240     -21.545  -5.601  12.460  1.00 50.69           N  
ANISOU  656  N   GLY A 240     4846   8078   6336  -1150    482    135       N  
ATOM    657  CA  GLY A 240     -20.369  -4.769  12.733  1.00 48.90           C  
ANISOU  657  CA  GLY A 240     4762   7748   6070   -985    532     89       C  
ATOM    658  C   GLY A 240     -19.050  -5.454  12.388  1.00 46.83           C  
ANISOU  658  C   GLY A 240     4728   7176   5888   -995    444    191       C  
ATOM    659  O   GLY A 240     -18.071  -5.346  13.130  1.00 45.60           O  
ANISOU  659  O   GLY A 240     4669   6975   5681  -1001    480    249       O  
ATOM    660  N   GLU A 241     -19.040  -6.162  11.256  1.00 46.56           N  
ANISOU  660  N   GLU A 241     4767   6944   5980   -986    322    193       N  
ATOM    661  CA  GLU A 241     -17.874  -6.922  10.782  1.00 45.01           C  
ANISOU  661  CA  GLU A 241     4759   6470   5871   -976    212    246       C  
ATOM    662  C   GLU A 241     -17.849  -6.985   9.270  1.00 43.36           C  
ANISOU  662  C   GLU A 241     4607   6111   5758   -833    119    138       C  
ATOM    663  O   GLU A 241     -18.890  -6.889   8.619  1.00 43.08           O  
ANISOU  663  O   GLU A 241     4468   6147   5752   -813     99     73       O  
ATOM    664  CB  GLU A 241     -17.924  -8.362  11.305  1.00 47.37           C  
ANISOU  664  CB  GLU A 241     5077   6692   6228  -1221     96    414       C  
ATOM    665  CG  GLU A 241     -17.294  -8.624  12.672  1.00 49.47           C  
ANISOU  665  CG  GLU A 241     5385   6993   6417  -1367    128    560       C  
ATOM    666  CD  GLU A 241     -17.655 -10.015  13.195  1.00 55.21           C  
ANISOU  666  CD  GLU A 241     6106   7672   7199  -1653    -14    755       C  
ATOM    667  OE1 GLU A 241     -18.357 -10.754  12.471  1.00 57.97           O  
ANISOU  667  OE1 GLU A 241     6420   7946   7658  -1726   -139    764       O  
ATOM    668  OE2 GLU A 241     -17.251 -10.375  14.323  1.00 57.15           O  
ANISOU  668  OE2 GLU A 241     6385   7950   7380  -1816    -17    908       O  
ATOM    669  N   LEU A 242     -16.648  -7.166   8.713  1.00 41.52           N  
ANISOU  669  N   LEU A 242     4525   5687   5562   -733     58    112       N  
ATOM    670  CA  LEU A 242     -16.467  -7.362   7.274  1.00 40.66           C  
ANISOU  670  CA  LEU A 242     4470   5457   5521   -606    -39      7       C  
ATOM    671  C   LEU A 242     -17.243  -8.599   6.786  1.00 41.86           C  
ANISOU  671  C   LEU A 242     4580   5533   5790   -717   -189     23       C  
ATOM    672  O   LEU A 242     -17.226  -9.627   7.443  1.00 42.26           O  
ANISOU  672  O   LEU A 242     4646   5508   5903   -885   -277    133       O  
ATOM    673  CB  LEU A 242     -14.968  -7.520   6.979  1.00 39.88           C  
ANISOU  673  CB  LEU A 242     4514   5213   5424   -512    -79    -21       C  
ATOM    674  CG  LEU A 242     -14.454  -7.691   5.554  1.00 37.84           C  
ANISOU  674  CG  LEU A 242     4310   4873   5193   -369   -167   -144       C  
ATOM    675  CD1 LEU A 242     -13.020  -7.164   5.514  1.00 38.65           C  
ANISOU  675  CD1 LEU A 242     4507   4955   5225   -262   -117   -174       C  
ATOM    676  CD2 LEU A 242     -14.525  -9.172   5.091  1.00 41.72           C  
ANISOU  676  CD2 LEU A 242     4820   5215   5815   -422   -356   -171       C  
ATOM    677  N   VAL A 243     -17.912  -8.505   5.633  1.00 42.31           N  
ANISOU  677  N   VAL A 243     4593   5600   5884   -631   -238    -80       N  
ATOM    678  CA  VAL A 243     -18.594  -9.678   5.077  1.00 43.99           C  
ANISOU  678  CA  VAL A 243     4773   5721   6220   -721   -402    -82       C  
ATOM    679  C   VAL A 243     -18.426  -9.777   3.561  1.00 44.36           C  
ANISOU  679  C   VAL A 243     4862   5688   6306   -554   -501   -233       C  
ATOM    680  O   VAL A 243     -18.484  -8.768   2.864  1.00 43.57           O  
ANISOU  680  O   VAL A 243     4750   5677   6125   -409   -424   -318       O  
ATOM    681  CB  VAL A 243     -20.119  -9.754   5.480  1.00 45.73           C  
ANISOU  681  CB  VAL A 243     4826   6096   6454   -876   -380    -23       C  
ATOM    682  CG1 VAL A 243     -20.291  -9.925   6.999  1.00 45.89           C  
ANISOU  682  CG1 VAL A 243     4788   6227   6421  -1085   -307    139       C  
ATOM    683  CG2 VAL A 243     -20.895  -8.537   4.985  1.00 45.05           C  
ANISOU  683  CG2 VAL A 243     4641   6181   6297   -740   -272   -131       C  
ATOM    684  N   SER A 244     -18.217 -10.996   3.064  1.00 45.46           N  
ANISOU  684  N   SER A 244     5049   5659   6563   -578   -689   -267       N  
ATOM    685  CA  SER A 244     -17.984 -11.235   1.639  1.00 46.46           C  
ANISOU  685  CA  SER A 244     5208   5729   6716   -416   -800   -434       C  
ATOM    686  C   SER A 244     -19.014 -12.168   1.017  1.00 48.09           C  
ANISOU  686  C   SER A 244     5353   5863   7054   -479   -974   -473       C  
ATOM    687  O   SER A 244     -19.627 -12.965   1.716  1.00 49.69           O  
ANISOU  687  O   SER A 244     5521   5999   7362   -671  -1062   -357       O  
ATOM    688  CB  SER A 244     -16.576 -11.812   1.416  1.00 46.49           C  
ANISOU  688  CB  SER A 244     5322   5603   6738   -320   -895   -513       C  
ATOM    689  OG  SER A 244     -16.134 -12.584   2.529  1.00 48.76           O  
ANISOU  689  OG  SER A 244     5664   5757   7107   -456   -966   -399       O  
ATOM    690  N   VAL A 245     -19.205 -12.060  -0.298  1.00 48.53           N  
ANISOU  690  N   VAL A 245     5397   5944   7099   -331  -1032   -626       N  
ATOM    691  CA  VAL A 245     -19.934 -13.077  -1.057  1.00 50.56           C  
ANISOU  691  CA  VAL A 245     5618   6098   7493   -354  -1238   -704       C  
ATOM    692  C   VAL A 245     -19.070 -14.336  -1.136  1.00 51.86           C  
ANISOU  692  C   VAL A 245     5873   6050   7782   -339  -1456   -771       C  
ATOM    693  O   VAL A 245     -17.891 -14.300  -0.803  1.00 50.78           O  
ANISOU  693  O   VAL A 245     5816   5878   7602   -275  -1429   -786       O  
ATOM    694  CB  VAL A 245     -20.290 -12.622  -2.511  1.00 50.57           C  
ANISOU  694  CB  VAL A 245     5587   6196   7432   -181  -1253   -868       C  
ATOM    695  CG1 VAL A 245     -21.330 -11.499  -2.512  1.00 50.39           C  
ANISOU  695  CG1 VAL A 245     5471   6346   7329   -193  -1103   -818       C  
ATOM    696  CG2 VAL A 245     -19.028 -12.235  -3.314  1.00 48.82           C  
ANISOU  696  CG2 VAL A 245     5441   6027   7081     17  -1224  -1004       C  
ATOM    697  N   ARG A 246     -19.650 -15.447  -1.580  1.00 54.44           N  
ANISOU  697  N   ARG A 246     6184   6227   8273   -388  -1693   -824       N  
ATOM    698  CA  ARG A 246     -18.872 -16.680  -1.733  1.00 56.65           C  
ANISOU  698  CA  ARG A 246     6550   6275   8698   -347  -1954   -923       C  
ATOM    699  C   ARG A 246     -18.113 -16.684  -3.058  1.00 56.55           C  
ANISOU  699  C   ARG A 246     6556   6306   8624    -77  -2018  -1196       C  
ATOM    700  O   ARG A 246     -18.663 -16.303  -4.094  1.00 56.62           O  
ANISOU  700  O   ARG A 246     6505   6442   8566     24  -1991  -1308       O  
ATOM    701  CB  ARG A 246     -19.761 -17.919  -1.579  1.00 59.25           C  
ANISOU  701  CB  ARG A 246     6865   6396   9250   -528  -2224   -858       C  
ATOM    702  CG  ARG A 246     -20.158 -18.183  -0.124  1.00 61.55           C  
ANISOU  702  CG  ARG A 246     7154   6633   9598   -823  -2209   -575       C  
ATOM    703  CD  ARG A 246     -20.418 -19.656   0.163  1.00 66.87           C  
ANISOU  703  CD  ARG A 246     7877   7018  10514  -1004  -2556   -499       C  
ATOM    704  NE  ARG A 246     -19.194 -20.461   0.118  1.00 68.79           N  
ANISOU  704  NE  ARG A 246     8252   7019  10866   -884  -2786   -616       N  
ATOM    705  CZ  ARG A 246     -18.992 -21.488  -0.705  1.00 71.36           C  
ANISOU  705  CZ  ARG A 246     8626   7116  11372   -764  -3113   -813       C  
ATOM    706  NH1 ARG A 246     -19.938 -21.868  -1.563  1.00 72.92           N  
ANISOU  706  NH1 ARG A 246     8760   7285  11662   -762  -3252   -902       N  
ATOM    707  NH2 ARG A 246     -17.839 -22.148  -0.662  1.00 73.20           N  
ANISOU  707  NH2 ARG A 246     8965   7149  11698   -636  -3319   -940       N  
ATOM    708  N   GLN A 247     -16.847 -17.102  -3.010  1.00 56.82           N  
ANISOU  708  N   GLN A 247     6662   6259   8667     38  -2103  -1307       N  
ATOM    709  CA  GLN A 247     -15.951 -17.103  -4.178  1.00 57.00           C  
ANISOU  709  CA  GLN A 247     6680   6382   8597    296  -2149  -1582       C  
ATOM    710  C   GLN A 247     -16.596 -17.650  -5.454  1.00 58.16           C  
ANISOU  710  C   GLN A 247     6773   6526   8799    406  -2333  -1786       C  
ATOM    711  O   GLN A 247     -16.332 -17.156  -6.552  1.00 57.80           O  
ANISOU  711  O   GLN A 247     6680   6691   8589    582  -2264  -1960       O  
ATOM    712  CB  GLN A 247     -14.663 -17.880  -3.885  1.00 57.81           C  
ANISOU  712  CB  GLN A 247     6848   6343   8774    392  -2311  -1706       C  
ATOM    713  CG  GLN A 247     -14.245 -17.865  -2.421  1.00 58.79           C  
ANISOU  713  CG  GLN A 247     7046   6347   8946    229  -2253  -1482       C  
ATOM    714  CD  GLN A 247     -12.753 -17.729  -2.218  1.00 59.60           C  
ANISOU  714  CD  GLN A 247     7186   6491   8967    368  -2214  -1585       C  
ATOM    715  OE1 GLN A 247     -11.956 -18.484  -2.788  1.00 59.74           O  
ANISOU  715  OE1 GLN A 247     7207   6445   9045    548  -2419  -1835       O  
ATOM    716  NE2 GLN A 247     -12.362 -16.759  -1.385  1.00 59.52           N  
ANISOU  716  NE2 GLN A 247     7196   6598   8822    292  -1957  -1409       N  
ATOM    717  N   GLU A 248     -17.450 -18.658  -5.290  1.00 59.71           N  
ANISOU  717  N   GLU A 248     6973   6494   9219    284  -2572  -1750       N  
ATOM    718  CA  GLU A 248     -18.056 -19.380  -6.406  1.00 61.36           C  
ANISOU  718  CA  GLU A 248     7141   6644   9528    381  -2805  -1952       C  
ATOM    719  C   GLU A 248     -19.019 -18.519  -7.222  1.00 60.33           C  
ANISOU  719  C   GLU A 248     6927   6736   9261    400  -2643  -1950       C  
ATOM    720  O   GLU A 248     -19.276 -18.818  -8.386  1.00 60.86           O  
ANISOU  720  O   GLU A 248     6952   6850   9324    545  -2774  -2163       O  
ATOM    721  CB  GLU A 248     -18.766 -20.647  -5.908  1.00 63.79           C  
ANISOU  721  CB  GLU A 248     7481   6627  10127    203  -3117  -1870       C  
ATOM    722  CG  GLU A 248     -17.831 -21.774  -5.432  1.00 66.06           C  
ANISOU  722  CG  GLU A 248     7865   6633  10602    232  -3408  -1947       C  
ATOM    723  CD  GLU A 248     -17.191 -21.505  -4.079  1.00 66.27           C  
ANISOU  723  CD  GLU A 248     7961   6617  10603     89  -3275  -1717       C  
ATOM    724  OE1 GLU A 248     -17.578 -20.522  -3.404  1.00 65.16           O  
ANISOU  724  OE1 GLU A 248     7791   6648  10320    -60  -2972  -1483       O  
ATOM    725  OE2 GLU A 248     -16.285 -22.280  -3.685  1.00 68.45           O  
ANISOU  725  OE2 GLU A 248     8319   6684  11004    137  -3491  -1786       O  
ATOM    726  N   LEU A 249     -19.544 -17.454  -6.610  1.00 58.54           N  
ANISOU  726  N   LEU A 249     6673   6646   8923    267  -2375  -1725       N  
ATOM    727  CA  LEU A 249     -20.429 -16.513  -7.312  1.00 57.83           C  
ANISOU  727  CA  LEU A 249     6508   6761   8702    293  -2225  -1715       C  
ATOM    728  C   LEU A 249     -19.647 -15.761  -8.385  1.00 56.54           C  
ANISOU  728  C   LEU A 249     6343   6831   8308    511  -2118  -1883       C  
ATOM    729  O   LEU A 249     -20.133 -15.546  -9.497  1.00 56.42           O  
ANISOU  729  O   LEU A 249     6281   6940   8217    610  -2148  -2004       O  
ATOM    730  CB  LEU A 249     -21.057 -15.523  -6.324  1.00 56.49           C  
ANISOU  730  CB  LEU A 249     6308   6684   8474    125  -1984  -1464       C  
ATOM    731  CG  LEU A 249     -22.139 -16.096  -5.403  1.00 58.41           C  
ANISOU  731  CG  LEU A 249     6502   6797   8893   -119  -2056  -1286       C  
ATOM    732  CD1 LEU A 249     -22.000 -15.536  -3.996  1.00 56.81           C  
ANISOU  732  CD1 LEU A 249     6304   6639   8642   -277  -1861  -1062       C  
ATOM    733  CD2 LEU A 249     -23.538 -15.848  -5.963  1.00 58.31           C  
ANISOU  733  CD2 LEU A 249     6382   6872   8902   -158  -2061  -1290       C  
ATOM    734  N   LEU A 250     -18.427 -15.379  -8.026  1.00 54.97           N  
ANISOU  734  N   LEU A 250     6191   6702   7992    568  -2000  -1879       N  
ATOM    735  CA  LEU A 250     -17.495 -14.724  -8.937  1.00 54.81           C  
ANISOU  735  CA  LEU A 250     6162   6926   7737    743  -1900  -2019       C  
ATOM    736  C   LEU A 250     -16.984 -15.686 -10.020  1.00 56.91           C  
ANISOU  736  C   LEU A 250     6398   7214   8011    932  -2121  -2325       C  
ATOM    737  O   LEU A 250     -16.944 -15.326 -11.203  1.00 57.05           O  
ANISOU  737  O   LEU A 250     6364   7458   7852   1059  -2105  -2469       O  
ATOM    738  CB  LEU A 250     -16.333 -14.109  -8.140  1.00 53.28           C  
ANISOU  738  CB  LEU A 250     6016   6794   7434    729  -1724  -1920       C  
ATOM    739  CG  LEU A 250     -16.571 -12.724  -7.509  1.00 51.15           C  
ANISOU  739  CG  LEU A 250     5762   6629   7045    621  -1468  -1683       C  
ATOM    740  CD1 LEU A 250     -17.952 -12.581  -6.857  1.00 50.16           C  
ANISOU  740  CD1 LEU A 250     5614   6398   7047    465  -1446  -1514       C  
ATOM    741  CD2 LEU A 250     -15.451 -12.347  -6.506  1.00 50.27           C  
ANISOU  741  CD2 LEU A 250     5704   6513   6882    587  -1335  -1583       C  
ATOM    742  N   GLU A 251     -16.620 -16.905  -9.606  1.00 58.43           N  
ANISOU  742  N   GLU A 251     6621   7173   8408    949  -2345  -2428       N  
ATOM    743  CA  GLU A 251     -16.172 -17.971 -10.514  1.00 60.88           C  
ANISOU  743  CA  GLU A 251     6899   7457   8776   1145  -2612  -2755       C  
ATOM    744  C   GLU A 251     -17.237 -18.324 -11.564  1.00 62.75           C  
ANISOU  744  C   GLU A 251     7081   7702   9057   1194  -2764  -2884       C  
ATOM    745  O   GLU A 251     -16.916 -18.617 -12.723  1.00 63.44           O  
ANISOU  745  O   GLU A 251     7109   7950   9045   1394  -2874  -3167       O  
ATOM    746  CB  GLU A 251     -15.819 -19.242  -9.727  1.00 62.15           C  
ANISOU  746  CB  GLU A 251     7120   7282   9211   1122  -2879  -2803       C  
ATOM    747  CG  GLU A 251     -14.696 -19.109  -8.711  1.00 61.84           C  
ANISOU  747  CG  GLU A 251     7137   7201   9156   1096  -2789  -2716       C  
ATOM    748  CD  GLU A 251     -14.576 -20.331  -7.797  1.00 64.19           C  
ANISOU  748  CD  GLU A 251     7517   7121   9752   1018  -3076  -2691       C  
ATOM    749  OE1 GLU A 251     -15.324 -21.312  -7.986  1.00 66.47           O  
ANISOU  749  OE1 GLU A 251     7819   7173  10264    984  -3362  -2747       O  
ATOM    750  OE2 GLU A 251     -13.732 -20.310  -6.879  1.00 64.45           O  
ANISOU  750  OE2 GLU A 251     7607   7083   9799    981  -3032  -2605       O  
ATOM    751  N   ARG A 252     -18.500 -18.308 -11.143  1.00 63.23           N  
ANISOU  751  N   ARG A 252     7151   7612   9260   1012  -2772  -2685       N  
ATOM    752  CA  ARG A 252     -19.610 -18.588 -12.045  1.00 65.57           C  
ANISOU  752  CA  ARG A 252     7395   7905   9612   1035  -2908  -2777       C  
ATOM    753  C   ARG A 252     -19.920 -17.393 -12.946  1.00 64.88           C  
ANISOU  753  C   ARG A 252     7256   8135   9259   1096  -2698  -2767       C  
ATOM    754  O   ARG A 252     -20.549 -17.553 -13.990  1.00 65.77           O  
ANISOU  754  O   ARG A 252     7319   8322   9347   1181  -2808  -2913       O  
ATOM    755  CB  ARG A 252     -20.865 -19.035 -11.271  1.00 66.24           C  
ANISOU  755  CB  ARG A 252     7487   7736   9945    804  -3003  -2570       C  
ATOM    756  CG  ARG A 252     -20.761 -20.393 -10.552  1.00 69.00           C  
ANISOU  756  CG  ARG A 252     7892   7737  10587    716  -3298  -2573       C  
ATOM    757  CD  ARG A 252     -20.459 -21.537 -11.509  1.00 74.60           C  
ANISOU  757  CD  ARG A 252     8598   8330  11418    917  -3644  -2910       C  
ATOM    758  NE  ARG A 252     -19.021 -21.697 -11.729  1.00 77.14           N  
ANISOU  758  NE  ARG A 252     8938   8730  11642   1132  -3672  -3135       N  
ATOM    759  CZ  ARG A 252     -18.329 -22.802 -11.460  1.00 79.90           C  
ANISOU  759  CZ  ARG A 252     9338   8834  12187   1207  -3965  -3290       C  
ATOM    760  NH1 ARG A 252     -18.938 -23.875 -10.969  1.00 82.41           N  
ANISOU  760  NH1 ARG A 252     9710   8784  12818   1067  -4277  -3223       N  
ATOM    761  NH2 ARG A 252     -17.022 -22.837 -11.696  1.00 81.18           N  
ANISOU  761  NH2 ARG A 252     9491   9121  12233   1420  -3963  -3516       N  
ATOM    762  N   GLY A 253     -19.457 -16.209 -12.544  1.00 63.36           N  
ANISOU  762  N   GLY A 253     7084   8117   8873   1050  -2420  -2595       N  
ATOM    763  CA  GLY A 253     -19.697 -14.973 -13.294  1.00 63.41           C  
ANISOU  763  CA  GLY A 253     7062   8398   8631   1081  -2236  -2541       C  
ATOM    764  C   GLY A 253     -21.077 -14.395 -13.019  1.00 63.50           C  
ANISOU  764  C   GLY A 253     7059   8353   8716    942  -2172  -2347       C  
ATOM    765  O   GLY A 253     -21.648 -13.692 -13.859  1.00 63.33           O  
ANISOU  765  O   GLY A 253     7008   8493   8562    981  -2132  -2351       O  
ATOM    766  N   GLU A 254     -21.602 -14.683 -11.831  1.00 63.77           N  
ANISOU  766  N   GLU A 254     7104   8177   8950    775  -2169  -2180       N  
ATOM    767  CA  GLU A 254     -22.989 -14.369 -11.497  1.00 64.54           C  
ANISOU  767  CA  GLU A 254     7151   8224   9146    640  -2141  -2033       C  
ATOM    768  C   GLU A 254     -23.205 -12.999 -10.855  1.00 63.30           C  
ANISOU  768  C   GLU A 254     6994   8183   8874    564  -1895  -1828       C  
ATOM    769  O   GLU A 254     -24.315 -12.703 -10.420  1.00 62.49           O  
ANISOU  769  O   GLU A 254     6831   8059   8853    456  -1860  -1717       O  
ATOM    770  CB  GLU A 254     -23.578 -15.468 -10.602  1.00 65.64           C  
ANISOU  770  CB  GLU A 254     7275   8111   9553    475  -2291  -1963       C  
ATOM    771  CG  GLU A 254     -24.290 -16.582 -11.375  1.00 68.18           C  
ANISOU  771  CG  GLU A 254     7558   8304  10043    502  -2569  -2124       C  
ATOM    772  CD  GLU A 254     -24.167 -17.941 -10.704  1.00 70.99           C  
ANISOU  772  CD  GLU A 254     7946   8379  10649    395  -2800  -2120       C  
ATOM    773  OE1 GLU A 254     -23.623 -18.019  -9.576  1.00 71.52           O  
ANISOU  773  OE1 GLU A 254     8062   8356  10757    279  -2734  -1969       O  
ATOM    774  OE2 GLU A 254     -24.599 -18.939 -11.316  1.00 73.44           O  
ANISOU  774  OE2 GLU A 254     8239   8546  11117    425  -3070  -2267       O  
ATOM    775  N   GLN A 255     -22.159 -12.170 -10.808  1.00 63.06           N  
ANISOU  775  N   GLN A 255     7020   8283   8658    624  -1739  -1791       N  
ATOM    776  CA  GLN A 255     -22.239 -10.875 -10.112  1.00 62.59           C  
ANISOU  776  CA  GLN A 255     6974   8301   8507    561  -1534  -1605       C  
ATOM    777  C   GLN A 255     -23.090  -9.796 -10.823  1.00 63.02           C  
ANISOU  777  C   GLN A 255     6998   8486   8460    601  -1497  -1577       C  
ATOM    778  O   GLN A 255     -23.810  -9.055 -10.153  1.00 62.78           O  
ANISOU  778  O   GLN A 255     6936   8452   8466    531  -1410  -1455       O  
ATOM    779  CB  GLN A 255     -20.840 -10.362  -9.739  1.00 61.68           C  
ANISOU  779  CB  GLN A 255     6932   8255   8249    590  -1401  -1558       C  
ATOM    780  CG  GLN A 255     -20.105  -9.593 -10.828  1.00 63.01           C  
ANISOU  780  CG  GLN A 255     7129   8636   8176    705  -1357  -1614       C  
ATOM    781  CD  GLN A 255     -18.714 -10.136 -11.111  1.00 65.30           C  
ANISOU  781  CD  GLN A 255     7441   8998   8372    786  -1376  -1739       C  
ATOM    782  OE1 GLN A 255     -18.073 -10.743 -10.247  1.00 65.11           O  
ANISOU  782  OE1 GLN A 255     7439   8852   8446    756  -1375  -1738       O  
ATOM    783  NE2 GLN A 255     -18.241  -9.922 -12.338  1.00 66.61           N  
ANISOU  783  NE2 GLN A 255     7590   9382   8336    891  -1401  -1856       N  
ATOM    784  N   ARG A 256     -23.013  -9.726 -12.156  1.00 64.30           N  
ANISOU  784  N   ARG A 256     7165   8771   8496    716  -1580  -1699       N  
ATOM    785  CA  ARG A 256     -23.781  -8.762 -12.974  1.00 65.22           C  
ANISOU  785  CA  ARG A 256     7268   9003   8511    759  -1588  -1677       C  
ATOM    786  C   ARG A 256     -25.287  -9.050 -12.945  1.00 66.08           C  
ANISOU  786  C   ARG A 256     7288   9024   8794    718  -1681  -1695       C  
ATOM    787  O   ARG A 256     -26.088  -8.162 -12.631  1.00 65.76           O  
ANISOU  787  O   ARG A 256     7216   8999   8772    690  -1629  -1603       O  
ATOM    788  CB  ARG A 256     -23.264  -8.735 -14.426  1.00 66.48           C  
ANISOU  788  CB  ARG A 256     7448   9342   8468    877  -1664  -1802       C  
ATOM    789  CG  ARG A 256     -22.144  -7.722 -14.704  1.00 67.08           C  
ANISOU  789  CG  ARG A 256     7594   9598   8294    894  -1549  -1715       C  
ATOM    790  CD  ARG A 256     -22.614  -6.551 -15.576  1.00 69.14           C  
ANISOU  790  CD  ARG A 256     7882   9993   8396    909  -1569  -1633       C  
ATOM    791  NE  ARG A 256     -23.764  -5.833 -15.019  1.00 70.33           N  
ANISOU  791  NE  ARG A 256     8022  10018   8682    866  -1567  -1522       N  
ATOM    792  CZ  ARG A 256     -23.685  -4.784 -14.202  1.00 69.82           C  
ANISOU  792  CZ  ARG A 256     8001   9907   8622    814  -1470  -1363       C  
ATOM    793  NH1 ARG A 256     -22.506  -4.305 -13.821  1.00 70.15           N  
ANISOU  793  NH1 ARG A 256     8110   9998   8545    780  -1362  -1268       N  
ATOM    794  NH2 ARG A 256     -24.794  -4.207 -13.760  1.00 70.01           N  
ANISOU  794  NH2 ARG A 256     7990   9839   8773    805  -1492  -1315       N  
ATOM    795  N   ALA A 257     -25.669 -10.282 -13.297  1.00 67.21           N  
ANISOU  795  N   ALA A 257     7386   9082   9070    723  -1837  -1827       N  
ATOM    796  CA  ALA A 257     -26.987 -10.809 -12.941  1.00 67.94           C  
ANISOU  796  CA  ALA A 257     7381   9064   9368    632  -1922  -1821       C  
ATOM    797  C   ALA A 257     -26.939 -10.919 -11.419  1.00 67.09           C  
ANISOU  797  C   ALA A 257     7255   8862   9375    480  -1811  -1674       C  
ATOM    798  O   ALA A 257     -25.846 -10.918 -10.856  1.00 66.09           O  
ANISOU  798  O   ALA A 257     7201   8715   9195    471  -1724  -1625       O  
ATOM    799  CB  ALA A 257     -27.205 -12.172 -13.577  1.00 69.45           C  
ANISOU  799  CB  ALA A 257     7545   9157   9686    655  -2135  -1985       C  
ATOM    800  N   HIS A 258     -28.083 -10.984 -10.734  1.00 67.38           N  
ANISOU  800  N   HIS A 258     7185   8868   9550    357  -1806  -1603       N  
ATOM    801  CA  HIS A 258     -28.047 -11.065  -9.261  1.00 66.36           C  
ANISOU  801  CA  HIS A 258     7023   8696   9495    198  -1693  -1456       C  
ATOM    802  C   HIS A 258     -27.620  -9.691  -8.692  1.00 64.20           C  
ANISOU  802  C   HIS A 258     6782   8532   9078    239  -1494  -1362       C  
ATOM    803  O   HIS A 258     -27.810  -9.401  -7.504  1.00 63.90           O  
ANISOU  803  O   HIS A 258     6692   8520   9068    132  -1377  -1253       O  
ATOM    804  CB  HIS A 258     -27.115 -12.237  -8.855  1.00 66.79           C  
ANISOU  804  CB  HIS A 258     7152   8596   9630    135  -1770  -1452       C  
ATOM    805  CG  HIS A 258     -26.898 -12.416  -7.381  1.00 67.55           C  
ANISOU  805  CG  HIS A 258     7239   8644   9784    -36  -1673  -1290       C  
ATOM    806  ND1 HIS A 258     -25.831 -13.138  -6.884  1.00 69.02           N  
ANISOU  806  ND1 HIS A 258     7519   8701  10005    -72  -1711  -1264       N  
ATOM    807  CD2 HIS A 258     -27.597 -11.990  -6.302  1.00 68.27           C  
ANISOU  807  CD2 HIS A 258     7231   8814   9893   -179  -1550  -1156       C  
ATOM    808  CE1 HIS A 258     -25.883 -13.148  -5.564  1.00 68.99           C  
ANISOU  808  CE1 HIS A 258     7488   8688  10037   -241  -1616  -1099       C  
ATOM    809  NE2 HIS A 258     -26.945 -12.458  -5.185  1.00 69.35           N  
ANISOU  809  NE2 HIS A 258     7410   8875  10063   -311  -1510  -1034       N  
ATOM    810  N   SER A 259     -27.070  -8.849  -9.570  1.00 62.55           N  
ANISOU  810  N   SER A 259     6657   8398   8712    387  -1475  -1406       N  
ATOM    811  CA  SER A 259     -26.628  -7.479  -9.259  1.00 60.53           C  
ANISOU  811  CA  SER A 259     6454   8223   8322    439  -1337  -1323       C  
ATOM    812  C   SER A 259     -26.060  -7.282  -7.836  1.00 58.48           C  
ANISOU  812  C   SER A 259     6206   7940   8073    348  -1188  -1206       C  
ATOM    813  O   SER A 259     -26.514  -6.416  -7.086  1.00 58.10           O  
ANISOU  813  O   SER A 259     6105   7946   8023    330  -1097  -1147       O  
ATOM    814  CB  SER A 259     -27.757  -6.480  -9.542  1.00 61.02           C  
ANISOU  814  CB  SER A 259     6443   8360   8381    492  -1356  -1335       C  
ATOM    815  OG  SER A 259     -27.249  -5.159  -9.622  1.00 60.94           O  
ANISOU  815  OG  SER A 259     6516   8399   8238    571  -1295  -1275       O  
ATOM    816  N   ALA A 260     -25.063  -8.084  -7.480  1.00 56.58           N  
ANISOU  816  N   ALA A 260     6031   7623   7843    303  -1178  -1189       N  
ATOM    817  CA  ALA A 260     -24.559  -8.111  -6.111  1.00 54.84           C  
ANISOU  817  CA  ALA A 260     5821   7368   7647    199  -1060  -1078       C  
ATOM    818  C   ALA A 260     -23.241  -7.353  -5.925  1.00 52.78           C  
ANISOU  818  C   ALA A 260     5675   7134   7247    262   -951  -1029       C  
ATOM    819  O   ALA A 260     -22.525  -7.067  -6.892  1.00 52.25           O  
ANISOU  819  O   ALA A 260     5682   7109   7062    365   -978  -1081       O  
ATOM    820  CB  ALA A 260     -24.412  -9.557  -5.640  1.00 55.72           C  
ANISOU  820  CB  ALA A 260     5927   7352   7893     80  -1148  -1069       C  
ATOM    821  N   LEU A 261     -22.931  -7.030  -4.670  1.00 50.91           N  
ANISOU  821  N   LEU A 261     5440   6891   7013    187   -830   -927       N  
ATOM    822  CA  LEU A 261     -21.616  -6.504  -4.317  1.00 48.68           C  
ANISOU  822  CA  LEU A 261     5262   6611   6625    220   -734   -873       C  
ATOM    823  C   LEU A 261     -20.648  -7.669  -4.202  1.00 48.34           C  
ANISOU  823  C   LEU A 261     5274   6473   6618    188   -783   -896       C  
ATOM    824  O   LEU A 261     -21.027  -8.806  -4.475  1.00 49.60           O  
ANISOU  824  O   LEU A 261     5403   6554   6889    152   -910   -956       O  
ATOM    825  CB  LEU A 261     -21.671  -5.749  -2.993  1.00 47.78           C  
ANISOU  825  CB  LEU A 261     5124   6526   6505    162   -601   -774       C  
ATOM    826  CG  LEU A 261     -22.343  -4.378  -3.028  1.00 46.88           C  
ANISOU  826  CG  LEU A 261     4972   6494   6344    234   -566   -774       C  
ATOM    827  CD1 LEU A 261     -22.713  -3.961  -1.624  1.00 45.01           C  
ANISOU  827  CD1 LEU A 261     4660   6307   6135    171   -461   -723       C  
ATOM    828  CD2 LEU A 261     -21.441  -3.354  -3.711  1.00 45.57           C  
ANISOU  828  CD2 LEU A 261     4924   6340   6050    335   -563   -755       C  
ATOM    829  N   GLN A 262     -19.407  -7.380  -3.816  1.00 46.28           N  
ANISOU  829  N   GLN A 262     5096   6213   6276    209   -704   -857       N  
ATOM    830  CA  GLN A 262     -18.417  -8.422  -3.537  1.00 45.68           C  
ANISOU  830  CA  GLN A 262     5070   6043   6244    190   -755   -887       C  
ATOM    831  C   GLN A 262     -18.023  -8.493  -2.046  1.00 44.03           C  
ANISOU  831  C   GLN A 262     4882   5768   6078     79   -669   -763       C  
ATOM    832  O   GLN A 262     -17.921  -9.585  -1.496  1.00 44.50           O  
ANISOU  832  O   GLN A 262     4949   5706   6252     -6   -755   -747       O  
ATOM    833  CB  GLN A 262     -17.178  -8.251  -4.424  1.00 45.65           C  
ANISOU  833  CB  GLN A 262     5127   6115   6103    311   -759   -976       C  
ATOM    834  CG  GLN A 262     -17.364  -8.665  -5.888  1.00 46.62           C  
ANISOU  834  CG  GLN A 262     5223   6304   6185    414   -884  -1131       C  
ATOM    835  CD  GLN A 262     -16.120  -8.394  -6.726  1.00 46.87           C  
ANISOU  835  CD  GLN A 262     5286   6485   6036    518   -864  -1215       C  
ATOM    836  OE1 GLN A 262     -15.083  -7.984  -6.203  1.00 45.03           O  
ANISOU  836  OE1 GLN A 262     5095   6287   5729    509   -767  -1159       O  
ATOM    837  NE2 GLN A 262     -16.220  -8.625  -8.036  1.00 47.78           N  
ANISOU  837  NE2 GLN A 262     5368   6715   6070    610   -957  -1354       N  
ATOM    838  N   VAL A 263     -17.800  -7.339  -1.402  1.00 42.19           N  
ANISOU  838  N   VAL A 263     4665   5609   5756     79   -523   -675       N  
ATOM    839  CA  VAL A 263     -17.514  -7.278   0.058  1.00 40.72           C  
ANISOU  839  CA  VAL A 263     4489   5393   5590    -23   -430   -561       C  
ATOM    840  C   VAL A 263     -17.945  -5.928   0.683  1.00 39.53           C  
ANISOU  840  C   VAL A 263     4304   5345   5371    -16   -299   -499       C  
ATOM    841  O   VAL A 263     -17.961  -4.895   0.003  1.00 38.81           O  
ANISOU  841  O   VAL A 263     4229   5316   5201     83   -280   -528       O  
ATOM    842  CB  VAL A 263     -16.007  -7.641   0.391  1.00 40.78           C  
ANISOU  842  CB  VAL A 263     4592   5334   5570     -5   -425   -557       C  
ATOM    843  CG1 VAL A 263     -15.050  -6.868  -0.475  1.00 41.19           C  
ANISOU  843  CG1 VAL A 263     4696   5467   5486    121   -386   -614       C  
ATOM    844  CG2 VAL A 263     -15.653  -7.442   1.870  1.00 39.97           C  
ANISOU  844  CG2 VAL A 263     4509   5212   5467   -100   -326   -436       C  
ATOM    845  N   CYS A 264     -18.313  -5.965   1.963  1.00 38.50           N  
ANISOU  845  N   CYS A 264     4121   5236   5269   -125   -230   -418       N  
ATOM    846  CA  CYS A 264     -18.692  -4.771   2.737  1.00 38.21           C  
ANISOU  846  CA  CYS A 264     4036   5308   5175   -107   -118   -391       C  
ATOM    847  C   CYS A 264     -17.832  -4.697   3.987  1.00 36.82           C  
ANISOU  847  C   CYS A 264     3907   5123   4962   -167    -29   -308       C  
ATOM    848  O   CYS A 264     -17.698  -5.679   4.713  1.00 37.63           O  
ANISOU  848  O   CYS A 264     4006   5184   5108   -295    -43   -240       O  
ATOM    849  CB  CYS A 264     -20.189  -4.780   3.111  1.00 39.24           C  
ANISOU  849  CB  CYS A 264     4009   5552   5349   -173   -111   -405       C  
ATOM    850  SG  CYS A 264     -21.262  -4.220   1.769  1.00 41.51           S  
ANISOU  850  SG  CYS A 264     4235   5882   5656    -52   -193   -519       S  
ATOM    851  N   VAL A 265     -17.217  -3.540   4.220  1.00 35.10           N  
ANISOU  851  N   VAL A 265     3741   4930   4666    -80     42   -307       N  
ATOM    852  CA  VAL A 265     -16.342  -3.375   5.374  1.00 33.25           C  
ANISOU  852  CA  VAL A 265     3556   4687   4390   -121    122   -239       C  
ATOM    853  C   VAL A 265     -16.788  -2.198   6.251  1.00 33.18           C  
ANISOU  853  C   VAL A 265     3484   4789   4332    -83    204   -254       C  
ATOM    854  O   VAL A 265     -16.806  -1.043   5.793  1.00 31.91           O  
ANISOU  854  O   VAL A 265     3346   4634   4145     38    190   -304       O  
ATOM    855  CB  VAL A 265     -14.860  -3.198   4.931  1.00 32.46           C  
ANISOU  855  CB  VAL A 265     3589   4500   4245    -55    116   -230       C  
ATOM    856  CG1 VAL A 265     -13.939  -3.203   6.135  1.00 31.12           C  
ANISOU  856  CG1 VAL A 265     3470   4308   4047   -106    185   -162       C  
ATOM    857  CG2 VAL A 265     -14.448  -4.316   3.925  1.00 30.86           C  
ANISOU  857  CG2 VAL A 265     3424   4219   4081    -52     17   -271       C  
ATOM    858  N   PRO A 266     -17.123  -2.479   7.519  1.00 32.67           N  
ANISOU  858  N   PRO A 266     3342   4819   4253   -187    272   -212       N  
ATOM    859  CA  PRO A 266     -17.529  -1.379   8.374  1.00 33.11           C  
ANISOU  859  CA  PRO A 266     3319   5008   4252   -129    342   -263       C  
ATOM    860  C   PRO A 266     -16.321  -0.711   9.033  1.00 32.08           C  
ANISOU  860  C   PRO A 266     3297   4824   4068    -82    389   -233       C  
ATOM    861  O   PRO A 266     -15.337  -1.391   9.358  1.00 31.31           O  
ANISOU  861  O   PRO A 266     3289   4643   3964   -157    403   -147       O  
ATOM    862  CB  PRO A 266     -18.399  -2.073   9.430  1.00 34.11           C  
ANISOU  862  CB  PRO A 266     3296   5308   4357   -283    399   -228       C  
ATOM    863  CG  PRO A 266     -17.749  -3.444   9.579  1.00 34.48           C  
ANISOU  863  CG  PRO A 266     3425   5239   4437   -442    366    -95       C  
ATOM    864  CD  PRO A 266     -17.101  -3.767   8.242  1.00 33.57           C  
ANISOU  864  CD  PRO A 266     3436   4927   4390   -363    270   -115       C  
ATOM    865  N   LEU A 267     -16.392   0.611   9.206  1.00 31.60           N  
ANISOU  865  N   LEU A 267     3228   4797   3982     47    390   -312       N  
ATOM    866  CA  LEU A 267     -15.359   1.368   9.906  1.00 30.82           C  
ANISOU  866  CA  LEU A 267     3216   4654   3840     94    421   -295       C  
ATOM    867  C   LEU A 267     -15.804   1.586  11.337  1.00 32.50           C  
ANISOU  867  C   LEU A 267     3314   5041   3994     70    500   -338       C  
ATOM    868  O   LEU A 267     -16.601   2.480  11.646  1.00 33.09           O  
ANISOU  868  O   LEU A 267     3281   5233   4057    174    489   -465       O  
ATOM    869  CB  LEU A 267     -15.081   2.715   9.206  1.00 30.63           C  
ANISOU  869  CB  LEU A 267     3270   4535   3834    243    335   -346       C  
ATOM    870  CG  LEU A 267     -14.225   2.713   7.927  1.00 28.11           C  
ANISOU  870  CG  LEU A 267     3086   4071   3523    251    268   -277       C  
ATOM    871  CD1 LEU A 267     -14.981   2.131   6.719  1.00 28.32           C  
ANISOU  871  CD1 LEU A 267     3077   4100   3583    245    212   -295       C  
ATOM    872  CD2 LEU A 267     -13.789   4.166   7.625  1.00 28.98           C  
ANISOU  872  CD2 LEU A 267     3281   4096   3633    354    179   -285       C  
ATOM    873  N   VAL A 268     -15.279   0.751  12.220  1.00 33.61           N  
ANISOU  873  N   VAL A 268     3470   5211   4090    -63    569   -240       N  
ATOM    874  CA  VAL A 268     -15.739   0.724  13.600  1.00 35.23           C  
ANISOU  874  CA  VAL A 268     3549   5629   4207   -131    653   -256       C  
ATOM    875  C   VAL A 268     -14.595   1.125  14.500  1.00 34.73           C  
ANISOU  875  C   VAL A 268     3581   5523   4090   -114    690   -223       C  
ATOM    876  O   VAL A 268     -13.488   0.594  14.363  1.00 33.75           O  
ANISOU  876  O   VAL A 268     3599   5237   3989   -167    677   -115       O  
ATOM    877  CB  VAL A 268     -16.251  -0.686  13.967  1.00 36.32           C  
ANISOU  877  CB  VAL A 268     3611   5863   4326   -345    683   -140       C  
ATOM    878  CG1 VAL A 268     -16.860  -0.687  15.362  1.00 37.12           C  
ANISOU  878  CG1 VAL A 268     3551   6252   4301   -442    776   -148       C  
ATOM    879  CG2 VAL A 268     -17.275  -1.166  12.933  1.00 35.95           C  
ANISOU  879  CG2 VAL A 268     3488   5818   4353   -367    627   -165       C  
ATOM    880  N   ASP A 269     -14.854   2.063  15.413  1.00 35.65           N  
ANISOU  880  N   ASP A 269     3613   5793   4139    -27    726   -335       N  
ATOM    881  CA  ASP A 269     -13.830   2.513  16.346  1.00 35.27           C  
ANISOU  881  CA  ASP A 269     3645   5720   4037     -3    754   -320       C  
ATOM    882  C   ASP A 269     -13.677   1.566  17.553  1.00 36.68           C  
ANISOU  882  C   ASP A 269     3783   6045   4109   -185    841   -209       C  
