CNRS Nantes University UFIP UFIP
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***  pablo  ***

elNémo ID: 191103230454114720

Job options:

ID        	=	 191103230454114720
JOBID     	=	 pablo
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER pablo

HEADER    SIGNALING PROTEIN                       29-OCT-18   6MW4              
TITLE     STRUCTURE OF PSEUDOPROTEASE CSPC FROM CLOSTRIDIOIDES DIFFICILE        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE GERMINATION-SPECIFIC PROTEASE;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CSPC;                                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PEPTOCLOSTRIDIUM DIFFICILE (STRAIN R20291);     
SOURCE   3 ORGANISM_TAXID: 645463;                                              
SOURCE   4 STRAIN: R20291;                                                      
SOURCE   5 GENE: CSPC, CDR20291_2146;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    CSPC, PEPTIDASE S8 FAMILY DOMAIN IN CSPA-LIKE PROTEINS, SIGNALING     
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.E.ECKENROTH,S.DOUBLIE                                               
REVDAT   2   24-JUL-19 6MW4    1       JRNL                                     
REVDAT   1   26-JUN-19 6MW4    0                                                
JRNL        AUTH   A.E.ROHLFING,B.E.ECKENROTH,E.R.FORSTER,Y.KEVORKIAN,          
JRNL        AUTH 2 M.L.DONNELLY,H.BENITO DE LA PUEBLA,S.DOUBLIE,A.SHEN          
JRNL        TITL   THE CSPC PSEUDOPROTEASE REGULATES GERMINATION OF             
JRNL        TITL 2 CLOSTRIDIOIDES DIFFICILE SPORES IN RESPONSE TO MULTIPLE      
JRNL        TITL 3 ENVIRONMENTAL SIGNALS.                                       
JRNL        REF    PLOS GENET.                   V.  15 08224 2019              
JRNL        REFN                   ESSN 1553-7404                               
JRNL        PMID   31276487                                                     
JRNL        DOI    10.1371/JOURNAL.PGEN.1008224                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 176693                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.030                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 17715                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.8575 -  4.8144    1.00     5290   637  0.1722 0.1928        
REMARK   3     2  4.8144 -  3.8219    1.00     5388   518  0.1295 0.1501        
REMARK   3     3  3.8219 -  3.3390    1.00     5356   543  0.1421 0.1597        
REMARK   3     4  3.3390 -  3.0338    1.00     5341   550  0.1640 0.1920        
REMARK   3     5  3.0338 -  2.8164    1.00     5335   591  0.1686 0.1936        
REMARK   3     6  2.8164 -  2.6503    1.00     5305   572  0.1616 0.1930        
REMARK   3     7  2.6503 -  2.5176    1.00     5302   599  0.1620 0.1883        
REMARK   3     8  2.5176 -  2.4080    1.00     5235   669  0.1558 0.1864        
REMARK   3     9  2.4080 -  2.3153    1.00     5376   568  0.1516 0.1720        
REMARK   3    10  2.3153 -  2.2354    1.00     5231   601  0.1420 0.1775        
REMARK   3    11  2.2354 -  2.1655    1.00     5353   596  0.1464 0.1739        
REMARK   3    12  2.1655 -  2.1036    1.00     5263   629  0.1432 0.1650        
REMARK   3    13  2.1036 -  2.0483    1.00     5272   623  0.1491 0.1520        
REMARK   3    14  2.0483 -  1.9983    1.00     5216   681  0.1464 0.1738        
REMARK   3    15  1.9983 -  1.9529    1.00     5357   545  0.1508 0.1708        
REMARK   3    16  1.9529 -  1.9113    1.00     5311   561  0.1682 0.1799        
REMARK   3    17  1.9113 -  1.8731    1.00     5252   687  0.1701 0.1922        
REMARK   3    18  1.8731 -  1.8377    1.00     5327   564  0.1717 0.2036        
REMARK   3    19  1.8377 -  1.8049    1.00     5318   528  0.1703 0.1830        
REMARK   3    20  1.8049 -  1.7743    1.00     5294   599  0.1706 0.1820        
REMARK   3    21  1.7743 -  1.7457    1.00     5360   565  0.1809 0.2067        
REMARK   3    22  1.7457 -  1.7188    1.00     5339   565  0.1887 0.2209        
REMARK   3    23  1.7188 -  1.6935    1.00     5256   651  0.2102 0.2296        
REMARK   3    24  1.6935 -  1.6697    1.00     5342   521  0.2161 0.2320        
REMARK   3    25  1.6697 -  1.6471    1.00     5294   627  0.2248 0.2391        
REMARK   3    26  1.6471 -  1.6257    1.00     5244   672  0.2470 0.2481        
REMARK   3    27  1.6257 -  1.6054    1.00     5256   583  0.2544 0.2753        
REMARK   3    28  1.6054 -  1.5861    0.99     5296   600  0.2756 0.2906        
REMARK   3    29  1.5861 -  1.5676    0.99     5229   554  0.2972 0.3141        
REMARK   3    30  1.5676 -  1.5500    0.96     5240   516  0.3096 0.3200        
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   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.070           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.87                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 70 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  70.6836  60.6844  78.7978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2663 T22:   0.1483                                     
REMARK   3      T33:   0.2374 T12:   0.0021                                     
REMARK   3      T13:   0.0240 T23:  -0.0589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6225 L22:   1.6522                                     
REMARK   3      L33:   1.5553 L12:   0.5452                                     
REMARK   3      L13:  -0.2151 L23:   0.6222                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0873 S12:  -0.3092 S13:   0.3943                       
REMARK   3      S21:   0.1845 S22:   0.0117 S23:  -0.0272                       
REMARK   3      S31:  -0.5511 S32:   0.1023 S33:  -0.0099                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 71 THROUGH 105 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  66.3535  30.9895  58.5137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1437 T22:   0.1655                                     
REMARK   3      T33:   0.1525 T12:  -0.0007                                     
REMARK   3      T13:   0.0247 T23:  -0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7341 L22:   1.6183                                     
REMARK   3      L33:   2.5239 L12:   0.2183                                     
REMARK   3      L13:   0.4145 L23:  -0.2692                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0070 S12:   0.3090 S13:  -0.2534                       
REMARK   3      S21:  -0.1023 S22:  -0.0380 S23:  -0.0671                       
REMARK   3      S31:   0.4313 S32:   0.0117 S33:   0.0355                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 106 THROUGH 188 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  55.3568  37.9195  71.8040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0931 T22:   0.1360                                     
REMARK   3      T33:   0.1197 T12:   0.0098                                     
REMARK   3      T13:  -0.0008 T23:   0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1757 L22:   1.0790                                     
REMARK   3      L33:   1.5075 L12:   0.5546                                     
REMARK   3      L13:  -0.1174 L23:   0.1364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0006 S12:   0.0130 S13:   0.0145                       
REMARK   3      S21:   0.0808 S22:   0.0103 S23:   0.0815                       
REMARK   3      S31:   0.0247 S32:  -0.1831 S33:  -0.0015                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 189 THROUGH 268 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  68.9547  47.0080  69.9576              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0726 T22:   0.0896                                     
REMARK   3      T33:   0.0808 T12:   0.0005                                     
REMARK   3      T13:   0.0053 T23:   0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1585 L22:   1.7914                                     
REMARK   3      L33:   1.1721 L12:  -0.0556                                     
REMARK   3      L13:  -0.2901 L23:   0.1053                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0132 S12:   0.0075 S13:   0.0976                       
REMARK   3      S21:   0.0456 S22:   0.0226 S23:   0.0010                       
REMARK   3      S31:  -0.0832 S32:   0.0466 S33:  -0.0144                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 269 THROUGH 294 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  78.2980  60.2818  54.2226              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1904 T22:   0.1328                                     
REMARK   3      T33:   0.2117 T12:  -0.0161                                     
REMARK   3      T13:   0.0251 T23:   0.0483                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5360 L22:   1.2434                                     
REMARK   3      L33:   0.9192 L12:   0.1382                                     
REMARK   3      L13:  -0.0227 L23:   0.0633                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0260 S12:   0.0523 S13:   0.2373                       
REMARK   3      S21:  -0.1813 S22:   0.0048 S23:  -0.2433                       
REMARK   3      S31:  -0.2174 S32:   0.1187 S33:   0.0309                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 295 THROUGH 335 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  74.0606  74.7972  56.3487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3875 T22:   0.2597                                     
REMARK   3      T33:   0.3279 T12:   0.0169                                     
REMARK   3      T13:  -0.0001 T23:   0.0738                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2908 L22:   1.4600                                     
REMARK   3      L33:   1.8000 L12:   0.4907                                     
REMARK   3      L13:  -0.4837 L23:  -0.2496                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0437 S12:  -0.2189 S13:   0.1182                       
REMARK   3      S21:   0.2284 S22:   0.0080 S23:   0.0282                       
REMARK   3      S31:  -0.4949 S32:   0.0811 S33:  -0.0649                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 336 THROUGH 380 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  72.8737  74.8606  65.4034              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4919 T22:   0.2845                                     
REMARK   3      T33:   0.3680 T12:   0.0585                                     
REMARK   3      T13:   0.0057 T23:   0.0431                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5104 L22:   0.6125                                     
REMARK   3      L33:   1.1869 L12:   0.3944                                     
REMARK   3      L13:  -0.3038 L23:   0.1581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1213 S12:  -0.1676 S13:  -0.0099                       
REMARK   3      S21:   0.3476 S22:   0.0867 S23:   0.0275                       
REMARK   3      S31:  -0.4437 S32:   0.0871 S33:  -0.0108                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 381 THROUGH 411 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  75.3414  69.0540  54.5580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2604 T22:   0.1465                                     
REMARK   3      T33:   0.2379 T12:   0.0179                                     
REMARK   3      T13:  -0.0146 T23:   0.0622                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9191 L22:   1.4339                                     
REMARK   3      L33:   1.3242 L12:   0.4214                                     
REMARK   3      L13:  -0.7596 L23:  -0.4157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0363 S12:   0.0021 S13:   0.1881                       
REMARK   3      S21:   0.0291 S22:   0.0709 S23:  -0.0583                       
REMARK   3      S31:  -0.2506 S32:   0.1020 S33:  -0.0143                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 455 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  75.2696  51.7312  51.9670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1135 T22:   0.1312                                     
REMARK   3      T33:   0.1265 T12:  -0.0071                                     
REMARK   3      T13:   0.0137 T23:   0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1362 L22:   1.9803                                     
REMARK   3      L33:   1.3631 L12:  -0.3556                                     
REMARK   3      L13:  -0.1271 L23:  -0.2094                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0137 S12:   0.1336 S13:   0.1757                       
REMARK   3      S21:  -0.0556 S22:  -0.0024 S23:  -0.1386                       
REMARK   3      S31:  -0.1841 S32:   0.0131 S33:   0.0092                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 458 THROUGH 483 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.3764  41.2053  54.6468              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1222 T22:   0.1760                                     
REMARK   3      T33:   0.1006 T12:  -0.0090                                     
REMARK   3      T13:  -0.0028 T23:   0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4579 L22:   0.8672                                     
REMARK   3      L33:   0.7093 L12:   0.6969                                     
REMARK   3      L13:  -0.2257 L23:   0.0732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0205 S12:   0.2102 S13:   0.0909                       
REMARK   3      S21:   0.0014 S22:   0.0419 S23:   0.0561                       
REMARK   3      S31:  -0.0050 S32:  -0.0865 S33:  -0.0290                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 484 THROUGH 503 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  73.3912  33.4402  61.3621              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1084 T22:   0.1371                                     
REMARK   3      T33:   0.1278 T12:   0.0093                                     
REMARK   3      T13:  -0.0048 T23:  -0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9490 L22:   3.9524                                     
REMARK   3      L33:   1.8435 L12:  -0.4845                                     
REMARK   3      L13:  -0.0391 L23:  -0.3378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0431 S12:   0.0434 S13:  -0.1606                       
REMARK   3      S21:   0.2012 S22:  -0.0035 S23:  -0.2919                       
REMARK   3      S31:   0.1257 S32:   0.1962 S33:   0.0334                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 504 THROUGH 514 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  83.7043  29.2303  71.1501              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4503 T22:   0.2551                                     
REMARK   3      T33:   0.4877 T12:   0.0226                                     
REMARK   3      T13:   0.0377 T23:   0.1452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6823 L22:   2.0116                                     
REMARK   3      L33:   0.9576 L12:   0.9061                                     
REMARK   3      L13:  -0.6526 L23:  -1.3853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0349 S12:  -0.3543 S13:  -1.3372                       
REMARK   3      S21:   0.2616 S22:  -0.2113 S23:  -0.3465                       
REMARK   3      S31:   1.0674 S32:   0.2982 S33:   0.0425                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 515 THROUGH 540 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  83.7298  39.2246  51.2245              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1397 T22:   0.2037                                     
REMARK   3      T33:   0.1721 T12:   0.0113                                     
REMARK   3      T13:   0.0030 T23:  -0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7780 L22:   0.7211                                     
REMARK   3      L33:   1.7938 L12:   0.4105                                     
REMARK   3      L13:  -0.3130 L23:   0.1270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0224 S12:   0.1370 S13:  -0.0513                       
REMARK   3      S21:  -0.0815 S22:   0.0366 S23:  -0.0419                       
REMARK   3      S31:   0.0610 S32:   0.1881 S33:  -0.0477                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 541 THROUGH 555 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  81.6197  29.5108  53.6983              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2642 T22:   0.1871                                     
REMARK   3      T33:   0.2598 T12:   0.0405                                     
REMARK   3      T13:  -0.0072 T23:  -0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1446 L22:   4.1897                                     
REMARK   3      L33:   2.7410 L12:   0.2339                                     
REMARK   3      L13:   0.2835 L23:  -0.9800                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:   0.1445 S13:  -0.5796                       
REMARK   3      S21:   0.2412 S22:  -0.0502 S23:  -0.2952                       
REMARK   3      S31:   0.5532 S32:   0.4088 S33:   0.0529                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 560 THROUGH 565 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  93.8614  37.4593  56.8195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5569 T22:   0.5360                                     
REMARK   3      T33:   0.8916 T12:  -0.0182                                     
REMARK   3      T13:  -0.1849 T23:   0.0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5202 L22:   2.2248                                     
REMARK   3      L33:   1.1411 L12:   0.1955                                     
REMARK   3      L13:   0.7693 L23:   0.2193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1878 S12:   0.0380 S13:   0.1580                       
REMARK   3      S21:  -0.0310 S22:  -0.1971 S23:  -0.2398                       
REMARK   3      S31:  -0.1502 S32:   0.1777 S33:   0.3335                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6MW4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237652.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 177295                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: 4I0W                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MES PH 6.5 WITH 2.5 M AMMONIUM      
REMARK 280  CHLORIDE AND 0.5 M GUANIDINIUM HYDROCHLORIDE MIXED EQUAL VOLUME     
REMARK 280  WITH 22 MG/ML PROTEIN AND EQUILIBRATED OVER 2M SODIUM CHLORIDE,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.83750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.83750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       44.32550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       77.58800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.32550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       77.58800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.83750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.32550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       77.58800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       45.83750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.32550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       77.58800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 818  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 907  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASN A    89                                                      
REMARK 465     PRO A    90                                                      
REMARK 465     TYR A    91                                                      
REMARK 465     ASN A    92                                                      
REMARK 465     ARG A   456                                                      
REMARK 465     GLY A   457                                                      
REMARK 465     ASP A   506                                                      
REMARK 465     ASN A   507                                                      
REMARK 465     VAL A   508                                                      
REMARK 465     THR A   556                                                      
REMARK 465     LEU A   557                                                      
REMARK 465     LEU A   558                                                      
REMARK 465     GLU A   559                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   3    NZ                                                  
REMARK 470     GLN A  10    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  19    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  24    NE   CZ   NH1  NH2                                  
REMARK 470     VAL A  39    CG1  CG2                                            
REMARK 470     ASP A  40    CG   OD1  OD2                                       
REMARK 470     ILE A  45    CD1                                                 
REMARK 470     GLU A  59    CD   OE1  OE2                                       
REMARK 470     GLU A  66    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  72    CG   OD1  ND2                                       
REMARK 470     ASP A  84    CG   OD1  OD2                                       
REMARK 470     TYR A  85    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A  88    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  93    CG   OD1  OD2                                       
REMARK 470     GLN A 187    OE1  NE2                                            
REMARK 470     ASP A 259    CG   OD1  OD2                                       
REMARK 470     ARG A 288    CZ   NH1  NH2                                       
REMARK 470     ASP A 304    CG   OD1  OD2                                       
REMARK 470     TYR A 306    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 315    CG   OD1  ND2                                       
REMARK 470     GLU A 330    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 337    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 347    NZ                                                  
REMARK 470     GLU A 372    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 376    NE   CZ   NH1  NH2                                  
REMARK 470     ASP A 429    CG   OD1  OD2                                       
REMARK 470     ARG A 454    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 503    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 504    CE   NZ                                             
REMARK 470     GLN A 505    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 510    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 547    CE   NZ                                             
REMARK 470     HIS A 560    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A 561    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   924     O    HOH A   994              2.07            
REMARK 500   OD1  ASP A   109     O    HOH A   701              2.11            
REMARK 500   O    HOH A   746     O    HOH A   897              2.17            
REMARK 500   O    HOH A   782     O    HOH A   895              2.17            
REMARK 500   OG   SER A   328     OE2  GLU A   351              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 105     -140.14   -169.28                                   
REMARK 500    ALA A 179        7.12   -152.58                                   
REMARK 500    ILE A 393      -71.89   -115.65                                   
REMARK 500    ILE A 531      -15.62     78.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1075        DISTANCE =  6.27 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605                 
DBREF  6MW4 A    1   557  UNP    C9YNI7   C9YNI7_PEPDR     1    557             
SEQADV 6MW4 LEU A  558  UNP  C9YNI7              EXPRESSION TAG                 
SEQADV 6MW4 GLU A  559  UNP  C9YNI7              EXPRESSION TAG                 
SEQADV 6MW4 HIS A  560  UNP  C9YNI7              EXPRESSION TAG                 
SEQADV 6MW4 HIS A  561  UNP  C9YNI7              EXPRESSION TAG                 
SEQADV 6MW4 HIS A  562  UNP  C9YNI7              EXPRESSION TAG                 
SEQADV 6MW4 HIS A  563  UNP  C9YNI7              EXPRESSION TAG                 
SEQADV 6MW4 HIS A  564  UNP  C9YNI7              EXPRESSION TAG                 
SEQADV 6MW4 HIS A  565  UNP  C9YNI7              EXPRESSION TAG                 
SEQRES   1 A  565  MET GLU LYS SER TYR CYS ILE ILE TYR GLN GLY ASP ILE          
SEQRES   2 A  565  GLU SER ALA LEU GLN GLU ASN GLY ILE ASN ARG TYR MET          
SEQRES   3 A  565  VAL LEU ASN SER GLN LEU ALA VAL ILE TYR VAL PRO VAL          
SEQRES   4 A  565  ASP PHE ASP GLU THR ILE LEU ASN ASN ILE ILE GLN VAL          
SEQRES   5 A  565  ALA TRP TRP GLU GLU SER GLU PRO MET SER SER LEU ILE          
SEQRES   6 A  565  GLU ILE THR ASN ASN VAL ASN ASN GLY GLU THR ILE THR          
SEQRES   7 A  565  THR ALA ALA GLU THR ASP TYR ILE TYR GLU ASN PRO TYR          
SEQRES   8 A  565  ASN ASP ILE THR GLY ARG GLY ILE LEU LEU ALA VAL ILE          
SEQRES   9 A  565  ASP SER GLY ILE ASP TYR LEU HIS PRO ASP PHE ILE ASN          
SEQRES  10 A  565  ASP ASP GLY THR SER LYS VAL LEU TYR LEU TRP ASP GLN          
SEQRES  11 A  565  GLU ALA ASN THR ASN PRO PRO PRO GLU GLY PHE ILE PHE          
SEQRES  12 A  565  GLY SER GLU PHE THR ARG SER GLN LEU ASN ILE ALA ILE          
SEQRES  13 A  565  ASN ARG ASN ASP GLY SER LEU SER GLN ASP ASN ILE GLY          
SEQRES  14 A  565  THR GLY THR LEU VAL SER GLY ILE LEU ALA GLY ASN GLY          
SEQRES  15 A  565  ARG ILE ASN SER GLN TYR ARG GLY ILE THR THR GLU SER          
