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***  135  ***

elNémo ID: 20102210243975480

Job options:

ID        	=	 20102210243975480
JOBID     	=	 135
USERID    	=	 daisuke
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 135

REMARK Date 2019-03-04 Time 14:06:16 JST +0900 (1551675976.22 s)
REMARK PHENIX refinement
REMARK 
REMARK ****************** INPUT FILES AND LABELS ******************************
REMARK Reflections:
REMARK   file name      : /Users/yuyataguchi/Desktop/190202_1756_all/ccp4i2_2/CCP4_JOBS/job_21/Reindexed.mtz
REMARK   labels         : ['F,SIGF']
REMARK R-free flags:
REMARK   file name      : /Users/yuyataguchi/Desktop/190202_1756_all/ccp4i2_2/CCP4_JOBS/job_21/Reindexed.mtz
REMARK   label          : FREER
REMARK   test_flag_value: 0
REMARK Model file name(s): 
REMARK   /Users/yuyataguchi/Desktop/190202_1756_all/phenix/Refine_133/190202_group2_all_refine_133_2.pdb
REMARK 
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS *******************
REMARK Start: r_work = 0.2030 r_free = 0.2536 bonds = 0.004 angles = 0.659
REMARK Final: r_work = 0.2011 r_free = 0.2528 bonds = 0.003 angles = 0.630
REMARK ************************************************************************
REMARK 
REMARK ****************** REFINEMENT STATISTICS STEP BY STEP ******************
REMARK leading digit, like 1_, means number of macro-cycle                     
REMARK 0    : statistics at the very beginning when nothing is done yet        
REMARK 1_bss: bulk solvent correction and/or (anisotropic) scaling             
REMARK 1_xyz: refinement of coordinates                                        
REMARK 1_adp: refinement of ADPs (Atomic Displacement Parameters)              
REMARK 1_occ: refinement of occupancies                                        
REMARK ------------------------------------------------------------------------
REMARK  stage       r-work r-free bonds angles b_min b_max b_ave n_water shift
REMARK       0    : 0.3823 0.4399 0.004  0.66  21.2 135.2  53.4  60      0.000
REMARK       1_bss: 0.2030 0.2536 0.004  0.66  20.9 134.9  53.1  60      0.000
REMARK 1_settarget: 0.2030 0.2536 0.004  0.66  20.9 134.9  53.1  60      0.000
REMARK       1_nqh: 0.2030 0.2536 0.004  0.66  20.9 134.9  53.1  60      0.000
REMARK    1_weight: 0.2030 0.2536 0.004  0.66  20.9 134.9  53.1  60      0.000
REMARK    1_xyzrec: 0.2049 0.2547 0.003  0.61  20.9 134.9  53.1  60      0.024
REMARK       1_adp: 0.2068 0.2565 0.003  0.61  23.5 139.6  54.5  60      0.024
REMARK       2_bss: 0.2067 0.2567 0.003  0.61  23.4 139.4  54.4  60      0.024
REMARK 2_settarget: 0.2067 0.2567 0.003  0.61  23.4 139.4  54.4  60      0.024
REMARK 2_updatecdl: 0.2067 0.2567 0.003  0.62  23.4 139.4  54.4  60      0.024
REMARK       2_nqh: 0.2067 0.2567 0.003  0.62  23.4 139.4  54.4  60      0.024
REMARK   2_realsrl: 0.2077 0.2554 0.003  0.70  23.4 139.4  54.4  60      0.038
REMARK    2_weight: 0.2077 0.2554 0.003  0.70  23.4 139.4  54.4  60      0.038
REMARK    2_xyzrec: 0.2068 0.2551 0.003  0.60  23.4 139.4  54.4  60      0.038
REMARK  2_realsrl2: 0.2069 0.2548 0.003  0.60  23.4 139.4  54.4  60      0.039
REMARK       2_adp: 0.2035 0.2522 0.003  0.60  19.6 159.7  55.5  60      0.039
REMARK       3_bss: 0.2032 0.2518 0.003  0.60  19.1 159.2  55.1  60      0.039
REMARK 3_settarget: 0.2032 0.2518 0.003  0.60  19.1 159.2  55.1  60      0.039
REMARK 3_updatecdl: 0.2032 0.2518 0.003  0.61  19.1 159.2  55.1  60      0.039
REMARK     3_setrh: 0.2032 0.2518 0.003  0.61  19.1 159.2  55.1  60      0.039
REMARK       3_nqh: 0.2032 0.2518 0.003  0.61  19.1 159.2  55.1  60      0.038
REMARK   3_realsrl: 0.2034 0.2530 0.003  0.62  19.1 159.2  55.1  60      0.045
REMARK    3_weight: 0.2034 0.2530 0.003  0.62  19.1 159.2  55.1  60      0.045
REMARK    3_xyzrec: 0.2012 0.2533 0.003  0.63  19.1 159.2  55.1  60      0.046
REMARK  3_realsrl2: 0.2012 0.2533 0.003  0.63  19.1 159.2  55.1  60      0.046
REMARK       3_adp: 0.2010 0.2528 0.003  0.63  18.6 160.7  55.9  60      0.046
REMARK         end: 0.2011 0.2528 0.003  0.63  18.1 160.1  55.3  60      0.046
REMARK ------------------------------------------------------------------------
REMARK MODEL CONTENT.
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM
REMARK        C                     4833         4833.00
REMARK       Mn                        1            1.00
REMARK        O                     1324         1324.00
REMARK        N                     1126         1126.00
REMARK        P                        1            1.00
REMARK        S                       18           18.00
REMARK      O1-                        1            1.00
REMARK    TOTAL                     7304         7304.00

REMARK -----------------------------------------------------------------------
REMARK r_free_flags.md5.hexdigest 303718ae9c8d501bafe2f7ea374b5211
REMARK 
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty,
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini,
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart
REMARK   3
REMARK   3  X-RAY DATA.
REMARK   3  
REMARK   3  REFINEMENT TARGET : ML
REMARK   3  
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.600   
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.837  
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.94 
REMARK   3   NUMBER OF REFLECTIONS             : 34217     
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 34217     
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2035
REMARK   3   R VALUE            (WORKING SET) : 0.2011
REMARK   3   FREE R VALUE                     : 0.2528
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.73  
REMARK   3   FREE R VALUE TEST SET COUNT      : 1617      
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWORK CCFREE
REMARK   3     1 24.8380 -  5.9277    1.00     2931   159  0.2022 0.2062   0.913  0.894
REMARK   3     2  5.9277 -  4.7156    1.00     2770   152  0.1949 0.2406   0.921  0.863
REMARK   3     3  4.7156 -  4.1226    1.00     2744   128  0.1673 0.2283   0.937  0.898
REMARK   3     4  4.1226 -  3.7470    1.00     2677   154  0.1741 0.2314   0.929  0.879
REMARK   3     5  3.7470 -  3.4792    1.00     2705   129  0.1937 0.2762   0.917  0.837
REMARK   3     6  3.4792 -  3.2746    1.00     2733   138  0.2004 0.2637   0.912  0.878
REMARK   3     7  3.2746 -  3.1109    1.00     2691   126  0.2091 0.2890   0.901  0.800
REMARK   3     8  3.1109 -  2.9757    1.00     2684   102  0.2216 0.2834   0.892  0.834
REMARK   3     9  2.9757 -  2.8613    1.00     2637   135  0.2332 0.3182   0.899  0.821
REMARK   3    10  2.8613 -  2.7627    1.00     2663   139  0.2344 0.2937   0.893  0.849
REMARK   3    11  2.7627 -  2.6764    1.00     2692   127  0.2574 0.3050   0.863  0.803
REMARK   3    12  2.6764 -  2.6000    1.00     2673   128  0.2814 0.3175   0.842  0.694
REMARK   3  
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11    
REMARK   3   SHRINKAGE RADIUS   : 0.90    
REMARK   3   GRID STEP FACTOR   : 4.00    
REMARK   3  
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.29    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.81   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  
REMARK   3  
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND      :  0.003   0.037   7463
REMARK   3    ANGLE     :  0.630  11.924  10135
REMARK   3    CHIRALITY :  0.044   0.143   1084
REMARK   3    PLANARITY :  0.005   0.060   1257
REMARK   3    DIHEDRAL  :  8.580 160.868   4262
REMARK   3    MIN NONBONDED DISTANCE : 2.091 
REMARK   3  REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3    ALL-ATOM CLASHSCORE : 5.47
REMARK   3    RAMACHANDRAN PLOT:
REMARK   3      OUTLIERS : 0.80  %
REMARK   3      ALLOWED  : 4.02  %
REMARK   3      FAVORED  : 95.18 %
REMARK   3    ROTAMER OUTLIERS : 0.14 %
REMARK   3    CBETA DEVIATIONS : 0
REMARK   3    PEPTIDE PLANE:
REMARK   3      CIS-PROLINE     : 4.6511627907
REMARK   3      CIS-GENERAL     : 0.120048019208
REMARK   3      TWISTED PROLINE : 0.0
REMARK   3      TWISTED GENERAL : 0.0
REMARK   3  
REMARK   3  ATOMIC DISPLACEMENT PARAMETERS.
REMARK   3   WILSON B : 44.56
REMARK   3   RMS(B_ISO_OR_EQUIVALENT_BONDED) : 4.64
REMARK   3   ATOMS          NUMBER OF ATOMS
REMARK   3                    ISO.  ANISO. 
REMARK   3    ALL         :   7304    7059
REMARK   3    ALL (NO H)  :   7304    7059
REMARK   3    SOLVENT     :     60       0
REMARK   3    NON-SOLVENT :   7244    7059
REMARK   3    HYDROGENS   :      0       0
REMARK   3  
REMARK   3  
REMARK   3  TLS DETAILS.
REMARK   3   NUMBER OF TLS GROUPS: 3     
REMARK   3   ORIGIN: CENTER OF MASS
REMARK   3   TLS GROUP : 1     
REMARK   3    SELECTION: chain 'A' and (resid 5 through 494 )
REMARK   3    ORIGIN FOR THE GROUP (A): -28.2635   7.2176  16.2129
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2819 T22:   0.2600                       
REMARK   3      T33:   0.3096 T12:  -0.0127                       
REMARK   3      T13:   0.0061 T23:  -0.0874                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   2.3180 L22:   1.1080                       
REMARK   3      L33:   1.1453 L12:  -0.3981                       
REMARK   3      L13:  -0.3862 L23:  -0.0998                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.1065 S12:   0.2558 S13:  -0.1840         
REMARK   3      S21:  -0.1567 S22:   0.0659 S23:  -0.1661         
REMARK   3      S31:   0.2117 S32:   0.0417 S33:   0.0163         
REMARK   3   TLS GROUP : 2     
REMARK   3    SELECTION: chain 'A' and (resid 495 through 872 )
REMARK   3    ORIGIN FOR THE GROUP (A): -73.0490  10.0483  14.2965
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.3154 T22:   0.2505                       
REMARK   3      T33:   0.4148 T12:  -0.0194                       
REMARK   3      T13:   0.0111 T23:   0.0413                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   1.1487 L22:   0.4288                       
REMARK   3      L33:   1.2565 L12:  -0.0017                       
REMARK   3      L13:   0.4100 L23:   0.2194                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0250 S12:  -0.0031 S13:  -0.1693         
REMARK   3      S21:  -0.0054 S22:   0.1066 S23:   0.0930         
REMARK   3      S31:   0.1629 S32:  -0.0519 S33:  -0.0654         
REMARK   3   TLS GROUP : 3     
REMARK   3    SELECTION: chain 'B' and (resid 2 through 11 )
REMARK   3    ORIGIN FOR THE GROUP (A): -52.7658   8.8076   9.1506
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.7872 T22:   0.9103                       
REMARK   3      T33:   0.8497 T12:   0.0369                       
REMARK   3      T13:   0.1032 T23:   0.2041                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   0.0058 L22:   4.1608                       
REMARK   3      L33:   0.0167 L12:  -0.1079                       
REMARK   3      L13:  -0.0095 L23:   0.2277                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0260 S12:   0.8096 S13:   0.2747         
REMARK   3      S21:  -0.7478 S22:   0.0830 S23:   0.3980         
REMARK   3      S31:   0.1378 S32:  -0.1893 S33:  -0.0365         

REMARK   3
HELIX    1   1 TRP A   12  ARG A   28  1                                  17
HELIX    2   2 TRP A   33  VAL A   36  1                                   4
HELIX    3   3 ASP A   47  HIS A   60  1                                  14
HELIX    4   4 PRO A   84  ILE A   96  1                                  13
HELIX    5   5 GLY A  102  VAL A  131  1                                  30
HELIX    6   6 LYS A  134  ALA A  145  1                                  12
HELIX    7   7 GLY A  149  ARG A  154  1                                   6
HELIX    8   8 HIS A  163  TRP A  184  1                                  22
HELIX    9   9 LEU A  189  ASN A  192  1                                   4
HELIX   10  10 ALA A  195  SER A  214  1                                  20
HELIX   11  11 GLY A  216  VAL A  234  5                                  19
HELIX   12  12 ARG A  243  PHE A  264  1                                  22
HELIX   13  13 PRO A  278  VAL A  303  1                                  26
HELIX   14  14 PHE A  305  ARG A  308  1                                   4
HELIX   15  15 ARG A  313  PHE A  331  5                                  19
HELIX   16  16 SER A  335  ARG A  347  1                                  13
HELIX   17  17 GLY A  353  LEU A  356  1                                   4
HELIX   18  18 THR A  375  ARG A  402  1                                  28
HELIX   19  19 PHE A  405  GLY A  423  1                                  19
HELIX   20  20 ASN A  425  LYS A  449  5                                  25
HELIX   21  21 LEU A  452  ALA A  459  1                                   8
HELIX   22  22 TYR A  468  SER A  494  1                                  27
HELIX   23  23 LYS A  501  ASN A  513  1                                  13
HELIX   24  24 GLY A  517  LEU A  525  1                                   9
HELIX   25  25 TRP A  551  ALA A  559  5                                   9
HELIX   26  26 ALA A  584  PHE A  588  1                                   5
HELIX   27  27 GLU A  593  LYS A  602  1                                  10
HELIX   28  28 ILE A  612  GLU A  615  1                                   4
HELIX   29  29 TYR A  619  GLU A  627  1                                   9
HELIX   30  30 PRO A  631  TYR A  636  5                                   6
HELIX   31  31 GLN A  655  ASP A  657  5                                   3
HELIX   32  32 TYR A  674  SER A  676  5                                   3
HELIX   33  33 MET A  678  HIS A  683  1                                   6
HELIX   34  34 ALA A  703  SER A  710  1                                   8
HELIX   35  35 GLU A  717  ALA A  732  1                                  16
HELIX   36  36 MET A  740  LEU A  754  1                                  15
HELIX   37  37 GLU A  756  MET A  759  1                                   4
HELIX   38  38 GLU A  855  ASN A  860  1                                   6
SHEET    1   A 4 GLY A 546  ILE A 548  0
SHEET    2   A 4 VAL A 605  ASP A 611  1  N  LYS A 606   O  GLY A 546
SHEET    3   A 4 VAL A 771  ARG A 776 -1  N  PHE A 774   O  VAL A 608
SHEET    4   A 4 TYR A 693  GLU A 698 -1  N  TYR A 697   O  ILE A 773
SHEET    1   B 2 TYR A 640  TYR A 643  0
SHEET    2   B 2 PHE A 649  ALA A 652 -1  N  ALA A 652   O  TYR A 640
SHEET    1   C 3 THR A 819  LEU A 824  0
SHEET    2   C 3 ALA A 780  LYS A 785 -1  N  GLY A 784   O  TYR A 820
SHEET    3   C 3 ILE A 863  GLN A 865  1  N  ILE A 864   O  VAL A 781
SHEET    1   D 4 THR A 806  GLU A 814  0
SHEET    2   D 4 GLU A 792  LYS A 800 -1  N  ILE A 799   O  PHE A 807
SHEET    3   D 4 TYR A 840  ALA A 844 -1  N  LYS A 843   O  SER A 794
SHEET    4   D 4 VAL A 847  ILE A 851 -1  N  ILE A 851   O  TYR A 840
SSBOND   1 CYS A  617    CYS B   10 
CRYST1  345.740   48.690   63.560  90.00  90.00  90.00 P 21 21 2
SCALE1      0.002892  0.000000  0.000000        0.00000
SCALE2      0.000000  0.020538  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015733        0.00000
HETATM    1  C1  PEG E   1     -81.116   0.140  15.194  1.00 58.65           C
HETATM    2  C2  PEG E   1     -80.624  -0.522  13.908  1.00 56.74           C
HETATM    3  C3  PEG E   1     -80.269  -0.047  11.636  1.00 57.60           C
HETATM    4  C4  PEG E   1     -80.589   0.969  10.537  1.00 58.68           C
HETATM    5  O1  PEG E   1     -80.158  -0.045  16.200  1.00 53.58           O
HETATM    6  O2  PEG E   1     -81.024   0.217  12.786  1.00 58.38           O
HETATM    7  O4  PEG E   1     -81.046   2.176  11.090  1.00 58.15           O
HETATM    8  C1  PEG E   2     -22.988  16.078  18.253  1.00 69.62           C
HETATM    9  C2  PEG E   2     -22.986  17.166  19.325  1.00 68.35           C
HETATM   10  C3  PEG E   2     -23.064  16.441  21.567  1.00 66.27           C
HETATM   11  C4  PEG E   2     -22.178  16.435  22.812  1.00 66.72           C
HETATM   12  O1  PEG E   2     -21.691  15.570  18.100  1.00 66.38           O
HETATM   13  O2  PEG E   2     -22.277  16.701  20.438  1.00 67.11           O
HETATM   14  O4  PEG E   2     -22.802  17.129  23.859  1.00 65.25           O
HETATM   15  C1  PEG E   3     -15.717  25.132  13.072  1.00110.68           C
HETATM   16  C2  PEG E   3     -16.404  23.768  12.997  1.00108.30           C
HETATM   17  C3  PEG E   3     -17.892  23.613  14.809  1.00 97.18           C
HETATM   18  C4  PEG E   3     -18.370  22.178  15.021  1.00 90.96           C
HETATM   19  O1  PEG E   3     -16.137  25.933  12.001  1.00111.16           O
HETATM   20  O2  PEG E   3     -17.729  23.868  13.442  1.00103.15           O
HETATM   21  O4  PEG E   3     -18.691  21.986  16.372  1.00 86.75           O
HETATM   22  C1  PEG E   4     -65.800  25.577  10.046  1.00 97.27           C
HETATM   23  C2  PEG E   4     -67.293  25.691  10.351  1.00101.62           C
HETATM   24  C3  PEG E   4     -68.508  27.241   9.073  1.00107.48           C
HETATM   25  C4  PEG E   4     -67.670  27.807   7.929  1.00108.34           C
HETATM   26  O1  PEG E   4     -65.390  24.247  10.202  1.00 92.99           O
HETATM   27  O2  PEG E   4     -67.704  27.020  10.196  1.00105.55           O
HETATM   28  O4  PEG E   4     -68.287  27.497   6.710  1.00109.21           O
HETATM   29  C1  PEG E   5     -64.981  29.870  10.686  1.00 90.01           C
HETATM   30  C2  PEG E   5     -65.809  30.481   9.558  1.00 94.55           C
HETATM   31  C3  PEG E   5     -68.001  31.197   9.993  1.00100.90           C
HETATM   32  C4  PEG E   5     -68.656  31.982   8.855  1.00102.85           C
HETATM   33  O1  PEG E   5     -65.622  28.722  11.171  1.00 81.70           O
HETATM   34  O2  PEG E   5     -66.634  31.492  10.064  1.00 97.87           O
HETATM   35  O4  PEG E   5     -67.691  32.394   7.925  1.00103.04           O
HETATM   36  C01 7MG E   6     -26.366  16.304  36.548  1.00 74.09           C
HETATM   37  C02 7MG E   6     -27.340  15.820  35.473  1.00 75.60           C
HETATM   38  C03 7MG E   6     -28.448  16.830  35.171  1.00 72.10           C
HETATM   39  C04 7MG E   6     -29.035  16.654  33.771  1.00 66.44           C
HETATM   40  C05 7MG E   6     -30.098  17.705  33.453  1.00 66.13           C
HETATM   41  C06 7MG E   6     -30.455  17.761  31.967  1.00 67.96           C
HETATM   42  C07 7MG E   6     -31.964  17.963  31.809  1.00 68.44           C
HETATM   43  C08 7MG E   6     -32.472  18.447  30.693  1.00 66.98           C
HETATM   44  C09 7MG E   6     -31.555  18.815  29.530  1.00 69.89           C
HETATM   45  C10 7MG E   6     -32.237  19.842  28.627  1.00 72.27           C
HETATM   46  C11 7MG E   6     -31.321  21.032  28.351  1.00 73.24           C
HETATM   47  C12 7MG E   6     -30.828  21.062  26.907  1.00 78.47           C
HETATM   48  C13 7MG E   6     -29.361  20.643  26.802  1.00 88.47           C
HETATM   49  C14 7MG E   6     -28.577  21.513  25.821  1.00 93.47           C
HETATM   50  C17 7MG E   6     -28.240  20.459  23.758  1.00 85.10           C
HETATM   51  C18 7MG E   6     -27.774  21.329  22.592  1.00 81.86           C
HETATM   52  C20 7MG E   6     -28.896  22.284  22.188  1.00 80.34           C
HETATM   53  O15 7MG E   6     -28.764  22.685  25.802  1.00 96.19           O
HETATM   54  O16 7MG E   6     -27.654  20.936  24.937  1.00 89.06           O
HETATM   55  O19 7MG E   6     -27.442  20.515  21.503  1.00 80.33           O
HETATM   56  O21 7MG E   6     -29.834  21.569  21.430  1.00 77.93           O
HETATM   57  C01 7MG E   7     -34.317  27.397  19.354  1.00 53.46           C
HETATM   58  C02 7MG E   7     -35.807  27.731  19.271  1.00 54.06           C
HETATM   59  C03 7MG E   7     -36.238  28.201  17.884  1.00 52.34           C
HETATM   60  C04 7MG E   7     -36.280  29.724  17.806  1.00 58.86           C
HETATM   61  C05 7MG E   7     -37.254  30.246  16.753  1.00 63.32           C
HETATM   62  C06 7MG E   7     -38.106  31.386  17.306  1.00 69.91           C
HETATM   63  C07 7MG E   7     -38.761  32.152  16.161  1.00 72.07           C
HETATM   64  C08 7MG E   7     -39.915  32.753  16.348  1.00 73.74           C
HETATM   65  C09 7MG E   7     -40.545  33.512  15.185  1.00 77.80           C
HETATM   66  C10 7MG E   7     -41.761  32.739  14.683  1.00 80.38           C
HETATM   67  C11 7MG E   7     -41.954  32.922  13.181  1.00 81.86           C
HETATM   68  C12 7MG E   7     -43.424  32.898  12.773  1.00 83.40           C
HETATM   69  C13 7MG E   7     -43.680  33.804  11.573  1.00 88.57           C
HETATM   70  C14 7MG E   7     -45.151  33.892  11.169  1.00 94.15           C
HETATM   71  C17 7MG E   7     -47.313  34.437  11.911  1.00 99.21           C
HETATM   72  C18 7MG E   7     -48.550  33.572  12.150  1.00 99.48           C
HETATM   73  C20 7MG E   7     -49.214  33.264  10.809  1.00 97.87           C
HETATM   74  O15 7MG E   7     -45.432  34.165  10.050  1.00 93.07           O
HETATM   75  O16 7MG E   7     -46.168  33.652  12.103  1.00100.17           O
HETATM   76  O19 7MG E   7     -49.448  34.258  12.978  1.00102.30           O
HETATM   77  O21 7MG E   7     -50.216  32.307  11.018  1.00 97.63           O
HETATM   78  C01 7MG E   8     -84.568  10.458  31.580  1.00 88.79           C
HETATM   79  C02 7MG E   8     -84.017   9.323  32.436  1.00 90.19           C
HETATM   80  C03 7MG E   8     -82.903   8.570  31.716  1.00 89.76           C
HETATM   81  C04 7MG E   8     -81.917   7.931  32.691  1.00 88.38           C
HETATM   82  C05 7MG E   8     -80.706   7.359  31.962  1.00 81.51           C
HETATM   83  C06 7MG E   8     -79.491   8.265  32.128  1.00 75.43           C
HETATM   84  C07 7MG E   8     -78.617   8.159  30.881  1.00 75.27           C
HETATM   85  C08 7MG E   8     -77.851   9.170  30.535  1.00 70.37           C
HETATM   86  C09 7MG E   8     -77.863  10.427  31.398  1.00 70.53           C
HETATM   87  C10 7MG E   8     -76.435  10.902  31.621  1.00 68.44           C
HETATM   88  C11 7MG E   8     -76.403  12.308  32.201  1.00 65.12           C
HETATM   89  C12 7MG E   8     -75.263  13.103  31.581  1.00 64.69           C
HETATM   90  C13 7MG E   8     -74.159  13.397  32.590  1.00 62.04           C
HETATM   91  C14 7MG E   8     -72.846  13.683  31.866  1.00 63.42           C
HETATM   92  C17 7MG E   8     -71.765  13.968  33.949  1.00 60.02           C
HETATM   93  C18 7MG E   8     -71.833  15.347  34.608  1.00 63.31           C
HETATM   94  C20 7MG E   8     -71.563  16.459  33.594  1.00 68.45           C
HETATM   95  O15 7MG E   8     -72.796  13.528  30.693  1.00 65.49           O
HETATM   96  O16 7MG E   8     -71.713  14.131  32.561  1.00 62.63           O
HETATM   97  O19 7MG E   8     -70.885  15.407  35.632  1.00 56.72           O
HETATM   98  O21 7MG E   8     -72.768  16.780  32.949  1.00 74.80           O
HETATM   99  C01 7MG E   9     -28.127 -10.735   8.461  1.00 60.37      A    C
HETATM  100  C02 7MG E   9     -29.469 -10.138   8.879  1.00 64.91      A    C
HETATM  101  C03 7MG E   9     -30.658 -10.758   8.147  1.00 71.88      A    C
HETATM  102  C04 7MG E   9     -31.836 -11.004   9.089  1.00 74.95      A    C
HETATM  103  C05 7MG E   9     -33.182 -10.673   8.450  1.00 80.82      A    C
HETATM  104  C06 7MG E   9     -34.353 -11.074   9.346  1.00 86.66      A    C
HETATM  105  C07 7MG E   9     -35.531 -10.127   9.124  1.00 85.25      A    C
HETATM  106  C08 7MG E   9     -36.399  -9.937  10.093  1.00 84.86      A    C
HETATM  107  C09 7MG E   9     -36.223 -10.658  11.429  1.00 86.22      A    C
HETATM  108  C10 7MG E   9     -37.180 -10.039  12.441  1.00 86.38      A    C
HETATM  109  C11 7MG E   9     -38.621 -10.216  11.976  1.00 87.48      A    C
HETATM  110  C12 7MG E   9     -39.601 -10.305  13.136  1.00 90.56      A    C
HETATM  111  C13 7MG E   9     -39.997 -11.750  13.426  1.00 98.83      A    C
HETATM  112  C14 7MG E   9     -41.359 -12.095  12.832  1.00107.68      A    C
HETATM  113  C17 7MG E   9     -43.064 -12.644  14.373  1.00116.57      A    C
HETATM  114  C18 7MG E   9     -44.574 -12.435  14.487  1.00117.07      A    C
HETATM  115  C20 7MG E   9     -45.219 -13.666  15.124  1.00112.50      A    C
HETATM  116  O15 7MG E   9     -41.413 -12.684  11.805  1.00109.42      A    O
HETATM  117  O16 7MG E   9     -42.538 -11.702  13.480  1.00113.69      A    O
HETATM  118  O19 7MG E   9     -45.108 -12.235  13.208  1.00120.58      A    O
HETATM  119  O21 7MG E   9     -46.224 -13.242  16.005  1.00110.28      A    O
TER
ATOM    120  N   GLU A   5      -6.419  28.811  -4.969  1.00133.99           N
ANISOU  120  N   GLU A   5    14721  17876  18313   -519   3086   2559       N
ATOM    121  CA  GLU A   5      -5.868  27.749  -4.136  1.00134.57           C
ANISOU  121  CA  GLU A   5    14738  17952  18441   -522   3037   2322       C
ATOM    122  C   GLU A   5      -5.897  28.147  -2.661  1.00134.13           C
ANISOU  122  C   GLU A   5    14625  17640  18696   -618   2891   2203       C
ATOM    123  O   GLU A   5      -5.595  27.343  -1.780  1.00129.49           O
ANISOU  123  O   GLU A   5    13994  17027  18178   -623   2818   2001       O
ATOM    124  CB  GLU A   5      -4.439  27.414  -4.572  1.00137.77           C
ANISOU  124  CB  GLU A   5    15025  18443  18878   -516   3154   2301       C
ATOM    125  CG  GLU A   5      -3.958  26.042  -4.126  1.00140.35           C
ANISOU  125  CG  GLU A   5    15319  18860  19147   -466   3139   2072       C
ATOM    126  CD  GLU A   5      -2.524  26.058  -3.635  1.00145.96           C
ANISOU  126  CD  GLU A   5    15863  19495  20100   -519   3158   2000       C
ATOM    127  OE1 GLU A   5      -1.959  24.967  -3.407  1.00147.22           O
ANISOU  127  OE1 GLU A   5    15981  19740  20216   -465   3165   1835       O
ATOM    128  OE2 GLU A   5      -1.961  27.162  -3.479  1.00148.81           O
ANISOU  128  OE2 GLU A   5    16134  19712  20696   -610   3164   2108       O
ATOM    129  N   SER A   6      -6.264  29.398  -2.400  1.00139.83           N
ANISOU  129  N   SER A   6    15351  18175  19603   -686   2845   2321       N
ATOM    130  CA  SER A   6      -6.377  29.892  -1.038  1.00143.08           C
ANISOU  130  CA  SER A   6    15723  18342  20297   -776   2699   2202       C
ATOM    131  C   SER A   6      -7.764  29.567  -0.483  1.00144.41           C
ANISOU  131  C   SER A   6    16011  18487  20371   -750   2582   2131       C
ATOM    132  O   SER A   6      -8.624  29.019  -1.178  1.00145.16           O
ANISOU  132  O   SER A   6    16241  18750  20164   -660   2583   2159       O
ATOM    133  CB  SER A   6      -6.086  31.393  -0.995  1.00146.27           C
ANISOU  133  CB  SER A   6    16075  18543  20956   -857   2708   2341       C
ATOM    134  OG  SER A   6      -6.588  32.047  -2.148  1.00147.42           O
ANISOU  134  OG  SER A   6    16289  18754  20969   -811   2810   2583       O
ATOM    135  N   TRP A   7      -7.975  29.892   0.797  1.00144.99           N
ANISOU  135  N   TRP A   7    16076  18356  20657   -816   2424   1985       N
ATOM    136  CA  TRP A   7      -9.242  29.669   1.494  1.00139.31           C
ANISOU  136  CA  TRP A   7    15514  17584  19833   -783   2240   1852       C
ATOM    137  C   TRP A   7      -9.568  28.182   1.595  1.00135.24           C
ANISOU  137  C   TRP A   7    15110  17235  19039   -693   2149   1650       C
ATOM    138  O   TRP A   7      -9.748  27.659   2.699  1.00136.52           O
ANISOU  138  O   TRP A   7    15308  17326  19236   -696   1990   1435       O
ATOM    139  CB  TRP A   7     -10.381  30.429   0.804  1.00138.89           C
ANISOU  139  CB  TRP A   7    15560  17529  19681   -754   2271   2057       C
ATOM    140  CG  TRP A   7     -11.668  30.476   1.585  1.00136.56           C
ANISOU  140  CG  TRP A   7    15399  17144  19345   -736   2092   1947       C
ATOM    141  CD1 TRP A   7     -12.067  29.623   2.578  1.00134.36           C
ANISOU  141  CD1 TRP A   7    15195  16855  18999   -715   1919   1694       C
ATOM    142  CD2 TRP A   7     -12.724  31.428   1.429  1.00137.65           C
ANISOU  142  CD2 TRP A   7    15603  17190  19507   -730   2077   2100       C
ATOM    143  NE1 TRP A   7     -13.304  29.987   3.046  1.00134.76           N
ANISOU  143  NE1 TRP A   7    15354  16820  19028   -701   1801   1676       N
ATOM    144  CE2 TRP A   7     -13.730  31.093   2.357  1.00136.86           C
ANISOU  144  CE2 TRP A   7    15615  17034  19352   -708   1892   1918       C
ATOM    145  CE3 TRP A   7     -12.917  32.531   0.593  1.00139.39           C
ANISOU  145  CE3 TRP A   7    15795  17372  19795   -735   2207   2383       C
ATOM    146  CZ2 TRP A   7     -14.911  31.823   2.473  1.00136.13           C
ANISOU  146  CZ2 TRP A   7    15603  16851  19270   -689   1834   2001       C
ATOM    147  CZ3 TRP A   7     -14.088  33.254   0.710  1.00139.36           C
ANISOU  147  CZ3 TRP A   7    15873  17271  19805   -713   2145   2471       C
ATOM    148  CH2 TRP A   7     -15.070  32.897   1.643  1.00137.08           C
ANISOU  148  CH2 TRP A   7    15692  16931  19461   -690   1960   2275       C
ATOM    149  N   PHE A   8      -9.648  27.488   0.461  1.00123.74           N
ANISOU  149  N   PHE A   8    13709  15997  17308   -611   2251   1714       N
ATOM    150  CA  PHE A   8      -9.877  26.049   0.482  1.00113.03           C
ANISOU  150  CA  PHE A   8    12451  14789  15708   -529   2183   1518       C
ATOM    151  C   PHE A   8      -8.758  25.278   1.177  1.00112.56           C
ANISOU  151  C   PHE A   8    12295  14712  15761   -536   2162   1337       C
ATOM    152  O   PHE A   8      -8.848  24.049   1.264  1.00109.50           O
ANISOU  152  O   PHE A   8    11980  14424  15203   -466   2111   1170       O
ATOM    153  CB  PHE A   8     -10.055  25.532  -0.945  1.00103.94           C
ANISOU  153  CB  PHE A   8    11359  13879  14254   -445   2314   1618       C
ATOM    154  CG  PHE A   8     -11.219  26.144  -1.663  1.00 98.98           C
ANISOU  154  CG  PHE A   8    10831  13307  13471   -420   2321   1788       C
ATOM    155  CD1 PHE A   8     -12.509  25.708  -1.411  1.00 95.63           C
ANISOU  155  CD1 PHE A   8    10556  12905  12876   -381   2173   1686       C
ATOM    156  CD2 PHE A   8     -11.024  27.159  -2.584  1.00 98.53           C
ANISOU  156  CD2 PHE A   8    10710  13283  13444   -432   2476   2062       C
ATOM    157  CE1 PHE A   8     -13.583  26.271  -2.067  1.00 95.00           C
ANISOU  157  CE1 PHE A   8    10555  12887  12654   -352   2173   1846       C
ATOM    158  CE2 PHE A   8     -12.094  27.727  -3.245  1.00 97.50           C
ANISOU  158  CE2 PHE A   8    10665  13213  13168   -396   2480   2234       C
ATOM    159  CZ  PHE A   8     -13.377  27.283  -2.987  1.00 96.18           C
ANISOU  159  CZ  PHE A   8    10642  13076  12827   -355   2324   2122       C
ATOM    160  N   LYS A   9      -7.717  25.965   1.658  1.00114.03           N
ANISOU  160  N   LYS A   9    12317  14775  16236   -617   2199   1369       N
ATOM    161  CA  LYS A   9      -6.656  25.365   2.458  1.00112.28           C
ANISOU  161  CA  LYS A   9    11984  14526  16153   -629   2158   1202       C
ATOM    162  C   LYS A   9      -7.236  24.632   3.662  1.00110.81           C
ANISOU  162  C   LYS A   9    11892  14277  15935   -603   1953    974       C
ATOM    163  O   LYS A   9      -7.340  25.202   4.754  1.00111.28           O
ANISOU  163  O   LYS A   9    11921  14176  16186   -667   1828    904       O
ATOM    164  CB  LYS A   9      -5.664  26.440   2.918  1.00113.01           C
ANISOU  164  CB  LYS A   9    11884  14467  16586   -741   2197   1270       C
ATOM    165  CG  LYS A   9      -4.202  26.004   2.943  1.00110.03           C
ANISOU  165  CG  LYS A   9    11331  14148  16327   -747   2278   1224       C
ATOM    166  CD  LYS A   9      -3.290  27.143   2.502  1.00107.73           C
ANISOU  166  CD  LYS A   9    10876  13792  16266   -839   2415   1403       C
ATOM    167  CE  LYS A   9      -3.608  27.582   1.081  1.00104.95           C
ANISOU  167  CE  LYS A   9    10591  13541  15742   -806   2575   1633       C
ATOM    168  NZ  LYS A   9      -2.857  28.809   0.702  1.00103.96           N
ANISOU  168  NZ  LYS A   9    10383  13322  15795   -883   2642   1784       N
ATOM    169  N   LYS A  10      -7.617  23.370   3.463  1.00110.18           N
ANISOU  169  N   LYS A  10    11926  14324  15615   -509   1924    857       N
ATOM    170  CA  LYS A  10      -8.188  22.533   4.520  1.00109.27           C
ANISOU  170  CA  LYS A  10    11906  14164  15447   -473   1747    655       C
ATOM    171  C   LYS A  10      -9.445  23.163   5.119  1.00109.75           C
ANISOU  171  C   LYS A  10    12075  14110  15514   -507   1614    655       C
ATOM    172  O   LYS A  10      -9.676  23.105   6.329  1.00107.59           O
ANISOU  172  O   LYS A  10    11816  13731  15333   -524   1465    525       O
ATOM    173  CB  LYS A  10      -7.153  22.231   5.609  1.00105.34           C
ANISOU  173  CB  LYS A  10    11282  13600  15144   -489   1677    520       C
ATOM    174  CG  LYS A  10      -6.494  20.865   5.469  1.00102.79           C
ANISOU  174  CG  LYS A  10    10947  13392  14715   -398   1713    407       C
ATOM    175  CD  LYS A  10      -5.611  20.543   6.664  1.00 99.54           C
ANISOU  175  CD  LYS A  10    10418  12919  14483   -401   1616    276       C
ATOM    176  CE  LYS A  10      -4.960  19.177   6.517  1.00 95.64           C
ANISOU  176  CE  LYS A  10     9911  12531  13897   -297   1658    175       C
ATOM    177  NZ  LYS A  10      -3.681  19.087   7.278  1.00 93.06           N
ANISOU  177  NZ  LYS A  10     9401  12185  13774   -303   1634    116       N
ATOM    178  N   TYR A  11     -10.270  23.771   4.260  1.00113.92           N
ANISOU  178  N   TYR A  11    12678  14672  15936   -509   1672    807       N
ATOM    179  CA  TYR A  11     -11.567  24.301   4.669  1.00115.59           C
ANISOU  179  CA  TYR A  11    12999  14797  16123   -524   1559    819       C
ATOM    180  C   TYR A  11     -12.679  23.954   3.681  1.00111.81           C
ANISOU  180  C   TYR A  11    12661  14456  15368   -463   1584    886       C
ATOM    181  O   TYR A  11     -13.796  24.465   3.828  1.00112.94           O
ANISOU  181  O   TYR A  11    12887  14547  15478   -469   1510    930       O
ATOM    182  CB  TYR A  11     -11.505  25.825   4.854  1.00123.51           C
ANISOU  182  CB  TYR A  11    13922  15643  17363   -609   1581    959       C
ATOM    183  CG  TYR A  11     -10.580  26.312   5.957  1.00129.11           C
ANISOU  183  CG  TYR A  11    14495  16198  18362   -686   1527    871       C
ATOM    184  CD1 TYR A  11     -10.708  25.850   7.263  1.00128.72           C
ANISOU  184  CD1 TYR A  11    14468  16081  18357   -683   1363    669       C
ATOM    185  CD2 TYR A  11      -9.595  27.255   5.692  1.00131.76           C
ANISOU  185  CD2 TYR A  11    14676  16462  18926   -762   1639    992       C
ATOM    186  CE1 TYR A  11      -9.866  26.305   8.269  1.00128.43           C
ANISOU  186  CE1 TYR A  11    14301  15926  18569   -751   1303    579       C
ATOM    187  CE2 TYR A  11      -8.753  27.715   6.687  1.00131.46           C
ANISOU  187  CE2 TYR A  11    14503  16290  19156   -840   1580    898       C
ATOM    188  CZ  TYR A  11      -8.892  27.239   7.973  1.00129.73           C
ANISOU  188  CZ  TYR A  11    14308  16021  18961   -833   1407    686       C
ATOM    189  OH  TYR A  11      -8.051  27.700   8.961  1.00128.47           O
ANISOU  189  OH  TYR A  11    14009  15749  19053   -908   1340    582       O
ATOM    190  N   TRP A  12     -12.405  23.106   2.681  1.00109.42           N
ANISOU  190  N   TRP A  12    12379  14331  14863   -402   1684    889       N
ATOM    191  CA  TRP A  12     -13.438  22.727   1.719  1.00 99.42           C
ANISOU  191  CA  TRP A  12    11239  13216  13319   -345   1699    931       C
ATOM    192  C   TRP A  12     -14.579  21.980   2.401  1.00 93.89           C
ANISOU  192  C   TRP A  12    10671  12495  12509   -320   1536    769       C
ATOM    193  O   TRP A  12     -15.752  22.126   2.020  1.00 92.55           O
ANISOU  193  O   TRP A  12    10597  12377  12191   -303   1492    818       O
ATOM    194  CB  TRP A  12     -12.823  21.870   0.606  1.00105.54           C
ANISOU  194  CB  TRP A  12    12008  14188  13905   -284   1833    924       C
ATOM    195  CG  TRP A  12     -13.332  22.189  -0.776  1.00111.23           C
ANISOU  195  CG  TRP A  12    12773  15082  14407   -248   1937   1091       C
ATOM    196  CD1 TRP A  12     -14.522  22.780  -1.093  1.00114.44           C
ANISOU  196  CD1 TRP A  12    13259  15511  14711   -246   1887   1200       C
ATOM    197  CD2 TRP A  12     -12.666  21.938  -2.027  1.00114.18           C
ANISOU  197  CD2 TRP A  12    13108  15648  14627   -201   2109   1173       C
ATOM    198  NE1 TRP A  12     -14.640  22.913  -2.456  1.00118.74           N
ANISOU  198  NE1 TRP A  12    13819  16256  15043   -200   2010   1349       N
ATOM    199  CE2 TRP A  12     -13.516  22.405  -3.053  1.00117.30           C
ANISOU  199  CE2 TRP A  12    13567  16183  14819   -172   2149   1333       C
ATOM    200  CE3 TRP A  12     -11.435  21.365  -2.379  1.00109.02           C
ANISOU  200  CE3 TRP A  12    12369  15071  13983   -174   2234   1129       C
ATOM    201  CZ2 TRP A  12     -13.177  22.317  -4.405  1.00113.77           C
ANISOU  201  CZ2 TRP A  12    13105  15957  14164   -118   2309   1448       C
ATOM    202  CZ3 TRP A  12     -11.101  21.279  -3.725  1.00106.97           C
ANISOU  202  CZ3 TRP A  12    12094  15022  13526   -121   2401   1238       C
ATOM    203  CH2 TRP A  12     -11.968  21.752  -4.719  1.00110.92           C
ANISOU  203  CH2 TRP A  12    12665  15668  13813    -93   2436   1394       C
ATOM    204  N   HIS A  13     -14.253  21.180   3.418  1.00 91.95           N
ANISOU  204  N   HIS A  13    10423  12177  12337   -315   1448    585       N
ATOM    205  CA  HIS A  13     -15.273  20.406   4.115  1.00 84.68           C
ANISOU  205  CA  HIS A  13     9619  11231  11324   -291   1304    435       C
ATOM    206  C   HIS A  13     -16.284  21.315   4.803  1.00 78.58           C
ANISOU  206  C   HIS A  13     8886  10340  10631   -330   1196    482       C
ATOM    207  O   HIS A  13     -17.486  21.022   4.812  1.00 81.92           O
ANISOU  207  O   HIS A  13     9415  10793  10917   -311   1116    449       O
ATOM    208  CB  HIS A  13     -14.616  19.450   5.116  1.00 79.62           C
ANISOU  208  CB  HIS A  13     8954  10529  10768   -273   1242    257       C
ATOM    209  CG  HIS A  13     -13.847  20.126   6.209  1.00 79.77           C
ANISOU  209  CG  HIS A  13     8862  10405  11041   -321   1196    248       C
ATOM    210  ND1 HIS A  13     -12.856  21.054   5.965  1.00 80.62           N
ANISOU  210  ND1 HIS A  13     8837  10482  11315   -368   1289    360       N
ATOM    211  CD2 HIS A  13     -13.912  19.992   7.555  1.00 78.32           C
ANISOU  211  CD2 HIS A  13     8676  10109  10971   -331   1066    133       C
ATOM    212  CE1 HIS A  13     -12.353  21.469   7.113  1.00 80.34           C
ANISOU  212  CE1 HIS A  13     8719  10317  11488   -410   1209    301       C
ATOM    213  NE2 HIS A  13     -12.975  20.839   8.094  1.00 80.23           N
ANISOU  213  NE2 HIS A  13     8785  10262  11437   -384   1072    163       N
ATOM    214  N   LEU A  14     -15.823  22.434   5.367  1.00 70.55           N
ANISOU  214  N   LEU A  14     7778   9188   9842   -387   1195    555       N
ATOM    215  CA  LEU A  14     -16.752  23.364   6.000  1.00 67.08           C
ANISOU  215  CA  LEU A  14     7371   8627   9490   -418   1104    596       C
ATOM    216  C   LEU A  14     -17.663  24.014   4.967  1.00 67.76           C
ANISOU  216  C   LEU A  14     7509   8783   9455   -405   1154    770       C
ATOM    217  O   LEU A  14     -18.846  24.256   5.239  1.00 66.52           O
ANISOU  217  O   LEU A  14     7429   8596   9249   -395   1067    776       O
ATOM    218  CB  LEU A  14     -15.986  24.423   6.792  1.00 62.01           C
ANISOU  218  CB  LEU A  14     6614   7817   9131   -485   1098    619       C
ATOM    219  CG  LEU A  14     -15.170  23.922   7.989  1.00 62.39           C
ANISOU  219  CG  LEU A  14     6600   7794   9309   -498   1020    445       C
ATOM    220  CD1 LEU A  14     -14.740  25.075   8.882  1.00 66.54           C
ANISOU  220  CD1 LEU A  14     7030   8151  10103   -571    979    444       C
ATOM    221  CD2 LEU A  14     -15.946  22.894   8.794  1.00 60.58           C
ANISOU  221  CD2 LEU A  14     6477   7583   8957   -451    890    284       C
ATOM    222  N   SER A  15     -17.136  24.287   3.771  1.00 65.93           N
ANISOU  222  N   SER A  15     7232   8655   9164   -397   1297    921       N
ATOM    223  CA  SER A  15     -17.969  24.832   2.703  1.00 63.30           C
ANISOU  223  CA  SER A  15     6945   8422   8684   -370   1349   1100       C
ATOM    224  C   SER A  15     -19.074  23.855   2.323  1.00 56.13           C
ANISOU  224  C   SER A  15     6159   7664   7504   -315   1277   1014       C
ATOM    225  O   SER A  15     -20.247  24.238   2.195  1.00 57.35           O
ANISOU  225  O   SER A  15     6376   7834   7579   -299   1217   1080       O
ATOM    226  CB  SER A  15     -17.104  25.176   1.487  1.00 66.29           C
ANISOU  226  CB  SER A  15     7248   8910   9027   -363   1525   1274       C
ATOM    227  OG  SER A  15     -16.512  24.014   0.932  1.00 65.74           O
ANISOU  227  OG  SER A  15     7187   9000   8792   -323   1583   1173       O
ATOM    228  N   VAL A  16     -18.719  22.579   2.144  1.00 52.27           N
ANISOU  228  N   VAL A  16     5700   7281   6878   -285   1283    861       N
ATOM    229  CA  VAL A  16     -19.741  21.592   1.803  1.00 53.66           C
ANISOU  229  CA  VAL A  16     5987   7588   6815   -244   1214    756       C
ATOM    230  C   VAL A  16     -20.752  21.464   2.936  1.00 51.26           C
ANISOU  230  C   VAL A  16     5745   7166   6564   -259   1057    650       C
ATOM    231  O   VAL A  16     -21.958  21.330   2.697  1.00 47.81           O
ANISOU  231  O   VAL A  16     5383   6799   5984   -242    989    651       O
ATOM    232  CB  VAL A  16     -19.103  20.235   1.458  1.00 49.58           C
ANISOU  232  CB  VAL A  16     5487   7176   6174   -212   1257    598       C
ATOM    233  CG1 VAL A  16     -20.189  19.188   1.266  1.00 55.11           C
ANISOU  233  CG1 VAL A  16     6300   7975   6664   -184   1171    460       C
ATOM    234  CG2 VAL A  16     -18.277  20.349   0.201  1.00 43.14           C
ANISOU  234  CG2 VAL A  16     4619   6512   5259   -185   1418    708       C
ATOM    235  N   LEU A  17     -20.282  21.515   4.184  1.00 51.22           N
ANISOU  235  N   LEU A  17     5705   6995   6763   -289    999    558       N
ATOM    236  CA  LEU A  17     -21.195  21.406   5.318  1.00 53.11           C
ANISOU  236  CA  LEU A  17     5998   7129   7050   -297    859    460       C
ATOM    237  C   LEU A  17     -22.179  22.570   5.349  1.00 55.67           C
ANISOU  237  C   LEU A  17     6335   7402   7415   -307    822    594       C
ATOM    238  O   LEU A  17     -23.368  22.380   5.630  1.00 57.71           O
ANISOU  238  O   LEU A  17     6663   7671   7593   -293    729    557       O
ATOM    239  CB  LEU A  17     -20.402  21.336   6.623  1.00 54.40           C
ANISOU  239  CB  LEU A  17     6110   7144   7416   -321    810    349       C
ATOM    240  CG  LEU A  17     -20.158  19.947   7.217  1.00 57.05           C
ANISOU  240  CG  LEU A  17     6481   7491   7706   -295    760    165       C
ATOM    241  CD1 LEU A  17     -19.794  18.949   6.132  1.00 60.16           C
ANISOU  241  CD1 LEU A  17     6897   8032   7930   -261    846    132       C
ATOM    242  CD2 LEU A  17     -19.070  20.002   8.279  1.00 58.19           C
ANISOU  242  CD2 LEU A  17     6542   7522   8044   -311    739     93       C
ATOM    243  N   VAL A  18     -21.703  23.782   5.057  1.00 48.62           N
ANISOU  243  N   VAL A  18     5369   6447   6658   -329    899    757       N
ATOM    244  CA  VAL A  18     -22.590  24.942   5.049  1.00 50.79           C
ANISOU  244  CA  VAL A  18     5650   6656   6991   -329    877    899       C
ATOM    245  C   VAL A  18     -23.604  24.832   3.916  1.00 51.82           C
ANISOU  245  C   VAL A  18     5840   6963   6887   -283    888   1005       C
ATOM    246  O   VAL A  18     -24.787  25.166   4.084  1.00 47.70           O
ANISOU  246  O   VAL A  18     5362   6432   6329   -264    813   1040       O
ATOM    247  CB  VAL A  18     -21.767  26.239   4.958  1.00 46.29           C
ANISOU  247  CB  VAL A  18     4983   5963   6642   -367    970   1052       C
ATOM    248  CG1 VAL A  18     -22.616  27.378   4.421  1.00 44.36           C
ANISOU  248  CG1 VAL A  18     4745   5699   6410   -348    996   1257       C
ATOM    249  CG2 VAL A  18     -21.216  26.593   6.321  1.00 46.83           C
ANISOU  249  CG2 VAL A  18     5001   5835   6958   -416    910    934       C
ATOM    250  N   ILE A  19     -23.162  24.358   2.748  1.00 49.50           N
ANISOU  250  N   ILE A  19     5543   6843   6422   -261    981   1054       N
ATOM    251  CA  ILE A  19     -24.094  24.130   1.646  1.00 49.19           C
ANISOU  251  CA  ILE A  19     5557   7004   6127   -214    981   1130       C
ATOM    252  C   ILE A  19     -25.163  23.119   2.052  1.00 56.07           C
ANISOU  252  C   ILE A  19     6513   7928   6864   -204    851    955       C
ATOM    253  O   ILE A  19     -26.362  23.301   1.778  1.00 56.97           O
ANISOU  253  O   ILE A  19     6665   8116   6867   -180    787   1009       O
ATOM    254  CB  ILE A  19     -23.328  23.668   0.394  1.00 50.42           C
ANISOU  254  CB  ILE A  19     5696   7349   6113   -190   1104   1174       C
ATOM    255  CG1 ILE A  19     -22.462  24.805  -0.152  1.00 56.53           C
ANISOU  255  CG1 ILE A  19     6382   8090   7007   -196   1244   1397       C
ATOM    256  CG2 ILE A  19     -24.293  23.164  -0.664  1.00 46.90           C
ANISOU  256  CG2 ILE A  19     5314   7138   5369   -142   1081   1190       C
ATOM    257  CD1 ILE A  19     -23.252  26.027  -0.549  1.00 57.70           C
ANISOU  257  CD1 ILE A  19     6521   8227   7174   -174   1254   1630       C
ATOM    258  N   ALA A  20     -24.747  22.040   2.718  1.00 49.56           N
ANISOU  258  N   ALA A  20     5711   7063   6057   -222    813    751       N
ATOM    259  CA  ALA A  20     -25.698  21.023   3.149  1.00 50.02           C
ANISOU  259  CA  ALA A  20     5844   7152   6011   -220    700    585       C
ATOM    260  C   ALA A  20     -26.690  21.594   4.154  1.00 54.64           C
ANISOU  260  C   ALA A  20     6443   7610   6706   -229    594    594       C
ATOM    261  O   ALA A  20     -27.889  21.292   4.096  1.00 57.16           O
ANISOU  261  O   ALA A  20     6810   7998   6911   -218    514    566       O
ATOM    262  CB  ALA A  20     -24.953  19.828   3.741  1.00 42.59           C
ANISOU  262  CB  ALA A  20     4916   6163   5101   -231    693    388       C
ATOM    263  N   ALA A  21     -26.207  22.423   5.081  1.00 50.31           N
ANISOU  263  N   ALA A  21     5850   6883   6384   -249    594    625       N
ATOM    264  CA  ALA A  21     -27.096  23.049   6.053  1.00 42.89           C
ANISOU  264  CA  ALA A  21     4920   5820   5556   -251    505    630       C
ATOM    265  C   ALA A  21     -28.122  23.940   5.365  1.00 45.44           C
ANISOU  265  C   ALA A  21     5246   6204   5817   -221    503    803       C
ATOM    266  O   ALA A  21     -29.299  23.957   5.747  1.00 52.02           O
ANISOU  266  O   ALA A  21     6111   7037   6617   -205    417    786       O
ATOM    267  CB  ALA A  21     -26.281  23.846   7.072  1.00 40.43           C
ANISOU  267  CB  ALA A  21     4552   5313   5496   -279    513    623       C
ATOM    268  N   LEU A  22     -27.700  24.678   4.335  1.00 45.26           N
ANISOU  268  N   LEU A  22     5182   6240   5775   -207    602    982       N
ATOM    269  CA  LEU A  22     -28.647  25.527   3.614  1.00 44.07           C
ANISOU  269  CA  LEU A  22     5028   6160   5557   -166    605   1171       C
ATOM    270  C   LEU A  22     -29.703  24.697   2.892  1.00 49.82           C
ANISOU  270  C   LEU A  22     5807   7101   6021   -137    543   1135       C
ATOM    271  O   LEU A  22     -30.885  25.069   2.865  1.00 58.21           O
ANISOU  271  O   LEU A  22     6879   8199   7038   -106    477   1202       O
ATOM    272  CB  LEU A  22     -27.905  26.427   2.629  1.00 43.35           C
ANISOU  272  CB  LEU A  22     4882   6097   5493   -154    736   1386       C
ATOM    273  CG  LEU A  22     -27.184  27.619   3.260  1.00 42.54           C
ANISOU  273  CG  LEU A  22     4715   5766   5682   -183    792   1473       C
ATOM    274  CD1 LEU A  22     -26.415  28.391   2.207  1.00 43.31           C
ANISOU  274  CD1 LEU A  22     4753   5900   5802   -176    936   1693       C
ATOM    275  CD2 LEU A  22     -28.172  28.522   3.982  1.00 38.28           C
ANISOU  275  CD2 LEU A  22     4181   5084   5280   -165    724   1522       C
ATOM    276  N   ILE A  23     -29.298  23.577   2.291  1.00 51.17           N
ANISOU  276  N   ILE A  23     6004   7417   6021   -145    563   1024       N
ATOM    277  CA  ILE A  23     -30.275  22.705   1.640  1.00 48.21           C
ANISOU  277  CA  ILE A  23     5674   7240   5402   -129    497    954       C
ATOM    278  C   ILE A  23     -31.256  22.144   2.667  1.00 54.91           C
ANISOU  278  C   ILE A  23     6560   8017   6288   -149    372    804       C
ATOM    279  O   ILE A  23     -32.475  22.083   2.430  1.00 50.12           O
ANISOU  279  O   ILE A  23     5964   7511   5567   -133    295    820       O
ATOM    280  CB  ILE A  23     -29.556  21.584   0.869  1.00 45.45           C
ANISOU  280  CB  ILE A  23     5347   7035   4886   -137    550    835       C
ATOM    281  CG1 ILE A  23     -28.746  22.172  -0.288  1.00 52.29           C
ANISOU  281  CG1 ILE A  23     6173   8015   5677   -106    679   1007       C
ATOM    282  CG2 ILE A  23     -30.553  20.566   0.350  1.00 43.03           C
ANISOU  282  CG2 ILE A  23     5088   6909   4353   -136    468    711       C
ATOM    283  CD1 ILE A  23     -27.493  21.386  -0.618  1.00 51.28           C
ANISOU  283  CD1 ILE A  23     6043   7925   5516   -118    771    901       C
ATOM    284  N   SER A  24     -30.737  21.725   3.824  1.00 51.07           N
ANISOU  284  N   SER A  24     6084   7363   5957   -183    352    662       N
ATOM    285  CA  SER A  24     -31.598  21.231   4.891  1.00 45.47           C
ANISOU  285  CA  SER A  24     5406   6576   5295   -199    248    535       C
ATOM    286  C   SER A  24     -32.595  22.297   5.326  1.00 46.84           C
ANISOU  286  C   SER A  24     5558   6686   5551   -174    198    653       C
ATOM    287  O   SER A  24     -33.755  21.990   5.621  1.00 47.06           O
ANISOU  287  O   SER A  24     5603   6751   5526   -170    113    608       O
ATOM    288  CB  SER A  24     -30.746  20.770   6.074  1.00 41.21           C
ANISOU  288  CB  SER A  24     4873   5872   4914   -226    246    397       C
ATOM    289  OG  SER A  24     -31.496  19.960   6.966  1.00 42.99           O
ANISOU  289  OG  SER A  24     5136   6058   5141   -240    159    259       O
ATOM    290  N   VAL A  25     -32.162  23.558   5.366  1.00 48.83           N
ANISOU  290  N   VAL A  25     5769   6838   5946   -155    254    803       N
ATOM    291  CA  VAL A  25     -33.071  24.643   5.728  1.00 45.31           C
ANISOU  291  CA  VAL A  25     5302   6319   5594   -121    220    922       C
ATOM    292  C   VAL A  25     -34.160  24.795   4.674  1.00 42.80           C
ANISOU  292  C   VAL A  25     4978   6188   5096    -79    194   1048       C
ATOM    293  O   VAL A  25     -35.354  24.841   4.996  1.00 47.47           O
ANISOU  293  O   VAL A  25     5570   6800   5664    -57    114   1045       O
ATOM    294  CB  VAL A  25     -32.295  25.957   5.928  1.00 45.15           C
ANISOU  294  CB  VAL A  25     5236   6135   5784   -115    297   1054       C
ATOM    295  CG1 VAL A  25     -33.246  27.141   5.893  1.00 44.68           C
ANISOU  295  CG1 VAL A  25     5152   6030   5795    -65    285   1219       C
ATOM    296  CG2 VAL A  25     -31.528  25.927   7.241  1.00 38.54           C
ANISOU  296  CG2 VAL A  25     4396   5105   5142   -154    286    912       C
ATOM    297  N   LYS A  26     -33.765  24.874   3.400  1.00 44.18           N
ANISOU  297  N   LYS A  26     5140   6514   5131    -61    261   1162       N
ATOM    298  CA  LYS A  26     -34.748  25.023   2.329  1.00 46.29           C
ANISOU  298  CA  LYS A  26     5395   6990   5203    -14    232   1288       C
ATOM    299  C   LYS A  26     -35.801  23.927   2.390  1.00 48.10           C
ANISOU  299  C   LYS A  26     5651   7349   5276    -31    121   1131       C
ATOM    300  O   LYS A  26     -36.995  24.190   2.199  1.00 48.14           O
ANISOU  300  O   LYS A  26     5635   7445   5212      3     52   1200       O
ATOM    301  CB  LYS A  26     -34.060  25.013   0.964  1.00 47.88           C
ANISOU  301  CB  LYS A  26     5586   7367   5240      5    322   1396       C
ATOM    302  CG  LYS A  26     -34.989  25.372  -0.194  1.00 52.32           C
ANISOU  302  CG  LYS A  26     6125   8157   5597     68    300   1565       C
ATOM    303  CD  LYS A  26     -35.445  24.138  -0.963  1.00 56.86           C
ANISOU  303  CD  LYS A  26     6726   8982   5894     54    237   1422       C
ATOM    304  CE  LYS A  26     -36.418  24.499  -2.077  1.00 57.84           C
ANISOU  304  CE  LYS A  26     6819   9356   5802    120    198   1582       C
ATOM    305  NZ  LYS A  26     -36.570  23.389  -3.060  1.00 57.90           N
ANISOU  305  NZ  LYS A  26     6846   9631   5521    106    163   1450       N
ATOM    306  N   LEU A  27     -35.380  22.691   2.663  1.00 47.32           N
ANISOU  306  N   LEU A  27     5593   7255   5133    -86    105    921       N
ATOM    307  CA  LEU A  27     -36.344  21.596   2.716  1.00 45.82           C
ANISOU  307  CA  LEU A  27     5425   7170   4815   -115      7    764       C
ATOM    308  C   LEU A  27     -37.183  21.638   3.986  1.00 51.03           C
ANISOU  308  C   LEU A  27     6084   7690   5616   -125    -70    704       C
ATOM    309  O   LEU A  27     -38.382  21.337   3.953  1.00 51.85           O
ANISOU  309  O   LEU A  27     6174   7888   5639   -125   -154    678       O
ATOM    310  CB  LEU A  27     -35.626  20.253   2.609  1.00 41.94           C
ANISOU  310  CB  LEU A  27     4978   6707   4250   -165     25    563       C
ATOM    311  CG  LEU A  27     -35.017  19.963   1.240  1.00 45.33           C
ANISOU  311  CG  LEU A  27     5411   7326   4486   -153     90    583       C
ATOM    312  CD1 LEU A  27     -34.176  18.701   1.297  1.00 43.68           C
ANISOU  312  CD1 LEU A  27     5246   7098   4253   -196    122    378       C
ATOM    313  CD2 LEU A  27     -36.106  19.854   0.179  1.00 44.23           C
ANISOU  313  CD2 LEU A  27     5256   7435   4116   -133     26    623       C
ATOM    314  N   ARG A  28     -36.584  22.022   5.110  1.00 47.68           N
ANISOU  314  N   ARG A  28     5666   7052   5398   -131    -42    681       N
ATOM    315  CA  ARG A  28     -37.224  21.833   6.402  1.00 44.42           C
ANISOU  315  CA  ARG A  28     5261   6514   5102   -144   -107    587       C
ATOM    316  C   ARG A  28     -37.979  23.051   6.909  1.00 50.92           C
ANISOU  316  C   ARG A  28     6048   7255   6044    -93   -127    716       C
ATOM    317  O   ARG A  28     -38.844  22.894   7.775  1.00 55.98           O
ANISOU  317  O   ARG A  28     6687   7850   6734    -92   -188    656       O
ATOM    318  CB  ARG A  28     -36.182  21.415   7.447  1.00 35.63           C
ANISOU  318  CB  ARG A  28     4177   5232   4128   -176    -79    458       C
ATOM    319  CG  ARG A  28     -35.956  19.919   7.479  1.00 35.06           C
ANISOU  319  CG  ARG A  28     4145   5204   3970   -223    -96    281       C
ATOM    320  CD  ARG A  28     -34.663  19.536   8.181  1.00 34.50           C
ANISOU  320  CD  ARG A  28     4095   5003   4012   -240    -49    187       C
ATOM    321  NE  ARG A  28     -34.499  18.085   8.187  1.00 35.42           N
ANISOU  321  NE  ARG A  28     4250   5152   4056   -276    -60     27       N
ATOM    322  CZ  ARG A  28     -33.907  17.395   7.216  1.00 35.49           C
ANISOU  322  CZ  ARG A  28     4274   5259   3951   -289    -15    -22       C
ATOM    323  NH1 ARG A  28     -33.401  18.024   6.162  1.00 32.17           N
ANISOU  323  NH1 ARG A  28     3832   4929   3463   -269     46     85       N
ATOM    324  NH2 ARG A  28     -33.809  16.075   7.303  1.00 37.83           N
ANISOU  324  NH2 ARG A  28     4608   5561   4206   -319    -24   -176       N
ATOM    325  N   ILE A  29     -37.699  24.250   6.395  1.00 46.24           N
ANISOU  325  N   ILE A  29     5424   6639   5505    -49    -70    897       N
ATOM    326  CA  ILE A  29     -38.266  25.482   6.929  1.00 45.89           C
ANISOU  326  CA  ILE A  29     5347   6477   5611      5    -73   1017       C
ATOM    327  C   ILE A  29     -39.060  26.246   5.874  1.00 51.20           C
ANISOU  327  C   ILE A  29     5976   7283   6193     69    -73   1221       C
ATOM    328  O   ILE A  29     -40.199  26.657   6.117  1.00 57.48           O
ANISOU  328  O   ILE A  29     6742   8091   7006    114   -126   1277       O
ATOM    329  CB  ILE A  29     -37.176  26.377   7.555  1.00 43.14           C
ANISOU  329  CB  ILE A  29     4995   5917   5480      2      0   1045       C
ATOM    330  CG1 ILE A  29     -36.668  25.732   8.845  1.00 43.84           C
ANISOU  330  CG1 ILE A  29     5115   5876   5666    -43    -24    845       C
ATOM    331  CG2 ILE A  29     -37.707  27.779   7.824  1.00 37.51           C
ANISOU  331  CG2 ILE A  29     4246   5085   4923     64     16   1193       C
ATOM    332  CD1 ILE A  29     -35.731  26.603   9.634  1.00 48.11           C
ANISOU  332  CD1 ILE A  29     5643   6211   6425    -49     24    841       C
ATOM    333  N   LEU A  30     -38.477  26.448   4.694  1.00 54.65           N
ANISOU  333  N   LEU A  30     6405   7831   6530     80    -12   1343       N
ATOM    334  CA  LEU A  30     -39.167  27.218   3.664  1.00 57.13           C
ANISOU  334  CA  LEU A  30     6674   8282   6749    153     -8   1562       C
ATOM    335  C   LEU A  30     -40.159  26.384   2.865  1.00 51.92           C
ANISOU  335  C   LEU A  30     6003   7887   5837    157    -94   1530       C
ATOM    336  O   LEU A  30     -41.211  26.899   2.468  1.00 48.95           O
ANISOU  336  O   LEU A  30     5581   7615   5404    220   -140   1665       O
ATOM    337  CB  LEU A  30     -38.152  27.863   2.718  1.00 61.40           C
ANISOU  337  CB  LEU A  30     7204   8842   7282    172    102   1732       C
ATOM    338  CG  LEU A  30     -36.984  28.555   3.421  1.00 66.97           C
ANISOU  338  CG  LEU A  30     7914   9295   8237    146    192   1740       C
ATOM    339  CD1 LEU A  30     -35.966  29.046   2.411  1.00 72.91           C
ANISOU  339  CD1 LEU A  30     8647  10086   8968    154    308   1905       C
ATOM    340  CD2 LEU A  30     -37.469  29.701   4.303  1.00 68.15           C
ANISOU  340  CD2 LEU A  30     8039   9234   8622    187    189   1814       C
ATOM    341  N   ASN A  31     -39.853  25.112   2.620  1.00 48.34           N
ANISOU  341  N   ASN A  31     5587   7542   5240     92   -119   1350       N
ATOM    342  CA  ASN A  31     -40.783  24.266   1.876  1.00 45.75           C
ANISOU  342  CA  ASN A  31     5243   7459   4680     82   -207   1288       C
ATOM    343  C   ASN A  31     -42.116  24.077   2.592  1.00 46.08           C
ANISOU  343  C   ASN A  31     5255   7496   4757     82   -309   1227       C
ATOM    344  O   ASN A  31     -43.165  24.225   1.941  1.00 45.00           O
ANISOU  344  O   ASN A  31     5065   7543   4490    122   -376   1314       O
ATOM    345  CB  ASN A  31     -40.115  22.926   1.561  1.00 40.99           C
ANISOU  345  CB  ASN A  31     4691   6935   3950      8   -202   1085       C
ATOM    346  CG  ASN A  31     -39.527  22.887   0.172  1.00 46.18           C
ANISOU  346  CG  ASN A  31     5348   7789   4408     29   -147   1161       C
ATOM    347  OD1 ASN A  31     -39.324  23.926  -0.457  1.00 49.07           O
ANISOU  347  OD1 ASN A  31     5685   8196   4763     95    -88   1382       O
ATOM    348  ND2 ASN A  31     -39.252  21.683  -0.320  1.00 48.79           N
ANISOU  348  ND2 ASN A  31     5712   8245   4580    -23   -161    981       N
ATOM    349  N   PRO A  32     -42.168  23.756   3.896  1.00 43.97           N
ANISOU  349  N   PRO A  32     5011   7043   4652     42   -327   1089       N
ATOM    350  CA  PRO A  32     -43.474  23.577   4.542  1.00 48.92           C
ANISOU  350  CA  PRO A  32     5601   7682   5306     45   -414   1044       C
ATOM    351  C   PRO A  32     -43.972  24.829   5.248  1.00 51.51           C
ANISOU  351  C   PRO A  32     5891   7868   5810    121   -402   1184       C
ATOM    352  O   PRO A  32     -44.841  24.743   6.123  1.00 54.49           O
ANISOU  352  O   PRO A  32     6246   8193   6263    124   -451   1128       O
ATOM    353  CB  PRO A  32     -43.196  22.452   5.541  1.00 49.13           C
ANISOU  353  CB  PRO A  32     5676   7596   5396    -36   -428    819       C
ATOM    354  CG  PRO A  32     -41.792  22.741   5.984  1.00 45.73           C
ANISOU  354  CG  PRO A  32     5296   6986   5092    -43   -339    806       C
ATOM    355  CD  PRO A  32     -41.071  23.363   4.803  1.00 37.81           C
ANISOU  355  CD  PRO A  32     4288   6068   4011     -9   -274    953       C
ATOM    356  N   TRP A  33     -43.439  25.996   4.874  1.00 45.96           N
ANISOU  356  N   TRP A  33     5180   7101   5180    183   -329   1366       N
ATOM    357  CA  TRP A  33     -43.734  27.218   5.619  1.00 43.01           C
ANISOU  357  CA  TRP A  33     4781   6548   5012    252   -301   1480       C
ATOM    358  C   TRP A  33     -45.215  27.572   5.563  1.00 46.69           C
ANISOU  358  C   TRP A  33     5177   7115   5448    320   -371   1572       C
ATOM    359  O   TRP A  33     -45.812  27.938   6.583  1.00 45.19           O
ANISOU  359  O   TRP A  33     4970   6796   5403    349   -385   1544       O
ATOM    360  CB  TRP A  33     -42.897  28.379   5.084  1.00 41.98           C
ANISOU  360  CB  TRP A  33     4648   6332   4969    302   -203   1672       C
ATOM    361  CG  TRP A  33     -43.079  29.648   5.862  1.00 39.90           C
ANISOU  361  CG  TRP A  33     4364   5851   4944    367   -164   1771       C
ATOM    362  CD1 TRP A  33     -44.060  30.581   5.693  1.00 42.05           C
ANISOU  362  CD1 TRP A  33     4580   6135   5264    463   -175   1944       C
ATOM    363  CD2 TRP A  33     -42.259  30.119   6.937  1.00 44.49           C
ANISOU  363  CD2 TRP A  33     4978   6173   5754    343   -107   1691       C
ATOM    364  NE1 TRP A  33     -43.902  31.603   6.597  1.00 45.06           N
ANISOU  364  NE1 TRP A  33     4960   6264   5896    501   -122   1970       N
ATOM    365  CE2 TRP A  33     -42.804  31.343   7.373  1.00 46.17           C
ANISOU  365  CE2 TRP A  33     5156   6240   6147    425    -84   1810       C
ATOM    366  CE3 TRP A  33     -41.115  29.624   7.575  1.00 49.15           C
ANISOU  366  CE3 TRP A  33     5618   6645   6413    265    -78   1526       C
ATOM    367  CZ2 TRP A  33     -42.243  32.083   8.414  1.00 50.88           C
ANISOU  367  CZ2 TRP A  33     5769   6576   6987    423    -34   1752       C
ATOM    368  CZ3 TRP A  33     -40.562  30.358   8.610  1.00 49.59           C
ANISOU  368  CZ3 TRP A  33     5683   6457   6700    263    -35   1478       C
ATOM    369  CH2 TRP A  33     -41.125  31.575   9.018  1.00 51.50           C
ANISOU  369  CH2 TRP A  33     5894   6558   7117    338    -15   1582       C
ATOM    370  N   ASN A  34     -45.824  27.483   4.380  1.00 49.35           N
ANISOU  370  N   ASN A  34     5467   7692   5593    351   -416   1681       N
ATOM    371  CA  ASN A  34     -47.213  27.898   4.233  1.00 51.50           C
ANISOU  371  CA  ASN A  34     5656   8078   5835    426   -485   1792       C
ATOM    372  C   ASN A  34     -48.199  26.899   4.826  1.00 55.21           C
ANISOU  372  C   ASN A  34     6099   8620   6259    372   -579   1616       C
ATOM    373  O   ASN A  34     -49.329  27.282   5.140  1.00 59.49           O
ANISOU  373  O   ASN A  34     6570   9188   6846    430   -625   1676       O
ATOM    374  CB  ASN A  34     -47.534  28.140   2.757  1.00 50.70           C
ANISOU  374  CB  ASN A  34     5503   8232   5528    483   -510   1973       C
ATOM    375  CG  ASN A  34     -46.835  29.371   2.204  1.00 54.71           C
ANISOU  375  CG  ASN A  34     6016   8663   6110    564   -409   2211       C
ATOM    376  OD1 ASN A  34     -46.733  30.395   2.879  1.00 54.37           O
ANISOU  376  OD1 ASN A  34     5971   8395   6292    619   -347   2304       O
ATOM    377  ND2 ASN A  34     -46.347  29.274   0.972  1.00 56.63           N
ANISOU  377  ND2 ASN A  34     6263   9090   6166    571   -388   2308       N
ATOM    378  N   SER A  35     -47.803  25.635   4.993  1.00 56.45           N
ANISOU  378  N   SER A  35     6304   8803   6341    264   -602   1406       N
ATOM    379  CA  SER A  35     -48.693  24.662   5.619  1.00 53.59           C
ANISOU  379  CA  SER A  35     5916   8484   5963    204   -679   1243       C
ATOM    380  C   SER A  35     -48.691  24.783   7.137  1.00 49.88           C
ANISOU  380  C   SER A  35     5472   7783   5698    200   -646   1158       C
ATOM    381  O   SER A  35     -49.684  24.429   7.783  1.00 43.92           O
ANISOU  381  O   SER A  35     4670   7044   4972    191   -696   1096       O
ATOM    382  CB  SER A  35     -48.300  23.242   5.212  1.00 56.19           C
ANISOU  382  CB  SER A  35     6287   8916   6148     93   -710   1053       C
ATOM    383  OG  SER A  35     -48.295  23.098   3.804  1.00 64.14           O
ANISOU  383  OG  SER A  35     7271  10155   6945     97   -742   1110       O
ATOM    384  N   VAL A  36     -47.597  25.268   7.719  1.00 47.32           N
ANISOU  384  N   VAL A  36     5215   7254   5510    207   -564   1151       N
ATOM    385  CA  VAL A  36     -47.508  25.431   9.168  1.00 45.55           C
ANISOU  385  CA  VAL A  36     5018   6822   5465    210   -534   1064       C
ATOM    386  C   VAL A  36     -48.079  26.773   9.612  1.00 47.22           C
ANISOU  386  C   VAL A  36     5185   6933   5824    317   -509   1202       C
ATOM    387  O   VAL A  36     -48.896  26.837  10.534  1.00 44.78           O
ANISOU  387  O   VAL A  36     4844   6575   5593    344   -527   1160       O
ATOM    388  CB  VAL A  36     -46.046  25.263   9.634  1.00 41.85           C
ANISOU  388  CB  VAL A  36     4635   6191   5074    163   -469    968       C
ATOM    389  CG1 VAL A  36     -45.946  25.461  11.136  1.00 37.36           C
ANISOU  389  CG1 VAL A  36     4092   5431   4674    173   -445    874       C
ATOM    390  CG2 VAL A  36     -45.517  23.896   9.244  1.00 39.78           C
ANISOU  390  CG2 VAL A  36     4416   6019   4680     68   -488    826       C
ATOM    391  N   PHE A  37     -47.661  27.864   8.970  1.00 44.06           N
ANISOU  391  N   PHE A  37     4778   6492   5469    382   -460   1371       N
ATOM    392  CA  PHE A  37     -48.110  29.209   9.331  1.00 45.02           C
ANISOU  392  CA  PHE A  37     4861   6490   5754    489   -423   1510       C
ATOM    393  C   PHE A  37     -49.254  29.588   8.397  1.00 47.94           C
ANISOU  393  C   PHE A  37     5141   7048   6026    568   -471   1687       C
ATOM    394  O   PHE A  37     -49.032  30.069   7.283  1.00 45.15           O
ANISOU  394  O   PHE A  37     4771   6783   5601    607   -455   1856       O
ATOM    395  CB  PHE A  37     -46.953  30.203   9.271  1.00 43.87           C
ANISOU  395  CB  PHE A  37     4757   6159   5752    512   -332   1592       C
ATOM    396  CG  PHE A  37     -45.894  29.949  10.309  1.00 40.32           C
ANISOU  396  CG  PHE A  37     4379   5524   5418    445   -293   1416       C
ATOM    397  CD1 PHE A  37     -46.157  30.171  11.650  1.00 39.14           C
ANISOU  397  CD1 PHE A  37     4238   5223   5410    464   -290   1303       C
ATOM    398  CD2 PHE A  37     -44.649  29.463   9.949  1.00 47.17           C
ANISOU  398  CD2 PHE A  37     5299   6382   6240    369   -262   1359       C
ATOM    399  CE1 PHE A  37     -45.194  29.923  12.615  1.00 44.55           C
ANISOU  399  CE1 PHE A  37     4983   5762   6184    409   -264   1140       C
ATOM    400  CE2 PHE A  37     -43.678  29.214  10.910  1.00 45.50           C
ANISOU  400  CE2 PHE A  37     5141   6014   6131    313   -234   1201       C
ATOM    401  CZ  PHE A  37     -43.953  29.443  12.246  1.00 39.75           C
ANISOU  401  CZ  PHE A  37     4421   5146   5536    333   -240   1091       C
ATOM    402  N   THR A  38     -50.484  29.364   8.863  1.00 51.44           N
ANISOU  402  N   THR A  38     5521   7562   6463    594   -530   1656       N
ATOM    403  CA  THR A  38     -51.678  29.549   8.049  1.00 53.31           C
ANISOU  403  CA  THR A  38     5655   8006   6594    661   -595   1801       C
ATOM    404  C   THR A  38     -52.774  30.219   8.878  1.00 53.21           C
ANISOU  404  C   THR A  38     5573   7924   6722    755   -596   1844       C
ATOM    405  O   THR A  38     -52.487  31.158   9.629  1.00 54.33           O
ANISOU  405  O   THR A  38     5741   7844   7056    819   -522   1870       O
ATOM    406  CB  THR A  38     -52.132  28.199   7.475  1.00 51.34           C
ANISOU  406  CB  THR A  38     5378   7998   6130    568   -689   1690       C
ATOM    407  OG1 THR A  38     -53.404  28.339   6.835  1.00 62.60           O
ANISOU  407  OG1 THR A  38     6688   9636   7462    629   -767   1807       O
ATOM    408  CG2 THR A  38     -52.217  27.138   8.568  1.00 43.35           C
ANISOU  408  CG2 THR A  38     4398   6922   5152    472   -706   1464       C
ATOM    409  N   TRP A  39     -54.027  29.756   8.756  1.00 44.82           N
ANISOU  409  N   TRP A  39     4414   7045   5569    765   -677   1844       N
ATOM    410  CA  TRP A  39     -55.108  30.295   9.579  1.00 45.18           C
ANISOU  410  CA  TRP A  39     4385   7039   5743    854   -674   1874       C
ATOM    411  C   TRP A  39     -54.847  30.103  11.069  1.00 46.39           C
ANISOU  411  C   TRP A  39     4598   6989   6037    821   -623   1695       C
ATOM    412  O   TRP A  39     -55.510  30.744  11.893  1.00 56.49           O
ANISOU  412  O   TRP A  39     5837   8174   7452    908   -591   1712       O
ATOM    413  CB  TRP A  39     -56.450  29.660   9.189  1.00 49.31           C
ANISOU  413  CB  TRP A  39     4785   7814   6137    849   -775   1884       C
ATOM    414  CG  TRP A  39     -56.344  28.234   8.729  1.00 51.34           C
ANISOU  414  CG  TRP A  39     5053   8243   6210    706   -850   1737       C
ATOM    415  CD1 TRP A  39     -56.231  27.794   7.442  1.00 48.39           C
ANISOU  415  CD1 TRP A  39     4662   8081   5643    665   -914   1777       C
ATOM    416  CD2 TRP A  39     -56.346  27.062   9.554  1.00 47.79           C
ANISOU  416  CD2 TRP A  39     4635   7765   5759    587   -862   1523       C
ATOM    417  NE1 TRP A  39     -56.155  26.423   7.415  1.00 46.46           N
ANISOU  417  NE1 TRP A  39     4438   7928   5288    525   -967   1585       N
ATOM    418  CE2 TRP A  39     -56.222  25.949   8.699  1.00 44.90           C
ANISOU  418  CE2 TRP A  39     4270   7578   5213    475   -933   1436       C
ATOM    419  CE3 TRP A  39     -56.438  26.847  10.932  1.00 44.64           C
ANISOU  419  CE3 TRP A  39     4263   7208   5491    570   -816   1400       C
ATOM    420  CZ2 TRP A  39     -56.185  24.642   9.176  1.00 42.31           C
ANISOU  420  CZ2 TRP A  39     3969   7253   4854    345   -956   1237       C
ATOM    421  CZ3 TRP A  39     -56.405  25.547  11.403  1.00 44.26           C
ANISOU  421  CZ3 TRP A  39     4240   7179   5397    445   -838   1219       C
ATOM    422  CH2 TRP A  39     -56.276  24.462  10.528  1.00 44.56           C
ANISOU  422  CH2 TRP A  39     4279   7376   5277    333   -905   1142       C
ATOM    423  N   THR A  40     -53.918  29.218  11.428  1.00 43.72           N
ANISOU  423  N   THR A  40     4353   6596   5662    705   -613   1525       N
ATOM    424  CA  THR A  40     -53.337  29.162  12.763  1.00 39.35           C
ANISOU  424  CA  THR A  40     3876   5839   5236    680   -555   1373       C
ATOM    425  C   THR A  40     -51.923  28.622  12.623  1.00 42.01           C
ANISOU  425  C   THR A  40     4318   6108   5535    582   -532   1275       C
ATOM    426  O   THR A  40     -51.492  28.242  11.531  1.00 41.42           O
ANISOU  426  O   THR A  40     4255   6150   5334    534   -558   1318       O
ATOM    427  CB  THR A  40     -54.151  28.287  13.723  1.00 43.99           C
ANISOU  427  CB  THR A  40     4431   6473   5810    641   -582   1238       C
ATOM    428  OG1 THR A  40     -53.734  28.551  15.068  1.00 40.93           O
ANISOU  428  OG1 THR A  40     4104   5893   5556    660   -519   1127       O
ATOM    429  CG2 THR A  40     -53.928  26.808  13.428  1.00 31.36           C
ANISOU  429  CG2 THR A  40     2856   4995   4063    505   -634   1114       C
ATOM    430  N   VAL A  41     -51.192  28.598  13.735  1.00 30.69           N
ANISOU  430  N   VAL A  41     2958   4498   4207    559   -484   1143       N
ATOM    431  CA  VAL A  41     -49.889  27.943  13.757  1.00 55.71           C
ANISOU  431  CA  VAL A  41     6216   7610   7342    464   -468   1031       C
ATOM    432  C   VAL A  41     -50.150  26.452  13.933  1.00 46.67           C
ANISOU  432  C   VAL A  41     5077   6583   6073    367   -518    897       C
ATOM    433  O   VAL A  41     -50.662  26.015  14.968  1.00 43.88           O
ANISOU  433  O   VAL A  41     4715   6205   5751    361   -521    802       O
ATOM    434  CB  VAL A  41     -48.976  28.496  14.859  1.00 46.14           C
ANISOU  434  CB  VAL A  41     5070   6175   6285    477   -406    941       C
ATOM    435  CG1 VAL A  41     -47.664  27.722  14.890  1.00 30.11           C
ANISOU  435  CG1 VAL A  41     3118   4107   4214    381   -396    827       C
ATOM    436  CG2 VAL A  41     -48.695  29.976  14.626  1.00 41.28           C
ANISOU  436  CG2 VAL A  41     4446   5422   5816    563   -351   1070       C
ATOM    437  N   ARG A  42     -49.809  25.677  12.917  1.00 40.84           N
ANISOU  437  N   ARG A  42     4351   5971   5197    294   -551    891       N
ATOM    438  CA  ARG A  42     -50.276  24.304  12.767  1.00 39.23           C
ANISOU  438  CA  ARG A  42     4132   5903   4871    205   -607    788       C
ATOM    439  C   ARG A  42     -49.129  23.347  13.069  1.00 41.32           C
ANISOU  439  C   ARG A  42     4487   6097   5118    116   -585    643       C
ATOM    440  O   ARG A  42     -48.310  23.055  12.193  1.00 49.92           O
ANISOU  440  O   ARG A  42     5613   7226   6128     74   -581    639       O
ATOM    441  CB  ARG A  42     -50.816  24.098  11.358  1.00 39.85           C
ANISOU  441  CB  ARG A  42     4151   6193   4799    191   -668    871       C
ATOM    442  CG  ARG A  42     -51.844  23.006  11.229  1.00 41.12           C
ANISOU  442  CG  ARG A  42     4248   6510   4866    123   -740    794       C
ATOM    443  CD  ARG A  42     -52.567  23.119   9.905  1.00 44.89           C
ANISOU  443  CD  ARG A  42     4642   7208   5205    138   -810    896       C
ATOM    444  NE  ARG A  42     -52.965  21.815   9.382  1.00 49.16           N
ANISOU  444  NE  ARG A  42     5156   7906   5617     29   -880    776       N
ATOM    445  CZ  ARG A  42     -52.309  21.168   8.426  1.00 46.81           C
ANISOU  445  CZ  ARG A  42     4900   7699   5187    -36   -899    714       C
ATOM    446  NH1 ARG A  42     -51.222  21.707   7.893  1.00 47.46           N
ANISOU  446  NH1 ARG A  42     5050   7739   5243     -3   -848    777       N
ATOM    447  NH2 ARG A  42     -52.740  19.985   8.001  1.00 42.82           N
ANISOU  447  NH2 ARG A  42     4365   7323   4580   -137   -963    586       N
ATOM    448  N   LEU A  43     -49.072  22.860  14.306  1.00 31.04           N
ANISOU  448  N   LEU A  43     3214   4695   3883     96   -566    531       N
ATOM    449  CA  LEU A  43     -48.145  21.786  14.630  1.00 30.33           C
ANISOU  449  CA  LEU A  43     3198   4556   3772     16   -552    398       C
ATOM    450  C   LEU A  43     -48.550  20.513  13.893  1.00 41.92           C
ANISOU  450  C   LEU A  43     4648   6164   5117    -73   -600    337       C
ATOM    451  O   LEU A  43     -49.728  20.285  13.601  1.00 49.89           O
ANISOU  451  O   LEU A  43     5581   7294   6080    -84   -648    362       O
ATOM    452  CB  LEU A  43     -48.108  21.535  16.138  1.00 27.40           C
ANISOU  452  CB  LEU A  43     2854   4069   3488     26   -524    309       C
ATOM    453  CG  LEU A  43     -47.508  22.633  17.025  1.00 33.06           C
ANISOU  453  CG  LEU A  43     3602   4634   4326    100   -478    317       C
ATOM    454  CD1 LEU A  43     -47.550  22.220  18.486  1.00 33.93           C
ANISOU  454  CD1 LEU A  43     3736   4673   4483    109   -459    219       C
ATOM    455  CD2 LEU A  43     -46.081  22.984  16.612  1.00 31.04           C
ANISOU  455  CD2 LEU A  43     3404   4296   4096     87   -449    312       C
ATOM    456  N   GLY A  44     -47.561  19.678  13.589  1.00 38.81           N
ANISOU  456  N   GLY A  44     4318   5750   4678   -139   -586    248       N
ATOM    457  CA  GLY A  44     -47.814  18.524  12.757  1.00 36.38           C
ANISOU  457  CA  GLY A  44     4001   5565   4258   -224   -627    176       C
ATOM    458  C   GLY A  44     -48.338  17.329  13.527  1.00 33.53           C
ANISOU  458  C   GLY A  44     3635   5182   3924   -290   -637     67       C
ATOM    459  O   GLY A  44     -48.231  17.245  14.749  1.00 36.83           O
ANISOU  459  O   GLY A  44     4077   5484   4434   -272   -602     39       O
ATOM    460  N   GLY A  45     -48.927  16.401  12.774  1.00 37.95           N
ANISOU  460  N   GLY A  45     4159   5861   4400   -369   -685      6       N
ATOM    461  CA  GLY A  45     -49.323  15.109  13.313  1.00 35.99           C
ANISOU  461  CA  GLY A  45     3908   5583   4183   -451   -688   -105       C
ATOM    462  C   GLY A  45     -50.236  15.225  14.516  1.00 40.87           C
ANISOU  462  C   GLY A  45     4478   6156   4896   -426   -677    -70       C
ATOM    463  O   GLY A  45     -51.178  16.026  14.547  1.00 41.33           O
ANISOU  463  O   GLY A  45     4458   6283   4960   -374   -702     20       O
ATOM    464  N   ASN A  46     -49.950  14.406  15.527  1.00 38.99           N
ANISOU  464  N   ASN A  46     4282   5802   4729   -455   -633   -137       N
ATOM    465  CA  ASN A  46     -50.698  14.388  16.777  1.00 40.78           C
ANISOU  465  CA  ASN A  46     4474   5983   5039   -430   -606   -108       C
ATOM    466  C   ASN A  46     -49.809  14.612  17.992  1.00 41.68           C
ANISOU  466  C   ASN A  46     4663   5957   5216   -367   -544   -110       C
ATOM    467  O   ASN A  46     -50.097  15.492  18.810  1.00 39.83           O
ANISOU  467  O   ASN A  46     4411   5698   5024   -285   -523    -51       O
ATOM    468  CB  ASN A  46     -51.458  13.054  16.909  1.00 48.10           C
ANISOU  468  CB  ASN A  46     5358   6927   5990   -532   -613   -176       C
ATOM    469  CG  ASN A  46     -52.620  12.937  15.929  1.00 50.14           C
ANISOU  469  CG  ASN A  46     5511   7342   6198   -591   -685   -174       C
ATOM    470  OD1 ASN A  46     -53.429  13.856  15.794  1.00 58.40           O
ANISOU  470  OD1 ASN A  46     6479   8481   7229   -534   -715    -85       O
ATOM    471  ND2 ASN A  46     -52.708  11.802  15.245  1.00 42.18           N
ANISOU  471  ND2 ASN A  46     4495   6365   5166   -702   -713   -277       N
ATOM    472  N   ASP A  47     -48.722  13.852  18.122  1.00 45.43           N
ANISOU  472  N   ASP A  47     5218   6345   5698   -399   -515   -182       N
ATOM    473  CA  ASP A  47     -47.891  13.939  19.321  1.00 43.09           C
ANISOU  473  CA  ASP A  47     4984   5934   5454   -341   -465   -189       C
ATOM    474  C   ASP A  47     -47.219  15.294  19.544  1.00 41.05           C
ANISOU  474  C   ASP A  47     4750   5638   5209   -251   -458   -148       C
ATOM    475  O   ASP A  47     -47.034  15.663  20.720  1.00 40.52           O
ANISOU  475  O   ASP A  47     4701   5509   5185   -188   -429   -143       O
ATOM    476  CB  ASP A  47     -46.837  12.827  19.283  1.00 43.63           C
ANISOU  476  CB  ASP A  47     5124   5926   5528   -389   -440   -269       C
ATOM    477  CG  ASP A  47     -47.454  11.461  19.159  1.00 49.27           C
ANISOU  477  CG  ASP A  47     5819   6644   6258   -481   -437   -318       C
ATOM    478  OD1 ASP A  47     -48.474  11.208  19.839  1.00 51.94           O
ANISOU  478  OD1 ASP A  47     6105   6997   6634   -491   -427   -285       O
ATOM    479  OD2 ASP A  47     -46.929  10.648  18.374  1.00 51.78           O
ANISOU  479  OD2 ASP A  47     6169   6948   6557   -544   -440   -392       O
ATOM    480  N   PRO A  48     -46.804  16.047  18.520  1.00 37.68           N
ANISOU  480  N   PRO A  48     4325   5242   4750   -240   -479   -119       N
ATOM    481  CA  PRO A  48     -46.347  17.418  18.789  1.00 35.49           C
ANISOU  481  CA  PRO A  48     4056   4914   4514   -157   -467    -69       C
ATOM    482  C   PRO A  48     -47.344  18.232  19.594  1.00 40.94           C
ANISOU  482  C   PRO A  48     4696   5610   5249    -87   -463    -17       C
ATOM    483  O   PRO A  48     -46.933  19.063  20.412  1.00 49.83           O
ANISOU  483  O   PRO A  48     5843   6658   6433    -18   -439    -19       O
ATOM    484  CB  PRO A  48     -46.142  17.994  17.383  1.00 34.80           C
ANISOU  484  CB  PRO A  48     3956   4890   4378   -165   -488    -17       C
ATOM    485  CG  PRO A  48     -45.762  16.819  16.566  1.00 36.02           C
ANISOU  485  CG  PRO A  48     4135   5088   4462   -248   -498    -83       C
ATOM    486  CD  PRO A  48     -46.567  15.664  17.114  1.00 36.34           C
ANISOU  486  CD  PRO A  48     4158   5144   4507   -301   -506   -138       C
ATOM    487  N   TRP A  49     -48.647  18.001  19.417  1.00 35.61           N
ANISOU  487  N   TRP A  49     3950   5027   4554   -103   -484     20       N
ATOM    488  CA  TRP A  49     -49.629  18.724  20.219  1.00 34.82           C
ANISOU  488  CA  TRP A  49     3796   4937   4499    -30   -472     68       C
ATOM    489  C   TRP A  49     -49.574  18.310  21.687  1.00 35.55           C
ANISOU  489  C   TRP A  49     3915   4969   4624     -5   -429     19       C
ATOM    490  O   TRP A  49     -49.789  19.145  22.575  1.00 39.01           O
ANISOU  490  O   TRP A  49     4344   5373   5103     80   -403     30       O
ATOM    491  CB  TRP A  49     -51.027  18.522  19.635  1.00 25.54           C
ANISOU  491  CB  TRP A  49     2522   3886   3294    -57   -507    122       C
ATOM    492  CG  TRP A  49     -51.152  19.168  18.290  1.00 30.20           C
ANISOU  492  CG  TRP A  49     3078   4555   3842    -52   -551    190       C
ATOM    493  CD1 TRP A  49     -50.786  18.633  17.089  1.00 31.10           C
ANISOU  493  CD1 TRP A  49     3203   4734   3878   -124   -588    172       C
ATOM    494  CD2 TRP A  49     -51.639  20.489  18.009  1.00 32.64           C
ANISOU  494  CD2 TRP A  49     3336   4885   4180     38   -557    292       C
ATOM    495  NE1 TRP A  49     -51.027  19.531  16.077  1.00 30.46           N
ANISOU  495  NE1 TRP A  49     3081   4731   3761    -83   -619    266       N
ATOM    496  CE2 TRP A  49     -51.554  20.677  16.614  1.00 36.71           C
ANISOU  496  CE2 TRP A  49     3833   5490   4625     17   -600    349       C
ATOM    497  CE3 TRP A  49     -52.150  21.525  18.799  1.00 31.46           C
ANISOU  497  CE3 TRP A  49     3155   4689   4110    140   -527    342       C
ATOM    498  CZ2 TRP A  49     -51.961  21.860  15.992  1.00 26.56           C
ANISOU  498  CZ2 TRP A  49     2495   4246   3349     97   -613    472       C
ATOM    499  CZ3 TRP A  49     -52.549  22.696  18.179  1.00 33.73           C
ANISOU  499  CZ3 TRP A  49     3393   5001   4422    217   -538    451       C
ATOM    500  CH2 TRP A  49     -52.451  22.854  16.790  1.00 26.77           C
ANISOU  500  CH2 TRP A  49     2492   4206   3473    197   -580    525       C
ATOM    501  N   TYR A  50     -49.248  17.048  21.975  1.00 28.50           N
ANISOU  501  N   TYR A  50     3056   4060   3711    -70   -417    -35       N
ATOM    502  CA  TYR A  50     -49.104  16.671  23.376  1.00 27.78           C
ANISOU  502  CA  TYR A  50     2994   3922   3639    -35   -373    -64       C
ATOM    503  C   TYR A  50     -47.809  17.214  23.971  1.00 33.96           C
ANISOU  503  C   TYR A  50     3850   4618   4436     21   -361   -111       C
ATOM    504  O   TYR A  50     -47.772  17.565  25.159  1.00 35.99           O
ANISOU  504  O   TYR A  50     4118   4852   4704     92   -334   -128       O
ATOM    505  CB  TYR A  50     -49.178  15.158  23.547  1.00 22.48           C
ANISOU  505  CB  TYR A  50     2334   3250   2958   -114   -356    -89       C
ATOM    506  CG  TYR A  50     -49.365  14.775  24.994  1.00 28.84           C
ANISOU  506  CG  TYR A  50     3148   4037   3774    -69   -304    -83       C
ATOM    507  CD1 TYR A  50     -50.609  14.883  25.604  1.00 24.21           C
ANISOU  507  CD1 TYR A  50     2490   3510   3197    -42   -277    -33       C
ATOM    508  CD2 TYR A  50     -48.291  14.339  25.763  1.00 22.70           C
ANISOU  508  CD2 TYR A  50     2442   3194   2989    -45   -281   -120       C
ATOM    509  CE1 TYR A  50     -50.786  14.548  26.934  1.00 27.16           C
ANISOU  509  CE1 TYR A  50     2870   3883   3566      7   -221    -17       C
ATOM    510  CE2 TYR A  50     -48.456  14.003  27.095  1.00 26.75           C
ANISOU  510  CE2 TYR A  50     2961   3709   3492      7   -233   -103       C
ATOM    511  CZ  TYR A  50     -49.706  14.110  27.677  1.00 30.49           C
ANISOU  511  CZ  TYR A  50     3369   4246   3968     32   -200    -50       C
ATOM    512  OH  TYR A  50     -49.883  13.778  29.003  1.00 27.06           O
ANISOU  512  OH  TYR A  50     2941   3830   3511     90   -144    -24       O
ATOM    513  N   TYR A  51     -46.742  17.301  23.172  1.00 37.22           N
ANISOU  513  N   TYR A  51     4305   4991   4846     -8   -380   -136       N
ATOM    514  CA  TYR A  51     -45.545  17.986  23.654  1.00 37.59           C
ANISOU  514  CA  TYR A  51     4402   4959   4923     41   -374   -179       C
ATOM    515  C   TYR A  51     -45.842  19.454  23.931  1.00 36.24           C
ANISOU  515  C   TYR A  51     4204   4764   4800    120   -373   -158       C
ATOM    516  O   TYR A  51     -45.338  20.029  24.900  1.00 38.14           O
ANISOU  516  O   TYR A  51     4468   4952   5071    179   -362   -208       O
ATOM    517  CB  TYR A  51     -44.402  17.843  22.646  1.00 41.32           C
ANISOU  517  CB  TYR A  51     4910   5399   5391     -7   -388   -198       C
ATOM    518  CG  TYR A  51     -43.449  16.704  22.956  1.00 35.14           C
ANISOU  518  CG  TYR A  51     4177   4582   4592    -40   -376   -256       C
ATOM    519  CD1 TYR A  51     -42.683  16.706  24.114  1.00 32.20           C
ANISOU  519  CD1 TYR A  51     3836   4162   4236      9   -365   -301       C
ATOM    520  CD2 TYR A  51     -43.318  15.627  22.089  1.00 34.68           C
ANISOU  520  CD2 TYR A  51     4131   4543   4501   -115   -377   -268       C
ATOM    521  CE1 TYR A  51     -41.819  15.668  24.400  1.00 31.05           C
ANISOU  521  CE1 TYR A  51     3729   3989   4079    -10   -355   -338       C
ATOM    522  CE2 TYR A  51     -42.454  14.585  22.365  1.00 36.02           C
ANISOU  522  CE2 TYR A  51     4345   4670   4671   -136   -360   -316       C
ATOM    523  CZ  TYR A  51     -41.709  14.611  23.521  1.00 36.93           C
ANISOU  523  CZ  TYR A  51     4487   4738   4807    -80   -348   -341       C
ATOM    524  OH  TYR A  51     -40.849  13.573  23.799  1.00 45.38           O
ANISOU  524  OH  TYR A  51     5594   5768   5879    -89   -331   -374       O
ATOM    525  N   TYR A  52     -46.674  20.069  23.090  1.00 34.83           N
ANISOU  525  N   TYR A  52     3975   4627   4631    124   -386    -88       N
ATOM    526  CA  TYR A  52     -47.119  21.443  23.305  1.00 32.84           C
ANISOU  526  CA  TYR A  52     3691   4346   4441    205   -377    -55       C
ATOM    527  C   TYR A  52     -47.887  21.576  24.621  1.00 34.15           C
ANISOU  527  C   TYR A  52     3837   4524   4615    273   -350    -81       C
ATOM    528  O   TYR A  52     -47.652  22.514  25.395  1.00 33.10           O
ANISOU  528  O   TYR A  52     3715   4328   4533    348   -333   -124       O
ATOM    529  CB  TYR A  52     -47.949  21.865  22.085  1.00 29.29           C
ANISOU  529  CB  TYR A  52     3182   3961   3986    198   -398     45       C
ATOM    530  CG  TYR A  52     -48.944  22.998  22.221  1.00 37.43           C
ANISOU  530  CG  TYR A  52     4153   4997   5074    283   -388    109       C
ATOM    531  CD1 TYR A  52     -48.531  24.300  22.474  1.00 36.25           C
ANISOU  531  CD1 TYR A  52     4015   4742   5017    357   -367    109       C
ATOM    532  CD2 TYR A  52     -50.304  22.771  22.016  1.00 42.23           C
ANISOU  532  CD2 TYR A  52     4683   5710   5653    290   -399    172       C
ATOM    533  CE1 TYR A  52     -49.451  25.334  22.568  1.00 35.74           C
ANISOU  533  CE1 TYR A  52     3894   4668   5016    443   -350    170       C
ATOM    534  CE2 TYR A  52     -51.227  23.795  22.106  1.00 34.80           C
ANISOU  534  CE2 TYR A  52     3678   4776   4768    378   -387    238       C
ATOM    535  CZ  TYR A  52     -50.798  25.072  22.381  1.00 37.30           C
ANISOU  535  CZ  TYR A  52     4016   4980   5178    459   -360    238       C
ATOM    536  OH  TYR A  52     -51.720  26.088  22.467  1.00 37.51           O
ANISOU  536  OH  TYR A  52     3980   5001   5273    555   -341    305       O
ATOM    537  N   ARG A  53     -48.791  20.630  24.898  1.00 29.40           N
ANISOU  537  N   ARG A  53     3201   4004   3964    248   -341    -61       N
ATOM    538  CA  ARG A  53     -49.472  20.575  26.194  1.00 27.89           C
ANISOU  538  CA  ARG A  53     2991   3839   3765    309   -303    -79       C
ATOM    539  C   ARG A  53     -48.471  20.515  27.351  1.00 32.19           C
ANISOU  539  C   ARG A  53     3604   4332   4296    347   -286   -167       C
ATOM    540  O   ARG A  53     -48.558  21.295  28.317  1.00 34.75           O
ANISOU  540  O   ARG A  53     3930   4640   4635    434   -264   -212       O
ATOM    541  CB  ARG A  53     -50.402  19.356  26.224  1.00 26.46           C
ANISOU  541  CB  ARG A  53     2767   3745   3542    251   -291    -38       C
ATOM    542  CG  ARG A  53     -51.226  19.172  27.506  1.00 28.39           C
ANISOU  542  CG  ARG A  53     2979   4036   3770    310   -238    -33       C
ATOM    543  CD  ARG A  53     -50.532  18.284  28.539  1.00 25.46           C
ANISOU  543  CD  ARG A  53     2669   3650   3353    308   -210    -76       C
ATOM    544  NE  ARG A  53     -51.379  17.974  29.689  1.00 28.40           N
ANISOU  544  NE  ARG A  53     3007   4088   3697    358   -151    -51       N
ATOM    545  CZ  ARG A  53     -51.761  18.860  30.607  1.00 34.88           C
ANISOU  545  CZ  ARG A  53     3812   4932   4509    465   -117    -72       C
ATOM    546  NH1 ARG A  53     -51.383  20.127  30.514  1.00 37.32           N
ANISOU  546  NH1 ARG A  53     4138   5187   4854    528   -139   -126       N
ATOM    547  NH2 ARG A  53     -52.532  18.479  31.620  1.00 34.95           N
ANISOU  547  NH2 ARG A  53     3786   5014   4478    509    -55    -41       N
ATOM    548  N   LEU A  54     -47.531  19.567  27.279  1.00 32.02           N
ANISOU  548  N   LEU A  54     3633   4292   4242    287   -298   -197       N
ATOM    549  CA  LEU A  54     -46.551  19.391  28.350  1.00 32.89           C
ANISOU  549  CA  LEU A  54     3797   4371   4326    323   -292   -271       C
ATOM    550  C   LEU A  54     -45.697  20.639  28.538  1.00 35.69           C
ANISOU  550  C   LEU A  54     4175   4652   4733    373   -310   -343       C
ATOM    551  O   LEU A  54     -45.358  21.004  29.668  1.00 31.68           O
ANISOU  551  O   LEU A  54     3686   4141   4211    439   -304   -416       O
ATOM    552  CB  LEU A  54     -45.664  18.181  28.056  1.00 29.34           C
ANISOU  552  CB  LEU A  54     3390   3908   3848    252   -303   -279       C
ATOM    553  CG  LEU A  54     -46.284  16.807  28.331  1.00 31.77           C
ANISOU  553  CG  LEU A  54     3690   4266   4116    213   -273   -232       C
ATOM    554  CD1 LEU A  54     -45.359  15.672  27.887  1.00 26.37           C
ANISOU  554  CD1 LEU A  54     3049   3544   3426    145   -280   -243       C
ATOM    555  CD2 LEU A  54     -46.641  16.671  29.807  1.00 28.67           C
ANISOU  555  CD2 LEU A  54     3297   3919   3679    289   -233   -232       C
ATOM    556  N   ILE A  55     -45.354  21.317  27.443  1.00 37.31           N
ANISOU  556  N   ILE A  55     4374   4801   5000    343   -331   -322       N
ATOM    557  CA  ILE A  55     -44.498  22.494  27.536  1.00 37.54           C
ANISOU  557  CA  ILE A  55     4418   4739   5104    376   -343   -384       C
ATOM    558  C   ILE A  55     -45.269  23.681  28.106  1.00 43.42           C
ANISOU  558  C   ILE A  55     5134   5461   5903    462   -323   -403       C
ATOM    559  O   ILE A  55     -44.715  24.480  28.866  1.00 46.02           O
ANISOU  559  O   ILE A  55     5479   5730   6277    512   -325   -499       O
ATOM    560  CB  ILE A  55     -43.888  22.808  26.159  1.00 34.90           C
ANISOU  560  CB  ILE A  55     4084   4353   4823    316   -359   -336       C
ATOM    561  CG1 ILE A  55     -42.796  21.781  25.824  1.00 30.61           C
ANISOU  561  CG1 ILE A  55     3578   3814   4239    248   -374   -358       C
ATOM    562  CG2 ILE A  55     -43.341  24.228  26.118  1.00 31.58           C
ANISOU  562  CG2 ILE A  55     3659   3826   4513    351   -357   -368       C
ATOM    563  CD1 ILE A  55     -42.615  21.537  24.334  1.00 29.60           C
ANISOU  563  CD1 ILE A  55     3444   3694   4108    179   -379   -287       C
ATOM    564  N   GLU A  56     -46.551  23.819  27.753  1.00 42.81           N
ANISOU  564  N   GLU A  56     5007   5432   5826    483   -304   -320       N
ATOM    565  CA  GLU A  56     -47.385  24.835  28.392  1.00 42.66           C
ANISOU  565  CA  GLU A  56     4955   5398   5854    578   -274   -338       C
ATOM    566  C   GLU A  56     -47.407  24.637  29.902  1.00 43.08           C
ANISOU  566  C   GLU A  56     5029   5493   5847    641   -253   -435       C
ATOM    567  O   GLU A  56     -47.143  25.571  30.677  1.00 47.43           O
ANISOU  567  O   GLU A  56     5592   5989   6441    710   -245   -535       O
ATOM    568  CB  GLU A  56     -48.807  24.787  27.829  1.00 48.05           C
ANISOU  568  CB  GLU A  56     5569   6154   6533    591   -258   -225       C
ATOM    569  CG  GLU A  56     -49.058  25.722  26.660  1.00 58.49           C
ANISOU  569  CG  GLU A  56     6856   7427   7941    598   -267   -139       C
ATOM    570  CD  GLU A  56     -50.437  25.553  26.042  1.00 67.07           C
ANISOU  570  CD  GLU A  56     7863   8611   9008    606   -265    -23       C
ATOM    571  OE1 GLU A  56     -50.948  24.411  26.007  1.00 69.79           O
ANISOU  571  OE1 GLU A  56     8187   9061   9271    551   -273      3       O
ATOM    572  OE2 GLU A  56     -51.004  26.567  25.577  1.00 68.37           O
ANISOU  572  OE2 GLU A  56     7982   8747   9249    667   -256     44       O
ATOM    573  N   ASN A  57     -47.700  23.408  30.333  1.00 36.72           N
ANISOU  573  N   ASN A  57     4227   4785   4941    616   -243   -409       N
ATOM    574  CA  ASN A  57     -47.704  23.111  31.763  1.00 32.04           C
ANISOU  574  CA  ASN A  57     3652   4253   4268    679   -218   -480       C
ATOM    575  C   ASN A  57     -46.344  23.399  32.400  1.00 35.23           C
ANISOU  575  C   ASN A  57     4110   4608   4666    694   -251   -604       C
ATOM    576  O   ASN A  57     -46.269  24.024  33.466  1.00 27.59           O
ANISOU  576  O   ASN A  57     3152   3651   3680    775   -242   -707       O
ATOM    577  CB  ASN A  57     -48.110  21.656  31.981  1.00 32.91           C
ANISOU  577  CB  ASN A  57     3758   4459   4287    638   -197   -407       C
ATOM    578  CG  ASN A  57     -48.316  21.321  33.441  1.00 40.19           C
ANISOU  578  CG  ASN A  57     4690   5466   5115    714   -158   -445       C
ATOM    579  OD1 ASN A  57     -47.372  21.333  34.236  1.00 47.51           O
ANISOU  579  OD1 ASN A  57     5663   6395   5993    747   -176   -532       O
ATOM    580  ND2 ASN A  57     -49.552  21.008  33.803  1.00 35.06           N
ANISOU  580  ND2 ASN A  57     3990   4900   4433    743   -103   -376       N
ATOM    581  N   THR A  58     -45.255  22.960  31.757  1.00 37.51           N
ANISOU  581  N   THR A  58     4430   4852   4971    617   -291   -603       N
ATOM    582  CA  THR A  58     -43.925  23.113  32.344  1.00 38.39           C
ANISOU  582  CA  THR A  58     4579   4931   5076    623   -329   -715       C
ATOM    583  C   THR A  58     -43.537  24.583  32.457  1.00 41.55           C
ANISOU  583  C   THR A  58     4974   5232   5581    660   -343   -818       C
ATOM    584  O   THR A  58     -43.026  25.020  33.496  1.00 38.80           O
ANISOU  584  O   THR A  58     4639   4891   5213    713   -360   -947       O
ATOM    585  CB  THR A  58     -42.887  22.349  31.518  1.00 39.68           C
ANISOU  585  CB  THR A  58     4764   5064   5248    535   -360   -682       C
ATOM    586  OG1 THR A  58     -43.272  20.975  31.405  1.00 43.47           O
ANISOU  586  OG1 THR A  58     5250   5616   5650    499   -342   -594       O
ATOM    587  CG2 THR A  58     -41.511  22.430  32.181  1.00 39.39           C
ANISOU  587  CG2 THR A  58     4752   5010   5203    544   -402   -792       C
ATOM    588  N   ILE A  59     -43.757  25.358  31.391  1.00 39.81           N
ANISOU  588  N   ILE A  59     4732   4920   5475    633   -336   -764       N
ATOM    589  CA  ILE A  59     -43.505  26.792  31.450  1.00 36.48           C
ANISOU  589  CA  ILE A  59     4301   4380   5181    668   -337   -847       C
ATOM    590  C   ILE A  59     -44.283  27.413  32.597  1.00 40.03           C
ANISOU  590  C   ILE A  59     4741   4857   5611    772   -308   -936       C
ATOM    591  O   ILE A  59     -43.768  28.271  33.324  1.00 48.38           O
ANISOU  591  O   ILE A  59     5807   5854   6720    812   -321  -1082       O
ATOM    592  CB  ILE A  59     -43.856  27.459  30.107  1.00 36.11           C
ANISOU  592  CB  ILE A  59     4226   4244   5250    638   -320   -734       C
ATOM    593  CG1 ILE A  59     -42.791  27.150  29.056  1.00 37.00           C
ANISOU  593  CG1 ILE A  59     4351   4312   5397    544   -346   -685       C
ATOM    594  CG2 ILE A  59     -43.986  28.958  30.279  1.00 34.85           C
ANISOU  594  CG2 ILE A  59     4050   3958   5235    697   -300   -797       C
ATOM    595  CD1 ILE A  59     -42.937  27.961  27.781  1.00 37.49           C
ANISOU  595  CD1 ILE A  59     4387   4284   5574    522   -328   -577       C
ATOM    596  N   HIS A  60     -45.526  26.970  32.802  1.00 37.79           N
ANISOU  596  N   HIS A  60     4435   4670   5254    816   -268   -859       N
ATOM    597  CA  HIS A  60     -46.292  27.519  33.915  1.00 45.32           C
ANISOU  597  CA  HIS A  60     5378   5665   6179    923   -229   -942       C
ATOM    598  C   HIS A  60     -45.672  27.148  35.260  1.00 45.22           C
ANISOU  598  C   HIS A  60     5399   5738   6046    962   -248  -1074       C
ATOM    599  O   HIS A  60     -45.658  27.967  36.185  1.00 47.30           O
ANISOU  599  O   HIS A  60     5667   5991   6314   1041   -241  -1218       O
ATOM    600  CB  HIS A  60     -47.746  27.057  33.848  1.00 45.79           C
ANISOU  600  CB  HIS A  60     5393   5822   6184    958   -177   -820       C
ATOM    601  CG  HIS A  60     -48.648  27.791  34.790  1.00 46.48           C
ANISOU  601  CG  HIS A  60     5456   5939   6266   1076   -123   -889       C
ATOM    602  ND1 HIS A  60     -49.166  27.211  35.930  1.00 47.86           N
ANISOU  602  ND1 HIS A  60     5628   6253   6302   1139    -86   -916       N
ATOM    603  CD2 HIS A  60     -49.113  29.062  34.772  1.00 44.87           C
ANISOU  603  CD2 HIS A  60     5228   5641   6180   1149    -94   -937       C
ATOM    604  CE1 HIS A  60     -49.917  28.090  36.568  1.00 44.28           C
ANISOU  604  CE1 HIS A  60     5150   5801   5873   1247    -35   -985       C
ATOM    605  NE2 HIS A  60     -49.903  29.221  35.885  1.00 46.72           N
ANISOU  605  NE2 HIS A  60     5446   5963   6343   1256    -40  -1003       N
ATOM    606  N   ASN A  61     -45.141  25.932  35.391  1.00 40.20           N
ANISOU  606  N   ASN A  61     4786   5188   5301    914   -272  -1032       N
ATOM    607  CA  ASN A  61     -44.629  25.454  36.671  1.00 39.83           C
ANISOU  607  CA  ASN A  61     4766   5250   5117    963   -289  -1127       C
ATOM    608  C   ASN A  61     -43.104  25.372  36.705  1.00 41.09           C
ANISOU  608  C   ASN A  61     4951   5372   5287    913   -360  -1215       C
ATOM    609  O   ASN A  61     -42.544  24.614  37.502  1.00 41.54           O
ANISOU  609  O   ASN A  61     5027   5534   5221    932   -385  -1243       O
ATOM    610  CB  ASN A  61     -45.232  24.093  37.012  1.00 40.48           C
ANISOU  610  CB  ASN A  61     4848   5470   5062    967   -252  -1004       C
ATOM    611  CG  ASN A  61     -46.738  24.119  37.034  1.00 50.21           C
ANISOU  611  CG  ASN A  61     6039   6752   6285   1012   -180   -917       C
ATOM    612  OD1 ASN A  61     -47.345  24.554  38.012  1.00 59.36           O
ANISOU  612  OD1 ASN A  61     7187   7981   7384   1110   -138   -981       O
ATOM    613  ND2 ASN A  61     -47.357  23.658  35.952  1.00 48.34           N
ANISOU  613  ND2 ASN A  61     5774   6489   6104    942   -164   -777       N
ATOM    614  N   PHE A  62     -42.424  26.151  35.868  1.00 40.76           N
ANISOU  614  N   PHE A  62     4903   5188   5394    854   -391  -1250       N
ATOM    615  CA  PHE A  62     -40.976  26.030  35.753  1.00 45.66           C
ANISOU  615  CA  PHE A  62     5535   5773   6042    795   -455  -1315       C
ATOM    616  C   PHE A  62     -40.315  26.226  37.115  1.00 44.61           C
ANISOU  616  C   PHE A  62     5409   5718   5823    857   -500  -1488       C
ATOM    617  O   PHE A  62     -40.722  27.106  37.881  1.00 47.71           O
ANISOU  617  O   PHE A  62     5797   6111   6218    929   -490  -1613       O
ATOM    618  CB  PHE A  62     -40.425  27.049  34.754  1.00 47.72           C
ANISOU  618  CB  PHE A  62     5779   5863   6491    732   -467  -1334       C
ATOM    619  CG  PHE A  62     -39.202  26.574  34.023  1.00 49.55           C
ANISOU  619  CG  PHE A  62     6009   6056   6761    641   -507  -1303       C
ATOM    620  CD1 PHE A  62     -39.309  25.662  32.989  1.00 49.59           C
ANISOU  620  CD1 PHE A  62     6021   6075   6748    580   -489  -1147       C
ATOM    621  CD2 PHE A  62     -37.943  27.031  34.379  1.00 55.48           C
ANISOU  621  CD2 PHE A  62     6747   6763   7568    617   -562  -1438       C
ATOM    622  CE1 PHE A  62     -38.187  25.218  32.318  1.00 49.23           C
ANISOU  622  CE1 PHE A  62     5973   5999   6734    505   -516  -1123       C
ATOM    623  CE2 PHE A  62     -36.815  26.587  33.711  1.00 52.08           C
ANISOU  623  CE2 PHE A  62     6306   6304   7177    539   -592  -1405       C
ATOM    624  CZ  PHE A  62     -36.940  25.680  32.679  1.00 50.59           C
ANISOU  624  CZ  PHE A  62     6129   6130   6965    487   -565  -1245       C
ATOM    625  N   PRO A  63     -39.290  25.425  37.454  1.00 45.24           N
ANISOU  625  N   PRO A  63     5497   5872   5821    836   -552  -1505       N
ATOM    626  CA  PRO A  63     -38.693  24.389  36.602  1.00 40.83           C
ANISOU  626  CA  PRO A  63     4943   5304   5266    758   -562  -1378       C
ATOM    627  C   PRO A  63     -39.331  23.006  36.735  1.00 42.65           C
ANISOU  627  C   PRO A  63     5193   5648   5365    775   -522  -1231       C
ATOM    628  O   PRO A  63     -38.769  22.024  36.242  1.00 36.02           O
ANISOU  628  O   PRO A  63     4362   4814   4512    724   -532  -1146       O
ATOM    629  CB  PRO A  63     -37.252  24.345  37.098  1.00 33.56           C
ANISOU  629  CB  PRO A  63     4010   4410   4331    747   -639  -1492       C
ATOM    630  CG  PRO A  63     -37.388  24.611  38.563  1.00 34.50           C
ANISOU  630  CG  PRO A  63     4132   4651   4324    846   -662  -1626       C
ATOM    631  CD  PRO A  63     -38.552  25.568  38.723  1.00 39.34           C
ANISOU  631  CD  PRO A  63     4748   5222   4978    894   -610  -1669       C
ATOM    632  N   HIS A  64     -40.486  22.927  37.387  1.00 45.69           N
ANISOU  632  N   HIS A  64     5582   6114   5664    845   -472  -1203       N
ATOM    633  CA  HIS A  64     -41.090  21.632  37.649  1.00 48.92           C
ANISOU  633  CA  HIS A  64     6003   6628   5958    862   -428  -1067       C
ATOM    634  C   HIS A  64     -41.868  21.138  36.431  1.00 48.34           C
ANISOU  634  C   HIS A  64     5920   6490   5955    786   -382   -918       C
ATOM    635  O   HIS A  64     -42.150  21.881  35.487  1.00 52.73           O
ANISOU  635  O   HIS A  64     6462   6947   6628    743   -379   -913       O
ATOM    636  CB  HIS A  64     -41.981  21.707  38.885  1.00 53.16           C
ANISOU  636  CB  HIS A  64     6538   7292   6368    968   -385  -1091       C
ATOM    637  CG  HIS A  64     -41.222  21.965  40.148  1.00 58.61           C
ANISOU  637  CG  HIS A  64     7237   8085   6946   1048   -433  -1231       C
ATOM    638  ND1 HIS A  64     -41.234  23.185  40.790  1.00 61.75           N
ANISOU  638  ND1 HIS A  64     7628   8484   7350   1107   -453  -1405       N
ATOM    639  CD2 HIS A  64     -40.409  21.165  40.877  1.00 59.11           C
ANISOU  639  CD2 HIS A  64     7312   8257   6888   1080   -470  -1228       C
ATOM    640  CE1 HIS A  64     -40.472  23.121  41.866  1.00 62.85           C
ANISOU  640  CE1 HIS A  64     7774   8742   7366   1169   -506  -1514       C
ATOM    641  NE2 HIS A  64     -39.960  21.906  41.943  1.00 62.55           N
ANISOU  641  NE2 HIS A  64     7745   8778   7245   1157   -519  -1401       N
ATOM    642  N   ARG A  65     -42.215  19.855  36.462  1.00 45.30           N
ANISOU  642  N   ARG A  65     5544   6167   5502    772   -348   -796       N
ATOM    643  CA  ARG A  65     -42.802  19.189  35.310  1.00 40.23           C
ANISOU  643  CA  ARG A  65     4892   5473   4919    688   -317   -671       C
ATOM    644  C   ARG A  65     -43.619  18.003  35.799  1.00 38.48           C
ANISOU  644  C   ARG A  65     4667   5337   4615    702   -258   -557       C
ATOM    645  O   ARG A  65     -43.220  17.325  36.748  1.00 45.94           O
ANISOU  645  O   ARG A  65     5630   6359   5464    753   -252   -545       O
ATOM    646  CB  ARG A  65     -41.705  18.743  34.336  1.00 40.18           C
ANISOU  646  CB  ARG A  65     4902   5389   4975    605   -356   -661       C
ATOM    647  CG  ARG A  65     -42.120  17.693  33.336  1.00 42.49           C
ANISOU  647  CG  ARG A  65     5195   5655   5295    523   -327   -546       C
ATOM    648  CD  ARG A  65     -41.027  16.653  33.161  1.00 43.30           C
ANISOU  648  CD  ARG A  65     5324   5740   5388    489   -344   -528       C
ATOM    649  NE  ARG A  65     -40.985  16.138  31.796  1.00 44.87           N
ANISOU  649  NE  ARG A  65     5524   5870   5653    394   -339   -478       N
ATOM    650  CZ  ARG A  65     -41.839  15.250  31.301  1.00 40.79           C
ANISOU  650  CZ  ARG A  65     5002   5357   5140    343   -301   -395       C
ATOM    651  NH1 ARG A  65     -42.813  14.763  32.059  1.00 40.53           N
ANISOU  651  NH1 ARG A  65     4956   5384   5061    374   -257   -336       N
ATOM    652  NH2 ARG A  65     -41.721  14.850  30.044  1.00 40.94           N
ANISOU  652  NH2 ARG A  65     5022   5323   5209    259   -304   -374       N
ATOM    653  N   ILE A  66     -44.764  17.765  35.156  1.00 36.99           N
ANISOU  653  N   ILE A  66     4447   5139   4467    659   -214   -467       N
ATOM    654  CA  ILE A  66     -45.640  16.665  35.547  1.00 35.92           C
ANISOU  654  CA  ILE A  66     4296   5071   4281    657   -150   -353       C
ATOM    655  C   ILE A  66     -45.113  15.361  34.970  1.00 34.81           C
ANISOU  655  C   ILE A  66     4177   4884   4164    577   -152   -282       C
ATOM    656  O   ILE A  66     -44.434  15.336  33.937  1.00 33.85           O
ANISOU  656  O   ILE A  66     4071   4681   4110    507   -193   -306       O
ATOM    657  CB  ILE A  66     -47.093  16.911  35.092  1.00 30.75           C
ANISOU  657  CB  ILE A  66     3584   4428   3670    637   -106   -291       C
ATOM    658  CG1 ILE A  66     -47.176  16.877  33.565  1.00 34.06           C
ANISOU  658  CG1 ILE A  66     3988   4764   4190    531   -138   -265       C
ATOM    659  CG2 ILE A  66     -47.632  18.223  35.645  1.00 26.40           C
ANISOU  659  CG2 ILE A  66     3009   3911   3110    726    -97   -363       C
ATOM    660  CD1 ILE A  66     -48.550  16.535  33.041  1.00 39.31           C
ANISOU  660  CD1 ILE A  66     4589   5458   4889    484    -99   -174       C
ATOM    661  N   TRP A  67     -45.439  14.262  35.647  1.00 37.82           N
ANISOU  661  N   TRP A  67     4559   5317   4493    593    -97   -190       N
ATOM    662  CA  TRP A  67     -45.167  12.925  35.143  1.00 39.62           C
ANISOU  662  CA  TRP A  67     4802   5489   4761    518    -80   -112       C
ATOM    663  C   TRP A  67     -46.426  12.076  35.055  1.00 48.25           C
ANISOU  663  C   TRP A  67     5854   6593   5885    468     -8      0       C
ATOM    664  O   TRP A  67     -46.347  10.903  34.672  1.00 52.63           O
ANISOU  664  O   TRP A  67     6417   7090   6490    401     17     65       O
ATOM    665  CB  TRP A  67     -44.111  12.237  36.018  1.00 36.92           C
ANISOU  665  CB  TRP A  67     4503   5173   4353    579    -83    -96       C
ATOM    666  CG  TRP A  67     -42.841  13.027  36.072  1.00 36.56           C
ANISOU  666  CG  TRP A  67     4483   5119   4288    616   -160   -212       C
ATOM    667  CD1 TRP A  67     -42.499  13.968  37.000  1.00 35.55           C
ANISOU  667  CD1 TRP A  67     4357   5069   4081    708   -193   -300       C
ATOM    668  CD2 TRP A  67     -41.754  12.969  35.140  1.00 30.36           C
ANISOU  668  CD2 TRP A  67     3718   4245   3572    557   -212   -263       C
ATOM    669  NE1 TRP A  67     -41.266  14.495  36.708  1.00 32.85           N
ANISOU  669  NE1 TRP A  67     4030   4685   3766    701   -266   -401       N
ATOM    670  CE2 TRP A  67     -40.784  13.896  35.572  1.00 35.54           C
ANISOU  670  CE2 TRP A  67     4381   4927   4197    612   -275   -372       C
ATOM    671  CE3 TRP A  67     -41.505  12.220  33.986  1.00 31.28           C
ANISOU  671  CE3 TRP A  67     3845   4268   3774    463   -209   -233       C
ATOM    672  CZ2 TRP A  67     -39.580  14.091  34.894  1.00 35.84           C
ANISOU  672  CZ2 TRP A  67     4427   4897   4292    575   -330   -438       C
ATOM    673  CZ3 TRP A  67     -40.307  12.418  33.311  1.00 37.71           C
ANISOU  673  CZ3 TRP A  67     4674   5022   4631    436   -260   -301       C
ATOM    674  CH2 TRP A  67     -39.362  13.348  33.767  1.00 34.09           C
ANISOU  674  CH2 TRP A  67     4215   4590   4147    490   -317   -394       C
ATOM    675  N   PHE A  68     -47.582  12.643  35.390  1.00 51.32           N
ANISOU  675  N   PHE A  68     6193   7049   6257    499     28     20       N
ATOM    676  CA  PHE A  68     -48.877  12.001  35.236  1.00 48.54           C
ANISOU  676  CA  PHE A  68     5780   6714   5948    444     93    119       C
ATOM    677  C   PHE A  68     -49.869  13.062  34.790  1.00 49.20           C
ANISOU  677  C   PHE A  68     5804   6829   6061    445     83     89       C
ATOM    678  O   PHE A  68     -49.823  14.201  35.264  1.00 43.62           O
ANISOU  678  O   PHE A  68     5100   6165   5308    533     68     21       O
ATOM    679  CB  PHE A  68     -49.336  11.349  36.543  1.00 48.94           C
ANISOU  679  CB  PHE A  68     5819   6848   5928    513    180    220       C
ATOM    680  CG  PHE A  68     -50.648  10.618  36.441  1.00 48.72           C
ANISOU  680  CG  PHE A  68     5718   6832   5961    448    257    331       C
ATOM    681  CD1 PHE A  68     -50.695   9.309  35.985  1.00 43.09           C
ANISOU  681  CD1 PHE A  68     5000   6037   5334    348    287    407       C
ATOM    682  CD2 PHE A  68     -51.831  11.229  36.836  1.00 49.31           C
ANISOU  682  CD2 PHE A  68     5722   6998   6016    490    303    356       C
ATOM    683  CE1 PHE A  68     -51.892   8.630  35.907  1.00 40.14           C
ANISOU  683  CE1 PHE A  68     4550   5668   5032    278    357    502       C
ATOM    684  CE2 PHE A  68     -53.038  10.555  36.761  1.00 43.73           C
ANISOU  684  CE2 PHE A  68     4934   6308   5374    426    375    461       C
ATOM    685  CZ  PHE A  68     -53.069   9.256  36.295  1.00 44.85           C
ANISOU  685  CZ  PHE A  68     5068   6365   5608    315    400    532       C
ATOM    686  N   ASP A  69     -50.760  12.689  33.877  1.00 50.63           N
ANISOU  686  N   ASP A  69     5925   6989   6322    349     90    134       N
ATOM    687  CA  ASP A  69     -51.678  13.639  33.253  1.00 43.09           C
ANISOU  687  CA  ASP A  69     4904   6062   5404    343     70    117       C
ATOM    688  C   ASP A  69     -53.104  13.134  33.401  1.00 43.56           C
ANISOU  688  C   ASP A  69     4870   6184   5496    311    135    211       C
ATOM    689  O   ASP A  69     -53.557  12.308  32.588  1.00 47.66           O
ANISOU  689  O   ASP A  69     5347   6673   6086    196    130    250       O
ATOM    690  CB  ASP A  69     -51.323  13.842  31.787  1.00 39.49           C
ANISOU  690  CB  ASP A  69     4456   5539   5011    256     -6     71       C
ATOM    691  CG  ASP A  69     -52.126  14.944  31.139  1.00 38.42           C
ANISOU  691  CG  ASP A  69     4257   5435   4907    270    -34     62       C
ATOM    692  OD1 ASP A  69     -52.844  15.667  31.860  1.00 37.39           O
ANISOU  692  OD1 ASP A  69     4084   5365   4757    357      3     74       O
ATOM    693  OD2 ASP A  69     -52.033  15.089  29.902  1.00 39.24           O
ANISOU  693  OD2 ASP A  69     4352   5508   5051    202    -91     47       O
ATOM    694  N   PRO A  70     -53.844  13.602  34.412  1.00 41.77           N
ANISOU  694  N   PRO A  70     4602   6047   5222    405    198    243       N
ATOM    695  CA  PRO A  70     -55.252  13.191  34.548  1.00 43.45           C
ANISOU  695  CA  PRO A  70     4708   6327   5475    376    266    338       C
ATOM    696  C   PRO A  70     -56.149  13.707  33.439  1.00 41.36           C
ANISOU  696  C   PRO A  70     4355   6074   5287    320    222    334       C
ATOM    697  O   PRO A  70     -57.281  13.222  33.318  1.00 42.89           O
ANISOU  697  O   PRO A  70     4447   6316   5533    265    263    408       O
ATOM    698  CB  PRO A  70     -55.667  13.778  35.907  1.00 42.60           C
ANISOU  698  CB  PRO A  70     4586   6321   5279    515    342    354       C
ATOM    699  CG  PRO A  70     -54.377  14.103  36.610  1.00 42.78           C
ANISOU  699  CG  PRO A  70     4717   6329   5207    600    316    276       C
ATOM    700  CD  PRO A  70     -53.412  14.459  35.525  1.00 39.98           C
ANISOU  700  CD  PRO A  70     4420   5871   4901    543    214    188       C
ATOM    701  N   PHE A  71     -55.691  14.668  32.630  1.00 37.40           N
ANISOU  701  N   PHE A  71     3880   5534   4794    332    142    258       N
ATOM    702  CA  PHE A  71     -56.552  15.226  31.592  1.00 41.15           C
ANISOU  702  CA  PHE A  71     4268   6037   5331    297     99    269       C
ATOM    703  C   PHE A  71     -56.854  14.202  30.507  1.00 43.58           C
ANISOU  703  C   PHE A  71     4532   6329   5699    147     62    296       C
ATOM    704  O   PHE A  71     -57.977  14.143  29.997  1.00 48.05           O
ANISOU  704  O   PHE A  71     4985   6959   6313    100     56    341       O
ATOM    705  CB  PHE A  71     -55.905  16.460  30.974  1.00 38.55           C
ANISOU  705  CB  PHE A  71     3984   5662   5001    348     29    198       C
ATOM    706  CG  PHE A  71     -56.576  17.753  31.337  1.00 43.75           C
ANISOU  706  CG  PHE A  71     4593   6364   5667    466     51    195       C
ATOM    707  CD1 PHE A  71     -56.325  18.355  32.558  1.00 46.53           C
ANISOU  707  CD1 PHE A  71     4987   6725   5969    587    102    149       C
ATOM    708  CD2 PHE A  71     -57.438  18.380  30.449  1.00 27.39           C
ANISOU  708  CD2 PHE A  71     2431   4327   3650    463     18    233       C
ATOM    709  CE1 PHE A  71     -56.927  19.552  32.893  1.00 51.19           C
ANISOU  709  CE1 PHE A  71     5533   7342   6575    700    127    131       C
ATOM    710  CE2 PHE A  71     -58.044  19.582  30.777  1.00 28.05           C
ANISOU  710  CE2 PHE A  71     2468   4437   3755    583     44    234       C
ATOM    711  CZ  PHE A  71     -57.791  20.166  32.005  1.00 54.49           C
ANISOU  711  CZ  PHE A  71     5862   7777   7064    700    102    177       C
ATOM    712  N   THR A  72     -55.872  13.398  30.133  1.00 31.90           N
ANISOU  712  N   THR A  72     3133   4770   4219     73     33    261       N
ATOM    713  CA  THR A  72     -56.030  12.456  29.039  1.00 32.34           C
ANISOU  713  CA  THR A  72     3159   4800   4330    -69     -8    257       C
ATOM    714  C   THR A  72     -56.323  11.065  29.594  1.00 40.91           C
ANISOU  714  C   THR A  72     4227   5860   5459   -142     62    309       C
ATOM    715  O   THR A  72     -56.140  10.797  30.783  1.00 27.42           O
ANISOU  715  O   THR A  72     2551   4147   3721    -77    137    354       O
ATOM    716  CB  THR A  72     -54.778  12.454  28.156  1.00 31.79           C
ANISOU  716  CB  THR A  72     3184   4651   4242   -105    -78    179       C
ATOM    717  OG1 THR A  72     -55.042  11.770  26.923  1.00 34.16           O
ANISOU  717  OG1 THR A  72     3447   4951   4583   -233   -129    156       O
ATOM    718  CG2 THR A  72     -53.608  11.798  28.879  1.00 29.92           C
ANISOU  718  CG2 THR A  72     3053   4333   3982    -87    -44    160       C
ATOM    719  N   TYR A  73     -56.817  10.186  28.718  1.00 39.13           N
ANISOU  719  N   TYR A  73     3943   5621   5304   -277     37    304       N
ATOM    720  CA  TYR A  73     -57.222   8.832  29.104  1.00 39.75           C
ANISOU  720  CA  TYR A  73     3987   5657   5458   -367    106    355       C
ATOM    721  C   TYR A  73     -58.329   8.881  30.163  1.00 40.65           C
ANISOU  721  C   TYR A  73     4007   5850   5588   -319    197    459       C
ATOM    722  O   TYR A  73     -58.304   8.165  31.168  1.00 35.77           O
ANISOU  722  O   TYR A  73     3404   5203   4983   -303    290    533       O
ATOM    723  CB  TYR A  73     -56.014   8.013  29.580  1.00 30.78           C
ANISOU  723  CB  TYR A  73     2971   4407   4316   -362    140    347       C
ATOM    724  CG  TYR A  73     -56.294   6.545  29.813  1.00 35.60           C
ANISOU  724  CG  TYR A  73     3559   4940   5028   -463    210    399       C
ATOM    725  CD1 TYR A  73     -57.381   5.911  29.213  1.00 39.56           C
ANISOU  725  CD1 TYR A  73     3946   5450   5633   -595    210    405       C
ATOM    726  CD2 TYR A  73     -55.477   5.794  30.645  1.00 36.87           C
ANISOU  726  CD2 TYR A  73     3805   5017   5189   -427    276    446       C
ATOM    727  CE1 TYR A  73     -57.640   4.568  29.437  1.00 38.62           C
ANISOU  727  CE1 TYR A  73     3803   5240   5632   -695    280    451       C
ATOM    728  CE2 TYR A  73     -55.729   4.453  30.874  1.00 40.18           C
ANISOU  728  CE2 TYR A  73     4202   5345   5718   -515    350    508       C
ATOM    729  CZ  TYR A  73     -56.804   3.843  30.269  1.00 39.65           C
ANISOU  729  CZ  TYR A  73     4025   5269   5769   -652    355    508       C
ATOM    730  OH  TYR A  73     -57.030   2.506  30.509  1.00 43.99           O
ANISOU  730  OH  TYR A  73     4554   5709   6452   -746    435    567       O
ATOM    731  N   TYR A  74     -59.316   9.739  29.919  1.00 47.34           N
ANISOU  731  N   TYR A  74     4751   6803   6434   -290    175    472       N
ATOM    732  CA  TYR A  74     -60.403   9.924  30.869  1.00 44.08           C
ANISOU  732  CA  TYR A  74     4238   6480   6031   -233    264    566       C
ATOM    733  C   TYR A  74     -61.179   8.620  31.045  1.00 42.58           C
ANISOU  733  C   TYR A  74     3958   6271   5948   -355    334    638       C
ATOM    734  O   TYR A  74     -61.417   7.904  30.065  1.00 44.55           O
ANISOU  734  O   TYR A  74     4161   6484   6283   -500    281    598       O
ATOM    735  CB  TYR A  74     -61.342  11.034  30.391  1.00 45.43           C
ANISOU  735  CB  TYR A  74     4300   6761   6199   -187    220    565       C
ATOM    736  CG  TYR A  74     -62.356  11.462  31.426  1.00 38.93           C
ANISOU  736  CG  TYR A  74     3382   6039   5371    -93    316    650       C
ATOM    737  CD1 TYR A  74     -62.018  12.368  32.422  1.00 35.83           C
ANISOU  737  CD1 TYR A  74     3051   5673   4889     69    365    650       C
ATOM    738  CD2 TYR A  74     -63.645  10.953  31.413  1.00 33.80           C
ANISOU  738  CD2 TYR A  74     2575   5460   4808   -166    360    724       C
ATOM    739  CE1 TYR A  74     -62.939  12.757  33.375  1.00 33.18           C
ANISOU  739  CE1 TYR A  74     2630   5436   4539    164    461    719       C
ATOM    740  CE2 TYR A  74     -64.575  11.339  32.362  1.00 36.40           C
ANISOU  740  CE2 TYR A  74     2810   5889   5132    -74    458    806       C
ATOM    741  CZ  TYR A  74     -64.215  12.241  33.339  1.00 37.61           C
ANISOU  741  CZ  TYR A  74     3035   6071   5185     95    511    803       C
ATOM    742  OH  TYR A  74     -65.139  12.624  34.286  1.00 39.01           O
ANISOU  742  OH  TYR A  74     3119   6355   5347    194    616    876       O
ATOM    743  N   PRO A  75     -61.597   8.279  32.279  1.00 41.41           N
ANISOU  743  N   PRO A  75     3781   6152   5801   -304    455    744       N
ATOM    744  CA  PRO A  75     -61.347   9.026  33.517  1.00 43.71           C
ANISOU  744  CA  PRO A  75     4125   6503   5979   -133    524    784       C
ATOM    745  C   PRO A  75     -60.211   8.495  34.403  1.00 46.83           C
ANISOU  745  C   PRO A  75     4656   6829   6308    -76    575    806       C
ATOM    746  O   PRO A  75     -60.313   8.627  35.623  1.00 51.14           O
ANISOU  746  O   PRO A  75     5210   7441   6780     34    668    880       O
ATOM    747  CB  PRO A  75     -62.677   8.886  34.255  1.00 43.45           C
ANISOU  747  CB  PRO A  75     3950   6571   5986   -119    634    899       C
ATOM    748  CG  PRO A  75     -63.124   7.509  33.896  1.00 35.62           C
ANISOU  748  CG  PRO A  75     2890   5510   5134   -289    665    953       C
ATOM    749  CD  PRO A  75     -62.611   7.229  32.491  1.00 39.43           C
ANISOU  749  CD  PRO A  75     3408   5903   5671   -414    536    836       C
ATOM    750  N   TYR A  76     -59.155   7.918  33.823  1.00 41.84           N
ANISOU  750  N   TYR A  76     4123   6079   5695   -141    516    747       N
ATOM    751  CA  TYR A  76     -58.068   7.348  34.613  1.00 40.77           C
ANISOU  751  CA  TYR A  76     4106   5880   5507    -87    558    776       C
ATOM    752  C   TYR A  76     -56.795   8.178  34.614  1.00 39.65           C
ANISOU  752  C   TYR A  76     4087   5724   5256     11    482    677       C
ATOM    753  O   TYR A  76     -56.034   8.119  35.584  1.00 35.10           O
ANISOU  753  O   TYR A  76     3589   5155   4592    109    520    703       O
ATOM    754  CB  TYR A  76     -57.722   5.940  34.114  1.00 39.82           C
ANISOU  754  CB  TYR A  76     4008   5621   5502   -223    567    794       C
ATOM    755  CG  TYR A  76     -58.924   5.045  33.973  1.00 45.59           C
ANISOU  755  CG  TYR A  76     4612   6339   6372   -348    633    874       C
ATOM    756  CD1 TYR A  76     -59.460   4.392  35.076  1.00 46.62           C
ANISOU  756  CD1 TYR A  76     4697   6488   6528   -326    767   1025       C
ATOM    757  CD2 TYR A  76     -59.528   4.859  32.740  1.00 48.02           C
ANISOU  757  CD2 TYR A  76     4839   6623   6784   -491    563    801       C
ATOM    758  CE1 TYR A  76     -60.560   3.576  34.952  1.00 55.37           C
ANISOU  758  CE1 TYR A  76     5679   7576   7783   -450    833   1101       C
ATOM    759  CE2 TYR A  76     -60.628   4.043  32.605  1.00 55.49           C
ANISOU  759  CE2 TYR A  76     5657   7557   7869   -616    616    861       C
ATOM    760  CZ  TYR A  76     -61.143   3.404  33.714  1.00 59.03           C
ANISOU  760  CZ  TYR A  76     6058   8008   8361   -600    754   1012       C
ATOM    761  OH  TYR A  76     -62.245   2.591  33.583  1.00 61.95           O
ANISOU  761  OH  TYR A  76     6291   8360   8889   -735    814   1076       O
ATOM    762  N   GLY A  77     -56.531   8.940  33.559  1.00 39.04           N
ANISOU  762  N   GLY A  77     4022   5632   5181    -13    378    568       N
ATOM    763  CA  GLY A  77     -55.253   9.611  33.469  1.00 40.13           C
ANISOU  763  CA  GLY A  77     4271   5736   5242     57    309    476       C
ATOM    764  C   GLY A  77     -54.167   8.631  33.088  1.00 39.80           C
ANISOU  764  C   GLY A  77     4313   5578   5232     -9    287    453       C
ATOM    765  O   GLY A  77     -54.262   7.437  33.393  1.00 43.95           O
ANISOU  765  O   GLY A  77     4834   6050   5815    -63    351    529       O
ATOM    766  N   SER A  78     -53.134   9.112  32.413  1.00 36.82           N
ANISOU  766  N   SER A  78     4008   5152   4829     -3    204    355       N
ATOM    767  CA  SER A  78     -52.064   8.248  31.951  1.00 39.24           C
ANISOU  767  CA  SER A  78     4391   5351   5169    -59    180    323       C
ATOM    768  C   SER A  78     -50.718   8.850  32.324  1.00 37.11           C
ANISOU  768  C   SER A  78     4214   5070   4816     38    141    264       C
ATOM    769  O   SER A  78     -50.567  10.072  32.421  1.00 37.23           O
ANISOU  769  O   SER A  78     4236   5138   4772    112    101    210       O
ATOM    770  CB  SER A  78     -52.144   8.025  30.439  1.00 43.16           C
ANISOU  770  CB  SER A  78     4868   5795   5737   -185    114    251       C
ATOM    771  OG  SER A  78     -51.820   9.212  29.747  1.00 49.75           O
ANISOU  771  OG  SER A  78     5716   6662   6525   -153     35    173       O
ATOM    772  N   TYR A  79     -49.745   7.970  32.541  1.00 40.42           N
ANISOU  772  N   TYR A  79     4700   5415   5244     37    155    276       N
ATOM    773  CA  TYR A  79     -48.389   8.397  32.855  1.00 35.31           C
ANISOU  773  CA  TYR A  79     4130   4758   4529    119    113    220       C
ATOM    774  C   TYR A  79     -47.711   8.949  31.605  1.00 38.05           C
ANISOU  774  C   TYR A  79     4502   5056   4900     70     30    112       C
ATOM    775  O   TYR A  79     -47.942   8.469  30.491  1.00 43.41           O
ANISOU  775  O   TYR A  79     5165   5682   5648    -36     13     88       O
ATOM    776  CB  TYR A  79     -47.594   7.224  33.433  1.00 33.49           C
ANISOU  776  CB  TYR A  79     3950   4466   4307    138    156    281       C
ATOM    777  CG  TYR A  79     -48.098   6.756  34.784  1.00 26.10           C
ANISOU  777  CG  TYR A  79     2997   3594   3327    211    243    405       C
ATOM    778  CD1 TYR A  79     -47.624   7.329  35.959  1.00 26.30           C
ANISOU  778  CD1 TYR A  79     3049   3716   3226    345    244    415       C
ATOM    779  CD2 TYR A  79     -49.048   5.743  34.885  1.00 30.80           C
ANISOU  779  CD2 TYR A  79     3544   4154   4003    144    325    511       C
ATOM    780  CE1 TYR A  79     -48.078   6.909  37.198  1.00 35.38           C
ANISOU  780  CE1 TYR A  79     4184   4944   4314    421    328    535       C
ATOM    781  CE2 TYR A  79     -49.515   5.315  36.125  1.00 30.78           C
ANISOU  781  CE2 TYR A  79     3522   4215   3957    214    417    644       C
ATOM    782  CZ  TYR A  79     -49.024   5.903  37.276  1.00 35.47           C
ANISOU  782  CZ  TYR A  79     4149   4921   4407    358    419    659       C
ATOM    783  OH  TYR A  79     -49.480   5.487  38.506  1.00 42.05           O
ANISOU  783  OH  TYR A  79     4963   5837   5177    436    514    797       O
ATOM    784  N   THR A  80     -46.882   9.975  31.788  1.00 38.04           N
ANISOU  784  N   THR A  80     4535   5078   4839    145    -20     45       N
ATOM    785  CA  THR A  80     -46.250  10.664  30.667  1.00 38.29           C
ANISOU  785  CA  THR A  80     4585   5073   4891    109    -89    -42       C
ATOM    786  C   THR A  80     -44.907  10.017  30.357  1.00 38.32           C
ANISOU  786  C   THR A  80     4648   5001   4911     94   -106    -77       C
ATOM    787  O   THR A  80     -43.989  10.053  31.183  1.00 39.05           O
ANISOU  787  O   THR A  80     4776   5100   4960    171   -110    -84       O
ATOM    788  CB  THR A  80     -46.061  12.149  30.972  1.00 34.81           C
ANISOU  788  CB  THR A  80     4143   4678   4406    188   -127    -98       C
ATOM    789  OG1 THR A  80     -45.088  12.302  32.013  1.00 44.17           O
ANISOU  789  OG1 THR A  80     5370   5878   5533    277   -132   -124       O
ATOM    790  CG2 THR A  80     -47.365  12.772  31.413  1.00 25.76           C
ANISOU  790  CG2 THR A  80     2937   3606   3244    224    -99    -63       C
ATOM    791  N   HIS A  81     -44.790   9.434  29.164  1.00 41.82           N