ATOM    883  O   ASP A 269     -14.378   0.537  17.642  1.00 37.33           O  
ANISOU  883  O   ASP A 269     3777   6242   4164   -348    869   -127       O  
ATOM    884  CB  ASP A 269     -14.065   3.990  16.753  1.00 36.41           C  
ANISOU  884  CB  ASP A 269     3734   5932   4167    192    719   -507       C  
ATOM    885  CG  ASP A 269     -15.255   4.186  17.694  1.00 40.10           C  
ANISOU  885  CG  ASP A 269     3975   6729   4534    209    778   -652       C  
ATOM    886  OD1 ASP A 269     -15.788   3.195  18.232  1.00 41.70           O  
ANISOU  886  OD1 ASP A 269     4063   7135   4646     35    869   -575       O  
ATOM    887  OD2 ASP A 269     -15.651   5.359  17.914  1.00 42.68           O  
ANISOU  887  OD2 ASP A 269     4228   7123   4867    397    720   -851       O  
ATOM    888  N   THR A 270     -12.766   1.900  18.474  1.00 36.33           N  
ANISOU  888  N   THR A 270     3805   5993   4004   -171    868   -194       N  
ATOM    889  CA  THR A 270     -12.473   1.024  19.607  1.00 37.81           C  
ANISOU  889  CA  THR A 270     3982   6296   4087   -350    930    -66       C  
ATOM    890  C   THR A 270     -13.669   0.871  20.572  1.00 40.22           C  
ANISOU  890  C   THR A 270     4069   6969   4246   -447   1012   -107       C  
ATOM    891  O   THR A 270     -13.696  -0.062  21.374  1.00 41.48           O  
ANISOU  891  O   THR A 270     4196   7255   4307   -654   1051     39       O  
ATOM    892  CB  THR A 270     -11.185   1.445  20.372  1.00 36.65           C  
ANISOU  892  CB  THR A 270     3959   6059   3907   -307    933    -46       C  
ATOM    893  OG1 THR A 270     -11.205   2.858  20.605  1.00 37.52           O  
ANISOU  893  OG1 THR A 270     4036   6214   4006   -110    922   -227       O  
ATOM    894  CG2 THR A 270      -9.936   1.114  19.552  1.00 35.36           C  
ANISOU  894  CG2 THR A 270     3990   5584   3860   -298    866     50       C  
ATOM    895  N   ASP A 271     -14.656   1.767  20.469  1.00 41.93           N  
ANISOU  895  N   ASP A 271     4127   7363   4443   -304   1023   -304       N  
ATOM    896  CA  ASP A 271     -15.918   1.651  21.224  1.00 44.94           C  
ANISOU  896  CA  ASP A 271     4255   8143   4677   -382   1103   -379       C  
ATOM    897  C   ASP A 271     -16.974   0.762  20.570  1.00 45.30           C  
ANISOU  897  C   ASP A 271     4192   8267   4754   -528   1103   -307       C  
ATOM    898  O   ASP A 271     -18.018   0.502  21.170  1.00 47.39           O  
ANISOU  898  O   ASP A 271     4233   8885   4887   -640   1174   -335       O  
ATOM    899  CB  ASP A 271     -16.568   3.026  21.451  1.00 46.78           C  
ANISOU  899  CB  ASP A 271     4335   8561   4878   -137   1096   -669       C  
ATOM    900  CG  ASP A 271     -15.677   3.996  22.196  1.00 48.39           C  
ANISOU  900  CG  ASP A 271     4616   8721   5048     18   1078   -774       C  
ATOM    901  OD1 ASP A 271     -14.792   3.561  22.967  1.00 50.72           O  
ANISOU  901  OD1 ASP A 271     5006   8998   5267    -99   1121   -636       O  
ATOM    902  OD2 ASP A 271     -15.882   5.213  22.008  1.00 52.13           O  
ANISOU  902  OD2 ASP A 271     5056   9168   5581    261    999  -1001       O  
ATOM    903  N   GLY A 272     -16.742   0.328  19.339  1.00 43.09           N  
ANISOU  903  N   GLY A 272     4050   7687   4636   -525   1022   -228       N  
ATOM    904  CA  GLY A 272     -17.759  -0.432  18.617  1.00 43.44           C  
ANISOU  904  CA  GLY A 272     3996   7778   4730   -636   1000   -184       C  
ATOM    905  C   GLY A 272     -18.781   0.465  17.941  1.00 43.59           C  
ANISOU  905  C   GLY A 272     3877   7889   4796   -446    977   -403       C  
ATOM    906  O   GLY A 272     -19.830   0.011  17.508  1.00 44.53           O  
ANISOU  906  O   GLY A 272     3858   8129   4931   -521    972   -411       O  
ATOM    907  N   ARG A 273     -18.452   1.747  17.850  1.00 43.23           N  
ANISOU  907  N   ARG A 273     3874   7769   4782   -201    940   -577       N  
ATOM    908  CA  ARG A 273     -19.227   2.718  17.086  1.00 43.46           C  
ANISOU  908  CA  ARG A 273     3825   7795   4891     13    864   -785       C  
ATOM    909  C   ARG A 273     -18.930   2.586  15.595  1.00 41.29           C  
ANISOU  909  C   ARG A 273     3720   7190   4777     57    760   -716       C  
ATOM    910  O   ARG A 273     -17.763   2.665  15.173  1.00 38.17           O  
ANISOU  910  O   ARG A 273     3538   6523   4443     82    717   -621       O  
ATOM    911  CB  ARG A 273     -18.895   4.129  17.589  1.00 44.43           C  
ANISOU  911  CB  ARG A 273     3954   7924   5003    248    820   -982       C  
ATOM    912  CG  ARG A 273     -19.478   5.266  16.779  1.00 47.66           C  
ANISOU  912  CG  ARG A 273     4335   8247   5526    493    684  -1190       C  
ATOM    913  CD  ARG A 273     -19.961   6.378  17.703  1.00 53.66           C  
ANISOU  913  CD  ARG A 273     4928   9240   6222    689    659  -1464       C  
ATOM    914  NE  ARG A 273     -21.115   5.952  18.504  1.00 59.10           N  
ANISOU  914  NE  ARG A 273     5320  10376   6761    613    774  -1572       N  
ATOM    915  CZ  ARG A 273     -21.598   6.614  19.553  1.00 62.65           C  
ANISOU  915  CZ  ARG A 273     5560  11153   7089    735    801  -1811       C  
ATOM    916  NH1 ARG A 273     -21.041   7.748  19.952  1.00 63.87           N  
ANISOU  916  NH1 ARG A 273     5783  11208   7277    954    702  -1979       N  
ATOM    917  NH2 ARG A 273     -22.647   6.137  20.211  1.00 66.83           N  
ANISOU  917  NH2 ARG A 273     5801  12132   7458    632    919  -1890       N  
ATOM    918  N   ILE A 274     -19.973   2.366  14.794  1.00 40.94           N  
ANISOU  918  N   ILE A 274     3572   7194   4789     61    722   -766       N  
ATOM    919  CA  ILE A 274     -19.786   2.290  13.348  1.00 39.87           C  
ANISOU  919  CA  ILE A 274     3580   6784   4786    112    618   -721       C  
ATOM    920  C   ILE A 274     -19.920   3.689  12.754  1.00 39.88           C  
ANISOU  920  C   ILE A 274     3612   6682   4859    357    500   -889       C  
ATOM    921  O   ILE A 274     -20.948   4.342  12.927  1.00 41.19           O  
ANISOU  921  O   ILE A 274     3606   7023   5022    479    467  -1078       O  
ATOM    922  CB  ILE A 274     -20.780   1.318  12.678  1.00 40.50           C  
ANISOU  922  CB  ILE A 274     3555   6928   4904     -9    609   -679       C  
ATOM    923  CG1 ILE A 274     -20.777  -0.027  13.427  1.00 40.65           C  
ANISOU  923  CG1 ILE A 274     3526   7065   4855   -274    694   -508       C  
ATOM    924  CG2 ILE A 274     -20.447   1.165  11.191  1.00 36.76           C  
ANISOU  924  CG2 ILE A 274     3243   6177   4548     40    503   -629       C  
ATOM    925  CD1 ILE A 274     -21.587  -1.110  12.760  1.00 40.52           C  
ANISOU  925  CD1 ILE A 274     3440   7060   4895   -423    657   -433       C  
ATOM    926  N   LEU A 275     -18.879   4.133  12.060  1.00 37.71           N  
ANISOU  926  N   LEU A 275     3550   6132   4647    422    421   -820       N  
ATOM    927  CA  LEU A 275     -18.808   5.501  11.547  1.00 37.29           C  
ANISOU  927  CA  LEU A 275     3564   5939   4664    624    276   -933       C  
ATOM    928  C   LEU A 275     -19.133   5.568  10.053  1.00 36.33           C  
ANISOU  928  C   LEU A 275     3510   5662   4631    665    156   -910       C  
ATOM    929  O   LEU A 275     -19.696   6.556   9.566  1.00 36.14           O  
ANISOU  929  O   LEU A 275     3470   5589   4673    823     12  -1034       O  
ATOM    930  CB  LEU A 275     -17.415   6.084  11.804  1.00 36.42           C  
ANISOU  930  CB  LEU A 275     3640   5647   4552    650    251   -856       C  
ATOM    931  CG  LEU A 275     -16.891   6.461  13.200  1.00 38.69           C  
ANISOU  931  CG  LEU A 275     3905   6027   4768    669    315   -903       C  
ATOM    932  CD1 LEU A 275     -16.671   5.254  14.120  1.00 41.11           C  
ANISOU  932  CD1 LEU A 275     4157   6492   4970    482    485   -796       C  
ATOM    933  CD2 LEU A 275     -15.564   7.231  13.049  1.00 37.67           C  
ANISOU  933  CD2 LEU A 275     3979   5658   4677    716    234   -829       C  
ATOM    934  N   ALA A 276     -18.786   4.500   9.336  1.00 34.09           N  
ANISOU  934  N   ALA A 276     3301   5303   4347    527    198   -761       N  
ATOM    935  CA  ALA A 276     -18.843   4.489   7.893  1.00 33.19           C  
ANISOU  935  CA  ALA A 276     3275   5046   4290    550     94   -718       C  
ATOM    936  C   ALA A 276     -18.872   3.068   7.362  1.00 32.82           C  
ANISOU  936  C   ALA A 276     3226   5005   4240    402    153   -618       C  
ATOM    937  O   ALA A 276     -18.482   2.125   8.045  1.00 32.06           O  
ANISOU  937  O   ALA A 276     3120   4953   4107    271    254   -539       O  
ATOM    938  CB  ALA A 276     -17.636   5.243   7.298  1.00 31.84           C  
ANISOU  938  CB  ALA A 276     3303   4670   4122    591      9   -629       C  
ATOM    939  N   LEU A 277     -19.343   2.935   6.130  1.00 33.33           N  
ANISOU  939  N   LEU A 277     3303   5012   4347    428     65   -626       N  
ATOM    940  CA  LEU A 277     -19.346   1.658   5.446  1.00 33.69           C  
ANISOU  940  CA  LEU A 277     3360   5036   4405    316     80   -555       C  
ATOM    941  C   LEU A 277     -18.541   1.726   4.147  1.00 32.57           C  
ANISOU  941  C   LEU A 277     3371   4752   4253    343      2   -493       C  
ATOM    942  O   LEU A 277     -18.747   2.639   3.352  1.00 33.31           O  
ANISOU  942  O   LEU A 277     3506   4798   4353    441   -103   -522       O  
ATOM    943  CB  LEU A 277     -20.784   1.240   5.162  1.00 34.86           C  
ANISOU  943  CB  LEU A 277     3347   5298   4601    306     52   -638       C  
ATOM    944  CG  LEU A 277     -20.988  -0.076   4.403  1.00 35.93           C  
ANISOU  944  CG  LEU A 277     3480   5401   4772    199     31   -587       C  
ATOM    945  CD1 LEU A 277     -20.241  -1.216   5.061  1.00 38.89           C  
ANISOU  945  CD1 LEU A 277     3894   5747   5134     47    102   -478       C  
ATOM    946  CD2 LEU A 277     -22.461  -0.388   4.317  1.00 40.23           C  
ANISOU  946  CD2 LEU A 277     3842   6078   5364    177      7   -669       C  
ATOM    947  N   LEU A 278     -17.619   0.780   3.960  1.00 31.12           N  
ANISOU  947  N   LEU A 278     3264   4514   4046    256     40   -413       N  
ATOM    948  CA  LEU A 278     -17.023   0.534   2.646  1.00 31.36           C  
ANISOU  948  CA  LEU A 278     3388   4478   4048    269    -25   -384       C  
ATOM    949  C   LEU A 278     -17.796  -0.589   1.965  1.00 31.92           C  
ANISOU  949  C   LEU A 278     3390   4569   4169    230    -67   -426       C  
ATOM    950  O   LEU A 278     -17.884  -1.699   2.494  1.00 32.72           O  
ANISOU  950  O   LEU A 278     3447   4672   4312    136    -34   -413       O  
ATOM    951  CB  LEU A 278     -15.523   0.176   2.731  1.00 29.44           C  
ANISOU  951  CB  LEU A 278     3252   4185   3749    226     20   -313       C  
ATOM    952  CG  LEU A 278     -14.840  -0.306   1.435  1.00 30.69           C  
ANISOU  952  CG  LEU A 278     3471   4336   3855    232    -33   -312       C  
ATOM    953  CD1 LEU A 278     -14.528   0.855   0.499  1.00 29.76           C  
ANISOU  953  CD1 LEU A 278     3421   4232   3655    284    -97   -276       C  
ATOM    954  CD2 LEU A 278     -13.555  -1.116   1.713  1.00 28.76           C  
ANISOU  954  CD2 LEU A 278     3277   4068   3582    187     13   -290       C  
ATOM    955  N   ALA A 279     -18.365  -0.282   0.806  1.00 33.21           N  
ANISOU  955  N   ALA A 279     3551   4738   4331    294   -161   -469       N  
ATOM    956  CA  ALA A 279     -19.075  -1.271  -0.024  1.00 34.31           C  
ANISOU  956  CA  ALA A 279     3632   4887   4516    273   -224   -522       C  
ATOM    957  C   ALA A 279     -18.307  -1.486  -1.323  1.00 34.35           C  
ANISOU  957  C   ALA A 279     3727   4876   4450    306   -287   -523       C  
ATOM    958  O   ALA A 279     -18.181  -0.571  -2.158  1.00 35.30           O  
ANISOU  958  O   ALA A 279     3902   5013   4496    367   -345   -507       O  
ATOM    959  CB  ALA A 279     -20.503  -0.807  -0.311  1.00 34.88           C  
ANISOU  959  CB  ALA A 279     3600   5012   4641    326   -288   -594       C  
ATOM    960  N   VAL A 280     -17.788  -2.694  -1.511  1.00 35.17           N  
ANISOU  960  N   VAL A 280     3841   4956   4567    263   -294   -544       N  
ATOM    961  CA  VAL A 280     -16.958  -2.959  -2.690  1.00 35.29           C  
ANISOU  961  CA  VAL A 280     3916   5001   4491    306   -346   -579       C  
ATOM    962  C   VAL A 280     -17.780  -3.674  -3.768  1.00 37.20           C  
ANISOU  962  C   VAL A 280     4104   5261   4767    336   -455   -674       C  
ATOM    963  O   VAL A 280     -18.317  -4.747  -3.533  1.00 36.65           O  
ANISOU  963  O   VAL A 280     3979   5137   4810    293   -496   -722       O  
ATOM    964  CB  VAL A 280     -15.630  -3.720  -2.319  1.00 34.86           C  
ANISOU  964  CB  VAL A 280     3908   4922   4414    280   -307   -581       C  
ATOM    965  CG1 VAL A 280     -14.803  -4.054  -3.558  1.00 34.97           C  
ANISOU  965  CG1 VAL A 280     3947   5022   4320    338   -362   -657       C  
ATOM    966  CG2 VAL A 280     -14.789  -2.897  -1.355  1.00 32.74           C  
ANISOU  966  CG2 VAL A 280     3697   4644   4101    256   -207   -486       C  
ATOM    967  N   GLU A 281     -17.884  -3.042  -4.941  1.00 39.02           N  
ANISOU  967  N   GLU A 281     4358   5569   4900    397   -515   -689       N  
ATOM    968  CA  GLU A 281     -18.513  -3.651  -6.113  1.00 41.05           C  
ANISOU  968  CA  GLU A 281     4575   5865   5158    439   -625   -789       C  
ATOM    969  C   GLU A 281     -17.525  -4.594  -6.809  1.00 41.60           C  
ANISOU  969  C   GLU A 281     4660   5989   5157    468   -659   -881       C  
ATOM    970  O   GLU A 281     -17.863  -5.739  -7.102  1.00 42.61           O  
ANISOU  970  O   GLU A 281     4742   6076   5371    482   -743   -992       O  
ATOM    971  CB  GLU A 281     -19.023  -2.576  -7.082  1.00 41.70           C  
ANISOU  971  CB  GLU A 281     4676   6018   5149    488   -692   -762       C  
ATOM    972  CG  GLU A 281     -19.540  -3.091  -8.438  1.00 45.11           C  
ANISOU  972  CG  GLU A 281     5077   6520   5542    539   -809   -863       C  
ATOM    973  CD  GLU A 281     -20.952  -3.659  -8.393  1.00 48.22           C  
ANISOU  973  CD  GLU A 281     5379   6847   6094    544   -880   -939       C  
ATOM    974  OE1 GLU A 281     -21.510  -3.854  -7.293  1.00 48.95           O  
ANISOU  974  OE1 GLU A 281     5416   6860   6324    494   -830   -920       O  
ATOM    975  OE2 GLU A 281     -21.514  -3.913  -9.486  1.00 52.47           O  
ANISOU  975  OE2 GLU A 281     5892   7434   6609    592   -988  -1017       O  
ATOM    976  N   GLN A 282     -16.312  -4.111  -7.062  1.00 41.57           N  
ANISOU  976  N   GLN A 282     4711   6085   5000    478   -607   -845       N  
ATOM    977  CA  GLN A 282     -15.316  -4.893  -7.801  1.00 42.24           C  
ANISOU  977  CA  GLN A 282     4784   6280   4986    526   -639   -963       C  
ATOM    978  C   GLN A 282     -13.911  -4.837  -7.199  1.00 41.48           C  
ANISOU  978  C   GLN A 282     4721   6218   4823    507   -548   -933       C  
ATOM    979  O   GLN A 282     -13.422  -3.782  -6.800  1.00 41.03           O  
ANISOU  979  O   GLN A 282     4713   6189   4688    459   -464   -798       O  
ATOM    980  CB  GLN A 282     -15.279  -4.484  -9.287  1.00 43.54           C  
ANISOU  980  CB  GLN A 282     4939   6645   4961    570   -698  -1001       C  
ATOM    981  CG  GLN A 282     -14.083  -5.059 -10.092  1.00 45.51           C  
ANISOU  981  CG  GLN A 282     5152   7096   5044    624   -708  -1133       C  
ATOM    982  CD  GLN A 282     -14.089  -4.680 -11.574  1.00 47.67           C  
ANISOU  982  CD  GLN A 282     5399   7618   5097    650   -764  -1167       C  
ATOM    983  OE1 GLN A 282     -15.069  -4.877 -12.279  1.00 49.66           O  
ANISOU  983  OE1 GLN A 282     5628   7865   5375    688   -860  -1226       O  
ATOM    984  NE2 GLN A 282     -12.971  -4.160 -12.050  1.00 51.27           N  
ANISOU  984  NE2 GLN A 282     5847   8310   5322    619   -706  -1127       N  
ATOM    985  N   MET A 283     -13.266  -5.997  -7.154  1.00 41.56           N  
ANISOU  985  N   MET A 283     4703   6214   4876    551   -590  -1071       N  
ATOM    986  CA  MET A 283     -11.837  -6.081  -6.898  1.00 40.93           C  
ANISOU  986  CA  MET A 283     4629   6214   4706    564   -532  -1097       C  
ATOM    987  C   MET A 283     -11.324  -7.303  -7.657  1.00 42.11           C  
ANISOU  987  C   MET A 283     4715   6445   4842    672   -643  -1331       C  
ATOM    988  O   MET A 283     -12.121  -8.182  -8.009  1.00 42.89           O  
ANISOU  988  O   MET A 283     4785   6452   5060    718   -769  -1446       O  
ATOM    989  CB  MET A 283     -11.551  -6.177  -5.391  1.00 39.11           C  
ANISOU  989  CB  MET A 283     4446   5802   4614    503   -467  -1005       C  
ATOM    990  CG  MET A 283     -12.126  -7.395  -4.730  1.00 40.29           C  
ANISOU  990  CG  MET A 283     4587   5746   4976    493   -560  -1064       C  
ATOM    991  SD  MET A 283     -12.171  -7.246  -2.946  1.00 40.28           S  
ANISOU  991  SD  MET A 283     4638   5564   5104    379   -474   -898       S  
ATOM    992  CE  MET A 283     -13.122  -8.675  -2.552  1.00 44.27           C  
ANISOU  992  CE  MET A 283     5118   5872   5829    330   -624   -944       C  
ATOM    993  N   PRO A 284     -10.012  -7.361  -7.944  1.00 42.47           N  
ANISOU  993  N   PRO A 284     4725   6671   4742    720   -611  -1418       N  
ATOM    994  CA  PRO A 284      -9.563  -8.530  -8.723  1.00 43.98           C  
ANISOU  994  CA  PRO A 284     4832   6959   4917    856   -739  -1690       C  
ATOM    995  C   PRO A 284      -9.755  -9.841  -7.956  1.00 43.95           C  
ANISOU  995  C   PRO A 284     4849   6673   5177    898   -878  -1798       C  
ATOM    996  O   PRO A 284      -9.654  -9.867  -6.737  1.00 42.09           O  
ANISOU  996  O   PRO A 284     4677   6238   5077    822   -840  -1673       O  
ATOM    997  CB  PRO A 284      -8.081  -8.254  -8.961  1.00 44.29           C  
ANISOU  997  CB  PRO A 284     4814   7261   4752    888   -661  -1754       C  
ATOM    998  CG  PRO A 284      -7.892  -6.799  -8.725  1.00 44.04           C  
ANISOU  998  CG  PRO A 284     4834   7318   4581    753   -503  -1497       C  
ATOM    999  CD  PRO A 284      -8.927  -6.387  -7.730  1.00 41.78           C  
ANISOU  999  CD  PRO A 284     4650   6740   4486    664   -478  -1303       C  
ATOM   1000  N   PHE A 285     -10.051 -10.924  -8.666  1.00 45.92           N  
ANISOU 1000  N   PHE A 285     5047   6900   5501   1010  -1058  -2022       N  
ATOM   1001  CA  PHE A 285     -10.233 -12.208  -8.004  1.00 46.84           C  
ANISOU 1001  CA  PHE A 285     5191   6724   5881   1037  -1239  -2116       C  
ATOM   1002  C   PHE A 285      -9.021 -12.613  -7.142  1.00 46.15           C  
ANISOU 1002  C   PHE A 285     5123   6563   5848   1066  -1251  -2158       C  
ATOM   1003  O   PHE A 285      -9.181 -13.238  -6.094  1.00 45.96           O  
ANISOU 1003  O   PHE A 285     5169   6256   6038   1001  -1337  -2086       O  
ATOM   1004  CB  PHE A 285     -10.558 -13.287  -9.036  1.00 49.80           C  
ANISOU 1004  CB  PHE A 285     5502   7105   6315   1180  -1462  -2390       C  
ATOM   1005  CG  PHE A 285     -10.894 -14.625  -8.438  1.00 53.19           C  
ANISOU 1005  CG  PHE A 285     5973   7195   7043   1189  -1702  -2470       C  
ATOM   1006  CD1 PHE A 285     -12.189 -14.889  -7.972  1.00 54.83           C  
ANISOU 1006  CD1 PHE A 285     6231   7157   7443   1055  -1768  -2315       C  
ATOM   1007  CD2 PHE A 285      -9.924 -15.629  -8.350  1.00 55.56           C  
ANISOU 1007  CD2 PHE A 285     6255   7424   7431   1325  -1882  -2700       C  
ATOM   1008  CE1 PHE A 285     -12.510 -16.133  -7.417  1.00 57.23           C  
ANISOU 1008  CE1 PHE A 285     6578   7144   8021   1025  -2013  -2353       C  
ATOM   1009  CE2 PHE A 285     -10.236 -16.878  -7.808  1.00 58.47           C  
ANISOU 1009  CE2 PHE A 285     6678   7445   8093   1321  -2150  -2757       C  
ATOM   1010  CZ  PHE A 285     -11.534 -17.132  -7.340  1.00 58.62           C  
ANISOU 1010  CZ  PHE A 285     6759   7214   8299   1154  -2218  -2567       C  
ATOM   1011  N   PHE A 286      -7.817 -12.225  -7.556  1.00 45.87           N  
ANISOU 1011  N   PHE A 286     5024   6796   5610   1146  -1165  -2260       N  
ATOM   1012  CA  PHE A 286      -6.590 -12.707  -6.902  1.00 45.76           C  
ANISOU 1012  CA  PHE A 286     5004   6743   5641   1210  -1205  -2360       C  
ATOM   1013  C   PHE A 286      -6.354 -12.061  -5.531  1.00 44.01           C  
ANISOU 1013  C   PHE A 286     4877   6372   5471   1061  -1060  -2094       C  
ATOM   1014  O   PHE A 286      -5.453 -12.468  -4.787  1.00 43.24           O  
ANISOU 1014  O   PHE A 286     4798   6185   5446   1091  -1100  -2137       O  
ATOM   1015  CB  PHE A 286      -5.373 -12.560  -7.834  1.00 47.04           C  
ANISOU 1015  CB  PHE A 286     5031   7286   5556   1348  -1165  -2586       C  
ATOM   1016  CG  PHE A 286      -4.842 -11.156  -7.946  1.00 46.10           C  
ANISOU 1016  CG  PHE A 286     4890   7449   5176   1241   -917  -2398       C  
ATOM   1017  CD1 PHE A 286      -3.850 -10.709  -7.083  1.00 44.60           C  
ANISOU 1017  CD1 PHE A 286     4720   7268   4957   1188   -806  -2300       C  
ATOM   1018  CD2 PHE A 286      -5.308 -10.294  -8.938  1.00 46.65           C  
ANISOU 1018  CD2 PHE A 286     4923   7769   5031   1187   -818  -2319       C  
ATOM   1019  CE1 PHE A 286      -3.345  -9.416  -7.173  1.00 43.89           C  
ANISOU 1019  CE1 PHE A 286     4616   7418   4642   1075   -604  -2117       C  
ATOM   1020  CE2 PHE A 286      -4.806  -8.991  -9.038  1.00 45.73           C  
ANISOU 1020  CE2 PHE A 286     4801   7889   4686   1066   -627  -2122       C  
ATOM   1021  CZ  PHE A 286      -3.822  -8.555  -8.148  1.00 43.99           C  
ANISOU 1021  CZ  PHE A 286     4600   7662   4451   1007   -522  -2021       C  
ATOM   1022  N   VAL A 287      -7.186 -11.062  -5.212  1.00 42.17           N  
ANISOU 1022  N   VAL A 287     4702   6115   5205    914   -908  -1836       N  
ATOM   1023  CA  VAL A 287      -7.140 -10.357  -3.943  1.00 41.30           C  
ANISOU 1023  CA  VAL A 287     4676   5882   5136    778   -771  -1591       C  
ATOM   1024  C   VAL A 287      -8.372 -10.698  -3.091  1.00 40.69           C  
ANISOU 1024  C   VAL A 287     4667   5531   5262    662   -822  -1442       C  
ATOM   1025  O   VAL A 287      -8.433 -10.344  -1.913  1.00 40.07           O  
ANISOU 1025  O   VAL A 287     4650   5334   5241    551   -739  -1261       O  
ATOM   1026  CB  VAL A 287      -7.032  -8.818  -4.183  1.00 40.50           C  
ANISOU 1026  CB  VAL A 287     4575   5992   4824    705   -567  -1423       C  
ATOM   1027  CG1 VAL A 287      -8.360  -8.215  -4.623  1.00 40.34           C  
ANISOU 1027  CG1 VAL A 287     4567   5967   4792    644   -540  -1311       C  
ATOM   1028  CG2 VAL A 287      -6.514  -8.102  -2.980  1.00 41.67           C  
ANISOU 1028  CG2 VAL A 287     4787   6067   4977    612   -440  -1242       C  
ATOM   1029  N   PHE A 288      -9.347 -11.373  -3.702  1.00 41.83           N  
ANISOU 1029  N   PHE A 288     4788   5604   5502    683   -959  -1523       N  
ATOM   1030  CA  PHE A 288     -10.550 -11.813  -3.014  1.00 41.99           C  
ANISOU 1030  CA  PHE A 288     4846   5402   5709    560  -1027  -1397       C  
ATOM   1031  C   PHE A 288     -10.201 -13.001  -2.119  1.00 43.02           C  
ANISOU 1031  C   PHE A 288     5027   5284   6036    529  -1198  -1414       C  
ATOM   1032  O   PHE A 288     -10.482 -14.156  -2.443  1.00 44.42           O  
ANISOU 1032  O   PHE A 288     5200   5311   6367    568  -1427  -1543       O  
ATOM   1033  CB  PHE A 288     -11.644 -12.169  -4.029  1.00 43.51           C  
ANISOU 1033  CB  PHE A 288     4990   5605   5939    592  -1134  -1487       C  
ATOM   1034  CG  PHE A 288     -13.019 -12.305  -3.428  1.00 43.66           C  
ANISOU 1034  CG  PHE A 288     5016   5471   6100    443  -1156  -1330       C  
ATOM   1035  CD1 PHE A 288     -13.561 -13.560  -3.171  1.00 44.71           C  
ANISOU 1035  CD1 PHE A 288     5159   5384   6445    387  -1368  -1358       C  
ATOM   1036  CD2 PHE A 288     -13.782 -11.176  -3.135  1.00 43.47           C  
ANISOU 1036  CD2 PHE A 288     4981   5533   6001    356   -981  -1161       C  
ATOM   1037  CE1 PHE A 288     -14.839 -13.686  -2.615  1.00 45.56           C  
ANISOU 1037  CE1 PHE A 288     5252   5393   6666    222  -1381  -1202       C  
ATOM   1038  CE2 PHE A 288     -15.065 -11.297  -2.590  1.00 43.82           C  
ANISOU 1038  CE2 PHE A 288     5000   5488   6161    223   -994  -1041       C  
ATOM   1039  CZ  PHE A 288     -15.585 -12.552  -2.327  1.00 44.00           C  
ANISOU 1039  CZ  PHE A 288     5019   5325   6373    145  -1182  -1053       C  
ATOM   1040  N   ASN A 289      -9.562 -12.700  -0.996  1.00 42.03           N  
ANISOU 1040  N   ASN A 289     4954   5107   5907    458  -1107  -1283       N  
ATOM   1041  CA  ASN A 289      -9.038 -13.722  -0.097  1.00 43.66           C  
ANISOU 1041  CA  ASN A 289     5223   5088   6279    426  -1272  -1282       C  
ATOM   1042  C   ASN A 289      -8.900 -13.168   1.308  1.00 42.47           C  
ANISOU 1042  C   ASN A 289     5131   4888   6116    278  -1129  -1049       C  
ATOM   1043  O   ASN A 289      -9.122 -11.984   1.534  1.00 41.07           O  
ANISOU 1043  O   ASN A 289     4941   4857   5806    229   -910   -923       O  
ATOM   1044  CB  ASN A 289      -7.682 -14.269  -0.597  1.00 44.42           C  
ANISOU 1044  CB  ASN A 289     5299   5220   6359    613  -1390  -1528       C  
ATOM   1045  CG  ASN A 289      -6.616 -13.182  -0.757  1.00 42.23           C  
ANISOU 1045  CG  ASN A 289     4985   5198   5861    681  -1174  -1545       C  
ATOM   1046  OD1 ASN A 289      -6.169 -12.571   0.210  1.00 40.69           O  
ANISOU 1046  OD1 ASN A 289     4836   4995   5628    599  -1039  -1387       O  
ATOM   1047  ND2 ASN A 289      -6.202 -12.953  -1.993  1.00 43.18           N  
ANISOU 1047  ND2 ASN A 289     5016   5561   5831    822  -1151  -1736       N  
ATOM   1048  N   GLU A 290      -8.500 -14.020   2.244  1.00 44.26           N  
ANISOU 1048  N   GLU A 290     5426   4909   6483    215  -1275  -1002       N  
ATOM   1049  CA  GLU A 290      -8.456 -13.643   3.660  1.00 44.01           C  
ANISOU 1049  CA  GLU A 290     5451   4827   6445     57  -1165   -774       C  
ATOM   1050  C   GLU A 290      -7.302 -12.713   4.061  1.00 42.64           C  
ANISOU 1050  C   GLU A 290     5292   4782   6127    118   -986   -764       C  
ATOM   1051  O   GLU A 290      -7.401 -12.003   5.065  1.00 41.57           O  
ANISOU 1051  O   GLU A 290     5182   4679   5933      6   -832   -584       O  
ATOM   1052  CB  GLU A 290      -8.487 -14.892   4.554  1.00 46.02           C  
ANISOU 1052  CB  GLU A 290     5783   4811   6892    -65  -1405   -691       C  
ATOM   1053  CG  GLU A 290      -9.655 -15.860   4.247  1.00 49.54           C  
ANISOU 1053  CG  GLU A 290     6218   5105   7498   -165  -1612   -668       C  
ATOM   1054  CD  GLU A 290     -11.034 -15.320   4.655  1.00 51.88           C  
ANISOU 1054  CD  GLU A 290     6463   5502   7747   -357  -1460   -463       C  
ATOM   1055  OE1 GLU A 290     -11.191 -14.861   5.807  1.00 52.79           O  
ANISOU 1055  OE1 GLU A 290     6590   5666   7801   -512  -1323   -261       O  
ATOM   1056  OE2 GLU A 290     -11.969 -15.364   3.817  1.00 53.18           O  
ANISOU 1056  OE2 GLU A 290     6562   5711   7932   -346  -1482   -520       O  
ATOM   1057  N   ARG A 291      -6.203 -12.722   3.306  1.00 42.26           N  
ANISOU 1057  N   ARG A 291     5216   4824   6018    293  -1010   -962       N  
ATOM   1058  CA  ARG A 291      -5.107 -11.804   3.597  1.00 41.27           C  
ANISOU 1058  CA  ARG A 291     5089   4843   5750    338   -841   -951       C  
ATOM   1059  C   ARG A 291      -5.580 -10.368   3.321  1.00 38.23           C  
ANISOU 1059  C   ARG A 291     4669   4658   5197    300   -603   -843       C  
ATOM   1060  O   ARG A 291      -5.395  -9.474   4.147  1.00 36.41           O  
ANISOU 1060  O   ARG A 291     4471   4465   4899    229   -452   -697       O  
ATOM   1061  CB  ARG A 291      -3.848 -12.170   2.785  1.00 42.65           C  
ANISOU 1061  CB  ARG A 291     5209   5116   5882    526   -925  -1202       C  
ATOM   1062  CG  ARG A 291      -2.638 -11.191   2.903  1.00 46.10           C  
ANISOU 1062  CG  ARG A 291     5618   5749   6150    569   -750  -1205       C  
ATOM   1063  CD  ARG A 291      -2.343 -10.687   4.332  1.00 50.44           C  
ANISOU 1063  CD  ARG A 291     6250   6204   6712    451   -650  -1001       C  
ATOM   1064  NE  ARG A 291      -2.027 -11.763   5.279  1.00 56.06           N  
ANISOU 1064  NE  ARG A 291     7035   6672   7594    429   -835   -995       N  
ATOM   1065  CZ  ARG A 291      -0.843 -11.953   5.864  1.00 58.19           C  
ANISOU 1065  CZ  ARG A 291     7326   6903   7879    480   -880  -1045       C  
ATOM   1066  NH1 ARG A 291       0.177 -11.140   5.613  1.00 58.19           N  
ANISOU 1066  NH1 ARG A 291     7268   7111   7732    552   -739  -1109       N  
ATOM   1067  NH2 ARG A 291      -0.680 -12.966   6.710  1.00 60.09           N  
ANISOU 1067  NH2 ARG A 291     7648   6896   8288    447  -1082  -1022       N  
ATOM   1068  N   THR A 292      -6.221 -10.173   2.173  1.00 37.70           N  
ANISOU 1068  N   THR A 292     4544   4705   5075    349   -597   -918       N  
ATOM   1069  CA  THR A 292      -6.704  -8.858   1.806  1.00 36.41           C  
ANISOU 1069  CA  THR A 292     4356   4707   4770    320   -421   -824       C  
ATOM   1070  C   THR A 292      -7.852  -8.388   2.710  1.00 35.61           C  
ANISOU 1070  C   THR A 292     4282   4531   4719    187   -344   -637       C  
ATOM   1071  O   THR A 292      -7.833  -7.262   3.212  1.00 34.85           O  
ANISOU 1071  O   THR A 292     4200   4503   4539    147   -199   -523       O  
ATOM   1072  CB  THR A 292      -7.186  -8.822   0.388  1.00 37.04           C  
ANISOU 1072  CB  THR A 292     4372   4917   4783    397   -455   -941       C  
ATOM   1073  OG1 THR A 292      -6.170  -9.353  -0.476  1.00 38.45           O  
ANISOU 1073  OG1 THR A 292     4499   5208   4901    529   -535  -1147       O  
ATOM   1074  CG2 THR A 292      -7.533  -7.399  -0.007  1.00 35.69           C  
ANISOU 1074  CG2 THR A 292     4192   4906   4464    367   -302   -833       C  
ATOM   1075  N   PHE A 293      -8.863  -9.233   2.878  1.00 36.05           N  
ANISOU 1075  N   PHE A 293     4330   4463   4905    119   -451   -618       N  
ATOM   1076  CA  PHE A 293     -10.007  -8.886   3.723  1.00 35.93           C  
ANISOU 1076  CA  PHE A 293     4303   4425   4922    -14   -381   -461       C  
ATOM   1077  C   PHE A 293      -9.451  -8.402   5.068  1.00 34.79           C  
ANISOU 1077  C   PHE A 293     4205   4269   4745    -85   -277   -334       C  
ATOM   1078  O   PHE A 293      -9.860  -7.369   5.577  1.00 34.38           O  
ANISOU 1078  O   PHE A 293     4137   4305   4622   -120   -140   -247       O  
ATOM   1079  CB  PHE A 293     -10.975 -10.080   3.915  1.00 35.77           C  
ANISOU 1079  CB  PHE A 293     4267   4269   5057   -117   -535   -436       C  
ATOM   1080  CG  PHE A 293     -11.698 -10.531   2.658  1.00 36.84           C  
ANISOU 1080  CG  PHE A 293     4351   4409   5235    -56   -644   -557       C  
ATOM   1081  CD1 PHE A 293     -11.822  -9.704   1.545  1.00 34.95           C  
ANISOU 1081  CD1 PHE A 293     4074   4324   4883     55   -570   -641       C  
ATOM   1082  CD2 PHE A 293     -12.308 -11.789   2.624  1.00 38.11           C  
ANISOU 1082  CD2 PHE A 293     4509   4416   5557   -128   -840   -570       C  
ATOM   1083  CE1 PHE A 293     -12.512 -10.130   0.408  1.00 36.63           C  
ANISOU 1083  CE1 PHE A 293     4240   4551   5128    110   -676   -754       C  
ATOM   1084  CE2 PHE A 293     -12.990 -12.232   1.491  1.00 40.25           C  
ANISOU 1084  CE2 PHE A 293     4733   4684   5878    -69   -956   -691       C  
ATOM   1085  CZ  PHE A 293     -13.097 -11.400   0.376  1.00 39.44           C  
ANISOU 1085  CZ  PHE A 293     4587   4751   5649     57   -865   -790       C  
ATOM   1086  N   SER A 294      -8.468  -9.121   5.611  1.00 36.05           N  
ANISOU 1086  N   SER A 294     4421   4321   4956    -87   -357   -345       N  
ATOM   1087  CA  SER A 294      -7.866  -8.757   6.905  1.00 35.66           C  
ANISOU 1087  CA  SER A 294     4421   4253   4876   -152   -275   -230       C  
ATOM   1088  C   SER A 294      -7.135  -7.399   6.909  1.00 34.88           C  
ANISOU 1088  C   SER A 294     4328   4287   4640    -81   -111   -227       C  
ATOM   1089  O   SER A 294      -7.243  -6.614   7.857  1.00 33.06           O  
ANISOU 1089  O   SER A 294     4108   4096   4359   -138      1   -122       O  
ATOM   1090  CB  SER A 294      -6.929  -9.865   7.393  1.00 37.32           C  
ANISOU 1090  CB  SER A 294     4696   4303   5183   -157   -430   -255       C  
ATOM   1091  OG  SER A 294      -6.114  -9.388   8.469  1.00 38.34           O  
ANISOU 1091  OG  SER A 294     4874   4437   5258   -187   -345   -171       O  
ATOM   1092  N   LEU A 295      -6.387  -7.084   5.861  1.00 34.87           N  
ANISOU 1092  N   LEU A 295     4312   4369   4569     35   -106   -340       N  
ATOM   1093  CA  LEU A 295      -5.735  -5.775   5.916  1.00 33.84           C  
ANISOU 1093  CA  LEU A 295     4192   4354   4314     64     29   -301       C  
ATOM   1094  C   LEU A 295      -6.768  -4.643   5.787  1.00 32.23           C  
ANISOU 1094  C   LEU A 295     3964   4223   4057     41    119   -229       C  
ATOM   1095  O   LEU A 295      -6.572  -3.575   6.346  1.00 31.20           O  
ANISOU 1095  O   LEU A 295     3856   4128   3870     28    208   -157       O  
ATOM   1096  CB  LEU A 295      -4.558  -5.647   4.941  1.00 35.37           C  
ANISOU 1096  CB  LEU A 295     4364   4658   4418    161     22   -414       C  
ATOM   1097  CG  LEU A 295      -4.662  -5.059   3.545  1.00 37.19           C  
ANISOU 1097  CG  LEU A 295     4543   5053   4534    214     42   -471       C  
ATOM   1098  CD1 LEU A 295      -3.257  -4.856   2.963  1.00 38.92           C  
ANISOU 1098  CD1 LEU A 295     4728   5426   4633    271     61   -551       C  
ATOM   1099  CD2 LEU A 295      -5.459  -5.961   2.639  1.00 40.08           C  
ANISOU 1099  CD2 LEU A 295     4865   5406   4955    256    -65   -579       C  
ATOM   1100  N   LEU A 296      -7.875  -4.898   5.094  1.00 31.92           N  
ANISOU 1100  N   LEU A 296     3880   4195   4052     41     75   -260       N  
ATOM   1101  CA  LEU A 296      -8.930  -3.883   4.987  1.00 32.19           C  
ANISOU 1101  CA  LEU A 296     3884   4291   4056     33    133   -212       C  
ATOM   1102  C   LEU A 296      -9.552  -3.621   6.357  1.00 32.15           C  
ANISOU 1102  C   LEU A 296     3867   4264   4083    -42    194   -127       C  
ATOM   1103  O   LEU A 296      -9.728  -2.468   6.747  1.00 31.69           O  
ANISOU 1103  O   LEU A 296     3808   4255   3977    -24    263    -92       O  
ATOM   1104  CB  LEU A 296      -9.983  -4.252   3.943  1.00 32.00           C  
ANISOU 1104  CB  LEU A 296     3806   4289   4063     54     64   -274       C  
ATOM   1105  CG  LEU A 296      -9.493  -4.144   2.502  1.00 34.23           C  
ANISOU 1105  CG  LEU A 296     4085   4656   4264    136     22   -358       C  
ATOM   1106  CD1 LEU A 296     -10.375  -4.941   1.550  1.00 36.58           C  
ANISOU 1106  CD1 LEU A 296     4333   4952   4614    160    -77   -447       C  
ATOM   1107  CD2 LEU A 296      -9.389  -2.677   2.071  1.00 34.36           C  
ANISOU 1107  CD2 LEU A 296     4120   4765   4169    159     78   -300       C  
ATOM   1108  N   ALA A 297      -9.835  -4.702   7.088  1.00 32.86           N  
ANISOU 1108  N   ALA A 297     3947   4289   4250   -131    153    -95       N  
ATOM   1109  CA  ALA A 297     -10.400  -4.610   8.441  1.00 33.62           C  
ANISOU 1109  CA  ALA A 297     4014   4411   4349   -230    212     -7       C  
ATOM   1110  C   ALA A 297      -9.462  -3.858   9.369  1.00 32.64           C  