SEQRES  16 A  565  ASP LEU ILE VAL VAL LYS LEU LYS SER TYR THR ASP THR          
SEQRES  17 A  565  TYR TYR ALA GLY ARG ILE ASN TYR SER VAL SER ASP PHE          
SEQRES  18 A  565  LEU ALA ALA ILE THR TYR VAL THR ASN ILE ALA ARG THR          
SEQRES  19 A  565  GLU ASN LYS PRO LEU ILE ILE ASN LEU THR ILE GLY VAL          
SEQRES  20 A  565  LYS SER SER ALA VAL ALA THR THR SER ILE LEU ASP THR          
SEQRES  21 A  565  PHE ASN ILE LEU SER SER ALA GLY VAL VAL VAL VAL SER          
SEQRES  22 A  565  GLY ALA GLY ASN GLN GLY ASN THR ASP ILE HIS TYR SER          
SEQRES  23 A  565  GLY ARG PHE SER SER VAL GLY GLU VAL GLN ASP VAL ILE          
SEQRES  24 A  565  ILE GLN ASP GLY ASP ASP TYR ALA LEU ASP ILE THR LEU          
SEQRES  25 A  565  ASN THR ASN GLY PRO ASP LYS VAL GLY ALA GLN ILE ILE          
SEQRES  26 A  565  SER PRO SER GLY GLU VAL SER HIS ASP ILE ARG TYR SER          
SEQRES  27 A  565  PRO ASP PHE TYR ILE TYR ARG GLY LYS PHE ASN LEU GLU          
SEQRES  28 A  565  ASN THR THR TYR ALA MET ARG PHE ILE TYR PRO TYR ILE          
SEQRES  29 A  565  THR SER GLY LYS GLU ASN LEU GLU ILE ARG LEU ARG ASP          
SEQRES  30 A  565  ILE LYS PRO GLY VAL TRP ILE LEU ARG LEU THR SER GLU          
SEQRES  31 A  565  LEU ILE ILE SER GLY GLU TYR ASP ILE TYR LEU PRO ASN          
SEQRES  32 A  565  LYS ASN LEU ILE ALA PRO ASP THR ARG PHE LEU ASP PRO          
SEQRES  33 A  565  ASP SER VAL ALA THR ILE THR MET TYR ALA ALA SER ASP          
SEQRES  34 A  565  ASP VAL ILE THR VAL GLY THR PHE ASN ASN LYS THR ASP          
SEQRES  35 A  565  SER MET TRP ILE GLY SER SER LYS GLY PRO ILE ARG GLY          
SEQRES  36 A  565  ARG GLY ILE LYS PRO ASP ILE VAL ALA SER GLY VAL ASP          
SEQRES  37 A  565  ILE ILE SER THR TYR LYS ASN GLY THR TYR ASN THR GLY          
SEQRES  38 A  565  THR GLY THR GLY VAL SER SER SER ILE VAL THR GLY VAL          
SEQRES  39 A  565  LEU ALA LEU LEU MET GLU TYR LEU GLU LYS GLN ASP ASN          
SEQRES  40 A  565  VAL PRO ARG LEU SER LEU PHE THR GLN VAL LEU LYS THR          
SEQRES  41 A  565  TYR LEU ILE LEU GLY ALA THR LYS LEU GLU ILE TYR THR          
SEQRES  42 A  565  TYR PRO ASN VAL SER GLN GLY TYR GLY ILE LEU ASN LEU          
SEQRES  43 A  565  LYS ASN THR ILE GLN GLN ILE ALA ASN THR LEU LEU GLU          
SEQRES  44 A  565  HIS HIS HIS HIS HIS HIS                                      
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    SO4  A 605       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  SO4    5(O4 S 2-)                                                   
FORMUL   7  HOH   *375(H2 O)                                                    
HELIX    1 AA1 ASP A   12  ASN A   20  1                                   9    
HELIX    2 AA2 ASP A   42  ILE A   49  5                                   8    
HELIX    3 AA3 ASN A   70  GLY A   74  5                                   5    
HELIX    4 AA4 THR A   76  GLU A   82  1                                   7    
HELIX    5 AA5 THR A   83  GLU A   88  1                                   6    
HELIX    6 AA6 HIS A  112  ILE A  116  5                                   5    
HELIX    7 AA7 ARG A  149  ASN A  159  1                                  11    
HELIX    8 AA8 GLY A  169  GLY A  180  1                                  12    
HELIX    9 AA9 ASN A  185  ARG A  189  5                                   5    
HELIX   10 AB1 VAL A  218  ASN A  236  1                                  19    
HELIX   11 AB2 SER A  256  SER A  266  5                                  11    
HELIX   12 AB3 PRO A  362  SER A  366  5                                   5    
HELIX   13 AB4 ASN A  403  ILE A  407  5                                   5    
HELIX   14 AB5 THR A  423  ALA A  427  5                                   5    
HELIX   15 AB6 LYS A  474  GLY A  476  5                                   3    
HELIX   16 AB7 GLY A  483  GLN A  505  1                                  23    
HELIX   17 AB8 PRO A  509  LEU A  513  5                                   5    
HELIX   18 AB9 PHE A  514  ALA A  526  1                                  13    
HELIX   19 AC1 ASN A  545  ASN A  555  1                                  11    
SHEET    1 AA1 4 TYR A  25  VAL A  27  0                                        
SHEET    2 AA1 4 LEU A  32  VAL A  37 -1  O  VAL A  34   N  MET A  26           
SHEET    3 AA1 4 LYS A   3  TYR A   9 -1  N  ILE A   7   O  ALA A  33           
SHEET    4 AA1 4 VAL A  52  GLU A  57 -1  O  GLU A  56   N  CYS A   6           
SHEET    1 AA2 4 TYR A 205  THR A 206  0                                        
SHEET    2 AA2 4 ILE A 214  SER A 217 -1  O  ASN A 215   N  TYR A 205           
SHEET    3 AA2 4 PRO A  60  SER A  63 -1  N  MET A  61   O  TYR A 216           
SHEET    4 AA2 4 ILE A 245  GLY A 246 -1  O  GLY A 246   N  SER A  62           
SHEET    1 AA3 3 GLU A  66  ILE A  67  0                                        
SHEET    2 AA3 3 THR A 477  THR A 482 -1  O  THR A 482   N  GLU A  66           
SHEET    3 AA3 3 ILE A 469  TYR A 473 -1  N  SER A 471   O  ASN A 479           
SHEET    1 AA4 8 SER A 145  THR A 148  0                                        
SHEET    2 AA4 8 VAL A 124  ASP A 129 -1  N  LEU A 127   O  PHE A 147           
SHEET    3 AA4 8 ASP A 196  LYS A 201  1  O  LEU A 197   N  LEU A 125           
SHEET    4 AA4 8 LEU A 100  ASP A 105  1  N  VAL A 103   O  ILE A 198           
SHEET    5 AA4 8 LEU A 239  LEU A 243  1  O  ILE A 240   N  ALA A 102           
SHEET    6 AA4 8 VAL A 269  GLY A 274  1  O  VAL A 272   N  LEU A 243           
SHEET    7 AA4 8 ILE A 432  ASN A 438  1  O  ILE A 432   N  SER A 273           
SHEET    8 AA4 8 SER A 443  MET A 444 -1  O  SER A 443   N  ASN A 438           
SHEET    1 AA5 8 SER A 145  THR A 148  0                                        
SHEET    2 AA5 8 VAL A 124  ASP A 129 -1  N  LEU A 127   O  PHE A 147           
SHEET    3 AA5 8 ASP A 196  LYS A 201  1  O  LEU A 197   N  LEU A 125           
SHEET    4 AA5 8 LEU A 100  ASP A 105  1  N  VAL A 103   O  ILE A 198           
SHEET    5 AA5 8 LEU A 239  LEU A 243  1  O  ILE A 240   N  ALA A 102           
SHEET    6 AA5 8 VAL A 269  GLY A 274  1  O  VAL A 272   N  LEU A 243           
SHEET    7 AA5 8 ILE A 432  ASN A 438  1  O  ILE A 432   N  SER A 273           
SHEET    8 AA5 8 ILE A 462  SER A 465  1  O  ILE A 462   N  GLY A 435           
SHEET    1 AA6 6 HIS A 284  ARG A 288  0                                        
SHEET    2 AA6 6 GLU A 396  TYR A 400 -1  O  ILE A 399   N  TYR A 285           
SHEET    3 AA6 6 ALA A 307  ASN A 313 -1  N  ASN A 313   O  ASP A 398           
SHEET    4 AA6 6 ASN A 370  ARG A 376 -1  O  LEU A 375   N  LEU A 308           
SHEET    5 AA6 6 THR A 353  ILE A 360 -1  N  ILE A 360   O  ASN A 370           
SHEET    6 AA6 6 TYR A 344  PHE A 348 -1  N  PHE A 348   O  THR A 353           
SHEET    1 AA7 4 LYS A 319  ILE A 325  0                                        
SHEET    2 AA7 4 GLY A 381  LEU A 391 -1  O  THR A 388   N  GLY A 321           
SHEET    3 AA7 4 VAL A 295  ASP A 302 -1  N  ILE A 300   O  TRP A 383           
SHEET    4 AA7 4 ARG A 412  PHE A 413 -1  O  ARG A 412   N  GLN A 301           
CISPEP   1 LYS A  459    PRO A  460          0        -4.69                     
CISPEP   2 TYR A  534    PRO A  535          0        -7.30                     
SITE     1 AC1  2 TYR A 473  LYS A 474                                          
SITE     1 AC2  4 ASN A 167  LYS A 474  ASN A 475  HOH A 741                    
SITE     1 AC3  8 ARG A 158  ILE A 184  ASN A 185  TYR A 188                    
SITE     2 AC3  8 TYR A 478  HOH A 788  HOH A 914  HOH A 957                    
SITE     1 AC4  3 TYR A 210  ARG A 213  HOH A 777                               
SITE     1 AC5  3 ARG A 345  ARG A 358  ARG A 374                               
CRYST1   88.651  155.176   91.675  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011280  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006444  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010908        0.00000                         
ATOM      1  N   GLU A   2      58.943  64.754  76.181  1.00 58.84           N  
ANISOU    1  N   GLU A   2     7821   6290   8245   1155    333   -515       N  
ATOM      2  CA  GLU A   2      60.142  64.222  76.821  1.00 56.42           C  
ANISOU    2  CA  GLU A   2     7575   6026   7835   1049    384   -536       C  
ATOM      3  C   GLU A   2      61.314  64.112  75.853  1.00 52.10           C  
ANISOU    3  C   GLU A   2     7103   5426   7267    968    350   -426       C  
ATOM      4  O   GLU A   2      61.246  63.388  74.858  1.00 54.72           O  
ANISOU    4  O   GLU A   2     7380   5820   7590    967    302   -316       O  
ATOM      5  CB  GLU A   2      59.859  62.844  77.435  1.00 57.05           C  
ANISOU    5  CB  GLU A   2     7550   6290   7835   1032    419   -550       C  
ATOM      6  CG  GLU A   2      59.970  62.792  78.949  1.00 61.20           C  
ANISOU    6  CG  GLU A   2     8100   6866   8286   1003    501   -682       C  
ATOM      7  CD  GLU A   2      59.906  61.372  79.496  1.00 63.07           C  
ANISOU    7  CD  GLU A   2     8257   7276   8431    965    536   -671       C  
ATOM      8  OE1 GLU A   2      59.549  61.203  80.683  1.00 64.06           O  
ANISOU    8  OE1 GLU A   2     8372   7476   8491    958    602   -771       O  
ATOM      9  OE2 GLU A   2      60.216  60.425  78.742  1.00 58.25           O1-
ANISOU    9  OE2 GLU A   2     7599   6726   7806    939    498   -562       O1-
ATOM     10  N   LYS A   3      62.384  64.841  76.142  1.00 43.38           N  
ANISOU   10  N   LYS A   3     6122   4209   6152    886    376   -468       N  
ATOM     11  CA  LYS A   3      63.672  64.584  75.520  1.00 37.82           C  
ANISOU   11  CA  LYS A   3     5482   3476   5412    775    367   -399       C  
ATOM     12  C   LYS A   3      64.510  63.736  76.468  1.00 26.94           C  
ANISOU   12  C   LYS A   3     4098   2189   3950    688    416   -469       C  
ATOM     13  O   LYS A   3      64.168  63.543  77.637  1.00 27.71           O  
ANISOU   13  O   LYS A   3     4169   2353   4005    704    459   -571       O  
ATOM     14  CB  LYS A   3      64.393  65.890  75.173  1.00 42.21           C  
ANISOU   14  CB  LYS A   3     6170   3855   6012    709    364   -404       C  
ATOM     15  CG  LYS A   3      64.769  66.744  76.365  1.00 46.70           C  
ANISOU   15  CG  LYS A   3     6813   4351   6580    659    415   -551       C  
ATOM     16  CD  LYS A   3      65.510  67.994  75.916  1.00 50.34           C  
ANISOU   16  CD  LYS A   3     7397   4641   7090    580    410   -545       C  
ATOM     17  CE  LYS A   3      65.027  69.218  76.672  1.00 51.58           C  
ANISOU   17  CE  LYS A   3     7607   4686   7304    626    433   -656       C  
ATOM     18  N   SER A   4      65.611  63.207  75.950  1.00 25.49           N  
ANISOU   18  N   SER A   4     3919   2032   3733    581    394   -412       N  
ATOM     19  CA  SER A   4      66.470  62.366  76.766  1.00 21.51           C  
ANISOU   19  CA  SER A   4     3353   1679   3143    469    380   -456       C  
ATOM     20  C   SER A   4      67.918  62.604  76.376  1.00 23.01           C  
ANISOU   20  C   SER A   4     3581   1837   3326    316    354   -449       C  
ATOM     21  O   SER A   4      68.214  63.128  75.299  1.00 24.08           O  
ANISOU   21  O   SER A   4     3775   1863   3512    292    350   -383       O  
ATOM     22  CB  SER A   4      66.108  60.879  76.634  1.00 21.14           C  
ANISOU   22  CB  SER A   4     3173   1808   3052    502    352   -382       C  
ATOM     23  OG  SER A   4      66.158  60.459  75.279  1.00 25.69           O  
ANISOU   23  OG  SER A   4     3715   2383   3663    511    318   -264       O  
ATOM     24  N   TYR A   5      68.819  62.222  77.279  1.00 20.83           N  
ANISOU   24  N   TYR A   5     3270   1661   2984    210    335   -519       N  
ATOM     25  CA  TYR A   5      70.248  62.433  77.103  1.00 19.77           C  
ANISOU   25  CA  TYR A   5     3147   1518   2847     57    311   -542       C  
ATOM     26  C   TYR A   5      70.999  61.170  77.486  1.00 19.75           C  
ANISOU   26  C   TYR A   5     3022   1698   2783     -4    253   -528       C  
ATOM     27  O   TYR A   5      70.612  60.471  78.425  1.00 21.92           O  
ANISOU   27  O   TYR A   5     3247   2089   2993     37    237   -550       O  
ATOM     28  CB  TYR A   5      70.769  63.588  77.966  1.00 23.22           C  
ANISOU   28  CB  TYR A   5     3683   1862   3278    -29    338   -678       C  
ATOM     29  CG  TYR A   5      70.264  64.946  77.562  1.00 23.70           C  
ANISOU   29  CG  TYR A   5     3881   1708   3417     12    395   -698       C  
ATOM     30  CD1 TYR A   5      71.042  65.789  76.782  1.00 25.34           C  
ANISOU   30  CD1 TYR A   5     4174   1774   3680    -88    411   -684       C  
ATOM     31  CD2 TYR A   5      69.010  65.390  77.964  1.00 27.60           C  
ANISOU   31  CD2 TYR A   5     4418   2132   3936    151    437   -731       C  
ATOM     32  CE1 TYR A   5      70.584  67.039  76.410  1.00 29.67           C  
ANISOU   32  CE1 TYR A   5     4847   2127   4299    -45    449   -681       C  
ATOM     33  CE2 TYR A   5      68.543  66.633  77.596  1.00 32.00           C  
ANISOU   33  CE2 TYR A   5     5085   2498   4577    203    471   -738       C  
ATOM     34  CZ  TYR A   5      69.334  67.452  76.820  1.00 32.02           C  
ANISOU   34  CZ  TYR A   5     5158   2387   4622    107    459   -698       C  
ATOM     35  OH  TYR A   5      68.872  68.691  76.454  1.00 36.46           O  
ANISOU   35  OH  TYR A   5     5796   2802   5256    160    460   -677       O  
ATOM     36  N   CYS A   6      72.072  60.887  76.760  1.00 19.89           N  
ANISOU   36  N   CYS A   6     2994   1739   2825   -102    226   -492       N  
ATOM     37  CA  CYS A   6      73.021  59.858  77.155  1.00 21.38           C  
ANISOU   37  CA  CYS A   6     3066   2080   2976   -170    164   -498       C  
ATOM     38  C   CYS A   6      74.143  60.517  77.940  1.00 21.97           C  
ANISOU   38  C   CYS A   6     3163   2155   3031   -301    141   -615       C  
ATOM     39  O   CYS A   6      74.629  61.583  77.558  1.00 23.67           O  
ANISOU   39  O   CYS A   6     3456   2249   3290   -386    178   -662       O  
ATOM     40  CB  CYS A   6      73.590  59.132  75.934  1.00 24.61           C  
ANISOU   40  CB  CYS A   6     3393   2524   3435   -203    152   -413       C  
ATOM     41  SG  CYS A   6      72.302  58.435  74.882  1.00 29.94           S  
ANISOU   41  SG  CYS A   6     4046   3198   4130    -68    176   -286       S  
ATOM     42  N   ILE A   7      74.534  59.893  79.053  1.00 18.32           N  
ANISOU   42  N   ILE A   7     2638   1826   2496   -322     78   -661       N  
ATOM     43  CA  ILE A   7      75.536  60.450  79.956  1.00 22.61           C  
ANISOU   43  CA  ILE A   7     3191   2398   3002   -442     40   -783       C  
ATOM     44  C   ILE A   7      76.649  59.429  80.155  1.00 21.29           C  
ANISOU   44  C   ILE A   7     2885   2383   2822   -499    -56   -770       C  
ATOM     45  O   ILE A   7      76.375  58.255  80.418  1.00 21.36           O  
ANISOU   45  O   ILE A   7     2819   2502   2795   -423   -105   -696       O  
ATOM     46  CB  ILE A   7      74.902  60.830  81.310  1.00 24.10           C  
ANISOU   46  CB  ILE A   7     3456   2607   3095   -414     45   -869       C  
ATOM     47  CG1 ILE A   7      73.981  62.040  81.127  1.00 29.53           C  
ANISOU   47  CG1 ILE A   7     4278   3121   3821   -368    143   -912       C  
ATOM     48  CG2 ILE A   7      75.976  61.087  82.376  1.00 28.63           C  
ANISOU   48  CG2 ILE A   7     4016   3264   3600   -538    -23   -989       C  
ATOM     49  CD1 ILE A   7      73.314  62.483  82.405  1.00 39.79           C  
ANISOU   49  CD1 ILE A   7     5652   4430   5036   -342    171  -1017       C  
ATOM     50  N   ILE A   8      77.898  59.874  80.041  1.00 21.38           N  
ANISOU   50  N   ILE A   8     2857   2396   2871   -632    -82   -845       N  
ATOM     51  CA  ILE A   8      79.048  59.112  80.514  1.00 25.64           C  
ANISOU   51  CA  ILE A   8     3260   3084   3398   -691   -189   -870       C  
ATOM     52  C   ILE A   8      79.405  59.657  81.888  1.00 24.41           C  
ANISOU   52  C   ILE A   8     3143   2984   3147   -760   -246   -992       C  
ATOM     53  O   ILE A   8      79.627  60.863  82.041  1.00 25.68           O  
ANISOU   53  O   ILE A   8     3390   3054   3314   -855   -200  -1101       O  
ATOM     54  CB  ILE A   8      80.242  59.214  79.550  1.00 25.98           C  
ANISOU   54  CB  ILE A   8     3211   3115   3545   -802   -183   -892       C  
ATOM     55  CG1 ILE A   8      79.873  58.651  78.180  1.00 27.49           C  
ANISOU   55  CG1 ILE A   8     3372   3262   3812   -742   -121   -777       C  
ATOM     56  CG2 ILE A   8      81.471  58.498  80.139  1.00 27.14           C  
ANISOU   56  CG2 ILE A   8     3200   3420   3692   -857   -304   -938       C  
ATOM     57  CD1 ILE A   8      79.796  57.139  78.139  1.00 31.36           C  
ANISOU   57  CD1 ILE A   8     3738   3871   4306   -644   -185   -686       C  
ATOM     58  N   TYR A   9      79.448  58.786  82.891  1.00 23.94           N  
ANISOU   58  N   TYR A   9     3031   3070   2995   -718   -346   -974       N  
ATOM     59  CA  TYR A   9      79.602  59.240  84.264  1.00 25.88           C  
ANISOU   59  CA  TYR A   9     3332   3384   3118   -774   -402  -1081       C  
ATOM     60  C   TYR A   9      80.804  58.600  84.945  1.00 30.97           C  
ANISOU   60  C   TYR A   9     3851   4194   3724   -832   -555  -1108       C  
ATOM     61  O   TYR A   9      81.336  57.574  84.508  1.00 29.87           O  
ANISOU   61  O   TYR A   9     3579   4127   3645   -793   -624  -1024       O  
ATOM     62  CB  TYR A   9      78.353  58.946  85.098  1.00 23.17           C  
ANISOU   62  CB  TYR A   9     3082   3067   2656   -672   -378  -1045       C  
ATOM     63  CG  TYR A   9      78.127  57.470  85.360  1.00 24.38           C  
ANISOU   63  CG  TYR A   9     3161   3344   2760   -575   -455   -914       C  
ATOM     64  CD1 TYR A   9      77.355  56.695  84.494  1.00 22.59           C  
ANISOU   64  CD1 TYR A   9     2907   3077   2600   -465   -401   -786       C  
ATOM     65  CD2 TYR A   9      78.684  56.849  86.476  1.00 26.58           C  
ANISOU   65  CD2 TYR A   9     3402   3776   2923   -598   -585   -918       C  
ATOM     66  CE1 TYR A   9      77.141  55.340  84.738  1.00 22.40           C  
ANISOU   66  CE1 TYR A   9     2823   3149   2538   -384   -463   -669       C  
ATOM     67  CE2 TYR A   9      78.485  55.510  86.721  1.00 25.27           C  
ANISOU   67  CE2 TYR A   9     3183   3703   2716   -510   -655   -789       C  
ATOM     68  CZ  TYR A   9      77.723  54.757  85.860  1.00 24.86           C  
ANISOU   68  CZ  TYR A   9     3108   3597   2741   -407   -589   -668       C  
ATOM     69  OH  TYR A   9      77.538  53.418  86.134  1.00 25.90           O  
ANISOU   69  OH  TYR A   9     3195   3808   2837   -328   -653   -543       O  
ATOM     70  N   GLN A  10      81.197  59.229  86.048  1.00 33.87           N  
ANISOU   70  N   GLN A  10     4261   4620   3988   -923   -609  -1233       N  
ATOM     71  CA  GLN A  10      82.163  58.688  86.993  1.00 38.16           C  
ANISOU   71  CA  GLN A  10     4709   5339   4450   -969   -775  -1264       C  
ATOM     72  C   GLN A  10      81.645  58.993  88.389  1.00 42.32           C  
ANISOU   72  C   GLN A  10     5357   5934   4789   -984   -803  -1330       C  
ATOM     73  O   GLN A  10      81.195  60.113  88.651  1.00 43.43           O  
ANISOU   73  O   GLN A  10     5622   5983   4896  -1042   -706  -1444       O  
ATOM     74  CB  GLN A  10      83.557  59.298  86.789  1.00 39.71           C  
ANISOU   74  CB  GLN A  10     4806   5551   4730  -1106   -822  -1375       C  
ATOM     75  N   GLY A  11      81.690  58.003  89.270  1.00 43.67           N  
ANISOU   75  N   GLY A  11     5499   6257   4838   -933   -929  -1257       N  
ATOM     76  CA  GLY A  11      81.274  58.206  90.645  1.00 43.98           C  
ANISOU   76  CA  GLY A  11     5652   6385   4672   -961   -964  -1316       C  
ATOM     77  C   GLY A  11      79.805  57.898  90.860  1.00 43.06           C  
ANISOU   77  C   GLY A  11     5658   6225   4477   -856   -854  -1237       C  
ATOM     78  O   GLY A  11      79.169  57.163  90.100  1.00 38.05           O  
ANISOU   78  O   GLY A  11     4998   5535   3925   -744   -799  -1101       O  
ATOM     79  N   ASP A  12      79.259  58.487  91.927  1.00 44.48           N  
ANISOU   79  N   ASP A  12     5970   6438   4494   -902   -817  -1337       N  
ATOM     80  CA  ASP A  12      77.875  58.247  92.341  1.00 41.88           C  
ANISOU   80  CA  ASP A  12     5754   6092   4066   -821   -710  -1289       C  
ATOM     81  C   ASP A  12      76.956  59.152  91.525  1.00 37.34           C  
ANISOU   81  C   ASP A  12     5242   5326   3619   -782   -523  -1342       C  
ATOM     82  O   ASP A  12      76.523  60.223  91.958  1.00 39.85           O  
ANISOU   82  O   ASP A  12     5666   5578   3896   -831   -427  -1487       O  
ATOM     83  CB  ASP A  12      77.725  58.476  93.842  1.00 48.08           C  
ANISOU   83  CB  ASP A  12     6648   7003   4616   -895   -745  -1384       C  
ATOM     84  CG  ASP A  12      76.298  58.276  94.336  1.00 54.22           C  
ANISOU   84  CG  ASP A  12     7542   7774   5285   -828   -616  -1357       C  
ATOM     85  OD1 ASP A  12      75.439  57.782  93.572  1.00 53.14           O  
ANISOU   85  OD1 ASP A  12     7386   7554   5250   -715   -523  -1246       O  
ATOM     86  OD2 ASP A  12      76.036  58.617  95.510  1.00 58.08           O1-
ANISOU   86  OD2 ASP A  12     8130   8328   5610   -875   -601  -1435       O1-
ATOM     87  N   ILE A  13      76.653  58.692  90.308  1.00 32.02           N  
ANISOU   87  N   ILE A  13     4502   4560   3104   -688   -476  -1221       N  
ATOM     88  CA  ILE A  13      75.832  59.477  89.393  1.00 30.42           C  
ANISOU   88  CA  ILE A  13     4349   4177   3034   -637   -322  -1244       C  
ATOM     89  C   ILE A  13      74.390  59.552  89.876  1.00 32.21           C  
ANISOU   89  C   ILE A  13     4673   4379   3186   -559   -204  -1255       C  
ATOM     90  O   ILE A  13      73.726  60.580  89.704  1.00 33.67           O  
ANISOU   90  O   ILE A  13     4937   4432   3425   -546    -83  -1349       O  
ATOM     91  CB  ILE A  13      75.931  58.885  87.973  1.00 30.29           C  
ANISOU   91  CB  ILE A  13     4232   4092   3185   -565   -317  -1109       C  
ATOM     92  CG1 ILE A  13      75.164  59.742  86.960  1.00 30.65           C  
ANISOU   92  CG1 ILE A  13     4332   3952   3363   -517   -178  -1122       C  
ATOM     93  CG2 ILE A  13      75.431  57.448  87.954  1.00 28.00           C  
ANISOU   93  CG2 ILE A  13     3886   3890   2862   -463   -352   -950       C  
ATOM     94  CD1 ILE A  13      75.688  61.163  86.830  1.00 31.36           C  
ANISOU   94  CD1 ILE A  13     4486   3921   3510   -619   -135  -1265       C  
ATOM     95  N   GLU A  14      73.887  58.482  90.497  1.00 34.74           N  
ANISOU   95  N   GLU A  14     4989   4821   3388   -508   -232  -1162       N  
ATOM     96  CA  GLU A  14      72.500  58.466  90.952  1.00 38.09           C  
ANISOU   96  CA  GLU A  14     5491   5237   3744   -441   -109  -1174       C  
ATOM     97  C   GLU A  14      72.238  59.564  91.975  1.00 39.14           C  
ANISOU   97  C   GLU A  14     5740   5365   3767   -514    -39  -1361       C  
ATOM     98  O   GLU A  14      71.261  60.313  91.859  1.00 39.28           O  
ANISOU   98  O   GLU A  14     5815   5273   3837   -465    101  -1443       O  
ATOM     99  CB  GLU A  14      72.157  57.091  91.525  1.00 44.86           C  
ANISOU   99  CB  GLU A  14     6332   6235   4477   -403   -157  -1042       C  
ATOM    100  CG  GLU A  14      71.912  56.046  90.451  1.00 51.66           C  
ANISOU  100  CG  GLU A  14     7096   7066   5465   -304   -164   -872       C  
ATOM    101  CD  GLU A  14      72.090  54.626  90.946  1.00 65.02           C  
ANISOU  101  CD  GLU A  14     8760   8889   7057   -290   -260   -731       C  
ATOM    102  OE1 GLU A  14      73.123  54.343  91.587  1.00 70.86           O  
ANISOU  102  OE1 GLU A  14     9489   9728   7706   -355   -400   -722       O  
ATOM    103  OE2 GLU A  14      71.200  53.790  90.678  1.00 70.37           O  
ANISOU  103  OE2 GLU A  14     9422   9564   7752   -214   -200   -627       O  
ATOM    104  N   SER A  15      73.104  59.683  92.984  1.00 39.83           N  
ANISOU  104  N   SER A  15     5859   5571   3705   -629   -138  -1440       N  
ATOM    105  CA  SER A  15      72.928  60.751  93.961  1.00 42.25           C  
ANISOU  105  CA  SER A  15     6277   5875   3901   -714    -72  -1637       C  
ATOM    106  C   SER A  15      73.050  62.118  93.303  1.00 41.04           C  
ANISOU  106  C   SER A  15     6149   5531   3914   -733     10  -1762       C  
ATOM    107  O   SER A  15      72.309  63.048  93.644  1.00 42.85           O  
ANISOU  107  O   SER A  15     6448   5660   4172   -703    129  -1857       O  
ATOM    108  CB  SER A  15      73.945  60.612  95.095  1.00 48.81           C  
ANISOU  108  CB  SER A  15     7114   6860   4570   -819   -217  -1661       C  
ATOM    109  OG  SER A  15      73.757  59.402  95.809  1.00 52.06           O  
ANISOU  109  OG  SER A  15     7531   7435   4814   -800   -287  -1541       O  
ATOM    110  N   ALA A  16      73.971  62.253  92.343  1.00 36.33           N  
ANISOU  110  N   ALA A  16     5480   4867   3459   -760    -57  -1724       N  
ATOM    111  CA  ALA A  16      74.197  63.548  91.714  1.00 33.21           C  
ANISOU  111  CA  ALA A  16     5119   4283   3216   -795     14  -1827       C  