ANISOU  791  N   HIS A  81     5095   5383   5410     -1   -119   -104       N
ATOM    792  CA  HIS A  81     -43.537   8.837  28.725  1.00 34.55           C
ANISOU  792  CA  HIS A  81     4225   4389   4512    -16   -130   -144       C
ATOM    793  C   HIS A  81     -42.694   9.781  27.878  1.00 39.48           C
ANISOU  793  C   HIS A  81     4864   5011   5126    -18   -187   -222       C
ATOM    794  O   HIS A  81     -41.533   9.461  27.596  1.00 55.94           O
ANISOU  794  O   HIS A  81     6984   7046   7223    -14   -196   -259       O
ATOM    795  CB  HIS A  81     -43.807   7.541  27.949  1.00 29.46           C
ANISOU  795  CB  HIS A  81     3583   3673   3940   -115   -100   -141       C
ATOM    796  CG  HIS A  81     -44.318   7.754  26.557  1.00 38.52           C
ANISOU  796  CG  HIS A  81     4703   4829   5105   -209   -135   -197       C
ATOM    797  ND1 HIS A  81     -45.659   7.903  26.271  1.00 44.25           N
ANISOU  797  ND1 HIS A  81     5366   5607   5840   -262   -138   -175       N
ATOM    798  CD2 HIS A  81     -43.671   7.822  25.370  1.00 43.66           C
ANISOU  798  CD2 HIS A  81     5373   5458   5757   -254   -169   -270       C
ATOM    799  CE1 HIS A  81     -45.814   8.063  24.969  1.00 45.22           C
ANISOU  799  CE1 HIS A  81     5473   5746   5963   -335   -180   -233       C
ATOM    800  NE2 HIS A  81     -44.623   8.017  24.399  1.00 41.24           N
ANISOU  800  NE2 HIS A  81     5021   5199   5449   -331   -196   -291       N
ATOM    801  N   PHE A  82     -43.243  10.927  27.476  1.00 33.44           N
ANISOU  801  N   PHE A  82     4067   4294   4345    -18   -219   -238       N
ATOM    802  CA  PHE A  82     -42.480  11.915  26.724  1.00 29.52           C
ANISOU  802  CA  PHE A  82     3579   3790   3848    -16   -263   -292       C
ATOM    803  C   PHE A  82     -41.339  12.447  27.577  1.00 35.92           C
ANISOU  803  C   PHE A  82     4416   4590   4643     64   -278   -325       C
ATOM    804  O   PHE A  82     -41.540  12.832  28.731  1.00 39.79           O
ANISOU  804  O   PHE A  82     4900   5117   5101    136   -274   -317       O
ATOM    805  CB  PHE A  82     -43.382  13.067  26.281  1.00 27.31           C
ANISOU  805  CB  PHE A  82     3256   3557   3564    -17   -285   -281       C
ATOM    806  CG  PHE A  82     -44.243  12.749  25.093  1.00 30.83           C
ANISOU  806  CG  PHE A  82     3668   4028   4018   -101   -294   -265       C
ATOM    807  CD1 PHE A  82     -44.358  11.447  24.626  1.00 35.93           C
ANISOU  807  CD1 PHE A  82     4321   4650   4678   -176   -276   -273       C
ATOM    808  CD2 PHE A  82     -44.941  13.752  24.442  1.00 34.10           C
ANISOU  808  CD2 PHE A  82     4039   4490   4428   -102   -320   -246       C
ATOM    809  CE1 PHE A  82     -45.154  11.153  23.536  1.00 29.56           C
ANISOU  809  CE1 PHE A  82     3478   3881   3873   -258   -294   -278       C
ATOM    810  CE2 PHE A  82     -45.738  13.462  23.343  1.00 34.03           C
ANISOU  810  CE2 PHE A  82     3991   4528   4411   -175   -339   -232       C
ATOM    811  CZ  PHE A  82     -45.842  12.161  22.891  1.00 30.26           C
ANISOU  811  CZ  PHE A  82     3519   4038   3939   -257   -329   -257       C
ATOM    812  N   GLY A  83     -40.143  12.483  26.997  1.00 37.91           N
ANISOU  812  N   GLY A  83     4690   4801   4915     52   -297   -370       N
ATOM    813  CA  GLY A  83     -38.938  12.720  27.751  1.00 34.68           C
ANISOU  813  CA  GLY A  83     4295   4381   4499    115   -315   -407       C
ATOM    814  C   GLY A  83     -38.727  14.160  28.164  1.00 36.85           C
ANISOU  814  C   GLY A  83     4552   4675   4776    163   -350   -450       C
ATOM    815  O   GLY A  83     -39.261  15.096  27.563  1.00 41.26           O
ANISOU  815  O   GLY A  83     5090   5232   5357    142   -359   -451       O
ATOM    816  N   PRO A  84     -37.916  14.358  29.207  1.00 40.20           N
ANISOU  816  N   PRO A  84     4979   5115   5179    230   -372   -490       N
ATOM    817  CA  PRO A  84     -37.665  15.722  29.693  1.00 41.03           C
ANISOU  817  CA  PRO A  84     5066   5229   5296    273   -407   -555       C
ATOM    818  C   PRO A  84     -36.759  16.543  28.796  1.00 39.65           C
ANISOU  818  C   PRO A  84     4875   4995   5194    233   -431   -600       C
ATOM    819  O   PRO A  84     -36.724  17.771  28.955  1.00 35.42           O
ANISOU  819  O   PRO A  84     4320   4440   4698    250   -452   -649       O
ATOM    820  CB  PRO A  84     -37.020  15.490  31.065  1.00 39.86           C
ANISOU  820  CB  PRO A  84     4922   5133   5091    352   -429   -591       C
ATOM    821  CG  PRO A  84     -36.381  14.148  30.945  1.00 39.10           C
ANISOU  821  CG  PRO A  84     4844   5028   4986    342   -413   -546       C
ATOM    822  CD  PRO A  84     -37.292  13.340  30.069  1.00 39.78           C
ANISOU  822  CD  PRO A  84     4944   5081   5090    276   -365   -474       C
ATOM    823  N   PHE A  85     -36.027  15.928  27.864  1.00 36.77           N
ANISOU  823  N   PHE A  85     4518   4597   4856    182   -421   -586       N
ATOM    824  CA  PHE A  85     -35.181  16.724  26.982  1.00 40.45           C
ANISOU  824  CA  PHE A  85     4964   5015   5391    145   -431   -614       C
ATOM    825  C   PHE A  85     -36.023  17.664  26.130  1.00 42.37           C
ANISOU  825  C   PHE A  85     5194   5238   5666    112   -420   -580       C
ATOM    826  O   PHE A  85     -35.855  18.886  26.181  1.00 37.48           O
ANISOU  826  O   PHE A  85     4552   4583   5106    123   -434   -608       O
ATOM    827  CB  PHE A  85     -34.320  15.840  26.082  1.00 35.93           C
ANISOU  827  CB  PHE A  85     4399   4422   4830    102   -411   -602       C
ATOM    828  CG  PHE A  85     -33.546  16.626  25.053  1.00 33.39           C
ANISOU  828  CG  PHE A  85     4053   4062   4573     60   -406   -611       C
ATOM    829  CD1 PHE A  85     -32.418  17.346  25.420  1.00 32.54           C
ANISOU  829  CD1 PHE A  85     3910   3928   4527     75   -431   -666       C
ATOM    830  CD2 PHE A  85     -33.965  16.676  23.733  1.00 32.27           C
ANISOU  830  CD2 PHE A  85     3916   3918   4429      6   -376   -563       C
ATOM    831  CE1 PHE A  85     -31.711  18.088  24.488  1.00 29.13           C
ANISOU  831  CE1 PHE A  85     3447   3454   4167     32   -415   -661       C
ATOM    832  CE2 PHE A  85     -33.262  17.416  22.793  1.00 33.79           C
ANISOU  832  CE2 PHE A  85     4083   4082   4674    -26   -361   -552       C
ATOM    833  CZ  PHE A  85     -32.134  18.125  23.173  1.00 28.43           C
ANISOU  833  CZ  PHE A  85     3368   3364   4070    -15   -375   -596       C
ATOM    834  N   LEU A  86     -36.929  17.106  25.326  1.00 38.57           N
ANISOU  834  N   LEU A  86     4724   4780   5152     73   -396   -519       N
ATOM    835  CA  LEU A  86     -37.741  17.952  24.460  1.00 34.79           C
ANISOU  835  CA  LEU A  86     4225   4300   4692     50   -390   -472       C
ATOM    836  C   LEU A  86     -38.656  18.859  25.275  1.00 33.58           C
ANISOU  836  C   LEU A  86     4056   4152   4552    103   -399   -474       C
ATOM    837  O   LEU A  86     -38.876  20.019  24.906  1.00 35.97           O
ANISOU  837  O   LEU A  86     4336   4422   4909    112   -400   -457       O
ATOM    838  CB  LEU A  86     -38.546  17.094  23.489  1.00 31.13           C
ANISOU  838  CB  LEU A  86     3768   3880   4178     -3   -374   -420       C
ATOM    839  CG  LEU A  86     -39.216  17.875  22.359  1.00 36.59           C
ANISOU  839  CG  LEU A  86     4434   4593   4875    -28   -374   -360       C
ATOM    840  CD1 LEU A  86     -38.224  18.826  21.710  1.00 33.82           C
ANISOU  840  CD1 LEU A  86     4074   4196   4581    -32   -368   -354       C
ATOM    841  CD2 LEU A  86     -39.832  16.932  21.332  1.00 32.75           C
ANISOU  841  CD2 LEU A  86     3949   4167   4327    -88   -369   -332       C
ATOM    842  N   VAL A  87     -39.166  18.366  26.405  1.00 28.01           N
ANISOU  842  N   VAL A  87     3359   3485   3800    146   -399   -490       N
ATOM    843  CA  VAL A  87     -40.051  19.182  27.232  1.00 33.88           C
ANISOU  843  CA  VAL A  87     4085   4243   4545    206   -399   -500       C
ATOM    844  C   VAL A  87     -39.316  20.416  27.744  1.00 37.61           C
ANISOU  844  C   VAL A  87     4548   4660   5082    246   -420   -578       C
ATOM    845  O   VAL A  87     -39.773  21.552  27.566  1.00 42.55           O
ANISOU  845  O   VAL A  87     5153   5246   5769    265   -416   -576       O
ATOM    846  CB  VAL A  87     -40.634  18.344  28.385  1.00 28.92           C
ANISOU  846  CB  VAL A  87     3467   3679   3842    248   -385   -498       C
ATOM    847  CG1 VAL A  87     -41.312  19.243  29.402  1.00 26.25           C
ANISOU  847  CG1 VAL A  87     3113   3365   3498    325   -381   -532       C
ATOM    848  CG2 VAL A  87     -41.628  17.328  27.840  1.00 30.29           C
ANISOU  848  CG2 VAL A  87     3634   3892   3982    200   -358   -419       C
ATOM    849  N   TYR A  88     -38.154  20.215  28.367  1.00 35.96           N
ANISOU  849  N   TYR A  88     4350   4444   4871    257   -444   -649       N
ATOM    850  CA  TYR A  88     -37.431  21.349  28.929  1.00 35.28           C
ANISOU  850  CA  TYR A  88     4247   4307   4852    286   -472   -744       C
ATOM    851  C   TYR A  88     -36.831  22.230  27.844  1.00 36.32           C
ANISOU  851  C   TYR A  88     4356   4347   5095    235   -467   -732       C
ATOM    852  O   TYR A  88     -36.768  23.455  28.009  1.00 36.80           O
ANISOU  852  O   TYR A  88     4397   4338   5247    251   -472   -780       O
ATOM    853  CB  TYR A  88     -36.356  20.857  29.892  1.00 32.54           C
ANISOU  853  CB  TYR A  88     3904   3996   4464    313   -508   -824       C
ATOM    854  CG  TYR A  88     -36.916  20.572  31.264  1.00 34.71           C
ANISOU  854  CG  TYR A  88     4191   4357   4641    390   -514   -859       C
ATOM    855  CD1 TYR A  88     -37.265  21.610  32.116  1.00 30.76           C
ANISOU  855  CD1 TYR A  88     3680   3859   4150    447   -527   -947       C
ATOM    856  CD2 TYR A  88     -37.126  19.268  31.699  1.00 34.18           C
ANISOU  856  CD2 TYR A  88     4145   4366   4473    410   -500   -802       C
ATOM    857  CE1 TYR A  88     -37.787  21.361  33.366  1.00 30.51           C
ANISOU  857  CE1 TYR A  88     3659   3924   4012    525   -527   -979       C
ATOM    858  CE2 TYR A  88     -37.649  19.011  32.956  1.00 28.85           C
ANISOU  858  CE2 TYR A  88     3480   3782   3702    486   -496   -816       C
ATOM    859  CZ  TYR A  88     -37.979  20.064  33.782  1.00 27.69           C
ANISOU  859  CZ  TYR A  88     3322   3655   3547    545   -510   -905       C
ATOM    860  OH  TYR A  88     -38.502  19.831  35.033  1.00 31.42           O
ANISOU  860  OH  TYR A  88     3801   4232   3905    629   -500   -921       O
ATOM    861  N   LEU A  89     -36.414  21.642  26.724  1.00 34.79           N
ANISOU  861  N   LEU A  89     4167   4150   4903    175   -452   -665       N
ATOM    862  CA  LEU A  89     -35.928  22.442  25.609  1.00 37.05           C
ANISOU  862  CA  LEU A  89     4430   4364   5282    130   -435   -627       C
ATOM    863  C   LEU A  89     -37.012  23.387  25.109  1.00 36.33           C
ANISOU  863  C   LEU A  89     4327   4243   5234    144   -413   -560       C
ATOM    864  O   LEU A  89     -36.794  24.600  25.001  1.00 36.26           O
ANISOU  864  O   LEU A  89     4294   4145   5336    150   -405   -570       O
ATOM    865  CB  LEU A  89     -35.446  21.522  24.491  1.00 37.76           C
ANISOU  865  CB  LEU A  89     4530   4483   5334     73   -414   -566       C
ATOM    866  CG  LEU A  89     -34.971  22.222  23.223  1.00 35.32           C
ANISOU  866  CG  LEU A  89     4199   4126   5097     28   -385   -504       C
ATOM    867  CD1 LEU A  89     -33.859  23.201  23.550  1.00 37.48           C
ANISOU  867  CD1 LEU A  89     4437   4311   5493     23   -391   -564       C
ATOM    868  CD2 LEU A  89     -34.521  21.199  22.200  1.00 29.41           C
ANISOU  868  CD2 LEU A  89     3463   3426   4286    -18   -362   -461       C
ATOM    869  N   GLY A  90     -38.194  22.845  24.803  1.00 34.98           N
ANISOU  869  N   GLY A  90     4166   4141   4986    150   -402   -489       N
ATOM    870  CA  GLY A  90     -39.296  23.691  24.383  1.00 33.46           C
ANISOU  870  CA  GLY A  90     3952   3936   4827    176   -385   -418       C
ATOM    871  C   GLY A  90     -39.660  24.738  25.417  1.00 33.63           C
ANISOU  871  C   GLY A  90     3961   3901   4916    243   -387   -484       C
ATOM    872  O   GLY A  90     -39.912  25.894  25.076  1.00 35.41           O
ANISOU  872  O   GLY A  90     4163   4050   5241    264   -370   -451       O
ATOM    873  N   SER A  91     -39.686  24.351  26.697  1.00 31.26           N
ANISOU  873  N   SER A  91     3676   3638   4563    283   -404   -576       N
ATOM    874  CA  SER A  91     -40.064  25.296  27.744  1.00 35.50           C
ANISOU  874  CA  SER A  91     4203   4138   5146    354   -405   -659       C
ATOM    875  C   SER A  91     -39.086  26.461  27.814  1.00 36.37           C
ANISOU  875  C   SER A  91     4300   4125   5393    348   -414   -739       C
ATOM    876  O   SER A  91     -39.489  27.630  27.880  1.00 38.38           O
ANISOU  876  O   SER A  91     4538   4294   5753    385   -396   -754       O
ATOM    877  CB  SER A  91     -40.144  24.578  29.091  1.00 35.93           C
ANISOU  877  CB  SER A  91     4277   4278   5095    399   -421   -741       C
ATOM    878  OG  SER A  91     -40.993  23.448  29.010  1.00 36.55           O
ANISOU  878  OG  SER A  91     4364   4456   5067    394   -405   -660       O
ATOM    879  N   ILE A  92     -37.790  26.157  27.796  1.00 37.38           N
ANISOU  879  N   ILE A  92     4430   4237   5535    299   -439   -790       N
ATOM    880  CA  ILE A  92     -36.781  27.206  27.848  1.00 37.07           C
ANISOU  880  CA  ILE A  92     4365   4080   5639    278   -449   -871       C
ATOM    881  C   ILE A  92     -36.853  28.076  26.599  1.00 37.90           C
ANISOU  881  C   ILE A  92     4449   4082   5870    245   -406   -760       C
ATOM    882  O   ILE A  92     -36.754  29.308  26.677  1.00 32.08           O
ANISOU  882  O   ILE A  92     3689   3220   5281    256   -391   -797       O
ATOM    883  CB  ILE A  92     -35.389  26.580  28.038  1.00 36.78           C
ANISOU  883  CB  ILE A  92     4323   4068   5585    232   -484   -936       C
ATOM    884  CG1 ILE A  92     -35.300  25.941  29.427  1.00 38.63           C
ANISOU  884  CG1 ILE A  92     4572   4401   5705    283   -529  -1047       C
ATOM    885  CG2 ILE A  92     -34.298  27.620  27.836  1.00 34.42           C
ANISOU  885  CG2 ILE A  92     3981   3643   5452    187   -489   -997       C
ATOM    886  CD1 ILE A  92     -34.222  24.892  29.552  1.00 41.11           C
ANISOU  886  CD1 ILE A  92     4885   4783   5953    256   -561  -1064       C
ATOM    887  N   ALA A  93     -37.038  27.457  25.430  1.00 37.44           N
ANISOU  887  N   ALA A  93     4396   4074   5756    207   -384   -623       N
ATOM    888  CA  ALA A  93     -37.141  28.235  24.201  1.00 34.85           C
ANISOU  888  CA  ALA A  93     4046   3674   5522    185   -341   -497       C
ATOM    889  C   ALA A  93     -38.330  29.183  24.253  1.00 45.13           C
ANISOU  889  C   ALA A  93     5336   4925   6885    250   -318   -449       C
ATOM    890  O   ALA A  93     -38.228  30.344  23.839  1.00 53.43           O
ANISOU  890  O   ALA A  93     6363   5853   8086    256   -285   -405       O
ATOM    891  CB  ALA A  93     -37.246  27.303  22.997  1.00 36.89           C
ANISOU  891  CB  ALA A  93     4313   4030   5672    143   -328   -372       C
ATOM    892  N   GLY A  94     -39.462  28.712  24.775  1.00 42.59           N
ANISOU  892  N   GLY A  94     5027   4695   6461    302   -329   -453       N
ATOM    893  CA  GLY A  94     -40.629  29.567  24.873  1.00 39.14           C
ANISOU  893  CA  GLY A  94     4571   4221   6080    374   -304   -409       C
ATOM    894  C   GLY A  94     -40.439  30.691  25.871  1.00 39.94           C
ANISOU  894  C   GLY A  94     4667   4195   6316    422   -298   -540       C
ATOM    895  O   GLY A  94     -40.901  31.813  25.649  1.00 39.63           O
ANISOU  895  O   GLY A  94     4604   4045   6407    467   -263   -498       O
ATOM    896  N   ILE A  95     -39.759  30.409  26.984  1.00 40.97           N
ANISOU  896  N   ILE A  95     4814   4338   6415    418   -333   -702       N
ATOM    897  CA  ILE A  95     -39.484  31.458  27.962  1.00 43.60           C
ANISOU  897  CA  ILE A  95     5140   4557   6869    457   -336   -859       C
ATOM    898  C   ILE A  95     -38.570  32.522  27.363  1.00 46.87           C
ANISOU  898  C   ILE A  95     5529   4796   7484    407   -316   -855       C
ATOM    899  O   ILE A  95     -38.758  33.724  27.587  1.00 53.47           O
ANISOU  899  O   ILE A  95     6348   5487   8482    444   -288   -903       O
ATOM    900  CB  ILE A  95     -38.883  30.849  29.241  1.00 40.77           C
ANISOU  900  CB  ILE A  95     4801   4280   6410    462   -387  -1031       C
ATOM    901  CG1 ILE A  95     -39.944  30.053  30.000  1.00 36.71           C
ANISOU  901  CG1 ILE A  95     4307   3915   5725    530   -388  -1033       C
ATOM    902  CG2 ILE A  95     -38.289  31.937  30.128  1.00 34.03           C
ANISOU  902  CG2 ILE A  95     3933   3308   5687    479   -404  -1217       C
ATOM    903  CD1 ILE A  95     -39.401  29.314  31.200  1.00 31.81           C
ANISOU  903  CD1 ILE A  95     3706   3402   4977    544   -435  -1166       C
ATOM    904  N   ILE A  96     -37.578  32.097  26.580  1.00 46.36           N
ANISOU  904  N   ILE A  96     5456   4736   7423    325   -322   -795       N
ATOM    905  CA  ILE A  96     -36.615  33.035  26.010  1.00 47.55           C
ANISOU  905  CA  ILE A  96     5573   4726   7767    267   -296   -782       C
ATOM    906  C   ILE A  96     -37.293  33.976  25.024  1.00 47.29           C
ANISOU  906  C   ILE A  96     5523   4586   7858    294   -230   -616       C
ATOM    907  O   ILE A  96     -36.988  35.173  24.979  1.00 60.48           O
ANISOU  907  O   ILE A  96     7167   6077   9737    290   -195   -634       O
ATOM    908  CB  ILE A  96     -35.456  32.262  25.354  1.00 47.17           C
ANISOU  908  CB  ILE A  96     5515   4732   7674    181   -307   -740       C
ATOM    909  CG1 ILE A  96     -34.536  31.674  26.420  1.00 44.82           C
ANISOU  909  CG1 ILE A  96     5217   4493   7319    158   -371   -920       C
ATOM    910  CG2 ILE A  96     -34.672  33.154  24.409  1.00 45.65           C
ANISOU  910  CG2 ILE A  96     5282   4394   7669    121   -257   -654       C
ATOM    911  CD1 ILE A  96     -33.614  30.614  25.880  1.00 48.01           C
ANISOU  911  CD1 ILE A  96     5617   4989   7634     96   -384   -874       C
ATOM    912  N   PHE A  97     -38.219  33.458  24.218  1.00 44.46           N
ANISOU  912  N   PHE A  97     5175   4337   7382    321   -214   -451       N
ATOM    913  CA  PHE A  97     -38.933  34.268  23.239  1.00 48.70           C
ANISOU  913  CA  PHE A  97     5690   4805   8009    359   -158   -271       C
ATOM    914  C   PHE A  97     -40.254  34.809  23.774  1.00 49.82           C
ANISOU  914  C   PHE A  97     5828   4927   8172    462   -146   -277       C
ATOM    915  O   PHE A  97     -41.120  35.192  22.976  1.00 50.84           O
ANISOU  915  O   PHE A  97     5937   5059   8321    512   -111   -109       O
ATOM    916  CB  PHE A  97     -39.168  33.463  21.959  1.00 48.09           C
ANISOU  916  CB  PHE A  97     5613   4869   7790    332   -152    -86       C
ATOM    917  CG  PHE A  97     -37.910  33.164  21.206  1.00 50.16           C
ANISOU  917  CG  PHE A  97     5869   5129   8059    244   -141    -47       C
ATOM    918  CD1 PHE A  97     -37.414  34.061  20.274  1.00 55.99           C
ANISOU  918  CD1 PHE A  97     6577   5753   8944    222    -81     84       C
ATOM    919  CD2 PHE A  97     -37.208  31.997  21.445  1.00 49.38           C
ANISOU  919  CD2 PHE A  97     5792   5141   7830    188   -181   -135       C
ATOM    920  CE1 PHE A  97     -36.243  33.793  19.587  1.00 52.79           C
ANISOU  920  CE1 PHE A  97     6160   5353   8546    143    -60    124       C
ATOM    921  CE2 PHE A  97     -36.036  31.724  20.763  1.00 54.15           C
ANISOU  921  CE2 PHE A  97     6384   5745   8445    114   -165   -102       C
ATOM    922  CZ  PHE A  97     -35.555  32.623  19.832  1.00 51.90           C
ANISOU  922  CZ  PHE A  97     6066   5356   8299     90   -103     25       C
ATOM    923  N   SER A  98     -40.409  34.869  25.095  1.00 50.43           N
ANISOU  923  N   SER A  98     5921   4995   8245    502   -171   -465       N
ATOM    924  CA  SER A  98     -41.615  35.367  25.760  1.00 52.95           C
ANISOU  924  CA  SER A  98     6235   5301   8582    606   -153   -499       C
ATOM    925  C   SER A  98     -42.872  34.858  25.060  1.00 47.34           C
ANISOU  925  C   SER A  98     5510   4729   7748    654   -144   -322       C
ATOM    926  O   SER A  98     -43.735  35.618  24.622  1.00 46.20           O
ANISOU  926  O   SER A  98     5336   4529   7689    725   -104   -207       O
ATOM    927  CB  SER A  98     -41.608  36.895  25.851  1.00 61.40           C
ANISOU  927  CB  SER A  98     7284   6144   9900    651   -102   -525       C
ATOM    928  OG  SER A  98     -41.179  37.493  24.640  1.00 68.08           O
ANISOU  928  OG  SER A  98     8107   6879  10883    612    -59   -354       O
ATOM    929  N   ALA A  99     -42.942  33.532  24.941  1.00 49.23           N
ANISOU  929  N   ALA A  99     5765   5150   7790    610   -184   -301       N
ATOM    930  CA  ALA A  99     -44.066  32.840  24.307  1.00 39.54           C
ANISOU  930  CA  ALA A  99     4518   4077   6428    633   -188   -158       C
ATOM    931  C   ALA A  99     -44.389  31.628  25.174  1.00 38.35           C
ANISOU  931  C   ALA A  99     4388   4079   6104    626   -224   -253       C
ATOM    932  O   ALA A  99     -43.747  30.582  25.047  1.00 42.97           O
ANISOU  932  O   ALA A  99     4999   4747   6580    552   -255   -273       O
ATOM    933  CB  ALA A  99     -43.736  32.432  22.877  1.00 33.15           C
ANISOU  933  CB  ALA A  99     3701   3325   5570    567   -192      4       C
ATOM    934  N   THR A 100     -45.395  31.769  26.038  1.00 42.21           N
ANISOU  934  N   THR A 100     4863   4602   6572    709   -211   -303       N
ATOM    935  CA  THR A 100     -45.680  30.790  27.075  1.00 42.88           C
ANISOU  935  CA  THR A 100     4966   4813   6514    717   -229   -400       C
ATOM    936  C   THR A 100     -46.940  29.965  26.835  1.00 47.19           C
ANISOU  936  C   THR A 100     5478   5513   6940    732   -228   -295       C
ATOM    937  O   THR A 100     -47.185  29.017  27.589  1.00 47.73           O
ANISOU  937  O   THR A 100     5557   5690   6888    727   -236   -349       O
ATOM    938  CB  THR A 100     -45.794  31.494  28.433  1.00 42.85           C
ANISOU  938  CB  THR A 100     4972   4750   6561    798   -210   -562       C
ATOM    939  OG1 THR A 100     -46.902  32.402  28.409  1.00 48.23           O
ANISOU  939  OG1 THR A 100     5612   5385   7329    894   -166   -512       O
ATOM    940  CG2 THR A 100     -44.525  32.273  28.716  1.00 38.43           C
ANISOU  940  CG2 THR A 100     4437   4039   6125    770   -221   -689       C
ATOM    941  N   SER A 101     -47.741  30.292  25.825  1.00 46.42           N
ANISOU  941  N   SER A 101     5332   5432   6874    751   -217   -145       N
ATOM    942  CA  SER A 101     -48.916  29.493  25.500  1.00 40.83           C
ANISOU  942  CA  SER A 101     4576   4878   6058    752   -225    -48       C
ATOM    943  C   SER A 101     -49.440  29.935  24.142  1.00 36.63           C
ANISOU  943  C   SER A 101     3993   4361   5564    758   -230    121       C
ATOM    944  O   SER A 101     -49.013  30.951  23.588  1.00 46.01           O
ANISOU  944  O   SER A 101     5182   5430   6870    780   -213    173       O
ATOM    945  CB  SER A 101     -50.008  29.622  26.566  1.00 41.03           C
ANISOU  945  CB  SER A 101     4568   4951   6071    843   -192    -94       C
ATOM    946  OG  SER A 101     -50.188  30.977  26.929  1.00 45.77           O
ANISOU  946  OG  SER A 101     5155   5424   6810    941   -153   -127       O
ATOM    947  N   GLY A 102     -50.365  29.147  23.611  1.00 28.40           N
ANISOU  947  N   GLY A 102     2901   3469   4421    736   -253    211       N
ATOM    948  CA  GLY A 102     -51.057  29.526  22.405  1.00 27.96           C
ANISOU  948  CA  GLY A 102     2782   3466   4376    756   -266    372       C
ATOM    949  C   GLY A 102     -50.203  29.542  21.147  1.00 31.02           C
ANISOU  949  C   GLY A 102     3193   3842   4752    690   -289    453       C
ATOM    950  O   GLY A 102     -49.156  28.886  21.032  1.00 32.64           O
ANISOU  950  O   GLY A 102     3457   4038   4907    604   -304    390       O
ATOM    951  N   GLU A 103     -50.688  30.331  20.185  1.00 34.36           N
ANISOU  951  N   GLU A 103     3563   4271   5220    742   -286    606       N
ATOM    952  CA  GLU A 103     -50.094  30.360  18.855  1.00 40.48           C
ANISOU  952  CA  GLU A 103     4346   5074   5961    694   -303    717       C
ATOM    953  C   GLU A 103     -48.629  30.777  18.896  1.00 42.53           C
ANISOU  953  C   GLU A 103     4677   5179   6304    655   -272    663       C
ATOM    954  O   GLU A 103     -47.814  30.251  18.133  1.00 39.38           O
ANISOU  954  O   GLU A 103     4308   4821   5833    576   -287    681       O
ATOM    955  CB  GLU A 103     -50.892  31.295  17.949  1.00 48.40           C
ANISOU  955  CB  GLU A 103     5276   6104   7011    781   -297    905       C
ATOM    956  CG  GLU A 103     -51.541  30.589  16.778  1.00 58.11           C
ANISOU  956  CG  GLU A 103     6449   7545   8085    747   -356   1017       C
ATOM    957  CD  GLU A 103     -52.237  31.540  15.829  1.00 67.16           C
ANISOU  957  CD  GLU A 103     7521   8732   9266    841   -355   1220       C
ATOM    958  OE1 GLU A 103     -51.544  32.320  15.140  1.00 70.17           O
ANISOU  958  OE1 GLU A 103     7924   9029   9710    862   -322   1326       O
ATOM    959  OE2 GLU A 103     -53.483  31.501  15.771  1.00 72.61           O
ANISOU  959  OE2 GLU A 103     8124   9542   9923    897   -384   1282       O
ATOM    960  N   SER A 104     -48.271  31.719  19.774  1.00 43.46           N
ANISOU  960  N   SER A 104     4816   5121   6576    707   -229    590       N
ATOM    961  CA  SER A 104     -46.888  32.193  19.801  1.00 45.91           C
ANISOU  961  CA  SER A 104     5178   5279   6986    664   -202    539       C
ATOM    962  C   SER A 104     -45.942  31.105  20.303  1.00 41.48           C
ANISOU  962  C   SER A 104     4674   4753   6334    570   -230    391       C
ATOM    963  O   SER A 104     -44.853  30.907  19.740  1.00 46.93           O
ANISOU  963  O   SER A 104     5394   5421   7018    500   -228    396       O
ATOM    964  CB  SER A 104     -46.778  33.462  20.651  1.00 42.85           C
ANISOU  964  CB  SER A 104     4793   4691   6795    739   -154    474       C
ATOM    965  OG  SER A 104     -47.194  33.241  21.986  1.00 45.93           O
ANISOU  965  OG  SER A 104     5195   5085   7172    774   -159    316       O
ATOM    966  N   LEU A 105     -46.354  30.367  21.341  1.00 34.17           N
ANISOU  966  N   LEU A 105     3760   3889   5334    572   -250    270       N
ATOM    967  CA  LEU A 105     -45.566  29.219  21.783  1.00 35.41           C
ANISOU  967  CA  LEU A 105     3966   4096   5394    492   -277    153       C
ATOM    968  C   LEU A 105     -45.458  28.171  20.681  1.00 38.84           C
ANISOU  968  C   LEU A 105     4401   4660   5696    414   -305    226       C
ATOM    969  O   LEU A 105     -44.377  27.612  20.456  1.00 40.80           O
ANISOU  969  O   LEU A 105     4688   4902   5912    344   -312    181       O
ATOM    970  CB  LEU A 105     -46.167  28.601  23.047  1.00 26.41           C
ANISOU  970  CB  LEU A 105     2831   3013   4190    519   -286     43       C
ATOM    971  CG  LEU A 105     -45.603  27.224  23.426  1.00 30.71           C
ANISOU  971  CG  LEU A 105     3416   3635   4615    445   -313    -41       C
ATOM    972  CD1 LEU A 105     -44.099  27.299  23.699  1.00 30.51           C
ANISOU  972  CD1 LEU A 105     3438   3517   4635    404   -316   -135       C
ATOM    973  CD2 LEU A 105     -46.324  26.641  24.632  1.00 27.05           C
ANISOU  973  CD2 LEU A 105     2952   3239   4089    481   -311   -116       C
ATOM    974  N   ARG A 106     -46.563  27.898  19.977  1.00 34.45           N
ANISOU  974  N   ARG A 106     3798   4229   5065    427   -324    331       N
ATOM    975  CA  ARG A 106     -46.509  26.944  18.870  1.00 39.74           C
ANISOU  975  CA  ARG A 106     4465   5029   5605    353   -355    385       C
ATOM    976  C   ARG A 106     -45.539  27.402  17.783  1.00 45.89           C
ANISOU  976  C   ARG A 106     5260   5772   6406    326   -337    463       C
ATOM    977  O   ARG A 106     -44.817  26.585  17.197  1.00 47.57           O
ANISOU  977  O   ARG A 106     5502   6040   6533    252   -347    440       O
ATOM    978  CB  ARG A 106     -47.905  26.740  18.285  1.00 40.75           C
ANISOU  978  CB  ARG A 106     4524   5301   5658    375   -385    482       C
ATOM    979  CG  ARG A 106     -48.843  25.933  19.165  1.00 38.54           C
ANISOU  979  CG  ARG A 106     4221   5093   5330    373   -401    412       C
ATOM    980  CD  ARG A 106     -49.863  25.160  18.335  1.00 40.43           C
ANISOU  980  CD  ARG A 106     4398   5506   5459    335   -447    474       C
ATOM    981  NE  ARG A 106     -50.776  26.027  17.590  1.00 33.39           N
ANISOU  981  NE  ARG A 106     3428   4675   4582    404   -460    615       N
ATOM    982  CZ  ARG A 106     -51.839  26.618  18.126  1.00 32.53           C
ANISOU  982  CZ  ARG A 106     3256   4571   4534    489   -449    656       C
ATOM    983  NH1 ARG A 106     -52.106  26.444  19.413  1.00 36.60           N
ANISOU  983  NH1 ARG A 106     3779   5036   5090    511   -421    562       N
ATOM    984  NH2 ARG A 106     -52.628  27.384  17.383  1.00 32.08           N
ANISOU  984  NH2 ARG A 106     3123   4574   4492    558   -462    797       N
ATOM    985  N   ALA A 107     -45.515  28.706  17.496  1.00 46.71           N
ANISOU  985  N   ALA A 107     5341   5778   6628    388   -303    561       N
ATOM    986  CA  ALA A 107     -44.595  29.238  16.495  1.00 43.54           C
ANISOU  986  CA  ALA A 107     4948   5333   6263    367   -272    655       C
ATOM    987  C   ALA A 107     -43.148  29.036  16.921  1.00 47.22           C
ANISOU  987  C   ALA A 107     5466   5697   6779    304   -252    541       C
ATOM    988  O   ALA A 107     -42.290  28.695  16.096  1.00 46.13           O
ANISOU  988  O   ALA A 107     5343   5593   6591    249   -239    572       O
ATOM    989  CB  ALA A 107     -44.878  30.721  16.253  1.00 36.35           C
ANISOU  989  CB  ALA A 107     4001   4308   5501    451   -229    787       C
ATOM    990  N   VAL A 108     -42.857  29.245  18.205  1.00 41.91           N
ANISOU  990  N   VAL A 108     4815   4911   6200    317   -248    405       N
ATOM    991  CA  VAL A 108     -41.507  28.967  18.688  1.00 39.84           C
ANISOU  991  CA  VAL A 108     4589   4573   5974    259   -242    286       C
ATOM    992  C   VAL A 108     -41.193  27.475  18.577  1.00 42.98           C
ANISOU  992  C   VAL A 108     5018   5096   6217    193   -274    221       C
ATOM    993  O   VAL A 108     -40.102  27.086  18.138  1.00 47.42           O
ANISOU  993  O   VAL A 108     5598   5656   6763    136   -263    203       O
ATOM    994  CB  VAL A 108     -41.335  29.485  20.126  1.00 39.76           C
ANISOU  994  CB  VAL A 108     4590   4440   6076    293   -243    144       C
ATOM    995  CG1 VAL A 108     -40.048  28.969  20.722  1.00 24.94           C
ANISOU  995  CG1 VAL A 108     2744   2528   4203    235   -256      9       C
ATOM    996  CG2 VAL A 108     -41.352  31.006  20.140  1.00 39.34           C
ANISOU  996  CG2 VAL A 108     4511   4225   6210    345   -201    192       C
ATOM    997  N   LEU A 109     -42.151  26.617  18.938  1.00 38.65           N
ANISOU  997  N   LEU A 109     4469   4653   5562    199   -308    188       N
ATOM    998  CA  LEU A 109     -41.895  25.179  18.958  1.00 33.86           C
ANISOU  998  CA  LEU A 109     3892   4139   4833    138   -332    117       C
ATOM    999  C   LEU A 109     -41.730  24.601  17.557  1.00 34.32           C
ANISOU  999  C   LEU A 109     3950   4300   4791     86   -334    191       C
ATOM   1000  O   LEU A 109     -41.063  23.575  17.390  1.00 38.22           O
ANISOU 1000  O   LEU A 109     4474   4832   5216     31   -338    128       O
ATOM   1001  CB  LEU A 109     -43.026  24.453  19.683  1.00 31.33           C
ANISOU 1001  CB  LEU A 109     3564   3895   4444    154   -359     77       C
ATOM   1002  CG  LEU A 109     -43.267  24.761  21.162  1.00 29.40           C
ANISOU 1002  CG  LEU A 109     3325   3587   4258    208   -356    -11       C
ATOM   1003  CD1 LEU A 109     -44.441  23.942  21.667  1.00 26.96           C
ANISOU 1003  CD1 LEU A 109     2999   3375   3868    217   -371    -21       C
ATOM   1004  CD2 LEU A 109     -42.034  24.506  22.009  1.00 29.46           C
ANISOU 1004  CD2 LEU A 109     3375   3526   4293    191   -356   -129       C
ATOM   1005  N   ALA A 110     -42.327  25.233  16.545  1.00 35.10           N
ANISOU 1005  N   ALA A 110     4012   4451   4874    111   -329    324       N
ATOM   1006  CA  ALA A 110     -42.286  24.664  15.200  1.00 37.87           C
ANISOU 1006  CA  ALA A 110     4359   4931   5101     69   -336    389       C
ATOM   1007  C   ALA A 110     -40.864  24.576  14.647  1.00 38.52           C
ANISOU 1007  C   ALA A 110     4469   4978   5188     26   -297    379       C
ATOM   1008  O   ALA A 110     -40.590  23.734  13.783  1.00 34.19           O
ANISOU 1008  O   ALA A 110     3935   4535   4522    -20   -300    372       O
ATOM   1009  CB  ALA A 110     -43.171  25.481  14.257  1.00 37.58           C
ANISOU 1009  CB  ALA A 110     4269   4966   5042    118   -339    548       C
ATOM   1010  N   PHE A 111     -39.949  25.424  15.123  1.00 38.40           N
ANISOU 1010  N   PHE A 111     4459   4819   5312     39   -259    371       N
ATOM   1011  CA  PHE A 111     -38.592  25.439  14.586  1.00 33.55           C
ANISOU 1011  CA  PHE A 111     3856   4170   4720     -0   -216    375       C
ATOM   1012  C   PHE A 111     -37.677  24.400  15.219  1.00 35.75           C
ANISOU 1012  C   PHE A 111     4170   4433   4981    -47   -224    229       C
ATOM   1013  O   PHE A 111     -36.645  24.068  14.627  1.00 40.94           O
ANISOU 1013  O   PHE A 111     4833   5103   5617    -84   -191    224       O
ATOM   1014  CB  PHE A 111     -37.973  26.829  14.753  1.00 31.30           C
ANISOU 1014  CB  PHE A 111     3548   3732   4612     24   -169    434       C
ATOM   1015  CG  PHE A 111     -38.560  27.859  13.836  1.00 36.51           C
ANISOU 1015  CG  PHE A 111     4172   4402   5297     70   -139    615       C
ATOM   1016  CD1 PHE A 111     -38.069  28.023  12.550  1.00 35.21           C
ANISOU 1016  CD1 PHE A 111     3995   4303   5082     56    -93    743       C
ATOM   1017  CD2 PHE A 111     -39.626  28.648  14.251  1.00 38.13           C
ANISOU 1017  CD2 PHE A 111     4355   4562   5571    135   -153    665       C
ATOM   1018  CE1 PHE A 111     -38.622  28.965  11.697  1.00 42.32           C
ANISOU 1018  CE1 PHE A 111     4861   5223   5997    108    -64    931       C
ATOM   1019  CE2 PHE A 111     -40.183  29.594  13.404  1.00 35.76           C
ANISOU 1019  CE2 PHE A 111     4018   4270   5299    189   -125    847       C
ATOM   1020  CZ  PHE A 111     -39.683  29.752  12.126  1.00 42.80           C
ANISOU 1020  CZ  PHE A 111     4898   5229   6136    177    -82    987       C
ATOM   1021  N   ILE A 112     -38.038  23.868  16.389  1.00 33.39           N
ANISOU 1021  N   ILE A 112     3889   4112   4686    -39   -261    119       N
ATOM   1022  CA  ILE A 112     -37.159  22.917  17.070  1.00 29.99           C
ANISOU 1022  CA  ILE A 112     3488   3662   4245    -69   -269     -4       C
ATOM   1023  C   ILE A 112     -36.898  21.667  16.243  1.00 32.87           C
ANISOU 1023  C   ILE A 112     3875   4127   4487   -115   -264    -24       C
ATOM   1024  O   ILE A 112     -35.722  21.279  16.103  1.00 32.03           O
ANISOU 1024  O   ILE A 112     3778   4000   4393   -140   -238    -67       O
ATOM   1025  CB  ILE A 112     -37.725  22.595  18.471  1.00 29.19           C
ANISOU 1025  CB  ILE A 112     3400   3535   4156    -41   -306    -95       C
ATOM   1026  CG1 ILE A 112     -37.772  23.866  19.320  1.00 27.73           C
ANISOU 1026  CG1 ILE A 112     3194   3242   4098      6   -306   -105       C
ATOM   1027  CG2 ILE A 112     -36.888  21.521  19.147  1.00 27.59           C
ANISOU 1027  CG2 ILE A 112     3226   3328   3929    -62   -315   -202       C
ATOM   1028  CD1 ILE A 112     -38.337  23.647  20.705  1.00 31.17           C
ANISOU 1028  CD1 ILE A 112     3643   3670   4532     45   -336   -193       C
ATOM   1029  N   PRO A 113     -37.900  20.988  15.669  1.00 36.33           N
ANISOU 1029  N   PRO A 113     4318   4675   4812   -129   -286     -4       N
ATOM   1030  CA  PRO A 113     -37.584  19.802  14.858  1.00 35.02           C
ANISOU 1030  CA  PRO A 113     4175   4594   4537   -176   -278    -46       C
ATOM   1031  C   PRO A 113     -36.758  20.127  13.629  1.00 38.48           C
ANISOU 1031  C   PRO A 113     4605   5072   4944   -189   -233     16       C
ATOM   1032  O   PRO A 113     -35.906  19.326  13.223  1.00 41.99           O
ANISOU 1032  O   PRO A 113     5070   5539   5346   -218   -205    -42       O
ATOM   1033  CB  PRO A 113     -38.968  19.255  14.485  1.00 33.87           C
ANISOU 1033  CB  PRO A 113     4020   4556   4293   -190   -319    -35       C
ATOM   1034  CG  PRO A 113     -39.871  20.432  14.570  1.00 32.36           C
ANISOU 1034  CG  PRO A 113     3789   4363   4142   -143   -335     65       C
ATOM   1035  CD  PRO A 113     -39.357  21.223  15.730  1.00 37.81           C
ANISOU 1035  CD  PRO A 113     4483   4916   4968   -104   -320     45       C
ATOM   1036  N   ALA A 114     -36.978  21.296  13.028  1.00 39.47           N
ANISOU 1036  N   ALA A 114     4699   5206   5092   -162   -216    140       N
ATOM   1037  CA  ALA A 114     -36.176  21.684  11.875  1.00 39.46           C
ANISOU 1037  CA  ALA A 114     4685   5245   5061   -169   -160    222       C
ATOM   1038  C   ALA A 114     -34.727  21.943  12.279  1.00 43.04           C
ANISOU 1038  C   ALA A 114     5134   5586   5631   -180   -112    188       C
ATOM   1039  O   ALA A 114     -33.793  21.540  11.571  1.00 37.57           O
ANISOU 1039  O   ALA A 114     4444   4934   4896   -202    -64    181       O
ATOM   1040  CB  ALA A 114     -36.790  22.912  11.208  1.00 33.35           C
ANISOU 1040  CB  ALA A 114     3875   4499   4299   -130   -149    385       C
ATOM   1041  N   ILE A 115     -34.522  22.606  13.420  1.00 42.95           N
ANISOU 1041  N   ILE A 115     5112   5442   5766   -163   -124    158       N
ATOM   1042  CA  ILE A 115     -33.167  22.845  13.904  1.00 43.22           C
ANISOU 1042  CA  ILE A 115     5130   5373   5918   -178    -92    109       C
ATOM   1043  C   ILE A 115     -32.467  21.524  14.187  1.00 42.20           C
ANISOU 1043  C   ILE A 115     5026   5273   5735   -201    -98    -12       C
ATOM   1044  O   ILE A 115     -31.288  21.351  13.863  1.00 50.63           O
ANISOU 1044  O   ILE A 115     6076   6331   6828   -219    -53    -27       O
ATOM   1045  CB  ILE A 115     -33.195  23.753  15.147  1.00 43.15           C
ANISOU 1045  CB  ILE A 115     5103   5229   6064   -156   -118     72       C
ATOM   1046  CG1 ILE A 115     -33.689  25.153  14.770  1.00 42.73           C
ANISOU 1046  CG1 ILE A 115     5020   5119   6098   -131    -94    200       C
ATOM   1047  CG2 ILE A 115     -31.816  23.820  15.797  1.00 35.08           C
ANISOU 1047  CG2 ILE A 115     4057   4118   5153   -178   -105    -11       C
ATOM   1048  CD1 ILE A 115     -33.928  26.056  15.958  1.00 42.41           C
ANISOU 1048  CD1 ILE A 115     4966   4945   6202   -103   -120    151       C
ATOM   1049  N   GLY A 116     -33.178  20.573  14.793  1.00 36.45           N
ANISOU 1049  N   GLY A 116     4334   4576   4941   -197   -146    -92       N
ATOM   1050  CA  GLY A 116     -32.584  19.265  15.021  1.00 32.53           C
ANISOU 1050  CA  GLY A 116     3863   4097   4400   -211   -146   -194       C
ATOM   1051  C   GLY A 116     -32.218  18.562  13.728  1.00 35.70           C
ANISOU 1051  C   GLY A 116     4276   4592   4697   -236   -101   -186       C
ATOM   1052  O   GLY A 116     -31.138  17.972  13.609  1.00 32.87           O
ANISOU 1052  O   GLY A 116     3916   4224   4348   -243    -65   -238       O
ATOM   1053  N   GLY A 117     -33.109  18.624  12.735  1.00 38.58           N
ANISOU 1053  N   GLY A 117     4647   5056   4956   -244   -103   -124       N
ATOM   1054  CA  GLY A 117     -32.811  18.012  11.451  1.00 37.83           C
ANISOU 1054  CA  GLY A 117     4563   5071   4741   -264    -62   -125       C
ATOM   1055  C   GLY A 117     -31.574  18.599  10.800  1.00 39.49           C
ANISOU 1055  C   GLY A 117     4741   5276   4987   -261     13    -65       C
ATOM   1056  O   GLY A 117     -30.765  17.874  10.216  1.00 36.39           O
ANISOU 1056  O   GLY A 117     4356   4927   4542   -270     61   -114       O
ATOM   1057  N   VAL A 118     -31.412  19.920  10.890  1.00 37.19           N
ANISOU 1057  N   VAL A 118     4411   4925   4795   -247     30     43       N
ATOM   1058  CA  VAL A 118     -30.231  20.556  10.315  1.00 38.91           C
ANISOU 1058  CA  VAL A 118     4587   5125   5072   -251    109    114       C
ATOM   1059  C   VAL A 118     -28.983  20.161  11.097  1.00 40.62           C
ANISOU 1059  C   VAL A 118     4786   5252   5396   -260    125     16       C
ATOM   1060  O   VAL A 118     -27.966  19.758  10.518  1.00 35.55           O
ANISOU 1060  O   VAL A 118     4126   4645   4735   -267    188      3       O
ATOM   1061  CB  VAL A 118     -30.407  22.084  10.265  1.00 38.69           C
ANISOU 1061  CB  VAL A 118     4518   5031   5151   -239    126    255       C
ATOM   1062  CG1 VAL A 118     -29.105  22.758   9.825  1.00 39.01           C
ANISOU 1062  CG1 VAL A 118     4506   5026   5290   -253    214    328       C
ATOM   1063  CG2 VAL A 118     -31.536  22.453   9.323  1.00 36.80           C
ANISOU 1063  CG2 VAL A 118     4287   4903   4793   -218    119    374       C
ATOM   1064  N   LEU A 119     -29.050  20.251  12.428  1.00 38.59           N
ANISOU 1064  N   LEU A 119     4528   4891   5244   -254     67    -54       N
ATOM   1065  CA  LEU A 119     -27.894  19.956  13.264  1.00 38.59           C
ANISOU 1065  CA  LEU A 119     4501   4817   5346   -256     68   -141       C
ATOM   1066  C   LEU A 119     -27.462  18.503  13.165  1.00 40.31           C
ANISOU 1066  C   LEU A 119     4748   5087   5482   -250     78   -237       C
ATOM   1067  O   LEU A 119     -26.316  18.190  13.503  1.00 47.96           O
ANISOU 1067  O   LEU A 119     5683   6022   6518   -245    100   -288       O
ATOM   1068  CB  LEU A 119     -28.198  20.311  14.720  1.00 39.16           C
ANISOU 1068  CB  LEU A 119     4571   4793   5515   -242     -5   -201       C
ATOM   1069  CG  LEU A 119     -28.291  21.808  15.021  1.00 42.19           C
ANISOU 1069  CG  LEU A 119     4914   5087   6030   -246     -9   -138       C
ATOM   1070  CD1 LEU A 119     -28.353  22.059  16.518  1.00 41.73           C
ANISOU 1070  CD1 LEU A 119     4849   4944   6062   -229    -78   -232       C
ATOM   1071  CD2 LEU A 119     -27.122  22.552  14.399  1.00 43.38           C
ANISOU 1071  CD2 LEU A 119     4999   5201   6284   -274     63    -75       C
ATOM   1072  N   ALA A 120     -28.349  17.610  12.712  1.00 35.54           N
ANISOU 1072  N   ALA A 120     4200   4559   4745   -250     63   -265       N
ATOM   1073  CA  ALA A 120     -27.971  16.212  12.516  1.00 31.42           C
ANISOU 1073  CA  ALA A 120     3709   4072   4157   -246     83   -360       C
ATOM   1074  C   ALA A 120     -26.752  16.046  11.615  1.00 37.61           C
ANISOU 1074  C   ALA A 120     4461   4898   4931   -244    169   -355       C
ATOM   1075  O   ALA A 120     -26.111  14.988  11.644  1.00 39.47           O
ANISOU 1075  O   ALA A 120     4708   5132   5157   -229    194   -439       O
ATOM   1076  CB  ALA A 120     -29.148  15.427  11.931  1.00 28.63           C
ANISOU 1076  CB  ALA A 120     3412   3799   3667   -260     61   -389       C
ATOM   1077  N   ILE A 121     -26.423  17.060  10.812  1.00 40.44           N
ANISOU 1077  N   ILE A 121     4779   5290   5297   -255    221   -250       N
ATOM   1078  CA  ILE A 121     -25.234  17.003   9.963  1.00 42.57           C
ANISOU 1078  CA  ILE A 121     5007   5606   5563   -252    315   -229       C
ATOM   1079  C   ILE A 121     -23.980  16.780  10.805  1.00 45.71           C
ANISOU 1079  C   ILE A 121     5353   5919   6095   -240    325   -290       C
ATOM   1080  O   ILE A 121     -23.054  16.068  10.393  1.00 42.49           O
ANISOU 1080  O   ILE A 121     4926   5544   5672   -224    387   -335       O
ATOM   1081  CB  ILE A 121     -25.136  18.289   9.120  1.00 40.76           C
ANISOU 1081  CB  ILE A 121     4733   5410   5343   -266    371    -78       C
ATOM   1082  CG1 ILE A 121     -26.041  18.190   7.891  1.00 43.19           C
ANISOU 1082  CG1 ILE A 121     5083   5859   5467   -263    388    -22       C
ATOM   1083  CG2 ILE A 121     -23.697  18.576   8.712  1.00 43.80           C
ANISOU 1083  CG2 ILE A 121     5045   5792   5805   -268    466    -40       C
ATOM   1084  CD1 ILE A 121     -26.522  19.527   7.389  1.00 44.99           C
ANISOU 1084  CD1 ILE A 121     5285   6104   5706   -265    403    145       C
ATOM   1085  N   LEU A 122     -23.941  17.366  12.011  1.00 46.90           N
ANISOU 1085  N   LEU A 122     5476   5969   6376   -243    261   -298       N
ATOM   1086  CA  LEU A 122     -22.733  17.270  12.831  1.00 42.07           C
ANISOU 1086  CA  LEU A 122     4800   5294   5891   -232    258   -352       C
ATOM   1087  C   LEU A 122     -22.494  15.857  13.356  1.00 47.42           C
ANISOU 1087  C   LEU A 122     5509   5973   6535   -192    237   -460       C
ATOM   1088  O   LEU A 122     -21.412  15.297  13.101  1.00 54.36           O
ANISOU 1088  O   LEU A 122     6347   6869   7437   -171    293   -491       O
ATOM   1089  CB  LEU A 122     -22.785  18.311  13.952  1.00 37.84           C
ANISOU 1089  CB  LEU A 122     4226   4664   5490   -246    190   -346       C
ATOM   1090  CG  LEU A 122     -23.102  19.730  13.484  1.00 36.17           C
ANISOU 1090  CG  LEU A 122     3986   4422   5335   -281    213   -236       C
ATOM   1091  CD1 LEU A 122     -23.204  20.663  14.676  1.00 34.12           C
ANISOU 1091  CD1 LEU A 122     3694   4057   5212   -292    141   -263       C
ATOM   1092  CD2 LEU A 122     -22.040  20.218  12.505  1.00 35.83           C
ANISOU 1092  CD2 LEU A 122     3869   4400   5343   -305    315   -156       C
ATOM   1093  N   PRO A 123     -23.426  15.223  14.082  1.00 47.52           N
ANISOU 1093  N   PRO A 123     5588   5965   6503   -177    168   -512       N
ATOM   1094  CA  PRO A 123     -23.135  13.869  14.588  1.00 41.37           C
ANISOU 1094  CA  PRO A 123     4835   5172   5712   -135    160   -598       C
ATOM   1095  C   PRO A 123     -22.916  12.847  13.488  1.00 39.45           C
ANISOU 1095  C   PRO A 123     4624   4984   5383   -125    237   -635       C
ATOM   1096  O   PRO A 123     -22.143  11.898  13.680  1.00 40.14           O
ANISOU 1096  O   PRO A 123     4700   5052   5498    -84    265   -694       O
ATOM   1097  CB  PRO A 123     -24.371  13.535  15.434  1.00 36.98           C
ANISOU 1097  CB  PRO A 123     4344   4587   5119   -131     83   -621       C
ATOM   1098  CG  PRO A 123     -25.442  14.412  14.907  1.00 41.48           C
ANISOU 1098  CG  PRO A 123     4937   5186   5636   -171     69   -558       C
ATOM   1099  CD  PRO A 123     -24.761  15.680  14.512  1.00 42.56           C
ANISOU 1099  CD  PRO A 123     5007   5321   5844   -191    101   -489       C
ATOM   1100  N   VAL A 124     -23.568  13.014  12.335  1.00 43.78           N
ANISOU 1100  N   VAL A 124     5207   5604   5823   -157    272   -605       N
ATOM   1101  CA  VAL A 124     -23.335  12.110  11.211  1.00 42.60           C
ANISOU 1101  CA  VAL A 124     5086   5523   5579   -148    348   -657       C
ATOM   1102  C   VAL A 124     -21.899  12.240  10.728  1.00 45.94           C
ANISOU 1102  C   VAL A 124     5436   5969   6050   -125    436   -643       C
ATOM   1103  O   VAL A 124     -21.177  11.243  10.580  1.00 52.93           O
ANISOU 1103  O   VAL A 124     6320   6851   6941    -86    487   -717       O
ATOM   1104  CB  VAL A 124     -24.337  12.390  10.076  1.00 43.52           C
ANISOU 1104  CB  VAL A 124     5245   5739   5553   -184    358   -624       C
ATOM   1105  CG1 VAL A 124     -23.923  11.663   8.804  1.00 46.21           C
ANISOU 1105  CG1 VAL A 124     5601   6173   5783   -174    446   -679       C
ATOM   1106  CG2 VAL A 124     -25.737  11.984  10.492  1.00 42.83           C
ANISOU 1106  CG2 VAL A 124     5222   5636   5417   -206    278   -659       C
ATOM   1107  N   TYR A 125     -21.473  13.476  10.453  1.00 40.95           N
ANISOU 1107  N   TYR A 125     4739   5357   5464   -148    461   -544       N
ATOM   1108  CA  TYR A 125     -20.085  13.724  10.089  1.00 42.21           C
ANISOU 1108  CA  TYR A 125     4812   5534   5694   -134    546   -517       C
ATOM   1109  C   TYR A 125     -19.136  13.092  11.097  1.00 42.03           C
ANISOU 1109  C   TYR A 125     4741   5441   5788    -92    526   -586       C
ATOM   1110  O   TYR A 125     -18.157  12.443  10.713  1.00 44.06           O
ANISOU 1110  O   TYR A 125     4959   5723   6057    -53    601   -623       O
ATOM   1111  CB  TYR A 125     -19.829  15.230   9.981  1.00 45.51           C
ANISOU 1111  CB  TYR A 125     5158   5943   6193   -175    559   -396       C
ATOM   1112  CG  TYR A 125     -18.375  15.591   9.744  1.00 45.61           C
ANISOU 1112  CG  TYR A 125     5059   5960   6310   -172    642   -360       C
ATOM   1113  CD1 TYR A 125     -17.503  15.780  10.809  1.00 48.80           C
ANISOU 1113  CD1 TYR A 125     5381   6285   6875   -168    602   -389       C
ATOM   1114  CD2 TYR A 125     -17.877  15.743   8.456  1.00 46.73           C
ANISOU 1114  CD2 TYR A 125     5172   6198   6385   -172    761   -295       C
ATOM   1115  CE1 TYR A 125     -16.178  16.101  10.599  1.00 55.80           C
ANISOU 1115  CE1 TYR A 125     6152   7180   7868   -171    675   -359       C
ATOM   1116  CE2 TYR A 125     -16.549  16.068   8.236  1.00 53.45           C
ANISOU 1116  CE2 TYR A 125     5912   7056   7340   -171    846   -256       C
ATOM   1117  CZ  TYR A 125     -15.705  16.245   9.314  1.00 56.92           C
ANISOU 1117  CZ  TYR A 125     6264   7409   7955   -174    801   -289       C
ATOM   1118  OH  TYR A 125     -14.381  16.568   9.116  1.00 63.85           O
ANISOU 1118  OH  TYR A 125     7016   8296   8947   -179    882   -252       O
ATOM   1119  N   LEU A 126     -19.421  13.256  12.394  1.00 36.47           N
ANISOU 1119  N   LEU A 126     4037   4658   5164    -90    427   -602       N
ATOM   1120  CA  LEU A 126     -18.516  12.732  13.414  1.00 41.13           C
ANISOU 1120  CA  LEU A 126     4572   5198   5857    -42    397   -653       C
ATOM   1121  C   LEU A 126     -18.421  11.214  13.337  1.00 44.47           C
ANISOU 1121  C   LEU A 126     5046   5617   6233     16    427   -733       C
ATOM   1122  O   LEU A 126     -17.319  10.649  13.328  1.00 49.57           O
ANISOU 1122  O   LEU A 126     5634   6266   6936     66    476   -762       O
ATOM   1123  CB  LEU A 126     -18.965  13.167  14.810  1.00 38.93           C
ANISOU 1123  CB  LEU A 126     4294   4857   5641    -45    282   -659       C
ATOM   1124  CG  LEU A 126     -18.166  12.517  15.948  1.00 34.15           C
ANISOU 1124  CG  LEU A 126     3640   4221   5114     16    236   -710       C
ATOM   1125  CD1 LEU A 126     -16.696  12.890  15.840  1.00 39.67           C
ANISOU 1125  CD1 LEU A 126     4213   4940   5921     23    277   -701       C
ATOM   1126  CD2 LEU A 126     -18.705  12.899  17.318  1.00 32.71           C
ANISOU 1126  CD2 LEU A 126     3467   4000   4961     20    122   -721       C
ATOM   1127  N   LEU A 127     -19.570  10.538  13.289  1.00 33.39           N
ANISOU 1127  N   LEU A 127     3745   4202   4740     11    400   -770       N
ATOM   1128  CA  LEU A 127     -19.574   9.078  13.249  1.00 30.38           C
ANISOU 1128  CA  LEU A 127     3417   3791   4334     60    429   -851       C
ATOM   1129  C   LEU A 127     -18.786   8.555  12.052  1.00 37.18           C
ANISOU 1129  C   LEU A 127     4263   4705   5159     84    544   -891       C
ATOM   1130  O   LEU A 127     -17.863   7.735  12.206  1.00 46.32           O
ANISOU 1130  O   LEU A 127     5387   5835   6379    149    590   -934       O
ATOM   1131  CB  LEU A 127     -21.015   8.565  13.218  1.00 33.12           C
ANISOU 1131  CB  LEU A 127     3869   4120   4595     30    388   -883       C
ATOM   1132  CG  LEU A 127     -21.246   7.051  13.248  1.00 38.65           C
ANISOU 1132  CG  LEU A 127     4635   4763   5288     65    413   -970       C
ATOM   1133  CD1 LEU A 127     -20.585   6.410  14.466  1.00 33.51           C
ANISOU 1133  CD1 LEU A 127     3954   4029   4748    138    388   -969       C
ATOM   1134  CD2 LEU A 127     -22.738   6.744  13.219  1.00 43.39           C
ANISOU 1134  CD2 LEU A 127     5321   5349   5816     14    366   -994       C
ATOM   1135  N   THR A 128     -19.114   9.029  10.843  1.00 35.37           N
ANISOU 1135  N   THR A 128     4052   4562   4826     40    596   -872       N
ATOM   1136  CA  THR A 128     -18.433   8.421   9.702  1.00 40.44           C
ANISOU 1136  CA  THR A 128     4688   5268   5411     71    711   -925       C
ATOM   1137  C   THR A 128     -17.003   8.920   9.532  1.00 50.01           C
ANISOU 1137  C   THR A 128     5784   6512   6705    100    784   -875       C
ATOM   1138  O   THR A 128     -16.225   8.272   8.824  1.00 52.78           O
ANISOU 1138  O   THR A 128     6114   6901   7038    146    884   -926       O
ATOM   1139  CB  THR A 128     -19.196   8.607   8.385  1.00 39.58           C
ANISOU 1139  CB  THR A 128     4636   5267   5138     28    751   -931       C
ATOM   1140  OG1 THR A 128     -18.350   9.248   7.427  1.00 49.62           O
ANISOU 1140  OG1 THR A 128     5839   6637   6375     32    848   -872       O
ATOM   1141  CG2 THR A 128     -20.439   9.401   8.564  1.00 29.92           C
ANISOU 1141  CG2 THR A 128     3451   4053   3862    -34    663   -868       C
ATOM   1142  N   ARG A 129     -16.625  10.032  10.171  1.00 50.31           N
ANISOU 1142  N   ARG A 129     5742   6533   6842     73    739   -786       N
ATOM   1143  CA  ARG A 129     -15.210  10.382  10.220  1.00 46.64           C
ANISOU 1143  CA  ARG A 129     5151   6083   6489     98    796   -751       C
ATOM   1144  C   ARG A 129     -14.460   9.449  11.157  1.00 48.02           C
ANISOU 1144  C   ARG A 129     5287   6193   6766    173    773   -812       C
ATOM   1145  O   ARG A 129     -13.348   9.008  10.846  1.00 48.32           O
ANISOU 1145  O   ARG A 129     5251   6256   6852    228    855   -831       O
ATOM   1146  CB  ARG A 129     -15.037  11.837  10.655  1.00 44.63           C
ANISOU 1146  CB  ARG A 129     4816   5815   6326     38    750   -653       C
ATOM   1147  CG  ARG A 129     -13.640  12.192  11.152  1.00 49.12           C
ANISOU 1147  CG  ARG A 129     5240   6372   7051     55    767   -632       C
ATOM   1148  CD  ARG A 129     -13.674  13.411  12.080  1.00 61.77           C
ANISOU 1148  CD  ARG A 129     6780   7919   8769     -3    672   -583       C
ATOM   1149  NE  ARG A 129     -12.421  13.589  12.813  1.00 72.13           N
ANISOU 1149  NE  ARG A 129     7954   9216  10235     14    654   -593       N
ATOM   1150  CZ  ARG A 129     -12.273  14.361  13.888  1.00 68.42           C
ANISOU 1150  CZ  ARG A 129     7420   8698   9880    -19    553   -595       C
ATOM   1151  NH1 ARG A 129     -13.303  15.041  14.376  1.00 53.92           N
ANISOU 1151  NH1 ARG A 129     5649   6813   8023    -65    469   -585       N
ATOM   1152  NH2 ARG A 129     -11.087  14.452  14.477  1.00 70.98           N
ANISOU 1152  NH2 ARG A 129     7606   9027  10335     -3    534   -615       N
ATOM   1153  N   GLU A 130     -15.062   9.116  12.300  1.00 47.47           N
ANISOU 1153  N   GLU A 130     5264   6047   6725    185    666   -835       N
ATOM   1154  CA  GLU A 130     -14.397   8.236  13.250  1.00 46.50           C
ANISOU 1154  CA  GLU A 130     5105   5870   6692    267    639   -872       C
ATOM   1155  C   GLU A 130     -14.340   6.794  12.767  1.00 49.20           C
ANISOU 1155  C   GLU A 130     5508   6185   6999    335    714   -952       C
ATOM   1156  O   GLU A 130     -13.557   6.009  13.313  1.00 51.38           O
ANISOU 1156  O   GLU A 130     5739   6423   7360    420    725   -973       O
ATOM   1157  CB  GLU A 130     -15.090   8.302  14.613  1.00 47.68           C
ANISOU 1157  CB  GLU A 130     5289   5959   6869    266    509   -862       C
ATOM   1158  CG  GLU A 130     -14.814   9.587  15.381  1.00 55.13           C
ANISOU 1158  CG  GLU A 130     6146   6915   7886    224    429   -810       C
ATOM   1159  CD  GLU A 130     -13.337   9.941  15.415  1.00 67.34           C
ANISOU 1159  CD  GLU A 130     7544   8498   9545    246    461   -795       C
ATOM   1160  OE1 GLU A 130     -12.966  11.001  14.868  1.00 70.73           O
ANISOU 1160  OE1 GLU A 130     7904   8961  10008    183    495   -752       O
ATOM   1161  OE2 GLU A 130     -12.547   9.160  15.988  1.00 71.85           O
ANISOU 1161  OE2 GLU A 130     8061   9062  10176    328    455   -818       O
ATOM   1162  N   VAL A 131     -15.144   6.415  11.777  1.00 47.32           N
ANISOU 1162  N   VAL A 131     5369   5966   6645    305    765  -1000       N
ATOM   1163  CA  VAL A 131     -15.050   5.075  11.204  1.00 44.05           C
ANISOU 1163  CA  VAL A 131     5011   5522   6204    363    846  -1098       C
ATOM   1164  C   VAL A 131     -14.239   5.060   9.911  1.00 49.43           C
ANISOU 1164  C   VAL A 131     5649   6292   6838    382    979  -1128       C
ATOM   1165  O   VAL A 131     -13.400   4.179   9.719  1.00 56.69           O
ANISOU 1165  O   VAL A 131     6540   7192   7809    464   1060  -1186       O
ATOM   1166  CB  VAL A 131     -16.452   4.466  10.983  1.00 47.26           C
ANISOU 1166  CB  VAL A 131     5551   5888   6518    321    816  -1163       C
ATOM   1167  CG1 VAL A 131     -16.326   3.030  10.479  1.00 44.38           C
ANISOU 1167  CG1 VAL A 131     5242   5467   6154    379    898  -1282       C
ATOM   1168  CG2 VAL A 131     -17.265   4.513  12.274  1.00 45.32           C
ANISOU 1168  CG2 VAL A 131     5341   5563   6317    304    696  -1121       C
ATOM   1169  N   PHE A 132     -14.469   6.009   9.015  1.00 53.35           N
ANISOU 1169  N   PHE A 132     6140   6892   7238    316   1009  -1084       N
ATOM   1170  CA  PHE A 132     -13.803   6.052   7.714  1.00 58.31           C
ANISOU 1170  CA  PHE A 132     6734   7629   7793    333   1142  -1101       C
ATOM   1171  C   PHE A 132     -12.852   7.249   7.688  1.00 61.50           C
ANISOU 1171  C   PHE A 132     7005   8094   8267    313   1172   -982       C
ATOM   1172  O   PHE A 132     -12.110   7.432   8.658  1.00 69.64           O
ANISOU 1172  O   PHE A 132     7944   9072   9444    338   1129   -944       O
ATOM   1173  CB  PHE A 132     -14.848   6.057   6.601  1.00 58.78           C
ANISOU 1173  CB  PHE A 132     6895   7771   7668    281   1164  -1143       C
ATOM   1174  CG  PHE A 132     -15.806   4.898   6.647  1.00 57.38           C
ANISOU 1174  CG  PHE A 132     6837   7524   7441    285   1128  -1271       C
ATOM   1175  CD1 PHE A 132     -15.347   3.593   6.658  1.00 60.01           C
ANISOU 1175  CD1 PHE A 132     7192   7784   7827    361   1188  -1389       C
ATOM   1176  CD2 PHE A 132     -17.174   5.121   6.657  1.00 59.62           C
ANISOU 1176  CD2 PHE A 132     7206   7812   7637    212   1040  -1272       C
ATOM   1177  CE1 PHE A 132     -16.238   2.527   6.690  1.00 58.84           C
ANISOU 1177  CE1 PHE A 132     7150   7554   7654    355   1161  -1509       C
ATOM   1178  CE2 PHE A 132     -18.066   4.064   6.690  1.00 59.47           C
ANISOU 1178  CE2 PHE A 132     7285   7726   7586    203   1009  -1391       C
ATOM   1179  CZ  PHE A 132     -17.596   2.765   6.706  1.00 57.41           C
ANISOU 1179  CZ  PHE A 132     7047   7379   7388    270   1071  -1511       C
ATOM   1180  N   ASP A 133     -12.832   8.056   6.628  1.00 59.65           N
ANISOU 1180  N   ASP A 133     6752   7975   7940    270   1245   -920       N
ATOM   1181  CA  ASP A 133     -11.999   9.242   6.509  1.00 60.53           C
ANISOU 1181  CA  ASP A 133     6737   8136   8127    238   1286   -796       C
ATOM   1182  C   ASP A 133     -12.880  10.493   6.538  1.00 64.25           C
ANISOU 1182  C   ASP A 133     7232   8615   8565    147   1216   -690       C
ATOM   1183  O   ASP A 133     -14.068  10.435   6.877  1.00 66.61           O
ANISOU 1183  O   ASP A 133     7632   8874   8804    116   1119   -713       O
ATOM   1184  CB  ASP A 133     -11.157   9.165   5.232  1.00 64.99           C
ANISOU 1184  CB  ASP A 133     7248   8824   8622    273   1451   -787       C
ATOM   1185  CG  ASP A 133     -11.951   8.672   4.031  1.00 74.77           C
ANISOU 1185  CG  ASP A 133     8603  10161   9646    278   1510   -854       C
ATOM   1186  OD1 ASP A 133     -12.913   9.359   3.627  1.00 78.21           O
ANISOU 1186  OD1 ASP A 133     9099  10648   9971    214   1470   -793       O
ATOM   1187  OD2 ASP A 133     -11.611   7.599   3.485  1.00 78.85           O
ANISOU 1187  OD2 ASP A 133     9148  10708  10106    348   1594   -971       O
ATOM   1188  N   LYS A 134     -12.295  11.637   6.177  1.00 63.22           N
ANISOU 1188  N   LYS A 134     7002   8531   8487    106   1271   -568       N
ATOM   1189  CA  LYS A 134     -13.058  12.882   6.180  1.00 63.73           C
ANISOU 1189  CA  LYS A 134     7081   8590   8544     27   1217   -456       C
ATOM   1190  C   LYS A 134     -13.869  13.063   4.901  1.00 59.16           C
ANISOU 1190  C   LYS A 134     6583   8129   7766     11   1276   -412       C
ATOM   1191  O   LYS A 134     -14.928  13.705   4.929  1.00 54.84           O
ANISOU 1191  O   LYS A 134     6096   7573   7166    -36   1206   -354       O
ATOM   1192  CB  LYS A 134     -12.121  14.073   6.396  1.00 68.30           C
ANISOU 1192  CB  LYS A 134     7516   9146   9289    -17   1249   -338       C
ATOM   1193  CG  LYS A 134     -11.444  14.075   7.764  1.00 77.20           C
ANISOU 1193  CG  LYS A 134     8556  10167  10608    -14   1159   -382       C
ATOM   1194  CD  LYS A 134     -10.495  15.258   7.928  1.00 83.29           C
ANISOU 1194  CD  LYS A 134     9174  10917  11557    -70   1190   -283       C
ATOM   1195  CE  LYS A 134      -9.703  15.171   9.230  1.00 82.77           C
ANISOU 1195  CE  LYS A 134     9005  10775  11668    -60   1101   -345       C
ATOM   1196  NZ  LYS A 134     -10.574  15.293  10.434  1.00 81.16           N
ANISOU 1196  NZ  LYS A 134     8870  10480  11485    -77    939   -397       N
ATOM   1197  N   ARG A 135     -13.399  12.500   3.784  1.00 54.31           N
ANISOU 1197  N   ARG A 135     5968   7634   7032     57   1404   -441       N
ATOM   1198  CA  ARG A 135     -14.154  12.564   2.535  1.00 56.01           C
ANISOU 1198  CA  ARG A 135     6261   7990   7030     53   1456   -415       C
ATOM   1199  C   ARG A 135     -15.538  11.943   2.697  1.00 62.33           C
ANISOU 1199  C   ARG A 135     7196   8773   7712     42   1345   -516       C
ATOM   1200  O   ARG A 135     -16.562  12.571   2.386  1.00 69.48           O
ANISOU 1200  O   ARG A 135     8153   9725   8520      0   1294   -444       O
ATOM   1201  CB  ARG A 135     -13.372  11.857   1.425  1.00 54.74           C
ANISOU 1201  CB  ARG A 135     6082   7962   6754    117   1608   -470       C
ATOM   1202  CG  ARG A 135     -12.266  12.697   0.788  1.00 60.05           C
ANISOU 1202  CG  ARG A 135     6628   8715   7473    118   1748   -325       C
ATOM   1203  CD  ARG A 135     -10.960  11.914   0.680  1.00 68.00           C
ANISOU 1203  CD  ARG A 135     7553   9739   8545    188   1860   -403       C
ATOM   1204  NE  ARG A 135     -10.234  12.192  -0.561  1.00 78.89           N
ANISOU 1204  NE  ARG A 135     8868  11283   9825    217   2036   -321       N
ATOM   1205  CZ  ARG A 135      -9.493  13.278  -0.775  1.00 84.48           C
ANISOU 1205  CZ  ARG A 135     9451  12018  10630    183   2120   -145       C
ATOM   1206  NH1 ARG A 135      -9.374  14.204   0.168  1.00 86.48           N
ANISOU 1206  NH1 ARG A 135     9631  12136  11091    114   2039    -49       N
ATOM   1207  NH2 ARG A 135      -8.868  13.442  -1.935  1.00 82.43           N
ANISOU 1207  NH2 ARG A 135     9137  11920  10264    217   2291    -68       N
ATOM   1208  N   ALA A 136     -15.586  10.701   3.187  1.00 57.51           N
ANISOU 1208  N   ALA A 136     6639   8094   7119     80   1309   -676       N
ATOM   1209  CA  ALA A 136     -16.864  10.029   3.374  1.00 54.80           C
ANISOU 1209  CA  ALA A 136     6414   7723   6686     63   1209   -777       C
ATOM   1210  C   ALA A 136     -17.734  10.756   4.387  1.00 52.13           C
ANISOU 1210  C   ALA A 136     6091   7287   6428      8   1075   -706       C
ATOM   1211  O   ALA A 136     -18.957  10.800   4.226  1.00 48.13           O
ANISOU 1211  O   ALA A 136     5661   6807   5817    -27   1004   -715       O
ATOM   1212  CB  ALA A 136     -16.642   8.581   3.806  1.00 53.46           C
ANISOU 1212  CB  ALA A 136     6284   7466   6560    115   1207   -946       C
ATOM   1213  N   ALA A 137     -17.129  11.341   5.424  1.00 47.04           N
ANISOU 1213  N   ALA A 137     5370   6537   5967      0   1037   -642       N
ATOM   1214  CA  ALA A 137     -17.910  12.074   6.418  1.00 50.62           C
ANISOU 1214  CA  ALA A 137     5836   6900   6497    -46    915   -586       C
ATOM   1215  C   ALA A 137     -18.567  13.306   5.810  1.00 51.25           C
ANISOU 1215  C   ALA A 137     5915   7046   6510    -95    914   -451       C
ATOM   1216  O   ALA A 137     -19.728  13.615   6.114  1.00 57.93           O
ANISOU 1216  O   ALA A 137     6820   7871   7321   -126    823   -432       O
ATOM   1217  CB  ALA A 137     -17.021  12.460   7.599  1.00 56.09           C
ANISOU 1217  CB  ALA A 137     6437   7485   7390    -41    879   -561       C
ATOM   1218  N   VAL A 138     -17.844  14.018   4.946  1.00 45.17           N
ANISOU 1218  N   VAL A 138     5077   6357   5729    -97   1019   -346       N
ATOM   1219  CA  VAL A 138     -18.426  15.161   4.249  1.00 47.21           C
ANISOU 1219  CA  VAL A 138     5334   6684   5919   -132   1035   -196       C
ATOM   1220  C   VAL A 138     -19.583  14.707   3.368  1.00 53.29           C
ANISOU 1220  C   VAL A 138     6202   7578   6466   -126   1017   -230       C
ATOM   1221  O   VAL A 138     -20.670  15.311   3.361  1.00 61.28           O
ANISOU 1221  O   VAL A 138     7254   8602   7429   -154    947   -161       O
ATOM   1222  CB  VAL A 138     -17.341  15.883   3.434  1.00 50.08           C
ANISOU 1222  CB  VAL A 138     5600   7117   6311   -130   1172    -70       C
ATOM   1223  CG1 VAL A 138     -17.955  16.857   2.469  1.00 48.14           C
ANISOU 1223  CG1 VAL A 138     5364   6972   5954   -148   1211     92       C
ATOM   1224  CG2 VAL A 138     -16.385  16.585   4.367  1.00 52.30           C
ANISOU 1224  CG2 VAL A 138     5771   7267   6833   -157   1167    -23       C
ATOM   1225  N   ILE A 139     -19.366  13.625   2.617  1.00 52.34           N
ANISOU 1225  N   ILE A 139     6120   7556   6212    -89   1078   -346       N
ATOM   1226  CA  ILE A 139     -20.428  13.097   1.765  1.00 53.45           C
ANISOU 1226  CA  ILE A 139     6348   7825   6135    -88   1054   -409       C
ATOM   1227  C   ILE A 139     -21.645  12.715   2.599  1.00 56.10           C
ANISOU 1227  C   ILE A 139     6754   8072   6487   -118    914   -487       C
ATOM   1228  O   ILE A 139     -22.789  12.963   2.205  1.00 56.35           O
ANISOU 1228  O   ILE A 139     6831   8182   6397   -141    854   -459       O
ATOM   1229  CB  ILE A 139     -19.910  11.907   0.939  1.00 46.61           C
ANISOU 1229  CB  ILE A 139     5509   7056   5145    -42   1143   -557       C
ATOM   1230  CG1 ILE A 139     -18.710  12.338   0.096  1.00 39.52           C
ANISOU 1230  CG1 ILE A 139     4532   6260   4224     -7   1293   -466       C
ATOM   1231  CG2 ILE A 139     -21.017  11.354   0.054  1.00 41.98           C
ANISOU 1231  CG2 ILE A 139     5008   6610   4332    -49   1108   -646       C
ATOM   1232  CD1 ILE A 139     -18.095  11.221  -0.710  1.00 40.82           C
ANISOU 1232  CD1 ILE A 139     4714   6521   4273     48   1396   -613       C
ATOM   1233  N   ALA A 140     -21.418  12.121   3.771  1.00 55.29           N
ANISOU 1233  N   ALA A 140     6656   7816   6537   -115    862   -577       N
ATOM   1234  CA  ALA A 140     -22.526  11.662   4.597  1.00 48.88           C
ANISOU 1234  CA  ALA A 140     5908   6920   5744   -141    743   -649       C
ATOM   1235  C   ALA A 140     -23.290  12.833   5.189  1.00 50.48           C
ANISOU 1235  C   ALA A 140     6097   7079   6005   -176    661   -522       C
ATOM   1236  O   ALA A 140     -24.515  12.773   5.321  1.00 47.17           O
ANISOU 1236  O   ALA A 140     5728   6669   5524   -201    577   -536       O
ATOM   1237  CB  ALA A 140     -22.016  10.745   5.706  1.00 46.96           C
ANISOU 1237  CB  ALA A 140     5668   6531   5646   -117    720   -755       C
ATOM   1238  N   ALA A 141     -22.585  13.900   5.566  1.00 47.45           N
ANISOU 1238  N   ALA A 141     5640   6641   5749   -179    684   -402       N
ATOM   1239  CA  ALA A 141     -23.279  15.105   6.007  1.00 46.34           C
ANISOU 1239  CA  ALA A 141     5484   6455   5666   -207    621   -281       C
ATOM   1240  C   ALA A 141     -24.187  15.631   4.903  1.00 48.60           C
ANISOU 1240  C   ALA A 141     5796   6881   5790   -216    628   -188       C
ATOM   1241  O   ALA A 141     -25.377  15.910   5.127  1.00 54.08           O
ANISOU 1241  O   ALA A 141     6524   7574   6449   -232    544   -163       O
ATOM   1242  CB  ALA A 141     -22.266  16.165   6.433  1.00 50.48           C
ANISOU 1242  CB  ALA A 141     5918   6899   6362   -215    660   -179       C
ATOM   1243  N   PHE A 142     -23.648  15.739   3.687  1.00 45.41           N
ANISOU 1243  N   PHE A 142     5370   6609   5274   -199    729   -133       N
ATOM   1244  CA  PHE A 142     -24.476  16.196   2.575  1.00 45.77           C
ANISOU 1244  CA  PHE A 142     5436   6815   5139   -196    736    -37       C
ATOM   1245  C   PHE A 142     -25.681  15.284   2.370  1.00 45.20           C
ANISOU 1245  C   PHE A 142     5441   6820   4915   -204    652   -161       C
ATOM   1246  O   PHE A 142     -26.806  15.761   2.180  1.00 45.95           O
ANISOU 1246  O   PHE A 142     5552   6974   4935   -214    584    -93       O
ATOM   1247  CB  PHE A 142     -23.654  16.279   1.296  1.00 48.77           C
ANISOU 1247  CB  PHE A 142     5786   7347   5399   -167    866     26       C
ATOM   1248  CG  PHE A 142     -24.371  16.955   0.164  1.00 50.27           C
ANISOU 1248  CG  PHE A 142     5981   7712   5407   -153    882    167       C
ATOM   1249  CD1 PHE A 142     -24.242  18.320  -0.034  1.00 51.95           C
ANISOU 1249  CD1 PHE A 142     6137   7913   5687   -151    927    387       C
ATOM   1250  CD2 PHE A 142     -25.176  16.227  -0.702  1.00 47.20           C
ANISOU 1250  CD2 PHE A 142     5649   7500   4784   -142    852     80       C
ATOM   1251  CE1 PHE A 142     -24.895  18.948  -1.074  1.00 53.69           C
ANISOU 1251  CE1 PHE A 142     6359   8301   5740   -127    945    539       C
ATOM   1252  CE2 PHE A 142     -25.834  16.849  -1.744  1.00 47.70           C
ANISOU 1252  CE2 PHE A 142     5711   7748   4665   -121    859    216       C
ATOM   1253  CZ  PHE A 142     -25.694  18.212  -1.931  1.00 51.23           C
ANISOU 1253  CZ  PHE A 142     6103   8188   5176   -108    907    456       C
ATOM   1254  N   LEU A 143     -25.468  13.969   2.412  1.00 45.32           N
ANISOU 1254  N   LEU A 143     5496   6829   4894   -201    655   -344       N
ATOM   1255  CA  LEU A 143     -26.558  13.040   2.138  1.00 47.14           C
ANISOU 1255  CA  LEU A 143     5792   7130   4990   -220    583   -477       C
ATOM   1256  C   LEU A 143     -27.604  13.049   3.247  1.00 50.72           C
ANISOU 1256  C   LEU A 143     6267   7464   5540   -253    464   -494       C
ATOM   1257  O   LEU A 143     -28.793  12.858   2.972  1.00 53.67           O
ANISOU 1257  O   LEU A 143     6669   7915   5807   -277    390   -523       O
ATOM   1258  CB  LEU A 143     -26.007  11.631   1.927  1.00 46.29           C
ANISOU 1258  CB  LEU A 143     5721   7019   4850   -208    628   -672       C
ATOM   1259  CG  LEU A 143     -25.142  11.471   0.673  1.00 48.46           C
ANISOU 1259  CG  LEU A 143     5982   7447   4986   -171    748   -685       C
ATOM   1260  CD1 LEU A 143     -24.725  10.020   0.475  1.00 44.37           C
ANISOU 1260  CD1 LEU A 143     5506   6914   4439   -155    789   -899       C
ATOM   1261  CD2 LEU A 143     -25.858  12.012  -0.564  1.00 50.15           C
ANISOU 1261  CD2 LEU A 143     6200   7882   4974   -169    747   -605       C
ATOM   1262  N   ILE A 144     -27.193  13.272   4.497  1.00 51.76           N
ANISOU 1262  N   ILE A 144     6378   7423   5865   -252    443   -476       N
ATOM   1263  CA  ILE A 144     -28.170  13.419   5.566  1.00 48.09           C
ANISOU 1263  CA  ILE A 144     5929   6859   5485   -275    341   -473       C
ATOM   1264  C   ILE A 144     -28.909  14.738   5.441  1.00 50.11           C
ANISOU 1264  C   ILE A 144     6157   7154   5729   -278    305   -312       C
ATOM   1265  O   ILE A 144     -29.981  14.903   6.034  1.00 47.47           O
ANISOU 1265  O   ILE A 144     5835   6785   5417   -294    221   -303       O
ATOM   1266  CB  ILE A 144     -27.520  13.304   6.958  1.00 39.83           C
ANISOU 1266  CB  ILE A 144     4867   5635   4630   -265    327   -502       C
ATOM   1267  CG1 ILE A 144     -28.526  12.741   7.965  1.00 38.82           C
ANISOU 1267  CG1 ILE A 144     4778   5425   4546   -284    235   -571       C
ATOM   1268  CG2 ILE A 144     -27.021  14.658   7.443  1.00 28.76           C
ANISOU 1268  CG2 ILE A 144     3406   4168   3353   -258    336   -366       C
ATOM   1269  CD1 ILE A 144     -28.949  11.320   7.678  1.00 37.87           C
ANISOU 1269  CD1 ILE A 144     4712   5327   4352   -301    227   -719       C
ATOM   1270  N   ALA A 145     -28.365  15.695   4.688  1.00 55.13           N
ANISOU 1270  N   ALA A 145     6751   7857   6340   -260    373   -176       N
ATOM   1271  CA  ALA A 145     -29.128  16.915   4.464  1.00 54.29           C
ANISOU 1271  CA  ALA A 145     6621   7788   6220   -255    346    -13       C
ATOM   1272  C   ALA A 145     -30.311  16.723   3.517  1.00 57.10           C
ANISOU 1272  C   ALA A 145     7000   8320   6374   -256    299     -4       C
ATOM   1273  O   ALA A 145     -31.150  17.626   3.425  1.00 60.96           O
ANISOU 1273  O   ALA A 145     7469   8841   6851   -245    258    125       O
ATOM   1274  CB  ALA A 145     -28.215  18.019   3.927  1.00 55.74           C
ANISOU 1274  CB  ALA A 145     6749   7982   6450   -236    441    150       C
ATOM   1275  N   ILE A 146     -30.413  15.587   2.818  1.00 51.92           N
ANISOU 1275  N   ILE A 146     6381   7781   5566   -266    302   -142       N
ATOM   1276  CA  ILE A 146     -31.404  15.420   1.760  1.00 49.15           C
ANISOU 1276  CA  ILE A 146     6042   7631   5003   -268    261   -143       C
ATOM   1277  C   ILE A 146     -32.144  14.092   1.819  1.00 51.26           C
ANISOU 1277  C   ILE A 146     6352   7925   5199   -309    190   -346       C
ATOM   1278  O   ILE A 146     -33.003  13.845   0.971  1.00 52.14           O
ANISOU 1278  O   ILE A 146     6467   8208   5133   -320    142   -378       O
ATOM   1279  CB  ILE A 146     -30.776  15.599   0.361  1.00 53.02           C
ANISOU 1279  CB  ILE A 146     6518   8308   5317   -235    352    -82       C
ATOM   1280  CG1 ILE A 146     -29.737  14.507   0.099  1.00 46.36           C
ANISOU 1280  CG1 ILE A 146     5702   7463   4448   -235    428   -246       C
ATOM   1281  CG2 ILE A 146     -30.165  16.985   0.201  1.00 56.80           C
ANISOU 1281  CG2 ILE A 146     6946   8766   5869   -199    427    146       C
ATOM   1282  CD1 ILE A 146     -29.499  14.239  -1.366  1.00 42.55           C
ANISOU 1282  CD1 ILE A 146     5225   7213   3729   -209    493   -264       C
ATOM   1283  N   VAL A 147     -31.848  13.217   2.771  1.00 45.51           N
ANISOU 1283  N   VAL A 147     5652   7036   4603   -333    182   -482       N
ATOM   1284  CA  VAL A 147     -32.582  11.944   2.793  1.00 45.35           C
ANISOU 1284  CA  VAL A 147     5671   7028   4533   -378    124   -668       C
ATOM   1285  C   VAL A 147     -34.024  12.203   3.223  1.00 50.20           C
ANISOU 1285  C   VAL A 147     6270   7651   5152   -408     15   -633       C
ATOM   1286  O   VAL A 147     -34.257  12.976   4.171  1.00 51.98           O
ANISOU 1286  O   VAL A 147     6475   7766   5510   -396    -12   -524       O
ATOM   1287  CB  VAL A 147     -31.889  10.934   3.716  1.00 42.50           C
ANISOU 1287  CB  VAL A 147     5341   6484   4322   -386    152   -801       C
ATOM   1288  CG1 VAL A 147     -31.935  11.380   5.175  1.00 41.05           C
ANISOU 1288  CG1 VAL A 147     5145   6120   4332   -382    117   -730       C
ATOM   1289  CG2 VAL A 147     -32.516   9.558   3.554  1.00 46.11           C
ANISOU 1289  CG2 VAL A 147     5839   6948   4733   -434    115   -997       C
ATOM   1290  N   PRO A 148     -35.024  11.624   2.545  1.00 49.85           N
ANISOU 1290  N   PRO A 148     6229   7744   4967   -446    -48   -725       N
ATOM   1291  CA  PRO A 148     -36.418  11.894   2.921  1.00 48.13           C
ANISOU 1291  CA  PRO A 148     5983   7550   4757   -474   -150   -684       C
ATOM   1292  C   PRO A 148     -37.005  10.838   3.848  1.00 49.12           C
ANISOU 1292  C   PRO A 148     6127   7541   4995   -532   -199   -826       C
ATOM   1293  O   PRO A 148     -36.320  10.349   4.753  1.00 52.07           O
ANISOU 1293  O   PRO A 148     6531   7738   5516   -530   -157   -876       O
ATOM   1294  CB  PRO A 148     -37.132  11.922   1.566  1.00 43.35           C
ANISOU 1294  CB  PRO A 148     5354   7195   3922   -482   -194   -694       C
ATOM   1295  CG  PRO A 148     -36.359  10.948   0.730  1.00 40.58           C
ANISOU 1295  CG  PRO A 148     5043   6911   3464   -493   -135   -858       C
ATOM   1296  CD  PRO A 148     -34.932  10.923   1.252  1.00 47.77           C
ANISOU 1296  CD  PRO A 148     5983   7659   4509   -457    -29   -847       C
ATOM   1297  N   GLY A 149     -38.277  10.493   3.639  1.00 43.28           N
ANISOU 1297  N   GLY A 149     5362   6890   4191   -582   -285   -881       N
ATOM   1298  CA  GLY A 149     -38.929   9.477   4.446  1.00 34.28           C
ANISOU 1298  CA  GLY A 149     4232   5631   3161   -646   -326  -1006       C
ATOM   1299  C   GLY A 149     -39.237   9.956   5.856  1.00 33.61           C
ANISOU 1299  C   GLY A 149     4133   5388   3249   -630   -341   -902       C
ATOM   1300  O   GLY A 149     -39.428  11.150   6.113  1.00 35.96           O
ANISOU 1300  O   GLY A 149     4398   5702   3562   -582   -354   -741       O
ATOM   1301  N   GLN A 150     -39.280   8.998   6.787  1.00 31.61           N
ANISOU 1301  N   GLN A 150     3906   4977   3129   -666   -334   -997       N
ATOM   1302  CA  GLN A 150     -39.645   9.316   8.164  1.00 35.72           C
ANISOU 1302  CA  GLN A 150     4413   5362   3797   -651   -348   -914       C
ATOM   1303  C   GLN A 150     -38.670  10.306   8.783  1.00 40.76           C
ANISOU 1303  C   GLN A 150     5061   5919   4508   -575   -300   -790       C
ATOM   1304  O   GLN A 150     -39.071  11.175   9.567  1.00 42.48           O
ANISOU 1304  O   GLN A 150     5253   6099   4791   -543   -323   -679       O
ATOM   1305  CB  GLN A 150     -39.715   8.040   9.004  1.00 39.44           C
ANISOU 1305  CB  GLN A 150     4914   5682   4390   -695   -333  -1026       C
ATOM   1306  CG  GLN A 150     -40.685   7.002   8.479  1.00 45.59           C
ANISOU 1306  CG  GLN A 150     5677   6511   5133   -785   -376  -1162       C
ATOM   1307  CD  GLN A 150     -42.117   7.270   8.895  1.00 60.11           C
ANISOU 1307  CD  GLN A 150     7453   8394   6992   -822   -449  -1107       C
ATOM   1308  OE1 GLN A 150     -42.505   8.415   9.135  1.00 62.38           O
ANISOU 1308  OE1 GLN A 150     7702   8738   7262   -775   -478   -966       O
ATOM   1309  NE2 GLN A 150     -42.916   6.210   8.981  1.00 62.72           N
ANISOU 1309  NE2 GLN A 150     7767   8693   7372   -907   -474  -1219       N
ATOM   1310  N   PHE A 151     -37.386  10.197   8.436  1.00 44.01           N
ANISOU 1310  N   PHE A 151     5504   6304   4912   -545   -233   -816       N
ATOM   1311  CA  PHE A 151     -36.390  11.106   8.992  1.00 35.15           C
ANISOU 1311  CA  PHE A 151     4380   5104   3870   -484   -189   -713       C
ATOM   1312  C   PHE A 151     -36.713  12.556   8.644  1.00 31.40           C
ANISOU 1312  C   PHE A 151     3864   4713   3353   -450   -208   -560       C
ATOM   1313  O   PHE A 151     -36.732  13.429   9.521  1.00 29.00           O
ANISOU 1313  O   PHE A 151     3542   4328   3148   -417   -216   -466       O
ATOM   1314  CB  PHE A 151     -34.996  10.727   8.492  1.00 30.92           C
ANISOU 1314  CB  PHE A 151     3871   4554   3324   -462   -111   -766       C
ATOM   1315  CG  PHE A 151     -33.906  11.607   9.033  1.00 28.81           C
ANISOU 1315  CG  PHE A 151     3589   4208   3149   -409    -67   -672       C
ATOM   1316  CD1 PHE A 151     -33.362  11.363  10.280  1.00 28.50           C
ANISOU 1316  CD1 PHE A 151     3558   4022   3248   -387    -59   -688       C
ATOM   1317  CD2 PHE A 151     -33.440  12.688   8.300  1.00 31.70           C
ANISOU 1317  CD2 PHE A 151     3927   4652   3467   -383    -34   -564       C
ATOM   1318  CE1 PHE A 151     -32.364  12.177  10.789  1.00 31.30           C
ANISOU 1318  CE1 PHE A 151     3889   4313   3691   -346    -29   -617       C
ATOM   1319  CE2 PHE A 151     -32.450  13.506   8.803  1.00 40.66           C
ANISOU 1319  CE2 PHE A 151     5037   5705   4707   -346      6   -486       C
ATOM   1320  CZ  PHE A 151     -31.908  13.247  10.051  1.00 39.43           C
ANISOU 1320  CZ  PHE A 151     4886   5406   4688   -331      3   -522       C
ATOM   1321  N   LEU A 152     -36.974  12.830   7.363  1.00 28.44           N
ANISOU 1321  N   LEU A 152     3473   4502   2831   -455   -213   -532       N
ATOM   1322  CA  LEU A 152     -37.273  14.197   6.949  1.00 34.41           C
ANISOU 1322  CA  LEU A 152     4188   5338   3548   -415   -223   -367       C
ATOM   1323  C   LEU A 152     -38.655  14.637   7.427  1.00 37.00           C
ANISOU 1323  C   LEU A 152     4478   5683   3897   -417   -300   -307       C
ATOM   1324  O   LEU A 152     -38.830  15.777   7.869  1.00 31.98           O
ANISOU 1324  O   LEU A 152     3815   5004   3333   -373   -304   -176       O
ATOM   1325  CB  LEU A 152     -37.168  14.315   5.428  1.00 32.65           C
ANISOU 1325  CB  LEU A 152     3956   5306   3144   -409   -205   -342       C
ATOM   1326  CG  LEU A 152     -37.782  15.546   4.763  1.00 39.14           C
ANISOU 1326  CG  LEU A 152     4730   6255   3886   -369   -228   -167       C
ATOM   1327  CD1 LEU A 152     -36.941  16.776   5.077  1.00 43.22           C
ANISOU 1327  CD1 LEU A 152     5234   6672   4516   -316   -164    -12       C
ATOM   1328  CD2 LEU A 152     -37.876  15.334   3.261  1.00 36.39           C
ANISOU 1328  CD2 LEU A 152     4375   6131   3320   -369   -227   -175       C
ATOM   1329  N   GLN A 153     -39.646  13.745   7.360  1.00 31.82           N
ANISOU 1329  N   GLN A 153     3815   5083   3191   -469   -359   -405       N
ATOM   1330  CA  GLN A 153     -41.002  14.120   7.746  1.00 31.14           C
ANISOU 1330  CA  GLN A 153     3680   5031   3121   -473   -430   -348       C
ATOM   1331  C   GLN A 153     -41.111  14.407   9.237  1.00 33.20           C
ANISOU 1331  C   GLN A 153     3943   5125   3547   -451   -426   -317       C
ATOM   1332  O   GLN A 153     -41.944  15.224   9.645  1.00 40.60           O
ANISOU 1332  O   GLN A 153     4837   6069   4520   -419   -460   -220       O
ATOM   1333  CB  GLN A 153     -41.983  13.021   7.338  1.00 34.21           C
ANISOU 1333  CB  GLN A 153     4052   5516   3432   -546   -491   -473       C
ATOM   1334  CG  GLN A 153     -42.305  13.015   5.847  1.00 43.93           C
ANISOU 1334  CG  GLN A 153     5256   6964   4470   -559   -526   -483       C
ATOM   1335  CD  GLN A 153     -42.935  11.716   5.386  1.00 63.92           C
ANISOU 1335  CD  GLN A 153     7782   9571   6932   -646   -576   -662       C
ATOM   1336  OE1 GLN A 153     -43.417  11.613   4.257  1.00 79.08           O
ANISOU 1336  OE1 GLN A 153     9671  11688   8690   -666   -625   -696       O
ATOM   1337  NE2 GLN A 153     -42.934  10.714   6.260  1.00 63.57           N
ANISOU 1337  NE2 GLN A 153     7767   9374   7015   -698   -563   -779       N
ATOM   1338  N   ARG A 154     -40.288  13.761  10.061  1.00 29.64           N
ANISOU 1338  N   ARG A 154     3537   4532   3191   -458   -385   -396       N
ATOM   1339  CA  ARG A 154     -40.287  14.008  11.496  1.00 31.01           C
ANISOU 1339  CA  ARG A 154     3715   4564   3502   -430   -379   -373       C
ATOM   1340  C   ARG A 154     -39.277  15.068  11.911  1.00 36.36           C
ANISOU 1340  C   ARG A 154     4400   5158   4257   -371   -338   -294       C
ATOM   1341  O   ARG A 154     -39.157  15.355  13.108  1.00 35.86           O
ANISOU 1341  O   ARG A 154     4341   4985   4300   -341   -335   -285       O
ATOM   1342  CB  ARG A 154     -40.012  12.709  12.257  1.00 36.56           C
ANISOU 1342  CB  ARG A 154     4458   5166   4268   -464   -362   -490       C
ATOM   1343  CG  ARG A 154     -41.210  11.773  12.323  1.00 46.11           C
ANISOU 1343  CG  ARG A 154     5649   6409   5463   -526   -404   -555       C
ATOM   1344  CD  ARG A 154     -40.786  10.317  12.249  1.00 52.15           C
ANISOU 1344  CD  ARG A 154     6455   7115   6243   -577   -376   -688       C
ATOM   1345  NE  ARG A 154     -41.912   9.444  11.934  1.00 58.82           N
ANISOU 1345  NE  ARG A 154     7274   8011   7064   -654   -416   -764       N
ATOM   1346  CZ  ARG A 154     -42.519   8.656  12.815  1.00 59.58           C
ANISOU 1346  CZ  ARG A 154     7365   8023   7251   -689   -417   -795       C
ATOM   1347  NH1 ARG A 154     -42.111   8.622  14.077  1.00 51.49           N
ANISOU 1347  NH1 ARG A 154     6365   6872   6329   -645   -380   -753       N
ATOM   1348  NH2 ARG A 154     -43.540   7.901  12.431  1.00 67.52           N
ANISOU 1348  NH2 ARG A 154     8334   9076   8242   -771   -453   -867       N
ATOM   1349  N   SER A 155     -38.541  15.642  10.956  1.00 34.38           N
ANISOU 1349  N   SER A 155     4148   4960   3956   -355   -303   -241       N
ATOM   1350  CA  SER A 155     -37.590  16.714  11.224  1.00 39.53           C
ANISOU 1350  CA  SER A 155     4793   5531   4694   -310   -260   -161       C
ATOM   1351  C   SER A 155     -37.975  17.984  10.479  1.00 43.54           C
ANISOU 1351  C   SER A 155     5262   6109   5172   -276   -260    -15       C
ATOM   1352  O   SER A 155     -37.154  18.898  10.338  1.00 43.27           O
ANISOU 1352  O   SER A 155     5217   6025   5197   -248   -213     65       O
ATOM   1353  CB  SER A 155     -36.167  16.283  10.854  1.00 38.63           C
ANISOU 1353  CB  SER A 155     4705   5392   4581   -317   -199   -212       C
ATOM   1354  OG  SER A 155     -36.070  15.922   9.484  1.00 39.79           O
ANISOU 1354  OG  SER A 155     4855   5672   4590   -336   -178   -219       O
ATOM   1355  N   ILE A 156     -39.213  18.047  10.003  1.00 43.36           N
ANISOU 1355  N   ILE A 156     5211   6199   5065   -278   -311     26       N
ATOM   1356  CA  ILE A 156     -39.714  19.177   9.239  1.00 44.36           C
ANISOU 1356  CA  ILE A 156     5294   6409   5150   -236   -316    179       C
ATOM   1357  C   ILE A 156     -40.271  20.226  10.193  1.00 44.93           C
ANISOU 1357  C   ILE A 156     5340   6379   5354   -187   -330    259       C
ATOM   1358  O   ILE A 156     -40.527  19.963  11.371  1.00 41.06           O
ANISOU 1358  O   ILE A 156     4858   5791   4950   -190   -349    186       O
ATOM   1359  CB  ILE A 156     -40.781  18.721   8.221  1.00 47.41           C
ANISOU 1359  CB  ILE A 156     5654   6990   5371   -256   -372    182       C
ATOM   1360  CG1 ILE A 156     -40.658  19.519   6.928  1.00 56.84           C
ANISOU 1360  CG1 ILE A 156     6822   8318   6459   -218   -351    324       C
ATOM   1361  CG2 ILE A 156     -42.189  18.832   8.802  1.00 39.86           C
ANISOU 1361  CG2 ILE A 156     4654   6050   4442   -248   -440    199       C
ATOM   1362  CD1 ILE A 156     -39.501  19.092   6.076  1.00 59.25           C
ANISOU 1362  CD1 ILE A 156     7160   8673   6678   -236   -290    287       C
ATOM   1363  N   LEU A 157     -40.453  21.438   9.672  1.00 51.15           N
ANISOU 1363  N   LEU A 157     6091   7186   6156   -136   -314    413       N
ATOM   1364  CA  LEU A 157     -41.040  22.517  10.456  1.00 47.53           C
ANISOU 1364  CA  LEU A 157     5604   6629   5828    -80   -321    492       C
ATOM   1365  C   LEU A 157     -42.409  22.110  10.985  1.00 42.29           C
ANISOU 1365  C   LEU A 157     4913   6015   5139    -78   -387    453       C
ATOM   1366  O   LEU A 157     -43.251  21.598  10.241  1.00 50.23           O
ANISOU 1366  O   LEU A 157     5890   7178   6016    -96   -435    461       O
ATOM   1367  CB  LEU A 157     -41.158  23.778   9.598  1.00 44.06           C
ANISOU 1367  CB  LEU A 157     5125   6222   5395    -22   -293    681       C
ATOM   1368  CG  LEU A 157     -41.891  24.985  10.180  1.00 40.89           C
ANISOU 1368  CG  LEU A 157     4686   5729   5124     49   -296    783       C
ATOM   1369  CD1 LEU A 157     -40.985  25.745  11.137  1.00 44.51           C
ANISOU 1369  CD1 LEU A 157     5162   5973   5774     60   -244    758       C
ATOM   1370  CD2 LEU A 157     -42.380  25.890   9.059  1.00 40.83           C
ANISOU 1370  CD2 LEU A 157     4631   5819   5065    109   -286    983       C
ATOM   1371  N   GLY A 158     -42.622  22.322  12.282  1.00 34.38           N
ANISOU 1371  N   GLY A 158     3916   4888   4260    -57   -390    405       N
ATOM   1372  CA  GLY A 158     -43.898  22.075  12.906  1.00 42.29           C
ANISOU 1372  CA  GLY A 158     4884   5923   5260    -46   -437    383       C
ATOM   1373  C   GLY A 158     -44.071  20.702  13.521  1.00 45.21           C
ANISOU 1373  C   GLY A 158     5278   6304   5595   -108   -461    242       C
ATOM   1374  O   GLY A 158     -45.017  20.501  14.292  1.00 47.99           O
ANISOU 1374  O   GLY A 158     5604   6656   5974    -99   -485    219       O
ATOM   1375  N   PHE A 159     -43.197  19.749  13.210  1.00 38.19           N
ANISOU 1375  N   PHE A 159     4435   5420   4655   -166   -447    153       N
ATOM   1376  CA  PHE A 159     -43.333  18.400  13.753  1.00 39.47           C
ANISOU 1376  CA  PHE A 159     4622   5576   4799   -223   -461     29       C
ATOM   1377  C   PHE A 159     -42.458  18.248  14.995  1.00 38.71           C
ANISOU 1377  C   PHE A 159     4571   5334   4803   -210   -427    -39       C
ATOM   1378  O   PHE A 159     -41.462  17.523  15.015  1.00 35.96           O
ANISOU 1378  O   PHE A 159     4267   4945   4453   -239   -402   -114       O
ATOM   1379  CB  PHE A 159     -42.991  17.356  12.693  1.00 40.64           C
ANISOU 1379  CB  PHE A 159     4790   5814   4836   -288   -466    -39       C
ATOM   1380  CG  PHE A 159     -43.748  16.066  12.867  1.00 44.42           C
ANISOU 1380  CG  PHE A 159     5263   6332   5281   -353   -498   -139       C
ATOM   1381  CD1 PHE A 159     -44.921  15.828  12.162  1.00 29.52           C
ANISOU 1381  CD1 PHE A 159     3320   4584   3312   -386   -553   -129       C
ATOM   1382  CD2 PHE A 159     -43.303  15.106  13.763  1.00 41.99           C
ANISOU 1382  CD2 PHE A 159     4998   5920   5035   -381   -474   -235       C
ATOM   1383  CE1 PHE A 159     -45.617  14.654  12.333  1.00 28.91           C
ANISOU 1383  CE1 PHE A 159     3228   4529   3226   -457   -580   -225       C
ATOM   1384  CE2 PHE A 159     -44.001  13.929  13.940  1.00 40.08           C
ANISOU 1384  CE2 PHE A 159     4749   5694   4787   -444   -493   -315       C
ATOM   1385  CZ  PHE A 159     -45.159  13.703  13.224  1.00 36.44           C
ANISOU 1385  CZ  PHE A 159     4230   5359   4256   -487   -545   -315       C
ATOM   1386  N   ASN A 160     -42.864  18.948  16.056  1.00 35.17           N
ANISOU 1386  N   ASN A 160     4107   4817   4439   -157   -427    -15       N
ATOM   1387  CA  ASN A 160     -42.096  18.956  17.301  1.00 37.12           C
ANISOU 1387  CA  ASN A 160     4389   4945   4769   -133   -404    -77       C
ATOM   1388  C   ASN A 160     -42.387  17.671  18.070  1.00 37.53           C
ANISOU 1388  C   ASN A 160     4460   4996   4802   -164   -409   -157       C
ATOM   1389  O   ASN A 160     -43.140  17.638  19.048  1.00 36.78           O
ANISOU 1389  O   ASN A 160     4350   4892   4734   -138   -415   -161       O
ATOM   1390  CB  ASN A 160     -42.409  20.193  18.133  1.00 36.28           C
ANISOU 1390  CB  ASN A 160     4261   4773   4752    -62   -400    -38       C
ATOM   1391  CG  ASN A 160     -41.364  20.450  19.203  1.00 39.99           C
ANISOU 1391  CG  ASN A 160     4763   5131   5301    -36   -381   -106       C
ATOM   1392  OD1 ASN A 160     -40.171  20.233  18.984  1.00 43.53           O
ANISOU 1392  OD1 ASN A 160     5237   5543   5761    -60   -366   -141       O
ATOM   1393  ND2 ASN A 160     -41.806  20.911  20.367  1.00 42.03           N
ANISOU 1393  ND2 ASN A 160     5012   5346   5610     16   -384   -130       N
ATOM   1394  N   ASP A 161     -41.770  16.591  17.606  1.00 36.42           N
ANISOU 1394  N   ASP A 161     4352   4865   4621   -218   -400   -217       N
ATOM   1395  CA  ASP A 161     -41.762  15.302  18.276  1.00 34.26           C
ANISOU 1395  CA  ASP A 161     4105   4562   4349   -248   -392   -288       C
ATOM   1396  C   ASP A 161     -40.318  14.911  18.571  1.00 42.49           C
ANISOU 1396  C   ASP A 161     5193   5528   5422   -240   -363   -343       C
ATOM   1397  O   ASP A 161     -39.370  15.535  18.083  1.00 43.80           O
ANISOU 1397  O   ASP A 161     5366   5678   5600   -227   -350   -333       O
ATOM   1398  CB  ASP A 161     -42.457  14.234  17.421  1.00 34.95           C
ANISOU 1398  CB  ASP A 161     4183   4724   4375   -321   -407   -321       C
ATOM   1399  CG  ASP A 161     -42.970  13.072  18.244  1.00 47.64           C
ANISOU 1399  CG  ASP A 161     5795   6296   6009   -351   -398   -364       C
ATOM   1400  OD1 ASP A 161     -42.613  12.984  19.439  1.00 52.69           O
ANISOU 1400  OD1 ASP A 161     6457   6863   6701   -308   -375   -366       O
ATOM   1401  OD2 ASP A 161     -43.732  12.247  17.699  1.00 53.60           O
ANISOU 1401  OD2 ASP A 161     6529   7100   6736   -418   -413   -395       O
ATOM   1402  N   HIS A 162     -40.150  13.858  19.370  1.00 38.30           N
ANISOU 1402  N   HIS A 162     4690   4953   4911   -245   -349   -391       N
ATOM   1403  CA  HIS A 162     -38.834  13.471  19.861  1.00 34.62           C
ANISOU 1403  CA  HIS A 162     4258   4418   4479   -221   -326   -434       C
ATOM   1404  C   HIS A 162     -38.087  12.511  18.937  1.00 34.84           C
ANISOU 1404  C   HIS A 162     4312   4441   4485   -265   -301   -486       C
ATOM   1405  O   HIS A 162     -36.982  12.085  19.283  1.00 37.05           O
ANISOU 1405  O   HIS A 162     4614   4666   4797   -242   -279   -520       O
ATOM   1406  CB  HIS A 162     -38.957  12.846  21.254  1.00 31.42           C
ANISOU 1406  CB  HIS A 162     3866   3970   4103   -187   -319   -444       C
ATOM   1407  CG  HIS A 162     -39.806  11.614  21.293  1.00 35.95           C
ANISOU 1407  CG  HIS A 162     4445   4547   4668   -232   -306   -451       C
ATOM   1408  ND1 HIS A 162     -40.821  11.441  22.208  1.00 40.22           N
ANISOU 1408  ND1 HIS A 162     4968   5098   5216   -219   -305   -415       N
ATOM   1409  CD2 HIS A 162     -39.787  10.492  20.537  1.00 36.34           C
ANISOU 1409  CD2 HIS A 162     4511   4584   4711   -293   -289   -494       C
ATOM   1410  CE1 HIS A 162     -41.393  10.267  22.012  1.00 40.97           C
ANISOU 1410  CE1 HIS A 162     5065   5182   5321   -277   -286   -427       C
ATOM   1411  NE2 HIS A 162     -40.784   9.671  21.003  1.00 38.97           N
ANISOU 1411  NE2 HIS A 162     4835   4910   5063   -324   -279   -482       N
ATOM   1412  N   HIS A 163     -38.652  12.155  17.783  1.00 29.59           N
ANISOU 1412  N   HIS A 163     3641   3838   3763   -321   -306   -500       N
ATOM   1413  CA  HIS A 163     -37.989  11.187  16.912  1.00 30.75           C
ANISOU 1413  CA  HIS A 163     3817   3984   3885   -360   -278   -569       C
ATOM   1414  C   HIS A 163     -36.692  11.744  16.330  1.00 35.46           C
ANISOU 1414  C   HIS A 163     4417   4579   4476   -335   -251   -568       C
ATOM   1415  O   HIS A 163     -35.684  11.024  16.232  1.00 44.45           O
ANISOU 1415  O   HIS A 163     5580   5674   5633   -329   -215   -622       O
ATOM   1416  CB  HIS A 163     -38.946  10.759  15.805  1.00 28.08           C
ANISOU 1416  CB  HIS A 163     3465   3732   3473   -427   -297   -598       C
ATOM   1417  CG  HIS A 163     -40.256  10.263  16.321  1.00 42.78           C
ANISOU 1417  CG  HIS A 163     5305   5598   5351   -461   -323   -596       C
ATOM   1418  ND1 HIS A 163     -40.369   9.112  17.070  1.00 45.56           N
ANISOU 1418  ND1 HIS A 163     5677   5867   5766   -480   -300   -636       N
ATOM   1419  CD2 HIS A 163     -41.506  10.773  16.222  1.00 48.20           C
ANISOU 1419  CD2 HIS A 163     5943   6360   6010   -477   -364   -549       C
ATOM   1420  CE1 HIS A 163     -41.634   8.925  17.398  1.00 46.64           C
ANISOU 1420  CE1 HIS A 163     5778   6029   5914   -514   -322   -615       C
ATOM   1421  NE2 HIS A 163     -42.345   9.918  16.895  1.00 47.90           N
ANISOU 1421  NE2 HIS A 163     5893   6288   6017   -512   -363   -566       N
ATOM   1422  N   ILE A 164     -36.697  13.022  15.935  1.00 27.94           N
ANISOU 1422  N   ILE A 164     3437   3670   3508   -317   -262   -499       N
ATOM   1423  CA  ILE A 164     -35.482  13.628  15.404  1.00 24.89           C
ANISOU 1423  CA  ILE A 164     3045   3280   3133   -298   -229   -483       C
ATOM   1424  C   ILE A 164     -34.383  13.582  16.451  1.00 31.90           C
ANISOU 1424  C   ILE A 164     3936   4075   4108   -257   -215   -508       C
ATOM   1425  O   ILE A 164     -33.218  13.321  16.137  1.00 32.30           O
ANISOU 1425  O   ILE A 164     3989   4108   4176   -250   -177   -537       O
ATOM   1426  CB  ILE A 164     -35.749  15.067  14.913  1.00 27.36           C
ANISOU 1426  CB  ILE A 164     3323   3636   3438   -283   -238   -386       C
ATOM   1427  CG1 ILE A 164     -34.472  15.663  14.313  1.00 30.29           C
ANISOU 1427  CG1 ILE A 164     3680   3997   3830   -272   -192   -359       C
ATOM   1428  CG2 ILE A 164     -36.264  15.975  16.035  1.00 20.61           C
ANISOU 1428  CG2 ILE A 164     2448   2726   2657   -245   -269   -343       C
ATOM   1429  CD1 ILE A 164     -33.845  14.788  13.261  1.00 21.90           C
ANISOU 1429  CD1 ILE A 164     2637   2991   2693   -297   -149   -410       C
ATOM   1430  N   TRP A 165     -34.746  13.781  17.716  1.00 31.20           N
ANISOU 1430  N   TRP A 165     3844   3939   4070   -226   -244   -500       N
ATOM   1431  CA  TRP A 165     -33.755  13.767  18.779  1.00 30.69           C
ANISOU 1431  CA  TRP A 165     3777   3809   4075   -182   -244   -526       C
ATOM   1432  C   TRP A 165     -33.329  12.351  19.126  1.00 34.78           C
ANISOU 1432  C   TRP A 165     4325   4295   4597   -176   -224   -579       C
ATOM   1433  O   TRP A 165     -32.177  12.139  19.517  1.00 41.65           O
ANISOU 1433  O   TRP A 165     5187   5129   5510   -142   -210   -603       O
ATOM   1434  CB  TRP A 165     -34.302  14.511  19.994  1.00 32.70           C
ANISOU 1434  CB  TRP A 165     4019   4043   4364   -144   -282   -505       C
ATOM   1435  CG  TRP A 165     -34.641  15.922  19.637  1.00 39.99           C
ANISOU 1435  CG  TRP A 165     4912   4975   5306   -143   -293   -454       C
ATOM   1436  CD1 TRP A 165     -35.886  16.474  19.542  1.00 39.13           C
ANISOU 1436  CD1 TRP A 165     4794   4898   5175   -144   -312   -407       C
ATOM   1437  CD2 TRP A 165     -33.717  16.954  19.280  1.00 41.78           C
ANISOU 1437  CD2 TRP A 165     5109   5173   5592   -140   -280   -436       C
ATOM   1438  NE1 TRP A 165     -35.791  17.792  19.167  1.00 37.53           N
ANISOU 1438  NE1 TRP A 165     4562   4681   5016   -135   -310   -357       N
ATOM   1439  CE2 TRP A 165     -34.470  18.111  18.999  1.00 40.70           C
ANISOU 1439  CE2 TRP A 165     4952   5041   5472   -137   -288   -374       C
ATOM   1440  CE3 TRP A 165     -32.324  17.014  19.178  1.00 38.11           C
ANISOU 1440  CE3 TRP A 165     4625   4677   5178   -140   -258   -463       C
ATOM   1441  CZ2 TRP A 165     -33.876  19.312  18.625  1.00 46.32           C
ANISOU 1441  CZ2 TRP A 165     5631   5711   6258   -136   -270   -333       C
ATOM   1442  CZ3 TRP A 165     -31.737  18.205  18.808  1.00 37.97           C
ANISOU 1442  CZ3 TRP A 165     4569   4628   5232   -146   -242   -427       C
ATOM   1443  CH2 TRP A 165     -32.510  19.340  18.537  1.00 43.93           C
ANISOU 1443  CH2 TRP A 165     5309   5372   6009   -146   -247   -361       C
ATOM   1444  N   GLU A 166     -34.223  11.376  18.958  1.00 33.75           N
ANISOU 1444  N   GLU A 166     4221   4173   4432   -207   -219   -595       N
ATOM   1445  CA  GLU A 166     -33.809   9.980  18.991  1.00 33.45           C
ANISOU 1445  CA  GLU A 166     4213   4088   4410   -210   -186   -646       C
ATOM   1446  C   GLU A 166     -32.650   9.752  18.034  1.00 36.21           C
ANISOU 1446  C   GLU A 166     4562   4439   4756   -213   -145   -688       C
ATOM   1447  O   GLU A 166     -31.579   9.276  18.428  1.00 39.70           O
ANISOU 1447  O   GLU A 166     5004   4833   5246   -171   -121   -709       O
ATOM   1448  CB  GLU A 166     -34.975   9.072  18.614  1.00 30.40           C
ANISOU 1448  CB  GLU A 166     3847   3709   3996   -266   -183   -669       C
ATOM   1449  CG  GLU A 166     -35.797   8.553  19.757  1.00 40.04           C
ANISOU 1449  CG  GLU A 166     5073   4892   5248   -255   -193   -640       C
ATOM   1450  CD  GLU A 166     -36.972   7.745  19.255  1.00 45.10           C
ANISOU 1450  CD  GLU A 166     5719   5541   5876   -327   -190   -666       C
ATOM   1451  OE1 GLU A 166     -36.777   6.564  18.897  1.00 45.42           O
ANISOU 1451  OE1 GLU A 166     5786   5527   5946   -357   -155   -724       O
ATOM   1452  OE2 GLU A 166     -38.085   8.305  19.185  1.00 48.25           O
ANISOU 1452  OE2 GLU A 166     6090   5999   6243   -355   -223   -633       O
ATOM   1453  N   ALA A 167     -32.857  10.099  16.759  1.00 32.60           N
ANISOU 1453  N   ALA A 167     4101   4047   4236   -255   -135   -694       N
ATOM   1454  CA  ALA A 167     -31.819   9.868  15.756  1.00 35.78           C
ANISOU 1454  CA  ALA A 167     4504   4470   4621   -257    -84   -734       C
ATOM   1455  C   ALA A 167     -30.556  10.663  16.079  1.00 38.72           C
ANISOU 1455  C   ALA A 167     4838   4823   5049   -212    -71   -701       C
ATOM   1456  O   ALA A 167     -29.436  10.127  16.040  1.00 39.89           O
ANISOU 1456  O   ALA A 167     4981   4941   5235   -184    -30   -737       O
ATOM   1457  CB  ALA A 167     -32.352  10.229  14.369  1.00 29.02           C
ANISOU 1457  CB  ALA A 167     3647   3714   3666   -304    -79   -732       C
ATOM   1458  N   PHE A 168     -30.731  11.945  16.420  1.00 31.48           N
ANISOU 1458  N   PHE A 168     3891   3919   4153   -206   -104   -637       N
ATOM   1459  CA  PHE A 168     -29.606  12.834  16.690  1.00 36.16           C
ANISOU 1459  CA  PHE A 168     4436   4489   4813   -179    -96   -611       C
ATOM   1460  C   PHE A 168     -28.740  12.294  17.817  1.00 37.70           C
ANISOU 1460  C   PHE A 168     4619   4626   5078   -131   -106   -648       C
ATOM   1461  O   PHE A 168     -27.517  12.182  17.679  1.00 42.90           O
ANISOU 1461  O   PHE A 168     5245   5274   5780   -110    -74   -666       O
ATOM   1462  CB  PHE A 168     -30.129  14.232  17.034  1.00 34.20           C
ANISOU 1462  CB  PHE A 168     4162   4241   4593   -182   -134   -549       C
ATOM   1463  CG  PHE A 168     -29.052  15.275  17.174  1.00 31.08           C
ANISOU 1463  CG  PHE A 168     3711   3815   4283   -171   -124   -527       C
ATOM   1464  CD1 PHE A 168     -28.379  15.442  18.375  1.00 25.72           C
ANISOU 1464  CD1 PHE A 168     3003   3085   3684   -138   -157   -562       C
ATOM   1465  CD2 PHE A 168     -28.735  16.108  16.114  1.00 35.53           C
ANISOU 1465  CD2 PHE A 168     4246   4406   4849   -196    -83   -468       C
ATOM   1466  CE1 PHE A 168     -27.394  16.404  18.509  1.00 30.82           C
ANISOU 1466  CE1 PHE A 168     3588   3700   4422   -139   -154   -555       C
ATOM   1467  CE2 PHE A 168     -27.757  17.073  16.242  1.00 35.73           C
ANISOU 1467  CE2 PHE A 168     4212   4389   4975   -197    -67   -444       C
ATOM   1468  CZ  PHE A 168     -27.083  17.221  17.440  1.00 33.57           C
ANISOU 1468  CZ  PHE A 168     3906   4057   4793   -173   -105   -496       C
ATOM   1469  N   TRP A 169     -29.360  11.935  18.940  1.00 34.08           N
ANISOU 1469  N   TRP A 169     4182   4140   4628   -107   -147   -652       N
ATOM   1470  CA  TRP A 169     -28.582  11.511  20.090  1.00 36.65           C
ANISOU 1470  CA  TRP A 169     4492   4429   5006    -49   -165   -671       C
ATOM   1471  C   TRP A 169     -28.071  10.082  19.954  1.00 36.90           C
ANISOU 1471  C   TRP A 169     4547   4431   5044    -26   -122   -704       C
ATOM   1472  O   TRP A 169     -27.021   9.766  20.516  1.00 36.15           O
ANISOU 1472  O   TRP A 169     4422   4317   4997     27   -120   -715       O
ATOM   1473  CB  TRP A 169     -29.406  11.676  21.365  1.00 39.18           C
ANISOU 1473  CB  TRP A 169     4824   4744   5318    -22   -218   -654       C
ATOM   1474  CG  TRP A 169     -29.600  13.113  21.741  1.00 44.79           C
ANISOU 1474  CG  TRP A 169     5502   5468   6049    -24   -259   -639       C
ATOM   1475  CD1 TRP A 169     -30.787  13.761  21.919  1.00 44.59           C
ANISOU 1475  CD1 TRP A 169     5490   5456   5998    -38   -283   -613       C
ATOM   1476  CD2 TRP A 169     -28.572  14.088  21.973  1.00 45.07           C
ANISOU 1476  CD2 TRP A 169     5481   5495   6149    -13   -277   -656       C
ATOM   1477  NE1 TRP A 169     -30.563  15.076  22.254  1.00 42.76           N
ANISOU 1477  NE1 TRP A 169     5220   5215   5813    -31   -312   -615       N
ATOM   1478  CE2 TRP A 169     -29.213  15.302  22.293  1.00 42.96           C
ANISOU 1478  CE2 TRP A 169     5201   5223   5897    -22   -310   -645       C
ATOM   1479  CE3 TRP A 169     -27.174  14.050  21.947  1.00 40.68           C
ANISOU 1479  CE3 TRP A 169     4875   4931   5648      2   -267   -683       C
ATOM   1480  CZ2 TRP A 169     -28.505  16.467  22.582  1.00 41.42           C
ANISOU 1480  CZ2 TRP A 169     4953   5005   5781    -23   -333   -667       C
ATOM   1481  CZ3 TRP A 169     -26.473  15.208  22.234  1.00 42.72           C
ANISOU 1481  CZ3 TRP A 169     5072   5178   5980     -3   -294   -701       C
ATOM   1482  CH2 TRP A 169     -27.138  16.399  22.547  1.00 43.09           C
ANISOU 1482  CH2 TRP A 169     5113   5209   6050    -19   -327   -697       C
ATOM   1483  N   GLN A 170     -28.749   9.214  19.194  1.00 32.70           N
ANISOU 1483  N   GLN A 170     4061   3891   4471    -62    -88   -727       N
ATOM   1484  CA  GLN A 170     -28.191   7.882  18.977  1.00 39.75           C
ANISOU 1484  CA  GLN A 170     4976   4737   5390    -39    -37   -770       C
ATOM   1485  C   GLN A 170     -26.918   7.956  18.142  1.00 38.20           C
ANISOU 1485  C   GLN A 170     4746   4557   5210    -26     12   -799       C
ATOM   1486  O   GLN A 170     -25.891   7.349  18.491  1.00 35.49           O
ANISOU 1486  O   GLN A 170     4381   4178   4923     32     37   -813       O
ATOM   1487  CB  GLN A 170     -29.213   6.967  18.305  1.00 34.18           C
ANISOU 1487  CB  GLN A 170     4324   4014   4647    -91    -12   -808       C
ATOM   1488  CG  GLN A 170     -28.700   5.543  18.161  1.00 39.94           C
ANISOU 1488  CG  GLN A 170     5081   4669   5425    -66     45   -861       C
ATOM   1489  CD  GLN A 170     -29.359   4.783  17.031  1.00 43.40           C
ANISOU 1489  CD  GLN A 170     5562   5103   5827   -131     81   -940       C
ATOM   1490  OE1 GLN A 170     -29.207   5.128  15.859  1.00 47.93           O
ANISOU 1490  OE1 GLN A 170     6131   5744   6336   -165    101   -983       O
ATOM   1491  NE2 GLN A 170     -30.092   3.734  17.378  1.00 41.49           N
ANISOU 1491  NE2 GLN A 170     5356   4784   5625   -149     91   -960       N
ATOM   1492  N   VAL A 171     -26.967   8.696  17.029  1.00 35.62           N
ANISOU 1492  N   VAL A 171     4409   4292   4835    -72     31   -800       N
ATOM   1493  CA  VAL A 171     -25.770   8.852  16.211  1.00 41.49           C
ANISOU 1493  CA  VAL A 171     5113   5063   5590    -61     89   -815       C
ATOM   1494  C   VAL A 171     -24.691   9.597  16.987  1.00 38.07           C
ANISOU 1494  C   VAL A 171     4608   4621   5237    -21     67   -782       C
ATOM   1495  O   VAL A 171     -23.501   9.282  16.877  1.00 38.05           O
ANISOU 1495  O   VAL A 171     4561   4613   5283     18    108   -800       O
ATOM   1496  CB  VAL A 171     -26.113   9.553  14.884  1.00 49.25           C
ANISOU 1496  CB  VAL A 171     6096   6125   6491   -115    116   -801       C
ATOM   1497  CG1 VAL A 171     -24.842   9.895  14.107  1.00 40.86           C
ANISOU 1497  CG1 VAL A 171     4981   5100   5442   -101    183   -796       C
ATOM   1498  CG2 VAL A 171     -27.031   8.669  14.056  1.00 23.14           C
ANISOU 1498  CG2 VAL A 171     2851   2842   3098   -153    134   -861       C
ATOM   1499  N   SER A 172     -25.088  10.572  17.812  1.00 36.49           N
ANISOU 1499  N   SER A 172     4387   4421   5056    -27      1   -741       N
ATOM   1500  CA  SER A 172     -24.111  11.273  18.636  1.00 41.27           C
ANISOU 1500  CA  SER A 172     4920   5019   5741      4    -32   -730       C
ATOM   1501  C   SER A 172     -23.437  10.326  19.615  1.00 42.86           C
ANISOU 1501  C   SER A 172     5107   5193   5984     76    -47   -753       C
ATOM   1502  O   SER A 172     -22.216  10.376  19.794  1.00 38.48           O
ANISOU 1502  O   SER A 172     4483   4645   5492    111    -40   -763       O
ATOM   1503  CB  SER A 172     -24.784  12.423  19.386  1.00 41.11           C
ANISOU 1503  CB  SER A 172     4892   4998   5731    -14   -101   -703       C
ATOM   1504  OG  SER A 172     -25.003  13.529  18.531  1.00 39.49           O
ANISOU 1504  OG  SER A 172     4669   4810   5524    -67    -82   -666       O
ATOM   1505  N   ALA A 173     -24.219   9.462  20.266  1.00 47.13           N
ANISOU 1505  N   ALA A 173     5706   5704   6495    101    -67   -752       N
ATOM   1506  CA  ALA A 173     -23.663   8.526  21.232  1.00 45.57           C
ANISOU 1506  CA  ALA A 173     5500   5481   6333    180    -78   -750       C
ATOM   1507  C   ALA A 173     -22.666   7.593  20.566  1.00 49.11           C
ANISOU 1507  C   ALA A 173     5933   5907   6822    215     -7   -777       C
ATOM   1508  O   ALA A 173     -21.557   7.384  21.073  1.00 48.37           O
ANISOU 1508  O   ALA A 173     5777   5819   6784    280    -13   -773       O
ATOM   1509  CB  ALA A 173     -24.786   7.731  21.896  1.00 35.97           C
ANISOU 1509  CB  ALA A 173     4353   4230   5082    193    -93   -727       C
ATOM   1510  N   LEU A 174     -23.041   7.030  19.416  1.00 46.73           N
ANISOU 1510  N   LEU A 174     5680   5585   6489    176     60   -810       N
ATOM   1511  CA  LEU A 174     -22.135   6.108  18.740  1.00 45.08           C
ANISOU 1511  CA  LEU A 174     5462   5350   6316    214    138   -849       C
ATOM   1512  C   LEU A 174     -20.871   6.816  18.270  1.00 45.67           C
ANISOU 1512  C   LEU A 174     5448   5477   6426    223    164   -851       C
ATOM   1513  O   LEU A 174     -19.757   6.297  18.445  1.00 47.73           O
ANISOU 1513  O   LEU A 174     5655   5728   6751    292    194   -859       O
ATOM   1514  CB  LEU A 174     -22.852   5.438  17.575  1.00 43.04           C
ANISOU 1514  CB  LEU A 174     5276   5073   6005    164    199   -906       C
ATOM   1515  CG  LEU A 174     -24.029   4.596  18.058  1.00 41.33           C
ANISOU 1515  CG  LEU A 174     5133   4790   5780    151    181   -908       C
ATOM   1516  CD1 LEU A 174     -24.884   4.192  16.881  1.00 45.63           C
ANISOU 1516  CD1 LEU A 174     5738   5337   6264     78    220   -976       C
ATOM   1517  CD2 LEU A 174     -23.542   3.373  18.839  1.00 38.94           C
ANISOU 1517  CD2 LEU A 174     4837   4398   5561    235    206   -898       C
ATOM   1518  N   GLY A 175     -21.020   8.011  17.693  1.00 42.17           N
ANISOU 1518  N   GLY A 175     4982   5089   5952    158    157   -836       N
ATOM   1519  CA  GLY A 175     -19.858   8.747  17.229  1.00 40.80           C
ANISOU 1519  CA  GLY A 175     4718   4960   5826    155    190   -826       C
ATOM   1520  C   GLY A 175     -18.916   9.124  18.354  1.00 36.68           C
ANISOU 1520  C   GLY A 175     4104   4441   5391    202    131   -809       C
ATOM   1521  O   GLY A 175     -17.701   8.974  18.230  1.00 37.43           O
ANISOU 1521  O   GLY A 175     4118   4554   5551    241    168   -817       O
ATOM   1522  N   THR A 176     -19.464   9.606  19.473  1.00 34.58           N
ANISOU 1522  N   THR A 176     3844   4169   5124    201     39   -793       N
ATOM   1523  CA  THR A 176     -18.621   9.994  20.597  1.00 36.14           C
ANISOU 1523  CA  THR A 176     3953   4388   5389    244    -31   -793       C
ATOM   1524  C   THR A 176     -17.986   8.783  21.265  1.00 39.43           C
ANISOU 1524  C   THR A 176     4354   4797   5831    344    -32   -793       C
ATOM   1525  O   THR A 176     -16.838   8.861  21.717  1.00 44.02           O
ANISOU 1525  O   THR A 176     4835   5413   6479    391    -55   -797       O
ATOM   1526  CB  THR A 176     -19.423  10.805  21.618  1.00 36.74           C
ANISOU 1526  CB  THR A 176     4047   4470   5442    224   -126   -788       C
ATOM   1527  OG1 THR A 176     -20.603  10.085  22.001  1.00 39.90           O
ANISOU 1527  OG1 THR A 176     4547   4844   5769    241   -138   -773       O
ATOM   1528  CG2 THR A 176     -19.812  12.137  21.031  1.00 30.93           C
ANISOU 1528  CG2 THR A 176     3302   3734   4715    138   -125   -781       C
ATOM   1529  N   PHE A 177     -18.695   7.654  21.320  1.00 32.72           N
ANISOU 1529  N   PHE A 177     3594   3898   4939    377     -6   -785       N
ATOM   1530  CA  PHE A 177     -18.094   6.448  21.876  1.00 36.47           C
ANISOU 1530  CA  PHE A 177     4057   4348   5452    479      8   -770       C
ATOM   1531  C   PHE A 177     -16.906   5.999  21.037  1.00 37.01           C
ANISOU 1531  C   PHE A 177     4063   4415   5582    514     91   -793       C
ATOM   1532  O   PHE A 177     -15.838   5.676  21.570  1.00 43.14           O
ANISOU 1532  O   PHE A 177     4755   5214   6421    596     79   -779       O
ATOM   1533  CB  PHE A 177     -19.136   5.335  21.973  1.00 26.23           C
ANISOU 1533  CB  PHE A 177     2871   2976   4120    495     37   -755       C
ATOM   1534  CG  PHE A 177     -18.610   4.079  22.590  1.00 32.63           C
ANISOU 1534  CG  PHE A 177     3676   3742   4981    605     58   -722       C
ATOM   1535  CD1 PHE A 177     -18.546   3.946  23.967  1.00 34.28           C
ANISOU 1535  CD1 PHE A 177     3860   3979   5185    680    -16   -660       C
ATOM   1536  CD2 PHE A 177     -18.158   3.037  21.796  1.00 36.75           C
ANISOU 1536  CD2 PHE A 177     4213   4195   5554    641    154   -749       C
ATOM   1537  CE1 PHE A 177     -18.046   2.790  24.544  1.00 36.66           C
ANISOU 1537  CE1 PHE A 177     4153   4241   5535    793      6   -607       C
ATOM   1538  CE2 PHE A 177     -17.658   1.879  22.365  1.00 37.28           C
ANISOU 1538  CE2 PHE A 177     4273   4206   5685    752    180   -708       C
ATOM   1539  CZ  PHE A 177     -17.604   1.755  23.741  1.00 37.45           C
ANISOU 1539  CZ  PHE A 177     4269   4255   5705    829    106   -627       C
ATOM   1540  N   LEU A 178     -17.073   5.973  19.713  1.00 36.95           N
ANISOU 1540  N   LEU A 178     4093   4394   5553    458    176   -829       N
ATOM   1541  CA  LEU A 178     -15.968   5.549  18.862  1.00 36.81           C
ANISOU 1541  CA  LEU A 178     4017   4384   5584    495    268   -856       C
ATOM   1542  C   LEU A 178     -14.844   6.575  18.848  1.00 39.52           C
ANISOU 1542  C   LEU A 178     4228   4801   5986    483    253   -844       C
ATOM   1543  O   LEU A 178     -13.671   6.205  18.735  1.00 45.48           O
ANISOU 1543  O   LEU A 178     4894   5576   6812    547    297   -847       O
ATOM   1544  CB  LEU A 178     -16.468   5.275  17.449  1.00 39.38           C
ANISOU 1544  CB  LEU A 178     4417   4696   5850    441    362   -905       C
ATOM   1545  CG  LEU A 178     -17.371   4.047  17.349  1.00 40.09           C
ANISOU 1545  CG  LEU A 178     4621   4702   5911    456    392   -940       C
ATOM   1546  CD1 LEU A 178     -17.544   3.630  15.897  1.00 43.74           C
ANISOU 1546  CD1 LEU A 178     5135   5165   6320    420    492  -1016       C
ATOM   1547  CD2 LEU A 178     -16.809   2.903  18.191  1.00 38.64           C
ANISOU 1547  CD2 LEU A 178     4422   4448   5811    568    398   -923       C
ATOM   1548  N   LEU A 179     -15.167   7.859  18.988  1.00 37.96           N
ANISOU 1548  N   LEU A 179     4008   4640   5775    403    195   -829       N
ATOM   1549  CA  LEU A 179     -14.116   8.859  19.130  1.00 42.63           C
ANISOU 1549  CA  LEU A 179     4465   5287   6447    383    172   -820       C
ATOM   1550  C   LEU A 179     -13.325   8.636  20.411  1.00 41.18           C
ANISOU 1550  C   LEU A 179     4192   5130   6326    463     88   -817       C
ATOM   1551  O   LEU A 179     -12.097   8.762  20.421  1.00 46.74           O
ANISOU 1551  O   LEU A 179     4768   5877   7114    492     99   -820       O
ATOM   1552  CB  LEU A 179     -14.721  10.264  19.102  1.00 38.69           C
ANISOU 1552  CB  LEU A 179     3968   4796   5936    283    125   -808       C
ATOM   1553  CG  LEU A 179     -13.821  11.424  19.533  1.00 42.80           C
ANISOU 1553  CG  LEU A 179     4353   5351   6558    247     75   -808       C
ATOM   1554  CD1 LEU A 179     -12.596  11.545  18.632  1.00 42.87           C
ANISOU 1554  CD1 LEU A 179     4252   5392   6644    240    168   -798       C
ATOM   1555  CD2 LEU A 179     -14.606  12.723  19.546  1.00 39.79           C
ANISOU 1555  CD2 LEU A 179     3997   4949   6172    154     33   -798       C
ATOM   1556  N   ALA A 180     -14.014   8.298  21.505  1.00 36.85           N
ANISOU 1556  N   ALA A 180     3701   4567   5732    502      4   -807       N
ATOM   1557  CA  ALA A 180     -13.319   8.017  22.755  1.00 38.79           C
ANISOU 1557  CA  ALA A 180     3867   4860   6013    591    -80   -796       C
ATOM   1558  C   ALA A 180     -12.425   6.793  22.617  1.00 44.70           C
ANISOU 1558  C   ALA A 180     4574   5599   6810    700    -18   -777       C
ATOM   1559  O   ALA A 180     -11.279   6.793  23.087  1.00 43.92           O
ANISOU 1559  O   ALA A 180     4347   5562   6779    761    -52   -772       O
ATOM   1560  CB  ALA A 180     -14.328   7.824  23.886  1.00 35.87           C
ANISOU 1560  CB  ALA A 180     3579   4484   5565    619   -165   -776       C
ATOM   1561  N   TYR A 181     -12.931   5.741  21.965  1.00 41.04           N
ANISOU 1561  N   TYR A 181     4215   5058   6320    726     73   -772       N
ATOM   1562  CA  TYR A 181     -12.105   4.563  21.724  1.00 46.38           C
ANISOU 1562  CA  TYR A 181     4860   5706   7058    832    149   -762       C
ATOM   1563  C   TYR A 181     -10.877   4.917  20.893  1.00 51.50           C
ANISOU 1563  C   TYR A 181     5386   6402   7779    827    216   -787       C
ATOM   1564  O   TYR A 181      -9.771   4.439  21.169  1.00 53.77           O
ANISOU 1564  O   TYR A 181     5567   6721   8142    924    226   -770       O
ATOM   1565  CB  TYR A 181     -12.916   3.463  21.034  1.00 41.68           C
ANISOU 1565  CB  TYR A 181     4400   5003   6432    841    243   -777       C
ATOM   1566  CG  TYR A 181     -12.042   2.339  20.531  1.00 41.40           C
ANISOU 1566  CG  TYR A 181     4334   4922   6471    940    345   -788       C
ATOM   1567  CD1 TYR A 181     -11.538   1.383  21.403  1.00 44.43           C
ANISOU 1567  CD1 TYR A 181     4686   5278   6916   1073    331   -733       C
ATOM   1568  CD2 TYR A 181     -11.694   2.250  19.190  1.00 49.01           C
ANISOU 1568  CD2 TYR A 181     5298   5879   7444    912    460   -849       C
ATOM   1569  CE1 TYR A 181     -10.718   0.362  20.951  1.00 47.57           C
ANISOU 1569  CE1 TYR A 181     5052   5626   7398   1174    430   -742       C
ATOM   1570  CE2 TYR A 181     -10.874   1.235  18.729  1.00 51.07           C
ANISOU 1570  CE2 TYR A 181     5528   6098   7777   1010    561   -870       C
ATOM   1571  CZ  TYR A 181     -10.388   0.294  19.613  1.00 49.17           C
ANISOU 1571  CZ  TYR A 181     5256   5815   7612   1142    546   -818       C
ATOM   1572  OH  TYR A 181      -9.567  -0.716  19.153  1.00 47.55           O
ANISOU 1572  OH  TYR A 181     5018   5558   7492   1249    652   -838       O
ATOM   1573  N   ASN A 182     -11.049   5.767  19.878  1.00 50.02           N
ANISOU 1573  N   ASN A 182     5205   6230   7571    721    266   -817       N
ATOM   1574  CA  ASN A 182      -9.932   6.124  19.010  1.00 45.19           C
ANISOU 1574  CA  ASN A 182     4478   5668   7025    710    347   -829       C
ATOM   1575  C   ASN A 182      -8.909   6.989  19.739  1.00 45.53           C
ANISOU 1575  C   ASN A 182     4353   5790   7155    707    265   -815       C
ATOM   1576  O   ASN A 182      -7.701   6.853  19.514  1.00 47.80           O
ANISOU 1576  O   ASN A 182     4510   6124   7529    755    311   -812       O
ATOM   1577  CB  ASN A 182     -10.455   6.832  17.762  1.00 42.32           C
ANISOU 1577  CB  ASN A 182     4169   5307   6605    600    422   -845       C
ATOM   1578  CG  ASN A 182     -11.135   5.878  16.800  1.00 37.43           C
ANISOU 1578  CG  ASN A 182     3680   4633   5909    612    522   -881       C
ATOM   1579  OD1 ASN A 182     -10.768   4.708  16.719  1.00 41.80           O
ANISOU 1579  OD1 ASN A 182     4246   5146   6489    706    581   -904       O
ATOM   1580  ND2 ASN A 182     -12.124   6.372  16.062  1.00 32.10           N
ANISOU 1580  ND2 ASN A 182     3098   3957   5142    520    541   -891       N
ATOM   1581  N   ARG A 183      -9.371   7.884  20.615  1.00 47.09           N
ANISOU 1581  N   ARG A 183     4547   6009   7336    650    145   -814       N
ATOM   1582  CA  ARG A 183      -8.452   8.716  21.384  1.00 46.54           C
ANISOU 1582  CA  ARG A 183     4318   6015   7350    639     52   -823       C
ATOM   1583  C   ARG A 183      -7.774   7.939  22.505  1.00 47.01           C
ANISOU 1583  C   ARG A 183     4301   6125   7435    767    -25   -809       C
ATOM   1584  O   ARG A 183      -6.710   8.353  22.976  1.00 44.04           O
ANISOU 1584  O   ARG A 183     3762   5830   7142    782    -82   -820       O
ATOM   1585  CB  ARG A 183      -9.189   9.929  21.965  1.00 41.99           C
ANISOU 1585  CB  ARG A 183     3767   5441   6748    540    -51   -846       C
ATOM   1586  CG  ARG A 183      -9.672  10.929  20.926  1.00 40.61           C
ANISOU 1586  CG  ARG A 183     3629   5226   6574    414     15   -845       C
ATOM   1587  CD  ARG A 183      -8.513  11.512  20.132  1.00 46.41           C
ANISOU 1587  CD  ARG A 183     4218   5993   7421    369     91   -838       C
ATOM   1588  NE  ARG A 183      -8.964  12.418  19.078  1.00 55.36           N
ANISOU 1588  NE  ARG A 183     5390   7093   8552    260    168   -812       N
ATOM   1589  CZ  ARG A 183      -9.305  12.029  17.852  1.00 61.62           C
ANISOU 1589  CZ  ARG A 183     6264   7871   9279    255    293   -782       C
ATOM   1590  NH1 ARG A 183      -9.250  10.745  17.519  1.00 60.71           N
ANISOU 1590  NH1 ARG A 183     6204   7756   9107    345    357   -790       N
ATOM   1591  NH2 ARG A 183      -9.708  12.925  16.959  1.00 61.88           N
ANISOU 1591  NH2 ARG A 183     6322   7888   9301    162    354   -744       N
ATOM   1592  N   TRP A 184      -8.360   6.824  22.939  1.00 45.59           N
ANISOU 1592  N   TRP A 184     4229   5903   7191    859    -26   -778       N
ATOM   1593  CA  TRP A 184      -7.813   6.054  24.047  1.00 37.83           C
ANISOU 1593  CA  TRP A 184     3184   4969   6221    993    -98   -740       C
ATOM   1594  C   TRP A 184      -6.945   4.886  23.608  1.00 43.23           C
ANISOU 1594  C   TRP A 184     3820   5632   6973   1113     -1   -708       C
ATOM   1595  O   TRP A 184      -6.038   4.495  24.351  1.00 45.25           O
ANISOU 1595  O   TRP A 184     3957   5959   7277   1222    -54   -674       O
ATOM   1596  CB  TRP A 184      -8.948   5.521  24.928  1.00 38.18           C
ANISOU 1596  CB  TRP A 184     3366   4977   6165   1034   -157   -703       C
ATOM   1597  CG  TRP A 184      -9.387   6.481  25.994  1.00 42.43           C
ANISOU 1597  CG  TRP A 184     3892   5588   6643    987   -297   -725       C
ATOM   1598  CD1 TRP A 184      -9.677   7.809  25.838  1.00 44.90           C
ANISOU 1598  CD1 TRP A 184     4191   5916   6955    858   -339   -786       C
ATOM   1599  CD2 TRP A 184      -9.583   6.187  27.381  1.00 40.82           C
ANISOU 1599  CD2 TRP A 184     3689   5450   6370   1076   -409   -687       C
ATOM   1600  NE1 TRP A 184     -10.041   8.358  27.045  1.00 43.36           N
ANISOU 1600  NE1 TRP A 184     3989   5788   6698    860   -471   -806       N
ATOM   1601  CE2 TRP A 184      -9.992   7.384  28.008  1.00 44.92           C
ANISOU 1601  CE2 TRP A 184     4196   6030   6842    993   -517   -746       C
ATOM   1602  CE3 TRP A 184      -9.455   5.029  28.155  1.00 36.32           C
ANISOU 1602  CE3 TRP A 184     3129   4896   5774   1223   -423   -603       C
ATOM   1603  CZ2 TRP A 184     -10.272   7.454  29.371  1.00 44.17           C
ANISOU 1603  CZ2 TRP A 184     4099   6026   6657   1052   -639   -736       C
ATOM   1604  CZ3 TRP A 184      -9.729   5.101  29.508  1.00 36.17           C
ANISOU 1604  CZ3 TRP A 184     3106   4971   5664   1283   -544   -573       C
ATOM   1605  CH2 TRP A 184     -10.131   6.304  30.103  1.00 40.31           C
ANISOU 1605  CH2 TRP A 184     3619   5571   6126   1198   -651   -645       C
ATOM   1606  N   LYS A 185      -7.195   4.319  22.428  1.00 42.25           N
ANISOU 1606  N   LYS A 185     3782   5421   6852   1101    139   -722       N
ATOM   1607  CA  LYS A 185      -6.523   3.086  22.039  1.00 43.54           C
ANISOU 1607  CA  LYS A 185     3924   5542   7078   1227    241   -702       C
ATOM   1608  C   LYS A 185      -5.018   3.298  21.926  1.00 46.06           C
ANISOU 1608  C   LYS A 185     4044   5953   7503   1276    256   -700       C
ATOM   1609  O   LYS A 185      -4.551   4.368  21.533  1.00 51.92           O
ANISOU 1609  O   LYS A 185     4687   6762   8278   1180    251   -731       O
ATOM   1610  CB  LYS A 185      -7.084   2.567  20.713  1.00 42.25           C
ANISOU 1610  CB  LYS A 185     3886   5277   6888   1189    388   -746       C
ATOM   1611  CG  LYS A 185      -6.828   3.477  19.515  1.00 50.39           C
ANISOU 1611  CG  LYS A 185     4878   6349   7919   1078    464   -794       C
ATOM   1612  CD  LYS A 185      -7.483   2.919  18.257  1.00 54.77           C
ANISOU 1612  CD  LYS A 185     5568   6825   8417   1048    596   -845       C
ATOM   1613  CE  LYS A 185      -7.551   3.946  17.135  1.00 52.40           C
ANISOU 1613  CE  LYS A 185     5258   6576   8075    926    656   -874       C
ATOM   1614  NZ  LYS A 185      -8.555   3.549  16.100  1.00 50.11           N
ANISOU 1614  NZ  LYS A 185     5125   6228   7686    878    742   -926       N
ATOM   1615  N   GLY A 186      -4.258   2.268  22.296  1.00 45.47           N
ANISOU 1615  N   GLY A 186     3903   5880   7494   1430    276   -655       N
ATOM   1616  CA  GLY A 186      -2.817   2.286  22.167  1.00 45.86           C
ANISOU 1616  CA  GLY A 186     3757   6017   7652   1498    301   -647       C
ATOM   1617  C   GLY A 186      -2.071   3.001  23.269  1.00 47.40           C