ANISOU 1110  C   ALA A 297     3942   4298   4160   -215    293     35       C  
ATOM   1111  O   ALA A 297      -9.891  -2.962  10.107  1.00 32.73           O  
ANISOU 1111  O   ALA A 297     3920   4393   4124   -217    373     57       O  
ATOM   1112  CB  ALA A 297     -10.746  -5.998   8.997  1.00 34.55           C  
ANISOU 1112  CB  ALA A 297     4123   4454   4551   -362    125     51       C  
ATOM   1113  N   ILE A 298      -8.172  -4.182   9.303  1.00 31.59           N  
ANISOU 1113  N   ILE A 298     3883   4092   4027   -185    262     24       N  
ATOM   1114  CA  ILE A 298      -7.162  -3.469  10.081  1.00 30.25           C  
ANISOU 1114  CA  ILE A 298     3766   3927   3800   -166    328     57       C  
ATOM   1115  C   ILE A 298      -7.169  -1.973   9.755  1.00 29.01           C  
ANISOU 1115  C   ILE A 298     3606   3842   3574    -90    394     42       C  
ATOM   1116  O   ILE A 298      -7.163  -1.129  10.647  1.00 27.20           O  
ANISOU 1116  O   ILE A 298     3382   3643   3310    -90    452     73       O  
ATOM   1117  CB  ILE A 298      -5.730  -4.052   9.824  1.00 30.77           C  
ANISOU 1117  CB  ILE A 298     3892   3921   3878   -128    272     19       C  
ATOM   1118  CG1 ILE A 298      -5.636  -5.490  10.364  1.00 34.28           C  
ANISOU 1118  CG1 ILE A 298     4362   4251   4413   -200    165     39       C  
ATOM   1119  CG2 ILE A 298      -4.663  -3.156  10.442  1.00 29.66           C  
ANISOU 1119  CG2 ILE A 298     3797   3799   3673   -101    341     47       C  
ATOM   1120  CD1 ILE A 298      -4.711  -6.486   9.522  1.00 34.63           C  
ANISOU 1120  CD1 ILE A 298     4427   4215   4517   -124     34    -75       C  
ATOM   1121  N   LEU A 299      -7.166  -1.657   8.462  1.00 28.63           N  
ANISOU 1121  N   LEU A 299     3552   3819   3507    -29    363     -5       N  
ATOM   1122  CA  LEU A 299      -7.108  -0.262   8.036  1.00 27.92           C  
ANISOU 1122  CA  LEU A 299     3477   3772   3359     24    382      5       C  
ATOM   1123  C   LEU A 299      -8.390   0.482   8.404  1.00 27.38           C  
ANISOU 1123  C   LEU A 299     3361   3733   3310     40    393     -1       C  
ATOM   1124  O   LEU A 299      -8.337   1.622   8.860  1.00 27.24           O  
ANISOU 1124  O   LEU A 299     3362   3717   3273     76    403     10       O  
ATOM   1125  CB  LEU A 299      -6.812  -0.186   6.529  1.00 27.89           C  
ANISOU 1125  CB  LEU A 299     3474   3813   3309     60    334    -26       C  
ATOM   1126  CG  LEU A 299      -6.727   1.171   5.810  1.00 29.81           C  
ANISOU 1126  CG  LEU A 299     3744   4096   3486     84    313     15       C  
ATOM   1127  CD1 LEU A 299      -5.531   2.005   6.339  1.00 30.59           C  
ANISOU 1127  CD1 LEU A 299     3900   4184   3539     66    337     78       C  
ATOM   1128  CD2 LEU A 299      -6.629   0.969   4.286  1.00 30.46           C  
ANISOU 1128  CD2 LEU A 299     3807   4264   3502     95    263    -12       C  
ATOM   1129  N   ALA A 300      -9.538  -0.175   8.216  1.00 27.10           N  
ANISOU 1129  N   ALA A 300     3254   3724   3318     18    376    -32       N  
ATOM   1130  CA  ALA A 300     -10.837   0.466   8.478  1.00 27.50           C  
ANISOU 1130  CA  ALA A 300     3228   3838   3385     45    381    -67       C  
ATOM   1131  C   ALA A 300     -10.963   0.841   9.939  1.00 26.83           C  
ANISOU 1131  C   ALA A 300     3110   3804   3280     27    445    -62       C  
ATOM   1132  O   ALA A 300     -11.490   1.901  10.263  1.00 27.27           O  
ANISOU 1132  O   ALA A 300     3128   3906   3327     98    442   -115       O  
ATOM   1133  CB  ALA A 300     -12.019  -0.436   8.048  1.00 27.23           C  
ANISOU 1133  CB  ALA A 300     3106   3841   3399      4    353    -98       C  
ATOM   1134  N   GLY A 301     -10.468  -0.025  10.816  1.00 27.47           N  
ANISOU 1134  N   GLY A 301     3205   3880   3353    -62    486     -7       N  
ATOM   1135  CA  GLY A 301     -10.491   0.245  12.272  1.00 27.19           C  
ANISOU 1135  CA  GLY A 301     3138   3922   3273    -95    552      7       C  
ATOM   1136  C   GLY A 301      -9.616   1.413  12.707  1.00 27.08           C  
ANISOU 1136  C   GLY A 301     3191   3874   3225    -13    563     -9       C  
ATOM   1137  O   GLY A 301     -10.049   2.272  13.479  1.00 27.54           O  
ANISOU 1137  O   GLY A 301     3197   4013   3253     40    584    -68       O  
ATOM   1138  N   HIS A 302      -8.366   1.436  12.242  1.00 26.35           N  
ANISOU 1138  N   HIS A 302     3202   3672   3136     -2    539     33       N  
ATOM   1139  CA  HIS A 302      -7.471   2.556  12.556  1.00 26.12           C  
ANISOU 1139  CA  HIS A 302     3241   3598   3084     58    531     34       C  
ATOM   1140  C   HIS A 302      -7.961   3.887  11.985  1.00 26.26           C  
ANISOU 1140  C   HIS A 302     3256   3602   3118    153    464    -16       C  
ATOM   1141  O   HIS A 302      -7.765   4.925  12.597  1.00 27.08           O  
ANISOU 1141  O   HIS A 302     3382   3687   3221    212    437    -45       O  
ATOM   1142  CB  HIS A 302      -6.077   2.288  12.032  1.00 25.33           C  
ANISOU 1142  CB  HIS A 302     3228   3420   2976     37    516     87       C  
ATOM   1143  CG  HIS A 302      -5.266   1.364  12.883  1.00 25.81           C  
ANISOU 1143  CG  HIS A 302     3318   3459   3030    -26    550    125       C  
ATOM   1144  ND1 HIS A 302      -4.345   1.823  13.805  1.00 24.29           N  
ANISOU 1144  ND1 HIS A 302     3174   3242   2811    -22    571    147       N  
ATOM   1145  CD2 HIS A 302      -5.201   0.012  12.921  1.00 25.32           C  
ANISOU 1145  CD2 HIS A 302     3251   3375   2995    -90    539    144       C  
ATOM   1146  CE1 HIS A 302      -3.743   0.792  14.365  1.00 26.29           C  
ANISOU 1146  CE1 HIS A 302     3452   3468   3070    -81    578    180       C  
ATOM   1147  NE2 HIS A 302      -4.253  -0.319  13.860  1.00 25.42           N  
ANISOU 1147  NE2 HIS A 302     3313   3349   2996   -124    549    182       N  
ATOM   1148  N   ILE A 303      -8.574   3.855  10.803  1.00 26.24           N  
ANISOU 1148  N   ILE A 303     3237   3595   3139    171    413    -28       N  
ATOM   1149  CA  ILE A 303      -9.153   5.073  10.225  1.00 26.03           C  
ANISOU 1149  CA  ILE A 303     3213   3538   3139    258    315    -68       C  
ATOM   1150  C   ILE A 303     -10.293   5.590  11.087  1.00 26.85           C  
ANISOU 1150  C   ILE A 303     3220   3716   3266    335    309   -182       C  
ATOM   1151  O   ILE A 303     -10.349   6.783  11.409  1.00 27.54           O  
ANISOU 1151  O   ILE A 303     3324   3761   3379    428    226   -240       O  
ATOM   1152  CB  ILE A 303      -9.642   4.860   8.762  1.00 25.86           C  
ANISOU 1152  CB  ILE A 303     3188   3511   3127    256    255    -56       C  
ATOM   1153  CG1 ILE A 303      -8.439   4.601   7.838  1.00 25.06           C  
ANISOU 1153  CG1 ILE A 303     3166   3380   2975    197    248     33       C  
ATOM   1154  CG2 ILE A 303     -10.466   6.102   8.302  1.00 28.03           C  
ANISOU 1154  CG2 ILE A 303     3460   3747   3445    350    127   -104       C  
ATOM   1155  CD1 ILE A 303      -8.765   4.103   6.359  1.00 25.55           C  
ANISOU 1155  CD1 ILE A 303     3215   3480   3015    183    206     39       C  
ATOM   1156  N   ALA A 304     -11.207   4.697  11.445  1.00 27.32           N  
ANISOU 1156  N   ALA A 304     3168   3895   3316    296    381   -222       N  
ATOM   1157  CA  ALA A 304     -12.309   5.036  12.330  1.00 30.08           C  
ANISOU 1157  CA  ALA A 304     3384   4387   3657    353    400   -343       C  
ATOM   1158  C   ALA A 304     -11.838   5.665  13.650  1.00 31.30           C  
ANISOU 1158  C   ALA A 304     3537   4584   3771    394    428   -390       C  
ATOM   1159  O   ALA A 304     -12.415   6.679  14.101  1.00 32.49           O  
ANISOU 1159  O   ALA A 304     3623   4788   3934    522    367   -530       O  
ATOM   1160  CB  ALA A 304     -13.191   3.817  12.575  1.00 30.49           C  
ANISOU 1160  CB  ALA A 304     3313   4587   3684    249    485   -336       C  
ATOM   1161  N   ASP A 305     -10.776   5.098  14.245  1.00 31.47           N  
ANISOU 1161  N   ASP A 305     3631   4576   3750    303    499   -291       N  
ATOM   1162  CA  ASP A 305     -10.186   5.638  15.468  1.00 32.78           C  
ANISOU 1162  CA  ASP A 305     3811   4772   3871    335    522   -325       C  
ATOM   1163  C   ASP A 305      -9.686   7.076  15.264  1.00 34.19           C  
ANISOU 1163  C   ASP A 305     4075   4812   4106    462    396   -378       C  
ATOM   1164  O   ASP A 305      -9.852   7.922  16.146  1.00 34.63           O  
ANISOU 1164  O   ASP A 305     4089   4917   4153    563    359   -498       O  
ATOM   1165  CB  ASP A 305      -8.988   4.799  15.933  1.00 31.80           C  
ANISOU 1165  CB  ASP A 305     3775   4598   3709    218    590   -196       C  
ATOM   1166  CG  ASP A 305      -9.375   3.427  16.453  1.00 33.95           C  
ANISOU 1166  CG  ASP A 305     3981   4989   3930     78    679   -130       C  
ATOM   1167  OD1 ASP A 305     -10.593   3.125  16.625  1.00 35.88           O  
ANISOU 1167  OD1 ASP A 305     4092   5395   4147     51    711   -177       O  
ATOM   1168  OD2 ASP A 305      -8.429   2.643  16.703  1.00 32.88           O  
ANISOU 1168  OD2 ASP A 305     3926   4782   3784    -13    701    -25       O  
ATOM   1169  N   LEU A 306      -9.047   7.326  14.115  1.00 34.43           N  
ANISOU 1169  N   LEU A 306     4218   4677   4187    448    319   -286       N  
ATOM   1170  CA  LEU A 306      -8.486   8.649  13.795  1.00 36.92           C  
ANISOU 1170  CA  LEU A 306     4633   4837   4559    522    171   -286       C  
ATOM   1171  C   LEU A 306      -9.565   9.686  13.546  1.00 39.82           C  
ANISOU 1171  C   LEU A 306     4951   5182   4996    662     24   -420       C  
ATOM   1172  O   LEU A 306      -9.392  10.866  13.868  1.00 40.87           O  
ANISOU 1172  O   LEU A 306     5128   5214   5186    762   -119   -487       O  
ATOM   1173  CB  LEU A 306      -7.563   8.571  12.572  1.00 35.56           C  
ANISOU 1173  CB  LEU A 306     4574   4546   4393    435    131   -132       C  
ATOM   1174  CG  LEU A 306      -6.138   8.019  12.725  1.00 34.73           C  
ANISOU 1174  CG  LEU A 306     4540   4417   4239    331    210    -18       C  
ATOM   1175  CD1 LEU A 306      -5.484   7.885  11.357  1.00 33.01           C  
ANISOU 1175  CD1 LEU A 306     4383   4159   4001    252    176     99       C  
ATOM   1176  CD2 LEU A 306      -5.265   8.875  13.633  1.00 33.21           C  
ANISOU 1176  CD2 LEU A 306     4409   4153   4058    356    164    -19       C  
ATOM   1177  N   LEU A 307     -10.672   9.241  12.957  1.00 42.37           N  
ANISOU 1177  N   LEU A 307     5184   5588   5326    675     38   -466       N  
ATOM   1178  CA  LEU A 307     -11.815  10.106  12.688  1.00 46.37           C  
ANISOU 1178  CA  LEU A 307     5623   6091   5904    819   -106   -615       C  
ATOM   1179  C   LEU A 307     -12.520  10.467  13.988  1.00 49.52           C  
ANISOU 1179  C   LEU A 307     5879   6650   6285    942    -88   -822       C  
ATOM   1180  O   LEU A 307     -13.044  11.569  14.111  1.00 50.88           O  
ANISOU 1180  O   LEU A 307     6023   6777   6531   1107   -256   -983       O  
ATOM   1181  CB  LEU A 307     -12.790   9.452  11.703  1.00 45.94           C  
ANISOU 1181  CB  LEU A 307     5499   6098   5857    793    -88   -610       C  
ATOM   1182  CG  LEU A 307     -12.322   9.287  10.252  1.00 46.44           C  
ANISOU 1182  CG  LEU A 307     5682   6031   5933    709   -145   -449       C  
ATOM   1183  CD1 LEU A 307     -13.211   8.295   9.516  1.00 46.48           C  
ANISOU 1183  CD1 LEU A 307     5602   6135   5925    665    -81   -452       C  
ATOM   1184  CD2 LEU A 307     -12.262  10.628   9.504  1.00 46.33           C  
ANISOU 1184  CD2 LEU A 307     5772   5834   5997    785   -380   -434       C  
ATOM   1185  N   GLN A 308     -12.492   9.540  14.950  1.00 51.85           N  
ANISOU 1185  N   GLN A 308     6086   7137   6477    858     99   -818       N  
ATOM   1186  CA  GLN A 308     -13.028   9.717  16.315  1.00 55.96           C  
ANISOU 1186  CA  GLN A 308     6454   7881   6926    937    156   -996       C  
ATOM   1187  C   GLN A 308     -12.511  11.003  16.989  1.00 58.12           C  
ANISOU 1187  C   GLN A 308     6781   8059   7245   1088     16  -1120       C  
ATOM   1188  O   GLN A 308     -12.628  11.167  18.201  1.00 59.42           O  
ANISOU 1188  O   GLN A 308     6843   8401   7332   1149     66  -1258       O  
ATOM   1189  CB  GLN A 308     -12.667   8.483  17.170  1.00 55.31           C  
ANISOU 1189  CB  GLN A 308     6331   7967   6717    765    360   -887       C  
ATOM   1190  CG  GLN A 308     -13.522   8.239  18.429  1.00 58.94           C  
ANISOU 1190  CG  GLN A 308     6583   8761   7050    773    467  -1030       C  
ATOM   1191  CD  GLN A 308     -12.833   7.344  19.470  1.00 60.73           C  
ANISOU 1191  CD  GLN A 308     6820   9102   7150    611    616   -903       C  
ATOM   1192  OE1 GLN A 308     -12.444   7.813  20.541  1.00 60.99           O  
ANISOU 1192  OE1 GLN A 308     6835   9223   7113    664    627   -983       O  
ATOM   1193  NE2 GLN A 308     -12.681   6.053  19.154  1.00 60.94           N  
ANISOU 1193  NE2 GLN A 308     6882   9118   7155    416    707   -709       N  
ATOM   1194  N   SER A 309     -11.957  11.913  16.183  1.00 60.08           N  
ANISOU 1194  N   SER A 309     7185   8030   7611   1140   -173  -1067       N  
ATOM   1195  CA  SER A 309     -11.266  13.129  16.654  1.00 62.35           C  
ANISOU 1195  CA  SER A 309     7568   8151   7970   1252   -347  -1135       C  
ATOM   1196  C   SER A 309     -12.173  14.224  17.241  1.00 65.61           C  
ANISOU 1196  C   SER A 309     7867   8616   8447   1494   -523  -1434       C  
ATOM   1197  O   SER A 309     -11.873  15.419  17.133  1.00 66.91           O  
ANISOU 1197  O   SER A 309     8132   8556   8737   1615   -771  -1498       O  
ATOM   1198  CB  SER A 309     -10.377  13.707  15.543  1.00 61.62           C  
ANISOU 1198  CB  SER A 309     7679   7756   7978   1187   -509   -946       C  
ATOM   1199  OG  SER A 309     -11.161  14.279  14.508  1.00 62.85           O  
ANISOU 1199  OG  SER A 309     7846   7802   8233   1261   -692   -979       O  
ATOM   1200  N   ASP A 310     -13.275  13.803  17.859  1.00 67.82           N  
ANISOU 1200  N   ASP A 310     7930   9199   8639   1560   -410  -1620       N  
ATOM   1201  CA  ASP A 310     -14.138  14.681  18.644  1.00 70.97           C  
ANISOU 1201  CA  ASP A 310     8165   9745   9055   1801   -535  -1954       C  
ATOM   1202  C   ASP A 310     -14.400  14.013  20.004  1.00 72.14           C  
ANISOU 1202  C   ASP A 310     8119  10281   9009   1773   -307  -2065       C  
ATOM   1203  O   ASP A 310     -13.813  12.970  20.304  1.00 70.98           O  
ANISOU 1203  O   ASP A 310     8005  10219   8744   1564    -94  -1859       O  
ATOM   1204  CB  ASP A 310     -15.446  14.957  17.888  1.00 72.37           C  
ANISOU 1204  CB  ASP A 310     8226   9958   9312   1929   -656  -2109       C  
ATOM   1205  CG  ASP A 310     -16.102  16.280  18.293  1.00 75.31           C  
ANISOU 1205  CG  ASP A 310     8507  10315   9792   2230   -925  -2457       C  
ATOM   1206  OD1 ASP A 310     -15.973  16.692  19.467  1.00 76.35           O  
ANISOU 1206  OD1 ASP A 310     8550  10593   9867   2352   -930  -2659       O  
ATOM   1207  OD2 ASP A 310     -16.757  16.906  17.430  1.00 76.86           O  
ANISOU 1207  OD2 ASP A 310     8718  10352  10132   2355  -1150  -2540       O  
ATOM   1208  N   ARG A 311     -15.259  14.624  20.826  1.00 75.31           N  
ANISOU 1208  N   ARG A 311     8316  10924   9373   1982   -370  -2395       N  
ATOM   1209  CA  ARG A 311     -15.644  14.101  22.157  1.00 76.84           C  
ANISOU 1209  CA  ARG A 311     8287  11560   9351   1962   -167  -2531       C  
ATOM   1210  C   ARG A 311     -14.497  13.913  23.167  1.00 76.11           C  
ANISOU 1210  C   ARG A 311     8283  11484   9152   1870    -66  -2431       C  
ATOM   1211  O   ARG A 311     -14.746  13.573  24.328  1.00 77.45           O  
ANISOU 1211  O   ARG A 311     8277  12022   9129   1853     81  -2541       O  
ATOM   1212  CB  ARG A 311     -16.500  12.829  22.038  1.00 76.92           C  
ANISOU 1212  CB  ARG A 311     8127  11879   9219   1774     68  -2431       C  
ATOM   1213  CG  ARG A 311     -17.995  13.096  22.072  1.00 79.92           C  
ANISOU 1213  CG  ARG A 311     8229  12565   9572   1933     33  -2727       C  
ATOM   1214  CD  ARG A 311     -18.711  12.494  20.870  1.00 80.47           C  
ANISOU 1214  CD  ARG A 311     8290  12571   9714   1836     52  -2601       C  
ATOM   1215  NE  ARG A 311     -18.459  13.267  19.653  1.00 80.84           N  
ANISOU 1215  NE  ARG A 311     8542  12183   9990   1948   -191  -2563       N  
ATOM   1216  CZ  ARG A 311     -19.282  13.341  18.609  1.00 81.64           C  
ANISOU 1216  CZ  ARG A 311     8614  12207  10198   1999   -292  -2595       C  
ATOM   1217  NH1 ARG A 311     -20.446  12.697  18.615  1.00 82.65           N  
ANISOU 1217  NH1 ARG A 311     8504  12660  10239   1961   -170  -2683       N  
ATOM   1218  NH2 ARG A 311     -18.942  14.074  17.554  1.00 81.34           N  
ANISOU 1218  NH2 ARG A 311     8782  11773  10351   2078   -525  -2530       N  
ATOM   1219  N   ARG A 312     -13.255  14.118  22.717  1.00 74.09           N  
ANISOU 1219  N   ARG A 312     8288  10854   9011   1799   -146  -2217       N  
ATOM   1220  CA  ARG A 312     -12.131  14.367  23.626  1.00 73.31           C  
ANISOU 1220  CA  ARG A 312     8287  10697   8869   1789   -143  -2190       C  
ATOM   1221  C   ARG A 312     -12.073  15.872  23.925  1.00 74.43           C  
ANISOU 1221  C   ARG A 312     8450  10685   9144   2064   -428  -2464       C  
ATOM   1222  O   ARG A 312     -11.361  16.309  24.836  1.00 74.89           O  
ANISOU 1222  O   ARG A 312     8545  10737   9172   2124   -468  -2540       O  
ATOM   1223  CB  ARG A 312     -10.801  13.841  23.059  1.00 71.04           C  
ANISOU 1223  CB  ARG A 312     8245  10117   8631   1579    -92  -1846       C  
ATOM   1224  CG  ARG A 312     -10.092  14.755  22.056  1.00 71.76           C  
ANISOU 1224  CG  ARG A 312     8549   9787   8931   1623   -327  -1756       C  
ATOM   1225  CD  ARG A 312     -10.626  14.571  20.643  1.00 73.80           C  
ANISOU 1225  CD  ARG A 312     8845   9912   9282   1574   -374  -1644       C  
ATOM   1226  NE  ARG A 312      -9.923  15.417  19.677  1.00 74.62           N  
ANISOU 1226  NE  ARG A 312     9150   9645   9555   1577   -599  -1523       N  
ATOM   1227  CZ  ARG A 312     -10.291  16.654  19.346  1.00 76.78           C  
ANISOU 1227  CZ  ARG A 312     9458   9731   9984   1755   -887  -1672       C  
ATOM   1228  NH1 ARG A 312     -11.369  17.213  19.892  1.00 78.57           N  
ANISOU 1228  NH1 ARG A 312     9518  10107  10228   1981   -989  -1988       N  
ATOM   1229  NH2 ARG A 312      -9.580  17.332  18.456  1.00 76.88           N  
ANISOU 1229  NH2 ARG A 312     9664   9414  10132   1703  -1090  -1505       N  
ATOM   1230  N   ALA A 313     -12.824  16.644  23.131  1.00 74.53           N  
ANISOU 1230  N   ALA A 313     8446  10555   9316   2230   -646  -2610       N  
ATOM   1231  CA  ALA A 313     -13.209  18.020  23.456  1.00 76.17           C  
ANISOU 1231  CA  ALA A 313     8605  10684   9652   2536   -947  -2955       C  
ATOM   1232  C   ALA A 313     -14.437  17.993  24.374  1.00 77.86           C  
ANISOU 1232  C   ALA A 313     8496  11372   9715   2713   -870  -3320       C  
ATOM   1233  O   ALA A 313     -15.068  19.023  24.637  1.00 80.38           O  
ANISOU 1233  O   ALA A 313     8703  11714  10122   3004  -1111  -3680       O  
ATOM   1234  CB  ALA A 313     -13.520  18.798  22.180  1.00 76.64           C  
ANISOU 1234  CB  ALA A 313     8786  10386   9948   2626  -1235  -2941       C  
ATOM   1235  N   LEU A 314     -14.764  16.794  24.847  1.00 76.13           N  
ANISOU 1235  N   LEU A 314     8123  11539   9265   2527   -547  -3223       N  
ATOM   1236  CA  LEU A 314     -15.898  16.556  25.729  1.00 77.21           C  
ANISOU 1236  CA  LEU A 314     7928  12208   9200   2618   -416  -3510       C  
ATOM   1237  C   LEU A 314     -15.516  15.526  26.800  1.00 75.92           C  
ANISOU 1237  C   LEU A 314     7685  12396   8763   2396   -114  -3367       C  
ATOM   1238  O   LEU A 314     -16.267  15.302  27.747  1.00 77.97           O  
ANISOU 1238  O   LEU A 314     7669  13153   8804   2430     18  -3576       O  
ATOM   1239  CB  LEU A 314     -17.103  16.075  24.916  1.00 77.48           C  
ANISOU 1239  CB  LEU A 314     7813  12386   9240   2586   -359  -3521       C  
ATOM   1240  CG  LEU A 314     -18.518  16.413  25.380  1.00 80.27           C  
ANISOU 1240  CG  LEU A 314     7818  13176   9504   2805   -384  -3931       C  
ATOM   1241  CD1 LEU A 314     -18.835  17.887  25.152  1.00 81.70           C  
ANISOU 1241  CD1 LEU A 314     8001  13133   9908   3176   -759  -4293       C  
ATOM   1242  CD2 LEU A 314     -19.512  15.538  24.638  1.00 79.65           C  
ANISOU 1242  CD2 LEU A 314     7608  13271   9385   2659   -240  -3824       C  
ATOM   1243  N   GLN A 315     -14.350  14.896  26.644  1.00 72.14           N  
ANISOU 1243  N   GLN A 315     7442  11677   8292   2163    -15  -3011       N  
ATOM   1244  CA  GLN A 315     -13.824  14.008  27.686  1.00 70.91           C  
ANISOU 1244  CA  GLN A 315     7255  11785   7905   1961    219  -2862       C  
ATOM   1245  C   GLN A 315     -12.812  14.739  28.583  1.00 70.32           C  
ANISOU 1245  C   GLN A 315     7280  11612   7827   2074    119  -2959       C  
ATOM   1246  O   GLN A 315     -12.168  15.713  28.166  1.00 69.18           O  
ANISOU 1246  O   GLN A 315     7316  11072   7897   2221   -116  -3003       O  
ATOM   1247  CB  GLN A 315     -13.242  12.712  27.091  1.00 68.50           C  
ANISOU 1247  CB  GLN A 315     7111  11330   7586   1636    393  -2437       C  
ATOM   1248  CG  GLN A 315     -12.845  11.640  28.122  1.00 68.74           C  
ANISOU 1248  CG  GLN A 315     7101  11639   7377   1399    618  -2259       C  
ATOM   1249  CD  GLN A 315     -14.032  10.972  28.797  1.00 72.05           C  
ANISOU 1249  CD  GLN A 315     7224  12600   7553   1306    792  -2343       C  
ATOM   1250  OE1 GLN A 315     -14.519  11.430  29.835  1.00 75.20           O  
ANISOU 1250  OE1 GLN A 315     7407  13386   7780   1431    811  -2613       O  
ATOM   1251  NE2 GLN A 315     -14.491   9.868  28.218  1.00 72.27           N  
ANISOU 1251  NE2 GLN A 315     7229  12674   7555   1075    915  -2113       N  
ATOM   1252  N   LEU A 316     -12.698  14.256  29.820  1.00 70.58           N  
ANISOU 1252  N   LEU A 316     7190  12017   7611   1990    289  -2981       N  
ATOM   1253  CA  LEU A 316     -11.979  14.946  30.889  1.00 71.09           C  
ANISOU 1253  CA  LEU A 316     7277  12113   7621   2126    208  -3148       C  
ATOM   1254  C   LEU A 316     -10.478  14.662  30.942  1.00 68.40           C  
ANISOU 1254  C   LEU A 316     7212  11439   7337   1965    222  -2849       C  
ATOM   1255  O   LEU A 316      -9.720  15.474  31.462  1.00 68.73           O  
ANISOU 1255  O   LEU A 316     7344  11332   7437   2106     77  -2969       O  
ATOM   1256  CB  LEU A 316     -12.626  14.607  32.232  1.00 73.48           C  
ANISOU 1256  CB  LEU A 316     7291  13030   7598   2118    379  -3337       C  
ATOM   1257  CG  LEU A 316     -14.140  14.829  32.239  1.00 75.78           C  
ANISOU 1257  CG  LEU A 316     7263  13729   7801   2268    387  -3652       C  
ATOM   1258  CD1 LEU A 316     -14.827  13.887  33.215  1.00 77.73           C  
ANISOU 1258  CD1 LEU A 316     7233  14614   7686   2076    655  -3639       C  
ATOM   1259  CD2 LEU A 316     -14.455  16.290  32.545  1.00 78.62           C  
ANISOU 1259  CD2 LEU A 316     7520  14087   8265   2670    122  -4128       C  
ATOM   1260  N   ALA A 317     -10.060  13.521  30.399  1.00 65.93           N  
ANISOU 1260  N   ALA A 317     7025  11012   7015   1684    378  -2480       N  
ATOM   1261  CA  ALA A 317      -8.659  13.097  30.457  1.00 63.63           C  
ANISOU 1261  CA  ALA A 317     6969  10449   6760   1520    408  -2199       C  
ATOM   1262  C   ALA A 317      -7.724  13.907  29.554  1.00 62.09           C  
ANISOU 1262  C   ALA A 317     7014   9743   6836   1600    201  -2131       C  
ATOM   1263  O   ALA A 317      -8.114  14.362  28.470  1.00 61.13           O  
ANISOU 1263  O   ALA A 317     6931   9403   6890   1673     76  -2150       O  
ATOM   1264  CB  ALA A 317      -8.537  11.605  30.150  1.00 61.98           C  
ANISOU 1264  CB  ALA A 317     6805  10278   6465   1214    608  -1857       C  
ATOM   1265  N   ASP A 318      -6.491  14.082  30.028  1.00 61.56           N  
ANISOU 1265  N   ASP A 318     7098   9502   6789   1571    161  -2045       N  
ATOM   1266  CA  ASP A 318      -5.401  14.649  29.245  1.00 60.63           C  
ANISOU 1266  CA  ASP A 318     7211   8931   6893   1569     -1  -1910       C  
ATOM   1267  C   ASP A 318      -5.442  13.958  27.888  1.00 58.44           C  
ANISOU 1267  C   ASP A 318     7020   8474   6710   1407     58  -1656       C  
ATOM   1268  O   ASP A 318      -5.574  12.730  27.816  1.00 57.79           O  
ANISOU 1268  O   ASP A 318     6908   8534   6516   1219    252  -1476       O  
ATOM   1269  CB  ASP A 318      -4.064  14.371  29.963  1.00 60.11           C  
ANISOU 1269  CB  ASP A 318     7272   8790   6777   1464     43  -1767       C  
ATOM   1270  CG  ASP A 318      -2.842  15.011  29.270  1.00 60.42           C  
ANISOU 1270  CG  ASP A 318     7528   8401   7027   1450   -125  -1634       C  
ATOM   1271  OD1 ASP A 318      -2.884  15.314  28.054  1.00 60.60           O  
ANISOU 1271  OD1 ASP A 318     7632   8179   7213   1435   -225  -1543       O  
ATOM   1272  OD2 ASP A 318      -1.812  15.195  29.964  1.00 61.65           O  
ANISOU 1272  OD2 ASP A 318     7768   8485   7173   1439   -157  -1610       O  
ATOM   1273  N   ILE A 319      -5.355  14.743  26.816  1.00 57.98           N  
ANISOU 1273  N   ILE A 319     7067   8109   6855   1475   -128  -1644       N  
ATOM   1274  CA  ILE A 319      -5.408  14.192  25.454  1.00 56.35           C  
ANISOU 1274  CA  ILE A 319     6937   7744   6731   1337    -92  -1424       C  
ATOM   1275  C   ILE A 319      -4.327  13.123  25.211  1.00 53.79           C  
ANISOU 1275  C   ILE A 319     6732   7340   6367   1109     57  -1133       C  
ATOM   1276  O   ILE A 319      -4.520  12.218  24.397  1.00 52.71           O  
ANISOU 1276  O   ILE A 319     6601   7205   6222    975    163   -972       O  
ATOM   1277  CB  ILE A 319      -5.386  15.298  24.343  1.00 56.97           C  
ANISOU 1277  CB  ILE A 319     7123   7500   7022   1428   -343  -1434       C  
ATOM   1278  CG1 ILE A 319      -3.952  15.653  23.918  1.00 56.47           C  
ANISOU 1278  CG1 ILE A 319     7261   7132   7065   1326   -442  -1234       C  
ATOM   1279  CG2 ILE A 319      -6.198  16.540  24.786  1.00 59.05           C  
ANISOU 1279  CG2 ILE A 319     7297   7782   7359   1693   -563  -1760       C  
ATOM   1280  CD1 ILE A 319      -3.849  16.304  22.538  1.00 56.80           C  
ANISOU 1280  CD1 ILE A 319     7420   6890   7273   1299   -629  -1115       C  
ATOM   1281  N   ASP A 320      -3.212  13.225  25.940  1.00 52.97           N  
ANISOU 1281  N   ASP A 320     6711   7172   6242   1081     51  -1089       N  
ATOM   1282  CA  ASP A 320      -2.102  12.275  25.825  1.00 50.74           C  
ANISOU 1282  CA  ASP A 320     6533   6816   5929    893    165   -851       C  
ATOM   1283  C   ASP A 320      -2.434  10.910  26.432  1.00 49.56           C  
ANISOU 1283  C   ASP A 320     6302   6918   5612    765    368   -775       C  
ATOM   1284  O   ASP A 320      -2.131   9.875  25.835  1.00 48.15           O  
ANISOU 1284  O   ASP A 320     6171   6692   5434    614    457   -588       O  
ATOM   1285  CB  ASP A 320      -0.819  12.858  26.442  1.00 51.24           C  
ANISOU 1285  CB  ASP A 320     6704   6735   6030    910     77   -840       C  
ATOM   1286  CG  ASP A 320      -0.217  13.980  25.603  1.00 52.12           C  
ANISOU 1286  CG  ASP A 320     6933   6550   6321    950   -129   -811       C  
ATOM   1287  OD1 ASP A 320      -0.708  14.224  24.474  1.00 54.11           O  
ANISOU 1287  OD1 ASP A 320     7197   6700   6661    947   -196   -770       O  
ATOM   1288  OD2 ASP A 320       0.749  14.621  26.076  1.00 53.35           O  
ANISOU 1288  OD2 ASP A 320     7169   6576   6527    971   -235   -817       O  
ATOM   1289  N   ALA A 321      -3.066  10.911  27.607  1.00 49.74           N  
ANISOU 1289  N   ALA A 321     6196   7214   5489    821    424   -923       N  
ATOM   1290  CA  ALA A 321      -3.592   9.677  28.207  1.00 48.90           C  
ANISOU 1290  CA  ALA A 321     5991   7383   5206    676    596   -843       C  
ATOM   1291  C   ALA A 321      -4.706   9.047  27.351  1.00 48.18           C  
ANISOU 1291  C   ALA A 321     5810   7375   5120    612    661   -800       C  
ATOM   1292  O   ALA A 321      -4.783   7.827  27.220  1.00 47.31           O  
ANISOU 1292  O   ALA A 321     5702   7321   4954    433    765   -625       O  
ATOM   1293  CB  ALA A 321      -4.090   9.948  29.615  1.00 50.59           C  
ANISOU 1293  CB  ALA A 321     6061   7922   5237    747    634  -1024       C  
ATOM   1294  N   GLN A 322      -5.568   9.891  26.785  1.00 48.30           N  
ANISOU 1294  N   GLN A 322     5752   7386   5213    761    577   -967       N  
ATOM   1295  CA  GLN A 322      -6.675   9.444  25.932  1.00 48.04           C  
ANISOU 1295  CA  GLN A 322     5628   7427   5199    726    619   -954       C  
ATOM   1296  C   GLN A 322      -6.164   8.742  24.682  1.00 44.57           C  
ANISOU 1296  C   GLN A 322     5323   6739   4872    597    625   -732       C  
ATOM   1297  O   GLN A 322      -6.671   7.686  24.319  1.00 44.25           O  
ANISOU 1297  O   GLN A 322     5238   6780   4794    463    717   -620       O  
ATOM   1298  CB  GLN A 322      -7.571  10.625  25.523  1.00 49.68           C  
ANISOU 1298  CB  GLN A 322     5750   7630   5496    939    484  -1191       C  
ATOM   1299  CG  GLN A 322      -8.736  10.917  26.469  1.00 55.19           C  
ANISOU 1299  CG  GLN A 322     6216   8702   6051   1053    520  -1445       C  
ATOM   1300  CD  GLN A 322      -9.153  12.389  26.451  1.00 60.54           C  
ANISOU 1300  CD  GLN A 322     6846   9321   6836   1328    319  -1740       C  
ATOM   1301  OE1 GLN A 322      -8.649  13.185  25.657  1.00 62.10           O  
ANISOU 1301  OE1 GLN A 322     7195   9177   7224   1412    140  -1724       O  
ATOM   1302  NE2 GLN A 322     -10.065  12.759  27.346  1.00 64.19           N  
ANISOU 1302  NE2 GLN A 322     7091  10128   7172   1467    330  -2015       N  
ATOM   1303  N   ARG A 323      -5.155   9.334  24.040  1.00 42.36           N  
ANISOU 1303  N   ARG A 323     5198   6173   4724    634    518   -675       N  
ATOM   1304  CA  ARG A 323      -4.552   8.768  22.820  1.00 39.49           C  
ANISOU 1304  CA  ARG A 323     4949   5604   4451    526    517   -488       C  
ATOM   1305  C   ARG A 323      -3.835   7.428  23.077  1.00 37.90           C  
ANISOU 1305  C   ARG A 323     4797   5415   4188    356    626   -314       C  
ATOM   1306  O   ARG A 323      -3.988   6.496  22.292  1.00 36.42           O  
ANISOU 1306  O   ARG A 323     4617   5197   4022    257    668   -205       O  
ATOM   1307  CB  ARG A 323      -3.609   9.784  22.139  1.00 39.21           C  
ANISOU 1307  CB  ARG A 323     5046   5308   4544    584    373   -463       C  
ATOM   1308  CG  ARG A 323      -3.163   9.395  20.706  1.00 37.28           C  
ANISOU 1308  CG  ARG A 323     4885   4906   4374    491    360   -305       C  
ATOM   1309  CD  ARG A 323      -2.109  10.359  20.125  1.00 37.22           C  
ANISOU 1309  CD  ARG A 323     4997   4685   4459    500    226   -245       C  
ATOM   1310  NE  ARG A 323      -2.643  11.699  19.863  1.00 39.13           N  
ANISOU 1310  NE  ARG A 323     5246   4830   4790    625     49   -350       N  
ATOM   1311  CZ  ARG A 323      -2.348  12.791  20.573  1.00 40.62           C  
ANISOU 1311  CZ  ARG A 323     5467   4938   5027    726    -85   -450       C  
ATOM   1312  NH1 ARG A 323      -1.502  12.734  21.600  1.00 39.28           N  
ANISOU 1312  NH1 ARG A 323     5322   4787   4814    715    -47   -457       N  
ATOM   1313  NH2 ARG A 323      -2.897  13.953  20.253  1.00 40.74           N  
ANISOU 1313  NH2 ARG A 323     5494   4839   5146    845   -283   -551       N  
ATOM   1314  N   PHE A 324      -3.057   7.355  24.168  1.00 37.62           N  
ANISOU 1314  N   PHE A 324     4796   5413   4085    333    649   -300       N  
ATOM   1315  CA  PHE A 324      -2.379   6.121  24.611  1.00 36.41           C  
ANISOU 1315  CA  PHE A 324     4691   5269   3873    183    719   -148       C  
ATOM   1316  C   PHE A 324      -3.371   4.983  24.880  1.00 37.66           C  
ANISOU 1316  C   PHE A 324     4753   5619   3936     58    807    -88       C  
ATOM   1317  O   PHE A 324      -3.159   3.844  24.469  1.00 37.38           O  
ANISOU 1317  O   PHE A 324     4761   5516   3925    -68    821     52       O  
ATOM   1318  CB  PHE A 324      -1.561   6.377  25.898  1.00 36.61           C  
ANISOU 1318  CB  PHE A 324     4754   5333   3823    196    716   -169       C  
ATOM   1319  CG  PHE A 324      -0.726   5.191  26.337  1.00 33.78           C  
ANISOU 1319  CG  PHE A 324     4467   4942   3425     53    749    -11       C  
ATOM   1320  CD1 PHE A 324       0.608   5.087  25.947  1.00 32.14           C  
ANISOU 1320  CD1 PHE A 324     4379   4526   3307     43    698     62       C  
ATOM   1321  CD2 PHE A 324      -1.277   4.187  27.117  1.00 32.44           C  
ANISOU 1321  CD2 PHE A 324     4240   4954   3130    -77    813     65       C  
ATOM   1322  CE1 PHE A 324       1.376   3.991  26.319  1.00 31.38           C  
ANISOU 1322  CE1 PHE A 324     4346   4383   3193    -66    699    183       C  
ATOM   1323  CE2 PHE A 324      -0.518   3.084  27.502  1.00 34.04           C  
ANISOU 1323  CE2 PHE A 324     4525   5092   3316   -210    800    217       C  
ATOM   1324  CZ  PHE A 324       0.811   2.987  27.098  1.00 33.44           C  
ANISOU 1324  CZ  PHE A 324     4571   4787   3348   -189    737    263       C  
ATOM   1325  N   SER A 325      -4.432   5.295  25.613  1.00 38.75           N  
ANISOU 1325  N   SER A 325     4751   6009   3963     90    851   -201       N  
ATOM   1326  CA  SER A 325      -5.464   4.315  25.918  1.00 40.47           C  
ANISOU 1326  CA  SER A 325     4851   6455   4073    -51    932   -140       C  
ATOM   1327  C   SER A 325      -6.156   3.754  24.661  1.00 39.38           C  
ANISOU 1327  C   SER A 325     4693   6241   4030    -97    928    -86       C  
ATOM   1328  O   SER A 325      -6.388   2.552  24.563  1.00 39.38           O  
ANISOU 1328  O   SER A 325     4689   6261   4011   -264    952     59       O  
ATOM   1329  CB  SER A 325      -6.501   4.931  26.866  1.00 42.74           C  
ANISOU 1329  CB  SER A 325     4954   7076   4210     15    983   -312       C  
ATOM   1330  OG  SER A 325      -7.638   4.097  26.953  1.00 46.02           O  
ANISOU 1330  OG  SER A 325     5228   7733   4526   -127   1059   -258       O  
ATOM   1331  N   GLN A 326      -6.472   4.627  23.706  1.00 38.24           N  
ANISOU 1331  N   GLN A 326     4542   5997   3991     47    874   -198       N  
ATOM   1332  CA  GLN A 326      -7.162   4.210  22.495  1.00 37.46           C  
ANISOU 1332  CA  GLN A 326     4420   5838   3975     21    863   -167       C  
ATOM   1333  C   GLN A 326      -6.201   3.383  21.651  1.00 34.64           C  
ANISOU 1333  C   GLN A 326     4205   5245   3712    -61    831    -14       C  
ATOM   1334  O   GLN A 326      -6.560   2.298  21.190  1.00 33.37           O  
ANISOU 1334  O   GLN A 326     4033   5077   3570   -177    840     81       O  
ATOM   1335  CB  GLN A 326      -7.671   5.413  21.681  1.00 37.97           C  
ANISOU 1335  CB  GLN A 326     4458   5841   4129    198    787   -319       C  
ATOM   1336  CG  GLN A 326      -8.420   5.009  20.387  1.00 40.33           C  
ANISOU 1336  CG  GLN A 326     4731   6085   4507    176    769   -290       C  
ATOM   1337  CD  GLN A 326      -8.380   6.069  19.303  1.00 42.51           C  