ATOM    112  C   ALA A  16      72.994  63.981  90.887  1.00 35.56           C  
ANISOU  112  C   ALA A  16     5459   4401   3652   -671    162  -1809       C  
ATOM    113  O   ALA A  16      72.583  65.147  90.944  1.00 41.63           O  
ANISOU  113  O   ALA A  16     6296   5024   4497   -652    254  -1895       O  
ATOM    114  CB  ALA A  16      75.455  63.500  90.852  1.00 34.90           C  
ANISOU  114  CB  ALA A  16     5244   4479   3539   -865    -82  -1786       C  
ATOM    115  N   LEU A  17      72.420  63.061  90.107  1.00 31.29           N  
ANISOU  115  N   LEU A  17     4846   3866   3176   -550    165  -1637       N  
ATOM    116  CA  LEU A  17      71.228  63.401  89.336  1.00 27.93           C  
ANISOU  116  CA  LEU A  17     4442   3290   2879   -418    287  -1604       C  
ATOM    117  C   LEU A  17      70.071  63.782  90.252  1.00 36.95           C  
ANISOU  117  C   LEU A  17     5662   4432   3944   -372    403  -1719       C  
ATOM    118  O   LEU A  17      69.364  64.763  89.998  1.00 39.13           O  
ANISOU  118  O   LEU A  17     5989   4549   4329   -306    504  -1786       O  
ATOM    119  CB  LEU A  17      70.830  62.235  88.430  1.00 27.82           C  
ANISOU  119  CB  LEU A  17     4330   3314   2926   -310    260  -1410       C  
ATOM    120  CG  LEU A  17      71.843  61.871  87.347  1.00 28.70           C  
ANISOU  120  CG  LEU A  17     4358   3407   3138   -340    171  -1300       C  
ATOM    121  CD1 LEU A  17      71.475  60.548  86.683  1.00 26.61           C  
ANISOU  121  CD1 LEU A  17     3996   3214   2901   -247    139  -1125       C  
ATOM    122  CD2 LEU A  17      71.948  62.990  86.327  1.00 28.49           C  
ANISOU  122  CD2 LEU A  17     4376   3181   3269   -342    228  -1330       C  
ATOM    123  N   GLN A  18      69.866  63.019  91.327  1.00 38.70           N  
ANISOU  123  N   GLN A  18     5885   4833   3986   -397    383  -1723       N  
ATOM    124  CA  GLN A  18      68.751  63.304  92.225  1.00 44.48           C  
ANISOU  124  CA  GLN A  18     6670   5584   4648   -350    493  -1805       C  
ATOM    125  C   GLN A  18      68.903  64.671  92.878  1.00 40.78           C  
ANISOU  125  C   GLN A  18     6268   5030   4199   -396    526  -1945       C  
ATOM    126  O   GLN A  18      67.924  65.415  93.010  1.00 38.37           O  
ANISOU  126  O   GLN A  18     5989   4627   3965   -313    633  -2005       O  
ATOM    127  CB  GLN A  18      68.639  62.208  93.285  1.00 51.95           C  
ANISOU  127  CB  GLN A  18     7615   6744   5381   -391    456  -1763       C  
ATOM    128  CG  GLN A  18      67.851  60.990  92.828  1.00 57.90           C  
ANISOU  128  CG  GLN A  18     8305   7559   6137   -298    480  -1618       C  
ATOM    129  CD  GLN A  18      68.021  59.804  93.754  1.00 66.72           C  
ANISOU  129  CD  GLN A  18     9424   8877   7048   -354    409  -1535       C  
ATOM    130  OE1 GLN A  18      68.984  59.045  93.639  1.00 68.50           O  
ANISOU  130  OE1 GLN A  18     9606   9182   7239   -393    264  -1418       O  
ATOM    131  NE2 GLN A  18      67.087  59.642  94.685  1.00 69.39           N  
ANISOU  131  NE2 GLN A  18     9808   9290   7268   -346    504  -1574       N  
ATOM    132  N   GLU A  19      70.127  65.026  93.276  1.00 41.92           N  
ANISOU  132  N   GLU A  19     6431   5209   4287   -524    432  -1998       N  
ATOM    133  CA  GLU A  19      70.374  66.328  93.884  1.00 45.04           C  
ANISOU  133  CA  GLU A  19     6890   5524   4700   -581    462  -2136       C  
ATOM    134  C   GLU A  19      70.099  67.475  92.922  1.00 45.02           C  
ANISOU  134  C   GLU A  19     6910   5287   4910   -517    535  -2161       C  
ATOM    135  O   GLU A  19      69.822  68.592  93.370  1.00 49.51           O  
ANISOU  135  O   GLU A  19     7537   5758   5517   -517    599  -2272       O  
ATOM    136  CB  GLU A  19      71.817  66.406  94.390  1.00 46.31           C  
ANISOU  136  CB  GLU A  19     7046   5776   4772   -732    335  -2176       C  
ATOM    137  N   ASN A  20      70.166  67.226  91.615  1.00 40.04           N  
ANISOU  137  N   ASN A  20     6240   4560   4414   -463    523  -2056       N  
ATOM    138  CA  ASN A  20      69.914  68.241  90.603  1.00 41.73           C  
ANISOU  138  CA  ASN A  20     6482   4551   4824   -396    577  -2045       C  
ATOM    139  C   ASN A  20      68.507  68.147  90.020  1.00 40.12           C  
ANISOU  139  C   ASN A  20     6259   4266   4718   -221    660  -1982       C  
ATOM    140  O   ASN A  20      68.249  68.699  88.945  1.00 43.37           O  
ANISOU  140  O   ASN A  20     6678   4509   5290   -143    679  -1921       O  
ATOM    141  CB  ASN A  20      70.961  68.147  89.489  1.00 42.72           C  
ANISOU  141  CB  ASN A  20     6578   4614   5037   -459    507  -1964       C  
ATOM    142  CG  ASN A  20      72.296  68.754  89.896  1.00 49.57           C  
ANISOU  142  CG  ASN A  20     7462   5497   5874   -620    441  -2045       C  
ATOM    143  OD1 ASN A  20      72.531  69.946  89.702  1.00 52.81           O  
ANISOU  143  OD1 ASN A  20     7928   5757   6381   -650    475  -2100       O  
ATOM    144  ND2 ASN A  20      73.173  67.935  90.471  1.00 48.37           N  
ANISOU  144  ND2 ASN A  20     7257   5532   5588   -723    341  -2048       N  
ATOM    145  N   GLY A  21      67.595  67.464  90.707  1.00 39.66           N  
ANISOU  145  N   GLY A  21     6174   4332   4565   -160    703  -1987       N  
ATOM    146  CA  GLY A  21      66.225  67.377  90.242  1.00 40.70           C  
ANISOU  146  CA  GLY A  21     6267   4408   4790      5    778  -1936       C  
ATOM    147  C   GLY A  21      66.016  66.521  89.016  1.00 41.22           C  
ANISOU  147  C   GLY A  21     6264   4461   4937     85    754  -1786       C  
ATOM    148  O   GLY A  21      65.002  66.677  88.330  1.00 48.05           O  
ANISOU  148  O   GLY A  21     7094   5243   5922    226    793  -1729       O  
ATOM    149  N   ILE A  22      66.945  65.623  88.712  1.00 34.30           N  
ANISOU  149  N   ILE A  22     5364   3669   3999      0    682  -1721       N  
ATOM    150  CA  ILE A  22      66.822  64.719  87.571  1.00 33.86           C  
ANISOU  150  CA  ILE A  22     5244   3610   4011     64    663  -1583       C  
ATOM    151  C   ILE A  22      66.405  63.368  88.146  1.00 36.29           C  
ANISOU  151  C   ILE A  22     5478   4123   4187     79    646  -1512       C  
ATOM    152  O   ILE A  22      67.236  62.559  88.561  1.00 38.79           O  
ANISOU  152  O   ILE A  22     5767   4585   4386    -13    555  -1460       O  
ATOM    153  CB  ILE A  22      68.121  64.640  86.770  1.00 30.94           C  
ANISOU  153  CB  ILE A  22     4857   3215   3683    -25    559  -1497       C  
ATOM    154  CG1 ILE A  22      68.530  66.040  86.301  1.00 35.15           C  
ANISOU  154  CG1 ILE A  22     5478   3541   4335    -59    586  -1569       C  
ATOM    155  CG2 ILE A  22      67.968  63.688  85.584  1.00 32.83           C  
ANISOU  155  CG2 ILE A  22     4999   3481   3995     53    510  -1305       C  
ATOM    156  CD1 ILE A  22      69.892  66.102  85.637  1.00 37.25           C  
ANISOU  156  CD1 ILE A  22     5739   3779   4635   -181    509  -1527       C  
ATOM    157  N   ASN A  23      65.095  63.119  88.168  1.00 32.79           N  
ANISOU  157  N   ASN A  23     5000   3689   3769    196    734  -1507       N  
ATOM    158  CA  ASN A  23      64.542  61.968  88.870  1.00 34.48           C  
ANISOU  158  CA  ASN A  23     5163   4085   3852    199    751  -1465       C  
ATOM    159  C   ASN A  23      64.250  60.772  87.974  1.00 30.09           C  
ANISOU  159  C   ASN A  23     4500   3587   3344    268    704  -1281       C  
ATOM    160  O   ASN A  23      63.996  59.685  88.498  1.00 34.85           O  
ANISOU  160  O   ASN A  23     5066   4339   3837    250    700  -1222       O  
ATOM    161  CB  ASN A  23      63.257  62.367  89.605  1.00 35.23           C  
ANISOU  161  CB  ASN A  23     5258   4191   3939    271    859  -1553       C  
ATOM    162  CG  ASN A  23      63.514  63.375  90.703  1.00 48.32           C  
ANISOU  162  CG  ASN A  23     6999   5834   5525    199    877  -1695       C  
ATOM    163  OD1 ASN A  23      64.473  63.245  91.465  1.00 52.45           O  
ANISOU  163  OD1 ASN A  23     7578   6445   5906     68    825  -1739       O  
ATOM    164  ND2 ASN A  23      62.668  64.397  90.780  1.00 52.52           N  
ANISOU  164  ND2 ASN A  23     7537   6260   6157    285    942  -1766       N  
ATOM    165  N   ARG A  24      64.285  60.930  86.655  1.00 24.54           N  
ANISOU  165  N   ARG A  24     3757   2773   2796    337    670  -1189       N  
ATOM    166  CA  ARG A  24      63.972  59.848  85.722  1.00 25.78           C  
ANISOU  166  CA  ARG A  24     3812   2978   3004    400    631  -1028       C  
ATOM    167  C   ARG A  24      65.255  59.459  84.994  1.00 24.46           C  
ANISOU  167  C   ARG A  24     3624   2812   2856    330    516   -923       C  
ATOM    168  O   ARG A  24      65.699  60.156  84.075  1.00 24.79           O  
ANISOU  168  O   ARG A  24     3686   2729   3005    334    491   -906       O  
ATOM    169  CB  ARG A  24      62.881  60.269  84.742  1.00 27.63           C  
ANISOU  169  CB  ARG A  24     4007   3101   3392    541    685  -1007       C  
ATOM    170  CG  ARG A  24      61.554  60.602  85.405  1.00 32.72           C  
ANISOU  170  CG  ARG A  24     4642   3749   4041    624    804  -1118       C  
ATOM    171  CD  ARG A  24      60.496  60.960  84.365  1.00 37.87           C  
ANISOU  171  CD  ARG A  24     5215   4327   4847    763    789  -1058       C  
ATOM    172  N   TYR A  25      65.842  58.336  85.393  1.00 22.38           N  
ANISOU  172  N   TYR A  25     3321   2688   2494    266    448   -851       N  
ATOM    173  CA  TYR A  25      67.119  57.935  84.818  1.00 20.29           C  
ANISOU  173  CA  TYR A  25     3023   2437   2251    197    341   -770       C  
ATOM    174  C   TYR A  25      67.274  56.430  84.945  1.00 19.51           C  
ANISOU  174  C   TYR A  25     2850   2473   2090    190    284   -653       C  
ATOM    175  O   TYR A  25      66.612  55.783  85.764  1.00 22.90           O  
ANISOU  175  O   TYR A  25     3283   2997   2423    202    318   -648       O  
ATOM    176  CB  TYR A  25      68.291  58.650  85.504  1.00 24.22           C  
ANISOU  176  CB  TYR A  25     3584   2932   2687     80    289   -867       C  
ATOM    177  CG  TYR A  25      68.379  58.353  86.985  1.00 25.38           C  
ANISOU  177  CG  TYR A  25     3772   3211   2662     17    276   -932       C  
ATOM    178  CD1 TYR A  25      68.997  57.199  87.443  1.00 27.68           C  
ANISOU  178  CD1 TYR A  25     4019   3641   2855    -28    182   -847       C  
ATOM    179  CD2 TYR A  25      67.823  59.211  87.918  1.00 28.20           C  
ANISOU  179  CD2 TYR A  25     4216   3550   2951      4    359  -1077       C  
ATOM    180  CE1 TYR A  25      69.065  56.914  88.787  1.00 31.93           C  
ANISOU  180  CE1 TYR A  25     4609   4304   3219    -88    162   -891       C  
ATOM    181  CE2 TYR A  25      67.890  58.938  89.276  1.00 36.00           C  
ANISOU  181  CE2 TYR A  25     5252   4669   3759    -66    351  -1138       C  
ATOM    182  CZ  TYR A  25      68.514  57.784  89.699  1.00 37.77           C  
ANISOU  182  CZ  TYR A  25     5441   5036   3874   -113    248  -1036       C  
ATOM    183  OH  TYR A  25      68.595  57.496  91.042  1.00 45.09           O  
ANISOU  183  OH  TYR A  25     6429   6098   4605   -186    229  -1081       O  
ATOM    184  N   MET A  26      68.175  55.888  84.132  1.00 18.78           N  
ANISOU  184  N   MET A  26     2695   2384   2057    165    202   -564       N  
ATOM    185  CA  MET A  26      68.587  54.500  84.240  1.00 17.41           C  
ANISOU  185  CA  MET A  26     2453   2319   1842    151    132   -458       C  
ATOM    186  C   MET A  26      70.098  54.429  84.106  1.00 19.26           C  
ANISOU  186  C   MET A  26     2655   2572   2091     71     23   -449       C  
ATOM    187  O   MET A  26      70.666  55.013  83.183  1.00 20.78           O  
ANISOU  187  O   MET A  26     2830   2682   2384     50     16   -461       O  
ATOM    188  CB  MET A  26      67.932  53.634  83.161  1.00 19.71           C  
ANISOU  188  CB  MET A  26     2664   2598   2225    228    157   -350       C  
ATOM    189  CG  MET A  26      66.435  53.512  83.364  1.00 22.60           C  
ANISOU  189  CG  MET A  26     3036   2973   2576    303    257   -358       C  
ATOM    190  SD  MET A  26      65.674  52.599  82.032  1.00 22.56           S  
ANISOU  190  SD  MET A  26     2932   2957   2683    382    281   -250       S  
ATOM    191  CE  MET A  26      65.642  53.824  80.714  1.00 21.03           C  
ANISOU  191  CE  MET A  26     2748   2626   2618    424    293   -275       C  
ATOM    192  N   VAL A  27      70.745  53.735  85.035  1.00 19.97           N  
ANISOU  192  N   VAL A  27     2737   2771   2078     24    -61   -429       N  
ATOM    193  CA  VAL A  27      72.156  53.393  84.880  1.00 20.10           C  
ANISOU  193  CA  VAL A  27     2688   2826   2124    -35   -178   -405       C  
ATOM    194  C   VAL A  27      72.239  52.119  84.050  1.00 22.29           C  
ANISOU  194  C   VAL A  27     2866   3119   2484     18   -207   -278       C  
ATOM    195  O   VAL A  27      71.680  51.082  84.426  1.00 25.11           O  
ANISOU  195  O   VAL A  27     3217   3532   2792     61   -207   -196       O  
ATOM    196  CB  VAL A  27      72.834  53.221  86.247  1.00 22.44           C  
ANISOU  196  CB  VAL A  27     3016   3236   2274   -100   -274   -437       C  
ATOM    197  CG1 VAL A  27      74.262  52.720  86.072  1.00 24.81           C  
ANISOU  197  CG1 VAL A  27     3221   3587   2619   -142   -408   -405       C  
ATOM    198  CG2 VAL A  27      72.784  54.532  87.014  1.00 25.31           C  
ANISOU  198  CG2 VAL A  27     3478   3580   2558   -164   -237   -584       C  
ATOM    199  N   LEU A  28      72.905  52.199  82.897  1.00 18.88           N  
ANISOU  199  N   LEU A  28     2361   2632   2180      7   -219   -266       N  
ATOM    200  CA  LEU A  28      72.924  51.090  81.951  1.00 18.81           C  
ANISOU  200  CA  LEU A  28     2260   2624   2265     54   -225   -165       C  
ATOM    201  C   LEU A  28      74.173  50.227  82.050  1.00 24.62           C  
ANISOU  201  C   LEU A  28     2901   3423   3030     29   -339   -128       C  
ATOM    202  O   LEU A  28      74.096  49.015  81.830  1.00 27.87           O  
ANISOU  202  O   LEU A  28     3252   3859   3477     78   -361    -37       O  
ATOM    203  CB  LEU A  28      72.796  51.614  80.521  1.00 15.95           C  
ANISOU  203  CB  LEU A  28     1875   2167   2020     60   -158   -171       C  
ATOM    204  CG  LEU A  28      71.507  52.384  80.268  1.00 16.85           C  
ANISOU  204  CG  LEU A  28     2067   2209   2129    110    -58   -192       C  
ATOM    205  CD1 LEU A  28      71.427  52.676  78.780  1.00 14.97           C  
ANISOU  205  CD1 LEU A  28     1803   1888   1997    121    -13   -167       C  
ATOM    206  CD2 LEU A  28      70.271  51.611  80.725  1.00 16.59           C  
ANISOU  206  CD2 LEU A  28     2042   2219   2042    184    -15   -141       C  
ATOM    207  N   ASN A  29      75.330  50.818  82.331  1.00 20.12           N  
ANISOU  207  N   ASN A  29     2307   2874   2461    -46   -411   -200       N  
ATOM    208  CA  ASN A  29      76.536  50.038  82.579  1.00 22.50           C  
ANISOU  208  CA  ASN A  29     2508   3250   2792    -62   -535   -176       C  
ATOM    209  C   ASN A  29      77.444  50.880  83.469  1.00 22.97           C  
ANISOU  209  C   ASN A  29     2585   3362   2782   -148   -616   -276       C  
ATOM    210  O   ASN A  29      77.022  51.915  83.995  1.00 20.29           O  
ANISOU  210  O   ASN A  29     2349   3002   2359   -189   -570   -355       O  
ATOM    211  CB  ASN A  29      77.176  49.580  81.254  1.00 23.68           C  
ANISOU  211  CB  ASN A  29     2535   3362   3100    -58   -523   -155       C  
ATOM    212  CG  ASN A  29      77.584  50.736  80.347  1.00 19.06           C  
ANISOU  212  CG  ASN A  29     1948   2707   2587   -134   -458   -243       C  
ATOM    213  OD1 ASN A  29      78.265  51.655  80.778  1.00 21.02           O  
ANISOU  213  OD1 ASN A  29     2213   2964   2809   -215   -489   -335       O  
ATOM    214  ND2 ASN A  29      77.163  50.686  79.077  1.00 18.30           N  
ANISOU  214  ND2 ASN A  29     1838   2542   2576   -115   -366   -214       N  
ATOM    215  N   SER A  30      78.686  50.425  83.665  1.00 22.45           N  
ANISOU  215  N   SER A  30     2410   3365   2754   -173   -740   -280       N  
ATOM    216  CA  SER A  30      79.576  51.105  84.602  1.00 24.39           C  
ANISOU  216  CA  SER A  30     2658   3684   2923   -258   -839   -376       C  
ATOM    217  C   SER A  30      79.961  52.511  84.154  1.00 23.49           C  
ANISOU  217  C   SER A  30     2563   3507   2853   -361   -773   -510       C  
ATOM    218  O   SER A  30      80.509  53.270  84.968  1.00 24.43           O  
ANISOU  218  O   SER A  30     2710   3675   2897   -446   -830   -611       O  
ATOM    219  CB  SER A  30      80.844  50.271  84.835  1.00 30.26           C  
ANISOU  219  CB  SER A  30     3258   4521   3719   -251   -997   -352       C  
ATOM    220  OG  SER A  30      81.626  50.182  83.653  1.00 31.67           O  
ANISOU  220  OG  SER A  30     3300   4661   4073   -268   -975   -379       O  
ATOM    221  N   GLN A  31      79.700  52.868  82.893  1.00 20.64           N  
ANISOU  221  N   GLN A  31     2196   3040   2606   -363   -657   -511       N  
ATOM    222  CA  GLN A  31      80.029  54.183  82.356  1.00 24.24           C  
ANISOU  222  CA  GLN A  31     2686   3413   3111   -463   -583   -619       C  
ATOM    223  C   GLN A  31      78.836  54.977  81.860  1.00 20.31           C  
ANISOU  223  C   GLN A  31     2321   2789   2607   -438   -444   -616       C  
ATOM    224  O   GLN A  31      78.946  56.202  81.747  1.00 22.94           O  
ANISOU  224  O   GLN A  31     2727   3042   2949   -516   -388   -708       O  
ATOM    225  CB  GLN A  31      80.998  54.072  81.166  1.00 29.84           C  
ANISOU  225  CB  GLN A  31     3267   4099   3969   -513   -568   -633       C  
ATOM    226  CG  GLN A  31      82.379  53.583  81.473  1.00 42.04           C  
ANISOU  226  CG  GLN A  31     4657   5755   5563   -559   -694   -674       C  
ATOM    227  CD  GLN A  31      83.298  53.777  80.288  1.00 51.08           C  
ANISOU  227  CD  GLN A  31     5690   6867   6853   -637   -644   -724       C  
ATOM    228  OE1 GLN A  31      83.852  54.861  80.088  1.00 53.80           O  
ANISOU  228  OE1 GLN A  31     6051   7172   7220   -760   -601   -830       O  
ATOM    229  NE2 GLN A  31      83.448  52.735  79.480  1.00 51.49           N  
ANISOU  229  NE2 GLN A  31     5632   6930   7003   -573   -637   -654       N  
ATOM    230  N   LEU A  32      77.726  54.327  81.528  1.00 19.42           N  
ANISOU  230  N   LEU A  32     2237   2652   2491   -331   -391   -516       N  
ATOM    231  CA  LEU A  32      76.668  54.935  80.741  1.00 18.13           C  
ANISOU  231  CA  LEU A  32     2160   2370   2358   -291   -270   -498       C  
ATOM    232  C   LEU A  32      75.375  54.996  81.537  1.00 18.05           C  
ANISOU  232  C   LEU A  32     2249   2358   2249   -216   -229   -487       C  
ATOM    233  O   LEU A  32      74.946  53.990  82.101  1.00 19.25           O  
ANISOU  233  O   LEU A  32     2381   2592   2343   -154   -263   -420       O  
ATOM    234  CB  LEU A  32      76.440  54.129  79.460  1.00 18.31           C  
ANISOU  234  CB  LEU A  32     2112   2369   2476   -236   -231   -402       C  
ATOM    235  CG  LEU A  32      75.215  54.510  78.648  1.00 20.56           C  
ANISOU  235  CG  LEU A  32     2473   2556   2783   -172   -129   -359       C  
ATOM    236  CD1 LEU A  32      75.390  55.908  78.039  1.00 19.11           C  
ANISOU  236  CD1 LEU A  32     2371   2250   2639   -240    -67   -421       C  
ATOM    237  CD2 LEU A  32      75.024  53.445  77.577  1.00 19.37           C  
ANISOU  237  CD2 LEU A  32     2238   2419   2701   -120   -113   -265       C  
ATOM    238  N   ALA A  33      74.741  56.165  81.547  1.00 17.40           N  
ANISOU  238  N   ALA A  33     2275   2177   2158   -221   -149   -551       N  
ATOM    239  CA  ALA A  33      73.394  56.318  82.072  1.00 17.14           C  
ANISOU  239  CA  ALA A  33     2325   2125   2062   -140    -83   -551       C  
ATOM    240  C   ALA A  33      72.577  57.099  81.052  1.00 21.90           C  
ANISOU  240  C   ALA A  33     2983   2589   2750    -89     12   -542       C  
ATOM    241  O   ALA A  33      73.131  57.781  80.189  1.00 19.40           O  
ANISOU  241  O   ALA A  33     2677   2181   2511   -141     28   -556       O  
ATOM    242  CB  ALA A  33      73.394  57.033  83.432  1.00 20.29           C  
ANISOU  242  CB  ALA A  33     2809   2552   2348   -189    -89   -666       C  
ATOM    243  N   VAL A  34      71.253  56.988  81.136  1.00 17.15           N  
ANISOU  243  N   VAL A  34     2413   1971   2133     11     74   -515       N  
ATOM    244  CA  VAL A  34      70.357  57.789  80.306  1.00 16.33           C  
ANISOU  244  CA  VAL A  34     2363   1737   2104     78    152   -510       C  
ATOM    245  C   VAL A  34      69.389  58.534  81.215  1.00 18.52           C  
ANISOU  245  C   VAL A  34     2723   1977   2335    127    216   -598       C  
ATOM    246  O   VAL A  34      68.995  58.026  82.271  1.00 19.33           O  
ANISOU  246  O   VAL A  34     2821   2180   2344    139    219   -624       O  
ATOM    247  CB  VAL A  34      69.598  56.932  79.262  1.00 16.14           C  
ANISOU  247  CB  VAL A  34     2272   1726   2136    167    167   -394       C  
ATOM    248  CG1 VAL A  34      70.564  56.434  78.181  1.00 17.13           C  
ANISOU  248  CG1 VAL A  34     2329   1860   2321    112    125   -328       C  
ATOM    249  CG2 VAL A  34      68.878  55.766  79.929  1.00 18.88           C  
ANISOU  249  CG2 VAL A  34     2564   2192   2419    223    167   -354       C  
ATOM    250  N   ILE A  35      69.031  59.758  80.826  1.00 18.40           N  
ANISOU  250  N   ILE A  35     2789   1814   2386    151    271   -649       N  
ATOM    251  CA  ILE A  35      68.099  60.558  81.610  1.00 20.66           C  
ANISOU  251  CA  ILE A  35     3151   2045   2655    207    342   -749       C  
ATOM    252  C   ILE A  35      66.965  61.034  80.721  1.00 21.63           C  
ANISOU  252  C   ILE A  35     3288   2050   2879    333    397   -708       C  
ATOM    253  O   ILE A  35      67.136  61.232  79.517  1.00 22.12           O  
ANISOU  253  O   ILE A  35     3352   2028   3023    347    379   -628       O  
ATOM    254  CB  ILE A  35      68.785  61.761  82.292  1.00 20.58           C  
ANISOU  254  CB  ILE A  35     3240   1953   2627    113    356   -886       C  
ATOM    255  CG1 ILE A  35      69.306  62.759  81.249  1.00 21.15           C  
ANISOU  255  CG1 ILE A  35     3373   1854   2808     78    363   -875       C  
ATOM    256  CG2 ILE A  35      69.905  61.282  83.216  1.00 21.55           C  
ANISOU  256  CG2 ILE A  35     3338   2212   2640    -11    284   -929       C  
ATOM    257  CD1 ILE A  35      69.904  64.024  81.890  1.00 25.25           C  
ANISOU  257  CD1 ILE A  35     3999   2268   3326    -19    391  -1021       C  
ATOM    258  N   TYR A  36      65.798  61.219  81.329  1.00 21.56           N  
ANISOU  258  N   TYR A  36     3288   2041   2862    426    462   -768       N  
ATOM    259  CA  TYR A  36      64.589  61.668  80.646  1.00 23.87           C  
ANISOU  259  CA  TYR A  36     3578   2235   3255    566    508   -745       C  
ATOM    260  C   TYR A  36      64.092  62.911  81.366  1.00 27.69           C  
ANISOU  260  C   TYR A  36     4151   2600   3769    605    583   -887       C  
ATOM    261  O   TYR A  36      63.873  62.879  82.580  1.00 25.36           O  
ANISOU  261  O   TYR A  36     3866   2378   3392    580    631   -998       O  
ATOM    262  CB  TYR A  36      63.529  60.561  80.646  1.00 22.12           C  
ANISOU  262  CB  TYR A  36     3248   2141   3016    653    525   -689       C  
ATOM    263  CG  TYR A  36      63.983  59.344  79.874  1.00 22.75           C  
ANISOU  263  CG  TYR A  36     3244   2319   3081    618    459   -557       C  
ATOM    264  CD1 TYR A  36      63.631  59.176  78.542  1.00 21.73           C  
ANISOU  264  CD1 TYR A  36     3074   2150   3034    683    432   -454       C  
ATOM    265  CD2 TYR A  36      64.810  58.390  80.458  1.00 18.52           C  
ANISOU  265  CD2 TYR A  36     2675   1910   2451    521    418   -537       C  
ATOM    266  CE1 TYR A  36      64.067  58.090  77.819  1.00 21.09           C  
ANISOU  266  CE1 TYR A  36     2919   2152   2942    645    382   -349       C  
ATOM    267  CE2 TYR A  36      65.253  57.297  79.738  1.00 20.13           C  
ANISOU  267  CE2 TYR A  36     2802   2187   2660    496    363   -426       C  
ATOM    268  CZ  TYR A  36      64.871  57.151  78.410  1.00 19.66           C  
ANISOU  268  CZ  TYR A  36     2700   2085   2683    554    352   -339       C  
ATOM    269  OH  TYR A  36      65.305  56.061  77.688  1.00 20.94           O  
ANISOU  269  OH  TYR A  36     2787   2319   2852    524    308   -245       O  
ATOM    270  N   VAL A  37      63.923  64.004  80.629  1.00 27.90           N  
ANISOU  270  N   VAL A  37     4238   2458   3907    655    579   -877       N  
ATOM    271  CA  VAL A  37      63.702  65.314  81.244  1.00 30.23           C  
ANISOU  271  CA  VAL A  37     4602   2651   4234    661    604   -991       C  
ATOM    272  C   VAL A  37      62.643  66.071  80.457  1.00 37.59           C  