ANISOU 1617  C   GLY A 186     3778   6352   7879   1509    147   -627       C
ATOM   1618  O   GLY A 186      -0.833   2.976  23.270  1.00 55.39           O
ANISOU 1618  O   GLY A 186     4607   7449   8990   1573    154   -616       O
ATOM   1619  N   HIS A 187      -2.770   3.641  24.199  1.00 40.84           N
ANISOU 1619  N   HIS A 187     2991   5557   6968   1449      8   -630       N
ATOM   1620  CA  HIS A 187      -2.152   4.341  25.312  1.00 44.48           C
ANISOU 1620  CA  HIS A 187     3297   6161   7443   1454   -153   -633       C
ATOM   1621  C   HIS A 187      -2.365   3.554  26.596  1.00 51.84           C
ANISOU 1621  C   HIS A 187     4257   7131   8308   1594   -255   -561       C
ATOM   1622  O   HIS A 187      -3.248   2.698  26.686  1.00 57.40           O
ANISOU 1622  O   HIS A 187     5125   7735   8950   1649   -211   -510       O
ATOM   1623  CB  HIS A 187      -2.721   5.756  25.460  1.00 47.92           C
ANISOU 1623  CB  HIS A 187     3749   6621   7836   1284   -239   -704       C
ATOM   1624  CG  HIS A 187      -2.538   6.612  24.245  1.00 47.38           C
ANISOU 1624  CG  HIS A 187     3651   6518   7834   1146   -140   -754       C
ATOM   1625  ND1 HIS A 187      -1.367   7.289  23.982  1.00 45.89           N
ANISOU 1625  ND1 HIS A 187     3263   6409   7766   1103   -138   -780       N
ATOM   1626  CD2 HIS A 187      -3.381   6.909  23.228  1.00 44.54           C
ANISOU 1626  CD2 HIS A 187     3429   6059   7435   1042    -39   -772       C
ATOM   1627  CE1 HIS A 187      -1.493   7.960  22.851  1.00 44.89           C
ANISOU 1627  CE1 HIS A 187     3157   6228   7673    981    -30   -802       C
ATOM   1628  NE2 HIS A 187      -2.705   7.745  22.373  1.00 45.56           N
ANISOU 1628  NE2 HIS A 187     3446   6211   7654    947     28   -797       N
ATOM   1629  N   ASP A 188      -1.538   3.854  27.593  1.00 58.86           N
ANISOU 1629  N   ASP A 188     4978   8174   9213   1651   -392   -552       N
ATOM   1630  CA  ASP A 188      -1.608   3.153  28.863  1.00 65.27           C
ANISOU 1630  CA  ASP A 188     5791   9057   9950   1799   -496   -469       C
ATOM   1631  C   ASP A 188      -2.614   3.836  29.786  1.00 64.50           C
ANISOU 1631  C   ASP A 188     5786   9002   9716   1728   -624   -498       C
ATOM   1632  O   ASP A 188      -3.229   4.850  29.446  1.00 62.34           O
ANISOU 1632  O   ASP A 188     5571   8695   9420   1569   -633   -586       O
ATOM   1633  CB  ASP A 188      -0.224   3.059  29.510  1.00 74.14           C
ANISOU 1633  CB  ASP A 188     6682  10349  11140   1913   -587   -442       C
ATOM   1634  CG  ASP A 188       0.436   4.416  29.711  1.00 81.47           C
ANISOU 1634  CG  ASP A 188     7435  11412  12108   1789   -702   -550       C
ATOM   1635  OD1 ASP A 188      -0.206   5.326  30.279  1.00 83.01           O
ANISOU 1635  OD1 ASP A 188     7676  11646  12219   1684   -811   -620       O
ATOM   1636  OD2 ASP A 188       1.613   4.566  29.316  1.00 84.53           O
ANISOU 1636  OD2 ASP A 188     7633  11864  12620   1797   -681   -568       O
ATOM   1637  N   LEU A 189      -2.770   3.268  30.982  1.00 66.07           N
ANISOU 1637  N   LEU A 189     5995   9283   9824   1859   -720   -417       N
ATOM   1638  CA  LEU A 189      -3.761   3.764  31.930  1.00 63.36           C
ANISOU 1638  CA  LEU A 189     5749   8989   9334   1818   -831   -433       C
ATOM   1639  C   LEU A 189      -3.467   5.203  32.339  1.00 63.54           C
ANISOU 1639  C   LEU A 189     5657   9142   9344   1696   -967   -566       C
ATOM   1640  O   LEU A 189      -4.354   6.063  32.307  1.00 64.96           O
ANISOU 1640  O   LEU A 189     5933   9280   9468   1565   -989   -644       O
ATOM   1641  CB  LEU A 189      -3.799   2.846  33.151  1.00 67.09           C
ANISOU 1641  CB  LEU A 189     6227   9553   9711   2001   -903   -305       C
ATOM   1642  CG  LEU A 189      -5.058   2.825  34.015  1.00 72.55           C
ANISOU 1642  CG  LEU A 189     7073  10250  10243   2005   -954   -266       C
ATOM   1643  CD1 LEU A 189      -6.303   3.051  33.172  1.00 74.03           C
ANISOU 1643  CD1 LEU A 189     7448  10255  10424   1863   -847   -311       C
ATOM   1644  CD2 LEU A 189      -5.140   1.505  34.772  1.00 75.82           C
ANISOU 1644  CD2 LEU A 189     7527  10676  10607   2201   -940    -89       C
ATOM   1645  N   SER A 190      -2.216   5.487  32.712  1.00 64.46           N
ANISOU 1645  N   SER A 190     5560   9410   9522   1735  -1060   -597       N
ATOM   1646  CA  SER A 190      -1.859   6.801  33.236  1.00 61.19           C
ANISOU 1646  CA  SER A 190     5018   9125   9106   1626  -1205   -733       C
ATOM   1647  C   SER A 190      -2.005   7.915  32.205  1.00 60.01           C
ANISOU 1647  C   SER A 190     4876   8865   9059   1425  -1139   -845       C
ATOM   1648  O   SER A 190      -2.117   9.085  32.589  1.00 57.76           O
ANISOU 1648  O   SER A 190     4547   8630   8768   1307  -1240   -965       O
ATOM   1649  CB  SER A 190      -0.428   6.774  33.767  1.00 58.49           C
ANISOU 1649  CB  SER A 190     4478   8941   8805   1680  -1287   -717       C
ATOM   1650  OG  SER A 190       0.409   6.036  32.898  1.00 62.70           O
ANISOU 1650  OG  SER A 190     4928   9421   9473   1748  -1166   -646       O
ATOM   1651  N   HIS A 191      -1.999   7.586  30.913  1.00 60.82           N
ANISOU 1651  N   HIS A 191     5031   8821   9257   1388   -969   -810       N
ATOM   1652  CA  HIS A 191      -2.241   8.601  29.894  1.00 60.83           C
ANISOU 1652  CA  HIS A 191     5056   8716   9339   1207   -893   -890       C
ATOM   1653  C   HIS A 191      -3.736   8.809  29.658  1.00 54.72           C
ANISOU 1653  C   HIS A 191     4508   7817   8468   1130   -847   -894       C
ATOM   1654  O   HIS A 191      -4.179   9.933  29.395  1.00 48.96           O
ANISOU 1654  O   HIS A 191     3802   7042   7757    984   -859   -974       O
ATOM   1655  CB  HIS A 191      -1.538   8.212  28.593  1.00 61.34           C
ANISOU 1655  CB  HIS A 191     5067   8706   9533   1204   -732   -852       C
ATOM   1656  CG  HIS A 191      -1.639   9.247  27.515  1.00 62.84           C
ANISOU 1656  CG  HIS A 191     5259   8810   9810   1030   -646   -913       C
ATOM   1657  ND1 HIS A 191      -2.393   9.063  26.376  1.00 63.11           N
ANISOU 1657  ND1 HIS A 191     5449   8703   9826    978   -495   -884       N
ATOM   1658  CD2 HIS A 191      -1.074  10.471  27.398  1.00 63.84           C
ANISOU 1658  CD2 HIS A 191     5243   8970  10042    899   -689   -995       C
ATOM   1659  CE1 HIS A 191      -2.291  10.131  25.606  1.00 62.49           C
ANISOU 1659  CE1 HIS A 191     5329   8584   9829    831   -446   -930       C
ATOM   1660  NE2 HIS A 191      -1.495  11.000  26.203  1.00 64.60           N
ANISOU 1660  NE2 HIS A 191     5417   8945  10184    778   -557   -995       N
ATOM   1661  N   ASN A 192      -4.532   7.750  29.754  1.00 47.31           N
ANISOU 1661  N   ASN A 192     3727   6815   7434   1226   -794   -805       N
ATOM   1662  CA  ASN A 192      -5.964   7.915  29.560  1.00 53.39           C
ANISOU 1662  CA  ASN A 192     4696   7476   8113   1154   -755   -807       C
ATOM   1663  C   ASN A 192      -6.666   8.483  30.788  1.00 55.30           C
ANISOU 1663  C   ASN A 192     4979   7797   8235   1146   -895   -847       C
ATOM   1664  O   ASN A 192      -7.836   8.866  30.689  1.00 50.21           O
ANISOU 1664  O   ASN A 192     4477   7076   7524   1070   -877   -866       O
ATOM   1665  CB  ASN A 192      -6.593   6.580  29.160  1.00 46.82           C
ANISOU 1665  CB  ASN A 192     4014   6535   7241   1244   -638   -706       C
ATOM   1666  CG  ASN A 192      -6.198   6.150  27.757  1.00 40.97           C
ANISOU 1666  CG  ASN A 192     3275   5692   6600   1225   -480   -695       C
ATOM   1667  OD1 ASN A 192      -5.976   6.983  26.879  1.00 41.90           O
ANISOU 1667  OD1 ASN A 192     3353   5785   6784   1106   -431   -754       O
ATOM   1668  ND2 ASN A 192      -6.090   4.845  27.548  1.00 39.07           N
ANISOU 1668  ND2 ASN A 192     3079   5392   6373   1346   -394   -618       N
ATOM   1669  N   LEU A 193      -5.986   8.572  31.928  1.00 55.94           N
ANISOU 1669  N   LEU A 193     4933   8041   8282   1222  -1035   -867       N
ATOM   1670  CA  LEU A 193      -6.591   9.134  33.128  1.00 54.93           C
ANISOU 1670  CA  LEU A 193     4835   8011   8025   1222  -1171   -921       C
ATOM   1671  C   LEU A 193      -6.385  10.639  33.253  1.00 55.44           C
ANISOU 1671  C   LEU A 193     4809   8112   8142   1079  -1261  -1077       C
ATOM   1672  O   LEU A 193      -6.867  11.232  34.222  1.00 63.11           O
ANISOU 1672  O   LEU A 193     5800   9165   9013   1068  -1375  -1151       O
ATOM   1673  CB  LEU A 193      -6.044   8.432  34.375  1.00 56.27           C
ANISOU 1673  CB  LEU A 193     4922   8357   8102   1389  -1285   -862       C
ATOM   1674  CG  LEU A 193      -6.449   6.967  34.554  1.00 55.88           C
ANISOU 1674  CG  LEU A 193     4980   8269   7982   1544  -1211   -694       C
ATOM   1675  CD1 LEU A 193      -6.176   6.505  35.971  1.00 58.89           C
ANISOU 1675  CD1 LEU A 193     5301   8841   8233   1701  -1340   -632       C
ATOM   1676  CD2 LEU A 193      -7.910   6.774  34.206  1.00 51.87           C
ANISOU 1676  CD2 LEU A 193     4686   7612   7411   1492  -1117   -657       C
ATOM   1677  N   THR A 194      -5.684  11.267  32.313  1.00 51.96           N
ANISOU 1677  N   THR A 194     4269   7613   7860    971  -1207  -1130       N
ATOM   1678  CA  THR A 194      -5.589  12.720  32.305  1.00 50.57           C
ANISOU 1678  CA  THR A 194     4021   7429   7763    819  -1268  -1270       C
ATOM   1679  C   THR A 194      -6.927  13.335  31.905  1.00 46.41           C
ANISOU 1679  C   THR A 194     3670   6765   7198    718  -1210  -1290       C
ATOM   1680  O   THR A 194      -7.711  12.740  31.159  1.00 47.00           O
ANISOU 1680  O   THR A 194     3893   6727   7237    727  -1088  -1199       O
ATOM   1681  CB  THR A 194      -4.484  13.182  31.352  1.00 52.77           C
ANISOU 1681  CB  THR A 194     4143   7673   8235    732  -1207  -1296       C
ATOM   1682  OG1 THR A 194      -4.987  13.245  30.011  1.00 50.93           O
ANISOU 1682  OG1 THR A 194     4016   7274   8061    651  -1043  -1242       O
ATOM   1683  CG2 THR A 194      -3.306  12.231  31.397  1.00 59.97           C
ANISOU 1683  CG2 THR A 194     4915   8684   9188    854  -1206  -1228       C
ATOM   1684  N   ALA A 195      -7.184  14.543  32.416  1.00 48.23           N
ANISOU 1684  N   ALA A 195     3877   7008   7440    623  -1301  -1419       N
ATOM   1685  CA  ALA A 195      -8.475  15.188  32.193  1.00 52.50           C
ANISOU 1685  CA  ALA A 195     4574   7431   7941    541  -1261  -1442       C
ATOM   1686  C   ALA A 195      -8.780  15.324  30.707  1.00 52.49           C
ANISOU 1686  C   ALA A 195     4642   7266   8037    450  -1101  -1375       C
ATOM   1687  O   ALA A 195      -9.920  15.102  30.275  1.00 47.60           O
ANISOU 1687  O   ALA A 195     4186   6555   7345    443  -1024  -1315       O
ATOM   1688  CB  ALA A 195      -8.500  16.556  32.872  1.00 51.46           C
ANISOU 1688  CB  ALA A 195     4380   7324   7850    446  -1375  -1606       C
ATOM   1689  N   ARG A 196      -7.767  15.674  29.907  1.00 51.86           N
ANISOU 1689  N   ARG A 196     4430   7157   8116    382  -1050  -1382       N
ATOM   1690  CA  ARG A 196      -7.966  15.809  28.469  1.00 51.90           C
ANISOU 1690  CA  ARG A 196     4488   7030   8201    304   -894  -1312       C
ATOM   1691  C   ARG A 196      -8.442  14.500  27.856  1.00 48.65           C
ANISOU 1691  C   ARG A 196     4204   6586   7694    394   -785  -1192       C
ATOM   1692  O   ARG A 196      -9.258  14.500  26.927  1.00 50.49           O
ANISOU 1692  O   ARG A 196     4561   6716   7905    348   -679  -1140       O
ATOM   1693  CB  ARG A 196      -6.673  16.274  27.798  1.00 57.11           C
ANISOU 1693  CB  ARG A 196     4967   7690   9040    235   -852  -1326       C
ATOM   1694  CG  ARG A 196      -6.249  17.687  28.166  1.00 69.10           C
ANISOU 1694  CG  ARG A 196     6360   9199  10696    112   -934  -1447       C
ATOM   1695  CD  ARG A 196      -5.265  18.249  27.151  1.00 80.93           C
ANISOU 1695  CD  ARG A 196     7714  10647  12387     13   -840  -1427       C
ATOM   1696  NE  ARG A 196      -5.864  18.374  25.825  1.00 87.34           N
ANISOU 1696  NE  ARG A 196     8637  11334  13213    -42   -678  -1326       N
ATOM   1697  CZ  ARG A 196      -6.541  19.440  25.408  1.00 93.81           C
ANISOU 1697  CZ  ARG A 196     9517  12037  14090   -153   -641  -1334       C
ATOM   1698  NH1 ARG A 196      -6.707  20.481  26.214  1.00 99.77           N
ANISOU 1698  NH1 ARG A 196    10235  12766  14908   -224   -749  -1449       N
ATOM   1699  NH2 ARG A 196      -7.053  19.465  24.184  1.00 91.11           N
ANISOU 1699  NH2 ARG A 196     9270  11608  13741   -188   -497  -1228       N
ATOM   1700  N   GLN A 197      -7.946  13.373  28.367  1.00 45.88           N
ANISOU 1700  N   GLN A 197     3823   6322   7289    525   -812  -1148       N
ATOM   1701  CA  GLN A 197      -8.367  12.080  27.842  1.00 45.50           C
ANISOU 1701  CA  GLN A 197     3893   6227   7170    613   -708  -1045       C
ATOM   1702  C   GLN A 197      -9.683  11.618  28.452  1.00 39.25           C
ANISOU 1702  C   GLN A 197     3270   5414   6230    660   -734  -1014       C
ATOM   1703  O   GLN A 197     -10.493  10.992  27.760  1.00 32.05           O
ANISOU 1703  O   GLN A 197     2494   4413   5272    664   -634   -953       O
ATOM   1704  CB  GLN A 197      -7.272  11.037  28.074  1.00 41.67           C
ANISOU 1704  CB  GLN A 197     3301   5822   6711    740   -710   -998       C
ATOM   1705  CG  GLN A 197      -6.060  11.207  27.163  1.00 40.60           C
ANISOU 1705  CG  GLN A 197     3016   5688   6721    705   -634  -1000       C
ATOM   1706  CD  GLN A 197      -6.350  10.820  25.720  1.00 42.01           C
ANISOU 1706  CD  GLN A 197     3286   5756   6921    674   -462   -946       C
ATOM   1707  OE1 GLN A 197      -6.437  11.678  24.840  1.00 43.56           O
ANISOU 1707  OE1 GLN A 197     3479   5896   7177    555   -396   -964       O
ATOM   1708  NE2 GLN A 197      -6.504   9.523  25.472  1.00 40.49           N
ANISOU 1708  NE2 GLN A 197     3174   5532   6677    782   -387   -880       N
ATOM   1709  N   MET A 198      -9.923  11.925  29.729  1.00 40.86           N
ANISOU 1709  N   MET A 198     3463   5705   6356    694   -865  -1060       N
ATOM   1710  CA  MET A 198     -11.198  11.573  30.335  1.00 46.61           C
ANISOU 1710  CA  MET A 198     4344   6421   6945    734   -882  -1027       C
ATOM   1711  C   MET A 198     -12.354  12.344  29.724  1.00 45.60           C
ANISOU 1711  C   MET A 198     4334   6185   6809    620   -831  -1051       C
ATOM   1712  O   MET A 198     -13.493  11.875  29.791  1.00 45.37           O
ANISOU 1712  O   MET A 198     4443   6111   6683    642   -798  -1000       O
ATOM   1713  CB  MET A 198     -11.153  11.805  31.842  1.00 51.98           C
ANISOU 1713  CB  MET A 198     4978   7240   7531    799  -1031  -1077       C
ATOM   1714  CG  MET A 198     -10.314  10.780  32.567  1.00 62.79           C
ANISOU 1714  CG  MET A 198     6268   8728   8863    946  -1080  -1014       C
ATOM   1715  SD  MET A 198     -11.098   9.162  32.480  1.00 72.08           S
ANISOU 1715  SD  MET A 198     7597   9836   9953   1065   -978   -852       S
ATOM   1716  CE  MET A 198     -12.170   9.207  33.910  1.00 69.16           C
ANISOU 1716  CE  MET A 198     7318   9560   9402   1126  -1072   -841       C
ATOM   1717  N   ALA A 199     -12.085  13.501  29.111  1.00 42.60           N
ANISOU 1717  N   ALA A 199     3894   5759   6535    502   -819  -1116       N
ATOM   1718  CA  ALA A 199     -13.156  14.290  28.509  1.00 38.89           C
ANISOU 1718  CA  ALA A 199     3526   5187   6064    402   -770  -1126       C
ATOM   1719  C   ALA A 199     -13.936  13.505  27.457  1.00 41.91           C
ANISOU 1719  C   ALA A 199     4038   5483   6404    402   -645  -1034       C
ATOM   1720  O   ALA A 199     -15.140  13.727  27.291  1.00 47.99           O
ANISOU 1720  O   ALA A 199     4925   6198   7113    366   -623  -1019       O
ATOM   1721  CB  ALA A 199     -12.583  15.566  27.893  1.00 33.90           C
ANISOU 1721  CB  ALA A 199     2796   4507   5578    282   -758  -1186       C
ATOM   1722  N   TYR A 200     -13.279  12.583  26.743  1.00 36.79           N
ANISOU 1722  N   TYR A 200     3367   4826   5787    444   -564   -979       N
ATOM   1723  CA  TYR A 200     -13.965  11.887  25.655  1.00 42.05           C
ANISOU 1723  CA  TYR A 200     4148   5412   6417    434   -446   -917       C
ATOM   1724  C   TYR A 200     -15.020  10.905  26.160  1.00 46.59           C
ANISOU 1724  C   TYR A 200     4852   5971   6879    502   -448   -872       C
ATOM   1725  O   TYR A 200     -16.178  10.987  25.707  1.00 46.65           O
ANISOU 1725  O   TYR A 200     4972   5919   6833    452   -409   -856       O
ATOM   1726  CB  TYR A 200     -12.936  11.208  24.743  1.00 43.63           C
ANISOU 1726  CB  TYR A 200     4284   5607   6686    462   -353   -889       C
ATOM   1727  CG  TYR A 200     -12.053  12.172  23.982  1.00 44.30           C
ANISOU 1727  CG  TYR A 200     4254   5694   6885    380   -316   -914       C
ATOM   1728  CD1 TYR A 200     -12.505  12.794  22.826  1.00 39.32           C
ANISOU 1728  CD1 TYR A 200     3669   5004   6267    285   -230   -897       C
ATOM   1729  CD2 TYR A 200     -10.760  12.452  24.415  1.00 54.19           C
ANISOU 1729  CD2 TYR A 200     5343   7014   8234    397   -365   -946       C
ATOM   1730  CE1 TYR A 200     -11.702  13.675  22.126  1.00 46.55           C
ANISOU 1730  CE1 TYR A 200     4476   5918   7292    211   -184   -900       C
ATOM   1731  CE2 TYR A 200      -9.945  13.332  23.720  1.00 57.05           C
ANISOU 1731  CE2 TYR A 200     5589   7372   8717    313   -323   -962       C
ATOM   1732  CZ  TYR A 200     -10.422  13.942  22.576  1.00 55.52           C
ANISOU 1732  CZ  TYR A 200     5449   7109   8537    221   -227   -933       C
ATOM   1733  OH  TYR A 200      -9.618  14.817  21.878  1.00 54.93           O
ANISOU 1733  OH  TYR A 200     5257   7027   8587    139   -173   -928       O
ATOM   1734  N   PRO A 201     -14.713   9.960  27.060  1.00 47.53           N
ANISOU 1734  N   PRO A 201     4959   6139   6962    614   -488   -840       N
ATOM   1735  CA  PRO A 201     -15.782   9.073  27.549  1.00 44.72           C
ANISOU 1735  CA  PRO A 201     4725   5757   6510    669   -480   -783       C
ATOM   1736  C   PRO A 201     -16.832   9.806  28.356  1.00 40.54           C
ANISOU 1736  C   PRO A 201     4252   5253   5900    639   -553   -805       C
ATOM   1737  O   PRO A 201     -17.993   9.379  28.374  1.00 39.27           O
ANISOU 1737  O   PRO A 201     4202   5046   5672    636   -521   -764       O
ATOM   1738  CB  PRO A 201     -15.027   8.045  28.403  1.00 44.90           C
ANISOU 1738  CB  PRO A 201     4695   5838   6526    804   -512   -731       C
ATOM   1739  CG  PRO A 201     -13.792   8.746  28.817  1.00 46.83           C
ANISOU 1739  CG  PRO A 201     4786   6180   6827    814   -591   -785       C
ATOM   1740  CD  PRO A 201     -13.409   9.595  27.642  1.00 45.24           C
ANISOU 1740  CD  PRO A 201     4539   5931   6718    700   -536   -839       C
ATOM   1741  N   VAL A 202     -16.459  10.897  29.026  1.00 36.12           N
ANISOU 1741  N   VAL A 202     3611   4763   5349    614   -648   -876       N
ATOM   1742  CA  VAL A 202     -17.451  11.735  29.690  1.00 36.82           C
ANISOU 1742  CA  VAL A 202     3750   4868   5370    579   -707   -916       C
ATOM   1743  C   VAL A 202     -18.447  12.278  28.671  1.00 39.28           C
ANISOU 1743  C   VAL A 202     4146   5081   5697    478   -636   -914       C
ATOM   1744  O   VAL A 202     -19.665  12.245  28.889  1.00 38.04           O
ANISOU 1744  O   VAL A 202     4085   4904   5466    472   -629   -891       O
ATOM   1745  CB  VAL A 202     -16.752  12.869  30.466  1.00 44.05           C
ANISOU 1745  CB  VAL A 202     4555   5865   6318    561   -817  -1019       C
ATOM   1746  CG1 VAL A 202     -17.771  13.893  30.942  1.00 41.05           C
ANISOU 1746  CG1 VAL A 202     4228   5477   5891    512   -861  -1080       C
ATOM   1747  CG2 VAL A 202     -15.960  12.310  31.643  1.00 28.76           C
ANISOU 1747  CG2 VAL A 202     2541   4057   4328    675   -906  -1018       C
ATOM   1748  N   ILE A 203     -17.944  12.769  27.536  1.00 34.07           N
ANISOU 1748  N   ILE A 203     3446   4369   5132    401   -580   -929       N
ATOM   1749  CA  ILE A 203     -18.820  13.290  26.491  1.00 31.95           C
ANISOU 1749  CA  ILE A 203     3248   4021   4870    312   -512   -914       C
ATOM   1750  C   ILE A 203     -19.712  12.183  25.946  1.00 37.11           C
ANISOU 1750  C   ILE A 203     4013   4633   5454    331   -439   -848       C
ATOM   1751  O   ILE A 203     -20.908  12.392  25.692  1.00 40.31           O
ANISOU 1751  O   ILE A 203     4502   5004   5811    290   -421   -831       O
ATOM   1752  CB  ILE A 203     -17.981  13.957  25.384  1.00 27.41           C
ANISOU 1752  CB  ILE A 203     2597   3413   4402    239   -458   -925       C
ATOM   1753  CG1 ILE A 203     -17.461  15.315  25.859  1.00 37.11           C
ANISOU 1753  CG1 ILE A 203     3731   4652   5718    188   -527   -996       C
ATOM   1754  CG2 ILE A 203     -18.790  14.153  24.117  1.00 25.67           C
ANISOU 1754  CG2 ILE A 203     2454   3130   4169    170   -370   -881       C
ATOM   1755  CD1 ILE A 203     -16.453  15.949  24.922  1.00 38.27           C
ANISOU 1755  CD1 ILE A 203     3779   4771   5992    120   -474   -998       C
ATOM   1756  N   ALA A 204     -19.150  10.984  25.769  1.00 33.88           N
ANISOU 1756  N   ALA A 204     3602   4223   5050    392   -395   -814       N
ATOM   1757  CA  ALA A 204     -19.950   9.863  25.285  1.00 32.97           C
ANISOU 1757  CA  ALA A 204     3587   4053   4887    406   -325   -767       C
ATOM   1758  C   ALA A 204     -21.075   9.529  26.262  1.00 40.36           C
ANISOU 1758  C   ALA A 204     4597   4995   5741    440   -364   -736       C
ATOM   1759  O   ALA A 204     -22.234   9.340  25.862  1.00 39.56           O
ANISOU 1759  O   ALA A 204     4582   4852   5599    398   -329   -716       O
ATOM   1760  CB  ALA A 204     -19.054   8.648  25.050  1.00 28.44           C
ANISOU 1760  CB  ALA A 204     2990   3465   4351    478   -272   -745       C
ATOM   1761  N   GLY A 205     -20.748   9.460  27.555  1.00 38.25           N
ANISOU 1761  N   GLY A 205     4293   4795   5447    517   -438   -729       N
ATOM   1762  CA  GLY A 205     -21.770   9.188  28.553  1.00 39.89           C
ANISOU 1762  CA  GLY A 205     4563   5025   5568    557   -469   -690       C
ATOM   1763  C   GLY A 205     -22.843  10.259  28.599  1.00 39.58           C
ANISOU 1763  C   GLY A 205     4561   4987   5490    488   -495   -723       C
ATOM   1764  O   GLY A 205     -24.022   9.960  28.796  1.00 42.36           O
ANISOU 1764  O   GLY A 205     4988   5323   5786    483   -475   -683       O
ATOM   1765  N   ILE A 206     -22.450  11.520  28.414  1.00 35.75           N
ANISOU 1765  N   ILE A 206     4019   4517   5048    434   -533   -792       N
ATOM   1766  CA  ILE A 206     -23.432  12.598  28.385  1.00 36.18           C
ANISOU 1766  CA  ILE A 206     4105   4557   5084    373   -550   -822       C
ATOM   1767  C   ILE A 206     -24.362  12.439  27.189  1.00 41.58           C
ANISOU 1767  C   ILE A 206     4859   5170   5769    304   -473   -782       C
ATOM   1768  O   ILE A 206     -25.582  12.616  27.305  1.00 40.13           O
ANISOU 1768  O   ILE A 206     4733   4978   5535    286   -469   -763       O
ATOM   1769  CB  ILE A 206     -22.724  13.964  28.382  1.00 36.40           C
ANISOU 1769  CB  ILE A 206     4051   4592   5186    327   -599   -903       C
ATOM   1770  CG1 ILE A 206     -22.107  14.237  29.753  1.00 37.11           C
ANISOU 1770  CG1 ILE A 206     4077   4772   5251    392   -696   -965       C
ATOM   1771  CG2 ILE A 206     -23.692  15.075  28.020  1.00 33.48           C
ANISOU 1771  CG2 ILE A 206     3715   4176   4829    258   -591   -921       C
ATOM   1772  CD1 ILE A 206     -21.259  15.484  29.798  1.00 36.32           C
ANISOU 1772  CD1 ILE A 206     3881   4673   5246    341   -748  -1062       C
ATOM   1773  N   THR A 207     -23.808  12.096  26.024  1.00 40.93           N
ANISOU 1773  N   THR A 207     4767   5048   5736    269   -411   -772       N
ATOM   1774  CA  THR A 207     -24.660  11.893  24.855  1.00 40.76           C
ANISOU 1774  CA  THR A 207     4808   4981   5698    207   -345   -743       C
ATOM   1775  C   THR A 207     -25.629  10.736  25.072  1.00 40.20           C
ANISOU 1775  C   THR A 207     4814   4892   5568    231   -319   -702       C
ATOM   1776  O   THR A 207     -26.795  10.810  24.667  1.00 39.00           O
ANISOU 1776  O   THR A 207     4713   4725   5379    185   -302   -684       O
ATOM   1777  CB  THR A 207     -23.810  11.656  23.611  1.00 37.59           C
ANISOU 1777  CB  THR A 207     4381   4558   5344    177   -280   -747       C
ATOM   1778  OG1 THR A 207     -22.882  10.594  23.862  1.00 49.49           O
ANISOU 1778  OG1 THR A 207     5865   6067   6874    242   -263   -747       O
ATOM   1779  CG2 THR A 207     -23.050  12.920  23.249  1.00 31.10           C
ANISOU 1779  CG2 THR A 207     3483   3743   4591    134   -291   -771       C
ATOM   1780  N   ILE A 208     -25.175   9.667  25.729  1.00 38.35           N
ANISOU 1780  N   ILE A 208     4581   4659   5333    303   -316   -679       N
ATOM   1781  CA  ILE A 208     -26.073   8.544  26.003  1.00 40.16           C
ANISOU 1781  CA  ILE A 208     4878   4856   5527    324   -284   -630       C
ATOM   1782  C   ILE A 208     -27.168   8.956  26.984  1.00 37.61           C
ANISOU 1782  C   ILE A 208     4579   4569   5141    334   -326   -604       C
ATOM   1783  O   ILE A 208     -28.347   8.608  26.812  1.00 31.99           O
ANISOU 1783  O   ILE A 208     3920   3832   4404    299   -297   -574       O
ATOM   1784  CB  ILE A 208     -25.277   7.333  26.520  1.00 40.55           C
ANISOU 1784  CB  ILE A 208     4917   4887   5603    410   -265   -595       C
ATOM   1785  CG1 ILE A 208     -24.439   6.729  25.396  1.00 38.77           C
ANISOU 1785  CG1 ILE A 208     4681   4609   5440    398   -201   -622       C
ATOM   1786  CG2 ILE A 208     -26.212   6.279  27.096  1.00 40.07           C
ANISOU 1786  CG2 ILE A 208     4917   4789   5518    439   -236   -527       C
ATOM   1787  CD1 ILE A 208     -23.713   5.473  25.802  1.00 35.34           C
ANISOU 1787  CD1 ILE A 208     4240   4139   5049    488   -169   -584       C
ATOM   1788  N   GLY A 209     -26.797   9.689  28.034  1.00 37.90           N
ANISOU 1788  N   GLY A 209     4573   4673   5154    382   -393   -622       N
ATOM   1789  CA  GLY A 209     -27.793  10.173  28.972  1.00 28.61           C
ANISOU 1789  CA  GLY A 209     3418   3543   3911    400   -428   -610       C
ATOM   1790  C   GLY A 209     -28.833  11.045  28.301  1.00 35.94           C
ANISOU 1790  C   GLY A 209     4368   4449   4837    321   -419   -629       C
ATOM   1791  O   GLY A 209     -30.027  10.926  28.577  1.00 41.83           O
ANISOU 1791  O   GLY A 209     5153   5201   5539    314   -405   -593       O
ATOM   1792  N   LEU A 210     -28.396  11.923  27.396  1.00 39.27           N
ANISOU 1792  N   LEU A 210     4761   4849   5311    263   -421   -674       N
ATOM   1793  CA  LEU A 210     -29.340  12.777  26.683  1.00 38.60           C
ANISOU 1793  CA  LEU A 210     4693   4744   5228    197   -409   -675       C
ATOM   1794  C   LEU A 210     -30.206  11.974  25.721  1.00 41.82           C
ANISOU 1794  C   LEU A 210     5150   5121   5619    147   -353   -633       C
ATOM   1795  O   LEU A 210     -31.378  12.315  25.508  1.00 43.03           O
ANISOU 1795  O   LEU A 210     5325   5280   5746    114   -349   -613       O
ATOM   1796  CB  LEU A 210     -28.590  13.878  25.941  1.00 37.71           C
ANISOU 1796  CB  LEU A 210     4534   4612   5182    153   -416   -714       C
ATOM   1797  CG  LEU A 210     -27.892  14.882  26.857  1.00 40.95           C
ANISOU 1797  CG  LEU A 210     4888   5045   5627    182   -479   -776       C
ATOM   1798  CD1 LEU A 210     -27.344  16.047  26.051  1.00 43.85           C
ANISOU 1798  CD1 LEU A 210     5209   5371   6083    123   -473   -802       C
ATOM   1799  CD2 LEU A 210     -28.843  15.371  27.944  1.00 41.30           C
ANISOU 1799  CD2 LEU A 210     4952   5123   5620    218   -518   -793       C
ATOM   1800  N   TYR A 211     -29.650  10.908  25.140  1.00 40.24           N
ANISOU 1800  N   TYR A 211     4963   4891   5437    143   -311   -628       N
ATOM   1801  CA  TYR A 211     -30.449   9.995  24.329  1.00 41.37           C
ANISOU 1801  CA  TYR A 211     5152   5002   5566     97   -262   -609       C
ATOM   1802  C   TYR A 211     -31.590   9.402  25.140  1.00 39.40           C
ANISOU 1802  C   TYR A 211     4934   4753   5284    111   -261   -565       C
ATOM   1803  O   TYR A 211     -32.736   9.354  24.681  1.00 39.13           O
ANISOU 1803  O   TYR A 211     4920   4718   5228     58   -248   -552       O
ATOM   1804  CB  TYR A 211     -29.565   8.880  23.777  1.00 40.01           C
ANISOU 1804  CB  TYR A 211     4988   4787   5428    106   -215   -625       C
ATOM   1805  CG  TYR A 211     -30.284   7.886  22.892  1.00 39.26           C
ANISOU 1805  CG  TYR A 211     4939   4651   5329     52   -164   -634       C
ATOM   1806  CD1 TYR A 211     -31.195   8.308  21.933  1.00 38.79           C
ANISOU 1806  CD1 TYR A 211     4892   4615   5233    -22   -162   -647       C
ATOM   1807  CD2 TYR A 211     -30.029   6.526  22.999  1.00 39.00           C
ANISOU 1807  CD2 TYR A 211     4931   4553   5332     78   -120   -632       C
ATOM   1808  CE1 TYR A 211     -31.838   7.396  21.112  1.00 39.81           C
ANISOU 1808  CE1 TYR A 211     5054   4718   5354    -77   -125   -674       C
ATOM   1809  CE2 TYR A 211     -30.662   5.615  22.186  1.00 40.20           C
ANISOU 1809  CE2 TYR A 211     5123   4658   5495     22    -75   -661       C
ATOM   1810  CZ  TYR A 211     -31.566   6.052  21.246  1.00 39.74           C
ANISOU 1810  CZ  TYR A 211     5073   4636   5391    -59    -82   -690       C
ATOM   1811  OH  TYR A 211     -32.196   5.133  20.442  1.00 43.84           O
ANISOU 1811  OH  TYR A 211     5624   5118   5916   -121    -47   -737       O
ATOM   1812  N   VAL A 212     -31.285   8.927  26.348  1.00 32.92           N
ANISOU 1812  N   VAL A 212     4112   3941   4455    186   -272   -536       N
ATOM   1813  CA  VAL A 212     -32.330   8.331  27.177  1.00 34.42           C
ANISOU 1813  CA  VAL A 212     4327   4135   4614    206   -258   -477       C
ATOM   1814  C   VAL A 212     -33.322   9.397  27.635  1.00 39.77           C
ANISOU 1814  C   VAL A 212     4996   4871   5246    199   -291   -473       C
ATOM   1815  O   VAL A 212     -34.538   9.170  27.652  1.00 37.21           O
ANISOU 1815  O   VAL A 212     4686   4548   4905    168   -269   -437       O
ATOM   1816  CB  VAL A 212     -31.713   7.582  28.368  1.00 36.04           C
ANISOU 1816  CB  VAL A 212     4530   4351   4811    300   -259   -428       C
ATOM   1817  CG1 VAL A 212     -32.811   6.912  29.192  1.00 33.05           C
ANISOU 1817  CG1 VAL A 212     4177   3976   4404    320   -228   -347       C
ATOM   1818  CG2 VAL A 212     -30.694   6.556  27.876  1.00 29.76           C
ANISOU 1818  CG2 VAL A 212     3739   3490   4077    316   -222   -430       C
ATOM   1819  N   LEU A 213     -32.822  10.578  27.999  1.00 38.34           N
ANISOU 1819  N   LEU A 213     4783   4732   5053    227   -341   -516       N
ATOM   1820  CA  LEU A 213     -33.674  11.672  28.439  1.00 28.83           C
ANISOU 1820  CA  LEU A 213     3568   3571   3816    230   -368   -526       C
ATOM   1821  C   LEU A 213     -34.542  12.233  27.318  1.00 33.82           C
ANISOU 1821  C   LEU A 213     4202   4183   4466    154   -355   -526       C
ATOM   1822  O   LEU A 213     -35.500  12.962  27.601  1.00 26.12           O
ANISOU 1822  O   LEU A 213     3219   3236   3471    157   -365   -518       O
ATOM   1823  CB  LEU A 213     -32.811  12.774  29.053  1.00 28.06           C
ANISOU 1823  CB  LEU A 213     3434   3505   3721    273   -424   -591       C
ATOM   1824  CG  LEU A 213     -32.215  12.423  30.418  1.00 32.02           C
ANISOU 1824  CG  LEU A 213     3925   4068   4174    363   -455   -594       C
ATOM   1825  CD1 LEU A 213     -31.512  13.631  31.034  1.00 31.41           C
ANISOU 1825  CD1 LEU A 213     3805   4031   4098    394   -521   -683       C
ATOM   1826  CD2 LEU A 213     -33.297  11.878  31.349  1.00 30.43           C
ANISOU 1826  CD2 LEU A 213     3751   3913   3898    409   -431   -529       C
ATOM   1827  N   SER A 214     -34.237  11.918  26.060  1.00 36.89           N
ANISOU 1827  N   SER A 214     4596   4534   4886     94   -332   -534       N
ATOM   1828  CA  SER A 214     -35.167  12.214  24.978  1.00 30.38           C
ANISOU 1828  CA  SER A 214     3773   3712   4057     26   -320   -520       C
ATOM   1829  C   SER A 214     -36.181  11.099  24.752  1.00 34.21           C
ANISOU 1829  C   SER A 214     4280   4192   4526    -13   -288   -489       C
ATOM   1830  O   SER A 214     -37.273  11.368  24.237  1.00 37.96           O
ANISOU 1830  O   SER A 214     4745   4693   4986    -57   -290   -471       O
ATOM   1831  CB  SER A 214     -34.403  12.465  23.672  1.00 24.65           C
ANISOU 1831  CB  SER A 214     3041   2970   3356    -20   -309   -545       C
ATOM   1832  OG  SER A 214     -33.287  13.309  23.887  1.00 33.04           O
ANISOU 1832  OG  SER A 214     4075   4023   4455      9   -329   -574       O
ATOM   1833  N   TRP A 215     -35.851   9.864  25.133  1.00 31.67           N
ANISOU 1833  N   TRP A 215     3981   3833   4218      1   -259   -480       N
ATOM   1834  CA  TRP A 215     -36.652   8.702  24.752  1.00 34.82           C
ANISOU 1834  CA  TRP A 215     4398   4201   4631    -52   -222   -464       C
ATOM   1835  C   TRP A 215     -36.353   7.581  25.738  1.00 38.54           C
ANISOU 1835  C   TRP A 215     4889   4627   5127     -2   -189   -424       C
ATOM   1836  O   TRP A 215     -35.260   7.011  25.704  1.00 45.35           O
ANISOU 1836  O   TRP A 215     5765   5447   6019     29   -174   -441       O
ATOM   1837  CB  TRP A 215     -36.328   8.282  23.324  1.00 29.53           C
ANISOU 1837  CB  TRP A 215     3739   3505   3975   -119   -205   -517       C
ATOM   1838  CG  TRP A 215     -37.315   7.342  22.706  1.00 39.58           C
ANISOU 1838  CG  TRP A 215     5022   4757   5261   -195   -181   -529       C
ATOM   1839  CD1 TRP A 215     -38.666   7.512  22.616  1.00 40.46           C
ANISOU 1839  CD1 TRP A 215     5110   4909   5355   -242   -193   -506       C
ATOM   1840  CD2 TRP A 215     -37.025   6.088  22.074  1.00 39.93           C
ANISOU 1840  CD2 TRP A 215     5093   4732   5347   -235   -140   -577       C
ATOM   1841  NE1 TRP A 215     -39.235   6.440  21.969  1.00 45.04           N
ANISOU 1841  NE1 TRP A 215     5696   5454   5964   -318   -170   -541       N
ATOM   1842  CE2 TRP A 215     -38.248   5.552  21.627  1.00 40.13           C
ANISOU 1842  CE2 TRP A 215     5109   4758   5381   -316   -135   -591       C
ATOM   1843  CE3 TRP A 215     -35.848   5.367  21.842  1.00 36.65           C
ANISOU 1843  CE3 TRP A 215     4703   4252   4969   -209   -106   -617       C
ATOM   1844  CZ2 TRP A 215     -38.329   4.330  20.964  1.00 36.55           C
ANISOU 1844  CZ2 TRP A 215     4676   4236   4976   -378    -99   -655       C
ATOM   1845  CZ3 TRP A 215     -35.930   4.155  21.184  1.00 39.02           C
ANISOU 1845  CZ3 TRP A 215     5028   4481   5317   -260    -64   -674       C
ATOM   1846  CH2 TRP A 215     -37.162   3.648  20.753  1.00 40.53           C
ANISOU 1846  CH2 TRP A 215     5214   4666   5518   -347    -61   -699       C
ATOM   1847  N   GLY A 216     -37.323   7.263  26.597  1.00 41.28           N
ANISOU 1847  N   GLY A 216     5232   4987   5464     11   -172   -363       N
ATOM   1848  CA  GLY A 216     -37.120   6.280  27.650  1.00 34.79           C
ANISOU 1848  CA  GLY A 216     4426   4133   4659     70   -136   -297       C
ATOM   1849  C   GLY A 216     -36.655   4.919  27.171  1.00 39.52           C
ANISOU 1849  C   GLY A 216     5053   4630   5333     46    -86   -300       C
ATOM   1850  O   GLY A 216     -36.008   4.194  27.933  1.00 47.12           O
ANISOU 1850  O   GLY A 216     6028   5558   6317    116    -60   -248       O
ATOM   1851  N   ALA A 217     -36.974   4.546  25.930  1.00 41.77           N
ANISOU 1851  N   ALA A 217     5345   4869   5657    -47    -72   -362       N
ATOM   1852  CA  ALA A 217     -36.462   3.303  25.367  1.00 46.45           C
ANISOU 1852  CA  ALA A 217     5965   5355   6328    -71    -23   -392       C
ATOM   1853  C   ALA A 217     -35.010   3.412  24.917  1.00 52.10           C
ANISOU 1853  C   ALA A 217     6690   6059   7047    -27    -31   -446       C
ATOM   1854  O   ALA A 217     -34.410   2.394  24.546  1.00 56.17           O
ANISOU 1854  O   ALA A 217     7228   6484   7630    -24     15   -473       O
ATOM   1855  CB  ALA A 217     -37.337   2.860  24.193  1.00 40.12           C
ANISOU 1855  CB  ALA A 217     5165   4521   5557   -188    -10   -461       C
ATOM   1856  N   GLY A 218     -34.430   4.614  24.964  1.00 46.21           N
ANISOU 1856  N   GLY A 218     5922   5395   6241      8    -82   -464       N
ATOM   1857  CA  GLY A 218     -33.058   4.824  24.541  1.00 43.60           C
ANISOU 1857  CA  GLY A 218     5584   5063   5919     44    -88   -510       C
ATOM   1858  C   GLY A 218     -32.040   3.973  25.270  1.00 39.98           C
ANISOU 1858  C   GLY A 218     5129   4554   5507    132    -62   -473       C
ATOM   1859  O   GLY A 218     -30.893   3.874  24.816  1.00 39.04           O
ANISOU 1859  O   GLY A 218     5000   4420   5415    159    -53   -514       O
ATOM   1860  N   PHE A 219     -32.432   3.346  26.387  1.00 31.22           N
ANISOU 1860  N   PHE A 219     4029   3425   4409    182    -45   -386       N
ATOM   1861  CA  PHE A 219     -31.552   2.396  27.055  1.00 32.76           C
ANISOU 1861  CA  PHE A 219     4228   3567   4653    273    -14   -330       C
ATOM   1862  C   PHE A 219     -31.065   1.317  26.103  1.00 40.15           C
ANISOU 1862  C   PHE A 219     5187   4385   5682    248     49   -379       C
ATOM   1863  O   PHE A 219     -30.036   0.685  26.371  1.00 41.37           O
ANISOU 1863  O   PHE A 219     5336   4497   5885    329     73   -354       O
ATOM   1864  CB  PHE A 219     -32.264   1.755  28.251  1.00 28.07           C
ANISOU 1864  CB  PHE A 219     3645   2960   4060    319     13   -212       C
ATOM   1865  CG  PHE A 219     -33.318   0.752  27.869  1.00 34.56           C
ANISOU 1865  CG  PHE A 219     4498   3675   4959    242     80   -194       C
ATOM   1866  CD1 PHE A 219     -33.004  -0.594  27.727  1.00 31.90           C
ANISOU 1866  CD1 PHE A 219     4186   3202   4733    256    152   -168       C
ATOM   1867  CD2 PHE A 219     -34.636   1.152  27.667  1.00 38.30           C
ANISOU 1867  CD2 PHE A 219     4968   4179   5405    155     72   -203       C
ATOM   1868  CE1 PHE A 219     -33.979  -1.521  27.376  1.00 37.58           C
ANISOU 1868  CE1 PHE A 219     4928   3809   5542    173    213   -163       C
ATOM   1869  CE2 PHE A 219     -35.617   0.229  27.322  1.00 31.70           C
ANISOU 1869  CE2 PHE A 219     4147   3247   4649     73    129   -194       C
ATOM   1870  CZ  PHE A 219     -35.288  -1.108  27.178  1.00 36.07           C
ANISOU 1870  CZ  PHE A 219     4727   3658   5321     77    199   -179       C
ATOM   1871  N   ILE A 220     -31.775   1.105  24.991  1.00 43.96           N
ANISOU 1871  N   ILE A 220     5692   4823   6186    143     74   -455       N
ATOM   1872  CA  ILE A 220     -31.361   0.124  23.993  1.00 43.60           C
ANISOU 1872  CA  ILE A 220     5673   4672   6221    114    133   -532       C
ATOM   1873  C   ILE A 220     -29.952   0.390  23.463  1.00 39.88           C
ANISOU 1873  C   ILE A 220     5182   4224   5748    164    132   -587       C
ATOM   1874  O   ILE A 220     -29.329  -0.513  22.893  1.00 33.93           O
ANISOU 1874  O   ILE A 220     4444   3381   5067    180    191   -636       O
ATOM   1875  CB  ILE A 220     -32.400   0.089  22.848  1.00 41.57           C
ANISOU 1875  CB  ILE A 220     5434   4406   5955    -13    139   -624       C
ATOM   1876  CG1 ILE A 220     -32.346  -1.246  22.102  1.00 47.47           C
ANISOU 1876  CG1 ILE A 220     6216   5017   6805    -51    211   -700       C
ATOM   1877  CG2 ILE A 220     -32.195   1.259  21.891  1.00 37.18           C
ANISOU 1877  CG2 ILE A 220     4858   3961   5307    -54     93   -698       C
ATOM   1878  CD1 ILE A 220     -32.701  -2.440  22.956  1.00 48.21           C
ANISOU 1878  CD1 ILE A 220     6328   4977   7013    -26    268   -618       C
ATOM   1879  N   ILE A 221     -29.424   1.606  23.642  1.00 38.13           N
ANISOU 1879  N   ILE A 221     4920   4115   5453    191     72   -584       N
ATOM   1880  CA  ILE A 221     -28.069   1.891  23.174  1.00 36.42           C
ANISOU 1880  CA  ILE A 221     4669   3924   5244    234     75   -628       C
ATOM   1881  C   ILE A 221     -27.029   1.137  23.993  1.00 37.40           C
ANISOU 1881  C   ILE A 221     4774   4005   5433    350     96   -570       C
ATOM   1882  O   ILE A 221     -25.928   0.875  23.499  1.00 40.26           O
ANISOU 1882  O   ILE A 221     5113   4349   5837    390    127   -609       O
ATOM   1883  CB  ILE A 221     -27.785   3.409  23.192  1.00 32.23           C
ANISOU 1883  CB  ILE A 221     4093   3511   4642    224      8   -637       C
ATOM   1884  CG1 ILE A 221     -26.525   3.744  22.385  1.00 34.07           C
ANISOU 1884  CG1 ILE A 221     4286   3769   4891    238     24   -693       C
ATOM   1885  CG2 ILE A 221     -27.618   3.918  24.613  1.00 22.77           C
ANISOU 1885  CG2 ILE A 221     2863   2371   3418    298    -52   -563       C
ATOM   1886  CD1 ILE A 221     -26.590   3.342  20.931  1.00 33.76           C
ANISOU 1886  CD1 ILE A 221     4275   3699   4853    174     84   -775       C
ATOM   1887  N   ALA A 222     -27.359   0.759  25.232  1.00 36.54           N
ANISOU 1887  N   ALA A 222     4670   3886   5328    410     84   -469       N
ATOM   1888  CA  ALA A 222     -26.377   0.072  26.069  1.00 35.72           C
ANISOU 1888  CA  ALA A 222     4541   3758   5273    534     97   -394       C
ATOM   1889  C   ALA A 222     -26.106  -1.350  25.595  1.00 43.79           C
ANISOU 1889  C   ALA A 222     5595   4630   6412    557    189   -399       C
ATOM   1890  O   ALA A 222     -24.924  -1.719  25.471  1.00 44.83           O
ANISOU 1890  O   ALA A 222     5695   4742   6596    636    212   -406       O
ATOM   1891  CB  ALA A 222     -26.820   0.117  27.535  1.00 30.44           C
ANISOU 1891  CB  ALA A 222     3867   3143   4556    600     59   -274       C
ATOM   1892  N   PRO A 223     -27.109  -2.199  25.325  1.00 45.95           N
ANISOU 1892  N   PRO A 223     5926   4790   6743    495    246   -401       N
ATOM   1893  CA  PRO A 223     -26.777  -3.538  24.802  1.00 43.47           C
ANISOU 1893  CA  PRO A 223     5643   4315   6560    515    338   -429       C
ATOM   1894  C   PRO A 223     -26.052  -3.490  23.472  1.00 39.43           C
ANISOU 1894  C   PRO A 223     5126   3793   6062    485    368   -570       C
ATOM   1895  O   PRO A 223     -25.107  -4.261  23.260  1.00 46.62           O
ANISOU 1895  O   PRO A 223     6029   4623   7061    561    426   -585       O
ATOM   1896  CB  PRO A 223     -28.149  -4.220  24.682  1.00 41.07           C
ANISOU 1896  CB  PRO A 223     5392   3904   6308    421    380   -429       C
ATOM   1897  CG  PRO A 223     -29.004  -3.510  25.653  1.00 39.39           C
ANISOU 1897  CG  PRO A 223     5168   3792   6007    410    322   -333       C
ATOM   1898  CD  PRO A 223     -28.552  -2.077  25.603  1.00 36.18           C
ANISOU 1898  CD  PRO A 223     4719   3554   5474    414    235   -370       C
ATOM   1899  N   ILE A 224     -26.463  -2.591  22.574  1.00 36.97           N
ANISOU 1899  N   ILE A 224     4817   3568   5664    383    333   -668       N
ATOM   1900  CA  ILE A 224     -25.749  -2.402  21.312  1.00 43.11           C
ANISOU 1900  CA  ILE A 224     5584   4369   6427    360    361   -790       C
ATOM   1901  C   ILE A 224     -24.261  -2.201  21.569  1.00 43.64           C
ANISOU 1901  C   ILE A 224     5589   4479   6513    470    361   -761       C
ATOM   1902  O   ILE A 224     -23.413  -2.923  21.028  1.00 44.69           O
ANISOU 1902  O   ILE A 224     5716   4544   6718    522    430   -812       O
ATOM   1903  CB  ILE A 224     -26.346  -1.219  20.531  1.00 38.53           C
ANISOU 1903  CB  ILE A 224     5000   3910   5729    255    309   -854       C
ATOM   1904  CG1 ILE A 224     -27.800  -1.511  20.156  1.00 32.38           C
ANISOU 1904  CG1 ILE A 224     4271   3094   4937    146    309   -894       C
ATOM   1905  CG2 ILE A 224     -25.515  -0.926  19.291  1.00 35.14           C
ANISOU 1905  CG2 ILE A 224     4552   3529   5269    243    342   -956       C
ATOM   1906  CD1 ILE A 224     -28.452  -0.397  19.383  1.00 34.33           C
ANISOU 1906  CD1 ILE A 224     4512   3465   5069     53    258   -942       C
ATOM   1907  N   ILE A 225     -23.922  -1.232  22.422  1.00 35.33           N
ANISOU 1907  N   ILE A 225     4483   3541   5400    511    284   -685       N
ATOM   1908  CA  ILE A 225     -22.516  -1.007  22.745  1.00 40.33           C
ANISOU 1908  CA  ILE A 225     5041   4228   6055    611    272   -658       C
ATOM   1909  C   ILE A 225     -21.912  -2.248  23.389  1.00 41.24           C
ANISOU 1909  C   ILE A 225     5151   4243   6275    731    321   -587       C
ATOM   1910  O   ILE A 225     -20.771  -2.623  23.091  1.00 49.22           O
ANISOU 1910  O   ILE A 225     6117   5236   7347    807    363   -607       O
ATOM   1911  CB  ILE A 225     -22.356   0.239  23.634  1.00 44.15           C
ANISOU 1911  CB  ILE A 225     5466   4849   6461    624    171   -602       C
ATOM   1912  CG1 ILE A 225     -22.719   1.489  22.835  1.00 41.32           C
ANISOU 1912  CG1 ILE A 225     5102   4574   6025    517    138   -672       C
ATOM   1913  CG2 ILE A 225     -20.921   0.345  24.163  1.00 42.98           C
ANISOU 1913  CG2 ILE A 225     5227   4758   6346    733    147   -567       C
ATOM   1914  CD1 ILE A 225     -22.730   2.750  23.653  1.00 43.48           C
ANISOU 1914  CD1 ILE A 225     5327   4958   6236    514     43   -636       C
ATOM   1915  N   LEU A 226     -22.669  -2.921  24.260  1.00 39.62           N
ANISOU 1915  N   LEU A 226     4989   3968   6098    755    326   -496       N
ATOM   1916  CA  LEU A 226     -22.175  -4.174  24.822  1.00 41.85           C
ANISOU 1916  CA  LEU A 226     5273   4135   6493    872    386   -412       C
ATOM   1917  C   LEU A 226     -21.956  -5.206  23.725  1.00 51.47           C
ANISOU 1917  C   LEU A 226     6530   5201   7825    860    493   -510       C
ATOM   1918  O   LEU A 226     -20.966  -5.949  23.747  1.00 59.18           O
ANISOU 1918  O   LEU A 226     7478   6111   8897    970    548   -489       O
ATOM   1919  CB  LEU A 226     -23.141  -4.707  25.879  1.00 39.92           C
ANISOU 1919  CB  LEU A 226     5071   3836   6261    887    385   -285       C
ATOM   1920  CG  LEU A 226     -23.176  -3.931  27.198  1.00 48.53           C
ANISOU 1920  CG  LEU A 226     6118   5076   7244    944    291   -170       C
ATOM   1921  CD1 LEU A 226     -23.968  -4.687  28.257  1.00 54.18           C
ANISOU 1921  CD1 LEU A 226     6872   5732   7983    989    316    -22       C
ATOM   1922  CD2 LEU A 226     -21.767  -3.636  27.684  1.00 50.33           C
ANISOU 1922  CD2 LEU A 226     6259   5407   7458   1067    244   -135       C
ATOM   1923  N   ALA A 227     -22.854  -5.245  22.736  1.00 52.16           N
ANISOU 1923  N   ALA A 227     6678   5240   7900    732    522   -626       N
ATOM   1924  CA  ALA A 227     -22.648  -6.135  21.600  1.00 52.90           C
ANISOU 1924  CA  ALA A 227     6809   5208   8084    712    618   -753       C
ATOM   1925  C   ALA A 227     -21.345  -5.819  20.880  1.00 53.55           C
ANISOU 1925  C   ALA A 227     6834   5357   8154    767    641   -826       C
ATOM   1926  O   ALA A 227     -20.726  -6.716  20.296  1.00 57.78           O
ANISOU 1926  O   ALA A 227     7379   5787   8790    821    732   -893       O
ATOM   1927  CB  ALA A 227     -23.832  -6.046  20.637  1.00 48.41           C
ANISOU 1927  CB  ALA A 227     6301   4621   7470    559    624   -878       C
ATOM   1928  N   PHE A 228     -20.902  -4.558  20.925  1.00 52.56           N
ANISOU 1928  N   PHE A 228     6647   5404   7921    757    567   -813       N
ATOM   1929  CA  PHE A 228     -19.599  -4.211  20.366  1.00 50.47           C
ANISOU 1929  CA  PHE A 228     6309   5211   7655    813    590   -859       C
ATOM   1930  C   PHE A 228     -18.476  -4.921  21.113  1.00 48.14           C
ANISOU 1930  C   PHE A 228     5955   4869   7466    970    618   -771       C
ATOM   1931  O   PHE A 228     -17.553  -5.465  20.495  1.00 44.19           O
ANISOU 1931  O   PHE A 228     5426   4325   7039   1037    697   -828       O
ATOM   1932  CB  PHE A 228     -19.379  -2.696  20.412  1.00 47.76           C
ANISOU 1932  CB  PHE A 228     5903   5046   7198    767    503   -845       C
ATOM   1933  CG  PHE A 228     -20.341  -1.905  19.567  1.00 49.06           C
ANISOU 1933  CG  PHE A 228     6113   5269   7258    627    482   -921       C
ATOM   1934  CD1 PHE A 228     -21.152  -2.530  18.634  1.00 48.96           C
ANISOU 1934  CD1 PHE A 228     6180   5181   7243    552    538  -1020       C
ATOM   1935  CD2 PHE A 228     -20.431  -0.530  19.709  1.00 47.38           C
ANISOU 1935  CD2 PHE A 228     5858   5190   6955    575    402   -894       C
ATOM   1936  CE1 PHE A 228     -22.038  -1.798  17.864  1.00 47.56           C
ANISOU 1936  CE1 PHE A 228     6035   5077   6960    432    510  -1081       C
ATOM   1937  CE2 PHE A 228     -21.315   0.206  18.939  1.00 46.33           C
ANISOU 1937  CE2 PHE A 228     5763   5112   6730    459    383   -947       C
ATOM   1938  CZ  PHE A 228     -22.119  -0.432  18.014  1.00 42.23           C
ANISOU 1938  CZ  PHE A 228     5317   4534   6195    391    435  -1035       C
ATOM   1939  N   MET A 229     -18.538  -4.926  22.447  1.00 47.86           N
ANISOU 1939  N   MET A 229     5897   4853   7435   1039    554   -630       N
ATOM   1940  CA  MET A 229     -17.459  -5.526  23.224  1.00 48.81           C
ANISOU 1940  CA  MET A 229     5948   4956   7640   1199    566   -529       C
ATOM   1941  C   MET A 229     -17.502  -7.042  23.140  1.00 56.48           C
ANISOU 1941  C   MET A 229     6975   5726   8759   1271    674   -513       C
ATOM   1942  O   MET A 229     -16.458  -7.688  22.984  1.00 64.24           O
ANISOU 1942  O   MET A 229     7911   6657   9842   1386    737   -509       O
ATOM   1943  CB  MET A 229     -17.538  -5.060  24.675  1.00 46.37           C
ANISOU 1943  CB  MET A 229     5599   4751   7270   1255    461   -385       C
ATOM   1944  CG  MET A 229     -17.522  -3.551  24.812  1.00 47.63           C
ANISOU 1944  CG  MET A 229     5704   5092   7299   1182    354   -413       C
ATOM   1945  SD  MET A 229     -17.885  -2.994  26.482  1.00 55.70           S
ANISOU 1945  SD  MET A 229     6700   6237   8228   1229    231   -278       S
ATOM   1946  CE  MET A 229     -16.715  -3.971  27.413  1.00 53.44           C
ANISOU 1946  CE  MET A 229     6337   5942   8024   1430    241   -144       C
ATOM   1947  N   PHE A 230     -18.703  -7.621  23.235  1.00 58.87           N
ANISOU 1947  N   PHE A 230     7372   5906   9091   1203    701   -504       N
ATOM   1948  CA  PHE A 230     -18.876  -9.064  23.101  1.00 55.61           C
ANISOU 1948  CA  PHE A 230     7018   5272   8840   1249    812   -501       C
ATOM   1949  C   PHE A 230     -18.136  -9.594  21.878  1.00 51.80           C
ANISOU 1949  C   PHE A 230     6535   4707   8438   1268    911   -653       C
ATOM   1950  O   PHE A 230     -17.223 -10.420  21.993  1.00 55.10           O
ANISOU 1950  O   PHE A 230     6920   5033   8981   1404    981   -616       O
ATOM   1951  CB  PHE A 230     -20.371  -9.389  23.023  1.00 52.79           C
ANISOU 1951  CB  PHE A 230     6756   4810   8492   1121    825   -525       C
ATOM   1952  CG  PHE A 230     -20.673 -10.841  22.780  1.00 51.98           C
ANISOU 1952  CG  PHE A 230     6718   4459   8573   1138    942   -547       C
ATOM   1953  CD1 PHE A 230     -20.699 -11.743  23.832  1.00 52.14           C
ANISOU 1953  CD1 PHE A 230     6744   4353   8714   1243    981   -373       C
ATOM   1954  CD2 PHE A 230     -20.946 -11.302  21.501  1.00 53.26           C
ANISOU 1954  CD2 PHE A 230     6935   4514   8788   1048   1016   -743       C
ATOM   1955  CE1 PHE A 230     -20.983 -13.080  23.613  1.00 49.79           C
ANISOU 1955  CE1 PHE A 230     6505   3803   8610   1255   1096   -390       C
ATOM   1956  CE2 PHE A 230     -21.230 -12.635  21.274  1.00 52.83           C
ANISOU 1956  CE2 PHE A 230     6939   4216   8918   1056   1124   -783       C
ATOM   1957  CZ  PHE A 230     -21.249 -13.525  22.333  1.00 52.66           C
ANISOU 1957  CZ  PHE A 230     6921   4046   9040   1157   1167   -604       C
ATOM   1958  N   PHE A 231     -18.498  -9.092  20.696  1.00 51.64           N
ANISOU 1958  N   PHE A 231     6547   4736   8340   1141    919   -822       N
ATOM   1959  CA  PHE A 231     -17.855  -9.549  19.469  1.00 53.72           C
ANISOU 1959  CA  PHE A 231     6814   4943   8653   1154   1017   -982       C
ATOM   1960  C   PHE A 231     -16.379  -9.177  19.431  1.00 56.07           C
ANISOU 1960  C   PHE A 231     7005   5351   8949   1272   1024   -957       C
ATOM   1961  O   PHE A 231     -15.583  -9.869  18.784  1.00 59.82           O
ANISOU 1961  O   PHE A 231     7465   5748   9516   1350   1124  -1036       O
ATOM   1962  CB  PHE A 231     -18.590  -8.985  18.252  1.00 52.38           C
ANISOU 1962  CB  PHE A 231     6695   4841   8367    995   1012  -1153       C
ATOM   1963  CG  PHE A 231     -19.844  -9.732  17.920  1.00 55.21           C
ANISOU 1963  CG  PHE A 231     7153   5051   8774    890   1044  -1237       C
ATOM   1964  CD1 PHE A 231     -21.043  -9.404  18.528  1.00 58.67           C
ANISOU 1964  CD1 PHE A 231     7625   5503   9163    796    969  -1165       C
ATOM   1965  CD2 PHE A 231     -19.820 -10.786  17.023  1.00 59.91           C
ANISOU 1965  CD2 PHE A 231     7800   5490   9473    887   1152  -1394       C
ATOM   1966  CE1 PHE A 231     -22.200 -10.104  18.236  1.00 64.00           C
ANISOU 1966  CE1 PHE A 231     8378   6043   9897    693    999  -1242       C
ATOM   1967  CE2 PHE A 231     -20.969 -11.488  16.726  1.00 65.52           C
ANISOU 1967  CE2 PHE A 231     8592   6059  10242    781   1178  -1485       C
ATOM   1968  CZ  PHE A 231     -22.162 -11.148  17.334  1.00 66.32           C
ANISOU 1968  CZ  PHE A 231     8720   6179  10301    681   1099  -1405       C
ATOM   1969  N   ALA A 232     -15.987  -8.102  20.120  1.00 55.15           N
ANISOU 1969  N   ALA A 232     6807   5411   8736   1287    920   -855       N
ATOM   1970  CA  ALA A 232     -14.568  -7.773  20.188  1.00 50.75           C
ANISOU 1970  CA  ALA A 232     6130   4958   8194   1397    920   -823       C
ATOM   1971  C   ALA A 232     -13.794  -8.827  20.965  1.00 52.59           C
ANISOU 1971  C   ALA A 232     6322   5086   8575   1574    964   -710       C
ATOM   1972  O   ALA A 232     -12.621  -9.080  20.665  1.00 56.26           O
ANISOU 1972  O   ALA A 232     6705   5563   9108   1682   1021   -726       O
ATOM   1973  CB  ALA A 232     -14.367  -6.395  20.818  1.00 47.32           C
ANISOU 1973  CB  ALA A 232     5615   4727   7639   1365    792   -749       C
ATOM   1974  N   PHE A 233     -14.430  -9.464  21.946  1.00 51.81           N
ANISOU 1974  N   PHE A 233     6271   4885   8530   1612    947   -587       N
ATOM   1975  CA  PHE A 233     -13.722 -10.436  22.768  1.00 57.03           C
ANISOU 1975  CA  PHE A 233     6889   5454   9326   1791    985   -448       C
ATOM   1976  C   PHE A 233     -13.768 -11.834  22.159  1.00 64.13           C
ANISOU 1976  C   PHE A 233     7859   6105  10402   1840   1131   -514       C
ATOM   1977  O   PHE A 233     -12.726 -12.479  22.009  1.00 70.11           O
ANISOU 1977  O   PHE A 233     8563   6817  11260   1971   1198   -504       O
ATOM   1978  CB  PHE A 233     -14.298 -10.440  24.188  1.00 56.78           C
ANISOU 1978  CB  PHE A 233     6867   5445   9263   1827    901   -259       C
ATOM   1979  CG  PHE A 233     -13.682  -9.405  25.096  1.00 55.74           C
ANISOU 1979  CG  PHE A 233     6623   5544   9010   1876    769   -160       C
ATOM   1980  CD1 PHE A 233     -13.880  -8.052  24.866  1.00 48.10           C
ANISOU 1980  CD1 PHE A 233     5632   4751   7894   1751    676   -238       C
ATOM   1981  CD2 PHE A 233     -12.898  -9.787  26.177  1.00 55.45           C
ANISOU 1981  CD2 PHE A 233     6503   5550   9015   2050    737      9       C
ATOM   1982  CE1 PHE A 233     -13.314  -7.101  25.702  1.00 47.71           C
ANISOU 1982  CE1 PHE A 233     5478   4902   7747   1788    554   -168       C
ATOM   1983  CE2 PHE A 233     -12.327  -8.841  27.015  1.00 49.88           C
ANISOU 1983  CE2 PHE A 233     5689   5068   8194   2090    606     80       C
ATOM   1984  CZ  PHE A 233     -12.536  -7.499  26.778  1.00 51.28           C
ANISOU 1984  CZ  PHE A 233     5845   5406   8233   1955    515    -17       C
ATOM   1985  N   VAL A 234     -14.956 -12.312  21.784  1.00 62.33           N
ANISOU 1985  N   VAL A 234     7750   5730  10205   1725   1174   -588       N
ATOM   1986  CA  VAL A 234     -15.074 -13.638  21.195  1.00 64.18           C
ANISOU 1986  CA  VAL A 234     8060   5762  10562   1725   1279   -662       C
ATOM   1987  C   VAL A 234     -14.365 -13.747  19.855  1.00 61.44           C
ANISOU 1987  C   VAL A 234     7706   5438  10200   1710   1346   -851       C
ATOM   1988  O   VAL A 234     -14.177 -14.858  19.354  1.00 61.07           O
ANISOU 1988  O   VAL A 234     7705   5258  10239   1730   1424   -912       O
ATOM   1989  CB  VAL A 234     -16.555 -14.042  21.036  1.00 70.71           C
ANISOU 1989  CB  VAL A 234     9004   6455  11408   1575   1292   -716       C
ATOM   1990  CG1 VAL A 234     -17.258 -14.036  22.385  1.00 70.46           C
ANISOU 1990  CG1 VAL A 234     8981   6394  11397   1599   1242   -512       C
ATOM   1991  CG2 VAL A 234     -17.250 -13.120  20.050  1.00 73.94           C
ANISOU 1991  CG2 VAL A 234     9447   6949  11698   1414   1269   -902       C
ATOM   1992  N   LEU A 235     -13.965 -12.625  19.260  1.00 56.57           N
ANISOU 1992  N   LEU A 235     7030   4989   9476   1676   1323   -942       N
ATOM   1993  CA  LEU A 235     -13.169 -12.621  18.040  1.00 57.17           C
ANISOU 1993  CA  LEU A 235     7082   5121   9520   1679   1391  -1098       C
ATOM   1994  C   LEU A 235     -11.794 -12.015  18.290  1.00 60.35           C
ANISOU 1994  C   LEU A 235     7340   5674   9914   1804   1377  -1025       C
ATOM   1995  O   LEU A 235     -11.235 -11.320  17.437  1.00 61.81           O
ANISOU 1995  O   LEU A 235     7471   5987  10028   1780   1402  -1129       O
ATOM   1996  CB  LEU A 235     -13.888 -11.873  16.921  1.00 56.98           C
ANISOU 1996  CB  LEU A 235     7108   5172   9368   1518   1393  -1280       C
ATOM   1997  CG  LEU A 235     -15.209 -12.472  16.442  1.00 61.28           C
ANISOU 1997  CG  LEU A 235     7782   5593   9907   1380   1404  -1387       C
ATOM   1998  CD1 LEU A 235     -15.623 -11.834  15.125  1.00 58.90           C
ANISOU 1998  CD1 LEU A 235     7516   5401   9463   1248   1414  -1580       C
ATOM   1999  CD2 LEU A 235     -15.106 -13.987  16.308  1.00 61.23           C
ANISOU 1999  CD2 LEU A 235     7833   5401  10030   1428   1477  -1406       C
ATOM   2000  N   ALA A 236     -11.223 -12.284  19.467  1.00 59.91           N
ANISOU 2000  N   ALA A 236     7216   5618   9930   1940   1335   -840       N
ATOM   2001  CA  ALA A 236      -9.942 -11.698  19.843  1.00 60.85           C
ANISOU 2001  CA  ALA A 236     7181   5896  10044   2056   1300   -759       C
ATOM   2002  C   ALA A 236      -8.786 -12.169  18.967  1.00 68.89           C
ANISOU 2002  C   ALA A 236     8149   6927  11097   2131   1389   -842       C
ATOM   2003  O   ALA A 236      -7.709 -11.563  19.014  1.00 74.99           O
ANISOU 2003  O   ALA A 236     8785   7851  11858   2202   1370   -810       O
ATOM   2004  CB  ALA A 236      -9.642 -12.004  21.312  1.00 59.26           C
ANISOU 2004  CB  ALA A 236     6922   5699   9894   2189   1226   -542       C
ATOM   2005  N   GLY A 237      -8.971 -13.222  18.179  1.00 64.40           N
ANISOU 2005  N   GLY A 237     7678   6212  10577   2116   1482   -950       N
ATOM   2006  CA  GLY A 237      -7.933 -13.641  17.260  1.00 69.27           C
ANISOU 2006  CA  GLY A 237     8254   6847  11218   2185   1573  -1045       C
ATOM   2007  C   GLY A 237      -8.153 -13.080  15.873  1.00 72.15           C
ANISOU 2007  C   GLY A 237     8654   7285  11474   2066   1630  -1241       C
ATOM   2008  O   GLY A 237      -7.224 -13.005  15.063  1.00 78.67           O
ANISOU 2008  O   GLY A 237     9417   8193  12280   2112   1698  -1317       O
ATOM   2009  N   PHE A 238      -9.390 -12.674  15.595  1.00 70.25           N
ANISOU 2009  N   PHE A 238     8510   7026  11155   1914   1601  -1318       N
ATOM   2010  CA  PHE A 238      -9.798 -12.172  14.290  1.00 71.70           C
ANISOU 2010  CA  PHE A 238     8743   7284  11216   1790   1643  -1502       C
ATOM   2011  C   PHE A 238      -9.770 -10.650  14.215  1.00 74.26           C
ANISOU 2011  C   PHE A 238     8987   7799  11429   1721   1593  -1495       C
ATOM   2012  O   PHE A 238      -9.163 -10.086  13.301  1.00 76.36           O
ANISOU 2012  O   PHE A 238     9197   8197  11620   1710   1647  -1577       O
ATOM   2013  CB  PHE A 238     -11.205 -12.686  13.964  1.00 78.52           C
ANISOU 2013  CB  PHE A 238     9757   8021  12058   1658   1636  -1601       C
ATOM   2014  CG  PHE A 238     -11.490 -12.807  12.495  1.00 86.08           C
ANISOU 2014  CG  PHE A 238    10784   9010  12914   1569   1701  -1808       C
ATOM   2015  CD1 PHE A 238     -11.661 -11.678  11.710  1.00 87.63           C
ANISOU 2015  CD1 PHE A 238    10962   9380  12953   1476   1694  -1893       C
ATOM   2016  CD2 PHE A 238     -11.606 -14.052  11.901  1.00 90.83           C
ANISOU 2016  CD2 PHE A 238    11468   9470  13574   1579   1768  -1917       C
ATOM   2017  CE1 PHE A 238     -11.932 -11.790  10.361  1.00 90.03           C
ANISOU 2017  CE1 PHE A 238    11329   9735  13143   1401   1749  -2075       C
ATOM   2018  CE2 PHE A 238     -11.875 -14.170  10.552  1.00 93.91           C
ANISOU 2018  CE2 PHE A 238    11919   9905  13857   1503   1819  -2114       C
ATOM   2019  CZ  PHE A 238     -12.037 -13.037   9.780  1.00 93.99           C
ANISOU 2019  CZ  PHE A 238    11911  10107  13693   1416   1808  -2189       C
ATOM   2020  N   VAL A 239     -10.419  -9.977  15.162  1.00 73.70           N
ANISOU 2020  N   VAL A 239     8906   7745  11351   1677   1495  -1395       N
ATOM   2021  CA  VAL A 239     -10.566  -8.526  15.159  1.00 72.28           C
ANISOU 2021  CA  VAL A 239     8676   7765  11021   1570   1398  -1360       C
ATOM   2022  C   VAL A 239      -9.396  -7.902  15.904  1.00 76.51           C
ANISOU 2022  C   VAL A 239     9054   8431  11584   1663   1343  -1224       C
ATOM   2023  O   VAL A 239      -8.875  -8.468  16.870  1.00 77.12           O
ANISOU 2023  O   VAL A 239     9077   8449  11777   1794   1326  -1110       O
ATOM   2024  CB  VAL A 239     -11.916  -8.112  15.786  1.00 68.02           C
ANISOU 2024  CB  VAL A 239     8223   7216  10405   1445   1282  -1306       C
ATOM   2025  CG1 VAL A 239     -12.111  -6.604  15.714  1.00 64.00           C
ANISOU 2025  CG1 VAL A 239     7671   6904   9740   1330   1183  -1276       C
ATOM   2026  CG2 VAL A 239     -13.067  -8.836  15.100  1.00 66.92           C
ANISOU 2026  CG2 VAL A 239     8225   6940  10260   1355   1333  -1442       C
ATOM   2027  N   ASN A 240      -8.975  -6.722  15.442  1.00 88.87           N
ANISOU 2027  N   ASN A 240    10540  10178  13047   1595   1316  -1235       N
ATOM   2028  CA  ASN A 240      -7.905  -5.962  16.078  1.00 97.34           C
ANISOU 2028  CA  ASN A 240    11452  11392  14141   1653   1252  -1124       C
ATOM   2029  C   ASN A 240      -8.290  -5.591  17.505  1.00 96.52           C
ANISOU 2029  C   ASN A 240    11332  11309  14030   1650   1102   -985       C
ATOM   2030  O   ASN A 240      -8.125  -6.398  18.425  1.00106.33           O
ANISOU 2030  O   ASN A 240    12567  12467  15368   1768   1084   -895       O
ATOM   2031  CB  ASN A 240      -7.595  -4.706  15.260  1.00107.05           C
ANISOU 2031  CB  ASN A 240    12616  12794  15265   1549   1254  -1165       C
ATOM   2032  CG  ASN A 240      -6.284  -4.058  15.656  1.00116.32           C
ANISOU 2032  CG  ASN A 240    13603  14100  16493   1612   1226  -1084       C
ATOM   2033  OD1 ASN A 240      -5.415  -4.695  16.252  1.00119.20           O
ANISOU 2033  OD1 ASN A 240    13878  14438  16975   1756   1237  -1024       O
ATOM   2034  ND2 ASN A 240      -6.132  -2.781  15.322  1.00119.49           N
ANISOU 2034  ND2 ASN A 240    13938  14644  16818   1506   1189  -1077       N
ATOM   2035  N   ALA A 241      -8.778  -4.364  17.692  1.00 78.15           N
ANISOU 2035  N   ALA A 241     9001   9101  11592   1524    998   -963       N
ATOM   2036  CA  ALA A 241      -9.430  -3.926  18.924  1.00 66.44           C
ANISOU 2036  CA  ALA A 241     7535   7642  10069   1493    857   -862       C
ATOM   2037  C   ALA A 241      -8.522  -3.934  20.150  1.00 56.17           C
ANISOU 2037  C   ALA A 241     6105   6405   8833   1617    777   -740       C
ATOM   2038  O   ALA A 241      -8.078  -4.990  20.606  1.00 53.78           O
ANISOU 2038  O   ALA A 241     5785   6019   8631   1760    815   -682       O
ATOM   2039  CB  ALA A 241     -10.670  -4.784  19.198  1.00 56.80           C
ANISOU 2039  CB  ALA A 241     6466   6268   8848   1474    863   -860       C
ATOM   2040  N   ASP A 242      -8.253  -2.752  20.695  1.00 50.60           N
ANISOU 2040  N   ASP A 242     5305   5847   8072   1566    663   -700       N
ATOM   2041  CA  ASP A 242      -7.631  -2.616  22.011  1.00 49.71           C
ANISOU 2041  CA  ASP A 242     5080   5821   7986   1661    550   -592       C
ATOM   2042  C   ASP A 242      -8.724  -2.874  23.042  1.00 55.91           C
ANISOU 2042  C   ASP A 242     5971   6558   8715   1659    469   -519       C
ATOM   2043  O   ASP A 242      -9.498  -1.977  23.388  1.00 55.63           O
ANISOU 2043  O   ASP A 242     5975   6581   8581   1551    379   -524       O
ATOM   2044  CB  ASP A 242      -7.006  -1.233  22.163  1.00 48.69           C
ANISOU 2044  CB  ASP A 242     4815   5861   7823   1590    459   -604       C
ATOM   2045  CG  ASP A 242      -6.374  -1.008  23.529  1.00 53.42           C
ANISOU 2045  CG  ASP A 242     5289   6574   8433   1677    325   -515       C
ATOM   2046  OD1 ASP A 242      -6.418  -1.917  24.384  1.00 57.63           O
ANISOU 2046  OD1 ASP A 242     5842   7068   8988   1804    302   -426       O
ATOM   2047  OD2 ASP A 242      -5.827   0.096  23.748  1.00 51.91           O
ANISOU 2047  OD2 ASP A 242     4977   6516   8231   1619    241   -534       O
ATOM   2048  N   ARG A 243      -8.786  -4.111  23.540  1.00 57.08           N
ANISOU 2048  N   ARG A 243     6162   6595   8931   1785    509   -443       N
ATOM   2049  CA  ARG A 243      -9.954  -4.543  24.301  1.00 58.88           C
ANISOU 2049  CA  ARG A 243     6511   6744   9118   1776    472   -373       C
ATOM   2050  C   ARG A 243     -10.022  -3.880  25.673  1.00 61.03           C
ANISOU 2050  C   ARG A 243     6727   7157   9305   1799    321   -275       C
ATOM   2051  O   ARG A 243     -11.112  -3.532  26.142  1.00 58.27           O
ANISOU 2051  O   ARG A 243     6465   6809   8865   1721    264   -258       O
ATOM   2052  CB  ARG A 243      -9.959  -6.067  24.445  1.00 55.16           C
ANISOU 2052  CB  ARG A 243     6095   6100   8764   1908    569   -306       C
ATOM   2053  CG  ARG A 243     -10.476  -6.804  23.220  1.00 50.55           C
ANISOU 2053  CG  ARG A 243     5627   5340   8242   1851    709   -421       C
ATOM   2054  CD  ARG A 243     -10.459  -8.303  23.445  1.00 54.05           C
ANISOU 2054  CD  ARG A 243     6119   5591   8825   1982    805   -355       C
ATOM   2055  NE  ARG A 243      -9.149  -8.763  23.893  1.00 60.98           N
ANISOU 2055  NE  ARG A 243     6869   6502   9799   2164    818   -266       N
ATOM   2056  CZ  ARG A 243      -8.152  -9.091  23.078  1.00 58.12           C
ANISOU 2056  CZ  ARG A 243     6438   6119   9527   2233    913   -339       C
ATOM   2057  NH1 ARG A 243      -8.311  -9.015  21.765  1.00 56.48           N
ANISOU 2057  NH1 ARG A 243     6284   5862   9314   2136   1006   -505       N
ATOM   2058  NH2 ARG A 243      -6.993  -9.493  23.578  1.00 63.18           N
ANISOU 2058  NH2 ARG A 243     6951   6799  10256   2406    915   -243       N
ATOM   2059  N   LYS A 244      -8.881  -3.695  26.338  1.00 58.07           N
ANISOU 2059  N   LYS A 244     6202   6910   8952   1906    253   -216       N
ATOM   2060  CA  LYS A 244      -8.959  -3.176  27.701  1.00 59.88           C
ANISOU 2060  CA  LYS A 244     6382   7282   9089   1941    107   -131       C
ATOM   2061  C   LYS A 244      -9.271  -1.679  27.719  1.00 64.41           C
ANISOU 2061  C   LYS A 244     6933   7981   9559   1790      6   -219       C
ATOM   2062  O   LYS A 244     -10.045  -1.217  28.567  1.00 62.19           O
ANISOU 2062  O   LYS A 244     6697   7758   9174   1755    -86   -190       O
ATOM   2063  CB  LYS A 244      -7.676  -3.509  28.466  1.00 60.24           C
ANISOU 2063  CB  LYS A 244     6268   7436   9184   2111     54    -40       C
ATOM   2064  CG  LYS A 244      -6.463  -2.671  28.132  1.00 73.83           C
ANISOU 2064  CG  LYS A 244     7818   9296  10937   2094     12   -114       C
ATOM   2065  CD  LYS A 244      -5.383  -2.798  29.212  1.00 85.91           C
ANISOU 2065  CD  LYS A 244     9182  10984  12477   2250    -92    -17       C
ATOM   2066  CE  LYS A 244      -5.434  -4.152  29.920  1.00 93.87           C
ANISOU 2066  CE  LYS A 244    10228  11917  13520   2434    -57    142       C
ATOM   2067  NZ  LYS A 244      -4.177  -4.478  30.665  1.00 97.97           N
ANISOU 2067  NZ  LYS A 244    10569  12574  14080   2613   -123    241       N
ATOM   2068  N   ASN A 245      -8.728  -0.908  26.772  1.00 61.93           N
ANISOU 2068  N   ASN A 245     6553   7702   9276   1699     31   -326       N
ATOM   2069  CA  ASN A 245      -9.115   0.497  26.675  1.00 57.13           C
ANISOU 2069  CA  ASN A 245     5937   7177   8591   1548    -45   -406       C
ATOM   2070  C   ASN A 245     -10.572   0.634  26.247  1.00 52.69           C
ANISOU 2070  C   ASN A 245     5543   6517   7959   1429    -10   -441       C
ATOM   2071  O   ASN A 245     -11.275   1.549  26.696  1.00 44.71           O
ANISOU 2071  O   ASN A 245     4562   5563   6863   1343    -95   -461       O
ATOM   2072  CB  ASN A 245      -8.192   1.240  25.708  1.00 53.10           C
ANISOU 2072  CB  ASN A 245     5317   6715   8145   1481     -8   -491       C
ATOM   2073  CG  ASN A 245      -6.925   1.730  26.381  1.00 56.08           C
ANISOU 2073  CG  ASN A 245     5501   7244   8563   1541   -103   -480       C
ATOM   2074  OD1 ASN A 245      -6.937   2.075  27.563  1.00 58.48           O
ANISOU 2074  OD1 ASN A 245     5760   7652   8808   1574   -235   -448       O
ATOM   2075  ND2 ASN A 245      -5.822   1.757  25.636  1.00 54.35           N
ANISOU 2075  ND2 ASN A 245     5161   7048   8442   1557    -38   -510       N
ATOM   2076  N   LEU A 246     -11.043  -0.271  25.387  1.00 48.05           N
ANISOU 2076  N   LEU A 246     5061   5784   7411   1425    113   -455       N
ATOM   2077  CA  LEU A 246     -12.456  -0.297  25.029  1.00 41.66           C
ANISOU 2077  CA  LEU A 246     4404   4884   6541   1322    143   -482       C
ATOM   2078  C   LEU A 246     -13.324  -0.535  26.260  1.00 45.26           C
ANISOU 2078  C   LEU A 246     4922   5341   6933   1357     71   -392       C
ATOM   2079  O   LEU A 246     -14.327   0.159  26.476  1.00 51.78           O
ANISOU 2079  O   LEU A 246     5811   6191   7672   1261     19   -408       O
ATOM   2080  CB  LEU A 246     -12.690  -1.378  23.974  1.00 43.17           C
ANISOU 2080  CB  LEU A 246     4682   4921   6798   1327    283   -522       C
ATOM   2081  CG  LEU A 246     -14.127  -1.723  23.580  1.00 43.88           C
ANISOU 2081  CG  LEU A 246     4925   4900   6848   1235    324   -551       C
ATOM   2082  CD1 LEU A 246     -14.842  -0.526  22.963  1.00 36.46           C
ANISOU 2082  CD1 LEU A 246     4018   4021   5815   1081    290   -626       C
ATOM   2083  CD2 LEU A 246     -14.130  -2.906  22.626  1.00 45.52           C
ANISOU 2083  CD2 LEU A 246     5197   4957   7140   1260    458   -605       C
ATOM   2084  N   SER A 247     -12.935  -1.501  27.093  1.00 46.38           N
ANISOU 2084  N   SER A 247     5041   5465   7115   1501     70   -285       N
ATOM   2085  CA  SER A 247     -13.694  -1.797  28.304  1.00 50.65           C
ANISOU 2085  CA  SER A 247     5635   6020   7591   1551     13   -178       C
ATOM   2086  C   SER A 247     -13.700  -0.613  29.261  1.00 45.43           C
ANISOU 2086  C   SER A 247     4911   5536   6815   1528   -129   -179       C
ATOM   2087  O   SER A 247     -14.737  -0.290  29.850  1.00 49.97           O
ANISOU 2087  O   SER A 247     5557   6131   7298   1482   -173   -157       O
ATOM   2088  CB  SER A 247     -13.119  -3.034  28.994  1.00 60.34           C
ANISOU 2088  CB  SER A 247     6832   7204   8888   1727     44    -45       C
ATOM   2089  OG  SER A 247     -13.069  -4.139  28.110  1.00 66.12           O
ANISOU 2089  OG  SER A 247     7622   7757   9746   1753    181    -58       O
ATOM   2090  N   LEU A 248     -12.551   0.047  29.432  1.00 45.46           N
ANISOU 2090  N   LEU A 248     4775   5669   6828   1557   -200   -214       N
ATOM   2091  CA  LEU A 248     -12.487   1.195  30.336  1.00 46.69           C
ANISOU 2091  CA  LEU A 248     4862   5992   6885   1531   -340   -241       C
ATOM   2092  C   LEU A 248     -13.325   2.364  29.821  1.00 45.01           C
ANISOU 2092  C   LEU A 248     4706   5772   6622   1364   -357   -347       C
ATOM   2093  O   LEU A 248     -14.031   3.025  30.601  1.00 47.18           O
ANISOU 2093  O   LEU A 248     5011   6118   6799   1331   -439   -353       O
ATOM   2094  CB  LEU A 248     -11.034   1.620  30.534  1.00 49.42           C
ANISOU 2094  CB  LEU A 248     5034   6468   7275   1586   -409   -270       C
ATOM   2095  CG  LEU A 248     -10.194   0.597  31.298  1.00 60.67           C
ANISOU 2095  CG  LEU A 248     6381   7941   8728   1771   -424   -150       C
ATOM   2096  CD1 LEU A 248      -8.737   1.035  31.415  1.00 59.01           C
ANISOU 2096  CD1 LEU A 248     5983   7869   8570   1819   -494   -187       C
ATOM   2097  CD2 LEU A 248     -10.802   0.341  32.669  1.00 63.05           C
ANISOU 2097  CD2 LEU A 248     6725   8324   8908   1857   -503    -45       C
ATOM   2098  N   VAL A 249     -13.239   2.653  28.519  1.00 42.88           N
ANISOU 2098  N   VAL A 249     4448   5427   6418   1265   -279   -427       N
ATOM   2099  CA  VAL A 249     -14.095   3.677  27.927  1.00 46.49           C
ANISOU 2099  CA  VAL A 249     4967   5865   6834   1115   -281   -507       C
ATOM   2100  C   VAL A 249     -15.555   3.356  28.199  1.00 43.36           C
ANISOU 2100  C   VAL A 249     4709   5402   6363   1085   -266   -469       C
ATOM   2101  O   VAL A 249     -16.337   4.236  28.577  1.00 45.68           O
ANISOU 2101  O   VAL A 249     5034   5738   6582   1016   -327   -496       O
ATOM   2102  CB  VAL A 249     -13.819   3.807  26.416  1.00 48.80           C
ANISOU 2102  CB  VAL A 249     5261   6086   7196   1033   -179   -574       C
ATOM   2103  CG1 VAL A 249     -15.019   4.439  25.703  1.00 44.00           C
ANISOU 2103  CG1 VAL A 249     4757   5425   6536    899   -153   -622       C
ATOM   2104  CG2 VAL A 249     -12.551   4.612  26.172  1.00 43.98           C
ANISOU 2104  CG2 VAL A 249     4502   5561   6648   1019   -208   -623       C
ATOM   2105  N   ALA A 250     -15.940   2.089  28.022  1.00 40.35           N
ANISOU 2105  N   ALA A 250     4408   4911   6014   1138   -181   -407       N
ATOM   2106  CA  ALA A 250     -17.318   1.691  28.282  1.00 38.50           C
ANISOU 2106  CA  ALA A 250     4293   4607   5726   1107   -159   -363       C
ATOM   2107  C   ALA A 250     -17.701   1.919  29.741  1.00 39.74           C
ANISOU 2107  C   ALA A 250     4445   4865   5789   1167   -252   -290       C
ATOM   2108  O   ALA A 250     -18.799   2.414  30.031  1.00 36.87           O
ANISOU 2108  O   ALA A 250     4145   4514   5350   1102   -278   -296       O
ATOM   2109  CB  ALA A 250     -17.517   0.227  27.895  1.00 40.07           C
ANISOU 2109  CB  ALA A 250     4562   4658   6004   1158    -49   -311       C
ATOM   2110  N   VAL A 251     -16.811   1.561  30.674  1.00 30.66           N
ANISOU 2110  N   VAL A 251     3214   3799   4635   1298   -303   -220       N
ATOM   2111  CA  VAL A 251     -17.116   1.740  32.094  1.00 34.97           C
ANISOU 2111  CA  VAL A 251     3751   4467   5069   1370   -392   -149       C
ATOM   2112  C   VAL A 251     -17.377   3.207  32.399  1.00 39.52           C
ANISOU 2112  C   VAL A 251     4298   5158   5559   1285   -492   -250       C
ATOM   2113  O   VAL A 251     -18.390   3.564  33.016  1.00 47.23           O
ANISOU 2113  O   VAL A 251     5335   6170   6441   1260   -522   -237       O
ATOM   2114  CB  VAL A 251     -15.981   1.193  32.977  1.00 38.29           C
ANISOU 2114  CB  VAL A 251     4071   4986   5490   1531   -442    -63       C
ATOM   2115  CG1 VAL A 251     -16.259   1.534  34.433  1.00 35.31           C
ANISOU 2115  CG1 VAL A 251     3676   4772   4968   1602   -547     -6       C
ATOM   2116  CG2 VAL A 251     -15.838  -0.297  32.813  1.00 33.63           C
ANISOU 2116  CG2 VAL A 251     3518   4268   4992   1631   -338     56       C
ATOM   2117  N   VAL A 252     -16.461   4.079  31.969  1.00 38.37           N
ANISOU 2117  N   VAL A 252     4057   5066   5456   1238   -538   -351       N
ATOM   2118  CA  VAL A 252     -16.611   5.507  32.246  1.00 36.39           C
ANISOU 2118  CA  VAL A 252     3769   4906   5151   1156   -629   -455       C
ATOM   2119  C   VAL A 252     -17.875   6.049  31.592  1.00 40.29           C
ANISOU 2119  C   VAL A 252     4368   5312   5629   1030   -583   -498       C
ATOM   2120  O   VAL A 252     -18.641   6.806  32.209  1.00 44.74           O
ANISOU 2120  O   VAL A 252     4961   5929   6110    998   -640   -529       O
ATOM   2121  CB  VAL A 252     -15.359   6.274  31.782  1.00 40.43           C
ANISOU 2121  CB  VAL A 252     4151   5464   5745   1118   -669   -548       C
ATOM   2122  CG1 VAL A 252     -15.555   7.780  31.940  1.00 31.92           C
ANISOU 2122  CG1 VAL A 252     3041   4443   4644   1016   -749   -664       C
ATOM   2123  CG2 VAL A 252     -14.133   5.800  32.553  1.00 38.64           C
ANISOU 2123  CG2 VAL A 252     3805   5352   5525   1248   -733   -507       C
ATOM   2124  N   THR A 253     -18.118   5.663  30.337  1.00 43.27           N
ANISOU 2124  N   THR A 253     4800   5562   6080    964   -481   -504       N
ATOM   2125  CA  THR A 253     -19.273   6.161  29.601  1.00 42.06           C
ANISOU 2125  CA  THR A 253     4734   5334   5911    847   -439   -542       C
ATOM   2126  C   THR A 253     -20.571   5.786  30.298  1.00 41.35           C
ANISOU 2126  C   THR A 253     4737   5234   5739    862   -436   -478       C
ATOM   2127  O   THR A 253     -21.448   6.634  30.508  1.00 39.71           O
ANISOU 2127  O   THR A 253     4563   5053   5474    801   -470   -512       O
ATOM   2128  CB  THR A 253     -19.255   5.604  28.177  1.00 42.14           C
ANISOU 2128  CB  THR A 253     4784   5230   5998    792   -331   -555       C
ATOM   2129  OG1 THR A 253     -18.119   6.119  27.474  1.00 49.50           O
ANISOU 2129  OG1 THR A 253     5626   6182   7000    768   -326   -613       O
ATOM   2130  CG2 THR A 253     -20.515   5.998  27.441  1.00 44.73           C
ANISOU 2130  CG2 THR A 253     5201   5497   6297    682   -294   -582       C
ATOM   2131  N   PHE A 254     -20.710   4.514  30.671  1.00 41.28           N
ANISOU 2131  N   PHE A 254     4768   5183   5735    945   -389   -379       N
ATOM   2132  CA  PHE A 254     -21.954   4.076  31.289  1.00 39.77           C
ANISOU 2132  CA  PHE A 254     4660   4973   5479    955   -369   -304       C
ATOM   2133  C   PHE A 254     -22.119   4.660  32.685  1.00 39.32           C
ANISOU 2133  C   PHE A 254     4575   5059   5306   1017   -461   -282       C
ATOM   2134  O   PHE A 254     -23.246   4.962  33.094  1.00 42.63           O
ANISOU 2134  O   PHE A 254     5049   5494   5654    987   -464   -268       O
ATOM   2135  CB  PHE A 254     -22.014   2.550  31.318  1.00 43.24           C
ANISOU 2135  CB  PHE A 254     5142   5312   5973   1026   -285   -196       C
ATOM   2136  CG  PHE A 254     -22.307   1.930  29.976  1.00 43.05           C
ANISOU 2136  CG  PHE A 254     5174   5136   6046    946   -186   -232       C
ATOM   2137  CD1 PHE A 254     -23.335   2.416  29.183  1.00 41.57           C
ANISOU 2137  CD1 PHE A 254     5043   4905   5845    821   -163   -296       C
ATOM   2138  CD2 PHE A 254     -21.552   0.867  29.505  1.00 48.57           C
ANISOU 2138  CD2 PHE A 254     5866   5744   6845   1003   -116   -209       C
ATOM   2139  CE1 PHE A 254     -23.610   1.850  27.947  1.00 44.47           C
ANISOU 2139  CE1 PHE A 254     5459   5154   6284    749    -81   -343       C
ATOM   2140  CE2 PHE A 254     -21.819   0.297  28.268  1.00 49.93           C
ANISOU 2140  CE2 PHE A 254     6091   5784   7097    931    -26   -265       C
ATOM   2141  CZ  PHE A 254     -22.852   0.791  27.488  1.00 48.10           C
ANISOU 2141  CZ  PHE A 254     5915   5523   6837    802    -12   -336       C
ATOM   2142  N   ALA A 255     -21.022   4.854  33.422  1.00 38.86           N
ANISOU 2142  N   ALA A 255     4427   5116   5222   1105   -539   -287       N
ATOM   2143  CA  ALA A 255     -21.139   5.496  34.728  1.00 41.33           C
ANISOU 2143  CA  ALA A 255     4709   5586   5409   1162   -636   -293       C
ATOM   2144  C   ALA A 255     -21.674   6.915  34.584  1.00 42.87           C
ANISOU 2144  C   ALA A 255     4907   5809   5574   1058   -685   -419       C
ATOM   2145  O   ALA A 255     -22.629   7.310  35.271  1.00 35.52           O
ANISOU 2145  O   ALA A 255     4019   4929   4546   1058   -705   -417       O
ATOM   2146  CB  ALA A 255     -19.786   5.493  35.442  1.00 37.00           C
ANISOU 2146  CB  ALA A 255     4049   5167   4842   1267   -723   -296       C
ATOM   2147  N   VAL A 256     -21.073   7.695  33.681  1.00 42.25           N
ANISOU 2147  N   VAL A 256     4780   5690   5582    971   -696   -523       N
ATOM   2148  CA  VAL A 256     -21.534   9.064  33.476  1.00 39.60           C
ANISOU 2148  CA  VAL A 256     4444   5360   5243    873   -734   -634       C
ATOM   2149  C   VAL A 256     -22.982   9.073  33.005  1.00 41.16           C
ANISOU 2149  C   VAL A 256     4744   5472   5423    804   -665   -606       C
ATOM   2150  O   VAL A 256     -23.776   9.931  33.410  1.00 46.80           O
ANISOU 2150  O   VAL A 256     5480   6220   6081    775   -697   -652       O
ATOM   2151  CB  VAL A 256     -20.608   9.798  32.491  1.00 33.04           C
ANISOU 2151  CB  VAL A 256     3541   4486   4526    792   -738   -723       C
ATOM   2152  CG1 VAL A 256     -21.206  11.142  32.102  1.00 30.47           C
ANISOU 2152  CG1 VAL A 256     3228   4128   4221    686   -752   -814       C
ATOM   2153  CG2 VAL A 256     -19.239   9.987  33.115  1.00 37.35           C
ANISOU 2153  CG2 VAL A 256     3966   5139   5087    853   -824   -768       C
ATOM   2154  N   SER A 257     -23.355   8.112  32.155  1.00 37.71           N
ANISOU 2154  N   SER A 257     4367   4927   5037    780   -572   -538       N
ATOM   2155  CA  SER A 257     -24.725   8.081  31.656  1.00 41.17           C
ANISOU 2155  CA  SER A 257     4889   5291   5463    709   -513   -516       C
ATOM   2156  C   SER A 257     -25.712   7.787  32.779  1.00 43.15           C
ANISOU 2156  C   SER A 257     5184   5597   5614    766   -519   -446       C
ATOM   2157  O   SER A 257     -26.772   8.418  32.865  1.00 44.19           O
ANISOU 2157  O   SER A 257     5350   5736   5705    720   -519   -465       O
ATOM   2158  CB  SER A 257     -24.852   7.047  30.539  1.00 39.03           C
ANISOU 2158  CB  SER A 257     4664   4900   5267    671   -419   -475       C
ATOM   2159  OG  SER A 257     -24.966   5.744  31.077  1.00 41.67           O
ANISOU 2159  OG  SER A 257     5029   5207   5595    749   -377   -373       O
ATOM   2160  N   ALA A 258     -25.378   6.833  33.650  1.00 42.31           N
ANISOU 2160  N   ALA A 258     5072   5534   5469    873   -517   -354       N
ATOM   2161  CA  ALA A 258     -26.241   6.540  34.788  1.00 39.56           C
ANISOU 2161  CA  ALA A 258     4759   5256   5017    938   -516   -271       C
ATOM   2162  C   ALA A 258     -26.370   7.751  35.701  1.00 40.16           C
ANISOU 2162  C   ALA A 258     4804   5469   4988    959   -603   -351       C
ATOM   2163  O   ALA A 258     -27.450   8.019  36.242  1.00 36.67           O
ANISOU 2163  O   ALA A 258     4400   5065   4469    961   -592   -333       O
ATOM   2164  CB  ALA A 258     -25.704   5.337  35.560  1.00 37.37           C
ANISOU 2164  CB  ALA A 258     4472   5010   4718   1062   -499   -144       C
ATOM   2165  N   LEU A 259     -25.278   8.496  35.885  1.00 43.84           N
ANISOU 2165  N   LEU A 259     5194   6006   5455    975   -689   -449       N
ATOM   2166  CA  LEU A 259     -25.355   9.705  36.701  1.00 43.46           C
ANISOU 2166  CA  LEU A 259     5113   6075   5323    985   -775   -556       C
ATOM   2167  C   LEU A 259     -26.266  10.744  36.056  1.00 40.09           C
ANISOU 2167  C   LEU A 259     4721   5577   4936    877   -757   -638       C
ATOM   2168  O   LEU A 259     -27.044  11.418  36.743  1.00 36.16           O
ANISOU 2168  O   LEU A 259     4241   5143   4357    890   -779   -678       O
ATOM   2169  CB  LEU A 259     -23.956  10.275  36.926  1.00 51.95           C
ANISOU 2169  CB  LEU A 259     6090   7227   6420   1006   -871   -657       C
ATOM   2170  CG  LEU A 259     -23.865  11.531  37.792  1.00 62.00           C
ANISOU 2170  CG  LEU A 259     7318   8620   7620   1014   -973   -797       C
ATOM   2171  CD1 LEU A 259     -24.592  11.329  39.113  1.00 62.06           C
ANISOU 2171  CD1 LEU A 259     7359   8766   7456   1115   -991   -752       C
ATOM   2172  CD2 LEU A 259     -22.407  11.902  38.027  1.00 64.81           C
ANISOU 2172  CD2 LEU A 259     7561   9054   8008   1034  -1069   -889       C
ATOM   2173  N   ILE A 260     -26.194  10.877  34.731  1.00 40.25           N
ANISOU 2173  N   ILE A 260     4748   5470   5075    778   -712   -658       N
ATOM   2174  CA  ILE A 260     -27.078  11.802  34.025  1.00 38.87           C
ANISOU 2174  CA  ILE A 260     4604   5225   4940    683   -688   -711       C
ATOM   2175  C   ILE A 260     -28.534  11.394  34.203  1.00 47.31           C
ANISOU 2175  C   ILE A 260     5743   6281   5950    684   -629   -632       C
ATOM   2176  O   ILE A 260     -29.417  12.240  34.403  1.00 47.60           O
ANISOU 2176  O   ILE A 260     5796   6333   5957    662   -636   -673       O
ATOM   2177  CB  ILE A 260     -26.695  11.872  32.536  1.00 36.22           C
ANISOU 2177  CB  ILE A 260     4263   4774   4726    589   -644   -725       C
ATOM   2178  CG1 ILE A 260     -25.323  12.523  32.373  1.00 34.59           C
ANISOU 2178  CG1 ILE A 260     3972   4582   4588    577   -700   -810       C
ATOM   2179  CG2 ILE A 260     -27.740  12.653  31.760  1.00 36.39           C
ANISOU 2179  CG2 ILE A 260     4321   4729   4777    502   -611   -745       C
ATOM   2180  CD1 ILE A 260     -25.296  13.962  32.824  1.00 30.99           C
ANISOU 2180  CD1 ILE A 260     3476   4160   4139    552   -768   -925       C
ATOM   2181  N   TYR A 261     -28.810  10.091  34.135  1.00 45.66           N
ANISOU 2181  N   TYR A 261     5573   6039   5737    709   -567   -518       N
ATOM   2182  CA  TYR A 261     -30.190   9.623  34.194  1.00 38.44           C
ANISOU 2182  CA  TYR A 261     4716   5100   4791    694   -502   -438       C
ATOM   2183  C   TYR A 261     -30.756   9.638  35.609  1.00 39.85           C
ANISOU 2183  C   TYR A 261     4899   5397   4845    784   -517   -396       C
ATOM   2184  O   TYR A 261     -31.973   9.771  35.777  1.00 47.43           O
ANISOU 2184  O   TYR A 261     5889   6362   5770    767   -479   -365       O
ATOM   2185  CB  TYR A 261     -30.293   8.214  33.618  1.00 23.28           C
ANISOU 2185  CB  TYR A 261     2830   3086   2930    680   -425   -338       C
ATOM   2186  CG  TYR A 261     -31.707   7.658  33.602  1.00 41.35           C
ANISOU 2186  CG  TYR A 261     5166   5337   5210    647   -355   -257       C
ATOM   2187  CD1 TYR A 261     -32.629   8.069  32.643  1.00 34.89           C
ANISOU 2187  CD1 TYR A 261     4365   4458   4433    546   -330   -291       C
ATOM   2188  CD2 TYR A 261     -32.117   6.719  34.543  1.00 33.00           C
ANISOU 2188  CD2 TYR A 261     4127   4309   4105    719   -314   -139       C
ATOM   2189  CE1 TYR A 261     -33.910   7.560  32.621  1.00 32.72           C
ANISOU 2189  CE1 TYR A 261     4118   4155   4159    511   -272   -223       C
ATOM   2190  CE2 TYR A 261     -33.399   6.204  34.527  1.00 38.67           C
ANISOU 2190  CE2 TYR A 261     4876   4987   4831    681   -245    -62       C
ATOM   2191  CZ  TYR A 261     -34.292   6.628  33.567  1.00 38.68           C
ANISOU 2191  CZ  TYR A 261     4887   4931   4880    574   -227   -111       C
ATOM   2192  OH  TYR A 261     -35.570   6.117  33.558  1.00 40.18           O
ANISOU 2192  OH  TYR A 261     5093   5090   5084    531   -164    -39       O
ATOM   2193  N   LEU A 262     -29.898   9.510  36.623  1.00 41.56           N
ANISOU 2193  N   LEU A 262     5082   5721   4986    884   -571   -394       N
ATOM   2194  CA  LEU A 262     -30.342   9.340  38.008  1.00 43.53           C
ANISOU 2194  CA  LEU A 262     5338   6106   5095    988   -579   -336       C
ATOM   2195  C   LEU A 262     -31.423  10.318  38.460  1.00 46.75           C
ANISOU 2195  C   LEU A 262     5760   6572   5432    978   -582   -395       C
ATOM   2196  O   LEU A 262     -32.438   9.860  39.010  1.00 43.67           O
ANISOU 2196  O   LEU A 262     5401   6218   4974   1013   -522   -298       O
ATOM   2197  CB  LEU A 262     -29.116   9.412  38.929  1.00 37.69           C
ANISOU 2197  CB  LEU A 262     4543   5499   4277   1089   -666   -369       C
ATOM   2198  CG  LEU A 262     -29.340   9.147  40.417  1.00 36.35           C
ANISOU 2198  CG  LEU A 262     4373   5503   3935   1218   -684   -302       C
ATOM   2199  CD1 LEU A 262     -29.859   7.740  40.629  1.00 37.19           C
ANISOU 2199  CD1 LEU A 262     4520   5577   4032   1268   -588   -101       C
ATOM   2200  CD2 LEU A 262     -28.055   9.365  41.207  1.00 38.47           C
ANISOU 2200  CD2 LEU A 262     4574   5918   4127   1309   -791   -363       C
ATOM   2201  N   PRO A 263     -31.297  11.639  38.273  1.00 51.67           N
ANISOU 2201  N   PRO A 263     6359   7200   6075    935   -641   -544       N
ATOM   2202  CA  PRO A 263     -32.321  12.549  38.813  1.00 49.80           C
ANISOU 2202  CA  PRO A 263     6134   7019   5770    945   -639   -602       C
ATOM   2203  C   PRO A 263     -33.685  12.434  38.147  1.00 47.99           C
ANISOU 2203  C   PRO A 263     5943   6703   5590    879   -554   -535       C
ATOM   2204  O   PRO A 263     -34.601  13.167  38.536  1.00 54.45           O
ANISOU 2204  O   PRO A 263     6766   7561   6362    890   -543   -574       O
ATOM   2205  CB  PRO A 263     -31.710  13.940  38.579  1.00 49.26           C
ANISOU 2205  CB  PRO A 263     6026   6934   5756    904   -717   -778       C
ATOM   2206  CG  PRO A 263     -30.784  13.757  37.445  1.00 50.10           C
ANISOU 2206  CG  PRO A 263     6112   6929   5995    828   -724   -784       C
ATOM   2207  CD  PRO A 263     -30.202  12.389  37.627  1.00 51.25           C
ANISOU 2207  CD  PRO A 263     6260   7098   6114    882   -706   -666       C
ATOM   2208  N   PHE A 264     -33.861  11.546  37.168  1.00 45.45           N
ANISOU 2208  N   PHE A 264     5642   6267   5359    811   -496   -444       N
ATOM   2209  CA  PHE A 264     -35.159  11.319  36.541  1.00 41.06           C
ANISOU 2209  CA  PHE A 264     5112   5641   4847    745   -422   -379       C
ATOM   2210  C   PHE A 264     -35.624   9.875  36.669  1.00 40.82           C
ANISOU 2210  C   PHE A 264     5106   5587   4816    755   -345   -228       C
ATOM   2211  O   PHE A 264     -36.596   9.488  36.011  1.00 45.96           O
ANISOU 2211  O   PHE A 264     5770   6166   5525    683   -285   -175       O
ATOM   2212  CB  PHE A 264     -35.117  11.714  35.062  1.00 39.03           C
ANISOU 2212  CB  PHE A 264     4854   5262   4713    632   -422   -429       C
ATOM   2213  CG  PHE A 264     -34.694  13.130  34.829  1.00 40.90           C
ANISOU 2213  CG  PHE A 264     5064   5495   4979    613   -483   -559       C
ATOM   2214  CD1 PHE A 264     -33.352  13.464  34.759  1.00 42.98           C
ANISOU 2214  CD1 PHE A 264     5299   5755   5274    618   -543   -636       C
ATOM   2215  CD2 PHE A 264     -35.637  14.132  34.686  1.00 37.78           C
ANISOU 2215  CD2 PHE A 264     4667   5095   4595    589   -477   -600       C
ATOM   2216  CE1 PHE A 264     -32.959  14.774  34.551  1.00 44.66           C
ANISOU 2216  CE1 PHE A 264     5483   5950   5537    591   -593   -753       C
ATOM   2217  CE2 PHE A 264     -35.253  15.441  34.476  1.00 36.00           C
ANISOU 2217  CE2 PHE A 264     4417   4844   4417    572   -525   -713       C
ATOM   2218  CZ  PHE A 264     -33.913  15.764  34.405  1.00 40.17           C
ANISOU 2218  CZ  PHE A 264     4919   5359   4986    568   -582   -790       C
ATOM   2219  N   ALA A 265     -34.968   9.073  37.505  1.00 42.33           N
ANISOU 2219  N   ALA A 265     5299   5838   4949    843   -346   -156       N
ATOM   2220  CA  ALA A 265     -35.198   7.635  37.525  1.00 41.94           C
ANISOU 2220  CA  ALA A 265     5272   5732   4933    851   -268     -6       C
ATOM   2221  C   ALA A 265     -36.399   7.213  38.366  1.00 42.01           C
ANISOU 2221  C   ALA A 265     5289   5800   4873    889   -195    112       C
ATOM   2222  O   ALA A 265     -36.811   6.055  38.287  1.00 43.80           O
ANISOU 2222  O   ALA A 265     5531   5955   5155    874   -117    241       O
ATOM   2223  CB  ALA A 265     -33.939   6.921  38.032  1.00 35.24           C
ANISOU 2223  CB  ALA A 265     4413   4914   4061    939   -294     42       C
ATOM   2224  N   PHE A 266     -36.981   8.096  39.161  1.00 41.38           N
ANISOU 2224  N   PHE A 266     5197   5842   4683    938   -211     73       N
ATOM   2225  CA  PHE A 266     -37.982   7.678  40.132  1.00 38.82           C
ANISOU 2225  CA  PHE A 266     4875   5604   4271    998   -137    195       C
ATOM   2226  C   PHE A 266     -39.325   8.345  39.872  1.00 37.77           C
ANISOU 2226  C   PHE A 266     4731   5469   4153    939   -100    165       C
ATOM   2227  O   PHE A 266     -40.035   8.736  40.800  1.00 39.34           O
ANISOU 2227  O   PHE A 266     4918   5788   4241   1007    -73    185       O
ATOM   2228  CB  PHE A 266     -37.485   7.949  41.549  1.00 39.68           C
ANISOU 2228  CB  PHE A 266     4975   5898   4204   1141   -176    199       C
ATOM   2229  CG  PHE A 266     -36.185   7.264  41.864  1.00 45.81           C
ANISOU 2229  CG  PHE A 266     5750   6696   4960   1212   -216    244       C
ATOM   2230  CD1 PHE A 266     -36.171   5.981  42.383  1.00 51.36           C
ANISOU 2230  CD1 PHE A 266     6464   7402   5650   1275   -146    433       C
ATOM   2231  CD2 PHE A 266     -34.974   7.894  41.617  1.00 50.04           C
ANISOU 2231  CD2 PHE A 266     6267   7243   5504   1215   -320    106       C
ATOM   2232  CE1 PHE A 266     -34.973   5.342  42.666  1.00 53.47           C
ANISOU 2232  CE1 PHE A 266     6724   7690   5904   1352   -182    485       C
ATOM   2233  CE2 PHE A 266     -33.775   7.262  41.895  1.00 51.30           C
ANISOU 2233  CE2 PHE A 266     6412   7430   5649   1284   -359    150       C
ATOM   2234  CZ  PHE A 266     -33.776   5.984  42.422  1.00 52.02           C
ANISOU 2234  CZ  PHE A 266     6515   7529   5719   1358   -292    341       C
ATOM   2235  N   ASN A 267     -39.699   8.458  38.597  1.00 31.99           N
ANISOU 2235  N   ASN A 267     3998   4607   3552    817    -96    121       N
ATOM   2236  CA  ASN A 267     -40.940   9.106  38.191  1.00 35.21           C
ANISOU 2236  CA  ASN A 267     4384   5006   3987    758    -70     93       C
ATOM   2237  C   ASN A 267     -42.006   8.114  37.733  1.00 40.89           C
ANISOU 2237  C   ASN A 267     5092   5649   4793    678     18    212       C
ATOM   2238  O   ASN A 267     -43.065   8.536  37.256  1.00 35.83           O
ANISOU 2238  O   ASN A 267     4423   4998   4192    617     38    197       O
ATOM   2239  CB  ASN A 267     -40.665  10.125  37.084  1.00 29.63           C
ANISOU 2239  CB  ASN A 267     3672   4231   3354    683   -137    -45       C
ATOM   2240  CG  ASN A 267     -39.915  11.344  37.585  1.00 42.30           C
ANISOU 2240  CG  ASN A 267     5273   5908   4890    749   -215   -175       C
ATOM   2241  OD1 ASN A 267     -38.921  11.762  36.993  1.00 49.90           O
ANISOU 2241  OD1 ASN A 267     6239   6818   5903    720   -278   -264       O
ATOM   2242  ND2 ASN A 267     -40.386  11.920  38.684  1.00 47.66           N
ANISOU 2242  ND2 ASN A 267     5943   6708   5459    837   -208   -194       N
ATOM   2243  N   TYR A 268     -41.754   6.809  37.858  1.00 40.02           N
ANISOU 2243  N   TYR A 268     4998   5482   4724    677     70    327       N
ATOM   2244  CA  TYR A 268     -42.738   5.793  37.505  1.00 39.44           C
ANISOU 2244  CA  TYR A 268     4910   5325   4750    597    157    437       C
ATOM   2245  C   TYR A 268     -42.689   4.731  38.601  1.00 42.15           C
ANISOU 2245  C   TYR A 268     5261   5699   5055    678    235    603       C
ATOM   2246  O   TYR A 268     -41.589   4.323  39.013  1.00 45.03           O
ANISOU 2246  O   TYR A 268     5654   6069   5385    754    213    630       O
ATOM   2247  CB  TYR A 268     -42.466   5.178  36.127  1.00 39.17           C
ANISOU 2247  CB  TYR A 268     4888   5132   4863    476    147    394       C
ATOM   2248  CG  TYR A 268     -43.499   4.166  35.680  1.00 44.34           C
ANISOU 2248  CG  TYR A 268     5521   5692   5636    376    228    477       C
ATOM   2249  CD1 TYR A 268     -44.741   4.571  35.201  1.00 48.19           C
ANISOU 2249  CD1 TYR A 268     5960   6194   6155    294    240    455       C
ATOM   2250  CD2 TYR A 268     -43.233   2.804  35.735  1.00 46.89           C
ANISOU 2250  CD2 TYR A 268     5863   5906   6048    362    292    575       C
ATOM   2251  CE1 TYR A 268     -45.690   3.645  34.792  1.00 44.19           C
ANISOU 2251  CE1 TYR A 268     5420   5605   5765    192    307    520       C
ATOM   2252  CE2 TYR A 268     -44.173   1.873  35.329  1.00 48.50           C
ANISOU 2252  CE2 TYR A 268     6040   6009   6380    259    367    638       C
ATOM   2253  CZ  TYR A 268     -45.398   2.298  34.857  1.00 47.13           C
ANISOU 2253  CZ  TYR A 268     5813   5861   6233    169    370    605       C
ATOM   2254  OH  TYR A 268     -46.333   1.370  34.451  1.00 52.72           O
ANISOU 2254  OH  TYR A 268     6484   6473   7076     57    438    657       O
ATOM   2255  N   PRO A 269     -43.838   4.272  39.096  1.00 44.03           N
ANISOU 2255  N   PRO A 269     5468   5961   5300    670    328    725       N
ATOM   2256  CA  PRO A 269     -43.835   3.402  40.282  1.00 46.74           C
ANISOU 2256  CA  PRO A 269     5816   6359   5584    767    411    904       C
ATOM   2257  C   PRO A 269     -43.559   1.932  39.993  1.00 46.66           C
ANISOU 2257  C   PRO A 269     5823   6191   5716    724    477   1025       C
ATOM   2258  O   PRO A 269     -44.072   1.058  40.699  1.00 54.94           O
ANISOU 2258  O   PRO A 269     6858   7236   6781    753    581   1202       O
ATOM   2259  CB  PRO A 269     -45.248   3.595  40.847  1.00 47.63           C
ANISOU 2259  CB  PRO A 269     5879   6559   5659    767    492    983       C
ATOM   2260  CG  PRO A 269     -46.083   3.882  39.647  1.00 42.93           C
ANISOU 2260  CG  PRO A 269     5249   5870   5191    622    479    893       C
ATOM   2261  CD  PRO A 269     -45.202   4.655  38.691  1.00 41.01           C
ANISOU 2261  CD  PRO A 269     5037   5583   4963    587    361    712       C
ATOM   2262  N   GLY A 270     -42.751   1.642  38.982  1.00 39.86           N
ANISOU 2262  N   GLY A 270     4990   5195   4961    660    427    937       N
ATOM   2263  CA  GLY A 270     -42.403   0.265  38.682  1.00 42.49           C
ANISOU 2263  CA  GLY A 270     5343   5363   5438    627    490   1033       C
ATOM   2264  C   GLY A 270     -41.359   0.222  37.590  1.00 42.89           C
ANISOU 2264  C   GLY A 270     5426   5303   5569    579    419    897       C
ATOM   2265  O   GLY A 270     -40.895   1.255  37.104  1.00 51.23           O
ANISOU 2265  O   GLY A 270     6486   6415   6566    572    323    745       O
ATOM   2266  N   PHE A 271     -40.982  -0.995  37.211  1.00 36.48           N
ANISOU 2266  N   PHE A 271     4635   4327   4900    549    473    957       N
ATOM   2267  CA  PHE A 271     -40.079  -1.161  36.081  1.00 39.42           C
ANISOU 2267  CA  PHE A 271     5034   4582   5362    496    424    828       C
ATOM   2268  C   PHE A 271     -40.812  -0.859  34.779  1.00 41.36           C
ANISOU 2268  C   PHE A 271     5266   4759   5690    339    401    687       C
ATOM   2269  O   PHE A 271     -41.954  -1.280  34.579  1.00 45.63           O
ANISOU 2269  O   PHE A 271     5779   5245   6313    245    460    723       O
ATOM   2270  CB  PHE A 271     -39.512  -2.581  36.051  1.00 41.88           C
ANISOU 2270  CB  PHE A 271     5371   4727   5813    515    498    927       C
ATOM   2271  CG  PHE A 271     -38.347  -2.789  36.976  1.00 44.84           C
ANISOU 2271  CG  PHE A 271     5763   5166   6110    677    486   1023       C
ATOM   2272  CD1 PHE A 271     -37.688  -1.707  37.535  1.00 42.64           C
ANISOU 2272  CD1 PHE A 271     5475   5071   5654    774    391    969       C
ATOM   2273  CD2 PHE A 271     -37.910  -4.066  37.286  1.00 49.49           C
ANISOU 2273  CD2 PHE A 271     6368   5628   6807    733    567   1167       C
ATOM   2274  CE1 PHE A 271     -36.621  -1.892  38.385  1.00 43.54           C
ANISOU 2274  CE1 PHE A 271     5592   5263   5689    922    368   1050       C
ATOM   2275  CE2 PHE A 271     -36.839  -4.259  38.135  1.00 54.36           C
ANISOU 2275  CE2 PHE A 271     6991   6318   7346    892    550   1266       C
ATOM   2276  CZ  PHE A 271     -36.194  -3.169  38.686  1.00 52.90           C
ANISOU 2276  CZ  PHE A 271     6791   6338   6971    986    446   1205       C
ATOM   2277  N   SER A 272     -40.155  -0.116  33.893  1.00 39.95           N
ANISOU 2277  N   SER A 272     5099   4594   5487    311    315    529       N
ATOM   2278  CA  SER A 272     -40.751   0.233  32.612  1.00 42.63           C
ANISOU 2278  CA  SER A 272     5425   4893   5881    175    284    397       C
ATOM   2279  C   SER A 272     -39.648   0.484  31.595  1.00 44.73           C
ANISOU 2279  C   SER A 272     5717   5118   6159    159    223    262       C
ATOM   2280  O   SER A 272     -38.607   1.058  31.929  1.00 48.03           O
ANISOU 2280  O   SER A 272     6146   5604   6499    249    172    239       O
ATOM   2281  CB  SER A 272     -41.660   1.466  32.733  1.00 41.65           C
ANISOU 2281  CB  SER A 272     5263   4905   5658    158    241    361       C
ATOM   2282  OG  SER A 272     -42.052   1.953  31.458  1.00 36.18           O
ANISOU 2282  OG  SER A 272     4555   4195   4996     48    194    235       O
ATOM   2283  N   THR A 273     -39.882   0.050  30.356  1.00 41.24           N
ANISOU 2283  N   THR A 273     5279   4575   5814     43    230    169       N
ATOM   2284  CA  THR A 273     -38.938   0.286  29.272  1.00 39.35           C
ANISOU 2284  CA  THR A 273     5061   4308   5581     20    183     38       C
ATOM   2285  C   THR A 273     -39.170   1.604  28.549  1.00 43.21           C
ANISOU 2285  C   THR A 273     5531   4902   5987    -24    105    -65       C
ATOM   2286  O   THR A 273     -38.358   1.965  27.690  1.00 44.87           O
ANISOU 2286  O   THR A 273     5754   5110   6185    -35     67   -161       O
ATOM   2287  CB  THR A 273     -38.987  -0.854  28.247  1.00 36.77           C
ANISOU 2287  CB  THR A 273     4753   3827   5389    -75    230    -26       C
ATOM   2288  OG1 THR A 273     -40.344  -1.126  27.881  1.00 40.92           O
ANISOU 2288  OG1 THR A 273     5249   4329   5969   -190    251    -35       O
ATOM   2289  CG2 THR A 273     -38.374  -2.105  28.823  1.00 40.11           C
ANISOU 2289  CG2 THR A 273     5205   4123   5913    -12    305     64       C
ATOM   2290  N   ILE A 274     -40.242   2.333  28.868  1.00 43.92           N
ANISOU 2290  N   ILE A 274     5586   5081   6022    -44     89    -38       N
ATOM   2291  CA  ILE A 274     -40.544   3.568  28.150  1.00 41.32           C
ANISOU 2291  CA  ILE A 274     5234   4840   5627    -82     22   -121       C
ATOM   2292  C   ILE A 274     -40.841   4.708  29.122  1.00 36.64           C
ANISOU 2292  C   ILE A 274     4618   4365   4938     -5     -8    -80       C
ATOM   2293  O   ILE A 274     -40.577   5.877  28.815  1.00 44.08           O
ANISOU 2293  O   ILE A 274     5553   5372   5824      9    -66   -141       O
ATOM   2294  CB  ILE A 274     -41.698   3.348  27.151  1.00 48.57           C
ANISOU 2294  CB  ILE A 274     6122   5741   6592   -208     25   -166       C
ATOM   2295  CG1 ILE A 274     -41.703   4.451  26.090  1.00 58.81           C
ANISOU 2295  CG1 ILE A 274     7405   7110   7830   -245    -43   -256       C
ATOM   2296  CG2 ILE A 274     -43.041   3.271  27.863  1.00 49.25           C
ANISOU 2296  CG2 ILE A 274     6163   5864   6686   -226     58    -80       C
ATOM   2297  CD1 ILE A 274     -40.341   4.713  25.468  1.00 57.94           C
ANISOU 2297  CD1 ILE A 274     7330   6983   7701   -217    -70   -328       C
ATOM   2298  N   PHE A 275     -41.371   4.387  30.302  1.00 28.98           N
ANISOU 2298  N   PHE A 275     3638   3423   3950     48     36     23       N
ATOM   2299  CA  PHE A 275     -41.579   5.397  31.332  1.00 31.01           C
ANISOU 2299  CA  PHE A 275     3877   3798   4105    136     14     52       C
ATOM   2300  C   PHE A 275     -40.295   5.620  32.121  1.00 40.15           C
ANISOU 2300  C   PHE A 275     5061   4992   5201    247    -14     51       C
ATOM   2301  O   PHE A 275     -39.436   4.739  32.215  1.00 48.31           O
ANISOU 2301  O   PHE A 275     6121   5963   6271    275      5     80       O
ATOM   2302  CB  PHE A 275     -42.705   4.991  32.281  1.00 33.82           C
ANISOU 2302  CB  PHE A 275     4205   4192   4452    153     80    165       C
ATOM   2303  CG  PHE A 275     -44.052   4.934  31.626  1.00 37.71           C
ANISOU 2303  CG  PHE A 275     4651   4676   5000     48    100    165       C
ATOM   2304  CD1 PHE A 275     -44.662   6.091  31.171  1.00 38.19           C
ANISOU 2304  CD1 PHE A 275     4678   4810   5023     27     52    104       C
ATOM   2305  CD2 PHE A 275     -44.704   3.726  31.451  1.00 36.65           C
ANISOU 2305  CD2 PHE A 275     4502   4457   4969    -30    166    226       C
ATOM   2306  CE1 PHE A 275     -45.899   6.045  30.558  1.00 30.56           C
ANISOU 2306  CE1 PHE A 275     3656   3850   4104    -64     62    107       C
ATOM   2307  CE2 PHE A 275     -45.943   3.675  30.838  1.00 35.60           C
ANISOU 2307  CE2 PHE A 275     4312   4325   4890   -134    175    216       C
ATOM   2308  CZ  PHE A 275     -46.540   4.837  30.394  1.00 30.54           C
ANISOU 2308  CZ  PHE A 275     3631   3776   4196   -147    120    158       C
ATOM   2309  N   TYR A 276     -40.170   6.810  32.699  1.00 35.77           N
ANISOU 2309  N   TYR A 276     4495   4540   4557    313    -63     12       N
ATOM   2310  CA  TYR A 276     -38.929   7.196  33.367  1.00 32.68           C
ANISOU 2310  CA  TYR A 276     4116   4197   4103    408   -110    -19       C
ATOM   2311  C   TYR A 276     -38.905   6.547  34.744  1.00 36.91           C
ANISOU 2311  C   TYR A 276     4657   4794   4573    509    -71     91       C
ATOM   2312  O   TYR A 276     -39.396   7.088  35.736  1.00 44.09           O
ANISOU 2312  O   TYR A 276     5552   5813   5387    577    -70    113       O
ATOM   2313  CB  TYR A 276     -38.790   8.714  33.383  1.00 26.76           C
ANISOU 2313  CB  TYR A 276     3349   3517   3302    427   -177   -120       C
ATOM   2314  CG  TYR A 276     -38.366   9.154  31.999  1.00 32.61           C
ANISOU 2314  CG  TYR A 276     4090   4188   4114    344   -211   -205       C
ATOM   2315  CD1 TYR A 276     -39.294   9.254  30.967  1.00 32.07           C
ANISOU 2315  CD1 TYR A 276     4011   4082   4093    251   -196   -213       C
ATOM   2316  CD2 TYR A 276     -37.027   9.366  31.695  1.00 25.55           C
ANISOU 2316  CD2 TYR A 276     3199   3271   3236    358   -254   -268       C
ATOM   2317  CE1 TYR A 276     -38.906   9.607  29.683  1.00 31.73           C
ANISOU 2317  CE1 TYR A 276     3968   3991   4096    182   -223   -277       C
ATOM   2318  CE2 TYR A 276     -36.630   9.717  30.413  1.00 23.98           C
ANISOU 2318  CE2 TYR A 276     2999   3015   3097    285   -272   -331       C
ATOM   2319  CZ  TYR A 276     -37.571   9.833  29.411  1.00 29.17           C
ANISOU 2319  CZ  TYR A 276     3652   3644   3785    200   -255   -333       C
ATOM   2320  OH  TYR A 276     -37.177  10.177  28.136  1.00 29.15           O
ANISOU 2320  OH  TYR A 276     3649   3604   3823    136   -271   -385       O
ATOM   2321  N   SER A 277     -38.317   5.359  34.782  1.00 35.02           N
ANISOU 2321  N   SER A 277     4437   4484   4384    524    -34    162       N
ATOM   2322  CA  SER A 277     -38.334   4.441  35.911  1.00 37.46           C
ANISOU 2322  CA  SER A 277     4752   4823   4657    612     22    303       C
ATOM   2323  C   SER A 277     -36.912   4.043  36.269  1.00 42.30           C
ANISOU 2323  C   SER A 277     5377   5442   5255    700    -10    316       C
ATOM   2324  O   SER A 277     -35.963   4.369  35.548  1.00 39.60           O
ANISOU 2324  O   SER A 277     5034   5063   4948    678    -65    215       O
ATOM   2325  CB  SER A 277     -39.168   3.203  35.545  1.00 39.11           C
ANISOU 2325  CB  SER A 277     4967   4911   4981    537    116    403       C
ATOM   2326  OG  SER A 277     -38.424   2.298  34.747  1.00 41.65           O
ANISOU 2326  OG  SER A 277     5313   5095   5419    498    131    391       O
ATOM   2327  N   PRO A 278     -36.717   3.353  37.400  1.00 42.69           N
ANISOU 2327  N   PRO A 278     5428   5547   5244    808     26    449       N
ATOM   2328  CA  PRO A 278     -35.360   2.902  37.747  1.00 41.96           C
ANISOU 2328  CA  PRO A 278     5336   5466   5139    902     -6    477       C
ATOM   2329  C   PRO A 278     -34.854   1.753  36.886  1.00 43.90           C
ANISOU 2329  C   PRO A 278     5601   5537   5540    859     43    508       C
ATOM   2330  O   PRO A 278     -33.681   1.370  37.025  1.00 41.40           O
ANISOU 2330  O   PRO A 278     5279   5216   5233    934     18    524       O
ATOM   2331  CB  PRO A 278     -35.497   2.479  39.215  1.00 43.62           C
ANISOU 2331  CB  PRO A 278     5542   5800   5232   1034     28    632       C
ATOM   2332  CG  PRO A 278     -36.919   2.116  39.365  1.00 45.57           C
ANISOU 2332  CG  PRO A 278     5795   6018   5502    983    121    727       C
ATOM   2333  CD  PRO A 278     -37.668   3.083  38.494  1.00 45.04           C
ANISOU 2333  CD  PRO A 278     5720   5928   5464    865     91    584       C
ATOM   2334  N   PHE A 279     -35.689   1.193  36.006  1.00 41.76           N
ANISOU 2334  N   PHE A 279     5348   5126   5393    742    108    509       N
ATOM   2335  CA  PHE A 279     -35.222   0.121  35.133  1.00 46.33           C
ANISOU 2335  CA  PHE A 279     5947   5532   6123    697    156    511       C
ATOM   2336  C   PHE A 279     -34.088   0.597  34.233  1.00 49.17           C
ANISOU 2336  C   PHE A 279     6304   5874   6505    680     88    369       C
ATOM   2337  O   PHE A 279     -33.081  -0.101  34.069  1.00 52.42           O
ANISOU 2337  O   PHE A 279     6719   6217   6981    729    100    386       O
ATOM   2338  CB  PHE A 279     -36.378  -0.419  34.293  1.00 41.98           C
ANISOU 2338  CB  PHE A 279     5409   4851   5692    560    223    501       C
ATOM   2339  CG  PHE A 279     -35.939  -1.275  33.142  1.00 44.03           C
ANISOU 2339  CG  PHE A 279     5690   4937   6100    490    256    438       C
ATOM   2340  CD1 PHE A 279     -35.560  -2.594  33.346  1.00 46.39           C
ANISOU 2340  CD1 PHE A 279     6008   5104   6513    533    334    540       C
ATOM   2341  CD2 PHE A 279     -35.905  -0.763  31.853  1.00 42.89           C
ANISOU 2341  CD2 PHE A 279     5548   4764   5983    387    214    277       C
ATOM   2342  CE1 PHE A 279     -35.153  -3.387  32.286  1.00 45.30           C
ANISOU 2342  CE1 PHE A 279     5893   4802   6518    472    369    465       C
ATOM   2343  CE2 PHE A 279     -35.496  -1.550  30.786  1.00 41.49           C
ANISOU 2343  CE2 PHE A 279     5393   4442   5928    327    247    205       C
ATOM   2344  CZ  PHE A 279     -35.121  -2.863  31.003  1.00 41.37           C
ANISOU 2344  CZ  PHE A 279     5399   4290   6031    369    325    289       C
ATOM   2345  N   GLN A 280     -34.237   1.781  33.636  1.00 37.17           N
ANISOU 2345  N   GLN A 280     4771   4413   4939    614     23    236       N
ATOM   2346  CA  GLN A 280     -33.190   2.305  32.767  1.00 35.37           C
ANISOU 2346  CA  GLN A 280     4533   4174   4733    594    -33    112       C
ATOM   2347  C   GLN A 280     -31.911   2.577  33.553  1.00 37.58           C
ANISOU 2347  C   GLN A 280     4783   4547   4949    714    -91    120       C
ATOM   2348  O   GLN A 280     -30.800   2.325  33.062  1.00 38.76           O
ANISOU 2348  O   GLN A 280     4921   4654   5154    733   -103     81       O
ATOM   2349  CB  GLN A 280     -33.687   3.570  32.073  1.00 35.82           C
ANISOU 2349  CB  GLN A 280     4578   4277   4753    507    -84     -6       C
ATOM   2350  CG  GLN A 280     -34.791   3.318  31.049  1.00 43.69           C
ANISOU 2350  CG  GLN A 280     5593   5191   5817    383    -41    -34       C
ATOM   2351  CD  GLN A 280     -36.203   3.335  31.643  1.00 41.03           C
ANISOU 2351  CD  GLN A 280     5252   4889   5449    361    -10     37       C
ATOM   2352  OE1 GLN A 280     -36.389   3.371  32.862  1.00 37.58           O
ANISOU 2352  OE1 GLN A 280     4807   4530   4941    446     -3    124       O
ATOM   2353  NE2 GLN A 280     -37.203   3.299  30.771  1.00 36.74           N
ANISOU 2353  NE2 GLN A 280     4708   4300   4953    251     11      1       N
ATOM   2354  N   LEU A 281     -32.052   3.093  34.776  1.00 31.59           N
ANISOU 2354  N   LEU A 281     4006   3926   4069    797   -130    166       N
ATOM   2355  CA  LEU A 281     -30.891   3.297  35.634  1.00 35.37           C
ANISOU 2355  CA  LEU A 281     4449   4516   4474    916   -194    175       C
ATOM   2356  C   LEU A 281     -30.167   1.984  35.891  1.00 40.61           C
ANISOU 2356  C   LEU A 281     5115   5119   5197   1001   -147    294       C
ATOM   2357  O   LEU A 281     -28.930   1.923  35.847  1.00 39.38           O
ANISOU 2357  O   LEU A 281     4925   4982   5057   1059   -189    269       O
ATOM   2358  CB  LEU A 281     -31.328   3.935  36.949  1.00 34.30           C
ANISOU 2358  CB  LEU A 281     4300   4548   4186    994   -233    207       C
ATOM   2359  CG  LEU A 281     -30.206   4.200  37.952  1.00 34.61           C
ANISOU 2359  CG  LEU A 281     4294   4735   4122   1120   -314    206       C
ATOM   2360  CD1 LEU A 281     -29.315   5.316  37.449  1.00 29.77           C
ANISOU 2360  CD1 LEU A 281     3638   4153   3520   1081   -407     37       C
ATOM   2361  CD2 LEU A 281     -30.785   4.543  39.315  1.00 30.55           C
ANISOU 2361  CD2 LEU A 281     3776   4388   3444   1209   -331    260       C
ATOM   2362  N   LEU A 282     -30.927   0.921  36.161  1.00 47.61           N
ANISOU 2362  N   LEU A 282     6036   5927   6128   1009    -56    431       N
ATOM   2363  CA  LEU A 282     -30.326  -0.393  36.355  1.00 46.86           C
ANISOU 2363  CA  LEU A 282     5947   5741   6115   1089      5    557       C
ATOM   2364  C   LEU A 282     -29.623  -0.869  35.094  1.00 44.59           C
ANISOU 2364  C   LEU A 282     5666   5300   5974   1032     29    474       C
ATOM   2365  O   LEU A 282     -28.524  -1.426  35.166  1.00 45.70           O
ANISOU 2365  O   LEU A 282     5786   5419   6160   1119     29    510       O
ATOM   2366  CB  LEU A 282     -31.390  -1.401  36.783  1.00 44.82           C
ANISOU 2366  CB  LEU A 282     5724   5401   5904   1087    111    716       C
ATOM   2367  CG  LEU A 282     -31.984  -1.166  38.168  1.00 52.25           C
ANISOU 2367  CG  LEU A 282     6656   6502   6694   1175    110    839       C
ATOM   2368  CD1 LEU A 282     -32.736  -2.401  38.639  1.00 61.47           C
ANISOU 2368  CD1 LEU A 282     7849   7573   7935   1197    231   1036       C
ATOM   2369  CD2 LEU A 282     -30.894  -0.781  39.154  1.00 49.78           C
ANISOU 2369  CD2 LEU A 282     6303   6370   6242   1324     24    863       C
ATOM   2370  N   VAL A 283     -30.245  -0.672  33.931  1.00 40.53           N
ANISOU 2370  N   VAL A 283     5179   4690   5532    892     52    363       N
ATOM   2371  CA  VAL A 283     -29.608  -1.068  32.676  1.00 41.87           C
ANISOU 2371  CA  VAL A 283     5355   4731   5821    836     77    268       C
ATOM   2372  C   VAL A 283     -28.254  -0.388  32.537  1.00 43.78           C
ANISOU 2372  C   VAL A 283     5549   5059   6027    890      1    187       C
ATOM   2373  O   VAL A 283     -27.245  -1.029  32.228  1.00 52.10           O
ANISOU 2373  O   VAL A 283     6586   6048   7159    944     24    190       O
ATOM   2374  CB  VAL A 283     -30.512  -0.743  31.473  1.00 43.77           C
ANISOU 2374  CB  VAL A 283     5624   4904   6103    681     93    150       C
ATOM   2375  CG1 VAL A 283     -29.766  -1.035  30.171  1.00 37.79           C
ANISOU 2375  CG1 VAL A 283     4872   4047   5439    633    114     37       C
ATOM   2376  CG2 VAL A 283     -31.817  -1.525  31.541  1.00 42.02           C
ANISOU 2376  CG2 VAL A 283     5438   4587   5942    618    170    223       C
ATOM   2377  N   LEU A 284     -28.212   0.922  32.789  1.00 39.19           N
ANISOU 2377  N   LEU A 284     4936   4618   5338    877    -86    113       N
ATOM   2378  CA  LEU A 284     -26.978   1.679  32.593  1.00 41.15           C
ANISOU 2378  CA  LEU A 284     5127   4942   5567    905   -160     23       C
ATOM   2379  C   LEU A 284     -25.899   1.260  33.590  1.00 42.37           C
ANISOU 2379  C   LEU A 284     5231   5173   5693   1052   -193    107       C
ATOM   2380  O   LEU A 284     -24.748   1.004  33.207  1.00 46.61           O
ANISOU 2380  O   LEU A 284     5727   5689   6293   1092   -198     81       O
ATOM   2381  CB  LEU A 284     -27.272   3.175  32.696  1.00 41.38           C
ANISOU 2381  CB  LEU A 284     5133   5085   5504    852   -240    -74       C
ATOM   2382  CG  LEU A 284     -28.185   3.694  31.582  1.00 34.85           C
ANISOU 2382  CG  LEU A 284     4341   4193   4708    715   -216   -157       C
ATOM   2383  CD1 LEU A 284     -28.627   5.117  31.856  1.00 35.70           C
ANISOU 2383  CD1 LEU A 284     4430   4402   4732    680   -285   -226       C
ATOM   2384  CD2 LEU A 284     -27.484   3.603  30.238  1.00 32.03           C
ANISOU 2384  CD2 LEU A 284     3976   3754   4439    655   -191   -241       C
ATOM   2385  N   LEU A 285     -26.254   1.164  34.875  1.00 42.76           N
ANISOU 2385  N   LEU A 285     5280   5323   5643   1140   -213    214       N
ATOM   2386  CA  LEU A 285     -25.268   0.767  35.879  1.00 43.76           C
ANISOU 2386  CA  LEU A 285     5355   5549   5722   1290   -252    306       C
ATOM   2387  C   LEU A 285     -24.787  -0.667  35.662  1.00 45.87           C
ANISOU 2387  C   LEU A 285     5635   5682   6113   1359   -166    420       C
ATOM   2388  O   LEU A 285     -23.593  -0.962  35.823  1.00 56.49           O
ANISOU 2388  O   LEU A 285     6922   7061   7482   1456   -194    443       O
ATOM   2389  CB  LEU A 285     -25.853   0.938  37.280  1.00 46.52           C
ANISOU 2389  CB  LEU A 285     5706   6047   5920   1373   -283    403       C
ATOM   2390  CG  LEU A 285     -25.892   2.373  37.808  1.00 48.44           C
ANISOU 2390  CG  LEU A 285     5914   6464   6026   1359   -391    284       C
ATOM   2391  CD1 LEU A 285     -26.614   2.420  39.135  1.00 53.26           C
ANISOU 2391  CD1 LEU A 285     6537   7216   6482   1442   -400    381       C
ATOM   2392  CD2 LEU A 285     -24.491   2.937  37.952  1.00 51.59           C
ANISOU 2392  CD2 LEU A 285     6226   6970   6405   1412   -494    197       C
ATOM   2393  N   GLY A 286     -25.693  -1.574  35.291  1.00 43.10           N
ANISOU 2393  N   GLY A 286     5352   5172   5853   1309    -61    488       N
ATOM   2394  CA  GLY A 286     -25.285  -2.935  35.001  1.00 47.54           C
ANISOU 2394  CA  GLY A 286     5931   5574   6559   1364     31    580       C
ATOM   2395  C   GLY A 286     -24.415  -3.035  33.768  1.00 48.86           C
ANISOU 2395  C   GLY A 286     6081   5642   6841   1321     46    455       C
ATOM   2396  O   GLY A 286     -23.507  -3.867  33.714  1.00 50.92           O
ANISOU 2396  O   GLY A 286     6318   5836   7192   1415     83    510       O
ATOM   2397  N   SER A 287     -24.664  -2.192  32.764  1.00 41.79           N
ANISOU 2397  N   SER A 287     5195   4741   5942   1188     23    292       N
ATOM   2398  CA  SER A 287     -23.752  -2.129  31.630  1.00 43.77           C
ANISOU 2398  CA  SER A 287     5420   4936   6275   1156     33    173       C
ATOM   2399  C   SER A 287     -22.368  -1.686  32.080  1.00 45.93           C
ANISOU 2399  C   SER A 287     5602   5340   6511   1260    -45    168       C
ATOM   2400  O   SER A 287     -21.353  -2.224  31.620  1.00 44.77           O
ANISOU 2400  O   SER A 287     5418   5138   6455   1315    -13    158       O
ATOM   2401  CB  SER A 287     -24.298  -1.180  30.567  1.00 38.37           C
ANISOU 2401  CB  SER A 287     4757   4253   5569   1003     16     20       C
ATOM   2402  OG  SER A 287     -25.463  -1.713  29.970  1.00 42.07           O
ANISOU 2402  OG  SER A 287     5299   4596   6090    905     88      9       O
ATOM   2403  N   ALA A 288     -22.311  -0.704  32.982  1.00 44.69           N
ANISOU 2403  N   ALA A 288     5399   5358   6223   1287   -147    167       N
ATOM   2404  CA  ALA A 288     -21.022  -0.257  33.501  1.00 43.83           C
ANISOU 2404  CA  ALA A 288     5190   5388   6074   1381   -234    155       C
ATOM   2405  C   ALA A 288     -20.274  -1.403  34.176  1.00 51.58           C
ANISOU 2405  C   ALA A 288     6139   6361   7096   1542   -209    302       C
ATOM   2406  O   ALA A 288     -19.086  -1.634  33.910  1.00 60.22           O
ANISOU 2406  O   ALA A 288     7162   7462   8258   1608   -215    289       O
ATOM   2407  CB  ALA A 288     -21.224   0.905  34.472  1.00 37.22           C
ANISOU 2407  CB  ALA A 288     4317   4737   5086   1385   -348    125       C
ATOM   2408  N   VAL A 289     -20.963  -2.148  35.044  1.00 51.01           N
ANISOU 2408  N   VAL A 289     6114   6275   6991   1612   -171    455       N
ATOM   2409  CA  VAL A 289     -20.268  -3.226  35.752  1.00 52.44           C
ANISOU 2409  CA  VAL A 289     6263   6454   7209   1780   -145    621       C
ATOM   2410  C   VAL A 289     -19.934  -4.382  34.808  1.00 49.29           C
ANISOU 2410  C   VAL A 289     5892   5835   7000   1788    -26    638       C
ATOM   2411  O   VAL A 289     -18.942  -5.090  35.015  1.00 54.82           O
ANISOU 2411  O   VAL A 289     6537   6524   7767   1921    -11    722       O
ATOM   2412  CB  VAL A 289     -21.076  -3.698  36.976  1.00 53.38           C
ANISOU 2412  CB  VAL A 289     6422   6624   7237   1861   -129    801       C
ATOM   2413  CG1 VAL A 289     -21.506  -2.503  37.813  1.00 51.12           C
ANISOU 2413  CG1 VAL A 289     6116   6549   6757   1841   -238    752       C
ATOM   2414  CG2 VAL A 289     -22.275  -4.519  36.555  1.00 57.03           C
ANISOU 2414  CG2 VAL A 289     6985   6883   7799   1783     -2    860       C
ATOM   2415  N   ILE A 290     -20.717  -4.578  33.745  1.00 45.24           N
ANISOU 2415  N   ILE A 290     5458   5153   6579   1652     57    551       N
ATOM   2416  CA  ILE A 290     -20.388  -5.618  32.773  1.00 45.93           C
ANISOU 2416  CA  ILE A 290     5573   5035   6844   1652    168    530       C
ATOM   2417  C   ILE A 290     -19.135  -5.237  31.992  1.00 48.37           C
ANISOU 2417  C   ILE A 290     5806   5379   7193   1662    142    408       C
ATOM   2418  O   ILE A 290     -18.270  -6.081  31.718  1.00 54.45           O
ANISOU 2418  O   ILE A 290     6546   6060   8082   1757    201    441       O
ATOM   2419  CB  ILE A 290     -21.591  -5.877  31.846  1.00 46.50           C
ANISOU 2419  CB  ILE A 290     5743   4940   6985   1496    251    449       C
ATOM   2420  CG1 ILE A 290     -22.687  -6.639  32.595  1.00 50.87           C
ANISOU 2420  CG1 ILE A 290     6360   5412   7557   1508    310    601       C
ATOM   2421  CG2 ILE A 290     -21.174  -6.661  30.613  1.00 42.80           C
ANISOU 2421  CG2 ILE A 290     5297   4286   6678   1468    348    356       C
ATOM   2422  CD1 ILE A 290     -23.980  -6.760  31.820  1.00 53.61           C
ANISOU 2422  CD1 ILE A 290     6787   5627   7955   1344    371    519       C
ATOM   2423  N   ALA A 291     -19.009  -3.959  31.633  1.00 41.43           N
ANISOU 2423  N   ALA A 291     4890   4625   6225   1569     59    273       N
ATOM   2424  CA  ALA A 291     -17.777  -3.492  31.006  1.00 44.49           C
ANISOU 2424  CA  ALA A 291     5189   5070   6645   1580     31    173       C
ATOM   2425  C   ALA A 291     -16.587  -3.649  31.948  1.00 48.73           C
ANISOU 2425  C   ALA A 291     5617   5732   7168   1746    -32    270       C
ATOM   2426  O   ALA A 291     -15.478  -3.989  31.515  1.00 49.97           O
ANISOU 2426  O   ALA A 291     5702   5871   7415   1814     -7    252       O
ATOM   2427  CB  ALA A 291     -17.936  -2.039  30.567  1.00 42.83           C
ANISOU 2427  CB  ALA A 291     4956   4969   6347   1449    -45     31       C
ATOM   2428  N   ALA A 292     -16.801  -3.411  33.246  1.00 46.01           N
ANISOU 2428  N   ALA A 292     5251   5527   6703   1817   -116    372       N
ATOM   2429  CA  ALA A 292     -15.738  -3.656  34.220  1.00 44.59           C
ANISOU 2429  CA  ALA A 292     4966   5482   6494   1987   -183    480       C
ATOM   2430  C   ALA A 292     -15.343  -5.128  34.245  1.00 50.90           C
ANISOU 2430  C   ALA A 292     5775   6140   7426   2125    -80    624       C
ATOM   2431  O   ALA A 292     -14.154  -5.465  34.351  1.00 53.95           O
ANISOU 2431  O   ALA A 292     6061   6571   7867   2249    -95    665       O
ATOM   2432  CB  ALA A 292     -16.182  -3.198  35.607  1.00 40.60           C
ANISOU 2432  CB  ALA A 292     4452   5159   5817   2041   -284    565       C
ATOM   2433  N   ALA A 293     -16.331  -6.022  34.147  1.00 50.54           N
ANISOU 2433  N   ALA A 293     5842   5916   7446   2106     27    704       N
ATOM   2434  CA  ALA A 293     -16.035  -7.451  34.098  1.00 50.94           C
ANISOU 2434  CA  ALA A 293     5911   5791   7651   2226    141    835       C
ATOM   2435  C   ALA A 293     -15.242  -7.808  32.846  1.00 50.07           C
ANISOU 2435  C   ALA A 293     5779   5548   7697   2211    217    715       C
ATOM   2436  O   ALA A 293     -14.349  -8.660  32.890  1.00 45.95           O
ANISOU 2436  O   ALA A 293     5205   4966   7287   2354    267    798       O
ATOM   2437  CB  ALA A 293     -17.332  -8.257  34.163  1.00 48.04           C
ANISOU 2437  CB  ALA A 293     5669   5244   7341   2178    244    922       C
ATOM   2438  N   PHE A 294     -15.563  -7.174  31.716  1.00 54.90           N
ANISOU 2438  N   PHE A 294     6428   6119   8315   2046    233    526       N
ATOM   2439  CA  PHE A 294     -14.781  -7.385  30.499  1.00 50.19           C
ANISOU 2439  CA  PHE A 294     5804   5429   7837   2029    304    399       C
ATOM   2440  C   PHE A 294     -13.346  -6.915  30.685  1.00 51.78           C
ANISOU 2440  C   PHE A 294     5857   5793   8024   2127    230    392       C
ATOM   2441  O   PHE A 294     -12.401  -7.557  30.206  1.00 47.67           O
ANISOU 2441  O   PHE A 294     5282   5203   7626   2219    298    388       O
ATOM   2442  CB  PHE A 294     -15.416  -6.645  29.325  1.00 49.18           C
ANISOU 2442  CB  PHE A 294     5735   5270   7681   1836    320    210       C
ATOM   2443  CG  PHE A 294     -16.377  -7.475  28.531  1.00 57.29           C
ANISOU 2443  CG  PHE A 294     6885   6080   8804   1752    438    162       C