ANISOU 1337  CD  GLN A 326     5065   6188   4900    316    656   -360       C  
ATOM   1338  OE1 GLN A 326      -7.308   6.468  18.847  1.00 40.72           O  
ANISOU 1338  OE1 GLN A 326     4972   5764   4734    334    595   -300       O  
ATOM   1339  NE2 GLN A 326      -9.558   6.501  18.850  1.00 44.37           N  
ANISOU 1339  NE2 GLN A 326     5195   6501   5161    400    619   -477       N  
ATOM   1340  N   TYR A 327      -4.971   3.888  21.487  1.00 32.65           N  
ANISOU 1340  N   TYR A 327     4075   4814   3516     -1    782     -2       N  
ATOM   1341  CA  TYR A 327      -3.973   3.202  20.676  1.00 31.15           C  
ANISOU 1341  CA  TYR A 327     3995   4436   3403    -55    749    105       C  
ATOM   1342  C   TYR A 327      -3.692   1.799  21.268  1.00 30.10           C  
ANISOU 1342  C   TYR A 327     3886   4317   3234   -202    767    225       C  
ATOM   1343  O   TYR A 327      -3.558   0.831  20.535  1.00 29.41           O  
ANISOU 1343  O   TYR A 327     3831   4137   3208   -265    733    292       O  
ATOM   1344  CB  TYR A 327      -2.680   4.035  20.523  1.00 30.68           C  
ANISOU 1344  CB  TYR A 327     4037   4230   3389     18    698     96       C  
ATOM   1345  CG  TYR A 327      -2.680   5.206  19.496  1.00 32.34           C  
ANISOU 1345  CG  TYR A 327     4268   4348   3671    118    629     42       C  
ATOM   1346  CD1 TYR A 327      -1.481   5.593  18.855  1.00 31.76           C  
ANISOU 1346  CD1 TYR A 327     4283   4139   3645    121    577     91       C  
ATOM   1347  CD2 TYR A 327      -3.848   5.909  19.175  1.00 33.58           C  
ANISOU 1347  CD2 TYR A 327     4353   4562   3843    196    601    -50       C  
ATOM   1348  CE1 TYR A 327      -1.443   6.665  17.923  1.00 34.49           C  
ANISOU 1348  CE1 TYR A 327     4656   4403   4044    174    493     80       C  
ATOM   1349  CE2 TYR A 327      -3.827   6.976  18.241  1.00 35.75           C  
ANISOU 1349  CE2 TYR A 327     4666   4727   4190    273    501    -78       C  
ATOM   1350  CZ  TYR A 327      -2.630   7.354  17.633  1.00 34.39           C  
ANISOU 1350  CZ  TYR A 327     4593   4417   4057    249    445      2       C  
ATOM   1351  OH  TYR A 327      -2.617   8.399  16.732  1.00 34.82           O  
ANISOU 1351  OH  TYR A 327     4688   4370   4170    289    328      9       O  
ATOM   1352  N   LEU A 328      -3.640   1.696  22.591  1.00 30.65           N  
ANISOU 1352  N   LEU A 328     3938   4505   3204   -256    800    247       N  
ATOM   1353  CA  LEU A 328      -3.380   0.417  23.237  1.00 30.02           C  
ANISOU 1353  CA  LEU A 328     3892   4426   3087   -412    785    383       C  
ATOM   1354  C   LEU A 328      -4.489  -0.598  22.952  1.00 30.21           C  
ANISOU 1354  C   LEU A 328     3844   4528   3107   -545    784    458       C  
ATOM   1355  O   LEU A 328      -4.215  -1.715  22.545  1.00 28.65           O  
ANISOU 1355  O   LEU A 328     3708   4197   2982   -636    711    556       O  
ATOM   1356  CB  LEU A 328      -3.171   0.580  24.743  1.00 31.85           C  
ANISOU 1356  CB  LEU A 328     4113   4803   3186   -457    818    402       C  
ATOM   1357  CG  LEU A 328      -2.990  -0.757  25.465  1.00 32.39           C  
ANISOU 1357  CG  LEU A 328     4223   4877   3207   -648    777    573       C  
ATOM   1358  CD1 LEU A 328      -1.657  -1.396  25.041  1.00 31.21           C  
ANISOU 1358  CD1 LEU A 328     4218   4460   3179   -641    675    632       C  
ATOM   1359  CD2 LEU A 328      -3.076  -0.593  26.991  1.00 36.97           C  
ANISOU 1359  CD2 LEU A 328     4761   5678   3609   -720    823    601       C  
ATOM   1360  N   LYS A 329      -5.738  -0.181  23.147  1.00 30.99           N  
ANISOU 1360  N   LYS A 329     3805   4842   3129   -546    851    395       N  
ATOM   1361  CA  LYS A 329      -6.890  -1.037  22.867  1.00 31.73           C  
ANISOU 1361  CA  LYS A 329     3806   5037   3213   -679    854    461       C  
ATOM   1362  C   LYS A 329      -6.849  -1.518  21.405  1.00 30.30           C  
ANISOU 1362  C   LYS A 329     3680   4646   3187   -648    784    465       C  
ATOM   1363  O   LYS A 329      -6.994  -2.710  21.136  1.00 30.68           O  
ANISOU 1363  O   LYS A 329     3753   4617   3287   -780    716    575       O  
ATOM   1364  CB  LYS A 329      -8.200  -0.304  23.184  1.00 32.39           C  
ANISOU 1364  CB  LYS A 329     3708   5405   3194   -643    939    344       C  
ATOM   1365  CG  LYS A 329      -9.433  -1.140  22.944  1.00 34.46           C  
ANISOU 1365  CG  LYS A 329     3851   5808   3436   -794    949    410       C  
ATOM   1366  CD  LYS A 329     -10.658  -0.638  23.725  1.00 35.46           C  
ANISOU 1366  CD  LYS A 329     3763   6311   3400   -813   1046    316       C  
ATOM   1367  CE  LYS A 329     -11.863  -1.538  23.458  1.00 38.30           C  
ANISOU 1367  CE  LYS A 329     3994   6819   3740   -993   1052    402       C  
ATOM   1368  NZ  LYS A 329     -13.140  -0.949  23.966  1.00 40.59           N  
ANISOU 1368  NZ  LYS A 329     4040   7500   3883   -978   1148    263       N  
ATOM   1369  N   ARG A 330      -6.620  -0.590  20.481  1.00 28.48           N  
ANISOU 1369  N   ARG A 330     3471   4323   3026   -479    783    348       N  
ATOM   1370  CA  ARG A 330      -6.488  -0.931  19.061  1.00 27.77           C  
ANISOU 1370  CA  ARG A 330     3429   4068   3056   -437    722    338       C  
ATOM   1371  C   ARG A 330      -5.339  -1.909  18.773  1.00 27.32           C  
ANISOU 1371  C   ARG A 330     3490   3819   3073   -478    639    412       C  
ATOM   1372  O   ARG A 330      -5.518  -2.818  17.984  1.00 28.31           O  
ANISOU 1372  O   ARG A 330     3625   3856   3274   -519    570    436       O  
ATOM   1373  CB  ARG A 330      -6.360   0.327  18.198  1.00 26.10           C  
ANISOU 1373  CB  ARG A 330     3225   3809   2881   -271    725    225       C  
ATOM   1374  CG  ARG A 330      -6.200   0.084  16.678  1.00 25.03           C  
ANISOU 1374  CG  ARG A 330     3129   3545   2836   -228    668    212       C  
ATOM   1375  CD  ARG A 330      -7.390  -0.705  16.049  1.00 29.37           C  
ANISOU 1375  CD  ARG A 330     3600   4139   3419   -290    650    218       C  
ATOM   1376  NE  ARG A 330      -8.654   0.009  16.230  1.00 30.21           N  
ANISOU 1376  NE  ARG A 330     3589   4403   3487   -256    694    148       N  
ATOM   1377  CZ  ARG A 330      -9.863  -0.473  15.933  1.00 31.97           C  
ANISOU 1377  CZ  ARG A 330     3710   4717   3719   -312    694    141       C  
ATOM   1378  NH1 ARG A 330     -10.013  -1.688  15.408  1.00 30.37           N  
ANISOU 1378  NH1 ARG A 330     3521   4445   3575   -412    641    211       N  
ATOM   1379  NH2 ARG A 330     -10.931   0.285  16.158  1.00 32.60           N  
ANISOU 1379  NH2 ARG A 330     3667   4960   3758   -258    731     48       N  
ATOM   1380  N   SER A 331      -4.165  -1.699  19.387  1.00 26.53           N  
ANISOU 1380  N   SER A 331     3471   3654   2956   -452    633    427       N  
ATOM   1381  CA  SER A 331      -3.058  -2.644  19.269  1.00 26.82           C  
ANISOU 1381  CA  SER A 331     3604   3526   3060   -480    540    475       C  
ATOM   1382  C   SER A 331      -3.437  -4.035  19.805  1.00 27.98           C  
ANISOU 1382  C   SER A 331     3763   3643   3224   -644    455    595       C  
ATOM   1383  O   SER A 331      -3.055  -5.047  19.224  1.00 28.72           O  
ANISOU 1383  O   SER A 331     3909   3584   3420   -661    335    608       O  
ATOM   1384  CB  SER A 331      -1.790  -2.096  19.943  1.00 26.13           C  
ANISOU 1384  CB  SER A 331     3586   3396   2944   -425    549    465       C  
ATOM   1385  OG  SER A 331      -1.164  -1.153  19.081  1.00 25.92           O  
ANISOU 1385  OG  SER A 331     3573   3333   2944   -298    570    378       O  
ATOM   1386  N   LEU A 332      -4.213  -4.075  20.892  1.00 28.79           N  
ANISOU 1386  N   LEU A 332     3811   3904   3225   -768    503    678       N  
ATOM   1387  CA  LEU A 332      -4.718  -5.325  21.431  1.00 29.94           C  
ANISOU 1387  CA  LEU A 332     3959   4050   3369   -969    414    829       C  
ATOM   1388  C   LEU A 332      -5.626  -6.059  20.441  1.00 30.00           C  
ANISOU 1388  C   LEU A 332     3921   4011   3468  -1021    349    837       C  
ATOM   1389  O   LEU A 332      -5.535  -7.276  20.282  1.00 29.15           O  
ANISOU 1389  O   LEU A 332     3872   3749   3455  -1125    193    924       O  
ATOM   1390  CB  LEU A 332      -5.453  -5.087  22.768  1.00 31.53           C  
ANISOU 1390  CB  LEU A 332     4075   4507   3400  -1107    502    915       C  
ATOM   1391  CG  LEU A 332      -4.742  -5.170  24.136  1.00 33.85           C  
ANISOU 1391  CG  LEU A 332     4427   4845   3588  -1190    492   1011       C  
ATOM   1392  CD1 LEU A 332      -3.264  -5.013  24.090  1.00 32.16           C  
ANISOU 1392  CD1 LEU A 332     4343   4426   3449  -1064    435    963       C  
ATOM   1393  CD2 LEU A 332      -5.384  -4.283  25.241  1.00 34.25           C  
ANISOU 1393  CD2 LEU A 332     4355   5221   3438  -1215    639    985       C  
ATOM   1394  N   LEU A 333      -6.509  -5.308  19.792  1.00 29.72           N  
ANISOU 1394  N   LEU A 333     3783   4098   3412   -943    447    739       N  
ATOM   1395  CA  LEU A 333      -7.372  -5.860  18.743  1.00 31.29           C  
ANISOU 1395  CA  LEU A 333     3932   4260   3698   -965    393    722       C  
ATOM   1396  C   LEU A 333      -6.575  -6.303  17.512  1.00 30.83           C  
ANISOU 1396  C   LEU A 333     3961   3976   3779   -848    283    642       C  
ATOM   1397  O   LEU A 333      -6.849  -7.358  16.945  1.00 32.86           O  
ANISOU 1397  O   LEU A 333     4233   4116   4137   -910    152    669       O  
ATOM   1398  CB  LEU A 333      -8.444  -4.844  18.345  1.00 31.02           C  
ANISOU 1398  CB  LEU A 333     3768   4410   3607   -887    515    619       C  
ATOM   1399  CG  LEU A 333      -9.479  -4.523  19.441  1.00 31.80           C  
ANISOU 1399  CG  LEU A 333     3729   4790   3562   -999    615    659       C  
ATOM   1400  CD1 LEU A 333     -10.218  -3.195  19.131  1.00 30.70           C  
ANISOU 1400  CD1 LEU A 333     3474   4814   3375   -842    723    495       C  
ATOM   1401  CD2 LEU A 333     -10.475  -5.655  19.633  1.00 35.17           C  
ANISOU 1401  CD2 LEU A 333     4082   5294   3987  -1225    557    794       C  
ATOM   1402  N   ASP A 334      -5.601  -5.499  17.104  1.00 29.73           N  
ANISOU 1402  N   ASP A 334     3867   3791   3636   -684    328    540       N  
ATOM   1403  CA  ASP A 334      -4.734  -5.855  15.971  1.00 29.63           C  
ANISOU 1403  CA  ASP A 334     3911   3627   3719   -570    239    447       C  
ATOM   1404  C   ASP A 334      -4.036  -7.185  16.225  1.00 30.68           C  
ANISOU 1404  C   ASP A 334     4126   3585   3946   -631     67    493       C  
ATOM   1405  O   ASP A 334      -3.956  -8.026  15.328  1.00 30.60           O  
ANISOU 1405  O   ASP A 334     4129   3456   4041   -595    -64    429       O  
ATOM   1406  CB  ASP A 334      -3.658  -4.809  15.755  1.00 28.05           C  
ANISOU 1406  CB  ASP A 334     3741   3439   3476   -431    312    366       C  
ATOM   1407  CG  ASP A 334      -4.187  -3.494  15.183  1.00 29.17           C  
ANISOU 1407  CG  ASP A 334     3825   3697   3562   -346    422    304       C  
ATOM   1408  OD1 ASP A 334      -5.360  -3.408  14.721  1.00 29.12           O  
ANISOU 1408  OD1 ASP A 334     3749   3757   3558   -360    441    291       O  
ATOM   1409  OD2 ASP A 334      -3.374  -2.543  15.191  1.00 28.23           O  
ANISOU 1409  OD2 ASP A 334     3734   3590   3403   -266    470    271       O  
ATOM   1410  N   ALA A 335      -3.516  -7.353  17.446  1.00 31.46           N  
ANISOU 1410  N   ALA A 335     4281   3663   4008   -712     49    590       N  
ATOM   1411  CA  ALA A 335      -2.886  -8.607  17.874  1.00 33.26           C  
ANISOU 1411  CA  ALA A 335     4601   3707   4331   -785   -147    656       C  
ATOM   1412  C   ALA A 335      -3.882  -9.785  17.985  1.00 35.80           C  
ANISOU 1412  C   ALA A 335     4921   3959   4724   -967   -294    780       C  
ATOM   1413  O   ALA A 335      -3.662 -10.846  17.394  1.00 36.11           O  
ANISOU 1413  O   ALA A 335     5009   3804   4908   -955   -497    744       O  
ATOM   1414  CB  ALA A 335      -2.156  -8.399  19.214  1.00 33.57           C  
ANISOU 1414  CB  ALA A 335     4701   3758   4296   -841   -128    748       C  
ATOM   1415  N   ARG A 336      -4.965  -9.599  18.742  1.00 37.03           N  
ANISOU 1415  N   ARG A 336     5010   4281   4777  -1136   -205    917       N  
ATOM   1416  CA  ARG A 336      -5.929 -10.674  18.993  1.00 40.44           C  
ANISOU 1416  CA  ARG A 336     5429   4681   5254  -1358   -340   1074       C  
ATOM   1417  C   ARG A 336      -6.642 -11.131  17.711  1.00 40.69           C  
ANISOU 1417  C   ARG A 336     5415   4640   5404  -1317   -417    989       C  
ATOM   1418  O   ARG A 336      -6.790 -12.331  17.457  1.00 42.26           O  
ANISOU 1418  O   ARG A 336     5666   4650   5742  -1412   -643   1046       O  
ATOM   1419  CB  ARG A 336      -6.968 -10.255  20.056  1.00 41.56           C  
ANISOU 1419  CB  ARG A 336     5469   5100   5223  -1549   -196   1221       C  
ATOM   1420  CG  ARG A 336      -8.000 -11.347  20.418  1.00 46.08           C  
ANISOU 1420  CG  ARG A 336     6009   5687   5813  -1832   -329   1423       C  
ATOM   1421  CD  ARG A 336      -9.285 -10.769  21.036  1.00 49.36           C  
ANISOU 1421  CD  ARG A 336     6251   6459   6043  -1978   -142   1494       C  
ATOM   1422  NE  ARG A 336     -10.152 -10.159  20.023  1.00 49.36           N  
ANISOU 1422  NE  ARG A 336     6129   6564   6060  -1852    -27   1339       N  
ATOM   1423  CZ  ARG A 336     -11.310  -9.544  20.263  1.00 49.91           C  
ANISOU 1423  CZ  ARG A 336     6024   6941   5997  -1909    133   1326       C  
ATOM   1424  NH1 ARG A 336     -11.786  -9.432  21.499  1.00 52.30           N  
ANISOU 1424  NH1 ARG A 336     6232   7523   6118  -2096    219   1452       N  
ATOM   1425  NH2 ARG A 336     -12.000  -9.039  19.250  1.00 49.25           N  
ANISOU 1425  NH2 ARG A 336     5851   6904   5958  -1774    200   1175       N  
ATOM   1426  N   ASP A 337      -7.078 -10.171  16.910  1.00 39.73           N  
ANISOU 1426  N   ASP A 337     5204   4658   5235  -1177   -250    852       N  
ATOM   1427  CA  ASP A 337      -7.906 -10.477  15.752  1.00 40.29           C  
ANISOU 1427  CA  ASP A 337     5216   4705   5389  -1147   -299    777       C  
ATOM   1428  C   ASP A 337      -7.111 -10.757  14.481  1.00 39.70           C  
ANISOU 1428  C   ASP A 337     5192   4462   5430   -948   -405    596       C  
ATOM   1429  O   ASP A 337      -7.573 -11.502  13.620  1.00 40.42           O  
ANISOU 1429  O   ASP A 337     5272   4455   5633   -945   -541    545       O  
ATOM   1430  CB  ASP A 337      -8.932  -9.362  15.535  1.00 40.16           C  
ANISOU 1430  CB  ASP A 337     5067   4931   5261  -1113    -92    730       C  
ATOM   1431  CG  ASP A 337      -9.886  -9.225  16.706  1.00 41.92           C  
ANISOU 1431  CG  ASP A 337     5197   5368   5362  -1312     -2    877       C  
ATOM   1432  OD1 ASP A 337      -9.980 -10.187  17.485  1.00 45.40           O  
ANISOU 1432  OD1 ASP A 337     5671   5763   5817  -1521   -121   1048       O  
ATOM   1433  OD2 ASP A 337     -10.536  -8.175  16.859  1.00 43.38           O  
ANISOU 1433  OD2 ASP A 337     5272   5777   5435  -1264    172    821       O  
ATOM   1434  N   HIS A 338      -5.916 -10.178  14.361  1.00 38.26           N  
ANISOU 1434  N   HIS A 338     5054   4266   5216   -787   -349    492       N  
ATOM   1435  CA  HIS A 338      -5.141 -10.330  13.122  1.00 38.26           C  
ANISOU 1435  CA  HIS A 338     5068   4184   5284   -596   -421    302       C  
ATOM   1436  C   HIS A 338      -3.678 -10.740  13.293  1.00 38.04           C  
ANISOU 1436  C   HIS A 338     5118   4028   5306   -501   -532    228       C  
ATOM   1437  O   HIS A 338      -2.954 -10.861  12.311  1.00 38.62           O  
ANISOU 1437  O   HIS A 338     5180   4080   5415   -338   -587     50       O  
ATOM   1438  CB  HIS A 338      -5.253  -9.081  12.254  1.00 36.68           C  
ANISOU 1438  CB  HIS A 338     4798   4155   4984   -462   -237    196       C  
ATOM   1439  CG  HIS A 338      -6.652  -8.563  12.131  1.00 38.59           C  
ANISOU 1439  CG  HIS A 338     4957   4528   5178   -529   -133    247       C  
ATOM   1440  ND1 HIS A 338      -7.527  -9.009  11.164  1.00 40.04           N  
ANISOU 1440  ND1 HIS A 338     5090   4699   5423   -525   -201    194       N  
ATOM   1441  CD2 HIS A 338      -7.333  -7.654  12.866  1.00 37.79           C  
ANISOU 1441  CD2 HIS A 338     4803   4578   4975   -591     21    326       C  
ATOM   1442  CE1 HIS A 338      -8.683  -8.387  11.302  1.00 41.05           C  
ANISOU 1442  CE1 HIS A 338     5137   4966   5492   -585    -89    244       C  
ATOM   1443  NE2 HIS A 338      -8.590  -7.558  12.326  1.00 39.25           N  
ANISOU 1443  NE2 HIS A 338     4903   4846   5166   -619     44    315       N  
ATOM   1444  N   GLY A 339      -3.251 -10.981  14.522  1.00 38.37           N  
ANISOU 1444  N   GLY A 339     5230   4005   5344   -603   -574    355       N  
ATOM   1445  CA  GLY A 339      -1.841 -11.294  14.787  1.00 38.73           C  
ANISOU 1445  CA  GLY A 339     5346   3935   5435   -508   -679    282       C  
ATOM   1446  C   GLY A 339      -0.811 -10.231  14.396  1.00 37.13           C  
ANISOU 1446  C   GLY A 339     5109   3861   5138   -339   -521    149       C  
ATOM   1447  O   GLY A 339       0.364 -10.569  14.174  1.00 37.64           O  
ANISOU 1447  O   GLY A 339     5194   3856   5252   -218   -621     21       O  
ATOM   1448  N   LEU A 340      -1.218  -8.960  14.322  1.00 34.73           N  
ANISOU 1448  N   LEU A 340     4750   3742   4705   -333   -297    175       N  
ATOM   1449  CA  LEU A 340      -0.261  -7.887  14.009  1.00 33.58           C  
ANISOU 1449  CA  LEU A 340     4579   3710   4469   -210   -165     86       C  
ATOM   1450  C   LEU A 340       0.538  -7.491  15.245  1.00 32.37           C  
ANISOU 1450  C   LEU A 340     4482   3547   4271   -243   -123    163       C  
ATOM   1451  O   LEU A 340      -0.006  -7.438  16.352  1.00 33.25           O  
ANISOU 1451  O   LEU A 340     4625   3660   4349   -367    -93    306       O  
ATOM   1452  CB  LEU A 340      -0.921  -6.647  13.411  1.00 32.91           C  
ANISOU 1452  CB  LEU A 340     4429   3792   4284   -186     12     83       C  
ATOM   1453  CG  LEU A 340      -1.793  -6.710  12.154  1.00 35.01           C  
ANISOU 1453  CG  LEU A 340     4632   4109   4561   -151      8     15       C  
ATOM   1454  CD1 LEU A 340      -2.181  -5.303  11.810  1.00 36.91           C  
ANISOU 1454  CD1 LEU A 340     4832   4494   4698   -126    166     30       C  
ATOM   1455  CD2 LEU A 340      -1.146  -7.379  10.950  1.00 37.52           C  
ANISOU 1455  CD2 LEU A 340     4921   4412   4924    -34   -101   -151       C  
ATOM   1456  N   PRO A 341       1.840  -7.233  15.072  1.00 30.64           N  
ANISOU 1456  N   PRO A 341     4265   3338   4039   -136   -125     65       N  
ATOM   1457  CA  PRO A 341       2.615  -7.052  16.293  1.00 29.40           C  
ANISOU 1457  CA  PRO A 341     4169   3142   3860   -169   -122    135       C  
ATOM   1458  C   PRO A 341       2.561  -5.605  16.789  1.00 27.59           C  
ANISOU 1458  C   PRO A 341     3926   3047   3510   -184     67    197       C  
ATOM   1459  O   PRO A 341       2.296  -4.697  16.009  1.00 25.97           O  
ANISOU 1459  O   PRO A 341     3665   2952   3249   -139    174    157       O  
ATOM   1460  CB  PRO A 341       4.038  -7.423  15.872  1.00 29.40           C  
ANISOU 1460  CB  PRO A 341     4159   3105   3907    -41   -218    -16       C  
ATOM   1461  CG  PRO A 341       4.093  -7.190  14.402  1.00 29.98           C  
ANISOU 1461  CG  PRO A 341     4139   3297   3955     62   -179   -162       C  
ATOM   1462  CD  PRO A 341       2.689  -7.385  13.873  1.00 31.61           C  
ANISOU 1462  CD  PRO A 341     4329   3505   4177      6   -169   -118       C  
ATOM   1463  N   ALA A 342       2.786  -5.422  18.090  1.00 26.64           N  
ANISOU 1463  N   ALA A 342     3860   2908   3354   -250     83    293       N  
ATOM   1464  CA  ALA A 342       3.075  -4.089  18.643  1.00 25.79           C  
ANISOU 1464  CA  ALA A 342     3748   2900   3150   -232    220    314       C  
ATOM   1465  C   ALA A 342       4.007  -4.348  19.819  1.00 25.58           C  
ANISOU 1465  C   ALA A 342     3791   2806   3123   -255    161    357       C  
ATOM   1466  O   ALA A 342       4.146  -5.507  20.249  1.00 26.48           O  
ANISOU 1466  O   ALA A 342     3957   2802   3302   -307     21    398       O  
ATOM   1467  CB  ALA A 342       1.795  -3.401  19.104  1.00 24.76           C  
ANISOU 1467  CB  ALA A 342     3588   2875   2946   -298    327    387       C  
ATOM   1468  N   CYS A 343       4.628  -3.286  20.333  1.00 25.16           N  
ANISOU 1468  N   CYS A 343     3744   2811   3007   -221    245    352       N  
ATOM   1469  CA  CYS A 343       5.547  -3.406  21.459  1.00 25.66           C  
ANISOU 1469  CA  CYS A 343     3869   2820   3059   -235    196    385       C  
ATOM   1470  C   CYS A 343       5.368  -2.310  22.505  1.00 25.52           C  
ANISOU 1470  C   CYS A 343     3862   2894   2942   -258    298    435       C  
ATOM   1471  O   CYS A 343       5.233  -1.128  22.162  1.00 24.86           O  
ANISOU 1471  O   CYS A 343     3739   2886   2821   -207    392    392       O  
ATOM   1472  CB  CYS A 343       6.990  -3.391  20.970  1.00 25.70           C  
ANISOU 1472  CB  CYS A 343     3866   2787   3113   -136    146    279       C  
ATOM   1473  SG  CYS A 343       8.154  -3.978  22.245  1.00 30.24           S  
ANISOU 1473  SG  CYS A 343     4523   3252   3715   -144     24    305       S  
ATOM   1474  N   LEU A 344       5.362  -2.717  23.777  1.00 26.07           N  
ANISOU 1474  N   LEU A 344     3984   2953   2966   -337    258    522       N  
ATOM   1475  CA  LEU A 344       5.339  -1.785  24.896  1.00 26.92           C  
ANISOU 1475  CA  LEU A 344     4100   3159   2970   -346    334    545       C  
ATOM   1476  C   LEU A 344       6.694  -1.813  25.579  1.00 26.76           C  
ANISOU 1476  C   LEU A 344     4144   3061   2964   -315    267    537       C  
ATOM   1477  O   LEU A 344       7.174  -2.895  25.968  1.00 27.92           O  
ANISOU 1477  O   LEU A 344     4351   3105   3153   -362    142    589       O  
ATOM   1478  CB  LEU A 344       4.294  -2.210  25.934  1.00 28.71           C  
ANISOU 1478  CB  LEU A 344     4323   3491   3096   -477    348    656       C  
ATOM   1479  CG  LEU A 344       2.908  -1.571  25.988  1.00 31.39           C  
ANISOU 1479  CG  LEU A 344     4571   4014   3343   -501    464    646       C  
ATOM   1480  CD1 LEU A 344       2.030  -2.358  26.940  1.00 34.17           C  
ANISOU 1480  CD1 LEU A 344     4906   4487   3591   -669    452    777       C  
ATOM   1481  CD2 LEU A 344       2.966  -0.087  26.417  1.00 30.54           C  
ANISOU 1481  CD2 LEU A 344     4426   4012   3164   -397    554    547       C  
ATOM   1482  N   TYR A 345       7.296  -0.644  25.732  1.00 24.44           N  
ANISOU 1482  N   TYR A 345     3839   2802   2644   -239    325    473       N  
ATOM   1483  CA  TYR A 345       8.495  -0.479  26.544  1.00 24.20           C  
ANISOU 1483  CA  TYR A 345     3861   2723   2611   -213    274    464       C  
ATOM   1484  C   TYR A 345       8.116   0.325  27.774  1.00 24.45           C  
ANISOU 1484  C   TYR A 345     3901   2862   2525   -230    330    483       C  
ATOM   1485  O   TYR A 345       7.475   1.386  27.650  1.00 24.43           O  
ANISOU 1485  O   TYR A 345     3849   2950   2483   -187    413    432       O  
ATOM   1486  CB  TYR A 345       9.576   0.317  25.770  1.00 22.48           C  
ANISOU 1486  CB  TYR A 345     3614   2475   2454   -122    283    372       C  
ATOM   1487  CG  TYR A 345      10.435  -0.467  24.794  1.00 22.29           C  
ANISOU 1487  CG  TYR A 345     3567   2381   2522    -84    211    315       C  
ATOM   1488  CD1 TYR A 345      11.463  -1.309  25.250  1.00 23.03           C  
ANISOU 1488  CD1 TYR A 345     3698   2386   2665    -67     93    296       C  
ATOM   1489  CD2 TYR A 345      10.237  -0.359  23.400  1.00 21.73           C  
ANISOU 1489  CD2 TYR A 345     3425   2349   2484    -54    247    261       C  
ATOM   1490  CE1 TYR A 345      12.276  -2.023  24.347  1.00 23.35           C  
ANISOU 1490  CE1 TYR A 345     3693   2388   2791     -4     12    199       C  
ATOM   1491  CE2 TYR A 345      11.022  -1.073  22.505  1.00 21.73           C  
ANISOU 1491  CE2 TYR A 345     3377   2331   2547     -5    182    177       C  
ATOM   1492  CZ  TYR A 345      12.035  -1.914  22.982  1.00 24.54           C  
ANISOU 1492  CZ  TYR A 345     3759   2608   2957     29     63    133       C  
ATOM   1493  OH  TYR A 345      12.816  -2.632  22.102  1.00 24.03           O  
ANISOU 1493  OH  TYR A 345     3628   2548   2957    103    -17      8       O  
ATOM   1494  N   ALA A 346       8.560  -0.136  28.941  1.00 24.47           N  
ANISOU 1494  N   ALA A 346     3964   2857   2475   -279    269    543       N  
ATOM   1495  CA  ALA A 346       8.514   0.661  30.162  1.00 24.57           C  
ANISOU 1495  CA  ALA A 346     3983   2982   2369   -274    308    533       C  
ATOM   1496  C   ALA A 346       9.921   1.048  30.641  1.00 24.65           C  
ANISOU 1496  C   ALA A 346     4046   2907   2415   -210    246    489       C  
ATOM   1497  O   ALA A 346      10.754   0.162  30.918  1.00 25.47           O  
ANISOU 1497  O   ALA A 346     4210   2906   2561   -238    141    535       O  
ATOM   1498  CB  ALA A 346       7.802  -0.115  31.259  1.00 24.70           C  
ANISOU 1498  CB  ALA A 346     4019   3113   2255   -405    292    651       C  
ATOM   1499  N   PHE A 347      10.164   2.349  30.799  1.00 23.74           N  
ANISOU 1499  N   PHE A 347     3907   2827   2286   -127    287    399       N  
ATOM   1500  CA  PHE A 347      11.449   2.831  31.310  1.00 24.38           C  
ANISOU 1500  CA  PHE A 347     4029   2838   2397    -74    227    357       C  
ATOM   1501  C   PHE A 347      11.282   3.334  32.744  1.00 25.06           C  
ANISOU 1501  C   PHE A 347     4135   3035   2352    -69    229    341       C  
ATOM   1502  O   PHE A 347      10.658   4.360  32.964  1.00 25.45           O  
ANISOU 1502  O   PHE A 347     4141   3180   2348    -13    279    261       O  
ATOM   1503  CB  PHE A 347      12.000   3.941  30.414  1.00 23.57           C  
ANISOU 1503  CB  PHE A 347     3890   2677   2389      1    237    276       C  
ATOM   1504  CG  PHE A 347      12.178   3.536  28.972  1.00 24.89           C  
ANISOU 1504  CG  PHE A 347     4017   2787   2652     -7    245    281       C  
ATOM   1505  CD1 PHE A 347      13.337   2.870  28.562  1.00 27.61           C  
ANISOU 1505  CD1 PHE A 347     4361   3058   3070     -3    182    272       C  
ATOM   1506  CD2 PHE A 347      11.184   3.814  28.016  1.00 24.13           C  
ANISOU 1506  CD2 PHE A 347     3872   2730   2565     -8    307    277       C  
ATOM   1507  CE1 PHE A 347      13.517   2.487  27.223  1.00 27.61           C  
ANISOU 1507  CE1 PHE A 347     4302   3050   3138      2    189    249       C  
ATOM   1508  CE2 PHE A 347      11.364   3.425  26.664  1.00 25.97           C  
ANISOU 1508  CE2 PHE A 347     4062   2936   2869    -15    313    276       C  
ATOM   1509  CZ  PHE A 347      12.515   2.768  26.279  1.00 25.09           C  
ANISOU 1509  CZ  PHE A 347     3940   2778   2814     -9    258    257       C  
ATOM   1510  N   GLU A 348      11.827   2.605  33.706  1.00 26.38           N  
ANISOU 1510  N   GLU A 348     4366   3192   2464   -121    160    406       N  
ATOM   1511  CA  GLU A 348      11.760   2.991  35.111  1.00 28.26           C  
ANISOU 1511  CA  GLU A 348     4623   3561   2555   -124    155    395       C  
ATOM   1512  C   GLU A 348      13.058   3.718  35.471  1.00 28.36           C  
ANISOU 1512  C   GLU A 348     4672   3476   2629    -37     87    316       C  
ATOM   1513  O   GLU A 348      14.157   3.195  35.234  1.00 28.49           O  
ANISOU 1513  O   GLU A 348     4732   3347   2747    -38      5    341       O  
ATOM   1514  CB  GLU A 348      11.557   1.760  36.020  1.00 29.21           C  
ANISOU 1514  CB  GLU A 348     4797   3743   2559   -260    102    541       C  
ATOM   1515  CG  GLU A 348      11.324   2.110  37.525  1.00 32.20           C  
ANISOU 1515  CG  GLU A 348     5176   4327   2730   -286    112    540       C  
ATOM   1516  CD  GLU A 348      11.366   0.883  38.450  1.00 37.80           C  
ANISOU 1516  CD  GLU A 348     5960   5079   3324   -448     24    720       C  
ATOM   1517  OE1 GLU A 348      11.718  -0.214  37.972  1.00 39.52           O  
ANISOU 1517  OE1 GLU A 348     6245   5117   3654   -519    -76    832       O  
ATOM   1518  OE2 GLU A 348      11.068   1.012  39.663  1.00 37.72           O  
ANISOU 1518  OE2 GLU A 348     5942   5282   3108   -505     36    747       O  
ATOM   1519  N   LEU A 349      12.916   4.914  36.039  1.00 29.29           N  
ANISOU 1519  N   LEU A 349     4762   3677   2689     44    106    205       N  
ATOM   1520  CA  LEU A 349      14.053   5.783  36.310  1.00 29.25           C  
ANISOU 1520  CA  LEU A 349     4784   3573   2756    126     33    121       C  
ATOM   1521  C   LEU A 349      14.395   5.666  37.810  1.00 30.73           C  
ANISOU 1521  C   LEU A 349     5019   3852   2806    121    -19    120       C  
ATOM   1522  O   LEU A 349      13.706   6.213  38.651  1.00 32.31           O  
ANISOU 1522  O   LEU A 349     5187   4226   2864    155     11     48       O  
ATOM   1523  CB  LEU A 349      13.761   7.232  35.861  1.00 29.15           C  
ANISOU 1523  CB  LEU A 349     4723   3546   2806    224     41     -4       C  
ATOM   1524  CG  LEU A 349      13.096   7.391  34.468  1.00 28.84           C  
ANISOU 1524  CG  LEU A 349     4634   3465   2860    217     96      7       C  
ATOM   1525  CD1 LEU A 349      12.805   8.851  34.047  1.00 30.93           C  
ANISOU 1525  CD1 LEU A 349     4867   3686   3197    306     59   -102       C  
ATOM   1526  CD2 LEU A 349      13.896   6.651  33.389  1.00 27.32           C  
ANISOU 1526  CD2 LEU A 349     4450   3144   2786    158     88     93       C  
ATOM   1527  N   THR A 350      15.455   4.938  38.117  1.00 30.62           N  
ANISOU 1527  N   THR A 350     5071   3733   2829     84   -104    187       N  
ATOM   1528  CA  THR A 350      15.751   4.544  39.521  1.00 32.48           C  
ANISOU 1528  CA  THR A 350     5366   4053   2920     48   -167    227       C  
ATOM   1529  C   THR A 350      16.712   5.522  40.200  1.00 32.69           C  
ANISOU 1529  C   THR A 350     5413   4042   2967    147   -239    111       C  
ATOM   1530  O   THR A 350      16.907   5.484  41.416  1.00 34.51           O  
ANISOU 1530  O   THR A 350     5682   4369   3061    142   -287    109       O  
ATOM   1531  CB  THR A 350      16.351   3.126  39.562  1.00 32.57           C  
ANISOU 1531  CB  THR A 350     5455   3952   2969    -45   -262    369       C  
ATOM   1532  OG1 THR A 350      17.554   3.114  38.789  1.00 33.74           O  
ANISOU 1532  OG1 THR A 350     5607   3901   3310     15   -330    323       O  
ATOM   1533  CG2 THR A 350      15.392   2.088  38.943  1.00 33.17           C  
ANISOU 1533  CG2 THR A 350     5521   4046   3034   -152   -224    491       C  
ATOM   1534  N   ASP A 351      17.328   6.399  39.416  1.00 31.81           N  
ANISOU 1534  N   ASP A 351     5273   3794   3020    223   -257     23       N  
ATOM   1535  CA  ASP A 351      18.297   7.349  39.961  1.00 32.04           C  
ANISOU 1535  CA  ASP A 351     5318   3759   3097    303   -345    -79       C  
ATOM   1536  C   ASP A 351      17.721   8.758  39.853  1.00 32.28           C  
ANISOU 1536  C   ASP A 351     5300   3821   3144    395   -335   -215       C  
ATOM   1537  O   ASP A 351      17.625   9.332  38.756  1.00 30.40           O  
ANISOU 1537  O   ASP A 351     5024   3487   3039    406   -322   -231       O  
ATOM   1538  CB  ASP A 351      19.620   7.224  39.201  1.00 32.01           C  
ANISOU 1538  CB  ASP A 351     5315   3572   3275    295   -411    -61       C  
ATOM   1539  CG  ASP A 351      20.758   8.026  39.832  1.00 33.21           C  
ANISOU 1539  CG  ASP A 351     5485   3652   3480    353   -519   -143       C  
ATOM   1540  OD1 ASP A 351      20.518   8.996  40.583  1.00 35.42           O  
ANISOU 1540  OD1 ASP A 351     5773   3983   3703    421   -552   -242       O  
ATOM   1541  OD2 ASP A 351      21.917   7.672  39.538  1.00 34.43           O  
ANISOU 1541  OD2 ASP A 351     5637   3704   3741    336   -582   -124       O  
ATOM   1542  N   ALA A 352      17.365   9.313  41.010  1.00 32.75           N  
ANISOU 1542  N   ALA A 352     5360   4017   3066    464   -361   -320       N  
ATOM   1543  CA  ALA A 352      16.709  10.616  41.092  1.00 33.79           C  
ANISOU 1543  CA  ALA A 352     5443   4193   3202    580   -385   -488       C  
ATOM   1544  C   ALA A 352      17.595  11.796  40.657  1.00 33.69           C  
ANISOU 1544  C   ALA A 352     5445   3966   3389    644   -513   -567       C  
ATOM   1545  O   ALA A 352      17.090  12.888  40.448  1.00 33.31           O  
ANISOU 1545  O   ALA A 352     5369   3888   3402    733   -571   -690       O  
ATOM   1546  CB  ALA A 352      16.168  10.846  42.511  1.00 35.74           C  
ANISOU 1546  CB  ALA A 352     5669   4678   3231    651   -392   -610       C  
ATOM   1547  N   ARG A 353      18.907  11.577  40.528  1.00 33.82           N  
ANISOU 1547  N   ARG A 353     5502   3837   3511    593   -576   -497       N  
ATOM   1548  CA  ARG A 353      19.814  12.635  40.054  1.00 33.83           C  
ANISOU 1548  CA  ARG A 353     5506   3647   3699    609   -700   -536       C  
ATOM   1549  C   ARG A 353      19.598  12.875  38.561  1.00 32.72           C  
ANISOU 1549  C   ARG A 353     5328   3409   3695    545   -667   -460       C  
ATOM   1550  O   ARG A 353      19.578  14.012  38.121  1.00 33.43           O  
ANISOU 1550  O   ARG A 353     5413   3388   3903    569   -767   -508       O  
ATOM   1551  CB  ARG A 353      21.282  12.253  40.279  1.00 34.03           C  
ANISOU 1551  CB  ARG A 353     5559   3583   3788    559   -764   -480       C  
ATOM   1552  CG  ARG A 353      21.713  12.144  41.744  1.00 34.50           C  
ANISOU 1552  CG  ARG A 353     5666   3709   3732    618   -832   -552       C  
ATOM   1553  CD  ARG A 353      23.117  11.540  41.875  1.00 35.36           C  
ANISOU 1553  CD  ARG A 353     5796   3734   3905    565   -889   -486       C  
ATOM   1554  NE  ARG A 353      23.256  10.225  41.259  1.00 34.94           N  
ANISOU 1554  NE  ARG A 353     5734   3690   3852    482   -807   -358       N  
ATOM   1555  CZ  ARG A 353      24.372   9.486  41.264  1.00 35.71           C  
ANISOU 1555  CZ  ARG A 353     5836   3728   4005    448   -857   -312       C  
ATOM   1556  NH1 ARG A 353      25.464   9.905  41.887  1.00 34.52           N  
ANISOU 1556  NH1 ARG A 353     5698   3515   3905    478   -974   -370       N  
ATOM   1557  NH2 ARG A 353      24.384   8.313  40.651  1.00 32.86           N  
ANISOU 1557  NH2 ARG A 353     5462   3367   3655    395   -805   -225       N  
ATOM   1558  N   TYR A 354      19.428  11.794  37.803  1.00 30.95           N  
ANISOU 1558  N   TYR A 354     5082   3226   3453    461   -547   -340       N  
ATOM   1559  CA  TYR A 354      19.294  11.863  36.348  1.00 30.30           C  
ANISOU 1559  CA  TYR A 354     4956   3081   3475    391   -505   -260       C  
ATOM   1560  C   TYR A 354      17.849  11.799  35.868  1.00 29.87           C  
ANISOU 1560  C   TYR A 354     4878   3104   3367    410   -416   -265       C  
ATOM   1561  O   TYR A 354      17.599  12.021  34.691  1.00 28.50           O  
ANISOU 1561  O   TYR A 354     4674   2882   3274    363   -396   -211       O  
ATOM   1562  CB  TYR A 354      20.071  10.728  35.689  1.00 29.48           C  
ANISOU 1562  CB  TYR A 354     4826   2978   3399    303   -445   -155       C  
ATOM   1563  CG  TYR A 354      21.556  10.729  35.957  1.00 31.25           C  
ANISOU 1563  CG  TYR A 354     5045   3138   3689    279   -530   -155       C  
ATOM   1564  CD1 TYR A 354      22.392  11.670  35.360  1.00 32.66           C  