ANISOU  272  C   VAL A  37     5509   3486   5285    793    574   -939       C  
ATOM    273  O   VAL A  37      62.408  65.797  79.273  1.00 36.23           O  
ANISOU  273  O   VAL A  37     5295   3300   5170    843    520   -810       O  
ATOM    274  CB  VAL A  37      65.002  66.140  81.299  1.00 34.12           C  
ANISOU  274  CB  VAL A  37     5207   3032   4724    526    595  -1041       C  
ATOM    275  CG1 VAL A  37      65.985  65.542  82.306  1.00 35.00           C  
ANISOU  275  CG1 VAL A  37     5335   3256   4709    385    608  -1133       C  
ATOM    276  CG2 VAL A  37      65.623  66.219  79.920  1.00 36.71           C  
ANISOU  276  CG2 VAL A  37     5559   3270   5119    499    544   -911       C  
ATOM    277  N   PRO A  38      61.988  67.044  81.096  1.00 39.37           N  
ANISOU  277  N   PRO A  38     5763   3650   5547    851    602  -1044       N  
ATOM    278  CA  PRO A  38      61.012  67.871  80.372  1.00 45.08           C  
ANISOU  278  CA  PRO A  38     6471   4265   6391    980    561  -1010       C  
ATOM    279  C   PRO A  38      61.662  68.674  79.253  1.00 49.88           C  
ANISOU  279  C   PRO A  38     7163   4707   7082    950    507   -918       C  
ATOM    280  O   PRO A  38      62.880  68.846  79.193  1.00 44.85           O  
ANISOU  280  O   PRO A  38     6610   4018   6412    823    514   -913       O  
ATOM    281  CB  PRO A  38      60.448  68.793  81.461  1.00 47.61           C  
ANISOU  281  CB  PRO A  38     6831   4541   6716   1026    615  -1162       C  
ATOM    282  CG  PRO A  38      60.690  68.066  82.742  1.00 43.91           C  
ANISOU  282  CG  PRO A  38     6349   4223   6113    947    687  -1258       C  
ATOM    283  CD  PRO A  38      61.987  67.334  82.543  1.00 40.51           C  
ANISOU  283  CD  PRO A  38     5943   3836   5612    808    671  -1202       C  
ATOM    284  N   VAL A  39      60.813  69.180  78.353  1.00 61.28           N  
ANISOU  284  N   VAL A  39     8581   6070   8632   1063    449   -849       N  
ATOM    285  CA  VAL A  39      61.303  69.937  77.203  1.00 65.35           C  
ANISOU  285  CA  VAL A  39     9178   6429   9221   1039    397   -742       C  
ATOM    286  C   VAL A  39      62.004  71.217  77.643  1.00 65.53           C  
ANISOU  286  C   VAL A  39     9337   6285   9275    973    427   -826       C  
ATOM    287  O   VAL A  39      62.939  71.682  76.980  1.00 65.66           O  
ANISOU  287  O   VAL A  39     9445   6198   9305    878    413   -758       O  
ATOM    288  CB  VAL A  39      60.144  70.240  76.231  1.00 67.38           C  
ANISOU  288  CB  VAL A  39     9373   6637   9590   1176    323   -658       C  
ATOM    289  N   ASP A  40      61.578  71.802  78.761  1.00 62.96           N  
ANISOU  289  N   ASP A  40     9029   5938   8955   1013    474   -976       N  
ATOM    290  CA  ASP A  40      62.177  73.036  79.255  1.00 63.87           C  
ANISOU  290  CA  ASP A  40     9270   5897   9100    949    506  -1070       C  
ATOM    291  C   ASP A  40      63.493  72.810  79.992  1.00 61.45           C  
ANISOU  291  C   ASP A  40     9017   5643   8689    769    557  -1142       C  
ATOM    292  O   ASP A  40      64.050  73.770  80.535  1.00 65.38           O  
ANISOU  292  O   ASP A  40     9609   6036   9198    693    589  -1240       O  
ATOM    293  CB  ASP A  40      61.191  73.764  80.174  1.00 65.65           C  
ANISOU  293  CB  ASP A  40     9497   6082   9364   1063    540  -1211       C  
ATOM    294  N   PHE A  41      64.003  71.581  80.014  1.00 56.65           N  
ANISOU  294  N   PHE A  41     8349   5193   7984    696    559  -1101       N  
ATOM    295  CA  PHE A  41      65.207  71.268  80.775  1.00 51.75           C  
ANISOU  295  CA  PHE A  41     7760   4642   7260    529    592  -1180       C  
ATOM    296  C   PHE A  41      66.409  72.040  80.243  1.00 55.52           C  
ANISOU  296  C   PHE A  41     8334   4992   7768    393    578  -1156       C  
ATOM    297  O   PHE A  41      66.647  72.095  79.032  1.00 55.74           O  
ANISOU  297  O   PHE A  41     8381   4952   7848    389    540  -1022       O  
ATOM    298  CB  PHE A  41      65.469  69.763  80.719  1.00 41.55           C  
ANISOU  298  CB  PHE A  41     6382   3528   5876    495    582  -1121       C  
ATOM    299  CG  PHE A  41      66.748  69.337  81.375  1.00 39.45           C  
ANISOU  299  CG  PHE A  41     6136   3345   5508    323    591  -1190       C  
ATOM    300  CD1 PHE A  41      66.845  69.267  82.757  1.00 39.19           C  
ANISOU  300  CD1 PHE A  41     6104   3407   5379    268    626  -1335       C  
ATOM    301  CD2 PHE A  41      67.847  68.975  80.609  1.00 40.60           C  
ANISOU  301  CD2 PHE A  41     6291   3489   5646    210    557  -1112       C  
ATOM    302  CE1 PHE A  41      68.018  68.866  83.366  1.00 38.82           C  
ANISOU  302  CE1 PHE A  41     6064   3456   5232    108    610  -1400       C  
ATOM    303  CE2 PHE A  41      69.023  68.569  81.210  1.00 42.02           C  
ANISOU  303  CE2 PHE A  41     6467   3759   5739     51    547  -1185       C  
ATOM    304  CZ  PHE A  41      69.111  68.515  82.590  1.00 43.13           C  
ANISOU  304  CZ  PHE A  41     6604   3998   5783      1    565  -1327       C  
ATOM    305  N   ASP A  42      67.170  72.633  81.162  1.00 59.11           N  
ANISOU  305  N   ASP A  42     8848   5428   8183    273    610  -1290       N  
ATOM    306  CA  ASP A  42      68.365  73.407  80.833  1.00 59.90           C  
ANISOU  306  CA  ASP A  42     9030   5424   8306    123    605  -1294       C  
ATOM    307  C   ASP A  42      69.557  72.457  80.825  1.00 54.58           C  
ANISOU  307  C   ASP A  42     8310   4888   7540    -29    585  -1280       C  
ATOM    308  O   ASP A  42      70.070  72.076  81.880  1.00 51.14           O  
ANISOU  308  O   ASP A  42     7847   4575   7010   -119    591  -1393       O  
ATOM    309  CB  ASP A  42      68.553  74.541  81.835  1.00 64.74           C  
ANISOU  309  CB  ASP A  42     9716   5954   8927     70    645  -1452       C  
ATOM    310  CG  ASP A  42      69.749  75.418  81.516  1.00 72.24           C  
ANISOU  310  CG  ASP A  42    10747   6793   9908    -87    646  -1464       C  
ATOM    311  OD1 ASP A  42      70.318  75.290  80.413  1.00 75.23           O  
ANISOU  311  OD1 ASP A  42    11133   7136  10316   -140    619  -1339       O  
ATOM    312  OD2 ASP A  42      70.122  76.242  82.377  1.00 77.11           O  
ANISOU  312  OD2 ASP A  42    11416   7364  10517   -164    677  -1601       O  
ATOM    313  N   GLU A  43      70.012  72.085  79.627  1.00 48.29           N  
ANISOU  313  N   GLU A  43     7503   4076   6768    -61    555  -1142       N  
ATOM    314  CA  GLU A  43      71.070  71.088  79.507  1.00 51.02           C  
ANISOU  314  CA  GLU A  43     7787   4556   7041   -190    531  -1123       C  
ATOM    315  C   GLU A  43      72.412  71.582  80.032  1.00 50.46           C  
ANISOU  315  C   GLU A  43     7736   4498   6937   -379    530  -1227       C  
ATOM    316  O   GLU A  43      73.301  70.759  80.277  1.00 49.80           O  
ANISOU  316  O   GLU A  43     7580   4557   6786   -489    499  -1253       O  
ATOM    317  CB  GLU A  43      71.219  70.648  78.051  1.00 51.52           C  
ANISOU  317  CB  GLU A  43     7837   4597   7141   -183    508   -956       C  
ATOM    318  CG  GLU A  43      71.706  71.743  77.125  1.00 57.26           C  
ANISOU  318  CG  GLU A  43     8650   5168   7937   -247    514   -894       C  
ATOM    319  CD  GLU A  43      71.591  71.359  75.666  1.00 62.92           C  
ANISOU  319  CD  GLU A  43     9363   5867   8677   -215    492   -722       C  
ATOM    320  OE1 GLU A  43      70.819  70.426  75.355  1.00 64.19           O  
ANISOU  320  OE1 GLU A  43     9462   6106   8822   -101    470   -647       O  
ATOM    321  OE2 GLU A  43      72.274  71.989  74.830  1.00 66.62           O1-
ANISOU  321  OE2 GLU A  43     9890   6251   9173   -310    500   -663       O1-
ATOM    322  N   THR A  44      72.585  72.898  80.205  1.00 50.83           N  
ANISOU  322  N   THR A  44     7870   4405   7037   -419    557  -1289       N  
ATOM    323  CA  THR A  44      73.828  73.410  80.774  1.00 50.34           C  
ANISOU  323  CA  THR A  44     7818   4365   6946   -598    557  -1398       C  
ATOM    324  C   THR A  44      74.044  72.917  82.197  1.00 48.94           C  
ANISOU  324  C   THR A  44     7585   4350   6660   -646    540  -1540       C  
ATOM    325  O   THR A  44      75.184  72.921  82.678  1.00 48.09           O  
ANISOU  325  O   THR A  44     7441   4328   6502   -798    512  -1618       O  
ATOM    326  CB  THR A  44      73.846  74.944  80.746  1.00 56.52           C  
ANISOU  326  CB  THR A  44     8712   4954   7809   -620    598  -1443       C  
ATOM    327  OG1 THR A  44      72.894  75.462  81.685  1.00 59.16           O  
ANISOU  327  OG1 THR A  44     9087   5241   8149   -517    625  -1545       O  
ATOM    328  CG2 THR A  44      73.515  75.461  79.350  1.00 55.50           C  
ANISOU  328  CG2 THR A  44     8649   4662   7778   -560    606  -1291       C  
ATOM    329  N   ILE A  45      72.969  72.503  82.876  1.00 44.78           N  
ANISOU  329  N   ILE A  45     7046   3876   6092   -519    552  -1573       N  
ATOM    330  CA  ILE A  45      73.077  71.864  84.187  1.00 44.80           C  
ANISOU  330  CA  ILE A  45     6998   4057   5968   -558    532  -1688       C  
ATOM    331  C   ILE A  45      74.118  70.752  84.161  1.00 40.07           C  
ANISOU  331  C   ILE A  45     6302   3631   5290   -670    462  -1665       C  
ATOM    332  O   ILE A  45      74.886  70.573  85.113  1.00 45.39           O  
ANISOU  332  O   ILE A  45     6939   4439   5870   -781    417  -1764       O  
ATOM    333  CB  ILE A  45      71.696  71.335  84.624  1.00 50.24           C  
ANISOU  333  CB  ILE A  45     7672   4792   6624   -395    563  -1686       C  
ATOM    334  CG1 ILE A  45      70.753  72.494  84.964  1.00 53.42           C  
ANISOU  334  CG1 ILE A  45     8152   5052   7094   -297    624  -1752       C  
ATOM    335  CG2 ILE A  45      71.820  70.366  85.792  1.00 53.91           C  
ANISOU  335  CG2 ILE A  45     8078   5471   6936   -438    535  -1763       C  
ATOM    336  N   LEU A  46      74.170  69.998  83.063  1.00 38.57           N  
ANISOU  336  N   LEU A  46     6065   3446   5142   -642    445  -1533       N  
ATOM    337  CA  LEU A  46      75.011  68.806  83.017  1.00 39.49           C  
ANISOU  337  CA  LEU A  46     6075   3733   5197   -724    376  -1508       C  
ATOM    338  C   LEU A  46      76.497  69.144  83.095  1.00 46.65           C  
ANISOU  338  C   LEU A  46     6938   4686   6100   -899    329  -1562       C  
ATOM    339  O   LEU A  46      77.289  68.321  83.569  1.00 48.86           O  
ANISOU  339  O   LEU A  46     7117   5140   6307   -978    251  -1593       O  
ATOM    340  CB  LEU A  46      74.697  68.008  81.752  1.00 37.44           C  
ANISOU  340  CB  LEU A  46     5778   3451   4995   -654    379  -1359       C  
ATOM    341  CG  LEU A  46      73.227  67.604  81.627  1.00 37.61           C  
ANISOU  341  CG  LEU A  46     5822   3441   5025   -472    421  -1298       C  
ATOM    342  CD1 LEU A  46      72.955  66.890  80.306  1.00 36.56           C  
ANISOU  342  CD1 LEU A  46     5643   3298   4950   -398    412  -1131       C  
ATOM    343  CD2 LEU A  46      72.829  66.731  82.801  1.00 32.85           C  
ANISOU  343  CD2 LEU A  46     5161   3019   4302   -433    394  -1354       C  
ATOM    344  N   ASN A  47      76.892  70.346  82.664  1.00 44.59           N  
ANISOU  344  N   ASN A  47     6745   4278   5918   -957    370  -1572       N  
ATOM    345  CA  ASN A  47      78.296  70.738  82.724  1.00 43.64           C  
ANISOU  345  CA  ASN A  47     6579   4200   5802  -1123    338  -1627       C  
ATOM    346  C   ASN A  47      78.771  70.988  84.147  1.00 47.79           C  
ANISOU  346  C   ASN A  47     7089   4831   6237  -1202    296  -1779       C  
ATOM    347  O   ASN A  47      79.981  70.965  84.397  1.00 47.12           O  
ANISOU  347  O   ASN A  47     6926   4845   6133  -1331    241  -1830       O  
ATOM    348  CB  ASN A  47      78.537  71.995  81.881  1.00 43.47           C  
ANISOU  348  CB  ASN A  47     6647   3987   5884  -1167    404  -1597       C  
ATOM    349  CG  ASN A  47      78.277  71.763  80.405  1.00 46.82           C  
ANISOU  349  CG  ASN A  47     7083   4325   6380  -1115    432  -1438       C  
ATOM    350  OD1 ASN A  47      78.511  70.669  79.885  1.00 44.21           O  
ANISOU  350  OD1 ASN A  47     6659   4105   6035  -1112    397  -1364       O  
ATOM    351  ND2 ASN A  47      77.791  72.793  79.720  1.00 49.09           N  
ANISOU  351  ND2 ASN A  47     7487   4420   6745  -1073    491  -1384       N  
ATOM    352  N   ASN A  48      77.852  71.225  85.081  1.00 45.74           N  
ANISOU  352  N   ASN A  48     6897   4563   5922  -1125    321  -1851       N  
ATOM    353  CA  ASN A  48      78.202  71.579  86.448  1.00 48.34           C  
ANISOU  353  CA  ASN A  48     7231   4982   6155  -1198    291  -1996       C  
ATOM    354  C   ASN A  48      77.955  70.436  87.421  1.00 45.35           C  
ANISOU  354  C   ASN A  48     6790   4809   5631  -1165    221  -2019       C  
ATOM    355  O   ASN A  48      78.028  70.637  88.638  1.00 49.39           O  
ANISOU  355  O   ASN A  48     7319   5410   6038  -1206    197  -2130       O  
ATOM    356  CB  ASN A  48      77.431  72.831  86.866  1.00 56.10           C  
ANISOU  356  CB  ASN A  48     8340   5802   7173  -1153    378  -2077       C  
ATOM    357  CG  ASN A  48      77.770  74.028  85.998  1.00 61.85           C  
ANISOU  357  CG  ASN A  48     9139   6329   8034  -1199    436  -2058       C  
ATOM    358  OD1 ASN A  48      78.941  74.364  85.817  1.00 62.65           O  
ANISOU  358  OD1 ASN A  48     9207   6443   8156  -1338    413  -2084       O  
ATOM    359  ND2 ASN A  48      76.749  74.660  85.433  1.00 65.21           N  
ANISOU  359  ND2 ASN A  48     9658   6569   8550  -1080    508  -2007       N  
ATOM    360  N   ILE A  49      77.665  69.245  86.913  1.00 41.97           N  
ANISOU  360  N   ILE A  49     6296   4462   5190  -1097    188  -1914       N  
ATOM    361  CA  ILE A  49      77.602  68.033  87.718  1.00 41.36           C  
ANISOU  361  CA  ILE A  49     6150   4593   4973  -1081    106  -1913       C  
ATOM    362  C   ILE A  49      78.925  67.309  87.514  1.00 36.71           C  
ANISOU  362  C   ILE A  49     5428   4146   4376  -1179    -10  -1881       C  
ATOM    363  O   ILE A  49      79.204  66.812  86.419  1.00 39.10           O  
ANISOU  363  O   ILE A  49     5664   4426   4767  -1172    -16  -1785       O  
ATOM    364  CB  ILE A  49      76.405  67.156  87.324  1.00 42.72           C  
ANISOU  364  CB  ILE A  49     6329   4766   5138   -939    146  -1823       C  
ATOM    365  CG1 ILE A  49      75.103  67.958  87.449  1.00 38.32           C  
ANISOU  365  CG1 ILE A  49     5883   4061   4617   -826    262  -1852       C  
ATOM    366  CG2 ILE A  49      76.359  65.897  88.177  1.00 39.77           C  
ANISOU  366  CG2 ILE A  49     5891   4614   4607   -930     60  -1814       C  
ATOM    367  CD1 ILE A  49      73.894  67.248  86.893  1.00 37.40           C  
ANISOU  367  CD1 ILE A  49     5766   3918   4526   -675    315  -1758       C  
ATOM    368  N   ILE A  50      79.754  67.263  88.561  1.00 40.68           N  
ANISOU  368  N   ILE A  50     5883   4795   4777  -1267   -105  -1959       N  
ATOM    369  CA  ILE A  50      81.110  66.739  88.402  1.00 44.15           C  
ANISOU  369  CA  ILE A  50     6183   5360   5232  -1355   -221  -1938       C  
ATOM    370  C   ILE A  50      81.091  65.269  88.006  1.00 42.66           C  
ANISOU  370  C   ILE A  50     5884   5298   5026  -1292   -300  -1823       C  
ATOM    371  O   ILE A  50      82.016  64.784  87.343  1.00 41.04           O  
ANISOU  371  O   ILE A  50     5553   5142   4896  -1328   -360  -1769       O  
ATOM    372  CB  ILE A  50      81.935  66.968  89.687  1.00 45.60           C  
ANISOU  372  CB  ILE A  50     6341   5680   5305  -1446   -318  -2041       C  
ATOM    373  CG1 ILE A  50      81.403  66.109  90.832  1.00 46.43           C  
ANISOU  373  CG1 ILE A  50     6457   5952   5233  -1390   -395  -2036       C  
ATOM    374  CG2 ILE A  50      81.918  68.440  90.076  1.00 50.28           C  
ANISOU  374  CG2 ILE A  50     7042   6141   5919  -1512   -232  -2164       C  
ATOM    375  CD1 ILE A  50      82.269  66.148  92.077  1.00 57.50           C  
ANISOU  375  CD1 ILE A  50     7826   7509   6512  -1472   -516  -2113       C  
ATOM    376  N   GLN A  51      80.037  64.539  88.379  1.00 37.75           N  
ANISOU  376  N   GLN A  51     5302   4730   4310  -1194   -295  -1785       N  
ATOM    377  CA  GLN A  51      79.938  63.131  88.010  1.00 38.15           C  
ANISOU  377  CA  GLN A  51     5252   4899   4342  -1131   -367  -1674       C  
ATOM    378  C   GLN A  51      79.644  62.924  86.531  1.00 34.42           C  
ANISOU  378  C   GLN A  51     4749   4302   4028  -1057   -291  -1550       C  
ATOM    379  O   GLN A  51      79.644  61.775  86.078  1.00 31.39           O  
ANISOU  379  O   GLN A  51     4264   3996   3667   -972   -344  -1411       O  
ATOM    380  CB  GLN A  51      78.856  62.435  88.842  1.00 42.22           C  
ANISOU  380  CB  GLN A  51     5822   5501   4717  -1020   -369  -1619       C  
ATOM    381  CG  GLN A  51      79.221  62.247  90.309  1.00 39.87           C  
ANISOU  381  CG  GLN A  51     5537   5379   4232  -1082   -476  -1694       C  
ATOM    382  CD  GLN A  51      79.101  63.526  91.103  1.00 43.35           C  
ANISOU  382  CD  GLN A  51     6092   5746   4635  -1136   -408  -1826       C  
ATOM    383  OE1 GLN A  51      78.482  64.491  90.655  1.00 38.23           O  
ANISOU  383  OE1 GLN A  51     5531   4920   4077  -1119   -272  -1877       O  
ATOM    384  NE2 GLN A  51      79.706  63.547  92.285  1.00 46.14           N  
ANISOU  384  NE2 GLN A  51     6440   6232   4859  -1196   -507  -1878       N  
ATOM    385  N   VAL A  52      79.392  63.988  85.775  1.00 32.16           N  
ANISOU  385  N   VAL A  52     4552   3821   3847  -1084   -172  -1591       N  
ATOM    386  CA  VAL A  52      79.133  63.893  84.341  1.00 31.10           C  
ANISOU  386  CA  VAL A  52     4404   3565   3847  -1024   -102  -1469       C  
ATOM    387  C   VAL A  52      80.424  64.197  83.592  1.00 34.96           C  
ANISOU  387  C   VAL A  52     4816   4032   4434  -1160   -117  -1499       C  
ATOM    388  O   VAL A  52      81.001  65.282  83.741  1.00 36.88           O  
ANISOU  388  O   VAL A  52     5103   4205   4703  -1242    -90  -1565       O  
ATOM    389  CB  VAL A  52      78.008  64.847  83.912  1.00 33.68           C  
ANISOU  389  CB  VAL A  52     4883   3686   4228   -956     31  -1471       C  
ATOM    390  CG1 VAL A  52      77.850  64.838  82.398  1.00 31.36           C  
ANISOU  390  CG1 VAL A  52     4585   3269   4060   -913     90  -1347       C  
ATOM    391  CG2 VAL A  52      76.700  64.480  84.610  1.00 33.61           C  
ANISOU  391  CG2 VAL A  52     4925   3712   4134   -814     55  -1444       C  
ATOM    392  N   ALA A  53      80.879  63.241  82.781  1.00 33.17           N  
ANISOU  392  N   ALA A  53     4460   3877   4268  -1137   -158  -1395       N  
ATOM    393  CA  ALA A  53      82.074  63.402  81.961  1.00 34.21           C  
ANISOU  393  CA  ALA A  53     4497   4002   4497  -1237   -159  -1390       C  
ATOM    394  C   ALA A  53      81.752  63.769  80.521  1.00 36.84           C  
ANISOU  394  C   ALA A  53     4888   4177   4933  -1225    -45  -1304       C  
ATOM    395  O   ALA A  53      82.484  64.549  79.902  1.00 38.16           O  
ANISOU  395  O   ALA A  53     5065   4273   5162  -1305      4  -1305       O  
ATOM    396  CB  ALA A  53      82.899  62.112  81.978  1.00 33.02           C  
ANISOU  396  CB  ALA A  53     4155   4036   4354  -1228   -275  -1348       C  
ATOM    397  N   TRP A  54      80.676  63.206  79.979  1.00 30.67           N  
ANISOU  397  N   TRP A  54     4142   3354   4158  -1101     -8  -1200       N  
ATOM    398  CA  TRP A  54      80.192  63.481  78.633  1.00 32.16           C  
ANISOU  398  CA  TRP A  54     4397   3399   4423  -1069     88  -1101       C  
ATOM    399  C   TRP A  54      78.673  63.488  78.670  1.00 27.61           C  
ANISOU  399  C   TRP A  54     3927   2749   3816   -903    127  -1021       C  
ATOM    400  O   TRP A  54      78.060  62.791  79.478  1.00 24.50           O  
ANISOU  400  O   TRP A  54     3501   2457   3349   -800     77  -1004       O  
ATOM    401  CB  TRP A  54      80.609  62.422  77.589  1.00 34.63           C  
ANISOU  401  CB  TRP A  54     4577   3793   4789  -1054     74   -998       C  
ATOM    402  CG  TRP A  54      82.072  62.231  77.351  1.00 47.22           C  
ANISOU  402  CG  TRP A  54     6033   5478   6430  -1181     41  -1049       C  
ATOM    403  CD1 TRP A  54      82.973  61.644  78.193  1.00 52.41           C  
ANISOU  403  CD1 TRP A  54     6549   6298   7066  -1208    -66  -1108       C  
ATOM    404  CD2 TRP A  54      82.801  62.586  76.167  1.00 41.06           C  
ANISOU  404  CD2 TRP A  54     5237   4655   5709  -1244    106  -1000       C  
ATOM    405  NE1 TRP A  54      84.221  61.628  77.614  1.00 51.15           N  
ANISOU  405  NE1 TRP A  54     6284   6188   6963  -1275    -65  -1103       N  
ATOM    406  CE2 TRP A  54      84.143  62.203  76.373  1.00 45.03           C  
ANISOU  406  CE2 TRP A  54     5583   5293   6232  -1305     46  -1045       C  
ATOM    407  CE3 TRP A  54      82.453  63.203  74.961  1.00 41.42           C  
ANISOU  407  CE3 TRP A  54     5389   4564   5782  -1250    205   -920       C  
ATOM    408  CZ2 TRP A  54      85.137  62.415  75.417  1.00 45.19           C  
ANISOU  408  CZ2 TRP A  54     5552   5317   6303  -1376     97  -1028       C  
ATOM    409  CZ3 TRP A  54      83.444  63.410  74.010  1.00 41.16           C  
ANISOU  409  CZ3 TRP A  54     5308   4545   5784  -1330    249   -898       C  
ATOM    410  CH2 TRP A  54      84.767  63.018  74.246  1.00 44.61           C  
ANISOU  410  CH2 TRP A  54     5589   5117   6243  -1393    202   -959       C  
ATOM    411  N   TRP A  55      78.067  64.246  77.766  1.00 26.66           N  
ANISOU  411  N   TRP A  55     3926   2454   3750   -877    213   -967       N  
ATOM    412  CA  TRP A  55      76.626  64.141  77.601  1.00 24.54           C  
ANISOU  412  CA  TRP A  55     3727   2127   3472   -706    242   -879       C  
ATOM    413  C   TRP A  55      76.257  64.479  76.169  1.00 28.66           C  
ANISOU  413  C   TRP A  55     4317   2512   4059   -681    303   -768       C  
ATOM    414  O   TRP A  55      76.924  65.282  75.509  1.00 29.84           O  
ANISOU  414  O   TRP A  55     4533   2548   4257   -800    350   -783       O  
ATOM    415  CB  TRP A  55      75.874  65.049  78.581  1.00 23.19           C  
ANISOU  415  CB  TRP A  55     3675   1864   3271   -662    275   -972       C  
ATOM    416  CG  TRP A  55      76.205  66.492  78.458  1.00 28.35           C  
ANISOU  416  CG  TRP A  55     4466   2326   3980   -763    342  -1057       C  
ATOM    417  CD1 TRP A  55      77.159  67.181  79.153  1.00 30.20           C  
ANISOU  417  CD1 TRP A  55     4695   2584   4195   -888    322  -1167       C  
ATOM    418  CD2 TRP A  55      75.568  67.444  77.598  1.00 33.09           C  
ANISOU  418  CD2 TRP A  55     5181   2747   4646   -696    398   -975       C  
ATOM    419  NE1 TRP A  55      77.158  68.503  78.773  1.00 34.50           N  
ANISOU  419  NE1 TRP A  55     5346   2967   4794   -907    375  -1161       N  
ATOM    420  CE2 TRP A  55      76.191  68.688  77.818  1.00 37.88           C  
ANISOU  420  CE2 TRP A  55     5850   3269   5275   -790    416  -1041       C  
ATOM    421  CE3 TRP A  55      74.533  67.362  76.660  1.00 38.21           C  
ANISOU  421  CE3 TRP A  55     5876   3307   5333   -561    423   -845       C  
ATOM    422  CZ2 TRP A  55      75.814  69.843  77.135  1.00 42.93           C  
ANISOU  422  CZ2 TRP A  55     6604   3731   5978   -756    461   -984       C  
ATOM    423  CZ3 TRP A  55      74.161  68.508  75.982  1.00 42.60           C  
ANISOU  423  CZ3 TRP A  55     6537   3702   5945   -523    452   -785       C  
ATOM    424  CH2 TRP A  55      74.797  69.732  76.225  1.00 42.15           C  
ANISOU  424  CH2 TRP A  55     6547   3554   5913   -622    472   -854       C  
ATOM    425  N   GLU A  56      75.175  63.863  75.704  1.00 23.68           N  
ANISOU  425  N   GLU A  56     3674   1900   3424   -530    301   -656       N  
ATOM    426  CA  GLU A  56      74.727  64.019  74.331  1.00 27.76           C  
ANISOU  426  CA  GLU A  56     4247   2318   3984   -490    338   -535       C  
ATOM    427  C   GLU A  56      73.222  63.814  74.318  1.00 25.42           C  
ANISOU  427  C   GLU A  56     3974   2002   3681   -303    337   -465       C  
ATOM    428  O   GLU A  56      72.726  62.863  74.931  1.00 25.33           O  
ANISOU  428  O   GLU A  56     3868   2127   3629   -218    301   -462       O  
ATOM    429  CB  GLU A  56      75.435  63.001  73.425  1.00 35.66           C  
ANISOU  429  CB  GLU A  56     5126   3435   4988   -546    320   -466       C  
ATOM    430  CG  GLU A  56      75.186  63.151  71.941  1.00 48.46           C  
ANISOU  430  CG  GLU A  56     6807   4973   6633   -543    360   -350       C  
ATOM    431  CD  GLU A  56      75.884  62.070  71.132  1.00 57.69           C  
ANISOU  431  CD  GLU A  56     7846   6273   7801   -603    352   -306       C  
ATOM    432  OE1 GLU A  56      76.365  61.087  71.738  1.00 56.95           O  
ANISOU  432  OE1 GLU A  56     7609   6331   7700   -607    305   -349       O  
ATOM    433  OE2 GLU A  56      75.954  62.202  69.891  1.00 59.94           O1-