ATOM   2444  CD1 PHE A 294     -15.917  -8.447  27.659  1.00 62.29           C
ANISOU 2444  CD1 PHE A 294     7535   6542   9591   1790    557    108       C
ATOM   2445  CD2 PHE A 294     -17.742  -7.275  28.646  1.00 52.95           C
ANISOU 2445  CD2 PHE A 294     6426   5499   8194   1633    430    158       C
ATOM   2446  CE1 PHE A 294     -16.804  -9.210  26.920  1.00 61.86           C
ANISOU 2446  CE1 PHE A 294     7589   6287   9628   1704    659     40       C
ATOM   2447  CE2 PHE A 294     -18.631  -8.034  27.911  1.00 52.35           C
ANISOU 2447  CE2 PHE A 294     6450   5229   8211   1547    531    102       C
ATOM   2448  CZ  PHE A 294     -18.162  -9.003  27.048  1.00 53.13           C
ANISOU 2448  CZ  PHE A 294     6568   5156   8463   1578    642     37       C
ATOM   2449  N   TYR A 295     -13.170  -5.780  31.364  1.00 49.02           N
ANISOU 2449  N   TYR A 295     5435   5659   7531   2107     93    379       N
ATOM   2450  CA  TYR A 295     -11.828  -5.290  31.658  1.00 50.55           C
ANISOU 2450  CA  TYR A 295     5473   6025   7710   2193      7    371       C
ATOM   2451  C   TYR A 295     -11.048  -6.299  32.495  1.00 53.16           C
ANISOU 2451  C   TYR A 295     5734   6370   8095   2405     13    547       C
ATOM   2452  O   TYR A 295      -9.865  -6.558  32.235  1.00 48.68           O
ANISOU 2452  O   TYR A 295     5056   5825   7615   2501     26    546       O
ATOM   2453  CB  TYR A 295     -11.921  -3.939  32.368  1.00 47.24           C
ANISOU 2453  CB  TYR A 295     4997   5822   7129   2129   -145    323       C
ATOM   2454  CG  TYR A 295     -10.596  -3.397  32.839  1.00 55.56           C
ANISOU 2454  CG  TYR A 295     5879   7070   8161   2212   -254    313       C
ATOM   2455  CD1 TYR A 295      -9.647  -2.942  31.930  1.00 62.11           C
ANISOU 2455  CD1 TYR A 295     6612   7914   9072   2167   -240    195       C
ATOM   2456  CD2 TYR A 295     -10.292  -3.336  34.191  1.00 62.41           C
ANISOU 2456  CD2 TYR A 295     6671   8117   8923   2334   -370    422       C
ATOM   2457  CE1 TYR A 295      -8.425  -2.444  32.357  1.00 63.46           C
ANISOU 2457  CE1 TYR A 295     6611   8264   9239   2233   -341    183       C
ATOM   2458  CE2 TYR A 295      -9.072  -2.839  34.628  1.00 68.86           C
ANISOU 2458  CE2 TYR A 295     7318   9124   9721   2405   -481    402       C
ATOM   2459  CZ  TYR A 295      -8.143  -2.395  33.706  1.00 66.70           C
ANISOU 2459  CZ  TYR A 295     6945   8851   9548   2350   -466    281       C
ATOM   2460  OH  TYR A 295      -6.935  -1.899  34.137  1.00 66.94           O
ANISOU 2460  OH  TYR A 295     6792   9069   9573   2411   -577    258       O
ATOM   2461  N   GLN A 296     -11.701  -6.887  33.501  1.00 54.76           N
ANISOU 2461  N   GLN A 296     5994   6562   8249   2486      9    711       N
ATOM   2462  CA  GLN A 296     -11.033  -7.893  34.325  1.00 59.33           C
ANISOU 2462  CA  GLN A 296     6513   7150   8878   2698     21    907       C
ATOM   2463  C   GLN A 296     -10.690  -9.139  33.512  1.00 62.21           C
ANISOU 2463  C   GLN A 296     6909   7272   9455   2769    179    935       C
ATOM   2464  O   GLN A 296      -9.592  -9.701  33.651  1.00 59.84           O
ANISOU 2464  O   GLN A 296     6506   6989   9240   2928    191   1013       O
ATOM   2465  CB  GLN A 296     -11.908  -8.256  35.524  1.00 62.41           C
ANISOU 2465  CB  GLN A 296     6971   7575   9169   2762      0   1089       C
ATOM   2466  CG  GLN A 296     -11.272  -9.263  36.474  1.00 74.64           C
ANISOU 2466  CG  GLN A 296     8462   9152  10746   2979      6   1314       C
ATOM   2467  CD  GLN A 296     -10.065  -8.700  37.203  1.00 84.27           C
ANISOU 2467  CD  GLN A 296     9525  10640  11855   3058   -146   1315       C
ATOM   2468  OE1 GLN A 296      -9.895  -7.484  37.306  1.00 88.28           O
ANISOU 2468  OE1 GLN A 296     9955  11343  12244   3009   -267   1199       O
ATOM   2469  NE2 GLN A 296      -9.223  -9.586  37.720  1.00 88.59           N
ANISOU 2469  NE2 GLN A 296    10021  11194  12444   3176   -143   1439       N
ATOM   2470  N   ILE A 297     -11.622  -9.588  32.668  1.00 58.36           N
ANISOU 2470  N   ILE A 297     6558   6561   9056   2652    299    864       N
ATOM   2471  CA  ILE A 297     -11.358 -10.722  31.785  1.00 57.27           C
ANISOU 2471  CA  ILE A 297     6458   6178   9123   2698    453    847       C
ATOM   2472  C   ILE A 297     -10.144 -10.440  30.911  1.00 54.70           C
ANISOU 2472  C   ILE A 297     6027   5896   8861   2716    463    715       C
ATOM   2473  O   ILE A 297      -9.302 -11.317  30.686  1.00 48.10           O
ANISOU 2473  O   ILE A 297     5152   4976   8147   2825    531    747       O
ATOM   2474  CB  ILE A 297     -12.605 -11.036  30.935  1.00 53.33           C
ANISOU 2474  CB  ILE A 297     6115   5463   8685   2534    557    743       C
ATOM   2475  CG1 ILE A 297     -13.684 -11.709  31.786  1.00 56.61           C
ANISOU 2475  CG1 ILE A 297     6625   5780   9104   2553    590    912       C
ATOM   2476  CG2 ILE A 297     -12.244 -11.916  29.746  1.00 52.80           C
ANISOU 2476  CG2 ILE A 297     6080   5172   8810   2542    704    640       C
ATOM   2477  CD1 ILE A 297     -15.061 -11.693  31.152  1.00 54.66           C
ANISOU 2477  CD1 ILE A 297     6512   5389   8867   2363    648    805       C
ATOM   2478  N   GLU A 298     -10.031  -9.205  30.415  1.00 51.77           N
ANISOU 2478  N   GLU A 298     5615   5670   8387   2579    386    555       N
ATOM   2479  CA  GLU A 298      -8.935  -8.858  29.520  1.00 50.82           C
ANISOU 2479  CA  GLU A 298     5392   5595   8324   2577    406    428       C
ATOM   2480  C   GLU A 298      -7.610  -8.803  30.262  1.00 57.48           C
ANISOU 2480  C   GLU A 298     6059   6610   9171   2746    326    527       C
ATOM   2481  O   GLU A 298      -6.582  -9.230  29.732  1.00 56.64           O
ANISOU 2481  O   GLU A 298     5864   6472   9184   2839    391    507       O
ATOM   2482  CB  GLU A 298      -9.219  -7.524  28.831  1.00 52.78           C
ANISOU 2482  CB  GLU A 298     5642   5947   8466   2383    350    251       C
ATOM   2483  CG  GLU A 298      -8.139  -7.087  27.855  1.00 56.05           C
ANISOU 2483  CG  GLU A 298     5949   6414   8934   2365    380    126       C
ATOM   2484  CD  GLU A 298      -7.746  -8.181  26.880  1.00 64.06           C
ANISOU 2484  CD  GLU A 298     6992   7239  10109   2432    543     85       C
ATOM   2485  OE1 GLU A 298      -8.623  -8.956  26.444  1.00 68.41           O
ANISOU 2485  OE1 GLU A 298     7683   7593  10715   2394    643     61       O
ATOM   2486  OE2 GLU A 298      -6.548  -8.268  26.545  1.00 73.01           O
ANISOU 2486  OE2 GLU A 298     7999   8421  11319   2522    574     67       O
ATOM   2487  N   LYS A 299      -7.609  -8.276  31.486  1.00 58.66           N
ANISOU 2487  N   LYS A 299     6148   6953   9185   2791    182    628       N
ATOM   2488  CA  LYS A 299      -6.388  -8.297  32.285  1.00 53.47           C
ANISOU 2488  CA  LYS A 299     5319   6476   8524   2962     93    732       C
ATOM   2489  C   LYS A 299      -5.928  -9.730  32.528  1.00 59.09           C
ANISOU 2489  C   LYS A 299     6058   7058   9336   3083    165    853       C
ATOM   2490  O   LYS A 299      -4.739 -10.057  32.368  1.00 64.71           O
ANISOU 2490  O   LYS A 299     6661   7806  10119   3163    166    848       O
ATOM   2491  CB  LYS A 299      -6.618  -7.567  33.608  1.00 58.36           C
ANISOU 2491  CB  LYS A 299     5894   7325   8954   2976    -77    807       C
ATOM   2492  CG  LYS A 299      -6.429  -6.062  33.529  1.00 68.05           C
ANISOU 2492  CG  LYS A 299     7044   8745  10068   2829   -205    644       C
ATOM   2493  CD  LYS A 299      -6.076  -5.483  34.892  1.00 78.93           C
ANISOU 2493  CD  LYS A 299     8310  10388  11292   2907   -384    714       C
ATOM   2494  CE  LYS A 299      -5.081  -4.334  34.776  1.00 83.23           C
ANISOU 2494  CE  LYS A 299     8683  11127  11815   2846   -501    575       C
ATOM   2495  NZ  LYS A 299      -3.825  -4.716  34.063  1.00 86.02           N
ANISOU 2495  NZ  LYS A 299     8902  11456  12327   2922   -440    558       N
ATOM   2496  N   TRP A 300      -6.868 -10.606  32.904  1.00 58.62           N
ANISOU 2496  N   TRP A 300     6141   6844   9290   3094    229    964       N
ATOM   2497  CA  TRP A 300      -6.535 -12.013  33.113  1.00 63.26           C
ANISOU 2497  CA  TRP A 300     6766   7285   9983   3201    310   1084       C
ATOM   2498  C   TRP A 300      -5.935 -12.620  31.852  1.00 62.78           C
ANISOU 2498  C   TRP A 300     6710   7055  10088   3199    439    963       C
ATOM   2499  O   TRP A 300      -4.843 -13.204  31.884  1.00 56.32           O
ANISOU 2499  O   TRP A 300     5807   6251   9340   3309    449   1000       O
ATOM   2500  CB  TRP A 300      -7.779 -12.793  33.541  1.00 72.44           C
ANISOU 2500  CB  TRP A 300     8087   8283  11155   3181    380   1202       C
ATOM   2501  CG  TRP A 300      -8.129 -12.663  34.999  1.00 82.05           C
ANISOU 2501  CG  TRP A 300     9295   9660  12218   3239    274   1382       C
ATOM   2502  CD1 TRP A 300      -7.311 -12.248  36.010  1.00 85.54           C
ANISOU 2502  CD1 TRP A 300     9610  10354  12536   3332    133   1463       C
ATOM   2503  CD2 TRP A 300      -9.396 -12.954  35.604  1.00 87.51           C
ANISOU 2503  CD2 TRP A 300    10109  10282  12857   3203    304   1496       C
ATOM   2504  NE1 TRP A 300      -7.990 -12.261  37.206  1.00 87.17           N
ANISOU 2504  NE1 TRP A 300     9859  10659  12602   3360     76   1616       N
ATOM   2505  CE2 TRP A 300      -9.271 -12.691  36.983  1.00 88.00           C
ANISOU 2505  CE2 TRP A 300    10115  10571  12751   3285    182   1646       C
ATOM   2506  CE3 TRP A 300     -10.623 -13.409  35.111  1.00 91.12           C
ANISOU 2506  CE3 TRP A 300    10714  10513  13395   3104    422   1480       C
ATOM   2507  CZ2 TRP A 300     -10.327 -12.869  37.874  1.00 91.67           C
ANISOU 2507  CZ2 TRP A 300    10667  11047  13118   3278    185   1788       C
ATOM   2508  CZ3 TRP A 300     -11.670 -13.584  35.997  1.00 91.93           C
ANISOU 2508  CZ3 TRP A 300    10895  10617  13416   3092    421   1624       C
ATOM   2509  CH2 TRP A 300     -11.516 -13.315  37.363  1.00 93.31           C
ANISOU 2509  CH2 TRP A 300    11013  11025  13417   3183    309   1781       C
ATOM   2510  N   ASN A 301      -6.631 -12.469  30.722  1.00 59.13           N
ANISOU 2510  N   ASN A 301     6344   6443   9681   3073    538    811       N
ATOM   2511  CA  ASN A 301      -6.126 -12.994  29.457  1.00 63.23           C
ANISOU 2511  CA  ASN A 301     6877   6815  10330   3057    664    672       C
ATOM   2512  C   ASN A 301      -4.775 -12.387  29.087  1.00 62.53           C
ANISOU 2512  C   ASN A 301     6622   6895  10242   3103    621    595       C
ATOM   2513  O   ASN A 301      -3.956 -13.041  28.432  1.00 54.65           O
ANISOU 2513  O   ASN A 301     5594   5825   9347   3161    704    546       O
ATOM   2514  CB  ASN A 301      -7.155 -12.737  28.357  1.00 60.19           C
ANISOU 2514  CB  ASN A 301     6618   6287   9966   2895    754    508       C
ATOM   2515  CG  ASN A 301      -6.692 -13.216  27.003  1.00 60.18           C
ANISOU 2515  CG  ASN A 301     6639   6158  10070   2868    881    345       C
ATOM   2516  OD1 ASN A 301      -6.636 -14.419  26.742  1.00 66.34           O
ANISOU 2516  OD1 ASN A 301     7488   6761  10958   2912    976    355       O
ATOM   2517  ND2 ASN A 301      -6.364 -12.275  26.127  1.00 54.31           N
ANISOU 2517  ND2 ASN A 301     5835   5507   9291   2791    885    192       N
ATOM   2518  N   ASP A 302      -4.521 -11.148  29.511  1.00 66.96           N
ANISOU 2518  N   ASP A 302     7066   7681  10694   3077    494    584       N
ATOM   2519  CA  ASP A 302      -3.277 -10.470  29.171  1.00 65.81           C
ANISOU 2519  CA  ASP A 302     6747   7702  10554   3100    449    508       C
ATOM   2520  C   ASP A 302      -2.100 -11.028  29.956  1.00 64.15           C
ANISOU 2520  C   ASP A 302     6412   7591  10369   3255    385    625       C
ATOM   2521  O   ASP A 302      -0.976 -11.068  29.441  1.00 57.34           O
ANISOU 2521  O   ASP A 302     5434   6777   9576   3302    410    567       O
ATOM   2522  CB  ASP A 302      -3.436  -8.970  29.421  1.00 67.41           C
ANISOU 2522  CB  ASP A 302     6863   8107  10645   3010    328    456       C
ATOM   2523  CG  ASP A 302      -2.253  -8.168  28.940  1.00 70.17           C
ANISOU 2523  CG  ASP A 302     7031   8614  11017   2999    295    361       C
ATOM   2524  OD1 ASP A 302      -1.846  -8.345  27.773  1.00 72.97           O
ANISOU 2524  OD1 ASP A 302     7384   8882  11460   2970    417    252       O
ATOM   2525  OD2 ASP A 302      -1.737  -7.353  29.730  1.00 70.63           O
ANISOU 2525  OD2 ASP A 302     6947   8889  10999   3011    146    390       O
ATOM   2526  N   VAL A 303      -2.329 -11.466  31.193  1.00 64.32           N
ANISOU 2526  N   VAL A 303     6453   7651  10335   3335    307    794       N
ATOM   2527  CA  VAL A 303      -1.243 -12.055  31.974  1.00 59.64           C
ANISOU 2527  CA  VAL A 303     5747   7149   9764   3485    248    917       C
ATOM   2528  C   VAL A 303      -1.170 -13.560  31.715  1.00 62.86           C
ANISOU 2528  C   VAL A 303     6246   7330  10307   3579    385    989       C
ATOM   2529  O   VAL A 303      -0.418 -14.285  32.378  1.00 64.09           O
ANISOU 2529  O   VAL A 303     6338   7517  10498   3716    361   1118       O
ATOM   2530  CB  VAL A 303      -1.412 -11.735  33.472  1.00 63.32           C
ANISOU 2530  CB  VAL A 303     6174   7800  10085   3529     91   1066       C
ATOM   2531  CG1 VAL A 303      -2.438 -12.658  34.116  1.00 71.07           C
ANISOU 2531  CG1 VAL A 303     7316   8640  11050   3563    142   1220       C
ATOM   2532  CG2 VAL A 303      -0.074 -11.794  34.196  1.00 70.06           C
ANISOU 2532  CG2 VAL A 303     6851   8838  10932   3650    -15   1140       C
ATOM   2533  N   GLY A 304      -1.935 -14.038  30.733  1.00 66.39           N
ANISOU 2533  N   GLY A 304     6841   7549  10834   3502    529    898       N
ATOM   2534  CA  GLY A 304      -1.913 -15.442  30.364  1.00 69.16           C
ANISOU 2534  CA  GLY A 304     7283   7668  11327   3570    666    934       C
ATOM   2535  C   GLY A 304      -2.750 -16.356  31.230  1.00 77.00           C
ANISOU 2535  C   GLY A 304     8394   8532  12330   3609    687   1109       C
ATOM   2536  O   GLY A 304      -2.481 -17.561  31.276  1.00 76.08           O
ANISOU 2536  O   GLY A 304     8312   8263  12331   3704    772   1191       O
ATOM   2537  N   PHE A 305      -3.776 -15.823  31.901  1.00 79.23           N
ANISOU 2537  N   PHE A 305     8739   8868  12496   3536    621   1169       N
ATOM   2538  CA  PHE A 305      -4.520 -16.601  32.889  1.00 81.98           C
ANISOU 2538  CA  PHE A 305     9178   9137  12834   3579    631   1362       C
ATOM   2539  C   PHE A 305      -5.226 -17.799  32.266  1.00 78.40           C
ANISOU 2539  C   PHE A 305     8876   8377  12537   3545    795   1350       C
ATOM   2540  O   PHE A 305      -5.423 -18.816  32.938  1.00 81.21           O
ANISOU 2540  O   PHE A 305     9279   8626  12950   3621    840   1520       O
ATOM   2541  CB  PHE A 305      -5.525 -15.693  33.601  1.00 92.15           C
ANISOU 2541  CB  PHE A 305    10503  10551  13959   3495    535   1402       C
ATOM   2542  CG  PHE A 305      -6.425 -16.403  34.576  1.00101.18           C
ANISOU 2542  CG  PHE A 305    11745  11621  15077   3522    557   1597       C
ATOM   2543  CD1 PHE A 305      -5.979 -16.723  35.848  1.00107.84           C
ANISOU 2543  CD1 PHE A 305    12525  12605  15845   3653    482   1800       C
ATOM   2544  CD2 PHE A 305      -7.730 -16.720  34.229  1.00 99.96           C
ANISOU 2544  CD2 PHE A 305    11742  11270  14970   3409    653   1576       C
ATOM   2545  CE1 PHE A 305      -6.813 -17.363  36.750  1.00109.21           C
ANISOU 2545  CE1 PHE A 305    12786  12723  15988   3677    513   1989       C
ATOM   2546  CE2 PHE A 305      -8.566 -17.359  35.124  1.00100.55           C
ANISOU 2546  CE2 PHE A 305    11897  11280  15027   3427    681   1760       C
ATOM   2547  CZ  PHE A 305      -8.108 -17.681  36.386  1.00104.99           C
ANISOU 2547  CZ  PHE A 305    12397  11984  15511   3563    616   1972       C
ATOM   2548  N   PHE A 306      -5.607 -17.709  30.993  1.00 73.40           N
ANISOU 2548  N   PHE A 306     8314   7601  11972   3427    887   1151       N
ATOM   2549  CA  PHE A 306      -6.323 -18.807  30.356  1.00 73.15           C
ANISOU 2549  CA  PHE A 306     8425   7283  12086   3373   1034   1110       C
ATOM   2550  C   PHE A 306      -5.399 -19.880  29.806  1.00 79.07           C
ANISOU 2550  C   PHE A 306     9154   7897  12993   3474   1133   1085       C
ATOM   2551  O   PHE A 306      -5.888 -20.914  29.337  1.00 77.36           O
ANISOU 2551  O   PHE A 306     9046   7436  12912   3444   1254   1056       O
ATOM   2552  CB  PHE A 306      -7.222 -18.267  29.247  1.00 66.03           C
ANISOU 2552  CB  PHE A 306     7618   6296  11176   3194   1083    900       C
ATOM   2553  CG  PHE A 306      -8.271 -17.330  29.747  1.00 66.96           C
ANISOU 2553  CG  PHE A 306     7773   6509  11160   3092   1004    926       C
ATOM   2554  CD1 PHE A 306      -9.437 -17.817  30.308  1.00 57.10           C
ANISOU 2554  CD1 PHE A 306     6632   5138   9924   3042   1033   1034       C
ATOM   2555  CD2 PHE A 306      -8.080 -15.962  29.689  1.00 64.86           C
ANISOU 2555  CD2 PHE A 306     7427   6456  10762   3049    903    849       C
ATOM   2556  CE1 PHE A 306     -10.398 -16.959  30.783  1.00 63.40           C
ANISOU 2556  CE1 PHE A 306     7461   6030  10598   2956    964   1062       C
ATOM   2557  CE2 PHE A 306      -9.041 -15.096  30.164  1.00 61.59           C
ANISOU 2557  CE2 PHE A 306     7045   6129  10227   2963    830    873       C
ATOM   2558  CZ  PHE A 306     -10.203 -15.594  30.710  1.00 61.94           C
ANISOU 2558  CZ  PHE A 306     7201   6055  10277   2920    861    979       C
ATOM   2559  N   GLU A 307      -4.087 -19.660  29.847  1.00 90.15           N
ANISOU 2559  N   GLU A 307    10416   9452  14386   3589   1083   1089       N
ATOM   2560  CA  GLU A 307      -3.125 -20.721  29.587  1.00100.78           C
ANISOU 2560  CA  GLU A 307    11725  10692  15875   3719   1165   1111       C
ATOM   2561  C   GLU A 307      -2.753 -21.458  30.865  1.00111.68           C
ANISOU 2561  C   GLU A 307    13061  12096  17277   3874   1129   1365       C
ATOM   2562  O   GLU A 307      -2.653 -22.689  30.862  1.00114.47           O
ANISOU 2562  O   GLU A 307    13461  12254  17777   3950   1231   1438       O
ATOM   2563  CB  GLU A 307      -1.867 -20.149  28.928  1.00102.70           C
ANISOU 2563  CB  GLU A 307    11829  11085  16106   3767   1140    986       C
ATOM   2564  CG  GLU A 307      -1.856 -20.234  27.413  1.00105.66           C
ANISOU 2564  CG  GLU A 307    12259  11336  16551   3683   1258    750       C
ATOM   2565  CD  GLU A 307      -3.116 -19.672  26.784  1.00110.27           C
ANISOU 2565  CD  GLU A 307    12968  11855  17075   3494   1282    610       C
ATOM   2566  OE1 GLU A 307      -3.599 -20.270  25.802  1.00112.63           O
ANISOU 2566  OE1 GLU A 307    13380  11959  17457   3419   1399    469       O
ATOM   2567  OE2 GLU A 307      -3.619 -18.632  27.263  1.00112.08           O
ANISOU 2567  OE2 GLU A 307    13180  12232  17173   3421   1180    636       O
ATOM   2568  N   ARG A 308      -2.557 -20.721  31.963  1.00124.57           N
ANISOU 2568  N   ARG A 308    14601  13968  18760   3919    985   1498       N
ATOM   2569  CA  ARG A 308      -2.231 -21.357  33.236  1.00128.10           C
ANISOU 2569  CA  ARG A 308    15004  14470  19198   4065    943   1747       C
ATOM   2570  C   ARG A 308      -3.352 -22.283  33.688  1.00126.84           C
ANISOU 2570  C   ARG A 308    14988  14104  19100   4040   1031   1884       C
ATOM   2571  O   ARG A 308      -3.095 -23.335  34.288  1.00133.14           O
ANISOU 2571  O   ARG A 308    15787  14813  19986   4161   1082   2063       O
ATOM   2572  CB  ARG A 308      -1.947 -20.295  34.301  1.00133.63           C
ANISOU 2572  CB  ARG A 308    15590  15483  19701   4094    764   1837       C
ATOM   2573  CG  ARG A 308      -1.310 -19.018  33.770  1.00134.39           C
ANISOU 2573  CG  ARG A 308    15568  15780  19713   4038    669   1658       C
ATOM   2574  CD  ARG A 308       0.209 -19.119  33.709  1.00137.87           C
ANISOU 2574  CD  ARG A 308    15845  16336  20203   4169    633   1655       C
ATOM   2575  NE  ARG A 308       0.829 -18.917  35.016  1.00140.86           N
ANISOU 2575  NE  ARG A 308    16100  16948  20471   4281    491   1827       N
ATOM   2576  CZ  ARG A 308       1.011 -17.730  35.587  1.00141.01           C
ANISOU 2576  CZ  ARG A 308    16017  17232  20328   4243    331   1805       C
ATOM   2577  NH1 ARG A 308       0.620 -16.624  34.968  1.00138.54           N
ANISOU 2577  NH1 ARG A 308    15706  16977  19954   4098    298   1629       N
ATOM   2578  NH2 ARG A 308       1.586 -17.649  36.779  1.00143.37           N
ANISOU 2578  NH2 ARG A 308    16210  17740  20525   4347    205   1957       N
ATOM   2579  N   VAL A 309      -4.603 -21.911  33.409  1.00110.78           N
ANISOU 2579  N   VAL A 309    13070  11993  17029   3883   1054   1808       N
ATOM   2580  CA  VAL A 309      -5.727 -22.798  33.688  1.00102.87           C
ANISOU 2580  CA  VAL A 309    12202  10776  16109   3835   1153   1913       C
ATOM   2581  C   VAL A 309      -5.898 -23.845  32.591  1.00102.72           C
ANISOU 2581  C   VAL A 309    12275  10452  16302   3792   1314   1788       C
ATOM   2582  O   VAL A 309      -6.557 -24.869  32.814  1.00104.23           O
ANISOU 2582  O   VAL A 309    12555  10433  16614   3785   1414   1889       O
ATOM   2583  CB  VAL A 309      -7.006 -21.967  33.891  1.00 95.99           C
ANISOU 2583  CB  VAL A 309    11407   9956  15111   3685   1107   1888       C
ATOM   2584  CG1 VAL A 309      -8.161 -22.842  34.358  1.00 98.14           C
ANISOU 2584  CG1 VAL A 309    11797  10035  15456   3641   1200   2027       C
ATOM   2585  CG2 VAL A 309      -6.751 -20.859  34.904  1.00 91.26           C
ANISOU 2585  CG2 VAL A 309    10710   9673  14293   3729    941   1979       C
ATOM   2586  N   GLY A 310      -5.311 -23.626  31.415  1.00102.81           N
ANISOU 2586  N   GLY A 310    12263  10438  16361   3764   1344   1569       N
ATOM   2587  CA  GLY A 310      -5.218 -24.661  30.402  1.00106.60           C
ANISOU 2587  CA  GLY A 310    12809  10660  17033   3754   1488   1445       C
ATOM   2588  C   GLY A 310      -6.451 -24.859  29.543  1.00108.84           C
ANISOU 2588  C   GLY A 310    13237  10737  17380   3572   1577   1282       C
ATOM   2589  O   GLY A 310      -7.114 -25.896  29.629  1.00111.94           O
ANISOU 2589  O   GLY A 310    13720  10903  17910   3548   1674   1341       O
ATOM   2590  N   LEU A 311      -6.770 -23.872  28.707  1.00107.66           N
ANISOU 2590  N   LEU A 311    13105  10666  17135   3440   1544   1076       N
ATOM   2591  CA  LEU A 311      -7.880 -23.993  27.769  1.00105.83           C
ANISOU 2591  CA  LEU A 311    13001  10261  16951   3261   1619    892       C
ATOM   2592  C   LEU A 311      -7.577 -23.417  26.394  1.00102.67           C
ANISOU 2592  C   LEU A 311    12598   9896  16515   3181   1638    621       C
ATOM   2593  O   LEU A 311      -8.416 -23.556  25.498  1.00 98.87           O
ANISOU 2593  O   LEU A 311    12219   9280  16067   3034   1700    445       O
ATOM   2594  CB  LEU A 311      -9.145 -23.318  28.328  1.00102.36           C
ANISOU 2594  CB  LEU A 311    12617   9871  16401   3135   1558    950       C
ATOM   2595  CG  LEU A 311      -9.561 -23.698  29.752  1.00102.41           C
ANISOU 2595  CG  LEU A 311    12624   9886  16400   3202   1531   1227       C
ATOM   2596  CD1 LEU A 311      -9.034 -22.691  30.764  1.00 99.95           C
ANISOU 2596  CD1 LEU A 311    12205   9867  15905   3293   1389   1369       C
ATOM   2597  CD2 LEU A 311     -11.069 -23.853  29.870  1.00101.80           C
ANISOU 2597  CD2 LEU A 311    12659   9677  16343   3051   1569   1238       C
ATOM   2598  N   GLY A 312      -6.426 -22.785  26.191  1.00103.57           N
ANISOU 2598  N   GLY A 312    12597  10194  16562   3267   1589    581       N
ATOM   2599  CA  GLY A 312      -6.050 -22.220  24.914  1.00100.83           C
ANISOU 2599  CA  GLY A 312    12236   9902  16173   3203   1615    342       C
ATOM   2600  C   GLY A 312      -6.326 -20.725  24.829  1.00 99.15           C
ANISOU 2600  C   GLY A 312    11986   9902  15786   3103   1518    277       C
ATOM   2601  O   GLY A 312      -7.088 -20.149  25.617  1.00 98.17           O
ANISOU 2601  O   GLY A 312    11878   9847  15576   3050   1438    379       O
ATOM   2602  N   ARG A 313      -5.669 -20.089  23.842  1.00101.67           N
ANISOU 2602  N   ARG A 313    12249  10328  16054   3083   1530    105       N
ATOM   2603  CA  ARG A 313      -5.920 -18.681  23.540  1.00108.77           C
ANISOU 2603  CA  ARG A 313    13116  11409  16804   2975   1459     14       C
ATOM   2604  C   ARG A 313      -7.387 -18.450  23.194  1.00111.84           C
ANISOU 2604  C   ARG A 313    13639  11703  17152   2796   1471    -77       C
ATOM   2605  O   ARG A 313      -7.952 -17.393  23.480  1.00110.76           O
ANISOU 2605  O   ARG A 313    13494  11689  16901   2713   1391    -67       O
ATOM   2606  CB  ARG A 313      -5.016 -18.190  22.387  1.00114.75           C
ANISOU 2606  CB  ARG A 313    13801  12268  17529   2974   1502   -162       C
ATOM   2607  CG  ARG A 313      -5.356 -18.636  20.936  1.00120.72           C
ANISOU 2607  CG  ARG A 313    14662  12889  18317   2877   1622   -390       C
ATOM   2608  CD  ARG A 313      -5.625 -20.132  20.796  1.00127.92           C
ANISOU 2608  CD  ARG A 313    15674  13551  19379   2911   1718   -398       C
ATOM   2609  NE  ARG A 313      -5.744 -20.572  19.406  1.00132.33           N
ANISOU 2609  NE  ARG A 313    16310  14008  19960   2841   1824   -626       N
ATOM   2610  CZ  ARG A 313      -6.329 -21.712  19.061  1.00136.20           C
ANISOU 2610  CZ  ARG A 313    16914  14273  20563   2808   1904   -692       C
ATOM   2611  NH1 ARG A 313      -6.853 -22.475  20.009  1.00138.76           N
ANISOU 2611  NH1 ARG A 313    17282  14449  20991   2834   1896   -536       N
ATOM   2612  NH2 ARG A 313      -6.422 -22.075  17.791  1.00137.41           N
ANISOU 2612  NH2 ARG A 313    17133  14356  20722   2746   1990   -912       N
ATOM   2613  N   LYS A 314      -8.021 -19.443  22.590  1.00113.59           N
ANISOU 2613  N   LYS A 314    13980  11708  17472   2734   1567   -168       N
ATOM   2614  CA  LYS A 314      -9.460 -19.474  22.380  1.00113.71           C
ANISOU 2614  CA  LYS A 314    14121  11608  17476   2570   1579   -235       C
ATOM   2615  C   LYS A 314     -10.223 -19.606  23.692  1.00111.86           C
ANISOU 2615  C   LYS A 314    13911  11340  17251   2577   1523    -24       C
ATOM   2616  O   LYS A 314     -11.454 -19.490  23.701  1.00111.80           O
ANISOU 2616  O   LYS A 314    13992  11265  17224   2443   1518    -51       O
ATOM   2617  CB  LYS A 314      -9.785 -20.643  21.427  1.00117.95           C
ANISOU 2617  CB  LYS A 314    14760  11922  18134   2517   1695   -387       C
ATOM   2618  CG  LYS A 314     -11.218 -20.744  20.953  1.00118.50           C
ANISOU 2618  CG  LYS A 314    14952  11874  18199   2332   1713   -506       C
ATOM   2619  CD  LYS A 314     -11.730 -22.171  21.077  1.00121.44           C
ANISOU 2619  CD  LYS A 314    15405  11992  18743   2327   1793   -478       C
ATOM   2620  CE  LYS A 314     -11.774 -22.604  22.524  1.00123.19           C
ANISOU 2620  CE  LYS A 314    15601  12169  19035   2427   1767   -205       C
ATOM   2621  NZ  LYS A 314     -12.420 -21.581  23.379  1.00121.39           N
ANISOU 2621  NZ  LYS A 314    15357  12084  18682   2379   1667    -82       N
ATOM   2622  N   GLY A 315      -9.512 -19.834  24.797  1.00109.11           N
ANISOU 2622  N   GLY A 315    13482  11054  16923   2733   1480    187       N
ATOM   2623  CA  GLY A 315     -10.173 -20.008  26.079  1.00103.77           C
ANISOU 2623  CA  GLY A 315    12823  10363  16240   2756   1433    404       C
ATOM   2624  C   GLY A 315     -10.870 -18.752  26.566  1.00 96.16           C
ANISOU 2624  C   GLY A 315    11850   9565  15122   2675   1330    435       C
ATOM   2625  O   GLY A 315     -12.001 -18.813  27.054  1.00 97.37           O
ANISOU 2625  O   GLY A 315    12077   9652  15265   2596   1324    506       O
ATOM   2626  N   MET A 316     -10.206 -17.599  26.457  1.00 88.97           N
ANISOU 2626  N   MET A 316    10843   8869  14094   2695   1250    385       N
ATOM   2627  CA  MET A 316     -10.842 -16.354  26.882  1.00 80.80           C
ANISOU 2627  CA  MET A 316     9793   7990  12917   2620   1152    402       C
ATOM   2628  C   MET A 316     -12.167 -16.093  26.174  1.00 77.19           C
ANISOU 2628  C   MET A 316     9453   7430  12447   2435   1188    260       C
ATOM   2629  O   MET A 316     -13.108 -15.630  26.844  1.00 75.33           O
ANISOU 2629  O   MET A 316     9251   7227  12145   2379   1136    342       O
ATOM   2630  CB  MET A 316      -9.884 -15.171  26.690  1.00 76.49           C
ANISOU 2630  CB  MET A 316     9118   7674  12272   2654   1073    340       C
ATOM   2631  CG  MET A 316     -10.432 -13.851  27.216  1.00 75.01           C
ANISOU 2631  CG  MET A 316     8899   7659  11944   2593    964    365       C
ATOM   2632  SD  MET A 316     -10.339 -12.503  26.020  1.00 76.08           S
ANISOU 2632  SD  MET A 316     8993   7904  12010   2466    957    139       S
ATOM   2633  CE  MET A 316     -11.682 -12.929  24.925  1.00 75.27           C
ANISOU 2633  CE  MET A 316     9063   7584  11951   2287   1061    -30       C
ATOM   2634  N   PRO A 317     -12.314 -16.330  24.859  1.00 72.98           N
ANISOU 2634  N   PRO A 317     8980   6789  11961   2335   1270     48       N
ATOM   2635  CA  PRO A 317     -13.646 -16.253  24.245  1.00 75.47           C
ANISOU 2635  CA  PRO A 317     9409   6999  12268   2156   1300    -80       C
ATOM   2636  C   PRO A 317     -14.692 -17.100  24.949  1.00 83.37           C
ANISOU 2636  C   PRO A 317    10493   7838  13346   2122   1326     44       C
ATOM   2637  O   PRO A 317     -15.720 -16.573  25.394  1.00 84.68           O
ANISOU 2637  O   PRO A 317    10695   8027  13452   2036   1282     89       O
ATOM   2638  CB  PRO A 317     -13.392 -16.750  22.820  1.00 72.68           C
ANISOU 2638  CB  PRO A 317     9097   6551  11966   2096   1390   -302       C
ATOM   2639  CG  PRO A 317     -12.032 -16.269  22.531  1.00 72.37           C
ANISOU 2639  CG  PRO A 317     8948   6661  11888   2201   1378   -330       C
ATOM   2640  CD  PRO A 317     -11.261 -16.372  23.826  1.00 72.54           C
ANISOU 2640  CD  PRO A 317     8875   6761  11925   2369   1320   -101       C
ATOM   2641  N   LEU A 318     -14.446 -18.406  25.064  1.00 92.32           N
ANISOU 2641  N   LEU A 318    11653   8805  14620   2188   1403    104       N
ATOM   2642  CA  LEU A 318     -15.465 -19.276  25.642  1.00 94.28           C
ANISOU 2642  CA  LEU A 318    11976   8883  14962   2142   1445    215       C
ATOM   2643  C   LEU A 318     -15.761 -18.899  27.089  1.00 92.85           C
ANISOU 2643  C   LEU A 318    11761   8807  14710   2210   1373    463       C
ATOM   2644  O   LEU A 318     -16.925 -18.919  27.508  1.00 95.36           O
ANISOU 2644  O   LEU A 318    12136   9068  15026   2119   1375    525       O
ATOM   2645  CB  LEU A 318     -15.054 -20.743  25.527  1.00101.13           C
ANISOU 2645  CB  LEU A 318    12866   9552  16005   2212   1545    243       C
ATOM   2646  CG  LEU A 318     -15.514 -21.395  24.224  1.00108.58           C
ANISOU 2646  CG  LEU A 318    13891  10322  17041   2082   1629      5       C
ATOM   2647  CD1 LEU A 318     -15.131 -22.853  24.199  1.00113.50           C
ANISOU 2647  CD1 LEU A 318    14535  10740  17851   2158   1729     42       C
ATOM   2648  CD2 LEU A 318     -17.005 -21.271  24.046  1.00109.57           C
ANISOU 2648  CD2 LEU A 318    14097  10376  17159   1897   1627    -62       C
ATOM   2649  N   ALA A 319     -14.734 -18.527  27.858  1.00 84.09           N
ANISOU 2649  N   ALA A 319    10553   7866  13530   2367   1306    602       N
ATOM   2650  CA  ALA A 319     -14.979 -17.949  29.177  1.00 74.06           C
ANISOU 2650  CA  ALA A 319     9243   6752  12144   2429   1217    811       C
ATOM   2651  C   ALA A 319     -15.989 -16.813  29.084  1.00 70.85           C
ANISOU 2651  C   ALA A 319     8867   6431  11620   2298   1159    739       C
ATOM   2652  O   ALA A 319     -17.017 -16.818  29.773  1.00 77.33           O
ANISOU 2652  O   ALA A 319     9735   7231  12416   2251   1153    853       O
ATOM   2653  CB  ALA A 319     -13.668 -17.458  29.783  1.00 73.44           C
ANISOU 2653  CB  ALA A 319     9039   6888  11978   2593   1129    905       C
ATOM   2654  N   VAL A 320     -15.717 -15.839  28.210  1.00 69.01           N
ANISOU 2654  N   VAL A 320     8607   6295  11319   2236   1124    551       N
ATOM   2655  CA  VAL A 320     -16.693 -14.789  27.922  1.00 68.16           C
ANISOU 2655  CA  VAL A 320     8534   6245  11119   2098   1082    453       C
ATOM   2656  C   VAL A 320     -18.064 -15.407  27.677  1.00 71.83           C
ANISOU 2656  C   VAL A 320     9112   6519  11661   1955   1150    420       C
ATOM   2657  O   VAL A 320     -19.044 -15.086  28.365  1.00 70.59           O
ANISOU 2657  O   VAL A 320     8984   6383  11454   1909   1121    520       O
ATOM   2658  CB  VAL A 320     -16.228 -13.942  26.722  1.00 64.31           C
ANISOU 2658  CB  VAL A 320     8017   5832  10588   2030   1072    225       C
ATOM   2659  CG1 VAL A 320     -17.418 -13.349  25.983  1.00 64.27           C
ANISOU 2659  CG1 VAL A 320     8091   5830  10499   1816   1054     62       C
ATOM   2660  CG2 VAL A 320     -15.291 -12.842  27.184  1.00 61.06           C
ANISOU 2660  CG2 VAL A 320     7488   5691  10024   2098    951    264       C
ATOM   2661  N   ILE A 321     -18.127 -16.368  26.751  1.00 73.60           N
ANISOU 2661  N   ILE A 321     9394   6559  12011   1890   1242    287       N
ATOM   2662  CA  ILE A 321     -19.404 -16.958  26.359  1.00 72.41           C
ANISOU 2662  CA  ILE A 321     9339   6234  11941   1734   1301    217       C
ATOM   2663  C   ILE A 321     -20.126 -17.539  27.569  1.00 74.23           C
ANISOU 2663  C   ILE A 321     9589   6397  12218   1762   1317    450       C
ATOM   2664  O   ILE A 321     -21.354 -17.420  27.687  1.00 71.57           O
ANISOU 2664  O   ILE A 321     9302   6012  11880   1639   1321    454       O
ATOM   2665  CB  ILE A 321     -19.187 -18.009  25.252  1.00 77.09           C
ANISOU 2665  CB  ILE A 321     9976   6653  12663   1685   1392     46       C
ATOM   2666  CG1 ILE A 321     -18.779 -17.317  23.948  1.00 73.72           C
ANISOU 2666  CG1 ILE A 321     9541   6311  12157   1619   1379   -203       C
ATOM   2667  CG2 ILE A 321     -20.443 -18.831  25.033  1.00 78.39           C
ANISOU 2667  CG2 ILE A 321    10221   6629  12935   1541   1452      4       C
ATOM   2668  CD1 ILE A 321     -18.552 -18.261  22.783  1.00 71.04           C
ANISOU 2668  CD1 ILE A 321     9246   5834  11914   1575   1462   -390       C
ATOM   2669  N   VAL A 322     -19.387 -18.136  28.510  1.00 71.89           N
ANISOU 2669  N   VAL A 322     9248   6112  11955   1925   1326    655       N
ATOM   2670  CA  VAL A 322     -20.082 -18.684  29.671  1.00 74.68           C
ANISOU 2670  CA  VAL A 322     9619   6419  12338   1953   1348    888       C
ATOM   2671  C   VAL A 322     -20.363 -17.586  30.688  1.00 84.43           C
ANISOU 2671  C   VAL A 322    10816   7869  13395   1997   1250   1033       C
ATOM   2672  O   VAL A 322     -21.456 -17.528  31.263  1.00 88.42           O
ANISOU 2672  O   VAL A 322    11356   8360  13879   1932   1257   1134       O
ATOM   2673  CB  VAL A 322     -19.307 -19.865  30.291  1.00 74.29           C
ANISOU 2673  CB  VAL A 322     9543   6287  12397   2100   1406   1060       C
ATOM   2674  CG1 VAL A 322     -19.192 -21.008  29.292  1.00 74.22           C
ANISOU 2674  CG1 VAL A 322     9580   6044  12576   2047   1511    912       C
ATOM   2675  CG2 VAL A 322     -17.942 -19.451  30.791  1.00 75.12           C
ANISOU 2675  CG2 VAL A 322     9556   6582  12405   2280   1333   1147       C
ATOM   2676  N   LEU A 323     -19.415 -16.664  30.889  1.00 86.89           N
ANISOU 2676  N   LEU A 323    11050   8390  13574   2101   1157   1034       N
ATOM   2677  CA  LEU A 323     -19.628 -15.644  31.905  1.00 87.32           C
ANISOU 2677  CA  LEU A 323    11062   8665  13450   2155   1055   1168       C
ATOM   2678  C   LEU A 323     -20.733 -14.694  31.489  1.00 89.56           C
ANISOU 2678  C   LEU A 323    11390   8989  13648   1988   1019   1040       C
ATOM   2679  O   LEU A 323     -21.300 -14.000  32.337  1.00 89.68           O
ANISOU 2679  O   LEU A 323    11396   9181  13497   1969    939   1134       O
ATOM   2680  CB  LEU A 323     -18.330 -14.885  32.185  1.00 89.67           C
ANISOU 2680  CB  LEU A 323    11254   9189  13628   2292    953   1177       C
ATOM   2681  CG  LEU A 323     -17.227 -15.703  32.868  1.00 93.48           C
ANISOU 2681  CG  LEU A 323    11675   9703  14140   2460    955   1333       C
ATOM   2682  CD1 LEU A 323     -16.366 -14.819  33.758  1.00 92.78           C
ANISOU 2682  CD1 LEU A 323    11475   9905  13871   2591    819   1424       C
ATOM   2683  CD2 LEU A 323     -17.793 -16.878  33.667  1.00 94.59           C
ANISOU 2683  CD2 LEU A 323    11866   9714  14360   2489   1033   1535       C
ATOM   2684  N   THR A 324     -21.038 -14.652  30.193  1.00 95.60           N
ANISOU 2684  N   THR A 324    12202   9645  14478   1838   1055    805       N
ATOM   2685  CA  THR A 324     -22.294 -14.120  29.681  1.00 96.28           C
ANISOU 2685  CA  THR A 324    12345   9738  14498   1633   1033    672       C
ATOM   2686  C   THR A 324     -23.437 -14.928  30.264  1.00 89.43           C
ANISOU 2686  C   THR A 324    11534   8708  13738   1594   1112    815       C
ATOM   2687  O   THR A 324     -24.135 -14.467  31.176  1.00 88.18           O
ANISOU 2687  O   THR A 324    11370   8677  13456   1581   1062    947       O
ATOM   2688  CB  THR A 324     -22.345 -14.196  28.144  1.00 99.89           C
ANISOU 2688  CB  THR A 324    12842  10081  15030   1501   1076    405       C
ATOM   2689  OG1 THR A 324     -21.197 -13.549  27.577  1.00100.95           O
ANISOU 2689  OG1 THR A 324    12919  10352  15087   1549   1025    289       O
ATOM   2690  CG2 THR A 324     -23.625 -13.549  27.599  1.00 95.52           C
ANISOU 2690  CG2 THR A 324    12335   9571  14388   1294   1036    269       C
ATOM   2691  N   ALA A 325     -23.579 -16.161  29.757  1.00 88.44           N
ANISOU 2691  N   ALA A 325    11454   8314  13835   1572   1234    785       N
ATOM   2692  CA  ALA A 325     -24.726 -16.995  30.094  1.00 86.71           C
ANISOU 2692  CA  ALA A 325    11282   7942  13721   1481   1307    875       C
ATOM   2693  C   ALA A 325     -24.901 -17.143  31.599  1.00 92.36           C
ANISOU 2693  C   ALA A 325    11973   8739  14381   1598   1304   1173       C
ATOM   2694  O   ALA A 325     -26.018 -17.373  32.075  1.00 96.21           O
ANISOU 2694  O   ALA A 325    12485   9173  14895   1520   1343   1274       O
ATOM   2695  CB  ALA A 325     -24.589 -18.368  29.441  1.00 82.53           C
ANISOU 2695  CB  ALA A 325    10784   7191  13382   1440   1405    795       C
ATOM   2696  N   LEU A 326     -23.818 -17.009  32.364  1.00 92.21           N
ANISOU 2696  N   LEU A 326    11897   8866  14274   1781   1257   1315       N
ATOM   2697  CA  LEU A 326     -23.939 -17.002  33.817  1.00 93.23           C
ANISOU 2697  CA  LEU A 326    11995   9130  14297   1899   1235   1589       C
ATOM   2698  C   LEU A 326     -24.475 -15.662  34.310  1.00 94.69           C
ANISOU 2698  C   LEU A 326    12165   9528  14284   1890   1140   1616       C
ATOM   2699  O   LEU A 326     -25.575 -15.587  34.872  1.00 88.72           O
ANISOU 2699  O   LEU A 326    11434   8794  13483   1822   1156   1713       O
ATOM   2700  CB  LEU A 326     -22.585 -17.310  34.462  1.00 90.32           C
ANISOU 2700  CB  LEU A 326    11563   8870  13885   2094   1203   1718       C
ATOM   2701  CG  LEU A 326     -22.189 -18.774  34.687  1.00 92.36           C
ANISOU 2701  CG  LEU A 326    11826   8960  14308   2160   1303   1835       C
ATOM   2702  CD1 LEU A 326     -22.668 -19.692  33.562  1.00 93.51           C
ANISOU 2702  CD1 LEU A 326    12033   8820  14675   2016   1412   1668       C
ATOM   2703  CD2 LEU A 326     -20.680 -18.885  34.867  1.00 92.59           C
ANISOU 2703  CD2 LEU A 326    11786   9090  14306   2330   1257   1870       C
ATOM   2704  N   ILE A 327     -23.713 -14.588  34.082  1.00101.62           N
ANISOU 2704  N   ILE A 327    12994  10629  14987   1905   1015   1482       N
ATOM   2705  CA  ILE A 327     -24.066 -13.281  34.636  1.00107.39           C
ANISOU 2705  CA  ILE A 327    13697  11644  15462   1865    885   1463       C
ATOM   2706  C   ILE A 327     -25.444 -12.855  34.154  1.00106.63           C
ANISOU 2706  C   ILE A 327    13654  11517  15342   1660    890   1344       C
ATOM   2707  O   ILE A 327     -26.284 -12.407  34.943  1.00106.97           O
ANISOU 2707  O   ILE A 327    13700  11685  15260   1635    861   1440       O
ATOM   2708  CB  ILE A 327     -22.998 -12.233  34.278  1.00110.61           C
ANISOU 2708  CB  ILE A 327    14042  12254  15732   1891    762   1309       C
ATOM   2709  CG1 ILE A 327     -21.758 -12.413  35.156  1.00108.53           C
ANISOU 2709  CG1 ILE A 327    13700  12111  15424   2107    721   1468       C
ATOM   2710  CG2 ILE A 327     -23.561 -10.823  34.418  1.00111.48           C
ANISOU 2710  CG2 ILE A 327    14141  12591  15624   1785    643   1206       C
ATOM   2711  CD1 ILE A 327     -20.650 -11.438  34.839  1.00105.36           C
ANISOU 2711  CD1 ILE A 327    13220  11900  14911   2133    603   1324       C
ATOM   2712  N   MET A 328     -25.695 -12.982  32.850  1.00105.61           N
ANISOU 2712  N   MET A 328    13563  11237  15326   1515    926   1131       N
ATOM   2713  CA  MET A 328     -27.052 -12.819  32.349  1.00106.57           C
ANISOU 2713  CA  MET A 328    13731  11297  15465   1324    946   1032       C
ATOM   2714  C   MET A 328     -28.006 -13.721  33.119  1.00107.38           C
ANISOU 2714  C   MET A 328    13860  11261  15678   1325   1047   1233       C
ATOM   2715  O   MET A 328     -28.875 -13.242  33.849  1.00103.50           O
ANISOU 2715  O   MET A 328    13364  10894  15068   1292   1021   1328       O
ATOM   2716  CB  MET A 328     -27.101 -13.120  30.850  1.00108.41           C
ANISOU 2716  CB  MET A 328    14001  11361  15831   1192    988    792       C
ATOM   2717  CG  MET A 328     -28.506 -13.161  30.276  1.00109.90           C
ANISOU 2717  CG  MET A 328    14230  11461  16067    997   1016    691       C
ATOM   2718  SD  MET A 328     -28.589 -14.088  28.733  1.00112.49           S
ANISOU 2718  SD  MET A 328    14606  11521  16614    874   1105    458       S
ATOM   2719  CE  MET A 328     -28.202 -15.740  29.306  1.00115.21           C
ANISOU 2719  CE  MET A 328    14969  11578  17227   1003   1255    644       C
ATOM   2720  N   GLY A 329     -27.799 -15.037  33.023  1.00112.57           N
ANISOU 2720  N   GLY A 329    14541  11662  16567   1375   1171   1314       N
ATOM   2721  CA  GLY A 329     -28.740 -15.978  33.616  1.00114.51           C
ANISOU 2721  CA  GLY A 329    14812  11735  16961   1355   1286   1499       C
ATOM   2722  C   GLY A 329     -28.970 -15.742  35.095  1.00115.14           C
ANISOU 2722  C   GLY A 329    14863  11992  16893   1472   1270   1768       C
ATOM   2723  O   GLY A 329     -30.112 -15.636  35.550  1.00113.22           O
ANISOU 2723  O   GLY A 329    14626  11774  16618   1390   1295   1850       O
ATOM   2724  N   LEU A 330     -27.889 -15.638  35.866  1.00116.87           N
ANISOU 2724  N   LEU A 330    15043  12352  17010   1669   1225   1908       N
ATOM   2725  CA  LEU A 330     -28.011 -15.443  37.305  1.00114.30           C
ANISOU 2725  CA  LEU A 330    14687  12219  16523   1802   1205   2165       C
ATOM   2726  C   LEU A 330     -28.304 -13.994  37.683  1.00113.17           C
ANISOU 2726  C   LEU A 330    14517  12391  16091   1764   1066   2084       C
ATOM   2727  O   LEU A 330     -28.189 -13.635  38.860  1.00115.79           O
ANISOU 2727  O   LEU A 330    14817  12938  16240   1892   1021   2256       O
ATOM   2728  CB  LEU A 330     -26.753 -15.948  38.016  1.00110.97           C
ANISOU 2728  CB  LEU A 330    14222  11875  16068   2001   1191   2314       C
ATOM   2729  CG  LEU A 330     -26.939 -17.347  38.622  1.00107.54           C
ANISOU 2729  CG  LEU A 330    13792  11302  15767   2031   1312   2508       C
ATOM   2730  CD1 LEU A 330     -27.289 -18.382  37.554  1.00104.90           C
ANISOU 2730  CD1 LEU A 330    13501  10646  15709   1891   1424   2379       C
ATOM   2731  CD2 LEU A 330     -25.713 -17.780  39.404  1.00107.52           C
ANISOU 2731  CD2 LEU A 330    13738  11415  15699   2222   1286   2656       C
ATOM   2732  N   PHE A 331     -28.690 -13.163  36.721  1.00110.48           N
ANISOU 2732  N   PHE A 331    14189  12083  15705   1597   1000   1828       N
ATOM   2733  CA  PHE A 331     -29.405 -11.933  37.030  1.00109.00           C
ANISOU 2733  CA  PHE A 331    13989  12126  15299   1522    906   1763       C
ATOM   2734  C   PHE A 331     -30.863 -12.207  37.361  1.00113.09           C
ANISOU 2734  C   PHE A 331    14530  12581  15858   1421    988   1859       C
ATOM   2735  O   PHE A 331     -31.697 -11.296  37.462  1.00111.09           O
ANISOU 2735  O   PHE A 331    14271  12474  15465   1331    933   1792       O
ATOM   2736  CB  PHE A 331     -29.295 -10.945  35.867  1.00103.24           C
ANISOU 2736  CB  PHE A 331    13260  11449  14517   1388    813   1474       C
ATOM   2737  CG  PHE A 331     -28.225  -9.901  36.052  1.00102.08           C
ANISOU 2737  CG  PHE A 331    13066  11532  14187   1475    680   1396       C
ATOM   2738  CD1 PHE A 331     -27.089 -10.171  36.800  1.00103.40           C
ANISOU 2738  CD1 PHE A 331    13192  11779  14317   1662    657   1528       C
ATOM   2739  CD2 PHE A 331     -28.361  -8.646  35.481  1.00100.40           C
ANISOU 2739  CD2 PHE A 331    12844  11455  13850   1370    579   1195       C
ATOM   2740  CE1 PHE A 331     -26.105  -9.211  36.967  1.00103.52           C
ANISOU 2740  CE1 PHE A 331    13150  12005  14176   1731    530   1445       C
ATOM   2741  CE2 PHE A 331     -27.382  -7.681  35.647  1.00101.81           C
ANISOU 2741  CE2 PHE A 331    12972  11829  13884   1438    462   1120       C
ATOM   2742  CZ  PHE A 331     -26.254  -7.963  36.390  1.00102.40           C
ANISOU 2742  CZ  PHE A 331    13000  11982  13925   1613    436   1238       C
ATOM   2743  N   PHE A 332     -31.144 -13.502  37.524  1.00118.06           N
ANISOU 2743  N   PHE A 332    15181  12979  16697   1440   1126   2022       N
ATOM   2744  CA  PHE A 332     -32.435 -14.028  37.955  1.00121.53           C
ANISOU 2744  CA  PHE A 332    15631  13324  17220   1363   1232   2166       C
ATOM   2745  C   PHE A 332     -32.727 -13.575  39.382  1.00119.75           C
ANISOU 2745  C   PHE A 332    15378  13344  16779   1482   1215   2385       C
ATOM   2746  O   PHE A 332     -33.737 -13.968  39.977  1.00123.27           O
ANISOU 2746  O   PHE A 332    15821  13754  17261   1453   1308   2552       O
ATOM   2747  CB  PHE A 332     -32.437 -15.559  37.836  1.00128.48           C
ANISOU 2747  CB  PHE A 332    16535  13885  18396   1378   1388   2302       C
ATOM   2748  CG  PHE A 332     -33.718 -16.221  38.281  1.00133.05           C
ANISOU 2748  CG  PHE A 332    17117  14335  19101   1296   1515   2469       C
ATOM   2749  CD1 PHE A 332     -34.911 -15.999  37.607  1.00134.60           C
ANISOU 2749  CD1 PHE A 332    17315  14470  19357   1085   1524   2317       C
ATOM   2750  CD2 PHE A 332     -33.724 -17.078  39.370  1.00136.43           C
ANISOU 2750  CD2 PHE A 332    17521  14777  19539   1399   1597   2720       C
ATOM   2751  CE1 PHE A 332     -36.086 -16.617  38.021  1.00136.88           C
ANISOU 2751  CE1 PHE A 332    17591  14640  19775   1004   1644   2473       C
ATOM   2752  CE2 PHE A 332     -34.893 -17.698  39.788  1.00139.01           C
ANISOU 2752  CE2 PHE A 332    17830  15027  19960   1306   1705   2842       C
ATOM   2753  CZ  PHE A 332     -36.075 -17.467  39.113  1.00138.17           C
ANISOU 2753  CZ  PHE A 332    17728  14824  19945   1108   1728   2717       C
ATOM   2754  N   VAL A 333     -31.837 -12.746  39.936  1.00112.66           N
ANISOU 2754  N   VAL A 333    14452  12701  15653   1617   1096   2379       N
ATOM   2755  CA  VAL A 333     -32.065 -12.114  41.232  1.00104.33           C
ANISOU 2755  CA  VAL A 333    13369  11923  14349   1727   1053   2531       C
ATOM   2756  C   VAL A 333     -33.398 -11.380  41.252  1.00103.20           C
ANISOU 2756  C   VAL A 333    13226  11868  14117   1587   1048   2462       C
ATOM   2757  O   VAL A 333     -34.044 -11.277  42.302  1.00106.35           O
ANISOU 2757  O   VAL A 333    13611  12408  14390   1645   1085   2638       O
ATOM   2758  CB  VAL A 333     -30.884 -11.177  41.574  1.00 92.06           C
ANISOU 2758  CB  VAL A 333    11779  10626  12574   1854    900   2450       C
ATOM   2759  CG1 VAL A 333     -30.971  -9.867  40.796  1.00 85.37           C
ANISOU 2759  CG1 VAL A 333    10927   9888  11621   1723    776   2158       C
ATOM   2760  CG2 VAL A 333     -30.826 -10.911  43.068  1.00 89.83           C
ANISOU 2760  CG2 VAL A 333    11465  10608  12057   2025    873   2659       C
ATOM   2761  N   ILE A 334     -33.838 -10.871  40.104  1.00 99.49           N
ANISOU 2761  N   ILE A 334    12768  11324  13708   1407   1008   2214       N
ATOM   2762  CA  ILE A 334     -35.151 -10.244  39.980  1.00 96.95           C
ANISOU 2762  CA  ILE A 334    12442  11060  13337   1265   1010   2142       C
ATOM   2763  C   ILE A 334     -35.687 -10.558  38.589  1.00 88.32           C
ANISOU 2763  C   ILE A 334    11367   9738  12452   1067   1040   1955       C
ATOM   2764  O   ILE A 334     -34.976 -10.427  37.588  1.00 85.72           O
ANISOU 2764  O   ILE A 334    11053   9339  12178   1025    982   1765       O
ATOM   2765  CB  ILE A 334     -35.098  -8.723  40.271  1.00100.40           C
ANISOU 2765  CB  ILE A 334    12856  11783  13507   1284    872   2010       C
ATOM   2766  CG1 ILE A 334     -36.494  -8.160  40.552  1.00 95.81           C
ANISOU 2766  CG1 ILE A 334    12260  11293  12851   1192    895   2015       C
ATOM   2767  CG2 ILE A 334     -34.413  -7.939  39.161  1.00101.14           C
ANISOU 2767  CG2 ILE A 334    12955  11882  13591   1212    757   1742       C
ATOM   2768  CD1 ILE A 334     -36.496  -7.058  41.592  1.00 93.05           C
ANISOU 2768  CD1 ILE A 334    11887  11242  12224   1298    815   2034       C
ATOM   2769  N   SER A 335     -36.926 -11.025  38.534  1.00 78.92           N
ANISOU 2769  N   SER A 335    10171   8434  11381    948   1135   2013       N
ATOM   2770  CA  SER A 335     -37.540 -11.442  37.281  1.00 72.30           C
ANISOU 2770  CA  SER A 335     9342   7380  10747    757   1169   1845       C
ATOM   2771  C   SER A 335     -38.259 -10.300  36.564  1.00 71.33           C
ANISOU 2771  C   SER A 335     9202   7381  10520    617   1074   1629       C
ATOM   2772  O   SER A 335     -38.361 -10.338  35.332  1.00 68.09           O
ANISOU 2772  O   SER A 335     8802   6854  10215    482   1049   1427       O
ATOM   2773  CB  SER A 335     -38.510 -12.600  37.529  1.00 73.80           C
ANISOU 2773  CB  SER A 335     9523   7366  11153    686   1321   2011       C
ATOM   2774  OG  SER A 335     -37.857 -13.678  38.176  1.00 73.60           O
ANISOU 2774  OG  SER A 335     9515   7210  11241    821   1419   2229       O
ATOM   2775  N   PRO A 336     -38.810  -9.298  37.270  1.00 75.05           N
ANISOU 2775  N   PRO A 336     9645   8082  10789    644   1025   1665       N
ATOM   2776  CA  PRO A 336     -39.335  -8.121  36.551  1.00 72.19           C
ANISOU 2776  CA  PRO A 336     9266   7839  10324    532    926   1456       C
ATOM   2777  C   PRO A 336     -38.330  -7.454  35.622  1.00 67.30           C
ANISOU 2777  C   PRO A 336     8669   7251   9652    528    813   1243       C
ATOM   2778  O   PRO A 336     -38.681  -7.098  34.486  1.00 69.84           O
ANISOU 2778  O   PRO A 336     8988   7532  10014    393    769   1055       O
ATOM   2779  CB  PRO A 336     -39.762  -7.194  37.694  1.00 74.80           C
ANISOU 2779  CB  PRO A 336     9568   8417  10434    621    897   1553       C
ATOM   2780  CG  PRO A 336     -40.214  -8.119  38.750  1.00 78.09           C
ANISOU 2780  CG  PRO A 336     9974   8793  10905    687   1024   1812       C
ATOM   2781  CD  PRO A 336     -39.355  -9.361  38.642  1.00 79.11           C
ANISOU 2781  CD  PRO A 336    10135   8718  11206    741   1091   1903       C
ATOM   2782  N   ASP A 337     -37.094  -7.247  36.084  1.00 67.28           N
ANISOU 2782  N   ASP A 337     8678   7332   9552    675    763   1273       N
ATOM   2783  CA  ASP A 337     -36.079  -6.663  35.214  1.00 67.12           C
ANISOU 2783  CA  ASP A 337     8669   7335   9497    672    667   1084       C
ATOM   2784  C   ASP A 337     -35.867  -7.527  33.980  1.00 59.47           C
ANISOU 2784  C   ASP A 337     7726   6139   8728    575    712    971       C
ATOM   2785  O   ASP A 337     -35.793  -7.014  32.859  1.00 60.97           O
ANISOU 2785  O   ASP A 337     7922   6326   8918    479    654    774       O
ATOM   2786  CB  ASP A 337     -34.765  -6.475  35.976  1.00 69.76           C
ANISOU 2786  CB  ASP A 337     9000   7785   9722    848    617   1152       C
ATOM   2787  CG  ASP A 337     -33.804  -5.526  35.266  1.00 72.99           C
ANISOU 2787  CG  ASP A 337     9401   8278  10053    846    504    962       C
ATOM   2788  OD1 ASP A 337     -33.937  -4.294  35.434  1.00 73.72           O
ANISOU 2788  OD1 ASP A 337     9475   8546   9990    840    416    882       O
ATOM   2789  OD2 ASP A 337     -32.910  -6.013  34.542  1.00 71.59           O
ANISOU 2789  OD2 ASP A 337     9236   7987   9979    854    511    894       O
ATOM   2790  N   PHE A 338     -35.807  -8.845  34.165  1.00 57.83           N
ANISOU 2790  N   PHE A 338     7535   5740   8696    600    820   1093       N
ATOM   2791  CA  PHE A 338     -35.620  -9.754  33.039  1.00 62.20           C
ANISOU 2791  CA  PHE A 338     8116   6062   9455    513    873    977       C
ATOM   2792  C   PHE A 338     -36.774  -9.669  32.048  1.00 63.62           C
ANISOU 2792  C   PHE A 338     8291   6179   9704    317    873    822       C
ATOM   2793  O   PHE A 338     -36.561  -9.644  30.829  1.00 59.54           O
ANISOU 2793  O   PHE A 338     7789   5597   9237    227    843    622       O
ATOM   2794  CB  PHE A 338     -35.476 -11.181  33.553  1.00 71.00           C
ANISOU 2794  CB  PHE A 338     9247   6971  10761    578   1000   1157       C
ATOM   2795  CG  PHE A 338     -34.085 -11.695  33.485  1.00 88.62           C
ANISOU 2795  CG  PHE A 338    11497   9129  13048    708   1009   1171       C
ATOM   2796  CD1 PHE A 338     -33.399 -11.694  32.282  1.00 89.80           C
ANISOU 2796  CD1 PHE A 338    11664   9202  13254    662    978    960       C
ATOM   2797  CD2 PHE A 338     -33.453 -12.178  34.618  1.00 93.36           C
ANISOU 2797  CD2 PHE A 338    12089   9746  13636    885   1051   1400       C
ATOM   2798  CE1 PHE A 338     -32.117 -12.163  32.210  1.00 86.93           C
ANISOU 2798  CE1 PHE A 338    11308   8775  12947    787    992    972       C
ATOM   2799  CE2 PHE A 338     -32.172 -12.651  34.545  1.00 87.61           C
ANISOU 2799  CE2 PHE A 338    11367   8955  12965   1012   1057   1417       C
ATOM   2800  CZ  PHE A 338     -31.510 -12.641  33.342  1.00 87.61           C
ANISOU 2800  CZ  PHE A 338    11383   8874  13033    961   1030   1200       C
ATOM   2801  N   ALA A 339     -38.008  -9.668  32.557  1.00 63.75           N
ANISOU 2801  N   ALA A 339     8279   6218   9725    251    912    917       N
ATOM   2802  CA  ALA A 339     -39.176  -9.627  31.685  1.00 61.37           C
ANISOU 2802  CA  ALA A 339     7956   5866   9495     65    910    783       C
ATOM   2803  C   ALA A 339     -39.205  -8.336  30.882  1.00 62.85           C
ANISOU 2803  C   ALA A 339     8134   6225   9521      8    787    592       C
ATOM   2804  O   ALA A 339     -39.367  -8.357  29.655  1.00 67.81           O
ANISOU 2804  O   ALA A 339     8767   6795  10204   -112    758    404       O
ATOM   2805  CB  ALA A 339     -40.456  -9.785  32.508  1.00 60.87           C
ANISOU 2805  CB  ALA A 339     7850   5822   9456     22    975    942       C
ATOM   2806  N   ARG A 340     -39.022  -7.195  31.555  1.00 57.52           N
ANISOU 2806  N   ARG A 340     7445   5765   8646     97    714    637       N
ATOM   2807  CA  ARG A 340     -39.014  -5.926  30.837  1.00 51.30           C
ANISOU 2807  CA  ARG A 340     6646   5128   7717     52    604    473       C
ATOM   2808  C   ARG A 340     -37.832  -5.831  29.876  1.00 57.19           C
ANISOU 2808  C   ARG A 340     7424   5842   8465     66    558    322       C
ATOM   2809  O   ARG A 340     -37.938  -5.180  28.832  1.00 61.37           O
ANISOU 2809  O   ARG A 340     7949   6421   8949    -18    495    160       O
ATOM   2810  CB  ARG A 340     -39.012  -4.757  31.827  1.00 43.01           C
ANISOU 2810  CB  ARG A 340     5576   4295   6473    151    544    547       C
ATOM   2811  CG  ARG A 340     -40.405  -4.207  32.137  1.00 38.85           C
ANISOU 2811  CG  ARG A 340     5006   3863   5894     83    545    581       C
ATOM   2812  CD  ARG A 340     -40.855  -3.187  31.089  1.00 56.82           C
ANISOU 2812  CD  ARG A 340     7262   6219   8108    -18    460    408       C
ATOM   2813  NE  ARG A 340     -42.052  -2.445  31.488  1.00 74.98           N
ANISOU 2813  NE  ARG A 340     9513   8642  10333    -50    448    444       N
ATOM   2814  CZ  ARG A 340     -42.975  -1.983  30.646  1.00 82.97           C
ANISOU 2814  CZ  ARG A 340    10489   9684  11352   -168    412    345       C
ATOM   2815  NH1 ARG A 340     -42.844  -2.178  29.341  1.00 85.09           N
ANISOU 2815  NH1 ARG A 340    10767   9879  11683   -268    381    198       N
ATOM   2816  NH2 ARG A 340     -44.028  -1.314  31.108  1.00 82.73           N
ANISOU 2816  NH2 ARG A 340    10409   9769  11257   -178    408    392       N
ATOM   2817  N   ASN A 341     -36.715  -6.491  30.188  1.00 56.48           N
ANISOU 2817  N   ASN A 341     7359   5672   8429    175    593    381       N
ATOM   2818  CA  ASN A 341     -35.559  -6.466  29.297  1.00 61.72           C
ANISOU 2818  CA  ASN A 341     8045   6303   9103    196    562    246       C
ATOM   2819  C   ASN A 341     -35.827  -7.261  28.027  1.00 61.20           C
ANISOU 2819  C   ASN A 341     8000   6068   9185     70    606     97       C
ATOM   2820  O   ASN A 341     -35.722  -6.736  26.912  1.00 64.38           O
ANISOU 2820  O   ASN A 341     8406   6516   9541     -3    553    -75       O
ATOM   2821  CB  ASN A 341     -34.332  -7.013  30.028  1.00 68.24           C
ANISOU 2821  CB  ASN A 341     8881   7091   9956    355    593    360       C
ATOM   2822  CG  ASN A 341     -33.035  -6.668  29.328  1.00 72.96           C
ANISOU 2822  CG  ASN A 341     9482   7717  10521    404    545    239       C
ATOM   2823  OD1 ASN A 341     -33.012  -6.430  28.122  1.00 75.81           O
ANISOU 2823  OD1 ASN A 341     9853   8061  10892    310    523     67       O
ATOM   2824  ND2 ASN A 341     -31.943  -6.639  30.085  1.00 74.11           N
ANISOU 2824  ND2 ASN A 341     9614   7920  10624    553    529    332       N
ATOM   2825  N   LEU A 342     -36.169  -8.540  28.176  1.00 56.55           N
ANISOU 2825  N   LEU A 342     7426   5284   8778     45    704    159       N
ATOM   2826  CA  LEU A 342     -36.497  -9.365  27.020  1.00 60.00           C
ANISOU 2826  CA  LEU A 342     7880   5549   9367    -82    748      2       C
ATOM   2827  C   LEU A 342     -37.731  -8.868  26.279  1.00 62.79           C
ANISOU 2827  C   LEU A 342     8207   5970   9682   -245    699   -121       C
ATOM   2828  O   LEU A 342     -37.965  -9.292  25.142  1.00 65.40           O
ANISOU 2828  O   LEU A 342     8546   6213  10089   -359    704   -296       O
ATOM   2829  CB  LEU A 342     -36.701 -10.816  27.456  1.00 56.60           C
ANISOU 2829  CB  LEU A 342     7465   4880   9160    -79    869    108       C
ATOM   2830  CG  LEU A 342     -35.523 -11.467  28.178  1.00 52.85           C
ANISOU 2830  CG  LEU A 342     7013   4317   8749     91    929    248       C
ATOM   2831  CD1 LEU A 342     -35.991 -12.670  28.987  1.00 51.93           C
ANISOU 2831  CD1 LEU A 342     6899   4007   8825    108   1050    433       C
ATOM   2832  CD2 LEU A 342     -34.460 -11.872  27.174  1.00 53.33           C
ANISOU 2832  CD2 LEU A 342     7106   4279   8879    113    939     85       C
ATOM   2833  N   LEU A 343     -38.517  -7.983  26.895  1.00 64.69           N
ANISOU 2833  N   LEU A 343     8409   6369   9800   -254    652    -37       N
ATOM   2834  CA  LEU A 343     -39.696  -7.425  26.250  1.00 66.88           C
ANISOU 2834  CA  LEU A 343     8648   6731  10031   -394    600   -136       C
ATOM   2835  C   LEU A 343     -39.383  -6.725  24.931  1.00 63.26           C
ANISOU 2835  C   LEU A 343     8198   6363   9477   -450    518   -337       C
ATOM   2836  O   LEU A 343     -40.294  -6.526  24.121  1.00 57.32           O
ANISOU 2836  O   LEU A 343     7416   5650   8714   -577    480   -449       O
ATOM   2837  CB  LEU A 343     -40.366  -6.458  27.226  1.00 72.32           C
ANISOU 2837  CB  LEU A 343     9297   7593  10589   -356    564     -3       C
ATOM   2838  CG  LEU A 343     -41.673  -5.775  26.843  1.00 83.87           C
ANISOU 2838  CG  LEU A 343    10705   9166  11995   -473    514    -56       C
ATOM   2839  CD1 LEU A 343     -42.862  -6.504  27.466  1.00 89.86           C
ANISOU 2839  CD1 LEU A 343    11421   9846  12878   -541    590     57       C
ATOM   2840  CD2 LEU A 343     -41.628  -4.313  27.262  1.00 81.56           C
ANISOU 2840  CD2 LEU A 343    10396   9086  11507   -399    433    -24       C
ATOM   2841  N   SER A 344     -38.123  -6.358  24.683  1.00 65.87           N
ANISOU 2841  N   SER A 344     8560   6734   9736   -357    492   -380       N
ATOM   2842  CA  SER A 344     -37.807  -5.600  23.476  1.00 66.62           C
ANISOU 2842  CA  SER A 344     8657   6932   9723   -399    421   -546       C
ATOM   2843  C   SER A 344     -38.083  -6.386  22.200  1.00 67.53           C
ANISOU 2843  C   SER A 344     8786   6944   9928   -519    442   -728       C
ATOM   2844  O   SER A 344     -38.319  -5.778  21.149  1.00 66.69           O
ANISOU 2844  O   SER A 344     8668   6946   9725   -591    381   -862       O
ATOM   2845  CB  SER A 344     -36.347  -5.148  23.513  1.00 63.31           C
ANISOU 2845  CB  SER A 344     8260   6563   9232   -276    404   -545       C
ATOM   2846  OG  SER A 344     -36.127  -4.277  24.609  1.00 59.47           O
ANISOU 2846  OG  SER A 344     7755   6198   8644   -177    365   -409       O
ATOM   2847  N   VAL A 345     -38.089  -7.717  22.268  1.00 71.66           N
ANISOU 2847  N   VAL A 345     9331   7263  10634   -542    528   -736       N
ATOM   2848  CA  VAL A 345     -38.244  -8.511  21.055  1.00 71.20           C
ANISOU 2848  CA  VAL A 345     9289   7097  10667   -650    550   -935       C
ATOM   2849  C   VAL A 345     -39.648  -8.370  20.468  1.00 73.35           C
ANISOU 2849  C   VAL A 345     9514   7427  10928   -810    502  -1026       C
ATOM   2850  O   VAL A 345     -39.833  -8.523  19.255  1.00 66.96           O
ANISOU 2850  O   VAL A 345     8706   6633  10103   -905    473  -1221       O
ATOM   2851  CB  VAL A 345     -37.889  -9.983  21.337  1.00 63.52           C
ANISOU 2851  CB  VAL A 345     8350   5867   9919   -630    662   -920       C
ATOM   2852  CG1 VAL A 345     -38.999 -10.672  22.131  1.00 58.20           C
ANISOU 2852  CG1 VAL A 345     7646   5072   9395   -699    716   -802       C
ATOM   2853  CG2 VAL A 345     -37.600 -10.721  20.037  1.00 61.37           C
ANISOU 2853  CG2 VAL A 345     8109   5488   9722   -701    686  -1154       C
ATOM   2854  N   VAL A 346     -40.653  -8.063  21.289  1.00 84.34           N
ANISOU 2854  N   VAL A 346    10859   8869  12318   -839    491   -891       N
ATOM   2855  CA  VAL A 346     -42.028  -8.046  20.795  1.00 89.81           C
ANISOU 2855  CA  VAL A 346    11492   9604  13026   -992    451   -967       C
ATOM   2856  C   VAL A 346     -42.392  -6.665  20.263  1.00 91.43           C
ANISOU 2856  C   VAL A 346    11662  10055  13024  -1007    342  -1006       C
ATOM   2857  O   VAL A 346     -43.564  -6.390  19.988  1.00 91.18           O
ANISOU 2857  O   VAL A 346    11567  10106  12971  -1110    294  -1034       O
ATOM   2858  CB  VAL A 346     -43.039  -8.494  21.872  1.00 94.56           C
ANISOU 2858  CB  VAL A 346    12046  10130  13751  -1029    506   -807       C
ATOM   2859  CG1 VAL A 346     -42.852  -9.966  22.208  1.00 97.42           C
ANISOU 2859  CG1 VAL A 346    12436  10228  14351  -1043    620   -782       C
ATOM   2860  CG2 VAL A 346     -42.950  -7.624  23.119  1.00 95.44           C
ANISOU 2860  CG2 VAL A 346    12148  10362  13752   -905    499   -595       C
ATOM   2861  N   ARG A 347     -41.401  -5.785  20.113  1.00 93.18           N
ANISOU 2861  N   ARG A 347    11916  10388  13099   -902    304  -1000       N
ATOM   2862  CA  ARG A 347     -41.670  -4.450  19.593  1.00 86.25           C
ANISOU 2862  CA  ARG A 347    11009   9726  12038   -907    209  -1024       C
ATOM   2863  C   ARG A 347     -41.386  -4.330  18.102  1.00 82.18           C
ANISOU 2863  C   ARG A 347    10506   9280  11440   -962    164  -1213       C
ATOM   2864  O   ARG A 347     -41.850  -3.372  17.473  1.00 85.74           O
ANISOU 2864  O   ARG A 347    10921   9904  11752   -993     87  -1245       O
ATOM   2865  CB  ARG A 347     -40.869  -3.402  20.379  1.00 85.89           C
ANISOU 2865  CB  ARG A 347    10978   9774  11882   -768    191   -892       C
ATOM   2866  CG  ARG A 347     -41.199  -3.388  21.885  1.00 91.58           C
ANISOU 2866  CG  ARG A 347    11683  10468  12644   -703    226   -706       C
ATOM   2867  CD  ARG A 347     -42.655  -3.814  22.158  1.00 97.79           C
ANISOU 2867  CD  ARG A 347    12413  11230  13513   -807    241   -670       C
ATOM   2868  NE  ARG A 347     -42.925  -4.136  23.560  1.00 99.32           N
ANISOU 2868  NE  ARG A 347    12597  11367  13774   -749    304   -492       N
ATOM   2869  CZ  ARG A 347     -44.143  -4.166  24.096  1.00100.10           C
ANISOU 2869  CZ  ARG A 347    12636  11488  13911   -805    319   -410       C
ATOM   2870  NH1 ARG A 347     -45.204  -3.902  23.348  1.00101.30           N
ANISOU 2870  NH1 ARG A 347    12727  11713  14048   -922    268   -495       N
ATOM   2871  NH2 ARG A 347     -44.308  -4.468  25.376  1.00100.02           N
ANISOU 2871  NH2 ARG A 347    12620  11436  13948   -740    386   -239       N
ATOM   2872  N   VAL A 348     -40.652  -5.285  17.526  1.00 80.50           N
ANISOU 2872  N   VAL A 348    10341   8939  11306   -968    216  -1336       N
ATOM   2873  CA  VAL A 348     -40.568  -5.440  16.079  1.00 74.42           C
ANISOU 2873  CA  VAL A 348     9580   8222  10474  -1039    187  -1541       C
ATOM   2874  C   VAL A 348     -41.484  -6.544  15.567  1.00 76.06           C
ANISOU 2874  C   VAL A 348     9766   8324  10809  -1182    199  -1685       C
ATOM   2875  O   VAL A 348     -41.501  -6.819  14.358  1.00 71.31           O
ANISOU 2875  O   VAL A 348     9170   7763  10161  -1251    174  -1881       O
ATOM   2876  CB  VAL A 348     -39.116  -5.700  15.635  1.00 61.61           C
ANISOU 2876  CB  VAL A 348     8021   6549   8840   -950    236  -1611       C
ATOM   2877  CG1 VAL A 348     -38.205  -4.620  16.185  1.00 57.33           C
ANISOU 2877  CG1 VAL A 348     7487   6105   8190   -819    221  -1471       C
ATOM   2878  CG2 VAL A 348     -38.659  -7.082  16.085  1.00 61.41           C
ANISOU 2878  CG2 VAL A 348     8036   6279   9020   -931    336  -1628       C
ATOM   2879  N   VAL A 349     -42.239  -7.194  16.450  1.00 81.78           N
ANISOU 2879  N   VAL A 349    10462   8916  11693  -1228    240  -1598       N
ATOM   2880  CA  VAL A 349     -43.271  -8.149  16.062  1.00 88.47           C
ANISOU 2880  CA  VAL A 349    11268   9665  12680  -1382    246  -1721       C
ATOM   2881  C   VAL A 349     -44.581  -7.655  16.669  1.00 99.24           C
ANISOU 2881  C   VAL A 349    12547  11119  14040  -1444    203  -1600       C
ATOM   2882  O   VAL A 349     -44.726  -7.577  17.895  1.00102.69           O
ANISOU 2882  O   VAL A 349    12974  11506  14539  -1385    249  -1403       O
ATOM   2883  CB  VAL A 349     -42.926  -9.592  16.482  1.00 89.39           C
ANISOU 2883  CB  VAL A 349    11425   9498  13039  -1391    360  -1739       C
ATOM   2884  CG1 VAL A 349     -41.549  -9.948  15.988  1.00 88.32           C
ANISOU 2884  CG1 VAL A 349    11371   9294  12893  -1297    406  -1830       C
ATOM   2885  CG2 VAL A 349     -42.962  -9.808  17.981  1.00 88.93           C
ANISOU 2885  CG2 VAL A 349    11365   9323  13101  -1318    434  -1498       C
ATOM   2886  N   GLN A 350     -45.520  -7.257  15.816  1.00104.23           N
ANISOU 2886  N   GLN A 350    13113  11907  14583  -1551    112  -1710       N
ATOM   2887  CA  GLN A 350     -46.796  -6.698  16.264  1.00108.18           C
ANISOU 2887  CA  GLN A 350    13518  12519  15066  -1607     63  -1605       C
ATOM   2888  C   GLN A 350     -47.947  -7.365  15.514  1.00114.86           C
ANISOU 2888  C   GLN A 350    14283  13361  15995  -1786     21  -1770       C
ATOM   2889  O   GLN A 350     -48.609  -6.748  14.669  1.00108.31           O
ANISOU 2889  O   GLN A 350    13393  12731  15031  -1845    -82  -1855       O
ATOM   2890  CB  GLN A 350     -46.813  -5.170  16.119  1.00102.58           C
ANISOU 2890  CB  GLN A 350    12789  12055  14132  -1528    -22  -1525       C
ATOM   2891  CG  GLN A 350     -46.709  -4.560  14.706  1.00 98.87           C
ANISOU 2891  CG  GLN A 350    12314  11773  13477  -1552   -116  -1679       C
ATOM   2892  CD  GLN A 350     -45.444  -4.939  13.963  1.00 97.45           C
ANISOU 2892  CD  GLN A 350    12224  11541  13261  -1507    -85  -1810       C
ATOM   2893  OE1 GLN A 350     -44.454  -5.351  14.565  1.00 96.70           O
ANISOU 2893  OE1 GLN A 350    12200  11296  13247  -1422     -3  -1755       O
ATOM   2894  NE2 GLN A 350     -45.472  -4.800  12.642  1.00 99.13           N
ANISOU 2894  NE2 GLN A 350    12430  11890  13346  -1557   -150  -1981       N
ATOM   2895  N   PRO A 351     -48.230  -8.638  15.819  1.00129.03           N
ANISOU 2895  N   PRO A 351    16078  14950  17998  -1849     93  -1784       N
ATOM   2896  CA  PRO A 351     -49.422  -9.283  15.246  1.00133.60           C
ANISOU 2896  CA  PRO A 351    16580  15551  18630  -1977     45  -1870       C
ATOM   2897  C   PRO A 351     -50.730  -8.691  15.745  1.00135.80           C
ANISOU 2897  C   PRO A 351    16735  15943  18918  -2051      3  -1769       C
ATOM   2898  O   PRO A 351     -51.796  -9.105  15.274  1.00138.52           O
ANISOU 2898  O   PRO A 351    17002  16331  19300  -2159    -49  -1834       O
ATOM   2899  CB  PRO A 351     -49.269 -10.749  15.680  1.00138.13           C
ANISOU 2899  CB  PRO A 351    17192  15857  19433  -1998    152  -1862       C
ATOM   2900  CG  PRO A 351     -48.444 -10.691  16.911  1.00136.57           C
ANISOU 2900  CG  PRO A 351    17051  15516  19325  -1893    259  -1688       C
ATOM   2901  CD  PRO A 351     -47.496  -9.540  16.725  1.00132.51           C
ANISOU 2901  CD  PRO A 351    16587  15139  18623  -1790    221  -1693       C
ATOM   2902  N   LYS A 352     -50.678  -7.748  16.688  1.00129.92           N
ANISOU 2902  N   LYS A 352    15970  15252  18141  -1990     24  -1607       N
ATOM   2903  CA  LYS A 352     -51.856  -7.002  17.108  1.00126.17           C
ANISOU 2903  CA  LYS A 352    15382  14934  17622  -2016    -23  -1487       C
ATOM   2904  C   LYS A 352     -52.450  -6.281  15.907  1.00115.99           C
ANISOU 2904  C   LYS A 352    14023  13884  16165  -2077   -160  -1625       C
ATOM   2905  O   LYS A 352     -51.962  -5.218  15.509  1.00113.46           O
ANISOU 2905  O   LYS A 352    13737  13733  15637  -1976   -222  -1606       O
ATOM   2906  CB  LYS A 352     -51.502  -6.008  18.220  1.00127.51           C
ANISOU 2906  CB  LYS A 352    15583  15173  17690  -1851      9  -1252       C
ATOM   2907  CG  LYS A 352     -52.655  -5.110  18.660  1.00125.10           C
ANISOU 2907  CG  LYS A 352    15167  15042  17323  -1853    -35  -1126       C
ATOM   2908  CD  LYS A 352     -53.685  -5.874  19.475  1.00124.66           C
ANISOU 2908  CD  LYS A 352    15021  14877  17467  -1945     39  -1035       C
ATOM   2909  CE  LYS A 352     -53.137  -6.266  20.837  1.00122.69           C
ANISOU 2909  CE  LYS A 352    14837  14468  17311  -1844    168   -845       C
ATOM   2910  NZ  LYS A 352     -54.132  -7.050  21.621  1.00123.97           N
ANISOU 2910  NZ  LYS A 352    14909  14521  17673  -1935    256   -740       N
ATOM   2911  N   GLY A 353     -53.490  -6.871  15.312  1.00108.48           N
ANISOU 2911  N   GLY A 353    12990  12961  15265  -2194   -213  -1713       N
ATOM   2912  CA  GLY A 353     -54.121  -6.253  14.161  1.00 98.84           C
ANISOU 2912  CA  GLY A 353    11705  11982  13867  -2224   -349  -1811       C
ATOM   2913  C   GLY A 353     -54.587  -4.839  14.431  1.00 88.21           C
ANISOU 2913  C   GLY A 353    10276  10851  12389  -2183   -408  -1700       C
ATOM   2914  O   GLY A 353     -54.534  -3.984  13.543  1.00 83.98           O
ANISOU 2914  O   GLY A 353     9733  10522  11653  -2142   -507  -1748       O
ATOM   2915  N   GLY A 354     -55.048  -4.571  15.655  1.00 84.23           N
ANISOU 2915  N   GLY A 354     9718  10307  11976  -2161   -344  -1519       N
ATOM   2916  CA  GLY A 354     -55.373  -3.204  16.021  1.00 82.92           C
ANISOU 2916  CA  GLY A 354     9514  10332  11661  -2048   -386  -1356       C
ATOM   2917  C   GLY A 354     -54.181  -2.280  15.879  1.00 83.43           C
ANISOU 2917  C   GLY A 354     9697  10457  11545  -1890   -396  -1313       C
ATOM   2918  O   GLY A 354     -54.294  -1.176  15.339  1.00 82.41           O
ANISOU 2918  O   GLY A 354     9544  10525  11244  -1830   -479  -1293       O
ATOM   2919  N   ALA A 355     -53.018  -2.719  16.368  1.00 85.75           N
ANISOU 2919  N   ALA A 355    10114  10580  11887  -1819   -309  -1292       N
ATOM   2920  CA  ALA A 355     -51.801  -1.937  16.181  1.00 80.70           C
ANISOU 2920  CA  ALA A 355     9582   9986  11096  -1683   -317  -1269       C
ATOM   2921  C   ALA A 355     -51.440  -1.841  14.705  1.00 77.43           C
ANISOU 2921  C   ALA A 355     9187   9682  10550  -1719   -399  -1448       C
ATOM   2922  O   ALA A 355     -50.932  -0.811  14.252  1.00 74.40           O
ANISOU 2922  O   ALA A 355     8835   9437   9996  -1627   -445  -1419       O
ATOM   2923  CB  ALA A 355     -50.645  -2.545  16.979  1.00 78.08           C
ANISOU 2923  CB  ALA A 355     9363   9451  10853  -1607   -210  -1218       C
ATOM   2924  N   LEU A 356     -51.717  -2.899  13.937  1.00 77.09           N
ANISOU 2924  N   LEU A 356     9123   9585  10584  -1853   -415  -1635       N
ATOM   2925  CA  LEU A 356     -51.434  -2.878  12.505  1.00 72.07           C
ANISOU 2925  CA  LEU A 356     8502   9074   9809  -1890   -493  -1823       C
ATOM   2926  C   LEU A 356     -52.117  -1.702  11.817  1.00 70.69           C
ANISOU 2926  C   LEU A 356     8245   9172   9444  -1872   -608  -1790       C
ATOM   2927  O   LEU A 356     -51.549  -1.098  10.899  1.00 73.05           O
ANISOU 2927  O   LEU A 356     8582   9611   9562  -1817   -657  -1839       O
ATOM   2928  CB  LEU A 356     -51.868  -4.198  11.866  1.00 70.40           C
ANISOU 2928  CB  LEU A 356     8280   8767   9700  -1996   -497  -1977       C
ATOM   2929  CG  LEU A 356     -50.894  -5.368  12.015  1.00 66.59           C
ANISOU 2929  CG  LEU A 356     7909   8044   9350  -1984   -396  -2049       C
ATOM   2930  CD1 LEU A 356     -51.441  -6.614  11.334  1.00 64.36           C
ANISOU 2930  CD1 LEU A 356     7611   7682   9160  -2081   -408  -2191       C
ATOM   2931  CD2 LEU A 356     -49.522  -4.995  11.465  1.00 64.43           C
ANISOU 2931  CD2 LEU A 356     7742   7801   8937  -1880   -381  -2100       C
ATOM   2932  N   THR A 357     -53.333  -1.353  12.253  1.00 66.60           N
ANISOU 2932  N   THR A 357     7608   8734   8963  -1910   -645  -1696       N
ATOM   2933  CA  THR A 357     -54.070  -0.239  11.655  1.00 62.70           C
ANISOU 2933  CA  THR A 357     7023   8496   8305  -1885   -753  -1647       C
ATOM   2934  C   THR A 357     -53.455   1.144  11.982  1.00 61.71           C
ANISOU 2934  C   THR A 357     6951   8448   8046  -1715   -744  -1468       C
ATOM   2935  O   THR A 357     -54.059   2.169  11.649  1.00 62.75           O
ANISOU 2935  O   THR A 357     7010   8772   8062  -1672   -818  -1389       O
ATOM   2936  CB  THR A 357     -55.538  -0.274  12.092  1.00 59.71           C
ANISOU 2936  CB  THR A 357     6493   8172   8021  -1966   -786  -1590       C
ATOM   2937  OG1 THR A 357     -55.637  -0.009  13.497  1.00 63.38           O
ANISOU 2937  OG1 THR A 357     6962   8526   8592  -1894   -697  -1398       O
ATOM   2938  CG2 THR A 357     -56.158  -1.632  11.796  1.00 54.00           C
ANISOU 2938  CG2 THR A 357     5736   7339   7444  -2098   -785  -1720       C
ATOM   2939  N   ILE A 358     -52.293   1.246  12.615  1.00 62.06           N
ANISOU 2939  N   ILE A 358     7115   8356   8111  -1616   -658  -1401       N
ATOM   2940  CA  ILE A 358     -51.625   2.529  12.799  1.00 68.24           C
ANISOU 2940  CA  ILE A 358     7947   9206   8774  -1469   -655  -1263       C
ATOM   2941  C   ILE A 358     -50.654   2.741  11.645  1.00 71.90           C
ANISOU 2941  C   ILE A 358     8481   9747   9091  -1438   -681  -1356       C
ATOM   2942  O   ILE A 358     -49.912   1.825  11.266  1.00 74.58           O
ANISOU 2942  O   ILE A 358     8890   9987   9460  -1478   -645  -1492       O
ATOM   2943  CB  ILE A 358     -50.896   2.589  14.151  1.00 66.58           C
ANISOU 2943  CB  ILE A 358     7813   8825   8659  -1377   -555  -1139       C
ATOM   2944  CG1 ILE A 358     -51.776   2.014  15.260  1.00 64.21           C
ANISOU 2944  CG1 ILE A 358     7453   8427   8518  -1425   -508  -1072       C
ATOM   2945  CG2 ILE A 358     -50.490   4.020  14.480  1.00 62.94           C
ANISOU 2945  CG2 ILE A 358     7374   8441   8100  -1239   -561   -994       C
ATOM   2946  CD1 ILE A 358     -51.066   1.908  16.587  1.00 60.41           C
ANISOU 2946  CD1 ILE A 358     7047   7787   8121  -1336   -410   -959       C
ATOM   2947  N   ALA A 359     -50.666   3.949  11.077  1.00 69.51           N
ANISOU 2947  N   ALA A 359     8158   9620   8634  -1363   -738  -1278       N
ATOM   2948  CA  ALA A 359     -49.774   4.247   9.961  1.00 67.83           C
ANISOU 2948  CA  ALA A 359     8003   9500   8267  -1326   -756  -1342       C
ATOM   2949  C   ALA A 359     -48.320   4.317  10.408  1.00 62.64           C
ANISOU 2949  C   ALA A 359     7464   8700   7637  -1238   -666  -1308       C
ATOM   2950  O   ALA A 359     -47.420   3.977   9.634  1.00 61.19           O
ANISOU 2950  O   ALA A 359     7343   8519   7386  -1236   -647  -1411       O
ATOM   2951  CB  ALA A 359     -50.192   5.557   9.294  1.00 62.81           C
ANISOU 2951  CB  ALA A 359     7309   9081   7473  -1262   -830  -1236       C
ATOM   2952  N   GLU A 360     -48.081   4.748  11.650  1.00 62.63           N
ANISOU 2952  N   GLU A 360     7484   8583   7728  -1164   -612  -1172       N
ATOM   2953  CA  GLU A 360     -46.723   4.856  12.177  1.00 61.88           C
ANISOU 2953  CA  GLU A 360     7486   8361   7664  -1079   -536  -1134       C
ATOM   2954  C   GLU A 360     -46.028   3.502  12.201  1.00 66.28           C
ANISOU 2954  C   GLU A 360     8108   8765   8311  -1127   -476  -1264       C
ATOM   2955  O   GLU A 360     -44.874   3.374  11.775  1.00 63.51           O
ANISOU 2955  O   GLU A 360     7827   8381   7922  -1087   -438  -1317       O
ATOM   2956  CB  GLU A 360     -46.776   5.453  13.580  1.00 60.50           C
ANISOU 2956  CB  GLU A 360     7310   8103   7573  -1003   -500   -982       C
ATOM   2957  CG  GLU A 360     -45.449   5.814  14.173  1.00 57.79           C
ANISOU 2957  CG  GLU A 360     7046   7663   7248   -906   -441   -928       C
ATOM   2958  CD  GLU A 360     -45.569   6.995  15.105  1.00 69.13           C
ANISOU 2958  CD  GLU A 360     8465   9109   8692   -816   -441   -782       C
ATOM   2959  OE1 GLU A 360     -45.748   8.127  14.607  1.00 72.04           O
ANISOU 2959  OE1 GLU A 360     8804   9592   8976   -776   -482   -721       O
ATOM   2960  OE2 GLU A 360     -45.504   6.791  16.335  1.00 74.85           O
ANISOU 2960  OE2 GLU A 360     9205   9729   9506   -782   -398   -729       O
ATOM   2961  N   VAL A 361     -46.714   2.479  12.709  1.00 69.67           N
ANISOU 2961  N   VAL A 361     8511   9090   8870  -1209   -459  -1312       N
ATOM   2962  CA  VAL A 361     -46.179   1.123  12.738  1.00 69.74           C
ANISOU 2962  CA  VAL A 361     8575   8932   8991  -1259   -397  -1435       C
ATOM   2963  C   VAL A 361     -46.437   0.479  11.380  1.00 73.10           C
ANISOU 2963  C   VAL A 361     8985   9436   9354  -1358   -443  -1631       C
ATOM   2964  O   VAL A 361     -46.631   1.188  10.386  1.00 85.90           O
ANISOU 2964  O   VAL A 361    10576  11250  10812  -1356   -513  -1656       O
ATOM   2965  CB  VAL A 361     -46.784   0.315  13.904  1.00 68.80           C
ANISOU 2965  CB  VAL A 361     8433   8654   9053  -1301   -348  -1386       C
ATOM   2966  CG1 VAL A 361     -46.799   1.156  15.169  1.00 63.58           C
ANISOU 2966  CG1 VAL A 361     7767   7981   8409  -1203   -324  -1193       C
ATOM   2967  CG2 VAL A 361     -48.187  -0.121  13.594  1.00 72.96           C
ANISOU 2967  CG2 VAL A 361     8864   9236   9624  -1428   -400  -1449       C
ATOM   2968  N   TYR A 362     -46.420  -0.859  11.329  1.00 64.94           N
ANISOU 2968  N   TYR A 362     7972   8255   8448  -1442   -402  -1770       N
ATOM   2969  CA  TYR A 362     -46.612  -1.718  10.161  1.00 66.79           C
ANISOU 2969  CA  TYR A 362     8199   8520   8657  -1547   -433  -1994       C
ATOM   2970  C   TYR A 362     -45.266  -1.941   9.486  1.00 66.66           C
ANISOU 2970  C   TYR A 362     8276   8479   8574  -1486   -384  -2094       C
ATOM   2971  O   TYR A 362     -44.508  -0.985   9.267  1.00 66.19           O
ANISOU 2971  O   TYR A 362     8248   8521   8381  -1384   -383  -2008       O
ATOM   2972  CB  TYR A 362     -47.633  -1.156   9.164  1.00 59.43           C
ANISOU 2972  CB  TYR A 362     7177   7833   7571  -1610   -549  -2049       C
ATOM   2973  CG  TYR A 362     -48.204  -2.218   8.246  1.00 64.07           C
ANISOU 2973  CG  TYR A 362     7748   8417   8177  -1689   -579  -2203       C
ATOM   2974  CD1 TYR A 362     -47.567  -2.554   7.055  1.00 66.03           C
ANISOU 2974  CD1 TYR A 362     8053   8726   8310  -1664   -580  -2336       C
ATOM   2975  CD2 TYR A 362     -49.368  -2.900   8.582  1.00 53.34           C
ANISOU 2975  CD2 TYR A 362     6316   6995   6957  -1787   -601  -2217       C
ATOM   2976  CE1 TYR A 362     -48.078  -3.535   6.221  1.00 61.72           C
ANISOU 2976  CE1 TYR A 362     7492   8177   7780  -1735   -609  -2488       C
ATOM   2977  CE2 TYR A 362     -49.886  -3.879   7.757  1.00 55.09           C
ANISOU 2977  CE2 TYR A 362     6521   7207   7204  -1863   -631  -2364       C
ATOM   2978  CZ  TYR A 362     -49.240  -4.194   6.579  1.00 61.15           C
ANISOU 2978  CZ  TYR A 362     7347   8034   7851  -1837   -637  -2504       C
ATOM   2979  OH  TYR A 362     -49.762  -5.172   5.760  1.00 59.89           O
ANISOU 2979  OH  TYR A 362     7170   7868   7716  -1915   -670  -2664       O
ATOM   2980  N   PRO A 363     -44.935  -3.186   9.151  1.00 61.29           N
ANISOU 2980  N   PRO A 363     7641   7657   7989  -1525   -333  -2241       N
ATOM   2981  CA  PRO A 363     -43.572  -3.488   8.702  1.00 60.98           C
ANISOU 2981  CA  PRO A 363     7692   7562   7918  -1447   -264  -2313       C
ATOM   2982  C   PRO A 363     -43.235  -2.842   7.367  1.00 62.92           C
ANISOU 2982  C   PRO A 363     7942   8032   7931  -1412   -312  -2378       C
ATOM   2983  O   PRO A 363     -44.075  -2.732   6.470  1.00 62.90           O
ANISOU 2983  O   PRO A 363     7888   8194   7815  -1462   -393  -2434       O
ATOM   2984  CB  PRO A 363     -43.566  -5.019   8.595  1.00 58.40           C
ANISOU 2984  CB  PRO A 363     7396   7041   7751  -1491   -209  -2430       C
ATOM   2985  CG  PRO A 363     -45.002  -5.394   8.441  1.00 57.76           C
ANISOU 2985  CG  PRO A 363     7237   6996   7714  -1602   -278  -2462       C
ATOM   2986  CD  PRO A 363     -45.756  -4.401   9.274  1.00 58.87           C
ANISOU 2986  CD  PRO A 363     7308   7216   7846  -1617   -325  -2308       C
ATOM   2987  N   PHE A 364     -41.983  -2.398   7.265  1.00 61.32           N
ANISOU 2987  N   PHE A 364     7798   7840   7660  -1322   -257  -2363       N
ATOM   2988  CA  PHE A 364     -41.348  -2.092   5.993  1.00 59.73           C
ANISOU 2988  CA  PHE A 364     7622   7807   7268  -1277   -261  -2441       C
ATOM   2989  C   PHE A 364     -41.397  -3.313   5.077  1.00 63.98           C
ANISOU 2989  C   PHE A 364     8184   8305   7822  -1312   -246  -2616       C
ATOM   2990  O   PHE A 364     -41.638  -4.442   5.515  1.00 68.01           O
ANISOU 2990  O   PHE A 364     8707   8620   8515  -1357   -212  -2674       O
ATOM   2991  CB  PHE A 364     -39.891  -1.686   6.234  1.00 57.90           C
ANISOU 2991  CB  PHE A 364     7450   7529   7021  -1172   -177  -2390       C
ATOM   2992  CG  PHE A 364     -39.417  -0.523   5.406  1.00 54.91           C
ANISOU 2992  CG  PHE A 364     7065   7373   6427  -1102   -196  -2319       C
ATOM   2993  CD1 PHE A 364     -39.865   0.760   5.664  1.00 54.25           C
ANISOU 2993  CD1 PHE A 364     6933   7413   6266  -1069   -255  -2127       C
ATOM   2994  CD2 PHE A 364     -38.484  -0.710   4.400  1.00 53.81           C
ANISOU 2994  CD2 PHE A 364     6966   7307   6173  -1062   -145  -2434       C
ATOM   2995  CE1 PHE A 364     -39.413   1.829   4.917  1.00 54.43           C
ANISOU 2995  CE1 PHE A 364     6949   7622   6111  -1004   -262  -2044       C
ATOM   2996  CE2 PHE A 364     -38.027   0.353   3.650  1.00 48.67           C
ANISOU 2996  CE2 PHE A 364     6305   6856   5330   -996   -149  -2349       C
ATOM   2997  CZ  PHE A 364     -38.490   1.624   3.908  1.00 52.84           C
ANISOU 2997  CZ  PHE A 364     6786   7497   5793   -969   -208  -2148       C
ATOM   2998  N   PHE A 365     -41.158  -3.075   3.787  1.00 63.66           N
ANISOU 2998  N   PHE A 365     8148   8452   7586  -1290   -269  -2698       N
ATOM   2999  CA  PHE A 365     -40.987  -4.124   2.783  1.00 67.81           C
ANISOU 2999  CA  PHE A 365     8705   8967   8095  -1306   -248  -2879       C
ATOM   3000  C   PHE A 365     -42.252  -4.934   2.527  1.00 70.22           C
ANISOU 3000  C   PHE A 365     8963   9253   8465  -1412   -316  -2975       C
ATOM   3001  O   PHE A 365     -42.182  -5.997   1.903  1.00 69.11           O
ANISOU 3001  O   PHE A 365     8848   9047   8363  -1440   -294  -3136       O
ATOM   3002  CB  PHE A 365     -39.852  -5.094   3.151  1.00 66.49           C
ANISOU 3002  CB  PHE A 365     8611   8570   8082  -1256   -130  -2942       C
ATOM   3003  CG  PHE A 365     -38.508  -4.443   3.311  1.00 69.25           C
ANISOU 3003  CG  PHE A 365     9003   8931   8377  -1150    -54  -2873       C
ATOM   3004  CD1 PHE A 365     -37.738  -4.129   2.203  1.00 72.04           C
ANISOU 3004  CD1 PHE A 365     9378   9446   8546  -1091    -28  -2936       C
ATOM   3005  CD2 PHE A 365     -38.002  -4.169   4.572  1.00 66.93           C
ANISOU 3005  CD2 PHE A 365     8723   8487   8219  -1108     -5  -2746       C
ATOM   3006  CE1 PHE A 365     -36.496  -3.539   2.349  1.00 72.01           C
ANISOU 3006  CE1 PHE A 365     9405   9455   8502   -996     50  -2873       C
ATOM   3007  CE2 PHE A 365     -36.760  -3.579   4.726  1.00 67.48           C
ANISOU 3007  CE2 PHE A 365     8824   8567   8248  -1013     64  -2690       C
ATOM   3008  CZ  PHE A 365     -36.007  -3.263   3.613  1.00 70.22           C
ANISOU 3008  CZ  PHE A 365     9187   9074   8419   -960     93  -2753       C
ATOM   3009  N   PHE A 366     -43.418  -4.474   2.973  1.00 77.09           N
ANISOU 3009  N   PHE A 366     9759  10178   9352  -1474   -398  -2887       N
ATOM   3010  CA  PHE A 366     -44.626  -5.259   2.766  1.00 85.55           C
ANISOU 3010  CA  PHE A 366    10777  11228  10500  -1580   -460  -2979       C
ATOM   3011  C   PHE A 366     -45.822  -4.350   2.533  1.00 87.79           C
ANISOU 3011  C   PHE A 366    10967  11729  10663  -1620   -576  -2901       C
ATOM   3012  O   PHE A 366     -45.980  -3.326   3.204  1.00 85.92           O
ANISOU 3012  O   PHE A 366    10697  11547  10401  -1590   -597  -2737       O
ATOM   3013  CB  PHE A 366     -44.891  -6.191   3.952  1.00 85.72           C
ANISOU 3013  CB  PHE A 366    10802  10974  10792  -1634   -406  -2958       C
ATOM   3014  CG  PHE A 366     -43.948  -7.355   4.021  1.00 85.75           C
ANISOU 3014  CG  PHE A 366    10886  10758  10935  -1609   -302  -3059       C
ATOM   3015  CD1 PHE A 366     -44.064  -8.407   3.131  1.00 84.54           C
ANISOU 3015  CD1 PHE A 366    10748  10576  10797  -1655   -302  -3248       C
ATOM   3016  CD2 PHE A 366     -42.937  -7.392   4.967  1.00 85.55           C
ANISOU 3016  CD2 PHE A 366    10919  10560  11024  -1534   -204  -2968       C
ATOM   3017  CE1 PHE A 366     -43.195  -9.480   3.185  1.00 87.99           C
ANISOU 3017  CE1 PHE A 366    11256  10809  11369  -1625   -203  -3340       C
ATOM   3018  CE2 PHE A 366     -42.065  -8.463   5.028  1.00 87.86           C
ANISOU 3018  CE2 PHE A 366    11280  10655  11449  -1499   -107  -3050       C
ATOM   3019  CZ  PHE A 366     -42.194  -9.508   4.135  1.00 89.19           C
ANISOU 3019  CZ  PHE A 366    11462  10790  11637  -1544   -105  -3234       C
ATOM   3020  N   THR A 367     -46.657  -4.739   1.573  1.00 90.22           N
ANISOU 3020  N   THR A 367    11226  12157  10896  -1684   -654  -3022       N
ATOM   3021  CA  THR A 367     -47.914  -4.061   1.307  1.00 89.86           C
ANISOU 3021  CA  THR A 367    11079  12309  10756  -1727   -769  -2963       C
ATOM   3022  C   THR A 367     -48.951  -4.454   2.356  1.00 90.43           C
ANISOU 3022  C   THR A 367    11086  12237  11037  -1816   -788  -2909       C
ATOM   3023  O   THR A 367     -48.712  -5.300   3.222  1.00 87.29           O
ANISOU 3023  O   THR A 367    10725  11591  10852  -1847   -710  -2922       O
ATOM   3024  CB  THR A 367     -48.415  -4.405  -0.094  1.00 87.30           C
ANISOU 3024  CB  THR A 367    10724  12165  10281  -1763   -845  -3120       C
ATOM   3025  OG1 THR A 367     -48.194  -5.798  -0.352  1.00 84.85           O
ANISOU 3025  OG1 THR A 367    10460  11685  10094  -1818   -799  -3311       O
ATOM   3026  CG2 THR A 367     -47.685  -3.579  -1.140  1.00 88.74           C
ANISOU 3026  CG2 THR A 367    10937  12576  10204  -1667   -851  -3109       C
ATOM   3027  N   HIS A 368     -50.130  -3.838   2.274  1.00 97.62           N
ANISOU 3027  N   HIS A 368    11893  13308  11889  -1854   -887  -2840       N
ATOM   3028  CA  HIS A 368     -51.258  -4.265   3.092  1.00 95.19           C
ANISOU 3028  CA  HIS A 368    11506  12896  11768  -1950   -912  -2807       C
ATOM   3029  C   HIS A 368     -51.882  -5.556   2.581  1.00 94.43           C
ANISOU 3029  C   HIS A 368    11386  12722  11772  -2058   -936  -2991       C
ATOM   3030  O   HIS A 368     -52.881  -6.015   3.146  1.00 98.79           O
ANISOU 3030  O   HIS A 368    11862  13190  12483  -2151   -958  -2978       O
ATOM   3031  CB  HIS A 368     -52.308  -3.151   3.173  1.00 98.66           C
ANISOU 3031  CB  HIS A 368    11833  13539  12116  -1946  -1009  -2667       C
ATOM   3032  CG  HIS A 368     -51.854  -1.956   3.955  1.00101.07           C
ANISOU 3032  CG  HIS A 368    12148  13875  12380  -1857   -981  -2475       C
ATOM   3033  ND1 HIS A 368     -50.641  -1.339   3.733  1.00101.73           N
ANISOU 3033  ND1 HIS A 368    12316  13997  12338  -1756   -933  -2439       N
ATOM   3034  CD2 HIS A 368     -52.442  -1.272   4.965  1.00100.62           C
ANISOU 3034  CD2 HIS A 368    12024  13813  12393  -1854   -991  -2314       C
ATOM   3035  CE1 HIS A 368     -50.504  -0.324   4.567  1.00 99.10           C
ANISOU 3035  CE1 HIS A 368    11971  13680  12004  -1700   -921  -2267       C
ATOM   3036  NE2 HIS A 368     -51.584  -0.261   5.326  1.00 98.33           N
ANISOU 3036  NE2 HIS A 368    11782  13558  12020  -1755   -954  -2191       N
ATOM   3037  N   ASN A 369     -51.315  -6.142   1.525  1.00 84.50           N
ANISOU 3037  N   ASN A 369    10187  11493  10426  -2050   -928  -3162       N
ATOM   3038  CA  ASN A 369     -51.642  -7.486   1.076  1.00 80.29           C
ANISOU 3038  CA  ASN A 369     9655  10846  10006  -2146   -929  -3358       C
ATOM   3039  C   ASN A 369     -50.573  -8.506   1.449  1.00 76.15           C
ANISOU 3039  C   ASN A 369     9238  10057   9639  -2130   -804  -3435       C
ATOM   3040  O   ASN A 369     -50.766  -9.701   1.203  1.00 78.24           O
ANISOU 3040  O   ASN A 369     9510  10184  10031  -2207   -787  -3593       O
ATOM   3041  CB  ASN A 369     -51.857  -7.499  -0.442  1.00 85.58           C
ANISOU 3041  CB  ASN A 369    10306  11745  10464  -2152  -1014  -3517       C
ATOM   3042  CG  ASN A 369     -53.300  -7.236  -0.826  1.00 89.97           C
ANISOU 3042  CG  ASN A 369    10735  12482  10969  -2229  -1144  -3521       C
ATOM   3043  OD1 ASN A 369     -53.793  -6.114  -0.703  1.00 89.53           O
ANISOU 3043  OD1 ASN A 369    10611  12601  10804  -2189  -1206  -3366       O
ATOM   3044  ND2 ASN A 369     -53.987  -8.273  -1.294  1.00 92.80           N
ANISOU 3044  ND2 ASN A 369    11053  12796  11411  -2339  -1187  -3700       N
ATOM   3045  N   GLY A 370     -49.450  -8.062   2.014  1.00 72.83           N
ANISOU 3045  N   GLY A 370     8895   9563   9213  -2029   -717  -3329       N
ATOM   3046  CA  GLY A 370     -48.465  -8.957   2.589  1.00 67.42           C
ANISOU 3046  CA  GLY A 370     8301   8613   8701  -2002   -594  -3360       C
ATOM   3047  C   GLY A 370     -47.535  -9.655   1.617  1.00 69.40           C
ANISOU 3047  C   GLY A 370     8631   8844   8892  -1964   -548  -3540       C
ATOM   3048  O   GLY A 370     -47.514 -10.887   1.561  1.00 69.53           O
ANISOU 3048  O   GLY A 370     8673   8678   9066  -2018   -504  -3673       O
ATOM   3049  N   GLU A 371     -46.748  -8.893   0.860  1.00 89.92           N
ANISOU 3049  N   GLU A 371    11269  11626  11272  -1871   -551  -3541       N
ATOM   3050  CA  GLU A 371     -45.733  -9.489   0.002  1.00 99.61           C
ANISOU 3050  CA  GLU A 371    12575  12836  12438  -1820   -492  -3697       C
ATOM   3051  C   GLU A 371     -44.543  -8.543  -0.108  1.00 96.03           C
ANISOU 3051  C   GLU A 371    12176  12483  11828  -1693   -442  -3602       C
ATOM   3052  O   GLU A 371     -44.676  -7.329   0.073  1.00 91.96           O
ANISOU 3052  O   GLU A 371    11628  12126  11189  -1655   -484  -3450       O
ATOM   3053  CB  GLU A 371     -46.298  -9.836  -1.385  1.00111.35           C
ANISOU 3053  CB  GLU A 371    14030  14500  13776  -1873   -574  -3891       C
ATOM   3054  CG  GLU A 371     -45.312 -10.498  -2.361  1.00119.43           C
ANISOU 3054  CG  GLU A 371    15131  15522  14726  -1823   -514  -4072       C
ATOM   3055  CD  GLU A 371     -44.464 -11.598  -1.728  1.00123.05           C
ANISOU 3055  CD  GLU A 371    15665  15672  15415  -1805   -389  -4123       C
ATOM   3056  OE1 GLU A 371     -44.992 -12.380  -0.909  1.00125.28           O
ANISOU 3056  OE1 GLU A 371    15931  15735  15936  -1881   -370  -4117       O
ATOM   3057  OE2 GLU A 371     -43.260 -11.677  -2.053  1.00123.30           O
ANISOU 3057  OE2 GLU A 371    15770  15686  15393  -1711   -307  -4161       O
ATOM   3058  N   PHE A 372     -43.374  -9.134  -0.369  1.00 94.12           N
ANISOU 3058  N   PHE A 372    12016  12137  11610  -1628   -345  -3690       N
ATOM   3059  CA  PHE A 372     -42.120  -8.412  -0.552  1.00 93.37           C
ANISOU 3059  CA  PHE A 372    11975  12119  11384  -1509   -282  -3625       C
ATOM   3060  C   PHE A 372     -42.296  -7.198  -1.454  1.00 88.40           C
ANISOU 3060  C   PHE A 372    11308  11807  10472  -1475   -357  -3578       C
ATOM   3061  O   PHE A 372     -42.967  -7.263  -2.487  1.00 92.46           O
ANISOU 3061  O   PHE A 372    11786  12499  10845  -1517   -436  -3686       O
ATOM   3062  CB  PHE A 372     -41.080  -9.361  -1.160  1.00100.22           C
ANISOU 3062  CB  PHE A 372    12917  12890  12274  -1461   -190  -3787       C
ATOM   3063  CG  PHE A 372     -39.652  -9.047  -0.785  1.00102.73           C
ANISOU 3063  CG  PHE A 372    13296  13140  12597  -1343    -83  -3706       C
ATOM   3064  CD1 PHE A 372     -39.270  -7.770  -0.402  1.00 99.05           C
ANISOU 3064  CD1 PHE A 372    12818  12790  12026  -1280    -84  -3531       C
ATOM   3065  CD2 PHE A 372     -38.686 -10.041  -0.834  1.00104.66           C
ANISOU 3065  CD2 PHE A 372    13604  13206  12956  -1294     21  -3809       C
ATOM   3066  CE1 PHE A 372     -37.958  -7.493  -0.068  1.00 98.01           C
ANISOU 3066  CE1 PHE A 372    12735  12598  11905  -1176     14  -3465       C
ATOM   3067  CE2 PHE A 372     -37.373  -9.771  -0.501  1.00102.94           C
ANISOU 3067  CE2 PHE A 372    13433  12931  12748  -1183    120  -3736       C
ATOM   3068  CZ  PHE A 372     -37.008  -8.495  -0.117  1.00 99.69           C
ANISOU 3068  CZ  PHE A 372    13006  12639  12232  -1126    115  -3566       C
ATOM   3069  N   THR A 373     -41.685  -6.087  -1.050  1.00 79.14           N
ANISOU 3069  N   THR A 373    10144  10706   9220  -1396   -332  -3413       N
ATOM   3070  CA  THR A 373     -41.607  -4.904  -1.892  1.00 74.86           C
ANISOU 3070  CA  THR A 373     9577  10452   8413  -1344   -379  -3347       C
ATOM   3071  C   THR A 373     -40.415  -4.062  -1.461  1.00 76.75           C
ANISOU 3071  C   THR A 373     9857  10690   8614  -1243   -298  -3213       C
ATOM   3072  O   THR A 373     -39.987  -4.107  -0.304  1.00 76.79           O
ANISOU 3072  O   THR A 373     9885  10499   8793  -1226   -241  -3128       O
ATOM   3073  CB  THR A 373     -42.891  -4.069  -1.829  1.00 65.79           C
ANISOU 3073  CB  THR A 373     8341   9468   7188  -1394   -498  -3239       C
ATOM   3074  OG1 THR A 373     -42.744  -2.909  -2.655  1.00 68.50           O
ANISOU 3074  OG1 THR A 373     8662  10088   7275  -1330   -535  -3155       O
ATOM   3075  CG2 THR A 373     -43.171  -3.624  -0.409  1.00 56.15           C
ANISOU 3075  CG2 THR A 373     7098   8108   6130  -1408   -496  -3073       C
ATOM   3076  N   LEU A 374     -39.876  -3.306  -2.415  1.00 72.87           N
ANISOU 3076  N   LEU A 374     9371  10424   7892  -1174   -291  -3194       N
ATOM   3077  CA  LEU A 374     -38.888  -2.275  -2.140  1.00 66.07           C
ANISOU 3077  CA  LEU A 374     8529   9618   6957  -1086   -229  -3049       C
ATOM   3078  C   LEU A 374     -39.452  -0.881  -2.370  1.00 70.55           C
ANISOU 3078  C   LEU A 374     9037  10428   7342  -1072   -308  -2887       C
ATOM   3079  O   LEU A 374     -38.687   0.088  -2.442  1.00 71.39           O
ANISOU 3079  O   LEU A 374     9151  10639   7335   -998   -264  -2769       O
ATOM   3080  CB  LEU A 374     -37.641  -2.495  -2.995  1.00 62.94           C
ANISOU 3080  CB  LEU A 374     8187   9275   6453  -1005   -132  -3134       C
ATOM   3081  CG  LEU A 374     -36.925  -3.818  -2.726  1.00 61.34           C
ANISOU 3081  CG  LEU A 374     8044   8824   6438   -997    -40  -3278       C
ATOM   3082  CD1 LEU A 374     -35.861  -4.082  -3.778  1.00 57.77           C
ANISOU 3082  CD1 LEU A 374     7636   8461   5855   -921     45  -3383       C
ATOM   3083  CD2 LEU A 374     -36.328  -3.817  -1.326  1.00 60.32           C
ANISOU 3083  CD2 LEU A 374     7935   8459   6522   -972     26  -3176       C
ATOM   3084  N   THR A 375     -40.780  -0.764  -2.489  1.00 70.50           N
ANISOU 3084  N   THR A 375     8966  10511   7310  -1140   -421  -2872       N
ATOM   3085  CA  THR A 375     -41.409   0.529  -2.739  1.00 66.55           C
ANISOU 3085  CA  THR A 375     8401  10242   6643  -1120   -502  -2709       C
ATOM   3086  C   THR A 375     -41.131   1.500  -1.603  1.00 64.40           C
ANISOU 3086  C   THR A 375     8122   9904   6444  -1090   -481  -2523       C
ATOM   3087  O   THR A 375     -40.724   2.645  -1.833  1.00 64.26           O
ANISOU 3087  O   THR A 375     8094  10045   6278  -1023   -473  -2380       O
ATOM   3088  CB  THR A 375     -42.917   0.351  -2.927  1.00 67.38           C
ANISOU 3088  CB  THR A 375     8430  10421   6750  -1200   -623  -2734       C
ATOM   3089  OG1 THR A 375     -43.174  -0.268  -4.191  1.00 72.23           O
ANISOU 3089  OG1 THR A 375     9041  11169   7235  -1217   -656  -2892       O
ATOM   3090  CG2 THR A 375     -43.625   1.694  -2.878  1.00 68.20           C
ANISOU 3090  CG2 THR A 375     8461  10717   6736  -1175   -703  -2536       C
ATOM   3091  N   ASN A 376     -41.348   1.058  -0.363  1.00 65.10           N
ANISOU 3091  N   ASN A 376     8215   9760   6759  -1137   -472  -2517       N
ATOM   3092  CA  ASN A 376     -41.087   1.925   0.777  1.00 65.26           C
ANISOU 3092  CA  ASN A 376     8230   9709   6856  -1111   -454  -2356       C
ATOM   3093  C   ASN A 376     -39.613   2.278   0.885  1.00 59.43           C
ANISOU 3093  C   ASN A 376     7552   8926   6104  -1024   -346  -2310       C
ATOM   3094  O   ASN A 376     -39.276   3.392   1.300  1.00 55.56           O
ANISOU 3094  O   ASN A 376     7049   8446   5613   -949   -329  -2091       O
ATOM   3095  CB  ASN A 376     -41.573   1.263   2.062  1.00 64.97           C
ANISOU 3095  CB  ASN A 376     8190   9428   7069  -1172   -454  -2362       C
ATOM   3096  CG  ASN A 376     -43.075   1.224   2.151  1.00 60.83           C
ANISOU 3096  CG  ASN A 376     7587   8956   6571  -1248   -558  -2343       C
ATOM   3097  OD1 ASN A 376     -43.742   2.240   1.956  1.00 63.52           O
ANISOU 3097  OD1 ASN A 376     7864   9480   6792  -1237   -634  -2224       O
ATOM   3098  ND2 ASN A 376     -43.623   0.048   2.433  1.00 58.03           N
ANISOU 3098  ND2 ASN A 376     7230   8442   6377  -1321   -559  -2453       N
ATOM   3099  N   ALA A 377     -38.722   1.352   0.523  1.00 57.97           N
ANISOU 3099  N   ALA A 377     7427   8653   5946  -1008   -262  -2464       N
ATOM   3100  CA  ALA A 377     -37.298   1.667   0.533  1.00 57.62           C
ANISOU 3100  CA  ALA A 377     7427   8572   5893   -914   -152  -2407       C
ATOM   3101  C   ALA A 377     -37.014   2.890  -0.327  1.00 60.96           C
ANISOU 3101  C   ALA A 377     7825   9238   6099   -844   -153  -2263       C
ATOM   3102  O   ALA A 377     -36.354   3.839   0.117  1.00 64.01           O
ANISOU 3102  O   ALA A 377     8207   9593   6522   -770   -108  -2061       O
ATOM   3103  CB  ALA A 377     -36.482   0.463   0.058  1.00 54.04           C
ANISOU 3103  CB  ALA A 377     7031   8026   5475   -904    -66  -2610       C
ATOM   3104  N   VAL A 378     -37.541   2.902  -1.553  1.00 61.06           N
ANISOU 3104  N   VAL A 378     7818   9498   5886   -870   -207  -2359       N
ATOM   3105  CA  VAL A 378     -37.355   4.060  -2.421  1.00 65.04           C
ANISOU 3105  CA  VAL A 378     8293  10249   6170   -800   -207  -2203       C
ATOM   3106  C   VAL A 378     -38.034   5.284  -1.821  1.00 65.76           C
ANISOU 3106  C   VAL A 378     8329  10359   6296   -782   -273  -1950       C
ATOM   3107  O   VAL A 378     -37.395   6.319  -1.604  1.00 67.50           O
ANISOU 3107  O   VAL A 378     8543  10572   6531   -705   -220  -1741       O
ATOM   3108  CB  VAL A 378     -37.868   3.761  -3.841  1.00 67.16           C
ANISOU 3108  CB  VAL A 378     8546  10746   6225   -809   -256  -2310       C
ATOM   3109  CG1 VAL A 378     -38.123   5.057  -4.597  1.00 67.63           C
ANISOU 3109  CG1 VAL A 378     8557  11085   6054   -753   -293  -2121       C
ATOM   3110  CG2 VAL A 378     -36.864   2.896  -4.590  1.00 65.76           C
ANISOU 3110  CG2 VAL A 378     8426  10547   6013   -772   -157  -2470       C
ATOM   3111  N   LEU A 379     -39.322   5.161  -1.487  1.00 63.88           N
ANISOU 3111  N   LEU A 379     8045  10130   6097   -854   -383  -1970       N
ATOM   3112  CA  LEU A 379     -40.094   6.307  -1.013  1.00 59.09           C
ANISOU 3112  CA  LEU A 379     7379   9564   5509   -833   -449  -1744       C
ATOM   3113  C   LEU A 379     -39.476   6.958   0.220  1.00 56.24           C
ANISOU 3113  C   LEU A 379     7033   8985   5349   -779   -387  -1562       C
ATOM   3114  O   LEU A 379     -39.676   8.155   0.452  1.00 59.43           O
ANISOU 3114  O   LEU A 379     7400   9428   5750   -728   -404  -1350       O
ATOM   3115  CB  LEU A 379     -41.529   5.876  -0.712  1.00 54.91           C
ANISOU 3115  CB  LEU A 379     6793   9045   5025   -926   -566  -1820       C
ATOM   3116  CG  LEU A 379     -42.366   5.478  -1.927  1.00 57.71           C
ANISOU 3116  CG  LEU A 379     7107   9628   5194   -970   -652  -1950       C
ATOM   3117  CD1 LEU A 379     -43.816   5.269  -1.527  1.00 53.53           C
ANISOU 3117  CD1 LEU A 379     6503   9076   4757  -1041   -758  -1951       C
ATOM   3118  CD2 LEU A 379     -42.248   6.524  -3.024  1.00 60.39           C
ANISOU 3118  CD2 LEU A 379     7418  10242   5284   -888   -664  -1810       C
ATOM   3119  N   HIS A 380     -38.723   6.202   1.020  1.00 53.86           N
ANISOU 3119  N   HIS A 380     6785   8457   5225   -786   -316  -1643       N
ATOM   3120  CA  HIS A 380     -38.177   6.752   2.252  1.00 57.11           C
ANISOU 3120  CA  HIS A 380     7205   8671   5821   -739   -270  -1489       C
ATOM   3121  C   HIS A 380     -36.691   7.084   2.185  1.00 54.16           C
ANISOU 3121  C   HIS A 380     6866   8249   5463   -662   -161  -1430       C
ATOM   3122  O   HIS A 380     -36.223   7.878   3.008  1.00 56.37           O
ANISOU 3122  O   HIS A 380     7138   8423   5857   -615   -133  -1274       O
ATOM   3123  CB  HIS A 380     -38.426   5.788   3.420  1.00 63.12           C
ANISOU 3123  CB  HIS A 380     7987   9208   6789   -790   -273  -1577       C
ATOM   3124  CG  HIS A 380     -39.836   5.811   3.925  1.00 75.36           C
ANISOU 3124  CG  HIS A 380     9487  10761   8386   -851   -367  -1554       C
ATOM   3125  ND1 HIS A 380     -40.211   6.500   5.058  1.00 76.12           N
ANISOU 3125  ND1 HIS A 380     9558  10761   8605   -827   -386  -1397       N
ATOM   3126  CD2 HIS A 380     -40.964   5.238   3.443  1.00 78.28           C
ANISOU 3126  CD2 HIS A 380     9820  11227   8697   -935   -447  -1673       C
ATOM   3127  CE1 HIS A 380     -41.509   6.347   5.254  1.00 75.81           C
ANISOU 3127  CE1 HIS A 380     9467  10757   8580   -889   -466  -1411       C
ATOM   3128  NE2 HIS A 380     -41.989   5.585   4.288  1.00 77.24           N
ANISOU 3128  NE2 HIS A 380     9636  11053   8657   -959   -507  -1575       N
ATOM   3129  N   PHE A 381     -35.931   6.525   1.237  1.00 49.72           N
ANISOU 3129  N   PHE A 381     6335   7764   4791   -649    -98  -1554       N
ATOM   3130  CA  PHE A 381     -34.501   6.788   1.213  1.00 52.24           C
ANISOU 3130  CA  PHE A 381     6675   8032   5141   -578     12  -1498       C
ATOM   3131  C   PHE A 381     -33.952   7.249  -0.130  1.00 59.26           C
ANISOU 3131  C   PHE A 381     7558   9139   5819   -532     65  -1472       C
ATOM   3132  O   PHE A 381     -32.747   7.499  -0.219  1.00 64.79           O
ANISOU 3132  O   PHE A 381     8265   9810   6542   -474    164  -1419       O
ATOM   3133  CB  PHE A 381     -33.722   5.539   1.658  1.00 43.60           C
ANISOU 3133  CB  PHE A 381     5629   6756   4180   -582     79  -1663       C
ATOM   3134  CG  PHE A 381     -34.117   5.031   3.016  1.00 41.80           C
ANISOU 3134  CG  PHE A 381     5410   6309   4163   -615     45  -1672       C
ATOM   3135  CD1 PHE A 381     -33.882   5.790   4.151  1.00 39.01           C
ANISOU 3135  CD1 PHE A 381     5038   5837   3947   -579     44  -1504       C
ATOM   3136  CD2 PHE A 381     -34.724   3.792   3.158  1.00 43.78           C
ANISOU 3136  CD2 PHE A 381     5686   6474   4475   -682     18  -1850       C
ATOM   3137  CE1 PHE A 381     -34.247   5.322   5.405  1.00 40.45           C
ANISOU 3137  CE1 PHE A 381     5228   5838   4303   -601     17  -1505       C
ATOM   3138  CE2 PHE A 381     -35.089   3.319   4.409  1.00 43.77           C
ANISOU 3138  CE2 PHE A 381     5690   6276   4665   -708     -2  -1837       C
ATOM   3139  CZ  PHE A 381     -34.852   4.088   5.533  1.00 40.42           C
ANISOU 3139  CZ  PHE A 381     5249   5754   4355   -663     -2  -1661       C
ATOM   3140  N   GLY A 382     -34.780   7.397  -1.163  1.00 57.91           N
ANISOU 3140  N   GLY A 382     7367   9196   5441   -552      3  -1497       N
ATOM   3141  CA  GLY A 382     -34.188   7.693  -2.450  1.00 61.34           C
ANISOU 3141  CA  GLY A 382     7800   9846   5659   -501     66  -1484       C
ATOM   3142  C   GLY A 382     -33.276   6.567  -2.899  1.00 62.78           C
ANISOU 3142  C   GLY A 382     8031  10002   5820   -494    155  -1695       C
ATOM   3143  O   GLY A 382     -33.438   5.402  -2.519  1.00 68.63           O
ANISOU 3143  O   GLY A 382     8807  10608   6661   -545    141  -1895       O
ATOM   3144  N   ALA A 383     -32.285   6.922  -3.718  1.00 58.59           N
ANISOU 3144  N   ALA A 383     7501   9596   5165   -426    258  -1645       N
ATOM   3145  CA  ALA A 383     -31.270   5.957  -4.122  1.00 59.89           C
ANISOU 3145  CA  ALA A 383     7707   9732   5319   -401    363  -1828       C
ATOM   3146  C   ALA A 383     -30.369   5.541  -2.970  1.00 56.62           C
ANISOU 3146  C   ALA A 383     7308   9035   5169   -385    429  -1835       C
ATOM   3147  O   ALA A 383     -29.526   4.645  -3.147  1.00 57.10           O
ANISOU 3147  O   ALA A 383     7400   9033   5261   -360    517  -1990       O
ATOM   3148  CB  ALA A 383     -30.422   6.534  -5.256  1.00 64.18           C
ANISOU 3148  CB  ALA A 383     8235  10490   5662   -325    467  -1745       C
ATOM   3149  N   LEU A 384     -30.534   6.167  -1.803  1.00 52.50           N
ANISOU 3149  N   LEU A 384     6764   8352   4834   -394    387  -1674       N
ATOM   3150  CA  LEU A 384     -29.619   5.927  -0.698  1.00 48.77           C
ANISOU 3150  CA  LEU A 384     6295   7641   4594   -368    444  -1653       C
ATOM   3151  C   LEU A 384     -29.784   4.532  -0.117  1.00 50.49           C
ANISOU 3151  C   LEU A 384     6558   7681   4945   -404    431  -1856       C
ATOM   3152  O   LEU A 384     -28.823   3.993   0.427  1.00 54.45           O
ANISOU 3152  O   LEU A 384     7072   8025   5592   -365    506  -1895       O
ATOM   3153  CB  LEU A 384     -29.802   6.986   0.388  1.00 42.69           C
ANISOU 3153  CB  LEU A 384     5488   6763   3970   -367    396  -1441       C
ATOM   3154  CG  LEU A 384     -29.578   8.430  -0.069  1.00 46.40           C
ANISOU 3154  CG  LEU A 384     5910   7364   4356   -330    419  -1222       C
ATOM   3155  CD1 LEU A 384     -29.599   9.380   1.118  1.00 45.76           C
ANISOU 3155  CD1 LEU A 384     5795   7134   4456   -327    384  -1047       C
ATOM   3156  CD2 LEU A 384     -28.272   8.560  -0.838  1.00 49.53           C
ANISOU 3156  CD2 LEU A 384     6291   7840   4687   -270    549  -1201       C
ATOM   3157  N   PHE A 385     -30.961   3.914  -0.244  1.00 47.03           N
ANISOU 3157  N   PHE A 385     6140   7263   4467   -477    343  -1985       N
ATOM   3158  CA  PHE A 385     -31.103   2.545   0.245  1.00 51.52           C
ANISOU 3158  CA  PHE A 385     6750   7649   5176   -516    344  -2178       C
ATOM   3159  C   PHE A 385     -30.192   1.595  -0.522  1.00 58.54           C
ANISOU 3159  C   PHE A 385     7676   8545   6021   -479    448  -2370       C
ATOM   3160  O   PHE A 385     -29.482   0.777   0.073  1.00 61.61           O
ANISOU 3160  O   PHE A 385     8090   8738   6581   -450    514  -2442       O
ATOM   3161  CB  PHE A 385     -32.553   2.078   0.143  1.00 54.65           C
ANISOU 3161  CB  PHE A 385     7149   8079   5537   -613    233  -2288       C
ATOM   3162  CG  PHE A 385     -32.750   0.637   0.539  1.00 51.20           C
ANISOU 3162  CG  PHE A 385     6752   7450   5250   -664    241  -2494       C
ATOM   3163  CD1 PHE A 385     -32.767   0.268   1.876  1.00 42.39           C
ANISOU 3163  CD1 PHE A 385     5643   6092   4370   -670    240  -2438       C
ATOM   3164  CD2 PHE A 385     -32.906  -0.350  -0.426  1.00 52.97           C
ANISOU 3164  CD2 PHE A 385     7006   7736   5382   -702    253  -2744       C
ATOM   3165  CE1 PHE A 385     -32.945  -1.058   2.243  1.00 43.51           C
ANISOU 3165  CE1 PHE A 385     5821   6045   4666   -714    258  -2606       C
ATOM   3166  CE2 PHE A 385     -33.084  -1.676  -0.065  1.00 46.38           C
ANISOU 3166  CE2 PHE A 385     6204   6682   4739   -733    261  -2864       C
ATOM   3167  CZ  PHE A 385     -33.104  -2.029   1.271  1.00 42.81           C
ANISOU 3167  CZ  PHE A 385     5758   5988   4518   -747    270  -2816       C
ATOM   3168  N   PHE A 386     -30.181   1.705  -1.848  1.00 59.02           N
ANISOU 3168  N   PHE A 386     7738   8838   5848   -469    468  -2449       N
ATOM   3169  CA  PHE A 386     -29.357   0.806  -2.646  1.00 60.23           C
ANISOU 3169  CA  PHE A 386     7928   9017   5941   -429    572  -2648       C
ATOM   3170  C   PHE A 386     -27.884   1.177  -2.556  1.00 59.21           C
ANISOU 3170  C   PHE A 386     7780   8855   5862   -329    700  -2538       C
ATOM   3171  O   PHE A 386     -27.021   0.293  -2.449  1.00 59.47           O
ANISOU 3171  O   PHE A 386     7838   8758   6000   -284    794  -2662       O
ATOM   3172  CB  PHE A 386     -29.851   0.813  -4.089  1.00 65.81           C
ANISOU 3172  CB  PHE A 386     8638   9993   6376   -444    544  -2752       C
ATOM   3173  CG  PHE A 386     -31.333   0.622  -4.204  1.00 72.81           C
ANISOU 3173  CG  PHE A 386     9516  10913   7235   -534    397  -2788       C
ATOM   3174  CD1 PHE A 386     -31.890  -0.640  -4.082  1.00 74.07           C
ANISOU 3174  CD1 PHE A 386     9705  10904   7534   -590    354  -2952       C
ATOM   3175  CD2 PHE A 386     -32.174   1.705  -4.393  1.00 75.21           C
ANISOU 3175  CD2 PHE A 386     9776  11411   7389   -560    307  -2646       C
ATOM   3176  CE1 PHE A 386     -33.255  -0.822  -4.171  1.00 75.93           C
ANISOU 3176  CE1 PHE A 386     9920  11172   7758   -677    226  -2984       C
ATOM   3177  CE2 PHE A 386     -33.542   1.530  -4.481  1.00 75.76           C
ANISOU 3177  CE2 PHE A 386     9826  11514   7446   -639    173  -2675       C
ATOM   3178  CZ  PHE A 386     -34.083   0.265  -4.371  1.00 76.25           C
ANISOU 3178  CZ  PHE A 386     9911  11413   7647   -700    134  -2848       C
ATOM   3179  N   PHE A 387     -27.571   2.478  -2.565  1.00 58.77           N
ANISOU 3179  N   PHE A 387     7677   8904   5750   -293    709  -2301       N
ATOM   3180  CA  PHE A 387     -26.177   2.880  -2.397  1.00 56.93           C
ANISOU 3180  CA  PHE A 387     7411   8630   5591   -209    826  -2186       C
ATOM   3181  C   PHE A 387     -25.647   2.477  -1.024  1.00 58.36           C
ANISOU 3181  C   PHE A 387     7588   8537   6049   -193    837  -2157       C
ATOM   3182  O   PHE A 387     -24.477   2.095  -0.896  1.00 67.18           O
ANISOU 3182  O   PHE A 387     8694   9574   7259   -125    941  -2182       O
ATOM   3183  CB  PHE A 387     -26.026   4.386  -2.625  1.00 52.05           C
ANISOU 3183  CB  PHE A 387     6736   8157   4885   -187    829  -1932       C
ATOM   3184  CG  PHE A 387     -25.811   4.771  -4.071  1.00 48.12           C
ANISOU 3184  CG  PHE A 387     6228   7934   4122   -152    895  -1927       C
ATOM   3185  CD1 PHE A 387     -24.532   4.906  -4.587  1.00 49.89           C
ANISOU 3185  CD1 PHE A 387     6424   8220   4313    -76   1037  -1893       C
ATOM   3186  CD2 PHE A 387     -26.888   5.002  -4.910  1.00 51.73           C
ANISOU 3186  CD2 PHE A 387     6696   8600   4358   -189    815  -1949       C
ATOM   3187  CE1 PHE A 387     -24.332   5.262  -5.917  1.00 53.83           C
ANISOU 3187  CE1 PHE A 387     6912   8985   4555    -36   1108  -1876       C
ATOM   3188  CE2 PHE A 387     -26.696   5.357  -6.240  1.00 54.62           C
ANISOU 3188  CE2 PHE A 387     7052   9240   4460   -147    875  -1934       C
ATOM   3189  CZ  PHE A 387     -25.415   5.487  -6.743  1.00 52.34           C
ANISOU 3189  CZ  PHE A 387     6742   9012   4135    -70   1026  -1894       C
ATOM   3190  N   GLY A 388     -26.502   2.496  -0.000  1.00 52.70           N
ANISOU 3190  N   GLY A 388     6878   7684   5461   -248    732  -2109       N
ATOM   3191  CA  GLY A 388     -26.129   2.070   1.328  1.00 52.05           C
ANISOU 3191  CA  GLY A 388     6795   7360   5621   -231    731  -2080       C
ATOM   3192  C   GLY A 388     -25.990   0.571   1.460  1.00 57.70           C
ANISOU 3192  C   GLY A 388     7561   7921   6443   -226    772  -2287       C
ATOM   3193  O   GLY A 388     -25.100   0.110   2.168  1.00 58.24           O
ANISOU 3193  O   GLY A 388     7621   7829   6677   -167    832  -2278       O
ATOM   3194  N   MET A 389     -26.854  -0.209   0.806  1.00 63.95           N
ANISOU 3194  N   MET A 389     8398   8752   7150   -287    739  -2476       N
ATOM   3195  CA  MET A 389     -26.642  -1.653   0.790  1.00 65.74           C
ANISOU 3195  CA  MET A 389     8672   8823   7482   -281    795  -2691       C
ATOM   3196  C   MET A 389     -25.318  -1.989   0.122  1.00 67.42           C
ANISOU 3196  C   MET A 389     8883   9069   7663   -186    932  -2769       C
ATOM   3197  O   MET A 389     -24.591  -2.886   0.573  1.00 70.41           O
ANISOU 3197  O   MET A 389     9277   9266   8212   -130   1007  -2842       O
ATOM   3198  CB  MET A 389     -27.799  -2.355   0.079  1.00 73.23           C
ANISOU 3198  CB  MET A 389     9661   9828   8335   -373    734  -2898       C
ATOM   3199  CG  MET A 389     -29.138  -2.268   0.798  1.00 75.92           C
ANISOU 3199  CG  MET A 389     9998  10106   8743   -470    607  -2848       C
ATOM   3200  SD  MET A 389     -29.072  -2.775   2.526  1.00 75.78           S
ANISOU 3200  SD  MET A 389     9984   9775   9032   -461    604  -2745       S
ATOM   3201  CE  MET A 389     -28.476  -4.458   2.361  1.00 77.28           C
ANISOU 3201  CE  MET A 389    10225   9762   9376   -424    696  -2935       C
ATOM   3202  N   ALA A 390     -24.982  -1.265  -0.950  1.00 66.83           N
ANISOU 3202  N   ALA A 390     8785   9232   7375   -160    972  -2742       N
ATOM   3203  CA  ALA A 390     -23.682  -1.443  -1.590  1.00 60.61           C
ANISOU 3203  CA  ALA A 390     7982   8500   6546    -63   1113  -2790       C
ATOM   3204  C   ALA A 390     -22.548  -1.103  -0.630  1.00 63.98           C
ANISOU 3204  C   ALA A 390     8355   8792   7161     13   1169  -2619       C
ATOM   3205  O   ALA A 390     -21.586  -1.868  -0.486  1.00 66.97           O
ANISOU 3205  O   ALA A 390     8731   9055   7658     89   1268  -2697       O
ATOM   3206  CB  ALA A 390     -23.603  -0.583  -2.851  1.00 48.55           C
ANISOU 3206  CB  ALA A 390     6433   7268   4747    -51   1143  -2748       C
ATOM   3207  N   GLY A 391     -22.643   0.053   0.030  1.00 62.30           N
ANISOU 3207  N   GLY A 391     8093   8598   6979     -4   1106  -2390       N
ATOM   3208  CA  GLY A 391     -21.640   0.426   1.012  1.00 58.68           C
ANISOU 3208  CA  GLY A 391     7575   8020   6700     57   1139  -2236       C
ATOM   3209  C   GLY A 391     -21.525  -0.564   2.154  1.00 61.99           C
ANISOU 3209  C   GLY A 391     8015   8191   7347     79   1126  -2285       C
ATOM   3210  O   GLY A 391     -20.431  -0.795   2.665  1.00 59.86           O
ANISOU 3210  O   GLY A 391     7704   7826   7215    160   1194  -2247       O
ATOM   3211  N   ILE A 392     -22.642  -1.182   2.550  1.00 63.01           N
ANISOU 3211  N   ILE A 392     8202   8217   7520     11   1043  -2365       N
ATOM   3212  CA  ILE A 392     -22.629  -2.138   3.655  1.00 59.06           C
ANISOU 3212  CA  ILE A 392     7723   7477   7238     31   1034  -2392       C
ATOM   3213  C   ILE A 392     -21.927  -3.423   3.239  1.00 61.03           C
ANISOU 3213  C   ILE A 392     8003   7626   7559     97   1147  -2578       C
ATOM   3214  O   ILE A 392     -21.091  -3.959   3.975  1.00 60.88           O
ANISOU 3214  O   ILE A 392     7964   7452   7716    179   1200  -2547       O
ATOM   3215  CB  ILE A 392     -24.060  -2.418   4.147  1.00 54.04           C
ANISOU 3215  CB  ILE A 392     7135   6766   6633    -68    924  -2417       C
ATOM   3216  CG1 ILE A 392     -24.608  -1.226   4.927  1.00 53.25           C
ANISOU 3216  CG1 ILE A 392     6997   6710   6524   -107    821  -2212       C
ATOM   3217  CG2 ILE A 392     -24.093  -3.646   5.034  1.00 47.60           C
ANISOU 3217  CG2 ILE A 392     6353   5704   6029    -49    940  -2479       C
ATOM   3218  CD1 ILE A 392     -26.102  -1.297   5.159  1.00 47.99           C
ANISOU 3218  CD1 ILE A 392     6364   6030   5840   -208    716  -2232       C
ATOM   3219  N   LEU A 393     -22.259  -3.942   2.054  1.00 61.21           N
ANISOU 3219  N   LEU A 393     8072   7739   7446     68   1184  -2777       N
ATOM   3220  CA  LEU A 393     -21.562  -5.126   1.561  1.00 61.25           C
ANISOU 3220  CA  LEU A 393     8105   7654   7512    137   1290  -2946       C
ATOM   3221  C   LEU A 393     -20.070  -4.854   1.396  1.00 66.31           C
ANISOU 3221  C   LEU A 393     8684   8344   8166    256   1417  -2902       C
ATOM   3222  O   LEU A 393     -19.227  -5.682   1.777  1.00 72.25           O
ANISOU 3222  O   LEU A 393     9429   8941   9084    346   1484  -2911       O
ATOM   3223  CB  LEU A 393     -22.178  -5.584   0.241  1.00 61.97           C
ANISOU 3223  CB  LEU A 393     8249   7867   7428     86   1268  -3096       C
ATOM   3224  CG  LEU A 393     -23.135  -6.778   0.307  1.00 66.01           C
ANISOU 3224  CG  LEU A 393     8825   8220   8036     18   1200  -3209       C
ATOM   3225  CD1 LEU A 393     -22.362  -8.072   0.518  1.00 70.70           C
ANISOU 3225  CD1 LEU A 393     9443   8603   8817    101   1282  -3277       C
ATOM   3226  CD2 LEU A 393     -24.193  -6.595   1.393  1.00 59.62           C
ANISOU 3226  CD2 LEU A 393     8018   7302   7334    -69   1093  -3123       C
ATOM   3227  N   TYR A 394     -19.722  -3.684   0.855  1.00 68.07           N
ANISOU 3227  N   TYR A 394     8854   8783   8228    260   1427  -2783       N
ATOM   3228  CA  TYR A 394     -18.313  -3.367   0.650  1.00 72.37           C
ANISOU 3228  CA  TYR A 394     9324   9388   8785    365   1542  -2712       C
ATOM   3229  C   TYR A 394     -17.583  -3.201   1.976  1.00 68.24           C
ANISOU 3229  C   TYR A 394     8735   8712   8480    422   1528  -2541       C
ATOM   3230  O   TYR A 394     -16.438  -3.642   2.117  1.00 72.50           O
ANISOU 3230  O   TYR A 394     9227   9188   9132    525   1626  -2549       O
ATOM   3231  CB  TYR A 394     -18.165  -2.105  -0.194  1.00 77.31           C
ANISOU 3231  CB  TYR A 394     9903  10271   9202    346   1556  -2599       C
ATOM   3232  CG  TYR A 394     -16.736  -1.630  -0.262  1.00 81.62           C
ANISOU 3232  CG  TYR A 394    10353  10873   9787    440   1668  -2488       C
ATOM   3233  CD1 TYR A 394     -15.775  -2.362  -0.945  1.00 84.16           C
ANISOU 3233  CD1 TYR A 394    10661  11214  10102    535   1813  -2621       C
ATOM   3234  CD2 TYR A 394     -16.339  -0.464   0.379  1.00 83.91           C
ANISOU 3234  CD2 TYR A 394    10558  11188  10134    432   1630  -2257       C
ATOM   3235  CE1 TYR A 394     -14.462  -1.940  -1.002  1.00 87.76           C
ANISOU 3235  CE1 TYR A 394    11016  11726  10602    619   1920  -2515       C
ATOM   3236  CE2 TYR A 394     -15.027  -0.034   0.327  1.00 85.51           C
ANISOU 3236  CE2 TYR A 394    10660  11440  10390    507   1730  -2159       C
ATOM   3237  CZ  TYR A 394     -14.093  -0.775  -0.365  1.00 88.71           C
ANISOU 3237  CZ  TYR A 394    11047  11874  10784    601   1876  -2282       C
ATOM   3238  OH  TYR A 394     -12.782  -0.351  -0.420  1.00 92.03           O
ANISOU 3238  OH  TYR A 394    11353  12349  11264    675   1980  -2181       O
ATOM   3239  N   SER A 395     -18.222  -2.558   2.954  1.00 64.87           N
ANISOU 3239  N   SER A 395     8300   8237   8110    361   1405  -2388       N
ATOM   3240  CA  SER A 395     -17.623  -2.428   4.273  1.00 61.38           C
ANISOU 3240  CA  SER A 395     7799   7662   7861    412   1375  -2239       C
ATOM   3241  C   SER A 395     -17.463  -3.783   4.943  1.00 64.02           C
ANISOU 3241  C   SER A 395     8169   7775   8383    473   1404  -2328       C
ATOM   3242  O   SER A 395     -16.493  -3.996   5.672  1.00 64.92           O
ANISOU 3242  O   SER A 395     8221   7799   8645    567   1439  -2252       O
ATOM   3243  CB  SER A 395     -18.471  -1.502   5.142  1.00 59.20           C
ANISOU 3243  CB  SER A 395     7519   7388   7589    332   1237  -2083       C
ATOM   3244  OG  SER A 395     -17.862  -1.285   6.398  1.00 61.20           O
ANISOU 3244  OG  SER A 395     7709   7542   8003    383   1203  -1944       O
ATOM   3245  N   ALA A 396     -18.392  -4.710   4.704  1.00 63.91           N
ANISOU 3245  N   ALA A 396     8245   7667   8370    423   1390  -2483       N
ATOM   3246  CA  ALA A 396     -18.244  -6.056   5.244  1.00 59.62           C
ANISOU 3246  CA  ALA A 396     7739   6896   8019    482   1435  -2571       C
ATOM   3247  C   ALA A 396     -17.017  -6.737   4.659  1.00 62.39           C
ANISOU 3247  C   ALA A 396     8063   7228   8416    601   1576  -2667       C
ATOM   3248  O   ALA A 396     -16.220  -7.344   5.385  1.00 71.68           O
ANISOU 3248  O   ALA A 396     9206   8262   9768    704   1614  -2606       O
ATOM   3249  CB  ALA A 396     -19.505  -6.874   4.967  1.00 42.69           C
ANISOU 3249  CB  ALA A 396     5691   4664   5867    388   1391  -2719       C
ATOM   3250  N   TYR A 397     -16.849  -6.640   3.339  1.00 61.55           N
ANISOU 3250  N   TYR A 397     7969   7283   8133    593   1632  -2774       N
ATOM   3251  CA  TYR A 397     -15.663  -7.212   2.704  1.00 70.45           C
ANISOU 3251  CA  TYR A 397     9070   8423   9275    706   1750  -2825       C
ATOM   3252  C   TYR A 397     -14.388  -6.567   3.247  1.00 71.39           C
ANISOU 3252  C   TYR A 397     9067   8578   9480    807   1817  -2690       C
ATOM   3253  O   TYR A 397     -13.420  -7.259   3.601  1.00 72.73           O
ANISOU 3253  O   TYR A 397     9199   8640   9797    921   1878  -2664       O
ATOM   3254  CB  TYR A 397     -15.769  -7.050   1.186  1.00 75.80           C
ANISOU 3254  CB  TYR A 397     9779   9302   9720    677   1795  -2949       C
ATOM   3255  CG  TYR A 397     -14.457  -6.825   0.470  1.00 82.95           C
ANISOU 3255  CG  TYR A 397    10613  10338  10566    782   1926  -2942       C
ATOM   3256  CD1 TYR A 397     -13.642  -7.894   0.119  1.00 84.51           C
ANISOU 3256  CD1 TYR A 397    10822  10449  10838    887   2013  -3023       C
ATOM   3257  CD2 TYR A 397     -14.042  -5.543   0.124  1.00 84.29           C
ANISOU 3257  CD2 TYR A 397    10701  10719  10608    777   1968  -2851       C
ATOM   3258  CE1 TYR A 397     -12.444  -7.692  -0.545  1.00 88.15           C
ANISOU 3258  CE1 TYR A 397    11214  11036  11244    987   2137  -3013       C
ATOM   3259  CE2 TYR A 397     -12.847  -5.330  -0.538  1.00 86.22           C
ANISOU 3259  CE2 TYR A 397    10870  11087  10802    869   2096  -2831       C
ATOM   3260  CZ  TYR A 397     -12.052  -6.408  -0.872  1.00 91.33           C
ANISOU 3260  CZ  TYR A 397    11530  11651  11521    976   2179  -2913       C
ATOM   3261  OH  TYR A 397     -10.862  -6.199  -1.533  1.00 97.44           O
ANISOU 3261  OH  TYR A 397    12225  12554  12245   1071   2309  -2889       O
ATOM   3262  N   ARG A 398     -14.386  -5.236   3.350  1.00 71.51           N
ANISOU 3262  N   ARG A 398     9018   8749   9404    759   1776  -2557       N
ATOM   3263  CA  ARG A 398     -13.204  -4.523   3.816  1.00 73.44           C
ANISOU 3263  CA  ARG A 398     9139   9049   9719    831   1803  -2387       C
ATOM   3264  C   ARG A 398     -12.895  -4.843   5.271  1.00 70.91           C
ANISOU 3264  C   ARG A 398     8777   8551   9613    888   1743  -2270       C
ATOM   3265  O   ARG A 398     -11.728  -4.859   5.667  1.00 74.17           O
ANISOU 3265  O   ARG A 398     9090   8951  10138    990   1795  -2195       O
ATOM   3266  CB  ARG A 398     -13.396  -3.017   3.631  1.00 78.18           C
ANISOU 3266  CB  ARG A 398     9689   9836  10179    747   1739  -2237       C
ATOM   3267  CG  ARG A 398     -12.252  -2.171   4.164  1.00 84.99           C
ANISOU 3267  CG  ARG A 398    10415  10751  11127    797   1752  -2061       C
ATOM   3268  CD  ARG A 398     -12.130  -0.854   3.414  1.00 89.02           C
ANISOU 3268  CD  ARG A 398    10871  11468  11484    738   1768  -1964       C
ATOM   3269  NE  ARG A 398     -11.621   0.227   4.257  1.00 89.66           N
ANISOU 3269  NE  ARG A 398    10843  11567  11657    721   1705  -1772       N
ATOM   3270  CZ  ARG A 398     -12.276   0.761   5.284  1.00 88.50           C