ANISOU 1564  CD1 TYR A 354     5184   3235   3989    227   -610   -145       C  
ATOM   1565  CD2 TYR A 354      22.129   9.781  36.809  1.00 31.93           C  
ANISOU 1565  CD2 TYR A 354     5164   3251   3717    295   -544   -156       C  
ATOM   1566  CE1 TYR A 354      23.776  11.665  35.596  1.00 33.40           C  
ANISOU 1566  CE1 TYR A 354     5253   3297   4142    197   -686   -150       C  
ATOM   1567  CE2 TYR A 354      23.519   9.764  37.046  1.00 31.92           C  
ANISOU 1567  CE2 TYR A 354     5147   3196   3783    284   -631   -172       C  
ATOM   1568  CZ  TYR A 354      24.326  10.708  36.435  1.00 34.64           C  
ANISOU 1568  CZ  TYR A 354     5434   3482   4245    237   -691   -175       C  
ATOM   1569  OH  TYR A 354      25.684  10.693  36.660  1.00 34.31           O  
ANISOU 1569  OH  TYR A 354     5357   3413   4266    218   -773   -195       O  
ATOM   1570  N   GLY A 355      16.911  11.537  36.790  1.00 30.40           N  
ANISOU 1570  N   GLY A 355     4951   3313   3289    473   -369   -331       N  
ATOM   1571  CA  GLY A 355      15.505  11.252  36.439  1.00 30.12           C  
ANISOU 1571  CA  GLY A 355     4874   3395   3176    481   -267   -334       C  
ATOM   1572  C   GLY A 355      14.874  12.308  35.544  1.00 30.01           C  
ANISOU 1572  C   GLY A 355     4831   3303   3267    524   -312   -386       C  
ATOM   1573  O   GLY A 355      14.266  12.002  34.506  1.00 29.15           O  
ANISOU 1573  O   GLY A 355     4693   3196   3188    477   -241   -318       O  
ATOM   1574  N   GLU A 356      15.063  13.557  35.923  1.00 30.36           N  
ANISOU 1574  N   GLU A 356     4892   3262   3382    613   -455   -505       N  
ATOM   1575  CA  GLU A 356      14.493  14.681  35.193  1.00 30.86           C  
ANISOU 1575  CA  GLU A 356     4945   3217   3562    663   -557   -564       C  
ATOM   1576  C   GLU A 356      14.922  14.769  33.717  1.00 28.35           C  
ANISOU 1576  C   GLU A 356     4633   2757   3381    539   -568   -408       C  
ATOM   1577  O   GLU A 356      14.069  14.842  32.812  1.00 26.85           O  
ANISOU 1577  O   GLU A 356     4418   2568   3216    528   -538   -380       O  
ATOM   1578  CB  GLU A 356      14.869  15.976  35.909  1.00 32.73           C  
ANISOU 1578  CB  GLU A 356     5216   3341   3879    772   -760   -712       C  
ATOM   1579  CG  GLU A 356      14.075  17.167  35.425  1.00 38.94           C  
ANISOU 1579  CG  GLU A 356     5999   4017   4780    864   -912   -818       C  
ATOM   1580  CD  GLU A 356      12.701  17.220  36.062  1.00 43.74           C  
ANISOU 1580  CD  GLU A 356     6539   4817   5263   1022   -872  -1014       C  
ATOM   1581  OE1 GLU A 356      12.551  17.943  37.074  1.00 47.20           O  
ANISOU 1581  OE1 GLU A 356     6967   5293   5676   1177   -995  -1225       O  
ATOM   1582  OE2 GLU A 356      11.800  16.504  35.569  1.00 44.33           O  
ANISOU 1582  OE2 GLU A 356     6560   5026   5255    989   -718   -965       O  
ATOM   1583  N   GLU A 357      16.235  14.787  33.500  1.00 26.88           N  
ANISOU 1583  N   GLU A 357     4468   2476   3270    445   -616   -315       N  
ATOM   1584  CA  GLU A 357      16.819  14.912  32.154  1.00 26.41           C  
ANISOU 1584  CA  GLU A 357     4392   2332   3313    306   -629   -167       C  
ATOM   1585  C   GLU A 357      16.635  13.673  31.270  1.00 25.84           C  
ANISOU 1585  C   GLU A 357     4269   2370   3177    227   -455    -63       C  
ATOM   1586  O   GLU A 357      16.461  13.781  30.047  1.00 25.08           O  
ANISOU 1586  O   GLU A 357     4145   2259   3125    146   -440     26       O  
ATOM   1587  CB  GLU A 357      18.298  15.274  32.270  1.00 27.34           C  
ANISOU 1587  CB  GLU A 357     4517   2363   3508    225   -727   -115       C  
ATOM   1588  CG  GLU A 357      18.523  16.705  32.850  1.00 27.91           C  
ANISOU 1588  CG  GLU A 357     4643   2273   3689    279   -952   -197       C  
ATOM   1589  CD  GLU A 357      17.886  17.784  31.997  1.00 30.83           C  
ANISOU 1589  CD  GLU A 357     5035   2510   4170    259  -1093   -169       C  
ATOM   1590  OE1 GLU A 357      18.048  17.736  30.749  1.00 28.71           O  
ANISOU 1590  OE1 GLU A 357     4737   2235   3935    113  -1067    -12       O  
ATOM   1591  OE2 GLU A 357      17.228  18.695  32.567  1.00 31.99           O  
ANISOU 1591  OE2 GLU A 357     5223   2562   4368    392  -1248   -313       O  
ATOM   1592  N   VAL A 358      16.651  12.500  31.889  1.00 24.60           N  
ANISOU 1592  N   VAL A 358     4107   2322   2919    247   -342    -74       N  
ATOM   1593  CA  VAL A 358      16.352  11.279  31.141  1.00 25.06           C  
ANISOU 1593  CA  VAL A 358     4126   2466   2929    193   -207      0       C  
ATOM   1594  C   VAL A 358      14.906  11.305  30.629  1.00 24.98           C  
ANISOU 1594  C   VAL A 358     4099   2502   2888    222   -148    -11       C  
ATOM   1595  O   VAL A 358      14.659  11.060  29.456  1.00 24.57           O  
ANISOU 1595  O   VAL A 358     4013   2459   2864    163   -101     57       O  
ATOM   1596  CB  VAL A 358      16.652  10.028  31.984  1.00 24.75           C  
ANISOU 1596  CB  VAL A 358     4101   2497   2803    202   -146      0       C  
ATOM   1597  CG1 VAL A 358      16.208   8.755  31.246  1.00 24.73           C  
ANISOU 1597  CG1 VAL A 358     4068   2558   2769    157    -43     64       C  
ATOM   1598  CG2 VAL A 358      18.164   9.972  32.279  1.00 24.87           C  
ANISOU 1598  CG2 VAL A 358     4119   2462   2868    174   -214      8       C  
ATOM   1599  N   GLN A 359      13.964  11.629  31.510  1.00 26.17           N  
ANISOU 1599  N   GLN A 359     4264   2706   2976    317   -155   -111       N  
ATOM   1600  CA  GLN A 359      12.569  11.734  31.101  1.00 27.09           C  
ANISOU 1600  CA  GLN A 359     4347   2883   3063    358   -110   -147       C  
ATOM   1601  C   GLN A 359      12.384  12.759  29.979  1.00 26.91           C  
ANISOU 1601  C   GLN A 359     4323   2741   3159    346   -202   -127       C  
ATOM   1602  O   GLN A 359      11.656  12.491  29.020  1.00 25.69           O  
ANISOU 1602  O   GLN A 359     4139   2613   3010    316   -145    -80       O  
ATOM   1603  CB  GLN A 359      11.677  12.065  32.286  1.00 27.30           C  
ANISOU 1603  CB  GLN A 359     4358   3022   2991    473   -119   -292       C  
ATOM   1604  CG  GLN A 359      10.261  12.518  31.856  1.00 32.73           C  
ANISOU 1604  CG  GLN A 359     4993   3766   3674    543   -112   -372       C  
ATOM   1605  CD  GLN A 359       9.291  12.566  33.013  1.00 35.79           C  
ANISOU 1605  CD  GLN A 359     5324   4353   3921    648    -81   -526       C  
ATOM   1606  OE1 GLN A 359       9.163  11.600  33.745  1.00 39.08           O  
ANISOU 1606  OE1 GLN A 359     5721   4934   4194    601     26   -492       O  
ATOM   1607  NE2 GLN A 359       8.612  13.686  33.185  1.00 38.76           N  
ANISOU 1607  NE2 GLN A 359     5668   4726   4333    787   -190   -699       N  
ATOM   1608  N   ARG A 360      13.042  13.920  30.095  1.00 27.38           N  
ANISOU 1608  N   ARG A 360     4421   2664   3318    359   -361   -151       N  
ATOM   1609  CA  ARG A 360      12.989  14.928  29.026  1.00 27.85           C  
ANISOU 1609  CA  ARG A 360     4496   2587   3498    313   -488    -93       C  
ATOM   1610  C   ARG A 360      13.506  14.397  27.703  1.00 27.00           C  
ANISOU 1610  C   ARG A 360     4359   2498   3403    160   -415     73       C  
ATOM   1611  O   ARG A 360      12.920  14.640  26.655  1.00 26.73           O  
ANISOU 1611  O   ARG A 360     4313   2445   3398    119   -430    132       O  
ATOM   1612  CB  ARG A 360      13.774  16.176  29.412  1.00 28.94           C  
ANISOU 1612  CB  ARG A 360     4688   2559   3750    318   -697   -119       C  
ATOM   1613  CG  ARG A 360      13.117  16.999  30.472  1.00 30.46           C  
ANISOU 1613  CG  ARG A 360     4903   2711   3958    493   -825   -315       C  
ATOM   1614  CD  ARG A 360      14.011  18.155  30.848  1.00 33.48           C  
ANISOU 1614  CD  ARG A 360     5345   2906   4469    491  -1053   -336       C  
ATOM   1615  NE  ARG A 360      13.397  19.037  31.839  1.00 33.69           N  
ANISOU 1615  NE  ARG A 360     5390   2884   4526    684  -1213   -561       N  
ATOM   1616  CZ  ARG A 360      12.601  20.060  31.555  1.00 36.66           C  
ANISOU 1616  CZ  ARG A 360     5787   3130   5012    780  -1407   -659       C  
ATOM   1617  NH1 ARG A 360      12.291  20.363  30.289  1.00 36.35           N  
ANISOU 1617  NH1 ARG A 360     5766   2984   5061    684  -1469   -524       N  
ATOM   1618  NH2 ARG A 360      12.107  20.783  32.547  1.00 37.11           N  
ANISOU 1618  NH2 ARG A 360     5841   3171   5087    982  -1555   -905       N  
ATOM   1619  N   LEU A 361      14.606  13.658  27.749  1.00 26.78           N  
ANISOU 1619  N   LEU A 361     4308   2524   3344     84   -344    134       N  
ATOM   1620  CA  LEU A 361      15.156  13.079  26.517  1.00 27.17           C  
ANISOU 1620  CA  LEU A 361     4301   2640   3384    -44   -270    255       C  
ATOM   1621  C   LEU A 361      14.179  12.072  25.893  1.00 26.29           C  
ANISOU 1621  C   LEU A 361     4152   2630   3206    -27   -132    257       C  
ATOM   1622  O   LEU A 361      13.890  12.109  24.681  1.00 24.48           O  
ANISOU 1622  O   LEU A 361     3890   2430   2982    -95   -115    330       O  
ATOM   1623  CB  LEU A 361      16.503  12.408  26.813  1.00 26.75           C  
ANISOU 1623  CB  LEU A 361     4212   2642   3310    -94   -230    271       C  
ATOM   1624  CG  LEU A 361      17.275  11.979  25.552  1.00 27.68           C  
ANISOU 1624  CG  LEU A 361     4241   2864   3414   -220   -178    364       C  
ATOM   1625  CD1 LEU A 361      17.665  13.181  24.679  1.00 29.31           C  
ANISOU 1625  CD1 LEU A 361     4433   3031   3673   -356   -291    478       C  
ATOM   1626  CD2 LEU A 361      18.513  11.227  25.985  1.00 26.34           C  
ANISOU 1626  CD2 LEU A 361     4022   2759   3225   -228   -147    333       C  
ATOM   1627  N   LEU A 362      13.648  11.196  26.748  1.00 26.40           N  
ANISOU 1627  N   LEU A 362     4174   2704   3153     55    -46    185       N  
ATOM   1628  CA  LEU A 362      12.671  10.198  26.330  1.00 27.15           C  
ANISOU 1628  CA  LEU A 362     4238   2885   3191     67     67    187       C  
ATOM   1629  C   LEU A 362      11.414  10.820  25.723  1.00 28.06           C  
ANISOU 1629  C   LEU A 362     4348   2989   3323     97     49    174       C  
ATOM   1630  O   LEU A 362      10.957  10.382  24.665  1.00 27.40           O  
ANISOU 1630  O   LEU A 362     4230   2947   3233     55    104    223       O  
ATOM   1631  CB  LEU A 362      12.287   9.304  27.509  1.00 26.53           C  
ANISOU 1631  CB  LEU A 362     4176   2871   3033    121    129    135       C  
ATOM   1632  CG  LEU A 362      13.348   8.319  27.987  1.00 28.11           C  
ANISOU 1632  CG  LEU A 362     4384   3082   3214     92    145    156       C  
ATOM   1633  CD1 LEU A 362      12.862   7.555  29.218  1.00 28.20           C  
ANISOU 1633  CD1 LEU A 362     4427   3153   3135    121    177    134       C  
ATOM   1634  CD2 LEU A 362      13.733   7.362  26.853  1.00 28.46           C  
ANISOU 1634  CD2 LEU A 362     4381   3154   3280     35    190    205       C  
ATOM   1635  N   GLU A 363      10.857  11.828  26.397  1.00 29.78           N  
ANISOU 1635  N   GLU A 363     4597   3153   3566    182    -41     90       N  
ATOM   1636  CA  GLU A 363       9.665  12.516  25.901  1.00 31.60           C  
ANISOU 1636  CA  GLU A 363     4820   3359   3829    236    -92     49       C  
ATOM   1637  C   GLU A 363       9.926  13.203  24.562  1.00 32.49           C  
ANISOU 1637  C   GLU A 363     4944   3378   4022    147   -182    157       C  
ATOM   1638  O   GLU A 363       9.106  13.135  23.638  1.00 32.20           O  
ANISOU 1638  O   GLU A 363     4886   3362   3988    135   -164    186       O  
ATOM   1639  CB  GLU A 363       9.128  13.496  26.951  1.00 33.21           C  
ANISOU 1639  CB  GLU A 363     5040   3527   4050    371   -203   -102       C  
ATOM   1640  CG  GLU A 363       8.467  12.758  28.105  1.00 33.29           C  
ANISOU 1640  CG  GLU A 363     5008   3704   3936    447    -90   -206       C  
ATOM   1641  CD  GLU A 363       7.932  13.637  29.216  1.00 38.94           C  
ANISOU 1641  CD  GLU A 363     5711   4452   4633    596   -183   -393       C  
ATOM   1642  OE1 GLU A 363       8.127  14.871  29.211  1.00 39.33           O  
ANISOU 1642  OE1 GLU A 363     5798   4353   4792    664   -365   -462       O  
ATOM   1643  OE2 GLU A 363       7.318  13.056  30.132  1.00 42.57           O  
ANISOU 1643  OE2 GLU A 363     6115   5099   4960    641    -84   -473       O  
ATOM   1644  N   GLY A 364      11.089  13.840  24.459  1.00 33.72           N  
ANISOU 1644  N   GLY A 364     5131   3448   4235     67   -282    229       N  
ATOM   1645  CA  GLY A 364      11.532  14.455  23.216  1.00 34.98           C  
ANISOU 1645  CA  GLY A 364     5294   3553   4444    -66   -370    369       C  
ATOM   1646  C   GLY A 364      11.757  13.518  22.042  1.00 34.25           C  
ANISOU 1646  C   GLY A 364     5135   3600   4280   -174   -236    469       C  
ATOM   1647  O   GLY A 364      11.730  13.972  20.895  1.00 36.05           O  
ANISOU 1647  O   GLY A 364     5354   3826   4518   -277   -293    579       O  
ATOM   1648  N   SER A 365      12.004  12.233  22.311  1.00 33.63           N  
ANISOU 1648  N   SER A 365     5008   3639   4129   -152    -82    428       N  
ATOM   1649  CA  SER A 365      12.221  11.214  21.258  1.00 33.49           C  
ANISOU 1649  CA  SER A 365     4917   3761   4048   -220     32    476       C  
ATOM   1650  C   SER A 365      10.958  10.744  20.518  1.00 32.31           C  
ANISOU 1650  C   SER A 365     4749   3655   3871   -187     93    465       C  
ATOM   1651  O   SER A 365      11.056  10.076  19.494  1.00 32.19           O  
ANISOU 1651  O   SER A 365     4673   3748   3809   -241    160    500       O  
ATOM   1652  CB  SER A 365      12.881   9.961  21.836  1.00 32.23           C  
ANISOU 1652  CB  SER A 365     4722   3678   3846   -188    131    418       C  
ATOM   1653  OG  SER A 365      11.955   9.222  22.637  1.00 32.89           O  
ANISOU 1653  OG  SER A 365     4833   3753   3910    -91    192    342       O  
ATOM   1654  N   GLN A 366       9.790  11.043  21.069  1.00 31.69           N  
ANISOU 1654  N   GLN A 366     4709   3514   3817    -90     71    398       N  
ATOM   1655  CA  GLN A 366       8.524  10.612  20.499  1.00 31.61           C  
ANISOU 1655  CA  GLN A 366     4675   3548   3788    -52    125    374       C  
ATOM   1656  C   GLN A 366       8.432  11.017  19.016  1.00 32.02           C  
ANISOU 1656  C   GLN A 366     4709   3615   3841   -139     81    472       C  
ATOM   1657  O   GLN A 366       8.685  12.164  18.666  1.00 31.65           O  
ANISOU 1657  O   GLN A 366     4701   3485   3841   -195    -51    543       O  
ATOM   1658  CB  GLN A 366       7.386  11.220  21.309  1.00 33.10           C  
ANISOU 1658  CB  GLN A 366     4889   3682   4005     64     74    275       C  
ATOM   1659  CG  GLN A 366       5.992  10.794  20.923  1.00 36.52           C  
ANISOU 1659  CG  GLN A 366     5283   4176   4417    114    129    230       C  
ATOM   1660  CD  GLN A 366       5.241  11.880  20.143  1.00 42.81           C  
ANISOU 1660  CD  GLN A 366     6097   4891   5278    137      1    235       C  
ATOM   1661  OE1 GLN A 366       4.085  12.188  20.452  1.00 48.44           O  
ANISOU 1661  OE1 GLN A 366     6790   5608   6008    241    -29    131       O  
ATOM   1662  NE2 GLN A 366       5.886  12.455  19.137  1.00 42.22           N  
ANISOU 1662  NE2 GLN A 366     6052   4756   5233     36    -86    355       N  
ATOM   1663  N   ARG A 367       8.067  10.057  18.173  1.00 31.23           N  
ANISOU 1663  N   ARG A 367     4555   3620   3690   -157    177    478       N  
ATOM   1664  CA  ARG A 367       7.975  10.253  16.720  1.00 33.01           C  
ANISOU 1664  CA  ARG A 367     4751   3906   3886   -243    154    565       C  
ATOM   1665  C   ARG A 367       6.853   9.362  16.143  1.00 31.68           C  
ANISOU 1665  C   ARG A 367     4544   3801   3691   -193    233    516       C  
ATOM   1666  O   ARG A 367       6.514   8.360  16.742  1.00 30.66           O  
ANISOU 1666  O   ARG A 367     4397   3696   3555   -129    318    438       O  
ATOM   1667  CB  ARG A 367       9.346  10.002  16.045  1.00 33.32           C  
ANISOU 1667  CB  ARG A 367     4729   4071   3860   -360    182    633       C  
ATOM   1668  CG  ARG A 367       9.975   8.647  16.384  1.00 37.59           C  
ANISOU 1668  CG  ARG A 367     5210   4707   4365   -318    294    546       C  
ATOM   1669  CD  ARG A 367      11.494   8.760  16.689  1.00 44.30           C  
ANISOU 1669  CD  ARG A 367     6024   5608   5197   -380    283    562       C  
ATOM   1670  NE  ARG A 367      11.971   7.828  17.749  1.00 45.16           N  
ANISOU 1670  NE  ARG A 367     6135   5695   5327   -298    329    464       N  
ATOM   1671  CZ  ARG A 367      13.233   7.391  17.840  1.00 45.91           C  
ANISOU 1671  CZ  ARG A 367     6167   5876   5401   -319    342    431       C  
ATOM   1672  NH1 ARG A 367      13.597   6.564  18.813  1.00 44.55           N  
ANISOU 1672  NH1 ARG A 367     6012   5658   5258   -241    356    349       N  
ATOM   1673  NH2 ARG A 367      14.143   7.769  16.938  1.00 45.23           N  
ANISOU 1673  NH2 ARG A 367     5991   5940   5254   -425    334    482       N  
ATOM   1674  N   GLY A 368       6.263   9.759  15.012  1.00 32.62           N  
ANISOU 1674  N   GLY A 368     4657   3940   3798   -232    187    573       N  
ATOM   1675  CA  GLY A 368       5.139   9.025  14.359  1.00 33.14           C  
ANISOU 1675  CA  GLY A 368     4686   4060   3845   -188    243    529       C  
ATOM   1676  C   GLY A 368       4.362   7.874  15.012  1.00 32.90           C  
ANISOU 1676  C   GLY A 368     4629   4047   3823   -101    340    425       C  
ATOM   1677  O   GLY A 368       4.744   6.720  14.918  1.00 35.43           O  
ANISOU 1677  O   GLY A 368     4910   4439   4115   -108    414    395       O  
ATOM   1678  N   LEU A 369       3.236   8.141  15.637  1.00 33.04           N  
ANISOU 1678  N   LEU A 369     4660   4013   3881    -25    325    368       N  
ATOM   1679  CA  LEU A 369       2.365   7.024  16.149  1.00 30.30           C  
ANISOU 1679  CA  LEU A 369     4273   3715   3526     19    413    297       C  
ATOM   1680  C   LEU A 369       2.801   6.418  17.494  1.00 29.49           C  
ANISOU 1680  C   LEU A 369     4180   3615   3410     29    465    266       C  
ATOM   1681  O   LEU A 369       1.991   5.844  18.228  1.00 27.36           O  
ANISOU 1681  O   LEU A 369     3884   3385   3125     50    511    226       O  
ATOM   1682  CB  LEU A 369       2.174   5.902  15.112  1.00 31.16           C  
ANISOU 1682  CB  LEU A 369     4335   3893   3610    -14    462    303       C  
ATOM   1683  CG  LEU A 369       0.825   5.743  14.380  1.00 30.03           C  
ANISOU 1683  CG  LEU A 369     4154   3778   3477     10    459    279       C  
ATOM   1684  CD1 LEU A 369       0.211   7.041  13.973  1.00 27.06           C  
ANISOU 1684  CD1 LEU A 369     3798   3357   3127     40    371    290       C  
ATOM   1685  CD2 LEU A 369       0.864   4.728  13.208  1.00 31.77           C  
ANISOU 1685  CD2 LEU A 369     4333   4065   3673    -20    483    279       C  
ATOM   1686  N   ASP A 370       4.082   6.540  17.832  1.00 28.16           N  
ANISOU 1686  N   ASP A 370     4043   3420   3237      1    452    294       N  
ATOM   1687  CA  ASP A 370       4.470   6.151  19.200  1.00 27.66           C  
ANISOU 1687  CA  ASP A 370     4000   3348   3160     15    479    268       C  
ATOM   1688  C   ASP A 370       3.699   7.029  20.168  1.00 27.17           C  
ANISOU 1688  C   ASP A 370     3946   3280   3097     80    455    211       C  
ATOM   1689  O   ASP A 370       3.529   8.216  19.905  1.00 27.55           O  
ANISOU 1689  O   ASP A 370     4010   3273   3182    117    375    196       O  
ATOM   1690  CB  ASP A 370       5.974   6.265  19.375  1.00 27.70           C  
ANISOU 1690  CB  ASP A 370     4032   3323   3168    -16    456    296       C  
ATOM   1691  CG  ASP A 370       6.729   5.371  18.393  1.00 30.25           C  
ANISOU 1691  CG  ASP A 370     4317   3696   3482    -58    476    311       C  
ATOM   1692  OD1 ASP A 370       6.129   4.404  17.829  1.00 35.24           O  
ANISOU 1692  OD1 ASP A 370     4915   4363   4110    -55    504    291       O  
ATOM   1693  OD2 ASP A 370       7.923   5.613  18.183  1.00 33.90           O  
ANISOU 1693  OD2 ASP A 370     4769   4174   3937    -90    454    328       O  
ATOM   1694  N   VAL A 371       3.167   6.434  21.240  1.00 26.31           N  
ANISOU 1694  N   VAL A 371     3817   3238   2941     92    507    175       N  
ATOM   1695  CA  VAL A 371       2.449   7.208  22.266  1.00 27.40           C  
ANISOU 1695  CA  VAL A 371     3934   3428   3050    165    493     87       C  
ATOM   1696  C   VAL A 371       3.023   6.924  23.655  1.00 26.25           C  
ANISOU 1696  C   VAL A 371     3809   3324   2842    156    516     78       C  
ATOM   1697  O   VAL A 371       3.455   5.791  23.942  1.00 26.97           O  
ANISOU 1697  O   VAL A 371     3915   3430   2901     81    559    146       O  
ATOM   1698  CB  VAL A 371       0.899   6.949  22.275  1.00 27.75           C  
ANISOU 1698  CB  VAL A 371     3892   3596   3056    188    539     31       C  
ATOM   1699  CG1 VAL A 371       0.218   7.649  21.099  1.00 28.56           C  
ANISOU 1699  CG1 VAL A 371     3977   3650   3224    235    481      4       C  
ATOM   1700  CG2 VAL A 371       0.574   5.462  22.248  1.00 28.57           C  
ANISOU 1700  CG2 VAL A 371     3968   3770   3118     89    619    103       C  
ATOM   1701  N   GLN A 372       3.016   7.929  24.527  1.00 25.89           N  
ANISOU 1701  N   GLN A 372     3765   3291   2782    237    468    -12       N  
ATOM   1702  CA  GLN A 372       3.667   7.775  25.834  1.00 25.56           C  
ANISOU 1702  CA  GLN A 372     3748   3291   2674    233    478    -24       C  
ATOM   1703  C   GLN A 372       2.742   8.114  26.966  1.00 27.39           C  
ANISOU 1703  C   GLN A 372     3909   3695   2804    300    499   -142       C  
ATOM   1704  O   GLN A 372       1.775   8.861  26.784  1.00 27.43           O  
ANISOU 1704  O   GLN A 372     3850   3753   2820    391    470   -256       O  
ATOM   1705  CB  GLN A 372       4.931   8.645  25.925  1.00 25.19           C  
ANISOU 1705  CB  GLN A 372     3774   3102   2695    263    385    -26       C  
ATOM   1706  CG  GLN A 372       5.863   8.515  24.706  1.00 25.64           C  
ANISOU 1706  CG  GLN A 372     3871   3036   2835    194    361     76       C  
ATOM   1707  CD  GLN A 372       7.122   9.374  24.815  1.00 28.75           C  
ANISOU 1707  CD  GLN A 372     4319   3316   3287    194    268     90       C  
ATOM   1708  OE1 GLN A 372       7.134  10.391  25.514  1.00 29.10           O  
ANISOU 1708  OE1 GLN A 372     4386   3321   3352    265    184     13       O  
ATOM   1709  NE2 GLN A 372       8.185   8.982  24.088  1.00 28.66           N  
ANISOU 1709  NE2 GLN A 372     4320   3264   3305    114    273    176       N  
ATOM   1710  N   LEU A 373       3.053   7.576  28.146  1.00 28.06           N  
ANISOU 1710  N   LEU A 373     3996   3882   2782    258    539   -125       N  
ATOM   1711  CA  LEU A 373       2.333   7.923  29.373  1.00 30.69           C  
ANISOU 1711  CA  LEU A 373     4247   4433   2981    316    563   -248       C  
ATOM   1712  C   LEU A 373       3.352   8.042  30.494  1.00 32.23           C  
ANISOU 1712  C   LEU A 373     4501   4624   3121    321    532   -253       C  
ATOM   1713  O   LEU A 373       4.167   7.138  30.687  1.00 31.32           O  
ANISOU 1713  O   LEU A 373     4455   4452   2994    215    549   -118       O  
ATOM   1714  CB  LEU A 373       1.303   6.852  29.715  1.00 31.34           C  
ANISOU 1714  CB  LEU A 373     4240   4741   2928    207    670   -191       C  
ATOM   1715  CG  LEU A 373       0.137   7.182  30.634  1.00 35.41           C  
ANISOU 1715  CG  LEU A 373     4608   5563   3282    256    720   -332       C  
ATOM   1716  CD1 LEU A 373      -0.831   8.117  29.912  1.00 35.61           C  
ANISOU 1716  CD1 LEU A 373     4548   5600   3381    397    684   -495       C  
ATOM   1717  CD2 LEU A 373      -0.552   5.875  31.027  1.00 37.57           C  
ANISOU 1717  CD2 LEU A 373     4815   6049   3411     73    821   -196       C  
ATOM   1718  N   ARG A 374       3.319   9.178  31.194  1.00 33.77           N  
ANISOU 1718  N   ARG A 374     4670   4864   3296    457    464   -422       N  
ATOM   1719  CA  ARG A 374       4.208   9.466  32.322  1.00 35.78           C  
ANISOU 1719  CA  ARG A 374     4971   5129   3496    488    420   -462       C  
ATOM   1720  C   ARG A 374       3.526   9.046  33.603  1.00 37.30           C  
ANISOU 1720  C   ARG A 374     5067   5638   3466    465    500   -516       C  
ATOM   1721  O   ARG A 374       2.406   9.491  33.865  1.00 39.02           O  
ANISOU 1721  O   ARG A 374     5158   6069   3598    549    523   -671       O  
ATOM   1722  CB  ARG A 374       4.481  10.970  32.403  1.00 36.89           C  
ANISOU 1722  CB  ARG A 374     5127   5151   3737    656    275   -636       C  
ATOM   1723  CG  ARG A 374       4.914  11.588  31.085  1.00 40.21           C  
ANISOU 1723  CG  ARG A 374     5621   5298   4361    666    177   -584       C  
ATOM   1724  CD  ARG A 374       4.789  13.123  31.090  1.00 47.91           C  
ANISOU 1724  CD  ARG A 374     6600   6159   5446    830     -3   -762       C  
ATOM   1725  NE  ARG A 374       3.418  13.613  31.245  1.00 53.94           N  
ANISOU 1725  NE  ARG A 374     7249   7079   6166    965    -22   -956       N  
ATOM   1726  CZ  ARG A 374       3.037  14.866  30.996  1.00 58.41           C  
ANISOU 1726  CZ  ARG A 374     7809   7529   6854   1120   -204  -1121       C  
ATOM   1727  NH1 ARG A 374       3.916  15.761  30.549  1.00 59.85           N  
ANISOU 1727  NH1 ARG A 374     8105   7425   7208   1131   -386  -1084       N  
ATOM   1728  NH2 ARG A 374       1.772  15.227  31.182  1.00 61.09           N  
ANISOU 1728  NH2 ARG A 374     8024   8039   7147   1259   -222  -1325       N  
ATOM   1729  N   LEU A 375       4.200   8.230  34.413  1.00 36.87           N  
ANISOU 1729  N   LEU A 375     5066   5633   3311    354    529   -396       N  
ATOM   1730  CA  LEU A 375       3.586   7.663  35.624  1.00 39.36           C  
ANISOU 1730  CA  LEU A 375     5294   6277   3384    278    608   -393       C  
ATOM   1731  C   LEU A 375       4.549   7.532  36.807  1.00 39.47           C  
ANISOU 1731  C   LEU A 375     5375   6324   3296    251    571   -364       C  
ATOM   1732  O   LEU A 375       5.771   7.580  36.634  1.00 37.29           O  
ANISOU 1732  O   LEU A 375     5223   5794   3150    259    494   -305       O  
ATOM   1733  CB  LEU A 375       2.975   6.279  35.303  1.00 39.33           C  
ANISOU 1733  CB  LEU A 375     5270   6358   3317     77    695   -190       C  
ATOM   1734  CG  LEU A 375       1.931   6.147  34.179  1.00 40.29           C  
ANISOU 1734  CG  LEU A 375     5317   6478   3513     69    743   -191       C  
ATOM   1735  CD1 LEU A 375       1.711   4.680  33.844  1.00 41.71           C  
ANISOU 1735  CD1 LEU A 375     5524   6649   3676   -141    784     38       C  
ATOM   1736  CD2 LEU A 375       0.594   6.839  34.502  1.00 41.79           C  
ANISOU 1736  CD2 LEU A 375     5326   6973   3579    165    796   -388       C  
ATOM   1737  N   ARG A 376       3.993   7.379  38.013  1.00 41.83           N  
ANISOU 1737  N   ARG A 376     5579   6965   3351    215    624   -410       N  
ATOM   1738  CA  ARG A 376       4.768   6.916  39.162  1.00 42.90           C  
ANISOU 1738  CA  ARG A 376     5778   7176   3347    131    602   -322       C  
ATOM   1739  C   ARG A 376       4.321   5.509  39.542  1.00 43.57           C  
ANISOU 1739  C   ARG A 376     5851   7442   3263   -117    669    -86       C  
ATOM   1740  O   ARG A 376       3.121   5.234  39.615  1.00 44.82           O  
ANISOU 1740  O   ARG A 376     5871   7883   3274   -193    760    -84       O  
ATOM   1741  CB  ARG A 376       4.649   7.862  40.370  1.00 46.13           C  
ANISOU 1741  CB  ARG A 376     6098   7846   3582    271    583   -551       C  
ATOM   1742  CG  ARG A 376       5.396   9.174  40.189  1.00 47.23           C  
ANISOU 1742  CG  ARG A 376     6293   7745   3906    492    459   -752       C  
ATOM   1743  CD  ARG A 376       5.881   9.829  41.496  1.00 50.90           C  
ANISOU 1743  CD  ARG A 376     6746   8360   4236    600    393   -916       C  
ATOM   1744  NE  ARG A 376       6.727  10.962  41.122  1.00 52.95           N  
ANISOU 1744  NE  ARG A 376     7089   8302   4727    775    245  -1054       N  
ATOM   1745  CZ  ARG A 376       8.059  10.961  41.094  1.00 52.41           C  
ANISOU 1745  CZ  ARG A 376     7166   7955   4794    752    158   -959       C  
ATOM   1746  NH1 ARG A 376       8.758   9.899  41.489  1.00 49.41           N  
ANISOU 1746  NH1 ARG A 376     6869   7563   4342    590    191   -749       N  
ATOM   1747  NH2 ARG A 376       8.693  12.056  40.691  1.00 53.46           N  
ANISOU 1747  NH2 ARG A 376     7355   7823   5136    892     18  -1079       N  
ATOM   1748  N   ASN A 377       5.276   4.614  39.771  1.00 42.89           N  
ANISOU 1748  N   ASN A 377     5904   7189   3204   -247    606    115       N  
ATOM   1749  CA  ASN A 377       4.940   3.266  40.222  1.00 44.18           C  
ANISOU 1749  CA  ASN A 377     6081   7488   3218   -499    618    361       C  
ATOM   1750  C   ASN A 377       4.887   3.156  41.751  1.00 47.09           C  
ANISOU 1750  C   ASN A 377     6408   8193   3291   -590    626    389       C  
ATOM   1751  O   ASN A 377       5.198   4.126  42.449  1.00 47.90           O  
ANISOU 1751  O   ASN A 377     6477   8406   3319   -434    620    194       O  
ATOM   1752  CB  ASN A 377       5.859   2.201  39.599  1.00 42.17           C  
ANISOU 1752  CB  ASN A 377     5993   6875   3153   -603    514    571       C  
ATOM   1753  CG  ASN A 377       7.278   2.219  40.146  1.00 41.49           C  
ANISOU 1753  CG  ASN A 377     6043   6600   3123   -560    401    588       C  
ATOM   1754  OD1 ASN A 377       7.563   2.772  41.212  1.00 43.80           O  
ANISOU 1754  OD1 ASN A 377     6322   7054   3266   -511    394    506       O  
ATOM   1755  ND2 ASN A 377       8.182   1.579  39.416  1.00 38.67           N  
ANISOU 1755  ND2 ASN A 377     5807   5910   2975   -574    304    684       N  
ATOM   1756  N   ASP A 378       4.516   1.978  42.258  1.00 49.38           N  
ANISOU 1756  N   ASP A 378     6705   8641   3416   -850    621    637       N  
ATOM   1757  CA  ASP A 378       4.358   1.765  43.710  1.00 52.88           C  
ANISOU 1757  CA  ASP A 378     7097   9459   3534   -988    632    705       C  
ATOM   1758  C   ASP A 378       5.679   1.802  44.502  1.00 53.29           C  
ANISOU 1758  C   ASP A 378     7297   9364   3586   -954    513    733       C  
ATOM   1759  O   ASP A 378       5.686   1.682  45.738  1.00 55.44           O  
ANISOU 1759  O   ASP A 378     7543   9936   3587  -1056    507    784       O  
ATOM   1760  CB  ASP A 378       3.571   0.471  43.990  1.00 55.01           C  
ANISOU 1760  CB  ASP A 378     7339   9934   3628  -1318    637   1003       C  
ATOM   1761  CG  ASP A 378       4.362  -0.795  43.661  1.00 55.48           C  
ANISOU 1761  CG  ASP A 378     7609   9611   3861  -1490    469   1293       C  
ATOM   1762  OD1 ASP A 378       5.122  -0.804  42.672  1.00 54.25           O  
ANISOU 1762  OD1 ASP A 378     7572   9031   4011  -1355    396   1252       O  
ATOM   1763  OD2 ASP A 378       4.221  -1.794  44.401  1.00 59.20           O  
ANISOU 1763  OD2 ASP A 378     8121  10218   4156  -1765    394   1561       O  
ATOM   1764  N   GLU A 379       6.794   1.986  43.802  1.00 51.68           N  
ANISOU 1764  N   GLU A 379     7237   8729   3672   -813    420    693       N  
ATOM   1765  CA  GLU A 379       8.097   2.086  44.469  1.00 52.16           C  
ANISOU 1765  CA  GLU A 379     7428   8629   3760   -759    302    695       C  
ATOM   1766  C   GLU A 379       8.656   3.511  44.555  1.00 51.01           C  
ANISOU 1766  C   GLU A 379     7257   8432   3693   -488    306    404       C  
ATOM   1767  O   GLU A 379       9.778   3.720  45.041  1.00 51.19           O  
ANISOU 1767  O   GLU A 379     7380   8307   3763   -421    207    379       O  
ATOM   1768  CB  GLU A 379       9.093   1.125  43.828  1.00 50.98           C  
ANISOU 1768  CB  GLU A 379     7456   8063   3853   -825    161    876       C  
ATOM   1769  CG  GLU A 379       8.745  -0.333  44.096  1.00 55.12           C  
ANISOU 1769  CG  GLU A 379     8041   8619   4282  -1107     83   1180       C  
ATOM   1770  CD  GLU A 379       9.575  -0.930  45.200  1.00 58.57           C  
ANISOU 1770  CD  GLU A 379     8603   9043   4608  -1224    -66   1337       C  
ATOM   1771  OE1 GLU A 379       9.064  -1.074  46.336  1.00 62.81           O  
ANISOU 1771  OE1 GLU A 379     9089   9937   4838  -1380    -42   1433       O  
ATOM   1772  OE2 GLU A 379      10.755  -1.243  44.930  1.00 58.95           O  
ANISOU 1772  OE2 GLU A 379     8791   8739   4867  -1158   -211   1358       O  
ATOM   1773  N   GLY A 380       7.864   4.486  44.111  1.00 50.38           N  
ANISOU 1773  N   GLY A 380     7043   8468   3631   -335    399    185       N  
ATOM   1774  CA  GLY A 380       8.238   5.902  44.188  1.00 49.65           C  
ANISOU 1774  CA  GLY A 380     6919   8326   3618    -80    372    -99       C  
ATOM   1775  C   GLY A 380       8.869   6.457  42.916  1.00 47.18           C  
ANISOU 1775  C   GLY A 380     6678   7608   3639     56    318   -164       C  
ATOM   1776  O   GLY A 380       9.273   7.629  42.860  1.00 47.20           O  
ANISOU 1776  O   GLY A 380     6678   7507   3751    247    261   -369       O  
ATOM   1777  N   ARG A 381       8.942   5.631  41.881  1.00 44.55           N  
ANISOU 1777  N   ARG A 381     6408   7056   3465    -48    325     10       N  
ATOM   1778  CA  ARG A 381       9.827   5.937  40.767  1.00 42.04           C  
ANISOU 1778  CA  ARG A 381     6172   6368   3432     37    262     -5       C  
ATOM   1779  C   ARG A 381       9.054   6.343  39.519  1.00 40.47           C  
ANISOU 1779  C   ARG A 381     5906   6104   3367     95    321    -68       C  
ATOM   1780  O   ARG A 381       7.955   5.834  39.268  1.00 39.92           O  
ANISOU 1780  O   ARG A 381     5761   6194   3214     12    406    -13       O  
ATOM   1781  CB  ARG A 381      10.811   4.766  40.550  1.00 41.69           C  
ANISOU 1781  CB  ARG A 381     6255   6100   3486    -88    188    200       C  
ATOM   1782  CG  ARG A 381      11.277   4.163  41.919  1.00 45.20           C  
ANISOU 1782  CG  ARG A 381     6761   6666   3748   -185    124    299       C  
ATOM   1783  CD  ARG A 381      12.651   3.499  41.956  1.00 46.87           C  
ANISOU 1783  CD  ARG A 381     7107   6615   4087   -218     -8    406       C  
ATOM   1784  NE  ARG A 381      12.578   2.078  41.617  1.00 49.67           N  
ANISOU 1784  NE  ARG A 381     7525   6873   4476   -382    -59    619       N  
ATOM   1785  CZ  ARG A 381      13.398   1.130  42.064  1.00 49.37           C  
ANISOU 1785  CZ  ARG A 381     7599   6704   4455   -469   -198    758       C  
ATOM   1786  NH1 ARG A 381      14.386   1.412  42.915  1.00 47.69           N  
ANISOU 1786  NH1 ARG A 381     7447   6458   4214   -416   -286    719       N  
ATOM   1787  NH2 ARG A 381      13.218  -0.120  41.653  1.00 49.01           N  
ANISOU 1787  NH2 ARG A 381     7608   6547   4466   -606   -272    933       N  
ATOM   1788  N   ARG A 382       9.611   7.292  38.766  1.00 39.42           N  
ANISOU 1788  N   ARG A 382     5798   5748   3433    227    265   -177       N  
ATOM   1789  CA  ARG A 382       9.041   7.695  37.483  1.00 38.39           C  
ANISOU 1789  CA  ARG A 382     5626   5514   3448    274    293   -215       C  
ATOM   1790  C   ARG A 382       9.108   6.494  36.559  1.00 35.92           C  
ANISOU 1790  C   ARG A 382     5353   5081   3214    139    328    -27       C  
ATOM   1791  O   ARG A 382      10.122   5.785  36.525  1.00 35.00           O  