ANISOU  433  OE2 GLU A  56     8176   6506   8092   -645    392   -228       O1-
ATOM    434  N   GLU A  57      72.500  64.707  73.646  1.00 24.26           N  
ANISOU  434  N   GLU A  57     3953   1686   3577   -240    374   -410       N  
ATOM    435  CA  GLU A  57      71.070  64.494  73.472  1.00 21.12           C  
ANISOU  435  CA  GLU A  57     3558   1277   3187    -58    366   -339       C  
ATOM    436  C   GLU A  57      70.830  63.239  72.638  1.00 22.22           C  
ANISOU  436  C   GLU A  57     3584   1555   3303    -13    331   -229       C  
ATOM    437  O   GLU A  57      71.549  62.973  71.668  1.00 23.44           O  
ANISOU  437  O   GLU A  57     3722   1727   3457   -103    332   -170       O  
ATOM    438  CB  GLU A  57      70.418  65.701  72.795  1.00 26.95           C  
ANISOU  438  CB  GLU A  57     4449   1806   3986      6    394   -288       C  
ATOM    439  CG  GLU A  57      68.898  65.642  72.818  1.00 35.35           C  
ANISOU  439  CG  GLU A  57     5487   2876   5068    203    371   -243       C  
ATOM    440  CD  GLU A  57      68.236  66.926  72.368  1.00 46.55           C  
ANISOU  440  CD  GLU A  57     6984   4159   6542    272    351   -203       C  
ATOM    441  OE1 GLU A  57      68.934  67.952  72.236  1.00 49.41           O  
ANISOU  441  OE1 GLU A  57     7440   4406   6928    175    368   -223       O  
ATOM    442  OE2 GLU A  57      67.007  66.905  72.143  1.00 53.29           O1-
ANISOU  442  OE2 GLU A  57     7799   5025   7424    422    317   -155       O1-
ATOM    443  N   SER A  58      69.808  62.471  73.026  1.00 18.88           N  
ANISOU  443  N   SER A  58     3082   1229   2862    118    310   -212       N  
ATOM    444  CA  SER A  58      69.438  61.253  72.318  1.00 17.70           C  
ANISOU  444  CA  SER A  58     2823   1206   2694    168    281   -120       C  
ATOM    445  C   SER A  58      68.827  61.599  70.965  1.00 19.80           C  
ANISOU  445  C   SER A  58     3151   1386   2986    225    279     -9       C  
ATOM    446  O   SER A  58      67.904  62.409  70.883  1.00 25.16           O  
ANISOU  446  O   SER A  58     3911   1949   3699    332    283      9       O  
ATOM    447  CB  SER A  58      68.445  60.450  73.164  1.00 19.85           C  
ANISOU  447  CB  SER A  58     3009   1591   2943    283    271   -140       C  
ATOM    448  OG  SER A  58      67.945  59.312  72.476  1.00 19.93           O  
ANISOU  448  OG  SER A  58     2919   1708   2944    336    249    -57       O  
ATOM    449  N   GLU A  59      69.316  60.953  69.913  1.00 18.75           N  
ANISOU  449  N   GLU A  59     2974   1315   2834    161    269     63       N  
ATOM    450  CA AGLU A  59      68.928  61.246  68.540  0.60 19.90           C  
ANISOU  450  CA AGLU A  59     3187   1395   2979    183    262    174       C  
ATOM    451  CA BGLU A  59      68.914  61.259  68.551  0.40 19.97           C  
ANISOU  451  CA BGLU A  59     3197   1403   2988    185    262    174       C  
ATOM    452  C   GLU A  59      67.952  60.210  68.007  1.00 18.26           C  
ANISOU  452  C   GLU A  59     2880   1306   2753    288    227    241       C  
ATOM    453  O   GLU A  59      67.840  59.106  68.551  1.00 16.75           O  
ANISOU  453  O   GLU A  59     2561   1254   2551    307    219    207       O  
ATOM    454  CB AGLU A  59      70.172  61.291  67.644  0.60 21.22           C  
ANISOU  454  CB AGLU A  59     3383   1553   3126     17    289    199       C  
ATOM    455  CB BGLU A  59      70.147  61.335  67.647  0.40 20.92           C  
ANISOU  455  CB BGLU A  59     3350   1509   3089     20    289    200       C  
ATOM    456  CG AGLU A  59      71.097  62.443  67.974  0.60 20.12           C  
ANISOU  456  CG AGLU A  59     3356   1279   3010   -101    330    139       C  
ATOM    457  CG BGLU A  59      70.749  59.990  67.404  0.40 17.50           C  
ANISOU  457  CG BGLU A  59     2771   1246   2632    -44    287    191       C  
ATOM    458  N   PRO A  60      67.231  60.529  66.928  1.00 18.63           N  
ANISOU  458  N   PRO A  60     2985   1300   2793    353    200    339       N  
ATOM    459  CA  PRO A  60      66.281  59.561  66.362  1.00 17.55           C  
ANISOU  459  CA  PRO A  60     2748   1283   2636    443    162    395       C  
ATOM    460  C   PRO A  60      66.955  58.353  65.733  1.00 16.73           C  
ANISOU  460  C   PRO A  60     2547   1318   2491    342    172    407       C  
ATOM    461  O   PRO A  60      68.077  58.424  65.218  1.00 18.43           O  
ANISOU  461  O   PRO A  60     2796   1521   2685    205    202    409       O  
ATOM    462  CB  PRO A  60      65.536  60.378  65.301  1.00 21.23           C  
ANISOU  462  CB  PRO A  60     3304   1670   3092    503    109    487       C  
ATOM    463  CG  PRO A  60      65.645  61.782  65.775  1.00 22.90           C  
ANISOU  463  CG  PRO A  60     3626   1730   3346    503    112    455       C  
ATOM    464  CD  PRO A  60      67.019  61.877  66.371  1.00 17.63           C  
ANISOU  464  CD  PRO A  60     3009   1009   2681    370    187    393       C  
ATOM    465  N   MET A  61      66.241  57.231  65.779  1.00 14.57           N  
ANISOU  465  N   MET A  61     2148   1175   2213    408    153    406       N  
ATOM    466  CA  MET A  61      66.588  56.021  65.043  1.00 13.95           C  
ANISOU  466  CA  MET A  61     1974   1223   2104    340    159    421       C  
ATOM    467  C   MET A  61      65.396  55.641  64.178  1.00 14.69           C  
ANISOU  467  C   MET A  61     2034   1372   2174    430    116    485       C  
ATOM    468  O   MET A  61      64.256  55.987  64.497  1.00 17.26           O  
ANISOU  468  O   MET A  61     2357   1677   2523    560     83    496       O  
ATOM    469  CB  MET A  61      66.942  54.867  65.976  1.00 16.93           C  
ANISOU  469  CB  MET A  61     2222   1706   2502    320    178    350       C  
ATOM    470  CG  MET A  61      68.117  55.181  66.878  1.00 14.10           C  
ANISOU  470  CG  MET A  61     1882   1314   2163    236    202    283       C  
ATOM    471  SD  MET A  61      68.556  53.797  67.957  1.00 17.25           S  
ANISOU  471  SD  MET A  61     2138   1835   2580    222    203    221       S  
ATOM    472  CE  MET A  61      69.375  52.677  66.819  1.00 17.65           C  
ANISOU  472  CE  MET A  61     2101   1968   2638    127    221    235       C  
ATOM    473  N   SER A  62      65.654  54.963  63.055  1.00 13.57           N  
ANISOU  473  N   SER A  62     1863   1306   1986    358    118    520       N  
ATOM    474  CA  SER A  62      64.543  54.560  62.198  1.00 12.63           C  
ANISOU  474  CA  SER A  62     1707   1258   1835    431     69    574       C  
ATOM    475  C   SER A  62      64.801  53.162  61.655  1.00 12.90           C  
ANISOU  475  C   SER A  62     1626   1428   1846    357     94    546       C  
ATOM    476  O   SER A  62      65.906  52.629  61.736  1.00 13.43           O  
ANISOU  476  O   SER A  62     1661   1520   1923    249    147    500       O  
ATOM    477  CB  SER A  62      64.297  55.568  61.065  1.00 15.81           C  
ANISOU  477  CB  SER A  62     2245   1582   2181    439     23    672       C  
ATOM    478  OG  SER A  62      65.383  55.582  60.149  1.00 17.09           O  
ANISOU  478  OG  SER A  62     2472   1741   2281    288     62    695       O  
ATOM    479  N   SER A  63      63.744  52.581  61.082  1.00 15.82           N  
ANISOU  479  N   SER A  63     1931   1885   2195    419     54    568       N  
ATOM    480  CA  SER A  63      63.805  51.214  60.580  1.00 13.32           C  
ANISOU  480  CA  SER A  63     1503   1694   1865    357     78    532       C  
ATOM    481  C   SER A  63      64.779  51.077  59.412  1.00 13.80           C  
ANISOU  481  C   SER A  63     1609   1773   1860    219    111    544       C  
ATOM    482  O   SER A  63      64.890  51.960  58.553  1.00 15.55           O  
ANISOU  482  O   SER A  63     1950   1945   2011    188     88    612       O  
ATOM    483  CB  SER A  63      62.409  50.779  60.120  1.00 17.50           C  
ANISOU  483  CB  SER A  63     1961   2310   2377    445     22    550       C  
ATOM    484  OG  SER A  63      62.415  49.438  59.658  1.00 16.13           O  
ANISOU  484  OG  SER A  63     1681   2251   2195    380     52    504       O  
ATOM    485  N   LEU A  64      65.471  49.940  59.377  1.00 13.01           N  
ANISOU  485  N   LEU A  64     1416   1744   1784    134    170    477       N  
ATOM    486  CA  LEU A  64      66.253  49.532  58.218  1.00 13.08           C  
ANISOU  486  CA  LEU A  64     1433   1799   1736      3    215    463       C  
ATOM    487  C   LEU A  64      65.476  48.580  57.329  1.00 13.21           C  
ANISOU  487  C   LEU A  64     1379   1932   1709     -1    201    451       C  
ATOM    488  O   LEU A  64      66.072  47.896  56.498  1.00 13.59           O  
ANISOU  488  O   LEU A  64     1398   2040   1725   -110    254    408       O  
ATOM    489  CB  LEU A  64      67.563  48.880  58.670  1.00 14.15           C  
ANISOU  489  CB  LEU A  64     1500   1936   1941    -86    292    381       C  
ATOM    490  CG  LEU A  64      68.445  49.729  59.595  1.00 13.01           C  
ANISOU  490  CG  LEU A  64     1407   1694   1843    -99    305    373       C  
ATOM    491  CD1 LEU A  64      69.752  48.992  59.933  1.00 13.69           C  
ANISOU  491  CD1 LEU A  64     1402   1800   2001   -185    368    289       C  
ATOM    492  CD2 LEU A  64      68.758  51.063  58.941  1.00 17.28           C  
ANISOU  492  CD2 LEU A  64     2098   2154   2313   -155    304    434       C  
ATOM    493  N   ILE A  65      64.151  48.549  57.459  1.00 15.09           N  
ANISOU  493  N   ILE A  65     1585   2206   1945    111    133    480       N  
ATOM    494  CA  ILE A  65      63.307  47.679  56.646  1.00 15.51           C  
ANISOU  494  CA  ILE A  65     1562   2375   1955    107    109    462       C  
ATOM    495  C   ILE A  65      62.187  48.491  56.009  1.00 15.08           C  
ANISOU  495  C   ILE A  65     1569   2337   1824    189      6    545       C  
ATOM    496  O   ILE A  65      61.552  49.325  56.667  1.00 18.80           O  
ANISOU  496  O   ILE A  65     2070   2744   2331    308    -48    591       O  
ATOM    497  CB  ILE A  65      62.733  46.532  57.491  1.00 16.75           C  
ANISOU  497  CB  ILE A  65     1577   2583   2203    156    130    392       C  
ATOM    498  CG1 ILE A  65      63.876  45.675  58.021  1.00 18.32           C  
ANISOU  498  CG1 ILE A  65     1726   2759   2476     81    216    319       C  
ATOM    499  CG2 ILE A  65      61.756  45.674  56.671  1.00 19.80           C  
ANISOU  499  CG2 ILE A  65     1881   3091   2551    149    104    364       C  
ATOM    500  CD1 ILE A  65      63.387  44.579  58.914  1.00 20.22           C  
ANISOU  500  CD1 ILE A  65     1990   2932   2761     96    192    200       C  
ATOM    501  N   GLU A  66      61.934  48.235  54.725  1.00 16.48           N  
ANISOU  501  N   GLU A  66     1761   2604   1896    127    -23    561       N  
ATOM    502  CA  GLU A  66      60.789  48.778  54.011  1.00 18.28           C  
ANISOU  502  CA  GLU A  66     2023   2879   2046    206   -139    637       C  
ATOM    503  C   GLU A  66      59.787  47.649  53.780  1.00 18.07           C  
ANISOU  503  C   GLU A  66     1848   2992   2027    223   -164    570       C  
ATOM    504  O   GLU A  66      60.156  46.584  53.284  1.00 19.63           O  
ANISOU  504  O   GLU A  66     1984   3270   2203    111   -101    492       O  
ATOM    505  CB  GLU A  66      61.231  49.393  52.673  1.00 20.66           C  
ANISOU  505  CB  GLU A  66     2468   3186   2195    113   -166    714       C  
ATOM    506  N   ILE A  67      58.530  47.861  54.152  1.00 17.48           N  
ANISOU  506  N   ILE A  67     1706   2943   1992    358   -248    587       N  
ATOM    507  CA  ILE A  67      57.505  46.857  53.870  1.00 19.09           C  
ANISOU  507  CA  ILE A  67     1765   3288   2201    366   -277    521       C  
ATOM    508  C   ILE A  67      57.005  47.057  52.444  1.00 20.59           C  
ANISOU  508  C   ILE A  67     1996   3580   2247    340   -380    571       C  
ATOM    509  O   ILE A  67      56.634  48.172  52.057  1.00 22.65           O  
ANISOU  509  O   ILE A  67     2353   3804   2449    421   -487    679       O  
ATOM    510  CB  ILE A  67      56.362  46.952  54.891  1.00 18.03           C  
ANISOU  510  CB  ILE A  67     1565   3105   2180    484   -295    475       C  
ATOM    511  CG1 ILE A  67      56.896  46.693  56.302  1.00 20.93           C  
ANISOU  511  CG1 ILE A  67     1941   3355   2658    470   -187    410       C  
ATOM    512  CG2 ILE A  67      55.221  45.983  54.554  1.00 19.39           C  
ANISOU  512  CG2 ILE A  67     1638   3365   2364    458   -308    383       C  
ATOM    513  CD1 ILE A  67      57.539  45.322  56.456  1.00 24.21           C  
ANISOU  513  CD1 ILE A  67     2309   3789   3101    354    -87    323       C  
ATOM    514  N   THR A  68      57.003  45.986  51.640  1.00 18.90           N  
ANISOU  514  N   THR A  68     1717   3491   1972    223   -352    495       N  
ATOM    515  CA  THR A  68      56.793  46.177  50.206  1.00 19.13           C  
ANISOU  515  CA  THR A  68     1814   3621   1832    162   -438    542       C  
ATOM    516  C   THR A  68      55.558  45.495  49.616  1.00 21.85           C  
ANISOU  516  C   THR A  68     2030   4135   2139    176   -527    489       C  
ATOM    517  O   THR A  68      55.277  45.703  48.428  1.00 24.43           O  
ANISOU  517  O   THR A  68     2413   4559   2311    135   -621    535       O  
ATOM    518  CB  THR A  68      58.050  45.751  49.417  1.00 21.34           C  
ANISOU  518  CB  THR A  68     2177   3912   2019    -20   -335    505       C  
ATOM    519  OG1 THR A  68      58.371  44.376  49.662  1.00 23.17           O  
ANISOU  519  OG1 THR A  68     2286   4189   2329   -111   -217    363       O  
ATOM    520  CG2 THR A  68      59.254  46.624  49.789  1.00 21.84           C  
ANISOU  520  CG2 THR A  68     2381   3822   2097    -43   -268    569       C  
ATOM    521  N   ASN A  69      54.800  44.705  50.389  1.00 22.28           N  
ANISOU  521  N   ASN A  69     1926   4217   2324    222   -495    393       N  
ATOM    522  CA  ASN A  69      53.503  44.173  49.945  1.00 21.18           C  
ANISOU  522  CA  ASN A  69     1706   4150   2191    233   -547    321       C  
ATOM    523  C   ASN A  69      53.589  43.450  48.600  1.00 20.47           C  
ANISOU  523  C   ASN A  69     1598   4229   1949     93   -570    275       C  
ATOM    524  O   ASN A  69      52.770  43.665  47.691  1.00 24.57           O  
ANISOU  524  O   ASN A  69     2130   4824   2382    107   -682    295       O  
ATOM    525  CB  ASN A  69      52.455  45.288  49.883  1.00 25.41           C  
ANISOU  525  CB  ASN A  69     2287   4626   2743    374   -679    397       C  
ATOM    526  CG  ASN A  69      52.247  45.943  51.223  1.00 32.74           C  
ANISOU  526  CG  ASN A  69     3229   5387   3825    490   -645    406       C  
ATOM    527  OD1 ASN A  69      51.553  45.399  52.077  1.00 31.78           O  
ANISOU  527  OD1 ASN A  69     3023   5225   3826    506   -587    318       O  
ATOM    528  ND2 ASN A  69      52.874  47.096  51.431  1.00 34.67           N  
ANISOU  528  ND2 ASN A  69     3595   5522   4055    550   -671    509       N  
ATOM    529  N   ASN A  70      54.576  42.566  48.478  1.00 22.92           N  
ANISOU  529  N   ASN A  70     1880   4590   2239    -49   -459    199       N  
ATOM    530  CA  ASN A  70      54.878  41.934  47.193  1.00 23.44           C  
ANISOU  530  CA  ASN A  70     1967   4783   2154   -211   -448    136       C  
ATOM    531  C   ASN A  70      55.079  40.431  47.356  1.00 23.42           C  
ANISOU  531  C   ASN A  70     1855   4802   2243   -325   -305    -31       C  
ATOM    532  O   ASN A  70      56.005  39.847  46.785  1.00 23.45           O  
ANISOU  532  O   ASN A  70     1894   4820   2196   -470   -205   -103       O  
ATOM    533  CB  ASN A  70      56.120  42.572  46.565  1.00 23.06           C  
ANISOU  533  CB  ASN A  70     2104   4671   1987   -297   -405    207       C  
ATOM    534  CG  ASN A  70      56.211  42.313  45.077  1.00 29.83           C  
ANISOU  534  CG  ASN A  70     3023   5672   2640   -443   -433    180       C  
ATOM    535  OD1 ASN A  70      55.219  41.975  44.434  1.00 29.31           O  
ANISOU  535  OD1 ASN A  70     2884   5757   2494   -449   -536    147       O  
ATOM    536  ND2 ASN A  70      57.413  42.457  44.523  1.00 30.73           N  
ANISOU  536  ND2 ASN A  70     3266   5746   2663   -569   -338    185       N  
ATOM    537  N   VAL A  71      54.226  39.780  48.146  1.00 25.03           N  
ANISOU  537  N   VAL A  71     2239   4768   2501   -337   -582     62       N  
ATOM    538  CA  VAL A  71      54.403  38.351  48.396  1.00 20.72           C  
ANISOU  538  CA  VAL A  71     1730   4210   1933   -441   -537    -69       C  
ATOM    539  C   VAL A  71      54.338  37.557  47.091  1.00 23.39           C  
ANISOU  539  C   VAL A  71     2132   4625   2129   -532   -579   -139       C  
ATOM    540  O   VAL A  71      55.097  36.601  46.896  1.00 25.52           O  
ANISOU  540  O   VAL A  71     2493   4877   2327   -590   -535   -243       O  
ATOM    541  CB  VAL A  71      53.359  37.851  49.413  1.00 23.53           C  
ANISOU  541  CB  VAL A  71     2011   4526   2402   -475   -521   -108       C  
ATOM    542  CG1 VAL A  71      53.382  36.335  49.492  1.00 26.43           C  
ANISOU  542  CG1 VAL A  71     2432   4867   2742   -605   -495   -235       C  
ATOM    543  CG2 VAL A  71      53.637  38.453  50.783  1.00 21.31           C  
ANISOU  543  CG2 VAL A  71     1699   4155   2243   -390   -455    -66       C  
ATOM    544  N   ASN A  72      53.450  37.948  46.174  1.00 23.42           N  
ANISOU  544  N   ASN A  72     2101   4710   2089   -536   -664    -92       N  
ATOM    545  CA  ASN A  72      53.271  37.187  44.940  1.00 25.86           C  
ANISOU  545  CA  ASN A  72     2473   5088   2263   -626   -711   -163       C  
ATOM    546  C   ASN A  72      54.532  37.131  44.082  1.00 31.99           C  
ANISOU  546  C   ASN A  72     3366   5891   2899   -619   -669   -183       C  
ATOM    547  O   ASN A  72      54.669  36.212  43.267  1.00 38.72           O  
ANISOU  547  O   ASN A  72     4304   6767   3639   -691   -671   -287       O  
ATOM    548  CB  ASN A  72      52.120  37.773  44.125  1.00 28.34           C  
ANISOU  548  CB  ASN A  72     2719   5490   2558   -620   -819    -91       C  
ATOM    549  N   ASN A  73      55.438  38.095  44.212  1.00 25.59           N  
ANISOU  549  N   ASN A  73     2562   5072   2088   -533   -630    -86       N  
ATOM    550  CA  ASN A  73      56.709  38.068  43.497  1.00 29.22           C  
ANISOU  550  CA  ASN A  73     3119   5562   2420   -523   -567    -95       C  
ATOM    551  C   ASN A  73      57.887  38.093  44.464  1.00 26.45           C  
ANISOU  551  C   ASN A  73     2786   5144   2120   -475   -469    -99       C  
ATOM    552  O   ASN A  73      58.977  38.545  44.119  1.00 27.80           O  
ANISOU  552  O   ASN A  73     3002   5328   2233   -434   -407    -44       O  
ATOM    553  CB  ASN A  73      56.796  39.226  42.508  1.00 32.73           C  
ANISOU  553  CB  ASN A  73     3567   6078   2791   -484   -612     44       C  
ATOM    554  CG  ASN A  73      55.606  39.265  41.560  1.00 48.13           C  
ANISOU  554  CG  ASN A  73     5497   8102   4690   -523   -722     56       C  
ATOM    555  OD1 ASN A  73      55.331  38.295  40.851  1.00 46.40           O  
ANISOU  555  OD1 ASN A  73     5328   7926   4376   -599   -740    -53       O  
ATOM    556  ND2 ASN A  73      54.884  40.381  41.560  1.00 56.97           N  
ANISOU  556  ND2 ASN A  73     6546   9225   5875   -467   -801    186       N  
ATOM    557  N   GLY A  74      57.672  37.616  45.686  1.00 20.45           N  
ANISOU  557  N   GLY A  74     2000   4263   1508   -471   -431   -151       N  
ATOM    558  CA  GLY A  74      58.713  37.626  46.687  1.00 20.30           C  
ANISOU  558  CA  GLY A  74     2009   4108   1595   -408   -323   -145       C  
ATOM    559  C   GLY A  74      59.564  36.370  46.684  1.00 22.56           C  
ANISOU  559  C   GLY A  74     2392   4328   1853   -424   -229   -278       C  
ATOM    560  O   GLY A  74      59.315  35.409  45.954  1.00 25.77           O  
ANISOU  560  O   GLY A  74     2859   4774   2159   -487   -243   -393       O  
ATOM    561  N   GLU A  75      60.583  36.407  47.530  1.00 18.96           N  
ANISOU  561  N   GLU A  75     1953   3766   1487   -360   -140   -261       N  
ATOM    562  CA  GLU A  75      61.569  35.351  47.700  1.00 18.82           C  
ANISOU  562  CA  GLU A  75     2015   3667   1470   -337    -45   -364       C  
ATOM    563  C   GLU A  75      61.408  34.775  49.097  1.00 17.85           C  
ANISOU  563  C   GLU A  75     1894   3391   1496   -335    -21   -396       C  
ATOM    564  O   GLU A  75      61.270  35.536  50.057  1.00 17.62           O  
ANISOU  564  O   GLU A  75     1805   3317   1573   -307    -30   -306       O  
ATOM    565  CB  GLU A  75      62.979  35.936  47.528  1.00 20.08           C  
ANISOU  565  CB  GLU A  75     2172   3851   1609   -263     35   -296       C  
ATOM    566  CG  GLU A  75      64.133  35.025  47.833  1.00 21.38           C  
ANISOU  566  CG  GLU A  75     2388   3938   1798   -206    137   -378       C  
ATOM    567  CD  GLU A  75      65.462  35.630  47.383  1.00 33.92           C  
ANISOU  567  CD  GLU A  75     3947   5607   3336   -148    212   -308       C  
ATOM    568  OE1 GLU A  75      65.483  36.358  46.362  1.00 38.28           O  
ANISOU  568  OE1 GLU A  75     4481   6297   3767   -171    197   -242       O  
ATOM    569  OE2 GLU A  75      66.486  35.389  48.053  1.00 39.95           O1-
ANISOU  569  OE2 GLU A  75     4699   6303   4178    -84    283   -308       O1-
ATOM    570  N   THR A  76      61.422  33.445  49.225  1.00 17.46           N  
ANISOU  570  N   THR A  76     1926   3257   1452   -364      7   -522       N  
ATOM    571  CA  THR A  76      61.295  32.887  50.577  1.00 16.69           C  
ANISOU  571  CA  THR A  76     1841   3011   1489   -369     28   -535       C  
ATOM    572  C   THR A  76      62.592  33.053  51.370  1.00 15.78           C  
ANISOU  572  C   THR A  76     1734   2813   1449   -271    104   -489       C  
ATOM    573  O   THR A  76      63.690  33.196  50.809  1.00 17.11           O  
ANISOU  573  O   THR A  76     1913   3022   1566   -203    156   -486       O  
ATOM    574  CB  THR A  76      60.932  31.400  50.544  1.00 17.64           C  
ANISOU  574  CB  THR A  76     2062   3038   1603   -438     26   -669       C  
ATOM    575  OG1 THR A  76      62.020  30.653  49.984  1.00 19.49           O  
ANISOU  575  OG1 THR A  76     2394   3230   1781   -373     91   -759       O  
ATOM    576  CG2 THR A  76      59.663  31.154  49.735  1.00 19.48           C  
ANISOU  576  CG2 THR A  76     2286   3360   1758   -557    -61   -722       C  
ATOM    577  N   ILE A  77      62.448  32.996  52.698  1.00 14.91           N  
ANISOU  577  N   ILE A  77     1614   2598   1455   -270    109   -454       N  
ATOM    578  CA  ILE A  77      63.603  33.040  53.591  1.00 14.19           C  
ANISOU  578  CA  ILE A  77     1532   2419   1438   -189    163   -413       C  
ATOM    579  C   ILE A  77      64.539  31.876  53.305  1.00 16.76           C  
ANISOU  579  C   ILE A  77     1944   2676   1748   -137    218   -505       C  
ATOM    580  O   ILE A  77      65.770  32.020  53.359  1.00 16.56           O  
ANISOU  580  O   ILE A  77     1904   2652   1736    -48    268   -479       O  
ATOM    581  CB  ILE A  77      63.134  33.026  55.054  1.00 13.40           C  
ANISOU  581  CB  ILE A  77     1426   2223   1443   -211    152   -373       C  
ATOM    582  CG1 ILE A  77      62.376  34.307  55.400  1.00 13.54           C  
ANISOU  582  CG1 ILE A  77     1355   2307   1482   -225    111   -285       C  
ATOM    583  CG2 ILE A  77      64.333  32.818  56.001  1.00 14.32           C  
ANISOU  583  CG2 ILE A  77     1572   2241   1629   -135    195   -343       C  
ATOM    584  CD1 ILE A  77      61.375  34.157  56.549  1.00 14.21           C  
ANISOU  584  CD1 ILE A  77     1426   2342   1633   -275    100   -276       C  
ATOM    585  N   THR A  78      63.972  30.694  53.043  1.00 16.58           N  
ANISOU  585  N   THR A  78     2009   2586   1704   -190    207   -614       N  
ATOM    586  CA  THR A  78      64.793  29.526  52.727  1.00 19.94           C  
ANISOU  586  CA  THR A  78     2537   2923   2116   -127    257   -719       C  
ATOM    587  C   THR A  78      65.672  29.776  51.507  1.00 18.81           C  
ANISOU  587  C   THR A  78     2380   2901   1867    -50    307   -753       C  
ATOM    588  O   THR A  78      66.847  29.393  51.491  1.00 19.12           O  
ANISOU  588  O   THR A  78     2434   2911   1918     61    375   -780       O  
ATOM    589  CB  THR A  78      63.901  28.304  52.502  1.00 21.55           C  
ANISOU  589  CB  THR A  78     2855   3032   2302   -220    222   -836       C  
ATOM    590  OG1 THR A  78      63.222  27.994  53.725  1.00 23.72           O  
ANISOU  590  OG1 THR A  78     3142   3195   2677   -293    191   -792       O  
ATOM    591  CG2 THR A  78      64.740  27.104  52.106  1.00 26.97           C  
ANISOU  591  CG2 THR A  78     3668   3608   2972   -139    270   -959       C  
ATOM    592  N   THR A  79      65.110  30.396  50.466  1.00 19.72           N  
ANISOU  592  N   THR A  79     2459   3162   1871   -107    277   -750       N  
ATOM    593  CA  THR A  79      65.893  30.748  49.282  1.00 21.55           C  
ANISOU  593  CA  THR A  79     2672   3535   1981    -50    329   -764       C  