ANISOU 3270  CZ  ARG A 398    10707  11354  11566    658   1565  -1671       C
ATOM   3271  NH1 ARG A 398     -13.497   0.345   5.595  1.00 88.01           N
ANISOU 3271  NH1 ARG A 398    10756  11209  11475    602   1476  -1727       N
ATOM   3272  NH2 ARG A 398     -11.714   1.739   5.984  1.00 86.69           N
ANISOU 3272  NH2 ARG A 398    10372  11146  11420    646   1516  -1521       N
ATOM   3273  N   PHE A 399     -13.920  -5.101   6.080  1.00 69.27           N
ANISOU 3273  N   PHE A 399     8641   8219   9461    827   1634  -2248       N
ATOM   3274  CA  PHE A 399     -13.685  -5.523   7.455  1.00 69.34           C
ANISOU 3274  CA  PHE A 399     8621   8064   9660    890   1583  -2139       C
ATOM   3275  C   PHE A 399     -13.105  -6.927   7.498  1.00 76.82           C
ANISOU 3275  C   PHE A 399     9584   8839  10765   1010   1688  -2241       C
ATOM   3276  O   PHE A 399     -12.180  -7.200   8.272  1.00 82.29           O
ANISOU 3276  O   PHE A 399    10199   9462  11605   1124   1708  -2146       O
ATOM   3277  CB  PHE A 399     -14.985  -5.468   8.257  1.00 62.83           C
ANISOU 3277  CB  PHE A 399     7870   7158   8845    795   1455  -2087       C
ATOM   3278  CG  PHE A 399     -14.980  -6.352   9.472  1.00 61.02           C
ANISOU 3278  CG  PHE A 399     7650   6729   8804    864   1430  -2027       C
ATOM   3279  CD1 PHE A 399     -14.238  -6.006  10.591  1.00 59.20           C
ANISOU 3279  CD1 PHE A 399     7329   6493   8670    941   1385  -1858       C
ATOM   3280  CD2 PHE A 399     -15.704  -7.534   9.493  1.00 60.58           C
ANISOU 3280  CD2 PHE A 399     7691   6495   8833    853   1454  -2136       C
ATOM   3281  CE1 PHE A 399     -14.224  -6.817  11.712  1.00 59.42           C
ANISOU 3281  CE1 PHE A 399     7364   6355   8856   1016   1364  -1785       C
ATOM   3282  CE2 PHE A 399     -15.692  -8.353  10.612  1.00 60.77           C
ANISOU 3282  CE2 PHE A 399     7722   6331   9036    923   1443  -2057       C
ATOM   3283  CZ  PHE A 399     -14.951  -7.992  11.723  1.00 61.35           C
ANISOU 3283  CZ  PHE A 399     7708   6417   9187   1010   1398  -1874       C
ATOM   3284  N   LEU A 400     -13.644  -7.835   6.680  1.00 74.67           N
ANISOU 3284  N   LEU A 400     9412   8504  10455    982   1734  -2411       N
ATOM   3285  CA  LEU A 400     -13.099  -9.185   6.637  1.00 72.45           C
ANISOU 3285  CA  LEU A 400     9159   8075  10292   1079   1793  -2455       C
ATOM   3286  C   LEU A 400     -11.641  -9.172   6.210  1.00 75.50           C
ANISOU 3286  C   LEU A 400     9451   8542  10693   1204   1899  -2442       C
ATOM   3287  O   LEU A 400     -10.878 -10.070   6.581  1.00 84.62           O
ANISOU 3287  O   LEU A 400    10584   9578  11988   1321   1941  -2412       O
ATOM   3288  CB  LEU A 400     -13.925 -10.066   5.699  1.00 68.93           C
ANISOU 3288  CB  LEU A 400     8834   7583   9774   1008   1799  -2628       C
ATOM   3289  CG  LEU A 400     -15.164 -10.707   6.330  1.00 67.90           C
ANISOU 3289  CG  LEU A 400     8791   7284   9724    922   1712  -2633       C
ATOM   3290  CD1 LEU A 400     -15.875 -11.607   5.337  1.00 68.14           C
ANISOU 3290  CD1 LEU A 400     8920   7275   9696    855   1721  -2815       C
ATOM   3291  CD2 LEU A 400     -14.785 -11.483   7.581  1.00 69.12           C
ANISOU 3291  CD2 LEU A 400     8927   7237  10099   1017   1709  -2507       C
ATOM   3292  N   LYS A 401     -11.232  -8.164   5.442  1.00 67.84           N
ANISOU 3292  N   LYS A 401     8418   7777   9581   1185   1945  -2453       N
ATOM   3293  CA  LYS A 401      -9.846  -8.098   5.000  1.00 65.29           C
ANISOU 3293  CA  LYS A 401     7993   7545   9268   1299   2053  -2432       C
ATOM   3294  C   LYS A 401      -8.972  -7.144   5.814  1.00 69.09           C
ANISOU 3294  C   LYS A 401     8320   8096   9834   1348   2045  -2267       C
ATOM   3295  O   LYS A 401      -7.754  -7.138   5.614  1.00 75.42           O
ANISOU 3295  O   LYS A 401     9018   8962  10678   1448   2127  -2228       O
ATOM   3296  CB  LYS A 401      -9.780  -7.717   3.517  1.00 67.13           C
ANISOU 3296  CB  LYS A 401     8242   7970   9294   1263   2135  -2545       C
ATOM   3297  CG  LYS A 401     -10.707  -8.533   2.623  1.00 72.72           C
ANISOU 3297  CG  LYS A 401     9094   8643   9892   1202   2127  -2721       C
ATOM   3298  CD  LYS A 401     -10.202  -9.961   2.422  1.00 81.38           C
ANISOU 3298  CD  LYS A 401    10234   9592  11094   1305   2189  -2811       C
ATOM   3299  CE  LYS A 401     -11.363 -10.953   2.352  1.00 84.15           C
ANISOU 3299  CE  LYS A 401    10721   9788  11463   1230   2125  -2935       C
ATOM   3300  NZ  LYS A 401     -10.922 -12.375   2.461  1.00 82.51           N
ANISOU 3300  NZ  LYS A 401    10550   9388  11412   1328   2175  -2996       N
ATOM   3301  N   ARG A 402      -9.540  -6.359   6.733  1.00 66.77           N
ANISOU 3301  N   ARG A 402     8007   7800   9563   1277   1933  -2155       N
ATOM   3302  CA  ARG A 402      -8.762  -5.367   7.476  1.00 64.41           C
ANISOU 3302  CA  ARG A 402     7570   7595   9307   1294   1873  -1968       C
ATOM   3303  C   ARG A 402      -8.957  -5.397   8.988  1.00 67.59           C
ANISOU 3303  C   ARG A 402     7955   7888   9838   1310   1743  -1829       C
ATOM   3304  O   ARG A 402      -8.119  -4.832   9.702  1.00 70.21           O
ANISOU 3304  O   ARG A 402     8160   8277  10240   1356   1702  -1696       O
ATOM   3305  CB  ARG A 402      -9.076  -3.950   6.972  1.00 68.86           C
ANISOU 3305  CB  ARG A 402     8111   8349   9704   1169   1825  -1904       C
ATOM   3306  CG  ARG A 402      -8.691  -3.705   5.522  1.00 78.99           C
ANISOU 3306  CG  ARG A 402     9380   9787  10845   1165   1956  -1994       C
ATOM   3307  CD  ARG A 402      -8.714  -2.221   5.178  1.00 85.26           C
ANISOU 3307  CD  ARG A 402    10114  10764  11515   1067   1920  -1877       C
ATOM   3308  NE  ARG A 402      -7.549  -1.516   5.707  1.00 91.12           N
ANISOU 3308  NE  ARG A 402    10693  11563  12365   1110   1924  -1734       N
ATOM   3309  CZ  ARG A 402      -6.498  -1.156   4.977  1.00 96.27           C
ANISOU 3309  CZ  ARG A 402    11234  12342  13001   1153   2046  -1714       C
ATOM   3310  NH1 ARG A 402      -6.461  -1.434   3.681  1.00100.08           N
ANISOU 3310  NH1 ARG A 402    11759  12919  13349   1169   2178  -1827       N
ATOM   3311  NH2 ARG A 402      -5.481  -0.518   5.543  1.00 95.26           N
ANISOU 3311  NH2 ARG A 402    10947  12256  12990   1180   2036  -1586       N
ATOM   3312  N   ARG A 403     -10.035  -5.998   9.498  1.00 70.87           N
ANISOU 3312  N   ARG A 403     8486   8161  10279   1269   1677  -1854       N
ATOM   3313  CA  ARG A 403     -10.205  -6.317  10.920  1.00 70.84           C
ANISOU 3313  CA  ARG A 403     8476   8036  10403   1312   1581  -1731       C
ATOM   3314  C   ARG A 403     -10.326  -5.081  11.811  1.00 68.04           C
ANISOU 3314  C   ARG A 403     8056   7789  10006   1247   1440  -1573       C
ATOM   3315  O   ARG A 403      -9.946  -5.123  12.982  1.00 73.38           O
ANISOU 3315  O   ARG A 403     8669   8431  10781   1315   1371  -1452       O
ATOM   3316  CB  ARG A 403      -9.066  -7.205  11.435  1.00 76.38           C
ANISOU 3316  CB  ARG A 403     9097   8643  11282   1485   1649  -1694       C
ATOM   3317  CG  ARG A 403      -8.611  -8.286  10.474  1.00 79.66           C
ANISOU 3317  CG  ARG A 403     9550   8985  11733   1563   1792  -1836       C
ATOM   3318  CD  ARG A 403      -9.764  -9.163  10.040  1.00 76.80           C
ANISOU 3318  CD  ARG A 403     9355   8493  11333   1487   1791  -1954       C
ATOM   3319  NE  ARG A 403      -9.343 -10.116   9.020  1.00 83.92           N
ANISOU 3319  NE  ARG A 403    10303   9362  12220   1535   1892  -2080       N
ATOM   3320  CZ  ARG A 403      -8.690 -11.245   9.277  1.00 85.02           C
ANISOU 3320  CZ  ARG A 403    10441   9375  12489   1657   1936  -2062       C
ATOM   3321  NH1 ARG A 403      -8.383 -11.569  10.527  1.00 82.01           N
ANISOU 3321  NH1 ARG A 403    10012   8896  12252   1743   1886  -1910       N
ATOM   3322  NH2 ARG A 403      -8.345 -12.050   8.283  1.00 88.49           N
ANISOU 3322  NH2 ARG A 403    10924   9791  12907   1697   2029  -2194       N
ATOM   3323  N   SER A 404     -10.872  -3.981  11.298  1.00 63.93           N
ANISOU 3323  N   SER A 404     7551   7399   9340   1120   1395  -1573       N
ATOM   3324  CA  SER A 404     -11.000  -2.764  12.092  1.00 66.49           C
ANISOU 3324  CA  SER A 404     7815   7815   9632   1055   1268  -1439       C
ATOM   3325  C   SER A 404     -12.206  -2.848  13.025  1.00 65.56           C
ANISOU 3325  C   SER A 404     7788   7612   9510    998   1153  -1393       C
ATOM   3326  O   SER A 404     -13.316  -3.183  12.595  1.00 62.20           O
ANISOU 3326  O   SER A 404     7479   7134   9020    923   1153  -1470       O
ATOM   3327  CB  SER A 404     -11.122  -1.549  11.175  1.00 72.17           C
ANISOU 3327  CB  SER A 404     8515   8692  10214    949   1274  -1444       C
ATOM   3328  OG  SER A 404     -11.857  -1.875  10.008  1.00 78.75           O
ANISOU 3328  OG  SER A 404     9454   9535  10932    891   1340  -1569       O
ATOM   3329  N   PHE A 405     -11.989  -2.529  14.308  1.00 61.39           N
ANISOU 3329  N   PHE A 405     7198   7083   9045   1034   1053  -1269       N
ATOM   3330  CA  PHE A 405     -13.077  -2.650  15.279  1.00 52.67           C
ANISOU 3330  CA  PHE A 405     6171   5905   7936    996    953  -1213       C
ATOM   3331  C   PHE A 405     -14.165  -1.604  15.078  1.00 54.89           C
ANISOU 3331  C   PHE A 405     6506   6262   8089    853    877  -1211       C
ATOM   3332  O   PHE A 405     -15.353  -1.963  15.166  1.00 64.12           O
ANISOU 3332  O   PHE A 405     7779   7359   9225    794    849  -1236       O
ATOM   3333  CB  PHE A 405     -12.529  -2.597  16.707  1.00 50.11           C
ANISOU 3333  CB  PHE A 405     5765   5582   7693   1084    868  -1084       C
ATOM   3334  CG  PHE A 405     -13.573  -2.244  17.730  1.00 53.31           C
ANISOU 3334  CG  PHE A 405     6224   5977   8055   1029    751  -1009       C
ATOM   3335  CD1 PHE A 405     -14.456  -3.207  18.195  1.00 49.70           C
ANISOU 3335  CD1 PHE A 405     5866   5386   7632   1042    753   -997       C
ATOM   3336  CD2 PHE A 405     -13.693  -0.948  18.205  1.00 52.52           C
ANISOU 3336  CD2 PHE A 405     6074   5995   7888    961    647   -955       C
ATOM   3337  CE1 PHE A 405     -15.425  -2.886  19.126  1.00 49.43           C
ANISOU 3337  CE1 PHE A 405     5876   5352   7554    995    656   -923       C
ATOM   3338  CE2 PHE A 405     -14.663  -0.621  19.135  1.00 47.22           C
ANISOU 3338  CE2 PHE A 405     5451   5319   7171    918    547   -895       C
ATOM   3339  CZ  PHE A 405     -15.528  -1.591  19.596  1.00 49.37           C
ANISOU 3339  CZ  PHE A 405     5819   5474   7466    937    553   -876       C
ATOM   3340  N   PRO A 406     -13.862  -0.315  14.874  1.00 48.16           N
ANISOU 3340  N   PRO A 406     5581   5542   7174    795    839  -1174       N
ATOM   3341  CA  PRO A 406     -14.956   0.633  14.598  1.00 46.01           C
ANISOU 3341  CA  PRO A 406     5366   5329   6787    668    778  -1171       C
ATOM   3342  C   PRO A 406     -15.800   0.225  13.405  1.00 52.00           C
ANISOU 3342  C   PRO A 406     6228   6076   7455    602    841  -1278       C
ATOM   3343  O   PRO A 406     -17.025   0.409  13.418  1.00 53.94           O
ANISOU 3343  O   PRO A 406     6553   6312   7631    518    784  -1285       O
ATOM   3344  CB  PRO A 406     -14.226   1.965  14.362  1.00 41.54           C
ANISOU 3344  CB  PRO A 406     4693   4891   6199    633    764  -1121       C
ATOM   3345  CG  PRO A 406     -12.768   1.620  14.246  1.00 40.96           C
ANISOU 3345  CG  PRO A 406     4510   4835   6216    731    838  -1122       C
ATOM   3346  CD  PRO A 406     -12.580   0.387  15.056  1.00 42.18           C
ANISOU 3346  CD  PRO A 406     4682   4879   6466    840    837  -1119       C
ATOM   3347  N   GLU A 407     -15.178  -0.343  12.374  1.00 49.06           N
ANISOU 3347  N   GLU A 407     5851   5712   7078    641    955  -1368       N
ATOM   3348  CA  GLU A 407     -15.955  -0.923  11.288  1.00 53.65           C
ANISOU 3348  CA  GLU A 407     6532   6280   7573    590   1013  -1496       C
ATOM   3349  C   GLU A 407     -16.945  -1.953  11.818  1.00 55.50           C
ANISOU 3349  C   GLU A 407     6863   6366   7858    580    982  -1538       C
ATOM   3350  O   GLU A 407     -18.159  -1.816  11.616  1.00 61.49           O
ANISOU 3350  O   GLU A 407     7696   7130   8537    484    932  -1568       O
ATOM   3351  CB  GLU A 407     -15.028  -1.548  10.254  1.00 60.01           C
ANISOU 3351  CB  GLU A 407     7316   7104   8381    657   1149  -1599       C
ATOM   3352  CG  GLU A 407     -15.648  -1.594   8.879  1.00 68.70           C
ANISOU 3352  CG  GLU A 407     8489   8281   9334    588   1203  -1724       C
ATOM   3353  CD  GLU A 407     -14.644  -1.343   7.769  1.00 77.98           C
ANISOU 3353  CD  GLU A 407     9603   9581  10445    628   1320  -1765       C
ATOM   3354  OE1 GLU A 407     -13.426  -1.457   8.028  1.00 86.98           O
ANISOU 3354  OE1 GLU A 407    10650  10712  11686    722   1378  -1726       O
ATOM   3355  OE2 GLU A 407     -15.081  -1.035   6.641  1.00 72.97           O
ANISOU 3355  OE2 GLU A 407     9008   9063   9655    569   1354  -1832       O
ATOM   3356  N   MET A 408     -16.434  -2.990  12.498  1.00 52.61           N
ANISOU 3356  N   MET A 408     6490   5866   7633    680   1015  -1531       N
ATOM   3357  CA  MET A 408     -17.280  -4.033  13.079  1.00 54.28           C
ANISOU 3357  CA  MET A 408     6785   5915   7923    679   1000  -1551       C
ATOM   3358  C   MET A 408     -18.450  -3.441  13.858  1.00 50.90           C
ANISOU 3358  C   MET A 408     6391   5499   7448    592    884  -1466       C
ATOM   3359  O   MET A 408     -19.600  -3.862  13.681  1.00 47.07           O
ANISOU 3359  O   MET A 408     5989   4953   6942    514    869  -1524       O
ATOM   3360  CB  MET A 408     -16.441  -4.942  13.984  1.00 53.45           C
ANISOU 3360  CB  MET A 408     6642   5685   7983    816   1034  -1489       C
ATOM   3361  CG  MET A 408     -17.159  -6.205  14.426  1.00 59.30           C
ANISOU 3361  CG  MET A 408     7467   6231   8833    830   1056  -1512       C
ATOM   3362  SD  MET A 408     -16.347  -6.990  15.829  1.00 62.24           S
ANISOU 3362  SD  MET A 408     7786   6481   9381    992   1060  -1364       S
ATOM   3363  CE  MET A 408     -16.855  -5.905  17.161  1.00 65.08           C
ANISOU 3363  CE  MET A 408     8112   6945   9670    954    909  -1190       C
ATOM   3364  N   ALA A 409     -18.179  -2.439  14.699  1.00 49.96           N
ANISOU 3364  N   ALA A 409     6205   5464   7313    601    801  -1338       N
ATOM   3365  CA  ALA A 409     -19.240  -1.830  15.497  1.00 53.50           C
ANISOU 3365  CA  ALA A 409     6680   5929   7717    531    695  -1258       C
ATOM   3366  C   ALA A 409     -20.273  -1.132  14.618  1.00 54.83           C
ANISOU 3366  C   ALA A 409     6896   6182   7754    406    669  -1314       C
ATOM   3367  O   ALA A 409     -21.482  -1.256  14.853  1.00 62.11           O
ANISOU 3367  O   ALA A 409     7880   7068   8652    337    622  -1315       O
ATOM   3368  CB  ALA A 409     -18.643  -0.848  16.504  1.00 46.03           C
ANISOU 3368  CB  ALA A 409     5646   5065   6776    569    616  -1135       C
ATOM   3369  N   LEU A 410     -19.818  -0.384  13.611  1.00 49.17           N
ANISOU 3369  N   LEU A 410     6145   5585   6952    378    700  -1350       N
ATOM   3370  CA  LEU A 410     -20.752   0.290  12.714  1.00 44.16           C
ANISOU 3370  CA  LEU A 410     5550   5047   6183    272    677  -1390       C
ATOM   3371  C   LEU A 410     -21.644  -0.713  11.995  1.00 49.01           C
ANISOU 3371  C   LEU A 410     6251   5600   6769    223    711  -1520       C
ATOM   3372  O   LEU A 410     -22.845  -0.474  11.814  1.00 58.65           O
ANISOU 3372  O   LEU A 410     7517   6851   7916    134    655  -1535       O
ATOM   3373  CB  LEU A 410     -19.983   1.143  11.706  1.00 42.09           C
ANISOU 3373  CB  LEU A 410     5232   4921   5840    267    725  -1395       C
ATOM   3374  CG  LEU A 410     -20.825   2.172  10.951  1.00 40.10           C
ANISOU 3374  CG  LEU A 410     4997   4793   5445    172    687  -1380       C
ATOM   3375  CD1 LEU A 410     -21.166   3.347  11.853  1.00 39.77           C
ANISOU 3375  CD1 LEU A 410     4919   4778   5414    141    590  -1252       C
ATOM   3376  CD2 LEU A 410     -20.112   2.643   9.696  1.00 36.91           C
ANISOU 3376  CD2 LEU A 410     4556   4515   4952    175    769  -1406       C
ATOM   3377  N   LEU A 411     -21.074  -1.847  11.585  1.00 45.20           N
ANISOU 3377  N   LEU A 411     5788   5032   6353    280    802  -1623       N
ATOM   3378  CA  LEU A 411     -21.868  -2.846  10.875  1.00 46.72           C
ANISOU 3378  CA  LEU A 411     6061   5157   6534    229    837  -1773       C
ATOM   3379  C   LEU A 411     -22.855  -3.539  11.810  1.00 47.27           C
ANISOU 3379  C   LEU A 411     6180   5081   6702    197    789  -1748       C
ATOM   3380  O   LEU A 411     -23.982  -3.859  11.406  1.00 42.34           O
ANISOU 3380  O   LEU A 411     5609   4439   6038    105    765  -1832       O
ATOM   3381  CB  LEU A 411     -20.955  -3.857  10.167  1.00 47.24           C
ANISOU 3381  CB  LEU A 411     6134   5160   6654    304    957  -1903       C
ATOM   3382  CG  LEU A 411     -20.379  -3.404   8.813  1.00 55.41           C
ANISOU 3382  CG  LEU A 411     7148   6354   7551    303   1023  -1988       C
ATOM   3383  CD1 LEU A 411     -19.278  -2.340   8.918  1.00 61.17           C
ANISOU 3383  CD1 LEU A 411     7782   7202   8257    358   1033  -1862       C
ATOM   3384  CD2 LEU A 411     -19.904  -4.606   8.005  1.00 51.56           C
ANISOU 3384  CD2 LEU A 411     6696   5792   7103    355   1139  -2167       C
ATOM   3385  N   ILE A 412     -22.469  -3.751  13.069  1.00 45.48           N
ANISOU 3385  N   ILE A 412     5926   4759   6596    272    772  -1627       N
ATOM   3386  CA  ILE A 412     -23.420  -4.251  14.062  1.00 48.28           C
ANISOU 3386  CA  ILE A 412     6318   4996   7031    245    727  -1566       C
ATOM   3387  C   ILE A 412     -24.592  -3.286  14.201  1.00 50.19           C
ANISOU 3387  C   ILE A 412     6567   5341   7164    142    630  -1515       C
ATOM   3388  O   ILE A 412     -25.766  -3.688  14.221  1.00 50.98           O
ANISOU 3388  O   ILE A 412     6711   5387   7271     61    605  -1550       O
ATOM   3389  CB  ILE A 412     -22.713  -4.467  15.411  1.00 45.52           C
ANISOU 3389  CB  ILE A 412     5928   4570   6796    357    720  -1421       C
ATOM   3390  CG1 ILE A 412     -21.791  -5.691  15.345  1.00 47.55           C
ANISOU 3390  CG1 ILE A 412     6188   4686   7192    462    821  -1468       C
ATOM   3391  CG2 ILE A 412     -23.729  -4.589  16.538  1.00 36.67           C
ANISOU 3391  CG2 ILE A 412     4832   3386   5714    328    658  -1316       C
ATOM   3392  CD1 ILE A 412     -20.712  -5.708  16.416  1.00 43.50           C
ANISOU 3392  CD1 ILE A 412     5608   4157   6762    596    817  -1329       C
ATOM   3393  N   TRP A 413     -24.275  -1.996  14.329  1.00 48.36           N
ANISOU 3393  N   TRP A 413     6282   5249   6843    146    576  -1429       N
ATOM   3394  CA  TRP A 413     -25.299  -0.959  14.392  1.00 44.43           C
ANISOU 3394  CA  TRP A 413     5784   4854   6243     60    491  -1378       C
ATOM   3395  C   TRP A 413     -26.225  -1.032  13.184  1.00 46.65           C
ANISOU 3395  C   TRP A 413     6106   5192   6425    -40    492  -1497       C
ATOM   3396  O   TRP A 413     -27.454  -0.963  13.320  1.00 50.38           O
ANISOU 3396  O   TRP A 413     6602   5669   6871   -118    437  -1492       O
ATOM   3397  CB  TRP A 413     -24.620   0.407  14.481  1.00 37.61           C
ANISOU 3397  CB  TRP A 413     4856   4119   5316     84    454  -1293       C
ATOM   3398  CG  TRP A 413     -25.534   1.583  14.339  1.00 38.84           C
ANISOU 3398  CG  TRP A 413     5006   4384   5366      6    381  -1246       C
ATOM   3399  CD1 TRP A 413     -26.566   1.926  15.162  1.00 39.71           C
ANISOU 3399  CD1 TRP A 413     5127   4486   5474    -30    308  -1178       C
ATOM   3400  CD2 TRP A 413     -25.483   2.589  13.318  1.00 38.43           C
ANISOU 3400  CD2 TRP A 413     4932   4467   5202    -35    379  -1254       C
ATOM   3401  NE1 TRP A 413     -27.162   3.083  14.716  1.00 39.11           N
ANISOU 3401  NE1 TRP A 413     5037   4525   5299    -89    260  -1148       N
ATOM   3402  CE2 TRP A 413     -26.515   3.509  13.586  1.00 36.61           C
ANISOU 3402  CE2 TRP A 413     4701   4295   4914    -93    302  -1187       C
ATOM   3403  CE3 TRP A 413     -24.666   2.798  12.203  1.00 38.55           C
ANISOU 3403  CE3 TRP A 413     4926   4562   5159    -24    444  -1301       C
ATOM   3404  CZ2 TRP A 413     -26.754   4.619  12.777  1.00 36.56           C
ANISOU 3404  CZ2 TRP A 413     4675   4414   4803   -136    284  -1159       C
ATOM   3405  CZ3 TRP A 413     -24.904   3.902  11.403  1.00 41.48           C
ANISOU 3405  CZ3 TRP A 413     5277   5066   5416    -70    428  -1268       C
ATOM   3406  CH2 TRP A 413     -25.940   4.798  11.694  1.00 38.44           C
ANISOU 3406  CH2 TRP A 413     4894   4728   4985   -124    348  -1194       C
ATOM   3407  N   ALA A 414     -25.648  -1.185  11.989  1.00 43.39           N
ANISOU 3407  N   ALA A 414     5697   4837   5954    -36    554  -1606       N
ATOM   3408  CA  ALA A 414     -26.456  -1.222  10.774  1.00 42.38           C
ANISOU 3408  CA  ALA A 414     5602   4794   5705   -124    550  -1727       C
ATOM   3409  C   ALA A 414     -27.389  -2.425  10.766  1.00 49.92           C
ANISOU 3409  C   ALA A 414     6612   5625   6731   -183    554  -1839       C
ATOM   3410  O   ALA A 414     -28.559  -2.308  10.387  1.00 52.90           O
ANISOU 3410  O   ALA A 414     7005   6058   7037   -278    499  -1883       O
ATOM   3411  CB  ALA A 414     -25.553  -1.233   9.540  1.00 36.71           C
ANISOU 3411  CB  ALA A 414     4877   4167   4904    -92    629  -1825       C
ATOM   3412  N   ILE A 415     -26.894  -3.590  11.189  1.00 50.98           N
ANISOU 3412  N   ILE A 415     6769   5587   7015   -128    620  -1881       N
ATOM   3413  CA  ILE A 415     -27.726  -4.793  11.199  1.00 49.14           C
ANISOU 3413  CA  ILE A 415     6585   5206   6881   -187    637  -1988       C
ATOM   3414  C   ILE A 415     -28.878  -4.636  12.183  1.00 51.60           C
ANISOU 3414  C   ILE A 415     6893   5476   7236   -247    562  -1879       C
ATOM   3415  O   ILE A 415     -30.036  -4.966  11.880  1.00 61.11           O
ANISOU 3415  O   ILE A 415     8116   6668   8433   -351    529  -1956       O
ATOM   3416  CB  ILE A 415     -26.876  -6.031  11.532  1.00 52.08           C
ANISOU 3416  CB  ILE A 415     6977   5383   7427   -100    733  -2030       C
ATOM   3417  CG1 ILE A 415     -25.806  -6.246  10.463  1.00 53.53           C
ANISOU 3417  CG1 ILE A 415     7161   5612   7565    -42    817  -2160       C
ATOM   3418  CG2 ILE A 415     -27.762  -7.258  11.671  1.00 51.43           C
ANISOU 3418  CG2 ILE A 415     6943   5118   7482   -166    754  -2122       C
ATOM   3419  CD1 ILE A 415     -24.766  -7.278  10.846  1.00 54.92           C
ANISOU 3419  CD1 ILE A 415     7342   5612   7912     73    916  -2173       C
ATOM   3420  N   ALA A 416     -28.573  -4.151  13.389  1.00 43.06           N
ANISOU 3420  N   ALA A 416     5783   4377   6201   -181    535  -1703       N
ATOM   3421  CA  ALA A 416     -29.625  -3.959  14.381  1.00 46.98           C
ANISOU 3421  CA  ALA A 416     6273   4848   6728   -224    473  -1591       C
ATOM   3422  C   ALA A 416     -30.683  -2.984  13.875  1.00 51.85           C
ANISOU 3422  C   ALA A 416     6874   5623   7203   -321    391  -1597       C
ATOM   3423  O   ALA A 416     -31.892  -3.232  14.014  1.00 60.79           O
ANISOU 3423  O   ALA A 416     8013   6732   8354   -407    356  -1608       O
ATOM   3424  CB  ALA A 416     -29.017  -3.474  15.695  1.00 43.07           C
ANISOU 3424  CB  ALA A 416     5746   4345   6273   -127    453  -1414       C
ATOM   3425  N   MET A 417     -30.247  -1.879  13.261  1.00 46.58           N
ANISOU 3425  N   MET A 417     6181   5116   6400   -308    365  -1583       N
ATOM   3426  CA  MET A 417     -31.202  -0.904  12.748  1.00 47.63           C
ANISOU 3426  CA  MET A 417     6295   5403   6398   -385    291  -1572       C
ATOM   3427  C   MET A 417     -32.009  -1.463  11.583  1.00 52.19           C
ANISOU 3427  C   MET A 417     6894   6020   6915   -481    287  -1733       C
ATOM   3428  O   MET A 417     -33.176  -1.097  11.415  1.00 41.55           O
ANISOU 3428  O   MET A 417     5531   4750   5506   -560    220  -1729       O
ATOM   3429  CB  MET A 417     -30.480   0.379  12.338  1.00 46.67           C
ANISOU 3429  CB  MET A 417     6140   5430   6164   -344    277  -1508       C
ATOM   3430  CG  MET A 417     -29.893   1.159  13.509  1.00 49.99           C
ANISOU 3430  CG  MET A 417     6526   5837   6631   -270    255  -1356       C
ATOM   3431  SD  MET A 417     -31.103   1.488  14.810  1.00 52.56           S
ANISOU 3431  SD  MET A 417     6843   6132   6995   -297    181  -1241       S
ATOM   3432  CE  MET A 417     -30.640   0.280  16.052  1.00 55.37           C
ANISOU 3432  CE  MET A 417     7218   6309   7512   -228    227  -1205       C
ATOM   3433  N   PHE A 418     -31.422  -2.359  10.782  1.00 55.58           N
ANISOU 3433  N   PHE A 418     7354   6401   7361   -473    355  -1883       N
ATOM   3434  CA  PHE A 418     -32.191  -2.990   9.712  1.00 60.50           C
ANISOU 3434  CA  PHE A 418     7998   7057   7931   -567    347  -2064       C
ATOM   3435  C   PHE A 418     -33.280  -3.891  10.278  1.00 67.37           C
ANISOU 3435  C   PHE A 418     8877   7786   8933   -648    328  -2098       C
ATOM   3436  O   PHE A 418     -34.401  -3.921   9.755  1.00 69.23           O
ANISOU 3436  O   PHE A 418     9100   8093   9112   -751    270  -2177       O
ATOM   3437  CB  PHE A 418     -31.277  -3.790   8.784  1.00 61.26           C
ANISOU 3437  CB  PHE A 418     8128   7124   8026   -533    434  -2232       C
ATOM   3438  CG  PHE A 418     -32.003  -4.433   7.630  1.00 67.57           C
ANISOU 3438  CG  PHE A 418     8948   7971   8754   -628    423  -2446       C
ATOM   3439  CD1 PHE A 418     -32.524  -5.714   7.742  1.00 72.27           C
ANISOU 3439  CD1 PHE A 418     9571   8393   9496   -687    445  -2573       C
ATOM   3440  CD2 PHE A 418     -32.173  -3.752   6.436  1.00 70.73           C
ANISOU 3440  CD2 PHE A 418     9335   8597   8942   -657    388  -2510       C
ATOM   3441  CE1 PHE A 418     -33.198  -6.303   6.685  1.00 73.49           C
ANISOU 3441  CE1 PHE A 418     9730   8612   9579   -759    412  -2710       C
ATOM   3442  CE2 PHE A 418     -32.845  -4.337   5.375  1.00 72.99           C
ANISOU 3442  CE2 PHE A 418     9634   8953   9147   -737    364  -2699       C
ATOM   3443  CZ  PHE A 418     -33.358  -5.613   5.501  1.00 73.59           C
ANISOU 3443  CZ  PHE A 418     9729   8864   9369   -782    368  -2776       C
ATOM   3444  N   ILE A 419     -32.963  -4.649  11.331  1.00 66.00           N
ANISOU 3444  N   ILE A 419     8721   7417   8941   -601    379  -2036       N
ATOM   3445  CA  ILE A 419     -33.987  -5.473  11.972  1.00 62.36           C
ANISOU 3445  CA  ILE A 419     8262   6811   8621   -675    373  -2037       C
ATOM   3446  C   ILE A 419     -35.125  -4.596  12.483  1.00 61.92           C
ANISOU 3446  C   ILE A 419     8162   6861   8503   -732    284  -1915       C
ATOM   3447  O   ILE A 419     -36.312  -4.868  12.241  1.00 65.84           O
ANISOU 3447  O   ILE A 419     8640   7368   9010   -842    242  -1979       O
ATOM   3448  CB  ILE A 419     -33.374  -6.315  13.104  1.00 59.97           C
ANISOU 3448  CB  ILE A 419     7980   6293   8511   -594    448  -1946       C
ATOM   3449  CG1 ILE A 419     -32.378  -7.332  12.539  1.00 53.25           C
ANISOU 3449  CG1 ILE A 419     7170   5315   7747   -543    543  -2085       C
ATOM   3450  CG2 ILE A 419     -34.470  -7.010  13.896  1.00 60.23           C
ANISOU 3450  CG2 ILE A 419     8008   6188   8690   -667    446  -1899       C
ATOM   3451  CD1 ILE A 419     -31.566  -8.043  13.604  1.00 48.31           C
ANISOU 3451  CD1 ILE A 419     6558   4500   7297   -433    619  -1972       C
ATOM   3452  N   ALA A 420     -34.776  -3.516  13.186  1.00 61.91           N
ANISOU 3452  N   ALA A 420     8139   6942   8442   -657    254  -1745       N
ATOM   3453  CA  ALA A 420     -35.802  -2.596  13.673  1.00 63.91           C
ANISOU 3453  CA  ALA A 420     8350   7299   8634   -695    176  -1630       C
ATOM   3454  C   ALA A 420     -36.636  -2.030  12.525  1.00 67.52           C
ANISOU 3454  C   ALA A 420     8780   7931   8943   -783    107  -1717       C
ATOM   3455  O   ALA A 420     -37.863  -1.916  12.636  1.00 69.06           O
ANISOU 3455  O   ALA A 420     8939   8167   9134   -862     52  -1702       O
ATOM   3456  CB  ALA A 420     -35.159  -1.467  14.478  1.00 62.70           C
ANISOU 3456  CB  ALA A 420     8180   7211   8434   -597    157  -1464       C
ATOM   3457  N   LEU A 421     -35.985  -1.673  11.413  1.00 68.14           N
ANISOU 3457  N   LEU A 421     8870   8125   8896   -765    112  -1800       N
ATOM   3458  CA  LEU A 421     -36.699  -1.133  10.259  1.00 60.01           C
ANISOU 3458  CA  LEU A 421     7814   7283   7705   -833     48  -1875       C
ATOM   3459  C   LEU A 421     -37.669  -2.155   9.686  1.00 57.80           C
ANISOU 3459  C   LEU A 421     7530   6973   7459   -949     28  -2044       C
ATOM   3460  O   LEU A 421     -38.778  -1.806   9.264  1.00 56.90           O
ANISOU 3460  O   LEU A 421     7370   6984   7263  -1027    -50  -2064       O
ATOM   3461  CB  LEU A 421     -35.697  -0.690   9.193  1.00 55.22           C
ANISOU 3461  CB  LEU A 421     7223   6799   6961   -781     76  -1928       C
ATOM   3462  CG  LEU A 421     -36.246  -0.375   7.803  1.00 56.75           C
ANISOU 3462  CG  LEU A 421     7399   7194   6970   -840     26  -2033       C
ATOM   3463  CD1 LEU A 421     -37.200   0.797   7.878  1.00 63.08           C
ANISOU 3463  CD1 LEU A 421     8147   8145   7677   -862    -63  -1901       C
ATOM   3464  CD2 LEU A 421     -35.116  -0.080   6.840  1.00 56.05           C
ANISOU 3464  CD2 LEU A 421     7331   7208   6759   -776     80  -2077       C
ATOM   3465  N   TRP A 422     -37.258  -3.422   9.651  1.00 56.29           N
ANISOU 3465  N   TRP A 422     7380   6612   7395   -960     98  -2173       N
ATOM   3466  CA  TRP A 422     -38.168  -4.488   9.251  1.00 55.12           C
ANISOU 3466  CA  TRP A 422     7226   6393   7323  -1079     86  -2343       C
ATOM   3467  C   TRP A 422     -39.381  -4.545  10.171  1.00 59.13           C
ANISOU 3467  C   TRP A 422     7687   6843   7937  -1149     44  -2244       C
ATOM   3468  O   TRP A 422     -40.507  -4.779   9.715  1.00 58.77           O
ANISOU 3468  O   TRP A 422     7598   6856   7877  -1258    -17  -2328       O
ATOM   3469  CB  TRP A 422     -37.435  -5.825   9.256  1.00 49.87           C
ANISOU 3469  CB  TRP A 422     6614   5522   6810  -1050    181  -2440       C
ATOM   3470  CG  TRP A 422     -38.158  -6.899   8.527  1.00 56.32           C
ANISOU 3470  CG  TRP A 422     7427   6305   7666  -1131    165  -2573       C
ATOM   3471  CD1 TRP A 422     -39.232  -7.609   8.970  1.00 56.48           C
ANISOU 3471  CD1 TRP A 422     7418   6219   7824  -1220    145  -2570       C
ATOM   3472  CD2 TRP A 422     -37.855  -7.399   7.218  1.00 65.49           C
ANISOU 3472  CD2 TRP A 422     8611   7540   8733  -1131    171  -2738       C
ATOM   3473  NE1 TRP A 422     -39.621  -8.522   8.017  1.00 63.86           N
ANISOU 3473  NE1 TRP A 422     8355   7149   8761  -1280    133  -2728       N
ATOM   3474  CE2 TRP A 422     -38.791  -8.412   6.932  1.00 67.78           C
ANISOU 3474  CE2 TRP A 422     8884   7756   9112  -1225    147  -2837       C
ATOM   3475  CE3 TRP A 422     -36.884  -7.088   6.261  1.00 67.32           C
ANISOU 3475  CE3 TRP A 422     8872   7894   8814  -1061    198  -2812       C
ATOM   3476  CZ2 TRP A 422     -38.785  -9.114   5.730  1.00 72.58           C
ANISOU 3476  CZ2 TRP A 422     9508   8409   9660  -1251    143  -3016       C
ATOM   3477  CZ3 TRP A 422     -36.880  -7.786   5.069  1.00 69.18           C
ANISOU 3477  CZ3 TRP A 422     9123   8179   8983  -1083    200  -2982       C
ATOM   3478  CH2 TRP A 422     -37.823  -8.787   4.814  1.00 74.31           C
ANISOU 3478  CH2 TRP A 422     9760   8754   9722  -1176    169  -3087       C
ATOM   3479  N   GLY A 423     -39.169  -4.336  11.468  1.00 60.83           N
ANISOU 3479  N   GLY A 423     7905   6957   8253  -1081     74  -2057       N
ATOM   3480  CA  GLY A 423     -40.266  -4.378  12.418  1.00 57.62           C
ANISOU 3480  CA  GLY A 423     7453   6499   7943  -1133     49  -1947       C
ATOM   3481  C   GLY A 423     -41.374  -3.372  12.166  1.00 58.78           C
ANISOU 3481  C   GLY A 423     7530   6844   7959  -1187    -50  -1897       C
ATOM   3482  O   GLY A 423     -42.538  -3.748  11.996  1.00 57.64           O
ANISOU 3482  O   GLY A 423     7333   6711   7855  -1298    -91  -1958       O
ATOM   3483  N   GLN A 424     -41.030  -2.087  12.150  1.00 57.14           N
ANISOU 3483  N   GLN A 424     7314   6788   7607  -1107    -87  -1784       N
ATOM   3484  CA  GLN A 424     -42.007  -1.025  11.959  1.00 57.91           C
ANISOU 3484  CA  GLN A 424     7346   7069   7587  -1135   -175  -1713       C
ATOM   3485  C   GLN A 424     -41.431   0.017  11.015  1.00 62.52           C
ANISOU 3485  C   GLN A 424     7937   7834   7982  -1080   -208  -1711       C
ATOM   3486  O   GLN A 424     -40.253   0.371  11.121  1.00 70.33           O
ANISOU 3486  O   GLN A 424     8970   8801   8950   -987   -162  -1664       O
ATOM   3487  CB  GLN A 424     -42.392  -0.360  13.289  1.00 57.61           C
ANISOU 3487  CB  GLN A 424     7280   7007   7601  -1083   -178  -1516       C
ATOM   3488  CG  GLN A 424     -43.036  -1.296  14.304  1.00 60.85           C
ANISOU 3488  CG  GLN A 424     7676   7256   8187  -1130   -137  -1481       C
ATOM   3489  CD  GLN A 424     -43.386  -0.592  15.601  1.00 55.80           C
ANISOU 3489  CD  GLN A 424     7009   6618   7572  -1067   -136  -1290       C
ATOM   3490  OE1 GLN A 424     -43.551   0.626  15.633  1.00 54.43           O
ANISOU 3490  OE1 GLN A 424     6809   6583   7289  -1019   -185  -1205       O
ATOM   3491  NE2 GLN A 424     -43.494  -1.356  16.681  1.00 53.39           N
ANISOU 3491  NE2 GLN A 424     6713   6161   7413  -1061    -74  -1221       N
ATOM   3492  N   ASN A 425     -42.265   0.511  10.097  1.00 57.81           N
ANISOU 3492  N   ASN A 425     7289   7423   7254  -1136   -287  -1753       N
ATOM   3493  CA  ASN A 425     -41.783   1.495   9.135  1.00 58.76           C
ANISOU 3493  CA  ASN A 425     7411   7725   7190  -1083   -314  -1735       C
ATOM   3494  C   ASN A 425     -41.332   2.784   9.812  1.00 61.25           C
ANISOU 3494  C   ASN A 425     7725   8066   7482   -981   -309  -1539       C
ATOM   3495  O   ASN A 425     -40.491   3.501   9.254  1.00 58.41           O
ANISOU 3495  O   ASN A 425     7384   7789   7021   -917   -293  -1504       O
ATOM   3496  CB  ASN A 425     -42.860   1.781   8.081  1.00 60.91           C
ANISOU 3496  CB  ASN A 425     7619   8203   7320  -1156   -407  -1799       C
ATOM   3497  CG  ASN A 425     -43.861   2.832   8.529  1.00 62.47           C
ANISOU 3497  CG  ASN A 425     7745   8500   7491  -1145   -474  -1638       C
ATOM   3498  OD1 ASN A 425     -43.754   4.004   8.169  1.00 65.77           O
ANISOU 3498  OD1 ASN A 425     8145   9057   7786  -1081   -502  -1527       O
ATOM   3499  ND2 ASN A 425     -44.846   2.413   9.311  1.00 57.54           N
ANISOU 3499  ND2 ASN A 425     7075   7801   6989  -1206   -493  -1621       N
ATOM   3500  N   ARG A 426     -41.843   3.079  11.013  1.00 64.22           N
ANISOU 3500  N   ARG A 426     8076   8368   7956   -965   -315  -1414       N
ATOM   3501  CA  ARG A 426     -41.407   4.277  11.723  1.00 61.34           C
ANISOU 3501  CA  ARG A 426     7710   8014   7582   -870   -310  -1250       C
ATOM   3502  C   ARG A 426     -39.892   4.290  11.880  1.00 53.74           C
ANISOU 3502  C   ARG A 426     6806   6972   6642   -791   -242  -1243       C
ATOM   3503  O   ARG A 426     -39.231   5.273  11.529  1.00 50.50           O
ANISOU 3503  O   ARG A 426     6396   6637   6154   -733   -240  -1179       O
ATOM   3504  CB  ARG A 426     -42.102   4.382  13.087  1.00 61.82           C
ANISOU 3504  CB  ARG A 426     7744   7993   7752   -860   -314  -1144       C
ATOM   3505  CG  ARG A 426     -41.834   3.234  14.056  1.00 67.74           C
ANISOU 3505  CG  ARG A 426     8528   8559   8650   -866   -253  -1166       C
ATOM   3506  CD  ARG A 426     -42.406   3.527  15.435  1.00 70.95           C
ANISOU 3506  CD  ARG A 426     8909   8914   9134   -834   -249  -1036       C
ATOM   3507  NE  ARG A 426     -41.536   4.383  16.236  1.00 70.62           N
ANISOU 3507  NE  ARG A 426     8891   8854   9087   -727   -231   -932       N
ATOM   3508  CZ  ARG A 426     -41.918   5.006  17.347  1.00 64.61           C
ANISOU 3508  CZ  ARG A 426     8109   8090   8352   -677   -237   -819       C
ATOM   3509  NH1 ARG A 426     -43.160   4.870  17.791  1.00 66.52           N
ANISOU 3509  NH1 ARG A 426     8301   8347   8625   -720   -252   -782       N
ATOM   3510  NH2 ARG A 426     -41.060   5.766  18.015  1.00 57.46           N
ANISOU 3510  NH2 ARG A 426     7223   7170   7438   -585   -226   -751       N
ATOM   3511  N   PHE A 427     -39.316   3.168  12.321  1.00 54.43           N
ANISOU 3511  N   PHE A 427     6935   6906   6838   -792   -183  -1311       N
ATOM   3512  CA  PHE A 427     -37.887   3.083  12.607  1.00 51.49           C
ANISOU 3512  CA  PHE A 427     6607   6450   6506   -712   -119  -1299       C
ATOM   3513  C   PHE A 427     -37.047   3.331  11.360  1.00 49.83           C
ANISOU 3513  C   PHE A 427     6413   6338   6183   -694    -99  -1367       C
ATOM   3514  O   PHE A 427     -35.816   3.266  11.419  1.00 53.26           O
ANISOU 3514  O   PHE A 427     6873   6720   6643   -631    -41  -1367       O
ATOM   3515  CB  PHE A 427     -37.543   1.726  13.228  1.00 42.37           C
ANISOU 3515  CB  PHE A 427     5490   5115   5494   -714    -59  -1358       C
ATOM   3516  CG  PHE A 427     -38.135   1.523  14.598  1.00 42.73           C
ANISOU 3516  CG  PHE A 427     5523   5063   5651   -707    -60  -1258       C
ATOM   3517  CD1 PHE A 427     -38.208   2.573  15.499  1.00 39.26           C
ANISOU 3517  CD1 PHE A 427     5060   4663   5195   -648    -88  -1117       C
ATOM   3518  CD2 PHE A 427     -38.636   0.288  14.978  1.00 46.51           C
ANISOU 3518  CD2 PHE A 427     6012   5410   6251   -759    -28  -1306       C
ATOM   3519  CE1 PHE A 427     -38.757   2.392  16.758  1.00 37.12           C
ANISOU 3519  CE1 PHE A 427     4777   4321   5006   -634    -84  -1027       C
ATOM   3520  CE2 PHE A 427     -39.186   0.102  16.234  1.00 44.71           C
ANISOU 3520  CE2 PHE A 427     5769   5103   6117   -749    -19  -1197       C
ATOM   3521  CZ  PHE A 427     -39.245   1.156  17.125  1.00 39.18           C
ANISOU 3521  CZ  PHE A 427     5046   4462   5378   -682    -47  -1058       C
ATOM   3522  N   ALA A 428     -37.701   3.625  10.231  1.00 48.47           N
ANISOU 3522  N   ALA A 428     6217   6319   5880   -746   -144  -1418       N
ATOM   3523  CA  ALA A 428     -36.985   4.199   9.099  1.00 51.07           C
ANISOU 3523  CA  ALA A 428     6551   6780   6073   -715   -127  -1434       C
ATOM   3524  C   ALA A 428     -36.166   5.414   9.521  1.00 52.90           C
ANISOU 3524  C   ALA A 428     6771   7023   6305   -632   -109  -1282       C
ATOM   3525  O   ALA A 428     -35.056   5.625   9.017  1.00 57.07           O
ANISOU 3525  O   ALA A 428     7313   7576   6796   -586    -55  -1286       O
ATOM   3526  CB  ALA A 428     -37.965   4.577   7.989  1.00 53.43           C
ANISOU 3526  CB  ALA A 428     6814   7270   6216   -770   -194  -1465       C
ATOM   3527  N   TYR A 429     -36.681   6.216  10.462  1.00 50.37           N
ANISOU 3527  N   TYR A 429     6422   6681   6035   -614   -149  -1155       N
ATOM   3528  CA  TYR A 429     -35.930   7.391  10.899  1.00 52.31           C
ANISOU 3528  CA  TYR A 429     6653   6924   6297   -543   -135  -1027       C
ATOM   3529  C   TYR A 429     -34.617   7.025  11.585  1.00 50.38           C
ANISOU 3529  C   TYR A 429     6433   6555   6153   -487    -75  -1035       C
ATOM   3530  O   TYR A 429     -33.785   7.913  11.798  1.00 51.48           O
ANISOU 3530  O   TYR A 429     6555   6695   6309   -435    -57   -955       O
ATOM   3531  CB  TYR A 429     -36.787   8.293  11.814  1.00 50.01           C
ANISOU 3531  CB  TYR A 429     6329   6628   6046   -532   -189   -909       C
ATOM   3532  CG  TYR A 429     -37.128   7.736  13.188  1.00 44.61           C
ANISOU 3532  CG  TYR A 429     5652   5817   5479   -528   -194   -902       C
ATOM   3533  CD1 TYR A 429     -36.206   7.765  14.230  1.00 35.47           C
ANISOU 3533  CD1 TYR A 429     4509   4554   4413   -467   -163   -866       C
ATOM   3534  CD2 TYR A 429     -38.388   7.217  13.450  1.00 48.89           C
ANISOU 3534  CD2 TYR A 429     6180   6360   6038   -583   -231   -921       C
ATOM   3535  CE1 TYR A 429     -36.519   7.259  15.478  1.00 40.29           C
ANISOU 3535  CE1 TYR A 429     5127   5069   5112   -454   -165   -846       C
ATOM   3536  CE2 TYR A 429     -38.713   6.708  14.694  1.00 49.51           C
ANISOU 3536  CE2 TYR A 429     6262   6330   6219   -576   -224   -898       C
ATOM   3537  CZ  TYR A 429     -37.777   6.732  15.706  1.00 49.00           C
ANISOU 3537  CZ  TYR A 429     6220   6170   6229   -507   -190   -856       C
ATOM   3538  OH  TYR A 429     -38.098   6.226  16.946  1.00 49.49           O
ANISOU 3538  OH  TYR A 429     6286   6144   6375   -491   -181   -820       O
ATOM   3539  N   TYR A 430     -34.412   5.752  11.932  1.00 48.02           N
ANISOU 3539  N   TYR A 430     6167   6147   5930   -496    -42  -1126       N
ATOM   3540  CA  TYR A 430     -33.115   5.276  12.403  1.00 44.45           C
ANISOU 3540  CA  TYR A 430     5733   5593   5564   -436     18  -1141       C
ATOM   3541  C   TYR A 430     -32.230   4.797  11.259  1.00 39.44           C
ANISOU 3541  C   TYR A 430     5115   4994   4875   -428     81  -1239       C
ATOM   3542  O   TYR A 430     -31.012   4.998  11.292  1.00 44.67           O
ANISOU 3542  O   TYR A 430     5769   5639   5566   -369    130  -1218       O
ATOM   3543  CB  TYR A 430     -33.294   4.137  13.410  1.00 45.26           C
ANISOU 3543  CB  TYR A 430     5861   5549   5788   -433     32  -1169       C
ATOM   3544  CG  TYR A 430     -33.549   4.585  14.829  1.00 44.41           C
ANISOU 3544  CG  TYR A 430     5737   5389   5750   -397     -1  -1056       C
ATOM   3545  CD1 TYR A 430     -32.752   5.553  15.431  1.00 38.45           C
ANISOU 3545  CD1 TYR A 430     4956   4645   5007   -332     -9   -970       C
ATOM   3546  CD2 TYR A 430     -34.588   4.034  15.570  1.00 38.69           C
ANISOU 3546  CD2 TYR A 430     5017   4606   5078   -430    -22  -1040       C
ATOM   3547  CE1 TYR A 430     -32.989   5.960  16.732  1.00 34.53           C
ANISOU 3547  CE1 TYR A 430     4446   4115   4560   -295    -42   -886       C
ATOM   3548  CE2 TYR A 430     -34.830   4.433  16.865  1.00 36.07           C
ANISOU 3548  CE2 TYR A 430     4670   4242   4792   -389    -46   -939       C
ATOM   3549  CZ  TYR A 430     -34.030   5.393  17.441  1.00 38.13           C
ANISOU 3549  CZ  TYR A 430     4912   4526   5050   -319    -59   -869       C
ATOM   3550  OH  TYR A 430     -34.284   5.783  18.733  1.00 46.50           O
ANISOU 3550  OH  TYR A 430     5959   5567   6142   -276    -85   -786       O
ATOM   3551  N   PHE A 431     -32.820   4.159  10.244  1.00 38.87           N
ANISOU 3551  N   PHE A 431     5062   4981   4725   -487     80  -1355       N
ATOM   3552  CA  PHE A 431     -32.019   3.614   9.156  1.00 42.67           C
ANISOU 3552  CA  PHE A 431     5564   5502   5145   -476    146  -1469       C
ATOM   3553  C   PHE A 431     -31.515   4.696   8.212  1.00 43.52           C
ANISOU 3553  C   PHE A 431     5646   5768   5122   -452    161  -1410       C
ATOM   3554  O   PHE A 431     -30.552   4.455   7.475  1.00 48.12           O
ANISOU 3554  O   PHE A 431     6236   6386   5663   -418    232  -1469       O
ATOM   3555  CB  PHE A 431     -32.822   2.568   8.376  1.00 45.13           C
ANISOU 3555  CB  PHE A 431     5904   5831   5413   -550    137  -1633       C
ATOM   3556  CG  PHE A 431     -31.971   1.653   7.537  1.00 47.93           C
ANISOU 3556  CG  PHE A 431     6292   6171   5750   -531    217  -1785       C
ATOM   3557  CD1 PHE A 431     -31.322   0.570   8.108  1.00 47.24           C
ANISOU 3557  CD1 PHE A 431     6234   5905   5810   -497    279  -1850       C
ATOM   3558  CD2 PHE A 431     -31.814   1.882   6.178  1.00 52.45           C
ANISOU 3558  CD2 PHE A 431     6864   6913   6152   -539    234  -1859       C
ATOM   3559  CE1 PHE A 431     -30.530  -0.270   7.337  1.00 51.27           C
ANISOU 3559  CE1 PHE A 431     6773   6394   6313   -471    360  -1996       C
ATOM   3560  CE2 PHE A 431     -31.030   1.048   5.404  1.00 54.81           C
ANISOU 3560  CE2 PHE A 431     7193   7206   6427   -514    314  -2010       C
ATOM   3561  CZ  PHE A 431     -30.386  -0.029   5.984  1.00 55.30           C
ANISOU 3561  CZ  PHE A 431     7285   7076   6651   -480    379  -2084       C
ATOM   3562  N   ALA A 432     -32.135   5.878   8.229  1.00 42.35           N
ANISOU 3562  N   ALA A 432     5464   5713   4915   -463    104  -1288       N
ATOM   3563  CA  ALA A 432     -31.705   6.966   7.356  1.00 41.45           C
ANISOU 3563  CA  ALA A 432     5322   5740   4688   -438    124  -1205       C
ATOM   3564  C   ALA A 432     -30.222   7.261   7.544  1.00 40.61           C
ANISOU 3564  C   ALA A 432     5199   5584   4647   -373    200  -1159       C
ATOM   3565  O   ALA A 432     -29.441   7.218   6.586  1.00 45.49           O
ANISOU 3565  O   ALA A 432     5814   6283   5188   -351    269  -1192       O
ATOM   3566  CB  ALA A 432     -32.551   8.213   7.619  1.00 28.84           C
ANISOU 3566  CB  ALA A 432     3689   4202   3068   -447     55  -1061       C
ATOM   3567  N   ALA A 433     -29.812   7.531   8.790  1.00 35.64           N
ANISOU 3567  N   ALA A 433     4553   4830   4159   -342    190  -1088       N
ATOM   3568  CA  ALA A 433     -28.397   7.765   9.071  1.00 40.40           C
ANISOU 3568  CA  ALA A 433     5125   5383   4840   -284    252  -1052       C
ATOM   3569  C   ALA A 433     -27.530   6.598   8.619  1.00 46.64           C
ANISOU 3569  C   ALA A 433     5937   6142   5640   -256    330  -1175       C
ATOM   3570  O   ALA A 433     -26.388   6.807   8.197  1.00 47.11           O
ANISOU 3570  O   ALA A 433     5967   6232   5701   -214    402  -1162       O
ATOM   3571  CB  ALA A 433     -28.181   8.032  10.560  1.00 28.98           C
ANISOU 3571  CB  ALA A 433     3660   3814   3537   -255    214   -987       C
ATOM   3572  N   VAL A 434     -28.046   5.368   8.686  1.00 44.52           N
ANISOU 3572  N   VAL A 434     5718   5810   5389   -277    325  -1296       N
ATOM   3573  CA  VAL A 434     -27.305   4.240   8.125  1.00 47.85           C
ANISOU 3573  CA  VAL A 434     6164   6199   5817   -249    406  -1428       C
ATOM   3574  C   VAL A 434     -27.128   4.433   6.624  1.00 52.61           C
ANISOU 3574  C   VAL A 434     6768   6965   6257   -258    455  -1483       C
ATOM   3575  O   VAL A 434     -26.004   4.457   6.108  1.00 56.42           O
ANISOU 3575  O   VAL A 434     7229   7485   6725   -207    540  -1493       O
ATOM   3576  CB  VAL A 434     -28.006   2.907   8.439  1.00 44.20           C
ANISOU 3576  CB  VAL A 434     5754   5622   5419   -281    392  -1551       C
ATOM   3577  CG1 VAL A 434     -27.218   1.755   7.841  1.00 38.45           C
ANISOU 3577  CG1 VAL A 434     5053   4844   4712   -246    483  -1697       C
ATOM   3578  CG2 VAL A 434     -28.158   2.722   9.940  1.00 44.74           C
ANISOU 3578  CG2 VAL A 434     5820   5542   5637   -262    353  -1475       C
ATOM   3579  N   SER A 435     -28.244   4.607   5.907  1.00 52.89           N
ANISOU 3579  N   SER A 435     6821   7116   6159   -319    403  -1512       N
ATOM   3580  CA  SER A 435     -28.183   4.713   4.452  1.00 48.95           C
ANISOU 3580  CA  SER A 435     6325   6796   5476   -325    443  -1571       C
ATOM   3581  C   SER A 435     -27.305   5.878   4.018  1.00 43.80           C
ANISOU 3581  C   SER A 435     5624   6248   4770   -279    497  -1430       C
ATOM   3582  O   SER A 435     -26.576   5.780   3.025  1.00 39.66           O
ANISOU 3582  O   SER A 435     5095   5829   4147   -247    581  -1473       O
ATOM   3583  CB  SER A 435     -29.590   4.866   3.879  1.00 54.19           C
ANISOU 3583  CB  SER A 435     7001   7583   6005   -395    357  -1597       C
ATOM   3584  OG  SER A 435     -30.022   6.215   3.967  1.00 56.63           O
ANISOU 3584  OG  SER A 435     7270   7977   6270   -398    306  -1419       O
ATOM   3585  N   ALA A 436     -27.353   6.989   4.754  1.00 35.75           N
ANISOU 3585  N   ALA A 436     4564   5198   3823   -276    456  -1262       N
ATOM   3586  CA  ALA A 436     -26.522   8.134   4.404  1.00 39.74           C
ANISOU 3586  CA  ALA A 436     5014   5776   4308   -242    510  -1120       C
ATOM   3587  C   ALA A 436     -25.047   7.835   4.641  1.00 48.87           C
ANISOU 3587  C   ALA A 436     6140   6858   5570   -185    602  -1136       C
ATOM   3588  O   ALA A 436     -24.185   8.282   3.873  1.00 50.10           O
ANISOU 3588  O   ALA A 436     6257   7107   5670   -154    688  -1088       O
ATOM   3589  CB  ALA A 436     -26.960   9.363   5.201  1.00 30.22           C
ANISOU 3589  CB  ALA A 436     3774   4530   3179   -256    442   -957       C
ATOM   3590  N   VAL A 437     -24.735   7.076   5.693  1.00 43.46           N
ANISOU 3590  N   VAL A 437     5464   6012   5035   -166    589  -1195       N
ATOM   3591  CA  VAL A 437     -23.340   6.805   6.014  1.00 42.19           C
ANISOU 3591  CA  VAL A 437     5262   5783   4986   -105    667  -1201       C
ATOM   3592  C   VAL A 437     -22.733   5.877   4.971  1.00 48.85           C
ANISOU 3592  C   VAL A 437     6125   6686   5750    -70    768  -1333       C
ATOM   3593  O   VAL A 437     -21.790   6.246   4.260  1.00 56.52           O
ANISOU 3593  O   VAL A 437     7049   7746   6678    -35    859  -1298       O
ATOM   3594  CB  VAL A 437     -23.212   6.228   7.435  1.00 42.60           C
ANISOU 3594  CB  VAL A 437     5316   5661   5208    -83    620  -1217       C
ATOM   3595  CG1 VAL A 437     -21.887   5.512   7.606  1.00 45.98           C
ANISOU 3595  CG1 VAL A 437     5712   6024   5734    -10    702  -1267       C
ATOM   3596  CG2 VAL A 437     -23.328   7.338   8.457  1.00 41.40           C
ANISOU 3596  CG2 VAL A 437     5121   5467   5142    -95    547  -1080       C
ATOM   3597  N   TYR A 438     -23.290   4.671   4.837  1.00 47.94           N
ANISOU 3597  N   TYR A 438     6076   6524   5615    -82    759  -1489       N
ATOM   3598  CA  TYR A 438     -22.668   3.669   3.979  1.00 49.44           C
ANISOU 3598  CA  TYR A 438     6289   6741   5757    -41    858  -1641       C
ATOM   3599  C   TYR A 438     -22.678   4.096   2.518  1.00 56.37           C
ANISOU 3599  C   TYR A 438     7165   7830   6425    -48    913  -1657       C
ATOM   3600  O   TYR A 438     -21.688   3.890   1.805  1.00 65.11           O
ANISOU 3600  O   TYR A 438     8248   9002   7489      8   1025  -1699       O
ATOM   3601  CB  TYR A 438     -23.359   2.324   4.172  1.00 43.39           C
ANISOU 3601  CB  TYR A 438     5594   5861   5033    -64    833  -1810       C
ATOM   3602  CG  TYR A 438     -22.904   1.647   5.437  1.00 48.03           C
ANISOU 3602  CG  TYR A 438     6177   6244   5828    -20    830  -1803       C
ATOM   3603  CD1 TYR A 438     -21.709   0.939   5.475  1.00 52.19           C
ANISOU 3603  CD1 TYR A 438     6684   6698   6448     64    927  -1858       C
ATOM   3604  CD2 TYR A 438     -23.645   1.743   6.602  1.00 48.87           C
ANISOU 3604  CD2 TYR A 438     6293   6242   6033    -53    735  -1729       C
ATOM   3605  CE1 TYR A 438     -21.280   0.328   6.631  1.00 50.56           C
ANISOU 3605  CE1 TYR A 438     6467   6317   6426    115    922  -1834       C
ATOM   3606  CE2 TYR A 438     -23.224   1.133   7.768  1.00 50.50           C
ANISOU 3606  CE2 TYR A 438     6493   6280   6413     -4    734  -1707       C
ATOM   3607  CZ  TYR A 438     -22.040   0.427   7.774  1.00 50.63           C
ANISOU 3607  CZ  TYR A 438     6490   6229   6518     81    824  -1755       C
ATOM   3608  OH  TYR A 438     -21.612  -0.183   8.929  1.00 52.65           O
ANISOU 3608  OH  TYR A 438     6735   6329   6941    141    821  -1719       O
ATOM   3609  N   SER A 439     -23.773   4.709   2.058  1.00 56.18           N
ANISOU 3609  N   SER A 439     7159   7925   6263   -108    840  -1615       N
ATOM   3610  CA  SER A 439     -23.780   5.284   0.716  1.00 56.96           C
ANISOU 3610  CA  SER A 439     7247   8246   6148   -106    887  -1589       C
ATOM   3611  C   SER A 439     -22.596   6.219   0.530  1.00 50.87           C
ANISOU 3611  C   SER A 439     6401   7529   5398    -55    980  -1434       C
ATOM   3612  O   SER A 439     -21.887   6.152  -0.483  1.00 50.56           O
ANISOU 3612  O   SER A 439     6346   7622   5242    -12   1087  -1463       O
ATOM   3613  CB  SER A 439     -25.088   6.031   0.452  1.00 56.61           C
ANISOU 3613  CB  SER A 439     7214   8314   5981   -167    784  -1512       C
ATOM   3614  OG  SER A 439     -26.198   5.153   0.482  1.00 54.40           O
ANISOU 3614  OG  SER A 439     6991   8009   5671   -222    703  -1664       O
ATOM   3615  N   ALA A 440     -22.358   7.089   1.516  1.00 42.03           N
ANISOU 3615  N   ALA A 440     5230   6308   4430    -61    942  -1275       N
ATOM   3616  CA  ALA A 440     -21.183   7.950   1.485  1.00 43.03           C
ANISOU 3616  CA  ALA A 440     5274   6454   4621    -24   1026  -1134       C
ATOM   3617  C   ALA A 440     -19.934   7.126   1.217  1.00 50.36           C
ANISOU 3617  C   ALA A 440     6179   7368   5590     43   1145  -1233       C
ATOM   3618  O   ALA A 440     -19.196   7.383   0.257  1.00 55.62           O
ANISOU 3618  O   ALA A 440     6805   8168   6160     78   1258  -1202       O
ATOM   3619  CB  ALA A 440     -21.055   8.718   2.801  1.00 36.33           C
ANISOU 3619  CB  ALA A 440     4378   5459   3968    -41    958  -1008       C
ATOM   3620  N   LEU A 441     -19.718   6.092   2.039  1.00 44.56           N
ANISOU 3620  N   LEU A 441     5466   6474   4992     66   1128  -1350       N
ATOM   3621  CA  LEU A 441     -18.612   5.171   1.815  1.00 52.69           C
ANISOU 3621  CA  LEU A 441     6477   7474   6069    140   1239  -1459       C
ATOM   3622  C   LEU A 441     -18.569   4.743   0.357  1.00 52.84           C
ANISOU 3622  C   LEU A 441     6528   7663   5884    162   1334  -1571       C
ATOM   3623  O   LEU A 441     -17.563   4.939  -0.338  1.00 56.59           O
ANISOU 3623  O   LEU A 441     6947   8239   6315    214   1457  -1543       O
ATOM   3624  CB  LEU A 441     -18.750   3.955   2.732  1.00 36.52           C
ANISOU 3624  CB  LEU A 441     4475   5239   4162    159   1197  -1586       C
ATOM   3625  CG  LEU A 441     -17.663   2.896   2.555  1.00 48.77           C
ANISOU 3625  CG  LEU A 441     6011   6737   5783    246   1310  -1706       C
ATOM   3626  CD1 LEU A 441     -16.303   3.465   2.922  1.00 37.73           C
ANISOU 3626  CD1 LEU A 441     4499   5333   4504    303   1375  -1585       C
ATOM   3627  CD2 LEU A 441     -17.973   1.661   3.383  1.00 47.68           C
ANISOU 3627  CD2 LEU A 441     5930   6408   5778    264   1269  -1824       C
ATOM   3628  N   ALA A 442     -19.692   4.212  -0.132  1.00 53.01           N
ANISOU 3628  N   ALA A 442     6636   7734   5772    119   1278  -1696       N
ATOM   3629  CA  ALA A 442     -19.816   3.858  -1.540  1.00 57.09           C
ANISOU 3629  CA  ALA A 442     7188   8439   6063    133   1348  -1816       C
ATOM   3630  C   ALA A 442     -19.321   4.994  -2.425  1.00 58.74           C
ANISOU 3630  C   ALA A 442     7335   8851   6131    152   1427  -1655       C
ATOM   3631  O   ALA A 442     -18.312   4.857  -3.130  1.00 59.16           O
ANISOU 3631  O   ALA A 442     7352   8996   6131    217   1562  -1676       O
ATOM   3632  CB  ALA A 442     -21.272   3.508  -1.861  1.00 53.62           C
ANISOU 3632  CB  ALA A 442     6829   8051   5495     61   1240  -1926       C
ATOM   3633  N   LEU A 443     -19.985   6.151  -2.344  1.00 55.83           N
ANISOU 3633  N   LEU A 443     6949   8544   5720    101   1351  -1477       N
ATOM   3634  CA  LEU A 443     -19.625   7.264  -3.214  1.00 54.41           C
ANISOU 3634  CA  LEU A 443     6713   8551   5408    116   1426  -1302       C
ATOM   3635  C   LEU A 443     -18.148   7.591  -3.079  1.00 57.24           C
ANISOU 3635  C   LEU A 443     6980   8876   5894    170   1553  -1208       C
ATOM   3636  O   LEU A 443     -17.467   7.851  -4.080  1.00 59.19           O
ANISOU 3636  O   LEU A 443     7187   9288   6015    215   1681  -1162       O
ATOM   3637  CB  LEU A 443     -20.492   8.485  -2.897  1.00 52.61           C
ANISOU 3637  CB  LEU A 443     6472   8337   5182     59   1324  -1108       C
ATOM   3638  CG  LEU A 443     -21.991   8.314  -3.177  1.00 54.31           C
ANISOU 3638  CG  LEU A 443     6760   8629   5248      8   1201  -1174       C
ATOM   3639  CD1 LEU A 443     -22.791   9.531  -2.729  1.00 46.70           C
ANISOU 3639  CD1 LEU A 443     5774   7651   4321    -37   1105   -974       C
ATOM   3640  CD2 LEU A 443     -22.236   8.026  -4.653  1.00 58.87           C
ANISOU 3640  CD2 LEU A 443     7368   9461   5538     32   1254  -1258       C
ATOM   3641  N   SER A 444     -17.619   7.509  -1.853  1.00 60.03           N
ANISOU 3641  N   SER A 444     7293   9023   6493    171   1522  -1187       N
ATOM   3642  CA  SER A 444     -16.214   7.830  -1.630  1.00 57.11           C
ANISOU 3642  CA  SER A 444     6818   8616   6265    216   1629  -1100       C
ATOM   3643  C   SER A 444     -15.316   6.924  -2.459  1.00 57.70           C
ANISOU 3643  C   SER A 444     6885   8775   6265    296   1774  -1234       C
ATOM   3644  O   SER A 444     -14.465   7.400  -3.222  1.00 57.64           O
ANISOU 3644  O   SER A 444     6805   8899   6196    332   1905  -1146       O
ATOM   3645  CB  SER A 444     -15.881   7.717  -0.141  1.00 55.90           C
ANISOU 3645  CB  SER A 444     6630   8241   6370    209   1552  -1089       C
ATOM   3646  OG  SER A 444     -14.628   8.310   0.150  1.00 57.53           O
ANISOU 3646  OG  SER A 444     6716   8422   6723    234   1628   -973       O
ATOM   3647  N   VAL A 445     -15.528   5.607  -2.366  1.00 56.73           N
ANISOU 3647  N   VAL A 445     6835   8578   6142    324   1760  -1450       N
ATOM   3648  CA  VAL A 445     -14.680   4.696  -3.120  1.00 55.24           C
ANISOU 3648  CA  VAL A 445     6640   8453   5894    407   1902  -1597       C
ATOM   3649  C   VAL A 445     -14.944   4.814  -4.611  1.00 57.77           C
ANISOU 3649  C   VAL A 445     6995   9026   5929    420   1982  -1635       C
ATOM   3650  O   VAL A 445     -14.114   4.384  -5.418  1.00 60.55           O
ANISOU 3650  O   VAL A 445     7322   9485   6199    495   2127  -1712       O
ATOM   3651  CB  VAL A 445     -14.859   3.244  -2.639  1.00 54.98           C
ANISOU 3651  CB  VAL A 445     6681   8256   5954    436   1872  -1821       C
ATOM   3652  CG1 VAL A 445     -14.773   3.176  -1.120  1.00 52.98           C
ANISOU 3652  CG1 VAL A 445     6401   7772   5957    423   1776  -1763       C
ATOM   3653  CG2 VAL A 445     -16.170   2.664  -3.138  1.00 57.96           C
ANISOU 3653  CG2 VAL A 445     7175   8679   6167    385   1793  -1982       C
ATOM   3654  N   VAL A 446     -16.075   5.402  -5.004  1.00 62.01           N
ANISOU 3654  N   VAL A 446     7582   9674   6304    355   1892  -1578       N
ATOM   3655  CA  VAL A 446     -16.309   5.633  -6.423  1.00 65.00           C
ANISOU 3655  CA  VAL A 446     7982  10322   6393    373   1963  -1584       C
ATOM   3656  C   VAL A 446     -15.617   6.914  -6.872  1.00 69.57           C
ANISOU 3656  C   VAL A 446     8463  11034   6935    389   2061  -1327       C
ATOM   3657  O   VAL A 446     -15.207   7.029  -8.033  1.00 77.29           O
ANISOU 3657  O   VAL A 446     9423  12232   7711    440   2189  -1313       O
ATOM   3658  CB  VAL A 446     -17.820   5.656  -6.718  1.00 63.65           C
ANISOU 3658  CB  VAL A 446     7899  10234   6052    306   1823  -1637       C
ATOM   3659  CG1 VAL A 446     -18.087   5.882  -8.201  1.00 62.71           C
ANISOU 3659  CG1 VAL A 446     7799  10421   5609    332   1886  -1644       C
ATOM   3660  CG2 VAL A 446     -18.457   4.353  -6.265  1.00 63.04           C
ANISOU 3660  CG2 VAL A 446     7908  10008   6037    283   1738  -1892       C
ATOM   3661  N   PHE A 447     -15.439   7.879  -5.965  1.00 66.11           N
ANISOU 3661  N   PHE A 447     7957  10465   6696    346   2013  -1125       N
ATOM   3662  CA  PHE A 447     -14.814   9.140  -6.343  1.00 66.88           C
ANISOU 3662  CA  PHE A 447     7956  10661   6793    348   2106   -874       C
ATOM   3663  C   PHE A 447     -13.293   9.068  -6.323  1.00 72.52           C
ANISOU 3663  C   PHE A 447     8563  11351   7640    406   2260   -842       C
ATOM   3664  O   PHE A 447     -12.635   9.908  -6.946  1.00 75.20           O
ANISOU 3664  O   PHE A 447     8817  11815   7939    422   2383   -663       O
ATOM   3665  CB  PHE A 447     -15.304  10.259  -5.426  1.00 60.72           C
ANISOU 3665  CB  PHE A 447     7146   9748   6175    272   1989   -681       C
ATOM   3666  CG  PHE A 447     -16.767  10.556  -5.574  1.00 58.98           C
ANISOU 3666  CG  PHE A 447     7010   9585   5815    222   1856   -663       C
ATOM   3667  CD1 PHE A 447     -17.437  10.234  -6.744  1.00 60.05           C
ANISOU 3667  CD1 PHE A 447     7211   9944   5660    243   1868   -737       C
ATOM   3668  CD2 PHE A 447     -17.476  11.148  -4.543  1.00 57.64           C
ANISOU 3668  CD2 PHE A 447     6847   9255   5798    158   1716   -580       C
ATOM   3669  CE1 PHE A 447     -18.782  10.505  -6.886  1.00 58.02           C
ANISOU 3669  CE1 PHE A 447     7018   9752   5276    199   1739   -719       C
ATOM   3670  CE2 PHE A 447     -18.823  11.422  -4.678  1.00 58.78           C
ANISOU 3670  CE2 PHE A 447     7058   9456   5820    117   1597   -560       C
ATOM   3671  CZ  PHE A 447     -19.476  11.098  -5.850  1.00 59.45           C
ANISOU 3671  CZ  PHE A 447     7199   9765   5623    137   1606   -626       C
ATOM   3672  N   ASP A 448     -12.723   8.086  -5.625  1.00 71.36           N
ANISOU 3672  N   ASP A 448     8410  11048   7654    441   2261  -1002       N
ATOM   3673  CA  ASP A 448     -11.287   7.857  -5.698  1.00 72.39           C
ANISOU 3673  CA  ASP A 448     8436  11176   7894    511   2413   -999       C
ATOM   3674  C   ASP A 448     -10.932   7.030  -6.927  1.00 76.74           C
ANISOU 3674  C   ASP A 448     9017  11912   8227    597   2559  -1151       C
ATOM   3675  O   ASP A 448     -10.020   7.385  -7.683  1.00 79.88           O
ANISOU 3675  O   ASP A 448     9330  12457   8565    647   2723  -1060       O
ATOM   3676  CB  ASP A 448     -10.805   7.165  -4.422  1.00 76.38           C
ANISOU 3676  CB  ASP A 448     8915  11444   8663    526   2352  -1094       C
ATOM   3677  CG  ASP A 448      -9.303   7.293  -4.211  1.00 85.76           C
ANISOU 3677  CG  ASP A 448     9955  12605  10025    580   2477  -1022       C
ATOM   3678  OD1 ASP A 448      -8.572   7.595  -5.181  1.00 89.23           O
ANISOU 3678  OD1 ASP A 448    10325  13213  10364    621   2639   -954       O
ATOM   3679  OD2 ASP A 448      -8.853   7.087  -3.064  1.00 86.52           O
ANISOU 3679  OD2 ASP A 448     9998  12520  10354    582   2414  -1031       O
ATOM   3680  N   LYS A 449     -11.657   5.930  -7.146  1.00 77.42           N
ANISOU 3680  N   LYS A 449     9224  11995   8198    613   2506  -1388       N
ATOM   3681  CA  LYS A 449     -11.352   5.039  -8.261  1.00 80.98           C
ANISOU 3681  CA  LYS A 449     9712  12607   8448    696   2637  -1576       C
ATOM   3682  C   LYS A 449     -11.586   5.710  -9.609  1.00 83.22           C
ANISOU 3682  C   LYS A 449    10001  13189   8429    705   2720  -1483       C
ATOM   3683  O   LYS A 449     -10.922   5.365 -10.592  1.00 82.45           O
ANISOU 3683  O   LYS A 449     9893  13245   8191    785   2869  -1540       O
ATOM   3684  CB  LYS A 449     -12.189   3.763  -8.159  1.00 82.48           C
ANISOU 3684  CB  LYS A 449    10031  12710   8597    694   2546  -1858       C
ATOM   3685  CG  LYS A 449     -11.475   2.585  -7.508  1.00 87.94           C
ANISOU 3685  CG  LYS A 449    10717  13199   9498    760   2586  -2033       C
ATOM   3686  CD  LYS A 449     -10.977   2.929  -6.112  1.00 90.03           C
ANISOU 3686  CD  LYS A 449    10900  13237  10070    740   2521  -1889       C
ATOM   3687  CE  LYS A 449     -10.787   1.677  -5.268  1.00 92.69           C
ANISOU 3687  CE  LYS A 449    11269  13341  10606    785   2491  -2067       C
ATOM   3688  NZ  LYS A 449     -10.126   1.977  -3.964  1.00 93.43           N
ANISOU 3688  NZ  LYS A 449    11268  13251  10982    787   2444  -1927       N
ATOM   3689  N   LEU A 450     -12.519   6.662  -9.679  1.00 86.24           N
ANISOU 3689  N   LEU A 450    10408  13639   8721    631   2617  -1322       N
ATOM   3690  CA  LEU A 450     -12.853   7.340 -10.925  1.00 85.85           C
ANISOU 3690  CA  LEU A 450    10366  13879   8375    643   2680  -1208       C
ATOM   3691  C   LEU A 450     -12.223   8.727 -11.022  1.00 86.15           C
ANISOU 3691  C   LEU A 450    10286  13974   8474    632   2769   -883       C
ATOM   3692  O   LEU A 450     -12.675   9.554 -11.821  1.00 88.41           O
ANISOU 3692  O   LEU A 450    10574  14461   8559    625   2789   -716       O
ATOM   3693  CB  LEU A 450     -14.371   7.422 -11.086  1.00 81.67           C
ANISOU 3693  CB  LEU A 450     9940  13414   7678    580   2512  -1249       C
ATOM   3694  CG  LEU A 450     -15.090   6.071 -11.173  1.00 76.32           C
ANISOU 3694  CG  LEU A 450     9382  12688   6926    578   2420  -1567       C
ATOM   3695  CD1 LEU A 450     -16.557   6.244 -11.544  1.00 74.79           C
ANISOU 3695  CD1 LEU A 450     9275  12595   6546    515   2260  -1583       C
ATOM   3696  CD2 LEU A 450     -14.386   5.156 -12.166  1.00 75.34           C
ANISOU 3696  CD2 LEU A 450     9303  12613   6710    660   2526  -1718       C
ATOM   3697  N   HIS A 451     -11.196   8.994 -10.215  1.00 85.76           N
ANISOU 3697  N   HIS A 451    10129  13750   8706    630   2821   -788       N
ATOM   3698  CA  HIS A 451     -10.320  10.158 -10.311  1.00 87.84           C
ANISOU 3698  CA  HIS A 451    10258  14048   9071    623   2939   -510       C
ATOM   3699  C   HIS A 451     -11.025  11.479 -10.030  1.00 86.97           C
ANISOU 3699  C   HIS A 451    10135  13905   9007    538   2845   -261       C
ATOM   3700  O   HIS A 451     -10.461  12.539 -10.322  1.00 90.99           O
ANISOU 3700  O   HIS A 451    10541  14469   9561    527   2950    -13       O
ATOM   3701  CB  HIS A 451      -9.638  10.247 -11.684  1.00 90.70           C
ANISOU 3701  CB  HIS A 451    10574  14688   9200    704   3150   -451       C
ATOM   3702  CG  HIS A 451      -8.933   8.992 -12.101  1.00 91.16           C
ANISOU 3702  CG  HIS A 451    10669  14737   9232    784   3231   -689       C
ATOM   3703  ND1 HIS A 451      -8.290   8.871 -13.314  1.00 93.97           N
ANISOU 3703  ND1 HIS A 451    11033  15232   9441    840   3369   -675       N
ATOM   3704  CD2 HIS A 451      -8.767   7.805 -11.469  1.00 89.67           C
ANISOU 3704  CD2 HIS A 451    10511  14405   9154    820   3198   -942       C
ATOM   3705  CE1 HIS A 451      -7.761   7.665 -13.413  1.00 95.20           C
ANISOU 3705  CE1 HIS A 451    11223  15331   9617    910   3421   -909       C
ATOM   3706  NE2 HIS A 451      -8.038   6.997 -12.307  1.00 93.58           N
ANISOU 3706  NE2 HIS A 451    11035  14947   9574    901   3317  -1068       N
ATOM   3707  N   LEU A 452     -12.239  11.458  -9.473  1.00 84.04           N
ANISOU 3707  N   LEU A 452     9859  13437   8636    478   2656   -314       N
ATOM   3708  CA  LEU A 452     -12.914  12.716  -9.170  1.00 83.64           C
ANISOU 3708  CA  LEU A 452     9794  13342   8644    407   2569    -81       C
ATOM   3709  C   LEU A 452     -12.138  13.526  -8.140  1.00 87.11           C
ANISOU 3709  C   LEU A 452    10117  13565   9416    355   2573     74       C
ATOM   3710  O   LEU A 452     -12.166  14.761  -8.172  1.00 88.54           O
ANISOU 3710  O   LEU A 452    10238  13739   9665    313   2592    319       O
ATOM   3711  CB  LEU A 452     -14.341  12.457  -8.682  1.00 76.68           C
ANISOU 3711  CB  LEU A 452     9029  12389   7718    357   2366   -187       C
ATOM   3712  CG  LEU A 452     -15.202  13.693  -8.394  1.00 69.93           C
ANISOU 3712  CG  LEU A 452     8172  11494   6907    293   2266     34       C
ATOM   3713  CD1 LEU A 452     -15.127  14.698  -9.533  1.00 69.70           C
ANISOU 3713  CD1 LEU A 452     8098  11684   6701    320   2385    282       C
ATOM   3714  CD2 LEU A 452     -16.643  13.300  -8.142  1.00 66.31           C
ANISOU 3714  CD2 LEU A 452     7826  11020   6351    259   2085    -89       C
ATOM   3715  N   TYR A 453     -11.428  12.852  -7.233  1.00 87.22           N
ANISOU 3715  N   TYR A 453    10093  13402   9643    360   2557    -64       N
ATOM   3716  CA  TYR A 453     -10.612  13.564  -6.256  1.00 84.07           C
ANISOU 3716  CA  TYR A 453     9572  12817   9555    313   2556     60       C
ATOM   3717  C   TYR A 453      -9.399  14.202  -6.922  1.00 84.70           C
ANISOU 3717  C   TYR A 453     9512  12999   9672    336   2754    235       C
ATOM   3718  O   TYR A 453      -9.094  15.378  -6.685  1.00 87.01           O
ANISOU 3718  O   TYR A 453     9709  13226  10125    277   2778    449       O
ATOM   3719  CB  TYR A 453     -10.187  12.610  -5.142  1.00 80.58           C
ANISOU 3719  CB  TYR A 453     9124  12186   9306    326   2482   -133       C
ATOM   3720  CG  TYR A 453     -11.310  12.266  -4.192  1.00 76.01           C
ANISOU 3720  CG  TYR A 453     8652  11456   8771    282   2282   -246       C
ATOM   3721  CD1 TYR A 453     -12.197  13.241  -3.758  1.00 76.72           C
ANISOU 3721  CD1 TYR A 453     8767  11480   8904    208   2166   -115       C
ATOM   3722  CD2 TYR A 453     -11.486  10.967  -3.733  1.00 76.21           C
ANISOU 3722  CD2 TYR A 453     8752  11401   8802    319   2219   -476       C
ATOM   3723  CE1 TYR A 453     -13.228  12.934  -2.888  1.00 79.09           C
ANISOU 3723  CE1 TYR A 453     9158  11651   9240    171   1993   -212       C
ATOM   3724  CE2 TYR A 453     -12.514  10.650  -2.862  1.00 77.48           C
ANISOU 3724  CE2 TYR A 453     9005  11427   9007    278   2047   -565       C
ATOM   3725  CZ  TYR A 453     -13.383  11.638  -2.443  1.00 79.00           C
ANISOU 3725  CZ  TYR A 453     9217  11570   9231    204   1935   -433       C
ATOM   3726  OH  TYR A 453     -14.412  11.335  -1.579  1.00 76.56           O
ANISOU 3726  OH  TYR A 453     8993  11136   8962    166   1772   -516       O
ATOM   3727  N   ARG A 454      -8.692  13.435  -7.755  1.00 85.61           N
ANISOU 3727  N   ARG A 454     9610  13269   9648    420   2903    142       N
ATOM   3728  CA  ARG A 454      -7.622  14.013  -8.562  1.00 89.03           C
ANISOU 3728  CA  ARG A 454     9915  13842  10073    450   3110    316       C
ATOM   3729  C   ARG A 454      -8.148  15.161  -9.411  1.00 95.16           C
ANISOU 3729  C   ARG A 454    10694  14764  10699    423   3161    566       C
ATOM   3730  O   ARG A 454      -7.474  16.184  -9.575  1.00100.27           O
ANISOU 3730  O   ARG A 454    11216  15412  11469    392   3274    801       O
ATOM   3731  CB  ARG A 454      -6.994  12.941  -9.455  1.00 86.29           C
ANISOU 3731  CB  ARG A 454     9574  13672   9540    559   3261    157       C
ATOM   3732  CG  ARG A 454      -6.408  11.751  -8.715  1.00 81.51           C
ANISOU 3732  CG  ARG A 454     8961  12929   9082    605   3234    -82       C
ATOM   3733  CD  ARG A 454      -6.565  10.482  -9.537  1.00 85.44           C
ANISOU 3733  CD  ARG A 454     9559  13573   9329    703   3295   -320       C
ATOM   3734  NE  ARG A 454      -5.531   9.495  -9.236  1.00 92.04           N
ANISOU 3734  NE  ARG A 454    10334  14340  10296    780   3374   -483       N
ATOM   3735  CZ  ARG A 454      -4.640   9.054 -10.119  1.00 99.26           C
ANISOU 3735  CZ  ARG A 454    11194  15412  11108    874   3568   -528       C
ATOM   3736  NH1 ARG A 454      -4.654   9.510 -11.364  1.00 99.48           N
ANISOU 3736  NH1 ARG A 454    11258  15607  10931    869   3654   -425       N
ATOM   3737  NH2 ARG A 454      -3.734   8.156  -9.758  1.00105.09           N
ANISOU 3737  NH2 ARG A 454    11878  16059  11994    946   3625   -674       N
ATOM   3738  N   ALA A 455      -9.359  15.010  -9.949  1.00 95.09           N
ANISOU 3738  N   ALA A 455    10821  14876  10432    435   3079    525       N
ATOM   3739  CA  ALA A 455      -9.944  16.058 -10.777  1.00 97.26           C
ANISOU 3739  CA  ALA A 455    11105  15304  10544    424   3118    768       C
ATOM   3740  C   ALA A 455     -10.160  17.333  -9.975  1.00 99.69           C
ANISOU 3740  C   ALA A 455    11355  15413  11109    330   3041    986       C
ATOM   3741  O   ALA A 455      -9.780  18.425 -10.410  1.00101.70           O
ANISOU 3741  O   ALA A 455    11519  15708  11413    311   3157   1253       O
ATOM   3742  CB  ALA A 455     -11.262  15.572 -11.379  1.00 97.84           C
ANISOU 3742  CB  ALA A 455    11331  15539  10305    452   3012    655       C
ATOM   3743  N   LEU A 456     -10.776  17.211  -8.796  1.00 99.09           N
ANISOU 3743  N   LEU A 456    11331  15117  11204    270   2850    874       N
ATOM   3744  CA  LEU A 456     -11.030  18.386  -7.970  1.00 93.19           C
ANISOU 3744  CA  LEU A 456    10537  14170  10703    184   2768   1048       C
ATOM   3745  C   LEU A 456      -9.728  19.043  -7.532  1.00 97.05           C
ANISOU 3745  C   LEU A 456    10860  14529  11485    141   2876   1172       C
ATOM   3746  O   LEU A 456      -9.642  20.274  -7.452  1.00 96.03           O
ANISOU 3746  O   LEU A 456    10656  14321  11510     83   2909   1402       O
ATOM   3747  CB  LEU A 456     -11.878  18.003  -6.759  1.00 79.79           C
ANISOU 3747  CB  LEU A 456     8924  12275   9118    139   2551    877       C
ATOM   3748  CG  LEU A 456     -13.388  18.104  -6.975  1.00 76.41           C
ANISOU 3748  CG  LEU A 456     8622  11908   8500    135   2420    879       C
ATOM   3749  CD1 LEU A 456     -14.145  17.670  -5.729  1.00 69.44           C
ANISOU 3749  CD1 LEU A 456     7811  10828   7743     92   2222    707       C
ATOM   3750  CD2 LEU A 456     -13.772  19.520  -7.381  1.00 77.08           C
ANISOU 3750  CD2 LEU A 456     8672  12017   8597    108   2455   1171       C
ATOM   3751  N   GLU A 457      -8.698  18.239  -7.250  1.00101.34           N
ANISOU 3751  N   GLU A 457    11337  15047  12120    169   2933   1023       N
ATOM   3752  CA  GLU A 457      -7.407  18.819  -6.894  1.00108.21           C
ANISOU 3752  CA  GLU A 457    12033  15819  13264    130   3039   1134       C
ATOM   3753  C   GLU A 457      -6.767  19.529  -8.082  1.00114.00           C
ANISOU 3753  C   GLU A 457    12671  16726  13917    150   3260   1375       C
ATOM   3754  O   GLU A 457      -6.088  20.546  -7.901  1.00114.85           O
ANISOU 3754  O   GLU A 457    12641  16740  14258     85   3337   1568       O
ATOM   3755  CB  GLU A 457      -6.479  17.736  -6.340  1.00112.54           C
ANISOU 3755  CB  GLU A 457    12528  16316  13917    169   3046    920       C
ATOM   3756  CG  GLU A 457      -6.990  17.107  -5.050  1.00113.89           C
ANISOU 3756  CG  GLU A 457    12772  16297  14204    147   2837    714       C
ATOM   3757  CD  GLU A 457      -5.959  16.228  -4.370  1.00117.53           C
ANISOU 3757  CD  GLU A 457    13152  16682  14822    183   2844    550       C
ATOM   3758  OE1 GLU A 457      -4.919  16.760  -3.930  1.00119.70           O
ANISOU 3758  OE1 GLU A 457    13265  16877  15338    145   2897    633       O
ATOM   3759  OE2 GLU A 457      -6.192  15.004  -4.271  1.00117.90           O
ANISOU 3759  OE2 GLU A 457    13291  16745  14761    251   2796    338       O
ATOM   3760  N   ASN A 458      -6.986  19.022  -9.299  1.00119.31           N
ANISOU 3760  N   ASN A 458    13412  17656  14263    239   3364   1366       N
ATOM   3761  CA  ASN A 458      -6.472  19.694 -10.489  1.00121.54           C
ANISOU 3761  CA  ASN A 458    13663  18066  14453    247   3499   1555       C
ATOM   3762  C   ASN A 458      -7.261  20.955 -10.813  1.00130.24           C
ANISOU 3762  C   ASN A 458    14799  19147  15540    199   3460   1804       C
ATOM   3763  O   ASN A 458      -6.731  21.860 -11.469  1.00134.12           O
ANISOU 3763  O   ASN A 458    15231  19648  16080    176   3553   2009       O
ATOM   3764  CB  ASN A 458      -6.504  18.747 -11.686  1.00113.28           C
ANISOU 3764  CB  ASN A 458    12712  17263  13066    346   3567   1424       C
ATOM   3765  CG  ASN A 458      -5.478  17.650 -11.578  1.00110.35           C
ANISOU 3765  CG  ASN A 458    12289  16907  12733    399   3644   1215       C
ATOM   3766  OD1 ASN A 458      -4.888  17.444 -10.520  1.00106.28           O
ANISOU 3766  OD1 ASN A 458    11677  16230  12475    373   3623   1143       O
ATOM   3767  ND2 ASN A 458      -5.253  16.939 -12.673  1.00114.29           N
ANISOU 3767  ND2 ASN A 458    12848  17595  12981    478   3731   1113       N
ATOM   3768  N   ALA A 459      -8.527  21.021 -10.381  1.00130.57           N
ANISOU 3768  N   ALA A 459    14934  19161  15514    189   3327   1790       N
ATOM   3769  CA  ALA A 459      -9.358  22.191 -10.649  1.00132.67           C
ANISOU 3769  CA  ALA A 459    15238  19400  15771    155   3280   2022       C
ATOM   3770  C   ALA A 459      -8.686  23.469 -10.173  1.00137.37           C
ANISOU 3770  C   ALA A 459    15707  19775  16712     64   3318   2227       C
ATOM   3771  O   ALA A 459      -8.831  24.522 -10.805  1.00141.81           O
ANISOU 3771  O   ALA A 459    16267  20338  17277     52   3353   2456       O
ATOM   3772  CB  ALA A 459     -10.727  22.031  -9.986  1.00129.94           C
ANISOU 3772  CB  ALA A 459    14989  19018  15364    148   3120   1954       C
ATOM   3773  N   ILE A 460      -7.949  23.393  -9.067  1.00136.37           N
ANISOU 3773  N   ILE A 460    15474  19457  16884      2   3303   2140       N
ATOM   3774  CA  ILE A 460      -7.034  24.453  -8.665  1.00135.46           C
ANISOU 3774  CA  ILE A 460    15223  19144  17104    -89   3346   2282       C
ATOM   3775  C   ILE A 460      -6.029  23.871  -7.677  1.00131.60           C
ANISOU 3775  C   ILE A 460    14618  18536  16849   -123   3340   2106       C
ATOM   3776  O   ILE A 460      -6.398  23.143  -6.746  1.00128.18           O
ANISOU 3776  O   ILE A 460    14206  18042  16455   -118   3244   1928       O
ATOM   3777  CB  ILE A 460      -7.789  25.673  -8.090  1.00130.76           C
ANISOU 3777  CB  ILE A 460    14635  18347  16699   -164   3254   2440       C
ATOM   3778  CG1 ILE A 460      -6.930  26.937  -8.191  1.00131.21           C
ANISOU 3778  CG1 ILE A 460    14578  18253  17022   -239   3325   2633       C
ATOM   3779  CG2 ILE A 460      -8.265  25.439  -6.657  1.00126.31           C
ANISOU 3779  CG2 ILE A 460    14068  17601  16324   -217   3114   2292       C
ATOM   3780  CD1 ILE A 460      -7.711  28.220  -8.003  1.00130.27           C
ANISOU 3780  CD1 ILE A 460    14488  17970  17040   -288   3263   2819       C
ATOM   3781  N   GLY A 461      -4.739  24.125  -7.916  1.00131.10           N
ANISOU 3781  N   GLY A 461    14429  18455  16927   -149   3445   2153       N
ATOM   3782  CA  GLY A 461      -3.690  23.875  -6.951  1.00129.61           C
ANISOU 3782  CA  GLY A 461    14103  18129  17013   -198   3428   2029       C
ATOM   3783  C   GLY A 461      -2.778  22.702  -7.270  1.00129.16           C
ANISOU 3783  C   GLY A 461    14002  18218  16854   -121   3514   1870       C
ATOM   3784  O   GLY A 461      -1.605  22.724  -6.874  1.00131.95           O
ANISOU 3784  O   GLY A 461    14214  18500  17421   -156   3547   1836       O
ATOM   3785  N   ALA A 462      -3.277  21.677  -7.961  1.00120.29           N
ANISOU 3785  N   ALA A 462    12997  17293  15414    -14   3547   1761       N
ATOM   3786  CA  ALA A 462      -2.556  20.412  -8.036  1.00112.19           C
ANISOU 3786  CA  ALA A 462    11945  16369  14312     68   3603   1560       C
ATOM   3787  C   ALA A 462      -2.394  19.936  -9.475  1.00107.20           C
ANISOU 3787  C   ALA A 462    11380  15981  13371    158   3736   1562       C
ATOM   3788  O   ALA A 462      -2.954  20.501 -10.419  1.00106.41           O
ANISOU 3788  O   ALA A 462    11357  15989  13083    165   3772   1712       O
ATOM   3789  CB  ALA A 462      -3.254  19.328  -7.204  1.00108.98           C
ANISOU 3789  CB  ALA A 462    11619  15931  13859    120   3492   1337       C
ATOM   3790  N   ARG A 463      -1.603  18.869  -9.615  1.00104.47           N
ANISOU 3790  N   ARG A 463    10998  15715  12979    231   3804   1388       N
ATOM   3791  CA  ARG A 463      -1.329  18.204 -10.882  1.00104.78           C
ANISOU 3791  CA  ARG A 463    11095  15976  12741    324   3930   1330       C
ATOM   3792  C   ARG A 463      -1.580  16.711 -10.713  1.00110.70           C
ANISOU 3792  C   ARG A 463    11932  16782  13346    422   3898   1047       C
ATOM   3793  O   ARG A 463      -1.089  16.103  -9.756  1.00112.96           O
ANISOU 3793  O   ARG A 463    12148  16952  13820    435   3857    907       O
ATOM   3794  CB  ARG A 463       0.117  18.454 -11.343  1.00102.10           C
ANISOU 3794  CB  ARG A 463    10605  15671  12519    317   4076   1408       C
ATOM   3795  CG  ARG A 463       1.183  18.037 -10.328  1.00101.07           C
ANISOU 3795  CG  ARG A 463    10322  15409  12669    304   4061   1293       C
ATOM   3796  CD  ARG A 463       2.446  17.505 -11.000  1.00108.08           C
ANISOU 3796  CD  ARG A 463    11115  16416  13534    365   4212   1241       C
ATOM   3797  NE  ARG A 463       3.341  16.853 -10.044  1.00111.29           N
ANISOU 3797  NE  ARG A 463    11396  16723  14164    381   4180   1094       N
ATOM   3798  CZ  ARG A 463       4.467  16.227 -10.375  1.00114.88           C
ANISOU 3798  CZ  ARG A 463    11754  17257  14637    443   4288   1012       C
ATOM   3799  NH1 ARG A 463       4.851  16.173 -11.643  1.00118.16           N
ANISOU 3799  NH1 ARG A 463    12186  17850  14861    490   4445   1058       N
ATOM   3800  NH2 ARG A 463       5.216  15.662  -9.436  1.00114.42           N
ANISOU 3800  NH2 ARG A 463    11582  17104  14787    464   4238    887       N
ATOM   3801  N   ASN A 464      -2.355  16.127 -11.625  1.00113.21           N
ANISOU 3801  N   ASN A 464    12406  17271  13339    492   3907    959       N
ATOM   3802  CA  ASN A 464      -2.642  14.700 -11.585  1.00112.80           C
ANISOU 3802  CA  ASN A 464    12454  17267  13139    583   3878    676       C
ATOM   3803  C   ASN A 464      -2.934  14.206 -12.992  1.00114.87           C
ANISOU 3803  C   ASN A 464    12839  17746  13058    654   3953    607       C
ATOM   3804  O   ASN A 464      -3.453  14.949 -13.828  1.00116.51           O
ANISOU 3804  O   ASN A 464    13102  18069  13098    634   3965    770       O
ATOM   3805  CB  ASN A 464      -3.839  14.367 -10.680  1.00111.72           C
ANISOU 3805  CB  ASN A 464    12417  17039  12993    574   3711    567       C
ATOM   3806  CG  ASN A 464      -3.616  14.762  -9.234  1.00112.73           C
ANISOU 3806  CG  ASN A 464    12433  16946  13454    512   3629    614       C
ATOM   3807  OD1 ASN A 464      -2.874  14.103  -8.505  1.00115.01           O
ANISOU 3807  OD1 ASN A 464    12650  17126  13923    540   3622    480       O
ATOM   3808  ND2 ASN A 464      -4.260  15.843  -8.811  1.00112.18           N
ANISOU 3808  ND2 ASN A 464    12366  16776  13480    418   3534    785       N
ATOM   3809  N   LYS A 465      -2.586  12.946 -13.250  1.00115.19           N
ANISOU 3809  N   LYS A 465    12925  17835  13008    741   3999    362       N
ATOM   3810  CA  LYS A 465      -3.083  12.272 -14.443  1.00118.33           C
ANISOU 3810  CA  LYS A 465    13469  18413  13076    809   4032    233       C
ATOM   3811  C   LYS A 465      -4.550  11.944 -14.238  1.00114.39           C
ANISOU 3811  C   LYS A 465    13130  17917  12417    803   3867    121       C
ATOM   3812  O   LYS A 465      -4.947  11.472 -13.169  1.00109.67           O
ANISOU 3812  O   LYS A 465    12549  17176  11944    794   3755     -6       O
ATOM   3813  CB  LYS A 465      -2.298  10.994 -14.727  1.00120.31           C
ANISOU 3813  CB  LYS A 465    13727  18681  13305    901   4128    -11       C
ATOM   3814  CG  LYS A 465      -3.091   9.943 -15.512  1.00122.12           C
ANISOU 3814  CG  LYS A 465    14142  19015  13243    969   4096   -244       C
ATOM   3815  CD  LYS A 465      -3.386   8.722 -14.653  1.00119.72           C
ANISOU 3815  CD  LYS A 465    13906  18558  13026   1010   4003   -517       C
ATOM   3816  CE  LYS A 465      -4.501   7.873 -15.241  1.00118.73           C
ANISOU 3816  CE  LYS A 465    13975  18501  12637   1043   3912   -728       C
ATOM   3817  NZ  LYS A 465      -4.523   6.514 -14.634  1.00117.17           N
ANISOU 3817  NZ  LYS A 465    13843  18148  12529   1101   3863  -1009       N
ATOM   3818  N   LEU A 466      -5.365  12.182 -15.254  1.00113.34           N
ANISOU 3818  N   LEU A 466    13109  17951  12006    809   3845    167       N
ATOM   3819  CA  LEU A 466      -6.792  12.220 -14.992  1.00107.56           C
ANISOU 3819  CA  LEU A 466    12495  17220  11152    778   3672    130       C
ATOM   3820  C   LEU A 466      -7.569  11.877 -16.254  1.00112.80           C
ANISOU 3820  C   LEU A 466    13300  18088  11469    819   3648     51       C
ATOM   3821  O   LEU A 466      -7.355  12.464 -17.320  1.00118.40           O
ANISOU 3821  O   LEU A 466    14000  18958  12030    836   3737    210       O
ATOM   3822  CB  LEU A 466      -7.156  13.598 -14.407  1.00101.12           C
ANISOU 3822  CB  LEU A 466    11609  16329  10483    693   3614    411       C
ATOM   3823  CG  LEU A 466      -7.190  14.957 -15.126  1.00 98.69           C
ANISOU 3823  CG  LEU A 466    11261  16108  10128    657   3665    726       C
ATOM   3824  CD1 LEU A 466      -7.800  15.951 -14.143  1.00 93.50           C
ANISOU 3824  CD1 LEU A 466    10565  15298   9661    574   3558    904       C
ATOM   3825  CD2 LEU A 466      -5.834  15.425 -15.723  1.00100.25           C
ANISOU 3825  CD2 LEU A 466    11335  16343  10413    666   3849    875       C
ATOM   3826  N   SER A 467      -8.414  10.856 -16.131  1.00110.06           N
ANISOU 3826  N   SER A 467    13079  17732  11006    838   3529   -208       N
ATOM   3827  CA  SER A 467      -9.268  10.365 -17.207  1.00105.53           C
ANISOU 3827  CA  SER A 467    12644  17333  10120    871   3470   -334       C
ATOM   3828  C   SER A 467     -10.646  10.990 -17.003  1.00105.53           C
ANISOU 3828  C   SER A 467    12703  17363  10031    812   3297   -240       C
ATOM   3829  O   SER A 467     -11.417  10.535 -16.152  1.00106.04           O
ANISOU 3829  O   SER A 467    12818  17313  10159    776   3155   -384       O
ATOM   3830  CB  SER A 467      -9.328   8.838 -17.191  1.00 97.88           C
ANISOU 3830  CB  SER A 467    11772  16310   9110    919   3440   -684       C
ATOM   3831  OG  SER A 467     -10.268   8.362 -18.138  1.00 93.81           O
ANISOU 3831  OG  SER A 467    11387  15947   8311    936   3356   -820       O
ATOM   3832  N   TYR A 468     -10.946  12.057 -17.767  1.00107.72           N
ANISOU 3832  N   TYR A 468    12967  17789  10174    803   3310     11       N
ATOM   3833  CA  TYR A 468     -12.250  12.707 -17.648  1.00110.75           C
ANISOU 3833  CA  TYR A 468    13398  18209  10471    757   3151    121       C
ATOM   3834  C   TYR A 468     -13.382  11.778 -18.031  1.00111.12           C
ANISOU 3834  C   TYR A 468    13579  18345  10297    767   3002   -132       C
ATOM   3835  O   TYR A 468     -14.531  12.056 -17.689  1.00109.90           O
ANISOU 3835  O   TYR A 468    13466  18185  10105    722   2846   -109       O
ATOM   3836  CB  TYR A 468     -12.362  13.969 -18.506  1.00115.32           C
ANISOU 3836  CB  TYR A 468    13941  18935  10941    762   3195    436       C
ATOM   3837  CG  TYR A 468     -11.437  15.110 -18.098  1.00116.97           C
ANISOU 3837  CG  TYR A 468    14015  19034  11396    730   3317    726       C
ATOM   3838  CD1 TYR A 468     -10.038  14.985 -18.156  1.00114.72           C
ANISOU 3838  CD1 TYR A 468    13637  18707  11246    750   3489    736       C
ATOM   3839  CD2 TYR A 468     -11.965  16.286 -17.605  1.00117.77           C
ANISOU 3839  CD2 TYR A 468    14075  19056  11618    676   3253    979       C
ATOM   3840  CE1 TYR A 468      -9.190  16.025 -17.799  1.00112.56           C
ANISOU 3840  CE1 TYR A 468    13231  18325  11213    709   3591    992       C
ATOM   3841  CE2 TYR A 468     -11.148  17.325 -17.211  1.00117.29           C
ANISOU 3841  CE2 TYR A 468    13891  18867  11808    636   3354   1231       C
ATOM   3842  CZ  TYR A 468      -9.743  17.192 -17.317  1.00113.80           C
ANISOU 3842  CZ  TYR A 468    13353  18390  11495    649   3521   1235       C
ATOM   3843  OH  TYR A 468      -8.860  18.173 -16.923  1.00112.90           O
ANISOU 3843  OH  TYR A 468    13106  18141  11651    599   3617   1463       O
ATOM   3844  N   PHE A 469     -13.097  10.714 -18.780  1.00113.40           N
ANISOU 3844  N   PHE A 469    13932  18716  10440    821   3048   -367       N
ATOM   3845  CA  PHE A 469     -14.065   9.632 -18.917  1.00116.37           C
ANISOU 3845  CA  PHE A 469    14426  19110  10678    817   2902   -659       C
ATOM   3846  C   PHE A 469     -14.491   9.148 -17.538  1.00108.88           C
ANISOU 3846  C   PHE A 469    13492  17935   9944    760   2786   -803       C
ATOM   3847  O   PHE A 469     -15.680   9.150 -17.195  1.00108.09           O
ANISOU 3847  O   PHE A 469    13443  17821   9804    707   2617   -849       O
ATOM   3848  CB  PHE A 469     -13.452   8.492 -19.743  1.00125.24           C
ANISOU 3848  CB  PHE A 469    15603  20296  11684    885   2995   -901       C
ATOM   3849  CG  PHE A 469     -14.458   7.507 -20.278  1.00132.02           C
ANISOU 3849  CG  PHE A 469    16582  21226  12351    883   2857  -1173       C
ATOM   3850  CD1 PHE A 469     -15.149   7.768 -21.451  1.00136.53           C
ANISOU 3850  CD1 PHE A 469    17197  22040  12638    901   2805  -1133       C
ATOM   3851  CD2 PHE A 469     -14.701   6.312 -19.615  1.00133.83           C
ANISOU 3851  CD2 PHE A 469    16876  21277  12698    864   2780  -1464       C
ATOM   3852  CE1 PHE A 469     -16.073   6.861 -21.947  1.00139.22           C
ANISOU 3852  CE1 PHE A 469    17635  22448  12814    892   2673  -1389       C
ATOM   3853  CE2 PHE A 469     -15.625   5.402 -20.108  1.00136.18           C
ANISOU 3853  CE2 PHE A 469    17276  21623  12845    851   2652  -1714       C
ATOM   3854  CZ  PHE A 469     -16.310   5.678 -21.275  1.00138.65           C
ANISOU 3854  CZ  PHE A 469    17624  22184  12874    862   2597  -1682       C
ATOM   3855  N   ARG A 470     -13.506   8.776 -16.716  1.00101.76           N
ANISOU 3855  N   ARG A 470    12531  16854   9278    771   2879   -860       N
ATOM   3856  CA  ARG A 470     -13.792   8.301 -15.368  1.00 93.73           C
ANISOU 3856  CA  ARG A 470    11516  15619   8477    725   2781   -993       C
ATOM   3857  C   ARG A 470     -14.434   9.389 -14.521  1.00 87.26           C
ANISOU 3857  C   ARG A 470    10646  14750   7758    655   2689   -779       C
ATOM   3858  O   ARG A 470     -15.305   9.105 -13.696  1.00 88.20           O
ANISOU 3858  O   ARG A 470    10806  14764   7941    601   2544   -887       O
ATOM   3859  CB  ARG A 470     -12.509   7.802 -14.703  1.00 94.44           C
ANISOU 3859  CB  ARG A 470    11532  15546   8805    764   2908  -1061       C
ATOM   3860  CG  ARG A 470     -11.933   6.534 -15.310  1.00 98.90           C
ANISOU 3860  CG  ARG A 470    12156  16104   9316    837   2986  -1311       C
ATOM   3861  CD  ARG A 470     -10.806   5.978 -14.451  1.00102.69           C
ANISOU 3861  CD  ARG A 470    12562  16392  10064    876   3081  -1386       C
ATOM   3862  NE  ARG A 470     -10.244   4.744 -14.997  1.00110.76           N
ANISOU 3862  NE  ARG A 470    13642  17387  11054    955   3160  -1618       N
ATOM   3863  CZ  ARG A 470     -10.718   3.528 -14.743  1.00113.46           C
ANISOU 3863  CZ  ARG A 470    14084  17600  11425    963   3069  -1887       C
ATOM   3864  NH1 ARG A 470     -11.770   3.375 -13.950  1.00111.14           N
ANISOU 3864  NH1 ARG A 470    13842  17195  11192    890   2897  -1962       N
ATOM   3865  NH2 ARG A 470     -10.141   2.462 -15.285  1.00115.73           N
ANISOU 3865  NH2 ARG A 470    14419  17860  11692   1042   3155  -2077       N
ATOM   3866  N   VAL A 471     -14.031  10.643 -14.719  1.00 83.38           N
ANISOU 3866  N   VAL A 471    10066  14324   7291    652   2773   -473       N
ATOM   3867  CA  VAL A 471     -14.534  11.718 -13.868  1.00 80.09           C
ANISOU 3867  CA  VAL A 471     9594  13833   7004    589   2702   -255       C
ATOM   3868  C   VAL A 471     -15.991  12.027 -14.197  1.00 75.07           C
ANISOU 3868  C   VAL A 471     9039  13303   6181    556   2540   -225       C
ATOM   3869  O   VAL A 471     -16.831  12.156 -13.300  1.00 70.23           O
ANISOU 3869  O   VAL A 471     8439  12597   5647    499   2411   -239       O
ATOM   3870  CB  VAL A 471     -13.638  12.961 -14.001  1.00 84.72           C
ANISOU 3870  CB  VAL A 471    10059  14423   7707    590   2842     67       C
ATOM   3871  CG1 VAL A 471     -14.310  14.170 -13.376  1.00 83.46           C
ANISOU 3871  CG1 VAL A 471     9858  14202   7650    529   2764    316       C
ATOM   3872  CG2 VAL A 471     -12.288  12.700 -13.355  1.00 87.17           C
ANISOU 3872  CG2 VAL A 471    10266  14593   8264    605   2970     37       C
ATOM   3873  N   ALA A 472     -16.310  12.160 -15.485  1.00 76.59           N
ANISOU 3873  N   ALA A 472     9280  13699   6124    593   2545   -180       N
ATOM   3874  CA  ALA A 472     -17.698  12.346 -15.890  1.00 76.91           C
ANISOU 3874  CA  ALA A 472     9389  13857   5975    572   2383   -172       C
ATOM   3875  C   ALA A 472     -18.552  11.150 -15.498  1.00 78.38           C
ANISOU 3875  C   ALA A 472     9666  13983   6131    538   2233   -494       C
ATOM   3876  O   ALA A 472     -19.725  11.315 -15.142  1.00 77.52           O
ANISOU 3876  O   ALA A 472     9590  13871   5995    489   2075   -498       O
ATOM   3877  CB  ALA A 472     -17.778  12.591 -17.397  1.00 76.65           C
ANISOU 3877  CB  ALA A 472     9382  14067   5676    629   2422    -89       C
ATOM   3878  N   PHE A 473     -17.979   9.944 -15.527  1.00 78.36           N
ANISOU 3878  N   PHE A 473     9702  13916   6156    562   2280   -762       N
ATOM   3879  CA  PHE A 473     -18.706   8.774 -15.047  1.00 77.93           C
ANISOU 3879  CA  PHE A 473     9728  13751   6130    522   2146  -1066       C
ATOM   3880  C   PHE A 473     -18.986   8.867 -13.551  1.00 74.98           C
ANISOU 3880  C   PHE A 473     9328  13169   5993    457   2071  -1072       C
ATOM   3881  O   PHE A 473     -20.086   8.529 -13.095  1.00 69.38           O
ANISOU 3881  O   PHE A 473     8670  12404   5286    397   1913  -1190       O
ATOM   3882  CB  PHE A 473     -17.907   7.515 -15.368  1.00 84.56           C
ANISOU 3882  CB  PHE A 473    10609  14535   6986    570   2233  -1323       C
ATOM   3883  CG  PHE A 473     -18.734   6.276 -15.410  1.00 94.06           C
ANISOU 3883  CG  PHE A 473    11911  15679   8150    539   2102  -1630       C
ATOM   3884  CD1 PHE A 473     -19.539   6.005 -16.503  1.00100.76           C
ANISOU 3884  CD1 PHE A 473    12822  16705   8758    540   2020  -1717       C
ATOM   3885  CD2 PHE A 473     -18.709   5.379 -14.358  1.00 96.41           C
ANISOU 3885  CD2 PHE A 473    12231  15735   8665    507   2059  -1827       C
ATOM   3886  CE1 PHE A 473     -20.305   4.860 -16.545  1.00105.25           C
ANISOU 3886  CE1 PHE A 473    13470  17208   9313    502   1899  -1999       C
ATOM   3887  CE2 PHE A 473     -19.472   4.231 -14.394  1.00100.44           C
ANISOU 3887  CE2 PHE A 473    12828  16166   9168    471   1943  -2097       C
ATOM   3888  CZ  PHE A 473     -20.272   3.971 -15.489  1.00103.96           C
ANISOU 3888  CZ  PHE A 473    13331  16786   9382    465   1863  -2185       C
ATOM   3889  N   ALA A 474     -17.997   9.309 -12.770  1.00 75.59           N
ANISOU 3889  N   ALA A 474     9317  13129   6277    466   2184   -950       N
ATOM   3890  CA  ALA A 474     -18.201   9.499 -11.338  1.00 74.73           C
ANISOU 3890  CA  ALA A 474     9186  12754   6454    399   2087   -918       C
ATOM   3891  C   ALA A 474     -19.270  10.547 -11.074  1.00 72.73           C
ANISOU 3891  C   ALA A 474     8934  12501   6199    341   1954   -713       C
ATOM   3892  O   ALA A 474     -20.074  10.407 -10.146  1.00 70.55           O
ANISOU 3892  O   ALA A 474     8694  12044   6067    276   1801   -770       O
ATOM   3893  CB  ALA A 474     -16.887   9.898 -10.666  1.00 73.37           C
ANISOU 3893  CB  ALA A 474     8919  12406   6553    413   2201   -785       C
ATOM   3894  N   LEU A 475     -19.289  11.610 -11.876  1.00 69.91           N
ANISOU 3894  N   LEU A 475     8533  12344   5685    369   2018   -465       N
ATOM   3895  CA  LEU A 475     -20.354  12.599 -11.760  1.00 67.92           C
ANISOU 3895  CA  LEU A 475     8283  12116   5408    330   1900   -267       C
ATOM   3896  C   LEU A 475     -21.712  11.973 -12.061  1.00 68.15           C
ANISOU 3896  C   LEU A 475     8394  12263   5235    306   1742   -449       C
ATOM   3897  O   LEU A 475     -22.697  12.235 -11.358  1.00 65.51           O
ANISOU 3897  O   LEU A 475     8079  11810   5000    247   1590   -421       O
ATOM   3898  CB  LEU A 475     -20.079  13.777 -12.692  1.00 68.97           C
ANISOU 3898  CB  LEU A 475     8354  12460   5393    380   2016     37       C
ATOM   3899  CG  LEU A 475     -18.742  14.484 -12.477  1.00 70.68           C
ANISOU 3899  CG  LEU A 475     8472  12571   5813    395   2182    236       C
ATOM   3900  CD1 LEU A 475     -18.581  15.636 -13.455  1.00 70.40           C
ANISOU 3900  CD1 LEU A 475     8384  12725   5642    438   2289    547       C
ATOM   3901  CD2 LEU A 475     -18.620  14.961 -11.038  1.00 70.86           C
ANISOU 3901  CD2 LEU A 475     8458  12256   6209    322   2106    303       C
ATOM   3902  N   LEU A 476     -21.780  11.145 -13.108  1.00 66.13           N
ANISOU 3902  N   LEU A 476     8191  12196   4741    345   1760   -635       N
ATOM   3903  CA  LEU A 476     -23.021  10.449 -13.434  1.00 63.93           C
ANISOU 3903  CA  LEU A 476     7989  11975   4327    310   1591   -829       C
ATOM   3904  C   LEU A 476     -23.499   9.603 -12.260  1.00 63.84           C
ANISOU 3904  C   LEU A 476     8013  11757   4486    239   1488  -1057       C
ATOM   3905  O   LEU A 476     -24.683   9.632 -11.901  1.00 67.38           O
ANISOU 3905  O   LEU A 476     8484  12192   4925    181   1333  -1086       O
ATOM   3906  CB  LEU A 476     -22.816   9.583 -14.677  1.00 64.22           C
ANISOU 3906  CB  LEU A 476     8079  12145   4178    356   1621  -1010       C
ATOM   3907  CG  LEU A 476     -24.056   9.064 -15.405  1.00 65.62           C
ANISOU 3907  CG  LEU A 476     8313  12449   4169    332   1462  -1161       C
ATOM   3908  CD1 LEU A 476     -23.799   9.031 -16.903  1.00 66.66           C
ANISOU 3908  CD1 LEU A 476     8459  12814   4057    401   1523  -1149       C
ATOM   3909  CD2 LEU A 476     -24.449   7.682 -14.899  1.00 66.27           C
ANISOU 3909  CD2 LEU A 476     8460  12369   4352    275   1373  -1495       C
ATOM   3910  N   ILE A 477     -22.584   8.860 -11.639  1.00 60.25           N
ANISOU 3910  N   ILE A 477     7559  11124   4208    244   1571  -1207       N
ATOM   3911  CA  ILE A 477     -22.946   8.020 -10.501  1.00 55.96           C
ANISOU 3911  CA  ILE A 477     7057  10304   3902    179   1464  -1393       C
ATOM   3912  C   ILE A 477     -23.398   8.872  -9.319  1.00 58.72           C
ANISOU 3912  C   ILE A 477     7378  10443   4491    123   1362  -1195       C
ATOM   3913  O   ILE A 477     -24.372   8.539  -8.628  1.00 63.52           O
ANISOU 3913  O   ILE A 477     8022  10929   5185     59   1220  -1283       O
ATOM   3914  CB  ILE A 477     -21.767   7.105 -10.130  1.00 58.46           C
ANISOU 3914  CB  ILE A 477     7375  10453   4383    215   1579  -1554       C
ATOM   3915  CG1 ILE A 477     -21.331   6.296 -11.351  1.00 63.28           C
ANISOU 3915  CG1 ILE A 477     8023  11231   4791    277   1670  -1731       C
ATOM   3916  CG2 ILE A 477     -22.141   6.190  -8.978  1.00 53.79           C
ANISOU 3916  CG2 ILE A 477     6827   9580   4029    157   1477  -1733       C
ATOM   3917  CD1 ILE A 477     -20.552   5.055 -11.016  1.00 68.80           C
ANISOU 3917  CD1 ILE A 477     8751  11741   5649    304   1736  -1962       C
ATOM   3918  N   ALA A 478     -22.710   9.989  -9.073  1.00 57.92           N
ANISOU 3918  N   ALA A 478     7207  10298   4503    145   1437   -931       N
ATOM   3919  CA  ALA A 478     -23.071  10.866  -7.961  1.00 56.19           C
ANISOU 3919  CA  ALA A 478     6957   9879   4514     96   1350   -750       C
ATOM   3920  C   ALA A 478     -24.484  11.410  -8.126  1.00 65.57           C
ANISOU 3920  C   ALA A 478     8164  11169   5581     62   1212   -668       C
ATOM   3921  O   ALA A 478     -25.279  11.411  -7.176  1.00 70.51           O
ANISOU 3921  O   ALA A 478     8806  11630   6353      6   1084   -686       O
ATOM   3922  CB  ALA A 478     -22.067  12.013  -7.863  1.00 47.31           C
ANISOU 3922  CB  ALA A 478     5748   8715   3511    124   1466   -488       C
ATOM   3923  N   LEU A 479     -24.814  11.886  -9.333  1.00 65.62           N
ANISOU 3923  N   LEU A 479     8162  11457   5313    101   1238   -568       N
ATOM   3924  CA  LEU A 479     -26.156  12.411  -9.566  1.00 66.14           C
ANISOU 3924  CA  LEU A 479     8235  11646   5251     80   1106   -480       C
ATOM   3925  C   LEU A 479     -27.197  11.302  -9.551  1.00 68.01           C
ANISOU 3925  C   LEU A 479     8531  11912   5398     30    970   -753       C
ATOM   3926  O   LEU A 479     -28.319  11.515  -9.095  1.00 64.71           O
ANISOU 3926  O   LEU A 479     8116  11454   5017    -16    831   -729       O
ATOM   3927  CB  LEU A 479     -26.216  13.191 -10.880  1.00 69.58           C
ANISOU 3927  CB  LEU A 479     8640  12392   5404    145   1170   -290       C
ATOM   3928  CG  LEU A 479     -25.031  14.140 -11.071  1.00 76.08           C
ANISOU 3928  CG  LEU A 479     9401  13204   6303    195   1338    -39       C
ATOM   3929  CD1 LEU A 479     -24.985  14.690 -12.493  1.00 80.07           C
ANISOU 3929  CD1 LEU A 479     9882  14045   6496    272   1426    126       C
ATOM   3930  CD2 LEU A 479     -25.014  15.255 -10.017  1.00 74.40           C
ANISOU 3930  CD2 LEU A 479     9140  12744   6384    163   1315    192       C
ATOM   3931  N   ALA A 480     -26.843  10.112 -10.022  1.00 69.57           N
ANISOU 3931  N   ALA A 480     8772  12167   5494     37   1012  -1017       N
ATOM   3932  CA  ALA A 480     -27.713   8.959  -9.826  1.00 64.54           C
ANISOU 3932  CA  ALA A 480     8189  11490   4843    -26    892  -1299       C
ATOM   3933  C   ALA A 480     -28.026   8.758  -8.349  1.00 63.44           C
ANISOU 3933  C   ALA A 480     8058  11030   5017    -91    808  -1322       C
ATOM   3934  O   ALA A 480     -29.152   8.404  -7.982  1.00 68.59           O
ANISOU 3934  O   ALA A 480     8729  11644   5689   -155    671  -1416       O
ATOM   3935  CB  ALA A 480     -27.048   7.712 -10.414  1.00 60.45           C
ANISOU 3935  CB  ALA A 480     7715  11016   4237     -3    977  -1579       C
ATOM   3936  N   ALA A 481     -27.039   8.985  -7.487  1.00 58.88           N
ANISOU 3936  N   ALA A 481     7461  10231   4681    -75    887  -1233       N
ATOM   3937  CA  ALA A 481     -27.273   8.823  -6.059  1.00 57.80           C
ANISOU 3937  CA  ALA A 481     7330   9806   4826   -127    812  -1245       C
ATOM   3938  C   ALA A 481     -28.091   9.969  -5.476  1.00 62.71           C
ANISOU 3938  C   ALA A 481     7917  10389   5521   -152    717  -1024       C
ATOM   3939  O   ALA A 481     -28.875   9.753  -4.544  1.00 62.46           O
ANISOU 3939  O   ALA A 481     7900  10205   5629   -206    609  -1067       O
ATOM   3940  CB  ALA A 481     -25.944   8.706  -5.317  1.00 54.03           C
ANISOU 3940  CB  ALA A 481     6833   9124   4571    -96    919  -1225       C
ATOM   3941  N   ILE A 482     -27.927  11.181  -5.996  1.00 62.88           N
ANISOU 3941  N   ILE A 482     7893  10538   5461   -112    762   -783       N
ATOM   3942  CA  ILE A 482     -28.390  12.391  -5.311  1.00 55.60           C
ANISOU 3942  CA  ILE A 482     6930   9524   4671   -122    706   -551       C
ATOM   3943  C   ILE A 482     -29.708  12.916  -5.876  1.00 61.19           C
ANISOU 3943  C   ILE A 482     7630  10418   5203   -127    601   -463       C
ATOM   3944  O   ILE A 482     -30.628  13.231  -5.120  1.00 65.86           O
ANISOU 3944  O   ILE A 482     8214  10910   5901   -162    492   -418       O
ATOM   3945  CB  ILE A 482     -27.288  13.472  -5.353  1.00 52.01           C
ANISOU 3945  CB  ILE A 482     6420   9037   4305    -77    830   -321       C
ATOM   3946  CG1 ILE A 482     -26.209  13.149  -4.325  1.00 51.28           C
ANISOU 3946  CG1 ILE A 482     6318   8698   4468    -86    888   -380       C
ATOM   3947  CG2 ILE A 482     -27.869  14.845  -5.092  1.00 52.11           C
ANISOU 3947  CG2 ILE A 482     6391   9027   4382    -75    786    -66       C
ATOM   3948  CD1 ILE A 482     -25.266  14.291  -4.068  1.00 55.58           C
ANISOU 3948  CD1 ILE A 482     6794   9160   5164    -65    980   -159       C
ATOM   3949  N   TYR A 483     -29.815  13.028  -7.201  1.00 63.64           N
ANISOU 3949  N   TYR A 483     7934  11011   5236    -85    632   -432       N
ATOM   3950  CA  TYR A 483     -30.951  13.716  -7.812  1.00 63.67           C
ANISOU 3950  CA  TYR A 483     7913  11218   5062    -71    543   -297       C
ATOM   3951  C   TYR A 483     -32.299  13.109  -7.447  1.00 62.93           C
ANISOU 3951  C   TYR A 483     7835  11119   4957   -134    380   -452       C
ATOM   3952  O   TYR A 483     -33.183  13.861  -6.999  1.00 62.80           O
ANISOU 3952  O   TYR A 483     7786  11068   5008   -141    292   -306       O
ATOM   3953  CB  TYR A 483     -30.755  13.765  -9.331  1.00 68.64           C
ANISOU 3953  CB  TYR A 483     8536  12176   5369     -9    608   -267       C
ATOM   3954  CG  TYR A 483     -31.811  14.543 -10.082  1.00 74.97           C
ANISOU 3954  CG  TYR A 483     9301  13223   5960     25    527    -95       C
ATOM   3955  CD1 TYR A 483     -31.845  15.930 -10.034  1.00 79.93           C
ANISOU 3955  CD1 TYR A 483     9880  13839   6650     73    558    229       C
ATOM   3956  CD2 TYR A 483     -32.763  13.890 -10.856  1.00 74.72           C
ANISOU 3956  CD2 TYR A 483     9281  13438   5673     13    420   -257       C
ATOM   3957  CE1 TYR A 483     -32.803  16.646 -10.727  1.00 83.35           C
ANISOU 3957  CE1 TYR A 483    10275  14497   6895    118    488    403       C
ATOM   3958  CE2 TYR A 483     -33.723  14.597 -11.552  1.00 81.22           C
ANISOU 3958  CE2 TYR A 483    10061  14452   6346     53    335    -92       C
ATOM   3959  CZ  TYR A 483     -33.739  15.974 -11.484  1.00 87.28           C
ANISOU 3959  CZ  TYR A 483    10781  15237   7145    111    374    244       C
ATOM   3960  OH  TYR A 483     -34.696  16.681 -12.177  1.00 94.92           O
ANISOU 3960  OH  TYR A 483    11701  16356   8007    160    289    414       O
ATOM   3961  N   PRO A 484     -32.542  11.803  -7.609  1.00 61.25           N
ANISOU 3961  N   PRO A 484     7664  10934   4675   -180    335   -740       N
ATOM   3962  CA  PRO A 484     -33.859  11.276  -7.217  1.00 58.87           C
ANISOU 3962  CA  PRO A 484     7364  10615   4389   -251    182   -872       C
ATOM   3963  C   PRO A 484     -34.132  11.422  -5.731  1.00 58.88           C
ANISOU 3963  C   PRO A 484     7362  10319   4689   -295    134   -831       C
ATOM   3964  O   PRO A 484     -35.285  11.656  -5.331  1.00 58.51           O
ANISOU 3964  O   PRO A 484     7288  10268   4676   -328     17   -794       O
ATOM   3965  CB  PRO A 484     -33.789   9.805  -7.646  1.00 59.29           C
ANISOU 3965  CB  PRO A 484     7466  10712   4351   -295    177  -1199       C
ATOM   3966  CG  PRO A 484     -32.340   9.487  -7.658  1.00 61.73           C
ANISOU 3966  CG  PRO A 484     7806  10923   4725   -254    329  -1241       C
ATOM   3967  CD  PRO A 484     -31.667  10.736  -8.130  1.00 61.71           C
ANISOU 3967  CD  PRO A 484     7766  11027   4654   -174    425   -962       C
ATOM   3968  N   THR A 485     -33.091  11.312  -4.901  1.00 53.01           N
ANISOU 3968  N   THR A 485     6640   9341   4160   -290    222   -831       N
ATOM   3969  CA  THR A 485     -33.262  11.498  -3.465  1.00 53.76           C
ANISOU 3969  CA  THR A 485     6731   9169   4526   -321    183   -785       C
ATOM   3970  C   THR A 485     -33.755  12.907  -3.156  1.00 59.40           C
ANISOU 3970  C   THR A 485     7396   9879   5293   -292    148   -523       C
ATOM   3971  O   THR A 485     -34.744  13.089  -2.432  1.00 59.16           O
ANISOU 3971  O   THR A 485     7350   9774   5355   -323     50   -499       O
ATOM   3972  CB  THR A 485     -31.945  11.200  -2.746  1.00 49.86           C
ANISOU 3972  CB  THR A 485     6259   8462   4223   -307    286   -819       C
ATOM   3973  OG1 THR A 485     -31.605   9.820  -2.935  1.00 54.72           O
ANISOU 3973  OG1 THR A 485     6921   9055   4816   -331    312  -1071       O
ATOM   3974  CG2 THR A 485     -32.059  11.485  -1.254  1.00 43.81           C
ANISOU 3974  CG2 THR A 485     5485   7443   3718   -329    246   -759       C
ATOM   3975  N   TYR A 486     -33.089  13.921  -3.718  1.00 59.97           N
ANISOU 3975  N   TYR A 486     7441  10032   5314   -231    234   -322       N
ATOM   3976  CA  TYR A 486     -33.533  15.289  -3.484  1.00 54.41           C
ANISOU 3976  CA  TYR A 486     6690   9312   4673   -198    212    -68       C
ATOM   3977  C   TYR A 486     -34.904  15.547  -4.094  1.00 53.08           C
ANISOU 3977  C   TYR A 486     6493   9346   4328   -192    102    -16       C
ATOM   3978  O   TYR A 486     -35.668  16.348  -3.555  1.00 53.23           O
ANISOU 3978  O   TYR A 486     6478   9304   4443   -184     40    124       O
ATOM   3979  CB  TYR A 486     -32.519  16.298  -4.026  1.00 48.07           C
ANISOU 3979  CB  TYR A 486     5857   8547   3860   -137    339    144       C
ATOM   3980  CG  TYR A 486     -33.003  17.727  -3.896  1.00 46.92           C
ANISOU 3980  CG  TYR A 486     5664   8384   3781    -99    324    412       C
ATOM   3981  CD1 TYR A 486     -32.961  18.386  -2.674  1.00 47.07           C
ANISOU 3981  CD1 TYR A 486     5667   8152   4064   -113    312    488       C
ATOM   3982  CD2 TYR A 486     -33.531  18.406  -4.989  1.00 45.48           C
ANISOU 3982  CD2 TYR A 486     5449   8436   3394    -45    320    585       C
ATOM   3983  CE1 TYR A 486     -33.418  19.686  -2.545  1.00 43.80           C
ANISOU 3983  CE1 TYR A 486     5211   7703   3727    -75    303    720       C
ATOM   3984  CE2 TYR A 486     -33.990  19.705  -4.868  1.00 41.82           C
ANISOU 3984  CE2 TYR A 486     4941   7942   3008     -2    311    838       C
ATOM   3985  CZ  TYR A 486     -33.929  20.338  -3.645  1.00 42.83           C
ANISOU 3985  CZ  TYR A 486     5057   7799   3417    -19    306    899       C
ATOM   3986  OH  TYR A 486     -34.382  21.628  -3.522  1.00 48.73           O
ANISOU 3986  OH  TYR A 486     5761   8498   4256     27    304   1139       O
ATOM   3987  N   ILE A 487     -35.234  14.892  -5.209  1.00 55.93           N
ANISOU 3987  N   ILE A 487     6862   9956   4433   -193     75   -132       N
ATOM   3988  CA  ILE A 487     -36.565  15.055  -5.794  1.00 59.70           C
ANISOU 3988  CA  ILE A 487     7301  10647   4734   -191    -45   -101       C
ATOM   3989  C   ILE A 487     -37.632  14.583  -4.812  1.00 62.62           C
ANISOU 3989  C   ILE A 487     7664  10883   5244   -260   -168   -217       C
ATOM   3990  O   ILE A 487     -38.616  15.288  -4.542  1.00 61.75           O
ANISOU 3990  O   ILE A 487     7506  10791   5165   -247   -248    -82       O
ATOM   3991  CB  ILE A 487     -36.661  14.303  -7.134  1.00 62.48           C
ANISOU 3991  CB  ILE A 487     7665  11296   4780   -187    -58   -249       C
ATOM   3992  CG1 ILE A 487     -35.948  15.083  -8.241  1.00 62.02           C
ANISOU 3992  CG1 ILE A 487     7591  11440   4533    -98     47    -56       C
ATOM   3993  CG2 ILE A 487     -38.115  14.048  -7.502  1.00 65.49           C
ANISOU 3993  CG2 ILE A 487     8006  11865   5012   -217   -214   -319       C
ATOM   3994  CD1 ILE A 487     -36.449  16.501  -8.417  1.00 61.24           C
ANISOU 3994  CD1 ILE A 487     7434  11415   4420    -29     33    265       C
ATOM   3995  N   LEU A 488     -37.444  13.382  -4.258  1.00 60.20           N
ANISOU 3995  N   LEU A 488     7402  10438   5032   -330   -175   -461       N
ATOM   3996  CA  LEU A 488     -38.385  12.871  -3.265  1.00 48.86           C
ANISOU 3996  CA  LEU A 488     5960   8859   3747   -398   -274   -566       C
ATOM   3997  C   LEU A 488     -38.449  13.780  -2.043  1.00 46.95           C
ANISOU 3997  C   LEU A 488     5700   8399   3741   -378   -269   -393       C
ATOM   3998  O   LEU A 488     -39.532  14.021  -1.501  1.00 50.92           O
ANISOU 3998  O   LEU A 488     6164   8876   4307   -396   -359   -352       O
ATOM   3999  CB  LEU A 488     -37.999  11.453  -2.849  1.00 45.13           C
ANISOU 3999  CB  LEU A 488     5542   8246   3359   -467   -257   -832       C
ATOM   4000  CG  LEU A 488     -38.170  10.369  -3.910  1.00 53.56           C
ANISOU 4000  CG  LEU A 488     6628   9501   4223   -507   -283  -1064       C
ATOM   4001  CD1 LEU A 488     -37.633   9.043  -3.399  1.00 55.21           C
ANISOU 4001  CD1 LEU A 488     6895   9518   4564   -564   -242  -1305       C
ATOM   4002  CD2 LEU A 488     -39.629  10.245  -4.310  1.00 52.75           C
ANISOU 4002  CD2 LEU A 488     6470   9576   3996   -553   -424  -1113       C
ATOM   4003  N   ALA A 489     -37.300  14.290  -1.594  1.00 48.03           N
ANISOU 4003  N   ALA A 489     5859   8380   4012   -341   -164   -297       N
ATOM   4004  CA  ALA A 489     -37.285  15.138  -0.403  1.00 49.21           C
ANISOU 4004  CA  ALA A 489     5992   8316   4387   -324   -159   -159       C
ATOM   4005  C   ALA A 489     -38.005  16.462  -0.649  1.00 53.73           C
ANISOU 4005  C   ALA A 489     6509   8976   4931   -269   -192     76       C
ATOM   4006  O   ALA A 489     -38.781  16.924   0.199  1.00 54.66           O
ANISOU 4006  O   ALA A 489     6601   8992   5177   -269   -250    138       O
ATOM   4007  CB  ALA A 489     -35.843  15.383   0.046  1.00 41.58           C
ANISOU 4007  CB  ALA A 489     5051   7184   3563   -301    -44   -122       C
ATOM   4008  N   ASP A 490     -37.751  17.085  -1.802  1.00 51.58           N
ANISOU 4008  N   ASP A 490     6217   8892   4491   -214   -148    215       N
ATOM   4009  CA  ASP A 490     -38.422  18.326  -2.170  1.00 53.43           C
ANISOU 4009  CA  ASP A 490     6394   9222   4683   -149   -173    455       C
ATOM   4010  C   ASP A 490     -39.925  18.122  -2.281  1.00 53.55           C
ANISOU 4010  C   ASP A 490     6368   9374   4606   -163   -307    423       C
ATOM   4011  O   ASP A 490     -40.712  18.978  -1.857  1.00 48.03           O
ANISOU 4011  O   ASP A 490     5622   8636   3992   -127   -352    572       O
ATOM   4012  CB  ASP A 490     -37.852  18.842  -3.493  1.00 58.55           C
ANISOU 4012  CB  ASP A 490     7031  10077   5138    -87    -96    601       C
ATOM   4013  CG  ASP A 490     -37.706  20.348  -3.522  1.00 64.75           C
ANISOU 4013  CG  ASP A 490     7776  10813   6012    -12    -37    896       C
ATOM   4014  OD1 ASP A 490     -38.139  21.011  -2.555  1.00 62.63           O
ANISOU 4014  OD1 ASP A 490     7489  10362   5947     -6    -66    975       O
ATOM   4015  OD2 ASP A 490     -37.159  20.868  -4.520  1.00 69.79           O
ANISOU 4015  OD2 ASP A 490     8401  11594   6520     43     45   1050       O
ATOM   4016  N   ALA A 491     -40.344  16.990  -2.851  1.00 53.84           N
ANISOU 4016  N   ALA A 491     6412   9569   4474   -216   -371    222       N
ATOM   4017  CA  ALA A 491     -41.769  16.692  -2.927  1.00 47.64           C
ANISOU 4017  CA  ALA A 491     5575   8913   3613   -245   -505    166       C
ATOM   4018  C   ALA A 491     -42.367  16.513  -1.536  1.00 48.47           C
ANISOU 4018  C   ALA A 491     5673   8792   3951   -292   -553    109       C
ATOM   4019  O   ALA A 491     -43.377  17.141  -1.198  1.00 50.62           O
ANISOU 4019  O   ALA A 491     5886   9076   4271   -267   -620    222       O
ATOM   4020  CB  ALA A 491     -41.995  15.444  -3.780  1.00 42.11           C
ANISOU 4020  CB  ALA A 491     4886   8407   2708   -306   -560    -70       C
ATOM   4021  N   GLN A 492     -41.745  15.673  -0.708  1.00 46.39           N
ANISOU 4021  N   GLN A 492     5468   8325   3832   -351   -512    -58       N
ATOM   4022  CA  GLN A 492     -42.345  15.325   0.574  1.00 45.85           C
ANISOU 4022  CA  GLN A 492     5395   8069   3957   -399   -557   -130       C
ATOM   4023  C   GLN A 492     -42.339  16.495   1.551  1.00 52.47           C
ANISOU 4023  C   GLN A 492     6217   8737   4983   -342   -528     55       C
ATOM   4024  O   GLN A 492     -43.209  16.564   2.426  1.00 56.06           O
ANISOU 4024  O   GLN A 492     6640   9108   5550   -355   -582     58       O
ATOM   4025  CB  GLN A 492     -41.625  14.123   1.179  1.00 45.84           C
ANISOU 4025  CB  GLN A 492     5460   7901   4056   -466   -514   -338       C
ATOM   4026  CG  GLN A 492     -41.844  12.831   0.411  1.00 49.94           C
ANISOU 4026  CG  GLN A 492     5992   8549   4433   -537   -553   -560       C
ATOM   4027  CD  GLN A 492     -40.894  11.733   0.843  1.00 52.20           C
ANISOU 4027  CD  GLN A 492     6350   8667   4816   -580   -485   -741       C
ATOM   4028  OE1 GLN A 492     -40.470  11.682   1.998  1.00 53.34           O
ANISOU 4028  OE1 GLN A 492     6522   8588   5155   -581   -445   -731       O
ATOM   4029  NE2 GLN A 492     -40.550  10.850  -0.085  1.00 51.17           N
ANISOU 4029  NE2 GLN A 492     6248   8649   4544   -611   -471   -908       N
ATOM   4030  N   SER A 493     -41.389  17.421   1.429  1.00 52.28           N
ANISOU 4030  N   SER A 493     6209   8655   4998   -280   -441    204       N
ATOM   4031  CA  SER A 493     -41.318  18.528   2.374  1.00 51.46           C
ANISOU 4031  CA  SER A 493     6093   8372   5088   -231   -410    355       C
ATOM   4032  C   SER A 493     -42.225  19.698   1.999  1.00 54.98           C
ANISOU 4032  C   SER A 493     6471   8918   5500   -160   -448    564       C
ATOM   4033  O   SER A 493     -42.268  20.690   2.734  1.00 58.34           O
ANISOU 4033  O   SER A 493     6882   9196   6090   -113   -424    691       O
ATOM   4034  CB  SER A 493     -39.864  19.008   2.522  1.00 45.14           C
ANISOU 4034  CB  SER A 493     5332   7435   4386   -207   -298    412       C
ATOM   4035  OG  SER A 493     -39.359  19.599   1.336  1.00 42.00           O
ANISOU 4035  OG  SER A 493     4922   7181   3856   -160   -241    549       O
ATOM   4036  N   SER A 494     -42.960  19.606   0.891  1.00 53.00           N
ANISOU 4036  N   SER A 494     6177   8918   5043   -146   -509    598       N
ATOM   4037  CA  SER A 494     -43.872  20.671   0.489  1.00 57.42           C
ANISOU 4037  CA  SER A 494     6665   9592   5561    -68   -551    807       C
ATOM   4038  C   SER A 494     -45.182  20.664   1.268  1.00 55.15           C
ANISOU 4038  C   SER A 494     6321   9274   5359    -75   -642    787       C
ATOM   4039  O   SER A 494     -46.032  21.527   1.024  1.00 54.11           O
ANISOU 4039  O   SER A 494     6121   9230   5209     -4   -682    957       O
ATOM   4040  CB  SER A 494     -44.172  20.573  -1.010  1.00 61.21           C
ANISOU 4040  CB  SER A 494     7110  10380   5767    -42   -590    857       C
ATOM   4041  OG  SER A 494     -43.233  21.316  -1.769  1.00 68.88           O
ANISOU 4041  OG  SER A 494     8100  11394   6679     22   -493   1023       O
ATOM   4042  N   TYR A 495     -45.364  19.730   2.199  1.00 54.15           N
ANISOU 4042  N   TYR A 495     5654   8594   6329   -992    536   -625       N
ATOM   4043  CA  TYR A 495     -46.614  19.606   2.931  1.00 64.82           C
ANISOU 4043  CA  TYR A 495     7123   9719   7787   -919    494   -566       C
ATOM   4044  C   TYR A 495     -46.326  19.340   4.401  1.00 61.62           C
ANISOU 4044  C   TYR A 495     6716   9238   7459   -818    471   -606       C
ATOM   4045  O   TYR A 495     -45.287  18.780   4.754  1.00 70.77           O
ANISOU 4045  O   TYR A 495     7785  10510   8593   -753    482   -705       O
ATOM   4046  CB  TYR A 495     -47.489  18.487   2.352  1.00 77.42           C
ANISOU 4046  CB  TYR A 495     8760  11262   9393   -819    479   -597       C
ATOM   4047  CG  TYR A 495     -47.854  18.697   0.901  1.00 91.86           C
ANISOU 4047  CG  TYR A 495    10594  13166  11142   -910    496   -560       C
ATOM   4048  CD1 TYR A 495     -48.784  19.661   0.532  1.00 97.29           C
ANISOU 4048  CD1 TYR A 495    11367  13757  11842  -1013    483   -433       C
ATOM   4049  CD2 TYR A 495     -47.266  17.936  -0.103  1.00 98.90           C
ANISOU 4049  CD2 TYR A 495    11404  14230  11942   -887    523   -654       C
ATOM   4050  CE1 TYR A 495     -49.123  19.860  -0.794  1.00102.42           C
ANISOU 4050  CE1 TYR A 495    12023  14481  12413  -1095    494   -393       C
ATOM   4051  CE2 TYR A 495     -47.599  18.127  -1.434  1.00103.57           C
ANISOU 4051  CE2 TYR A 495    11997  14903  12450   -970    539   -621       C
ATOM   4052  CZ  TYR A 495     -48.528  19.091  -1.772  1.00106.17           C
ANISOU 4052  CZ  TYR A 495    12415  15133  12791  -1076    524   -486       C
ATOM   4053  OH  TYR A 495     -48.864  19.287  -3.092  1.00109.66           O
ANISOU 4053  OH  TYR A 495    12862  15660  13145  -1157    536   -448       O
ATOM   4054  N   ALA A 496     -47.260  19.753   5.254  1.00 53.68           N
ANISOU 4054  N   ALA A 496     5808   8046   6541   -803    439   -530       N
ATOM   4055  CA  ALA A 496     -47.167  19.534   6.691  1.00 47.81           C
ANISOU 4055  CA  ALA A 496     5077   7219   5871   -707    415   -554       C
ATOM   4056  C   ALA A 496     -48.542  19.149   7.214  1.00 50.10           C
ANISOU 4056  C   ALA A 496     5474   7317   6246   -627    382   -502       C
ATOM   4057  O   ALA A 496     -49.533  19.813   6.900  1.00 53.52           O
ANISOU 4057  O   ALA A 496     5982   7650   6701   -691    371   -412       O
ATOM   4058  CB  ALA A 496     -46.647  20.783   7.412  1.00 40.06           C
ANISOU 4058  CB  ALA A 496     4086   6236   4900   -802    413   -515       C
ATOM   4059  N   GLY A 497     -48.602  18.081   8.004  1.00 47.37           N
ANISOU 4059  N   GLY A 497     5132   6922   5944   -488    363   -556       N
ATOM   4060  CA  GLY A 497     -49.858  17.565   8.505  1.00 40.45           C
ANISOU 4060  CA  GLY A 497     4346   5880   5142   -410    335   -512       C
ATOM   4061  C   GLY A 497     -50.386  18.348   9.690  1.00 41.34           C
ANISOU 4061  C   GLY A 497     4517   5874   5318   -417    316   -446       C
ATOM   4062  O   GLY A 497     -50.037  19.509   9.917  1.00 45.45           O
ANISOU 4062  O   GLY A 497     5029   6411   5830   -506    321   -414       O
ATOM   4063  N   GLY A 498     -51.239  17.686  10.465  1.00 38.90           N
ANISOU 4063  N   GLY A 498     4266   5444   5072   -322    293   -427       N
ATOM   4064  CA  GLY A 498     -51.929  18.332  11.557  1.00 40.45           C
ANISOU 4064  CA  GLY A 498     4519   5526   5324   -317    275   -366       C
ATOM   4065  C   GLY A 498     -53.415  18.444  11.280  1.00 39.37           C
ANISOU 4065  C   GLY A 498     4463   5267   5231   -331    263   -288       C
ATOM   4066  O   GLY A 498     -53.908  17.985  10.244  1.00 34.68           O
ANISOU 4066  O   GLY A 498     3882   4673   4623   -344    266   -282       O
ATOM   4067  N   PRO A 499     -54.159  19.056  12.199  1.00 37.77           N
ANISOU 4067  N   PRO A 499     4310   4964   5076   -324    248   -234       N
ATOM   4068  CA  PRO A 499     -55.612  19.151  12.021  1.00 35.23           C
ANISOU 4068  CA  PRO A 499     4057   4533   4797   -327    235   -164       C
ATOM   4069  C   PRO A 499     -55.988  20.101  10.897  1.00 37.42           C
ANISOU 4069  C   PRO A 499     4355   4811   5054   -433    236   -113       C
ATOM   4070  O   PRO A 499     -55.289  21.078  10.613  1.00 41.26           O
ANISOU 4070  O   PRO A 499     4822   5348   5509   -517    241   -108       O
ATOM   4071  CB  PRO A 499     -56.102  19.675  13.376  1.00 33.43           C
ANISOU 4071  CB  PRO A 499     3862   4225   4615   -292    221   -133       C
ATOM   4072  CG  PRO A 499     -54.934  20.408  13.939  1.00 38.58           C
ANISOU 4072  CG  PRO A 499     4473   4941   5245   -320    224   -170       C
ATOM   4073  CD  PRO A 499     -53.711  19.667  13.463  1.00 39.97           C
ANISOU 4073  CD  PRO A 499     4581   5235   5372   -308    241   -241       C
ATOM   4074  N   ASN A 500     -57.110  19.796  10.248  1.00 36.54           N
ANISOU 4074  N   ASN A 500     4284   4641   4958   -432    226    -72       N
ATOM   4075  CA  ASN A 500     -57.655  20.698   9.246  1.00 36.02           C
ANISOU 4075  CA  ASN A 500     4247   4562   4876   -522    218    -12       C
ATOM   4076  C   ASN A 500     -58.455  21.811   9.923  1.00 32.91           C
ANISOU 4076  C   ASN A 500     3906   4067   4531   -536    195     51       C
ATOM   4077  O   ASN A 500     -58.671  21.809  11.139  1.00 26.85           O
ANISOU 4077  O   ASN A 500     3149   3247   3807   -475    189     45       O
ATOM   4078  CB  ASN A 500     -58.516  19.936   8.235  1.00 32.75           C
ANISOU 4078  CB  ASN A 500     3850   4137   4455   -514    213     -0       C
ATOM   4079  CG  ASN A 500     -59.653  19.157   8.883  1.00 42.84           C
ANISOU 4079  CG  ASN A 500     5162   5321   5794   -431    199     14       C
ATOM   4080  OD1 ASN A 500     -60.101  19.471   9.987  1.00 46.66           O
ANISOU 4080  OD1 ASN A 500     5669   5736   6325   -394    190     38       O
ATOM   4081  ND2 ASN A 500     -60.136  18.137   8.183  1.00 41.42           N
ANISOU 4081  ND2 ASN A 500     4983   5143   5610   -408    195     -3       N
ATOM   4082  N   LYS A 501     -58.900  22.778   9.115  1.00 37.68           N
ANISOU 4082  N   LYS A 501     4543   4647   5126   -616    180    111       N
ATOM   4083  CA  LYS A 501     -59.608  23.920   9.683  1.00 39.33           C
ANISOU 4083  CA  LYS A 501     4804   4758   5383   -627    151    164       C
ATOM   4084  C   LYS A 501     -60.925  23.506  10.324  1.00 38.12           C
ANISOU 4084  C   LYS A 501     4681   4519   5285   -542    137    183       C
ATOM   4085  O   LYS A 501     -61.350  24.121  11.304  1.00 45.69           O
ANISOU 4085  O   LYS A 501     5664   5411   6287   -508    121    195       O
ATOM   4086  CB  LYS A 501     -59.847  24.991   8.616  1.00 35.19           C
ANISOU 4086  CB  LYS A 501     4316   4218   4837   -724    130    231       C
ATOM   4087  CG  LYS A 501     -60.091  26.379   9.196  1.00 35.99           C
ANISOU 4087  CG  LYS A 501     4465   4228   4980   -752     97    272       C
ATOM   4088  CD  LYS A 501     -60.059  27.453   8.117  1.00 44.44           C
ANISOU 4088  CD  LYS A 501     5573   5287   6024   -862     73    341       C
ATOM   4089  CE  LYS A 501     -60.048  28.853   8.722  1.00 50.30           C
ANISOU 4089  CE  LYS A 501     6365   5936   6810   -897     35    371       C
ATOM   4090  NZ  LYS A 501     -61.286  29.138   9.501  1.00 53.66           N
ANISOU 4090  NZ  LYS A 501     6835   6248   7305   -808      2    383       N
ATOM   4091  N   GLN A 502     -61.574  22.466   9.803  1.00 38.59           N
ANISOU 4091  N   GLN A 502     4736   4585   5343   -507    142    182       N
ATOM   4092  CA  GLN A 502     -62.837  22.023  10.385  1.00 36.88           C
ANISOU 4092  CA  GLN A 502     4540   4296   5175   -438    130    203       C
ATOM   4093  C   GLN A 502     -62.625  21.439  11.777  1.00 40.87           C
ANISOU 4093  C   GLN A 502     5029   4792   5708   -360    144    167       C
ATOM   4094  O   GLN A 502     -63.348  21.778  12.722  1.00 46.40           O
ANISOU 4094  O   GLN A 502     5747   5437   6447   -317    135    186       O
ATOM   4095  CB  GLN A 502     -63.508  21.005   9.465  1.00 31.00           C
ANISOU 4095  CB  GLN A 502     3792   3564   4422   -431    130    206       C
ATOM   4096  CG  GLN A 502     -63.869  21.554   8.094  1.00 26.18           C
ANISOU 4096  CG  GLN A 502     3199   2967   3779   -502    113    248       C