ANISOU 1791  O   ARG A 382     5322   4815   3160     74    276     85       O  
ATOM   1792  CB  ARG A 382       9.833   8.831  36.801  1.00 38.04           C  
ANISOU 1792  CB  ARG A 382     5623   5224   3607    393    196   -310       C  
ATOM   1793  CG  ARG A 382      10.086  10.117  37.598  1.00 42.53           C  
ANISOU 1793  CG  ARG A 382     6182   5809   4168    543     99   -504       C  
ATOM   1794  CD  ARG A 382      11.039  11.000  36.772  1.00 45.88           C  
ANISOU 1794  CD  ARG A 382     6670   5946   4819    593    -17   -519       C  
ATOM   1795  NE  ARG A 382      11.460  12.231  37.445  1.00 48.94           N  
ANISOU 1795  NE  ARG A 382     7070   6281   5244    725   -154   -687       N  
ATOM   1796  CZ  ARG A 382      11.093  13.450  37.062  1.00 50.12           C  
ANISOU 1796  CZ  ARG A 382     7200   6337   5508    843   -265   -828       C  
ATOM   1797  NH1 ARG A 382      10.296  13.609  36.013  1.00 50.96           N  
ANISOU 1797  NH1 ARG A 382     7271   6402   5688    843   -245   -813       N  
ATOM   1798  NH2 ARG A 382      11.522  14.512  37.726  1.00 53.03           N  
ANISOU 1798  NH2 ARG A 382     7588   6637   5923    964   -419   -985       N  
ATOM   1799  N   VAL A 383       8.033   6.275  35.813  1.00 35.02           N  
ANISOU 1799  N   VAL A 383     5172   5032   3103    110    400    -11       N  
ATOM   1800  CA  VAL A 383       8.035   5.310  34.699  1.00 32.77           C  
ANISOU 1800  CA  VAL A 383     4916   4608   2928     14    416    127       C  
ATOM   1801  C   VAL A 383       7.462   5.986  33.466  1.00 31.58           C  
ANISOU 1801  C   VAL A 383     4714   4388   2896     89    441     54       C  
ATOM   1802  O   VAL A 383       6.413   6.618  33.527  1.00 32.00           O  
ANISOU 1802  O   VAL A 383     4681   4586   2891    151    480    -52       O  
ATOM   1803  CB  VAL A 383       7.179   4.031  34.990  1.00 34.13           C  
ANISOU 1803  CB  VAL A 383     5062   4932   2973   -146    467    270       C  
ATOM   1804  CG1 VAL A 383       7.240   3.061  33.789  1.00 31.87           C  
ANISOU 1804  CG1 VAL A 383     4812   4470   2828   -220    451    386       C  
ATOM   1805  CG2 VAL A 383       7.622   3.329  36.261  1.00 34.22           C  
ANISOU 1805  CG2 VAL A 383     5127   5031   2843   -249    425    373       C  
ATOM   1806  N   LEU A 384       8.168   5.863  32.353  1.00 29.76           N  
ANISOU 1806  N   LEU A 384     4531   3953   2825     84    408    103       N  
ATOM   1807  CA  LEU A 384       7.657   6.307  31.084  1.00 29.33           C  
ANISOU 1807  CA  LEU A 384     4438   3835   2872    121    424     74       C  
ATOM   1808  C   LEU A 384       7.325   5.079  30.245  1.00 28.69           C  
ANISOU 1808  C   LEU A 384     4352   3729   2819     23    464    187       C  
ATOM   1809  O   LEU A 384       8.223   4.318  29.870  1.00 27.68           O  
ANISOU 1809  O   LEU A 384     4275   3483   2760    -23    427    259       O  
ATOM   1810  CB  LEU A 384       8.687   7.178  30.367  1.00 28.99           C  
ANISOU 1810  CB  LEU A 384     4435   3612   2969    175    351     46       C  
ATOM   1811  CG  LEU A 384       8.047   7.907  29.179  1.00 31.49           C  
ANISOU 1811  CG  LEU A 384     4713   3882   3368    214    346     13       C  
ATOM   1812  CD1 LEU A 384       7.515   9.284  29.622  1.00 34.16           C  
ANISOU 1812  CD1 LEU A 384     5029   4241   3708    330    281   -127       C  
ATOM   1813  CD2 LEU A 384       8.993   7.981  28.001  1.00 32.38           C  
ANISOU 1813  CD2 LEU A 384     4853   3854   3598    175    309     79       C  
ATOM   1814  N   LEU A 385       6.035   4.893  29.979  1.00 28.29           N  
ANISOU 1814  N   LEU A 385     4232   3797   2720      1    526    182       N  
ATOM   1815  CA  LEU A 385       5.529   3.789  29.153  1.00 28.18           C  
ANISOU 1815  CA  LEU A 385     4205   3763   2738    -88    551    276       C  
ATOM   1816  C   LEU A 385       5.417   4.271  27.710  1.00 27.32           C  
ANISOU 1816  C   LEU A 385     4078   3556   2748    -33    551    239       C  
ATOM   1817  O   LEU A 385       4.898   5.365  27.455  1.00 26.28           O  
ANISOU 1817  O   LEU A 385     3906   3450   2630     49    554    150       O  
ATOM   1818  CB  LEU A 385       4.143   3.403  29.660  1.00 30.71           C  
ANISOU 1818  CB  LEU A 385     4446   4291   2932   -154    617    293       C  
ATOM   1819  CG  LEU A 385       3.575   1.992  29.650  1.00 32.78           C  
ANISOU 1819  CG  LEU A 385     4702   4596   3156   -308    623    432       C  
ATOM   1820  CD1 LEU A 385       4.485   1.041  30.426  1.00 36.22           C  
ANISOU 1820  CD1 LEU A 385     5231   4961   3570   -404    547    550       C  
ATOM   1821  CD2 LEU A 385       2.198   2.066  30.326  1.00 33.78           C  
ANISOU 1821  CD2 LEU A 385     4714   4997   3123   -363    702    417       C  
ATOM   1822  N   VAL A 386       5.940   3.476  26.779  1.00 24.89           N  
ANISOU 1822  N   VAL A 386     3797   3137   2524    -74    528    300       N  
ATOM   1823  CA  VAL A 386       5.919   3.819  25.385  1.00 24.21           C  
ANISOU 1823  CA  VAL A 386     3688   2987   2525    -41    527    278       C  
ATOM   1824  C   VAL A 386       5.287   2.647  24.621  1.00 25.07           C  
ANISOU 1824  C   VAL A 386     3772   3098   2656   -101    541    327       C  
ATOM   1825  O   VAL A 386       5.771   1.492  24.711  1.00 24.53           O  
ANISOU 1825  O   VAL A 386     3737   2974   2609   -154    497    379       O  
ATOM   1826  CB  VAL A 386       7.338   4.094  24.819  1.00 23.90           C  
ANISOU 1826  CB  VAL A 386     3680   2842   2558    -20    479    275       C  
ATOM   1827  CG1 VAL A 386       7.227   4.623  23.377  1.00 22.79           C  
ANISOU 1827  CG1 VAL A 386     3504   2683   2473     -6    480    265       C  
ATOM   1828  CG2 VAL A 386       8.112   5.128  25.685  1.00 26.28           C  
ANISOU 1828  CG2 VAL A 386     4016   3118   2851     23    442    239       C  
ATOM   1829  N   LEU A 387       4.215   2.938  23.889  1.00 24.79           N  
ANISOU 1829  N   LEU A 387     3682   3112   2625    -87    577    304       N  
ATOM   1830  CA  LEU A 387       3.644   1.950  22.961  1.00 24.41           C  
ANISOU 1830  CA  LEU A 387     3608   3053   2615   -133    578    336       C  
ATOM   1831  C   LEU A 387       4.052   2.230  21.508  1.00 23.82           C  
ANISOU 1831  C   LEU A 387     3521   2921   2609    -91    562    307       C  
ATOM   1832  O   LEU A 387       3.944   3.363  21.035  1.00 24.21           O  
ANISOU 1832  O   LEU A 387     3557   2978   2665    -43    568    275       O  
ATOM   1833  CB  LEU A 387       2.113   1.877  23.109  1.00 25.40           C  
ANISOU 1833  CB  LEU A 387     3666   3297   2689   -164    627    337       C  
ATOM   1834  CG  LEU A 387       1.347   1.035  22.081  1.00 24.74           C  
ANISOU 1834  CG  LEU A 387     3546   3203   2651   -206    622    360       C  
ATOM   1835  CD1 LEU A 387       1.504  -0.477  22.390  1.00 22.52           C  
ANISOU 1835  CD1 LEU A 387     3300   2870   2388   -310    563    447       C  
ATOM   1836  CD2 LEU A 387      -0.162   1.443  22.025  1.00 24.26           C  
ANISOU 1836  CD2 LEU A 387     3396   3275   2546   -203    677    326       C  
ATOM   1837  N   LEU A 388       4.505   1.183  20.820  1.00 22.32           N  
ANISOU 1837  N   LEU A 388     3333   2682   2465   -111    524    314       N  
ATOM   1838  CA  LEU A 388       4.853   1.229  19.400  1.00 22.76           C  
ANISOU 1838  CA  LEU A 388     3356   2736   2558    -81    513    277       C  
ATOM   1839  C   LEU A 388       3.785   0.434  18.636  1.00 23.40           C  
ANISOU 1839  C   LEU A 388     3399   2831   2660   -100    510    273       C  
ATOM   1840  O   LEU A 388       3.888  -0.787  18.490  1.00 24.58           O  
ANISOU 1840  O   LEU A 388     3554   2934   2852   -118    451    267       O  
ATOM   1841  CB  LEU A 388       6.257   0.653  19.170  1.00 22.43           C  
ANISOU 1841  CB  LEU A 388     3318   2659   2545    -64    461    242       C  
ATOM   1842  CG  LEU A 388       7.374   1.130  20.140  1.00 22.47           C  
ANISOU 1842  CG  LEU A 388     3362   2636   2538    -56    447    249       C  
ATOM   1843  CD1 LEU A 388       8.707   0.442  19.817  1.00 25.87           C  
ANISOU 1843  CD1 LEU A 388     3772   3053   3003    -28    386    189       C  
ATOM   1844  CD2 LEU A 388       7.530   2.608  20.079  1.00 25.63           C  
ANISOU 1844  CD2 LEU A 388     3761   3067   2912    -48    480    261       C  
ATOM   1845  N   PRO A 389       2.721   1.108  18.195  1.00 24.18           N  
ANISOU 1845  N   PRO A 389     3464   2982   2742    -91    550    272       N  
ATOM   1846  CA  PRO A 389       1.709   0.352  17.405  1.00 24.62           C  
ANISOU 1846  CA  PRO A 389     3479   3053   2823   -109    542    264       C  
ATOM   1847  C   PRO A 389       2.258  -0.152  16.079  1.00 22.92           C  
ANISOU 1847  C   PRO A 389     3240   2831   2636    -81    502    215       C  
ATOM   1848  O   PRO A 389       3.157   0.473  15.506  1.00 22.01           O  
ANISOU 1848  O   PRO A 389     3117   2747   2498    -52    507    194       O  
ATOM   1849  CB  PRO A 389       0.608   1.395  17.123  1.00 25.23           C  
ANISOU 1849  CB  PRO A 389     3518   3191   2876    -84    583    253       C  
ATOM   1850  CG  PRO A 389       0.950   2.615  18.006  1.00 27.28           C  
ANISOU 1850  CG  PRO A 389     3805   3455   3105    -51    598    250       C  
ATOM   1851  CD  PRO A 389       2.441   2.554  18.235  1.00 24.63           C  
ANISOU 1851  CD  PRO A 389     3517   3067   2774    -54    575    264       C  
ATOM   1852  N   LEU A 390       1.695  -1.263  15.587  1.00 24.17           N  
ANISOU 1852  N   LEU A 390     3378   2967   2839    -95    457    195       N  
ATOM   1853  CA  LEU A 390       1.965  -1.750  14.227  1.00 25.25           C  
ANISOU 1853  CA  LEU A 390     3472   3128   2992    -51    414    117       C  
ATOM   1854  C   LEU A 390       3.457  -1.866  13.976  1.00 24.81           C  
ANISOU 1854  C   LEU A 390     3407   3092   2926     -5    384     53       C  
ATOM   1855  O   LEU A 390       3.968  -1.427  12.948  1.00 25.44           O  
ANISOU 1855  O   LEU A 390     3435   3276   2955     26    403      5       O  
ATOM   1856  CB  LEU A 390       1.323  -0.836  13.171  1.00 24.50           C  
ANISOU 1856  CB  LEU A 390     3336   3119   2852    -34    461    114       C  
ATOM   1857  CG  LEU A 390      -0.204  -0.765  13.216  1.00 27.10           C  
ANISOU 1857  CG  LEU A 390     3648   3449   3198    -59    480    144       C  
ATOM   1858  CD1 LEU A 390      -0.759   0.299  12.261  1.00 27.33           C  
ANISOU 1858  CD1 LEU A 390     3652   3545   3190    -33    502    144       C  
ATOM   1859  CD2 LEU A 390      -0.809  -2.173  12.922  1.00 27.05           C  
ANISOU 1859  CD2 LEU A 390     3623   3399   3257    -81    412    115       C  
ATOM   1860  N   THR A 391       4.154  -2.458  14.935  1.00 25.11           N  
ANISOU 1860  N   THR A 391     3489   3049   3004     -9    333     55       N  
ATOM   1861  CA  THR A 391       5.587  -2.518  14.835  1.00 26.30           C  
ANISOU 1861  CA  THR A 391     3618   3227   3146     41    303    -18       C  
ATOM   1862  C   THR A 391       6.085  -3.942  15.058  1.00 26.65           C  
ANISOU 1862  C   THR A 391     3676   3168   3280     82    165    -98       C  
ATOM   1863  O   THR A 391       5.797  -4.556  16.074  1.00 27.84           O  
ANISOU 1863  O   THR A 391     3900   3191   3487     34    100    -30       O  
ATOM   1864  CB  THR A 391       6.229  -1.522  15.821  1.00 25.06           C  
ANISOU 1864  CB  THR A 391     3502   3070   2950     14    359     51       C  
ATOM   1865  OG1 THR A 391       5.869  -1.890  17.161  1.00 33.25           O  
ANISOU 1865  OG1 THR A 391     4613   4002   4018    -29    335    123       O  
ATOM   1866  CG2 THR A 391       5.751  -0.144  15.595  1.00 21.53           C  
ANISOU 1866  CG2 THR A 391     3050   2688   2442    -14    445    116       C  
ATOM   1867  N   SER A 392       6.847  -4.451  14.100  1.00 28.03           N  
ANISOU 1867  N   SER A 392     3775   3412   3463    168    104   -246       N  
ATOM   1868  CA  SER A 392       7.438  -5.778  14.193  1.00 28.18           C  
ANISOU 1868  CA  SER A 392     3796   3326   3583    242    -67   -368       C  
ATOM   1869  C   SER A 392       8.598  -5.748  15.174  1.00 28.32           C  
ANISOU 1869  C   SER A 392     3847   3296   3619    259   -105   -370       C  
ATOM   1870  O   SER A 392       8.988  -4.671  15.656  1.00 25.55           O  
ANISOU 1870  O   SER A 392     3504   3012   3192    215     11   -290       O  
ATOM   1871  CB  SER A 392       7.953  -6.243  12.821  1.00 29.53           C  
ANISOU 1871  CB  SER A 392     3847   3634   3741    359   -120   -573       C  
ATOM   1872  OG  SER A 392       9.068  -5.450  12.417  1.00 31.70           O  
ANISOU 1872  OG  SER A 392     4026   4111   3907    390    -31   -636       O  
ATOM   1873  N   ALA A 393       9.131  -6.938  15.447  1.00 28.66           N  
ANISOU 1873  N   ALA A 393     3912   3206   3772    326   -292   -469       N  
ATOM   1874  CA  ALA A 393      10.310  -7.126  16.289  1.00 30.03           C  
ANISOU 1874  CA  ALA A 393     4111   3318   3983    366   -373   -507       C  
ATOM   1875  C   ALA A 393      11.534  -6.395  15.732  1.00 30.67           C  
ANISOU 1875  C   ALA A 393     4067   3613   3975    439   -286   -631       C  
ATOM   1876  O   ALA A 393      12.295  -5.791  16.490  1.00 29.80           O  
ANISOU 1876  O   ALA A 393     3974   3517   3834    416   -240   -582       O  
ATOM   1877  CB  ALA A 393      10.604  -8.600  16.435  1.00 31.89           C  
ANISOU 1877  CB  ALA A 393     4382   3364   4370    446   -632   -621       C  
ATOM   1878  N   GLU A 394      11.745  -6.443  14.417  1.00 31.35           N  
ANISOU 1878  N   GLU A 394     4017   3885   4010    517   -265   -790       N  
ATOM   1879  CA  GLU A 394      12.852  -5.648  13.858  1.00 32.71           C  
ANISOU 1879  CA  GLU A 394     4050   4315   4062    544   -162   -876       C  
ATOM   1880  C   GLU A 394      12.677  -4.133  14.125  1.00 30.77           C  
ANISOU 1880  C   GLU A 394     3834   4151   3706    406     25   -674       C  
ATOM   1881  O   GLU A 394      13.642  -3.465  14.480  1.00 30.98           O  
ANISOU 1881  O   GLU A 394     3825   4262   3684    384     72   -661       O  
ATOM   1882  CB  GLU A 394      13.141  -5.962  12.376  1.00 34.51           C  
ANISOU 1882  CB  GLU A 394     4105   4790   4219    640   -169  -1086       C  
ATOM   1883  CG  GLU A 394      12.157  -5.371  11.378  1.00 37.92           C  
ANISOU 1883  CG  GLU A 394     4509   5349   4548    568    -47  -1006       C  
ATOM   1884  CD  GLU A 394      12.455  -5.751   9.933  1.00 42.44           C  
ANISOU 1884  CD  GLU A 394     4904   6192   5030    664    -62  -1223       C  
ATOM   1885  OE1 GLU A 394      13.548  -6.293   9.652  1.00 46.07           O  
ANISOU 1885  OE1 GLU A 394     5229   6797   5479    786   -141  -1449       O  
ATOM   1886  OE2 GLU A 394      11.581  -5.503   9.070  1.00 46.79           O  
ANISOU 1886  OE2 GLU A 394     5440   6826   5512    623      0  -1180       O  
ATOM   1887  N   GLY A 395      11.447  -3.625  14.019  1.00 29.39           N  
ANISOU 1887  N   GLY A 395     3729   3931   3508    321    107   -528       N  
ATOM   1888  CA  GLY A 395      11.155  -2.215  14.301  1.00 27.80           C  
ANISOU 1888  CA  GLY A 395     3570   3764   3230    210    240   -354       C  
ATOM   1889  C   GLY A 395      11.302  -1.798  15.764  1.00 27.26           C  
ANISOU 1889  C   GLY A 395     3611   3546   3200    166    243   -240       C  
ATOM   1890  O   GLY A 395      11.844  -0.718  16.087  1.00 24.59           O  
ANISOU 1890  O   GLY A 395     3273   3260   2810    114    306   -171       O  
ATOM   1891  N   SER A 396      10.837  -2.648  16.671  1.00 27.33           N  
ANISOU 1891  N   SER A 396     3714   3374   3295    175    162   -216       N  
ATOM   1892  CA  SER A 396      10.893  -2.262  18.077  1.00 27.80           C  
ANISOU 1892  CA  SER A 396     3874   3324   3366    127    169   -107       C  
ATOM   1893  C   SER A 396      12.314  -2.427  18.623  1.00 28.36           C  
ANISOU 1893  C   SER A 396     3929   3387   3459    174    103   -177       C  
ATOM   1894  O   SER A 396      12.713  -1.681  19.530  1.00 28.38           O  
ANISOU 1894  O   SER A 396     3979   3368   3438    137    138   -106       O  
ATOM   1895  CB  SER A 396       9.885  -3.059  18.898  1.00 28.44           C  
ANISOU 1895  CB  SER A 396     4053   3254   3501     85    108    -26       C  
ATOM   1896  OG  SER A 396      10.052  -4.433  18.632  1.00 30.48           O  
ANISOU 1896  OG  SER A 396     4309   3422   3850    137    -43   -115       O  
ATOM   1897  N   GLN A 397      13.084  -3.378  18.073  1.00 28.99           N  
ANISOU 1897  N   GLN A 397     3936   3491   3588    266     -2   -336       N  
ATOM   1898  CA  GLN A 397      14.509  -3.480  18.446  1.00 29.94           C  
ANISOU 1898  CA  GLN A 397     4010   3640   3727    327    -66   -435       C  
ATOM   1899  C   GLN A 397      15.314  -2.276  17.902  1.00 29.61           C  
ANISOU 1899  C   GLN A 397     3857   3813   3581    293     55   -442       C  
ATOM   1900  O   GLN A 397      16.134  -1.689  18.630  1.00 29.02           O  
ANISOU 1900  O   GLN A 397     3791   3739   3495    270     66   -410       O  
ATOM   1901  CB  GLN A 397      15.147  -4.815  18.025  1.00 30.78           C  
ANISOU 1901  CB  GLN A 397     4051   3722   3921    459   -238   -638       C  
ATOM   1902  CG  GLN A 397      14.563  -6.091  18.742  1.00 32.05           C  
ANISOU 1902  CG  GLN A 397     4344   3619   4214    475   -425   -613       C  
ATOM   1903  CD  GLN A 397      14.425  -5.930  20.256  1.00 30.56           C  
ANISOU 1903  CD  GLN A 397     4305   3267   4039    385   -446   -435       C  
ATOM   1904  OE1 GLN A 397      13.315  -5.865  20.790  1.00 30.26           O  
ANISOU 1904  OE1 GLN A 397     4367   3146   3985    279   -407   -269       O  
ATOM   1905  NE2 GLN A 397      15.555  -5.881  20.950  1.00 29.04           N  
ANISOU 1905  NE2 GLN A 397     4115   3053   3867    427   -508   -481       N  
ATOM   1906  N   GLY A 398      15.029  -1.894  16.652  1.00 29.08           N  
ANISOU 1906  N   GLY A 398     3691   3924   3434    272    137   -464       N  
ATOM   1907  CA  GLY A 398      15.581  -0.675  16.021  1.00 28.13           C  
ANISOU 1907  CA  GLY A 398     3474   4015   3199    189    245   -417       C  
ATOM   1908  C   GLY A 398      15.242   0.616  16.762  1.00 27.21           C  
ANISOU 1908  C   GLY A 398     3462   3812   3066     80    311   -227       C  
ATOM   1909  O   GLY A 398      16.085   1.539  16.878  1.00 26.98           O  
ANISOU 1909  O   GLY A 398     3392   3868   2991     15    339   -180       O  
ATOM   1910  N   TYR A 399      14.029   0.666  17.312  1.00 24.57           N  
ANISOU 1910  N   TYR A 399     3254   3310   2771     64    321   -129       N  
ATOM   1911  CA  TYR A 399      13.601   1.786  18.138  1.00 23.44           C  
ANISOU 1911  CA  TYR A 399     3208   3073   2624     -2    359      8       C  
ATOM   1912  C   TYR A 399      14.604   2.026  19.309  1.00 23.13           C  
ANISOU 1912  C   TYR A 399     3206   2970   2613      3    320     10       C  
ATOM   1913  O   TYR A 399      15.043   3.148  19.535  1.00 22.90           O  
ANISOU 1913  O   TYR A 399     3181   2959   2560    -55    337     75       O  
ATOM   1914  CB  TYR A 399      12.170   1.565  18.665  1.00 21.72           C  
ANISOU 1914  CB  TYR A 399     3092   2722   2437      1    369     70       C  
ATOM   1915  CG  TYR A 399      11.785   2.514  19.778  1.00 21.51           C  
ANISOU 1915  CG  TYR A 399     3155   2608   2409    -30    386    159       C  
ATOM   1916  CD1 TYR A 399      11.349   3.806  19.490  1.00 24.40           C  
ANISOU 1916  CD1 TYR A 399     3530   2991   2748    -72    417    225       C  
ATOM   1917  CD2 TYR A 399      11.871   2.131  21.113  1.00 24.77           C  
ANISOU 1917  CD2 TYR A 399     3643   2924   2846    -12    352    168       C  
ATOM   1918  CE1 TYR A 399      11.010   4.687  20.499  1.00 26.32           C  
ANISOU 1918  CE1 TYR A 399     3845   3158   2999    -72    409    267       C  
ATOM   1919  CE2 TYR A 399      11.521   3.001  22.142  1.00 25.28           C  
ANISOU 1919  CE2 TYR A 399     3773   2943   2891    -26    366    220       C  
ATOM   1920  CZ  TYR A 399      11.092   4.281  21.820  1.00 27.46           C  
ANISOU 1920  CZ  TYR A 399     4046   3237   3150    -43    393    254       C  
ATOM   1921  OH  TYR A 399      10.762   5.176  22.808  1.00 28.53           O  
ANISOU 1921  OH  TYR A 399     4235   3330   3276    -30    383    268       O  
ATOM   1922  N   LEU A 400      14.938   0.977  20.046  1.00 23.32           N  
ANISOU 1922  N   LEU A 400     3263   2903   2692     68    247    -55       N  
ATOM   1923  CA  LEU A 400      15.859   1.096  21.185  1.00 24.28           C  
ANISOU 1923  CA  LEU A 400     3426   2958   2841     80    196    -58       C  
ATOM   1924  C   LEU A 400      17.302   1.413  20.761  1.00 25.35           C  
ANISOU 1924  C   LEU A 400     3442   3234   2958     83    186   -135       C  
ATOM   1925  O   LEU A 400      18.035   2.136  21.467  1.00 25.34           O  
ANISOU 1925  O   LEU A 400     3456   3216   2956     53    177   -101       O  
ATOM   1926  CB  LEU A 400      15.788  -0.161  22.053  1.00 24.92           C  
ANISOU 1926  CB  LEU A 400     3585   2897   2987    136     93    -90       C  
ATOM   1927  CG  LEU A 400      16.535  -0.091  23.396  1.00 27.37           C  
ANISOU 1927  CG  LEU A 400     3966   3117   3317    144     29    -71       C  
ATOM   1928  CD1 LEU A 400      16.084   1.093  24.247  1.00 26.85           C  
ANISOU 1928  CD1 LEU A 400     3975   3026   3200     84     98     40       C  
ATOM   1929  CD2 LEU A 400      16.300  -1.380  24.148  1.00 28.23           C  
ANISOU 1929  CD2 LEU A 400     4163   3080   3483    171    -94    -68       C  
ATOM   1930  N   GLN A 401      17.694   0.902  19.604  1.00 26.96           N  
ANISOU 1930  N   GLN A 401     3512   3595   3136    115    187   -245       N  
ATOM   1931  CA  GLN A 401      19.006   1.220  19.019  1.00 28.87           C  
ANISOU 1931  CA  GLN A 401     3596   4048   3328    101    196   -327       C  
ATOM   1932  C   GLN A 401      19.104   2.729  18.738  1.00 29.00           C  
ANISOU 1932  C   GLN A 401     3594   4155   3270    -43    272   -182       C  
ATOM   1933  O   GLN A 401      20.071   3.360  19.142  1.00 29.92           O  
ANISOU 1933  O   GLN A 401     3673   4314   3379    -92    258   -161       O  
ATOM   1934  CB  GLN A 401      19.321   0.367  17.778  1.00 30.63           C  
ANISOU 1934  CB  GLN A 401     3654   4472   3512    171    185   -498       C  
ATOM   1935  CG  GLN A 401      20.793   0.529  17.265  1.00 34.64           C  
ANISOU 1935  CG  GLN A 401     3959   5252   3949    169    188   -622       C  
ATOM   1936  CD  GLN A 401      21.229  -0.510  16.208  1.00 43.34           C  
ANISOU 1936  CD  GLN A 401     4876   6576   5016    288    150   -861       C  
ATOM   1937  OE1 GLN A 401      20.582  -0.690  15.161  1.00 45.96           O  
ANISOU 1937  OE1 GLN A 401     5154   7027   5283    285    193   -886       O  
ATOM   1938  NE2 GLN A 401      22.359  -1.176  16.472  1.00 44.71           N  
ANISOU 1938  NE2 GLN A 401     4941   6817   5231    403     57  -1057       N  
ATOM   1939  N   ARG A 402      18.107   3.300  18.060  1.00 28.30           N  
ANISOU 1939  N   ARG A 402     3535   4079   3138   -112    329    -78       N  
ATOM   1940  CA  ARG A 402      18.023   4.762  17.890  1.00 28.07           C  
ANISOU 1940  CA  ARG A 402     3529   4068   3068   -249    354     81       C  
ATOM   1941  C   ARG A 402      18.052   5.508  19.232  1.00 27.60           C  
ANISOU 1941  C   ARG A 402     3600   3808   3078   -259    310    157       C  
ATOM   1942  O   ARG A 402      18.741   6.515  19.378  1.00 28.11           O  
ANISOU 1942  O   ARG A 402     3650   3895   3135   -352    282    231       O  
ATOM   1943  CB  ARG A 402      16.775   5.147  17.087  1.00 27.19           C  
ANISOU 1943  CB  ARG A 402     3458   3949   2924   -294    390    169       C  
ATOM   1944  CG  ARG A 402      16.868   4.759  15.573  1.00 30.25           C  
ANISOU 1944  CG  ARG A 402     3697   4588   3208   -324    434    120       C  
ATOM   1945  CD  ARG A 402      15.787   5.458  14.724  1.00 31.76           C  
ANISOU 1945  CD  ARG A 402     3927   4785   3354   -405    453    244       C  
ATOM   1946  NE  ARG A 402      14.436   5.119  15.164  1.00 34.74           N  
ANISOU 1946  NE  ARG A 402     4431   4959   3810   -319    452    244       N  
ATOM   1947  CZ  ARG A 402      13.790   3.996  14.857  1.00 33.96           C  
ANISOU 1947  CZ  ARG A 402     4322   4857   3726   -224    468    144       C  
ATOM   1948  NH1 ARG A 402      14.351   3.072  14.080  1.00 32.39           N  
ANISOU 1948  NH1 ARG A 402     3996   4834   3479   -177    475     10       N  
ATOM   1949  NH2 ARG A 402      12.568   3.808  15.326  1.00 35.30           N  
ANISOU 1949  NH2 ARG A 402     4597   4857   3959   -177    466    167       N  
ATOM   1950  N   LEU A 403      17.298   5.004  20.208  1.00 26.31           N  
ANISOU 1950  N   LEU A 403     3558   3465   2974   -170    295    138       N  
ATOM   1951  CA  LEU A 403      17.223   5.618  21.521  1.00 25.67           C  
ANISOU 1951  CA  LEU A 403     3592   3224   2938   -160    255    184       C  
ATOM   1952  C   LEU A 403      18.609   5.639  22.210  1.00 26.66           C  
ANISOU 1952  C   LEU A 403     3685   3360   3085   -156    204    139       C  
ATOM   1953  O   LEU A 403      19.012   6.650  22.834  1.00 26.20           O  
ANISOU 1953  O   LEU A 403     3667   3242   3046   -201    163    194       O  
ATOM   1954  CB  LEU A 403      16.160   4.895  22.349  1.00 25.26           C  
ANISOU 1954  CB  LEU A 403     3644   3045   2909    -83    260    169       C  
ATOM   1955  CG  LEU A 403      15.246   5.617  23.336  1.00 26.98           C  
ANISOU 1955  CG  LEU A 403     3972   3149   3132    -73    255    221       C  
ATOM   1956  CD1 LEU A 403      14.596   6.847  22.706  1.00 29.49           C  
ANISOU 1956  CD1 LEU A 403     4293   3466   3445   -121    259    285       C  
ATOM   1957  CD2 LEU A 403      14.168   4.685  23.903  1.00 29.13           C  
ANISOU 1957  CD2 LEU A 403     4301   3373   3392    -27    276    212       C  
ATOM   1958  N   ARG A 404      19.351   4.543  22.084  1.00 26.08           N  
ANISOU 1958  N   ARG A 404     3535   3358   3018    -94    188     28       N  
ATOM   1959  CA  ARG A 404      20.692   4.465  22.689  1.00 26.32           C  
ANISOU 1959  CA  ARG A 404     3518   3411   3073    -76    130    -37       C  
ATOM   1960  C   ARG A 404      21.665   5.480  22.065  1.00 26.44           C  
ANISOU 1960  C   ARG A 404     3412   3589   3047   -192    141      3       C  
ATOM   1961  O   ARG A 404      22.493   6.044  22.760  1.00 26.11           O  
ANISOU 1961  O   ARG A 404     3373   3516   3030   -222     93     18       O  
ATOM   1962  CB  ARG A 404      21.274   3.046  22.612  1.00 26.23           C  
ANISOU 1962  CB  ARG A 404     3438   3439   3091     35     78   -191       C  
ATOM   1963  CG  ARG A 404      20.502   2.027  23.433  1.00 27.14           C  
ANISOU 1963  CG  ARG A 404     3687   3365   3258    119     22   -202       C  
ATOM   1964  CD  ARG A 404      21.294   0.685  23.612  1.00 27.66           C  
ANISOU 1964  CD  ARG A 404     3711   3409   3388    234    -97   -354       C  
ATOM   1965  NE  ARG A 404      20.582  -0.265  24.473  1.00 26.38           N  
ANISOU 1965  NE  ARG A 404     3695   3048   3279    278   -184   -323       N  
ATOM   1966  CZ  ARG A 404      20.642  -0.297  25.807  1.00 28.49           C  
ANISOU 1966  CZ  ARG A 404     4088   3173   3564    274   -248   -258       C  
ATOM   1967  NH1 ARG A 404      21.382   0.591  26.476  1.00 26.78           N  
ANISOU 1967  NH1 ARG A 404     3874   2970   3330    248   -238   -236       N  
ATOM   1968  NH2 ARG A 404      19.954  -1.224  26.486  1.00 27.01           N  
ANISOU 1968  NH2 ARG A 404     4023   2836   3406    282   -334   -207       N  
ATOM   1969  N   ILE A 405      21.549   5.672  20.758  1.00 26.82           N  
ANISOU 1969  N   ILE A 405     3350   3818   3023   -268    197     28       N  
ATOM   1970  CA  ILE A 405      22.320   6.665  20.018  1.00 28.84           C  
ANISOU 1970  CA  ILE A 405     3486   4260   3213   -426    207    109       C  
ATOM   1971  C   ILE A 405      21.979   8.082  20.528  1.00 28.54           C  
ANISOU 1971  C   ILE A 405     3573   4055   3214   -532    155    277       C  
ATOM   1972  O   ILE A 405      22.872   8.891  20.786  1.00 29.43           O  
ANISOU 1972  O   ILE A 405     3652   4192   3338   -633    101    336       O  
ATOM   1973  CB  ILE A 405      22.057   6.536  18.493  1.00 29.34           C  
ANISOU 1973  CB  ILE A 405     3420   4561   3167   -494    275    117       C  
ATOM   1974  CG1 ILE A 405      22.724   5.258  17.941  1.00 30.70           C  
ANISOU 1974  CG1 ILE A 405     3421   4949   3294   -386    299    -90       C  
ATOM   1975  CG2 ILE A 405      22.573   7.776  17.748  1.00 30.62           C  
ANISOU 1975  CG2 ILE A 405     3495   4893   3246   -711    272    275       C  
ATOM   1976  CD1 ILE A 405      22.282   4.890  16.511  1.00 34.89           C  
ANISOU 1976  CD1 ILE A 405     3834   5708   3714   -405    364   -127       C  
ATOM   1977  N   LEU A 406      20.688   8.341  20.707  1.00 27.50           N  
ANISOU 1977  N   LEU A 406     3582   3753   3116   -498    155    336       N  
ATOM   1978  CA  LEU A 406      20.222   9.602  21.264  1.00 28.67           C  
ANISOU 1978  CA  LEU A 406     3855   3719   3320   -550     78    449       C  
ATOM   1979  C   LEU A 406      20.759   9.848  22.693  1.00 27.38           C  
ANISOU 1979  C   LEU A 406     3770   3407   3228   -490      8    408       C  
ATOM   1980  O   LEU A 406      21.239  10.933  23.009  1.00 27.08           O  
ANISOU 1980  O   LEU A 406     3757   3301   3231   -574    -84    480       O  
ATOM   1981  CB  LEU A 406      18.687   9.652  21.204  1.00 28.59           C  
ANISOU 1981  CB  LEU A 406     3953   3586   3325   -487     95    469       C  
ATOM   1982  CG  LEU A 406      17.926  10.867  21.745  1.00 33.25           C  
ANISOU 1982  CG  LEU A 406     4671   3982   3981   -491      0    537       C  
ATOM   1983  CD1 LEU A 406      18.363  12.205  21.120  1.00 35.36           C  
ANISOU 1983  CD1 LEU A 406     4927   4242   4266   -657   -111    680       C  
ATOM   1984  CD2 LEU A 406      16.403  10.636  21.573  1.00 33.73           C  
ANISOU 1984  CD2 LEU A 406     4794   3982   4039   -408     40    518       C  
ATOM   1985  N   PHE A 407      20.694   8.835  23.543  1.00 26.13           N  
ANISOU 1985  N   PHE A 407     3650   3195   3083   -355     34    298       N  
ATOM   1986  CA  PHE A 407      21.280   8.927  24.877  1.00 26.34           C  
ANISOU 1986  CA  PHE A 407     3740   3111   3156   -299    -30    253       C  
ATOM   1987  C   PHE A 407      22.778   9.196  24.867  1.00 26.89           C  
ANISOU 1987  C   PHE A 407     3707   3274   3238   -370    -77    243       C  
ATOM   1988  O   PHE A 407      23.255   9.935  25.731  1.00 26.09           O  
ANISOU 1988  O   PHE A 407     3659   3071   3184   -384   -160    259       O  
ATOM   1989  CB  PHE A 407      20.990   7.677  25.700  1.00 26.87           C  
ANISOU 1989  CB  PHE A 407     3863   3124   3222   -168     -9    161       C  
ATOM   1990  CG  PHE A 407      19.735   7.785  26.526  1.00 29.87           C  
ANISOU 1990  CG  PHE A 407     4375   3379   3597   -105     -4    176       C  
ATOM   1991  CD1 PHE A 407      19.805   8.129  27.874  1.00 34.67           C  
ANISOU 1991  CD1 PHE A 407     5071   3887   4213    -55    -61    154       C  
ATOM   1992  CD2 PHE A 407      18.482   7.584  25.946  1.00 33.00           C  
ANISOU 1992  CD2 PHE A 407     4788   3782   3966    -96     58    201       C  
ATOM   1993  CE1 PHE A 407      18.644   8.237  28.646  1.00 35.27           C  
ANISOU 1993  CE1 PHE A 407     5239   3907   4256      2    -49    149       C  
ATOM   1994  CE2 PHE A 407      17.311   7.697  26.698  1.00 33.97           C  
ANISOU 1994  CE2 PHE A 407     5003   3835   4070    -43     68    202       C  
ATOM   1995  CZ  PHE A 407      17.395   8.018  28.056  1.00 36.17           C  
ANISOU 1995  CZ  PHE A 407     5355   4047   4340      6     19    171       C  
ATOM   1996  N   ALA A 408      23.497   8.583  23.910  1.00 26.56           N  
ANISOU 1996  N   ALA A 408     3507   3439   3147   -408    -28    200       N  
ATOM   1997  CA  ALA A 408      24.948   8.774  23.733  1.00 28.32           C  
ANISOU 1997  CA  ALA A 408     3584   3820   3358   -487    -57    177       C  
ATOM   1998  C   ALA A 408      25.303  10.200  23.307  1.00 28.81           C  
ANISOU 1998  C   ALA A 408     3615   3916   3415   -682   -110    332       C  
ATOM   1999  O   ALA A 408      26.317  10.762  23.772  1.00 29.63           O  
ANISOU 1999  O   ALA A 408     3679   4028   3552   -752   -182    350       O  
ATOM   2000  CB  ALA A 408      25.532   7.761  22.696  1.00 27.62           C  
ANISOU 2000  CB  ALA A 408     3301   3998   3196   -469     10     63       C  
ATOM   2001  N   GLU A 409      24.499  10.777  22.414  1.00 29.23           N  
ANISOU 2001  N   GLU A 409     3688   3985   3433   -780    -93    452       N  
ATOM   2002  CA  GLU A 409      24.643  12.202  22.077  1.00 31.23           C  
ANISOU 2002  CA  GLU A 409     3957   4205   3703   -975   -191    631       C  
ATOM   2003  C   GLU A 409      24.470  13.083  23.315  1.00 30.24           C  
ANISOU 2003  C   GLU A 409     3998   3795   3698   -932   -324    653       C  
ATOM   2004  O   GLU A 409      25.299  13.951  23.590  1.00 32.12           O  
ANISOU 2004  O   GLU A 409     4220   4001   3982  -1051   -435    725       O  
ATOM   2005  CB  GLU A 409      23.623  12.644  21.023  1.00 32.59           C  
ANISOU 2005  CB  GLU A 409     4161   4388   3833  -1061   -182    755       C  
ATOM   2006  CG  GLU A 409      23.831  12.123  19.613  1.00 35.89           C  
ANISOU 2006  CG  GLU A 409     4404   5119   4112  -1158    -77    773       C  
ATOM   2007  CD  GLU A 409      22.668  12.488  18.691  1.00 41.97           C  
ANISOU 2007  CD  GLU A 409     5235   5865   4847  -1215    -76    886       C  
ATOM   2008  OE1 GLU A 409      21.981  13.503  18.955  1.00 46.01           O  
ANISOU 2008  OE1 GLU A 409     5895   6142   5443  -1253   -196    999       O  
ATOM   2009  OE2 GLU A 409      22.452  11.781  17.687  1.00 42.88           O  
ANISOU 2009  OE2 GLU A 409     5245   6195   4853  -1215     27    849       O  
ATOM   2010  N   ARG A 410      23.390  12.853  24.059  1.00 28.61           N  
ANISOU 2010  N   ARG A 410     3937   3401   3534   -766   -317    582       N  
ATOM   2011  CA  ARG A 410      23.022  13.715  25.170  1.00 27.83           C  
ANISOU 2011  CA  ARG A 410     3986   3059   3529   -702   -443    574       C  
ATOM   2012  C   ARG A 410      23.963  13.578  26.379  1.00 29.09           C  
ANISOU 2012  C   ARG A 410     4156   3169   3728   -636   -489    484       C  
ATOM   2013  O   ARG A 410      24.381  14.576  26.963  1.00 29.42           O  
ANISOU 2013  O   ARG A 410     4249   3083   3847   -680   -631    514       O  
ATOM   2014  CB  ARG A 410      21.575  13.440  25.599  1.00 26.54           C  
ANISOU 2014  CB  ARG A 410     3940   2777   3367   -544   -405    506       C  
ATOM   2015  CG  ARG A 410      21.163  14.193  26.879  1.00 23.54           C  
ANISOU 2015  CG  ARG A 410     3690   2194   3059   -438   -523    441       C  
ATOM   2016  CD  ARG A 410      21.218  15.764  26.717  1.00 26.89           C  
ANISOU 2016  CD  ARG A 410     4169   2464   3586   -538   -723    532       C  
ATOM   2017  NE  ARG A 410      20.715  16.359  27.941  1.00 28.26           N  
ANISOU 2017  NE  ARG A 410     4454   2463   3821   -391   -836    419       N  
ATOM   2018  CZ  ARG A 410      21.428  16.530  29.051  1.00 28.12           C  