ATOM    594  C   THR A  79      66.953  31.793  49.605  1.00 19.02           C  
ANISOU  594  C   THR A  79     2247   3282   1700     23    375   -635       C  
ATOM    595  O   THR A  79      68.102  31.688  49.143  1.00 21.83           O  
ANISOU  595  O   THR A  79     2586   3695   2013    111    457   -652       O  
ATOM    596  CB  THR A  79      64.956  31.265  48.185  1.00 25.16           C  
ANISOU  596  CB  THR A  79     3117   4136   2308   -141    268   -764       C  
ATOM    597  OG1 THR A  79      64.101  30.200  47.750  1.00 28.85           O  
ANISOU  597  OG1 THR A  79     3686   4552   2723   -217    224   -901       O  
ATOM    598  CG2 THR A  79      65.750  31.790  46.970  1.00 25.14           C  
ANISOU  598  CG2 THR A  79     3091   4302   2161    -94    323   -751       C  
ATOM    599  N   ALA A  80      66.581  32.822  50.362  1.00 17.85           N  
ANISOU  599  N   ALA A  80     2023   3133   1627    -15    325   -508       N  
ATOM    600  CA  ALA A  80      67.504  33.916  50.636  1.00 18.14           C  
ANISOU  600  CA  ALA A  80     1969   3227   1697     27    349   -381       C  
ATOM    601  C   ALA A  80      68.672  33.465  51.504  1.00 18.92           C  
ANISOU  601  C   ALA A  80     2055   3242   1891    115    404   -378       C  
ATOM    602  O   ALA A  80      69.809  33.912  51.309  1.00 22.45           O  
ANISOU  602  O   ALA A  80     2434   3767   2330    167    456   -322       O  
ATOM    603  CB  ALA A  80      66.754  35.064  51.305  1.00 18.62           C  
ANISOU  603  CB  ALA A  80     1977   3277   1820    -28    274   -266       C  
ATOM    604  N   ALA A  81      68.415  32.590  52.470  1.00 18.50           N  
ANISOU  604  N   ALA A  81     2062   3038   1928    126    389   -428       N  
ATOM    605  CA  ALA A  81      69.444  32.128  53.395  1.00 17.65           C  
ANISOU  605  CA  ALA A  81     1948   2841   1915    212    421   -415       C  
ATOM    606  C   ALA A  81      70.146  30.869  52.917  1.00 21.55           C  
ANISOU  606  C   ALA A  81     2503   3296   2388    310    487   -533       C  
ATOM    607  O   ALA A  81      71.193  30.505  53.469  1.00 22.00           O  
ANISOU  607  O   ALA A  81     2535   3309   2515    409    521   -520       O  
ATOM    608  CB  ALA A  81      68.807  31.882  54.773  1.00 16.76           C  
ANISOU  608  CB  ALA A  81     1878   2584   1907    173    367   -390       C  
ATOM    609  N   GLU A  82      69.611  30.217  51.882  1.00 21.43           N  
ANISOU  609  N   GLU A  82     2568   3300   2276    290    501   -651       N  
ATOM    610  CA  GLU A  82      70.160  28.974  51.328  1.00 24.92           C  
ANISOU  610  CA  GLU A  82     3096   3688   2684    388    563   -792       C  
ATOM    611  C   GLU A  82      70.260  27.885  52.396  1.00 27.24           C  
ANISOU  611  C   GLU A  82     3478   3772   3099    438    545   -828       C  
ATOM    612  O   GLU A  82      71.259  27.167  52.488  1.00 30.07           O  
ANISOU  612  O   GLU A  82     3855   4074   3496    576    598   -875       O  
ATOM    613  CB  GLU A  82      71.511  29.217  50.651  1.00 28.64           C  
ANISOU  613  CB  GLU A  82     3479   4300   3105    507    660   -787       C  
ATOM    614  CG  GLU A  82      71.476  30.382  49.667  1.00 32.70           C  
ANISOU  614  CG  GLU A  82     3905   5023   3497    443    677   -719       C  
ATOM    615  CD  GLU A  82      72.725  30.481  48.812  1.00 47.16           C  
ANISOU  615  CD  GLU A  82     5656   7015   5246    545    789   -730       C  
ATOM    616  OE1 GLU A  82      73.678  31.173  49.229  1.00 51.83           O  
ANISOU  616  OE1 GLU A  82     6125   7662   5906    572    809   -605       O  
ATOM    617  OE2 GLU A  82      72.748  29.873  47.720  1.00 51.83           O1-
ANISOU  617  OE2 GLU A  82     6326   7634   5734    568    834   -834       O1-
ATOM    618  N   THR A  83      69.198  27.731  53.185  1.00 24.57           N  
ANISOU  618  N   THR A  83     3197   3321   2817    329    470   -805       N  
ATOM    619  CA  THR A  83      69.222  26.812  54.314  1.00 29.19           C  
ANISOU  619  CA  THR A  83     3868   3709   3512    352    444   -806       C  
ATOM    620  C   THR A  83      68.792  25.390  53.961  1.00 35.44           C  
ANISOU  620  C   THR A  83     4831   4343   4293    345    438   -950       C  
ATOM    621  O   THR A  83      68.764  24.534  54.852  1.00 36.71           O  
ANISOU  621  O   THR A  83     5087   4319   4543    355    411   -949       O  
ATOM    622  CB  THR A  83      68.346  27.352  55.441  1.00 29.93           C  
ANISOU  622  CB  THR A  83     3938   3767   3669    235    378   -700       C  
ATOM    623  OG1 THR A  83      67.158  27.926  54.882  1.00 34.69           O  
ANISOU  623  OG1 THR A  83     4515   4463   4202    106    344   -705       O  
ATOM    624  CG2 THR A  83      69.104  28.418  56.222  1.00 29.86           C  
ANISOU  624  CG2 THR A  83     3806   3828   3711    281    379   -566       C  
ATOM    625  N   ASP A  84      68.470  25.105  52.697  1.00 37.12           N  
ANISOU  625  N   ASP A  84     5097   4612   4393    322    456  -1073       N  
ATOM    626  CA  ASP A  84      68.225  23.715  52.314  1.00 44.00           C  
ANISOU  626  CA  ASP A  84     6150   5317   5253    327    450  -1227       C  
ATOM    627  C   ASP A  84      69.446  22.835  52.573  1.00 50.94           C  
ANISOU  627  C   ASP A  84     7091   6064   6199    521    505  -1278       C  
ATOM    628  O   ASP A  84      69.299  21.642  52.861  1.00 53.60           O  
ANISOU  628  O   ASP A  84     7592   6184   6591    535    480  -1357       O  
ATOM    629  CB  ASP A  84      67.815  23.633  50.844  1.00 46.59           C  
ANISOU  629  CB  ASP A  84     6525   5751   5428    283    463  -1360       C  
ATOM    630  N   TYR A  85      70.656  23.405  52.499  1.00 50.69           N  
ANISOU  630  N   TYR A  85     6928   6159   6174    670    575  -1225       N  
ATOM    631  CA  TYR A  85      71.868  22.615  52.708  1.00 48.86           C  
ANISOU  631  CA  TYR A  85     6724   5830   6010    877    629  -1268       C  
ATOM    632  C   TYR A  85      71.933  22.028  54.112  1.00 48.85           C  
ANISOU  632  C   TYR A  85     6784   5619   6155    896    566  -1187       C  
ATOM    633  O   TYR A  85      72.594  21.007  54.328  1.00 54.72           O  
ANISOU  633  O   TYR A  85     7623   6202   6967   1047    580  -1246       O  
ATOM    634  CB  TYR A  85      73.110  23.468  52.443  1.00 44.99           C  
ANISOU  634  CB  TYR A  85     6041   5550   5503   1007    710  -1199       C  
ATOM    635  N   ILE A  86      71.266  22.653  55.076  1.00 45.06           N  
ANISOU  635  N   ILE A  86     6258   5140   5721    755    499  -1053       N  
ATOM    636  CA  ILE A  86      71.263  22.153  56.447  1.00 45.16           C  
ANISOU  636  CA  ILE A  86     6334   4973   5852    754    438   -963       C  
ATOM    637  C   ILE A  86      70.085  21.223  56.693  1.00 46.79           C  
ANISOU  637  C   ILE A  86     6725   4982   6070    609    378  -1014       C  
ATOM    638  O   ILE A  86      70.252  20.093  57.160  1.00 47.09           O  
ANISOU  638  O   ILE A  86     6914   4799   6180    664    352  -1041       O  
ATOM    639  CB  ILE A  86      71.258  23.338  57.436  1.00 42.64           C  
ANISOU  639  CB  ILE A  86     5868   4767   5565    686    405   -792       C  
ATOM    640  CG1 ILE A  86      72.616  24.041  57.438  1.00 43.49           C  
ANISOU  640  CG1 ILE A  86     5811   5021   5692    833    447   -726       C  
ATOM    641  CG2 ILE A  86      70.881  22.870  58.835  1.00 44.22           C  
ANISOU  641  CG2 ILE A  86     6155   4797   5851    626    336   -701       C  
ATOM    642  CD1 ILE A  86      73.756  23.155  57.867  1.00 46.15           C  
ANISOU  642  CD1 ILE A  86     6176   5244   6116   1025    455   -730       C  
ATOM    643  N   TYR A  87      68.881  21.679  56.355  1.00 42.52           N  
ANISOU  643  N   TYR A  87     6172   4520   5462    421    352  -1023       N  
ATOM    644  CA  TYR A  87      67.655  21.017  56.777  1.00 43.86           C  
ANISOU  644  CA  TYR A  87     6471   4544   5650    242    289  -1031       C  
ATOM    645  C   TYR A  87      67.210  19.897  55.844  1.00 52.45           C  
ANISOU  645  C   TYR A  87     7736   5499   6695    202    277  -1201       C  
ATOM    646  O   TYR A  87      66.531  18.967  56.293  1.00 51.57           O  
ANISOU  646  O   TYR A  87     7775   5192   6628     90    224  -1216       O  
ATOM    647  CB  TYR A  87      66.535  22.052  56.914  1.00 37.89           C  
ANISOU  647  CB  TYR A  87     5597   3950   4850     62    261   -956       C  
ATOM    648  CG  TYR A  87      66.693  22.976  58.105  0.75 35.83           C  
ANISOU  648  CG  TYR A  87     5214   3758   4640     62    254   -794       C  
ATOM    649  CD1 TYR A  87      66.573  22.489  59.403  0.75 34.81           C  
ANISOU  649  CD1 TYR A  87     5153   3485   4587     26    222   -706       C  
ATOM    650  CD2 TYR A  87      66.951  24.335  57.934  0.75 32.05           C  
ANISOU  650  CD2 TYR A  87     4567   3484   4127     90    276   -729       C  
ATOM    651  CE1 TYR A  87      66.708  23.326  60.502  0.75 30.70           C  
ANISOU  651  CE1 TYR A  87     4536   3032   4095     23    214   -570       C  
ATOM    652  CE2 TYR A  87      67.089  25.182  59.029  0.75 25.71           C  
ANISOU  652  CE2 TYR A  87     3672   2730   3365     86    264   -596       C  
ATOM    653  CZ  TYR A  87      66.963  24.667  60.311  0.75 26.71           C  
ANISOU  653  CZ  TYR A  87     3870   2722   3557     54    234   -524       C  
ATOM    654  OH  TYR A  87      67.083  25.492  61.411  0.75 20.16           O  
ANISOU  654  OH  TYR A  87     2964   1944   2751     47    220   -405       O  
ATOM    655  N   GLU A  88      67.565  19.954  54.564  1.00 57.49           N  
ANISOU  655  N   GLU A  88     8368   6235   7241    279    325  -1329       N  
ATOM    656  CA  GLU A  88      67.165  18.900  53.634  1.00 58.07           C  
ANISOU  656  CA  GLU A  88     8626   6182   7258    242    310  -1510       C  
ATOM    657  C   GLU A  88      68.061  17.678  53.791  1.00 59.65           C  
ANISOU  657  C   GLU A  88     8919   6194   7552    407    313  -1559       C  
ATOM    658  O   GLU A  88      67.806  16.630  53.195  1.00 62.06           O  
ANISOU  658  O   GLU A  88     9335   6389   7858    379    282  -1676       O  
ATOM    659  CB  GLU A  88      67.200  19.402  52.187  1.00 58.67           C  
ANISOU  659  CB  GLU A  88     8646   6460   7184    260    355  -1623       C  
ATOM    660  N   ASP A  93      71.115  17.944  62.333  1.00 41.31           N  
ANISOU  660  N   ASP A  93     6480   3405   5811    742    118   -576       N  
ATOM    661  CA  ASP A  93      71.023  18.163  63.772  1.00 41.85           C  
ANISOU  661  CA  ASP A  93     6553   3440   5906    679     60   -404       C  
ATOM    662  C   ASP A  93      71.374  19.602  64.164  1.00 38.29           C  
ANISOU  662  C   ASP A  93     5884   3243   5420    677     74   -312       C  
ATOM    663  O   ASP A  93      71.634  19.887  65.336  1.00 42.72           O  
ANISOU  663  O   ASP A  93     6420   3812   5999    670     26   -175       O  
ATOM    664  CB  ASP A  93      71.935  17.184  64.514  1.00 43.95           C  
ANISOU  664  CB  ASP A  93     6855   3579   6265    806      9   -327       C  
ATOM    665  N   ILE A  94      71.391  20.505  63.187  1.00 30.46           N  
ANISOU  665  N   ILE A  94     4749   2451   4374    678    133   -385       N  
ATOM    666  CA  ILE A  94      71.690  21.917  63.423  1.00 27.12           C  
ANISOU  666  CA  ILE A  94     4132   2253   3917    665    144   -308       C  
ATOM    667  C   ILE A  94      70.392  22.704  63.302  1.00 29.37           C  
ANISOU  667  C   ILE A  94     4382   2645   4132    464    157   -311       C  
ATOM    668  O   ILE A  94      69.762  22.729  62.238  1.00 29.15           O  
ANISOU  668  O   ILE A  94     4356   2664   4056    404    193   -414       O  
ATOM    669  CB  ILE A  94      72.751  22.448  62.446  1.00 31.23           C  
ANISOU  669  CB  ILE A  94     4505   2930   4430    817    199   -363       C  
ATOM    670  CG1 ILE A  94      74.056  21.665  62.609  1.00 35.80           C  
ANISOU  670  CG1 ILE A  94     5094   3421   5088   1036    189   -357       C  
ATOM    671  CG2 ILE A  94      72.994  23.924  62.676  1.00 27.71           C  
ANISOU  671  CG2 ILE A  94     3878   2699   3953    774    200   -278       C  
ATOM    672  CD1 ILE A  94      74.650  21.743  64.005  1.00 33.43           C  
ANISOU  672  CD1 ILE A  94     4771   3085   4845   1075    111   -205       C  
ATOM    673  N   THR A  95      70.009  23.363  64.391  1.00 22.46           N  
ANISOU  673  N   THR A  95     3471   1818   3246    369    126   -199       N  
ATOM    674  CA  THR A  95      68.711  24.004  64.515  1.00 21.67           C  
ANISOU  674  CA  THR A  95     3343   1800   3090    190    136   -190       C  
ATOM    675  C   THR A  95      68.791  25.397  65.115  1.00 21.02           C  
ANISOU  675  C   THR A  95     3128   1878   2979    168    132   -109       C  
ATOM    676  O   THR A  95      67.771  26.101  65.153  1.00 16.97           O  
ANISOU  676  O   THR A  95     2570   1455   2421     49    146   -107       O  
ATOM    677  CB  THR A  95      67.787  23.150  65.400  1.00 22.06           C  
ANISOU  677  CB  THR A  95     3533   1703   3145     58    110   -146       C  
ATOM    678  OG1 THR A  95      68.374  23.018  66.699  1.00 21.32           O  
ANISOU  678  OG1 THR A  95     3479   1546   3076    100     67    -28       O  
ATOM    679  CG2 THR A  95      67.599  21.755  64.824  1.00 25.84           C  
ANISOU  679  CG2 THR A  95     4170   1993   3655     53    103   -229       C  
ATOM    680  N   GLY A  96      69.958  25.812  65.609  1.00 16.96           N  
ANISOU  680  N   GLY A  96     2552   1400   2492    279    106    -43       N  
ATOM    681  CA  GLY A  96      70.043  27.015  66.404  1.00 16.77           C  
ANISOU  681  CA  GLY A  96     2441   1490   2443    244     84     38       C  
ATOM    682  C   GLY A  96      69.779  26.787  67.872  1.00 17.50           C  
ANISOU  682  C   GLY A  96     2616   1509   2524    185     42    130       C  
ATOM    683  O   GLY A  96      69.691  27.767  68.625  1.00 15.72           O  
ANISOU  683  O   GLY A  96     2342   1369   2262    142     25    184       O  
ATOM    684  N   ARG A  97      69.650  25.530  68.296  1.00 16.94           N  
ANISOU  684  N   ARG A  97     2680   1278   2477    180     23    148       N  
ATOM    685  CA  ARG A  97      69.417  25.204  69.696  1.00 19.82           C  
ANISOU  685  CA  ARG A  97     3140   1572   2819    118    -17    249       C  
ATOM    686  C   ARG A  97      70.502  25.820  70.566  1.00 20.39           C  
ANISOU  686  C   ARG A  97     3159   1701   2889    199    -77    336       C  
ATOM    687  O   ARG A  97      71.690  25.741  70.244  1.00 22.09           O  
ANISOU  687  O   ARG A  97     3317   1919   3156    336   -109    340       O  
ATOM    688  CB  ARG A  97      69.400  23.686  69.873  1.00 23.22           C  
ANISOU  688  CB  ARG A  97     3732   1799   3290    128    -40    266       C  
ATOM    689  CG  ARG A  97      69.055  23.216  71.284  1.00 27.06           C  
ANISOU  689  CG  ARG A  97     4340   2202   3741     42    -79    384       C  
ATOM    690  CD  ARG A  97      69.169  21.707  71.399  1.00 37.07           C  
ANISOU  690  CD  ARG A  97     5780   3244   5061     64   -115    412       C  
ATOM    691  NE  ARG A  97      68.462  21.028  70.316  1.00 49.64           N  
ANISOU  691  NE  ARG A  97     7426   4752   6683      8    -72    302       N  
ATOM    692  CZ  ARG A  97      67.160  20.754  70.322  1.00 58.79           C  
ANISOU  692  CZ  ARG A  97     8640   5891   7805   -179    -37    289       C  
ATOM    693  NH1 ARG A  97      66.409  21.097  71.359  1.00 61.43           N  
ANISOU  693  NH1 ARG A  97     8977   6292   8071   -319    -24    379       N  
ATOM    694  NH2 ARG A  97      66.609  20.134  69.288  1.00 61.50           N  
ANISOU  694  NH2 ARG A  97     9031   6159   8175   -230    -14    183       N  
ATOM    695  N   GLY A  98      70.080  26.445  71.662  1.00 20.99           N  
ANISOU  695  N   GLY A  98     3248   1831   2897    111    -93    401       N  
ATOM    696  CA  GLY A  98      71.005  26.996  72.633  1.00 21.35           C  
ANISOU  696  CA  GLY A  98     3266   1924   2921    160   -165    484       C  
ATOM    697  C   GLY A  98      71.472  28.404  72.354  1.00 20.73           C  
ANISOU  697  C   GLY A  98     3048   1996   2834    179   -171    460       C  
ATOM    698  O   GLY A  98      72.326  28.911  73.093  1.00 21.68           O  
ANISOU  698  O   GLY A  98     3137   2161   2940    212   -243    523       O  
ATOM    699  N   ILE A  99      70.956  29.047  71.311  1.00 16.72           N  
ANISOU  699  N   ILE A  99     2458   1563   2330    154   -108    377       N  
ATOM    700  CA  ILE A  99      71.313  30.409  70.945  1.00 14.66           C  
ANISOU  700  CA  ILE A  99     2078   1429   2064    160   -112    358       C  
ATOM    701  C   ILE A  99      70.134  31.326  71.240  1.00 18.63           C  
ANISOU  701  C   ILE A  99     2586   1990   2501     56    -73    331       C  
ATOM    702  O   ILE A  99      68.982  30.992  70.921  1.00 20.80           O  
ANISOU  702  O   ILE A  99     2892   2251   2760     -6    -12    286       O  
ATOM    703  CB  ILE A  99      71.692  30.507  69.449  1.00 13.67           C  
ANISOU  703  CB  ILE A  99     1853   1352   1988    222    -71    294       C  
ATOM    704  CG1 ILE A  99      72.701  29.421  69.054  1.00 16.90           C  
ANISOU  704  CG1 ILE A  99     2261   1697   2462    343    -85    298       C  
ATOM    705  CG2 ILE A  99      72.231  31.888  69.153  1.00 18.70           C  
ANISOU  705  CG2 ILE A  99     2373   2109   2622    221    -88    302       C  
ATOM    706  CD1 ILE A  99      74.027  29.467  69.828  1.00 20.09           C  
ANISOU  706  CD1 ILE A  99     2622   2115   2896    424   -168    384       C  
ATOM    707  N   LEU A 100      70.419  32.495  71.823  1.00 14.35           N  
ANISOU  707  N   LEU A 100     2012   1516   1926     40   -111    352       N  
ATOM    708  CA  LEU A 100      69.418  33.544  72.027  1.00 14.46           C  
ANISOU  708  CA  LEU A 100     2022   1587   1886    -27    -76    315       C  
ATOM    709  C   LEU A 100      69.529  34.577  70.917  1.00 12.48           C  
ANISOU  709  C   LEU A 100     1668   1405   1668     -9    -64    274       C  
ATOM    710  O   LEU A 100      70.641  34.981  70.565  1.00 13.94           O  
ANISOU  710  O   LEU A 100     1790   1617   1891     32   -111    299       O  
ATOM    711  CB  LEU A 100      69.621  34.239  73.379  1.00 15.42           C  
ANISOU  711  CB  LEU A 100     2198   1723   1939    -56   -128    351       C  
ATOM    712  CG  LEU A 100      69.588  33.345  74.614  1.00 19.37           C  
ANISOU  712  CG  LEU A 100     2809   2169   2381    -82   -150    411       C  
ATOM    713  CD1 LEU A 100      70.158  34.122  75.814  1.00 19.82           C  
ANISOU  713  CD1 LEU A 100     2910   2253   2366    -97   -227    446       C  
ATOM    714  CD2 LEU A 100      68.176  32.863  74.896  1.00 24.04           C  
ANISOU  714  CD2 LEU A 100     3460   2753   2921   -153    -63    389       C  
ATOM    715  N   LEU A 101      68.385  35.026  70.384  1.00 12.64           N  
ANISOU  715  N   LEU A 101     1668   1462   1674    -43     -7    221       N  
ATOM    716  CA  LEU A 101      68.365  36.040  69.327  1.00 11.28           C  
ANISOU  716  CA  LEU A 101     1411   1349   1525    -29     -1    194       C  
ATOM    717  C   LEU A 101      67.561  37.239  69.804  1.00 11.82           C  
ANISOU  717  C   LEU A 101     1490   1445   1556    -55      4    173       C  
ATOM    718  O   LEU A 101      66.388  37.091  70.161  1.00 14.66           O  
ANISOU  718  O   LEU A 101     1874   1814   1882    -83     54    142       O  
ATOM    719  CB  LEU A 101      67.756  35.496  68.025  1.00 11.41           C  
ANISOU  719  CB  LEU A 101     1386   1388   1562    -28     52    148       C  
ATOM    720  CG  LEU A 101      68.385  34.189  67.560  1.00 13.74           C  
ANISOU  720  CG  LEU A 101     1694   1638   1887      7     59    145       C  
ATOM    721  CD1 LEU A 101      67.618  33.639  66.349  1.00 14.92           C  
ANISOU  721  CD1 LEU A 101     1826   1804   2037     -8    107     82       C  
ATOM    722  CD2 LEU A 101      69.855  34.396  67.180  1.00 15.15           C  
ANISOU  722  CD2 LEU A 101     1814   1840   2102     73     23    179       C  
ATOM    723  N   ALA A 102      68.166  38.422  69.769  1.00 11.99           N  
ANISOU  723  N   ALA A 102     1490   1479   1587    -46    -46    188       N  
ATOM    724  CA  ALA A 102      67.495  39.637  70.224  1.00 12.75           C  
ANISOU  724  CA  ALA A 102     1613   1576   1654    -53    -49    160       C  
ATOM    725  C   ALA A 102      66.905  40.419  69.056  1.00 13.57           C  
ANISOU  725  C   ALA A 102     1654   1714   1786    -35    -31    140       C  
ATOM    726  O   ALA A 102      67.611  40.726  68.084  1.00 14.06           O  
ANISOU  726  O   ALA A 102     1663   1794   1885    -32    -58    171       O  
ATOM    727  CB  ALA A 102      68.452  40.538  71.000  1.00 14.30           C  
ANISOU  727  CB  ALA A 102     1852   1741   1839    -65   -130    186       C  
ATOM    728  N   VAL A 103      65.624  40.758  69.180  1.00 12.55           N  
ANISOU  728  N   VAL A 103     1528   1603   1636    -23     13     96       N  
ATOM    729  CA  VAL A 103      64.884  41.586  68.229  1.00 11.96           C  
ANISOU  729  CA  VAL A 103     1400   1560   1585      6     21     81       C  
ATOM    730  C   VAL A 103      64.532  42.879  68.957  1.00 13.91           C  
ANISOU  730  C   VAL A 103     1699   1767   1818     41      0     56       C  
ATOM    731  O   VAL A 103      63.761  42.863  69.925  1.00 16.29           O  
ANISOU  731  O   VAL A 103     2037   2075   2079     57     43     11       O  
ATOM    732  CB  VAL A 103      63.623  40.870  67.730  1.00 15.30           C  
ANISOU  732  CB  VAL A 103     1766   2046   2002      4     84     47       C  
ATOM    733  CG1 VAL A 103      62.864  41.728  66.695  1.00 15.56           C  
ANISOU  733  CG1 VAL A 103     1734   2122   2057     42     76     42       C  
ATOM    734  CG2 VAL A 103      63.991  39.516  67.137  1.00 18.17           C  
ANISOU  734  CG2 VAL A 103     2110   2421   2372    -34    101     56       C  
ATOM    735  N   ILE A 104      65.105  43.992  68.521  1.00 13.29           N  
ANISOU  735  N   ILE A 104     1633   1647   1771     51    -62     83       N  
ATOM    736  CA  ILE A 104      64.883  45.300  69.133  1.00 13.53           C  
ANISOU  736  CA  ILE A 104     1735   1608   1797     87    -97     54       C  
ATOM    737  C   ILE A 104      64.276  46.173  68.040  1.00 13.91           C  
ANISOU  737  C   ILE A 104     1742   1655   1887    135   -111     69       C  
ATOM    738  O   ILE A 104      64.977  46.641  67.138  1.00 14.32           O  
ANISOU  738  O   ILE A 104     1778   1690   1973    107   -164    131       O  
ATOM    739  CB  ILE A 104      66.173  45.903  69.702  1.00 12.57           C  
ANISOU  739  CB  ILE A 104     1689   1410   1676     38   -180     82       C  
ATOM    740  CG1 ILE A 104      66.765  44.981  70.779  1.00 12.54           C  
ANISOU  740  CG1 ILE A 104     1722   1418   1625     -3   -179     79       C  
ATOM    741  CG2 ILE A 104      65.908  47.272  70.295  1.00 14.38           C  
ANISOU  741  CG2 ILE A 104     2018   1546   1901     72   -222     39       C  
ATOM    742  CD1 ILE A 104      68.172  45.403  71.270  1.00 14.51           C  
ANISOU  742  CD1 ILE A 104     2017   1618   1876    -66   -276    120       C  
ATOM    743  N   ASP A 105      62.962  46.375  68.096  1.00 13.65           N  
ANISOU  743  N   ASP A 105     1683   1653   1851    207    -63     20       N  
ATOM    744  CA  ASP A 105      62.239  46.892  66.944  1.00 15.14           C  
ANISOU  744  CA  ASP A 105     1805   1871   2076    258    -75     43       C  
ATOM    745  C   ASP A 105      60.827  47.268  67.379  1.00 15.11           C  
ANISOU  745  C   ASP A 105     1776   1895   2070    357    -26    -21       C  
ATOM    746  O   ASP A 105      60.651  47.795  68.476  1.00 14.55           O  
ANISOU  746  O   ASP A 105     1781   1769   1978    404    -10    -80       O  
ATOM    747  CB  ASP A 105      62.262  45.821  65.833  1.00 16.35           C  
ANISOU  747  CB  ASP A 105     1862   2122   2228    207    -54     80       C  
ATOM    748  CG  ASP A 105      62.052  46.384  64.420  1.00 23.79           C  
ANISOU  748  CG  ASP A 105     2752   3092   3194    227    -98    136       C  
ATOM    749  OD1 ASP A 105      63.017  46.383  63.610  1.00 24.51           O  
ANISOU  749  OD1 ASP A 105     2843   3184   3286    173   -133    198       O  
ATOM    750  OD2 ASP A 105      60.916  46.771  64.100  1.00 23.00           O1-
ANISOU  750  OD2 ASP A 105     2604   3029   3106    296    -94    122       O1-
ATOM    751  N   SER A 106      59.825  46.988  66.550  1.00 14.11           N  
ANISOU  751  N   SER A 106     1725   1785   1851    172    -89    216       N  
ATOM    752  CA  SER A 106      58.463  47.458  66.770  1.00 13.70           C  
ANISOU  752  CA  SER A 106     1659   1720   1826    239    -94    244       C  
ATOM    753  C   SER A 106      57.635  46.499  67.619  1.00 16.31           C  
ANISOU  753  C   SER A 106     1941   2091   2167    264    -81    215       C  
ATOM    754  O   SER A 106      56.447  46.757  67.838  1.00 18.76           O  
ANISOU  754  O   SER A 106     2220   2406   2500    318    -79    230       O  