ATOM   4097  CD  GLN A 502     -62.904  21.104   7.016  1.00 31.99           C
ANISOU 4097  CD  GLN A 502     3905   3799   4449   -551    131    212       C
ATOM   4098  OE1 GLN A 502     -61.684  21.180   7.182  1.00 41.10           O
ANISOU 4098  OE1 GLN A 502     5029   5014   5573   -570    152    173       O
ATOM   4099  NE2 GLN A 502     -63.446  20.620   5.905  1.00 29.45           N
ANISOU 4099  NE2 GLN A 502     3586   3502   4103   -570    122    220       N
ATOM   4100  N   TRP A 503     -61.628  20.563  11.923  1.00 39.61           N
ANISOU 4100  N   TRP A 503     4835   4693   5524   -337    165    113       N
ATOM   4101  CA  TRP A 503     -61.302  20.007  13.232  1.00 38.62           C
ANISOU 4101  CA  TRP A 503     4695   4565   5416   -263    174     82       C
ATOM   4102  C   TRP A 503     -60.897  21.103  14.213  1.00 35.72           C
ANISOU 4102  C   TRP A 503     4330   4188   5056   -266    169     78       C
ATOM   4103  O   TRP A 503     -61.355  21.127  15.362  1.00 33.07           O
ANISOU 4103  O   TRP A 503     4002   3815   4747   -209    166     84       O
ATOM   4104  CB  TRP A 503     -60.181  18.979  13.090  1.00 37.28           C
ANISOU 4104  CB  TRP A 503     4487   4465   5215   -238    189     21       C
ATOM   4105  CG  TRP A 503     -60.640  17.566  13.087  1.00 30.76           C
ANISOU 4105  CG  TRP A 503     3665   3617   4406   -179    189     11       C
ATOM   4106  CD1 TRP A 503     -60.672  16.715  12.019  1.00 31.91           C
ANISOU 4106  CD1 TRP A 503     3806   3783   4537   -187    188    -10       C
ATOM   4107  CD2 TRP A 503     -61.127  16.823  14.209  1.00 31.01           C
ANISOU 4107  CD2 TRP A 503     3710   3600   4471   -106    186     23       C
ATOM   4108  NE1 TRP A 503     -61.151  15.485  12.409  1.00 25.28           N
ANISOU 4108  NE1 TRP A 503     2980   2898   3729   -125    181    -14       N
ATOM   4109  CE2 TRP A 503     -61.438  15.526  13.748  1.00 26.17           C
ANISOU 4109  CE2 TRP A 503     3104   2968   3870    -78    181     13       C
ATOM   4110  CE3 TRP A 503     -61.334  17.129  15.559  1.00 26.62           C
ANISOU 4110  CE3 TRP A 503     3161   3018   3934    -64    186     43       C
ATOM   4111  CZ2 TRP A 503     -61.941  14.535  14.589  1.00 25.77           C
ANISOU 4111  CZ2 TRP A 503     3072   2867   3852    -17    174     30       C
ATOM   4112  CZ3 TRP A 503     -61.835  16.147  16.391  1.00 28.17           C
ANISOU 4112  CZ3 TRP A 503     3371   3179   4155     -1    184     60       C
ATOM   4113  CH2 TRP A 503     -62.131  14.863  15.903  1.00 30.16           C
ANISOU 4113  CH2 TRP A 503     3633   3405   4420     18    178     58       C
ATOM   4114  N   TYR A 504     -60.033  22.021  13.773  1.00 33.74           N
ANISOU 4114  N   TYR A 504     4068   3972   4778   -336    167     67       N
ATOM   4115  CA  TYR A 504     -59.567  23.083  14.659  1.00 36.14           C
ANISOU 4115  CA  TYR A 504     4375   4264   5092   -347    157     56       C
ATOM   4116  C   TYR A 504     -60.719  23.985  15.089  1.00 33.45           C
ANISOU 4116  C   TYR A 504     4081   3834   4795   -336    133     99       C
ATOM   4117  O   TYR A 504     -60.867  24.306  16.276  1.00 30.40           O
ANISOU 4117  O   TYR A 504     3698   3422   4429   -286    126     83       O
ATOM   4118  CB  TYR A 504     -58.466  23.892  13.970  1.00 41.13           C
ANISOU 4118  CB  TYR A 504     4989   4949   5688   -443    158     43       C
ATOM   4119  CG  TYR A 504     -57.777  24.884  14.880  1.00 42.83           C
ANISOU 4119  CG  TYR A 504     5201   5161   5912   -462    146     18       C
ATOM   4120  CD1 TYR A 504     -56.703  24.502  15.671  1.00 40.87           C
ANISOU 4120  CD1 TYR A 504     4904   4983   5643   -431    159    -44       C
ATOM   4121  CD2 TYR A 504     -58.207  26.204  14.953  1.00 45.72           C
ANISOU 4121  CD2 TYR A 504     5613   5451   6308   -508    117     52       C
ATOM   4122  CE1 TYR A 504     -56.074  25.408  16.511  1.00 47.61           C
ANISOU 4122  CE1 TYR A 504     5751   5837   6503   -451    145    -73       C
ATOM   4123  CE2 TYR A 504     -57.586  27.114  15.787  1.00 48.20           C
ANISOU 4123  CE2 TYR A 504     5927   5755   6633   -528    101     21       C
ATOM   4124  CZ  TYR A 504     -56.519  26.713  16.563  1.00 52.25           C
ANISOU 4124  CZ  TYR A 504     6387   6344   7123   -503    116    -43       C
ATOM   4125  OH  TYR A 504     -55.898  27.623  17.394  1.00 55.55           O
ANISOU 4125  OH  TYR A 504     6801   6755   7550   -526     97    -79       O
ATOM   4126  N   ASP A 505     -61.547  24.405  14.131  1.00 36.20           N
ANISOU 4126  N   ASP A 505     4462   4140   5153   -377    116    149       N
ATOM   4127  CA  ASP A 505     -62.688  25.255  14.451  1.00 34.15           C
ANISOU 4127  CA  ASP A 505     4244   3797   4936   -357     88    186       C
ATOM   4128  C   ASP A 505     -63.652  24.550  15.398  1.00 34.37           C
ANISOU 4128  C   ASP A 505     4264   3804   4990   -264     96    185       C
ATOM   4129  O   ASP A 505     -64.110  25.143  16.383  1.00 31.29           O
ANISOU 4129  O   ASP A 505     3885   3378   4626   -219     83    178       O
ATOM   4130  CB  ASP A 505     -63.397  25.680  13.164  1.00 35.35           C
ANISOU 4130  CB  ASP A 505     4427   3916   5087   -411     66    243       C
ATOM   4131  CG  ASP A 505     -62.618  26.738  12.391  1.00 47.11           C
ANISOU 4131  CG  ASP A 505     5937   5408   6556   -509     49    261       C
ATOM   4132  OD1 ASP A 505     -61.767  27.417  13.006  1.00 50.60           O
ANISOU 4132  OD1 ASP A 505     6376   5850   6999   -533     46    233       O
ATOM   4133  OD2 ASP A 505     -62.857  26.895  11.173  1.00 50.48           O
ANISOU 4133  OD2 ASP A 505     6381   5838   6961   -567     38    306       O
ATOM   4134  N   ALA A 506     -63.954  23.275  15.132  1.00 29.53           N
ANISOU 4134  N   ALA A 506     3634   3219   4369   -238    116    188       N
ATOM   4135  CA  ALA A 506     -64.851  22.530  16.007  1.00 32.22           C
ANISOU 4135  CA  ALA A 506     3966   3545   4731   -164    125    196       C
ATOM   4136  C   ALA A 506     -64.289  22.425  17.418  1.00 41.13           C
ANISOU 4136  C   ALA A 506     5078   4695   5855   -109    137    160       C
ATOM   4137  O   ALA A 506     -65.030  22.564  18.399  1.00 34.13           O
ANISOU 4137  O   ALA A 506     4191   3791   4984    -56    137    167       O
ATOM   4138  CB  ALA A 506     -65.107  21.137  15.429  1.00 30.92           C
ANISOU 4138  CB  ALA A 506     3789   3398   4560   -157    140    204       C
ATOM   4139  N   LEU A 507     -62.977  22.192  17.545  1.00 43.29           N
ANISOU 4139  N   LEU A 507     5331   5017   6100   -120    148    119       N
ATOM   4140  CA  LEU A 507     -62.399  21.990  18.870  1.00 35.42           C
ANISOU 4140  CA  LEU A 507     4315   4051   5093    -63    156     84       C
ATOM   4141  C   LEU A 507     -62.333  23.297  19.652  1.00 33.99           C
ANISOU 4141  C   LEU A 507     4144   3852   4921    -62    139     64       C
ATOM   4142  O   LEU A 507     -62.631  23.323  20.854  1.00 38.16           O
ANISOU 4142  O   LEU A 507     4666   4383   5449     -1    141     53       O
ATOM   4143  CB  LEU A 507     -61.019  21.346  18.746  1.00 36.24           C
ANISOU 4143  CB  LEU A 507     4388   4219   5164    -69    167     40       C
ATOM   4144  CG  LEU A 507     -61.052  19.870  18.332  1.00 35.66           C
ANISOU 4144  CG  LEU A 507     4305   4159   5084    -40    180     45       C
ATOM   4145  CD1 LEU A 507     -59.661  19.298  18.222  1.00 32.67           C
ANISOU 4145  CD1 LEU A 507     3892   3848   4673    -32    186     -8       C
ATOM   4146  CD2 LEU A 507     -61.877  19.051  19.311  1.00 37.34           C
ANISOU 4146  CD2 LEU A 507     4529   4347   5313     30    184     74       C
ATOM   4147  N   THR A 508     -61.961  24.396  18.990  1.00 31.01           N
ANISOU 4147  N   THR A 508     3782   3453   4548   -131    120     61       N
ATOM   4148  CA  THR A 508     -62.010  25.694  19.660  1.00 41.97           C
ANISOU 4148  CA  THR A 508     5190   4803   5955   -131     95     41       C
ATOM   4149  C   THR A 508     -63.438  26.045  20.064  1.00 37.74           C
ANISOU 4149  C   THR A 508     4676   4212   5451    -79     82     67       C
ATOM   4150  O   THR A 508     -63.670  26.578  21.160  1.00 43.94           O
ANISOU 4150  O   THR A 508     5462   4988   6243    -28     72     37       O
ATOM   4151  CB  THR A 508     -61.417  26.788  18.768  1.00 44.83           C
ANISOU 4151  CB  THR A 508     5574   5139   6321   -226     72     45       C
ATOM   4152  OG1 THR A 508     -62.018  26.734  17.469  1.00 50.46           O
ANISOU 4152  OG1 THR A 508     6309   5824   7040   -271     67     99       O
ATOM   4153  CG2 THR A 508     -59.907  26.610  18.631  1.00 41.71           C
ANISOU 4153  CG2 THR A 508     5142   4816   5889   -276     85      6       C
ATOM   4154  N   TRP A 509     -64.414  25.731  19.205  1.00 32.57           N
ANISOU 4154  N   TRP A 509     4035   3530   4811    -87     81    116       N
ATOM   4155  CA  TRP A 509     -65.811  25.936  19.572  1.00 26.68           C
ANISOU 4155  CA  TRP A 509     3297   2748   4092    -33     72    138       C
ATOM   4156  C   TRP A 509     -66.167  25.139  20.819  1.00 39.63           C
ANISOU 4156  C   TRP A 509     4906   4433   5719     44     98    125       C
ATOM   4157  O   TRP A 509     -66.782  25.671  21.748  1.00 43.21           O
ANISOU 4157  O   TRP A 509     5357   4882   6181     99     91    108       O
ATOM   4158  CB  TRP A 509     -66.733  25.557  18.412  1.00 27.70           C
ANISOU 4158  CB  TRP A 509     3435   2855   4233    -57     68    191       C
ATOM   4159  CG  TRP A 509     -68.196  25.792  18.723  1.00 37.15           C
ANISOU 4159  CG  TRP A 509     4631   4026   5457     -2     56    212       C
ATOM   4160  CD1 TRP A 509     -68.922  26.924  18.461  1.00 30.44           C
ANISOU 4160  CD1 TRP A 509     3808   3120   4638      5     17    221       C
ATOM   4161  CD2 TRP A 509     -69.097  24.882  19.368  1.00 32.69           C
ANISOU 4161  CD2 TRP A 509     4034   3496   4891     53     81    225       C
ATOM   4162  NE1 TRP A 509     -70.210  26.771  18.900  1.00 30.11           N
ANISOU 4162  NE1 TRP A 509     3744   3086   4611     68     19    232       N
ATOM   4163  CE2 TRP A 509     -70.347  25.526  19.457  1.00 36.53           C
ANISOU 4163  CE2 TRP A 509     4519   3958   5403     91     60    237       C
ATOM   4164  CE3 TRP A 509     -68.968  23.585  19.873  1.00 35.35           C
ANISOU 4164  CE3 TRP A 509     4343   3881   5207     71    117    230       C
ATOM   4165  CZ2 TRP A 509     -71.465  24.914  20.030  1.00 38.56           C
ANISOU 4165  CZ2 TRP A 509     4739   4251   5660    140     80    252       C
ATOM   4166  CZ3 TRP A 509     -70.078  22.978  20.442  1.00 42.50           C
ANISOU 4166  CZ3 TRP A 509     5222   4810   6115    114    134    254       C
ATOM   4167  CH2 TRP A 509     -71.311  23.644  20.515  1.00 39.94           C
ANISOU 4167  CH2 TRP A 509     4889   4475   5813    144    118    264       C
ATOM   4168  N   MET A 510     -65.794  23.855  20.850  1.00 24.92           N
ANISOU 4168  N   MET A 510     3021   2614   3833     50    127    134       N
ATOM   4169  CA  MET A 510     -66.059  23.030  22.026  1.00 24.86           C
ANISOU 4169  CA  MET A 510     2990   2648   3808    115    150    134       C
ATOM   4170  C   MET A 510     -65.454  23.651  23.278  1.00 41.50           C
ANISOU 4170  C   MET A 510     5089   4785   5895    155    147     85       C
ATOM   4171  O   MET A 510     -66.086  23.663  24.343  1.00 34.70           O
ANISOU 4171  O   MET A 510     4213   3947   5023    214    155     81       O
ATOM   4172  CB  MET A 510     -65.517  21.613  21.814  1.00 24.65           C
ANISOU 4172  CB  MET A 510     2952   2650   3762    111    171    148       C
ATOM   4173  CG  MET A 510     -65.455  20.773  23.092  1.00 47.06           C
ANISOU 4173  CG  MET A 510     5773   5532   6576    173    190    151       C
ATOM   4174  SD  MET A 510     -65.087  19.016  22.834  1.00 43.92           S
ANISOU 4174  SD  MET A 510     5375   5144   6170    178    204    178       S
ATOM   4175  CE  MET A 510     -66.722  18.366  22.500  1.00 41.98           C
ANISOU 4175  CE  MET A 510     5133   4865   5951    169    213    243       C
ATOM   4176  N   ARG A 511     -64.230  24.177  23.164  1.00 36.14           N
ANISOU 4176  N   ARG A 511     4413   4112   5207    121    134     43       N
ATOM   4177  CA  ARG A 511     -63.592  24.834  24.301  1.00 32.45           C
ANISOU 4177  CA  ARG A 511     3936   3673   4722    152    125    -13       C
ATOM   4178  C   ARG A 511     -64.392  26.043  24.761  1.00 37.83           C
ANISOU 4178  C   ARG A 511     4633   4314   5426    178    101    -34       C
ATOM   4179  O   ARG A 511     -64.449  26.344  25.961  1.00 30.34           O
ANISOU 4179  O   ARG A 511     3672   3397   4458    235    100    -73       O
ATOM   4180  CB  ARG A 511     -62.175  25.265  23.934  1.00 36.94           C
ANISOU 4180  CB  ARG A 511     4501   4253   5280     95    112    -53       C
ATOM   4181  CG  ARG A 511     -61.468  26.009  25.049  1.00 33.19           C
ANISOU 4181  CG  ARG A 511     4016   3807   4790    118     96   -118       C
ATOM   4182  CD  ARG A 511     -60.056  26.354  24.665  1.00 31.61           C
ANISOU 4182  CD  ARG A 511     3802   3630   4578     52     85   -156       C
ATOM   4183  NE  ARG A 511     -59.435  27.237  25.643  1.00 35.02           N
ANISOU 4183  NE  ARG A 511     4226   4078   5000     62     62   -223       N
ATOM   4184  CZ  ARG A 511     -58.176  27.657  25.566  1.00 36.19           C
ANISOU 4184  CZ  ARG A 511     4356   4258   5137      6     50   -268       C
ATOM   4185  NH1 ARG A 511     -57.411  27.263  24.558  1.00 30.28           N
ANISOU 4185  NH1 ARG A 511     3590   3535   4380    -59     62   -253       N
ATOM   4186  NH2 ARG A 511     -57.682  28.464  26.496  1.00 37.45           N
ANISOU 4186  NH2 ARG A 511     4509   4429   5291     14     25   -332       N
ATOM   4187  N   GLU A 512     -65.003  26.757  23.820  1.00 45.00           N
ANISOU 4187  N   GLU A 512     5572   5155   6373    141     79    -11       N
ATOM   4188  CA  GLU A 512     -65.696  27.993  24.158  1.00 45.97           C
ANISOU 4188  CA  GLU A 512     5716   5226   6525    169     46    -37       C
ATOM   4189  C   GLU A 512     -67.165  27.805  24.538  1.00 48.87           C
ANISOU 4189  C   GLU A 512     6069   5602   6900    238     55    -16       C
ATOM   4190  O   GLU A 512     -67.751  28.722  25.123  1.00 49.48           O
ANISOU 4190  O   GLU A 512     6151   5657   6991    287     31    -54       O
ATOM   4191  CB  GLU A 512     -65.595  28.978  22.991  1.00 51.96           C
ANISOU 4191  CB  GLU A 512     6519   5902   7322     99      7    -22       C
ATOM   4192  CG  GLU A 512     -65.398  30.416  23.426  1.00 68.74           C
ANISOU 4192  CG  GLU A 512     8677   7968   9475    101    -38    -75       C
ATOM   4193  CD  GLU A 512     -64.643  31.236  22.400  1.00 86.09           C
ANISOU 4193  CD  GLU A 512    10917  10100  11695      2    -72    -61       C
ATOM   4194  OE1 GLU A 512     -63.704  30.695  21.776  1.00 89.52           O
ANISOU 4194  OE1 GLU A 512    11338  10573  12105    -68    -50    -42       O
ATOM   4195  OE2 GLU A 512     -64.989  32.423  22.220  1.00 92.61           O
ANISOU 4195  OE2 GLU A 512    11788  10837  12562     -6   -121    -68       O
ATOM   4196  N   ASN A 513     -67.777  26.650  24.243  1.00 46.43           N
ANISOU 4196  N   ASN A 513     5738   5325   6580    242     86     38       N
ATOM   4197  CA  ASN A 513     -69.222  26.493  24.390  1.00 47.32           C
ANISOU 4197  CA  ASN A 513     5830   5447   6701    289     94     65       C
ATOM   4198  C   ASN A 513     -69.663  25.312  25.248  1.00 47.63           C
ANISOU 4198  C   ASN A 513     5828   5564   6704    329    137     89       C
ATOM   4199  O   ASN A 513     -70.874  25.103  25.400  1.00 47.79           O
ANISOU 4199  O   ASN A 513     5823   5608   6728    360    149    115       O
ATOM   4200  CB  ASN A 513     -69.894  26.369  23.013  1.00 42.74           C
ANISOU 4200  CB  ASN A 513     5266   4821   6154    243     82    118       C
ATOM   4201  CG  ASN A 513     -69.900  27.676  22.247  1.00 44.21           C
ANISOU 4201  CG  ASN A 513     5494   4926   6377    218     33    107       C
ATOM   4202  OD1 ASN A 513     -69.076  27.889  21.359  1.00 44.12           O
ANISOU 4202  OD1 ASN A 513     5514   4878   6372    148     18    119       O
ATOM   4203  ND2 ASN A 513     -70.830  28.561  22.590  1.00 42.53           N
ANISOU 4203  ND2 ASN A 513     5283   4689   6189    275      5     86       N
ATOM   4204  N   THR A 514     -68.738  24.532  25.800  1.00 37.89           N
ANISOU 4204  N   THR A 514     4587   4374   5435    327    159     86       N
ATOM   4205  CA  THR A 514     -69.118  23.514  26.765  1.00 33.50           C
ANISOU 4205  CA  THR A 514     3999   3890   4841    367    194    113       C
ATOM   4206  C   THR A 514     -68.839  24.004  28.182  1.00 34.74           C
ANISOU 4206  C   THR A 514     4138   4106   4956    429    197     61       C
ATOM   4207  O   THR A 514     -68.021  24.905  28.389  1.00 34.36           O
ANISOU 4207  O   THR A 514     4104   4041   4909    431    172      0       O
ATOM   4208  CB  THR A 514     -68.368  22.203  26.485  1.00 36.13           C
ANISOU 4208  CB  THR A 514     4337   4231   5159    336    212    151       C
ATOM   4209  OG1 THR A 514     -66.952  22.420  26.554  1.00 34.25           O
ANISOU 4209  OG1 THR A 514     4111   3994   4907    325    199    107       O
ATOM   4210  CG2 THR A 514     -68.729  21.692  25.102  1.00 28.77           C
ANISOU 4210  CG2 THR A 514     3421   3248   4264    279    208    194       C
ATOM   4211  N   PRO A 515     -69.531  23.464  29.183  1.00 34.91           N
ANISOU 4211  N   PRO A 515     4125   4200   4937    475    226     82       N
ATOM   4212  CA  PRO A 515     -69.420  24.024  30.535  1.00 32.72           C
ANISOU 4212  CA  PRO A 515     3827   3992   4614    539    228     27       C
ATOM   4213  C   PRO A 515     -68.040  23.848  31.156  1.00 37.42           C
ANISOU 4213  C   PRO A 515     4430   4616   5173    545    223     -5       C
ATOM   4214  O   PRO A 515     -67.273  22.951  30.799  1.00 36.16           O
ANISOU 4214  O   PRO A 515     4283   4446   5010    512    228     30       O
ATOM   4215  CB  PRO A 515     -70.489  23.258  31.330  1.00 32.28           C
ANISOU 4215  CB  PRO A 515     3730   4021   4516    572    267     76       C
ATOM   4216  CG  PRO A 515     -70.868  22.088  30.481  1.00 34.23           C
ANISOU 4216  CG  PRO A 515     3983   4237   4786    517    284    161       C
ATOM   4217  CD  PRO A 515     -70.658  22.523  29.070  1.00 34.73           C
ANISOU 4217  CD  PRO A 515     4079   4203   4913    467    255    153       C
ATOM   4218  N   ASP A 516     -67.730  24.764  32.081  1.00 43.19           N
ANISOU 4218  N   ASP A 516     5152   5382   5876    591    207    -81       N
ATOM   4219  CA  ASP A 516     -66.574  24.697  32.976  1.00 36.98           C
ANISOU 4219  CA  ASP A 516     4360   4650   5041    613    201   -123       C
ATOM   4220  C   ASP A 516     -65.252  24.969  32.260  1.00 39.47           C
ANISOU 4220  C   ASP A 516     4701   4910   5386    560    173   -154       C
ATOM   4221  O   ASP A 516     -64.190  24.554  32.733  1.00 46.01           O
ANISOU 4221  O   ASP A 516     5522   5782   6178    566    170   -169       O
ATOM   4222  CB  ASP A 516     -66.524  23.356  33.713  1.00 42.81           C
ANISOU 4222  CB  ASP A 516     5079   5467   5719    635    234    -59       C
ATOM   4223  CG  ASP A 516     -67.504  23.293  34.867  1.00 49.84           C
ANISOU 4223  CG  ASP A 516     5934   6452   6551    694    261    -51       C
ATOM   4224  OD1 ASP A 516     -67.637  24.303  35.587  1.00 52.64           O
ANISOU 4224  OD1 ASP A 516     6272   6845   6883    741    248   -129       O
ATOM   4225  OD2 ASP A 516     -68.148  22.241  35.052  1.00 55.46           O
ANISOU 4225  OD2 ASP A 516     6632   7201   7237    690    293     32       O
ATOM   4226  N   GLY A 517     -65.299  25.695  31.141  1.00 36.06           N
ANISOU 4226  N   GLY A 517     4297   4389   5017    509    150   -163       N
ATOM   4227  CA  GLY A 517     -64.086  25.982  30.393  1.00 36.02           C
ANISOU 4227  CA  GLY A 517     4310   4339   5035    447    127   -187       C
ATOM   4228  C   GLY A 517     -63.015  26.680  31.207  1.00 46.41           C
ANISOU 4228  C   GLY A 517     5619   5690   6326    458    102   -269       C
ATOM   4229  O   GLY A 517     -61.821  26.454  30.994  1.00 48.17           O
ANISOU 4229  O   GLY A 517     5836   5928   6540    421     95   -285       O
ATOM   4230  N   GLU A 518     -63.419  27.529  32.153  1.00 50.09           N
ANISOU 4230  N   GLU A 518     6079   6175   6778    511     87   -330       N
ATOM   4231  CA  GLU A 518     -62.437  28.219  32.983  1.00 49.53           C
ANISOU 4231  CA  GLU A 518     5999   6138   6681    522     60   -416       C
ATOM   4232  C   GLU A 518     -61.806  27.267  33.994  1.00 44.64           C
ANISOU 4232  C   GLU A 518     5345   5630   5988    567     80   -414       C
ATOM   4233  O   GLU A 518     -60.598  27.341  34.257  1.00 46.66           O
ANISOU 4233  O   GLU A 518     5588   5919   6223    551     62   -459       O
ATOM   4234  CB  GLU A 518     -63.088  29.416  33.681  1.00 57.06           C
ANISOU 4234  CB  GLU A 518     6961   7078   7643    572     33   -491       C
ATOM   4235  CG  GLU A 518     -64.079  29.064  34.783  1.00 69.24           C
ANISOU 4235  CG  GLU A 518     8471   8708   9130    663     60   -491       C
ATOM   4236  CD  GLU A 518     -65.414  28.551  34.257  1.00 77.80           C
ANISOU 4236  CD  GLU A 518     9553   9776  10233    674     91   -413       C
ATOM   4237  OE1 GLU A 518     -65.998  29.204  33.364  1.00 81.24           O
ANISOU 4237  OE1 GLU A 518    10016  10121  10732    649     71   -408       O
ATOM   4238  OE2 GLU A 518     -65.880  27.495  34.738  1.00 77.84           O
ANISOU 4238  OE2 GLU A 518     9528   9860  10187    704    132   -354       O
ATOM   4239  N   LYS A 519     -62.602  26.356  34.557  1.00 42.31           N
ANISOU 4239  N   LYS A 519     5032   5394   5650    621    114   -357       N
ATOM   4240  CA  LYS A 519     -62.040  25.343  35.440  1.00 43.31           C
ANISOU 4240  CA  LYS A 519     5133   5617   5706    661    130   -335       C
ATOM   4241  C   LYS A 519     -61.067  24.450  34.687  1.00 42.71           C
ANISOU 4241  C   LYS A 519     5062   5525   5643    618    131   -295       C
ATOM   4242  O   LYS A 519     -59.985  24.138  35.196  1.00 43.33           O
ANISOU 4242  O   LYS A 519     5121   5661   5680    633    119   -322       O
ATOM   4243  CB  LYS A 519     -63.155  24.512  36.072  1.00 43.32           C
ANISOU 4243  CB  LYS A 519     5121   5676   5664    711    168   -266       C
ATOM   4244  CG  LYS A 519     -64.091  25.314  36.954  1.00 43.56           C
ANISOU 4244  CG  LYS A 519     5133   5753   5665    767    172   -314       C
ATOM   4245  CD  LYS A 519     -64.551  24.510  38.161  1.00 48.32           C
ANISOU 4245  CD  LYS A 519     5705   6475   6179    826    204   -272       C
ATOM   4246  CE  LYS A 519     -66.068  24.546  38.311  1.00 52.77           C
ANISOU 4246  CE  LYS A 519     6250   7063   6737    850    235   -239       C
ATOM   4247  NZ  LYS A 519     -66.646  25.890  38.009  1.00 54.39           N
ANISOU 4247  NZ  LYS A 519     6458   7217   6993    862    213   -321       N
ATOM   4248  N   TYR A 520     -61.433  24.031  33.473  1.00 40.62           N
ANISOU 4248  N   TYR A 520     4818   5187   5430    568    144   -236       N
ATOM   4249  CA  TYR A 520     -60.521  23.225  32.669  1.00 40.90           C
ANISOU 4249  CA  TYR A 520     4855   5208   5479    530    143   -209       C
ATOM   4250  C   TYR A 520     -59.255  24.002  32.342  1.00 44.36           C
ANISOU 4250  C   TYR A 520     5282   5643   5928    485    114   -283       C
ATOM   4251  O   TYR A 520     -58.151  23.449  32.383  1.00 49.98           O
ANISOU 4251  O   TYR A 520     5973   6400   6616    487    107   -297       O
ATOM   4252  CB  TYR A 520     -61.211  22.752  31.387  1.00 36.97           C
ANISOU 4252  CB  TYR A 520     4381   4634   5033    483    159   -144       C
ATOM   4253  CG  TYR A 520     -62.152  21.591  31.614  1.00 44.10           C
ANISOU 4253  CG  TYR A 520     5287   5547   5922    514    187    -62       C
ATOM   4254  CD1 TYR A 520     -61.664  20.323  31.914  1.00 42.71           C
ANISOU 4254  CD1 TYR A 520     5109   5404   5715    542    193    -20       C
ATOM   4255  CD2 TYR A 520     -63.531  21.765  31.549  1.00 42.70           C
ANISOU 4255  CD2 TYR A 520     5115   5345   5762    516    203    -25       C
ATOM   4256  CE1 TYR A 520     -62.525  19.257  32.136  1.00 40.75           C
ANISOU 4256  CE1 TYR A 520     4870   5155   5457    560    214     61       C
ATOM   4257  CE2 TYR A 520     -64.397  20.707  31.770  1.00 42.36           C
ANISOU 4257  CE2 TYR A 520     5072   5317   5705    532    230     52       C
ATOM   4258  CZ  TYR A 520     -63.891  19.456  32.062  1.00 41.06           C
ANISOU 4258  CZ  TYR A 520     4912   5177   5513    549    235     98       C
ATOM   4259  OH  TYR A 520     -64.757  18.405  32.280  1.00 40.33           O
ANISOU 4259  OH  TYR A 520     4826   5088   5411    555    257    182       O
ATOM   4260  N   ASP A 521     -59.392  25.290  32.030  1.00 37.28           N
ANISOU 4260  N   ASP A 521     4401   4694   5070    444     94   -331       N
ATOM   4261  CA  ASP A 521     -58.221  26.104  31.733  1.00 34.59           C
ANISOU 4261  CA  ASP A 521     4052   4349   4743    387     65   -398       C
ATOM   4262  C   ASP A 521     -57.280  26.179  32.929  1.00 37.93           C
ANISOU 4262  C   ASP A 521     4439   4862   5110    429     47   -464       C
ATOM   4263  O   ASP A 521     -56.060  26.052  32.775  1.00 36.67           O
ANISOU 4263  O   ASP A 521     4252   4744   4937    399     35   -497       O
ATOM   4264  CB  ASP A 521     -58.662  27.496  31.295  1.00 32.02           C
ANISOU 4264  CB  ASP A 521     3758   3937   4469    338     40   -430       C
ATOM   4265  CG  ASP A 521     -58.985  27.553  29.821  1.00 45.50           C
ANISOU 4265  CG  ASP A 521     5495   5564   6231    266     45   -376       C
ATOM   4266  OD1 ASP A 521     -58.932  26.485  29.167  1.00 39.71           O
ANISOU 4266  OD1 ASP A 521     4754   4844   5492    257     70   -319       O
ATOM   4267  OD2 ASP A 521     -59.290  28.656  29.318  1.00 54.20           O
ANISOU 4267  OD2 ASP A 521     6629   6585   7378    220     19   -391       O
ATOM   4268  N   GLU A 522     -57.830  26.366  34.130  1.00 36.05           N
ANISOU 4268  N   GLU A 522     4197   4668   4833    500     46   -488       N
ATOM   4269  CA  GLU A 522     -56.998  26.390  35.330  1.00 37.21           C
ANISOU 4269  CA  GLU A 522     4309   4912   4918    547     28   -550       C
ATOM   4270  C   GLU A 522     -56.357  25.030  35.584  1.00 38.19           C
ANISOU 4270  C   GLU A 522     4407   5110   4992    587     41   -506       C
ATOM   4271  O   GLU A 522     -55.150  24.939  35.828  1.00 44.74           O
ANISOU 4271  O   GLU A 522     5203   6001   5794    585     21   -551       O
ATOM   4272  CB  GLU A 522     -57.825  26.829  36.540  1.00 50.06           C
ANISOU 4272  CB  GLU A 522     5936   6579   6505    619     27   -582       C
ATOM   4273  CG  GLU A 522     -57.049  26.850  37.854  1.00 63.87           C
ANISOU 4273  CG  GLU A 522     7649   8440   8178    675      7   -647       C
ATOM   4274  CD  GLU A 522     -57.896  27.306  39.035  1.00 80.32           C
ANISOU 4274  CD  GLU A 522     9728  10575  10214    748      8   -685       C
ATOM   4275  OE1 GLU A 522     -59.121  27.486  38.858  1.00 83.34           O
ANISOU 4275  OE1 GLU A 522    10131  10914  10620    761     29   -654       O
ATOM   4276  OE2 GLU A 522     -57.337  27.484  40.142  1.00 84.51           O
ANISOU 4276  OE2 GLU A 522    10232  11200  10680    794    -12   -750       O
ATOM   4277  N   TYR A 523     -57.152  23.957  35.526  1.00 40.43           N
ANISOU 4277  N   TYR A 523     4706   5390   5266    622     72   -417       N
ATOM   4278  CA  TYR A 523     -56.649  22.616  35.807  1.00 41.06           C
ANISOU 4278  CA  TYR A 523     4772   5524   5304    667     78   -366       C
ATOM   4279  C   TYR A 523     -55.647  22.143  34.759  1.00 40.63           C
ANISOU 4279  C   TYR A 523     4707   5450   5280    624     71   -367       C
ATOM   4280  O   TYR A 523     -54.877  21.214  35.024  1.00 39.54           O
ANISOU 4280  O   TYR A 523     4549   5365   5107    667     62   -356       O
ATOM   4281  CB  TYR A 523     -57.824  21.635  35.904  1.00 39.75           C
ANISOU 4281  CB  TYR A 523     4632   5341   5131    700    110   -267       C
ATOM   4282  CG  TYR A 523     -57.484  20.318  36.572  1.00 38.82           C
ANISOU 4282  CG  TYR A 523     4511   5282   4959    762    110   -210       C
ATOM   4283  CD1 TYR A 523     -56.835  20.287  37.799  1.00 40.01           C
ANISOU 4283  CD1 TYR A 523     4636   5532   5035    823     90   -243       C
ATOM   4284  CD2 TYR A 523     -57.811  19.105  35.975  1.00 30.59           C
ANISOU 4284  CD2 TYR A 523     3493   4190   3938    760    124   -123       C
ATOM   4285  CE1 TYR A 523     -56.520  19.089  38.412  1.00 38.70           C
ANISOU 4285  CE1 TYR A 523     4473   5414   4818    882     83   -183       C
ATOM   4286  CE2 TYR A 523     -57.496  17.899  36.580  1.00 30.19           C
ANISOU 4286  CE2 TYR A 523     3449   4178   3844    817    116    -66       C
ATOM   4287  CZ  TYR A 523     -56.853  17.900  37.800  1.00 34.83           C
ANISOU 4287  CZ  TYR A 523     4014   4863   4357    879     95    -92       C
ATOM   4288  OH  TYR A 523     -56.535  16.713  38.417  1.00 39.73           O
ANISOU 4288  OH  TYR A 523     4646   5518   4931    939     81    -29       O
ATOM   4289  N   TYR A 524     -55.645  22.769  33.583  1.00 40.69           N
ANISOU 4289  N   TYR A 524     4725   5387   5348    545     72   -381       N
ATOM   4290  CA  TYR A 524     -54.714  22.419  32.518  1.00 41.99           C
ANISOU 4290  CA  TYR A 524     4873   5546   5536    497     69   -389       C
ATOM   4291  C   TYR A 524     -53.274  22.763  32.882  1.00 43.86           C
ANISOU 4291  C   TYR A 524     5059   5863   5741    491     42   -470       C
ATOM   4292  O   TYR A 524     -52.339  22.148  32.358  1.00 40.52           O
ANISOU 4292  O   TYR A 524     4605   5478   5314    485     38   -480       O
ATOM   4293  CB  TYR A 524     -55.141  23.153  31.251  1.00 37.25           C
ANISOU 4293  CB  TYR A 524     4297   4858   4998    407     77   -381       C
ATOM   4294  CG  TYR A 524     -54.428  22.785  29.978  1.00 34.31           C
ANISOU 4294  CG  TYR A 524     3910   4478   4648    349     82   -378       C
ATOM   4295  CD1 TYR A 524     -54.870  21.726  29.203  1.00 32.34           C
ANISOU 4295  CD1 TYR A 524     3679   4195   4415    359    102   -316       C
ATOM   4296  CD2 TYR A 524     -53.349  23.532  29.518  1.00 31.11           C
ANISOU 4296  CD2 TYR A 524     3472   4101   4246    279     68   -438       C
ATOM   4297  CE1 TYR A 524     -54.241  21.394  28.024  1.00 31.43           C
ANISOU 4297  CE1 TYR A 524     3547   4081   4314    310    107   -321       C
ATOM   4298  CE2 TYR A 524     -52.715  23.208  28.330  1.00 31.48           C
ANISOU 4298  CE2 TYR A 524     3498   4157   4304    224     77   -437       C
ATOM   4299  CZ  TYR A 524     -53.172  22.134  27.591  1.00 28.02           C
ANISOU 4299  CZ  TYR A 524     3078   3691   3878    245     97   -381       C
ATOM   4300  OH  TYR A 524     -52.568  21.789  26.410  1.00 38.32           O
ANISOU 4300  OH  TYR A 524     4359   5013   5188    197    107   -387       O
ATOM   4301  N   LEU A 525     -53.076  23.740  33.764  1.00 36.82           N
ANISOU 4301  N   LEU A 525     4155   5006   4829    493     21   -534       N
ATOM   4302  CA  LEU A 525     -51.747  24.210  34.121  1.00 41.73           C
ANISOU 4302  CA  LEU A 525     4725   5705   5424    476     -9   -619       C
ATOM   4303  C   LEU A 525     -51.317  23.751  35.506  1.00 44.98           C
ANISOU 4303  C   LEU A 525     5108   6220   5764    569    -28   -644       C
ATOM   4304  O   LEU A 525     -50.257  24.169  35.983  1.00 46.69           O
ANISOU 4304  O   LEU A 525     5276   6513   5950    564    -57   -721       O
ATOM   4305  CB  LEU A 525     -51.692  25.736  34.034  1.00 42.97           C
ANISOU 4305  CB  LEU A 525     4889   5823   5614    397    -29   -685       C
ATOM   4306  CG  LEU A 525     -52.033  26.332  32.669  1.00 38.43           C
ANISOU 4306  CG  LEU A 525     4346   5148   5108    297    -18   -659       C
ATOM   4307  CD1 LEU A 525     -52.175  27.846  32.763  1.00 37.51           C
ANISOU 4307  CD1 LEU A 525     4253   4972   5026    233    -46   -715       C
ATOM   4308  CD2 LEU A 525     -50.974  25.950  31.647  1.00 29.78           C
ANISOU 4308  CD2 LEU A 525     3211   4087   4017    235    -12   -662       C
ATOM   4309  N   GLN A 526     -52.104  22.903  36.162  1.00 44.47           N
ANISOU 4309  N   GLN A 526     5069   6163   5667    650    -13   -578       N
ATOM   4310  CA  GLN A 526     -51.745  22.441  37.494  1.00 47.35           C
ANISOU 4310  CA  GLN A 526     5409   6627   5953    739    -32   -590       C
ATOM   4311  C   GLN A 526     -50.664  21.366  37.423  1.00 49.17           C
ANISOU 4311  C   GLN A 526     5605   6920   6156    782    -49   -582       C
ATOM   4312  O   GLN A 526     -50.572  20.605  36.456  1.00 48.46           O
ANISOU 4312  O   GLN A 526     5524   6786   6102    769    -36   -538       O
ATOM   4313  CB  GLN A 526     -52.977  21.913  38.234  1.00 39.49           C
ANISOU 4313  CB  GLN A 526     4453   5626   4927    802    -10   -513       C
ATOM   4314  CG  GLN A 526     -53.355  22.753  39.446  1.00 41.98           C
ANISOU 4314  CG  GLN A 526     4762   5997   5191    835    -20   -564       C
ATOM   4315  CD  GLN A 526     -54.744  22.449  39.976  1.00 54.06           C
ANISOU 4315  CD  GLN A 526     6324   7517   6698    875     12   -493       C
ATOM   4316  OE1 GLN A 526     -55.082  21.296  40.246  1.00 58.79           O
ANISOU 4316  OE1 GLN A 526     6939   8134   7265    921     27   -403       O
ATOM   4317  NE2 GLN A 526     -55.559  23.488  40.127  1.00 59.32           N
ANISOU 4317  NE2 GLN A 526     7002   8155   7381    858     19   -533       N
ATOM   4318  N   LEU A 527     -49.829  21.320  38.458  1.00 47.57           N
ANISOU 4318  N   LEU A 527     5362   6826   5888    840    -81   -631       N
ATOM   4319  CA  LEU A 527     -48.753  20.333  38.553  1.00 49.87           C
ANISOU 4319  CA  LEU A 527     5614   7188   6145    900   -107   -632       C
ATOM   4320  C   LEU A 527     -49.302  19.116  39.289  1.00 48.98           C
ANISOU 4320  C   LEU A 527     5539   7083   5986    996   -106   -537       C
ATOM   4321  O   LEU A 527     -49.332  19.079  40.521  1.00 54.94           O
ANISOU 4321  O   LEU A 527     6290   7914   6670   1060   -124   -536       O
ATOM   4322  CB  LEU A 527     -47.541  20.927  39.261  1.00 32.86           C
ANISOU 4322  CB  LEU A 527     3393   5151   3943    909   -148   -734       C
ATOM   4323  CG  LEU A 527     -46.240  20.121  39.234  1.00 41.06           C
ANISOU 4323  CG  LEU A 527     4372   6277   4951    963   -180   -761       C
ATOM   4324  CD1 LEU A 527     -45.552  20.203  37.870  1.00 38.27           C
ANISOU 4324  CD1 LEU A 527     3983   5903   4656    888   -170   -796       C
ATOM   4325  CD2 LEU A 527     -45.302  20.584  40.344  1.00 38.78           C
ANISOU 4325  CD2 LEU A 527     4023   6119   4593    999   -225   -847       C
ATOM   4326  N   TYR A 528     -49.737  18.115  38.532  1.00 46.61           N
ANISOU 4326  N   TYR A 528     5278   6706   5726   1004    -88   -456       N
ATOM   4327  CA  TYR A 528     -50.420  16.979  39.130  1.00 45.36           C
ANISOU 4327  CA  TYR A 528     5167   6531   5536   1076    -86   -351       C
ATOM   4328  C   TYR A 528     -49.433  16.094  39.885  1.00 45.50           C
ANISOU 4328  C   TYR A 528     5162   6633   5493   1174   -132   -348       C
ATOM   4329  O   TYR A 528     -48.316  15.866  39.415  1.00 48.53           O
ANISOU 4329  O   TYR A 528     5502   7049   5887   1189   -159   -403       O
ATOM   4330  CB  TYR A 528     -51.130  16.157  38.059  1.00 42.24           C
ANISOU 4330  CB  TYR A 528     4822   6021   5208   1051    -60   -272       C
ATOM   4331  CG  TYR A 528     -51.741  17.000  36.969  1.00 40.41           C
ANISOU 4331  CG  TYR A 528     4599   5711   5045    951    -25   -293       C
ATOM   4332  CD1 TYR A 528     -52.967  17.638  37.156  1.00 40.26           C
ANISOU 4332  CD1 TYR A 528     4610   5651   5036    914      5   -263       C
ATOM   4333  CD2 TYR A 528     -51.097  17.156  35.750  1.00 31.78           C
ANISOU 4333  CD2 TYR A 528     3482   4591   4004    898    -25   -341       C
ATOM   4334  CE1 TYR A 528     -53.528  18.414  36.155  1.00 37.89           C
ANISOU 4334  CE1 TYR A 528     4321   5276   4799    830     30   -279       C
ATOM   4335  CE2 TYR A 528     -51.649  17.924  34.745  1.00 35.04           C
ANISOU 4335  CE2 TYR A 528     3906   4933   4474    807      4   -351       C
ATOM   4336  CZ  TYR A 528     -52.861  18.552  34.950  1.00 37.40           C
ANISOU 4336  CZ  TYR A 528     4241   5183   4786    775     28   -319       C
ATOM   4337  OH  TYR A 528     -53.394  19.316  33.940  1.00 37.31           O
ANISOU 4337  OH  TYR A 528     4244   5099   4832    691     49   -326       O
ATOM   4338  N   PRO A 529     -49.816  15.576  41.047  1.00 47.88           N
ANISOU 4338  N   PRO A 529     5490   6977   5726   1244   -143   -283       N
ATOM   4339  CA  PRO A 529     -48.970  14.586  41.716  1.00 44.58           C
ANISOU 4339  CA  PRO A 529     5063   6623   5251   1344   -192   -259       C
ATOM   4340  C   PRO A 529     -48.922  13.297  40.917  1.00 41.49           C
ANISOU 4340  C   PRO A 529     4712   6142   4912   1374   -202   -191       C
ATOM   4341  O   PRO A 529     -49.846  12.961  40.173  1.00 53.31           O
ANISOU 4341  O   PRO A 529     6259   7529   6468   1327   -168   -128       O
ATOM   4342  CB  PRO A 529     -49.665  14.380  43.066  1.00 49.64           C
ANISOU 4342  CB  PRO A 529     5736   7317   5809   1393   -192   -185       C
ATOM   4343  CG  PRO A 529     -51.100  14.686  42.782  1.00 52.92           C
ANISOU 4343  CG  PRO A 529     6195   7652   6258   1324   -136   -129       C
ATOM   4344  CD  PRO A 529     -51.085  15.796  41.762  1.00 50.44           C
ANISOU 4344  CD  PRO A 529     5854   7294   6019   1235   -111   -220       C
ATOM   4345  N   THR A 530     -47.821  12.574  41.070  1.00 45.08           N
ANISOU 4345  N   THR A 530     5141   6645   5344   1457   -254   -211       N
ATOM   4346  CA  THR A 530     -47.658  11.293  40.403  1.00 41.73           C
ANISOU 4346  CA  THR A 530     4754   6137   4964   1505   -276   -158       C
ATOM   4347  C   THR A 530     -48.280  10.213  41.276  1.00 41.25           C
ANISOU 4347  C   THR A 530     4768   6041   4864   1572   -296    -27       C
ATOM   4348  O   THR A 530     -47.776   9.958  42.380  1.00 46.90           O
ANISOU 4348  O   THR A 530     5475   6844   5501   1653   -339    -11       O
ATOM   4349  CB  THR A 530     -46.187  11.005  40.151  1.00 38.59           C
ANISOU 4349  CB  THR A 530     4292   5810   4561   1573   -326   -246       C
ATOM   4350  OG1 THR A 530     -45.672  11.990  39.248  1.00 39.53           O
ANISOU 4350  OG1 THR A 530     4342   5959   4718   1492   -301   -357       O
ATOM   4351  CG2 THR A 530     -46.002   9.620  39.540  1.00 35.78           C
ANISOU 4351  CG2 THR A 530     3979   5367   4251   1642   -358   -198       C
ATOM   4352  N   PRO A 531     -49.365   9.579  40.852  1.00 43.70           N
ANISOU 4352  N   PRO A 531     5152   6231   5222   1536   -269     72       N
ATOM   4353  CA  PRO A 531     -50.012   8.568  41.688  1.00 46.80           C
ANISOU 4353  CA  PRO A 531     5618   6587   5576   1583   -287    208       C
ATOM   4354  C   PRO A 531     -49.300   7.227  41.608  1.00 52.82           C
ANISOU 4354  C   PRO A 531     6418   7300   6353   1681   -353    248       C
ATOM   4355  O   PRO A 531     -48.543   6.940  40.679  1.00 49.32           O
ANISOU 4355  O   PRO A 531     5951   6823   5966   1706   -375    177       O
ATOM   4356  CB  PRO A 531     -51.417   8.475  41.091  1.00 46.15           C
ANISOU 4356  CB  PRO A 531     5591   6392   5552   1491   -232    285       C
ATOM   4357  CG  PRO A 531     -51.200   8.785  39.639  1.00 45.63           C
ANISOU 4357  CG  PRO A 531     5500   6262   5575   1437   -213    201       C
ATOM   4358  CD  PRO A 531     -50.099   9.816  39.599  1.00 41.15           C
ANISOU 4358  CD  PRO A 531     4846   5804   4986   1442   -221     66       C
ATOM   4359  N   GLN A 532     -49.565   6.396  42.618  1.00 57.43           N
ANISOU 4359  N   GLN A 532     7059   7880   6880   1739   -385    364       N
ATOM   4360  CA  GLN A 532     -49.018   5.046  42.633  1.00 55.15           C
ANISOU 4360  CA  GLN A 532     6824   7524   6608   1838   -456    421       C
ATOM   4361  C   GLN A 532     -49.696   4.139  41.618  1.00 55.92           C
ANISOU 4361  C   GLN A 532     6995   7449   6803   1801   -450    482       C
ATOM   4362  O   GLN A 532     -49.105   3.134  41.209  1.00 56.86           O
ANISOU 4362  O   GLN A 532     7147   7492   6966   1878   -509    484       O
ATOM   4363  CB  GLN A 532     -49.148   4.440  44.029  1.00 57.69           C
ANISOU 4363  CB  GLN A 532     7194   7888   6837   1902   -495    541       C
ATOM   4364  CG  GLN A 532     -48.073   3.426  44.368  1.00 67.12           C
ANISOU 4364  CG  GLN A 532     8408   9080   8013   2038   -588    555       C
ATOM   4365  CD  GLN A 532     -47.586   3.568  45.793  1.00 75.94           C
ANISOU 4365  CD  GLN A 532     9506  10340   9008   2113   -627    582       C
ATOM   4366  OE1 GLN A 532     -47.980   4.494  46.502  1.00 76.52           O
ANISOU 4366  OE1 GLN A 532     9541  10524   9009   2063   -583    573       O
ATOM   4367  NE2 GLN A 532     -46.731   2.647  46.224  1.00 80.40           N
ANISOU 4367  NE2 GLN A 532    10096  10906   9548   2238   -714    613       N
ATOM   4368  N   SER A 533     -50.918   4.469  41.206  1.00 56.18           N
ANISOU 4368  N   SER A 533     7053   7421   6872   1690   -385    525       N
ATOM   4369  CA  SER A 533     -51.664   3.627  40.284  1.00 53.06           C
ANISOU 4369  CA  SER A 533     6728   6866   6567   1645   -379    586       C
ATOM   4370  C   SER A 533     -52.717   4.476  39.592  1.00 48.45           C
ANISOU 4370  C   SER A 533     6126   6261   6024   1520   -300    569       C
ATOM   4371  O   SER A 533     -53.057   5.571  40.047  1.00 51.69           O
ANISOU 4371  O   SER A 533     6489   6767   6386   1472   -253    542       O
ATOM   4372  CB  SER A 533     -52.317   2.444  41.010  1.00 52.61           C
ANISOU 4372  CB  SER A 533     6769   6725   6494   1664   -411    750       C
ATOM   4373  OG  SER A 533     -53.007   1.609  40.099  1.00 54.53           O
ANISOU 4373  OG  SER A 533     7081   6807   6830   1617   -411    802       O
ATOM   4374  N   ASN A 534     -53.231   3.951  38.475  1.00 45.03           N
ANISOU 4374  N   ASN A 534     5732   5698   5680   1472   -290    580       N
ATOM   4375  CA  ASN A 534     -54.320   4.611  37.766  1.00 45.04           C
ANISOU 4375  CA  ASN A 534     5724   5665   5723   1356   -222    577       C
ATOM   4376  C   ASN A 534     -55.414   3.629  37.356  1.00 46.68           C
ANISOU 4376  C   ASN A 534     6013   5733   5990   1302   -219    686       C
ATOM   4377  O   ASN A 534     -56.171   3.916  36.421  1.00 49.75           O
ANISOU 4377  O   ASN A 534     6399   6067   6438   1218   -178    669       O
ATOM   4378  CB  ASN A 534     -53.801   5.349  36.526  1.00 38.85           C
ANISOU 4378  CB  ASN A 534     4880   4890   4991   1326   -203    443       C
ATOM   4379  CG  ASN A 534     -53.270   4.402  35.470  1.00 40.83           C
ANISOU 4379  CG  ASN A 534     5157   5044   5314   1364   -243    408       C
ATOM   4380  OD1 ASN A 534     -52.912   3.259  35.768  1.00 36.87           O
ANISOU 4380  OD1 ASN A 534     4708   4483   4819   1443   -301    456       O
ATOM   4381  ND2 ASN A 534     -53.213   4.872  34.229  1.00 34.54           N
ANISOU 4381  ND2 ASN A 534     4325   4230   4570   1312   -216    321       N
ATOM   4382  N   LYS A 535     -55.519   2.479  38.024  1.00 44.88           N
ANISOU 4382  N   LYS A 535     5858   5444   5749   1346   -265    798       N
ATOM   4383  CA  LYS A 535     -56.525   1.501  37.629  1.00 52.48           C
ANISOU 4383  CA  LYS A 535     6901   6265   6774   1287   -267    902       C
ATOM   4384  C   LYS A 535     -57.922   1.889  38.101  1.00 52.66           C
ANISOU 4384  C   LYS A 535     6926   6314   6767   1183   -204    995       C
ATOM   4385  O   LYS A 535     -58.912   1.476  37.490  1.00 54.53           O
ANISOU 4385  O   LYS A 535     7200   6455   7064   1101   -184   1048       O
ATOM   4386  CB  LYS A 535     -56.143   0.118  38.151  1.00 48.96           C
ANISOU 4386  CB  LYS A 535     6540   5731   6331   1364   -345    995       C
ATOM   4387  CG  LYS A 535     -55.061  -0.553  37.322  1.00 61.20           C
ANISOU 4387  CG  LYS A 535     8104   7205   7945   1455   -411    906       C
ATOM   4388  CD  LYS A 535     -55.464  -0.645  35.850  1.00 72.07           C
ANISOU 4388  CD  LYS A 535     9483   8481   9420   1392   -390    841       C
ATOM   4389  CE  LYS A 535     -55.065  -1.986  35.242  1.00 76.23           C
ANISOU 4389  CE  LYS A 535    10085   8856  10024   1458   -467    842       C
ATOM   4390  NZ  LYS A 535     -55.158  -1.983  33.753  1.00 75.47           N
ANISOU 4390  NZ  LYS A 535     9973   8692  10009   1419   -453    742       N
ATOM   4391  N   GLU A 536     -58.025   2.667  39.160  1.00 52.48           N
ANISOU 4391  N   GLU A 536     6860   6426   6652   1186   -173   1010       N
ATOM   4392  CA  GLU A 536     -59.307   3.240  39.537  1.00 49.21           C
ANISOU 4392  CA  GLU A 536     6428   6064   6206   1094   -106   1068       C
ATOM   4393  C   GLU A 536     -59.426   4.658  38.993  1.00 50.14           C
ANISOU 4393  C   GLU A 536     6466   6255   6332   1055    -53    947       C
ATOM   4394  O   GLU A 536     -58.413   5.334  38.788  1.00 55.21           O
ANISOU 4394  O   GLU A 536     7059   6950   6968   1105    -66    832       O
ATOM   4395  CB  GLU A 536     -59.468   3.261  41.059  1.00 54.88           C
ANISOU 4395  CB  GLU A 536     7146   6894   6810   1118   -102   1157       C
ATOM   4396  CG  GLU A 536     -58.942   2.020  41.746  1.00 67.54           C
ANISOU 4396  CG  GLU A 536     8824   8450   8388   1186   -170   1260       C
ATOM   4397  CD  GLU A 536     -60.048   1.178  42.346  1.00 78.44           C
ANISOU 4397  CD  GLU A 536    10268   9790   9746   1118   -159   1432       C
ATOM   4398  OE1 GLU A 536     -61.214   1.336  41.927  1.00 80.33           O
ANISOU 4398  OE1 GLU A 536    10499  10003  10018   1015   -105   1464       O
ATOM   4399  OE2 GLU A 536     -59.748   0.354  43.235  1.00 86.53           O
ANISOU 4399  OE2 GLU A 536    11350  10811  10717   1166   -207   1537       O
ATOM   4400  N   PRO A 537     -60.645   5.133  38.739  1.00 42.21           N
ANISOU 4400  N   PRO A 537     5444   5252   5343    965      5    971       N
ATOM   4401  CA  PRO A 537     -60.804   6.477  38.169  1.00 43.32           C
ANISOU 4401  CA  PRO A 537     5517   5444   5498    930     48    861       C
ATOM   4402  C   PRO A 537     -60.173   7.546  39.050  1.00 44.36           C
ANISOU 4402  C   PRO A 537     5590   5714   5549    980     55    787       C
ATOM   4403  O   PRO A 537     -60.241   7.486  40.279  1.00 48.71           O
ANISOU 4403  O   PRO A 537     6140   6353   6013   1012     55    842       O
ATOM   4404  CB  PRO A 537     -62.326   6.646  38.080  1.00 42.22           C
ANISOU 4404  CB  PRO A 537     5373   5298   5370    839    102    925       C
ATOM   4405  CG  PRO A 537     -62.850   5.255  37.984  1.00 37.17           C
ANISOU 4405  CG  PRO A 537     4805   4554   4766    807     82   1046       C
ATOM   4406  CD  PRO A 537     -61.932   4.422  38.842  1.00 41.54           C
ANISOU 4406  CD  PRO A 537     5402   5111   5271    888     27   1098       C
ATOM   4407  N   PHE A 538     -59.553   8.529  38.399  1.00 41.38           N
ANISOU 4407  N   PHE A 538     5166   5358   5199    983     59    662       N
ATOM   4408  CA  PHE A 538     -58.872   9.608  39.101  1.00 43.50           C
ANISOU 4408  CA  PHE A 538     5379   5747   5404   1024     59    575       C
ATOM   4409  C   PHE A 538     -59.860  10.455  39.896  1.00 45.44           C
ANISOU 4409  C   PHE A 538     5595   6079   5592    995    105    589       C
ATOM   4410  O   PHE A 538     -61.013  10.648  39.499  1.00 50.40           O
ANISOU 4410  O   PHE A 538     6224   6674   6252    930    146    620       O
ATOM   4411  CB  PHE A 538     -58.114  10.495  38.109  1.00 45.33           C
ANISOU 4411  CB  PHE A 538     5569   5968   5686   1010     56    447       C
ATOM   4412  CG  PHE A 538     -57.098  11.405  38.753  1.00 46.59           C
ANISOU 4412  CG  PHE A 538     5676   6236   5789   1056     39    350       C
ATOM   4413  CD1 PHE A 538     -55.834  10.936  39.080  1.00 44.71           C
ANISOU 4413  CD1 PHE A 538     5429   6034   5522   1130    -10    322       C
ATOM   4414  CD2 PHE A 538     -57.402  12.732  39.018  1.00 44.74           C
ANISOU 4414  CD2 PHE A 538     5400   6066   5534   1027     67    283       C
ATOM   4415  CE1 PHE A 538     -54.896  11.769  39.667  1.00 40.12           C
ANISOU 4415  CE1 PHE A 538     4794   5559   4889   1167    -28    230       C
ATOM   4416  CE2 PHE A 538     -56.465  13.569  39.608  1.00 41.88           C
ANISOU 4416  CE2 PHE A 538     4991   5797   5123   1063     47    190       C
ATOM   4417  CZ  PHE A 538     -55.213  13.086  39.931  1.00 39.00           C
ANISOU 4417  CZ  PHE A 538     4614   5476   4728   1129      1    164       C
ATOM   4418  N   SER A 539     -59.387  10.969  41.029  1.00 44.11           N
ANISOU 4418  N   SER A 539     5395   6029   5336   1048     97    557       N
ATOM   4419  CA  SER A 539     -60.173  11.862  41.877  1.00 48.31           C
ANISOU 4419  CA  SER A 539     5890   6663   5802   1037    136    546       C
ATOM   4420  C   SER A 539     -59.883  13.299  41.458  1.00 47.64           C
ANISOU 4420  C   SER A 539     5757   6601   5744   1023    144    409       C
ATOM   4421  O   SER A 539     -58.865  13.880  41.846  1.00 47.51           O
ANISOU 4421  O   SER A 539     5710   6647   5694   1066    117    322       O
ATOM   4422  CB  SER A 539     -59.847  11.627  43.346  1.00 60.67           C
ANISOU 4422  CB  SER A 539     7450   8350   7252   1101    120    584       C
ATOM   4423  OG  SER A 539     -60.565  10.512  43.842  1.00 72.31           O
ANISOU 4423  OG  SER A 539     8969   9814   8693   1090    129    729       O
ATOM   4424  N   TYR A 540     -60.788  13.879  40.664  1.00 43.44           N
ANISOU 4424  N   TYR A 540     5219   6015   5274    961    179    391       N
ATOM   4425  CA  TYR A 540     -60.614  15.229  40.153  1.00 41.88           C
ANISOU 4425  CA  TYR A 540     4986   5814   5112    940    183    273       C
ATOM   4426  C   TYR A 540     -61.080  16.259  41.182  1.00 48.01           C
ANISOU 4426  C   TYR A 540     5725   6697   5821    963    201    223       C
ATOM   4427  O   TYR A 540     -61.977  15.986  41.981  1.00 52.94           O
ANISOU 4427  O   TYR A 540     6345   7384   6385    973    228    288       O
ATOM   4428  CB  TYR A 540     -61.388  15.403  38.849  1.00 34.43           C
ANISOU 4428  CB  TYR A 540     4055   4765   4261    870    205    279       C
ATOM   4429  CG  TYR A 540     -60.889  14.511  37.731  1.00 34.21           C
ANISOU 4429  CG  TYR A 540     4060   4636   4302    847    186    306       C
ATOM   4430  CD1 TYR A 540     -61.377  13.218  37.576  1.00 34.26           C
ANISOU 4430  CD1 TYR A 540     4106   4586   4323    837    188    412       C
ATOM   4431  CD2 TYR A 540     -59.920  14.957  36.837  1.00 38.02           C
ANISOU 4431  CD2 TYR A 540     4531   5081   4832    834    164    222       C
ATOM   4432  CE1 TYR A 540     -60.915  12.394  36.558  1.00 39.78           C
ANISOU 4432  CE1 TYR A 540     4837   5191   5086    823    166    424       C
ATOM   4433  CE2 TYR A 540     -59.453  14.139  35.818  1.00 40.47           C
ANISOU 4433  CE2 TYR A 540     4866   5313   5198    819    147    237       C
ATOM   4434  CZ  TYR A 540     -59.954  12.861  35.682  1.00 42.79           C
ANISOU 4434  CZ  TYR A 540     5202   5549   5509    819    147    333       C
ATOM   4435  OH  TYR A 540     -59.490  12.048  34.669  1.00 46.52           O
ANISOU 4435  OH  TYR A 540     5698   5940   6036    812    126    336       O
ATOM   4436  N   PRO A 541     -60.476  17.450  41.193  1.00 46.24           N
ANISOU 4436  N   PRO A 541     5471   6498   5601    971    184    103       N
ATOM   4437  CA  PRO A 541     -60.854  18.463  42.186  1.00 46.67           C
ANISOU 4437  CA  PRO A 541     5491   6650   5591   1001    193     38       C
ATOM   4438  C   PRO A 541     -62.172  19.160  41.893  1.00 47.13           C
ANISOU 4438  C   PRO A 541     5540   6685   5681    971    229     30       C
ATOM   4439  O   PRO A 541     -62.599  19.994  42.698  1.00 47.23           O
ANISOU 4439  O   PRO A 541     5523   6779   5644   1003    237    -29       O
ATOM   4440  CB  PRO A 541     -59.679  19.452  42.129  1.00 38.55           C
ANISOU 4440  CB  PRO A 541     4441   5632   4575   1009    155    -88       C
ATOM   4441  CG  PRO A 541     -59.185  19.348  40.739  1.00 41.50           C
ANISOU 4441  CG  PRO A 541     4833   5891   5044    954    143    -95       C
ATOM   4442  CD  PRO A 541     -59.377  17.911  40.325  1.00 44.27           C
ANISOU 4442  CD  PRO A 541     5216   6193   5410    950    153     21       C
ATOM   4443  N   PHE A 542     -62.824  18.842  40.776  1.00 50.32           N
ANISOU 4443  N   PHE A 542     5966   6987   6165    916    246     82       N
ATOM   4444  CA  PHE A 542     -64.135  19.388  40.454  1.00 52.35           C
ANISOU 4444  CA  PHE A 542     6213   7226   6454    891    277     83       C
ATOM   4445  C   PHE A 542     -64.869  18.382  39.574  1.00 53.78           C
ANISOU 4445  C   PHE A 542     6419   7327   6688    839    299    189       C
ATOM   4446  O   PHE A 542     -64.281  17.417  39.079  1.00 51.79           O
ANISOU 4446  O   PHE A 542     6199   7018   6462    821    285    243       O
ATOM   4447  CB  PHE A 542     -64.017  20.757  39.771  1.00 51.24           C
ANISOU 4447  CB  PHE A 542     6067   7025   6378    873    258    -26       C
ATOM   4448  CG  PHE A 542     -63.360  20.706  38.424  1.00 48.97           C
ANISOU 4448  CG  PHE A 542     5808   6622   6178    818    238    -32       C
ATOM   4449  CD1 PHE A 542     -61.984  20.634  38.313  1.00 53.35           C
ANISOU 4449  CD1 PHE A 542     6366   7171   6733    818    206    -73       C
ATOM   4450  CD2 PHE A 542     -64.120  20.725  37.269  1.00 50.33           C
ANISOU 4450  CD2 PHE A 542     5997   6703   6425    766    250     -0       C
ATOM   4451  CE1 PHE A 542     -61.376  20.582  37.072  1.00 55.21           C
ANISOU 4451  CE1 PHE A 542     6620   7317   7039    766    191    -81       C
ATOM   4452  CE2 PHE A 542     -63.518  20.672  36.026  1.00 53.53           C
ANISOU 4452  CE2 PHE A 542     6425   7015   6901    714    233     -6       C
ATOM   4453  CZ  PHE A 542     -62.145  20.602  35.928  1.00 53.41           C
ANISOU 4453  CZ  PHE A 542     6412   7000   6882    713    205    -47       C
ATOM   4454  N   GLU A 543     -66.169  18.615  39.383  1.00 51.74           N
ANISOU 4454  N   GLU A 543     6144   7068   6445    817    331    213       N
ATOM   4455  CA  GLU A 543     -66.995  17.697  38.600  1.00 55.44           C
ANISOU 4455  CA  GLU A 543     6631   7472   6962    762    352    311       C
ATOM   4456  C   GLU A 543     -66.567  17.748  37.137  1.00 51.07           C
ANISOU 4456  C   GLU A 543     6108   6791   6506    715    329    289       C
ATOM   4457  O   GLU A 543     -66.746  18.768  36.463  1.00 50.20           O
ANISOU 4457  O   GLU A 543     5990   6637   6445    701    321    222       O
ATOM   4458  CB  GLU A 543     -68.476  18.038  38.750  1.00 62.80           C
ANISOU 4458  CB  GLU A 543     7526   8450   7886    752    389    329       C
ATOM   4459  CG  GLU A 543     -69.404  16.989  38.142  1.00 72.33           C
ANISOU 4459  CG  GLU A 543     8743   9610   9127    691    413    438       C
ATOM   4460  CD  GLU A 543     -70.837  17.072  38.656  1.00 79.63           C
ANISOU 4460  CD  GLU A 543     9618  10626  10014    686    456    474       C
ATOM   4461  OE1 GLU A 543     -71.091  17.831  39.616  1.00 80.58           O
ANISOU 4461  OE1 GLU A 543     9695  10857  10066    738    470    420       O
ATOM   4462  OE2 GLU A 543     -71.710  16.372  38.096  1.00 79.16           O
ANISOU 4462  OE2 GLU A 543     9557  10531   9988    628    475    552       O
ATOM   4463  N   THR A 544     -66.008  16.646  36.649  1.00 45.98           N
ANISOU 4463  N   THR A 544     5499   6087   5886    694    316    347       N
ATOM   4464  CA  THR A 544     -65.474  16.537  35.300  1.00 42.60           C
ANISOU 4464  CA  THR A 544     5097   5553   5537    654    295    327       C
ATOM   4465  C   THR A 544     -66.475  15.866  34.368  1.00 37.52           C
ANISOU 4465  C   THR A 544     4469   4837   4949    597    311    397       C
ATOM   4466  O   THR A 544     -67.491  15.309  34.786  1.00 34.22           O
ANISOU 4466  O   THR A 544     4044   4447   4511    584    337    472       O
ATOM   4467  CB  THR A 544     -64.168  15.736  35.292  1.00 46.46           C
ANISOU 4467  CB  THR A 544     5609   6024   6018    675    266    331       C
ATOM   4468  OG1 THR A 544     -64.368  14.477  35.957  1.00 42.91           O
ANISOU 4468  OG1 THR A 544     5180   5591   5530    692    270    427       O
ATOM   4469  CG2 THR A 544     -63.062  16.511  35.982  1.00 47.35           C
ANISOU 4469  CG2 THR A 544     5701   6203   6087    722    244    245       C
ATOM   4470  N   TYR A 545     -66.159  15.916  33.080  1.00 34.55           N
ANISOU 4470  N   TYR A 545     4111   4374   4640    558    295    371       N
ATOM   4471  CA  TYR A 545     -66.843  15.095  32.097  1.00 35.49           C
ANISOU 4471  CA  TYR A 545     4252   4419   4814    505    300    431       C
ATOM   4472  C   TYR A 545     -65.832  14.717  31.024  1.00 38.90           C
ANISOU 4472  C   TYR A 545     4710   4778   5291    489    273    401       C
ATOM   4473  O   TYR A 545     -64.768  15.331  30.904  1.00 49.51           O
ANISOU 4473  O   TYR A 545     6048   6133   6630    507    255    330       O
ATOM   4474  CB  TYR A 545     -68.068  15.809  31.506  1.00 32.59           C
ANISOU 4474  CB  TYR A 545     3862   4038   4481    468    317    427       C
ATOM   4475  CG  TYR A 545     -67.775  17.134  30.841  1.00 30.58           C
ANISOU 4475  CG  TYR A 545     3601   3761   4257    464    302    343       C
ATOM   4476  CD1 TYR A 545     -67.243  17.187  29.557  1.00 27.81           C
ANISOU 4476  CD1 TYR A 545     3271   3337   3958    424    283    317       C
ATOM   4477  CD2 TYR A 545     -68.052  18.333  31.484  1.00 28.28           C
ANISOU 4477  CD2 TYR A 545     3283   3522   3942    497    306    289       C
ATOM   4478  CE1 TYR A 545     -66.981  18.393  28.940  1.00 29.03           C
ANISOU 4478  CE1 TYR A 545     3423   3468   4137    410    267    253       C
ATOM   4479  CE2 TYR A 545     -67.793  19.548  30.871  1.00 33.21           C
ANISOU 4479  CE2 TYR A 545     3908   4109   4599    488    285    218       C
ATOM   4480  CZ  TYR A 545     -67.258  19.571  29.600  1.00 34.63           C
ANISOU 4480  CZ  TYR A 545     4113   4215   4830    440    266    206       C
ATOM   4481  OH  TYR A 545     -67.001  20.778  28.987  1.00 43.19           O
ANISOU 4481  OH  TYR A 545     5204   5261   5944    422    244    148       O
ATOM   4482  N   GLY A 546     -66.167  13.687  30.255  1.00 29.80           N
ANISOU 4482  N   GLY A 546     3585   3558   4180    453    269    453       N
ATOM   4483  CA  GLY A 546     -65.276  13.146  29.249  1.00 30.85           C
ANISOU 4483  CA  GLY A 546     3742   3629   4350    443    244    425       C
ATOM   4484  C   GLY A 546     -65.799  13.397  27.849  1.00 34.65           C
ANISOU 4484  C   GLY A 546     4225   4052   4887    384    245    410       C
ATOM   4485  O   GLY A 546     -67.010  13.510  27.633  1.00 33.27           O
ANISOU 4485  O   GLY A 546     4044   3866   4731    348    261    447       O
ATOM   4486  N   VAL A 547     -64.869  13.485  26.899  1.00 33.81           N
ANISOU 4486  N   VAL A 547     4124   3920   4802    376    226    354       N
ATOM   4487  CA  VAL A 547     -65.163  13.654  25.480  1.00 34.76           C
ANISOU 4487  CA  VAL A 547     4249   3992   4967    321    223    335       C
ATOM   4488  C   VAL A 547     -64.677  12.404  24.761  1.00 36.60           C
ANISOU 4488  C   VAL A 547     4509   4175   5225    321    204    337       C
ATOM   4489  O   VAL A 547     -63.474  12.117  24.756  1.00 36.98           O
ANISOU 4489  O   VAL A 547     4556   4235   5258    356    187    294       O
ATOM   4490  CB  VAL A 547     -64.487  14.910  24.908  1.00 32.39           C
ANISOU 4490  CB  VAL A 547     3929   3712   4664    304    219    265       C
ATOM   4491  CG1 VAL A 547     -64.974  15.189  23.488  1.00 31.22           C
ANISOU 4491  CG1 VAL A 547     3787   3523   4554    244    216    259       C
ATOM   4492  CG2 VAL A 547     -64.736  16.106  25.810  1.00 29.96           C
ANISOU 4492  CG2 VAL A 547     3601   3449   4332    321    228    249       C
ATOM   4493  N   ILE A 548     -65.600  11.655  24.159  1.00 32.74           N
ANISOU 4493  N   ILE A 548     4040   3630   4772    283    203    381       N
ATOM   4494  CA  ILE A 548     -65.252  10.402  23.499  1.00 26.06           C
ANISOU 4494  CA  ILE A 548     3224   2724   3953    285    179    380       C
ATOM   4495  C   ILE A 548     -65.148  10.632  21.999  1.00 32.68           C
ANISOU 4495  C   ILE A 548     4058   3543   4818    242    172    329       C
ATOM   4496  O   ILE A 548     -65.955  11.353  21.400  1.00 39.88           O
ANISOU 4496  O   ILE A 548     4956   4456   5741    193    184    335       O
ATOM   4497  CB  ILE A 548     -66.255   9.279  23.835  1.00 38.62           C
ANISOU 4497  CB  ILE A 548     4845   4260   5569    266    176    460       C
ATOM   4498  CG1 ILE A 548     -65.728   7.933  23.332  1.00 30.55           C
ANISOU 4498  CG1 ILE A 548     3865   3166   4578    283    141    452       C
ATOM   4499  CG2 ILE A 548     -67.648   9.571  23.269  1.00 39.20           C
ANISOU 4499  CG2 ILE A 548     4906   4320   5669    199    192    493       C
ATOM   4500  CD1 ILE A 548     -66.095   6.757  24.214  1.00 37.63           C
ANISOU 4500  CD1 ILE A 548     4802   4013   5483    296    127    533       C
ATOM   4501  N   SER A 549     -64.121  10.043  21.400  1.00 32.86           N
ANISOU 4501  N   SER A 549     4087   3555   4842    266    152    276       N
ATOM   4502  CA  SER A 549     -63.851  10.128  19.972  1.00 31.95           C
ANISOU 4502  CA  SER A 549     3965   3436   4740    232    145    221       C
ATOM   4503  C   SER A 549     -62.879   9.003  19.646  1.00 29.88           C
ANISOU 4503  C   SER A 549     3718   3152   4483    279    118    175       C
ATOM   4504  O   SER A 549     -62.485   8.234  20.526  1.00 30.93           O
ANISOU 4504  O   SER A 549     3871   3266   4616    337    101    192       O
ATOM   4505  CB  SER A 549     -63.292  11.503  19.588  1.00 31.14           C
ANISOU 4505  CB  SER A 549     3827   3398   4607    208    160    175       C
ATOM   4506  OG  SER A 549     -62.992  11.569  18.204  1.00 28.47           O
ANISOU 4506  OG  SER A 549     3480   3068   4270    171    155    128       O
ATOM   4507  N   TRP A 550     -62.502   8.893  18.377  1.00 26.22           N
ANISOU 4507  N   TRP A 550     3245   2695   4023    259    110    115       N
ATOM   4508  CA  TRP A 550     -61.475   7.926  18.029  1.00 29.04           C
ANISOU 4508  CA  TRP A 550     3607   3046   4381    315     83     52       C
ATOM   4509  C   TRP A 550     -60.139   8.384  18.606  1.00 32.40           C
ANISOU 4509  C   TRP A 550     3995   3550   4764    368     86      4       C
ATOM   4510  O   TRP A 550     -59.909   9.579  18.808  1.00 26.57           O
ANISOU 4510  O   TRP A 550     3223   2877   3995    340    110     -1       O
ATOM   4511  CB  TRP A 550     -61.396   7.743  16.513  1.00 32.09           C
ANISOU 4511  CB  TRP A 550     3984   3438   4770    282     77     -9       C
ATOM   4512  CG  TRP A 550     -60.601   6.535  16.091  1.00 33.08           C
ANISOU 4512  CG  TRP A 550     4122   3541   4907    344     43    -77       C
ATOM   4513  CD1 TRP A 550     -59.654   6.485  15.108  1.00 37.34           C
ANISOU 4513  CD1 TRP A 550     4626   4143   5419    360     40   -170       C
ATOM   4514  CD2 TRP A 550     -60.681   5.208  16.637  1.00 34.28           C
ANISOU 4514  CD2 TRP A 550     4323   3602   5099    402      6    -59       C
ATOM   4515  NE1 TRP A 550     -59.138   5.215  15.008  1.00 35.89           N
ANISOU 4515  NE1 TRP A 550     4464   3914   5257    434      1   -221       N
ATOM   4516  CE2 TRP A 550     -59.748   4.412  15.935  1.00 35.74           C
ANISOU 4516  CE2 TRP A 550     4503   3792   5284    461    -24   -152       C
ATOM   4517  CE3 TRP A 550     -61.449   4.615  17.649  1.00 35.18           C
ANISOU 4517  CE3 TRP A 550     4486   3633   5247    409     -7     29       C
ATOM   4518  CZ2 TRP A 550     -59.560   3.055  16.212  1.00 33.52           C
ANISOU 4518  CZ2 TRP A 550     4272   3421   5044    532    -72   -162       C
ATOM   4519  CZ3 TRP A 550     -61.260   3.266  17.925  1.00 44.52           C
ANISOU 4519  CZ3 TRP A 550     5719   4727   6467    468    -53     30       C
ATOM   4520  CH2 TRP A 550     -60.322   2.502  17.208  1.00 41.61           C
ANISOU 4520  CH2 TRP A 550     5352   4351   6106    532    -88    -66       C
ATOM   4521  N   TRP A 551     -59.257   7.417  18.892  1.00 34.87           N
ANISOU 4521  N   TRP A 551     4316   3854   5078    447     57    -33       N
ATOM   4522  CA  TRP A 551     -58.072   7.728  19.690  1.00 33.69           C
ANISOU 4522  CA  TRP A 551     4132   3779   4890    507     54    -68       C
ATOM   4523  C   TRP A 551     -57.175   8.757  19.013  1.00 33.33           C
ANISOU 4523  C   TRP A 551     4023   3838   4803    475     76   -141       C
ATOM   4524  O   TRP A 551     -56.582   9.599  19.700  1.00 38.12           O
ANISOU 4524  O   TRP A 551     4594   4513   5376    480     88   -150       O
ATOM   4525  CB  TRP A 551     -57.289   6.454  20.028  1.00 36.77           C
ANISOU 4525  CB  TRP A 551     4541   4139   5290    605     12    -98       C
ATOM   4526  CG  TRP A 551     -56.758   5.646  18.881  1.00 42.24           C
ANISOU 4526  CG  TRP A 551     5230   4823   5998    634    -12   -181       C
ATOM   4527  CD1 TRP A 551     -57.314   4.522  18.346  1.00 44.48           C
ANISOU 4527  CD1 TRP A 551     5565   5006   6328    644    -42   -177       C
ATOM   4528  CD2 TRP A 551     -55.533   5.863  18.169  1.00 50.47           C
ANISOU 4528  CD2 TRP A 551     6208   5965   7002    661    -10   -286       C
ATOM   4529  NE1 TRP A 551     -56.524   4.036  17.331  1.00 41.97           N
ANISOU 4529  NE1 TRP A 551     5222   4719   6006    683    -61   -280       N
ATOM   4530  CE2 TRP A 551     -55.426   4.844  17.200  1.00 50.78           C
ANISOU 4530  CE2 TRP A 551     6263   5963   7066    694    -39   -346       C
ATOM   4531  CE3 TRP A 551     -54.524   6.827  18.247  1.00 54.78           C
ANISOU 4531  CE3 TRP A 551     6683   6635   7496    656     12   -336       C
ATOM   4532  CZ2 TRP A 551     -54.348   4.761  16.319  1.00 57.82           C
ANISOU 4532  CZ2 TRP A 551     7098   6947   7926    727    -41   -458       C
ATOM   4533  CZ3 TRP A 551     -53.457   6.745  17.369  1.00 58.77           C
ANISOU 4533  CZ3 TRP A 551     7129   7231   7971    680     11   -440       C
ATOM   4534  CH2 TRP A 551     -53.379   5.721  16.416  1.00 59.37           C
ANISOU 4534  CH2 TRP A 551     7217   7275   8065    718    -14   -501       C
ATOM   4535  N   ASP A 552     -57.106   8.738  17.678  1.00 34.49           N
ANISOU 4535  N   ASP A 552     4154   4003   4949    436     81   -190       N
ATOM   4536  CA  ASP A 552     -56.314   9.697  16.909  1.00 35.40           C
ANISOU 4536  CA  ASP A 552     4209   4221   5020    390    105   -250       C
ATOM   4537  C   ASP A 552     -56.387  11.120  17.440  1.00 35.05           C
ANISOU 4537  C   ASP A 552     4144   4218   4954    333    130   -217       C
ATOM   4538  O   ASP A 552     -55.374  11.826  17.516  1.00 38.38           O
ANISOU 4538  O   ASP A 552     4515   4729   5338    324    140   -263       O
ATOM   4539  CB  ASP A 552     -56.786   9.699  15.457  1.00 29.19           C
ANISOU 4539  CB  ASP A 552     3424   3431   4235    326    113   -269       C
ATOM   4540  CG  ASP A 552     -56.614   8.377  14.800  1.00 34.69           C
ANISOU 4540  CG  ASP A 552     4134   4096   4949    380     85   -323       C
ATOM   4541  OD1 ASP A 552     -56.426   7.371  15.520  1.00 43.16           O
ANISOU 4541  OD1 ASP A 552     5235   5115   6049    463     55   -324       O
ATOM   4542  OD2 ASP A 552     -56.658   8.337  13.558  1.00 36.63           O
ANISOU 4542  OD2 ASP A 552     4366   4371   5180    341     91   -365       O
ATOM   4543  N   TYR A 553     -57.587  11.559  17.788  1.00 29.14           N
ANISOU 4543  N   TYR A 553     3435   3407   4232    293    139   -142       N
ATOM   4544  CA  TYR A 553     -57.860  12.964  18.029  1.00 34.82           C
ANISOU 4544  CA  TYR A 553     4143   4150   4939    233    160   -114       C
ATOM   4545  C   TYR A 553     -57.679  13.361  19.488  1.00 37.43           C
ANISOU 4545  C   TYR A 553     4470   4491   5260    273    159    -95       C
ATOM   4546  O   TYR A 553     -57.815  14.550  19.816  1.00 32.01           O
ANISOU 4546  O   TYR A 553     3775   3823   4565    232    170    -83       O
ATOM   4547  CB  TYR A 553     -59.273  13.277  17.524  1.00 29.47           C
ANISOU 4547  CB  TYR A 553     3500   3407   4290    174    167    -54       C
ATOM   4548  CG  TYR A 553     -59.487  12.712  16.131  1.00 32.62           C
ANISOU 4548  CG  TYR A 553     3904   3795   4695    143    163    -74       C
ATOM   4549  CD1 TYR A 553     -58.813  13.248  15.039  1.00 32.76           C
ANISOU 4549  CD1 TYR A 553     3888   3880   4678     93    172   -121       C
ATOM   4550  CD2 TYR A 553     -60.322  11.624  15.911  1.00 38.37           C
ANISOU 4550  CD2 TYR A 553     4668   4451   5459    160    148    -50       C
ATOM   4551  CE1 TYR A 553     -58.981  12.736  13.763  1.00 30.62           C
ANISOU 4551  CE1 TYR A 553     3619   3614   4403     67    168   -146       C
ATOM   4552  CE2 TYR A 553     -60.498  11.101  14.628  1.00 35.34           C
ANISOU 4552  CE2 TYR A 553     4288   4062   5078    133    141    -80       C
ATOM   4553  CZ  TYR A 553     -59.819  11.665  13.561  1.00 35.01           C
ANISOU 4553  CZ  TYR A 553     4211   4096   4995     91    151   -130       C
ATOM   4554  OH  TYR A 553     -59.972  11.169  12.285  1.00 37.91           O
ANISOU 4554  OH  TYR A 553     4578   4471   5355     66    144   -164       O
ATOM   4555  N   GLY A 554     -57.325  12.404  20.350  1.00 34.19           N
ANISOU 4555  N   GLY A 554     4069   4073   4850    354    141    -95       N
ATOM   4556  CA  GLY A 554     -57.150  12.670  21.765  1.00 34.76           C
ANISOU 4556  CA  GLY A 554     4138   4165   4905    398    137    -76       C
ATOM   4557  C   GLY A 554     -56.331  13.908  22.070  1.00 33.84           C
ANISOU 4557  C   GLY A 554     3976   4128   4755    373    146   -120       C
ATOM   4558  O   GLY A 554     -56.824  14.839  22.718  1.00 30.82           O
ANISOU 4558  O   GLY A 554     3599   3742   4369    349    155    -94       O
ATOM   4559  N   HIS A 555     -55.087  13.947  21.582  1.00 26.94           N
ANISOU 4559  N   HIS A 555     3054   3327   3855    375    141   -192       N
ATOM   4560  CA  HIS A 555     -54.228  15.091  21.870  1.00 31.18           C
ANISOU 4560  CA  HIS A 555     3544   3943   4361    341    147   -236       C
ATOM   4561  C   HIS A 555     -54.823  16.378  21.316  1.00 27.74           C
ANISOU 4561  C   HIS A 555     3118   3486   3936    243    164   -215       C
ATOM   4562  O   HIS A 555     -54.809  17.415  21.992  1.00 32.92           O
ANISOU 4562  O   HIS A 555     3770   4153   4585    219    164   -216       O
ATOM   4563  CB  HIS A 555     -52.825  14.849  21.320  1.00 27.18           C
ANISOU 4563  CB  HIS A 555     2976   3530   3823    352    142   -317       C
ATOM   4564  CG  HIS A 555     -52.124  13.695  21.966  1.00 48.05           C
ANISOU 4564  CG  HIS A 555     5605   6197   6454    461    116   -345       C
ATOM   4565  ND1 HIS A 555     -51.174  12.938  21.316  1.00 42.22           N
ANISOU 4565  ND1 HIS A 555     4825   5517   5701    502    105   -412       N
ATOM   4566  CD2 HIS A 555     -52.244  13.164  23.206  1.00 44.50           C
ANISOU 4566  CD2 HIS A 555     5179   5725   6003    542     95   -315       C
ATOM   4567  CE1 HIS A 555     -50.736  11.993  22.129  1.00 43.31           C
ANISOU 4567  CE1 HIS A 555     4966   5656   5834    608     74   -422       C
ATOM   4568  NE2 HIS A 555     -51.369  12.108  23.282  1.00 41.53           N
ANISOU 4568  NE2 HIS A 555     4782   5382   5616    631     68   -358       N
ATOM   4569  N   TRP A 556     -55.388  16.323  20.106  1.00 29.30           N
ANISOU 4569  N   TRP A 556     3334   3649   4151    189    175   -197       N
ATOM   4570  CA  TRP A 556     -56.060  17.501  19.565  1.00 28.97           C
ANISOU 4570  CA  TRP A 556     3310   3575   4122    102    184   -166       C
ATOM   4571  C   TRP A 556     -57.149  17.982  20.513  1.00 34.85           C
ANISOU 4571  C   TRP A 556     4093   4256   4891    118    182   -114       C
ATOM   4572  O   TRP A 556     -57.295  19.190  20.743  1.00 39.39           O
ANISOU 4572  O   TRP A 556     4674   4825   5470     76    180   -111       O
ATOM   4573  CB  TRP A 556     -56.666  17.195  18.196  1.00 28.65           C
ANISOU 4573  CB  TRP A 556     3289   3504   4094     56    191   -144       C
ATOM   4574  CG  TRP A 556     -55.681  16.988  17.094  1.00 33.78           C
ANISOU 4574  CG  TRP A 556     3897   4228   4711     23    198   -197       C
ATOM   4575  CD1 TRP A 556     -54.322  17.119  17.161  1.00 34.82           C
ANISOU 4575  CD1 TRP A 556     3970   4455   4805     23    201   -261       C
ATOM   4576  CD2 TRP A 556     -55.983  16.606  15.748  1.00 33.53           C
ANISOU 4576  CD2 TRP A 556     3870   4195   4675    -15    204   -196       C
ATOM   4577  NE1 TRP A 556     -53.762  16.844  15.935  1.00 28.62           N
ANISOU 4577  NE1 TRP A 556     3152   3734   3990    -13    211   -299       N
ATOM   4578  CE2 TRP A 556     -54.761  16.526  15.052  1.00 33.11           C
ANISOU 4578  CE2 TRP A 556     3760   4243   4576    -36    213   -261       C
ATOM   4579  CE3 TRP A 556     -57.170  16.327  15.064  1.00 31.68           C
ANISOU 4579  CE3 TRP A 556     3678   3892   4466    -35    202   -150       C
ATOM   4580  CZ2 TRP A 556     -54.692  16.178  13.705  1.00 32.06           C
ANISOU 4580  CZ2 TRP A 556     3614   4148   4420    -72    222   -282       C
ATOM   4581  CZ3 TRP A 556     -57.099  15.983  13.728  1.00 32.86           C
ANISOU 4581  CZ3 TRP A 556     3817   4073   4595    -72    207   -171       C
ATOM   4582  CH2 TRP A 556     -55.868  15.908  13.064  1.00 29.86           C
ANISOU 4582  CH2 TRP A 556     3382   3797   4166    -89    217   -237       C
ATOM   4583  N   ILE A 557     -57.913  17.047  21.087  1.00 28.01           N
ANISOU 4583  N   ILE A 557     3254   3347   4041    179    180    -75       N
ATOM   4584  CA  ILE A 557     -58.981  17.423  22.006  1.00 35.26           C
ANISOU 4584  CA  ILE A 557     4200   4223   4974    197    182    -27       C
ATOM   4585  C   ILE A 557     -58.408  18.066  23.259  1.00 40.97           C
ANISOU 4585  C   ILE A 557     4904   4991   5672    230    176    -56       C
ATOM   4586  O   ILE A 557     -59.008  18.991  23.823  1.00 42.15           O
ANISOU 4586  O   ILE A 557     5064   5124   5827    221    176    -45       O
ATOM   4587  CB  ILE A 557     -59.845  16.194  22.348  1.00 37.52           C
ANISOU 4587  CB  ILE A 557     4514   4465   5278    245    183     25       C
ATOM   4588  CG1 ILE A 557     -60.674  15.771  21.134  1.00 35.08           C
ANISOU 4588  CG1 ILE A 557     4226   4103   4999    202    186     55       C
ATOM   4589  CG2 ILE A 557     -60.742  16.480  23.546  1.00 36.80           C
ANISOU 4589  CG2 ILE A 557     4436   4362   5186    275    189     68       C
ATOM   4590  CD1 ILE A 557     -61.284  14.397  21.267  1.00 32.66           C
ANISOU 4590  CD1 ILE A 557     3945   3751   4712    238    182     95       C
ATOM   4591  N   GLU A 558     -57.233  17.618  23.701  1.00 35.21           N
ANISOU 4591  N   GLU A 558     4143   4322   4912    271    167   -100       N
ATOM   4592  CA  GLU A 558     -56.696  18.134  24.953  1.00 32.56           C
ANISOU 4592  CA  GLU A 558     3787   4036   4548    308    158   -129       C
ATOM   4593  C   GLU A 558     -56.046  19.504  24.773  1.00 34.13           C
ANISOU 4593  C   GLU A 558     3961   4265   4740    244    153   -181       C
ATOM   4594  O   GLU A 558     -56.271  20.409  25.585  1.00 33.84           O
ANISOU 4594  O   GLU A 558     3929   4228   4700    245    147   -191       O
ATOM   4595  CB  GLU A 558     -55.701  17.135  25.539  1.00 30.34           C
ANISOU 4595  CB  GLU A 558     3481   3811   4236    382    144   -155       C
ATOM   4596  CG  GLU A 558     -55.239  17.465  26.938  1.00 29.29           C
ANISOU 4596  CG  GLU A 558     3330   3734   4066    433    131   -178       C
ATOM   4597  CD  GLU A 558     -54.307  16.410  27.491  1.00 40.26           C
ANISOU 4597  CD  GLU A 558     4697   5175   5424    515    111   -197       C
ATOM   4598  OE1 GLU A 558     -53.963  15.460  26.751  1.00 41.40           O
ANISOU 4598  OE1 GLU A 558     4841   5309   5580    533    106   -200       O
ATOM   4599  OE2 GLU A 558     -53.918  16.533  28.668  1.00 42.73           O
ANISOU 4599  OE2 GLU A 558     4995   5542   5700    566     97   -211       O
ATOM   4600  N   ALA A 559     -55.249  19.682  23.715  1.00 34.17           N
ANISOU 4600  N   ALA A 559     3940   4299   4742    186    155   -214       N
ATOM   4601  CA  ALA A 559     -54.483  20.915  23.562  1.00 34.79           C
ANISOU 4601  CA  ALA A 559     3992   4413   4812    114    148   -260       C
ATOM   4602  C   ALA A 559     -55.294  22.031  22.919  1.00 34.60           C
ANISOU 4602  C   ALA A 559     4007   4319   4821     35    148   -229       C
ATOM   4603  O   ALA A 559     -55.045  23.207  23.203  1.00 39.44           O
ANISOU 4603  O   ALA A 559     4620   4928   5438    -11    135   -254       O
ATOM   4604  CB  ALA A 559     -53.219  20.658  22.736  1.00 27.25           C
ANISOU 4604  CB  ALA A 559     2985   3537   3832     79    152   -309       C
ATOM   4605  N   VAL A 560     -56.245  21.697  22.053  1.00 36.19           N
ANISOU 4605  N   VAL A 560     4241   4462   5046     19    158   -177       N
ATOM   4606  CA  VAL A 560     -57.036  22.693  21.334  1.00 37.45           C
ANISOU 4606  CA  VAL A 560     4439   4555   5236    -50    153   -142       C
ATOM   4607  C   VAL A 560     -58.373  22.954  22.020  1.00 40.28           C
ANISOU 4607  C   VAL A 560     4836   4846   5623     -6    148   -104       C
ATOM   4608  O   VAL A 560     -58.777  24.104  22.188  1.00 46.92           O
ANISOU 4608  O   VAL A 560     5700   5642   6484    -33    131   -104       O
ATOM   4609  CB  VAL A 560     -57.235  22.262  19.864  1.00 34.23           C
ANISOU 4609  CB  VAL A 560     4037   4138   4830   -101    164   -112       C
ATOM   4610  CG1 VAL A 560     -57.957  23.352  19.085  1.00 37.50           C
ANISOU 4610  CG1 VAL A 560     4491   4488   5270   -175    153    -73       C
ATOM   4611  CG2 VAL A 560     -55.901  21.935  19.223  1.00 27.49           C
ANISOU 4611  CG2 VAL A 560     3135   3371   3940   -136    174   -158       C
ATOM   4612  N   ALA A 561     -59.079  21.897  22.419  1.00 38.90           N
ANISOU 4612  N   ALA A 561     4668   4664   5450     60    160    -73       N
ATOM   4613  CA  ALA A 561     -60.371  22.057  23.073  1.00 36.46           C
ANISOU 4613  CA  ALA A 561     4384   4310   5160    101    160    -37       C
ATOM   4614  C   ALA A 561     -60.267  22.171  24.587  1.00 38.67           C
ANISOU 4614  C   ALA A 561     4652   4624   5417    167    157    -62       C
ATOM   4615  O   ALA A 561     -61.235  22.599  25.223  1.00 42.55           O
ANISOU 4615  O   ALA A 561     5156   5093   5918    198    157    -47       O
ATOM   4616  CB  ALA A 561     -61.300  20.890  22.714  1.00 32.87           C
ANISOU 4616  CB  ALA A 561     3942   3830   4718    125    175     17       C
ATOM   4617  N   HIS A 562     -59.130  21.801  25.175  1.00 37.96           N
ANISOU 4617  N   HIS A 562     4532   4597   5294    194    155   -102       N
ATOM   4618  CA  HIS A 562     -58.945  21.856  26.626  1.00 39.96           C
ANISOU 4618  CA  HIS A 562     4772   4897   5516    259    150   -127       C
ATOM   4619  C   HIS A 562     -60.032  21.062  27.344  1.00 38.15           C
ANISOU 4619  C   HIS A 562     4555   4661   5278    321    166    -72       C
ATOM   4620  O   HIS A 562     -60.596  21.496  28.350  1.00 35.61           O
ANISOU 4620  O   HIS A 562     4234   4355   4942    360    166    -76       O
ATOM   4621  CB  HIS A 562     -58.899  23.300  27.127  1.00 42.95           C
ANISOU 4621  CB  HIS A 562     5153   5268   5899    240    132   -175       C
ATOM   4622  CG  HIS A 562     -57.566  23.954  26.949  1.00 46.57           C
ANISOU 4622  CG  HIS A 562     5587   5761   6348    191    114   -237       C
ATOM   4623  ND1 HIS A 562     -57.301  25.235  27.381  1.00 48.80           N
ANISOU 4623  ND1 HIS A 562     5872   6033   6637    164     90   -289       N
ATOM   4624  CD2 HIS A 562     -56.422  23.504  26.382  1.00 46.85           C
ANISOU 4624  CD2 HIS A 562     5590   5842   6367    160    116   -258       C
ATOM   4625  CE1 HIS A 562     -56.050  25.546  27.088  1.00 45.19           C
ANISOU 4625  CE1 HIS A 562     5385   5615   6168    109     79   -334       C
ATOM   4626  NE2 HIS A 562     -55.495  24.513  26.482  1.00 47.77           N
ANISOU 4626  NE2 HIS A 562     5687   5984   6479    108     96   -318       N
ATOM   4627  N   ARG A 563     -60.340  19.890  26.804  1.00 40.05           N
ANISOU 4627  N   ARG A 563     4806   4881   5529    326    178    -23       N
ATOM   4628  CA  ARG A 563     -61.266  18.964  27.427  1.00 37.83           C
ANISOU 4628  CA  ARG A 563     4537   4596   5240    372    192     37       C
ATOM   4629  C   ARG A 563     -60.581  17.608  27.548  1.00 37.76           C
ANISOU 4629  C   ARG A 563     4527   4604   5214    409    188     54       C
ATOM   4630  O   ARG A 563     -59.535  17.358  26.943  1.00 40.09           O
ANISOU 4630  O   ARG A 563     4811   4912   5509    400    177     16       O
ATOM   4631  CB  ARG A 563     -62.578  18.873  26.637  1.00 36.84           C
ANISOU 4631  CB  ARG A 563     4432   4410   5154    337    204     90       C
ATOM   4632  CG  ARG A 563     -63.368  20.186  26.586  1.00 31.42           C
ANISOU 4632  CG  ARG A 563     3749   3703   4487    316    201     76       C
ATOM   4633  CD  ARG A 563     -63.673  20.728  27.985  1.00 31.01           C
ANISOU 4633  CD  ARG A 563     3683   3697   4402    370    204     58       C
ATOM   4634  NE  ARG A 563     -64.489  21.939  27.942  1.00 30.08           N
ANISOU 4634  NE  ARG A 563     3568   3554   4307    363    196     39       N
ATOM   4635  CZ  ARG A 563     -64.004  23.180  27.939  1.00 37.57           C
ANISOU 4635  CZ  ARG A 563     4522   4489   5265    348    173    -22       C
ATOM   4636  NH1 ARG A 563     -62.690  23.389  27.978  1.00 26.01           N
ANISOU 4636  NH1 ARG A 563     3051   3044   3787    331    159    -68       N
ATOM   4637  NH2 ARG A 563     -64.834  24.215  27.888  1.00 26.07           N
ANISOU 4637  NH2 ARG A 563     3075   2997   3835    351    160    -37       N
ATOM   4638  N   MET A 564     -61.181  16.731  28.349  1.00 31.01           N
ANISOU 4638  N   MET A 564     3686   3754   4343    453    195    111       N
ATOM   4639  CA  MET A 564     -60.543  15.481  28.736  1.00 27.81           C
ANISOU 4639  CA  MET A 564     3288   3361   3918    503    183    131       C
ATOM   4640  C   MET A 564     -60.968  14.352  27.806  1.00 30.77           C
ANISOU 4640  C   MET A 564     3692   3667   4333    483    182    177       C
ATOM   4641  O   MET A 564     -62.113  13.882  27.903  1.00 33.96           O
ANISOU 4641  O   MET A 564     4118   4034   4753    470    195    243       O
ATOM   4642  CB  MET A 564     -60.892  15.142  30.178  1.00 27.36           C
ANISOU 4642  CB  MET A 564     3234   3347   3815    557    187    175       C
ATOM   4643  CG  MET A 564     -60.338  16.153  31.171  1.00 27.90           C
ANISOU 4643  CG  MET A 564     3272   3492   3836    587    182    119       C
ATOM   4644  SD  MET A 564     -60.837  15.842  32.875  1.00 43.34           S
ANISOU 4644  SD  MET A 564     5227   5518   5723    650    190    169       S
ATOM   4645  CE  MET A 564     -59.825  17.037  33.745  1.00 40.98           C
ANISOU 4645  CE  MET A 564     4889   5307   5375    682    172     72       C
ATOM   4646  N   PRO A 565     -60.095  13.865  26.928  1.00 42.25           N
ANISOU 4646  N   PRO A 565     5143   5106   5802    481    167    139       N
ATOM   4647  CA  PRO A 565     -60.489  12.802  26.000  1.00 26.20           C
ANISOU 4647  CA  PRO A 565     3140   3006   3810    464    162    169       C
ATOM   4648  C   PRO A 565     -60.463  11.425  26.645  1.00 33.83           C
ANISOU 4648  C   PRO A 565     4137   3943   4772    520    143    220       C
ATOM   4649  O   PRO A 565     -59.740  11.168  27.610  1.00 35.75           O
ANISOU 4649  O   PRO A 565     4376   4228   4979    582    128    216       O
ATOM   4650  CB  PRO A 565     -59.436  12.905  24.893  1.00 33.27           C
ANISOU 4650  CB  PRO A 565     4013   3916   4712    449    151     96       C
ATOM   4651  CG  PRO A 565     -58.199  13.362  25.630  1.00 27.80           C
ANISOU 4651  CG  PRO A 565     3284   3301   3976    491    141     41       C
ATOM   4652  CD  PRO A 565     -58.690  14.275  26.740  1.00 32.79           C
ANISOU 4652  CD  PRO A 565     3910   3963   4583    492    153     60       C
ATOM   4653  N   ILE A 566     -61.274  10.532  26.082  1.00 36.33           N
ANISOU 4653  N   ILE A 566     4490   4185   5129    495    140    268       N
ATOM   4654  CA  ILE A 566     -61.336   9.154  26.554  1.00 32.63           C
ANISOU 4654  CA  ILE A 566     4063   3665   4668    536    117    324       C
ATOM   4655  C   ILE A 566     -60.174   8.348  25.997  1.00 38.15           C
ANISOU 4655  C   ILE A 566     4770   4346   5381    586     81    268       C
ATOM   4656  O   ILE A 566     -59.589   7.510  26.696  1.00 45.33           O
ANISOU 4656  O   ILE A 566     5700   5247   6277    655     51    285       O
ATOM   4657  CB  ILE A 566     -62.689   8.534  26.157  1.00 39.06           C
ANISOU 4657  CB  ILE A 566     4911   4403   5525    480    125    395       C
ATOM   4658  CG1 ILE A 566     -63.844   9.255  26.861  1.00 38.21           C
ANISOU 4658  CG1 ILE A 566     4788   4331   5399    443    159    451       C
ATOM   4659  CG2 ILE A 566     -62.699   7.037  26.419  1.00 28.11           C
ANISOU 4659  CG2 ILE A 566     3578   2942   4161    510     92    450       C
ATOM   4660  CD1 ILE A 566     -63.913   8.983  28.338  1.00 37.93           C
ANISOU 4660  CD1 ILE A 566     4761   4335   5318    484    162    513       C
ATOM   4661  N   ALA A 567     -59.827   8.584  24.735  1.00 35.63           N
ANISOU 4661  N   ALA A 567     4431   4025   5083    557     83    200       N
ATOM   4662  CA  ALA A 567     -58.787   7.854  24.030  1.00 35.49           C
ANISOU 4662  CA  ALA A 567     4410   4000   5075    602     53    133       C
ATOM   4663  C   ALA A 567     -57.772   8.838  23.459  1.00 37.81           C
ANISOU 4663  C   ALA A 567     4643   4383   5339    591     65     42       C
ATOM   4664  O   ALA A 567     -58.112   9.988  23.159  1.00 36.40           O
ANISOU 4664  O   ALA A 567     4440   4238   5153    526     95     36       O
ATOM   4665  CB  ALA A 567     -59.395   6.998  22.916  1.00 30.70           C
ANISOU 4665  CB  ALA A 567     3838   3306   4519    571     41    136       C
ATOM   4666  N   ASN A 568     -56.525   8.394  23.318  1.00 34.84           N
ANISOU 4666  N   ASN A 568     4242   4047   4948    655     40    -27       N
ATOM   4667  CA  ASN A 568     -55.441   9.283  22.920  1.00 35.80           C
ANISOU 4667  CA  ASN A 568     4297   4270   5035    643     52   -111       C
ATOM   4668  C   ASN A 568     -54.456   8.556  22.018  1.00 40.80           C
ANISOU 4668  C   ASN A 568     4905   4929   5670    687     30   -195       C
ATOM   4669  O   ASN A 568     -54.459   7.322  21.950  1.00 28.84           O
ANISOU 4669  O   ASN A 568     3428   3349   4182    749     -3   -192       O
ATOM   4670  CB  ASN A 568     -54.707   9.867  24.138  1.00 27.99           C
ANISOU 4670  CB  ASN A 568     3275   3359   4002    684     48   -122       C
ATOM   4671  CG  ASN A 568     -54.159   8.803  25.079  1.00 34.32           C
ANISOU 4671  CG  ASN A 568     4095   4153   4793    790      8   -110       C
ATOM   4672  OD1 ASN A 568     -53.790   7.697  24.667  1.00 29.19           O
ANISOU 4672  OD1 ASN A 568     3463   3465   4164    848    -24   -132       O
ATOM   4673  ND2 ASN A 568     -54.096   9.146  26.361  1.00 37.46           N
ANISOU 4673  ND2 ASN A 568     4490   4588   5157    820      5    -77       N
ATOM   4674  N   PRO A 569     -53.587   9.304  21.303  1.00 38.44           N
ANISOU 4674  N   PRO A 569     4541   4725   5340    654     47   -272       N
ATOM   4675  CA  PRO A 569     -52.586   8.657  20.441  1.00 40.50           C
ANISOU 4675  CA  PRO A 569     4762   5034   5591    699     31   -363       C
ATOM   4676  C   PRO A 569     -51.525   7.845  21.176  1.00 34.34           C
ANISOU 4676  C   PRO A 569     3963   4288   4797    818    -10   -406       C
ATOM   4677  O   PRO A 569     -50.556   7.409  20.549  1.00 32.81           O
ANISOU 4677  O   PRO A 569     3722   4156   4588    867    -24   -494       O
ATOM   4678  CB  PRO A 569     -51.958   9.840  19.692  1.00 42.18           C
ANISOU 4678  CB  PRO A 569     4904   5358   5765    620     65   -419       C
ATOM   4679  CG  PRO A 569     -53.035  10.873  19.672  1.00 34.07           C
ANISOU 4679  CG  PRO A 569     3906   4289   4749    521     95   -349       C
ATOM   4680  CD  PRO A 569     -53.707  10.744  21.008  1.00 31.22           C
ANISOU 4680  CD  PRO A 569     3593   3864   4406    558     84   -274       C
ATOM   4681  N   PHE A 570     -51.674   7.627  22.482  1.00 37.15           N
ANISOU 4681  N   PHE A 570     4352   4612   5152    871    -30   -347       N
ATOM   4682  CA  PHE A 570     -50.917   6.577  23.158  1.00 44.80           C
ANISOU 4682  CA  PHE A 570     5328   5577   6118    995    -81   -367       C
ATOM   4683  C   PHE A 570     -51.620   5.226  23.074  1.00 48.97           C
ANISOU 4683  C   PHE A 570     5941   5967   6700   1043   -118   -317       C
ATOM   4684  O   PHE A 570     -51.177   4.269  23.719  1.00 46.99           O
ANISOU 4684  O   PHE A 570     5718   5682   6455   1146   -168   -312       O
ATOM   4685  CB  PHE A 570     -50.668   6.934  24.629  1.00 41.12           C
ANISOU 4685  CB  PHE A 570     4857   5150   5618   1034    -92   -325       C
ATOM   4686  CG  PHE A 570     -50.018   8.272  24.831  1.00 43.86           C
ANISOU 4686  CG  PHE A 570     5126   5620   5917    983    -62   -372       C
ATOM   4687  CD1 PHE A 570     -49.105   8.761  23.912  1.00 45.25           C
ANISOU 4687  CD1 PHE A 570     5224   5896   6072    953    -46   -468       C
ATOM   4688  CD2 PHE A 570     -50.330   9.046  25.937  1.00 37.76           C
ANISOU 4688  CD2 PHE A 570     4359   4869   5120    961    -50   -322       C
ATOM   4689  CE1 PHE A 570     -48.519   9.995  24.090  1.00 41.46           C
ANISOU 4689  CE1 PHE A 570     4678   5523   5553    894    -22   -506       C
ATOM   4690  CE2 PHE A 570     -49.744  10.281  26.122  1.00 37.09           C
ANISOU 4690  CE2 PHE A 570     4208   4886   4997    910    -29   -370       C
ATOM   4691  CZ  PHE A 570     -48.840  10.756  25.198  1.00 42.56           C
ANISOU 4691  CZ  PHE A 570     4829   5667   5676    873    -16   -459       C
ATOM   4692  N   GLN A 571     -52.700   5.137  22.291  1.00 49.90           N
ANISOU 4692  N   GLN A 571     6101   6002   6855    967    -98   -281       N
ATOM   4693  CA  GLN A 571     -53.525   3.933  22.169  1.00 48.43           C
ANISOU 4693  CA  GLN A 571     6000   5676   6727    987   -130   -228       C
ATOM   4694  C   GLN A 571     -54.169   3.553  23.498  1.00 42.36           C
ANISOU 4694  C   GLN A 571     5294   4835   5966   1007   -147   -114       C
ATOM   4695  O   GLN A 571     -54.518   2.392  23.723  1.00 46.39           O
ANISOU 4695  O   GLN A 571     5875   5235   6517   1051   -190    -68       O
ATOM   4696  CB  GLN A 571     -52.731   2.753  21.597  1.00 54.19           C
ANISOU 4696  CB  GLN A 571     6735   6376   7478   1086   -182   -310       C
ATOM   4697  CG  GLN A 571     -52.444   2.864  20.110  1.00 62.31           C
ANISOU 4697  CG  GLN A 571     7719   7452   8506   1056   -166   -411       C
ATOM   4698  CD  GLN A 571     -51.132   3.570  19.822  1.00 73.08           C
ANISOU 4698  CD  GLN A 571     8980   8976   9811   1078   -148   -513       C
ATOM   4699  OE1 GLN A 571     -51.091   4.791  19.675  1.00 75.46           O
ANISOU 4699  OE1 GLN A 571     9228   9369  10074    992    -99   -514       O
ATOM   4700  NE2 GLN A 571     -50.051   2.802  19.736  1.00 75.96           N
ANISOU 4700  NE2 GLN A 571     9315   9377  10169   1192   -191   -602       N
ATOM   4701  N   ALA A 572     -54.336   4.529  24.383  1.00 33.54           N
ANISOU 4701  N   ALA A 572     4153   3782   4809    973   -115    -69       N
ATOM   4702  CA  ALA A 572     -55.074   4.325  25.618  1.00 39.86           C
ANISOU 4702  CA  ALA A 572     5005   4536   5605    975   -120     42       C
ATOM   4703  C   ALA A 572     -56.557   4.581  25.389  1.00 40.77           C
ANISOU 4703  C   ALA A 572     5155   4588   5749    873    -84    119       C
ATOM   4704  O   ALA A 572     -56.945   5.358  24.513  1.00 38.56           O
ANISOU 4704  O   ALA A 572     4845   4330   5476    796    -47     88       O
ATOM   4705  CB  ALA A 572     -54.559   5.246  26.724  1.00 30.50           C
ANISOU 4705  CB  ALA A 572     3774   3459   4357    994   -105     44       C
ATOM   4706  N   GLY A 573     -57.385   3.917  26.191  1.00 44.00           N
ANISOU 4706  N   GLY A 573     5626   4922   6172    871    -96    224       N
ATOM   4707  CA  GLY A 573     -58.815   4.151  26.138  1.00 45.03           C
ANISOU 4707  CA  GLY A 573     5779   5008   6322    777    -61    302       C
ATOM   4708  C   GLY A 573     -59.489   3.672  24.873  1.00 43.00           C
ANISOU 4708  C   GLY A 573     5547   4667   6124    720    -63    288       C
ATOM   4709  O   GLY A 573     -60.529   4.214  24.491  1.00 41.74           O
ANISOU 4709  O   GLY A 573     5381   4503   5977    635    -27    318       O
ATOM   4710  N   ILE A 574     -58.921   2.667  24.206  1.00 43.84           N
ANISOU 4710  N   ILE A 574     5682   4710   6267    771   -108    238       N
ATOM   4711  CA  ILE A 574     -59.555   2.125  23.010  1.00 42.80           C
ANISOU 4711  CA  ILE A 574     5577   4496   6191    721   -116    218       C
ATOM   4712  C   ILE A 574     -60.673   1.159  23.383  1.00 44.92           C
ANISOU 4712  C   ILE A 574     5920   4644   6505    682   -136    322       C
ATOM   4713  O   ILE A 574     -61.762   1.192  22.796  1.00 42.75           O
ANISOU 4713  O   ILE A 574     5654   4327   6261    596   -118    351       O
ATOM   4714  CB  ILE A 574     -58.501   1.454  22.110  1.00 42.66           C
ANISOU 4714  CB  ILE A 574     5555   4464   6191    793   -157    108       C
ATOM   4715  CG1 ILE A 574     -57.595   2.509  21.474  1.00 39.08           C
ANISOU 4715  CG1 ILE A 574     5017   4141   5691    795   -126      6       C
ATOM   4716  CG2 ILE A 574     -59.170   0.614  21.036  1.00 40.15           C
ANISOU 4716  CG2 ILE A 574     5281   4042   5934    755   -180     91       C
ATOM   4717  CD1 ILE A 574     -56.600   1.937  20.488  1.00 36.26           C
ANISOU 4717  CD1 ILE A 574     4639   3796   5341    859   -157   -112       C
ATOM   4718  N   GLY A 575     -60.432   0.298  24.368  1.00 42.97           N
ANISOU 4718  N   GLY A 575     5725   4342   6261    742   -176    385       N
ATOM   4719  CA  GLY A 575     -61.421  -0.681  24.774  1.00 42.19           C
ANISOU 4719  CA  GLY A 575     5702   4126   6205    700   -200    493       C
ATOM   4720  C   GLY A 575     -61.663  -1.712  23.687  1.00 41.98           C
ANISOU 4720  C   GLY A 575     5724   3973   6251    686   -243    455       C
ATOM   4721  O   GLY A 575     -61.021  -1.730  22.639  1.00 43.37           O
ANISOU 4721  O   GLY A 575     5878   4159   6442    720   -257    341       O
ATOM   4722  N   ASN A 576     -62.622  -2.590  23.954  1.00 44.09           N
ANISOU 4722  N   ASN A 576     6061   4127   6565    630   -266    552       N
ATOM   4723  CA  ASN A 576     -63.000  -3.596  22.972  1.00 48.98           C
ANISOU 4723  CA  ASN A 576     6734   4616   7261    604   -311    522       C
ATOM   4724  C   ASN A 576     -64.379  -4.126  23.332  1.00 45.76           C
ANISOU 4724  C   ASN A 576     6376   4121   6889    495   -309    647       C
ATOM   4725  O   ASN A 576     -64.882  -3.909  24.437  1.00 45.15           O
ANISOU 4725  O   ASN A 576     6300   4079   6777    461   -281    760       O
ATOM   4726  CB  ASN A 576     -61.965  -4.728  22.897  1.00 51.73           C
ANISOU 4726  CB  ASN A 576     7143   4867   7646    718   -391    469       C
ATOM   4727  CG  ASN A 576     -61.619  -5.303  24.261  1.00 53.07           C
ANISOU 4727  CG  ASN A 576     7368   4995   7800    779   -428    569       C
ATOM   4728  OD1 ASN A 576     -62.497  -5.591  25.073  1.00 55.30           O
ANISOU 4728  OD1 ASN A 576     7693   5231   8086    710   -422    702       O
ATOM   4729  ND2 ASN A 576     -60.330  -5.473  24.517  1.00 56.01           N
ANISOU 4729  ND2 ASN A 576     7736   5393   8151    907   -466    506       N
ATOM   4730  N   LYS A 577     -64.987  -4.825  22.373  1.00 44.91           N
ANISOU 4730  N   LYS A 577     6304   3909   6849    439   -338    622       N
ATOM   4731  CA  LYS A 577     -66.276  -5.468  22.598  1.00 41.76           C
ANISOU 4731  CA  LYS A 577     5954   3417   6495    329   -345    733       C
ATOM   4732  C   LYS A 577     -66.127  -6.888  23.133  1.00 45.65           C
ANISOU 4732  C   LYS A 577     6554   3747   7042    356   -422    801       C
ATOM   4733  O   LYS A 577     -66.866  -7.279  24.042  1.00 49.76           O
ANISOU 4733  O   LYS A 577     7114   4226   7564    289   -421    939       O
ATOM   4734  CB  LYS A 577     -67.097  -5.476  21.304  1.00 36.61           C
ANISOU 4734  CB  LYS A 577     5285   2737   5889    242   -340    675       C
ATOM   4735  CG  LYS A 577     -68.078  -4.318  21.193  1.00 38.48           C
ANISOU 4735  CG  LYS A 577     5439   3094   6086    149   -264    702       C
ATOM   4736  CD  LYS A 577     -68.364  -3.955  19.744  1.00 41.62           C
ANISOU 4736  CD  LYS A 577     5797   3515   6502    111   -256    598       C
ATOM   4737  CE  LYS A 577     -69.370  -4.896  19.109  1.00 48.00           C
ANISOU 4737  CE  LYS A 577     6649   4205   7383     19   -293    617       C
ATOM   4738  NZ  LYS A 577     -69.646  -4.536  17.687  1.00 45.99           N
ANISOU 4738  NZ  LYS A 577     6353   3983   7138    -15   -288    513       N
ATOM   4739  N   TYR A 578     -65.167  -7.659  22.608  1.00 46.28           N
ANISOU 4739  N   TYR A 578     6683   3737   7165    456   -491    708       N
ATOM   4740  CA  TYR A 578     -65.027  -9.061  22.997  1.00 50.45           C
ANISOU 4740  CA  TYR A 578     7324   4086   7757    488   -578    764       C
ATOM   4741  C   TYR A 578     -64.783  -9.241  24.491  1.00 53.19           C
ANISOU 4741  C   TYR A 578     7710   4437   8064    523   -587    896       C
ATOM   4742  O   TYR A 578     -65.043 -10.326  25.020  1.00 55.64           O
ANISOU 4742  O   TYR A 578     8119   4600   8421    505   -647    996       O
ATOM   4743  CB  TYR A 578     -63.894  -9.728  22.205  1.00 51.72           C
ANISOU 4743  CB  TYR A 578     7517   4172   7961    616   -651    622       C
ATOM   4744  CG  TYR A 578     -62.510  -9.152  22.448  1.00 54.92           C
ANISOU 4744  CG  TYR A 578     7868   4697   8304    756   -643    539       C
ATOM   4745  CD1 TYR A 578     -61.765  -9.512  23.567  1.00 54.40           C
ANISOU 4745  CD1 TYR A 578     7843   4612   8215    852   -682    600       C
ATOM   4746  CD2 TYR A 578     -61.940  -8.264  21.545  1.00 52.62           C
ANISOU 4746  CD2 TYR A 578     7483   4538   7973    790   -601    400       C
ATOM   4747  CE1 TYR A 578     -60.509  -8.990  23.787  1.00 52.43           C
ANISOU 4747  CE1 TYR A 578     7536   4478   7907    977   -678    521       C
ATOM   4748  CE2 TYR A 578     -60.681  -7.741  21.756  1.00 50.81           C
ANISOU 4748  CE2 TYR A 578     7197   4423   7686    907   -594    324       C
ATOM   4749  CZ  TYR A 578     -59.970  -8.106  22.878  1.00 54.15           C
ANISOU 4749  CZ  TYR A 578     7656   4829   8089   1001   -633    381       C
ATOM   4750  OH  TYR A 578     -58.715  -7.582  23.094  1.00 56.02           O
ANISOU 4750  OH  TYR A 578     7829   5188   8268   1115   -628    301       O
ATOM   4751  N   ASN A 579     -64.279  -8.218  25.180  1.00 54.18           N
ANISOU 4751  N   ASN A 579     7763   4721   8102    570   -532    901       N
ATOM   4752  CA  ASN A 579     -64.048  -8.298  26.617  1.00 57.00           C
ANISOU 4752  CA  ASN A 579     8148   5105   8406    604   -536   1022       C
ATOM   4753  C   ASN A 579     -64.906  -7.313  27.395  1.00 56.04           C
ANISOU 4753  C   ASN A 579     7961   5122   8212    511   -449   1117       C
ATOM   4754  O   ASN A 579     -64.706  -7.158  28.606  1.00 57.26           O
ANISOU 4754  O   ASN A 579     8117   5336   8301    539   -439   1207       O
ATOM   4755  CB  ASN A 579     -62.570  -8.063  26.936  1.00 64.40           C
ANISOU 4755  CB  ASN A 579     9062   6109   9299    761   -561    942       C
ATOM   4756  CG  ASN A 579     -61.854  -9.330  27.339  1.00 68.76           C
ANISOU 4756  CG  ASN A 579     9718   6515   9893    862   -662    970       C
ATOM   4757  OD1 ASN A 579     -62.273 -10.434  26.989  1.00 67.87           O
ANISOU 4757  OD1 ASN A 579     9697   6228   9864    831   -724   1001       O
ATOM   4758  ND2 ASN A 579     -60.764  -9.179  28.080  1.00 72.32           N
ANISOU 4758  ND2 ASN A 579    10155   7033  10289    986   -683    958       N
ATOM   4759  N   ASN A 580     -65.852  -6.646  26.731  1.00 55.42           N
ANISOU 4759  N   ASN A 580     7822   5099   8137    407   -389   1095       N
ATOM   4760  CA  ASN A 580     -66.698  -5.630  27.357  1.00 50.97           C
ANISOU 4760  CA  ASN A 580     7185   4674   7506    327   -307   1164       C
ATOM   4761  C   ASN A 580     -65.871  -4.545  28.039  1.00 49.97           C
ANISOU 4761  C   ASN A 580     6991   4704   7291    411   -267   1128       C
ATOM   4762  O   ASN A 580     -66.264  -4.018  29.082  1.00 53.68           O
ANISOU 4762  O   ASN A 580     7431   5272   7694    385   -222   1212       O
ATOM   4763  CB  ASN A 580     -67.676  -6.256  28.354  1.00 56.12           C
ANISOU 4763  CB  ASN A 580     7885   5284   8152    235   -305   1334       C
ATOM   4764  CG  ASN A 580     -68.732  -7.101  27.679  1.00 58.89           C
ANISOU 4764  CG  ASN A 580     8283   5507   8585    118   -328   1374       C
ATOM   4765  OD1 ASN A 580     -69.345  -6.682  26.695  1.00 55.75           O
ANISOU 4765  OD1 ASN A 580     7835   5131   8216     55   -299   1306       O
ATOM   4766  ND2 ASN A 580     -68.952  -8.301  28.203  1.00 59.26           N
ANISOU 4766  ND2 ASN A 580     8427   5418   8672     84   -384   1487       N
ATOM   4767  N   VAL A 581     -64.717  -4.216  27.464  1.00 45.16           N
ANISOU 4767  N   VAL A 581     6355   4125   6679    511   -284    998       N
ATOM   4768  CA  VAL A 581     -63.872  -3.139  27.977  1.00 37.16           C
ANISOU 4768  CA  VAL A 581     5271   3259   5588    585   -250    947       C
ATOM   4769  C   VAL A 581     -64.373  -1.825  27.392  1.00 39.56           C
ANISOU 4769  C   VAL A 581     5486   3676   5868    523   -178    886       C
ATOM   4770  O   VAL A 581     -64.221  -1.590  26.185  1.00 37.44           O
ANISOU 4770  O   VAL A 581     5192   3399   5633    516   -177    784       O
ATOM   4771  CB  VAL A 581     -62.391  -3.361  27.634  1.00 35.67           C
ANISOU 4771  CB  VAL A 581     5085   3063   5404    714   -300    835       C
ATOM   4772  CG1 VAL A 581     -61.572  -2.177  28.106  1.00 34.61           C
ANISOU 4772  CG1 VAL A 581     4870   3088   5191    772   -261    778       C
ATOM   4773  CG2 VAL A 581     -61.880  -4.641  28.262  1.00 36.78           C
ANISOU 4773  CG2 VAL A 581     5318   3088   5569    789   -379    896       C
ATOM   4774  N   PRO A 582     -64.972  -0.948  28.196  1.00 46.60           N
ANISOU 4774  N   PRO A 582     6330   4676   6700    481   -121    944       N
ATOM   4775  CA  PRO A 582     -65.548   0.283  27.640  1.00 47.78           C
ANISOU 4775  CA  PRO A 582     6403   4918   6834    423    -60    893       C
ATOM   4776  C   PRO A 582     -64.462   1.207  27.111  1.00 52.07           C
ANISOU 4776  C   PRO A 582     6891   5539   7354    488    -52    767       C
ATOM   4777  O   PRO A 582     -63.505   1.542  27.815  1.00 51.36           O
ANISOU 4777  O   PRO A 582     6785   5515   7214    566    -57    743       O
ATOM   4778  CB  PRO A 582     -66.297   0.897  28.829  1.00 50.04           C
ANISOU 4778  CB  PRO A 582     6656   5301   7055    386    -10    983       C
ATOM   4779  CG  PRO A 582     -65.650   0.312  30.032  1.00 50.50           C
ANISOU 4779  CG  PRO A 582     6755   5359   7071    454    -41   1050       C
ATOM   4780  CD  PRO A 582     -65.206  -1.065  29.645  1.00 50.93           C
ANISOU 4780  CD  PRO A 582     6895   5268   7190    484   -111   1062       C
ATOM   4781  N   GLY A 583     -64.617   1.604  25.856  1.00 51.43           N
ANISOU 4781  N   GLY A 583     6782   5453   7306    452    -40    687       N
ATOM   4782  CA  GLY A 583     -63.647   2.462  25.209  1.00 46.45           C
ANISOU 4782  CA  GLY A 583     6101   4894   6656    494    -31    572       C
ATOM   4783  C   GLY A 583     -64.215   2.998  23.917  1.00 42.53           C
ANISOU 4783  C   GLY A 583     5573   4400   6186    426     -8    518       C
ATOM   4784  O   GLY A 583     -65.403   2.840  23.627  1.00 42.01           O
ANISOU 4784  O   GLY A 583     5517   4295   6151    348      4    569       O
ATOM   4785  N   ALA A 584     -63.342   3.629  23.130  1.00 32.82           N
ANISOU 4785  N   ALA A 584     4303   3223   4943    453     -5    416       N
ATOM   4786  CA  ALA A 584     -63.796   4.268  21.899  1.00 32.64           C
ANISOU 4786  CA  ALA A 584     4249   3218   4935    389     17    367       C
ATOM   4787  C   ALA A 584     -64.356   3.241  20.922  1.00 39.39           C
ANISOU 4787  C   ALA A 584     5144   3974   5848    353    -13    360       C
ATOM   4788  O   ALA A 584     -65.425   3.444  20.332  1.00 50.16           O
ANISOU 4788  O   ALA A 584     6502   5324   7234    276      3    382       O
ATOM   4789  CB  ALA A 584     -62.651   5.054  21.261  1.00 31.68           C
ANISOU 4789  CB  ALA A 584     4080   3176   4782    421     24    265       C
ATOM   4790  N   SER A 585     -63.646   2.125  20.744  1.00 37.02           N
ANISOU 4790  N   SER A 585     4886   3605   5576    412    -61    326       N
ATOM   4791  CA  SER A 585     -64.081   1.118  19.782  1.00 35.85           C
ANISOU 4791  CA  SER A 585     4779   3356   5485    385    -97    303       C
ATOM   4792  C   SER A 585     -65.404   0.482  20.197  1.00 40.24           C
ANISOU 4792  C   SER A 585     5379   3827   6081    312   -102    409       C
ATOM   4793  O   SER A 585     -66.299   0.304  19.362  1.00 44.66           O
ANISOU 4793  O   SER A 585     5943   4348   6676    240   -104    407       O
ATOM   4794  CB  SER A 585     -62.996   0.054  19.609  1.00 33.77           C
ANISOU 4794  CB  SER A 585     4554   3032   5244    478   -153    238       C
ATOM   4795  OG  SER A 585     -62.936  -0.819  20.725  1.00 32.83           O
ANISOU 4795  OG  SER A 585     4495   2838   5142    520   -188    316       O
ATOM   4796  N   SER A 586     -65.556   0.141  21.481  1.00 38.32           N
ANISOU 4796  N   SER A 586     5166   3562   5830    326   -105    503       N
ATOM   4797  CA  SER A 586     -66.800  -0.477  21.931  1.00 44.62           C
ANISOU 4797  CA  SER A 586     6002   4291   6661    248   -107    612       C
ATOM   4798  C   SER A 586     -67.954   0.520  21.987  1.00 43.65           C
ANISOU 4798  C   SER A 586     5822   4248   6514    162    -50    657       C
ATOM   4799  O   SER A 586     -69.116   0.104  22.027  1.00 42.33           O
ANISOU 4799  O   SER A 586     5668   4038   6377     80    -47    728       O
ATOM   4800  CB  SER A 586     -66.607  -1.146  23.298  1.00 38.92           C
ANISOU 4800  CB  SER A 586     5330   3531   5927    284   -127    708       C
ATOM   4801  OG  SER A 586     -66.024  -0.258  24.237  1.00 43.24           O
ANISOU 4801  OG  SER A 586     5835   4189   6404    338    -95    717       O
ATOM   4802  N   PHE A 587     -67.665   1.820  21.987  1.00 45.36           N
ANISOU 4802  N   PHE A 587     5976   4578   6681    180     -8    615       N
ATOM   4803  CA  PHE A 587     -68.731   2.812  21.933  1.00 39.97           C
ANISOU 4803  CA  PHE A 587     5240   3966   5981    112     39    643       C
ATOM   4804  C   PHE A 587     -69.193   3.042  20.500  1.00 45.76           C
ANISOU 4804  C   PHE A 587     5954   4690   6744     60     36    582       C
ATOM   4805  O   PHE A 587     -70.395   3.002  20.214  1.00 47.95           O
ANISOU 4805  O   PHE A 587     6218   4956   7043    -16     45    623       O
ATOM   4806  CB  PHE A 587     -68.261   4.124  22.565  1.00 34.73           C
ANISOU 4806  CB  PHE A 587     4525   3416   5255    153     77    624       C
ATOM   4807  CG  PHE A 587     -69.222   5.269  22.386  1.00 32.95           C
ANISOU 4807  CG  PHE A 587     4245   3262   5014    100    118    632       C
ATOM   4808  CD1 PHE A 587     -70.322   5.405  23.217  1.00 35.29           C
ANISOU 4808  CD1 PHE A 587     4522   3591   5298     60    146    714       C
ATOM   4809  CD2 PHE A 587     -69.020   6.215  21.395  1.00 29.72           C
ANISOU 4809  CD2 PHE A 587     3801   2891   4600     94    126    558       C
ATOM   4810  CE1 PHE A 587     -71.204   6.460  23.060  1.00 32.81           C
ANISOU 4810  CE1 PHE A 587     4154   3343   4970     25    178    713       C
ATOM   4811  CE2 PHE A 587     -69.897   7.270  21.232  1.00 31.77           C
ANISOU 4811  CE2 PHE A 587     4016   3206   4848     55    155    566       C
ATOM   4812  CZ  PHE A 587     -70.991   7.393  22.067  1.00 35.32           C
ANISOU 4812  CZ  PHE A 587     4445   3685   5289     26    180    639       C
ATOM   4813  N   PHE A 588     -68.250   3.269  19.582  1.00 40.30           N
ANISOU 4813  N   PHE A 588     5255   4011   6047    100     22    485       N
ATOM   4814  CA  PHE A 588     -68.604   3.638  18.217  1.00 39.91           C
ANISOU 4814  CA  PHE A 588     5181   3974   6010     54     23    426       C
ATOM   4815  C   PHE A 588     -69.014   2.455  17.351  1.00 42.46           C
ANISOU 4815  C   PHE A 588     5545   4200   6389     19    -19    407       C
ATOM   4816  O   PHE A 588     -69.591   2.671  16.279  1.00 45.07           O
ANISOU 4816  O   PHE A 588     5855   4540   6730    -33    -20    374       O
ATOM   4817  CB  PHE A 588     -67.443   4.384  17.557  1.00 38.29           C
ANISOU 4817  CB  PHE A 588     4946   3833   5768    100     28    332       C
ATOM   4818  CG  PHE A 588     -67.260   5.774  18.077  1.00 36.13           C
ANISOU 4818  CG  PHE A 588     4626   3654   5446    108     68    340       C
ATOM   4819  CD1 PHE A 588     -68.198   6.755  17.804  1.00 26.77           C
ANISOU 4819  CD1 PHE A 588     3408   2512   4253     53     94    364       C
ATOM   4820  CD2 PHE A 588     -66.163   6.097  18.857  1.00 33.55           C
ANISOU 4820  CD2 PHE A 588     4292   3372   5085    174     74    321       C
ATOM   4821  CE1 PHE A 588     -68.041   8.035  18.290  1.00 35.36           C
ANISOU 4821  CE1 PHE A 588     4460   3672   5302     64    123    367       C
ATOM   4822  CE2 PHE A 588     -66.000   7.374  19.345  1.00 32.94           C
ANISOU 4822  CE2 PHE A 588     4176   3374   4967    178    105    323       C
ATOM   4823  CZ  PHE A 588     -66.937   8.345  19.061  1.00 38.60           C
ANISOU 4823  CZ  PHE A 588     4866   4121   5681    123    129    345       C
ATOM   4824  N   THR A 589     -68.734   1.222  17.773  1.00 43.19           N
ANISOU 4824  N   THR A 589     5695   4197   6516     47    -58    426       N
ATOM   4825  CA  THR A 589     -69.221   0.036  17.081  1.00 39.48           C
ANISOU 4825  CA  THR A 589     5274   3619   6109      8   -104    415       C
ATOM   4826  C   THR A 589     -70.351  -0.648  17.838  1.00 39.12           C
ANISOU 4826  C   THR A 589     5258   3505   6099    -63   -109    527       C
ATOM   4827  O   THR A 589     -70.760  -1.749  17.458  1.00 43.85           O
ANISOU 4827  O   THR A 589     5908   3997   6757   -101   -153    531       O
ATOM   4828  CB  THR A 589     -68.084  -0.960  16.843  1.00 40.30           C
ANISOU 4828  CB  THR A 589     5429   3648   6237     89   -156    345       C
ATOM   4829  OG1 THR A 589     -67.563  -1.401  18.101  1.00 40.03           O
ANISOU 4829  OG1 THR A 589     5432   3579   6199    146   -168    406       O
ATOM   4830  CG2 THR A 589     -66.971  -0.316  16.027  1.00 30.76           C
ANISOU 4830  CG2 THR A 589     4180   2523   4986    151   -147    230       C
ATOM   4831  N   ALA A 590     -70.852  -0.027  18.905  1.00 42.00           N
ANISOU 4831  N   ALA A 590     5594   3935   6430    -83    -66    614       N
ATOM   4832  CA  ALA A 590     -71.977  -0.581  19.645  1.00 38.95           C
ANISOU 4832  CA  ALA A 590     5224   3511   6067   -160    -62    726       C
ATOM   4833  C   ALA A 590     -73.196  -0.709  18.741  1.00 41.35           C
ANISOU 4833  C   ALA A 590     5505   3798   6408   -259    -66    725       C
ATOM   4834  O   ALA A 590     -73.521   0.202  17.976  1.00 43.05           O
ANISOU 4834  O   ALA A 590     5664   4090   6604   -276    -42    675       O
ATOM   4835  CB  ALA A 590     -72.300   0.305  20.848  1.00 36.51           C
ANISOU 4835  CB  ALA A 590     4867   3305   5698   -158     -8    801       C
ATOM   4836  N   GLU A 591     -73.875  -1.849  18.831  1.00 49.02           N
ANISOU 4836  N   GLU A 591     6523   4668   7434   -328    -99    781       N
ATOM   4837  CA  GLU A 591     -74.973  -2.147  17.923  1.00 48.73           C
ANISOU 4837  CA  GLU A 591     6471   4605   7440   -425   -113    772       C
ATOM   4838  C   GLU A 591     -76.334  -1.706  18.446  1.00 47.70           C
ANISOU 4838  C   GLU A 591     6278   4552   7294   -516    -70    862       C
ATOM   4839  O   GLU A 591     -77.321  -1.811  17.711  1.00 51.69           O
ANISOU 4839  O   GLU A 591     6754   5057   7828   -598    -77    854       O
ATOM   4840  CB  GLU A 591     -74.993  -3.643  17.611  1.00 52.24           C
ANISOU 4840  CB  GLU A 591     6997   4891   7959   -459   -180    772       C
ATOM   4841  CG  GLU A 591     -73.669  -4.160  17.079  1.00 57.25           C
ANISOU 4841  CG  GLU A 591     7690   5449   8612   -360   -229    673       C
ATOM   4842  CD  GLU A 591     -73.479  -5.637  17.342  1.00 70.14           C
ANISOU 4842  CD  GLU A 591     9422   6916  10314   -364   -296    701       C
ATOM   4843  OE1 GLU A 591     -74.365  -6.430  16.951  1.00 72.26           O
ANISOU 4843  OE1 GLU A 591     9718   7096  10641   -459   -330    723       O
ATOM   4844  OE2 GLU A 591     -72.447  -6.004  17.948  1.00 70.55           O
ANISOU 4844  OE2 GLU A 591     9523   6922  10360   -273   -319    703       O
ATOM   4845  N   ASN A 592     -76.415  -1.213  19.681  1.00 45.67           N
ANISOU 4845  N   ASN A 592     5996   4369   6988   -500    -25    941       N
ATOM   4846  CA  ASN A 592     -77.640  -0.611  20.190  1.00 47.30           C
ANISOU 4846  CA  ASN A 592     6127   4678   7166   -569     24   1011       C
ATOM   4847  C   ASN A 592     -77.271   0.477  21.189  1.00 51.42           C
ANISOU 4847  C   ASN A 592     6606   5316   7614   -498     75   1030       C
ATOM   4848  O   ASN A 592     -76.169   0.485  21.744  1.00 58.71           O
ANISOU 4848  O   ASN A 592     7568   6225   8513   -416     71   1021       O
ATOM   4849  CB  ASN A 592     -78.565  -1.656  20.828  1.00 45.01           C
ANISOU 4849  CB  ASN A 592     5858   4336   6907   -673     16   1122       C
ATOM   4850  CG  ASN A 592     -77.926  -2.366  22.002  1.00 48.28           C
ANISOU 4850  CG  ASN A 592     6341   4694   7310   -644      6   1203       C
ATOM   4851  OD1 ASN A 592     -77.724  -1.773  23.062  1.00 48.85           O
ANISOU 4851  OD1 ASN A 592     6387   4857   7319   -600     49   1249       O
ATOM   4852  ND2 ASN A 592     -77.613  -3.648  21.826  1.00 47.51           N
ANISOU 4852  ND2 ASN A 592     6333   4444   7274   -665    -53   1218       N
ATOM   4853  N   GLU A 593     -78.205   1.408  21.415  1.00 50.41           N
ANISOU 4853  N   GLU A 593     6396   5307   7452   -527    121   1051       N
ATOM   4854  CA  GLU A 593     -77.908   2.520  22.311  1.00 47.35           C
ANISOU 4854  CA  GLU A 593     5965   5030   6996   -457    167   1055       C
ATOM   4855  C   GLU A 593     -77.748   2.071  23.758  1.00 48.02           C
ANISOU 4855  C   GLU A 593     6072   5130   7044   -449    185   1148       C
ATOM   4856  O   GLU A 593     -77.126   2.790  24.545  1.00 48.87           O
ANISOU 4856  O   GLU A 593     6167   5307   7096   -373    211   1140       O
ATOM   4857  CB  GLU A 593     -78.988   3.604  22.223  1.00 44.25           C
ANISOU 4857  CB  GLU A 593     5478   4757   6577   -480    206   1049       C
ATOM   4858  CG  GLU A 593     -78.552   4.950  22.827  1.00 48.25           C
ANISOU 4858  CG  GLU A 593     5945   5366   7023   -393    242   1016       C
ATOM   4859  CD  GLU A 593     -79.580   6.062  22.656  1.00 51.90           C
ANISOU 4859  CD  GLU A 593     6320   5934   7465   -401    270    998       C
ATOM   4860  OE1 GLU A 593     -80.741   5.759  22.301  1.00 52.80           O
ANISOU 4860  OE1 GLU A 593     6392   6067   7602   -477    271   1027       O
ATOM   4861  OE2 GLU A 593     -79.223   7.241  22.884  1.00 45.49           O
ANISOU 4861  OE2 GLU A 593     5481   5187   6616   -329    288    952       O
ATOM   4862  N   SER A 594     -78.277   0.902  24.128  1.00 37.61           N
ANISOU 4862  N   SER A 594     4789   3748   5753   -528    170   1237       N
ATOM   4863  CA  SER A 594     -78.108   0.436  25.501  1.00 42.57           C
ANISOU 4863  CA  SER A 594     5445   4391   6340   -525    185   1337       C
ATOM   4864  C   SER A 594     -76.652   0.092  25.787  1.00 47.52           C
ANISOU 4864  C   SER A 594     6149   4944   6963   -429    151   1313       C
ATOM   4865  O   SER A 594     -76.111   0.467  26.834  1.00 55.35           O
ANISOU 4865  O   SER A 594     7138   6001   7892   -367    173   1340       O
ATOM   4866  CB  SER A 594     -79.014  -0.767  25.767  1.00 43.23           C
ANISOU 4866  CB  SER A 594     5554   4414   6458   -645    172   1445       C
ATOM   4867  OG  SER A 594     -80.379  -0.395  25.681  1.00 43.27           O
ANISOU 4867  OG  SER A 594     5470   4516   6454   -732    210   1472       O
ATOM   4868  N   TYR A 595     -75.993  -0.601  24.857  1.00 45.86           N
ANISOU 4868  N   TYR A 595     6005   4605   6816   -412     95   1255       N
ATOM   4869  CA  TYR A 595     -74.576  -0.904  25.030  1.00 45.40           C
ANISOU 4869  CA  TYR A 595     6011   4485   6755   -311     59   1217       C
ATOM   4870  C   TYR A 595     -73.726   0.360  24.949  1.00 40.60           C
ANISOU 4870  C   TYR A 595     5357   3972   6097   -214     85   1125       C
ATOM   4871  O   TYR A 595     -72.757   0.520  25.707  1.00 45.87           O
ANISOU 4871  O   TYR A 595     6042   4664   6723   -132     83   1123       O
ATOM   4872  CB  TYR A 595     -74.134  -1.927  23.983  1.00 47.56           C
ANISOU 4872  CB  TYR A 595     6357   4608   7108   -312     -7   1163       C
ATOM   4873  CG  TYR A 595     -72.790  -2.550  24.275  1.00 53.23           C
ANISOU 4873  CG  TYR A 595     7149   5245   7831   -213    -54   1142       C
ATOM   4874  CD1 TYR A 595     -71.615  -1.948  23.840  1.00 50.84           C
ANISOU 4874  CD1 TYR A 595     6833   4974   7508   -110    -60   1032       C
ATOM   4875  CD2 TYR A 595     -72.695  -3.735  24.991  1.00 54.31           C
ANISOU 4875  CD2 TYR A 595     7367   5277   7991   -225    -96   1235       C
ATOM   4876  CE1 TYR A 595     -70.390  -2.510  24.106  1.00 51.20           C
ANISOU 4876  CE1 TYR A 595     6937   4960   7558    -14   -104   1007       C
ATOM   4877  CE2 TYR A 595     -71.470  -4.304  25.263  1.00 55.88           C
ANISOU 4877  CE2 TYR A 595     7633   5403   8196   -124   -145   1214       C
ATOM   4878  CZ  TYR A 595     -70.321  -3.685  24.817  1.00 55.40           C
ANISOU 4878  CZ  TYR A 595     7550   5386   8115    -16   -149   1096       C
ATOM   4879  OH  TYR A 595     -69.096  -4.244  25.082  1.00 59.38           O
ANISOU 4879  OH  TYR A 595     8110   5829   8622     90   -199   1068       O
ATOM   4880  N   ALA A 596     -74.061   1.262  24.025  1.00 37.19           N
ANISOU 4880  N   ALA A 596     4868   3593   5671   -225    104   1048       N
ATOM   4881  CA  ALA A 596     -73.356   2.535  23.964  1.00 39.34           C
ANISOU 4881  CA  ALA A 596     5096   3954   5897   -149    129    970       C
ATOM   4882  C   ALA A 596     -73.491   3.290  25.278  1.00 43.40           C
ANISOU 4882  C   ALA A 596     5569   4580   6341   -122    174   1019       C
ATOM   4883  O   ALA A 596     -72.530   3.909  25.745  1.00 45.92           O
ANISOU 4883  O   ALA A 596     5884   4946   6619    -42    180    980       O
ATOM   4884  CB  ALA A 596     -73.876   3.377  22.800  1.00 29.97           C
ANISOU 4884  CB  ALA A 596     3858   2802   4725   -179    140    900       C
ATOM   4885  N   GLU A 597     -74.669   3.228  25.903  1.00 38.04           N
ANISOU 4885  N   GLU A 597     4857   3952   5646   -188    205   1102       N
ATOM   4886  CA  GLU A 597     -74.858   3.886  27.191  1.00 37.63           C
ANISOU 4886  CA  GLU A 597     4762   4017   5521   -161    249   1147       C
ATOM   4887  C   GLU A 597     -74.075   3.180  28.286  1.00 38.42           C
ANISOU 4887  C   GLU A 597     4915   4096   5586   -119    234   1209       C
ATOM   4888  O   GLU A 597     -73.576   3.828  29.208  1.00 38.89           O
ANISOU 4888  O   GLU A 597     4954   4241   5580    -55    256   1203       O
ATOM   4889  CB  GLU A 597     -76.343   3.949  27.542  1.00 41.30           C
ANISOU 4889  CB  GLU A 597     5167   4555   5971   -244    287   1217       C
ATOM   4890  CG  GLU A 597     -77.059   5.164  26.957  1.00 51.66           C
ANISOU 4890  CG  GLU A 597     6400   5949   7280   -246    315   1152       C
ATOM   4891  CD  GLU A 597     -76.482   6.485  27.449  1.00 55.11           C
ANISOU 4891  CD  GLU A 597     6801   6476   7661   -156    338   1088       C
ATOM   4892  OE1 GLU A 597     -76.847   6.925  28.559  1.00 57.32           O
ANISOU 4892  OE1 GLU A 597     7039   6863   7880   -138    375   1123       O
ATOM   4893  OE2 GLU A 597     -75.658   7.086  26.727  1.00 54.61           O
ANISOU 4893  OE2 GLU A 597     6753   6382   7616   -106    318   1002       O
ATOM   4894  N   PHE A 598     -73.963   1.853  28.206  1.00 35.27           N
ANISOU 4894  N   PHE A 598     4589   3581   5230   -153    193   1267       N
ATOM   4895  CA  PHE A 598     -73.060   1.121  29.089  1.00 44.95           C
ANISOU 4895  CA  PHE A 598     5880   4766   6433    -99    164   1318       C
ATOM   4896  C   PHE A 598     -71.661   1.722  29.040  1.00 53.64           C
ANISOU 4896  C   PHE A 598     6985   5884   7511     15    149   1222       C
ATOM   4897  O   PHE A 598     -71.101   2.149  30.062  1.00 57.14           O
ANISOU 4897  O   PHE A 598     7416   6407   7887     78    163   1233       O
ATOM   4898  CB  PHE A 598     -73.037  -0.355  28.680  1.00 46.95           C
ANISOU 4898  CB  PHE A 598     6221   4861   6758   -142    107   1367       C
ATOM   4899  CG  PHE A 598     -71.839  -1.114  29.174  1.00 47.40           C
ANISOU 4899  CG  PHE A 598     6356   4842   6813    -61     56   1382       C
ATOM   4900  CD1 PHE A 598     -71.628  -1.303  30.531  1.00 47.09           C
ANISOU 4900  CD1 PHE A 598     6334   4850   6707    -35     63   1476       C
ATOM   4901  CD2 PHE A 598     -70.928  -1.654  28.278  1.00 48.64           C
ANISOU 4901  CD2 PHE A 598     6566   4883   7030     -7     -1   1301       C
ATOM   4902  CE1 PHE A 598     -70.524  -2.009  30.985  1.00 50.36           C
ANISOU 4902  CE1 PHE A 598     6821   5194   7118     47      9   1492       C
ATOM   4903  CE2 PHE A 598     -69.823  -2.361  28.727  1.00 46.30           C
ANISOU 4903  CE2 PHE A 598     6338   4519   6733     79    -53   1310       C
ATOM   4904  CZ  PHE A 598     -69.623  -2.536  30.081  1.00 35.87           C
ANISOU 4904  CZ  PHE A 598     5037   3242   5349    107    -50   1407       C
ATOM   4905  N   VAL A 599     -71.103   1.795  27.830  1.00 51.09           N
ANISOU 4905  N   VAL A 599     6672   5499   7240     38    121   1122       N
ATOM   4906  CA  VAL A 599     -69.746   2.309  27.658  1.00 43.71           C
ANISOU 4906  CA  VAL A 599     5737   4583   6288    136    106   1026       C
ATOM   4907  C   VAL A 599     -69.656   3.757  28.135  1.00 42.44           C
ANISOU 4907  C   VAL A 599     5506   4557   6064    169    152    984       C
ATOM   4908  O   VAL A 599     -68.738   4.128  28.876  1.00 42.97           O
ANISOU 4908  O   VAL A 599     5568   4678   6082    243    151    963       O
ATOM   4909  CB  VAL A 599     -69.300   2.161  26.192  1.00 44.31           C
ANISOU 4909  CB  VAL A 599     5826   4585   6425    141     75    928       C
ATOM   4910  CG1 VAL A 599     -67.902   2.740  25.996  1.00 33.97           C
ANISOU 4910  CG1 VAL A 599     4503   3312   5091    233     64    828       C
ATOM   4911  CG2 VAL A 599     -69.336   0.696  25.777  1.00 31.78           C
ANISOU 4911  CG2 VAL A 599     4315   2858   4903    119     21    959       C
ATOM   4912  N   ALA A 600     -70.624   4.590  27.742  1.00 45.87           N
ANISOU 4912  N   ALA A 600     5883   5045   6499    116    189    970       N
ATOM   4913  CA  ALA A 600     -70.548   6.018  28.041  1.00 44.46           C
ANISOU 4913  CA  ALA A 600     5643   4977   6272    150    225    916       C
ATOM   4914  C   ALA A 600     -70.685   6.287  29.533  1.00 43.97           C
ANISOU 4914  C   ALA A 600     5560   5009   6136    177    253    973       C
ATOM   4915  O   ALA A 600     -69.948   7.110  30.091  1.00 44.44           O
ANISOU 4915  O   ALA A 600     5598   5139   6148    242    261    924       O
ATOM   4916  CB  ALA A 600     -71.621   6.777  27.262  1.00 38.38           C
ANISOU 4916  CB  ALA A 600     4824   4234   5525     93    250    892       C
ATOM   4917  N   GLU A 601     -71.629   5.612  30.193  1.00 37.64           N
ANISOU 4917  N   GLU A 601     4763   4218   5321    124    269   1076       N
ATOM   4918  CA  GLU A 601     -71.779   5.751  31.633  1.00 38.23           C
ANISOU 4918  CA  GLU A 601     4818   4393   5316    146    296   1139       C
ATOM   4919  C   GLU A 601     -70.523   5.298  32.355  1.00 40.05           C
ANISOU 4919  C   GLU A 601     5096   4609   5512    221    264   1147       C
ATOM   4920  O   GLU A 601     -70.071   5.961  33.294  1.00 43.90           O
ANISOU 4920  O   GLU A 601     5556   5194   5929    280    279   1129       O
ATOM   4921  CB  GLU A 601     -72.989   4.950  32.111  1.00 44.21           C
ANISOU 4921  CB  GLU A 601     5573   5158   6065     61    316   1258       C
ATOM   4922  CG  GLU A 601     -73.199   4.985  33.616  1.00 54.12           C
ANISOU 4922  CG  GLU A 601     6808   6528   7227     75    347   1335       C
ATOM   4923  CD  GLU A 601     -73.784   6.303  34.096  1.00 63.27           C