ANISOU 2018  CZ  ARG A 410     4463   2386   3834   -337   -906    341       C  
ATOM   2019  NH1 ARG A 410      22.727  16.232  29.096  1.00 26.47           N  
ANISOU 2019  NH1 ARG A 410     4182   2255   3620   -425   -890    375       N  
ATOM   2020  NH2 ARG A 410      20.837  17.045  30.114  1.00 29.81           N  
ANISOU 2020  NH2 ARG A 410     4767   2478   4082   -188  -1001    215       N  
ATOM   2021  N   PHE A 411      24.277  12.335  26.740  1.00 28.93           N  
ANISOU 2021  N   PHE A 411     4093   3237   3663   -529   -392    372       N  
ATOM   2022  CA  PHE A 411      25.056  12.018  27.941  1.00 31.12           C  
ANISOU 2022  CA  PHE A 411     4393   3463   3969   -443   -436    277       C  
ATOM   2023  C   PHE A 411      26.400  11.385  27.528  1.00 33.94           C  
ANISOU 2023  C   PHE A 411     4585   4008   4302   -494   -406    236       C  
ATOM   2024  O   PHE A 411      26.768  11.396  26.355  1.00 35.21           O  
ANISOU 2024  O   PHE A 411     4608   4354   4418   -614   -358    287       O  
ATOM   2025  CB  PHE A 411      24.232  11.077  28.839  1.00 29.07           C  
ANISOU 2025  CB  PHE A 411     4236   3130   3679   -271   -384    183       C  
ATOM   2026  CG  PHE A 411      22.876  11.646  29.256  1.00 29.47           C  
ANISOU 2026  CG  PHE A 411     4412   3053   3730   -211   -400    193       C  
ATOM   2027  CD1 PHE A 411      22.794  12.627  30.246  1.00 29.93           C  
ANISOU 2027  CD1 PHE A 411     4561   2976   3834   -170   -515    166       C  
ATOM   2028  CD2 PHE A 411      21.692  11.196  28.658  1.00 27.56           C  
ANISOU 2028  CD2 PHE A 411     4184   2842   3443   -183   -309    208       C  
ATOM   2029  CE1 PHE A 411      21.548  13.162  30.632  1.00 32.30           C  
ANISOU 2029  CE1 PHE A 411     4951   3190   4129    -91   -540    135       C  
ATOM   2030  CE2 PHE A 411      20.453  11.702  29.044  1.00 30.12           C  
ANISOU 2030  CE2 PHE A 411     4600   3080   3764   -118   -324    194       C  
ATOM   2031  CZ  PHE A 411      20.379  12.710  30.034  1.00 30.29           C  
ANISOU 2031  CZ  PHE A 411     4698   2983   3826    -66   -441    148       C  
ATOM   2032  N   GLY A 412      27.160  10.837  28.453  1.00 36.21           N  
ANISOU 2032  N   GLY A 412     4872   4275   4610   -405   -439    136       N  
ATOM   2033  CA  GLY A 412      28.317  10.030  27.993  1.00 41.46           C  
ANISOU 2033  CA  GLY A 412     5362   5138   5251   -414   -410     54       C  
ATOM   2034  C   GLY A 412      28.154   9.193  26.698  1.00 43.33           C  
ANISOU 2034  C   GLY A 412     5465   5582   5417   -423   -302     20       C  
ATOM   2035  O   GLY A 412      27.160   8.493  26.499  1.00 41.88           O  
ANISOU 2035  O   GLY A 412     5346   5355   5210   -337   -242     -1       O  
ATOM   2036  N   GLN A 413      29.135   9.267  25.802  1.00 47.04           N  
ANISOU 2036  N   GLN A 413     5731   6300   5842   -532   -279      9       N  
ATOM   2037  CA  GLN A 413      29.351   8.167  24.858  1.00 49.99           C  
ANISOU 2037  CA  GLN A 413     5941   6906   6149   -476   -201   -114       C  
ATOM   2038  C   GLN A 413      29.982   7.032  25.678  1.00 50.97           C  
ANISOU 2038  C   GLN A 413     6057   6984   6327   -292   -260   -301       C  
ATOM   2039  O   GLN A 413      29.951   5.863  25.283  1.00 51.90           O  
ANISOU 2039  O   GLN A 413     6107   7180   6432   -168   -245   -443       O  
ATOM   2040  CB  GLN A 413      30.247   8.594  23.691  1.00 51.89           C  
ANISOU 2040  CB  GLN A 413     5938   7481   6297   -649   -159    -88       C  
ATOM   2041  CG  GLN A 413      30.469   7.540  22.601  1.00 54.87           C  
ANISOU 2041  CG  GLN A 413     6114   8153   6581   -587    -78   -243       C  
ATOM   2042  CD  GLN A 413      29.322   7.427  21.602  1.00 56.95           C  
ANISOU 2042  CD  GLN A 413     6409   8456   6774   -613      6   -177       C  
ATOM   2043  OE1 GLN A 413      28.864   8.422  21.031  1.00 58.92           O  
ANISOU 2043  OE1 GLN A 413     6685   8726   6975   -791     29     14       O  
ATOM   2044  NE2 GLN A 413      28.864   6.196  21.371  1.00 57.09           N  
ANISOU 2044  NE2 GLN A 413     6422   8474   6793   -435     31   -335       N  
ATOM   2045  N   ALA A 414      30.523   7.397  26.840  1.00 52.02           N  
ANISOU 2045  N   ALA A 414     6270   6969   6528   -271   -351   -299       N  
ATOM   2046  CA  ALA A 414      31.108   6.456  27.795  1.00 52.99           C  
ANISOU 2046  CA  ALA A 414     6420   7003   6710   -108   -439   -447       C  
ATOM   2047  C   ALA A 414      30.122   6.018  28.891  1.00 52.40           C  
ANISOU 2047  C   ALA A 414     6587   6652   6672      6   -480   -418       C  
ATOM   2048  O   ALA A 414      30.530   5.504  29.944  1.00 53.21           O  
ANISOU 2048  O   ALA A 414     6764   6632   6821    107   -579   -485       O  
ATOM   2049  CB  ALA A 414      32.362   7.066  28.416  1.00 54.24           C  
ANISOU 2049  CB  ALA A 414     6507   7194   6909   -158   -521   -468       C  
ATOM   2050  N   ARG A 415      28.832   6.242  28.651  1.00 51.69           N  
ANISOU 2050  N   ARG A 415     6611   6481   6550    -22   -410   -313       N  
ATOM   2051  CA  ARG A 415      27.770   5.768  29.534  1.00 50.76           C  
ANISOU 2051  CA  ARG A 415     6688   6165   6434     63   -426   -280       C  
ATOM   2052  C   ARG A 415      26.751   4.984  28.709  1.00 49.53           C  
ANISOU 2052  C   ARG A 415     6537   6035   6247     92   -354   -278       C  
ATOM   2053  O   ARG A 415      26.484   5.330  27.562  1.00 50.13           O  
ANISOU 2053  O   ARG A 415     6519   6239   6287     19   -271   -247       O  
ATOM   2054  CB  ARG A 415      27.049   6.935  30.218  1.00 50.34           C  
ANISOU 2054  CB  ARG A 415     6772   5984   6370     10   -422   -166       C  
ATOM   2055  CG  ARG A 415      27.888   7.721  31.196  1.00 52.29           C  
ANISOU 2055  CG  ARG A 415     7048   6165   6655     -4   -515   -170       C  
ATOM   2056  CD  ARG A 415      27.102   8.066  32.455  1.00 54.14           C  
ANISOU 2056  CD  ARG A 415     7462   6241   6870     50   -552   -140       C  
ATOM   2057  NE  ARG A 415      28.001   8.571  33.491  1.00 57.20           N  
ANISOU 2057  NE  ARG A 415     7877   6566   7291     66   -659   -175       N  
ATOM   2058  CZ  ARG A 415      27.880   8.329  34.797  1.00 58.93           C  
ANISOU 2058  CZ  ARG A 415     8217   6692   7481    148   -722   -203       C  
ATOM   2059  NH1 ARG A 415      26.889   7.575  35.269  1.00 58.51           N  
ANISOU 2059  NH1 ARG A 415     8267   6610   7356    204   -688   -185       N  
ATOM   2060  NH2 ARG A 415      28.773   8.835  35.638  1.00 59.82           N  
ANISOU 2060  NH2 ARG A 415     8343   6759   7628    160   -825   -243       N  
ATOM   2061  N   GLU A 416      26.191   3.931  29.292  1.00 48.46           N  
ANISOU 2061  N   GLU A 416     6510   5780   6123    184   -398   -301       N  
ATOM   2062  CA  GLU A 416      25.009   3.283  28.729  1.00 46.75           C  
ANISOU 2062  CA  GLU A 416     6336   5545   5883    197   -343   -271       C  
ATOM   2063  C   GLU A 416      23.786   3.796  29.462  1.00 44.31           C  
ANISOU 2063  C   GLU A 416     6183   5125   5530    164   -301   -150       C  
ATOM   2064  O   GLU A 416      23.892   4.224  30.614  1.00 44.03           O  
ANISOU 2064  O   GLU A 416     6240   5007   5484    169   -347   -121       O  
ATOM   2065  CB  GLU A 416      25.097   1.754  28.836  1.00 47.73           C  
ANISOU 2065  CB  GLU A 416     6476   5606   6053    301   -444   -362       C  
ATOM   2066  CG  GLU A 416      26.347   1.111  28.224  1.00 49.94           C  
ANISOU 2066  CG  GLU A 416     6589   6000   6386    379   -519   -537       C  
ATOM   2067  CD  GLU A 416      26.624   1.503  26.770  1.00 51.58           C  
ANISOU 2067  CD  GLU A 416     6599   6447   6550    336   -415   -597       C  
ATOM   2068  OE1 GLU A 416      25.683   1.606  25.947  1.00 51.00           O  
ANISOU 2068  OE1 GLU A 416     6524   6420   6432    291   -320   -539       O  
ATOM   2069  OE2 GLU A 416      27.811   1.691  26.449  1.00 54.22           O  
ANISOU 2069  OE2 GLU A 416     6770   6945   6886    341   -433   -703       O  
ATOM   2070  N   LEU A 417      22.630   3.774  28.790  1.00 42.28           N  
ANISOU 2070  N   LEU A 417     5939   4884   5239    136   -217    -97       N  
ATOM   2071  CA  LEU A 417      21.335   4.149  29.402  1.00 39.43           C  
ANISOU 2071  CA  LEU A 417     5700   4454   4828    117   -173     -8       C  
ATOM   2072  C   LEU A 417      21.183   3.676  30.839  1.00 38.50           C  
ANISOU 2072  C   LEU A 417     5703   4246   4681    149   -241     13       C  
ATOM   2073  O   LEU A 417      20.689   4.408  31.705  1.00 37.67           O  
ANISOU 2073  O   LEU A 417     5670   4122   4522    140   -227     51       O  
ATOM   2074  CB  LEU A 417      20.159   3.551  28.608  1.00 39.48           C  
ANISOU 2074  CB  LEU A 417     5705   4481   4814    108   -107     22       C  
ATOM   2075  CG  LEU A 417      19.359   4.430  27.645  1.00 39.69           C  
ANISOU 2075  CG  LEU A 417     5693   4569   4819     58    -13     66       C  
ATOM   2076  CD1 LEU A 417      19.979   4.384  26.251  1.00 41.69           C  
ANISOU 2076  CD1 LEU A 417     5810   4941   5089     32     14     26       C  
ATOM   2077  CD2 LEU A 417      17.915   3.985  27.575  1.00 40.12           C  
ANISOU 2077  CD2 LEU A 417     5801   4606   4837     57     39    111       C  
ATOM   2078  N   GLU A 418      21.572   2.423  31.082  1.00 36.40           N  
ANISOU 2078  N   GLU A 418     5457   3930   4445    187   -331    -16       N  
ATOM   2079  CA  GLU A 418      21.353   1.804  32.375  1.00 36.11           C  
ANISOU 2079  CA  GLU A 418     5542   3811   4366    189   -413     37       C  
ATOM   2080  C   GLU A 418      22.205   2.429  33.479  1.00 35.60           C  
ANISOU 2080  C   GLU A 418     5517   3724   4286    207   -475     19       C  
ATOM   2081  O   GLU A 418      21.824   2.407  34.652  1.00 36.04           O  
ANISOU 2081  O   GLU A 418     5673   3760   4261    191   -505     76       O  
ATOM   2082  CB  GLU A 418      21.587   0.291  32.274  1.00 36.35           C  
ANISOU 2082  CB  GLU A 418     5595   3760   4458    219   -540     19       C  
ATOM   2083  CG  GLU A 418      20.563  -0.422  31.382  1.00 35.93           C  
ANISOU 2083  CG  GLU A 418     5528   3708   4414    196   -503     48       C  
ATOM   2084  CD  GLU A 418      20.899  -0.446  29.867  1.00 36.57           C  
ANISOU 2084  CD  GLU A 418     5469   3864   4562    241   -457    -62       C  
ATOM   2085  OE1 GLU A 418      21.741   0.337  29.373  1.00 35.81           O  
ANISOU 2085  OE1 GLU A 418     5267   3860   4478    259   -410   -135       O  
ATOM   2086  OE2 GLU A 418      20.292  -1.278  29.155  1.00 33.87           O  
ANISOU 2086  OE2 GLU A 418     5116   3504   4251    247   -474    -71       O  
ATOM   2087  N   SER A 419      23.344   3.001  33.098  1.00 34.67           N  
ANISOU 2087  N   SER A 419     5309   3632   4234    231   -492    -60       N  
ATOM   2088  CA  SER A 419      24.219   3.702  34.052  1.00 34.99           C  
ANISOU 2088  CA  SER A 419     5373   3647   4274    247   -556    -87       C  
ATOM   2089  C   SER A 419      23.588   5.005  34.569  1.00 34.27           C  
ANISOU 2089  C   SER A 419     5327   3573   4120    220   -496    -50       C  
ATOM   2090  O   SER A 419      24.048   5.576  35.556  1.00 34.95           O  
ANISOU 2090  O   SER A 419     5459   3632   4188    240   -556    -70       O  
ATOM   2091  CB  SER A 419      25.583   3.992  33.419  1.00 35.14           C  
ANISOU 2091  CB  SER A 419     5260   3713   4379    260   -590   -177       C  
ATOM   2092  OG  SER A 419      25.510   5.183  32.637  1.00 36.66           O  
ANISOU 2092  OG  SER A 419     5374   3978   4575    196   -502   -158       O  
ATOM   2093  N   LEU A 420      22.535   5.474  33.896  1.00 32.67           N  
ANISOU 2093  N   LEU A 420     5110   3411   3892    189   -394    -13       N  
ATOM   2094  CA  LEU A 420      21.779   6.633  34.356  1.00 32.30           C  
ANISOU 2094  CA  LEU A 420     5104   3374   3795    189   -362     -5       C  
ATOM   2095  C   LEU A 420      20.603   6.256  35.274  1.00 31.72           C  
ANISOU 2095  C   LEU A 420     5113   3340   3598    201   -331     26       C  
ATOM   2096  O   LEU A 420      19.773   7.098  35.591  1.00 31.34           O  
ANISOU 2096  O   LEU A 420     5079   3333   3495    221   -297      5       O  
ATOM   2097  CB  LEU A 420      21.293   7.453  33.166  1.00 31.97           C  
ANISOU 2097  CB  LEU A 420     4999   3354   3795    151   -296     10       C  
ATOM   2098  CG  LEU A 420      22.380   7.954  32.207  1.00 34.91           C  
ANISOU 2098  CG  LEU A 420     5273   3736   4257     99   -319      5       C  
ATOM   2099  CD1 LEU A 420      21.912   7.865  30.761  1.00 35.10           C  
ANISOU 2099  CD1 LEU A 420     5220   3824   4293     45   -239     44       C  
ATOM   2100  CD2 LEU A 420      22.800   9.371  32.546  1.00 35.18           C  
ANISOU 2100  CD2 LEU A 420     5317   3715   4334     78   -394     -2       C  
ATOM   2101  N   GLY A 421      20.551   4.995  35.707  1.00 31.79           N  
ANISOU 2101  N   GLY A 421     5169   3346   3564    186   -361     74       N  
ATOM   2102  CA  GLY A 421      19.439   4.493  36.534  1.00 31.35           C  
ANISOU 2102  CA  GLY A 421     5178   3364   3371    155   -334    137       C  
ATOM   2103  C   GLY A 421      18.205   4.086  35.714  1.00 30.95           C  
ANISOU 2103  C   GLY A 421     5097   3364   3300    112   -238    188       C  
ATOM   2104  O   GLY A 421      17.091   4.047  36.238  1.00 32.35           O  
ANISOU 2104  O   GLY A 421     5290   3646   3354     81   -183    225       O  
ATOM   2105  N   VAL A 422      18.387   3.775  34.436  1.00 28.78           N  
ANISOU 2105  N   VAL A 422     4766   3039   3132    109   -217    182       N  
ATOM   2106  CA  VAL A 422      17.247   3.306  33.629  1.00 27.96           C  
ANISOU 2106  CA  VAL A 422     4635   2973   3016     70   -139    228       C  
ATOM   2107  C   VAL A 422      17.143   1.764  33.647  1.00 28.12           C  
ANISOU 2107  C   VAL A 422     4698   2942   3045     23   -209    301       C  
ATOM   2108  O   VAL A 422      18.091   1.057  33.283  1.00 28.04           O  
ANISOU 2108  O   VAL A 422     4682   2841   3132     50   -302    270       O  
ATOM   2109  CB  VAL A 422      17.255   3.881  32.187  1.00 27.15           C  
ANISOU 2109  CB  VAL A 422     4446   2867   3001     86    -76    186       C  
ATOM   2110  CG1 VAL A 422      15.988   3.478  31.443  1.00 27.67           C  
ANISOU 2110  CG1 VAL A 422     4490   2978   3046     53      1    227       C  
ATOM   2111  CG2 VAL A 422      17.322   5.400  32.207  1.00 27.37           C  
ANISOU 2111  CG2 VAL A 422     4453   2910   3036    113    -54    139       C  
ATOM   2112  N   ARG A 423      15.996   1.268  34.116  1.00 28.02           N  
ANISOU 2112  N   ARG A 423     4721   2995   2930    -50   -181    390       N  
ATOM   2113  CA  ARG A 423      15.645  -0.135  34.056  1.00 28.86           C  
ANISOU 2113  CA  ARG A 423     4873   3044   3050   -124   -261    486       C  
ATOM   2114  C   ARG A 423      14.643  -0.303  32.906  1.00 28.19           C  
ANISOU 2114  C   ARG A 423     4727   2986   2997   -144   -176    491       C  
ATOM   2115  O   ARG A 423      13.580   0.316  32.904  1.00 28.41           O  
ANISOU 2115  O   ARG A 423     4718   3137   2940   -168    -59    502       O  
ATOM   2116  CB  ARG A 423      15.030  -0.607  35.377  1.00 30.92           C  
ANISOU 2116  CB  ARG A 423     5208   3382   3158   -232   -299    613       C  
ATOM   2117  CG  ARG A 423      16.018  -0.680  36.562  1.00 34.26           C  
ANISOU 2117  CG  ARG A 423     5708   3767   3541   -226   -414    629       C  
ATOM   2118  CD  ARG A 423      15.436  -1.535  37.706  1.00 43.75           C  
ANISOU 2118  CD  ARG A 423     6993   5035   4593   -374   -492    800       C  
ATOM   2119  NE  ARG A 423      14.518  -2.536  37.152  1.00 49.24           N  
ANISOU 2119  NE  ARG A 423     7694   5706   5309   -484   -515    913       N  
ATOM   2120  CZ  ARG A 423      14.855  -3.768  36.779  1.00 51.88           C  
ANISOU 2120  CZ  ARG A 423     8093   5848   5772   -521   -691    978       C  
ATOM   2121  NH1 ARG A 423      16.103  -4.207  36.922  1.00 52.39           N  
ANISOU 2121  NH1 ARG A 423     8217   5736   5953   -450   -862    935       N  
ATOM   2122  NH2 ARG A 423      13.927  -4.571  36.267  1.00 53.80           N  
ANISOU 2122  NH2 ARG A 423     8335   6072   6035   -622   -713   1076       N  
ATOM   2123  N   ILE A 424      14.998  -1.138  31.937  1.00 27.46           N  
ANISOU 2123  N   ILE A 424     4618   2788   3029   -121   -246    464       N  
ATOM   2124  CA  ILE A 424      14.172  -1.348  30.753  1.00 27.74           C  
ANISOU 2124  CA  ILE A 424     4594   2841   3106   -128   -182    453       C  
ATOM   2125  C   ILE A 424      13.347  -2.618  30.867  1.00 28.33           C  
ANISOU 2125  C   ILE A 424     4719   2865   3178   -226   -266    564       C  
ATOM   2126  O   ILE A 424      13.872  -3.694  31.181  1.00 28.41           O  
ANISOU 2126  O   ILE A 424     4798   2744   3253   -246   -439    601       O  
ATOM   2127  CB  ILE A 424      15.033  -1.422  29.476  1.00 28.14           C  
ANISOU 2127  CB  ILE A 424     4569   2843   3281    -37   -203    331       C  
ATOM   2128  CG1 ILE A 424      15.888  -0.152  29.353  1.00 26.31           C  
ANISOU 2128  CG1 ILE A 424     4281   2668   3047     23   -134    251       C  
ATOM   2129  CG2 ILE A 424      14.135  -1.685  28.243  1.00 26.72           C  
ANISOU 2129  CG2 ILE A 424     4329   2691   3131    -44   -144    319       C  
ATOM   2130  CD1 ILE A 424      16.894  -0.197  28.222  1.00 29.68           C  
ANISOU 2130  CD1 ILE A 424     4611   3103   3561     90   -155    137       C  
ATOM   2131  N   ARG A 425      12.047  -2.499  30.612  1.00 27.68           N  
ANISOU 2131  N   ARG A 425     4605   2881   3032   -292   -164    619       N  
ATOM   2132  CA  ARG A 425      11.191  -3.687  30.551  1.00 28.56           C  
ANISOU 2132  CA  ARG A 425     4749   2948   3153   -404   -246    733       C  
ATOM   2133  C   ARG A 425      10.373  -3.638  29.261  1.00 28.25           C  
ANISOU 2133  C   ARG A 425     4632   2938   3165   -382   -163    683       C  
ATOM   2134  O   ARG A 425       9.900  -2.576  28.854  1.00 27.11           O  
ANISOU 2134  O   ARG A 425     4416   2912   2973   -339     -9    626       O  
ATOM   2135  CB  ARG A 425      10.274  -3.791  31.766  1.00 29.77           C  
ANISOU 2135  CB  ARG A 425     4937   3232   3142   -556   -222    886       C  
ATOM   2136  CG  ARG A 425      10.994  -4.027  33.139  1.00 32.49           C  
ANISOU 2136  CG  ARG A 425     5374   3559   3414   -609   -330    968       C  
ATOM   2137  CD  ARG A 425       9.995  -3.959  34.266  1.00 34.00           C  
ANISOU 2137  CD  ARG A 425     5562   3959   3396   -765   -269   1107       C  
ATOM   2138  NE  ARG A 425      10.565  -4.149  35.599  1.00 40.16           N  
ANISOU 2138  NE  ARG A 425     6425   4763   4070   -834   -364   1199       N  
ATOM   2139  CZ  ARG A 425      10.902  -3.161  36.431  1.00 42.12           C  
ANISOU 2139  CZ  ARG A 425     6656   5149   4198   -774   -281   1131       C  
ATOM   2140  NH1 ARG A 425      10.763  -1.894  36.069  1.00 41.85           N  
ANISOU 2140  NH1 ARG A 425     6532   5216   4153   -640   -122    969       N  
ATOM   2141  NH2 ARG A 425      11.396  -3.440  37.637  1.00 43.86           N  
ANISOU 2141  NH2 ARG A 425     6957   5395   4314   -848   -382   1225       N  
ATOM   2142  N   GLN A 426      10.210  -4.790  28.629  1.00 29.31           N  
ANISOU 2142  N   GLN A 426     4784   2950   3402   -408   -287    702       N  
ATOM   2143  CA  GLN A 426       9.596  -4.833  27.305  1.00 29.27           C  
ANISOU 2143  CA  GLN A 426     4704   2958   3459   -368   -232    634       C  
ATOM   2144  C   GLN A 426       8.542  -5.916  27.234  1.00 29.78           C  
ANISOU 2144  C   GLN A 426     4796   2974   3545   -493   -320    748       C  
ATOM   2145  O   GLN A 426       8.701  -7.004  27.824  1.00 31.16           O  
ANISOU 2145  O   GLN A 426     5059   3016   3765   -580   -508    848       O  
ATOM   2146  CB  GLN A 426      10.693  -5.085  26.283  1.00 29.31           C  
ANISOU 2146  CB  GLN A 426     4674   2871   3593   -229   -308    476       C  
ATOM   2147  CG  GLN A 426      10.292  -5.236  24.837  1.00 32.41           C  
ANISOU 2147  CG  GLN A 426     4986   3281   4048   -171   -277    381       C  
ATOM   2148  CD  GLN A 426      11.522  -5.501  23.943  1.00 33.50           C  
ANISOU 2148  CD  GLN A 426     5064   3383   4281    -30   -357    203       C  
ATOM   2149  OE1 GLN A 426      12.663  -5.496  24.412  1.00 31.07           O  
ANISOU 2149  OE1 GLN A 426     4770   3039   3998     26   -426    149       O  
ATOM   2150  NE2 GLN A 426      11.284  -5.697  22.660  1.00 34.06           N  
ANISOU 2150  NE2 GLN A 426     5055   3493   4392     29   -343    101       N  
ATOM   2151  N   TYR A 427       7.472  -5.618  26.489  1.00 29.00           N  
ANISOU 2151  N   TYR A 427     4624   2971   3423   -509   -204    739       N  
ATOM   2152  CA  TYR A 427       6.387  -6.556  26.299  1.00 30.72           C  
ANISOU 2152  CA  TYR A 427     4849   3160   3665   -634   -275    842       C  
ATOM   2153  C   TYR A 427       5.853  -6.520  24.867  1.00 30.55           C  
ANISOU 2153  C   TYR A 427     4748   3143   3715   -560   -225    738       C  
ATOM   2154  O   TYR A 427       5.246  -5.543  24.448  1.00 27.23           O  
ANISOU 2154  O   TYR A 427     4251   2868   3227   -525    -54    694       O  
ATOM   2155  CB  TYR A 427       5.262  -6.311  27.309  1.00 32.04           C  
ANISOU 2155  CB  TYR A 427     5000   3504   3671   -799   -180    995       C  
ATOM   2156  CG  TYR A 427       4.148  -7.338  27.215  1.00 35.73           C  
ANISOU 2156  CG  TYR A 427     5467   3955   4153   -968   -267   1132       C  
ATOM   2157  CD1 TYR A 427       4.124  -8.448  28.050  1.00 40.78           C  
ANISOU 2157  CD1 TYR A 427     6198   4502   4795  -1146   -456   1315       C  
ATOM   2158  CD2 TYR A 427       3.130  -7.198  26.274  1.00 36.95           C  
ANISOU 2158  CD2 TYR A 427     5534   4181   4325   -962   -180   1090       C  
ATOM   2159  CE1 TYR A 427       3.103  -9.390  27.953  1.00 44.38           C  
ANISOU 2159  CE1 TYR A 427     6654   4937   5271  -1329   -556   1462       C  
ATOM   2160  CE2 TYR A 427       2.112  -8.133  26.160  1.00 39.68           C  
ANISOU 2160  CE2 TYR A 427     5872   4512   4693  -1125   -267   1215       C  
ATOM   2161  CZ  TYR A 427       2.100  -9.218  27.000  1.00 42.88           C  
ANISOU 2161  CZ  TYR A 427     6366   4827   5102  -1314   -454   1405       C  
ATOM   2162  OH  TYR A 427       1.075 -10.131  26.885  1.00 46.93           O  
ANISOU 2162  OH  TYR A 427     6869   5322   5639  -1503   -556   1550       O  
ATOM   2163  N   GLU A 428       6.105  -7.605  24.146  1.00 32.27           N  
ANISOU 2163  N   GLU A 428     4991   3197   4075   -530   -400    690       N  
ATOM   2164  CA  GLU A 428       5.580  -7.817  22.801  1.00 35.21           C  
ANISOU 2164  CA  GLU A 428     5296   3563   4519   -469   -393    594       C  
ATOM   2165  C   GLU A 428       4.145  -8.335  22.851  1.00 37.27           C  
ANISOU 2165  C   GLU A 428     5550   3847   4765   -625   -405    726       C  
ATOM   2166  O   GLU A 428       3.867  -9.367  23.488  1.00 38.36           O  
ANISOU 2166  O   GLU A 428     5761   3872   4943   -768   -575    865       O  
ATOM   2167  CB  GLU A 428       6.472  -8.825  22.072  1.00 36.18           C  
ANISOU 2167  CB  GLU A 428     5437   3510   4800   -356   -603    458       C  
ATOM   2168  CG  GLU A 428       7.832  -8.230  21.687  1.00 38.56           C  
ANISOU 2168  CG  GLU A 428     5693   3855   5105   -188   -560    286       C  
ATOM   2169  CD  GLU A 428       8.580  -9.056  20.640  1.00 41.53           C  
ANISOU 2169  CD  GLU A 428     6026   4143   5611    -38   -725     85       C  
ATOM   2170  OE1 GLU A 428       7.951  -9.892  19.952  1.00 45.01           O  
ANISOU 2170  OE1 GLU A 428     6461   4504   6138    -38   -841     50       O  
ATOM   2171  OE2 GLU A 428       9.800  -8.856  20.503  1.00 40.69           O  
ANISOU 2171  OE2 GLU A 428     5879   4065   5516     84   -743    -54       O  
ATOM   2172  N   LEU A 429       3.237  -7.600  22.208  1.00 38.97           N  
ANISOU 2172  N   LEU A 429     5676   4210   4921   -611   -237    694       N  
ATOM   2173  CA  LEU A 429       1.814  -7.975  22.121  1.00 42.64           C  
ANISOU 2173  CA  LEU A 429     6103   4732   5367   -747   -226    795       C  
ATOM   2174  C   LEU A 429       1.693  -9.100  21.123  1.00 45.29           C  
ANISOU 2174  C   LEU A 429     6452   4901   5858   -727   -406    743       C  
ATOM   2175  O   LEU A 429       2.351  -9.077  20.091  1.00 45.44           O  
ANISOU 2175  O   LEU A 429     6447   4867   5951   -565   -432    573       O  
ATOM   2176  CB  LEU A 429       0.954  -6.798  21.639  1.00 41.66           C  
ANISOU 2176  CB  LEU A 429     5874   4804   5149   -702    -12    740       C  
ATOM   2177  CG  LEU A 429       0.463  -5.713  22.601  1.00 42.31           C  
ANISOU 2177  CG  LEU A 429     5911   5090   5074   -743    158    788       C  
ATOM   2178  CD1 LEU A 429       1.584  -5.076  23.429  1.00 42.93           C  
ANISOU 2178  CD1 LEU A 429     6041   5170   5100   -682    186    768       C  
ATOM   2179  CD2 LEU A 429      -0.280  -4.640  21.823  1.00 41.14           C  
ANISOU 2179  CD2 LEU A 429     5667   5074   4889   -653    306    690       C  
ATOM   2180  N   ASP A 430       0.832 -10.063  21.417  1.00 49.56           N  
ANISOU 2180  N   ASP A 430     7018   5377   6437   -899   -534    885       N  
ATOM   2181  CA  ASP A 430       0.763 -11.295  20.634  1.00 53.17           C  
ANISOU 2181  CA  ASP A 430     7509   5626   7068   -893   -769    845       C  
ATOM   2182  C   ASP A 430      -0.672 -11.800  20.503  1.00 55.50           C  
ANISOU 2182  C   ASP A 430     7767   5953   7370  -1070   -798    973       C  
ATOM   2183  O   ASP A 430      -1.614 -11.165  20.988  1.00 56.10           O  
ANISOU 2183  O   ASP A 430     7771   6241   7304  -1187   -618   1077       O  
ATOM   2184  CB  ASP A 430       1.647 -12.364  21.303  1.00 54.52           C  
ANISOU 2184  CB  ASP A 430     7806   5560   7350   -934  -1043    903       C  
ATOM   2185  CG  ASP A 430       2.428 -13.202  20.308  1.00 55.67           C  
ANISOU 2185  CG  ASP A 430     7976   5491   7687   -757  -1271    703       C  
ATOM   2186  OD1 ASP A 430       2.710 -14.381  20.631  1.00 59.15           O  
ANISOU 2186  OD1 ASP A 430     8517   5687   8271   -814  -1574    756       O  
ATOM   2187  OD2 ASP A 430       2.762 -12.690  19.217  1.00 53.67           O  
ANISOU 2187  OD2 ASP A 430     7637   5321   7435   -564  -1164    491       O  
ATOM   2188  N   ALA A 431      -0.827 -12.933  19.820  1.00 58.24           N  
ANISOU 2188  N   ALA A 431     8148   6096   7884  -1077  -1034    943       N  
ATOM   2189  CA  ALA A 431      -2.091 -13.654  19.752  1.00 60.85           C  
ANISOU 2189  CA  ALA A 431     8459   6405   8255  -1273  -1129   1086       C  
ATOM   2190  C   ALA A 431      -2.013 -14.868  20.682  1.00 64.08           C  
ANISOU 2190  C   ALA A 431     8991   6609   8749  -1487  -1418   1297       C  
ATOM   2191  O   ALA A 431      -2.927 -15.116  21.481  1.00 65.55           O  
ANISOU 2191  O   ALA A 431     9166   6886   8852  -1754  -1420   1538       O  
ATOM   2192  CB  ALA A 431      -2.365 -14.088  18.328  1.00 60.92           C  
ANISOU 2192  CB  ALA A 431     8429   6314   8404  -1142  -1223    911       C  
ATOM   2193  N   GLY A 432      -0.901 -15.600  20.586  1.00 65.55           N  
ANISOU 2193  N   GLY A 432     9283   6531   9092  -1373  -1670   1206       N  
ATOM   2194  CA  GLY A 432      -0.640 -16.776  21.424  1.00 69.10           C  
ANISOU 2194  CA  GLY A 432     9875   6729   9653  -1549  -2004   1392       C  
ATOM   2195  C   GLY A 432      -0.294 -16.432  22.863  1.00 70.10           C  
ANISOU 2195  C   GLY A 432    10057   6956   9624  -1699  -1935   1593       C  
ATOM   2196  O   GLY A 432      -0.188 -17.322  23.714  1.00 72.47           O  
ANISOU 2196  O   GLY A 432    10477   7084   9975  -1898  -2196   1804       O  
ATOM   2197  N   ASN A 433      -0.115 -15.135  23.118  1.00 68.84           N  
ANISOU 2197  N   ASN A 433     9813   7068   9274  -1606  -1601   1526       N  
ATOM   2198  CA  ASN A 433       0.090 -14.577  24.453  1.00 69.50           C  
ANISOU 2198  CA  ASN A 433     9917   7319   9170  -1728  -1475   1685       C  
ATOM   2199  C   ASN A 433      -0.964 -14.985  25.467  1.00 71.96           C  
ANISOU 2199  C   ASN A 433    10228   7759   9354  -2075  -1503   1997       C  
ATOM   2200  O   ASN A 433      -2.063 -15.412  25.106  1.00 72.75           O  
ANISOU 2200  O   ASN A 433    10272   7896   9474  -2227  -1534   2090       O  
ATOM   2201  CB  ASN A 433       0.080 -13.050  24.378  1.00 67.10           C  
ANISOU 2201  CB  ASN A 433     9494   7311   8691  -1580  -1106   1549       C  
ATOM   2202  CG  ASN A 433       1.468 -12.442  24.410  1.00 65.79           C  
ANISOU 2202  CG  ASN A 433     9363   7100   8535  -1355  -1060   1379       C  
ATOM   2203  OD1 ASN A 433       1.613 -11.228  24.281  1.00 63.56           O  
ANISOU 2203  OD1 ASN A 433     9001   7007   8141  -1225   -808   1262       O  
ATOM   2204  ND2 ASN A 433       2.492 -13.275  24.578  1.00 66.87           N  
ANISOU 2204  ND2 ASN A 433     9615   6981   8811  -1309  -1320   1361       N  
ATOM   2205  N   ASP A 434      -0.625 -14.823  26.742  1.00 73.24           N  
ANISOU 2205  N   ASP A 434    10440   8019   9369  -2206  -1486   2159       N  
ATOM   2206  CA  ASP A 434      -1.607 -14.978  27.804  1.00 75.58           C  
ANISOU 2206  CA  ASP A 434    10697   8550   9469  -2542  -1448   2450       C  
ATOM   2207  C   ASP A 434      -2.452 -13.702  27.886  1.00 74.03           C  
ANISOU 2207  C   ASP A 434    10313   8770   9046  -2512  -1065   2374       C  
ATOM   2208  O   ASP A 434      -1.933 -12.589  27.780  1.00 71.88           O  
ANISOU 2208  O   ASP A 434     9993   8608   8711  -2277   -849   2172       O  
ATOM   2209  CB  ASP A 434      -0.922 -15.276  29.140  1.00 77.32           C  
ANISOU 2209  CB  ASP A 434    11037   8746   9596  -2694  -1579   2647       C  
ATOM   2210  CG  ASP A 434      -1.889 -15.770  30.203  1.00 81.07           C  
ANISOU 2210  CG  ASP A 434    11490   9430   9882  -3098  -1626   2994       C  
ATOM   2211  OD1 ASP A 434      -3.110 -15.842  29.932  1.00 83.36           O  
ANISOU 2211  OD1 ASP A 434    11657   9906  10110  -3259  -1540   3075       O  
ATOM   2212  OD2 ASP A 434      -1.421 -16.089  31.320  1.00 83.21           O  
ANISOU 2212  OD2 ASP A 434    11860   9697  10057  -3264  -1753   3193       O  
ATOM   2213  N   ARG A 435      -3.757 -13.885  28.072  1.00 75.40           N  
ANISOU 2213  N   ARG A 435    10375   9168   9105  -2753  -1005   2533       N  
ATOM   2214  CA  ARG A 435      -4.709 -12.773  28.144  1.00 74.01           C  
ANISOU 2214  CA  ARG A 435     9999   9398   8722  -2731   -677   2449       C  
ATOM   2215  C   ARG A 435      -4.623 -12.018  29.482  1.00 73.81           C  
ANISOU 2215  C   ARG A 435     9917   9704   8423  -2804   -501   2511       C  
ATOM   2216  O   ARG A 435      -5.183 -10.923  29.630  1.00 73.08           O  
ANISOU 2216  O   ARG A 435     9663   9943   8160  -2717   -234   2380       O  
ATOM   2217  CB  ARG A 435      -6.134 -13.282  27.867  1.00 75.92           C  
ANISOU 2217  CB  ARG A 435    10121   9785   8939  -2964   -685   2581       C  
ATOM   2218  CG  ARG A 435      -6.337 -13.779  26.428  1.00 75.16           C  
ANISOU 2218  CG  ARG A 435    10048   9413   9097  -2841   -808   2458       C  
ATOM   2219  CD  ARG A 435      -7.719 -14.382  26.198  1.00 77.70           C  
ANISOU 2219  CD  ARG A 435    10260   9854   9409  -3094   -851   2609       C  
ATOM   2220  NE  ARG A 435      -7.902 -15.666  26.883  1.00 81.51           N  
ANISOU 2220  NE  ARG A 435    10835  10219   9917  -3452  -1137   2935       N  
ATOM   2221  CZ  ARG A 435      -8.731 -15.869  27.908  1.00 83.82           C  
ANISOU 2221  CZ  ARG A 435    11032  10828   9989  -3802  -1101   3203       C  
ATOM   2222  NH1 ARG A 435      -9.472 -14.876  28.382  1.00 83.55           N  
ANISOU 2222  NH1 ARG A 435    10790  11266   9691  -3818   -782   3149       N  
ATOM   2223  NH2 ARG A 435      -8.823 -17.073  28.460  1.00 86.81           N  
ANISOU 2223  NH2 ARG A 435    11517  11060  10408  -4143  -1400   3523       N  
ATOM   2224  N   GLN A 436      -3.907 -12.608  30.440  1.00 74.08           N  
ANISOU 2224  N   GLN A 436    10084   9640   8421  -2949   -673   2697       N  
ATOM   2225  CA  GLN A 436      -3.635 -11.982  31.735  1.00 73.42           C  
ANISOU 2225  CA  GLN A 436     9973   9838   8086  -3006   -544   2752       C  
ATOM   2226  C   GLN A 436      -2.168 -11.545  31.904  1.00 70.44           C  
ANISOU 2226  C   GLN A 436     9728   9253   7782  -2760   -573   2608       C  
ATOM   2227  O   GLN A 436      -1.823 -10.929  32.916  1.00 70.57           O  
ANISOU 2227  O   GLN A 436     9729   9479   7606  -2761   -467   2614       O  
ATOM   2228  CB  GLN A 436      -4.022 -12.937  32.866  1.00 77.15           C  
ANISOU 2228  CB  GLN A 436    10481  10429   8403  -3409   -708   3111       C  
ATOM   2229  CG  GLN A 436      -5.517 -13.232  32.979  1.00 80.31           C  
ANISOU 2229  CG  GLN A 436    10707  11156   8650  -3704   -640   3281       C  
ATOM   2230  CD  GLN A 436      -6.197 -12.456  34.099  1.00 82.92           C  
ANISOU 2230  CD  GLN A 436    10841  12055   8610  -3835   -384   3316       C  
ATOM   2231  OE1 GLN A 436      -5.680 -12.366  35.215  1.00 84.04           O  
ANISOU 2231  OE1 GLN A 436    11028  12334   8570  -3927   -392   3424       O  
ATOM   2232  NE2 GLN A 436      -7.375 -11.910  33.809  1.00 83.36           N  
ANISOU 2232  NE2 GLN A 436    10668  12460   8546  -3840   -165   3214       N  
ATOM   2233  N   ALA A 437      -1.318 -11.863  30.921  1.00 67.33           N  
ANISOU 2233  N   ALA A 437     9449   8475   7656  -2551   -719   2468       N  
ATOM   2234  CA  ALA A 437       0.145 -11.637  31.004  1.00 64.59           C  
ANISOU 2234  CA  ALA A 437     9227   7906   7408  -2335   -790   2339       C  
ATOM   2235  C   ALA A 437       0.562 -10.171  30.845  1.00 61.00           C  
ANISOU 2235  C   ALA A 437     8687   7608   6882  -2062   -521   2083       C  
ATOM   2236  O   ALA A 437       1.637  -9.752  31.304  1.00 60.21           O  
ANISOU 2236  O   ALA A 437     8655   7448   6773  -1936   -525   2011       O  
ATOM   2237  CB  ALA A 437       0.870 -12.485  29.971  1.00 64.36           C  
ANISOU 2237  CB  ALA A 437     9315   7464   7676  -2201  -1038   2249       C  
ATOM   2238  N   LEU A 438      -0.285  -9.408  30.169  1.00 58.20           N  
ANISOU 2238  N   LEU A 438     8189   7434   6490  -1974   -314   1949       N  
ATOM   2239  CA  LEU A 438      -0.094  -7.981  30.042  1.00 54.89           C  
ANISOU 2239  CA  LEU A 438     7683   7172   5999  -1747    -83   1730       C  
ATOM   2240  C   LEU A 438      -0.298  -7.323  31.408  1.00 54.91           C  
ANISOU 2240  C   LEU A 438     7624   7494   5745  -1831     45   1782       C  
ATOM   2241  O   LEU A 438       0.415  -6.390  31.771  1.00 53.20           O  
ANISOU 2241  O   LEU A 438     7414   7318   5481  -1668    132   1649       O  
ATOM   2242  CB  LEU A 438      -1.043  -7.418  28.984  1.00 53.23           C  
ANISOU 2242  CB  LEU A 438     7343   7060   5821  -1650     63   1591       C  
ATOM   2243  CG  LEU A 438      -1.028  -5.915  28.738  1.00 50.97           C  
ANISOU 2243  CG  LEU A 438     6966   6922   5480  -1427    270   1371       C  
ATOM   2244  CD1 LEU A 438       0.359  -5.446  28.292  1.00 47.56           C  
ANISOU 2244  CD1 LEU A 438     6629   6268   5175  -1212    238   1232       C  
ATOM   2245  CD2 LEU A 438      -2.094  -5.557  27.704  1.00 48.56           C  