ATOM    755  CB  SER A 106      57.778  47.696  65.416  1.00 16.76           C  
ANISOU  755  CB  SER A 106     2032   2137   2200    247   -129    306       C  
ATOM    756  OG  SER A 106      57.551  46.468  64.741  1.00 16.47           O  
ANISOU  756  OG  SER A 106     1946   2181   2131    212   -143    301       O  
ATOM    757  N   GLY A 107      58.226  45.415  68.092  1.00 14.91           N  
ANISOU  757  N   GLY A 107     1753   1939   1974    226    -73    177       N  
ATOM    758  CA  GLY A 107      57.538  44.396  68.858  1.00 18.14           C  
ANISOU  758  CA  GLY A 107     2127   2381   2383    234    -61    155       C  
ATOM    759  C   GLY A 107      57.426  43.095  68.084  1.00 20.53           C  
ANISOU  759  C   GLY A 107     2395   2738   2667    197    -75    154       C  
ATOM    760  O   GLY A 107      58.195  42.822  67.156  1.00 18.78           O  
ANISOU  760  O   GLY A 107     2179   2527   2428    161    -88    154       O  
ATOM    761  N   ILE A 108      56.449  42.277  68.480  1.00 14.10           N  
ANISOU  761  N   ILE A 108     1545   1959   1854    199    -68    148       N  
ATOM    762  CA  ILE A 108      56.181  41.011  67.793  1.00 13.78           C  
ANISOU  762  CA  ILE A 108     1477   1963   1796    157    -78    142       C  
ATOM    763  C   ILE A 108      54.707  40.658  67.969  1.00 17.69           C  
ANISOU  763  C   ILE A 108     1921   2506   2294    164    -73    150       C  
ATOM    764  O   ILE A 108      54.148  40.799  69.062  1.00 16.07           O  
ANISOU  764  O   ILE A 108     1708   2297   2102    187    -49    142       O  
ATOM    765  CB  ILE A 108      57.084  39.866  68.309  1.00 13.82           C  
ANISOU  765  CB  ILE A 108     1507   1947   1798    125    -68    109       C  
ATOM    766  CG1 ILE A 108      56.868  38.619  67.436  1.00 13.69           C  
ANISOU  766  CG1 ILE A 108     1473   1962   1767     80    -74     96       C  
ATOM    767  CG2 ILE A 108      56.803  39.543  69.810  1.00 13.35           C  
ANISOU  767  CG2 ILE A 108     1460   1870   1744    135    -49     98       C  
ATOM    768  CD1 ILE A 108      57.737  37.432  67.808  1.00 12.51           C  
ANISOU  768  CD1 ILE A 108     1350   1779   1626     59    -66     65       C  
ATOM    769  N   ASP A 109      54.078  40.176  66.891  1.00 15.11           N  
ANISOU  769  N   ASP A 109     1557   2235   1950    135    -95    162       N  
ATOM    770  CA  ASP A 109      52.728  39.598  66.979  1.00 15.33           C  
ANISOU  770  CA  ASP A 109     1525   2323   1976    120    -94    164       C  
ATOM    771  C   ASP A 109      52.869  38.179  67.521  1.00 17.01           C  
ANISOU  771  C   ASP A 109     1756   2528   2179     64    -71    129       C  
ATOM    772  O   ASP A 109      52.970  37.212  66.769  1.00 16.50           O  
ANISOU  772  O   ASP A 109     1696   2480   2094      9    -80    114       O  
ATOM    773  CB  ASP A 109      52.060  39.617  65.605  1.00 15.93           C  
ANISOU  773  CB  ASP A 109     1555   2467   2030     99   -134    191       C  
ATOM    774  CG  ASP A 109      50.708  38.878  65.588  1.00 29.90           C  
ANISOU  774  CG  ASP A 109     3253   4314   3793     66   -136    187       C  
ATOM    775  OD1 ASP A 109      50.083  38.747  66.663  1.00 29.67           O  
ANISOU  775  OD1 ASP A 109     3198   4288   3786     80   -104    174       O  
ATOM    776  OD2 ASP A 109      50.285  38.420  64.502  1.00 34.61           O1-
ANISOU  776  OD2 ASP A 109     3820   4973   4358     17   -169    193       O1-
ATOM    777  N   TYR A 110      52.907  38.034  68.853  1.00 13.61           N  
ANISOU  777  N   TYR A 110     1347   2066   1759     75    -40    117       N  
ATOM    778  CA  TYR A 110      53.218  36.718  69.406  1.00 14.86           C  
ANISOU  778  CA  TYR A 110     1541   2198   1907     26    -25     96       C  
ATOM    779  C   TYR A 110      52.075  35.720  69.225  1.00 15.82           C  
ANISOU  779  C   TYR A 110     1626   2370   2017    -34    -16     90       C  
ATOM    780  O   TYR A 110      52.277  34.530  69.493  1.00 15.81           O  
ANISOU  780  O   TYR A 110     1661   2338   2007    -85     -5     75       O  
ATOM    781  CB  TYR A 110      53.612  36.820  70.902  1.00 15.80           C  
ANISOU  781  CB  TYR A 110     1702   2273   2028     44     -1     93       C  
ATOM    782  CG  TYR A 110      52.537  37.440  71.767  1.00 14.66           C  
ANISOU  782  CG  TYR A 110     1522   2165   1884     65     30     95       C  
ATOM    783  CD1 TYR A 110      51.482  36.676  72.239  1.00 13.41           C  
ANISOU  783  CD1 TYR A 110     1335   2048   1713     20     58     90       C  
ATOM    784  CD2 TYR A 110      52.555  38.797  72.061  1.00 16.89           C  
ANISOU  784  CD2 TYR A 110     1798   2438   2181    125     38     96       C  
ATOM    785  CE1 TYR A 110      50.465  37.247  73.010  1.00 14.52           C  
ANISOU  785  CE1 TYR A 110     1431   2232   1855     38     96     84       C  
ATOM    786  CE2 TYR A 110      51.557  39.379  72.827  1.00 17.92           C  
ANISOU  786  CE2 TYR A 110     1891   2598   2318    152     76     88       C  
ATOM    787  CZ  TYR A 110      50.508  38.596  73.289  1.00 16.15           C  
ANISOU  787  CZ  TYR A 110     1628   2427   2081    110    106     80       C  
ATOM    788  OH  TYR A 110      49.487  39.145  74.035  1.00 18.76           O  
ANISOU  788  OH  TYR A 110     1911   2799   2420    135    153     64       O  
ATOM    789  N   LEU A 111      50.882  36.162  68.809  1.00 14.00           N  
ANISOU  789  N   LEU A 111     1321   2214   1786    -30    -22    102       N  
ATOM    790  CA  LEU A 111      49.815  35.216  68.499  1.00 13.18           C  
ANISOU  790  CA  LEU A 111     1171   2171   1666   -101    -18     92       C  
ATOM    791  C   LEU A 111      49.881  34.703  67.069  1.00 14.08           C  
ANISOU  791  C   LEU A 111     1279   2314   1758   -151    -52     84       C  
ATOM    792  O   LEU A 111      49.066  33.854  66.706  1.00 16.38           O  
ANISOU  792  O   LEU A 111     1538   2655   2030   -224    -53     70       O  
ATOM    793  CB  LEU A 111      48.419  35.828  68.737  1.00 13.05           C  
ANISOU  793  CB  LEU A 111     1059   2239   1660    -80     -9    105       C  
ATOM    794  CG  LEU A 111      48.103  36.135  70.193  1.00 17.17           C  
ANISOU  794  CG  LEU A 111     1580   2749   2193    -53     41     98       C  
ATOM    795  CD1 LEU A 111      46.700  36.688  70.256  1.00 21.23           C  
ANISOU  795  CD1 LEU A 111     1984   3356   2726    -29     54    102       C  
ATOM    796  CD2 LEU A 111      48.233  34.887  71.053  1.00 20.03           C  
ANISOU  796  CD2 LEU A 111     1999   3079   2532   -130     75     82       C  
ATOM    797  N   HIS A 112      50.812  35.187  66.252  1.00 13.90           N  
ANISOU  797  N   HIS A 112     1286   2265   1731   -123    -77     89       N  
ATOM    798  CA  HIS A 112      50.964  34.607  64.921  1.00 13.91           C  
ANISOU  798  CA  HIS A 112     1292   2292   1699   -182   -101     71       C  
ATOM    799  C   HIS A 112      51.209  33.107  65.074  1.00 12.30           C  
ANISOU  799  C   HIS A 112     1139   2045   1490   -254    -74     27       C  
ATOM    800  O   HIS A 112      52.100  32.713  65.837  1.00 13.63           O  
ANISOU  800  O   HIS A 112     1367   2129   1681   -235    -50     15       O  
ATOM    801  CB  HIS A 112      52.135  35.260  64.179  1.00 13.37           C  
ANISOU  801  CB  HIS A 112     1264   2193   1624   -150   -116     76       C  
ATOM    802  CG  HIS A 112      52.091  35.064  62.695  1.00 14.20           C  
ANISOU  802  CG  HIS A 112     1361   2352   1682   -204   -144     67       C  
ATOM    803  ND1 HIS A 112      52.125  33.817  62.101  1.00 15.02           N  
ANISOU  803  ND1 HIS A 112     1488   2460   1759   -286   -132     18       N  
ATOM    804  CD2 HIS A 112      52.023  35.959  61.681  1.00 14.92           C  
ANISOU  804  CD2 HIS A 112     1432   2494   1742   -194   -182    102       C  
ATOM    805  CE1 HIS A 112      52.068  33.955  60.786  1.00 17.16           C  
ANISOU  805  CE1 HIS A 112     1749   2791   1978   -329   -159     16       C  
ATOM    806  NE2 HIS A 112      51.982  35.243  60.506  1.00 14.95           N  
ANISOU  806  NE2 HIS A 112     1443   2545   1693   -275   -194     72       N  
ATOM    807  N   PRO A 113      50.443  32.252  64.401  1.00 13.22           N  
ANISOU  807  N   PRO A 113     1234   2212   1579   -338    -79      4       N  
ATOM    808  CA  PRO A 113      50.659  30.802  64.545  1.00 15.00           C  
ANISOU  808  CA  PRO A 113     1519   2377   1804   -410    -50    -40       C  
ATOM    809  C   PRO A 113      52.087  30.366  64.272  1.00 14.41           C  
ANISOU  809  C   PRO A 113     1521   2210   1744   -391    -36    -72       C  
ATOM    810  O   PRO A 113      52.535  29.345  64.827  1.00 14.86           O  
ANISOU  810  O   PRO A 113     1639   2181   1825   -408     -9    -95       O  
ATOM    811  CB  PRO A 113      49.688  30.207  63.518  1.00 17.52           C  
ANISOU  811  CB  PRO A 113     1800   2778   2081   -508    -66    -65       C  
ATOM    812  CG  PRO A 113      48.570  31.229  63.447  1.00 21.12           C  
ANISOU  812  CG  PRO A 113     2153   3346   2526   -484    -99    -20       C  
ATOM    813  CD  PRO A 113      49.295  32.559  63.531  1.00 15.41           C  
ANISOU  813  CD  PRO A 113     1430   2601   1822   -375   -115     19       C  
ATOM    814  N   ASP A 114      52.824  31.119  63.457  1.00 13.23           N  
ANISOU  814  N   ASP A 114     1368   2074   1583   -354    -52    -72       N  
ATOM    815  CA  ASP A 114      54.191  30.743  63.127  1.00 12.26           C  
ANISOU  815  CA  ASP A 114     1303   1880   1477   -336    -33   -110       C  
ATOM    816  C   ASP A 114      55.180  30.985  64.267  1.00 11.51           C  
ANISOU  816  C   ASP A 114     1238   1706   1431   -258    -23    -92       C  
ATOM    817  O   ASP A 114      56.371  30.667  64.125  1.00 12.95           O  
ANISOU  817  O   ASP A 114     1455   1830   1637   -233     -8   -121       O  
ATOM    818  CB  ASP A 114      54.653  31.485  61.869  1.00 12.78           C  
ANISOU  818  CB  ASP A 114     1353   1997   1504   -337    -49   -116       C  
ATOM    819  CG  ASP A 114      53.892  31.064  60.617  1.00 15.82           C  
ANISOU  819  CG  ASP A 114     1722   2459   1830   -427    -61   -144       C  
ATOM    820  OD1 ASP A 114      52.800  30.434  60.703  1.00 15.89           O  
ANISOU  820  OD1 ASP A 114     1711   2501   1824   -487    -67   -149       O  
ATOM    821  OD2 ASP A 114      54.420  31.354  59.512  1.00 16.88           O1-
ANISOU  821  OD2 ASP A 114     1865   2627   1924   -447    -64   -163       O1-
ATOM    822  N   PHE A 115      54.734  31.547  65.391  1.00 11.23           N  
ANISOU  822  N   PHE A 115     1185   1674   1408   -221    -29    -48       N  
ATOM    823  CA  PHE A 115      55.561  31.667  66.588  1.00 12.04           C  
ANISOU  823  CA  PHE A 115     1321   1710   1545   -163    -24    -30       C  
ATOM    824  C   PHE A 115      55.052  30.796  67.722  1.00 12.78           C  
ANISOU  824  C   PHE A 115     1445   1764   1648   -186    -10    -18       C  
ATOM    825  O   PHE A 115      55.463  30.994  68.877  1.00 13.24           O  
ANISOU  825  O   PHE A 115     1527   1785   1720   -147    -11      8       O  
ATOM    826  CB  PHE A 115      55.645  33.120  67.066  1.00 12.48           C  
ANISOU  826  CB  PHE A 115     1349   1793   1601   -103    -37      6       C  
ATOM    827  CG  PHE A 115      56.180  34.065  66.019  1.00 13.89           C  
ANISOU  827  CG  PHE A 115     1508   2001   1768    -84    -51      6       C  
ATOM    828  CD1 PHE A 115      57.399  33.820  65.415  1.00 16.16           C  
ANISOU  828  CD1 PHE A 115     1819   2259   2064    -81    -45    -25       C  
ATOM    829  CD2 PHE A 115      55.455  35.184  65.650  1.00 13.38           C  
ANISOU  829  CD2 PHE A 115     1403   1995   1686    -69    -69     38       C  
ATOM    830  CE1 PHE A 115      57.890  34.684  64.439  1.00 19.11           C  
ANISOU  830  CE1 PHE A 115     2180   2665   2417    -79    -52    -25       C  
ATOM    831  CE2 PHE A 115      55.939  36.061  64.667  1.00 16.50           C  
ANISOU  831  CE2 PHE A 115     1794   2413   2064    -60    -84     47       C  
ATOM    832  CZ  PHE A 115      57.156  35.803  64.069  1.00 13.39           C  
ANISOU  832  CZ  PHE A 115     1428   1993   1668    -72    -74     16       C  
ATOM    833  N   ILE A 116      54.157  29.855  67.433  1.00 13.10           N  
ANISOU  833  N   ILE A 116     1488   1815   1674   -260      3    -35       N  
ATOM    834  CA  ILE A 116      53.572  28.985  68.448  1.00 13.38           C  
ANISOU  834  CA  ILE A 116     1558   1815   1711   -302     21    -20       C  
ATOM    835  C   ILE A 116      53.995  27.548  68.146  1.00 14.67           C  
ANISOU  835  C   ILE A 116     1790   1890   1893   -345     34    -53       C  
ATOM    836  O   ILE A 116      53.758  27.040  67.044  1.00 16.03           O  
ANISOU  836  O   ILE A 116     1959   2076   2054   -399     41    -97       O  
ATOM    837  CB  ILE A 116      52.045  29.137  68.505  1.00 15.19           C  
ANISOU  837  CB  ILE A 116     1729   2134   1910   -361     30    -11       C  
ATOM    838  CG1 ILE A 116      51.675  30.601  68.780  1.00 14.49           C  
ANISOU  838  CG1 ILE A 116     1572   2118   1815   -300     20     18       C  
ATOM    839  CG2 ILE A 116      51.442  28.212  69.577  1.00 15.40           C  
ANISOU  839  CG2 ILE A 116     1795   2127   1931   -420     57      4       C  
ATOM    840  CD1 ILE A 116      50.197  30.914  68.611  1.00 17.48           C  
ANISOU  840  CD1 ILE A 116     1867   2601   2175   -338     24     24       C  
ATOM    841  N   ASN A 117      54.616  26.895  69.132  1.00 14.73           N  
ANISOU  841  N   ASN A 117     1863   1805   1927   -322     36    -31       N  
ATOM    842  CA  ASN A 117      55.066  25.522  68.980  1.00 17.99           C  
ANISOU  842  CA  ASN A 117     2351   2112   2371   -347     48    -56       C  
ATOM    843  C   ASN A 117      53.883  24.557  68.959  1.00 19.53           C  
ANISOU  843  C   ASN A 117     2574   2303   2545   -456     73    -65       C  
ATOM    844  O   ASN A 117      52.743  24.908  69.283  1.00 18.13           O  
ANISOU  844  O   ASN A 117     2353   2208   2329   -509     80    -46       O  
ATOM    845  CB  ASN A 117      56.014  25.144  70.119  1.00 17.18           C  
ANISOU  845  CB  ASN A 117     2310   1913   2303   -285     33    -14       C  
ATOM    846  CG  ASN A 117      57.289  25.969  70.122  1.00 20.92           C  
ANISOU  846  CG  ASN A 117     2756   2390   2804   -186      7    -11       C  
ATOM    847  OD1 ASN A 117      57.939  26.144  69.087  1.00 22.82           O  
ANISOU  847  OD1 ASN A 117     2969   2639   3064   -159     12    -58       O  
ATOM    848  ND2 ASN A 117      57.662  26.479  71.296  1.00 18.14           N  
ANISOU  848  ND2 ASN A 117     2409   2037   2445   -140    -17     41       N  
ATOM    849  N   ASP A 118      54.178  23.312  68.568  1.00 22.20           N  
ANISOU  849  N   ASP A 118     2984   2540   2910   -492     89   -101       N  
ATOM    850  CA  ASP A 118      53.147  22.278  68.500  1.00 28.56           C  
ANISOU  850  CA  ASP A 118     3830   3324   3697   -610    116   -117       C  
ATOM    851  C   ASP A 118      52.417  22.120  69.829  1.00 29.11           C  
ANISOU  851  C   ASP A 118     3923   3394   3745   -652    122    -53       C  
ATOM    852  O   ASP A 118      51.214  21.839  69.850  1.00 30.43           O  
ANISOU  852  O   ASP A 118     4071   3616   3874   -757    143    -57       O  
ATOM    853  CB  ASP A 118      53.762  20.939  68.085  1.00 34.92           C  
ANISOU  853  CB  ASP A 118     4732   3988   4549   -626    135   -161       C  
ATOM    854  CG  ASP A 118      54.215  20.921  66.639  1.00 51.13           C  
ANISOU  854  CG  ASP A 118     6765   6054   6608   -623    147   -244       C  
ATOM    855  OD1 ASP A 118      53.937  21.895  65.910  1.00 55.47           O  
ANISOU  855  OD1 ASP A 118     7230   6730   7118   -625    135   -260       O  
ATOM    856  OD2 ASP A 118      54.850  19.925  66.231  1.00 56.52           O1-
ANISOU  856  OD2 ASP A 118     7521   6619   7336   -619    170   -293       O1-
ATOM    857  N   ASP A 119      53.126  22.292  70.948  1.00 27.44           N  
ANISOU  857  N   ASP A 119     3748   3128   3548   -578    104      5       N  
ATOM    858  CA  ASP A 119      52.526  22.132  72.268  1.00 27.99           C  
ANISOU  858  CA  ASP A 119     3852   3197   3586   -621    112     67       C  
ATOM    859  C   ASP A 119      51.873  23.411  72.791  1.00 26.89           C  
ANISOU  859  C   ASP A 119     3623   3193   3403   -609    115     89       C  
ATOM    860  O   ASP A 119      51.501  23.465  73.971  1.00 25.57           O  
ANISOU  860  O   ASP A 119     3478   3036   3202   -632    126    137       O  
ATOM    861  CB  ASP A 119      53.572  21.623  73.274  1.00 29.08           C  
ANISOU  861  CB  ASP A 119     4084   3213   3753   -557     87    125       C  
ATOM    862  CG  ASP A 119      54.729  22.599  73.493  1.00 31.57           C  
ANISOU  862  CG  ASP A 119     4361   3546   4088   -431     48    140       C  
ATOM    863  OD1 ASP A 119      54.721  23.708  72.919  1.00 28.19           O  
ANISOU  863  OD1 ASP A 119     3843   3216   3651   -395     45    109       O  
ATOM    864  OD2 ASP A 119      55.656  22.259  74.273  1.00 33.94           O1-
ANISOU  864  OD2 ASP A 119     4722   3761   4412   -371     15    188       O1-
ATOM    865  N   GLY A 120      51.735  24.440  71.952  1.00 22.44           N  
ANISOU  865  N   GLY A 120     2963   2726   2836   -572    107     55       N  
ATOM    866  CA  GLY A 120      51.078  25.668  72.353  1.00 18.97           C  
ANISOU  866  CA  GLY A 120     2438   2405   2367   -550    112     69       C  
ATOM    867  C   GLY A 120      51.960  26.709  73.010  1.00 19.37           C  
ANISOU  867  C   GLY A 120     2481   2454   2423   -447     90     96       C  
ATOM    868  O   GLY A 120      51.448  27.762  73.410  1.00 23.25           O  
ANISOU  868  O   GLY A 120     2911   3030   2894   -424    100    103       O  
ATOM    869  N   THR A 121      53.254  26.461  73.142  1.00 17.85           N  
ANISOU  869  N   THR A 121     2348   2173   2261   -384     62    107       N  
ATOM    870  CA  THR A 121      54.115  27.415  73.826  1.00 16.49           C  
ANISOU  870  CA  THR A 121     2171   2005   2089   -299     38    132       C  
ATOM    871  C   THR A 121      54.730  28.408  72.838  1.00 16.50           C  
ANISOU  871  C   THR A 121     2112   2044   2115   -232     20     99       C  
ATOM    872  O   THR A 121      54.803  28.164  71.633  1.00 15.93           O  
ANISOU  872  O   THR A 121     2020   1973   2061   -242     20     62       O  
ATOM    873  CB  THR A 121      55.222  26.697  74.604  1.00 20.69           C  
ANISOU  873  CB  THR A 121     2787   2435   2640   -265      9    169       C  
ATOM    874  OG1 THR A 121      55.998  25.892  73.710  1.00 21.59           O  
ANISOU  874  OG1 THR A 121     2926   2469   2806   -242     -4    142       O  
ATOM    875  CG2 THR A 121      54.623  25.808  75.691  1.00 20.61           C  
ANISOU  875  CG2 THR A 121     2850   2387   2596   -335     24    215       C  
ATOM    876  N   SER A 122      55.172  29.541  73.378  1.00 14.63           N  
ANISOU  876  N   SER A 122     1852   1838   1869   -174      8    113       N  
ATOM    877  CA  SER A 122      55.696  30.639  72.583  1.00 14.13           C  
ANISOU  877  CA  SER A 122     1737   1810   1821   -119     -6     92       C  
ATOM    878  C   SER A 122      57.166  30.433  72.250  1.00 16.21           C  
ANISOU  878  C   SER A 122     2025   2015   2121    -69    -34     82       C  
ATOM    879  O   SER A 122      57.954  30.000  73.099  1.00 15.65           O  
ANISOU  879  O   SER A 122     1998   1888   2059    -44    -54    106       O  
ATOM    880  CB  SER A 122      55.552  31.955  73.345  1.00 13.04           C  
ANISOU  880  CB  SER A 122     1574   1719   1662    -84     -3    105       C  
ATOM    881  OG  SER A 122      56.019  33.026  72.541  1.00 13.25           O  
ANISOU  881  OG  SER A 122     1560   1771   1703    -38    -16     89       O  
ATOM    882  N   LYS A 123      57.549  30.816  71.027  1.00 12.77           N  
ANISOU  882  N   LYS A 123     1552   1600   1701    -53    -35     49       N  
ATOM    883  CA  LYS A 123      58.969  30.889  70.710  1.00 12.64           C  
ANISOU  883  CA  LYS A 123     1538   1549   1717     -3    -53     33       C  
ATOM    884  C   LYS A 123      59.651  32.097  71.349  1.00 15.96           C  
ANISOU  884  C   LYS A 123     1942   1991   2131     43    -72     51       C  
ATOM    885  O   LYS A 123      60.888  32.171  71.333  1.00 15.89           O  
ANISOU  885  O   LYS A 123     1929   1961   2149     81    -91     43       O  
ATOM    886  CB  LYS A 123      59.142  30.907  69.186  1.00 15.46           C  
ANISOU  886  CB  LYS A 123     1865   1928   2081    -15    -40    -12       C  
ATOM    887  CG  LYS A 123      58.668  29.603  68.536  1.00 20.78           C  
ANISOU  887  CG  LYS A 123     2564   2569   2761    -65    -20    -43       C  
ATOM    888  CD  LYS A 123      59.228  29.377  67.141  1.00 22.79           C  
ANISOU  888  CD  LYS A 123     2806   2827   3025    -74     -4    -99       C  
ATOM    889  CE  LYS A 123      60.716  28.975  67.150  1.00 22.04           C  
ANISOU  889  CE  LYS A 123     2721   2671   2982    -15     -4   -124       C  
ATOM    890  NZ  LYS A 123      61.214  28.577  65.754  1.00 19.20           N  
ANISOU  890  NZ  LYS A 123     2352   2314   2630    -32     28   -194       N  
ATOM    891  N   VAL A 124      58.883  33.035  71.903  1.00 12.12           N  
ANISOU  891  N   VAL A 124     1443   1549   1613     37    -65     69       N  
ATOM    892  CA  VAL A 124      59.443  34.191  72.586  1.00 11.03           C  
ANISOU  892  CA  VAL A 124     1301   1424   1465     69    -78     79       C  
ATOM    893  C   VAL A 124      59.767  33.789  74.022  1.00 13.32           C  
ANISOU  893  C   VAL A 124     1635   1686   1741     72    -95    107       C  
ATOM    894  O   VAL A 124      58.917  33.234  74.731  1.00 14.98           O  
ANISOU  894  O   VAL A 124     1871   1893   1926     41    -81    127       O  
ATOM    895  CB  VAL A 124      58.460  35.376  72.550  1.00 12.96           C  
ANISOU  895  CB  VAL A 124     1518   1718   1688     69    -57     81       C  
ATOM    896  CG1 VAL A 124      59.033  36.577  73.322  1.00 14.24           C  
ANISOU  896  CG1 VAL A 124     1690   1880   1840     96    -64     83       C  
ATOM    897  CG2 VAL A 124      58.121  35.769  71.110  1.00 13.27           C  
ANISOU  897  CG2 VAL A 124     1517   1789   1735     65    -53     67       C  
ATOM    898  N   LEU A 125      60.991  34.077  74.460  1.00 11.52           N  
ANISOU  898  N   LEU A 125     1412   1444   1521    102   -126    111       N  
ATOM    899  CA  LEU A 125      61.424  33.760  75.821  1.00 11.32           C  
ANISOU  899  CA  LEU A 125     1428   1400   1473    104   -156    144       C  
ATOM    900  C   LEU A 125      61.143  34.908  76.793  1.00 13.32           C  
ANISOU  900  C   LEU A 125     1693   1691   1677     92   -148    145       C  
ATOM    901  O   LEU A 125      60.709  34.674  77.939  1.00 14.19           O  
ANISOU  901  O   LEU A 125     1845   1805   1743     66   -147    169       O  
ATOM    902  CB  LEU A 125      62.931  33.428  75.815  1.00 13.00           C  
ANISOU  902  CB  LEU A 125     1631   1588   1722    143   -203    147       C  
ATOM    903  CG  LEU A 125      63.484  32.889  77.130  1.00 13.84           C  
ANISOU  903  CG  LEU A 125     1777   1673   1807    150   -251    193       C  
ATOM    904  CD1 LEU A 125      62.961  31.488  77.381  1.00 17.38           C  
ANISOU  904  CD1 LEU A 125     2276   2067   2262    139   -252    228       C  
ATOM    905  CD2 LEU A 125      65.022  32.922  77.050  1.00 17.10           C  
ANISOU  905  CD2 LEU A 125     2152   2086   2259    196   -300    189       C  
ATOM    906  N   TYR A 126      61.376  36.145  76.346  1.00 12.77           N  
ANISOU  906  N   TYR A 126     1594   1645   1614    105   -138    117       N  
ATOM    907  CA  TYR A 126      61.158  37.359  77.122  1.00 12.27           C  
ANISOU  907  CA  TYR A 126     1544   1605   1513     96   -123    105       C  
ATOM    908  C   TYR A 126      60.729  38.456  76.173  1.00 14.89           C  
ANISOU  908  C   TYR A 126     1845   1948   1866    110    -93     79       C  
ATOM    909  O   TYR A 126      61.213  38.517  75.033  1.00 13.79           O  
ANISOU  909  O   TYR A 126     1676   1805   1760    122   -101     72       O  
ATOM    910  CB  TYR A 126      62.427  37.848  77.858  1.00 12.96           C  
ANISOU  910  CB  TYR A 126     1646   1695   1584     96   -164    103       C  
ATOM    911  CG  TYR A 126      62.903  36.982  78.997  1.00 12.28           C  
ANISOU  911  CG  TYR A 126     1595   1605   1465     84   -206    138       C  
ATOM    912  CD1 TYR A 126      62.400  37.158  80.283  1.00 14.07           C  
ANISOU  912  CD1 TYR A 126     1870   1849   1625     51   -198    147       C  
ATOM    913  CD2 TYR A 126      63.874  36.016  78.804  1.00 12.45           C  
ANISOU  913  CD2 TYR A 126     1604   1606   1522    109   -256    162       C  
ATOM    914  CE1 TYR A 126      62.858  36.371  81.333  1.00 16.02           C  
ANISOU  914  CE1 TYR A 126     2158   2096   1831     34   -245    190       C  
ATOM    915  CE2 TYR A 126      64.333  35.224  79.837  1.00 17.12           C  