ANISOU 4923  CD  GLU A 601     7879   7834   8327     95    399   1287       C
ATOM   4924  OE1 GLU A 601     -74.256   7.091  33.247  1.00 66.76           O
ANISOU 4924  OE1 GLU A 601     8278   8281   8808     83    410   1214       O
ATOM   4925  OE2 GLU A 601     -73.778   6.549  35.322  1.00 66.88           O
ANISOU 4925  OE2 GLU A 601     8311   8403   8696    127    424   1321       O
ATOM   4926  N   LYS A 602     -69.936   4.174  31.923  1.00 42.69           N
ANISOU 4926  N   LYS A 602     5501   4824   5896    226    216   1168       N
ATOM   4927  CA  LYS A 602     -68.710   3.702  32.560  1.00 41.26           C
ANISOU 4927  CA  LYS A 602     5364   4626   5685    307    177   1172       C
ATOM   4928  C   LYS A 602     -67.584   4.729  32.456  1.00 47.47           C
ANISOU 4928  C   LYS A 602     6117   5472   6448    389    175   1055       C
ATOM   4929  O   LYS A 602     -66.735   4.813  33.353  1.00 50.68           O
ANISOU 4929  O   LYS A 602     6526   5932   6797    460    162   1053       O
ATOM   4930  CB  LYS A 602     -68.283   2.372  31.941  1.00 39.12           C
ANISOU 4930  CB  LYS A 602     5173   4206   5484    306    119   1195       C
ATOM   4931  CG  LYS A 602     -68.115   1.259  32.952  1.00 47.29           C
ANISOU 4931  CG  LYS A 602     6273   5201   6493    320     87   1310       C
ATOM   4932  CD  LYS A 602     -69.374   1.082  33.784  1.00 52.40           C
ANISOU 4932  CD  LYS A 602     6908   5904   7100    235    127   1434       C
ATOM   4933  CE  LYS A 602     -69.108   0.219  35.007  1.00 58.23           C
ANISOU 4933  CE  LYS A 602     7702   6638   7784    256    102   1554       C
ATOM   4934  NZ  LYS A 602     -70.360  -0.063  35.762  1.00 55.65           N
ANISOU 4934  NZ  LYS A 602     7363   6366   7416    158    142   1685       N
ATOM   4935  N   LEU A 603     -67.569   5.529  31.391  1.00 40.04           N
ANISOU 4935  N   LEU A 603     5141   4526   5545    376    185    960       N
ATOM   4936  CA  LEU A 603     -66.512   6.504  31.156  1.00 36.43           C
ANISOU 4936  CA  LEU A 603     4652   4116   5073    437    181    850       C
ATOM   4937  C   LEU A 603     -66.958   7.936  31.421  1.00 41.25           C
ANISOU 4937  C   LEU A 603     5198   4828   5646    429    224    806       C
ATOM   4938  O   LEU A 603     -66.205   8.870  31.128  1.00 36.11           O
ANISOU 4938  O   LEU A 603     4519   4210   4989    461    222    714       O
ATOM   4939  CB  LEU A 603     -65.992   6.376  29.724  1.00 33.97           C
ANISOU 4939  CB  LEU A 603     4353   3726   4828    431    156    772       C
ATOM   4940  CG  LEU A 603     -65.403   5.000  29.405  1.00 38.55           C
ANISOU 4940  CG  LEU A 603     4996   4203   5449    456    106    790       C
ATOM   4941  CD1 LEU A 603     -65.103   4.853  27.920  1.00 34.67           C
ANISOU 4941  CD1 LEU A 603     4511   3643   5020    441     86    711       C
ATOM   4942  CD2 LEU A 603     -64.161   4.762  30.238  1.00 30.39           C
ANISOU 4942  CD2 LEU A 603     3976   3199   4372    548     75    778       C
ATOM   4943  N   ASN A 604     -68.162   8.132  31.959  1.00 42.93           N
ANISOU 4943  N   ASN A 604     5385   5091   5834    387    260    866       N
ATOM   4944  CA  ASN A 604     -68.675   9.462  32.284  1.00 36.07           C
ANISOU 4944  CA  ASN A 604     4456   4318   4930    389    297    822       C
ATOM   4945  C   ASN A 604     -68.576  10.400  31.080  1.00 37.16           C
ANISOU 4945  C   ASN A 604     4573   4427   5118    375    294    730       C
ATOM   4946  O   ASN A 604     -68.063  11.517  31.165  1.00 33.39           O
ANISOU 4946  O   ASN A 604     4068   3996   4621    409    296    653       O
ATOM   4947  CB  ASN A 604     -67.947  10.040  33.497  1.00 35.31           C
ANISOU 4947  CB  ASN A 604     4341   4319   4757    460    300    796       C
ATOM   4948  CG  ASN A 604     -68.663  11.232  34.085  1.00 41.06           C
ANISOU 4948  CG  ASN A 604     5010   5149   5440    466    336    765       C
ATOM   4949  OD1 ASN A 604     -69.876  11.361  33.952  1.00 49.74           O
ANISOU 4949  OD1 ASN A 604     6083   6267   6550    420    365    797       O
ATOM   4950  ND2 ASN A 604     -67.915  12.116  34.733  1.00 47.69           N
ANISOU 4950  ND2 ASN A 604     5828   6059   6233    525    333    695       N
ATOM   4951  N   VAL A 605     -69.081   9.926  29.944  1.00 37.38           N
ANISOU 4951  N   VAL A 605     4617   4375   5210    320    286    741       N
ATOM   4952  CA  VAL A 605     -69.012  10.668  28.689  1.00 38.24           C
ANISOU 4952  CA  VAL A 605     4714   4452   5365    299    280    666       C
ATOM   4953  C   VAL A 605     -70.135  11.697  28.637  1.00 44.57           C
ANISOU 4953  C   VAL A 605     5468   5303   6164    274    308    658       C
ATOM   4954  O   VAL A 605     -71.307  11.367  28.857  1.00 41.70           O
ANISOU 4954  O   VAL A 605     5087   4957   5801    235    328    719       O
ATOM   4955  CB  VAL A 605     -69.094   9.704  27.494  1.00 41.17           C
ANISOU 4955  CB  VAL A 605     5120   4724   5798    254    256    677       C
ATOM   4956  CG1 VAL A 605     -69.614  10.423  26.249  1.00 38.67           C
ANISOU 4956  CG1 VAL A 605     4782   4389   5520    211    259    631       C
ATOM   4957  CG2 VAL A 605     -67.741   9.056  27.239  1.00 45.84           C
ANISOU 4957  CG2 VAL A 605     5750   5269   6398    297    222    641       C
ATOM   4958  N   LYS A 606     -69.781  12.952  28.334  1.00 45.38           N
ANISOU 4958  N   LYS A 606     5549   5428   6264    294    306    581       N
ATOM   4959  CA  LYS A 606     -70.764  14.002  28.110  1.00 37.87           C
ANISOU 4959  CA  LYS A 606     4560   4508   5322    280    322    561       C
ATOM   4960  C   LYS A 606     -70.784  14.518  26.681  1.00 41.71           C
ANISOU 4960  C   LYS A 606     5053   4937   5860    246    303    518       C
ATOM   4961  O   LYS A 606     -71.814  15.041  26.247  1.00 49.12           O
ANISOU 4961  O   LYS A 606     5966   5880   6818    223    309    521       O
ATOM   4962  CB  LYS A 606     -70.518  15.191  29.052  1.00 29.75           C
ANISOU 4962  CB  LYS A 606     3504   3554   4248    335    330    510       C
ATOM   4963  CG  LYS A 606     -71.662  16.196  29.092  1.00 38.05           C
ANISOU 4963  CG  LYS A 606     4512   4644   5300    337    345    493       C
ATOM   4964  CD  LYS A 606     -71.414  17.299  30.108  1.00 44.23           C
ANISOU 4964  CD  LYS A 606     5271   5497   6038    398    349    435       C
ATOM   4965  CE  LYS A 606     -72.517  18.340  30.082  1.00 47.01           C
ANISOU 4965  CE  LYS A 606     5582   5880   6397    413    355    405       C
ATOM   4966  NZ  LYS A 606     -73.850  17.750  30.394  1.00 54.51           N
ANISOU 4966  NZ  LYS A 606     6492   6885   7333    394    386    469       N
ATOM   4967  N   TYR A 607     -69.695  14.368  25.933  1.00 35.62           N
ANISOU 4967  N   TYR A 607     4309   4118   5105    242    281    479       N
ATOM   4968  CA  TYR A 607     -69.640  14.879  24.574  1.00 29.28           C
ANISOU 4968  CA  TYR A 607     3513   3273   4340    206    265    441       C
ATOM   4969  C   TYR A 607     -69.020  13.838  23.658  1.00 30.72           C
ANISOU 4969  C   TYR A 607     3726   3400   4547    182    247    439       C
ATOM   4970  O   TYR A 607     -68.151  13.062  24.063  1.00 34.95           O
ANISOU 4970  O   TYR A 607     4280   3929   5069    210    240    439       O
ATOM   4971  CB  TYR A 607     -68.870  16.205  24.516  1.00 30.71           C
ANISOU 4971  CB  TYR A 607     3688   3472   4510    225    255    375       C
ATOM   4972  CG  TYR A 607     -69.628  17.299  25.221  1.00 36.80           C
ANISOU 4972  CG  TYR A 607     4432   4284   5267    250    265    366       C
ATOM   4973  CD1 TYR A 607     -70.723  17.906  24.615  1.00 37.57           C
ANISOU 4973  CD1 TYR A 607     4516   4368   5392    229    262    373       C
ATOM   4974  CD2 TYR A 607     -69.287  17.692  26.506  1.00 33.87           C
ANISOU 4974  CD2 TYR A 607     4047   3969   4854    301    274    346       C
ATOM   4975  CE1 TYR A 607     -71.441  18.891  25.261  1.00 40.67           C
ANISOU 4975  CE1 TYR A 607     4881   4798   5774    263    266    356       C
ATOM   4976  CE2 TYR A 607     -70.000  18.683  27.161  1.00 40.01           C
ANISOU 4976  CE2 TYR A 607     4798   4786   5617    332    281    326       C
ATOM   4977  CZ  TYR A 607     -71.076  19.277  26.533  1.00 42.40           C
ANISOU 4977  CZ  TYR A 607     5087   5071   5951    315    276    330       C
ATOM   4978  OH  TYR A 607     -71.791  20.258  27.177  1.00 47.89           O
ANISOU 4978  OH  TYR A 607     5753   5807   6634    357    279    302       O
ATOM   4979  N   VAL A 608     -69.495  13.829  22.416  1.00 28.32           N
ANISOU 4979  N   VAL A 608     3425   3058   4277    135    237    435       N
ATOM   4980  CA  VAL A 608     -69.081  12.874  21.396  1.00 30.60           C
ANISOU 4980  CA  VAL A 608     3740   3298   4591    109    219    424       C
ATOM   4981  C   VAL A 608     -68.619  13.669  20.182  1.00 36.10           C
ANISOU 4981  C   VAL A 608     4433   3992   5291     83    207    372       C
ATOM   4982  O   VAL A 608     -69.370  14.503  19.669  1.00 44.59           O
ANISOU 4982  O   VAL A 608     5496   5071   6375     55    206    376       O
ATOM   4983  CB  VAL A 608     -70.229  11.922  21.017  1.00 31.33           C
ANISOU 4983  CB  VAL A 608     3838   3350   4715     66    216    475       C
ATOM   4984  CG1 VAL A 608     -69.732  10.822  20.107  1.00 34.71           C
ANISOU 4984  CG1 VAL A 608     4297   3721   5168     50    192    456       C
ATOM   4985  CG2 VAL A 608     -70.872  11.332  22.273  1.00 25.86           C
ANISOU 4985  CG2 VAL A 608     3142   2672   4013     77    232    541       C
ATOM   4986  N   VAL A 609     -67.389  13.432  19.729  1.00 28.62           N
ANISOU 4986  N   VAL A 609     3497   3045   4333     93    196    324       N
ATOM   4987  CA  VAL A 609     -66.882  14.073  18.518  1.00 29.94           C
ANISOU 4987  CA  VAL A 609     3659   3220   4495     59    187    279       C
ATOM   4988  C   VAL A 609     -66.627  12.991  17.482  1.00 38.09           C
ANISOU 4988  C   VAL A 609     4706   4226   5541     42    173    258       C
ATOM   4989  O   VAL A 609     -65.886  12.035  17.745  1.00 44.11           O
ANISOU 4989  O   VAL A 609     5479   4979   6302     78    166    238       O
ATOM   4990  CB  VAL A 609     -65.609  14.894  18.773  1.00 32.69           C
ANISOU 4990  CB  VAL A 609     3996   3613   4813     76    190    231       C
ATOM   4991  CG1 VAL A 609     -65.235  15.671  17.516  1.00 24.39           C
ANISOU 4991  CG1 VAL A 609     2939   2574   3752     25    183    199       C
ATOM   4992  CG2 VAL A 609     -65.805  15.851  19.934  1.00 27.95           C
ANISOU 4992  CG2 VAL A 609     3384   3034   4200    102    199    242       C
ATOM   4993  N   SER A 610     -67.229  13.146  16.304  1.00 37.82           N
ANISOU 4993  N   SER A 610     4672   4181   5518     -7    164    258       N
ATOM   4994  CA  SER A 610     -67.079  12.184  15.219  1.00 33.24           C
ANISOU 4994  CA  SER A 610     4103   3580   4946    -26    148    229       C
ATOM   4995  C   SER A 610     -66.801  12.926  13.922  1.00 31.48           C
ANISOU 4995  C   SER A 610     3870   3393   4700    -70    144    196       C
ATOM   4996  O   SER A 610     -67.488  13.902  13.606  1.00 32.89           O
ANISOU 4996  O   SER A 610     4042   3578   4877   -104    144    224       O
ATOM   4997  CB  SER A 610     -68.337  11.321  15.070  1.00 33.34           C
ANISOU 4997  CB  SER A 610     4129   3542   4997    -50    138    270       C
ATOM   4998  OG  SER A 610     -68.435  10.775  13.764  1.00 36.12           O
ANISOU 4998  OG  SER A 610     4488   3881   5356    -83    119    237       O
ATOM   4999  N   ASP A 611     -65.808  12.469  13.168  1.00 26.95           N
ANISOU 4999  N   ASP A 611     3292   2844   4104    -68    138    137       N
ATOM   5000  CA  ASP A 611     -65.519  13.072  11.876  1.00 31.52           C
ANISOU 5000  CA  ASP A 611     3859   3469   4650   -116    136    109       C
ATOM   5001  C   ASP A 611     -65.808  12.083  10.752  1.00 34.28           C
ANISOU 5001  C   ASP A 611     4214   3806   5003   -133    119     78       C
ATOM   5002  O   ASP A 611     -66.027  10.888  10.979  1.00 35.04           O
ANISOU 5002  O   ASP A 611     4328   3855   5132   -104    106     68       O
ATOM   5003  CB  ASP A 611     -64.074  13.592  11.818  1.00 29.46           C
ANISOU 5003  CB  ASP A 611     3574   3274   4345   -111    149     60       C
ATOM   5004  CG  ASP A 611     -63.040  12.492  11.630  1.00 37.55           C
ANISOU 5004  CG  ASP A 611     4588   4323   5357    -68    145     -9       C
ATOM   5005  OD1 ASP A 611     -63.361  11.296  11.790  1.00 41.06           O
ANISOU 5005  OD1 ASP A 611     5053   4715   5834    -31    130    -16       O
ATOM   5006  OD2 ASP A 611     -61.878  12.839  11.327  1.00 34.72           O
ANISOU 5006  OD2 ASP A 611     4199   4037   4956    -71    155    -58       O
ATOM   5007  N   ILE A 612     -65.822  12.605   9.523  1.00 32.22           N
ANISOU 5007  N   ILE A 612     3944   3590   4708   -183    115     65       N
ATOM   5008  CA  ILE A 612     -66.162  11.788   8.366  1.00 31.25           C
ANISOU 5008  CA  ILE A 612     3824   3467   4580   -204     96     30       C
ATOM   5009  C   ILE A 612     -65.141  10.684   8.143  1.00 38.68           C
ANISOU 5009  C   ILE A 612     4761   4424   5511   -161     91    -50       C
ATOM   5010  O   ILE A 612     -65.443   9.686   7.479  1.00 39.20           O
ANISOU 5010  O   ILE A 612     4838   4466   5590   -158     70    -88       O
ATOM   5011  CB  ILE A 612     -66.306  12.678   7.113  1.00 31.77           C
ANISOU 5011  CB  ILE A 612     3879   3593   4599   -267     93     36       C
ATOM   5012  CG1 ILE A 612     -67.058  11.935   6.004  1.00 31.28           C
ANISOU 5012  CG1 ILE A 612     3822   3525   4536   -292     69     16       C
ATOM   5013  CG2 ILE A 612     -64.942  13.169   6.635  1.00 27.67           C
ANISOU 5013  CG2 ILE A 612     3336   3161   4019   -279    111     -9       C
ATOM   5014  CD1 ILE A 612     -67.297  12.776   4.766  1.00 28.97           C
ANISOU 5014  CD1 ILE A 612     3521   3294   4191   -353     62     30       C
ATOM   5015  N   GLU A 613     -63.933  10.833   8.692  1.00 42.45           N
ANISOU 5015  N   GLU A 613     5221   4941   5967   -123    107    -83       N
ATOM   5016  CA  GLU A 613     -62.953   9.755   8.612  1.00 37.85           C
ANISOU 5016  CA  GLU A 613     4631   4371   5379    -64     98   -163       C
ATOM   5017  C   GLU A 613     -63.396   8.562   9.448  1.00 36.38           C
ANISOU 5017  C   GLU A 613     4482   4086   5256    -11     75   -151       C
ATOM   5018  O   GLU A 613     -63.352   7.416   8.985  1.00 38.21           O
ANISOU 5018  O   GLU A 613     4730   4282   5506     17     49   -204       O
ATOM   5019  CB  GLU A 613     -61.581  10.261   9.056  1.00 38.69           C
ANISOU 5019  CB  GLU A 613     4701   4553   5446    -37    119   -199       C
ATOM   5020  CG  GLU A 613     -60.984  11.291   8.108  1.00 45.69           C
ANISOU 5020  CG  GLU A 613     5549   5545   6265    -98    140   -218       C
ATOM   5021  CD  GLU A 613     -59.618  11.768   8.543  1.00 45.79           C
ANISOU 5021  CD  GLU A 613     5519   5640   6240    -80    160   -256       C
ATOM   5022  OE1 GLU A 613     -58.768  10.917   8.863  1.00 51.30           O
ANISOU 5022  OE1 GLU A 613     6199   6355   6938     -9    154   -321       O
ATOM   5023  OE2 GLU A 613     -59.393  12.995   8.575  1.00 50.58           O
ANISOU 5023  OE2 GLU A 613     6111   6290   6819   -137    178   -221       O
ATOM   5024  N   MET A 614     -63.846   8.816  10.680  1.00 37.19           N
ANISOU 5024  N   MET A 614     4600   4140   5390      1     83    -81       N
ATOM   5025  CA  MET A 614     -64.398   7.745  11.503  1.00 34.47           C
ANISOU 5025  CA  MET A 614     4294   3701   5101     36     63    -49       C
ATOM   5026  C   MET A 614     -65.609   7.111  10.842  1.00 38.28           C
ANISOU 5026  C   MET A 614     4801   4123   5620     -9     41    -31       C
ATOM   5027  O   MET A 614     -65.904   5.933  11.079  1.00 42.82           O
ANISOU 5027  O   MET A 614     5411   4617   6241     12     14    -31       O
ATOM   5028  CB  MET A 614     -64.781   8.278  12.884  1.00 30.44           C
ANISOU 5028  CB  MET A 614     3790   3173   4605     44     80     28       C
ATOM   5029  CG  MET A 614     -63.604   8.775  13.711  1.00 31.02           C
ANISOU 5029  CG  MET A 614     3841   3298   4646     93     95      9       C
ATOM   5030  SD  MET A 614     -64.145   9.711  15.150  1.00 38.41           S
ANISOU 5030  SD  MET A 614     4775   4234   5584     92    118     91       S
ATOM   5031  CE  MET A 614     -65.423   8.624  15.795  1.00 34.18           C
ANISOU 5031  CE  MET A 614     4280   3605   5101     91    104    163       C
ATOM   5032  N   GLU A 615     -66.319   7.870  10.009  1.00 41.78           N
ANISOU 5032  N   GLU A 615     5229   4601   6046    -72     48    -14       N
ATOM   5033  CA  GLU A 615     -67.507   7.336   9.357  1.00 41.08           C
ANISOU 5033  CA  GLU A 615     5154   4465   5988   -118     26      1       C
ATOM   5034  C   GLU A 615     -67.148   6.386   8.220  1.00 35.35           C
ANISOU 5034  C   GLU A 615     4437   3737   5258   -112     -3    -86       C
ATOM   5035  O   GLU A 615     -67.832   5.377   8.015  1.00 38.28           O
ANISOU 5035  O   GLU A 615     4835   4036   5674   -124    -33    -92       O
ATOM   5036  CB  GLU A 615     -68.374   8.484   8.847  1.00 40.41           C
ANISOU 5036  CB  GLU A 615     5048   4424   5883   -178     37     46       C
ATOM   5037  CG  GLU A 615     -69.656   8.038   8.186  1.00 39.92           C
ANISOU 5037  CG  GLU A 615     4992   4327   5849   -228     13     63       C
ATOM   5038  CD  GLU A 615     -70.304   9.139   7.384  1.00 45.93           C
ANISOU 5038  CD  GLU A 615     5729   5144   6577   -278     14     89       C
ATOM   5039  OE1 GLU A 615     -69.570   9.926   6.750  1.00 49.52           O
ANISOU 5039  OE1 GLU A 615     6170   5667   6979   -284     25     64       O
ATOM   5040  OE2 GLU A 615     -71.549   9.215   7.382  1.00 49.43           O
ANISOU 5040  OE2 GLU A 615     6166   5566   7048   -312      4    137       O
ATOM   5041  N   THR A 616     -66.069   6.680   7.487  1.00 34.24           N
ANISOU 5041  N   THR A 616     4271   3678   5062    -95      6   -157       N
ATOM   5042  CA  THR A 616     -65.730   5.935   6.288  1.00 43.86           C
ANISOU 5042  CA  THR A 616     5486   4918   6260    -89    -18   -250       C
ATOM   5043  C   THR A 616     -64.428   5.194   6.510  1.00 50.30           C
ANISOU 5043  C   THR A 616     6300   5741   7070     -8    -25   -331       C
ATOM   5044  O   THR A 616     -64.396   4.216   7.282  1.00 53.14           O
ANISOU 5044  O   THR A 616     6697   6009   7485     43    -50   -331       O
ATOM   5045  CB  THR A 616     -65.687   6.886   5.080  1.00 42.78           C
ANISOU 5045  CB  THR A 616     5314   4888   6053   -144     -3   -266       C
ATOM   5046  OG1 THR A 616     -64.660   7.866   5.280  1.00 38.05           O
ANISOU 5046  OG1 THR A 616     4681   4374   5400   -137     31   -266       O
ATOM   5047  CG2 THR A 616     -67.024   7.591   4.901  1.00 35.77           C
ANISOU 5047  CG2 THR A 616     4430   3986   5176   -212     -4   -184       C
ATOM   5048  N   CYS A 617     -63.324   5.598   5.878  1.00 58.74           N
ANISOU 5048  N   CYS A 617     7326   6919   8072      7     -7   -400       N
ATOM   5049  CA  CYS A 617     -62.090   4.813   5.749  1.00 70.16           C
ANISOU 5049  CA  CYS A 617     8758   8397   9503     88    -20   -504       C
ATOM   5050  C   CYS A 617     -61.346   4.575   7.081  1.00 65.28           C
ANISOU 5050  C   CYS A 617     8148   7742   8913    162    -19   -491       C
ATOM   5051  O   CYS A 617     -60.238   4.022   7.021  1.00 71.33           O
ANISOU 5051  O   CYS A 617     8894   8546   9663    237    -30   -578       O
ATOM   5052  CB  CYS A 617     -61.154   5.486   4.742  1.00 81.80           C
ANISOU 5052  CB  CYS A 617    10171  10023  10886     71      8   -572       C
ATOM   5053  SG  CYS A 617     -61.119   7.285   4.838  1.00 92.74           S
ANISOU 5053  SG  CYS A 617    11521  11499  12216    -13     57   -484       S
ATOM   5054  N   LYS A 618     -61.878   4.962   8.240  1.00 55.06           N
ANISOU 5054  N   LYS A 618     6877   6388   7655    150     -9   -392       N
ATOM   5055  CA  LYS A 618     -61.288   4.604   9.521  1.00 40.24           C
ANISOU 5055  CA  LYS A 618     5015   4470   5804    222    -16   -374       C
ATOM   5056  C   LYS A 618     -62.176   3.695  10.354  1.00 41.35           C
ANISOU 5056  C   LYS A 618     5219   4473   6020    235    -46   -310       C
ATOM   5057  O   LYS A 618     -61.692   3.123  11.340  1.00 45.38           O
ANISOU 5057  O   LYS A 618     5753   4936   6555    303    -63   -299       O
ATOM   5058  CB  LYS A 618     -60.971   5.862  10.346  1.00 37.93           C
ANISOU 5058  CB  LYS A 618     4691   4241   5480    204     23   -316       C
ATOM   5059  CG  LYS A 618     -59.702   6.565   9.951  1.00 42.38           C
ANISOU 5059  CG  LYS A 618     5193   4933   5976    213     48   -381       C
ATOM   5060  CD  LYS A 618     -59.451   7.757  10.843  1.00 27.74           C
ANISOU 5060  CD  LYS A 618     3316   3122   4101    191     79   -324       C
ATOM   5061  CE  LYS A 618     -58.060   8.304  10.608  1.00 27.96           C
ANISOU 5061  CE  LYS A 618     3281   3275   4068    203     99   -392       C
ATOM   5062  NZ  LYS A 618     -57.806   9.505  11.443  1.00 27.48           N
ANISOU 5062  NZ  LYS A 618     3200   3253   3989    174    125   -342       N
ATOM   5063  N   TYR A 619     -63.459   3.563  10.001  1.00 30.42           N
ANISOU 5063  N   TYR A 619     3861   3028   4668    167    -54   -262       N
ATOM   5064  CA  TYR A 619     -64.348   2.660  10.723  1.00 34.56           C
ANISOU 5064  CA  TYR A 619     4442   3427   5262    163    -82   -197       C
ATOM   5065  C   TYR A 619     -63.799   1.243  10.741  1.00 41.16           C
ANISOU 5065  C   TYR A 619     5322   4177   6139    237   -133   -259       C
ATOM   5066  O   TYR A 619     -64.013   0.505  11.710  1.00 40.31           O
ANISOU 5066  O   TYR A 619     5265   3972   6081    263   -158   -203       O
ATOM   5067  CB  TYR A 619     -65.747   2.675  10.097  1.00 29.93           C
ANISOU 5067  CB  TYR A 619     3866   2806   4701     75    -87   -158       C
ATOM   5068  CG  TYR A 619     -66.753   1.861  10.879  1.00 34.57           C
ANISOU 5068  CG  TYR A 619     4504   3277   5356     51   -110    -79       C
ATOM   5069  CD1 TYR A 619     -67.476   2.432  11.918  1.00 35.00           C
ANISOU 5069  CD1 TYR A 619     4553   3329   5416     18    -81     27       C
ATOM   5070  CD2 TYR A 619     -66.959   0.514  10.600  1.00 38.15           C
ANISOU 5070  CD2 TYR A 619     5008   3622   5865     60   -161   -111       C
ATOM   5071  CE1 TYR A 619     -68.382   1.690  12.646  1.00 40.23           C
ANISOU 5071  CE1 TYR A 619     5254   3900   6132    -13    -97    104       C
ATOM   5072  CE2 TYR A 619     -67.859  -0.235  11.325  1.00 38.96           C
ANISOU 5072  CE2 TYR A 619     5157   3618   6029     25   -182    -31       C
ATOM   5073  CZ  TYR A 619     -68.568   0.359  12.344  1.00 45.23           C
ANISOU 5073  CZ  TYR A 619     5939   4425   6820    -15   -147     80       C
ATOM   5074  OH  TYR A 619     -69.471  -0.378  13.069  1.00 56.91           O
ANISOU 5074  OH  TYR A 619     7459   5813   8353    -59   -164    165       O
ATOM   5075  N   TYR A 620     -63.108   0.850   9.668  1.00 50.13           N
ANISOU 5075  N   TYR A 620     6443   5351   7255    272   -153   -374       N
ATOM   5076  CA  TYR A 620     -62.426  -0.439   9.600  1.00 56.37           C
ANISOU 5076  CA  TYR A 620     7270   6068   8080    360   -206   -455       C
ATOM   5077  C   TYR A 620     -61.597  -0.701  10.853  1.00 51.68           C
ANISOU 5077  C   TYR A 620     6691   5447   7497    447   -216   -430       C
ATOM   5078  O   TYR A 620     -61.716  -1.758  11.488  1.00 52.08           O
ANISOU 5078  O   TYR A 620     6807   5372   7608    490   -263   -404       O
ATOM   5079  CB  TYR A 620     -61.544  -0.459   8.352  1.00 69.45           C
ANISOU 5079  CB  TYR A 620     8880   7823   9685    397   -208   -592       C
ATOM   5080  CG  TYR A 620     -60.817  -1.754   8.090  1.00 79.11           C
ANISOU 5080  CG  TYR A 620    10134   8985  10940    498   -266   -702       C
ATOM   5081  CD1 TYR A 620     -61.515  -2.932   7.857  1.00 81.07           C
ANISOU 5081  CD1 TYR A 620    10451   9089  11261    497   -325   -717       C
ATOM   5082  CD2 TYR A 620     -59.430  -1.793   8.057  1.00 84.84           C
ANISOU 5082  CD2 TYR A 620    10815   9797  11623    596   -267   -796       C
ATOM   5083  CE1 TYR A 620     -60.849  -4.115   7.609  1.00 85.04           C
ANISOU 5083  CE1 TYR A 620    10988   9523  11799    597   -386   -824       C
ATOM   5084  CE2 TYR A 620     -58.757  -2.971   7.810  1.00 90.56           C
ANISOU 5084  CE2 TYR A 620    11564  10466  12377    702   -325   -905       C
ATOM   5085  CZ  TYR A 620     -59.471  -4.128   7.587  1.00 88.49           C
ANISOU 5085  CZ  TYR A 620    11381  10049  12193    705   -386   -919       C
ATOM   5086  OH  TYR A 620     -58.802  -5.302   7.341  1.00 91.44           O
ANISOU 5086  OH  TYR A 620    11785  10356  12602    817   -452  -1034       O
ATOM   5087  N   ALA A 621     -60.749   0.260  11.225  1.00 48.91           N
ANISOU 5087  N   ALA A 621     6283   5213   7086    470   -175   -433       N
ATOM   5088  CA  ALA A 621     -59.873   0.069  12.373  1.00 50.39           C
ANISOU 5088  CA  ALA A 621     6477   5396   7274    557   -186   -418       C
ATOM   5089  C   ALA A 621     -60.661  -0.015  13.669  1.00 49.07           C
ANISOU 5089  C   ALA A 621     6359   5140   7145    533   -187   -287       C
ATOM   5090  O   ALA A 621     -60.302  -0.783  14.568  1.00 50.31           O
ANISOU 5090  O   ALA A 621     6560   5225   7332    604   -223   -262       O
ATOM   5091  CB  ALA A 621     -58.858   1.201  12.451  1.00 48.48           C
ANISOU 5091  CB  ALA A 621     6156   5307   6958    571   -141   -451       C
ATOM   5092  N   MET A 622     -61.715   0.795  13.801  1.00 45.49           N
ANISOU 5092  N   MET A 622     5897   4700   6687    437   -147   -201       N
ATOM   5093  CA  MET A 622     -62.561   0.715  14.986  1.00 39.72           C
ANISOU 5093  CA  MET A 622     5206   3900   5986    408   -144    -79       C
ATOM   5094  C   MET A 622     -63.165  -0.674  15.126  1.00 41.25           C
ANISOU 5094  C   MET A 622     5477   3945   6251    410   -197    -48       C
ATOM   5095  O   MET A 622     -63.206  -1.237  16.228  1.00 44.27           O
ANISOU 5095  O   MET A 622     5906   4258   6658    439   -218     26       O
ATOM   5096  CB  MET A 622     -63.653   1.780  14.920  1.00 39.41           C
ANISOU 5096  CB  MET A 622     5137   3905   5930    308    -97    -10       C
ATOM   5097  CG  MET A 622     -63.126   3.176  14.634  1.00 40.25           C
ANISOU 5097  CG  MET A 622     5177   4144   5974    294    -51    -42       C
ATOM   5098  SD  MET A 622     -64.181   4.473  15.308  1.00 39.47           S
ANISOU 5098  SD  MET A 622     5055   4085   5858    220     -3     60       S
ATOM   5099  CE  MET A 622     -65.655   4.260  14.314  1.00 46.19           C
ANISOU 5099  CE  MET A 622     5919   4887   6745    128    -10     84       C
ATOM   5100  N   ALA A 623     -63.611  -1.256  14.010  1.00 35.50           N
ANISOU 5100  N   ALA A 623     4767   3167   5556    376   -224   -103       N
ATOM   5101  CA  ALA A 623     -64.136  -2.615  14.048  1.00 38.47           C
ANISOU 5101  CA  ALA A 623     5221   3390   6007    374   -283    -85       C
ATOM   5102  C   ALA A 623     -63.047  -3.618  14.415  1.00 47.72           C
ANISOU 5102  C   ALA A 623     6437   4493   7202    492   -339   -136       C
ATOM   5103  O   ALA A 623     -63.285  -4.547  15.198  1.00 54.14           O
ANISOU 5103  O   ALA A 623     7323   5181   8068    508   -382    -69       O
ATOM   5104  CB  ALA A 623     -64.767  -2.969  12.701  1.00 34.71           C
ANISOU 5104  CB  ALA A 623     4748   2884   5555    317   -302   -152       C
ATOM   5105  N   VAL A 624     -61.845  -3.446  13.861  1.00 48.51           N
ANISOU 5105  N   VAL A 624     6494   4677   7263    576   -341   -254       N
ATOM   5106  CA  VAL A 624     -60.748  -4.364  14.165  1.00 47.86           C
ANISOU 5106  CA  VAL A 624     6443   4542   7199    703   -398   -316       C
ATOM   5107  C   VAL A 624     -60.427  -4.333  15.656  1.00 42.08           C
ANISOU 5107  C   VAL A 624     5733   3794   6460    748   -399   -218       C
ATOM   5108  O   VAL A 624     -60.302  -5.377  16.304  1.00 45.04           O
ANISOU 5108  O   VAL A 624     6183   4046   6886    806   -459   -184       O
ATOM   5109  CB  VAL A 624     -59.512  -4.031  13.310  1.00 54.01           C
ANISOU 5109  CB  VAL A 624     7150   5449   7923    779   -389   -462       C
ATOM   5110  CG1 VAL A 624     -58.286  -4.809  13.800  1.00 50.85           C
ANISOU 5110  CG1 VAL A 624     6767   5022   7532    924   -443   -524       C
ATOM   5111  CG2 VAL A 624     -59.790  -4.332  11.841  1.00 53.50           C
ANISOU 5111  CG2 VAL A 624     7077   5386   7866    749   -402   -566       C
ATOM   5112  N   TRP A 625     -60.307  -3.132  16.224  1.00 41.21           N
ANISOU 5112  N   TRP A 625     5561   3807   6288    721   -337   -171       N
ATOM   5113  CA  TRP A 625     -60.025  -3.003  17.652  1.00 48.06           C
ANISOU 5113  CA  TRP A 625     6443   4680   7139    761   -334    -81       C
ATOM   5114  C   TRP A 625     -61.149  -3.602  18.492  1.00 49.33           C
ANISOU 5114  C   TRP A 625     6680   4717   7347    701   -351     56       C
ATOM   5115  O   TRP A 625     -60.896  -4.342  19.452  1.00 45.27           O
ANISOU 5115  O   TRP A 625     6222   4125   6852    759   -393    116       O
ATOM   5116  CB  TRP A 625     -59.821  -1.533  18.020  1.00 48.67           C
ANISOU 5116  CB  TRP A 625     6439   4909   7143    729   -264    -62       C
ATOM   5117  CG  TRP A 625     -58.462  -0.976  17.709  1.00 51.98           C
ANISOU 5117  CG  TRP A 625     6786   5456   7507    802   -253   -171       C
ATOM   5118  CD1 TRP A 625     -58.122  -0.200  16.639  1.00 48.65           C
ANISOU 5118  CD1 TRP A 625     6295   5143   7047    771   -217   -258       C
ATOM   5119  CD2 TRP A 625     -57.270  -1.123  18.492  1.00 54.92           C
ANISOU 5119  CD2 TRP A 625     7143   5871   7854    911   -276   -198       C
ATOM   5120  NE1 TRP A 625     -56.792   0.136  16.701  1.00 51.76           N
ANISOU 5120  NE1 TRP A 625     6627   5646   7391    847   -214   -339       N
ATOM   5121  CE2 TRP A 625     -56.246  -0.418  17.829  1.00 54.08           C
ANISOU 5121  CE2 TRP A 625     6951   5904   7694    937   -251   -308       C
ATOM   5122  CE3 TRP A 625     -56.968  -1.786  19.686  1.00 57.11           C
ANISOU 5122  CE3 TRP A 625     7468   6087   8143    987   -318   -137       C
ATOM   5123  CZ2 TRP A 625     -54.942  -0.357  18.321  1.00 55.42           C
ANISOU 5123  CZ2 TRP A 625     7075   6156   7825   1037   -266   -365       C
ATOM   5124  CZ3 TRP A 625     -55.673  -1.725  20.171  1.00 52.91           C
ANISOU 5124  CZ3 TRP A 625     6897   5634   7572   1094   -336   -193       C
ATOM   5125  CH2 TRP A 625     -54.676  -1.019  19.488  1.00 53.23           C
ANISOU 5125  CH2 TRP A 625     6845   5817   7563   1118   -310   -310       C
ATOM   5126  N   ALA A 626     -62.402  -3.285  18.148  1.00 46.96           N
ANISOU 5126  N   ALA A 626     6377   4403   7062    584   -318    111       N
ATOM   5127  CA  ALA A 626     -63.533  -3.751  18.943  1.00 46.78           C
ANISOU 5127  CA  ALA A 626     6411   4288   7075    511   -324    245       C
ATOM   5128  C   ALA A 626     -63.638  -5.269  18.930  1.00 49.67           C
ANISOU 5128  C   ALA A 626     6873   4481   7518    534   -402    258       C
ATOM   5129  O   ALA A 626     -63.943  -5.886  19.957  1.00 49.57           O
ANISOU 5129  O   ALA A 626     6922   4385   7526    528   -427    369       O
ATOM   5130  CB  ALA A 626     -64.826  -3.123  18.427  1.00 46.83           C
ANISOU 5130  CB  ALA A 626     6385   4325   7084    385   -277    282       C
ATOM   5131  N   GLU A 627     -63.395  -5.890  17.780  1.00 49.88           N
ANISOU 5131  N   GLU A 627     6917   4449   7585    559   -445    147       N
ATOM   5132  CA  GLU A 627     -63.518  -7.337  17.681  1.00 52.54           C
ANISOU 5132  CA  GLU A 627     7351   4607   8004    580   -527    148       C
ATOM   5133  C   GLU A 627     -62.220  -8.066  17.990  1.00 60.64           C
ANISOU 5133  C   GLU A 627     8416   5585   9041    729   -591     87       C
ATOM   5134  O   GLU A 627     -62.257  -9.239  18.378  1.00 58.09           O
ANISOU 5134  O   GLU A 627     8187   5101   8782    760   -664    127       O
ATOM   5135  CB  GLU A 627     -64.015  -7.724  16.284  1.00 56.82           C
ANISOU 5135  CB  GLU A 627     7898   5100   8590    531   -549     53       C
ATOM   5136  CG  GLU A 627     -65.289  -7.007  15.866  1.00 62.04           C
ANISOU 5136  CG  GLU A 627     8516   5817   9241    390   -492    102       C
ATOM   5137  CD  GLU A 627     -66.538  -7.702  16.370  1.00 69.63           C
ANISOU 5137  CD  GLU A 627     9541   6653  10262    284   -513    226       C
ATOM   5138  OE1 GLU A 627     -66.398  -8.716  17.084  1.00 72.38           O
ANISOU 5138  OE1 GLU A 627     9975   6869  10660    315   -570    285       O
ATOM   5139  OE2 GLU A 627     -67.656  -7.237  16.058  1.00 72.19           O
ANISOU 5139  OE2 GLU A 627     9829   7015  10584    169   -474    268       O
ATOM   5140  N   GLY A 628     -61.086  -7.404  17.840  1.00 69.51           N
ANISOU 5140  N   GLY A 628     9467   6840  10103    820   -568     -6       N
ATOM   5141  CA  GLY A 628     -59.785  -8.036  18.031  1.00 74.28           C
ANISOU 5141  CA  GLY A 628    10090   7421  10711    973   -628    -83       C
ATOM   5142  C   GLY A 628     -59.274  -8.800  16.826  1.00 84.45           C
ANISOU 5142  C   GLY A 628    11390   8657  12040   1043   -684   -239       C
ATOM   5143  O   GLY A 628     -58.102  -8.693  16.468  1.00 81.78           O
ANISOU 5143  O   GLY A 628    11000   8406  11667   1155   -693   -360       O
ATOM   5144  N   ASP A 629     -60.151  -9.574  16.193  1.00107.77           N
ANISOU 5144  N   ASP A 629    14408  11475  15063    978   -722   -241       N
ATOM   5145  CA  ASP A 629     -59.798 -10.376  15.028  1.00117.79           C
ANISOU 5145  CA  ASP A 629    15697  12681  16376   1039   -781   -392       C
ATOM   5146  C   ASP A 629     -60.101  -9.577  13.765  1.00118.46           C
ANISOU 5146  C   ASP A 629    15697  12895  16416    966   -721   -483       C
ATOM   5147  O   ASP A 629     -61.264  -9.259  13.495  1.00122.61           O
ANISOU 5147  O   ASP A 629    16223  13410  16951    832   -687   -418       O
ATOM   5148  CB  ASP A 629     -60.570 -11.696  15.047  1.00124.72           C
ANISOU 5148  CB  ASP A 629    16699  13331  17359   1006   -864   -349       C
ATOM   5149  CG  ASP A 629     -60.198 -12.612  13.898  1.00131.90           C
ANISOU 5149  CG  ASP A 629    17638  14158  18320   1080   -936   -514       C
ATOM   5150  OD1 ASP A 629     -59.052 -13.107  13.873  1.00135.09           O
ANISOU 5150  OD1 ASP A 629    18048  14554  18728   1234   -990   -616       O
ATOM   5151  OD2 ASP A 629     -61.061 -12.845  13.026  1.00133.54           O
ANISOU 5151  OD2 ASP A 629    17862  14314  18564    987   -943   -546       O
ATOM   5152  N   LEU A 630     -59.057  -9.244  13.005  1.00 99.32           N
ANISOU 5152  N   LEU A 630    13197  10601  13939   1052   -709   -629       N
ATOM   5153  CA  LEU A 630     -59.259  -8.501  11.763  1.00 88.54           C
ANISOU 5153  CA  LEU A 630    11753   9366  12522    987   -656   -715       C
ATOM   5154  C   LEU A 630     -60.206  -9.195  10.790  1.00 84.90           C
ANISOU 5154  C   LEU A 630    11342   8799  12120    917   -693   -757       C
ATOM   5155  O   LEU A 630     -61.024  -8.492  10.170  1.00 81.15           O
ANISOU 5155  O   LEU A 630    10826   8393  11616    802   -642   -736       O
ATOM   5156  CB  LEU A 630     -57.909  -8.223  11.091  1.00 83.38           C
ANISOU 5156  CB  LEU A 630    11015   8864  11803   1097   -646   -872       C
ATOM   5157  CG  LEU A 630     -56.787  -7.669  11.965  1.00 85.72           C
ANISOU 5157  CG  LEU A 630    11255   9270  12043   1184   -622   -861       C
ATOM   5158  CD1 LEU A 630     -55.835  -8.782  12.395  1.00 87.19           C
ANISOU 5158  CD1 LEU A 630    11489   9366  12272   1345   -707   -926       C
ATOM   5159  CD2 LEU A 630     -56.048  -6.575  11.213  1.00 86.72           C
ANISOU 5159  CD2 LEU A 630    11260   9617  12072   1179   -553   -952       C
ATOM   5160  N   PRO A 631     -60.149 -10.517  10.580  1.00 84.09           N
ANISOU 5160  N   PRO A 631    11323   8530  12096    981   -784   -819       N
ATOM   5161  CA  PRO A 631     -61.198 -11.149   9.762  1.00 81.96           C
ANISOU 5161  CA  PRO A 631    11105   8148  11888    893   -820   -842       C
ATOM   5162  C   PRO A 631     -62.593 -10.907  10.303  1.00 79.04           C
ANISOU 5162  C   PRO A 631    10768   7715  11548    738   -792   -676       C
ATOM   5163  O   PRO A 631     -63.528 -10.691   9.522  1.00 81.01           O
ANISOU 5163  O   PRO A 631    11000   7981  11799    629   -773   -683       O
ATOM   5164  CB  PRO A 631     -60.818 -12.634   9.796  1.00 80.47           C
ANISOU 5164  CB  PRO A 631    11019   7766  11790    998   -931   -913       C
ATOM   5165  CG  PRO A 631     -59.353 -12.627   9.977  1.00 80.78           C
ANISOU 5165  CG  PRO A 631    11017   7887  11788   1163   -943  -1008       C
ATOM   5166  CD  PRO A 631     -59.055 -11.462  10.876  1.00 81.68           C
ANISOU 5166  CD  PRO A 631    11061   8147  11826   1143   -861   -900       C
ATOM   5167  N   LEU A 632     -62.756 -10.910  11.629  1.00 74.17           N
ANISOU 5167  N   LEU A 632    10192   7040  10950    725   -787   -528       N
ATOM   5168  CA  LEU A 632     -64.053 -10.626  12.229  1.00 73.70           C
ANISOU 5168  CA  LEU A 632    10150   6943  10908    580   -752   -368       C
ATOM   5169  C   LEU A 632     -64.543  -9.217  11.925  1.00 70.03           C
ANISOU 5169  C   LEU A 632     9584   6658  10364    490   -657   -339       C
ATOM   5170  O   LEU A 632     -65.691  -8.896  12.250  1.00 66.26           O
ANISOU 5170  O   LEU A 632     9106   6172   9897    369   -624   -224       O
ATOM   5171  CB  LEU A 632     -63.988 -10.836  13.742  1.00 78.13           C
ANISOU 5171  CB  LEU A 632    10765   7436  11486    598   -760   -221       C
ATOM   5172  CG  LEU A 632     -65.285 -11.271  14.424  1.00 80.78           C
ANISOU 5172  CG  LEU A 632    11165   7649  11879    468   -770    -64       C
ATOM   5173  CD1 LEU A 632     -65.867 -12.491  13.730  1.00 81.30           C
ANISOU 5173  CD1 LEU A 632    11316   7534  12041    426   -852   -108       C
ATOM   5174  CD2 LEU A 632     -65.042 -11.549  15.898  1.00 82.21           C
ANISOU 5174  CD2 LEU A 632    11401   7770  12065    503   -784     71       C
ATOM   5175  N   ALA A 633     -63.707  -8.371  11.317  1.00 69.69           N
ANISOU 5175  N   ALA A 633     9455   6779  10243    546   -613   -437       N
ATOM   5176  CA  ALA A 633     -64.160  -7.053  10.893  1.00 67.15           C
ANISOU 5176  CA  ALA A 633     9047   6616   9852    461   -532   -416       C
ATOM   5177  C   ALA A 633     -64.869  -7.101   9.547  1.00 67.52           C
ANISOU 5177  C   ALA A 633     9077   6676   9902    388   -539   -491       C
ATOM   5178  O   ALA A 633     -65.723  -6.250   9.275  1.00 69.74           O
ANISOU 5178  O   ALA A 633     9312   7033  10152    287   -489   -438       O
ATOM   5179  CB  ALA A 633     -62.984  -6.079  10.832  1.00 64.55           C
ANISOU 5179  CB  ALA A 633     8635   6456   9435    535   -483   -477       C
ATOM   5180  N   GLU A 634     -64.546  -8.087   8.701  1.00 65.42           N
ANISOU 5180  N   GLU A 634     8847   6337   9674    441   -603   -617       N
ATOM   5181  CA  GLU A 634     -65.241  -8.236   7.425  1.00 64.83           C
ANISOU 5181  CA  GLU A 634     8760   6269   9602    373   -617   -695       C
ATOM   5182  C   GLU A 634     -66.742  -8.422   7.598  1.00 62.26           C
ANISOU 5182  C   GLU A 634     8471   5853   9334    237   -624   -587       C
ATOM   5183  O   GLU A 634     -67.485  -8.307   6.616  1.00 60.72           O
ANISOU 5183  O   GLU A 634     8252   5688   9131    161   -624   -628       O
ATOM   5184  CB  GLU A 634     -64.655  -9.410   6.636  1.00 66.71           C
ANISOU 5184  CB  GLU A 634     9043   6422   9881    462   -697   -851       C
ATOM   5185  CG  GLU A 634     -63.344  -9.086   5.934  1.00 72.73           C
ANISOU 5185  CG  GLU A 634     9739   7330  10567    574   -681   -997       C
ATOM   5186  CD  GLU A 634     -63.360  -9.454   4.461  1.00 84.01           C
ANISOU 5186  CD  GLU A 634    11148   8795  11977    579   -710  -1155       C
ATOM   5187  OE1 GLU A 634     -64.019 -10.454   4.102  1.00 88.72           O
ANISOU 5187  OE1 GLU A 634    11814   9246  12651    552   -778  -1190       O
ATOM   5188  OE2 GLU A 634     -62.712  -8.746   3.661  1.00 86.77           O
ANISOU 5188  OE2 GLU A 634    11413   9323  12234    606   -666  -1243       O
ATOM   5189  N   LYS A 635     -67.196  -8.708   8.820  1.00 59.90           N
ANISOU 5189  N   LYS A 635     8223   5453   9084    205   -629   -450       N
ATOM   5190  CA  LYS A 635     -68.618  -8.709   9.134  1.00 56.94           C
ANISOU 5190  CA  LYS A 635     7862   5024   8747     68   -620   -330       C
ATOM   5191  C   LYS A 635     -69.300  -7.415   8.703  1.00 56.62           C
ANISOU 5191  C   LYS A 635     7732   5143   8639    -15   -547   -299       C
ATOM   5192  O   LYS A 635     -70.462  -7.435   8.282  1.00 60.29           O
ANISOU 5192  O   LYS A 635     8187   5594   9126   -122   -549   -269       O
ATOM   5193  CB  LYS A 635     -68.793  -8.924  10.639  1.00 57.86           C
ANISOU 5193  CB  LYS A 635     8026   5063   8897     57   -615   -180       C
ATOM   5194  CG  LYS A 635     -70.117  -9.510  11.066  1.00 65.97           C
ANISOU 5194  CG  LYS A 635     9099   5975   9991    -69   -636    -66       C
ATOM   5195  CD  LYS A 635     -70.321  -9.343  12.568  1.00 72.16           C
ANISOU 5195  CD  LYS A 635     9900   6746  10771    -90   -605     95       C
ATOM   5196  CE  LYS A 635     -69.047  -9.629  13.352  1.00 74.71           C
ANISOU 5196  CE  LYS A 635    10264   7037  11087     43   -626     90       C
ATOM   5197  NZ  LYS A 635     -68.897 -11.076  13.663  1.00 78.65           N
ANISOU 5197  NZ  LYS A 635    10877   7333  11674     69   -717    102       N
ATOM   5198  N   TYR A 636     -68.592  -6.289   8.778  1.00 54.73           N
ANISOU 5198  N   TYR A 636     7425   5053   8318     34   -486   -307       N
ATOM   5199  CA  TYR A 636     -69.183  -4.966   8.615  1.00 51.99           C
ANISOU 5199  CA  TYR A 636     7001   4845   7908    -36   -418   -254       C
ATOM   5200  C   TYR A 636     -69.152  -4.448   7.177  1.00 48.19           C
ANISOU 5200  C   TYR A 636     6465   4472   7372    -51   -409   -359       C
ATOM   5201  O   TYR A 636     -69.406  -3.258   6.965  1.00 41.63           O
ANISOU 5201  O   TYR A 636     5571   3765   6481    -89   -355   -326       O
ATOM   5202  CB  TYR A 636     -68.468  -3.949   9.519  1.00 48.72           C
ANISOU 5202  CB  TYR A 636     6546   4529   7435     15   -360   -199       C
ATOM   5203  CG  TYR A 636     -68.529  -4.229  11.011  1.00 43.04           C
ANISOU 5203  CG  TYR A 636     5869   3737   6748     26   -358    -83       C
ATOM   5204  CD1 TYR A 636     -67.740  -5.218  11.593  1.00 45.92           C
ANISOU 5204  CD1 TYR A 636     6297   3999   7152    109   -405    -97       C
ATOM   5205  CD2 TYR A 636     -69.351  -3.480  11.841  1.00 38.02           C
ANISOU 5205  CD2 TYR A 636     5205   3144   6097    -40   -309     39       C
ATOM   5206  CE1 TYR A 636     -67.788  -5.463  12.958  1.00 46.31           C
ANISOU 5206  CE1 TYR A 636     6386   3989   7222    118   -405     16       C
ATOM   5207  CE2 TYR A 636     -69.405  -3.716  13.204  1.00 39.98           C
ANISOU 5207  CE2 TYR A 636     5485   3343   6362    -32   -304    145       C
ATOM   5208  CZ  TYR A 636     -68.624  -4.707  13.757  1.00 47.22           C
ANISOU 5208  CZ  TYR A 636     6470   4158   7315     45   -352    138       C
ATOM   5209  OH  TYR A 636     -68.685  -4.936  15.114  1.00 50.43           O
ANISOU 5209  OH  TYR A 636     6910   4522   7730     51   -348    251       O
ATOM   5210  N   TYR A 637     -68.852  -5.291   6.187  1.00 49.56           N
ANISOU 5210  N   TYR A 637     6663   4603   7564    -20   -461   -483       N
ATOM   5211  CA  TYR A 637     -68.673  -4.802   4.825  1.00 49.70           C
ANISOU 5211  CA  TYR A 637     6626   4743   7516    -24   -451   -588       C
ATOM   5212  C   TYR A 637     -69.270  -5.771   3.812  1.00 52.95           C
ANISOU 5212  C   TYR A 637     7069   5079   7969    -60   -514   -677       C
ATOM   5213  O   TYR A 637     -69.324  -6.982   4.040  1.00 57.68           O
ANISOU 5213  O   TYR A 637     7740   5527   8650    -41   -576   -702       O
ATOM   5214  CB  TYR A 637     -67.188  -4.555   4.526  1.00 49.00           C
ANISOU 5214  CB  TYR A 637     6506   4749   7363     85   -436   -689       C
ATOM   5215  CG  TYR A 637     -66.628  -3.411   5.335  1.00 46.61           C
ANISOU 5215  CG  TYR A 637     6158   4546   7006    105   -371   -613       C
ATOM   5216  CD1 TYR A 637     -66.844  -2.096   4.950  1.00 42.47           C
ANISOU 5216  CD1 TYR A 637     5569   4160   6409     50   -314   -577       C
ATOM   5217  CD2 TYR A 637     -65.911  -3.644   6.501  1.00 46.09           C
ANISOU 5217  CD2 TYR A 637     6118   4431   6963    177   -371   -573       C
ATOM   5218  CE1 TYR A 637     -66.350  -1.044   5.693  1.00 40.69           C
ANISOU 5218  CE1 TYR A 637     5307   4015   6140     64   -260   -511       C
ATOM   5219  CE2 TYR A 637     -65.412  -2.597   7.253  1.00 46.41           C
ANISOU 5219  CE2 TYR A 637     6117   4563   6955    193   -316   -510       C
ATOM   5220  CZ  TYR A 637     -65.636  -1.299   6.843  1.00 46.51           C
ANISOU 5220  CZ  TYR A 637     6066   4706   6899    134   -260   -482       C
ATOM   5221  OH  TYR A 637     -65.142  -0.249   7.583  1.00 53.84           O
ANISOU 5221  OH  TYR A 637     6957   5717   7783    147   -210   -424       O
ATOM   5222  N   GLY A 638     -69.713  -5.214   2.683  1.00 50.30           N
ANISOU 5222  N   GLY A 638     6683   4852   7579   -113   -500   -722       N
ATOM   5223  CA  GLY A 638     -70.344  -5.979   1.623  1.00 47.69           C
ANISOU 5223  CA  GLY A 638     6370   4477   7274   -155   -557   -811       C
ATOM   5224  C   GLY A 638     -69.599  -5.950   0.301  1.00 54.54           C
ANISOU 5224  C   GLY A 638     7201   5454   8066   -102   -566   -965       C
ATOM   5225  O   GLY A 638     -68.429  -6.338   0.235  1.00 61.06           O
ANISOU 5225  O   GLY A 638     8035   6286   8877      2   -577  -1060       O
ATOM   5226  N   GLY A 639     -70.262  -5.493  -0.760  1.00 52.39           N
ANISOU 5226  N   GLY A 639     6886   5278   7742   -170   -561   -993       N
ATOM   5227  CA  GLY A 639     -69.680  -5.529  -2.090  1.00 46.61           C
ANISOU 5227  CA  GLY A 639     6119   4657   6932   -131   -573  -1139       C
ATOM   5228  C   GLY A 639     -69.259  -4.177  -2.632  1.00 50.33           C
ANISOU 5228  C   GLY A 639     6513   5327   7283   -138   -507  -1123       C
ATOM   5229  O   GLY A 639     -68.723  -3.344  -1.893  1.00 49.94           O
ANISOU 5229  O   GLY A 639     6440   5328   7205   -117   -452  -1043       O
ATOM   5230  N   TYR A 640     -69.500  -3.943  -3.923  1.00 51.56           N
ANISOU 5230  N   TYR A 640     6631   5597   7364   -171   -514  -1196       N
ATOM   5231  CA  TYR A 640     -69.052  -2.721  -4.578  1.00 48.49           C
ANISOU 5231  CA  TYR A 640     6173   5399   6853   -181   -458  -1186       C
ATOM   5232  C   TYR A 640     -70.106  -2.209  -5.548  1.00 49.48           C
ANISOU 5232  C   TYR A 640     6268   5602   6928   -272   -466  -1165       C
ATOM   5233  O   TYR A 640     -70.907  -2.976  -6.092  1.00 53.01           O
ANISOU 5233  O   TYR A 640     6737   5991   7413   -307   -522  -1219       O
ATOM   5234  CB  TYR A 640     -67.740  -2.933  -5.346  1.00 53.48           C
ANISOU 5234  CB  TYR A 640     6774   6143   7404    -97   -453  -1331       C
ATOM   5235  CG  TYR A 640     -66.581  -3.388  -4.493  1.00 55.78           C
ANISOU 5235  CG  TYR A 640     7083   6381   7732      6   -447  -1366       C
ATOM   5236  CD1 TYR A 640     -66.361  -4.738  -4.249  1.00 56.75           C
ANISOU 5236  CD1 TYR A 640     7262   6361   7939     77   -508  -1459       C
ATOM   5237  CD2 TYR A 640     -65.701  -2.468  -3.937  1.00 57.72           C
ANISOU 5237  CD2 TYR A 640     7289   6717   7926     33   -385  -1309       C
ATOM   5238  CE1 TYR A 640     -65.300  -5.159  -3.468  1.00 59.98           C
ANISOU 5238  CE1 TYR A 640     7688   6722   8380    179   -510  -1490       C
ATOM   5239  CE2 TYR A 640     -64.636  -2.880  -3.155  1.00 59.81           C
ANISOU 5239  CE2 TYR A 640     7563   6942   8219    129   -383  -1344       C
ATOM   5240  CZ  TYR A 640     -64.441  -4.225  -2.925  1.00 65.63           C
ANISOU 5240  CZ  TYR A 640     8356   7541   9039    206   -446  -1433       C
ATOM   5241  OH  TYR A 640     -63.383  -4.636  -2.148  1.00 74.25           O
ANISOU 5241  OH  TYR A 640     9458   8595  10159    311   -450  -1466       O
ATOM   5242  N   PHE A 641     -70.088  -0.896  -5.760  1.00 49.44           N
ANISOU 5242  N   PHE A 641     6216   5730   6839   -309   -415  -1085       N
ATOM   5243  CA  PHE A 641     -70.808  -0.285  -6.866  1.00 45.11           C
ANISOU 5243  CA  PHE A 641     5631   5294   6213   -377   -421  -1077       C
ATOM   5244  C   PHE A 641     -69.993  -0.418  -8.145  1.00 46.58           C
ANISOU 5244  C   PHE A 641     5784   5624   6291   -344   -424  -1212       C
ATOM   5245  O   PHE A 641     -68.759  -0.429  -8.121  1.00 43.80           O
ANISOU 5245  O   PHE A 641     5415   5333   5895   -278   -395  -1274       O
ATOM   5246  CB  PHE A 641     -71.075   1.195  -6.595  1.00 41.56           C
ANISOU 5246  CB  PHE A 641     5151   4923   5717   -425   -370   -936       C
ATOM   5247  CG  PHE A 641     -72.175   1.450  -5.612  1.00 49.61           C
ANISOU 5247  CG  PHE A 641     6188   5837   6823   -471   -372   -808       C
ATOM   5248  CD1 PHE A 641     -73.479   1.070  -5.893  1.00 47.95           C
ANISOU 5248  CD1 PHE A 641     5983   5578   6656   -531   -416   -794       C
ATOM   5249  CD2 PHE A 641     -71.911   2.093  -4.413  1.00 52.69           C
ANISOU 5249  CD2 PHE A 641     6585   6190   7246   -455   -328   -706       C
ATOM   5250  CE1 PHE A 641     -74.495   1.313  -4.991  1.00 42.89           C
ANISOU 5250  CE1 PHE A 641     5348   4858   6089   -574   -414   -680       C
ATOM   5251  CE2 PHE A 641     -72.927   2.340  -3.504  1.00 52.04           C
ANISOU 5251  CE2 PHE A 641     6512   6026   7235   -494   -327   -594       C
ATOM   5252  CZ  PHE A 641     -74.220   1.949  -3.795  1.00 46.59           C
ANISOU 5252  CZ  PHE A 641     5822   5294   6586   -553   -368   -580       C
ATOM   5253  N   TYR A 642     -70.693  -0.512  -9.271  1.00 45.80           N
ANISOU 5253  N   TYR A 642     5669   5591   6143   -392   -458  -1260       N
ATOM   5254  CA  TYR A 642     -70.020  -0.595 -10.560  1.00 47.06           C
ANISOU 5254  CA  TYR A 642     5791   5906   6183   -368   -461  -1387       C
ATOM   5255  C   TYR A 642     -70.778   0.219 -11.595  1.00 49.05           C
ANISOU 5255  C   TYR A 642     6008   6289   6340   -445   -465  -1343       C
ATOM   5256  O   TYR A 642     -72.012   0.254 -11.591  1.00 44.14           O
ANISOU 5256  O   TYR A 642     5398   5609   5764   -506   -498  -1281       O
ATOM   5257  CB  TYR A 642     -69.866  -2.051 -11.039  1.00 42.59           C
ANISOU 5257  CB  TYR A 642     5249   5277   5655   -315   -522  -1561       C
ATOM   5258  CG  TYR A 642     -71.164  -2.816 -11.231  1.00 45.72           C
ANISOU 5258  CG  TYR A 642     5682   5559   6132   -369   -591  -1578       C
ATOM   5259  CD1 TYR A 642     -71.929  -2.655 -12.383  1.00 45.17           C
ANISOU 5259  CD1 TYR A 642     5583   5588   5990   -428   -620  -1610       C
ATOM   5260  CD2 TYR A 642     -71.610  -3.720 -10.272  1.00 46.00           C
ANISOU 5260  CD2 TYR A 642     5776   5391   6311   -364   -628  -1562       C
ATOM   5261  CE1 TYR A 642     -73.111  -3.354 -12.563  1.00 51.29           C
ANISOU 5261  CE1 TYR A 642     6384   6266   6839   -482   -685  -1630       C
ATOM   5262  CE2 TYR A 642     -72.792  -4.428 -10.447  1.00 47.90           C
ANISOU 5262  CE2 TYR A 642     6044   5529   6625   -425   -691  -1577       C
ATOM   5263  CZ  TYR A 642     -73.535  -4.242 -11.595  1.00 48.15           C
ANISOU 5263  CZ  TYR A 642     6042   5665   6586   -484   -720  -1614       C
ATOM   5264  OH  TYR A 642     -74.706  -4.938 -11.783  1.00 43.85           O
ANISOU 5264  OH  TYR A 642     5519   5027   6114   -550   -784  -1634       O
ATOM   5265  N   TYR A 643     -70.027   0.875 -12.475  1.00 48.83           N
ANISOU 5265  N   TYR A 643     5934   6444   6175   -443   -431  -1372       N
ATOM   5266  CA  TYR A 643     -70.581   1.581 -13.623  1.00 49.93           C
ANISOU 5266  CA  TYR A 643     6041   6729   6202   -508   -438  -1345       C
ATOM   5267  C   TYR A 643     -70.495   0.635 -14.815  1.00 53.54           C
ANISOU 5267  C   TYR A 643     6483   7263   6598   -486   -483  -1519       C
ATOM   5268  O   TYR A 643     -69.396   0.289 -15.263  1.00 57.40           O
ANISOU 5268  O   TYR A 643     6946   7846   7017   -428   -465  -1637       O
ATOM   5269  CB  TYR A 643     -69.827   2.886 -13.876  1.00 52.71           C
ANISOU 5269  CB  TYR A 643     6355   7237   6436   -530   -376  -1263       C
ATOM   5270  CG  TYR A 643     -70.480   3.778 -14.907  1.00 55.07           C
ANISOU 5270  CG  TYR A 643     6630   7668   6625   -603   -386  -1196       C
ATOM   5271  CD1 TYR A 643     -71.842   4.046 -14.855  1.00 50.21           C
ANISOU 5271  CD1 TYR A 643     6032   6987   6059   -656   -425  -1107       C
ATOM   5272  CD2 TYR A 643     -69.738   4.347 -15.936  1.00 56.71           C
ANISOU 5272  CD2 TYR A 643     6795   8075   6677   -620   -356  -1219       C
ATOM   5273  CE1 TYR A 643     -72.449   4.857 -15.796  1.00 52.82           C
ANISOU 5273  CE1 TYR A 643     6343   7436   6289   -715   -441  -1044       C
ATOM   5274  CE2 TYR A 643     -70.337   5.160 -16.886  1.00 57.32           C
ANISOU 5274  CE2 TYR A 643     6857   8272   6650   -687   -370  -1149       C
ATOM   5275  CZ  TYR A 643     -71.694   5.410 -16.809  1.00 59.91           C
ANISOU 5275  CZ  TYR A 643     7208   8523   7033   -730   -415  -1062       C
ATOM   5276  OH  TYR A 643     -72.304   6.217 -17.746  1.00 62.55           O
ANISOU 5276  OH  TYR A 643     7528   8974   7264   -789   -436   -989       O
ATOM   5277  N   SER A 644     -71.651   0.204 -15.317  1.00 53.62           N
ANISOU 5277  N   SER A 644     6504   7235   6633   -529   -543  -1541       N
ATOM   5278  CA  SER A 644     -71.707  -0.853 -16.313  1.00 55.46           C
ANISOU 5278  CA  SER A 644     6734   7505   6835   -507   -599  -1716       C
ATOM   5279  C   SER A 644     -71.785  -0.282 -17.719  1.00 53.98           C
ANISOU 5279  C   SER A 644     6497   7531   6482   -545   -601  -1743       C
ATOM   5280  O   SER A 644     -72.241   0.847 -17.919  1.00 51.03           O
ANISOU 5280  O   SER A 644     6105   7238   6046   -607   -581  -1607       O
ATOM   5281  CB  SER A 644     -72.919  -1.754 -16.060  1.00 60.30           C
ANISOU 5281  CB  SER A 644     7387   7951   7575   -539   -670  -1737       C
ATOM   5282  OG  SER A 644     -74.006  -1.402 -16.901  1.00 59.30           O
ANISOU 5282  OG  SER A 644     7237   7901   7393   -612   -707  -1708       O
ATOM   5283  N   PRO A 645     -71.355  -1.061 -18.732  1.00 56.91           N
ANISOU 5283  N   PRO A 645     6847   7998   6776   -506   -629  -1922       N
ATOM   5284  CA  PRO A 645     -71.413  -0.587 -20.124  1.00 55.76           C
ANISOU 5284  CA  PRO A 645     6653   8073   6460   -542   -633  -1956       C
ATOM   5285  C   PRO A 645     -72.779  -0.072 -20.547  1.00 52.06           C
ANISOU 5285  C   PRO A 645     6185   7617   5978   -627   -674  -1857       C
ATOM   5286  O   PRO A 645     -72.880   0.741 -21.470  1.00 52.96           O
ANISOU 5286  O   PRO A 645     6263   7909   5950   -670   -665  -1811       O
ATOM   5287  CB  PRO A 645     -71.023  -1.835 -20.926  1.00 55.30           C
ANISOU 5287  CB  PRO A 645     6586   8053   6371   -479   -678  -2185       C
ATOM   5288  CG  PRO A 645     -70.132  -2.588 -20.012  1.00 55.39           C
ANISOU 5288  CG  PRO A 645     6624   7934   6486   -391   -664  -2258       C
ATOM   5289  CD  PRO A 645     -70.669  -2.362 -18.625  1.00 57.06           C
ANISOU 5289  CD  PRO A 645     6886   7941   6854   -418   -656  -2101       C
ATOM   5290  N   THR A 646     -73.837  -0.532 -19.883  1.00 53.78           N
ANISOU 5290  N   THR A 646     6441   7655   6340   -653   -721  -1821       N
ATOM   5291  CA  THR A 646     -75.185  -0.075 -20.201  1.00 56.00           C
ANISOU 5291  CA  THR A 646     6715   7944   6620   -730   -763  -1729       C
ATOM   5292  C   THR A 646     -75.442   1.369 -19.790  1.00 53.51           C
ANISOU 5292  C   THR A 646     6391   7664   6278   -773   -719  -1524       C
ATOM   5293  O   THR A 646     -76.539   1.873 -20.051  1.00 51.32           O
ANISOU 5293  O   THR A 646     6104   7405   5992   -828   -753  -1439       O
ATOM   5294  CB  THR A 646     -76.216  -0.977 -19.525  1.00 55.51           C
ANISOU 5294  CB  THR A 646     6688   7681   6723   -751   -820  -1745       C
ATOM   5295  OG1 THR A 646     -76.028  -0.929 -18.104  1.00 53.90           O
ANISOU 5295  OG1 THR A 646     6518   7312   6648   -733   -783  -1651       O
ATOM   5296  CG2 THR A 646     -76.074  -2.413 -20.009  1.00 54.25           C
ANISOU 5296  CG2 THR A 646     6545   7474   6595   -715   -879  -1950       C
ATOM   5297  N   GLY A 647     -74.480   2.038 -19.157  1.00 53.30           N
ANISOU 5297  N   GLY A 647     6367   7644   6240   -747   -649  -1449       N
ATOM   5298  CA  GLY A 647     -74.685   3.387 -18.675  1.00 49.30           C
ANISOU 5298  CA  GLY A 647     5861   7148   5723   -784   -612  -1261       C
ATOM   5299  C   GLY A 647     -75.373   3.487 -17.335  1.00 51.54           C
ANISOU 5299  C   GLY A 647     6175   7245   6162   -790   -610  -1153       C
ATOM   5300  O   GLY A 647     -75.683   4.601 -16.894  1.00 53.21           O
ANISOU 5300  O   GLY A 647     6388   7453   6376   -817   -587  -1001       O
ATOM   5301  N   THR A 648     -75.623   2.364 -16.673  1.00 50.25           N
ANISOU 5301  N   THR A 648     6038   6928   6128   -768   -636  -1226       N
ATOM   5302  CA  THR A 648     -76.289   2.332 -15.382  1.00 48.88           C
ANISOU 5302  CA  THR A 648     5890   6582   6100   -778   -635  -1131       C
ATOM   5303  C   THR A 648     -75.328   1.847 -14.303  1.00 51.95           C
ANISOU 5303  C   THR A 648     6310   6858   6572   -720   -594  -1154       C
ATOM   5304  O   THR A 648     -74.262   1.286 -14.580  1.00 49.10           O
ANISOU 5304  O   THR A 648     5950   6530   6174   -668   -581  -1269       O
ATOM   5305  CB  THR A 648     -77.524   1.431 -15.434  1.00 47.20           C
ANISOU 5305  CB  THR A 648     5683   6277   5975   -816   -703  -1176       C
ATOM   5306  OG1 THR A 648     -77.113   0.072 -15.632  1.00 51.69           O
ANISOU 5306  OG1 THR A 648     6273   6783   6583   -783   -735  -1338       O
ATOM   5307  CG2 THR A 648     -78.422   1.851 -16.578  1.00 46.75           C
ANISOU 5307  CG2 THR A 648     5589   6347   5826   -866   -749  -1169       C
ATOM   5308  N   PHE A 649     -75.726   2.068 -13.056  1.00 53.31           N
ANISOU 5308  N   PHE A 649     6503   6901   6853   -727   -577  -1045       N
ATOM   5309  CA  PHE A 649     -74.929   1.702 -11.896  1.00 49.87           C
ANISOU 5309  CA  PHE A 649     6098   6351   6500   -675   -541  -1042       C
ATOM   5310  C   PHE A 649     -75.559   0.499 -11.213  1.00 49.13           C
ANISOU 5310  C   PHE A 649     6040   6085   6542   -679   -583  -1080       C
ATOM   5311  O   PHE A 649     -76.765   0.490 -10.948  1.00 55.27           O
ANISOU 5311  O   PHE A 649     6815   6803   7381   -734   -611  -1015       O
ATOM   5312  CB  PHE A 649     -74.822   2.868 -10.912  1.00 49.07           C
ANISOU 5312  CB  PHE A 649     5995   6234   6414   -678   -486   -889       C
ATOM   5313  CG  PHE A 649     -74.002   4.019 -11.419  1.00 55.75           C
ANISOU 5313  CG  PHE A 649     6816   7226   7139   -674   -441   -848       C
ATOM   5314  CD1 PHE A 649     -74.559   4.967 -12.263  1.00 57.52           C
ANISOU 5314  CD1 PHE A 649     7016   7564   7273   -723   -452   -784       C
ATOM   5315  CD2 PHE A 649     -72.674   4.157 -11.045  1.00 59.30           C
ANISOU 5315  CD2 PHE A 649     7267   7700   7563   -626   -392   -870       C
ATOM   5316  CE1 PHE A 649     -73.805   6.032 -12.727  1.00 62.46           C
ANISOU 5316  CE1 PHE A 649     7626   8318   7789   -731   -414   -735       C
ATOM   5317  CE2 PHE A 649     -71.917   5.217 -11.504  1.00 61.67           C
ANISOU 5317  CE2 PHE A 649     7542   8136   7752   -637   -350   -827       C
ATOM   5318  CZ  PHE A 649     -72.482   6.157 -12.346  1.00 63.45           C
ANISOU 5318  CZ  PHE A 649     7750   8467   7891   -693   -361   -756       C
ATOM   5319  N   GLY A 650     -74.739  -0.511 -10.932  1.00 47.13           N
ANISOU 5319  N   GLY A 650     5819   5754   6335   -620   -589  -1183       N
ATOM   5320  CA  GLY A 650     -75.165  -1.683 -10.205  1.00 44.24           C
ANISOU 5320  CA  GLY A 650     5498   5209   6101   -621   -629  -1213       C
ATOM   5321  C   GLY A 650     -74.369  -1.862  -8.923  1.00 46.66           C
ANISOU 5321  C   GLY A 650     5840   5408   6480   -564   -593  -1173       C
ATOM   5322  O   GLY A 650     -73.471  -1.079  -8.599  1.00 50.09           O
ANISOU 5322  O   GLY A 650     6259   5909   6863   -523   -537  -1129       O
ATOM   5323  N   TYR A 651     -74.715  -2.929  -8.203  1.00 44.61           N
ANISOU 5323  N   TYR A 651     5629   4978   6341   -566   -630  -1187       N
ATOM   5324  CA  TYR A 651     -74.089  -3.264  -6.932  1.00 42.53           C
ANISOU 5324  CA  TYR A 651     5409   4595   6158   -514   -609  -1145       C
ATOM   5325  C   TYR A 651     -73.917  -4.771  -6.873  1.00 42.49           C
ANISOU 5325  C   TYR A 651     5463   4442   6240   -481   -671  -1258       C
ATOM   5326  O   TYR A 651     -74.886  -5.515  -7.040  1.00 44.45           O
ANISOU 5326  O   TYR A 651     5734   4599   6555   -543   -727  -1277       O
ATOM   5327  CB  TYR A 651     -74.927  -2.776  -5.738  1.00 45.12           C
ANISOU 5327  CB  TYR A 651     5739   4849   6554   -567   -583   -982       C
ATOM   5328  CG  TYR A 651     -74.481  -3.327  -4.392  1.00 52.78           C
ANISOU 5328  CG  TYR A 651     6760   5677   7616   -526   -573   -937       C
ATOM   5329  CD1 TYR A 651     -75.007  -4.514  -3.890  1.00 57.44           C
ANISOU 5329  CD1 TYR A 651     7405   6103   8318   -552   -624   -946       C
ATOM   5330  CD2 TYR A 651     -73.542  -2.654  -3.620  1.00 53.09           C
ANISOU 5330  CD2 TYR A 651     6793   5747   7630   -466   -516   -882       C
ATOM   5331  CE1 TYR A 651     -74.601  -5.018  -2.667  1.00 57.28           C
ANISOU 5331  CE1 TYR A 651     7435   5954   8375   -515   -618   -896       C
ATOM   5332  CE2 TYR A 651     -73.134  -3.151  -2.394  1.00 55.49           C
ANISOU 5332  CE2 TYR A 651     7144   5931   8011   -426   -510   -840       C
ATOM   5333  CZ  TYR A 651     -73.666  -4.333  -1.924  1.00 59.25           C
ANISOU 5333  CZ  TYR A 651     7675   6245   8591   -448   -562   -843       C
ATOM   5334  OH  TYR A 651     -73.262  -4.828  -0.704  1.00 61.49           O
ANISOU 5334  OH  TYR A 651     8009   6410   8945   -409   -559   -792       O
ATOM   5335  N   ALA A 652     -72.695  -5.220  -6.632  1.00 50.48           N
ANISOU 5335  N   ALA A 652     6498   5427   7253   -385   -666  -1334       N
ATOM   5336  CA  ALA A 652     -72.402  -6.642  -6.585  1.00 54.60           C
ANISOU 5336  CA  ALA A 652     7083   5802   7859   -336   -732  -1449       C
ATOM   5337  C   ALA A 652     -71.894  -7.017  -5.204  1.00 62.96           C
ANISOU 5337  C   ALA A 652     8194   6721   9006   -285   -722  -1382       C
ATOM   5338  O   ALA A 652     -71.162  -6.250  -4.569  1.00 69.61           O
ANISOU 5338  O   ALA A 652     9013   7625   9810   -241   -662  -1314       O
ATOM   5339  CB  ALA A 652     -71.379  -7.035  -7.647  1.00 60.01           C
ANISOU 5339  CB  ALA A 652     7753   6579   8468   -249   -750  -1630       C
ATOM   5340  N   ASN A 653     -72.295  -8.200  -4.743  1.00 66.20           N
ANISOU 5340  N   ASN A 653     8677   6943   9533   -296   -786  -1398       N
ATOM   5341  CA  ASN A 653     -71.830  -8.696  -3.458  1.00 70.45           C
ANISOU 5341  CA  ASN A 653     9275   7336  10157   -246   -789  -1335       C
ATOM   5342  C   ASN A 653     -70.427  -9.273  -3.535  1.00 69.15           C
ANISOU 5342  C   ASN A 653     9134   7157   9982   -109   -808  -1463       C
ATOM   5343  O   ASN A 653     -69.732  -9.312  -2.516  1.00 67.96           O
ANISOU 5343  O   ASN A 653     9009   6951   9863    -44   -790  -1408       O
ATOM   5344  CB  ASN A 653     -72.798  -9.749  -2.921  1.00 78.91           C
ANISOU 5344  CB  ASN A 653    10420   8206  11356   -318   -853  -1292       C
ATOM   5345  CG  ASN A 653     -73.102  -9.554  -1.454  1.00 85.80           C
ANISOU 5345  CG  ASN A 653    11318   8992  12290   -351   -820  -1119       C
ATOM   5346  OD1 ASN A 653     -73.672  -8.536  -1.059  1.00 86.37           O
ANISOU 5346  OD1 ASN A 653    11338   9152  12325   -413   -760   -994       O
ATOM   5347  ND2 ASN A 653     -72.716 -10.525  -0.634  1.00 89.18           N
ANISOU 5347  ND2 ASN A 653    11827   9249  12808   -306   -863  -1111       N
ATOM   5348  N   SER A 654     -70.001  -9.721  -4.715  1.00 75.36           N
ANISOU 5348  N   SER A 654     9908   8002  10724    -59   -845  -1634       N
ATOM   5349  CA  SER A 654     -68.654 -10.224  -4.929  1.00 79.35           C
ANISOU 5349  CA  SER A 654    10419   8524  11206     80   -862  -1776       C
ATOM   5350  C   SER A 654     -68.167  -9.750  -6.289  1.00 87.14           C
ANISOU 5350  C   SER A 654    11328   9720  12061    107   -839  -1907       C
ATOM   5351  O   SER A 654     -68.962  -9.477  -7.193  1.00 89.77           O
ANISOU 5351  O   SER A 654    11631  10131  12348     26   -844  -1924       O
ATOM   5352  CB  SER A 654     -68.596 -11.751  -4.858  1.00 77.88           C
ANISOU 5352  CB  SER A 654    10325   8131  11134    134   -960  -1882       C
ATOM   5353  OG  SER A 654     -68.729 -12.310  -6.153  1.00 77.46           O
ANISOU 5353  OG  SER A 654    10265   8112  11054    141  -1014  -2053       O
ATOM   5354  N   GLN A 655     -66.840  -9.671  -6.432  1.00 90.77           N
ANISOU 5354  N   GLN A 655    11754  10278  12457    224   -816  -2001       N
ATOM   5355  CA  GLN A 655     -66.254  -9.123  -7.651  1.00 91.60           C
ANISOU 5355  CA  GLN A 655    11775  10609  12421    249   -782  -2113       C
ATOM   5356  C   GLN A 655     -66.588  -9.951  -8.887  1.00 87.03           C
ANISOU 5356  C   GLN A 655    11204  10034  11828    253   -850  -2284       C
ATOM   5357  O   GLN A 655     -66.468  -9.443 -10.007  1.00 87.01           O
ANISOU 5357  O   GLN A 655    11133  10224  11702    238   -824  -2357       O
ATOM   5358  CB  GLN A 655     -64.735  -8.999  -7.498  1.00 97.93           C
ANISOU 5358  CB  GLN A 655    12534  11511  13162    376   -748  -2189       C
ATOM   5359  CG  GLN A 655     -64.290  -7.838  -6.614  1.00100.55           C
ANISOU 5359  CG  GLN A 655    12825  11923  13456    360   -664  -2037       C
ATOM   5360  CD  GLN A 655     -62.878  -7.364  -6.927  1.00103.98           C
ANISOU 5360  CD  GLN A 655    13179  12549  13780    448   -613  -2121       C
ATOM   5361  OE1 GLN A 655     -62.457  -7.343  -8.085  1.00104.68           O
ANISOU 5361  OE1 GLN A 655    13210  12796  13768    472   -607  -2253       O
ATOM   5362  NE2 GLN A 655     -62.140  -6.981  -5.891  1.00104.18           N
ANISOU 5362  NE2 GLN A 655    13196  12569  13820    494   -575  -2046       N
ATOM   5363  N   TRP A 656     -67.012 -11.204  -8.717  1.00 83.77           N
ANISOU 5363  N   TRP A 656    10877   9415  11538    269   -938  -2349       N
ATOM   5364  CA  TRP A 656     -67.365 -12.020  -9.871  1.00 86.02           C
ANISOU 5364  CA  TRP A 656    11175   9692  11818    271  -1009  -2519       C
ATOM   5365  C   TRP A 656     -68.772 -11.736 -10.384  1.00 83.59           C
ANISOU 5365  C   TRP A 656    10861   9394  11507    125  -1021  -2454       C
ATOM   5366  O   TRP A 656     -69.088 -12.108 -11.519  1.00 85.25           O
ANISOU 5366  O   TRP A 656    11056   9661  11674    111  -1065  -2589       O
ATOM   5367  CB  TRP A 656     -67.222 -13.508  -9.536  1.00 96.07           C
ANISOU 5367  CB  TRP A 656    12546  10730  13227    348  -1109  -2628       C
ATOM   5368  CG  TRP A 656     -65.800 -14.039  -9.606  1.00105.16           C
ANISOU 5368  CG  TRP A 656    13692  11906  14358    520  -1126  -2785       C
ATOM   5369  CD1 TRP A 656     -65.209 -14.900  -8.725  1.00106.57           C
ANISOU 5369  CD1 TRP A 656    13945  11901  14645    623  -1177  -2805       C
ATOM   5370  CD2 TRP A 656     -64.807 -13.752 -10.610  1.00108.96           C
ANISOU 5370  CD2 TRP A 656    14084  12616  14699    610  -1094  -2944       C
ATOM   5371  NE1 TRP A 656     -63.917 -15.162  -9.112  1.00108.08           N
ANISOU 5371  NE1 TRP A 656    14097  12191  14777    778  -1181  -2972       N
ATOM   5372  CE2 TRP A 656     -63.645 -14.472 -10.263  1.00108.18           C
ANISOU 5372  CE2 TRP A 656    14007  12462  14636    771  -1128  -3061       C
ATOM   5373  CE3 TRP A 656     -64.787 -12.959 -11.764  1.00109.38           C
ANISOU 5373  CE3 TRP A 656    14042  12921  14596    570  -1042  -2996       C
ATOM   5374  CZ2 TRP A 656     -62.479 -14.419 -11.026  1.00106.97           C
ANISOU 5374  CZ2 TRP A 656    13773  12505  14367    892  -1106  -3233       C
ATOM   5375  CZ3 TRP A 656     -63.627 -12.908 -12.519  1.00106.73           C
ANISOU 5375  CZ3 TRP A 656    13631  12780  14143    682  -1018  -3158       C
ATOM   5376  CH2 TRP A 656     -62.491 -13.634 -12.147  1.00106.46           C
ANISOU 5376  CH2 TRP A 656    13611  12693  14147    841  -1048  -3279       C
ATOM   5377  N   ASP A 657     -69.619 -11.090  -9.580  1.00 77.55           N
ANISOU 5377  N   ASP A 657    10101   8581  10783     20   -984  -2258       N
ATOM   5378  CA  ASP A 657     -70.932 -10.665 -10.046  1.00 71.14           C
ANISOU 5378  CA  ASP A 657     9268   7807   9957   -114   -987  -2186       C
ATOM   5379  C   ASP A 657     -70.875  -9.397 -10.886  1.00 63.29           C
ANISOU 5379  C   ASP A 657     8178   7062   8805   -146   -919  -2161       C
ATOM   5380  O   ASP A 657     -71.874  -9.053 -11.522  1.00 61.06           O
ANISOU 5380  O   ASP A 657     7870   6842   8489   -241   -929  -2133       O
ATOM   5381  CB  ASP A 657     -71.873 -10.438  -8.859  1.00 75.22           C
ANISOU 5381  CB  ASP A 657     9817   8190  10572   -208   -973  -1989       C
ATOM   5382  CG  ASP A 657     -72.198 -11.717  -8.118  1.00 81.44           C
ANISOU 5382  CG  ASP A 657    10703   8725  11516   -211  -1049  -1996       C
ATOM   5383  OD1 ASP A 657     -72.347 -12.766  -8.779  1.00 85.62           O
ANISOU 5383  OD1 ASP A 657    11274   9168  12090   -199  -1131  -2142       O
ATOM   5384  OD2 ASP A 657     -72.307 -11.671  -6.874  1.00 81.78           O
ANISOU 5384  OD2 ASP A 657    10783   8656  11636   -228  -1028  -1854       O
ATOM   5385  N   ILE A 658     -69.745  -8.702 -10.901  1.00 58.15           N
ANISOU 5385  N   ILE A 658     7478   6556   8059    -73   -854  -2167       N
ATOM   5386  CA  ILE A 658     -69.630  -7.448 -11.647  1.00 51.41           C
ANISOU 5386  CA  ILE A 658     6542   5937   7056   -111   -789  -2127       C
ATOM   5387  C   ILE A 658     -69.520  -7.764 -13.137  1.00 52.30           C
ANISOU 5387  C   ILE A 658     6617   6189   7066    -95   -821  -2300       C
ATOM   5388  O   ILE A 658     -68.704  -8.615 -13.522  1.00 52.05           O
ANISOU 5388  O   ILE A 658     6594   6155   7028      4   -855  -2471       O
ATOM   5389  CB  ILE A 658     -68.426  -6.649 -11.165  1.00 48.99           C
ANISOU 5389  CB  ILE A 658     6195   5735   6684    -47   -711  -2080       C
ATOM   5390  CG1 ILE A 658     -68.659  -6.169  -9.729  1.00 44.70           C
ANISOU 5390  CG1 ILE A 658     5680   5075   6227    -76   -675  -1897       C
ATOM   5391  CG2 ILE A 658     -68.157  -5.477 -12.101  1.00 50.76           C
ANISOU 5391  CG2 ILE A 658     6336   6205   6744    -81   -652  -2063       C
ATOM   5392  CD1 ILE A 658     -67.602  -5.219  -9.205  1.00 44.52           C
ANISOU 5392  CD1 ILE A 658     5615   5161   6140    -33   -598  -1830       C
ATOM   5393  N   PRO A 659     -70.310  -7.118 -13.991  1.00 53.85           N
ANISOU 5393  N   PRO A 659     6771   6511   7177   -182   -816  -2266       N
ATOM   5394  CA  PRO A 659     -70.245  -7.412 -15.426  1.00 52.92           C
ANISOU 5394  CA  PRO A 659     6618   6539   6952   -170   -849  -2430       C
ATOM   5395  C   PRO A 659     -68.916  -6.986 -16.026  1.00 52.64           C
ANISOU 5395  C   PRO A 659     6518   6710   6774    -91   -794  -2516       C
ATOM   5396  O   PRO A 659     -68.193  -6.143 -15.491  1.00 48.30           O
ANISOU 5396  O   PRO A 659     5938   6230   6183    -75   -722  -2419       O
ATOM   5397  CB  PRO A 659     -71.401  -6.594 -16.017  1.00 50.05           C
ANISOU 5397  CB  PRO A 659     6221   6270   6527   -287   -846  -2329       C
ATOM   5398  CG  PRO A 659     -72.266  -6.238 -14.854  1.00 45.09           C
ANISOU 5398  CG  PRO A 659     5626   5492   6014   -357   -835  -2143       C
ATOM   5399  CD  PRO A 659     -71.354  -6.130 -13.680  1.00 51.87           C
ANISOU 5399  CD  PRO A 659     6507   6273   6928   -292   -787  -2080       C
ATOM   5400  N   LEU A 660     -68.610  -7.587 -17.171  1.00 52.26           N
ANISOU 5400  N   LEU A 660     6445   6766   6645    -45   -831  -2705       N
ATOM   5401  CA  LEU A 660     -67.393  -7.266 -17.899  1.00 48.97           C
ANISOU 5401  CA  LEU A 660     5956   6572   6077     26   -782  -2808       C
ATOM   5402  C   LEU A 660     -67.434  -5.830 -18.408  1.00 55.14           C
ANISOU 5402  C   LEU A 660     6669   7572   6708    -56   -709  -2678       C
ATOM   5403  O   LEU A 660     -68.503  -5.258 -18.638  1.00 63.58           O
ANISOU 5403  O   LEU A 660     7741   8650   7765   -158   -717  -2565       O
ATOM   5404  CB  LEU A 660     -67.209  -8.228 -19.073  1.00 50.80           C
ANISOU 5404  CB  LEU A 660     6175   6877   6251     86   -843  -3044       C
ATOM   5405  CG  LEU A 660     -66.423  -9.526 -18.850  1.00 54.60           C
ANISOU 5405  CG  LEU A 660     6692   7238   6814    222   -896  -3234       C
ATOM   5406  CD1 LEU A 660     -66.746 -10.176 -17.508  1.00 54.31           C
ANISOU 5406  CD1 LEU A 660     6750   6907   6978    235   -937  -3158       C
ATOM   5407  CD2 LEU A 660     -66.685 -10.499 -19.988  1.00 57.80           C
ANISOU 5407  CD2 LEU A 660     7102   7671   7189    254   -976  -3452       C
ATOM   5408  N   ASN A 661     -66.244  -5.250 -18.579  1.00 57.68           N
ANISOU 5408  N   ASN A 661     6929   8072   6916    -11   -640  -2693       N
ATOM   5409  CA  ASN A 661     -66.079  -3.901 -19.124  1.00 61.70           C
ANISOU 5409  CA  ASN A 661     7373   8801   7271    -85   -569  -2580       C
ATOM   5410  C   ASN A 661     -66.766  -2.858 -18.245  1.00 64.82           C
ANISOU 5410  C   ASN A 661     7794   9109   7725   -175   -536  -2344       C
ATOM   5411  O   ASN A 661     -67.326  -1.874 -18.734  1.00 72.45           O
ANISOU 5411  O   ASN A 661     8739  10183   8608   -265   -516  -2229       O
ATOM   5412  CB  ASN A 661     -66.585  -3.819 -20.569  1.00 71.39           C
ANISOU 5412  CB  ASN A 661     8562  10203   8360   -134   -594  -2652       C
ATOM   5413  CG  ASN A 661     -66.158  -5.013 -21.408  1.00 81.47           C
ANISOU 5413  CG  ASN A 661     9825  11531   9601    -43   -645  -2902       C
ATOM   5414  OD1 ASN A 661     -64.996  -5.425 -21.385  1.00 84.78           O
ANISOU 5414  OD1 ASN A 661    10212  12011   9991     57   -623  -3027       O
ATOM   5415  ND2 ASN A 661     -67.102  -5.577 -22.156  1.00 83.84           N
ANISOU 5415  ND2 ASN A 661    10145  11809   9902    -74   -716  -2983       N
ATOM   5416  N   SER A 662     -66.721  -3.071 -16.935  1.00 61.72           N
ANISOU 5416  N   SER A 662     7451   8524   7478   -147   -534  -2274       N
ATOM   5417  CA  SER A 662     -67.329  -2.161 -15.979  1.00 60.99           C
ANISOU 5417  CA  SER A 662     7384   8339   7452   -219   -504  -2064       C
ATOM   5418  C   SER A 662     -66.254  -1.383 -15.234  1.00 56.54           C
ANISOU 5418  C   SER A 662     6793   7825   6864   -193   -430  -1985       C
ATOM   5419  O   SER A 662     -65.094  -1.794 -15.156  1.00 53.65           O
ANISOU 5419  O   SER A 662     6402   7507   6476   -107   -411  -2091       O
ATOM   5420  CB  SER A 662     -68.214  -2.920 -14.982  1.00 59.99           C
ANISOU 5420  CB  SER A 662     7331   7957   7504   -222   -557  -2026       C
ATOM   5421  OG  SER A 662     -69.383  -3.411 -15.614  1.00 63.47           O
ANISOU 5421  OG  SER A 662     7793   8355   7968   -275   -622  -2063       O
ATOM   5422  N   ILE A 663     -66.657  -0.240 -14.692  1.00 60.20           N
ANISOU 5422  N   ILE A 663     7261   8280   7333   -266   -391  -1800       N
ATOM   5423  CA  ILE A 663     -65.795   0.589 -13.860  1.00 56.58           C
ANISOU 5423  CA  ILE A 663     6784   7845   6869   -257   -325  -1704       C
ATOM   5424  C   ILE A 663     -66.183   0.303 -12.415  1.00 54.54           C
ANISOU 5424  C   ILE A 663     6585   7366   6772   -238   -338  -1621       C
ATOM   5425  O   ILE A 663     -67.228   0.752 -11.938  1.00 50.81           O
ANISOU 5425  O   ILE A 663     6144   6799   6362   -302   -347  -1491       O
ATOM   5426  CB  ILE A 663     -65.930   2.076 -14.197  1.00 48.50           C
ANISOU 5426  CB  ILE A 663     5729   6954   5743   -348   -277  -1557       C
ATOM   5427  CG1 ILE A 663     -65.921   2.284 -15.710  1.00 50.55           C
ANISOU 5427  CG1 ILE A 663     5943   7418   5846   -386   -280  -1621       C
ATOM   5428  CG2 ILE A 663     -64.815   2.866 -13.541  1.00 39.48           C
ANISOU 5428  CG2 ILE A 663     4558   5870   4573   -337   -210  -1494       C
ATOM   5429  CD1 ILE A 663     -64.610   1.939 -16.353  1.00 56.57           C
ANISOU 5429  CD1 ILE A 663     6645   8350   6500   -327   -250  -1767       C
ATOM   5430  N   ILE A 664     -65.346  -0.456 -11.717  1.00 53.40           N
ANISOU 5430  N   ILE A 664     6453   7144   6692   -147   -339  -1699       N
ATOM   5431  CA  ILE A 664     -65.588  -0.770 -10.313  1.00 50.92           C
ANISOU 5431  CA  ILE A 664     6195   6631   6522   -123   -350  -1622       C
ATOM   5432  C   ILE A 664     -65.149   0.419  -9.469  1.00 51.03           C
ANISOU 5432  C   ILE A 664     6190   6677   6521   -148   -285  -1480       C
ATOM   5433  O   ILE A 664     -63.981   0.818  -9.505  1.00 52.18           O
ANISOU 5433  O   ILE A 664     6288   6943   6594   -113   -240  -1510       O
ATOM   5434  CB  ILE A 664     -64.844  -2.045  -9.899  1.00 50.26           C
ANISOU 5434  CB  ILE A 664     6137   6449   6511    -10   -385  -1757       C
ATOM   5435  CG1 ILE A 664     -65.072  -3.146 -10.935  1.00 51.23           C
ANISOU 5435  CG1 ILE A 664     6269   6571   6624     22   -448  -1925       C
ATOM   5436  CG2 ILE A 664     -65.287  -2.497  -8.515  1.00 49.01           C
ANISOU 5436  CG2 ILE A 664     6047   6071   6502      4   -408  -1671       C
ATOM   5437  CD1 ILE A 664     -64.277  -4.398 -10.677  1.00 51.33           C
ANISOU 5437  CD1 ILE A 664     6308   6497   6700    144   -490  -2076       C
ATOM   5438  N   ILE A 665     -66.083   0.994  -8.718  1.00 46.78           N
ANISOU 5438  N   ILE A 665     5684   6038   6051   -209   -282  -1330       N
ATOM   5439  CA  ILE A 665     -65.743   2.089  -7.812  1.00 48.42           C
ANISOU 5439  CA  ILE A 665     5883   6256   6260   -229   -228  -1199       C
ATOM   5440  C   ILE A 665     -64.968   1.489  -6.646  1.00 52.06           C
ANISOU 5440  C   ILE A 665     6364   6614   6802   -144   -224  -1223       C
ATOM   5441  O   ILE A 665     -65.511   0.664  -5.897  1.00 54.29           O
ANISOU 5441  O   ILE A 665     6701   6730   7197   -120   -262  -1215       O
ATOM   5442  CB  ILE A 665     -66.989   2.854  -7.338  1.00 45.99           C
ANISOU 5442  CB  ILE A 665     5602   5874   6001   -307   -229  -1044       C
ATOM   5443  CG1 ILE A 665     -67.402   3.891  -8.380  1.00 51.88           C
ANISOU 5443  CG1 ILE A 665     6314   6757   6639   -385   -217   -992       C
ATOM   5444  CG2 ILE A 665     -66.718   3.560  -6.022  1.00 41.64           C
ANISOU 5444  CG2 ILE A 665     5060   5262   5499   -301   -190   -930       C
ATOM   5445  CD1 ILE A 665     -68.145   3.316  -9.557  1.00 55.33           C
ANISOU 5445  CD1 ILE A 665     6749   7231   7041   -411   -265  -1068       C
ATOM   5446  N   PRO A 666     -63.697   1.855  -6.465  1.00 54.79           N
ANISOU 5446  N   PRO A 666     6668   7057   7092   -100   -181  -1251       N
ATOM   5447  CA  PRO A 666     -62.880   1.201  -5.434  1.00 49.80           C
ANISOU 5447  CA  PRO A 666     6051   6340   6530     -7   -184  -1290       C
ATOM   5448  C   PRO A 666     -63.249   1.642  -4.029  1.00 47.88           C
ANISOU 5448  C   PRO A 666     5845   5975   6373    -22   -170  -1151       C
ATOM   5449  O   PRO A 666     -62.428   2.213  -3.307  1.00 52.49           O
ANISOU 5449  O   PRO A 666     6405   6594   6944      1   -131  -1113       O
ATOM   5450  CB  PRO A 666     -61.453   1.620  -5.802  1.00 47.82           C
ANISOU 5450  CB  PRO A 666     5728   6267   6176     30   -138  -1361       C
ATOM   5451  CG  PRO A 666     -61.615   2.923  -6.511  1.00 50.09           C
ANISOU 5451  CG  PRO A 666     5975   6699   6359    -71    -94  -1280       C
ATOM   5452  CD  PRO A 666     -62.927   2.842  -7.245  1.00 54.18           C
ANISOU 5452  CD  PRO A 666     6524   7181   6882   -136   -130  -1254       C
ATOM   5453  N   LEU A 667     -64.489   1.380  -3.635  1.00 43.56           N
ANISOU 5453  N   LEU A 667     5352   5290   5910    -63   -201  -1078       N
ATOM   5454  CA  LEU A 667     -64.954   1.671  -2.287  1.00 43.59           C
ANISOU 5454  CA  LEU A 667     5390   5175   5996    -75   -192   -952       C
ATOM   5455  C   LEU A 667     -65.799   0.497  -1.831  1.00 39.89           C
ANISOU 5455  C   LEU A 667     4985   4534   5638    -64   -247   -956       C
ATOM   5456  O   LEU A 667     -66.796   0.163  -2.480  1.00 38.90           O
ANISOU 5456  O   LEU A 667     4874   4377   5527   -116   -280   -966       O
ATOM   5457  CB  LEU A 667     -65.758   2.973  -2.238  1.00 44.81           C
ANISOU 5457  CB  LEU A 667     5532   5368   6125   -166   -161   -820       C
ATOM   5458  CG  LEU A 667     -66.502   3.236  -0.928  1.00 45.97           C
ANISOU 5458  CG  LEU A 667     5714   5396   6357   -184   -155   -695       C
ATOM   5459  CD1 LEU A 667     -65.523   3.511   0.204  1.00 39.22           C
ANISOU 5459  CD1 LEU A 667     4855   4533   5515   -129   -124   -668       C
ATOM   5460  CD2 LEU A 667     -67.497   4.385  -1.086  1.00 48.83           C
ANISOU 5460  CD2 LEU A 667     6064   5791   6698   -267   -139   -585       C
ATOM   5461  N   ARG A 668     -65.386  -0.136  -0.737  1.00 44.32           N
ANISOU 5461  N   ARG A 668     5582   4986   6272      1   -259   -949       N
ATOM   5462  CA  ARG A 668     -66.121  -1.267  -0.189  1.00 49.43           C
ANISOU 5462  CA  ARG A 668     6296   5459   7027      7   -312   -939       C
ATOM   5463  C   ARG A 668     -67.362  -0.755   0.528  1.00 54.51           C
ANISOU 5463  C   ARG A 668     6957   6036   7718    -76   -299   -793       C
ATOM   5464  O   ARG A 668     -67.259  -0.020   1.517  1.00 56.66           O
ANISOU 5464  O   ARG A 668     7222   6313   7994    -78   -260   -694       O
ATOM   5465  CB  ARG A 668     -65.235  -2.074   0.758  1.00 44.92           C
ANISOU 5465  CB  ARG A 668     5759   4796   6511    106   -331   -970       C
ATOM   5466  CG  ARG A 668     -65.939  -3.260   1.386  1.00 50.76           C
ANISOU 5466  CG  ARG A 668     6577   5344   7364    108   -389   -947       C
ATOM   5467  CD  ARG A 668     -65.670  -4.533   0.614  1.00 54.54           C
ANISOU 5467  CD  ARG A 668     7090   5761   7873    165   -455  -1094       C
ATOM   5468  NE  ARG A 668     -64.558  -5.276   1.194  1.00 65.85           N
ANISOU 5468  NE  ARG A 668     8549   7135   9336    284   -481  -1157       N
ATOM   5469  CZ  ARG A 668     -64.702  -6.291   2.040  1.00 74.77           C
ANISOU 5469  CZ  ARG A 668     9756   8088  10565    319   -534  -1131       C
ATOM   5470  NH1 ARG A 668     -65.915  -6.690   2.398  1.00 76.30           N
ANISOU 5470  NH1 ARG A 668    10004   8150  10835    234   -561  -1043       N
ATOM   5471  NH2 ARG A 668     -63.632  -6.909   2.522  1.00 77.78           N
ANISOU 5471  NH2 ARG A 668    10158   8426  10967    437   -561  -1192       N
ATOM   5472  N   ILE A 669     -68.528  -1.129   0.024  1.00 52.43           N
ANISOU 5472  N   ILE A 669     6711   5723   7488   -143   -333   -786       N
ATOM   5473  CA  ILE A 669     -69.781  -0.666   0.629  1.00 52.46           C
ANISOU 5473  CA  ILE A 669     6720   5680   7533   -224   -323   -655       C
ATOM   5474  C   ILE A 669     -70.020  -1.436   1.923  1.00 58.03           C
ANISOU 5474  C   ILE A 669     7480   6235   8335   -209   -340   -592       C
ATOM   5475  O   ILE A 669     -69.895  -2.674   1.936  1.00 62.98           O
ANISOU 5475  O   ILE A 669     8156   6751   9023   -178   -391   -655       O
ATOM   5476  CB  ILE A 669     -70.940  -0.848  -0.349  1.00 46.08           C
ANISOU 5476  CB  ILE A 669     5904   4877   6725   -301   -357   -673       C
ATOM   5477  CG1 ILE A 669     -70.719   0.022  -1.591  1.00 42.87           C
ANISOU 5477  CG1 ILE A 669     5445   4632   6212   -318   -337   -717       C
ATOM   5478  CG2 ILE A 669     -72.263  -0.521   0.323  1.00 38.61           C
ANISOU 5478  CG2 ILE A 669     4959   3881   5831   -378   -351   -547       C
ATOM   5479  CD1 ILE A 669     -70.243   1.429  -1.275  1.00 37.74           C
ANISOU 5479  CD1 ILE A 669     4756   4086   5496   -317   -277   -639       C
ATOM   5480  N   PRO A 670     -70.334  -0.765   3.028  1.00 56.07           N
ANISOU 5480  N   PRO A 670     7225   5977   8101   -228   -303   -471       N
ATOM   5481  CA  PRO A 670     -70.479  -1.474   4.300  1.00 53.57           C
ANISOU 5481  CA  PRO A 670     6958   5532   7863   -214   -315   -405       C
ATOM   5482  C   PRO A 670     -71.715  -2.356   4.316  1.00 56.68           C
ANISOU 5482  C   PRO A 670     7387   5814   8333   -288   -359   -374       C
ATOM   5483  O   PRO A 670     -72.670  -2.161   3.562  1.00 67.38           O
ANISOU 5483  O   PRO A 670     8717   7202   9681   -361   -368   -374       O
ATOM   5484  CB  PRO A 670     -70.583  -0.345   5.330  1.00 51.75           C
ANISOU 5484  CB  PRO A 670     6699   5354   7610   -223   -259   -289       C
ATOM   5485  CG  PRO A 670     -71.007   0.839   4.562  1.00 55.37           C
ANISOU 5485  CG  PRO A 670     7102   5932   8005   -271   -229   -276       C
ATOM   5486  CD  PRO A 670     -70.403   0.694   3.201  1.00 57.33           C
ANISOU 5486  CD  PRO A 670     7335   6247   8201   -252   -247   -395       C
ATOM   5487  N   SER A 671     -71.674  -3.351   5.196  1.00 50.20           N
ANISOU 5487  N   SER A 671     6627   4860   7586   -270   -389   -344       N
ATOM   5488  CA  SER A 671     -72.760  -4.305   5.323  1.00 46.72           C
ANISOU 5488  CA  SER A 671     6228   4297   7226   -346   -434   -310       C
ATOM   5489  C   SER A 671     -73.923  -3.671   6.080  1.00 48.22           C
ANISOU 5489  C   SER A 671     6386   4512   7425   -431   -396   -173       C
ATOM   5490  O   SER A 671     -73.845  -2.538   6.560  1.00 52.12           O
ANISOU 5490  O   SER A 671     6833   5102   7867   -420   -339   -111       O
ATOM   5491  CB  SER A 671     -72.272  -5.570   6.021  1.00 46.46           C
ANISOU 5491  CB  SER A 671     6277   4108   7268   -299   -482   -316       C
ATOM   5492  OG  SER A 671     -72.206  -5.374   7.422  1.00 50.24           O
ANISOU 5492  OG  SER A 671     6769   4560   7759   -289   -451   -197       O
ATOM   5493  N   GLU A 672     -75.023  -4.417   6.194  1.00 51.05           N
ANISOU 5493  N   GLU A 672     6767   4782   7849   -519   -429   -131       N
ATOM   5494  CA  GLU A 672     -76.178  -3.905   6.923  1.00 55.00           C
ANISOU 5494  CA  GLU A 672     7229   5312   8357   -601   -394     -7       C
ATOM   5495  C   GLU A 672     -75.860  -3.704   8.399  1.00 58.09           C
ANISOU 5495  C   GLU A 672     7635   5686   8750   -569   -356     98       C
ATOM   5496  O   GLU A 672     -76.433  -2.817   9.043  1.00 62.53           O
ANISOU 5496  O   GLU A 672     8147   6328   9284   -597   -306    186       O
ATOM   5497  CB  GLU A 672     -77.370  -4.848   6.755  1.00 55.73           C
ANISOU 5497  CB  GLU A 672     7339   5314   8520   -708   -440     15       C
ATOM   5498  CG  GLU A 672     -78.613  -4.402   7.510  1.00 64.06           C
ANISOU 5498  CG  GLU A 672     8346   6412   9583   -798   -404    140       C
ATOM   5499  CD  GLU A 672     -79.817  -5.281   7.247  1.00 76.11           C
ANISOU 5499  CD  GLU A 672     9877   7867  11174   -917   -448    156       C
ATOM   5500  OE1 GLU A 672     -79.655  -6.365   6.647  1.00 80.84           O
ANISOU 5500  OE1 GLU A 672    10534   8354  11825   -930   -512     80       O
ATOM   5501  OE2 GLU A 672     -80.929  -4.887   7.651  1.00 81.03           O
ANISOU 5501  OE2 GLU A 672    10442   8549  11796   -997   -421    242       O
ATOM   5502  N   LEU A 673     -74.944  -4.504   8.946  1.00 55.84           N
ANISOU 5502  N   LEU A 673     7417   5304   8497   -503   -381     85       N
ATOM   5503  CA  LEU A 673     -74.603  -4.377  10.358  1.00 53.68           C
ANISOU 5503  CA  LEU A 673     7160   5015   8220   -469   -350    183       C
ATOM   5504  C   LEU A 673     -73.994  -3.014  10.656  1.00 50.86           C
ANISOU 5504  C   LEU A 673     6746   4795   7784   -408   -288    192       C
ATOM   5505  O   LEU A 673     -74.243  -2.433  11.720  1.00 51.75           O
ANISOU 5505  O   LEU A 673     6836   4950   7877   -414   -244    288       O
ATOM   5506  CB  LEU A 673     -73.645  -5.494  10.762  1.00 53.95           C
ANISOU 5506  CB  LEU A 673     7279   4919   8299   -398   -399    156       C
ATOM   5507  CG  LEU A 673     -72.998  -5.315  12.131  1.00 60.53           C
ANISOU 5507  CG  LEU A 673     8132   5753   9115   -336   -371    238       C
ATOM   5508  CD1 LEU A 673     -73.974  -5.670  13.241  1.00 56.22           C
ANISOU 5508  CD1 LEU A 673     7605   5155   8602   -421   -363    380       C
ATOM   5509  CD2 LEU A 673     -71.736  -6.145  12.221  1.00 67.32           C
ANISOU 5509  CD2 LEU A 673     9059   6523   9997   -229   -420    172       C
ATOM   5510  N   TYR A 674     -73.195  -2.490   9.723  1.00 46.37           N
ANISOU 5510  N   TYR A 674     6152   4298   7167   -351   -284     91       N
ATOM   5511  CA  TYR A 674     -72.602  -1.166   9.880  1.00 44.14           C
ANISOU 5511  CA  TYR A 674     5817   4142   6812   -304   -229     94       C
ATOM   5512  C   TYR A 674     -73.660  -0.115  10.193  1.00 51.86           C
ANISOU 5512  C   TYR A 674     6737   5201   7766   -367   -185    179       C
ATOM   5513  O   TYR A 674     -73.488   0.708  11.099  1.00 50.43           O
ANISOU 5513  O   TYR A 674     6532   5076   7553   -341   -142    239       O
ATOM   5514  CB  TYR A 674     -71.835  -0.802   8.606  1.00 42.81           C
ANISOU 5514  CB  TYR A 674     5625   4045   6595   -265   -235    -22       C
ATOM   5515  CG  TYR A 674     -71.465   0.659   8.458  1.00 44.04           C
ANISOU 5515  CG  TYR A 674     5722   4336   6676   -248   -183    -18       C
ATOM   5516  CD1 TYR A 674     -72.342   1.566   7.874  1.00 47.25           C
ANISOU 5516  CD1 TYR A 674     6080   4818   7053   -310   -165      6       C
ATOM   5517  CD2 TYR A 674     -70.223   1.125   8.870  1.00 41.65           C
ANISOU 5517  CD2 TYR A 674     5411   4081   6333   -172   -159    -41       C
ATOM   5518  CE1 TYR A 674     -72.001   2.903   7.729  1.00 49.00           C
ANISOU 5518  CE1 TYR A 674     6258   5147   7212   -296   -125     14       C
ATOM   5519  CE2 TYR A 674     -69.873   2.457   8.726  1.00 43.11           C
ANISOU 5519  CE2 TYR A 674     5547   4379   6454   -166   -117    -36       C
ATOM   5520  CZ  TYR A 674     -70.765   3.341   8.155  1.00 45.79           C
ANISOU 5520  CZ  TYR A 674     5849   4779   6769   -230   -101     -6       C
ATOM   5521  OH  TYR A 674     -70.424   4.666   8.011  1.00 42.66           O
ANISOU 5521  OH  TYR A 674     5414   4481   6315   -226    -66      4       O
ATOM   5522  N   TYR A 675     -74.773  -0.134   9.453  1.00 47.61           N
ANISOU 5522  N   TYR A 675     6175   4674   7243   -446   -199    180       N
ATOM   5523  CA  TYR A 675     -75.781   0.912   9.593  1.00 39.40           C
ANISOU 5523  CA  TYR A 675     5072   3721   6176   -495   -163    245       C
ATOM   5524  C   TYR A 675     -76.549   0.831  10.904  1.00 33.80           C
ANISOU 5524  C   TYR A 675     4356   2995   5493   -531   -139    356       C
ATOM   5525  O   TYR A 675     -77.335   1.736  11.200  1.00 33.46           O
ANISOU 5525  O   TYR A 675     4257   3032   5426   -557   -105    409       O
ATOM   5526  CB  TYR A 675     -76.750   0.858   8.416  1.00 38.54           C
ANISOU 5526  CB  TYR A 675     4934   3635   6075   -565   -190    210       C
ATOM   5527  CG  TYR A 675     -76.089   1.133   7.087  1.00 41.60           C
ANISOU 5527  CG  TYR A 675     5316   4070   6419   -535   -207    108       C
ATOM   5528  CD1 TYR A 675     -75.919   2.435   6.632  1.00 41.26           C
ANISOU 5528  CD1 TYR A 675     5229   4137   6311   -516   -178    103       C
ATOM   5529  CD2 TYR A 675     -75.627   0.094   6.288  1.00 41.33           C
ANISOU 5529  CD2 TYR A 675     5323   3973   6407   -525   -254     15       C
ATOM   5530  CE1 TYR A 675     -75.313   2.697   5.418  1.00 33.50           C
ANISOU 5530  CE1 TYR A 675     4239   3209   5279   -497   -191     18       C
ATOM   5531  CE2 TYR A 675     -75.022   0.347   5.069  1.00 40.78           C
ANISOU 5531  CE2 TYR A 675     5243   3966   6287   -498   -266    -81       C
ATOM   5532  CZ  TYR A 675     -74.869   1.653   4.642  1.00 36.22           C
ANISOU 5532  CZ  TYR A 675     4617   3506   5638   -488   -232    -75       C
ATOM   5533  OH  TYR A 675     -74.272   1.921   3.433  1.00 42.53           O
ANISOU 5533  OH  TYR A 675     5403   4378   6378   -470   -241   -161       O
ATOM   5534  N   SER A 676     -76.345  -0.217  11.693  1.00 36.85           N
ANISOU 5534  N   SER A 676     4797   3283   5922   -530   -156    392       N
ATOM   5535  CA  SER A 676     -76.970  -0.324  13.002  1.00 41.99           C
ANISOU 5535  CA  SER A 676     5443   3927   6585   -564   -130    503       C
ATOM   5536  C   SER A 676     -76.046   0.115  14.125  1.00 45.73           C
ANISOU 5536  C   SER A 676     5928   4425   7022   -484    -97    537       C
ATOM   5537  O   SER A 676     -76.487   0.190  15.277  1.00 45.52           O
ANISOU 5537  O   SER A 676     5890   4416   6989   -502    -68    629       O
ATOM   5538  CB  SER A 676     -77.430  -1.764  13.255  1.00 38.12           C
ANISOU 5538  CB  SER A 676     5009   3311   6164   -629   -172    542       C
ATOM   5539  OG  SER A 676     -76.319  -2.637  13.345  1.00 52.31           O
ANISOU 5539  OG  SER A 676     6884   5006   7987   -565   -210    502       O
ATOM   5540  N   THR A 677     -74.785   0.406  13.817  1.00 41.57           N
ANISOU 5540  N   THR A 677     5417   3910   6467   -399   -100    464       N
ATOM   5541  CA  THR A 677     -73.813   0.730  14.843  1.00 42.24           C
ANISOU 5541  CA  THR A 677     5515   4016   6520   -321    -76    486       C
ATOM   5542  C   THR A 677     -73.883   2.211  15.207  1.00 40.11           C
ANISOU 5542  C   THR A 677     5182   3866   6191   -302    -24    504       C
ATOM   5543  O   THR A 677     -74.466   3.039  14.496  1.00 31.66           O
ANISOU 5543  O   THR A 677     4063   2860   5104   -333    -11    486       O
ATOM   5544  CB  THR A 677     -72.403   0.358  14.388  1.00 49.75           C
ANISOU 5544  CB  THR A 677     6504   4933   7466   -238   -104    395       C
ATOM   5545  OG1 THR A 677     -72.044   1.141  13.243  1.00 51.31           O
ANISOU 5545  OG1 THR A 677     6663   5204   7628   -225    -97    309       O
ATOM   5546  CG2 THR A 677     -72.334  -1.122  14.035  1.00 50.86           C
ANISOU 5546  CG2 THR A 677     6712   4943   7670   -246   -164    368       C
ATOM   5547  N   MET A 678     -73.262   2.537  16.340  1.00 39.94           N
ANISOU 5547  N   MET A 678     5164   3871   6140   -246      1    540       N
ATOM   5548  CA  MET A 678     -73.352   3.887  16.882  1.00 39.54           C
ANISOU 5548  CA  MET A 678     5060   3924   6039   -226     47    561       C
ATOM   5549  C   MET A 678     -72.730   4.912  15.942  1.00 42.37           C
ANISOU 5549  C   MET A 678     5391   4342   6366   -197     53    482       C
ATOM   5550  O   MET A 678     -73.246   6.027  15.808  1.00 45.36           O
ANISOU 5550  O   MET A 678     5724   4791   6720   -212     76    489       O
ATOM   5551  CB  MET A 678     -72.679   3.937  18.250  1.00 47.79           C
ANISOU 5551  CB  MET A 678     6119   4983   7056   -168     65    603       C
ATOM   5552  CG  MET A 678     -73.096   5.114  19.093  1.00 55.83           C
ANISOU 5552  CG  MET A 678     7086   6097   8031   -160    110    642       C
ATOM   5553  SD  MET A 678     -74.790   4.959  19.671  1.00 52.76           S
ANISOU 5553  SD  MET A 678     6661   5732   7653   -240    132    737       S
ATOM   5554  CE  MET A 678     -74.919   6.444  20.659  1.00 48.28           C
ANISOU 5554  CE  MET A 678     6034   5284   7025   -195    181    751       C
ATOM   5555  N   GLU A 679     -71.620   4.557  15.285  1.00 36.70           N
ANISOU 5555  N   GLU A 679     4699   3599   5645   -156     29    406       N
ATOM   5556  CA  GLU A 679     -70.965   5.504  14.386  1.00 30.89           C
ANISOU 5556  CA  GLU A 679     3938   2929   4872   -138     37    337       C
ATOM   5557  C   GLU A 679     -71.858   5.859  13.205  1.00 36.95           C
ANISOU 5557  C   GLU A 679     4679   3717   5642   -199     29    321       C
ATOM   5558  O   GLU A 679     -71.919   7.025  12.796  1.00 33.53           O
ANISOU 5558  O   GLU A 679     4213   3352   5175   -206     46    312       O
ATOM   5559  CB  GLU A 679     -69.631   4.942  13.894  1.00 34.98           C
ANISOU 5559  CB  GLU A 679     4480   3429   5382    -83     15    255       C
ATOM   5560  CG  GLU A 679     -68.878   5.866  12.930  1.00 27.15           C
ANISOU 5560  CG  GLU A 679     3456   2516   4343    -74     25    185       C
ATOM   5561  CD  GLU A 679     -68.614   7.247  13.514  1.00 32.79           C
ANISOU 5561  CD  GLU A 679     4138   3305   5017    -63     61    210       C
ATOM   5562  OE1 GLU A 679     -68.576   7.382  14.757  1.00 31.30           O
ANISOU 5562  OE1 GLU A 679     3952   3114   4828    -34     77    257       O
ATOM   5563  OE2 GLU A 679     -68.442   8.204  12.727  1.00 32.11           O
ANISOU 5563  OE2 GLU A 679     4025   3279   4897    -84     71    182       O
ATOM   5564  N   ALA A 680     -72.555   4.870  12.639  1.00 42.86           N
ANISOU 5564  N   ALA A 680     5446   4406   6431   -244     -1    317       N
ATOM   5565  CA  ALA A 680     -73.496   5.156  11.561  1.00 42.23           C
ANISOU 5565  CA  ALA A 680     5339   4352   6353   -304    -12    306       C
ATOM   5566  C   ALA A 680     -74.656   6.002  12.063  1.00 36.76           C
ANISOU 5566  C   ALA A 680     4603   3708   5657   -338     12    377       C
ATOM   5567  O   ALA A 680     -75.000   7.024  11.457  1.00 28.47           O
ANISOU 5567  O   ALA A 680     3518   2719   4579   -350     18    370       O
ATOM   5568  CB  ALA A 680     -74.014   3.859  10.946  1.00 28.64           C
ANISOU 5568  CB  ALA A 680     3646   2554   4680   -349    -54    284       C
ATOM   5569  N   LYS A 681     -75.268   5.588  13.177  1.00 44.11           N
ANISOU 5569  N   LYS A 681     5534   4614   6612   -353     25    447       N
ATOM   5570  CA  LYS A 681     -76.384   6.341  13.740  1.00 40.73           C
ANISOU 5570  CA  LYS A 681     5056   4243   6177   -378     51    509       C
ATOM   5571  C   LYS A 681     -76.000   7.786  14.012  1.00 44.18           C
ANISOU 5571  C   LYS A 681     5465   4753   6569   -329     78    503       C
ATOM   5572  O   LYS A 681     -76.833   8.689  13.864  1.00 37.29           O
ANISOU 5572  O   LYS A 681     4548   3934   5686   -341     86    520       O
ATOM   5573  CB  LYS A 681     -76.873   5.679  15.030  1.00 35.70           C
ANISOU 5573  CB  LYS A 681     4422   3583   5559   -395     67    585       C
ATOM   5574  CG  LYS A 681     -77.486   4.306  14.837  1.00 42.67           C
ANISOU 5574  CG  LYS A 681     5331   4389   6493   -462     38    608       C
ATOM   5575  CD  LYS A 681     -78.816   4.390  14.109  1.00 55.36           C
ANISOU 5575  CD  LYS A 681     6890   6026   8117   -536     27    615       C
ATOM   5576  CE  LYS A 681     -79.437   3.015  13.931  1.00 63.39           C
ANISOU 5576  CE  LYS A 681     7932   6963   9189   -615     -5    636       C
ATOM   5577  NZ  LYS A 681     -80.789   3.104  13.311  1.00 66.57           N
ANISOU 5577  NZ  LYS A 681     8278   7408   9607   -691    -15    645       N
ATOM   5578  N   LEU A 682     -74.739   8.024  14.383  1.00 42.57           N
ANISOU 5578  N   LEU A 682     5285   4547   6340   -271     88    475       N
ATOM   5579  CA  LEU A 682     -74.293   9.357  14.772  1.00 31.05           C
ANISOU 5579  CA  LEU A 682     3806   3147   4843   -228    111    470       C
ATOM   5580  C   LEU A 682     -73.940  10.206  13.558  1.00 31.49           C
ANISOU 5580  C   LEU A 682     3856   3232   4877   -234     99    420       C
ATOM   5581  O   LEU A 682     -74.472  11.306  13.384  1.00 39.22           O
ANISOU 5581  O   LEU A 682     4808   4252   5843   -237    102    433       O
ATOM   5582  CB  LEU A 682     -73.092   9.253  15.713  1.00 34.07           C
ANISOU 5582  CB  LEU A 682     4214   3525   5208   -171    125    461       C
ATOM   5583  CG  LEU A 682     -73.408   8.942  17.174  1.00 39.03           C
ANISOU 5583  CG  LEU A 682     4839   4154   5837   -154    147    522       C
ATOM   5584  CD1 LEU A 682     -72.122   8.723  17.977  1.00 27.99           C
ANISOU 5584  CD1 LEU A 682     3469   2750   4418    -94    151    507       C
ATOM   5585  CD2 LEU A 682     -74.248  10.057  17.771  1.00 26.16           C
ANISOU 5585  CD2 LEU A 682     3163   2589   4188   -150    172    554       C
ATOM   5586  N   HIS A 683     -73.033   9.721  12.713  1.00 31.36           N
ANISOU 5586  N   HIS A 683     3864   3198   4852   -232     82    364       N
ATOM   5587  CA  HIS A 683     -72.525  10.568  11.643  1.00 34.88           C
ANISOU 5587  CA  HIS A 683     4304   3685   5264   -239     75    322       C
ATOM   5588  C   HIS A 683     -73.319  10.443  10.353  1.00 38.59           C
ANISOU 5588  C   HIS A 683     4765   4160   5736   -289     49    311       C
ATOM   5589  O   HIS A 683     -73.431  11.427   9.611  1.00 42.61           O
ANISOU 5589  O   HIS A 683     5260   4711   6217   -304     43    308       O
ATOM   5590  CB  HIS A 683     -71.051  10.259  11.360  1.00 34.75           C
ANISOU 5590  CB  HIS A 683     4308   3674   5223   -209     75    261       C
ATOM   5591  CG  HIS A 683     -70.310  11.412  10.758  1.00 32.82           C
ANISOU 5591  CG  HIS A 683     4051   3486   4932   -211     82    235       C
ATOM   5592  ND1 HIS A 683     -69.451  12.207  11.485  1.00 32.05           N
ANISOU 5592  ND1 HIS A 683     3949   3415   4812   -180    103    233       N
ATOM   5593  CD2 HIS A 683     -70.332  11.928   9.506  1.00 33.01           C
ANISOU 5593  CD2 HIS A 683     4068   3548   4926   -249     70    214       C
ATOM   5594  CE1 HIS A 683     -68.962  13.152  10.702  1.00 33.58           C
ANISOU 5594  CE1 HIS A 683     4135   3655   4969   -204    103    215       C
ATOM   5595  NE2 HIS A 683     -69.484  13.008   9.497  1.00 32.14           N
ANISOU 5595  NE2 HIS A 683     3952   3482   4779   -245     84    207       N
ATOM   5596  N   LEU A 684     -73.869   9.266  10.060  1.00 38.18           N
ANISOU 5596  N   LEU A 684     4722   4066   5717   -317     29    304       N
ATOM   5597  CA  LEU A 684     -74.574   9.086   8.798  1.00 37.85           C
ANISOU 5597  CA  LEU A 684     4670   4036   5675   -365     -0    283       C
ATOM   5598  C   LEU A 684     -76.052   9.439   8.903  1.00 40.35           C
ANISOU 5598  C   LEU A 684     4952   4367   6012   -400     -6    338       C
ATOM   5599  O   LEU A 684     -76.599  10.081   7.999  1.00 43.79           O
ANISOU 5599  O   LEU A 684     5367   4844   6428   -424    -24    336       O
ATOM   5600  CB  LEU A 684     -74.410   7.649   8.303  1.00 37.17           C
ANISOU 5600  CB  LEU A 684     4611   3896   5616   -381    -27    235       C
ATOM   5601  CG  LEU A 684     -74.888   7.430   6.867  1.00 43.24           C
ANISOU 5601  CG  LEU A 684     5371   4684   6373   -425    -61    191       C
ATOM   5602  CD1 LEU A 684     -73.777   6.832   6.023  1.00 38.61           C
ANISOU 5602  CD1 LEU A 684     4810   4100   5762   -405    -75    104       C
ATOM   5603  CD2 LEU A 684     -76.120   6.545   6.842  1.00 51.66           C
ANISOU 5603  CD2 LEU A 684     6433   5707   7491   -477    -86    211       C
ATOM   5604  N   PHE A 685     -76.711   9.031   9.987  1.00 35.35           N
ANISOU 5604  N   PHE A 685     4308   3710   5414   -404      8    387       N
ATOM   5605  CA  PHE A 685     -78.102   9.380  10.239  1.00 33.93           C
ANISOU 5605  CA  PHE A 685     4083   3559   5249   -432      9    437       C
ATOM   5606  C   PHE A 685     -78.241  10.616  11.114  1.00 36.05           C
ANISOU 5606  C   PHE A 685     4325   3874   5499   -389     36    474       C
ATOM   5607  O   PHE A 685     -79.360  10.950  11.522  1.00 36.41           O
ANISOU 5607  O   PHE A 685     4326   3953   5556   -398     41    513       O
ATOM   5608  CB  PHE A 685     -78.833   8.201  10.881  1.00 36.58           C
ANISOU 5608  CB  PHE A 685     4414   3854   5629   -473      9    472       C
ATOM   5609  CG  PHE A 685     -78.761   6.937  10.077  1.00 33.29           C
ANISOU 5609  CG  PHE A 685     4029   3378   5241   -517    -25    432       C
ATOM   5610  CD1 PHE A 685     -79.528   6.782   8.935  1.00 36.03           C
ANISOU 5610  CD1 PHE A 685     4355   3741   5593   -566    -59    406       C
ATOM   5611  CD2 PHE A 685     -77.918   5.906  10.459  1.00 31.41           C
ANISOU 5611  CD2 PHE A 685     3842   3067   5024   -502    -29    416       C
ATOM   5612  CE1 PHE A 685     -79.461   5.618   8.189  1.00 40.66           C
ANISOU 5612  CE1 PHE A 685     4972   4271   6207   -605    -95    359       C
ATOM   5613  CE2 PHE A 685     -77.845   4.742   9.718  1.00 38.73           C
ANISOU 5613  CE2 PHE A 685     4803   3929   5982   -535    -67    370       C
ATOM   5614  CZ  PHE A 685     -78.618   4.596   8.583  1.00 40.70           C
ANISOU 5614  CZ  PHE A 685     5032   4195   6237   -588    -99    338       C
ATOM   5615  N   ASP A 686     -77.128  11.286  11.417  1.00 38.96           N
ANISOU 5615  N   ASP A 686     4717   4246   5840   -342     52    456       N
ATOM   5616  CA  ASP A 686     -77.115  12.559  12.142  1.00 38.90           C
ANISOU 5616  CA  ASP A 686     4693   4274   5814   -298     71    477       C
ATOM   5617  C   ASP A 686     -77.749  12.438  13.528  1.00 39.22           C
ANISOU 5617  C   ASP A 686     4705   4327   5868   -280     98    521       C
ATOM   5618  O   ASP A 686     -78.327  13.398  14.046  1.00 37.41           O
ANISOU 5618  O   ASP A 686     4444   4139   5632   -252    108    540       O
ATOM   5619  CB  ASP A 686     -77.790  13.665  11.324  1.00 39.92           C
ANISOU 5619  CB  ASP A 686     4799   4438   5932   -302     48    480       C
ATOM   5620  CG  ASP A 686     -76.893  14.201  10.216  1.00 48.24           C
ANISOU 5620  CG  ASP A 686     5883   5493   6954   -309     30    446       C
ATOM   5621  OD1 ASP A 686     -75.720  14.526  10.496  1.00 48.81           O
ANISOU 5621  OD1 ASP A 686     5982   5558   7006   -285     45    426       O
ATOM   5622  OD2 ASP A 686     -77.361  14.297   9.064  1.00 53.80           O
ANISOU 5622  OD2 ASP A 686     6581   6212   7648   -340     -0    440       O
ATOM   5623  N   GLY A 687     -77.627  11.262  14.147  1.00 32.89           N
ANISOU 5623  N   GLY A 687     3919   3494   5084   -295    110    538       N
ATOM   5624  CA  GLY A 687     -78.163  11.032  15.470  1.00 30.17           C
ANISOU 5624  CA  GLY A 687     3551   3170   4744   -286    138    588       C
ATOM   5625  C   GLY A 687     -79.608  10.585  15.507  1.00 37.62           C
ANISOU 5625  C   GLY A 687     4447   4138   5710   -338    137    629       C
ATOM   5626  O   GLY A 687     -80.144  10.368  16.603  1.00 40.66           O
ANISOU 5626  O   GLY A 687     4804   4555   6092   -341    165    675       O
ATOM   5627  N   SER A 688     -80.259  10.452  14.355  1.00 36.16           N
ANISOU 5627  N   SER A 688     4246   3950   5541   -383    108    613       N
ATOM   5628  CA  SER A 688     -81.628   9.964  14.334  1.00 39.98           C
ANISOU 5628  CA  SER A 688     4679   4463   6047   -440    104    648       C
ATOM   5629  C   SER A 688     -81.692   8.560  14.921  1.00 42.35           C
ANISOU 5629  C   SER A 688     5001   4716   6375   -493    111    686       C
ATOM   5630  O   SER A 688     -80.761   7.762  14.784  1.00 42.35           O
ANISOU 5630  O   SER A 688     5062   4640   6387   -494     99    668       O
ATOM   5631  CB  SER A 688     -82.174   9.969  12.907  1.00 37.24           C
ANISOU 5631  CB  SER A 688     4319   4118   5712   -480     63    617       C
ATOM   5632  OG  SER A 688     -83.537   9.587  12.884  1.00 33.99           O
ANISOU 5632  OG  SER A 688     3848   3746   5322   -536     57    646       O
ATOM   5633  N   GLY A 689     -82.799   8.269  15.598  1.00 39.60           N
ANISOU 5633  N   GLY A 689     4599   4413   6033   -535    130    739       N
ATOM   5634  CA  GLY A 689     -82.971   6.980  16.234  1.00 41.73           C
ANISOU 5634  CA  GLY A 689     4888   4639   6327   -596    137    791       C
ATOM   5635  C   GLY A 689     -82.311   6.834  17.585  1.00 47.86           C
ANISOU 5635  C   GLY A 689     5692   5412   7081   -558    171    833       C
ATOM   5636  O   GLY A 689     -82.279   5.720  18.120  1.00 56.35           O
ANISOU 5636  O   GLY A 689     6800   6436   8175   -605    171    883       O
ATOM   5637  N   LEU A 690     -81.783   7.915  18.155  1.00 45.72           N
ANISOU 5637  N   LEU A 690     5412   5191   6769   -477    195    817       N
ATOM   5638  CA  LEU A 690     -81.132   7.887  19.457  1.00 38.67           C
ANISOU 5638  CA  LEU A 690     4539   4309   5844   -433    226    850       C
ATOM   5639  C   LEU A 690     -81.890   8.777  20.430  1.00 36.78           C
ANISOU 5639  C   LEU A 690     4226   4184   5563   -404    266    875       C
ATOM   5640  O   LEU A 690     -82.401   9.835  20.051  1.00 38.17           O
ANISOU 5640  O   LEU A 690     4354   4419   5731   -374    265    839       O
ATOM   5641  CB  LEU A 690     -79.679   8.347  19.359  1.00 40.51           C
ANISOU 5641  CB  LEU A 690     4828   4503   6062   -358    218    797       C
ATOM   5642  CG  LEU A 690     -78.749   7.411  18.589  1.00 35.42           C
ANISOU 5642  CG  LEU A 690     4254   3755   5448   -369    183    766       C
ATOM   5643  CD1 LEU A 690     -77.365   8.015  18.486  1.00 30.76           C
ANISOU 5643  CD1 LEU A 690     3700   3153   4835   -295    179    708       C
ATOM   5644  CD2 LEU A 690     -78.702   6.055  19.260  1.00 36.36           C
ANISOU 5644  CD2 LEU A 690     4414   3814   5588   -406    179    824       C
ATOM   5645  N   SER A 691     -81.954   8.351  21.689  1.00 34.84           N
ANISOU 5645  N   SER A 691     3975   3973   5290   -410    298    935       N
ATOM   5646  CA  SER A 691     -82.727   9.066  22.690  1.00 42.52           C
ANISOU 5646  CA  SER A 691     4872   5068   6217   -386    340    958       C
ATOM   5647  C   SER A 691     -81.879   9.788  23.726  1.00 44.02           C
ANISOU 5647  C   SER A 691     5074   5296   6355   -298    363    942       C
ATOM   5648  O   SER A 691     -82.432  10.542  24.531  1.00 52.45           O
ANISOU 5648  O   SER A 691     6079   6470   7380   -261    395    942       O
ATOM   5649  CB  SER A 691     -83.690   8.101  23.403  1.00 48.91           C
ANISOU 5649  CB  SER A 691     5644   5923   7019   -470    365   1046       C
ATOM   5650  OG  SER A 691     -83.077   6.860  23.684  1.00 56.81           O
ANISOU 5650  OG  SER A 691     6718   6831   8035   -514    354   1100       O
ATOM   5651  N   HIS A 692     -80.560   9.593  23.727  1.00 42.76           N
ANISOU 5651  N   HIS A 692     4990   5060   6198   -260    347    921       N
ATOM   5652  CA  HIS A 692     -79.694  10.215  24.721  1.00 36.22           C
ANISOU 5652  CA  HIS A 692     4174   4268   5320   -181    365    903       C
ATOM   5653  C   HIS A 692     -78.593  11.059  24.089  1.00 41.55           C
ANISOU 5653  C   HIS A 692     4887   4897   6004   -119    341    822       C
ATOM   5654  O   HIS A 692     -77.615  11.399  24.765  1.00 43.86           O
ANISOU 5654  O   HIS A 692     5204   5197   6265    -61    346    801       O
ATOM   5655  CB  HIS A 692     -79.079   9.151  25.627  1.00 29.48           C
ANISOU 5655  CB  HIS A 692     3368   3386   4447   -191    372    965       C
ATOM   5656  CG  HIS A 692     -80.072   8.449  26.496  1.00 39.67           C
ANISOU 5656  CG  HIS A 692     4621   4738   5712   -251    403   1055       C
ATOM   5657  ND1 HIS A 692     -80.664   9.050  27.586  1.00 40.00           N
ANISOU 5657  ND1 HIS A 692     4598   4909   5693   -226    446   1074       N
ATOM   5658  CD2 HIS A 692     -80.567   7.190  26.447  1.00 39.66           C
ANISOU 5658  CD2 HIS A 692     4639   4690   5738   -340    397   1132       C
ATOM   5659  CE1 HIS A 692     -81.487   8.194  28.165  1.00 39.98           C
ANISOU 5659  CE1 HIS A 692     4569   4947   5673   -301    469   1164       C
ATOM   5660  NE2 HIS A 692     -81.444   7.057  27.495  1.00 42.06           N
ANISOU 5660  NE2 HIS A 692     4887   5100   5993   -375    438   1204       N
ATOM   5661  N   TYR A 693     -78.719  11.397  22.808  1.00 31.77           N
ANISOU 5661  N   TYR A 693     3650   3617   4803   -135    313    779       N
ATOM   5662  CA  TYR A 693     -77.695  12.159  22.109  1.00 31.73           C
ANISOU 5662  CA  TYR A 693     3681   3571   4804    -93    290    711       C
ATOM   5663  C   TYR A 693     -78.360  13.128  21.145  1.00 35.35           C
ANISOU 5663  C   TYR A 693     4108   4044   5281    -95    272    676       C
ATOM   5664  O   TYR A 693     -79.269  12.748  20.401  1.00 40.44           O
ANISOU 5664  O   TYR A 693     4729   4683   5952   -146    260    692       O
ATOM   5665  CB  TYR A 693     -76.729  11.227  21.364  1.00 26.91           C
ANISOU 5665  CB  TYR A 693     3133   2871   4220   -115    263    699       C
ATOM   5666  CG  TYR A 693     -75.993  10.275  22.284  1.00 33.22           C
ANISOU 5666  CG  TYR A 693     3971   3645   5005   -102    270    733       C
ATOM   5667  CD1 TYR A 693     -74.750  10.605  22.814  1.00 31.24           C
ANISOU 5667  CD1 TYR A 693     3747   3397   4726    -41    271    701       C
ATOM   5668  CD2 TYR A 693     -76.550   9.052  22.638  1.00 35.56           C
ANISOU 5668  CD2 TYR A 693     4277   3917   5316   -153    273    801       C
ATOM   5669  CE1 TYR A 693     -74.082   9.735  23.665  1.00 32.00           C
ANISOU 5669  CE1 TYR A 693     3878   3474   4806    -22    272    734       C
ATOM   5670  CE2 TYR A 693     -75.894   8.185  23.490  1.00 35.11           C
ANISOU 5670  CE2 TYR A 693     4262   3831   5245   -139    273    841       C
ATOM   5671  CZ  TYR A 693     -74.661   8.525  23.996  1.00 37.52           C
ANISOU 5671  CZ  TYR A 693     4594   4142   5521    -68    271    807       C
ATOM   5672  OH  TYR A 693     -74.016   7.645  24.837  1.00 40.97           O
ANISOU 5672  OH  TYR A 693     5072   4552   5943    -48    265    849       O
ATOM   5673  N   ARG A 694     -77.911  14.379  21.171  1.00 36.39           N
ANISOU 5673  N   ARG A 694     4239   4190   5396    -39    267    628       N
ATOM   5674  CA  ARG A 694     -78.367  15.406  20.248  1.00 34.11           C
ANISOU 5674  CA  ARG A 694     3935   3902   5124    -32    242    595       C
ATOM   5675  C   ARG A 694     -77.161  16.079  19.611  1.00 41.11           C
ANISOU 5675  C   ARG A 694     4871   4740   6010    -13    219    548       C
ATOM   5676  O   ARG A 694     -76.139  16.299  20.270  1.00 45.02           O
ANISOU 5676  O   ARG A 694     5390   5231   6483     21    229    527       O
ATOM   5677  CB  ARG A 694     -79.238  16.453  20.962  1.00 35.04           C
ANISOU 5677  CB  ARG A 694     3997   4091   5225     19    253    586       C
ATOM   5678  CG  ARG A 694     -78.559  17.126  22.147  1.00 36.19           C
ANISOU 5678  CG  ARG A 694     4148   4266   5336     84    271    559       C
ATOM   5679  CD  ARG A 694     -79.363  18.308  22.654  1.00 40.78           C
ANISOU 5679  CD  ARG A 694     4681   4909   5906    144    271    530       C
ATOM   5680  NE  ARG A 694     -78.740  18.944  23.811  1.00 42.72           N
ANISOU 5680  NE  ARG A 694     4930   5186   6117    207    286    496       N
ATOM   5681  CZ  ARG A 694     -79.378  19.765  24.638  1.00 43.84           C
ANISOU 5681  CZ  ARG A 694     5024   5397   6236    270    295    467       C
ATOM   5682  NH1 ARG A 694     -80.659  20.041  24.434  1.00 42.11           N
ANISOU 5682  NH1 ARG A 694     4747   5227   6028    280    292    470       N
ATOM   5683  NH2 ARG A 694     -78.742  20.306  25.670  1.00 38.08           N
ANISOU 5683  NH2 ARG A 694     4301   4695   5472    325    305    428       N
ATOM   5684  N   MET A 695     -77.272  16.390  18.324  1.00 38.03           N
ANISOU 5684  N   MET A 695     4492   4319   5639    -41    189    533       N
ATOM   5685  CA  MET A 695     -76.239  17.187  17.685  1.00 36.78           C
ANISOU 5685  CA  MET A 695     4373   4126   5474    -32    169    495       C
ATOM   5686  C   MET A 695     -76.314  18.617  18.200  1.00 37.77           C
ANISOU 5686  C   MET A 695     4490   4269   5592     21    162    472       C
ATOM   5687  O   MET A 695     -77.400  19.176  18.371  1.00 42.20           O
ANISOU 5687  O   MET A 695     5014   4859   6161     46    156    479       O
ATOM   5688  CB  MET A 695     -76.389  17.162  16.163  1.00 31.90           C
ANISOU 5688  CB  MET A 695     3770   3481   4870    -78    137    491       C
ATOM   5689  CG  MET A 695     -75.261  17.881  15.433  1.00 28.09           C
ANISOU 5689  CG  MET A 695     3327   2972   4373    -84    120    459       C
ATOM   5690  SD  MET A 695     -75.422  17.854  13.642  1.00 36.39           S
ANISOU 5690  SD  MET A 695     4394   4009   5426   -140     85    459       S
ATOM   5691  CE  MET A 695     -75.430  16.087  13.340  1.00 30.91           C
ANISOU 5691  CE  MET A 695     3699   3305   4741   -179     95    458       C
ATOM   5692  N   ILE A 696     -75.152  19.201  18.472  1.00 34.61           N
ANISOU 5692  N   ILE A 696     4122   3852   5178     41    161    440       N
ATOM   5693  CA  ILE A 696     -75.085  20.578  18.939  1.00 33.85           C
ANISOU 5693  CA  ILE A 696     4028   3756   5079     87    148    411       C
ATOM   5694  C   ILE A 696     -74.238  21.466  18.045  1.00 38.55           C
ANISOU 5694  C   ILE A 696     4665   4304   5677     65    117    389       C
ATOM   5695  O   ILE A 696     -74.365  22.699  18.131  1.00 35.48           O
ANISOU 5695  O   ILE A 696     4287   3896   5297     93     92    371       O
ATOM   5696  CB  ILE A 696     -74.575  20.648  20.394  1.00 34.12           C
ANISOU 5696  CB  ILE A 696     4053   3823   5088    136    174    390       C
ATOM   5697  CG1 ILE A 696     -73.160  20.077  20.494  1.00 34.09           C
ANISOU 5697  CG1 ILE A 696     4081   3807   5067    118    185    376       C
ATOM   5698  CG2 ILE A 696     -75.516  19.890  21.324  1.00 35.20           C
ANISOU 5698  CG2 ILE A 696     4144   4017   5213    155    205    420       C
ATOM   5699  CD1 ILE A 696     -72.522  20.264  21.859  1.00 31.39           C
ANISOU 5699  CD1 ILE A 696     3733   3498   4696    166    203    350       C
ATOM   5700  N   TYR A 697     -73.399  20.899  17.178  1.00 40.67           N
ANISOU 5700  N   TYR A 697     4960   4555   5939     14    116    390       N
ATOM   5701  CA  TYR A 697     -72.526  21.669  16.304  1.00 29.51           C
ANISOU 5701  CA  TYR A 697     3583   3112   4519    -21     93    375       C
ATOM   5702  C   TYR A 697     -71.975  20.749  15.225  1.00 29.87           C
ANISOU 5702  C   TYR A 697     3639   3160   4551    -76     96    379       C
ATOM   5703  O   TYR A 697     -71.675  19.584  15.493  1.00 35.89           O
ANISOU 5703  O   TYR A 697     4392   3937   5308    -76    119    374       O
ATOM   5704  CB  TYR A 697     -71.378  22.302  17.102  1.00 35.16           C
ANISOU 5704  CB  TYR A 697     4313   3827   5221     -3     99    338       C
ATOM   5705  CG  TYR A 697     -70.324  22.988  16.260  1.00 38.08           C
ANISOU 5705  CG  TYR A 697     4714   4174   5578    -53     81    325       C
ATOM   5706  CD1 TYR A 697     -69.239  22.280  15.753  1.00 37.57           C
ANISOU 5706  CD1 TYR A 697     4653   4133   5490    -93     96    311       C
ATOM   5707  CD2 TYR A 697     -70.404  24.346  15.990  1.00 37.26           C
ANISOU 5707  CD2 TYR A 697     4638   4031   5488    -62     46    327       C
ATOM   5708  CE1 TYR A 697     -68.276  22.904  14.990  1.00 38.88           C
ANISOU 5708  CE1 TYR A 697     4839   4296   5637   -147     84    300       C
ATOM   5709  CE2 TYR A 697     -69.445  24.976  15.230  1.00 42.92           C
ANISOU 5709  CE2 TYR A 697     5385   4731   6191   -121     30    324       C
ATOM   5710  CZ  TYR A 697     -68.381  24.251  14.735  1.00 43.72           C
ANISOU 5710  CZ  TYR A 697     5479   4870   6261   -167     52    312       C
ATOM   5711  OH  TYR A 697     -67.423  24.879  13.977  1.00 52.48           O
ANISOU 5711  OH  TYR A 697     6610   5979   7350   -233     41    311       O
ATOM   5712  N   GLU A 698     -71.850  21.273  14.009  1.00 27.33           N
ANISOU 5712  N   GLU A 698     3337   2824   4222   -120     70    386       N
ATOM   5713  CA  GLU A 698     -71.161  20.565  12.942  1.00 25.93           C
ANISOU 5713  CA  GLU A 698     3169   2662   4023   -171     73    378       C
ATOM   5714  C   GLU A 698     -70.312  21.563  12.173  1.00 35.34           C
ANISOU 5714  C   GLU A 698     4387   3850   5190   -215     56    374       C
ATOM   5715  O   GLU A 698     -70.682  22.732  12.029  1.00 41.71           O
ANISOU 5715  O   GLU A 698     5213   4628   6007   -218     28    396       O
ATOM   5716  CB  GLU A 698     -72.131  19.838  12.000  1.00 30.54           C
ANISOU 5716  CB  GLU A 698     3743   3250   4613   -195     60    399       C
ATOM   5717  CG  GLU A 698     -72.763  20.698  10.909  1.00 32.89           C
ANISOU 5717  CG  GLU A 698     4052   3539   4906   -224     23    428       C
ATOM   5718  CD  GLU A 698     -73.468  19.865   9.846  1.00 38.17           C
ANISOU 5718  CD  GLU A 698     4708   4224   5569   -256     10    438       C
ATOM   5719  OE1 GLU A 698     -73.152  18.663   9.723  1.00 40.35           O
ANISOU 5719  OE1 GLU A 698     4976   4513   5841   -269     28    414       O
ATOM   5720  OE2 GLU A 698     -74.340  20.408   9.136  1.00 41.91           O
ANISOU 5720  OE2 GLU A 698     5182   4696   6045   -266    -23    467       O
ATOM   5721  N   SER A 699     -69.160  21.097  11.701  1.00 36.60           N
ANISOU 5721  N   SER A 699     4548   4042   5319   -250     71    347       N
ATOM   5722  CA  SER A 699     -68.214  21.956  11.003  1.00 39.06           C
ANISOU 5722  CA  SER A 699     4877   4365   5598   -304     62    344       C
ATOM   5723  C   SER A 699     -68.685  22.181   9.569  1.00 38.53           C
ANISOU 5723  C   SER A 699     4824   4305   5511   -356     37    378       C
ATOM   5724  O   SER A 699     -69.762  21.738   9.161  1.00 43.84           O
ANISOU 5724  O   SER A 699     5490   4969   6196   -345     24    398       O
ATOM   5725  CB  SER A 699     -66.816  21.345  11.043  1.00 45.58           C
ANISOU 5725  CB  SER A 699     5686   5242   6392   -318     90    297       C
ATOM   5726  OG  SER A 699     -66.687  20.303  10.086  1.00 40.76           O
ANISOU 5726  OG  SER A 699     5062   4669   5756   -338     97    280       O
ATOM   5727  N   ASP A 700     -67.863  22.866   8.780  1.00 38.03           N
ANISOU 5727  N   ASP A 700     4776   4263   5409   -418     30    386       N
ATOM   5728  CA  ASP A 700     -68.133  23.039   7.364  1.00 40.00           C
ANISOU 5728  CA  ASP A 700     5039   4536   5624   -475      8    419       C
ATOM   5729  C   ASP A 700     -68.035  21.697   6.634  1.00 42.71           C
ANISOU 5729  C   ASP A 700     5354   4937   5937   -482     27    385       C
ATOM   5730  O   ASP A 700     -67.601  20.682   7.186  1.00 42.96           O
ANISOU 5730  O   ASP A 700     5361   4985   5976   -448     54    336       O
ATOM   5731  CB  ASP A 700     -67.158  24.051   6.763  1.00 45.71           C
ANISOU 5731  CB  ASP A 700     5783   5278   6307   -549      1    439       C
ATOM   5732  CG  ASP A 700     -67.658  24.644   5.462  1.00 52.14           C
ANISOU 5732  CG  ASP A 700     6626   6097   7089   -605    -34    498       C
ATOM   5733  OD1 ASP A 700     -68.860  24.482   5.147  1.00 45.42           O
ANISOU 5733  OD1 ASP A 700     5780   5222   6257   -576    -60    524       O
ATOM   5734  OD2 ASP A 700     -66.843  25.275   4.757  1.00 55.68           O
ANISOU 5734  OD2 ASP A 700     7088   6578   7490   -681    -36    520       O
ATOM   5735  N   TYR A 701     -68.446  21.707   5.367  1.00 41.31           N
ANISOU 5735  N   TYR A 701     5184   4788   5726   -525      6    409       N
ATOM   5736  CA  TYR A 701     -68.411  20.511   4.546  1.00 36.14           C
ANISOU 5736  CA  TYR A 701     4505   4187   5038   -534     16    371       C
ATOM   5737  C   TYR A 701     -66.971  20.120   4.222  1.00 37.74           C
ANISOU 5737  C   TYR A 701     4687   4464   5189   -562     47    318       C
ATOM   5738  O   TYR A 701     -66.048  20.924   4.376  1.00 37.08           O
ANISOU 5738  O   TYR A 701     4606   4399   5082   -596     58    325       O
ATOM   5739  CB  TYR A 701     -69.181  20.739   3.247  1.00 35.64           C
ANISOU 5739  CB  TYR A 701     4454   4147   4942   -574    -18    409       C
ATOM   5740  CG  TYR A 701     -70.673  20.868   3.422  1.00 39.71           C
ANISOU 5740  CG  TYR A 701     4976   4607   5505   -540    -51    448       C
ATOM   5741  CD1 TYR A 701     -71.472  19.747   3.590  1.00 33.97           C
ANISOU 5741  CD1 TYR A 701     4226   3872   4810   -506    -50    421       C
ATOM   5742  CD2 TYR A 701     -71.286  22.114   3.413  1.00 39.92           C
ANISOU 5742  CD2 TYR A 701     5031   4591   5546   -542    -87    511       C
ATOM   5743  CE1 TYR A 701     -72.836  19.864   3.745  1.00 35.31           C
ANISOU 5743  CE1 TYR A 701     4390   4007   5020   -479    -79    454       C
ATOM   5744  CE2 TYR A 701     -72.647  22.237   3.568  1.00 38.42           C
ANISOU 5744  CE2 TYR A 701     4838   4363   5397   -503   -118    540       C
ATOM   5745  CZ  TYR A 701     -73.419  21.112   3.734  1.00 37.01           C
ANISOU 5745  CZ  TYR A 701     4626   4192   5245   -474   -112    511       C
ATOM   5746  OH  TYR A 701     -74.781  21.237   3.891  1.00 39.98           O
ANISOU 5746  OH  TYR A 701     4988   4545   5659   -439   -141    538       O
ATOM   5747  N   PRO A 702     -66.749  18.877   3.791  1.00 44.16           N
ANISOU 5747  N   PRO A 702     5476   5321   5984   -548     60    259       N
ATOM   5748  CA  PRO A 702     -65.484  18.555   3.122  1.00 35.31           C
ANISOU 5748  CA  PRO A 702     4328   4293   4797   -579     84    205       C
ATOM   5749  C   PRO A 702     -65.238  19.539   1.989  1.00 40.47           C
ANISOU 5749  C   PRO A 702     4989   5007   5381   -661     75    249       C