ANISOU 2245  CD2 LEU A 438     6541   6696   5212  -1369    368   1272       C  
ATOM   2246  N   GLY A 439      -1.255  -7.845  32.172  1.00 56.61           N  
ANISOU 2246  N   GLY A 439     7775   7946   5790  -2098     42   1979       N  
ATOM   2247  CA  GLY A 439      -1.487  -7.391  33.532  1.00 57.03           C  
ANISOU 2247  CA  GLY A 439     7755   8347   5568  -2211    146   2044       C  
ATOM   2248  C   GLY A 439      -0.271  -7.567  34.426  1.00 56.91           C  
ANISOU 2248  C   GLY A 439     7888   8208   5528  -2217     26   2117       C  
ATOM   2249  O   GLY A 439       0.077  -6.662  35.182  1.00 56.62           O  
ANISOU 2249  O   GLY A 439     7814   8356   5343  -2117    143   2013       O  
ATOM   2250  N   HIS A 440       0.379  -8.728  34.338  1.00 56.85           N  
ANISOU 2250  N   HIS A 440     8048   7877   5676  -2321   -226   2281       N  
ATOM   2251  CA  HIS A 440       1.568  -9.003  35.150  1.00 56.54           C  
ANISOU 2251  CA  HIS A 440     8160   7684   5638  -2326   -378   2355       C  
ATOM   2252  C   HIS A 440       2.705  -8.053  34.796  1.00 52.60           C  
ANISOU 2252  C   HIS A 440     7695   7043   5249  -2005   -305   2095       C  
ATOM   2253  O   HIS A 440       3.427  -7.555  35.673  1.00 51.99           O  
ANISOU 2253  O   HIS A 440     7653   7033   5067  -1953   -285   2067       O  
ATOM   2254  CB  HIS A 440       2.028 -10.458  35.012  1.00 58.33           C  
ANISOU 2254  CB  HIS A 440     8561   7552   6049  -2474   -705   2554       C  
ATOM   2255  CG  HIS A 440       3.315 -10.744  35.726  1.00 60.15           C  
ANISOU 2255  CG  HIS A 440     8952   7584   6318  -2443   -887   2600       C  
ATOM   2256  ND1 HIS A 440       3.379 -10.970  37.085  1.00 63.68           N  
ANISOU 2256  ND1 HIS A 440     9446   8198   6551  -2660   -951   2816       N  
ATOM   2257  CD2 HIS A 440       4.589 -10.812  35.272  1.00 59.55           C  
ANISOU 2257  CD2 HIS A 440     8987   7182   6458  -2218  -1016   2450       C  
ATOM   2258  CE1 HIS A 440       4.636 -11.178  37.437  1.00 64.04           C  
ANISOU 2258  CE1 HIS A 440     9639   7998   6694  -2565  -1124   2799       C  
ATOM   2259  NE2 HIS A 440       5.391 -11.088  36.354  1.00 61.76           N  
ANISOU 2259  NE2 HIS A 440     9384   7412   6669  -2294  -1165   2572       N  
ATOM   2260  N   PHE A 441       2.858  -7.803  33.500  1.00 49.35           N  
ANISOU 2260  N   PHE A 441     7265   6446   5039  -1802   -273   1911       N  
ATOM   2261  CA  PHE A 441       3.819  -6.835  33.042  1.00 45.22           C  
ANISOU 2261  CA  PHE A 441     6748   5826   4608  -1526   -191   1676       C  
ATOM   2262  C   PHE A 441       3.510  -5.468  33.669  1.00 44.46           C  
ANISOU 2262  C   PHE A 441     6538   6037   4317  -1443     32   1557       C  
ATOM   2263  O   PHE A 441       4.308  -4.946  34.460  1.00 43.43           O  
ANISOU 2263  O   PHE A 441     6449   5937   4117  -1376     39   1515       O  
ATOM   2264  CB  PHE A 441       3.811  -6.757  31.509  1.00 43.40           C  
ANISOU 2264  CB  PHE A 441     6487   5423   4580  -1361   -172   1519       C  
ATOM   2265  CG  PHE A 441       4.693  -5.679  30.966  1.00 39.89           C  
ANISOU 2265  CG  PHE A 441     6026   4923   4207  -1111    -75   1299       C  
ATOM   2266  CD1 PHE A 441       6.069  -5.848  30.923  1.00 38.63           C  
ANISOU 2266  CD1 PHE A 441     5958   4554   4165  -1002   -195   1239       C  
ATOM   2267  CD2 PHE A 441       4.150  -4.491  30.514  1.00 37.65           C  
ANISOU 2267  CD2 PHE A 441     5631   4801   3875   -995    118   1157       C  
ATOM   2268  CE1 PHE A 441       6.878  -4.851  30.444  1.00 35.30           C  
ANISOU 2268  CE1 PHE A 441     5509   4107   3795   -806   -109   1060       C  
ATOM   2269  CE2 PHE A 441       4.955  -3.489  30.027  1.00 36.39           C  
ANISOU 2269  CE2 PHE A 441     5462   4583   3780   -799    182    987       C  
ATOM   2270  CZ  PHE A 441       6.326  -3.669  29.996  1.00 37.50           C  
ANISOU 2270  CZ  PHE A 441     5688   4537   4023   -716     75    948       C  
ATOM   2271  N   LEU A 442       2.342  -4.913  33.335  1.00 43.94           N  
ANISOU 2271  N   LEU A 442     6330   6196   4171  -1441    194   1493       N  
ATOM   2272  CA  LEU A 442       1.975  -3.558  33.753  1.00 43.37           C  
ANISOU 2272  CA  LEU A 442     6136   6393   3948  -1318    381   1326       C  
ATOM   2273  C   LEU A 442       1.870  -3.371  35.269  1.00 46.01           C  
ANISOU 2273  C   LEU A 442     6437   7018   4027  -1429    416   1394       C  
ATOM   2274  O   LEU A 442       2.480  -2.460  35.811  1.00 45.31           O  
ANISOU 2274  O   LEU A 442     6351   6983   3884  -1287    463   1262       O  
ATOM   2275  CB  LEU A 442       0.684  -3.111  33.073  1.00 43.17           C  
ANISOU 2275  CB  LEU A 442     5957   6545   3899  -1293    514   1237       C  
ATOM   2276  CG  LEU A 442       0.692  -2.950  31.542  1.00 39.40           C  
ANISOU 2276  CG  LEU A 442     5487   5843   3642  -1145    515   1123       C  
ATOM   2277  CD1 LEU A 442      -0.723  -2.706  31.022  1.00 39.02           C  
ANISOU 2277  CD1 LEU A 442     5287   5990   3548  -1165    623   1074       C  
ATOM   2278  CD2 LEU A 442       1.668  -1.852  31.072  1.00 36.04           C  
ANISOU 2278  CD2 LEU A 442     5100   5270   3324   -903    542    935       C  
ATOM   2279  N   PHE A 443       1.085  -4.226  35.930  1.00 48.79           N  
ANISOU 2279  N   PHE A 443     6751   7570   4217  -1693    388   1603       N  
ATOM   2280  CA  PHE A 443       0.905  -4.186  37.378  1.00 52.03           C  
ANISOU 2280  CA  PHE A 443     7115   8310   4344  -1844    418   1699       C  
ATOM   2281  C   PHE A 443       1.644  -5.392  37.937  1.00 53.70           C  
ANISOU 2281  C   PHE A 443     7501   8327   4577  -2046    204   1961       C  
ATOM   2282  O   PHE A 443       1.389  -6.523  37.518  1.00 55.09           O  
ANISOU 2282  O   PHE A 443     7741   8334   4854  -2224     62   2154       O  
ATOM   2283  CB  PHE A 443      -0.572  -4.254  37.793  1.00 54.12           C  
ANISOU 2283  CB  PHE A 443     7185   9011   4368  -2032    540   1763       C  
ATOM   2284  CG  PHE A 443      -1.547  -3.840  36.726  1.00 53.11           C  
ANISOU 2284  CG  PHE A 443     6922   8929   4330  -1930    655   1615       C  
ATOM   2285  CD1 PHE A 443      -1.550  -2.542  36.216  1.00 51.78           C  
ANISOU 2285  CD1 PHE A 443     6678   8767   4228  -1635    773   1319       C  
ATOM   2286  CD2 PHE A 443      -2.494  -4.750  36.253  1.00 54.63           C  
ANISOU 2286  CD2 PHE A 443     7064   9156   4539  -2141    624   1781       C  
ATOM   2287  CE1 PHE A 443      -2.464  -2.160  35.221  1.00 51.61           C  
ANISOU 2287  CE1 PHE A 443     6539   8778   4292  -1542    858   1188       C  
ATOM   2288  CE2 PHE A 443      -3.415  -4.379  35.260  1.00 54.33           C  
ANISOU 2288  CE2 PHE A 443     6898   9162   4584  -2045    723   1641       C  
ATOM   2289  CZ  PHE A 443      -3.402  -3.083  34.747  1.00 51.76           C  
ANISOU 2289  CZ  PHE A 443     6503   8842   4323  -1742    841   1344       C  
ATOM   2290  N   ASN A 444       2.560  -5.143  38.866  1.00 54.40           N  
ANISOU 2290  N   ASN A 444     7668   8420   4581  -2010    158   1960       N  
ATOM   2291  CA  ASN A 444       3.533  -6.146  39.336  1.00 55.97           C  
ANISOU 2291  CA  ASN A 444     8059   8361   4846  -2135    -78   2164       C  
ATOM   2292  C   ASN A 444       4.936  -5.856  38.843  1.00 53.50           C  
ANISOU 2292  C   ASN A 444     7873   7680   4774  -1883   -163   2006       C  
ATOM   2293  O   ASN A 444       5.740  -5.304  39.583  1.00 53.34           O  
ANISOU 2293  O   ASN A 444     7891   7690   4684  -1790   -161   1935       O  
ATOM   2294  CB  ASN A 444       3.152  -7.583  38.959  1.00 57.79           C  
ANISOU 2294  CB  ASN A 444     8373   8405   5182  -2381   -274   2425       C  
ATOM   2295  CG  ASN A 444       2.653  -8.393  40.138  1.00 62.84           C  
ANISOU 2295  CG  ASN A 444     9025   9280   5572  -2737   -372   2739       C  
ATOM   2296  OD1 ASN A 444       2.306  -9.565  39.985  1.00 66.09           O  
ANISOU 2296  OD1 ASN A 444     9510   9553   6050  -2979   -561   2987       O  
ATOM   2297  ND2 ASN A 444       2.624  -7.785  41.323  1.00 66.29           N  
ANISOU 2297  ND2 ASN A 444     9392  10078   5719  -2782   -261   2737       N  
ATOM   2298  N   GLU A 445       5.226  -6.224  37.593  1.00 51.79           N  
ANISOU 2298  N   GLU A 445     7708   7142   4829  -1775   -238   1943       N  
ATOM   2299  CA  GLU A 445       6.566  -6.061  37.051  1.00 49.69           C  
ANISOU 2299  CA  GLU A 445     7539   6555   4785  -1556   -327   1798       C  
ATOM   2300  C   GLU A 445       6.884  -4.576  36.978  1.00 47.92           C  
ANISOU 2300  C   GLU A 445     7232   6444   4532  -1323   -138   1551       C  
ATOM   2301  O   GLU A 445       7.920  -4.128  37.479  1.00 47.41           O  
ANISOU 2301  O   GLU A 445     7224   6316   4474  -1216   -173   1478       O  
ATOM   2302  CB  GLU A 445       6.694  -6.762  35.691  1.00 49.51           C  
ANISOU 2302  CB  GLU A 445     7555   6231   5027  -1494   -435   1762       C  
ATOM   2303  CG  GLU A 445       8.120  -6.910  35.137  1.00 49.33           C  
ANISOU 2303  CG  GLU A 445     7624   5890   5228  -1304   -572   1634       C  
ATOM   2304  CD  GLU A 445       9.129  -7.448  36.159  1.00 53.38           C  
ANISOU 2304  CD  GLU A 445     8271   6281   5730  -1356   -771   1736       C  
ATOM   2305  OE1 GLU A 445       8.878  -8.505  36.796  1.00 56.72           O  
ANISOU 2305  OE1 GLU A 445     8785   6655   6112  -1572   -959   1964       O  
ATOM   2306  OE2 GLU A 445      10.190  -6.804  36.317  1.00 52.56           O  
ANISOU 2306  OE2 GLU A 445     8183   6125   5663  -1189   -754   1594       O  
ATOM   2307  N   CYS A 446       5.979  -3.799  36.387  1.00 46.53           N  
ANISOU 2307  N   CYS A 446     6923   6431   4327  -1250     41   1427       N  
ATOM   2308  CA  CYS A 446       6.192  -2.357  36.310  1.00 44.80           C  
ANISOU 2308  CA  CYS A 446     6630   6300   4092  -1037    183   1200       C  
ATOM   2309  C   CYS A 446       5.793  -1.625  37.589  1.00 45.77           C  
ANISOU 2309  C   CYS A 446     6676   6757   3958  -1059    279   1164       C  
ATOM   2310  O   CYS A 446       6.208  -0.487  37.802  1.00 45.60           O  
ANISOU 2310  O   CYS A 446     6625   6776   3925   -884    339    983       O  
ATOM   2311  CB  CYS A 446       5.510  -1.766  35.078  1.00 43.51           C  
ANISOU 2311  CB  CYS A 446     6370   6130   4033   -922    297   1063       C  
ATOM   2312  SG  CYS A 446       6.372  -2.181  33.562  1.00 41.42           S  
ANISOU 2312  SG  CYS A 446     6180   5499   4057   -811    203   1015       S  
ATOM   2313  N   GLY A 447       5.028  -2.300  38.447  1.00 47.64           N  
ANISOU 2313  N   GLY A 447     6879   7237   3986  -1281    275   1339       N  
ATOM   2314  CA  GLY A 447       4.513  -1.717  39.682  1.00 48.55           C  
ANISOU 2314  CA  GLY A 447     6889   7746   3812  -1326    373   1305       C  
ATOM   2315  C   GLY A 447       3.481  -0.627  39.453  1.00 48.50           C  
ANISOU 2315  C   GLY A 447     6697   8011   3721  -1196    551   1089       C  
ATOM   2316  O   GLY A 447       3.381   0.303  40.254  1.00 48.51           O  
ANISOU 2316  O   GLY A 447     6609   8266   3556  -1095    625    929       O  
ATOM   2317  N   LEU A 448       2.718  -0.734  38.357  1.00 47.45           N  
ANISOU 2317  N   LEU A 448     6501   7818   3708  -1185    600   1066       N  
ATOM   2318  CA  LEU A 448       1.629   0.212  38.077  1.00 48.16           C  
ANISOU 2318  CA  LEU A 448     6409   8158   3731  -1068    745    865       C  
ATOM   2319  C   LEU A 448       0.299  -0.333  38.631  1.00 51.27           C  
ANISOU 2319  C   LEU A 448     6646   8958   3877  -1289    826    977       C  
ATOM   2320  O   LEU A 448       0.293  -1.329  39.373  1.00 52.85           O  
ANISOU 2320  O   LEU A 448     6885   9262   3933  -1542    767   1219       O  
ATOM   2321  CB  LEU A 448       1.541   0.565  36.563  1.00 46.06           C  
ANISOU 2321  CB  LEU A 448     6153   7623   3726   -913    755    755       C  
ATOM   2322  CG  LEU A 448       2.820   0.866  35.757  1.00 43.16           C  
ANISOU 2322  CG  LEU A 448     5931   6856   3612   -753    670    697       C  
ATOM   2323  CD1 LEU A 448       2.542   1.147  34.273  1.00 41.93           C  
ANISOU 2323  CD1 LEU A 448     5759   6514   3659   -644    690    615       C  
ATOM   2324  CD2 LEU A 448       3.634   2.002  36.345  1.00 42.78           C  
ANISOU 2324  CD2 LEU A 448     5905   6801   3551   -575    662    528       C  
ATOM   2325  N   ASN A 449      -0.812   0.335  38.313  1.00 52.55           N  
ANISOU 2325  N   ASN A 449     6623   9363   3981  -1203    947    803       N  
ATOM   2326  CA  ASN A 449      -2.157  -0.139  38.697  1.00 55.48           C  
ANISOU 2326  CA  ASN A 449     6807  10149   4123  -1409   1037    887       C  
ATOM   2327  C   ASN A 449      -3.225   0.190  37.644  1.00 55.20           C  
ANISOU 2327  C   ASN A 449     6637  10150   4188  -1321   1114    754       C  
ATOM   2328  O   ASN A 449      -3.005   1.033  36.770  1.00 53.04           O  
ANISOU 2328  O   ASN A 449     6390   9643   4118  -1072   1110    555       O  
ATOM   2329  CB  ASN A 449      -2.573   0.403  40.071  1.00 58.41           C  
ANISOU 2329  CB  ASN A 449     7009  11028   4156  -1426   1127    781       C  
ATOM   2330  CG  ASN A 449      -2.767   1.912  40.072  1.00 59.17           C  
ANISOU 2330  CG  ASN A 449     6979  11251   4253  -1099   1197    401       C  
ATOM   2331  OD1 ASN A 449      -3.608   2.447  39.349  1.00 58.90           O  
ANISOU 2331  OD1 ASN A 449     6816  11273   4291   -969   1256    225       O  
ATOM   2332  ND2 ASN A 449      -1.984   2.605  40.888  1.00 60.80           N  
ANISOU 2332  ND2 ASN A 449     7226  11486   4389   -960   1168    269       N  
ATOM   2333  N   ASP A 450      -4.384  -0.462  37.752  1.00 57.35           N  
ANISOU 2333  N   ASP A 450     6757  10726   4306  -1540   1175    873       N  
ATOM   2334  CA  ASP A 450      -5.468  -0.339  36.759  1.00 57.42           C  
ANISOU 2334  CA  ASP A 450     6635  10778   4405  -1496   1237    781       C  
ATOM   2335  C   ASP A 450      -6.211   1.016  36.750  1.00 57.78           C  
ANISOU 2335  C   ASP A 450     6474  11096   4386  -1232   1343    426       C  
ATOM   2336  O   ASP A 450      -7.186   1.199  35.977  1.00 57.54           O  
ANISOU 2336  O   ASP A 450     6313  11133   4416  -1180   1391    324       O  
ATOM   2337  CB  ASP A 450      -6.466  -1.497  36.918  1.00 59.60           C  
ANISOU 2337  CB  ASP A 450     6806  11304   4537  -1835   1254   1032       C  
ATOM   2338  CG  ASP A 450      -7.390  -1.321  38.110  1.00 63.65           C  
ANISOU 2338  CG  ASP A 450     7065  12441   4677  -1971   1378    998       C  
ATOM   2339  OD1 ASP A 450      -6.930  -1.441  39.271  1.00 64.87           O  
ANISOU 2339  OD1 ASP A 450     7237  12794   4617  -2082   1370   1086       O  
ATOM   2340  OD2 ASP A 450      -8.592  -1.085  37.878  1.00 65.84           O  
ANISOU 2340  OD2 ASP A 450     7114  13035   4867  -1972   1480    879       O  
ATOM   2341  N   GLN A 451      -5.769   1.941  37.617  1.00 58.48           N  
ANISOU 2341  N   GLN A 451     6531  11334   4356  -1063   1359    230       N  
ATOM   2342  CA  GLN A 451      -6.259   3.323  37.619  1.00 58.95           C  
ANISOU 2342  CA  GLN A 451     6429  11568   4400   -763   1402   -142       C  
ATOM   2343  C   GLN A 451      -5.417   4.187  36.679  1.00 56.40           C  
ANISOU 2343  C   GLN A 451     6278  10759   4391   -490   1302   -285       C  
ATOM   2344  O   GLN A 451      -5.870   5.231  36.202  1.00 56.05           O  
ANISOU 2344  O   GLN A 451     6147  10709   4441   -247   1288   -553       O  
ATOM   2345  CB  GLN A 451      -6.198   3.920  39.028  1.00 61.42           C  
ANISOU 2345  CB  GLN A 451     6617  12286   4433   -702   1443   -307       C  
ATOM   2346  CG  GLN A 451      -6.894   3.110  40.108  1.00 64.21           C  
ANISOU 2346  CG  GLN A 451     6797  13174   4424   -999   1540   -148       C  
ATOM   2347  CD  GLN A 451      -8.402   3.168  39.998  1.00 67.29           C  
ANISOU 2347  CD  GLN A 451     6891  14016   4659  -1036   1654   -272       C  
ATOM   2348  OE1 GLN A 451      -9.007   2.430  39.219  1.00 68.71           O  
ANISOU 2348  OE1 GLN A 451     7060  14119   4929  -1201   1668   -101       O  
ATOM   2349  NE2 GLN A 451      -9.020   4.041  40.784  1.00 68.43           N  
ANISOU 2349  NE2 GLN A 451     6782  14647   4570   -877   1726   -589       N  
ATOM   2350  N   GLN A 452      -4.185   3.749  36.431  1.00 54.41           N  
ANISOU 2350  N   GLN A 452     6265  10112   4297   -538   1217   -103       N  
ATOM   2351  CA  GLN A 452      -3.256   4.490  35.585  1.00 52.39           C  
ANISOU 2351  CA  GLN A 452     6171   9420   4314   -326   1123   -198       C  
ATOM   2352  C   GLN A 452      -3.262   3.948  34.157  1.00 50.27           C  
ANISOU 2352  C   GLN A 452     5999   8822   4279   -369   1091    -69       C  
ATOM   2353  O   GLN A 452      -3.030   4.696  33.206  1.00 49.15           O  
ANISOU 2353  O   GLN A 452     5913   8425   4338   -192   1038   -186       O  
ATOM   2354  CB  GLN A 452      -1.841   4.454  36.174  1.00 51.58           C  
ANISOU 2354  CB  GLN A 452     6245   9116   4236   -326   1049   -118       C  
ATOM   2355  CG  GLN A 452      -1.737   4.959  37.619  1.00 54.99           C  
ANISOU 2355  CG  GLN A 452     6596   9868   4430   -283   1069   -243       C  
ATOM   2356  CD  GLN A 452      -0.380   4.651  38.239  1.00 56.08           C  
ANISOU 2356  CD  GLN A 452     6913   9820   4576   -337    994   -111       C  
ATOM   2357  OE1 GLN A 452      -0.084   3.501  38.582  1.00 56.68           O  
ANISOU 2357  OE1 GLN A 452     7066   9888   4580   -566    984    146       O  
ATOM   2358  NE2 GLN A 452       0.455   5.681  38.377  1.00 55.19           N  
ANISOU 2358  NE2 GLN A 452     6868   9539   4562   -127    921   -286       N  
ATOM   2359  N   VAL A 453      -3.512   2.646  34.009  1.00 50.45           N  
ANISOU 2359  N   VAL A 453     6045   8851   4274   -611   1106    175       N  
ATOM   2360  CA  VAL A 453      -3.604   2.011  32.681  1.00 49.02           C  
ANISOU 2360  CA  VAL A 453     5939   8389   4296   -660   1070    287       C  
ATOM   2361  C   VAL A 453      -4.856   1.127  32.616  1.00 50.75           C  
ANISOU 2361  C   VAL A 453     6023   8848   4411   -864   1126    405       C  
ATOM   2362  O   VAL A 453      -5.001   0.191  33.404  1.00 51.99           O  
ANISOU 2362  O   VAL A 453     6166   9174   4413  -1101   1129    599       O  
ATOM   2363  CB  VAL A 453      -2.324   1.181  32.327  1.00 47.66           C  
ANISOU 2363  CB  VAL A 453     5982   7848   4278   -736    967    476       C  
ATOM   2364  CG1 VAL A 453      -2.344   0.729  30.867  1.00 46.05           C  
ANISOU 2364  CG1 VAL A 453     5843   7365   4290   -726    922    525       C  
ATOM   2365  CG2 VAL A 453      -1.049   1.987  32.596  1.00 45.60           C  
ANISOU 2365  CG2 VAL A 453     5835   7406   4084   -573    916    380       C  
ATOM   2366  N   ALA A 454      -5.766   1.452  31.697  1.00 50.85           N  
ANISOU 2366  N   ALA A 454     5935   8879   4505   -781   1159    294       N  
ATOM   2367  CA  ALA A 454      -6.996   0.665  31.490  1.00 52.68           C  
ANISOU 2367  CA  ALA A 454     6027   9323   4663   -966   1207    392       C  
ATOM   2368  C   ALA A 454      -7.375   0.527  30.009  1.00 51.60           C  
ANISOU 2368  C   ALA A 454     5919   8944   4743   -908   1173    378       C  
ATOM   2369  O   ALA A 454      -7.596   1.520  29.308  1.00 51.08           O  
ANISOU 2369  O   ALA A 454     5819   8811   4780   -688   1176    176       O  
ATOM   2370  CB  ALA A 454      -8.171   1.243  32.309  1.00 54.96           C  
ANISOU 2370  CB  ALA A 454     6055  10114   4713   -952   1319    226       C  
TER    2371      ALA A 454                                                      
HETATM 2372  O   HOH A 501       8.224  -2.389  11.938  1.00 13.67           O  
HETATM 2373  O   HOH A 502      -0.795  -2.593  16.423  1.00 14.85           O  
HETATM 2374  O   HOH A 503      -0.701  -5.015  17.645  1.00 14.88           O  
HETATM 2375  O   HOH A 504       9.709   7.519  22.026  1.00 15.89           O  
HETATM 2376  O   HOH A 505      15.616  -5.103  32.942  1.00 19.91           O  
HETATM 2377  O   HOH A 506      16.998   7.605  36.690  1.00 15.62           O  
HETATM 2378  O   HOH A 507     -17.178  13.222  10.466  1.00 15.48           O  
HETATM 2379  O   HOH A 508     -10.304  -7.577  -1.359  1.00 31.61           O  
HETATM 2380  O   HOH A 509      10.514  -8.655  12.532  1.00  9.03           O  
HETATM 2381  O   HOH A 510       3.060  10.714  23.680  1.00 26.84           O  
HETATM 2382  O   HOH A 511      -2.712   1.043  17.797  1.00 21.20           O  
HETATM 2383  O   HOH A 512      18.286  15.200  35.858  1.00 11.94           O  
HETATM 2384  O   HOH A 513       1.536   9.528  18.167  1.00 23.15           O  
HETATM 2385  O   HOH A 514      -0.775  -9.648  25.284  1.00 27.01           O  
HETATM 2386  O   HOH A 515      -0.804   5.573   1.504  1.00 25.63           O  
HETATM 2387  O   HOH A 516     -27.014   9.623  12.817  1.00 16.12           O  
HETATM 2388  O   HOH A 517      23.171   2.778  26.204  1.00 30.89           O  
HETATM 2389  O   HOH A 518      17.718  16.010  28.482  1.00 19.59           O  
HETATM 2390  O   HOH A 519      13.251  11.037  39.160  1.00 22.71           O  
HETATM 2391  O   HOH A 520      -6.011   3.832  16.925  1.00 25.86           O  
HETATM 2392  O   HOH A 521       9.071   7.408  19.305  1.00 22.92           O  
HETATM 2393  O   HOH A 522     -20.045   8.711  11.297  1.00 23.96           O  
HETATM 2394  O   HOH A 523      18.228  -3.026  19.417  1.00 23.27           O  
HETATM 2395  O   HOH A 524       4.512  10.330  18.382  1.00 39.68           O  
HETATM 2396  O   HOH A 525     -23.180   8.321   2.716  1.00 18.38           O  
HETATM 2397  O   HOH A 526      23.525   5.321  25.064  1.00 16.81           O  
HETATM 2398  O   HOH A 527      16.944  19.677  34.923  1.00 12.45           O  
HETATM 2399  O   HOH A 528     -10.216  13.778   0.548  1.00 26.58           O  
HETATM 2400  O   HOH A 529       0.908  12.638  11.419  1.00 24.84           O  
HETATM 2401  O   HOH A 530      11.035  -0.681  33.544  1.00 22.14           O  
HETATM 2402  O   HOH A 531     -22.159  12.921   5.700  1.00 20.61           O  
HETATM 2403  O   HOH A 532      13.103  19.402  27.843  1.00 20.75           O  
HETATM 2404  O   HOH A 533      -4.463  -5.611  -2.285  1.00 37.66           O  
HETATM 2405  O   HOH A 534       7.106  -5.487  18.085  1.00 24.69           O  
HETATM 2406  O   HOH A 535       6.344  13.273  23.937  1.00 42.82           O  
HETATM 2407  O   HOH A 536      18.948  -3.652  29.686  1.00 32.19           O  
HETATM 2408  O   HOH A 537     -13.010 -16.279   2.007  1.00 20.32           O  
HETATM 2409  O   HOH A 538      22.871   5.472  38.281  1.00 32.60           O  
HETATM 2410  O   HOH A 539       6.414  12.202  13.062  1.00 33.80           O  
HETATM 2411  O   HOH A 540      12.261   8.241  39.608  1.00 24.09           O  
HETATM 2412  O   HOH A 541      17.396  -2.796  31.710  1.00 34.70           O  
HETATM 2413  O   HOH A 542       1.071  10.862  30.665  1.00 20.86           O  
HETATM 2414  O   HOH A 543      -4.429   4.849  14.854  1.00 36.61           O  
HETATM 2415  O   HOH A 544      -4.861  10.200  17.113  1.00 27.69           O  
HETATM 2416  O   HOH A 545      16.860  17.316  38.154  1.00 19.99           O  
HETATM 2417  O   HOH A 546     -15.558   7.316  -9.161  1.00 17.73           O  
HETATM 2418  O   HOH A 547     -14.072  -8.464  -9.985  1.00 32.69           O  
HETATM 2419  O   HOH A 548       1.578  16.744  14.571  1.00 35.95           O  
HETATM 2420  O   HOH A 549       0.811  12.101  18.451  1.00 40.98           O  
HETATM 2421  O   HOH A 550       4.376  11.896  16.339  1.00 33.54           O  
HETATM 2422  O   HOH A 551      11.245  11.635  41.163  1.00 36.86           O  
HETATM 2423  O   HOH A 552       3.530  -3.377   1.321  1.00 36.79           O  
HETATM 2424  O   HOH A 553      -4.260  13.015  17.377  1.00 33.17           O  
HETATM 2425  O   HOH A 554       5.791   7.581  43.570  1.00 84.25           O  
HETATM 2426  O   HOH A 555      -9.987  10.556  17.753  1.00 33.44           O  
HETATM 2427  O   HOH A 556       5.986  13.156  34.291  1.00 63.65           O  
HETATM 2428  O   HOH A 557       0.985   8.330  38.029  1.00 12.27           O  
HETATM 2429  O   HOH A 558      -7.882  -3.942  14.628  1.00 27.41           O  
HETATM 2430  O   HOH A 559     -20.824 -10.354 -13.282  1.00 29.33           O  
HETATM 2431  O   HOH A 560     -29.576  -0.720   1.880  1.00 31.88           O  
HETATM 2432  O   HOH A 561       0.912  -6.015   2.055  1.00 41.07           O  
HETATM 2433  O   HOH A 562     -23.580 -11.904 -14.256  1.00 32.01           O  
HETATM 2434  O   HOH A 563       5.658  -6.140   7.978  1.00 39.24           O  
HETATM 2435  O   HOH A 564      22.120  -0.348  20.139  1.00 24.18           O  
HETATM 2436  O   HOH A 565       6.088  10.292  37.364  1.00 29.88           O  
HETATM 2437  O   HOH A 566      24.480  10.473  16.824  1.00 30.04           O  
HETATM 2438  O   HOH A 567       0.702  -6.215   4.582  1.00 35.54           O  
HETATM 2439  O   HOH A 568      -9.250  12.951  18.421  1.00 29.76           O  
HETATM 2440  O   HOH A 569     -13.282  15.729  14.500  1.00 46.18           O  
HETATM 2441  O   HOH A 570     -20.224  -7.723  -8.178  1.00 30.70           O  
HETATM 2442  O   HOH A 571       7.145  10.585  35.173  1.00 27.59           O  
HETATM 2443  O   HOH A 572     -29.618  -2.642   3.579  1.00 25.45           O  
HETATM 2444  O   HOH A 573      -7.375 -11.642 -11.213  1.00 10.25           O  
HETATM 2445  O   HOH A 574      -2.954  -8.777   7.434  1.00 42.06           O  
HETATM 2446  O   HOH A 575     -22.550   7.625  15.943  1.00 33.42           O  
HETATM 2447  O   HOH A 576     -27.493 -15.306 -10.339  1.00 26.32           O  
HETATM 2448  O   HOH A 577     -26.006  -2.333  -3.006  1.00 29.04           O  
HETATM 2449  O   HOH A 578       7.912   2.078  15.332  1.00 40.30           O  
HETATM 2450  O   HOH A 579      18.592  -0.674  14.386  1.00 34.23           O  
HETATM 2451  O   HOH A 580       6.075   5.243  47.116  1.00 28.88           O  
HETATM 2452  O   HOH A 581     -12.735  19.486  12.055  1.00 27.69           O  
HETATM 2453  O   HOH A 582     -16.209 -17.742  -0.356  1.00 26.88           O  
HETATM 2454  O   HOH A 583       8.234  -1.834  16.367  1.00 32.61           O  
HETATM 2455  O   HOH A 584     -13.524  -1.206  11.450  1.00 18.24           O  
HETATM 2456  O   HOH A 585      -4.865  -8.413  -5.057  1.00 27.66           O  
HETATM 2457  O   HOH A 586       6.622  14.712  12.510  1.00 31.74           O  
MASTER      285    0    0   13    9    0    0    6 2456    1    0   24          
END                                                                             


A second structure was input as follows:


HEADER    SIGNALING PROTEIN                       24-APR-12   4ETZ              
TITLE     CRYSTAL STRUCTURE OF PELD 158-CT FROM PSEUDOMONAS AERUGINOSA PAO1     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PELD;                                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 158-454;                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 GENE: PA3061, PELD;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA(DE3);                         
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    C-DI-GMP, SIGNALING PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.LI,J.CHEN,S.K.NAIR                                                  
REVDAT   2   19-SEP-12 4ETZ    1       JRNL                                     
REVDAT   1   25-JUL-12 4ETZ    0                                                
JRNL        AUTH   Z.LI,J.H.CHEN,Y.HAO,S.K.NAIR                                 
JRNL        TITL   STRUCTURES OF THE PELD CYCLIC DIGUANYLATE EFFECTOR INVOLVED  
JRNL        TITL 2 IN PELLICLE FORMATION IN PSEUDOMONAS AERUGINOSA PAO1.        
JRNL        REF    J.BIOL.CHEM.                  V. 287 30191 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22810222                                                     
JRNL        DOI    10.1074/JBC.M112.378273                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 40287                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2015                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2768                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 146                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4536                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 140                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.43000                                             
REMARK   3    B22 (A**2) : -0.74000                                             
REMARK   3    B33 (A**2) : 3.19000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.11000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.240         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.204         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.173         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.433        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4698 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6374 ; 1.510 ; 2.027       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   570 ; 6.333 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   238 ;35.673 ;23.025       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   812 ;19.294 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    62 ;17.493 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   730 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3558 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2846 ; 0.776 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4526 ; 1.444 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1852 ; 1.991 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1848 ; 3.250 ; 4.500       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   158        A   454                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0717  -0.1407  11.8160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1487 T22:   0.1153                                     
REMARK   3      T33:   0.0744 T12:   0.0113                                     
REMARK   3      T13:   0.0248 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8542 L22:   0.9682                                     
REMARK   3      L33:   0.9988 L12:   0.9181                                     
REMARK   3      L13:   1.8891 L23:   0.3018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0328 S12:  -0.4447 S13:   0.1649                       
REMARK   3      S21:   0.0803 S22:  -0.0202 S23:   0.1740                       
REMARK   3      S31:  -0.0538 S32:   0.0263 S33:   0.0530                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   158        B   454                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3539 -18.7671  43.3493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2761 T22:   0.2749                                     
REMARK   3      T33:   0.1153 T12:   0.0001                                     
REMARK   3      T13:  -0.0316 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1765 L22:   1.1428                                     
REMARK   3      L33:   0.9412 L12:  -0.6552                                     
REMARK   3      L13:  -2.4005 L23:   0.2554                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0389 S12:   0.3908 S13:   0.0036                       
REMARK   3      S21:  -0.1061 S22:  -0.0501 S23:   0.2856                       
REMARK   3      S31:   0.0139 S32:   0.0321 S33:   0.0112                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 4ETZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072066.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40304                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.6800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.89700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.310                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS, PH 8.5, 200 MM LI2SO4,      
REMARK 280  AND 1.26 M (NH4)2SO4, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       20.65500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLU A   248                                                      
REMARK 465     LEU A   249                                                      
REMARK 465     LEU A   250                                                      
REMARK 465     GLU A   251                                                      
REMARK 465     ARG A   252                                                      
REMARK 465     GLY A   253                                                      
REMARK 465     GLU A   254                                                      
REMARK 465     GLN A   255                                                      
REMARK 465     ARG A   256                                                      
REMARK 465     ALA A   257                                                      
REMARK 465     HIS A   258                                                      
REMARK 465     SER A   259                                                      
REMARK 465     ARG B   252                                                      
REMARK 465     GLY B   253                                                      
REMARK 465     GLU B   254                                                      
REMARK 465     GLN B   255                                                      
REMARK 465     ARG B   256                                                      
REMARK 465     ALA B   257                                                      
REMARK 465     HIS B   258                                                      
REMARK 465     SER B   259                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA B   228     O    HOH B   626              2.17            
REMARK 500   NH1  ARG A   246     OE2  GLU A   290              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 369   CB  -  CG  -  CD1 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    GLY A 395   C   -  N   -  CA  ANGL. DEV. = -13.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 227       88.91    -66.44                                   
REMARK 500    ARG A 246      170.75    -50.29                                   
REMARK 500    SER A 309     -127.62    -81.19                                   
REMARK 500    ASP A 310      -43.73    -24.10                                   
REMARK 500    LEU A 316       25.93    -69.29                                   
REMARK 500    ARG A 435      -90.53     10.78                                   
REMARK 500    GLN A 436       31.83    -91.75                                   
REMARK 500    GLU A 445      -68.93   -157.03                                   
REMARK 500    ALA B 228      -81.17    -29.65                                   
REMARK 500    ARG B 246     -163.06    -71.61                                   
REMARK 500    GLN B 247       49.98     33.53                                   
REMARK 500    GLU B 248      110.86     61.13                                   
REMARK 500    ASP B 310     -144.87    -88.75                                   
REMARK 500    ARG B 311      -28.64     54.40                                   
REMARK 500    ARG B 312       80.48    -44.90                                   
REMARK 500    PHE B 411     -167.02   -108.28                                   
REMARK 500    ALA B 431      -84.90     21.32                                   
REMARK 500    ASP B 434     -179.09    -61.17                                   
REMARK 500    ARG B 435      -76.39    -57.52                                   
REMARK 500    GLU B 445      -44.45   -133.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA



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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.