ATOM   5750  O   PRO A 702     -66.168  19.956   1.295  1.00 50.26           O
ANISOU 5750  O   PRO A 702     6253   6231   6613   -688     45    302       O
ATOM   5751  CB  PRO A 702     -65.709  17.132   2.604  1.00 32.83           C
ANISOU 5751  CB  PRO A 702     3996   4000   4479   -548     83    142       C
ATOM   5752  CG  PRO A 702     -66.716  16.546   3.552  1.00 35.68           C
ANISOU 5752  CG  PRO A 702     4371   4267   4919   -491     71    153       C
ATOM   5753  CD  PRO A 702     -67.598  17.684   3.991  1.00 40.96           C
ANISOU 5753  CD  PRO A 702     5064   4878   5620   -501     53    233       C
ATOM   5754  N   ALA A 703     -63.970  19.919   1.813  1.00 36.97           N
ANISOU 5754  N   ALA A 703     4524   4638   4886   -705    101    229       N
ATOM   5755  CA  ALA A 703     -63.639  21.016   0.907  1.00 41.26           C
ANISOU 5755  CA  ALA A 703     5079   5234   5364   -796     95    287       C
ATOM   5756  C   ALA A 703     -64.158  20.757  -0.503  1.00 39.80           C
ANISOU 5756  C   ALA A 703     4895   5111   5116   -833     78    299       C
ATOM   5757  O   ALA A 703     -64.635  21.681  -1.177  1.00 39.92           O
ANISOU 5757  O   ALA A 703     4943   5120   5104   -890     50    379       O
ATOM   5758  CB  ALA A 703     -62.126  21.244   0.894  1.00 38.46           C
ANISOU 5758  CB  ALA A 703     4686   4972   4955   -842    131    251       C
ATOM   5759  N   GLU A 704     -64.084  19.505  -0.962  1.00 39.35           N
ANISOU 5759  N   GLU A 704     4804   5110   5036   -798     89    221       N
ATOM   5760  CA  GLU A 704     -64.547  19.189  -2.309  1.00 44.58           C
ANISOU 5760  CA  GLU A 704     5463   5842   5634   -830     72    219       C
ATOM   5761  C   GLU A 704     -66.030  19.495  -2.466  1.00 45.30           C
ANISOU 5761  C   GLU A 704     5595   5852   5765   -822     26    287       C
ATOM   5762  O   GLU A 704     -66.453  20.051  -3.485  1.00 48.70           O
ANISOU 5762  O   GLU A 704     6042   6322   6139   -875      1    342       O
ATOM   5763  CB  GLU A 704     -64.262  17.724  -2.637  1.00 44.89           C
ANISOU 5763  CB  GLU A 704     5462   5937   5655   -782     87    108       C
ATOM   5764  CG  GLU A 704     -62.815  17.319  -2.421  1.00 47.40           C
ANISOU 5764  CG  GLU A 704     5733   6339   5939   -770    129     28       C
ATOM   5765  CD  GLU A 704     -62.576  16.718  -1.050  1.00 53.54           C
ANISOU 5765  CD  GLU A 704     6507   7033   6801   -689    139    -15       C
ATOM   5766  OE1 GLU A 704     -61.746  15.790  -0.945  1.00 57.99           O
ANISOU 5766  OE1 GLU A 704     7033   7646   7354   -642    159   -109       O
ATOM   5767  OE2 GLU A 704     -63.219  17.168  -0.078  1.00 54.43           O
ANISOU 5767  OE2 GLU A 704     6656   7036   6990   -669    126     43       O
ATOM   5768  N   TRP A 705     -66.837  19.168  -1.458  1.00 38.41           N
ANISOU 5768  N   TRP A 705     4736   4872   4985   -757     14    287       N
ATOM   5769  CA  TRP A 705     -68.266  19.415  -1.586  1.00 40.55           C
ANISOU 5769  CA  TRP A 705     5034   5080   5294   -744    -30    343       C
ATOM   5770  C   TRP A 705     -68.616  20.874  -1.338  1.00 47.16           C
ANISOU 5770  C   TRP A 705     5910   5860   6148   -769    -55    439       C
ATOM   5771  O   TRP A 705     -69.551  21.394  -1.958  1.00 37.18           O
ANISOU 5771  O   TRP A 705     4668   4582   4875   -784    -97    499       O
ATOM   5772  CB  TRP A 705     -69.037  18.487  -0.652  1.00 36.59           C
ANISOU 5772  CB  TRP A 705     4525   4499   4878   -673    -32    308       C
ATOM   5773  CG  TRP A 705     -69.272  17.165  -1.310  1.00 35.66           C
ANISOU 5773  CG  TRP A 705     4384   4419   4745   -660    -36    237       C
ATOM   5774  CD1 TRP A 705     -68.473  16.060  -1.242  1.00 31.84           C
ANISOU 5774  CD1 TRP A 705     3877   3965   4254   -634    -11    148       C
ATOM   5775  CD2 TRP A 705     -70.357  16.825  -2.177  1.00 38.44           C
ANISOU 5775  CD2 TRP A 705     4735   4783   5086   -672    -74    243       C
ATOM   5776  NE1 TRP A 705     -69.006  15.045  -2.002  1.00 37.23           N
ANISOU 5776  NE1 TRP A 705     4550   4669   4928   -629    -32     96       N
ATOM   5777  CE2 TRP A 705     -70.164  15.491  -2.584  1.00 38.29           C
ANISOU 5777  CE2 TRP A 705     4695   4796   5057   -656    -69    152       C
ATOM   5778  CE3 TRP A 705     -71.480  17.517  -2.641  1.00 37.16           C
ANISOU 5778  CE3 TRP A 705     4588   4608   4923   -690   -115    313       C
ATOM   5779  CZ2 TRP A 705     -71.050  14.836  -3.433  1.00 35.15           C
ANISOU 5779  CZ2 TRP A 705     4290   4416   4648   -665   -103    128       C
ATOM   5780  CZ3 TRP A 705     -72.359  16.863  -3.483  1.00 35.78           C
ANISOU 5780  CZ3 TRP A 705     4401   4460   4734   -697   -148    291       C
ATOM   5781  CH2 TRP A 705     -72.138  15.538  -3.870  1.00 36.50           C
ANISOU 5781  CH2 TRP A 705     4471   4583   4815   -688   -141    198       C
ATOM   5782  N   LYS A 706     -67.880  21.553  -0.455  1.00 57.29           N
ANISOU 5782  N   LYS A 706     7203   7108   7456   -771    -35    452       N
ATOM   5783  CA  LYS A 706     -68.029  22.999  -0.344  1.00 52.46           C
ANISOU 5783  CA  LYS A 706     6635   6443   6854   -804    -63    537       C
ATOM   5784  C   LYS A 706     -67.796  23.666  -1.693  1.00 49.49           C
ANISOU 5784  C   LYS A 706     6278   6136   6391   -889    -82    594       C
ATOM   5785  O   LYS A 706     -68.493  24.622  -2.053  1.00 54.02           O
ANISOU 5785  O   LYS A 706     6895   6664   6967   -908   -129    676       O
ATOM   5786  CB  LYS A 706     -67.064  23.549   0.706  1.00 57.95           C
ANISOU 5786  CB  LYS A 706     7333   7106   7578   -805    -37    527       C
ATOM   5787  CG  LYS A 706     -67.275  25.015   1.041  1.00 60.15           C
ANISOU 5787  CG  LYS A 706     7663   7303   7887   -827    -72    604       C
ATOM   5788  CD  LYS A 706     -68.593  25.229   1.769  1.00 64.46           C
ANISOU 5788  CD  LYS A 706     8230   7750   8513   -750   -107    625       C
ATOM   5789  CE  LYS A 706     -68.938  26.706   1.855  1.00 64.26           C
ANISOU 5789  CE  LYS A 706     8261   7641   8513   -766   -156    701       C
ATOM   5790  NZ  LYS A 706     -67.808  27.500   2.412  1.00 61.54           N
ANISOU 5790  NZ  LYS A 706     7935   7276   8172   -810   -141    702       N
ATOM   5791  N   SER A 707     -66.833  23.155  -2.462  1.00 40.02           N
ANISOU 5791  N   SER A 707     5045   5052   5110   -937    -49    552       N
ATOM   5792  CA  SER A 707     -66.594  23.681  -3.802  1.00 36.36           C
ANISOU 5792  CA  SER A 707     4592   4677   4548  -1024    -62    605       C
ATOM   5793  C   SER A 707     -67.692  23.256  -4.772  1.00 37.61           C
ANISOU 5793  C   SER A 707     4753   4860   4676  -1011    -99    618       C
ATOM   5794  O   SER A 707     -68.087  24.033  -5.650  1.00 39.03           O
ANISOU 5794  O   SER A 707     4967   5057   4806  -1062   -137    700       O
ATOM   5795  CB  SER A 707     -65.225  23.219  -4.300  1.00 37.43           C
ANISOU 5795  CB  SER A 707     4678   4946   4598  -1075    -10    545       C
ATOM   5796  OG  SER A 707     -65.034  23.564  -5.660  1.00 46.15           O
ANISOU 5796  OG  SER A 707     5783   6158   5593  -1158    -17    590       O
ATOM   5797  N   TYR A 708     -68.183  22.020  -4.640  1.00 40.85           N
ANISOU 5797  N   TYR A 708     5131   5274   5117   -948    -92    538       N
ATOM   5798  CA  TYR A 708     -69.276  21.552  -5.489  1.00 36.82           C
ANISOU 5798  CA  TYR A 708     4619   4786   4587   -935   -131    540       C
ATOM   5799  C   TYR A 708     -70.516  22.419  -5.322  1.00 41.19           C
ANISOU 5799  C   TYR A 708     5213   5246   5191   -914   -187    628       C
ATOM   5800  O   TYR A 708     -71.249  22.663  -6.288  1.00 46.57           O
ANISOU 5800  O   TYR A 708     5907   5960   5826   -935   -231    674       O
ATOM   5801  CB  TYR A 708     -69.627  20.103  -5.156  1.00 33.96           C
ANISOU 5801  CB  TYR A 708     4219   4414   4269   -871   -118    440       C
ATOM   5802  CG  TYR A 708     -68.589  19.083  -5.531  1.00 35.89           C
ANISOU 5802  CG  TYR A 708     4422   4755   4460   -875    -76    340       C
ATOM   5803  CD1 TYR A 708     -67.606  19.368  -6.467  1.00 41.61           C
ANISOU 5803  CD1 TYR A 708     5131   5602   5076   -940    -55    337       C
ATOM   5804  CD2 TYR A 708     -68.600  17.820  -4.953  1.00 34.94           C
ANISOU 5804  CD2 TYR A 708     4277   4604   4395   -813    -60    248       C
ATOM   5805  CE1 TYR A 708     -66.650  18.419  -6.811  1.00 45.13           C
ANISOU 5805  CE1 TYR A 708     5530   6145   5470   -934    -17    233       C
ATOM   5806  CE2 TYR A 708     -67.657  16.869  -5.291  1.00 40.97           C
ANISOU 5806  CE2 TYR A 708     5005   5448   5115   -805    -29    148       C
ATOM   5807  CZ  TYR A 708     -66.684  17.173  -6.219  1.00 44.77           C
ANISOU 5807  CZ  TYR A 708     5465   6059   5488   -861     -8    136       C
ATOM   5808  OH  TYR A 708     -65.746  16.225  -6.550  1.00 43.84           O
ANISOU 5808  OH  TYR A 708     5303   6030   5324   -842     22     26       O
ATOM   5809  N   SER A 709     -70.768  22.888  -4.098  1.00 43.97           N
ANISOU 5809  N   SER A 709     5583   5488   5634   -868   -189    648       N
ATOM   5810  CA  SER A 709     -72.024  23.551  -3.768  1.00 51.69           C
ANISOU 5810  CA  SER A 709     6589   6378   6674   -825   -241    709       C
ATOM   5811  C   SER A 709     -72.215  24.877  -4.492  1.00 56.43           C
ANISOU 5811  C   SER A 709     7241   6966   7234   -871   -291    813       C
ATOM   5812  O   SER A 709     -73.287  25.478  -4.361  1.00 58.76           O
ANISOU 5812  O   SER A 709     7559   7193   7573   -830   -344    864       O
ATOM   5813  CB  SER A 709     -72.121  23.775  -2.259  1.00 44.43           C
ANISOU 5813  CB  SER A 709     5673   5356   5852   -765   -227    697       C
ATOM   5814  OG  SER A 709     -71.511  24.996  -1.887  1.00 41.90           O
ANISOU 5814  OG  SER A 709     5394   4987   5538   -792   -233    750       O
ATOM   5815  N   SER A 710     -71.217  25.350  -5.239  1.00 54.27           N
ANISOU 5815  N   SER A 710     6985   6759   6878   -954   -279    846       N
ATOM   5816  CA  SER A 710     -71.411  26.540  -6.056  1.00 56.62           C
ANISOU 5816  CA  SER A 710     7337   7048   7127  -1008   -331    956       C
ATOM   5817  C   SER A 710     -72.206  26.251  -7.322  1.00 60.49           C
ANISOU 5817  C   SER A 710     7821   7614   7546  -1019   -372    980       C
ATOM   5818  O   SER A 710     -72.815  27.170  -7.879  1.00 62.29           O
ANISOU 5818  O   SER A 710     8097   7814   7757  -1032   -434   1075       O
ATOM   5819  CB  SER A 710     -70.061  27.156  -6.430  1.00 51.42           C
ANISOU 5819  CB  SER A 710     6697   6443   6397  -1108   -302    992       C
ATOM   5820  OG  SER A 710     -69.355  26.313  -7.324  1.00 48.90           O
ANISOU 5820  OG  SER A 710     6331   6271   5979  -1158   -260    941       O
ATOM   5821  N   GLN A 711     -72.212  25.000  -7.788  1.00 59.29           N
ANISOU 5821  N   GLN A 711     7615   7557   7355  -1012   -344    896       N
ATOM   5822  CA  GLN A 711     -72.957  24.612  -8.976  1.00 62.24           C
ANISOU 5822  CA  GLN A 711     7976   8013   7660  -1021   -382    902       C
ATOM   5823  C   GLN A 711     -74.027  23.564  -8.713  1.00 61.01           C
ANISOU 5823  C   GLN A 711     7777   7840   7563   -948   -395    829       C
ATOM   5824  O   GLN A 711     -74.830  23.290  -9.612  1.00 62.13           O
ANISOU 5824  O   GLN A 711     7907   8038   7661   -947   -437    834       O
ATOM   5825  CB  GLN A 711     -72.005  24.077 -10.057  1.00 67.41           C
ANISOU 5825  CB  GLN A 711     8603   8819   8191  -1093   -346    865       C
ATOM   5826  CG  GLN A 711     -71.480  25.128 -11.020  1.00 79.40           C
ANISOU 5826  CG  GLN A 711    10163  10401   9605  -1185   -364    969       C
ATOM   5827  CD  GLN A 711     -70.419  24.577 -11.956  1.00 90.13           C
ANISOU 5827  CD  GLN A 711    11482  11926  10838  -1256   -315    921       C
ATOM   5828  OE1 GLN A 711     -69.669  23.669 -11.595  1.00 93.68           O
ANISOU 5828  OE1 GLN A 711    11882  12420  11294  -1241   -257    814       O
ATOM   5829  NE2 GLN A 711     -70.348  25.127 -13.165  1.00 93.08           N
ANISOU 5829  NE2 GLN A 711    11876  12398  11093  -1330   -341   1000       N
ATOM   5830  N   VAL A 712     -74.064  22.970  -7.523  1.00 55.77           N
ANISOU 5830  N   VAL A 712     7090   7107   6995   -891   -361    764       N
ATOM   5831  CA  VAL A 712     -74.953  21.857  -7.218  1.00 51.28           C
ANISOU 5831  CA  VAL A 712     6478   6525   6481   -836   -365    692       C
ATOM   5832  C   VAL A 712     -75.882  22.271  -6.087  1.00 50.72           C
ANISOU 5832  C   VAL A 712     6412   6342   6517   -770   -386    720       C
ATOM   5833  O   VAL A 712     -75.433  22.831  -5.079  1.00 49.42           O
ANISOU 5833  O   VAL A 712     6267   6104   6405   -751   -363    737       O
ATOM   5834  CB  VAL A 712     -74.167  20.588  -6.838  1.00 49.15           C
ANISOU 5834  CB  VAL A 712     6171   6282   6221   -830   -306    583       C
ATOM   5835  CG1 VAL A 712     -75.122  19.434  -6.572  1.00 46.43           C
ANISOU 5835  CG1 VAL A 712     5791   5915   5937   -786   -316    518       C
ATOM   5836  CG2 VAL A 712     -73.178  20.226  -7.935  1.00 47.56           C
ANISOU 5836  CG2 VAL A 712     5958   6202   5909   -889   -282    545       C
ATOM   5837  N   ASN A 713     -77.172  21.994  -6.259  1.00 45.56           N
ANISOU 5837  N   ASN A 713     5735   5684   5891   -734   -429    721       N
ATOM   5838  CA  ASN A 713     -78.168  22.248  -5.226  1.00 43.17           C
ANISOU 5838  CA  ASN A 713     5420   5298   5684   -667   -447    735       C
ATOM   5839  C   ASN A 713     -78.061  21.154  -4.168  1.00 43.01           C
ANISOU 5839  C   ASN A 713     5363   5248   5732   -639   -395    657       C
ATOM   5840  O   ASN A 713     -78.453  20.009  -4.410  1.00 45.57           O
ANISOU 5840  O   ASN A 713     5649   5607   6060   -644   -390    597       O
ATOM   5841  CB  ASN A 713     -79.559  22.289  -5.851  1.00 50.37           C
ANISOU 5841  CB  ASN A 713     6308   6235   6593   -644   -512    760       C
ATOM   5842  CG  ASN A 713     -80.607  22.848  -4.915  1.00 51.57           C
ANISOU 5842  CG  ASN A 713     6447   6316   6830   -572   -539    788       C
ATOM   5843  OD1 ASN A 713     -80.457  22.802  -3.693  1.00 51.26           O
ANISOU 5843  OD1 ASN A 713     6401   6216   6861   -536   -501    766       O
ATOM   5844  ND2 ASN A 713     -81.688  23.370  -5.487  1.00 50.14           N
ANISOU 5844  ND2 ASN A 713     6260   6152   6641   -546   -607    833       N
ATOM   5845  N   LEU A 714     -77.532  21.502  -2.992  1.00 40.98           N
ANISOU 5845  N   LEU A 714     5120   4924   5528   -612   -359    658       N
ATOM   5846  CA  LEU A 714     -77.360  20.522  -1.925  1.00 42.72           C
ANISOU 5846  CA  LEU A 714     5311   5114   5807   -585   -311    595       C
ATOM   5847  C   LEU A 714     -78.677  20.088  -1.296  1.00 49.41           C
ANISOU 5847  C   LEU A 714     6117   5935   6722   -540   -326    587       C
ATOM   5848  O   LEU A 714     -78.672  19.170  -0.469  1.00 51.81           O
ANISOU 5848  O   LEU A 714     6396   6217   7072   -525   -290    542       O
ATOM   5849  CB  LEU A 714     -76.436  21.077  -0.840  1.00 43.63           C
ANISOU 5849  CB  LEU A 714     5450   5174   5952   -568   -272    601       C
ATOM   5850  CG  LEU A 714     -74.960  21.209  -1.219  1.00 44.17           C
ANISOU 5850  CG  LEU A 714     5543   5277   5962   -617   -240    588       C
ATOM   5851  CD1 LEU A 714     -74.135  21.604  -0.005  1.00 41.46           C
ANISOU 5851  CD1 LEU A 714     5214   4881   5659   -595   -203    582       C
ATOM   5852  CD2 LEU A 714     -74.444  19.914  -1.835  1.00 44.86           C
ANISOU 5852  CD2 LEU A 714     5605   5431   6009   -644   -214    515       C
ATOM   5853  N   ASN A 715     -79.788  20.733  -1.646  1.00 51.99           N
ANISOU 5853  N   ASN A 715     6435   6266   7054   -519   -379    633       N
ATOM   5854  CA  ASN A 715     -81.117  20.307  -1.233  1.00 51.01           C
ANISOU 5854  CA  ASN A 715     6257   6141   6982   -484   -397    624       C
ATOM   5855  C   ASN A 715     -81.813  19.499  -2.314  1.00 55.77           C
ANISOU 5855  C   ASN A 715     6828   6809   7553   -519   -430    599       C
ATOM   5856  O   ASN A 715     -83.011  19.215  -2.198  1.00 59.43           O
ANISOU 5856  O   ASN A 715     7242   7288   8051   -501   -456    596       O
ATOM   5857  CB  ASN A 715     -81.970  21.519  -0.858  1.00 56.59           C
ANISOU 5857  CB  ASN A 715     6964   6818   7720   -425   -439    679       C
ATOM   5858  CG  ASN A 715     -81.578  22.116   0.475  1.00 56.80           C
ANISOU 5858  CG  ASN A 715     7006   6779   7797   -379   -406    684       C
ATOM   5859  OD1 ASN A 715     -81.563  21.429   1.498  1.00 58.46           O
ANISOU 5859  OD1 ASN A 715     7186   6975   8049   -364   -361    648       O
ATOM   5860  ND2 ASN A 715     -81.258  23.404   0.472  1.00 57.59           N
ANISOU 5860  ND2 ASN A 715     7154   6836   7890   -358   -433    731       N
ATOM   5861  N   ASN A 716     -81.091  19.140  -3.366  1.00 52.70           N
ANISOU 5861  N   ASN A 716     6460   6467   7095   -570   -430    577       N
ATOM   5862  CA  ASN A 716     -81.599  18.320  -4.458  1.00 49.03           C
ANISOU 5862  CA  ASN A 716     5968   6070   6591   -607   -461    540       C
ATOM   5863  C   ASN A 716     -80.882  16.974  -4.391  1.00 46.83           C
ANISOU 5863  C   ASN A 716     5684   5794   6316   -637   -418    458       C
ATOM   5864  O   ASN A 716     -79.720  16.861  -4.794  1.00 40.69           O
ANISOU 5864  O   ASN A 716     4936   5038   5487   -662   -392    432       O
ATOM   5865  CB  ASN A 716     -81.377  19.014  -5.797  1.00 49.72           C
ANISOU 5865  CB  ASN A 716     6084   6221   6586   -636   -503    578       C
ATOM   5866  CG  ASN A 716     -82.130  18.353  -6.923  1.00 57.84           C
ANISOU 5866  CG  ASN A 716     7080   7327   7570   -664   -547    546       C
ATOM   5867  OD1 ASN A 716     -81.780  17.257  -7.355  1.00 60.71           O
ANISOU 5867  OD1 ASN A 716     7431   7725   7911   -699   -531    472       O
ATOM   5868  ND2 ASN A 716     -83.175  19.015  -7.406  1.00 60.33           N
ANISOU 5868  ND2 ASN A 716     7381   7669   7873   -645   -610    598       N
ATOM   5869  N   GLU A 717     -81.578  15.957  -3.870  1.00 43.52           N
ANISOU 5869  N   GLU A 717     5226   5351   5957   -636   -413    417       N
ATOM   5870  CA  GLU A 717     -80.985  14.627  -3.766  1.00 44.29           C
ANISOU 5870  CA  GLU A 717     5324   5433   6069   -659   -382    339       C
ATOM   5871  C   GLU A 717     -80.509  14.126  -5.123  1.00 51.32           C
ANISOU 5871  C   GLU A 717     6223   6392   6882   -699   -401    283       C
ATOM   5872  O   GLU A 717     -79.479  13.447  -5.219  1.00 57.23           O
ANISOU 5872  O   GLU A 717     6991   7141   7613   -707   -371    222       O
ATOM   5873  CB  GLU A 717     -81.990  13.646  -3.167  1.00 41.14           C
ANISOU 5873  CB  GLU A 717     4884   5001   5745   -666   -387    314       C
ATOM   5874  CG  GLU A 717     -82.302  13.874  -1.704  1.00 44.30           C
ANISOU 5874  CG  GLU A 717     5272   5342   6218   -630   -355    354       C
ATOM   5875  CD  GLU A 717     -83.017  12.694  -1.081  1.00 56.93           C
ANISOU 5875  CD  GLU A 717     6838   6909   7884   -653   -348    327       C
ATOM   5876  OE1 GLU A 717     -82.386  11.961  -0.292  1.00 62.61           O
ANISOU 5876  OE1 GLU A 717     7578   7572   8640   -651   -310    304       O
ATOM   5877  OE2 GLU A 717     -84.211  12.493  -1.386  1.00 64.35           O
ANISOU 5877  OE2 GLU A 717     7730   7881   8839   -674   -384    331       O
ATOM   5878  N   SER A 718     -81.238  14.466  -6.185  1.00 52.27           N
ANISOU 5878  N   SER A 718     6329   6581   6952   -717   -453    300       N
ATOM   5879  CA  SER A 718     -80.883  13.989  -7.516  1.00 52.82           C
ANISOU 5879  CA  SER A 718     6401   6730   6937   -754   -474    244       C
ATOM   5880  C   SER A 718     -79.573  14.608  -7.996  1.00 51.55           C
ANISOU 5880  C   SER A 718     6278   6614   6694   -763   -447    256       C
ATOM   5881  O   SER A 718     -78.700  13.905  -8.520  1.00 51.33           O
ANISOU 5881  O   SER A 718     6256   6628   6620   -781   -428    181       O
ATOM   5882  CB  SER A 718     -82.024  14.288  -8.488  1.00 48.97           C
ANISOU 5882  CB  SER A 718     5885   6310   6410   -769   -540    268       C
ATOM   5883  OG  SER A 718     -81.581  14.242  -9.830  1.00 52.99           O
ANISOU 5883  OG  SER A 718     6405   6916   6814   -801   -562    238       O
ATOM   5884  N   GLN A 719     -79.415  15.923  -7.822  1.00 50.77           N
ANISOU 5884  N   GLN A 719     6204   6509   6578   -752   -448    346       N
ATOM   5885  CA  GLN A 719     -78.178  16.580  -8.238  1.00 52.91           C
ANISOU 5885  CA  GLN A 719     6509   6823   6771   -774   -421    367       C
ATOM   5886  C   GLN A 719     -76.989  16.100  -7.416  1.00 44.46           C
ANISOU 5886  C   GLN A 719     5447   5713   5731   -763   -358    317       C
ATOM   5887  O   GLN A 719     -75.903  15.868  -7.961  1.00 47.51           O
ANISOU 5887  O   GLN A 719     5840   6163   6050   -787   -331    273       O
ATOM   5888  CB  GLN A 719     -78.315  18.095  -8.117  1.00 61.43           C
ANISOU 5888  CB  GLN A 719     7620   7881   7841   -767   -441    479       C
ATOM   5889  CG  GLN A 719     -79.317  18.726  -9.052  1.00 64.73           C
ANISOU 5889  CG  GLN A 719     8036   8346   8213   -774   -509    539       C
ATOM   5890  CD  GLN A 719     -79.295  20.235  -8.947  1.00 68.60           C
ANISOU 5890  CD  GLN A 719     8569   8802   8693   -765   -532    648       C
ATOM   5891  OE1 GLN A 719     -78.231  20.855  -8.996  1.00 63.72           O
ANISOU 5891  OE1 GLN A 719     7989   8187   8034   -795   -505    682       O
ATOM   5892  NE2 GLN A 719     -80.469  20.836  -8.786  1.00 73.69           N
ANISOU 5892  NE2 GLN A 719     9208   9411   9379   -725   -586    703       N
ATOM   5893  N   VAL A 720     -77.172  15.965  -6.100  1.00 40.67           N
ANISOU 5893  N   VAL A 720     4965   5139   5347   -725   -335    323       N
ATOM   5894  CA  VAL A 720     -76.113  15.444  -5.241  1.00 39.60           C
ANISOU 5894  CA  VAL A 720     4838   4965   5245   -707   -281    275       C
ATOM   5895  C   VAL A 720     -75.706  14.049  -5.687  1.00 43.68           C
ANISOU 5895  C   VAL A 720     5339   5509   5748   -714   -273    169       C
ATOM   5896  O   VAL A 720     -74.513  13.724  -5.761  1.00 47.15           O
ANISOU 5896  O   VAL A 720     5784   5978   6153   -712   -238    116       O
ATOM   5897  CB  VAL A 720     -76.570  15.452  -3.771  1.00 35.61           C
ANISOU 5897  CB  VAL A 720     4329   4360   4840   -665   -264    301       C
ATOM   5898  CG1 VAL A 720     -75.653  14.574  -2.912  1.00 31.11           C
ANISOU 5898  CG1 VAL A 720     3763   3748   4309   -643   -218    241       C
ATOM   5899  CG2 VAL A 720     -76.621  16.873  -3.245  1.00 32.86           C
ANISOU 5899  CG2 VAL A 720     4001   3982   4501   -649   -266    388       C
ATOM   5900  N   LEU A 721     -76.691  13.202  -5.990  1.00 39.71           N
ANISOU 5900  N   LEU A 721     4816   4997   5273   -719   -307    132       N
ATOM   5901  CA  LEU A 721     -76.391  11.840  -6.414  1.00 45.13           C
ANISOU 5901  CA  LEU A 721     5495   5696   5958   -723   -309     25       C
ATOM   5902  C   LEU A 721     -75.633  11.835  -7.735  1.00 51.67           C
ANISOU 5902  C   LEU A 721     6321   6638   6673   -748   -313    -27       C
ATOM   5903  O   LEU A 721     -74.645  11.106  -7.894  1.00 52.76           O
ANISOU 5903  O   LEU A 721     6459   6799   6789   -736   -289   -113       O
ATOM   5904  CB  LEU A 721     -77.682  11.030  -6.527  1.00 39.18           C
ANISOU 5904  CB  LEU A 721     4720   4910   5256   -736   -352      1       C
ATOM   5905  CG  LEU A 721     -77.460   9.541  -6.789  1.00 42.82           C
ANISOU 5905  CG  LEU A 721     5181   5350   5738   -739   -361   -113       C
ATOM   5906  CD1 LEU A 721     -76.617   8.925  -5.677  1.00 45.50           C
ANISOU 5906  CD1 LEU A 721     5542   5605   6141   -702   -320   -142       C
ATOM   5907  CD2 LEU A 721     -78.784   8.812  -6.929  1.00 41.62           C
ANISOU 5907  CD2 LEU A 721     5008   5168   5639   -766   -408   -131       C
ATOM   5908  N   GLN A 722     -76.095  12.633  -8.702  1.00 48.65           N
ANISOU 5908  N   GLN A 722     5934   6335   6217   -780   -345     24       N
ATOM   5909  CA  GLN A 722     -75.404  12.714  -9.984  1.00 51.31           C
ANISOU 5909  CA  GLN A 722     6266   6797   6432   -810   -347    -14       C
ATOM   5910  C   GLN A 722     -73.964  13.160  -9.796  1.00 50.70           C
ANISOU 5910  C   GLN A 722     6199   6756   6309   -810   -293    -12       C
ATOM   5911  O   GLN A 722     -73.046  12.590 -10.397  1.00 52.11           O
ANISOU 5911  O   GLN A 722     6363   7014   6422   -813   -273    -98       O
ATOM   5912  CB  GLN A 722     -76.132  13.672 -10.922  1.00 58.70           C
ANISOU 5912  CB  GLN A 722     7202   7805   7295   -844   -391     66       C
ATOM   5913  CG  GLN A 722     -77.436  13.141 -11.476  1.00 69.28           C
ANISOU 5913  CG  GLN A 722     8520   9154   8648   -851   -449     43       C
ATOM   5914  CD  GLN A 722     -78.063  14.096 -12.471  1.00 76.74           C
ANISOU 5914  CD  GLN A 722     9466  10183   9509   -879   -497    121       C
ATOM   5915  OE1 GLN A 722     -78.004  13.878 -13.682  1.00 83.33           O
ANISOU 5915  OE1 GLN A 722    10289  11129  10243   -907   -522     81       O
ATOM   5916  NE2 GLN A 722     -78.661  15.168 -11.964  1.00 76.69           N
ANISOU 5916  NE2 GLN A 722     9473  10124   9540   -866   -514    232       N
ATOM   5917  N   THR A 723     -73.748  14.170  -8.951  1.00 51.33           N
ANISOU 5917  N   THR A 723     6299   6781   6423   -805   -270     78       N
ATOM   5918  CA  THR A 723     -72.399  14.667  -8.709  1.00 47.28           C
ANISOU 5918  CA  THR A 723     5792   6301   5871   -813   -221     85       C
ATOM   5919  C   THR A 723     -71.523  13.587  -8.089  1.00 43.41           C
ANISOU 5919  C   THR A 723     5288   5786   5421   -772   -183    -18       C
ATOM   5920  O   THR A 723     -70.379  13.376  -8.514  1.00 43.47           O
ANISOU 5920  O   THR A 723     5278   5879   5359   -778   -152    -78       O
ATOM   5921  CB  THR A 723     -72.457  15.902  -7.805  1.00 53.16           C
ANISOU 5921  CB  THR A 723     6564   6973   6662   -812   -212    194       C
ATOM   5922  OG1 THR A 723     -73.260  16.914  -8.427  1.00 56.03           O
ANISOU 5922  OG1 THR A 723     6946   7355   6989   -843   -256    289       O
ATOM   5923  CG2 THR A 723     -71.054  16.453  -7.539  1.00 47.79           C
ANISOU 5923  CG2 THR A 723     5888   6328   5943   -831   -164    202       C
ATOM   5924  N   ALA A 724     -72.046  12.894  -7.074  1.00 39.73           N
ANISOU 5924  N   ALA A 724     4827   5205   5062   -729   -187    -37       N
ATOM   5925  CA  ALA A 724     -71.257  11.872  -6.393  1.00 36.60           C
ANISOU 5925  CA  ALA A 724     4426   4767   4712   -684   -159   -124       C
ATOM   5926  C   ALA A 724     -70.882  10.748  -7.347  1.00 38.18           C
ANISOU 5926  C   ALA A 724     4608   5036   4862   -676   -170   -246       C
ATOM   5927  O   ALA A 724     -69.729  10.304  -7.377  1.00 51.06           O
ANISOU 5927  O   ALA A 724     6226   6712   6464   -650   -141   -323       O
ATOM   5928  CB  ALA A 724     -72.020  11.326  -5.187  1.00 33.12           C
ANISOU 5928  CB  ALA A 724     3999   4193   4391   -648   -167   -109       C
ATOM   5929  N   LEU A 725     -71.844  10.281  -8.147  1.00 34.43           N
ANISOU 5929  N   LEU A 725     4129   4576   4378   -696   -215   -272       N
ATOM   5930  CA  LEU A 725     -71.551   9.218  -9.103  1.00 39.24           C
ANISOU 5930  CA  LEU A 725     4722   5250   4938   -688   -232   -398       C
ATOM   5931  C   LEU A 725     -70.546   9.680 -10.152  1.00 46.80           C
ANISOU 5931  C   LEU A 725     5655   6366   5761   -710   -208   -428       C
ATOM   5932  O   LEU A 725     -69.639   8.926 -10.530  1.00 45.74           O
ANISOU 5932  O   LEU A 725     5501   6293   5586   -681   -194   -541       O
ATOM   5933  CB  LEU A 725     -72.842   8.739  -9.766  1.00 39.79           C
ANISOU 5933  CB  LEU A 725     4790   5310   5020   -712   -288   -414       C
ATOM   5934  CG  LEU A 725     -73.850   8.080  -8.823  1.00 43.11           C
ANISOU 5934  CG  LEU A 725     5226   5585   5568   -699   -313   -400       C
ATOM   5935  CD1 LEU A 725     -75.026   7.494  -9.597  1.00 38.82           C
ANISOU 5935  CD1 LEU A 725     4672   5048   5029   -730   -371   -437       C
ATOM   5936  CD2 LEU A 725     -73.167   7.013  -7.976  1.00 43.39           C
ANISOU 5936  CD2 LEU A 725     5278   5529   5679   -649   -296   -476       C
ATOM   5937  N   TYR A 726     -70.687  10.920 -10.629  1.00 48.39           N
ANISOU 5937  N   TYR A 726     5856   6639   5890   -762   -205   -326       N
ATOM   5938  CA  TYR A 726     -69.761  11.446 -11.626  1.00 46.76           C
ANISOU 5938  CA  TYR A 726     5626   6592   5548   -799   -181   -336       C
ATOM   5939  C   TYR A 726     -68.339  11.468 -11.089  1.00 46.63           C
ANISOU 5939  C   TYR A 726     5592   6604   5520   -777   -124   -372       C
ATOM   5940  O   TYR A 726     -67.404  10.994 -11.745  1.00 49.99           O
ANISOU 5940  O   TYR A 726     5983   7148   5864   -769   -103   -470       O
ATOM   5941  CB  TYR A 726     -70.202  12.848 -12.047  1.00 43.13           C
ANISOU 5941  CB  TYR A 726     5182   6174   5030   -862   -193   -197       C
ATOM   5942  CG  TYR A 726     -69.397  13.447 -13.174  1.00 44.47           C
ANISOU 5942  CG  TYR A 726     5331   6515   5050   -917   -173   -187       C
ATOM   5943  CD1 TYR A 726     -69.672  13.126 -14.495  1.00 42.25           C
ANISOU 5943  CD1 TYR A 726     5030   6360   4664   -942   -200   -234       C
ATOM   5944  CD2 TYR A 726     -68.366  14.344 -12.917  1.00 50.13           C
ANISOU 5944  CD2 TYR A 726     6047   7276   5726   -951   -127   -127       C
ATOM   5945  CE1 TYR A 726     -68.942  13.676 -15.531  1.00 49.60           C
ANISOU 5945  CE1 TYR A 726     5939   7460   5446   -999   -180   -218       C
ATOM   5946  CE2 TYR A 726     -67.626  14.899 -13.948  1.00 53.64           C
ANISOU 5946  CE2 TYR A 726     6468   7884   6027  -1014   -106   -109       C
ATOM   5947  CZ  TYR A 726     -67.920  14.563 -15.255  1.00 56.84           C
ANISOU 5947  CZ  TYR A 726     6854   8419   6324  -1038   -131   -152       C
ATOM   5948  OH  TYR A 726     -67.190  15.110 -16.288  1.00 58.18           O
ANISOU 5948  OH  TYR A 726     6998   8766   6340  -1105   -107   -129       O
ATOM   5949  N   GLU A 727     -68.159  12.017  -9.888  1.00 44.24           N
ANISOU 5949  N   GLU A 727     5310   6203   5297   -765   -101   -300       N
ATOM   5950  CA  GLU A 727     -66.827  12.073  -9.298  1.00 44.32           C
ANISOU 5950  CA  GLU A 727     5300   6239   5300   -743    -51   -332       C
ATOM   5951  C   GLU A 727     -66.282  10.675  -9.039  1.00 44.83           C
ANISOU 5951  C   GLU A 727     5346   6284   5403   -669    -47   -472       C
ATOM   5952  O   GLU A 727     -65.099  10.405  -9.288  1.00 46.86           O
ANISOU 5952  O   GLU A 727     5564   6640   5599   -650    -14   -553       O
ATOM   5953  CB  GLU A 727     -66.865  12.886  -8.005  1.00 41.38           C
ANISOU 5953  CB  GLU A 727     4954   5755   5012   -740    -35   -232       C
ATOM   5954  CG  GLU A 727     -65.512  13.106  -7.376  1.00 45.05           C
ANISOU 5954  CG  GLU A 727     5398   6253   5468   -727     14   -253       C
ATOM   5955  CD  GLU A 727     -65.546  12.959  -5.871  1.00 49.59           C
ANISOU 5955  CD  GLU A 727     5993   6688   6159   -673     21   -235       C
ATOM   5956  OE1 GLU A 727     -65.481  11.811  -5.383  1.00 50.33           O
ANISOU 5956  OE1 GLU A 727     6086   6724   6314   -606     16   -317       O
ATOM   5957  OE2 GLU A 727     -65.642  13.992  -5.176  1.00 49.63           O
ANISOU 5957  OE2 GLU A 727     6019   6642   6195   -697     30   -138       O
ATOM   5958  N   ALA A 728     -67.135   9.767  -8.552  1.00 40.21           N
ANISOU 5958  N   ALA A 728     4787   5572   4919   -626    -82   -503       N
ATOM   5959  CA  ALA A 728     -66.679   8.418  -8.240  1.00 45.85           C
ANISOU 5959  CA  ALA A 728     5498   6240   5683   -553    -88   -629       C
ATOM   5960  C   ALA A 728     -66.221   7.683  -9.493  1.00 49.41           C
ANISOU 5960  C   ALA A 728     5916   6817   6043   -541    -98   -760       C
ATOM   5961  O   ALA A 728     -65.224   6.952  -9.462  1.00 54.43           O
ANISOU 5961  O   ALA A 728     6527   7488   6666   -482    -84   -872       O
ATOM   5962  CB  ALA A 728     -67.788   7.643  -7.532  1.00 32.97           C
ANISOU 5962  CB  ALA A 728     3907   4446   4175   -527   -128   -621       C
ATOM   5963  N   VAL A 729     -66.919   7.877 -10.614  1.00 47.76           N
ANISOU 5963  N   VAL A 729     5701   6683   5762   -591   -125   -753       N
ATOM   5964  CA  VAL A 729     -66.483   7.238 -11.852  1.00 48.83           C
ANISOU 5964  CA  VAL A 729     5800   6956   5796   -582   -133   -882       C
ATOM   5965  C   VAL A 729     -65.214   7.900 -12.377  1.00 58.56           C
ANISOU 5965  C   VAL A 729     6982   8366   6901   -603    -80   -893       C
ATOM   5966  O   VAL A 729     -64.271   7.215 -12.795  1.00 59.58           O
ANISOU 5966  O   VAL A 729     7071   8592   6976   -556    -65  -1024       O
ATOM   5967  CB  VAL A 729     -67.607   7.259 -12.901  1.00 46.60           C
ANISOU 5967  CB  VAL A 729     5525   6715   5467   -631   -180   -871       C
ATOM   5968  CG1 VAL A 729     -67.080   6.778 -14.248  1.00 39.81           C
ANISOU 5968  CG1 VAL A 729     4622   6027   4478   -627   -184   -999       C
ATOM   5969  CG2 VAL A 729     -68.770   6.392 -12.442  1.00 52.25           C
ANISOU 5969  CG2 VAL A 729     6279   7268   6307   -610   -233   -889       C
ATOM   5970  N   MET A 730     -65.166   9.237 -12.362  1.00 60.05           N
ANISOU 5970  N   MET A 730     7171   8602   7042   -674    -53   -757       N
ATOM   5971  CA  MET A 730     -63.989   9.949 -12.852  1.00 54.38           C
ANISOU 5971  CA  MET A 730     6405   8054   6201   -714     -2   -751       C
ATOM   5972  C   MET A 730     -62.728   9.506 -12.119  1.00 53.75           C
ANISOU 5972  C   MET A 730     6292   7984   6148   -651     38   -833       C
ATOM   5973  O   MET A 730     -61.679   9.291 -12.741  1.00 45.78           O
ANISOU 5973  O   MET A 730     5222   7135   5038   -641     70   -926       O
ATOM   5974  CB  MET A 730     -64.204  11.457 -12.705  1.00 63.13           C
ANISOU 5974  CB  MET A 730     7537   9164   7287   -801     13   -578       C
ATOM   5975  CG  MET A 730     -62.924  12.281 -12.691  1.00 79.86           C
ANISOU 5975  CG  MET A 730     9616  11403   9325   -846     70   -546       C
ATOM   5976  SD  MET A 730     -63.178  13.990 -12.161  1.00 89.68           S
ANISOU 5976  SD  MET A 730    10903  12583  10586   -935     78   -345       S
ATOM   5977  CE  MET A 730     -63.273  13.797 -10.381  1.00 88.05           C
ANISOU 5977  CE  MET A 730    10730  12171  10553   -862     79   -332       C
ATOM   5978  N   ARG A 731     -62.811   9.342 -10.800  1.00 54.21           N
ANISOU 5978  N   ARG A 731     6382   7879   6335   -604     36   -804       N
ATOM   5979  CA  ARG A 731     -61.644   8.909 -10.042  1.00 48.43           C
ANISOU 5979  CA  ARG A 731     5620   7150   5632   -537     67   -879       C
ATOM   5980  C   ARG A 731     -61.437   7.401 -10.083  1.00 56.54           C
ANISOU 5980  C   ARG A 731     6640   8144   6699   -435     40  -1040       C
ATOM   5981  O   ARG A 731     -60.312   6.940  -9.864  1.00 61.92           O
ANISOU 5981  O   ARG A 731     7278   8883   7365   -372     63  -1137       O
ATOM   5982  CB  ARG A 731     -61.760   9.384  -8.594  1.00 39.74           C
ANISOU 5982  CB  ARG A 731     4557   5899   4644   -527     75   -780       C
ATOM   5983  CG  ARG A 731     -61.892  10.888  -8.479  1.00 34.11           C
ANISOU 5983  CG  ARG A 731     3855   5205   3901   -619     97   -630       C
ATOM   5984  CD  ARG A 731     -62.436  11.287  -7.129  1.00 43.51           C
ANISOU 5984  CD  ARG A 731     5094   6225   5212   -606     89   -534       C
ATOM   5985  NE  ARG A 731     -61.536  10.915  -6.045  1.00 43.18           N
ANISOU 5985  NE  ARG A 731     5038   6143   5226   -540    112   -580       N
ATOM   5986  CZ  ARG A 731     -60.531  11.673  -5.619  1.00 45.70           C
ANISOU 5986  CZ  ARG A 731     5326   6523   5514   -563    152   -552       C
ATOM   5987  NH1 ARG A 731     -60.298  12.848  -6.193  1.00 49.19           N
ANISOU 5987  NH1 ARG A 731     5754   7062   5874   -657    174   -475       N
ATOM   5988  NH2 ARG A 731     -59.761  11.258  -4.620  1.00 40.70           N
ANISOU 5988  NH2 ARG A 731     4678   5854   4934   -495    166   -599       N
ATOM   5989  N   ALA A 732     -62.487   6.624 -10.363  1.00 59.24           N
ANISOU 5989  N   ALA A 732     7022   8393   7094   -418    -12  -1074       N
ATOM   5990  CA  ALA A 732     -62.331   5.176 -10.434  1.00 56.54           C
ANISOU 5990  CA  ALA A 732     6683   8003   6796   -325    -48  -1229       C
ATOM   5991  C   ALA A 732     -61.540   4.754 -11.665  1.00 54.34           C
ANISOU 5991  C   ALA A 732     6342   7914   6391   -302    -38  -1373       C
ATOM   5992  O   ALA A 732     -60.779   3.782 -11.604  1.00 57.19           O
ANISOU 5992  O   ALA A 732     6680   8284   6764   -208    -46  -1515       O
ATOM   5993  CB  ALA A 732     -63.703   4.501 -10.424  1.00 55.69           C
ANISOU 5993  CB  ALA A 732     6635   7745   6779   -327   -108  -1223       C
ATOM   5994  N   ARG A 733     -61.705   5.467 -12.785  1.00 53.43           N
ANISOU 5994  N   ARG A 733     6197   7955   6149   -382    -24  -1341       N
ATOM   5995  CA  ARG A 733     -60.939   5.151 -13.986  1.00 58.26           C
ANISOU 5995  CA  ARG A 733     6740   8774   6621   -368     -8  -1473       C
ATOM   5996  C   ARG A 733     -59.441   5.268 -13.738  1.00 65.50           C
ANISOU 5996  C   ARG A 733     7589   9815   7484   -328     47  -1532       C
ATOM   5997  O   ARG A 733     -58.648   4.579 -14.389  1.00 71.51           O
ANISOU 5997  O   ARG A 733     8291  10711   8170   -267     54  -1688       O
ATOM   5998  CB  ARG A 733     -61.362   6.063 -15.139  1.00 54.86           C
ANISOU 5998  CB  ARG A 733     6291   8495   6056   -474      2  -1396       C
ATOM   5999  CG  ARG A 733     -62.828   5.934 -15.517  1.00 63.17           C
ANISOU 5999  CG  ARG A 733     7400   9453   7148   -510    -56  -1351       C
ATOM   6000  CD  ARG A 733     -63.259   7.013 -16.502  1.00 71.40           C
ANISOU 6000  CD  ARG A 733     8433  10632   8065   -616    -48  -1244       C
ATOM   6001  NE  ARG A 733     -64.536   6.686 -17.135  1.00 80.28           N
ANISOU 6001  NE  ARG A 733     9591  11714   9198   -636   -109  -1246       N
ATOM   6002  CZ  ARG A 733     -65.249   7.532 -17.873  1.00 85.92           C
ANISOU 6002  CZ  ARG A 733    10314  12498   9832   -720   -123  -1139       C
ATOM   6003  NH1 ARG A 733     -64.814   8.767 -18.077  1.00 92.29           N
ANISOU 6003  NH1 ARG A 733    11106  13412  10548   -795    -81  -1016       N
ATOM   6004  NH2 ARG A 733     -66.400   7.143 -18.406  1.00 82.42           N
ANISOU 6004  NH2 ARG A 733     9896  12016   9403   -729   -182  -1155       N
ATOM   6005  N   TYR A 734     -59.036   6.129 -12.804  1.00 67.19           N
ANISOU 6005  N   TYR A 734     7804   9992   7733   -360     85  -1415       N
ATOM   6006  CA  TYR A 734     -57.648   6.246 -12.385  1.00 67.10           C
ANISOU 6006  CA  TYR A 734     7727  10080   7689   -323    134  -1464       C
ATOM   6007  C   TYR A 734     -57.331   5.375 -11.175  1.00 57.17           C
ANISOU 6007  C   TYR A 734     6494   8663   6565   -208    112  -1525       C
ATOM   6008  O   TYR A 734     -56.305   5.588 -10.521  1.00 55.77           O
ANISOU 6008  O   TYR A 734     6273   8527   6388   -178    147  -1534       O
ATOM   6009  CB  TYR A 734     -57.307   7.707 -12.081  1.00 73.88           C
ANISOU 6009  CB  TYR A 734     8571  10998   8503   -429    185  -1308       C
ATOM   6010  CG  TYR A 734     -57.339   8.617 -13.290  1.00 85.59           C
ANISOU 6010  CG  TYR A 734    10020  12665   9835   -544    212  -1246       C
ATOM   6011  CD1 TYR A 734     -56.502   8.392 -14.376  1.00 94.39           C
ANISOU 6011  CD1 TYR A 734    11050  14011  10802   -545    242  -1358       C
ATOM   6012  CD2 TYR A 734     -58.201   9.706 -13.343  1.00 87.95           C
ANISOU 6012  CD2 TYR A 734    10373  12910  10135   -648    205  -1076       C
ATOM   6013  CE1 TYR A 734     -56.525   9.225 -15.483  1.00 98.86           C
ANISOU 6013  CE1 TYR A 734    11588  14754  11221   -657    268  -1292       C
ATOM   6014  CE2 TYR A 734     -58.231  10.545 -14.444  1.00 91.30           C
ANISOU 6014  CE2 TYR A 734    10775  13496  10420   -754    224  -1009       C
ATOM   6015  CZ  TYR A 734     -57.391  10.299 -15.511  1.00 97.38           C
ANISOU 6015  CZ  TYR A 734    11462  14498  11040   -762    256  -1113       C
ATOM   6016  OH  TYR A 734     -57.416  11.128 -16.610  1.00 99.98           O
ANISOU 6016  OH  TYR A 734    11770  14995  11221   -873    276  -1037       O
ATOM   6017  N   GLY A 735     -58.192   4.411 -10.857  1.00 52.75           N
ANISOU 6017  N   GLY A 735     6001   7922   6118   -149     53  -1562       N
ATOM   6018  CA  GLY A 735     -57.946   3.530  -9.727  1.00 52.51           C
ANISOU 6018  CA  GLY A 735     6004   7731   6215    -42     25  -1611       C
ATOM   6019  C   GLY A 735     -57.869   4.230  -8.389  1.00 53.99           C
ANISOU 6019  C   GLY A 735     6218   7814   6482    -60     47  -1477       C
ATOM   6020  O   GLY A 735     -57.170   3.756  -7.487  1.00 59.65           O
ANISOU 6020  O   GLY A 735     6931   8473   7260     26     45  -1520       O
ATOM   6021  N   VAL A 736     -58.576   5.345  -8.229  1.00 47.26           N
ANISOU 6021  N   VAL A 736     5394   6934   5630   -164     65  -1319       N
ATOM   6022  CA  VAL A 736     -58.558   6.121  -6.997  1.00 45.11           C
ANISOU 6022  CA  VAL A 736     5145   6569   5425   -188     85  -1192       C
ATOM   6023  C   VAL A 736     -59.962   6.152  -6.403  1.00 50.74           C
ANISOU 6023  C   VAL A 736     5941   7094   6246   -215     49  -1085       C
ATOM   6024  O   VAL A 736     -60.955   6.284  -7.127  1.00 45.09           O
ANISOU 6024  O   VAL A 736     5249   6370   5512   -272     27  -1051       O
ATOM   6025  CB  VAL A 736     -58.036   7.549  -7.252  1.00 42.61           C
ANISOU 6025  CB  VAL A 736     4784   6394   5012   -287    140  -1100       C
ATOM   6026  CG1 VAL A 736     -58.099   8.382  -5.980  1.00 34.52           C
ANISOU 6026  CG1 VAL A 736     3790   5264   4062   -312    155   -973       C
ATOM   6027  CG2 VAL A 736     -56.619   7.492  -7.809  1.00 40.22           C
ANISOU 6027  CG2 VAL A 736     4388   6293   4599   -266    180  -1207       C
ATOM   6028  N   SER A 737     -60.036   6.030  -5.075  1.00 53.80           N
ANISOU 6028  N   SER A 737     6366   7338   6738   -174     43  -1034       N
ATOM   6029  CA  SER A 737     -61.301   6.112  -4.368  1.00 50.62           C
ANISOU 6029  CA  SER A 737     6030   6768   6434   -200     16   -928       C
ATOM   6030  C   SER A 737     -61.919   7.500  -4.530  1.00 55.33           C
ANISOU 6030  C   SER A 737     6632   7395   6995   -302     37   -792       C
ATOM   6031  O   SER A 737     -61.223   8.470  -4.840  1.00 52.28           O
ANISOU 6031  O   SER A 737     6207   7132   6527   -351     76   -761       O
ATOM   6032  CB  SER A 737     -61.093   5.801  -2.886  1.00 46.35           C
ANISOU 6032  CB  SER A 737     5519   6097   5993   -137     13   -898       C
ATOM   6033  OG  SER A 737     -61.033   4.402  -2.667  1.00 52.20           O
ANISOU 6033  OG  SER A 737     6287   6747   6800    -48    -28   -995       O
ATOM   6034  N   PRO A 738     -63.232   7.618  -4.335  1.00 56.31           N
ANISOU 6034  N   PRO A 738     6805   7409   7180   -337      9   -710       N
ATOM   6035  CA  PRO A 738     -63.861   8.944  -4.340  1.00 53.48           C
ANISOU 6035  CA  PRO A 738     6458   7060   6804   -418     21   -579       C
ATOM   6036  C   PRO A 738     -63.470   9.738  -3.102  1.00 46.51           C
ANISOU 6036  C   PRO A 738     5581   6128   5963   -415     50   -498       C
ATOM   6037  O   PRO A 738     -62.909   9.217  -2.137  1.00 43.89           O
ANISOU 6037  O   PRO A 738     5251   5740   5685   -351     57   -531       O
ATOM   6038  CB  PRO A 738     -65.361   8.631  -4.360  1.00 50.33           C
ANISOU 6038  CB  PRO A 738     6101   6553   6470   -436    -21   -535       C
ATOM   6039  CG  PRO A 738     -65.467   7.260  -3.793  1.00 50.41           C
ANISOU 6039  CG  PRO A 738     6135   6454   6566   -365    -48   -609       C
ATOM   6040  CD  PRO A 738     -64.230   6.538  -4.238  1.00 48.97           C
ANISOU 6040  CD  PRO A 738     5918   6354   6334   -308    -39   -740       C
ATOM   6041  N   THR A 739     -63.772  11.034  -3.148  1.00 40.71           N
ANISOU 6041  N   THR A 739     4852   5414   5201   -485     63   -393       N
ATOM   6042  CA  THR A 739     -63.511  11.891  -2.005  1.00 38.73           C
ANISOU 6042  CA  THR A 739     4612   5113   4991   -487     84   -316       C
ATOM   6043  C   THR A 739     -64.398  11.486  -0.830  1.00 42.04           C
ANISOU 6043  C   THR A 739     5071   5381   5521   -443     64   -276       C
ATOM   6044  O   THR A 739     -65.381  10.753  -0.980  1.00 46.64           O
ANISOU 6044  O   THR A 739     5677   5897   6148   -431     33   -285       O
ATOM   6045  CB  THR A 739     -63.733  13.361  -2.366  1.00 41.72           C
ANISOU 6045  CB  THR A 739     4997   5531   5322   -571     92   -212       C
ATOM   6046  OG1 THR A 739     -65.072  13.544  -2.841  1.00 48.32           O
ANISOU 6046  OG1 THR A 739     5864   6321   6174   -600     57   -154       O
ATOM   6047  CG2 THR A 739     -62.760  13.790  -3.451  1.00 38.12           C
ANISOU 6047  CG2 THR A 739     4499   5234   4750   -625    117   -241       C
ATOM   6048  N   MET A 740     -64.040  11.984   0.356  1.00 40.97           N
ANISOU 6048  N   MET A 740     4942   5199   5427   -423     83   -233       N
ATOM   6049  CA  MET A 740     -64.663  11.496   1.584  1.00 46.46           C
ANISOU 6049  CA  MET A 740     5667   5768   6216   -374     72   -206       C
ATOM   6050  C   MET A 740     -66.158  11.808   1.616  1.00 47.17           C
ANISOU 6050  C   MET A 740     5787   5786   6350   -405     47   -127       C
ATOM   6051  O   MET A 740     -66.983  10.922   1.877  1.00 40.76           O
ANISOU 6051  O   MET A 740     4993   4897   5596   -382     25   -133       O
ATOM   6052  CB  MET A 740     -63.939  12.083   2.797  1.00 50.69           C
ANISOU 6052  CB  MET A 740     6198   6288   6773   -350     97   -177       C
ATOM   6053  CG  MET A 740     -62.603  11.394   3.086  1.00 62.32           C
ANISOU 6053  CG  MET A 740     7643   7807   8231   -292    112   -264       C
ATOM   6054  SD  MET A 740     -61.564  12.223   4.310  1.00 70.65           S
ANISOU 6054  SD  MET A 740     8678   8878   9286   -276    142   -241       S
ATOM   6055  CE  MET A 740     -61.321  13.816   3.527  1.00 71.87           C
ANISOU 6055  CE  MET A 740     8816   9124   9369   -377    161   -186       C
ATOM   6056  N   GLY A 741     -66.528  13.062   1.347  1.00 43.58           N
ANISOU 6056  N   GLY A 741     5335   5356   5868   -458     49    -52       N
ATOM   6057  CA  GLY A 741     -67.941  13.404   1.285  1.00 45.05           C
ANISOU 6057  CA  GLY A 741     5542   5488   6088   -480     22     16       C
ATOM   6058  C   GLY A 741     -68.692  12.584   0.252  1.00 42.58           C
ANISOU 6058  C   GLY A 741     5227   5188   5765   -496     -8    -20       C
ATOM   6059  O   GLY A 741     -69.853  12.212   0.460  1.00 39.13           O
ANISOU 6059  O   GLY A 741     4800   4687   5380   -493    -33      5       O
ATOM   6060  N   THR A 742     -68.035  12.281  -0.869  1.00 35.62           N
ANISOU 6060  N   THR A 742     4327   4396   4810   -514     -8    -85       N
ATOM   6061  CA  THR A 742     -68.647  11.412  -1.865  1.00 38.41           C
ANISOU 6061  CA  THR A 742     4678   4767   5149   -524    -39   -138       C
ATOM   6062  C   THR A 742     -68.816   9.999  -1.324  1.00 41.30           C
ANISOU 6062  C   THR A 742     5055   5050   5587   -474    -53   -202       C
ATOM   6063  O   THR A 742     -69.807   9.326  -1.627  1.00 41.54           O
ANISOU 6063  O   THR A 742     5094   5037   5652   -484    -86   -213       O
ATOM   6064  CB  THR A 742     -67.813  11.416  -3.143  1.00 36.17           C
ANISOU 6064  CB  THR A 742     4368   4612   4762   -550    -32   -200       C
ATOM   6065  OG1 THR A 742     -67.677  12.764  -3.608  1.00 34.27           O
ANISOU 6065  OG1 THR A 742     4124   4440   4455   -607    -21   -124       O
ATOM   6066  CG2 THR A 742     -68.479  10.577  -4.227  1.00 34.75           C
ANISOU 6066  CG2 THR A 742     4186   4459   4561   -561    -68   -261       C
ATOM   6067  N   GLN A 743     -67.873   9.540  -0.502  1.00 41.29           N
ANISOU 6067  N   GLN A 743     5055   5022   5612   -421    -32   -241       N
ATOM   6068  CA  GLN A 743     -68.035   8.236   0.130  1.00 38.97           C
ANISOU 6068  CA  GLN A 743     4781   4631   5393   -372    -50   -287       C
ATOM   6069  C   GLN A 743     -69.231   8.230   1.071  1.00 40.10           C
ANISOU 6069  C   GLN A 743     4948   4672   5618   -381    -61   -204       C
ATOM   6070  O   GLN A 743     -69.964   7.238   1.144  1.00 45.35           O
ANISOU 6070  O   GLN A 743     5630   5263   6338   -380    -90   -222       O
ATOM   6071  CB  GLN A 743     -66.763   7.850   0.876  1.00 36.10           C
ANISOU 6071  CB  GLN A 743     4414   4264   5037   -309    -28   -335       C
ATOM   6072  CG  GLN A 743     -65.562   7.715  -0.023  1.00 37.37           C
ANISOU 6072  CG  GLN A 743     4542   4538   5118   -293    -16   -430       C
ATOM   6073  CD  GLN A 743     -64.331   7.275   0.729  1.00 38.24           C
ANISOU 6073  CD  GLN A 743     4642   4648   5239   -221      0   -485       C
ATOM   6074  OE1 GLN A 743     -64.422   6.751   1.839  1.00 36.05           O
ANISOU 6074  OE1 GLN A 743     4392   4269   5035   -175     -8   -465       O
ATOM   6075  NE2 GLN A 743     -63.168   7.494   0.133  1.00 39.47           N
ANISOU 6075  NE2 GLN A 743     4755   4926   5317   -212     23   -551       N
ATOM   6076  N   GLU A 744     -69.449   9.330   1.798  1.00 35.98           N
ANISOU 6076  N   GLU A 744     4423   4145   5102   -393    -39   -117       N
ATOM   6077  CA  GLU A 744     -70.616   9.404   2.674  1.00 39.48           C
ANISOU 6077  CA  GLU A 744     4877   4511   5612   -400    -46    -42       C
ATOM   6078  C   GLU A 744     -71.912   9.392   1.866  1.00 41.86           C
ANISOU 6078  C   GLU A 744     5171   4816   5917   -448    -79    -21       C
ATOM   6079  O   GLU A 744     -72.875   8.691   2.220  1.00 39.08           O
ANISOU 6079  O   GLU A 744     4826   4400   5624   -458    -98     -6       O
ATOM   6080  CB  GLU A 744     -70.541  10.652   3.551  1.00 35.76           C
ANISOU 6080  CB  GLU A 744     4401   4044   5140   -395    -19     34       C
ATOM   6081  CG  GLU A 744     -71.801  10.895   4.369  1.00 39.19           C
ANISOU 6081  CG  GLU A 744     4836   4423   5630   -401    -25    108       C
ATOM   6082  CD  GLU A 744     -71.765  12.202   5.139  1.00 45.17           C
ANISOU 6082  CD  GLU A 744     5591   5189   6385   -391     -4    171       C
ATOM   6083  OE1 GLU A 744     -72.620  13.077   4.884  1.00 46.91           O
ANISOU 6083  OE1 GLU A 744     5802   5421   6600   -413    -17    221       O
ATOM   6084  OE2 GLU A 744     -70.876  12.356   6.000  1.00 51.04           O
ANISOU 6084  OE2 GLU A 744     6338   5925   7129   -356     21    166       O
ATOM   6085  N   VAL A 745     -71.950  10.158   0.772  1.00 38.63           N
ANISOU 6085  N   VAL A 745     4749   4487   5442   -483    -87    -18       N
ATOM   6086  CA  VAL A 745     -73.121  10.148  -0.101  1.00 37.44           C
ANISOU 6086  CA  VAL A 745     4588   4353   5283   -525   -123     -5       C
ATOM   6087  C   VAL A 745     -73.367   8.747  -0.649  1.00 37.73           C
ANISOU 6087  C   VAL A 745     4629   4365   5341   -531   -153    -85       C
ATOM   6088  O   VAL A 745     -74.514   8.287  -0.731  1.00 33.11           O
ANISOU 6088  O   VAL A 745     4039   3744   4798   -557   -183    -73       O
ATOM   6089  CB  VAL A 745     -72.953  11.178  -1.233  1.00 44.72           C
ANISOU 6089  CB  VAL A 745     5500   5372   6120   -559   -129     12       C
ATOM   6090  CG1 VAL A 745     -74.119  11.096  -2.212  1.00 29.10           C
ANISOU 6090  CG1 VAL A 745     3509   3421   4126   -598   -173     18       C
ATOM   6091  CG2 VAL A 745     -72.848  12.573  -0.654  1.00 45.32           C
ANISOU 6091  CG2 VAL A 745     5580   5450   6189   -558   -110     96       C
ATOM   6092  N   LEU A 746     -72.297   8.043  -1.025  1.00 42.22           N
ANISOU 6092  N   LEU A 746     5204   4954   5883   -505   -148   -173       N
ATOM   6093  CA  LEU A 746     -72.457   6.695  -1.557  1.00 35.25           C
ANISOU 6093  CA  LEU A 746     4331   4038   5023   -502   -182   -262       C
ATOM   6094  C   LEU A 746     -72.963   5.734  -0.488  1.00 37.47           C
ANISOU 6094  C   LEU A 746     4638   4195   5404   -488   -194   -248       C
ATOM   6095  O   LEU A 746     -73.813   4.884  -0.770  1.00 38.24           O
ANISOU 6095  O   LEU A 746     4743   4242   5544   -517   -231   -272       O
ATOM   6096  CB  LEU A 746     -71.139   6.205  -2.147  1.00 32.33           C
ANISOU 6096  CB  LEU A 746     3960   3723   4600   -464   -175   -366       C
ATOM   6097  CG  LEU A 746     -70.754   6.796  -3.506  1.00 40.33           C
ANISOU 6097  CG  LEU A 746     4947   4872   5506   -491   -173   -402       C
ATOM   6098  CD1 LEU A 746     -69.637   5.984  -4.137  1.00 46.63           C
ANISOU 6098  CD1 LEU A 746     5735   5723   6258   -450   -173   -528       C
ATOM   6099  CD2 LEU A 746     -71.949   6.853  -4.433  1.00 41.98           C
ANISOU 6099  CD2 LEU A 746     5147   5107   5696   -545   -212   -389       C
ATOM   6100  N   TYR A 747     -72.451   5.848   0.741  1.00 39.00           N
ANISOU 6100  N   TYR A 747     4845   4339   5633   -450   -163   -207       N
ATOM   6101  CA  TYR A 747     -72.962   5.033   1.842  1.00 37.90           C
ANISOU 6101  CA  TYR A 747     4731   4088   5581   -443   -171   -174       C
ATOM   6102  C   TYR A 747     -74.461   5.246   2.032  1.00 35.79           C
ANISOU 6102  C   TYR A 747     4448   3799   5352   -499   -184    -99       C
ATOM   6103  O   TYR A 747     -75.220   4.285   2.236  1.00 35.27           O
ANISOU 6103  O   TYR A 747     4395   3659   5347   -527   -212   -100       O
ATOM   6104  CB  TYR A 747     -72.221   5.370   3.139  1.00 36.93           C
ANISOU 6104  CB  TYR A 747     4618   3939   5475   -394   -134   -129       C
ATOM   6105  CG  TYR A 747     -70.827   4.795   3.277  1.00 42.15           C
ANISOU 6105  CG  TYR A 747     5296   4593   6124   -330   -128   -203       C
ATOM   6106  CD1 TYR A 747     -70.161   4.241   2.192  1.00 43.90           C
ANISOU 6106  CD1 TYR A 747     5517   4855   6309   -313   -148   -309       C
ATOM   6107  CD2 TYR A 747     -70.173   4.813   4.505  1.00 38.09           C
ANISOU 6107  CD2 TYR A 747     4796   4044   5634   -281   -105   -171       C
ATOM   6108  CE1 TYR A 747     -68.884   3.722   2.327  1.00 38.80           C
ANISOU 6108  CE1 TYR A 747     4879   4212   5652   -244   -145   -383       C
ATOM   6109  CE2 TYR A 747     -68.903   4.297   4.650  1.00 31.38           C
ANISOU 6109  CE2 TYR A 747     3956   3193   4773   -215   -104   -240       C
ATOM   6110  CZ  TYR A 747     -68.260   3.753   3.559  1.00 39.17           C
ANISOU 6110  CZ  TYR A 747     4938   4220   5726   -195   -124   -347       C
ATOM   6111  OH  TYR A 747     -66.987   3.234   3.703  1.00 44.64           O
ANISOU 6111  OH  TYR A 747     5633   4921   6407   -120   -125   -424       O
ATOM   6112  N   LYS A 748     -74.905   6.503   1.972  1.00 31.39           N
ANISOU 6112  N   LYS A 748     3861   3307   4760   -516   -167    -35       N
ATOM   6113  CA  LYS A 748     -76.327   6.785   2.151  1.00 34.57           C
ANISOU 6113  CA  LYS A 748     4238   3704   5193   -559   -180     31       C
ATOM   6114  C   LYS A 748     -77.156   6.211   1.006  1.00 38.45           C
ANISOU 6114  C   LYS A 748     4717   4212   5682   -610   -226    -13       C
ATOM   6115  O   LYS A 748     -78.207   5.592   1.234  1.00 43.86           O
ANISOU 6115  O   LYS A 748     5391   4853   6421   -650   -248      6       O
ATOM   6116  CB  LYS A 748     -76.540   8.292   2.284  1.00 31.40           C
ANISOU 6116  CB  LYS A 748     3812   3365   4754   -553   -159     99       C
ATOM   6117  CG  LYS A 748     -75.916   8.873   3.537  1.00 32.26           C
ANISOU 6117  CG  LYS A 748     3929   3453   4874   -509   -118    144       C
ATOM   6118  CD  LYS A 748     -76.032  10.385   3.581  1.00 32.72           C
ANISOU 6118  CD  LYS A 748     3971   3564   4897   -500   -105    200       C
ATOM   6119  CE  LYS A 748     -75.446  10.926   4.875  1.00 26.98           C
ANISOU 6119  CE  LYS A 748     3252   2815   4184   -457    -67    235       C
ATOM   6120  NZ  LYS A 748     -75.408  12.410   4.876  1.00 26.66           N
ANISOU 6120  NZ  LYS A 748     3205   2814   4111   -447    -60    278       N
ATOM   6121  N   TYR A 749     -76.696   6.408  -0.232  1.00 35.56           N
ANISOU 6121  N   TYR A 749     4347   3915   5248   -612   -241    -72       N
ATOM   6122  CA  TYR A 749     -77.385   5.846  -1.389  1.00 37.80           C
ANISOU 6122  CA  TYR A 749     4619   4225   5519   -656   -288   -126       C
ATOM   6123  C   TYR A 749     -77.488   4.329  -1.284  1.00 44.44           C
ANISOU 6123  C   TYR A 749     5486   4975   6424   -668   -317   -192       C
ATOM   6124  O   TYR A 749     -78.530   3.743  -1.603  1.00 43.74           O
ANISOU 6124  O   TYR A 749     5385   4863   6371   -719   -356   -201       O
ATOM   6125  CB  TYR A 749     -76.650   6.257  -2.663  1.00 43.85           C
ANISOU 6125  CB  TYR A 749     5381   5090   6191   -650   -294   -185       C
ATOM   6126  CG  TYR A 749     -77.313   5.823  -3.945  1.00 47.48           C
ANISOU 6126  CG  TYR A 749     5824   5598   6618   -691   -343   -243       C
ATOM   6127  CD1 TYR A 749     -78.679   5.975  -4.130  1.00 50.12           C
ANISOU 6127  CD1 TYR A 749     6130   5940   6973   -737   -375   -200       C
ATOM   6128  CD2 TYR A 749     -76.567   5.278  -4.982  1.00 48.46           C
ANISOU 6128  CD2 TYR A 749     5956   5771   6685   -682   -359   -348       C
ATOM   6129  CE1 TYR A 749     -79.289   5.583  -5.308  1.00 54.88           C
ANISOU 6129  CE1 TYR A 749     6715   6594   7544   -775   -424   -257       C
ATOM   6130  CE2 TYR A 749     -77.167   4.884  -6.165  1.00 53.80           C
ANISOU 6130  CE2 TYR A 749     6617   6500   7325   -718   -406   -408       C
ATOM   6131  CZ  TYR A 749     -78.529   5.038  -6.323  1.00 56.89           C
ANISOU 6131  CZ  TYR A 749     6982   6893   7740   -767   -440   -361       C
ATOM   6132  OH  TYR A 749     -79.133   4.648  -7.498  1.00 58.79           O
ANISOU 6132  OH  TYR A 749     7204   7191   7942   -804   -490   -424       O
ATOM   6133  N   ALA A 750     -76.418   3.678  -0.825  1.00 38.67           N
ANISOU 6133  N   ALA A 750     4792   4188   5712   -621   -304   -238       N
ATOM   6134  CA  ALA A 750     -76.444   2.230  -0.663  1.00 40.94           C
ANISOU 6134  CA  ALA A 750     5117   4371   6069   -625   -338   -297       C
ATOM   6135  C   ALA A 750     -77.461   1.813   0.389  1.00 44.35           C
ANISOU 6135  C   ALA A 750     5553   4713   6586   -667   -342   -217       C
ATOM   6136  O   ALA A 750     -78.226   0.862   0.177  1.00 45.10           O
ANISOU 6136  O   ALA A 750     5657   4745   6733   -718   -384   -242       O
ATOM   6137  CB  ALA A 750     -75.053   1.718  -0.297  1.00 42.68           C
ANISOU 6137  CB  ALA A 750     5375   4551   6291   -553   -324   -355       C
ATOM   6138  N   TYR A 751     -77.479   2.498   1.538  1.00 41.94           N
ANISOU 6138  N   TYR A 751     5239   4404   6293   -650   -298   -123       N
ATOM   6139  CA  TYR A 751     -78.477   2.171   2.552  1.00 44.85           C
ANISOU 6139  CA  TYR A 751     5602   4710   6729   -694   -295    -42       C
ATOM   6140  C   TYR A 751     -79.884   2.282   1.987  1.00 49.40           C
ANISOU 6140  C   TYR A 751     6132   5326   7313   -768   -322    -22       C
ATOM   6141  O   TYR A 751     -80.758   1.461   2.298  1.00 41.69           O
ANISOU 6141  O   TYR A 751     5155   4289   6399   -828   -345     -2       O
ATOM   6142  CB  TYR A 751     -78.345   3.079   3.774  1.00 43.91           C
ANISOU 6142  CB  TYR A 751     5468   4610   6604   -661   -243     50       C
ATOM   6143  CG  TYR A 751     -79.499   2.900   4.747  1.00 47.40           C
ANISOU 6143  CG  TYR A 751     5888   5022   7099   -711   -235    137       C
ATOM   6144  CD1 TYR A 751     -79.555   1.793   5.586  1.00 48.50           C
ANISOU 6144  CD1 TYR A 751     6065   5060   7302   -731   -242    161       C
ATOM   6145  CD2 TYR A 751     -80.542   3.820   4.809  1.00 43.23           C
ANISOU 6145  CD2 TYR A 751     5301   4570   6556   -738   -222    196       C
ATOM   6146  CE1 TYR A 751     -80.606   1.613   6.468  1.00 49.10           C
ANISOU 6146  CE1 TYR A 751     6115   5121   7418   -786   -230    245       C
ATOM   6147  CE2 TYR A 751     -81.598   3.647   5.690  1.00 44.55           C
ANISOU 6147  CE2 TYR A 751     5435   4726   6764   -783   -211    270       C
ATOM   6148  CZ  TYR A 751     -81.623   2.541   6.517  1.00 50.32           C
ANISOU 6148  CZ  TYR A 751     6201   5367   7552   -813   -212    296       C
ATOM   6149  OH  TYR A 751     -82.665   2.356   7.399  1.00 54.28           O
ANISOU 6149  OH  TYR A 751     6667   5871   8087   -867   -197    374       O
ATOM   6150  N   THR A 752     -80.126   3.296   1.157  1.00 46.87           N
ANISOU 6150  N   THR A 752     5771   5109   6928   -767   -323    -24       N
ATOM   6151  CA  THR A 752     -81.473   3.468   0.627  1.00 47.89           C
ANISOU 6151  CA  THR A 752     5849   5286   7061   -829   -352     -4       C
ATOM   6152  C   THR A 752     -81.801   2.452  -0.461  1.00 48.69           C
ANISOU 6152  C   THR A 752     5959   5370   7173   -877   -409    -92       C
ATOM   6153  O   THR A 752     -82.966   2.077  -0.615  1.00 62.30           O
ANISOU 6153  O   THR A 752     7648   7091   8930   -944   -440    -81       O
ATOM   6154  CB  THR A 752     -81.651   4.892   0.108  1.00 54.29           C
ANISOU 6154  CB  THR A 752     6620   6207   7801   -807   -342     29       C
ATOM   6155  OG1 THR A 752     -80.618   5.188  -0.833  1.00 64.55           O
ANISOU 6155  OG1 THR A 752     7943   7553   9031   -772   -345    -33       O
ATOM   6156  CG2 THR A 752     -81.537   5.860   1.260  1.00 53.17           C
ANISOU 6156  CG2 THR A 752     6468   6074   7662   -765   -293    114       C
ATOM   6157  N   GLN A 753     -80.803   1.982  -1.206  1.00 50.60           N
ANISOU 6157  N   GLN A 753     6240   5601   7385   -845   -425   -186       N
ATOM   6158  CA  GLN A 753     -81.052   0.989  -2.244  1.00 53.25           C
ANISOU 6158  CA  GLN A 753     6586   5918   7729   -884   -482   -285       C
ATOM   6159  C   GLN A 753     -81.141  -0.435  -1.708  1.00 54.60           C
ANISOU 6159  C   GLN A 753     6804   5950   7993   -913   -511   -314       C
ATOM   6160  O   GLN A 753     -81.745  -1.289  -2.365  1.00 51.22           O
ANISOU 6160  O   GLN A 753     6378   5489   7595   -969   -565   -377       O
ATOM   6161  CB  GLN A 753     -79.956   1.040  -3.311  1.00 58.58           C
ANISOU 6161  CB  GLN A 753     7279   6651   8327   -833   -490   -385       C
ATOM   6162  CG  GLN A 753     -79.864   2.355  -4.059  1.00 65.74           C
ANISOU 6162  CG  GLN A 753     8148   7696   9135   -818   -473   -362       C
ATOM   6163  CD  GLN A 753     -81.097   2.648  -4.887  1.00 69.90           C
ANISOU 6163  CD  GLN A 753     8626   8294   9637   -876   -512   -352       C
ATOM   6164  OE1 GLN A 753     -82.121   3.085  -4.364  1.00 72.62           O
ANISOU 6164  OE1 GLN A 753     8935   8643  10015   -908   -510   -268       O
ATOM   6165  NE2 GLN A 753     -81.003   2.412  -6.190  1.00 70.29           N
ANISOU 6165  NE2 GLN A 753     8670   8411   9625   -885   -551   -441       N
ATOM   6166  N   LEU A 754     -80.555  -0.717  -0.548  1.00 53.35           N
ANISOU 6166  N   LEU A 754     6685   5706   7880   -880   -481   -270       N
ATOM   6167  CA  LEU A 754     -80.445  -2.094  -0.081  1.00 46.95           C
ANISOU 6167  CA  LEU A 754     5933   4751   7154   -898   -513   -298       C
ATOM   6168  C   LEU A 754     -81.167  -2.371   1.228  1.00 48.30           C
ANISOU 6168  C   LEU A 754     6107   4848   7397   -948   -496   -186       C
ATOM   6169  O   LEU A 754     -81.693  -3.470   1.405  1.00 58.81           O
ANISOU 6169  O   LEU A 754     7469   6074   8803  -1012   -537   -191       O
ATOM   6170  CB  LEU A 754     -78.965  -2.478   0.077  1.00 46.03           C
ANISOU 6170  CB  LEU A 754     5876   4584   7031   -806   -506   -360       C
ATOM   6171  CG  LEU A 754     -78.065  -2.257  -1.140  1.00 52.69           C
ANISOU 6171  CG  LEU A 754     6715   5510   7796   -748   -516   -476       C
ATOM   6172  CD1 LEU A 754     -76.627  -2.669  -0.838  1.00 51.49           C
ANISOU 6172  CD1 LEU A 754     6611   5313   7642   -654   -507   -535       C
ATOM   6173  CD2 LEU A 754     -78.595  -3.010  -2.349  1.00 51.45           C
ANISOU 6173  CD2 LEU A 754     6557   5349   7642   -794   -580   -581       C
ATOM   6174  N   TYR A 755     -81.199  -1.420   2.162  1.00 56.42           N
ANISOU 6174  N   TYR A 755     7105   5927   8404   -925   -439    -87       N
ATOM   6175  CA  TYR A 755     -81.663  -1.708   3.515  1.00 70.49           C
ANISOU 6175  CA  TYR A 755     8893   7647  10243   -959   -415     17       C
ATOM   6176  C   TYR A 755     -82.722  -0.736   4.020  1.00 91.17           C
ANISOU 6176  C   TYR A 755    11436  10362  12843   -996   -377    113       C
ATOM   6177  O   TYR A 755     -83.073  -0.786   5.204  1.00127.71           O
ANISOU 6177  O   TYR A 755    16057  14966  17500  -1017   -347    203       O
ATOM   6178  CB  TYR A 755     -80.479  -1.716   4.485  1.00 64.12           C
ANISOU 6178  CB  TYR A 755     8138   6790   9436   -878   -382     42       C
ATOM   6179  CG  TYR A 755     -79.309  -2.533   3.998  1.00 58.50           C
ANISOU 6179  CG  TYR A 755     7494   6001   8734   -818   -416    -60       C
ATOM   6180  CD1 TYR A 755     -79.470  -3.868   3.649  1.00 57.30           C
ANISOU 6180  CD1 TYR A 755     7394   5730   8648   -857   -478   -118       C
ATOM   6181  CD2 TYR A 755     -78.048  -1.971   3.879  1.00 43.83           C
ANISOU 6181  CD2 TYR A 755     5645   4190   6820   -722   -391   -104       C
ATOM   6182  CE1 TYR A 755     -78.406  -4.616   3.199  1.00 54.37           C
ANISOU 6182  CE1 TYR A 755     7083   5290   8287   -791   -514   -222       C
ATOM   6183  CE2 TYR A 755     -76.980  -2.712   3.430  1.00 40.02           C
ANISOU 6183  CE2 TYR A 755     5214   3651   6341   -660   -422   -205       C
ATOM   6184  CZ  TYR A 755     -77.165  -4.033   3.092  1.00 47.17           C
ANISOU 6184  CZ  TYR A 755     6170   4438   7312   -689   -484   -266       C
ATOM   6185  OH  TYR A 755     -76.104  -4.777   2.644  1.00 53.36           O
ANISOU 6185  OH  TYR A 755     7004   5167   8102   -615   -519   -377       O
ATOM   6186  N   GLU A 756     -83.241   0.142   3.168  1.00 83.36           N
ANISOU 6186  N   GLU A 756    10387   9484  11803  -1001   -381     95       N
ATOM   6187  CA  GLU A 756     -84.190   1.139   3.642  1.00 76.05           C
ANISOU 6187  CA  GLU A 756     9387   8652  10858  -1017   -349    177       C
ATOM   6188  C   GLU A 756     -85.631   0.656   3.530  1.00 76.79           C
ANISOU 6188  C   GLU A 756     9426   8758  10992  -1119   -377    201       C
ATOM   6189  O   GLU A 756     -86.406   0.803   4.480  1.00 77.47           O
ANISOU 6189  O   GLU A 756     9468   8866  11099  -1154   -348    284       O
ATOM   6190  CB  GLU A 756     -84.004   2.450   2.872  1.00 73.97           C
ANISOU 6190  CB  GLU A 756     9088   8499  10517   -962   -340    159       C
ATOM   6191  CG  GLU A 756     -84.621   3.664   3.552  1.00 72.77           C
ANISOU 6191  CG  GLU A 756     8876   8432  10342   -941   -302    241       C
ATOM   6192  CD  GLU A 756     -86.083   3.853   3.189  1.00 76.51           C
ANISOU 6192  CD  GLU A 756     9271   8977  10821  -1001   -326    262       C
ATOM   6193  OE1 GLU A 756     -86.556   3.169   2.258  1.00 78.77           O
ANISOU 6193  OE1 GLU A 756     9551   9259  11121  -1059   -375    208       O
ATOM   6194  OE2 GLU A 756     -86.762   4.680   3.832  1.00 76.32           O
ANISOU 6194  OE2 GLU A 756     9189   9018  10789   -988   -299    326       O
ATOM   6195  N   LYS A 757     -86.004   0.087   2.377  1.00 74.63           N
ANISOU 6195  N   LYS A 757     9150   8480  10725  -1168   -433    125       N
ATOM   6196  CA  LYS A 757     -87.379  -0.366   2.182  1.00 67.31           C
ANISOU 6196  CA  LYS A 757     8165   7575   9835  -1271   -465    138       C
ATOM   6197  C   LYS A 757     -87.806  -1.345   3.268  1.00 65.54           C
ANISOU 6197  C   LYS A 757     7957   7259   9687  -1347   -458    202       C
ATOM   6198  O   LYS A 757     -88.977  -1.360   3.668  1.00 66.13           O
ANISOU 6198  O   LYS A 757     7963   7381   9784  -1424   -452    261       O
ATOM   6199  CB  LYS A 757     -87.534  -1.008   0.801  1.00 65.14           C
ANISOU 6199  CB  LYS A 757     7901   7291   9561  -1311   -533     33       C
ATOM   6200  CG  LYS A 757     -88.044  -0.061  -0.281  1.00 64.39           C
ANISOU 6200  CG  LYS A 757     7740   7331   9397  -1295   -552      3       C
ATOM   6201  CD  LYS A 757     -87.040   1.046  -0.567  1.00 65.37           C
ANISOU 6201  CD  LYS A 757     7882   7513   9443  -1189   -522     -4       C
ATOM   6202  CE  LYS A 757     -87.402   1.828  -1.821  1.00 71.46           C
ANISOU 6202  CE  LYS A 757     8608   8402  10141  -1177   -554    -42       C
ATOM   6203  NZ  LYS A 757     -86.295   2.740  -2.242  1.00 76.63           N
ANISOU 6203  NZ  LYS A 757     9294   9101  10720  -1088   -531    -57       N
ATOM   6204  N   LYS A 758     -86.871  -2.160   3.760  1.00 63.46           N
ANISOU 6204  N   LYS A 758     7782   6870   9461  -1326   -458    195       N
ATOM   6205  CA  LYS A 758     -87.170  -3.056   4.871  1.00 70.69           C
ANISOU 6205  CA  LYS A 758     8724   7691  10443  -1395   -450    271       C
ATOM   6206  C   LYS A 758     -87.626  -2.277   6.099  1.00 67.31           C
ANISOU 6206  C   LYS A 758     8238   7343   9993  -1389   -384    385       C
ATOM   6207  O   LYS A 758     -88.611  -2.649   6.749  1.00 57.03           O
ANISOU 6207  O   LYS A 758     6893   6051   8725  -1482   -375    457       O
ATOM   6208  CB  LYS A 758     -85.939  -3.910   5.188  1.00 77.57           C
ANISOU 6208  CB  LYS A 758     9706   8418  11349  -1347   -464    243       C
ATOM   6209  CG  LYS A 758     -85.962  -4.603   6.536  1.00 80.80           C
ANISOU 6209  CG  LYS A 758    10156   8734  11809  -1387   -445    343       C
ATOM   6210  CD  LYS A 758     -84.564  -4.690   7.112  1.00 79.95           C
ANISOU 6210  CD  LYS A 758    10130   8554  11695  -1281   -429    340       C
ATOM   6211  CE  LYS A 758     -83.626  -5.438   6.186  1.00 81.13           C
ANISOU 6211  CE  LYS A 758    10357   8603  11864  -1233   -486    219       C
ATOM   6212  NZ  LYS A 758     -83.819  -6.907   6.292  1.00 83.25           N
ANISOU 6212  NZ  LYS A 758    10700   8708  12222  -1309   -547    215       N
ATOM   6213  N   MET A 759     -86.937  -1.178   6.417  1.00 71.79           N
ANISOU 6213  N   MET A 759     8798   7976  10502  -1284   -338    398       N
ATOM   6214  CA  MET A 759     -87.218  -0.415   7.627  1.00 71.13           C
ANISOU 6214  CA  MET A 759     8668   7964  10395  -1261   -275    494       C
ATOM   6215  C   MET A 759     -88.285   0.655   7.413  1.00 67.41           C
ANISOU 6215  C   MET A 759     8088   7639   9885  -1267   -260    512       C
ATOM   6216  O   MET A 759     -89.203   0.790   8.226  1.00 67.95           O
ANISOU 6216  O   MET A 759     8090   7770   9958  -1313   -230    585       O
ATOM   6217  CB  MET A 759     -85.929   0.221   8.151  1.00 72.83           C
ANISOU 6217  CB  MET A 759     8931   8170  10571  -1146   -238    496       C
ATOM   6218  CG  MET A 759     -85.953   0.518   9.636  1.00 78.12           C
ANISOU 6218  CG  MET A 759     9588   8863  11233  -1129   -181    591       C
ATOM   6219  SD  MET A 759     -84.304   0.783  10.298  1.00 82.61           S
ANISOU 6219  SD  MET A 759    10235   9379  11774  -1012   -153    586       S
ATOM   6220  CE  MET A 759     -83.685  -0.896  10.308  1.00 83.37           C
ANISOU 6220  CE  MET A 759    10434   9305  11937  -1049   -199    568       C
ATOM   6221  N   GLY A 760     -88.173   1.432   6.333  1.00 65.13           N
ANISOU 6221  N   GLY A 760     7780   7413   9554  -1217   -281    449       N
ATOM   6222  CA  GLY A 760     -89.101   2.496   6.019  1.00 59.34           C
ANISOU 6222  CA  GLY A 760     6953   6810   8782  -1205   -277    460       C
ATOM   6223  C   GLY A 760     -88.554   3.888   6.275  1.00 64.21           C
ANISOU 6223  C   GLY A 760     7562   7491   9343  -1095   -241    474       C
ATOM   6224  O   GLY A 760     -89.007   4.846   5.639  1.00 70.32           O
ANISOU 6224  O   GLY A 760     8285   8354  10079  -1062   -255    460       O
ATOM   6225  N   ILE A 761     -87.592   4.020   7.186  1.00 66.57           N
ANISOU 6225  N   ILE A 761     7914   7745   9636  -1038   -200    502       N
ATOM   6226  CA  ILE A 761     -87.029   5.323   7.541  1.00 72.22           C
ANISOU 6226  CA  ILE A 761     8626   8510  10303   -939   -166    515       C
ATOM   6227  C   ILE A 761     -85.941   5.717   6.546  1.00 71.01           C
ANISOU 6227  C   ILE A 761     8530   8336  10115   -882   -187    451       C
ATOM   6228  O   ILE A 761     -84.916   5.027   6.433  1.00 74.59           O
ANISOU 6228  O   ILE A 761     9054   8709  10578   -873   -191    415       O
ATOM   6229  CB  ILE A 761     -86.488   5.327   8.982  1.00 76.87           C
ANISOU 6229  CB  ILE A 761     9239   9072  10895   -904   -113    571       C
ATOM   6230  CG1 ILE A 761     -85.691   6.606   9.256  1.00 69.44           C
ANISOU 6230  CG1 ILE A 761     8311   8166   9908   -802    -86    568       C
ATOM   6231  CG2 ILE A 761     -85.644   4.090   9.265  1.00 79.99           C
ANISOU 6231  CG2 ILE A 761     9716   9350  11326   -929   -119    564       C
ATOM   6232  CD1 ILE A 761     -86.478   7.867   9.048  1.00 64.83           C
ANISOU 6232  CD1 ILE A 761     7656   7682   9294   -766    -87    576       C
ATOM   6233  N   PRO A 762     -86.115   6.811   5.814  1.00 66.76           N
ANISOU 6233  N   PRO A 762     7961   7871   9533   -842   -201    436       N
ATOM   6234  CA  PRO A 762     -85.104   7.231   4.841  1.00 60.57           C
ANISOU 6234  CA  PRO A 762     7227   7080   8707   -799   -218    383       C
ATOM   6235  C   PRO A 762     -83.987   8.052   5.479  1.00 55.17           C
ANISOU 6235  C   PRO A 762     6582   6387   7995   -722   -179    398       C
ATOM   6236  O   PRO A 762     -84.062   8.498   6.625  1.00 56.30           O
ANISOU 6236  O   PRO A 762     6709   6538   8146   -691   -141    447       O
ATOM   6237  CB  PRO A 762     -85.914   8.081   3.856  1.00 52.00           C
ANISOU 6237  CB  PRO A 762     6090   6081   7586   -798   -254    377       C
ATOM   6238  CG  PRO A 762     -86.998   8.656   4.682  1.00 51.37           C
ANISOU 6238  CG  PRO A 762     5940   6058   7522   -791   -237    435       C
ATOM   6239  CD  PRO A 762     -87.361   7.586   5.677  1.00 60.82           C
ANISOU 6239  CD  PRO A 762     7125   7213   8769   -846   -212    462       C
ATOM   6240  N   VAL A 763     -82.930   8.239   4.696  1.00 44.71           N
ANISOU 6240  N   VAL A 763     5304   5052   6633   -694   -188    351       N
ATOM   6241  CA  VAL A 763     -81.853   9.163   5.020  1.00 40.10           C
ANISOU 6241  CA  VAL A 763     4750   4472   6014   -630   -159    358       C
ATOM   6242  C   VAL A 763     -81.665  10.077   3.820  1.00 38.21           C
ANISOU 6242  C   VAL A 763     4511   4288   5718   -618   -185    337       C
ATOM   6243  O   VAL A 763     -81.725   9.627   2.670  1.00 43.71           O
ANISOU 6243  O   VAL A 763     5213   5001   6395   -651   -220    291       O
ATOM   6244  CB  VAL A 763     -80.543   8.423   5.383  1.00 41.82           C
ANISOU 6244  CB  VAL A 763     5026   4625   6237   -610   -139    324       C
ATOM   6245  CG1 VAL A 763     -80.170   7.409   4.307  1.00 42.13           C
ANISOU 6245  CG1 VAL A 763     5094   4638   6275   -640   -173    250       C
ATOM   6246  CG2 VAL A 763     -79.407   9.412   5.632  1.00 31.95           C
ANISOU 6246  CG2 VAL A 763     3800   3392   4947   -551   -112    325       C
ATOM   6247  N   LYS A 764     -81.484  11.365   4.085  1.00 35.78           N
ANISOU 6247  N   LYS A 764     4201   4011   5384   -572   -172    373       N
ATOM   6248  CA  LYS A 764     -81.310  12.332   3.012  1.00 34.35           C
ANISOU 6248  CA  LYS A 764     4026   3876   5148   -564   -198    370       C
ATOM   6249  C   LYS A 764     -79.998  12.072   2.279  1.00 44.05           C
ANISOU 6249  C   LYS A 764     5301   5102   6334   -569   -194    320       C
ATOM   6250  O   LYS A 764     -78.933  11.987   2.900  1.00 53.05           O
ANISOU 6250  O   LYS A 764     6471   6211   7474   -544   -160    308       O
ATOM   6251  CB  LYS A 764     -81.341  13.750   3.583  1.00 34.76           C
ANISOU 6251  CB  LYS A 764     4074   3941   5190   -514   -188    421       C
ATOM   6252  CG  LYS A 764     -81.460  14.858   2.547  1.00 43.12           C
ANISOU 6252  CG  LYS A 764     5139   5044   6202   -508   -225    439       C
ATOM   6253  CD  LYS A 764     -81.364  16.239   3.191  1.00 44.33           C
ANISOU 6253  CD  LYS A 764     5302   5188   6354   -456   -219    484       C
ATOM   6254  CE  LYS A 764     -82.736  16.773   3.566  1.00 56.67           C
ANISOU 6254  CE  LYS A 764     6813   6773   7946   -425   -241    519       C
ATOM   6255  NZ  LYS A 764     -82.779  18.263   3.504  1.00 62.22           N
ANISOU 6255  NZ  LYS A 764     7533   7474   8634   -378   -267    556       N
ATOM   6256  N   ILE A 765     -80.077  11.924   0.955  1.00 44.64           N
ANISOU 6256  N   ILE A 765     5376   5219   6365   -600   -229    286       N
ATOM   6257  CA  ILE A 765     -78.887  11.795   0.120  1.00 47.59           C
ANISOU 6257  CA  ILE A 765     5783   5617   6683   -605   -226    236       C
ATOM   6258  C   ILE A 765     -78.255  13.173  -0.028  1.00 48.29           C
ANISOU 6258  C   ILE A 765     5888   5739   6721   -585   -216    277       C
ATOM   6259  O   ILE A 765     -78.578  13.919  -0.959  1.00 50.02           O
ANISOU 6259  O   ILE A 765     6103   6010   6891   -600   -247    301       O
ATOM   6260  CB  ILE A 765     -79.219  11.189  -1.257  1.00 48.15           C
ANISOU 6260  CB  ILE A 765     5845   5734   6716   -646   -268    183       C
ATOM   6261  CG1 ILE A 765     -79.915   9.841  -1.092  1.00 46.10           C
ANISOU 6261  CG1 ILE A 765     5571   5429   6515   -674   -285    143       C
ATOM   6262  CG2 ILE A 765     -77.954  11.028  -2.094  1.00 48.22           C
ANISOU 6262  CG2 ILE A 765     5880   5783   6659   -647   -259    123       C
ATOM   6263  CD1 ILE A 765     -79.119   8.850  -0.298  1.00 50.03           C
ANISOU 6263  CD1 ILE A 765     6099   5853   7057   -658   -256    105       C
ATOM   6264  N   ALA A 766     -77.356  13.517   0.893  1.00 44.16           N
ANISOU 6264  N   ALA A 766     5385   5184   6209   -554   -177    288       N
ATOM   6265  CA  ALA A 766     -76.720  14.826   0.931  1.00 42.37           C
ANISOU 6265  CA  ALA A 766     5178   4975   5946   -541   -166    329       C
ATOM   6266  C   ALA A 766     -75.438  14.709   1.737  1.00 41.39           C
ANISOU 6266  C   ALA A 766     5073   4827   5826   -517   -123    305       C
ATOM   6267  O   ALA A 766     -75.339  13.837   2.608  1.00 41.87           O
ANISOU 6267  O   ALA A 766     5131   4843   5933   -496   -102    281       O
ATOM   6268  CB  ALA A 766     -77.648  15.875   1.561  1.00 27.54           C
ANISOU 6268  CB  ALA A 766     3288   3077   4099   -514   -179    397       C
ATOM   6269  N   PRO A 767     -74.444  15.551   1.472  1.00 38.03           N
ANISOU 6269  N   PRO A 767     4666   4430   5352   -524   -110    313       N
ATOM   6270  CA  PRO A 767     -73.260  15.594   2.330  1.00 36.33           C
ANISOU 6270  CA  PRO A 767     4463   4200   5143   -500    -71    294       C
ATOM   6271  C   PRO A 767     -73.566  16.340   3.620  1.00 38.74           C
ANISOU 6271  C   PRO A 767     4770   4453   5495   -464    -59    342       C
ATOM   6272  O   PRO A 767     -74.623  16.952   3.781  1.00 46.64           O
ANISOU 6272  O   PRO A 767     5764   5437   6520   -455    -81    389       O
ATOM   6273  CB  PRO A 767     -72.237  16.349   1.480  1.00 37.37           C
ANISOU 6273  CB  PRO A 767     4607   4392   5201   -534    -66    293       C
ATOM   6274  CG  PRO A 767     -73.073  17.252   0.641  1.00 38.89           C
ANISOU 6274  CG  PRO A 767     4806   4604   5366   -564   -104    351       C
ATOM   6275  CD  PRO A 767     -74.340  16.490   0.342  1.00 38.23           C
ANISOU 6275  CD  PRO A 767     4703   4512   5312   -560   -134    343       C
ATOM   6276  N   SER A 768     -72.610  16.285   4.545  1.00 32.55           N
ANISOU 6276  N   SER A 768     3993   3651   4722   -437    -26    323       N
ATOM   6277  CA  SER A 768     -72.756  16.939   5.837  1.00 32.20           C
ANISOU 6277  CA  SER A 768     3951   3567   4716   -399    -12    356       C
ATOM   6278  C   SER A 768     -71.400  17.461   6.291  1.00 34.89           C
ANISOU 6278  C   SER A 768     4304   3918   5035   -393     13    340       C
ATOM   6279  O   SER A 768     -70.395  17.339   5.584  1.00 37.48           O
ANISOU 6279  O   SER A 768     4634   4289   5317   -421     21    307       O
ATOM   6280  CB  SER A 768     -73.360  15.987   6.874  1.00 27.57           C
ANISOU 6280  CB  SER A 768     3350   2943   4183   -365      1    353       C
ATOM   6281  OG  SER A 768     -72.586  14.810   6.998  1.00 28.74           O
ANISOU 6281  OG  SER A 768     3502   3086   4332   -359     18    304       O
ATOM   6282  N   GLY A 769     -71.382  18.046   7.487  1.00 32.48           N
ANISOU 6282  N   GLY A 769     4001   3580   4759   -357     25    358       N
ATOM   6283  CA  GLY A 769     -70.161  18.630   8.006  1.00 35.30           C
ANISOU 6283  CA  GLY A 769     4367   3945   5099   -352     45    342       C
ATOM   6284  C   GLY A 769     -69.081  17.594   8.254  1.00 40.75           C
ANISOU 6284  C   GLY A 769     5047   4659   5777   -339     72    287       C
ATOM   6285  O   GLY A 769     -69.350  16.416   8.504  1.00 45.47           O
ANISOU 6285  O   GLY A 769     5637   5241   6397   -314     77    267       O
ATOM   6286  N   TYR A 770     -67.831  18.054   8.175  1.00 35.43           N
ANISOU 6286  N   TYR A 770     4372   4021   5067   -356     85    262       N
ATOM   6287  CA  TYR A 770     -66.689  17.167   8.369  1.00 29.25           C
ANISOU 6287  CA  TYR A 770     3574   3273   4268   -335    107    203       C
ATOM   6288  C   TYR A 770     -66.647  16.630   9.792  1.00 28.60           C
ANISOU 6288  C   TYR A 770     3489   3153   4225   -273    121    195       C
ATOM   6289  O   TYR A 770     -66.456  15.429  10.006  1.00 32.25           O
ANISOU 6289  O   TYR A 770     3947   3607   4699   -239    125    163       O
ATOM   6290  CB  TYR A 770     -65.393  17.907   8.040  1.00 31.09           C
ANISOU 6290  CB  TYR A 770     3796   3564   4451   -372    120    181       C
ATOM   6291  CG  TYR A 770     -64.204  17.008   7.786  1.00 30.96           C
ANISOU 6291  CG  TYR A 770     3752   3610   4401   -359    138    110       C
ATOM   6292  CD1 TYR A 770     -63.587  16.323   8.827  1.00 34.98           C
ANISOU 6292  CD1 TYR A 770     4250   4111   4931   -298    151     72       C
ATOM   6293  CD2 TYR A 770     -63.690  16.852   6.503  1.00 30.31           C
ANISOU 6293  CD2 TYR A 770     3652   3600   4262   -403    141     79       C
ATOM   6294  CE1 TYR A 770     -62.493  15.502   8.598  1.00 36.02           C
ANISOU 6294  CE1 TYR A 770     4353   4299   5033   -274    162      2       C
ATOM   6295  CE2 TYR A 770     -62.595  16.038   6.263  1.00 30.44           C
ANISOU 6295  CE2 TYR A 770     3637   3684   4246   -382    157      3       C
ATOM   6296  CZ  TYR A 770     -62.004  15.364   7.316  1.00 34.16           C
ANISOU 6296  CZ  TYR A 770     4097   4139   4744   -314    165    -37       C
ATOM   6297  OH  TYR A 770     -60.922  14.549   7.088  1.00 31.65           O
ANISOU 6297  OH  TYR A 770     3745   3885   4395   -281    175   -117       O
ATOM   6298  N   VAL A 771     -66.807  17.506  10.778  1.00 29.82           N
ANISOU 6298  N   VAL A 771     3649   3284   4398   -255    124    224       N
ATOM   6299  CA  VAL A 771     -66.751  17.132  12.184  1.00 24.52           C
ANISOU 6299  CA  VAL A 771     2973   2590   3752   -197    137    222       C
ATOM   6300  C   VAL A 771     -68.095  17.453  12.817  1.00 30.95           C
ANISOU 6300  C   VAL A 771     3792   3363   4603   -179    130    271       C
ATOM   6301  O   VAL A 771     -68.692  18.497  12.533  1.00 29.86           O
ANISOU 6301  O   VAL A 771     3662   3214   4469   -198    115    299       O
ATOM   6302  CB  VAL A 771     -65.604  17.860  12.919  1.00 32.71           C
ANISOU 6302  CB  VAL A 771     4003   3653   4771   -186    149    197       C
ATOM   6303  CG1 VAL A 771     -65.534  17.423  14.378  1.00 28.17           C
ANISOU 6303  CG1 VAL A 771     3423   3065   4213   -122    161    194       C
ATOM   6304  CG2 VAL A 771     -64.268  17.602  12.221  1.00 24.71           C
ANISOU 6304  CG2 VAL A 771     2973   2700   3717   -209    157    146       C
ATOM   6305  N   LYS A 772     -68.572  16.550  13.668  1.00 27.91           N
ANISOU 6305  N   LYS A 772     3404   2959   4242   -140    140    281       N
ATOM   6306  CA  LYS A 772     -69.849  16.706  14.342  1.00 35.09           C
ANISOU 6306  CA  LYS A 772     4305   3847   5179   -122    139    325       C
ATOM   6307  C   LYS A 772     -69.671  16.459  15.832  1.00 32.71           C
ANISOU 6307  C   LYS A 772     3998   3549   4882    -71    159    329       C
ATOM   6308  O   LYS A 772     -68.965  15.528  16.243  1.00 26.74           O
ANISOU 6308  O   LYS A 772     3246   2792   4120    -50    168    313       O
ATOM   6309  CB  LYS A 772     -70.905  15.749  13.768  1.00 29.40           C
ANISOU 6309  CB  LYS A 772     3580   3108   4482   -144    130    347       C
ATOM   6310  CG  LYS A 772     -71.311  16.076  12.336  1.00 28.93           C
ANISOU 6310  CG  LYS A 772     3524   3054   4415   -192    106    347       C
ATOM   6311  CD  LYS A 772     -72.253  15.027  11.776  1.00 35.22           C
ANISOU 6311  CD  LYS A 772     4314   3836   5233   -216     94    358       C
ATOM   6312  CE  LYS A 772     -72.425  15.183  10.273  1.00 40.14           C
ANISOU 6312  CE  LYS A 772     4939   4474   5837   -261     70    347       C
ATOM   6313  NZ  LYS A 772     -73.183  14.041   9.682  1.00 39.86           N
ANISOU 6313  NZ  LYS A 772     4899   4425   5821   -288     54    343       N
ATOM   6314  N   ILE A 773     -70.320  17.301  16.634  1.00 29.19           N
ANISOU 6314  N   ILE A 773     3541   3108   4442    -47    162    349       N
ATOM   6315  CA  ILE A 773     -70.284  17.217  18.086  1.00 34.21           C
ANISOU 6315  CA  ILE A 773     4167   3761   5072      2    181    355       C
ATOM   6316  C   ILE A 773     -71.696  16.939  18.586  1.00 36.65           C
ANISOU 6316  C   ILE A 773     4453   4074   5397     11    189    399       C
ATOM   6317  O   ILE A 773     -72.651  17.611  18.176  1.00 38.43           O
ANISOU 6317  O   ILE A 773     4665   4301   5637      1    178    412       O
ATOM   6318  CB  ILE A 773     -69.720  18.508  18.706  1.00 33.24           C
ANISOU 6318  CB  ILE A 773     4043   3652   4933     28    179    327       C
ATOM   6319  CG1 ILE A 773     -68.284  18.733  18.222  1.00 33.00           C
ANISOU 6319  CG1 ILE A 773     4027   3628   4884      7    174    285       C
ATOM   6320  CG2 ILE A 773     -69.792  18.448  20.225  1.00 27.45           C
ANISOU 6320  CG2 ILE A 773     3296   2949   4187     82    198    330       C
ATOM   6321  CD1 ILE A 773     -67.727  20.102  18.547  1.00 35.96           C
ANISOU 6321  CD1 ILE A 773     4406   4007   5250     10    164    257       C
ATOM   6322  N   PHE A 774     -71.819  15.945  19.462  1.00 35.78           N
ANISOU 6322  N   PHE A 774     4337   3973   5284     28    207    424       N
ATOM   6323  CA  PHE A 774     -73.070  15.545  20.089  1.00 36.31           C
ANISOU 6323  CA  PHE A 774     4377   4059   5359     29    222    471       C
ATOM   6324  C   PHE A 774     -72.933  15.654  21.601  1.00 37.42           C
ANISOU 6324  C   PHE A 774     4504   4243   5470     78    245    480       C
ATOM   6325  O   PHE A 774     -71.842  15.479  22.150  1.00 40.40           O
ANISOU 6325  O   PHE A 774     4901   4623   5826    105    248    461       O
ATOM   6326  CB  PHE A 774     -73.442  14.099  19.728  1.00 34.49           C
ANISOU 6326  CB  PHE A 774     4157   3798   5150    -11    220    505       C
ATOM   6327  CG  PHE A 774     -73.536  13.843  18.255  1.00 38.57           C
ANISOU 6327  CG  PHE A 774     4687   4279   5690    -58    196    489       C
ATOM   6328  CD1 PHE A 774     -72.394  13.641  17.495  1.00 36.41           C
ANISOU 6328  CD1 PHE A 774     4442   3980   5411    -62    182    447       C
ATOM   6329  CD2 PHE A 774     -74.770  13.794  17.628  1.00 37.02           C
ANISOU 6329  CD2 PHE A 774     4466   4084   5515    -96    186    513       C
ATOM   6330  CE1 PHE A 774     -72.483  13.402  16.135  1.00 36.70           C
ANISOU 6330  CE1 PHE A 774     4488   3997   5460   -104    160    428       C
ATOM   6331  CE2 PHE A 774     -74.865  13.554  16.271  1.00 35.91           C
ANISOU 6331  CE2 PHE A 774     4337   3918   5390   -138    161    495       C
ATOM   6332  CZ  PHE A 774     -73.722  13.358  15.523  1.00 33.42           C
ANISOU 6332  CZ  PHE A 774     4054   3580   5065   -142    149    453       C
ATOM   6333  N   GLU A 775     -74.047  15.921  22.281  1.00 31.14           N
ANISOU 6333  N   GLU A 775     3672   3492   4669     91    261    507       N
ATOM   6334  CA  GLU A 775     -74.074  15.936  23.738  1.00 33.58           C
ANISOU 6334  CA  GLU A 775     3960   3858   4939    134    287    520       C
ATOM   6335  C   GLU A 775     -74.856  14.735  24.250  1.00 41.27           C
ANISOU 6335  C   GLU A 775     4919   4851   5909    105    307    588       C
ATOM   6336  O   GLU A 775     -75.986  14.493  23.811  1.00 46.60           O
ANISOU 6336  O   GLU A 775     5566   5533   6606     66    310    619       O
ATOM   6337  CB  GLU A 775     -74.694  17.227  24.279  1.00 35.10           C
ANISOU 6337  CB  GLU A 775     4116   4102   5117    178    291    491       C
ATOM   6338  CG  GLU A 775     -74.796  17.245  25.802  1.00 38.62           C
ANISOU 6338  CG  GLU A 775     4534   4625   5515    225    320    499       C
ATOM   6339  CD  GLU A 775     -75.438  18.510  26.337  1.00 46.60           C
ANISOU 6339  CD  GLU A 775     5505   5690   6511    278    322    458       C
ATOM   6340  OE1 GLU A 775     -76.092  19.227  25.552  1.00 48.78           O
ANISOU 6340  OE1 GLU A 775     5770   5946   6820    275    302    439       O
ATOM   6341  OE2 GLU A 775     -75.289  18.788  27.546  1.00 52.46           O
ANISOU 6341  OE2 GLU A 775     6228   6497   7207    327    340    441       O
ATOM   6342  N   ARG A 776     -74.251  13.978  25.164  1.00 40.63           N
ANISOU 6342  N   ARG A 776     4857   4781   5801    121    320    616       N
ATOM   6343  CA  ARG A 776     -74.980  12.917  25.843  1.00 31.43           C
ANISOU 6343  CA  ARG A 776     3679   3638   4623     91    340    691       C
ATOM   6344  C   ARG A 776     -75.958  13.548  26.819  1.00 34.22           C
ANISOU 6344  C   ARG A 776     3974   4092   4938    113    371    706       C
ATOM   6345  O   ARG A 776     -75.596  14.432  27.597  1.00 35.09           O
ANISOU 6345  O   ARG A 776     4069   4256   5009    173    380    666       O
ATOM   6346  CB  ARG A 776     -74.041  11.968  26.576  1.00 32.36           C
ANISOU 6346  CB  ARG A 776     3840   3737   4719    107    338    722       C
ATOM   6347  CG  ARG A 776     -74.751  10.729  27.110  1.00 39.52           C
ANISOU 6347  CG  ARG A 776     4750   4644   5622     60    351    814       C
ATOM   6348  CD  ARG A 776     -73.777   9.624  27.450  1.00 41.50           C
ANISOU 6348  CD  ARG A 776     5061   4837   5871     70    332    846       C
ATOM   6349  NE  ARG A 776     -73.370   9.685  28.848  1.00 44.20           N
ANISOU 6349  NE  ARG A 776     5400   5248   6148    119    349    873       N
ATOM   6350  CZ  ARG A 776     -73.861   8.902  29.801  1.00 46.71           C
ANISOU 6350  CZ  ARG A 776     5719   5598   6433     96    366    962       C
ATOM   6351  NH1 ARG A 776     -74.779   7.991  29.510  1.00 40.28           N
ANISOU 6351  NH1 ARG A 776     4909   4746   5650     19    368   1033       N
ATOM   6352  NH2 ARG A 776     -73.432   9.032  31.049  1.00 54.51           N
ANISOU 6352  NH2 ARG A 776     6702   6657   7352    145    380    982       N
ATOM   6353  N   VAL A 777     -77.198  13.091  26.771  1.00 39.05           N
ANISOU 6353  N   VAL A 777     4546   4734   5557     64    387    757       N
ATOM   6354  CA  VAL A 777     -78.322  13.814  27.344  1.00 39.99           C
ANISOU 6354  CA  VAL A 777     4592   4955   5648     82    414    755       C
ATOM   6355  C   VAL A 777     -79.204  12.828  28.092  1.00 37.92           C
ANISOU 6355  C   VAL A 777     4295   4753   5358     31    446    841       C
ATOM   6356  O   VAL A 777     -79.463  11.722  27.610  1.00 39.30           O
ANISOU 6356  O   VAL A 777     4493   4873   5567    -42    438    898       O
ATOM   6357  CB  VAL A 777     -79.108  14.559  26.244  1.00 38.88           C
ANISOU 6357  CB  VAL A 777     4421   4802   5551     74    395    716       C
ATOM   6358  CG1 VAL A 777     -80.534  14.736  26.641  1.00 44.42           C
ANISOU 6358  CG1 VAL A 777     5041   5603   6234     65    420    738       C
ATOM   6359  CG2 VAL A 777     -78.451  15.917  25.959  1.00 36.66           C
ANISOU 6359  CG2 VAL A 777     4156   4500   5274    139    371    634       C
ATOM   6360  N   LYS A 778     -79.634  13.214  29.295  1.00 36.51           N
ANISOU 6360  N   LYS A 778     4065   4691   5116     67    482    850       N
ATOM   6361  CA  LYS A 778     -80.573  12.385  30.042  1.00 41.97           C
ANISOU 6361  CA  LYS A 778     4713   5464   5772     11    519    937       C
ATOM   6362  C   LYS A 778     -81.850  12.154  29.237  1.00 44.19           C
ANISOU 6362  C   LYS A 778     4941   5755   6094    -58    520    958       C
ATOM   6363  O   LYS A 778     -82.311  11.015  29.097  1.00 41.54           O
ANISOU 6363  O   LYS A 778     4612   5396   5776   -147    524   1036       O
ATOM   6364  CB  LYS A 778     -80.878  13.036  31.390  1.00 43.01           C
ANISOU 6364  CB  LYS A 778     4783   5740   5820     69    559    926       C
ATOM   6365  CG  LYS A 778     -81.352  12.063  32.440  1.00 50.11           C
ANISOU 6365  CG  LYS A 778     5658   6723   6659     16    598   1027       C
ATOM   6366  CD  LYS A 778     -81.297  12.669  33.829  1.00 61.92           C
ANISOU 6366  CD  LYS A 778     7109   8358   8058     85    634   1009       C
ATOM   6367  CE  LYS A 778     -79.865  12.900  34.272  1.00 72.49           C
ANISOU 6367  CE  LYS A 778     8516   9650   9375    154    612    972       C
ATOM   6368  NZ  LYS A 778     -79.786  13.409  35.671  1.00 79.20           N
ANISOU 6368  NZ  LYS A 778     9326  10642  10126    219    644    955       N
ATOM   6369  N   GLY A 779     -82.430  13.220  28.704  1.00 38.04           N
ANISOU 6369  N   GLY A 779     4113   5009   5333    -19    511    890       N
ATOM   6370  CA  GLY A 779     -83.542  13.134  27.778  1.00 44.18           C
ANISOU 6370  CA  GLY A 779     4842   5791   6153    -72    502    896       C
ATOM   6371  C   GLY A 779     -84.883  13.345  28.457  1.00 49.53           C
ANISOU 6371  C   GLY A 779     5411   6621   6788    -78    541    914       C
ATOM   6372  O   GLY A 779     -85.089  12.983  29.622  1.00 50.25           O
ANISOU 6372  O   GLY A 779     5470   6809   6816    -88    584    963       O
ATOM   6373  N   ALA A 780     -85.819  13.939  27.716  1.00 45.88           N
ANISOU 6373  N   ALA A 780     4888   6190   6354    -72    527    874       N
ATOM   6374  CA  ALA A 780     -87.165  14.177  28.226  1.00 49.09           C
ANISOU 6374  CA  ALA A 780     5177   6751   6724    -73    561    880       C
ATOM   6375  C   ALA A 780     -88.050  12.976  27.919  1.00 44.85           C
ANISOU 6375  C   ALA A 780     4604   6232   6205   -198    574    963       C
ATOM   6376  O   ALA A 780     -88.137  12.540  26.768  1.00 48.24           O
ANISOU 6376  O   ALA A 780     5064   6567   6699   -256    537    969       O
ATOM   6377  CB  ALA A 780     -87.767  15.445  27.621  1.00 52.29           C
ANISOU 6377  CB  ALA A 780     5530   7187   7151      6    533    793       C
ATOM   6378  N   VAL A 781     -88.697  12.447  28.950  1.00 39.39           N
ANISOU 6378  N   VAL A 781     3846   5666   5454   -245    625   1027       N
ATOM   6379  CA  VAL A 781     -89.464  11.211  28.854  1.00 45.49           C
ANISOU 6379  CA  VAL A 781     4589   6457   6238   -380    641   1120       C
ATOM   6380  C   VAL A 781     -90.923  11.587  28.642  1.00 49.10           C
ANISOU 6380  C   VAL A 781     4914   7054   6689   -396    656   1100       C
ATOM   6381  O   VAL A 781     -91.619  11.970  29.583  1.00 55.58           O
ANISOU 6381  O   VAL A 781     5635   8043   7439   -368    703   1098       O
ATOM   6382  CB  VAL A 781     -89.291  10.343  30.100  1.00 46.86           C
ANISOU 6382  CB  VAL A 781     4772   6685   6347   -436    687   1216       C
ATOM   6383  CG1 VAL A 781     -90.170   9.109  30.007  1.00 47.97           C
ANISOU 6383  CG1 VAL A 781     4879   6845   6501   -587    702   1318       C
ATOM   6384  CG2 VAL A 781     -87.835   9.961  30.275  1.00 45.19           C
ANISOU 6384  CG2 VAL A 781     4690   6336   6144   -411    665   1233       C
ATOM   6385  N   VAL A 782     -91.397  11.455  27.409  1.00 45.58           N
ANISOU 6385  N   VAL A 782     4461   6547   6311   -440    615   1082       N
ATOM   6386  CA  VAL A 782     -92.801  11.659  27.079  1.00 49.88           C
ANISOU 6386  CA  VAL A 782     4879   7216   6857   -468    621   1068       C
ATOM   6387  C   VAL A 782     -93.475  10.294  27.034  1.00 51.85           C
ANISOU 6387  C   VAL A 782     5102   7481   7119   -630    637   1166       C
ATOM   6388  O   VAL A 782     -93.112   9.438  26.217  1.00 49.57           O
ANISOU 6388  O   VAL A 782     4894   7047   6893   -711    600   1198       O
ATOM   6389  CB  VAL A 782     -92.963  12.405  25.746  1.00 47.38           C
ANISOU 6389  CB  VAL A 782     4565   6834   6602   -414    561    988       C
ATOM   6390  CG1 VAL A 782     -94.429  12.740  25.504  1.00 48.04           C
ANISOU 6390  CG1 VAL A 782     4507   7067   6680   -421    565    964       C
ATOM   6391  CG2 VAL A 782     -92.103  13.663  25.736  1.00 42.80           C
ANISOU 6391  CG2 VAL A 782     4041   6202   6020   -270    537    903       C
ATOM   6392  N   THR A 783     -94.448  10.083  27.914  1.00 49.48           N
ANISOU 6392  N   THR A 783     4687   7355   6757   -679    693   1211       N
ATOM   6393  CA  THR A 783     -95.143   8.809  27.992  1.00 53.14           C
ANISOU 6393  CA  THR A 783     5117   7845   7227   -846    712   1313       C
ATOM   6394  C   THR A 783     -96.641   9.063  28.025  1.00 65.70           C
ANISOU 6394  C   THR A 783     6539   9633   8790   -879    739   1301       C
ATOM   6395  O   THR A 783     -97.101  10.133  28.436  1.00 73.17           O
ANISOU 6395  O   THR A 783     7389  10726   9686   -769    762   1230       O
ATOM   6396  CB  THR A 783     -94.708   7.997  29.227  1.00 49.06           C
ANISOU 6396  CB  THR A 783     4642   7348   6651   -909    760   1418       C
ATOM   6397  OG1 THR A 783     -95.244   6.672  29.150  1.00 41.78           O
ANISOU 6397  OG1 THR A 783     3717   6404   5752  -1083    765   1525       O
ATOM   6398  CG2 THR A 783     -95.181   8.659  30.504  1.00 46.04           C
ANISOU 6398  CG2 THR A 783     4150   7180   6163   -847    827   1412       C
ATOM   6399  N   GLY A 784     -97.400   8.081  27.569  1.00 63.03           N
ANISOU 6399  N   GLY A 784     6164   9297   8487  -1030    734   1363       N
ATOM   6400  CA  GLY A 784     -98.830   8.284  27.493  1.00 59.42           C
ANISOU 6400  CA  GLY A 784     5539   9028   8008  -1069    755   1347       C
ATOM   6401  C   GLY A 784     -99.587   7.009  27.210  1.00 55.60           C
ANISOU 6401  C   GLY A 784     5022   8548   7556  -1265    756   1437       C
ATOM   6402  O   GLY A 784     -99.060   6.057  26.625  1.00 56.89           O
ANISOU 6402  O   GLY A 784     5300   8529   7786  -1359    716   1486       O
ATOM   6403  N   LYS A 785    -100.843   7.008  27.645  1.00 54.72           N
ANISOU 6403  N   LYS A 785     4745   8651   7393  -1326    801   1456       N
ATOM   6404  CA  LYS A 785    -101.763   5.951  27.274  1.00 54.97           C
ANISOU 6404  CA  LYS A 785     4716   8713   7457  -1514    799   1526       C
ATOM   6405  C   LYS A 785    -102.071   6.050  25.788  1.00 52.43           C
ANISOU 6405  C   LYS A 785     4395   8301   7223  -1515    724   1453       C
ATOM   6406  O   LYS A 785    -101.937   7.109  25.171  1.00 47.41           O
ANISOU 6406  O   LYS A 785     3754   7655   6603  -1366    688   1347       O
ATOM   6407  CB  LYS A 785    -103.047   6.054  28.096  1.00 59.70           C
ANISOU 6407  CB  LYS A 785     5121   9590   7973  -1569    869   1552       C
ATOM   6408  CG  LYS A 785    -103.807   4.741  28.226  1.00 72.69           C
ANISOU 6408  CG  LYS A 785     6719  11276   9625  -1799    890   1671       C
ATOM   6409  CD  LYS A 785    -103.381   3.966  29.472  1.00 78.30           C
ANISOU 6409  CD  LYS A 785     7484  11995  10273  -1891    948   1802       C
ATOM   6410  CE  LYS A 785    -103.258   2.476  29.181  1.00 78.82           C
ANISOU 6410  CE  LYS A 785     7649  11892  10404  -2095    919   1922       C
ATOM   6411  NZ  LYS A 785    -104.422   1.986  28.396  1.00 81.83           N
ANISOU 6411  NZ  LYS A 785     7923  12332  10835  -2240    897   1923       N
ATOM   6412  N   VAL A 786    -102.500   4.935  25.212  1.00 58.25           N
ANISOU 6412  N   VAL A 786     5140   8975   8018  -1687    698   1511       N
ATOM   6413  CA  VAL A 786    -102.649   4.850  23.769  1.00 56.65           C
ANISOU 6413  CA  VAL A 786     4961   8662   7900  -1702    621   1449       C
ATOM   6414  C   VAL A 786    -103.931   4.101  23.439  1.00 67.94           C
ANISOU 6414  C   VAL A 786     6268  10198   9349  -1875    619   1485       C
ATOM   6415  O   VAL A 786    -104.441   3.313  24.241  1.00 68.10           O
ANISOU 6415  O   VAL A 786     6233  10304   9336  -2020    669   1583       O
ATOM   6416  CB  VAL A 786    -101.420   4.175  23.130  1.00 58.90           C
ANISOU 6416  CB  VAL A 786     5444   8677   8259  -1720    566   1462       C
ATOM   6417  CG1 VAL A 786    -101.534   2.663  23.210  1.00 51.73           C
ANISOU 6417  CG1 VAL A 786     4587   7677   7391  -1922    560   1568       C
ATOM   6418  CG2 VAL A 786    -101.222   4.663  21.720  1.00 62.81           C
ANISOU 6418  CG2 VAL A 786     5977   9071   8815  -1643    490   1361       C
ATOM   6419  N   SER A 787    -104.461   4.367  22.248  1.00 74.29           N
ANISOU 6419  N   SER A 787     7025  11000  10203  -1862    560   1406       N
ATOM   6420  CA  SER A 787    -105.720   3.770  21.806  1.00 75.16           C
ANISOU 6420  CA  SER A 787     7005  11220  10334  -2015    549   1421       C
ATOM   6421  C   SER A 787    -105.461   2.444  21.092  1.00 82.58           C
ANISOU 6421  C   SER A 787     8056  11963  11358  -2183    496   1471       C
ATOM   6422  O   SER A 787    -105.752   2.271  19.910  1.00 89.87           O
ANISOU 6422  O   SER A 787     8978  12826  12342  -2216    429   1414       O
ATOM   6423  CB  SER A 787    -106.479   4.739  20.909  1.00 73.06           C
ANISOU 6423  CB  SER A 787     6621  11065  10073  -1911    507   1308       C
ATOM   6424  OG  SER A 787    -106.016   4.673  19.572  1.00 69.29           O
ANISOU 6424  OG  SER A 787     6246  10410   9670  -1888    422   1250       O
ATOM   6425  N   ALA A 788    -104.893   1.504  21.845  1.00 86.85           N
ANISOU 6425  N   ALA A 788     8697  12402  11901  -2285    524   1576       N
ATOM   6426  CA  ALA A 788    -104.714   0.147  21.351  1.00 87.30           C
ANISOU 6426  CA  ALA A 788     8858  12276  12038  -2458    477   1634       C
ATOM   6427  C   ALA A 788    -106.042  -0.388  20.825  1.00 76.24           C
ANISOU 6427  C   ALA A 788     7321  10984  10664  -2623    459   1638       C
ATOM   6428  O   ALA A 788    -107.106  -0.067  21.358  1.00 77.14           O
ANISOU 6428  O   ALA A 788     7258  11333  10717  -2660    511   1652       O
ATOM   6429  CB  ALA A 788    -104.158  -0.739  22.468  1.00 97.81           C
ANISOU 6429  CB  ALA A 788    10283  13530  13350  -2552    519   1765       C
ATOM   6430  N   ASN A 789    -105.995  -1.217  19.779  1.00 60.62           N
ANISOU 6430  N   ASN A 789     5417   8843   8774  -2725    384   1619       N
ATOM   6431  CA  ASN A 789    -104.800  -1.909  19.297  1.00 68.59           C
ANISOU 6431  CA  ASN A 789     6632   9575   9854  -2724    327   1621       C
ATOM   6432  C   ASN A 789    -103.917  -1.111  18.344  1.00 69.27           C
ANISOU 6432  C   ASN A 789     6807   9552   9961  -2538    276   1505       C
ATOM   6433  O   ASN A 789    -104.146  -1.075  17.130  1.00 76.43           O
ANISOU 6433  O   ASN A 789     7707  10420  10914  -2536    210   1421       O
ATOM   6434  CB  ASN A 789    -105.208  -3.220  18.624  1.00 72.37           C
ANISOU 6434  CB  ASN A 789     7146   9933  10418  -2927    267   1648       C
ATOM   6435  CG  ASN A 789    -106.384  -3.887  19.311  1.00 79.09           C
ANISOU 6435  CG  ASN A 789     7891  10920  11240  -3094    311   1723       C
ATOM   6436  OD1 ASN A 789    -107.493  -3.917  18.781  1.00 77.74           O
ANISOU 6436  OD1 ASN A 789     7600  10865  11073  -3157    296   1672       O
ATOM   6437  ND2 ASN A 789    -106.146  -4.422  20.506  1.00 83.22           N
ANISOU 6437  ND2 ASN A 789     8478  11420  11722  -3135    366   1824       N
ATOM   6438  N   VAL A 790    -102.897  -0.480  18.910  1.00 57.64           N
ANISOU 6438  N   VAL A 790     5417   8034   8450  -2387    306   1504       N
ATOM   6439  CA  VAL A 790    -101.810   0.141  18.172  1.00 65.63           C
ANISOU 6439  CA  VAL A 790     6543   8912   9480  -2225    263   1416       C
ATOM   6440  C   VAL A 790    -100.529  -0.522  18.641  1.00 59.18           C
ANISOU 6440  C   VAL A 790     5900   7901   8685  -2220    262   1469       C
ATOM   6441  O   VAL A 790    -100.301  -0.663  19.843  1.00 54.16           O
ANISOU 6441  O   VAL A 790     5276   7297   8005  -2231    319   1555       O
ATOM   6442  CB  VAL A 790    -101.750   1.656  18.390  1.00 74.81           C
ANISOU 6442  CB  VAL A 790     7637  10210  10576  -2035    294   1353       C
ATOM   6443  CG1 VAL A 790    -102.901   2.337  17.684  1.00 75.92           C
ANISOU 6443  CG1 VAL A 790     7624  10513  10708  -2016    274   1282       C
ATOM   6444  CG2 VAL A 790    -101.823   1.934  19.853  1.00 79.35           C
ANISOU 6444  CG2 VAL A 790     8160  10911  11079  -2014    377   1424       C
ATOM   6445  N   THR A 791     -99.701  -0.947  17.706  1.00 60.65           N
ANISOU 6445  N   THR A 791     6218   7894   8933  -2202    196   1418       N
ATOM   6446  CA  THR A 791     -98.567  -1.762  18.101  1.00 66.75           C
ANISOU 6446  CA  THR A 791     7151   8476   9736  -2213    186   1469       C
ATOM   6447  C   THR A 791     -97.305  -0.939  18.341  1.00 62.08           C
ANISOU 6447  C   THR A 791     6645   7834   9110  -2031    201   1431       C
ATOM   6448  O   THR A 791     -96.512  -1.287  19.225  1.00 60.86           O
ANISOU 6448  O   THR A 791     6577   7605   8940  -2015    226   1496       O
ATOM   6449  CB  THR A 791     -98.328  -2.855  17.051  1.00 78.56           C
ANISOU 6449  CB  THR A 791     8746   9781  11321  -2305    106   1437       C
ATOM   6450  OG1 THR A 791     -97.285  -3.722  17.505  1.00 86.95           O
ANISOU 6450  OG1 THR A 791     9962  10658  12415  -2318     92   1491       O
ATOM   6451  CG2 THR A 791     -97.963  -2.260  15.694  1.00 79.28           C
ANISOU 6451  CG2 THR A 791     8860   9830  11431  -2200     50   1308       C
ATOM   6452  N   GLU A 792     -97.110   0.158  17.612  1.00 62.83           N
ANISOU 6452  N   GLU A 792     6715   7970   9187  -1896    186   1332       N
ATOM   6453  CA  GLU A 792     -95.933   0.996  17.783  1.00 61.29           C
ANISOU 6453  CA  GLU A 792     6596   7731   8960  -1732    197   1292       C
ATOM   6454  C   GLU A 792     -96.350   2.460  17.771  1.00 60.29           C
ANISOU 6454  C   GLU A 792     6363   7765   8778  -1609    223   1236       C
ATOM   6455  O   GLU A 792     -97.458   2.814  17.364  1.00 62.84           O
ANISOU 6455  O   GLU A 792     6566   8215   9095  -1636    217   1210       O
ATOM   6456  CB  GLU A 792     -94.882   0.715  16.698  1.00 62.14           C
ANISOU 6456  CB  GLU A 792     6833   7660   9119  -1687    133   1221       C
ATOM   6457  CG  GLU A 792     -95.427   0.646  15.277  1.00 71.27           C
ANISOU 6457  CG  GLU A 792     7959   8806  10316  -1724     72   1143       C
ATOM   6458  CD  GLU A 792     -95.892   1.995  14.752  1.00 88.37           C
ANISOU 6458  CD  GLU A 792    10029  11108  12440  -1621     73   1075       C
ATOM   6459  OE1 GLU A 792     -95.045   2.903  14.603  1.00 93.18           O
ANISOU 6459  OE1 GLU A 792    10684  11698  13022  -1486     75   1029       O
ATOM   6460  OE2 GLU A 792     -97.108   2.150  14.498  1.00 95.35           O
ANISOU 6460  OE2 GLU A 792    10792  12117  13320  -1677     69   1070       O
ATOM   6461  N   VAL A 793     -95.437   3.315  18.220  1.00 58.67           N
ANISOU 6461  N   VAL A 793     6205   7552   8534  -1470    246   1214       N
ATOM   6462  CA  VAL A 793     -95.639   4.759  18.227  1.00 56.29           C
ANISOU 6462  CA  VAL A 793     5828   7373   8185  -1336    262   1156       C
ATOM   6463  C   VAL A 793     -94.378   5.413  17.680  1.00 50.80           C
ANISOU 6463  C   VAL A 793     5239   6566   7495  -1211    234   1091       C
ATOM   6464  O   VAL A 793     -93.264   4.971  17.979  1.00 57.29           O
ANISOU 6464  O   VAL A 793     6173   7268   8325  -1196    235   1110       O
ATOM   6465  CB  VAL A 793     -95.972   5.269  19.647  1.00 57.52           C
ANISOU 6465  CB  VAL A 793     5906   7675   8273  -1299    334   1203       C
ATOM   6466  CG1 VAL A 793     -95.947   6.783  19.696  1.00 57.21           C
ANISOU 6466  CG1 VAL A 793     5818   7729   8193  -1141    343   1132       C
ATOM   6467  CG2 VAL A 793     -97.330   4.744  20.086  1.00 59.17           C
ANISOU 6467  CG2 VAL A 793     5987   8025   8469  -1424    364   1260       C
ATOM   6468  N   SER A 794     -94.543   6.453  16.861  1.00 47.67           N
ANISOU 6468  N   SER A 794     4809   6210   7092  -1123    204   1017       N
ATOM   6469  CA  SER A 794     -93.400   7.103  16.229  1.00 47.26           C
ANISOU 6469  CA  SER A 794     4852   6060   7043  -1017    175    959       C
ATOM   6470  C   SER A 794     -93.330   8.579  16.605  1.00 45.76           C
ANISOU 6470  C   SER A 794     4624   5955   6809   -880    193    923       C
ATOM   6471  O   SER A 794     -94.343   9.209  16.915  1.00 50.90           O
ANISOU 6471  O   SER A 794     5162   6742   7434   -855    209    918       O
ATOM   6472  CB  SER A 794     -93.447   6.965  14.703  1.00 50.28           C
ANISOU 6472  CB  SER A 794     5259   6381   7462  -1040    109    902       C
ATOM   6473  OG  SER A 794     -94.257   7.974  14.126  1.00 60.43           O
ANISOU 6473  OG  SER A 794     6458   7771   8732   -985     87    859       O
ATOM   6474  N   VAL A 795     -92.113   9.117  16.580  1.00 44.34           N
ANISOU 6474  N   VAL A 795     4536   5691   6620   -791    189    894       N
ATOM   6475  CA  VAL A 795     -91.833  10.520  16.858  1.00 43.85           C
ANISOU 6475  CA  VAL A 795     4463   5674   6524   -661    196    855       C
ATOM   6476  C   VAL A 795     -90.968  11.056  15.729  1.00 42.52           C
ANISOU 6476  C   VAL A 795     4376   5409   6370   -607    148    802       C
ATOM   6477  O   VAL A 795     -90.064  10.362  15.249  1.00 44.41           O
ANISOU 6477  O   VAL A 795     4707   5537   6631   -643    131    799       O
ATOM   6478  CB  VAL A 795     -91.120  10.714  18.214  1.00 44.03           C
ANISOU 6478  CB  VAL A 795     4515   5704   6511   -609    248    880       C
ATOM   6479  CG1 VAL A 795     -91.047  12.193  18.574  1.00 37.06           C
ANISOU 6479  CG1 VAL A 795     3603   4882   5594   -480    254    833       C
ATOM   6480  CG2 VAL A 795     -91.814   9.919  19.311  1.00 47.10           C
ANISOU 6480  CG2 VAL A 795     4841   6176   6879   -686    298    948       C
ATOM   6481  N   ASN A 796     -91.233  12.301  15.330  1.00 42.26           N
ANISOU 6481  N   ASN A 796     4312   5422   6325   -519    124    760       N
ATOM   6482  CA  ASN A 796     -90.623  12.913  14.157  1.00 40.67           C
ANISOU 6482  CA  ASN A 796     4173   5149   6130   -477     73    717       C
ATOM   6483  C   ASN A 796     -90.363  14.388  14.440  1.00 35.64           C
ANISOU 6483  C   ASN A 796     3538   4532   5470   -357     69    688       C
ATOM   6484  O   ASN A 796     -91.221  15.085  14.982  1.00 39.81           O
ANISOU 6484  O   ASN A 796     3984   5156   5984   -303     78    681       O
ATOM   6485  CB  ASN A 796     -91.549  12.706  12.934  1.00 48.82           C
ANISOU 6485  CB  ASN A 796     5158   6210   7181   -526     23    702       C
ATOM   6486  CG  ASN A 796     -91.390  13.765  11.843  1.00 55.17           C
ANISOU 6486  CG  ASN A 796     5987   6997   7977   -458    -31    663       C
ATOM   6487  OD1 ASN A 796     -90.394  14.485  11.764  1.00 69.97           O
ANISOU 6487  OD1 ASN A 796     7936   8811   9840   -395    -36    648       O
ATOM   6488  ND2 ASN A 796     -92.388  13.841  10.975  1.00 48.20           N
ANISOU 6488  ND2 ASN A 796     5042   6172   7101   -478    -75    651       N
ATOM   6489  N   ALA A 797     -89.181  14.864  14.061  1.00 30.43           N
ANISOU 6489  N   ALA A 797     2971   3784   4807   -316     54    667       N
ATOM   6490  CA  ALA A 797     -88.864  16.280  14.201  1.00 39.41           C
ANISOU 6490  CA  ALA A 797     4125   4920   5930   -212     40    638       C
ATOM   6491  C   ALA A 797     -87.823  16.664  13.165  1.00 42.83           C
ANISOU 6491  C   ALA A 797     4649   5260   6364   -204      2    620       C
ATOM   6492  O   ALA A 797     -87.077  15.822  12.670  1.00 50.38           O
ANISOU 6492  O   ALA A 797     5663   6153   7325   -264      3    623       O
ATOM   6493  CB  ALA A 797     -88.359  16.620  15.606  1.00 33.05           C
ANISOU 6493  CB  ALA A 797     3325   4128   5104   -157     88    639       C
ATOM   6494  N   THR A 798     -87.777  17.950  12.835  1.00 42.49           N
ANISOU 6494  N   THR A 798     4619   5209   6314   -129    -32    600       N
ATOM   6495  CA  THR A 798     -86.819  18.465  11.867  1.00 43.19           C
ANISOU 6495  CA  THR A 798     4792   5220   6397   -124    -68    589       C
ATOM   6496  C   THR A 798     -85.747  19.277  12.582  1.00 43.93           C
ANISOU 6496  C   THR A 798     4944   5267   6482    -67    -51    576       C
ATOM   6497  O   THR A 798     -86.062  20.206  13.335  1.00 41.79           O
ANISOU 6497  O   THR A 798     4648   5020   6211      8    -50    563       O
ATOM   6498  CB  THR A 798     -87.512  19.321  10.807  1.00 41.33           C
ANISOU 6498  CB  THR A 798     4542   5000   6162    -94   -130    586       C
ATOM   6499  OG1 THR A 798     -88.634  18.604  10.279  1.00 47.96           O
ANISOU 6499  OG1 THR A 798     5312   5902   7009   -142   -147    593       O
ATOM   6500  CG2 THR A 798     -86.546  19.640   9.676  1.00 33.90           C
ANISOU 6500  CG2 THR A 798     3685   3989   5206   -115   -165    586       C
ATOM   6501  N   ILE A 799     -84.485  18.929  12.342  1.00 42.48           N
ANISOU 6501  N   ILE A 799     4833   5019   6290   -101    -39    573       N
ATOM   6502  CA  ILE A 799     -83.351  19.607  12.954  1.00 40.22           C
ANISOU 6502  CA  ILE A 799     4601   4687   5993    -61    -24    558       C
ATOM   6503  C   ILE A 799     -82.619  20.401  11.884  1.00 35.30           C
ANISOU 6503  C   ILE A 799     4042   4010   5361    -64    -65    553       C
ATOM   6504  O   ILE A 799     -82.443  19.927  10.754  1.00 31.54           O
ANISOU 6504  O   ILE A 799     3587   3521   4876   -119    -85    559       O
ATOM   6505  CB  ILE A 799     -82.405  18.605  13.644  1.00 39.06           C
ANISOU 6505  CB  ILE A 799     4481   4519   5839    -94     23    558       C
ATOM   6506  CG1 ILE A 799     -83.208  17.627  14.508  1.00 34.90           C
ANISOU 6506  CG1 ILE A 799     3896   4045   5320   -114     59    578       C
ATOM   6507  CG2 ILE A 799     -81.371  19.339  14.482  1.00 34.41           C
ANISOU 6507  CG2 ILE A 799     3931   3903   5238    -45     41    538       C
ATOM   6508  CD1 ILE A 799     -84.058  18.299  15.567  1.00 35.26           C
ANISOU 6508  CD1 ILE A 799     3879   4158   5361    -51     75    577       C
ATOM   6509  N   LYS A 800     -82.211  21.619  12.238  1.00 38.87           N
ANISOU 6509  N   LYS A 800     4524   4432   5813     -8    -79    542       N
ATOM   6510  CA  LYS A 800     -81.401  22.482  11.386  1.00 38.78           C
ANISOU 6510  CA  LYS A 800     4580   4365   5791    -17   -115    545       C
ATOM   6511  C   LYS A 800     -80.082  22.758  12.093  1.00 39.25           C
ANISOU 6511  C   LYS A 800     4685   4386   5842    -12    -87    526       C
ATOM   6512  O   LYS A 800     -80.068  23.059  13.292  1.00 38.99           O
ANISOU 6512  O   LYS A 800     4637   4360   5816     39    -65    506       O
ATOM   6513  CB  LYS A 800     -82.130  23.793  11.073  1.00 41.53           C
ANISOU 6513  CB  LYS A 800     4928   4698   6151     41   -172    553       C
ATOM   6514  CG  LYS A 800     -81.518  24.628   9.950  1.00 39.60           C
ANISOU 6514  CG  LYS A 800     4753   4399   5894     16   -219    575       C
ATOM   6515  CD  LYS A 800     -81.951  26.088  10.062  1.00 42.84           C
ANISOU 6515  CD  LYS A 800     5183   4768   6326     88   -273    578       C
ATOM   6516  CE  LYS A 800     -81.726  26.862   8.767  1.00 51.93           C
ANISOU 6516  CE  LYS A 800     6395   5872   7462     59   -334    618       C
ATOM   6517  NZ  LYS A 800     -82.881  26.774   7.824  1.00 51.86           N
ANISOU 6517  NZ  LYS A 800     6354   5902   7450     66   -380    644       N
ATOM   6518  N   THR A 801     -78.981  22.644  11.361  1.00 39.79           N
ANISOU 6518  N   THR A 801     4805   4424   5889    -64    -88    527       N
ATOM   6519  CA  THR A 801     -77.656  22.795  11.941  1.00 41.25           C
ANISOU 6519  CA  THR A 801     5027   4583   6063    -69    -62    506       C
ATOM   6520  C   THR A 801     -77.094  24.181  11.643  1.00 40.81           C
ANISOU 6520  C   THR A 801     5022   4478   6006    -62    -98    509       C
ATOM   6521  O   THR A 801     -77.644  24.951  10.852  1.00 38.40           O
ANISOU 6521  O   THR A 801     4733   4153   5706    -60   -146    534       O
ATOM   6522  CB  THR A 801     -76.703  21.714  11.417  1.00 42.84           C
ANISOU 6522  CB  THR A 801     5244   4793   6241   -130    -36    497       C
ATOM   6523  OG1 THR A 801     -76.413  21.952  10.032  1.00 43.39           O
ANISOU 6523  OG1 THR A 801     5343   4857   6288   -180    -66    511       O
ATOM   6524  CG2 THR A 801     -77.318  20.325  11.582  1.00 39.14           C
ANISOU 6524  CG2 THR A 801     4735   4355   5781   -143    -12    498       C
ATOM   6525  N   ASN A 802     -75.963  24.485  12.286  1.00 39.48           N
ANISOU 6525  N   ASN A 802     4881   4290   5831    -63    -78    485       N
ATOM   6526  CA  ASN A 802     -75.305  25.775  12.114  1.00 38.11           C
ANISOU 6526  CA  ASN A 802     4758   4063   5658    -69   -110    487       C
ATOM   6527  C   ASN A 802     -74.781  25.991  10.700  1.00 39.78           C
ANISOU 6527  C   ASN A 802     5009   4263   5843   -143   -135    519       C
ATOM   6528  O   ASN A 802     -74.300  27.090  10.402  1.00 47.16           O
ANISOU 6528  O   ASN A 802     5991   5150   6778   -162   -168    535       O
ATOM   6529  CB  ASN A 802     -74.162  25.919  13.121  1.00 35.76           C
ANISOU 6529  CB  ASN A 802     4472   3758   5356    -63    -80    449       C
ATOM   6530  CG  ASN A 802     -73.246  24.713  13.140  1.00 37.42           C
ANISOU 6530  CG  ASN A 802     4669   4010   5538   -103    -34    433       C
ATOM   6531  OD1 ASN A 802     -73.677  23.600  13.435  1.00 36.72           O
ANISOU 6531  OD1 ASN A 802     4544   3958   5450    -90     -5    431       O
ATOM   6532  ND2 ASN A 802     -71.970  24.930  12.833  1.00 40.54           N
ANISOU 6532  ND2 ASN A 802     5092   4402   5911   -152    -28    422       N
ATOM   6533  N   GLN A 803     -74.853  24.980   9.833  1.00 30.84           N
ANISOU 6533  N   GLN A 803     3859   3173   4685   -187   -122    530       N
ATOM   6534  CA  GLN A 803     -74.527  25.127   8.422  1.00 26.52           C
ANISOU 6534  CA  GLN A 803     3341   2633   4103   -253   -147    561       C
ATOM   6535  C   GLN A 803     -75.771  25.278   7.553  1.00 40.92           C
ANISOU 6535  C   GLN A 803     5157   4461   5929   -245   -191    598       C
ATOM   6536  O   GLN A 803     -75.685  25.128   6.329  1.00 27.14           O
ANISOU 6536  O   GLN A 803     3425   2741   4146   -299   -209    622       O
ATOM   6537  CB  GLN A 803     -73.692  23.938   7.946  1.00 35.14           C
ANISOU 6537  CB  GLN A 803     4419   3776   5157   -305   -107    536       C
ATOM   6538  CG  GLN A 803     -72.457  23.652   8.801  1.00 32.89           C
ANISOU 6538  CG  GLN A 803     4133   3498   4867   -306    -64    496       C
ATOM   6539  CD  GLN A 803     -71.426  24.764   8.727  1.00 33.94           C
ANISOU 6539  CD  GLN A 803     4304   3609   4984   -342    -75    502       C
ATOM   6540  OE1 GLN A 803     -70.701  25.018   9.689  1.00 34.99           O
ANISOU 6540  OE1 GLN A 803     4438   3729   5128   -325    -56    474       O
ATOM   6541  NE2 GLN A 803     -71.354  25.431   7.580  1.00 34.56           N
ANISOU 6541  NE2 GLN A 803     4414   3683   5034   -397   -107    543       N
ATOM   6542  N   ASN A 804     -76.921  25.571   8.166  1.00 36.69           N
ANISOU 6542  N   ASN A 804     4595   3912   5432   -177   -210    599       N
ATOM   6543  CA  ASN A 804     -78.219  25.648   7.495  1.00 41.53           C
ANISOU 6543  CA  ASN A 804     5186   4540   6052   -156   -253    626       C
ATOM   6544  C   ASN A 804     -78.600  24.338   6.812  1.00 45.51           C
ANISOU 6544  C   ASN A 804     5651   5106   6535   -196   -236    621       C
ATOM   6545  O   ASN A 804     -79.442  24.327   5.908  1.00 48.19           O
ANISOU 6545  O   ASN A 804     5977   5467   6864   -203   -275    645       O
ATOM   6546  CB  ASN A 804     -78.265  26.799   6.483  1.00 45.63           C
ANISOU 6546  CB  ASN A 804     5759   5021   6558   -171   -317    675       C
ATOM   6547  CG  ASN A 804     -77.879  28.127   7.098  1.00 51.61           C
ANISOU 6547  CG  ASN A 804     6565   5702   7342   -137   -343    680       C
ATOM   6548  OD1 ASN A 804     -78.198  28.407   8.254  1.00 51.06           O
ANISOU 6548  OD1 ASN A 804     6477   5613   7312    -68   -335    646       O
ATOM   6549  ND2 ASN A 804     -77.178  28.951   6.328  1.00 53.11           N
ANISOU 6549  ND2 ASN A 804     6819   5850   7509   -190   -376    721       N
ATOM   6550  N   ARG A 805     -77.988  23.233   7.226  1.00 39.09           N
ANISOU 6550  N   ARG A 805     4820   4315   5715   -221   -184    588       N
ATOM   6551  CA  ARG A 805     -78.363  21.913   6.747  1.00 38.24           C
ANISOU 6551  CA  ARG A 805     4679   4253   5600   -254   -169    574       C
ATOM   6552  C   ARG A 805     -79.454  21.344   7.643  1.00 41.88           C
ANISOU 6552  C   ARG A 805     5082   4731   6099   -215   -154    566       C
ATOM   6553  O   ARG A 805     -79.463  21.576   8.856  1.00 39.56           O
ANISOU 6553  O   ARG A 805     4777   4426   5829   -168   -130    556       O
ATOM   6554  CB  ARG A 805     -77.149  20.983   6.730  1.00 36.33           C
ANISOU 6554  CB  ARG A 805     4450   4018   5334   -296   -127    541       C
ATOM   6555  CG  ARG A 805     -77.429  19.578   6.225  1.00 31.32           C
ANISOU 6555  CG  ARG A 805     3790   3416   4696   -330   -117    518       C
ATOM   6556  CD  ARG A 805     -76.159  18.740   6.239  1.00 40.17           C
ANISOU 6556  CD  ARG A 805     4927   4539   5796   -355    -82    477       C
ATOM   6557  NE  ARG A 805     -75.697  18.458   7.596  1.00 38.32           N
ANISOU 6557  NE  ARG A 805     4690   4282   5590   -320    -43    462       N
ATOM   6558  CZ  ARG A 805     -76.085  17.406   8.310  1.00 38.14           C
ANISOU 6558  CZ  ARG A 805     4643   4252   5596   -308    -22    452       C
ATOM   6559  NH1 ARG A 805     -76.943  16.535   7.796  1.00 32.37           N
ANISOU 6559  NH1 ARG A 805     3890   3531   4877   -334    -36    451       N
ATOM   6560  NH2 ARG A 805     -75.614  17.222   9.535  1.00 42.83           N
ANISOU 6560  NH2 ARG A 805     5238   4831   6206   -275     10    445       N
ATOM   6561  N   THR A 806     -80.375  20.598   7.045  1.00 36.77           N
ANISOU 6561  N   THR A 806     4397   4119   5453   -237   -169    569       N
ATOM   6562  CA  THR A 806     -81.518  20.092   7.784  1.00 38.35           C
ANISOU 6562  CA  THR A 806     4536   4348   5686   -212   -158    568       C
ATOM   6563  C   THR A 806     -81.643  18.585   7.601  1.00 37.11           C
ANISOU 6563  C   THR A 806     4356   4210   5534   -266   -136    552       C
ATOM   6564  O   THR A 806     -81.310  18.033   6.547  1.00 41.21           O
ANISOU 6564  O   THR A 806     4895   4733   6030   -316   -151    540       O
ATOM   6565  CB  THR A 806     -82.807  20.811   7.352  1.00 42.62           C
ANISOU 6565  CB  THR A 806     5040   4917   6236   -179   -208    589       C
ATOM   6566  OG1 THR A 806     -83.751  20.782   8.429  1.00 56.40           O
ANISOU 6566  OG1 THR A 806     6724   6693   8011   -132   -191    586       O
ATOM   6567  CG2 THR A 806     -83.413  20.168   6.113  1.00 34.24           C
ANISOU 6567  CG2 THR A 806     3959   3892   5159   -230   -240    593       C
ATOM   6568  N   PHE A 807     -82.103  17.921   8.657  1.00 32.44           N
ANISOU 6568  N   PHE A 807     3725   3631   4970   -258   -103    551       N
ATOM   6569  CA  PHE A 807     -82.336  16.486   8.599  1.00 32.80           C
ANISOU 6569  CA  PHE A 807     3752   3682   5029   -312    -87    542       C
ATOM   6570  C   PHE A 807     -83.514  16.129   9.495  1.00 39.28           C
ANISOU 6570  C   PHE A 807     4506   4541   5877   -306    -71    561       C
ATOM   6571  O   PHE A 807     -84.040  16.966  10.236  1.00 44.66           O
ANISOU 6571  O   PHE A 807     5153   5251   6563   -251    -66    573       O
ATOM   6572  CB  PHE A 807     -81.080  15.691   8.982  1.00 32.49           C
ANISOU 6572  CB  PHE A 807     3759   3600   4987   -328    -53    522       C
ATOM   6573  CG  PHE A 807     -80.624  15.897  10.403  1.00 32.87           C
ANISOU 6573  CG  PHE A 807     3810   3637   5042   -285    -12    530       C
ATOM   6574  CD1 PHE A 807     -79.709  16.889  10.714  1.00 31.18           C
ANISOU 6574  CD1 PHE A 807     3630   3407   4811   -244     -6    522       C
ATOM   6575  CD2 PHE A 807     -81.086  15.078  11.421  1.00 30.45           C
ANISOU 6575  CD2 PHE A 807     3474   3339   4757   -291     18    546       C
ATOM   6576  CE1 PHE A 807     -79.277  17.073  12.017  1.00 31.91