ANISOU  915  CE2 TYR A 126     2230   2189   2086    106   -306    206       C  
ATOM    916  CZ  TYR A 126      63.817  35.405  81.102  1.00 19.25           C  
ANISOU  916  CZ  TYR A 126     2555   2480   2281     65   -304    225       C  
ATOM    917  OH  TYR A 126      64.290  34.622  82.138  1.00 20.49           O  
ANISOU  917  OH  TYR A 126     2754   2631   2400     56   -362    280       O  
ATOM    918  N   LEU A 127      59.835  39.323  76.652  1.00 14.41           N  
ANISOU  918  N   LEU A 127     1791   1899   1783    110    -57     67       N  
ATOM    919  CA  LEU A 127      59.335  40.450  75.870  1.00 12.18           C  
ANISOU  919  CA  LEU A 127     1485   1618   1524    133    -32     51       C  
ATOM    920  C   LEU A 127      59.285  41.659  76.786  1.00 18.60           C  
ANISOU  920  C   LEU A 127     2330   2421   2316    136     -9     26       C  
ATOM    921  O   LEU A 127      58.561  41.635  77.784  1.00 17.67           O  
ANISOU  921  O   LEU A 127     2229   2317   2167    127     22     16       O  
ATOM    922  CB  LEU A 127      57.937  40.150  75.289  1.00 12.95           C  
ANISOU  922  CB  LEU A 127     1545   1739   1634    141     -4     59       C  
ATOM    923  CG  LEU A 127      57.418  40.901  74.048  1.00 27.47           C  
ANISOU  923  CG  LEU A 127     3347   3586   3505    169      1     63       C  
ATOM    924  CD1 LEU A 127      55.982  40.454  73.670  1.00 25.10           C  
ANISOU  924  CD1 LEU A 127     2999   3327   3211    171     20     73       C  
ATOM    925  CD2 LEU A 127      57.461  42.408  74.202  1.00 27.37           C  
ANISOU  925  CD2 LEU A 127     3350   3547   3502    200     16     51       C  
ATOM    926  N   TRP A 128      60.041  42.711  76.469  1.00 11.96           N  
ANISOU  926  N   TRP A 128     1501   1556   1488    142    -17     12       N  
ATOM    927  CA  TRP A 128      59.892  43.994  77.156  1.00 12.45           C  
ANISOU  927  CA  TRP A 128     1599   1594   1538    146     13    -20       C  
ATOM    928  C   TRP A 128      59.192  44.972  76.215  1.00 14.02           C  
ANISOU  928  C   TRP A 128     1782   1766   1780    187     37    -18       C  
ATOM    929  O   TRP A 128      59.741  45.346  75.177  1.00 12.29           O  
ANISOU  929  O   TRP A 128     1556   1529   1585    189     17     -2       O  
ATOM    930  CB  TRP A 128      61.244  44.537  77.605  1.00 13.21           C  
ANISOU  930  CB  TRP A 128     1730   1675   1615    111    -14    -39       C  
ATOM    931  CG  TRP A 128      61.185  45.882  78.278  1.00 11.45           C  
ANISOU  931  CG  TRP A 128     1556   1417   1379    103     19    -81       C  
ATOM    932  CD1 TRP A 128      60.113  46.444  78.919  1.00 13.63           C  
ANISOU  932  CD1 TRP A 128     1853   1679   1647    125     73   -110       C  
ATOM    933  CD2 TRP A 128      62.254  46.825  78.375  1.00 13.18           C  
ANISOU  933  CD2 TRP A 128     1810   1608   1591     68      6   -106       C  
ATOM    934  NE1 TRP A 128      60.456  47.683  79.408  1.00 14.07           N  
ANISOU  934  NE1 TRP A 128     1962   1689   1695    110     96   -154       N  
ATOM    935  CE2 TRP A 128      61.767  47.937  79.083  1.00 12.46           C  
ANISOU  935  CE2 TRP A 128     1770   1475   1488     69     53   -151       C  
ATOM    936  CE3 TRP A 128      63.585  46.833  77.928  1.00 14.16           C  
ANISOU  936  CE3 TRP A 128     1921   1739   1719     31    -38    -99       C  
ATOM    937  CZ2 TRP A 128      62.558  49.045  79.376  1.00 12.51           C  
ANISOU  937  CZ2 TRP A 128     1828   1441   1484     27     56   -189       C  
ATOM    938  CZ3 TRP A 128      64.383  47.943  78.222  1.00 14.62           C  
ANISOU  938  CZ3 TRP A 128     2021   1770   1765    -14    -37   -134       C  
ATOM    939  CH2 TRP A 128      63.861  49.036  78.933  1.00 13.29           C  
ANISOU  939  CH2 TRP A 128     1915   1552   1582    -20      9   -178       C  
ATOM    940  N   ASP A 129      57.973  45.364  76.556  1.00 12.72           N  
ANISOU  940  N   ASP A 129     1608   1601   1623    221     81    -30       N  
ATOM    941  CA  ASP A 129      57.239  46.376  75.806  1.00 13.84           C  
ANISOU  941  CA  ASP A 129     1735   1712   1811    275    100    -24       C  
ATOM    942  C   ASP A 129      57.459  47.703  76.523  1.00 15.86           C  
ANISOU  942  C   ASP A 129     2049   1907   2069    284    133    -65       C  
ATOM    943  O   ASP A 129      56.919  47.922  77.613  1.00 14.32           O  
ANISOU  943  O   ASP A 129     1871   1714   1857    290    179   -107       O  
ATOM    944  CB  ASP A 129      55.760  46.005  75.725  1.00 16.06           C  
ANISOU  944  CB  ASP A 129     1957   2035   2111    314    128    -15       C  
ATOM    945  CG  ASP A 129      54.951  46.982  74.891  1.00 21.26           C  
ANISOU  945  CG  ASP A 129     2587   2668   2823    382    135      3       C  
ATOM    946  OD1 ASP A 129      55.272  48.187  74.867  1.00 19.34           O  
ANISOU  946  OD1 ASP A 129     2389   2357   2604    409    144     -7       O  
ATOM    947  OD2 ASP A 129      53.964  46.544  74.268  1.00 22.45           O1-
ANISOU  947  OD2 ASP A 129     2670   2867   2994    408    129     29       O1-
ATOM    948  N   GLN A 130      58.270  48.582  75.928  1.00 14.64           N  
ANISOU  948  N   GLN A 130     1931   1698   1933    277    115    -59       N  
ATOM    949  CA  GLN A 130      58.622  49.837  76.589  1.00 12.90           C  
ANISOU  949  CA  GLN A 130     1780   1409   1714    271    145   -103       C  
ATOM    950  C   GLN A 130      57.450  50.806  76.726  1.00 16.29           C  
ANISOU  950  C   GLN A 130     2215   1786   2188    345    197   -122       C  
ATOM    951  O   GLN A 130      57.546  51.753  77.518  1.00 16.17           O  
ANISOU  951  O   GLN A 130     2262   1711   2172    343    238   -176       O  
ATOM    952  CB  GLN A 130      59.755  50.523  75.838  1.00 13.92           C  
ANISOU  952  CB  GLN A 130     1947   1491   1851    235    114    -87       C  
ATOM    953  CG  GLN A 130      61.076  49.752  75.888  1.00 14.80           C  
ANISOU  953  CG  GLN A 130     2050   1651   1923    162     71    -85       C  
ATOM    954  CD  GLN A 130      62.210  50.557  75.306  1.00 18.05           C  
ANISOU  954  CD  GLN A 130     2497   2023   2339    114     54    -83       C  
ATOM    955  OE1 GLN A 130      61.984  51.500  74.554  1.00 15.19           O  
ANISOU  955  OE1 GLN A 130     2164   1598   2010    134     65    -63       O  
ATOM    956  NE2 GLN A 130      63.438  50.209  75.673  1.00 13.82           N  
ANISOU  956  NE2 GLN A 130     1958   1523   1770     48     25   -101       N  
ATOM    957  N   GLU A 131      56.355  50.583  75.995  1.00 17.29           N  
ANISOU  957  N   GLU A 131     2278   1936   2355    410    196    -84       N  
ATOM    958  CA  GLU A 131      55.193  51.460  76.044  1.00 19.89           C  
ANISOU  958  CA  GLU A 131     2594   2223   2742    497    240    -96       C  
ATOM    959  C   GLU A 131      54.078  50.964  76.958  1.00 20.52           C  
ANISOU  959  C   GLU A 131     2621   2361   2815    524    293   -136       C  
ATOM    960  O   GLU A 131      53.210  51.759  77.336  1.00 24.29           O  
ANISOU  960  O   GLU A 131     3091   2801   3336    594    347   -171       O  
ATOM    961  CB  GLU A 131      54.639  51.642  74.629  1.00 21.07           C  
ANISOU  961  CB  GLU A 131     2696   2369   2942    556    199    -23       C  
ATOM    962  CG  GLU A 131      55.623  52.386  73.752  1.00 28.59           C  
ANISOU  962  CG  GLU A 131     3713   3250   3901    531    161     15       C  
ATOM    963  CD  GLU A 131      55.027  52.856  72.459  1.00 36.62           C  
ANISOU  963  CD  GLU A 131     4704   4246   4964    594    124     89       C  
ATOM    964  OE1 GLU A 131      54.229  52.098  71.862  1.00 38.20           O  
ANISOU  964  OE1 GLU A 131     4821   4527   5168    620     98    128       O  
ATOM    965  OE2 GLU A 131      55.358  53.994  72.050  1.00 30.16           O1-
ANISOU  965  OE2 GLU A 131     3954   3331   4175    611    120    111       O1-
ATOM    966  N   ALA A 132      54.079  49.690  77.323  1.00 20.46           N  
ANISOU  966  N   ALA A 132     2579   2440   2757    471    283   -133       N  
ATOM    967  CA  ALA A 132      52.970  49.129  78.082  1.00 20.86           C  
ANISOU  967  CA  ALA A 132     2575   2556   2796    483    334   -163       C  
ATOM    968  C   ALA A 132      53.037  49.555  79.547  1.00 25.57           C  
ANISOU  968  C   ALA A 132     3229   3136   3352    458    402   -241       C  
ATOM    969  O   ALA A 132      54.088  49.937  80.065  1.00 24.23           O  
ANISOU  969  O   ALA A 132     3140   2923   3143    407    394   -268       O  
ATOM    970  CB  ALA A 132      52.974  47.605  77.970  1.00 22.84           C  
ANISOU  970  CB  ALA A 132     2783   2892   3002    423    302   -128       C  
ATOM    971  N   ASN A 133      51.893  49.482  80.227  1.00 20.75           N  
ANISOU  971  N   ASN A 133     2572   2569   2744    486    470   -282       N  
ATOM    972  CA  ASN A 133      51.867  49.829  81.648  1.00 21.51           C  
ANISOU  972  CA  ASN A 133     2722   2661   2789    453    544   -364       C  
ATOM    973  C   ASN A 133      51.011  48.849  82.450  1.00 25.95           C  
ANISOU  973  C   ASN A 133     3236   3324   3301    415    593   -383       C  
ATOM    974  O   ASN A 133      50.339  49.234  83.411  1.00 30.42           O  
ANISOU  974  O   ASN A 133     3802   3905   3850    422    681   -455       O  
ATOM    975  CB  ASN A 133      51.377  51.263  81.856  1.00 31.34           C  
ANISOU  975  CB  ASN A 133     3987   3824   4096    535    612   -427       C  
ATOM    976  CG  ASN A 133      49.966  51.492  81.324  1.00 47.13           C  
ANISOU  976  CG  ASN A 133     5880   5844   6183    642    647   -420       C  
ATOM    977  OD1 ASN A 133      49.341  50.591  80.757  1.00 48.65           O  
ANISOU  977  OD1 ASN A 133     5981   6119   6384    646    619   -368       O  
ATOM    978  ND2 ASN A 133      49.458  52.708  81.510  1.00 54.10           N  
ANISOU  978  ND2 ASN A 133     6773   6650   7133    730    709   -475       N  
ATOM    979  N   THR A 134      51.046  47.562  82.100  1.00 21.81           N  
ANISOU  979  N   THR A 134     2674   2866   2746    365    544   -323       N  
ATOM    980  CA  THR A 134      50.193  46.568  82.749  1.00 25.08           C  
ANISOU  980  CA  THR A 134     3043   3371   3114    318    588   -330       C  
ATOM    981  C   THR A 134      50.933  45.594  83.656  1.00 31.66           C  
ANISOU  981  C   THR A 134     3948   4237   3844    211    568   -318       C  
ATOM    982  O   THR A 134      50.301  44.981  84.519  1.00 44.13           O  
ANISOU  982  O   THR A 134     5520   5882   5365    158    621   -337       O  
ATOM    983  CB  THR A 134      49.433  45.739  81.708  1.00 28.25           C  
ANISOU  983  CB  THR A 134     3345   3828   3560    336    555   -271       C  
ATOM    984  OG1 THR A 134      50.375  45.157  80.790  1.00 26.07           O  
ANISOU  984  OG1 THR A 134     3093   3528   3285    312    462   -205       O  
ATOM    985  CG2 THR A 134      48.433  46.598  80.949  1.00 29.47           C  
ANISOU  985  CG2 THR A 134     3410   3977   3809    443    577   -279       C  
ATOM    986  N   ASN A 135      52.221  45.396  83.443  1.00 21.55           N  
ANISOU  986  N   ASN A 135     2729   2917   2541    178    491   -281       N  
ATOM    987  CA  ASN A 135      53.127  44.610  84.265  1.00 23.35           C  
ANISOU  987  CA  ASN A 135     3030   3164   2680     91    453   -261       C  
ATOM    988  C   ASN A 135      54.290  45.511  84.643  1.00 21.71           C  
ANISOU  988  C   ASN A 135     2898   2901   2448     79    428   -292       C  
ATOM    989  O   ASN A 135      54.559  46.496  83.947  1.00 21.23           O  
ANISOU  989  O   ASN A 135     2835   2780   2451    133    421   -306       O  
ATOM    990  CB  ASN A 135      53.634  43.393  83.473  1.00 24.60           C  
ANISOU  990  CB  ASN A 135     3170   3330   2848     70    371   -182       C  
ATOM    991  CG  ASN A 135      53.584  42.108  84.260  1.00 29.35           C  
ANISOU  991  CG  ASN A 135     3800   3978   3373     -8    364   -149       C  
ATOM    992  OD1 ASN A 135      52.677  41.887  85.065  1.00 29.23           O  
ANISOU  992  OD1 ASN A 135     3781   4012   3312    -43    431   -173       O  
ATOM    993  ND2 ASN A 135      54.553  41.235  84.013  1.00 30.97           N  
ANISOU  993  ND2 ASN A 135     4033   4166   3567    -34    285    -92       N  
ATOM    994  N   PRO A 136      55.010  45.208  85.724  1.00 18.45           N  
ANISOU  994  N   PRO A 136     2557   2510   1943      2    411   -299       N  
ATOM    995  CA  PRO A 136      56.165  46.026  86.090  1.00 19.65           C  
ANISOU  995  CA  PRO A 136     2777   2622   2067    -24    380   -329       C  
ATOM    996  C   PRO A 136      57.222  46.008  85.005  1.00 17.54           C  
ANISOU  996  C   PRO A 136     2494   2315   1856     -2    295   -280       C  
ATOM    997  O   PRO A 136      57.368  45.015  84.263  1.00 17.05           O  
ANISOU  997  O   PRO A 136     2389   2268   1821      8    243   -214       O  
ATOM    998  CB  PRO A 136      56.676  45.363  87.375  1.00 23.39           C  
ANISOU  998  CB  PRO A 136     3315   3150   2422   -116    359   -322       C  
ATOM    999  CG  PRO A 136      55.463  44.733  87.961  1.00 25.30           C  
ANISOU  999  CG  PRO A 136     3539   3448   2624   -136    428   -328       C  
ATOM   1000  CD  PRO A 136      54.636  44.266  86.801  1.00 23.46           C  
ANISOU 1000  CD  PRO A 136     3218   3212   2485    -71    434   -289       C  
ATOM   1001  N   PRO A 137      58.018  47.070  84.901  1.00 18.78           N  
ANISOU 1001  N   PRO A 137     2689   2421   2027     -3    283   -314       N  
ATOM   1002  CA  PRO A 137      59.169  47.058  84.016  1.00 19.86           C  
ANISOU 1002  CA  PRO A 137     2815   2532   2201     -3    206   -273       C  
ATOM   1003  C   PRO A 137      60.178  46.023  84.476  1.00 18.71           C  
ANISOU 1003  C   PRO A 137     2678   2436   1996    -60    129   -229       C  
ATOM   1004  O   PRO A 137      60.148  45.593  85.642  1.00 20.14           O  
ANISOU 1004  O   PRO A 137     2898   2662   2093   -112    131   -236       O  
ATOM   1005  CB  PRO A 137      59.743  48.482  84.155  1.00 24.57           C  
ANISOU 1005  CB  PRO A 137     3465   3068   2803    -16    224   -333       C  
ATOM   1006  CG  PRO A 137      58.716  49.275  84.875  1.00 25.37           C  
ANISOU 1006  CG  PRO A 137     3598   3147   2894      2    317   -405       C  
ATOM   1007  CD  PRO A 137      57.945  48.305  85.700  1.00 18.88           C  
ANISOU 1007  CD  PRO A 137     2763   2399   2013    -19    345   -400       C  
ATOM   1008  N   PRO A 138      61.109  45.623  83.611  1.00 17.30           N  
ANISOU 1008  N   PRO A 138     2466   2252   1857    -52     61   -184       N  
ATOM   1009  CA  PRO A 138      62.201  44.759  84.074  1.00 17.07           C  
ANISOU 1009  CA  PRO A 138     2440   2264   1782    -95    -18   -145       C  
ATOM   1010  C   PRO A 138      62.981  45.451  85.172  1.00 18.20           C  
ANISOU 1010  C   PRO A 138     2639   2424   1850   -162    -35   -187       C  
ATOM   1011  O   PRO A 138      63.039  46.684  85.240  1.00 18.41           O  
ANISOU 1011  O   PRO A 138     2698   2415   1880   -176      3   -247       O  
ATOM   1012  CB  PRO A 138      63.081  44.565  82.831  1.00 19.57           C  
ANISOU 1012  CB  PRO A 138     2703   2564   2168    -67    -69   -112       C  
ATOM   1013  CG  PRO A 138      62.369  45.207  81.703  1.00 18.93           C  
ANISOU 1013  CG  PRO A 138     2597   2437   2157    -17    -21   -123       C  
ATOM   1014  CD  PRO A 138      61.283  46.075  82.222  1.00 17.53           C  
ANISOU 1014  CD  PRO A 138     2455   2237   1968     -6     54   -171       C  
ATOM   1015  N   GLU A 139      63.583  44.642  86.044  1.00 20.97           N  
ANISOU 1015  N   GLU A 139     3007   2829   2132   -207    -95   -153       N  
ATOM   1016  CA  GLU A 139      64.327  45.193  87.164  1.00 26.08           C  
ANISOU 1016  CA  GLU A 139     3707   3510   2692   -282   -123   -188       C  
ATOM   1017  C   GLU A 139      65.466  46.060  86.652  1.00 20.57           C  
ANISOU 1017  C   GLU A 139     2991   2796   2029   -301   -158   -216       C  
ATOM   1018  O   GLU A 139      66.245  45.642  85.792  1.00 27.76           O  
ANISOU 1018  O   GLU A 139     3840   3709   2999   -274   -212   -175       O  
ATOM   1019  CB  GLU A 139      64.857  44.069  88.052  1.00 30.33           C  
ANISOU 1019  CB  GLU A 139     4257   4112   3155   -319   -202   -126       C  
ATOM   1020  CG  GLU A 139      65.632  44.554  89.279  1.00 39.13           C  
ANISOU 1020  CG  GLU A 139     5425   5280   4162   -408   -244   -156       C  
ATOM   1021  CD  GLU A 139      64.851  45.559  90.107  0.70 47.90           C  
ANISOU 1021  CD  GLU A 139     6611   6385   5202   -459   -154   -243       C  
ATOM   1022  OE1 GLU A 139      63.699  45.259  90.485  0.70 52.26           O  
ANISOU 1022  OE1 GLU A 139     7191   6939   5728   -451    -84   -249       O  
ATOM   1023  OE2 GLU A 139      65.393  46.652  90.379  0.70 51.72           O1-
ANISOU 1023  OE2 GLU A 139     7126   6863   5660   -510   -147   -312       O1-
ATOM   1024  N   GLY A 140      65.559  47.273  87.193  1.00 23.84           N  
ANISOU 1024  N   GLY A 140     3461   3193   2403   -354   -120   -292       N  
ATOM   1025  CA  GLY A 140      66.576  48.208  86.764  1.00 29.22           C  
ANISOU 1025  CA  GLY A 140     4136   3853   3111   -390   -143   -325       C  
ATOM   1026  C   GLY A 140      66.135  49.185  85.701  1.00 26.65           C  
ANISOU 1026  C   GLY A 140     3813   3440   2873   -347    -77   -357       C  
ATOM   1027  O   GLY A 140      66.939  50.039  85.298  1.00 26.46           O  
ANISOU 1027  O   GLY A 140     3793   3388   2871   -385    -87   -385       O  
ATOM   1028  N   PHE A 141      64.893  49.086  85.227  1.00 19.65           N  
ANISOU 1028  N   PHE A 141     2921   2512   2035   -272    -13   -349       N  
ATOM   1029  CA  PHE A 141      64.366  49.972  84.196  1.00 18.29           C  
ANISOU 1029  CA  PHE A 141     2748   2255   1945   -219     42   -365       C  
ATOM   1030  C   PHE A 141      63.133  50.690  84.736  1.00 22.75           C  
ANISOU 1030  C   PHE A 141     3366   2772   2506   -191    134   -424       C  
ATOM   1031  O   PHE A 141      62.544  50.274  85.737  1.00 24.44           O  
ANISOU 1031  O   PHE A 141     3600   3029   2658   -205    161   -443       O  
ATOM   1032  CB  PHE A 141      64.072  49.184  82.908  1.00 16.53           C  
ANISOU 1032  CB  PHE A 141     2451   2032   1798   -147     24   -295       C  
ATOM   1033  CG  PHE A 141      65.270  48.425  82.402  1.00 17.11           C  
ANISOU 1033  CG  PHE A 141     2468   2153   1880   -167    -55   -247       C  
ATOM   1034  CD1 PHE A 141      66.162  49.009  81.507  1.00 20.87           C  
ANISOU 1034  CD1 PHE A 141     2926   2607   2398   -187    -74   -247       C  
ATOM   1035  CD2 PHE A 141      65.545  47.145  82.871  1.00 24.36           C  
ANISOU 1035  CD2 PHE A 141     3354   3137   2764   -170   -109   -205       C  
ATOM   1036  CE1 PHE A 141      67.284  48.316  81.063  1.00 18.95           C  
ANISOU 1036  CE1 PHE A 141     2620   2415   2166   -203   -139   -214       C  
ATOM   1037  CE2 PHE A 141      66.666  46.445  82.428  1.00 23.98           C  
ANISOU 1037  CE2 PHE A 141     3248   3128   2735   -176   -179   -167       C  
ATOM   1038  CZ  PHE A 141      67.535  47.036  81.523  1.00 19.25           C  
ANISOU 1038  CZ  PHE A 141     2619   2516   2180   -191   -191   -176       C  
ATOM   1039  N   ILE A 142      62.770  51.807  84.105  1.00 19.80           N  
ANISOU 1039  N   ILE A 142     3018   2309   2198   -154    185   -453       N  
ATOM   1040  CA  ILE A 142      61.790  52.723  84.683  1.00 19.38           C  
ANISOU 1040  CA  ILE A 142     3020   2194   2148   -128    275   -526       C  
ATOM   1041  C   ILE A 142      60.520  52.859  83.858  1.00 18.81           C  
ANISOU 1041  C   ILE A 142     2907   2075   2164    -17    326   -504       C  
ATOM   1042  O   ILE A 142      59.633  53.632  84.244  1.00 24.73           O  
ANISOU 1042  O   ILE A 142     3690   2771   2936     25    405   -563       O  
ATOM   1043  CB  ILE A 142      62.396  54.118  84.933  1.00 22.08           C  
ANISOU 1043  CB  ILE A 142     3448   2454   2488   -181    302   -598       C  
ATOM   1044  CG1 ILE A 142      62.797  54.759  83.604  1.00 24.74           C  
ANISOU 1044  CG1 ILE A 142     3778   2712   2909   -154    282   -559       C  
ATOM   1045  CG2 ILE A 142      63.571  54.030  85.905  1.00 24.44           C  
ANISOU 1045  CG2 ILE A 142     3785   2815   2688   -302    253   -632       C  
ATOM   1046  CD1 ILE A 142      63.291  56.191  83.747  1.00 27.51           C  
ANISOU 1046  CD1 ILE A 142     4223   2959   3269   -206    316   -626       C  
ATOM   1047  N   PHE A 143      60.391  52.156  82.739  1.00 18.39           N  
ANISOU 1047  N   PHE A 143     2781   2043   2163     32    283   -424       N  
ATOM   1048  CA  PHE A 143      59.148  52.240  81.990  1.00 20.57           C  
ANISOU 1048  CA  PHE A 143     3010   2291   2514    131    321   -399       C  
ATOM   1049  C   PHE A 143      58.872  50.927  81.280  1.00 16.92           C  
ANISOU 1049  C   PHE A 143     2464   1903   2063    155    276   -324       C  
ATOM   1050  O   PHE A 143      59.758  50.080  81.106  1.00 17.13           O  
ANISOU 1050  O   PHE A 143     2471   1978   2059    108    213   -285       O  
ATOM   1051  CB  PHE A 143      59.140  53.400  80.974  1.00 20.39           C  
ANISOU 1051  CB  PHE A 143     3011   2165   2572    179    329   -388       C  
ATOM   1052  CG  PHE A 143      60.384  53.503  80.112  1.00 20.35           C  
ANISOU 1052  CG  PHE A 143     3016   2146   2572    128    265   -345       C  
ATOM   1053  CD1 PHE A 143      61.194  54.623  80.191  1.00 23.06           C  
ANISOU 1053  CD1 PHE A 143     3437   2410   2914     77    271   -382       C  
ATOM   1054  CD2 PHE A 143      60.706  52.512  79.191  1.00 17.38           C  
ANISOU 1054  CD2 PHE A 143     2572   1831   2202    129    205   -274       C  
ATOM   1055  CE1 PHE A 143      62.330  54.740  79.376  1.00 23.50           C  
ANISOU 1055  CE1 PHE A 143     3494   2460   2973     21    219   -345       C  
ATOM   1056  CE2 PHE A 143      61.850  52.619  78.371  1.00 19.15           C  
ANISOU 1056  CE2 PHE A 143     2798   2049   2431     80    157   -242       C  
ATOM   1057  CZ  PHE A 143      62.650  53.734  78.471  1.00 21.65           C  
ANISOU 1057  CZ  PHE A 143     3185   2297   2745     25    164   -276       C  
ATOM   1058  N   GLY A 144      57.617  50.782  80.864  1.00 16.63           N  
ANISOU 1058  N   GLY A 144     2373   1872   2074    231    310   -307       N  
ATOM   1059  CA  GLY A 144      57.196  49.606  80.132  1.00 15.09           C  
ANISOU 1059  CA  GLY A 144     2100   1741   1892    251    275   -243       C  
ATOM   1060  C   GLY A 144      56.835  48.448  81.042  1.00 15.75           C  
ANISOU 1060  C   GLY A 144     2165   1905   1915    214    285   -247       C  
ATOM   1061  O   GLY A 144      56.716  48.575  82.281  1.00 16.91           O  
ANISOU 1061  O   GLY A 144     2353   2067   2005    179    327   -299       O  
ATOM   1062  N   SER A 145      56.664  47.289  80.400  1.00 14.67           N  
ANISOU 1062  N   SER A 145     1971   1818   1786    214    246   -190       N  
ATOM   1063  CA  SER A 145      56.229  46.049  81.035  1.00 14.21           C  
ANISOU 1063  CA  SER A 145     1893   1828   1679    179    250   -176       C  
ATOM   1064  C   SER A 145      57.035  44.869  80.508  1.00 13.71           C  
ANISOU 1064  C   SER A 145     1816   1788   1607    147    179   -120       C  
ATOM   1065  O   SER A 145      57.204  44.721  79.288  1.00 13.39           O  
ANISOU 1065  O   SER A 145     1738   1735   1614    173    145    -85       O  
ATOM   1066  CB  SER A 145      54.732  45.792  80.784  1.00 15.91           C  
ANISOU 1066  CB  SER A 145     2039   2078   1926    223    299   -174       C  
ATOM   1067  OG  SER A 145      53.940  46.871  81.241  1.00 19.36           O  
ANISOU 1067  OG  SER A 145     2478   2494   2386    268    370   -230       O  
ATOM   1068  N   GLU A 146      57.509  44.019  81.424  1.00 13.85           N  
ANISOU 1068  N   GLU A 146     1865   1836   1560     92    158   -110       N  
ATOM   1069  CA  GLU A 146      58.244  42.808  81.079  1.00 14.70           C  
ANISOU 1069  CA  GLU A 146     1963   1958   1663     69     94    -59       C  
ATOM   1070  C   GLU A 146      57.294  41.621  81.122  1.00 14.78           C  
ANISOU 1070  C   GLU A 146     1949   2003   1665     58    110    -30       C  
ATOM   1071  O   GLU A 146      56.504  41.497  82.064  1.00 16.92           O  
ANISOU 1071  O   GLU A 146     2236   2304   1891     32    157    -46       O  
ATOM   1072  CB  GLU A 146      59.415  42.584  82.047  1.00 17.04           C  
ANISOU 1072  CB  GLU A 146     2312   2263   1900     20     47    -54       C  
ATOM   1073  CG  GLU A 146      60.203  41.317  81.775  1.00 17.81           C  
ANISOU 1073  CG  GLU A 146     2398   2367   2002     11    -20      0       C  
ATOM   1074  CD  GLU A 146      61.390  41.139  82.706  1.00 20.65           C  
ANISOU 1074  CD  GLU A 146     2796   2742   2309    -27    -78     12       C  
ATOM   1075  OE1 GLU A 146      61.330  41.639  83.856  1.00 21.45           O  
ANISOU 1075  OE1 GLU A 146     2946   2863   2340    -68    -62    -15       O  
ATOM   1076  OE2 GLU A 146      62.366  40.472  82.289  1.00 19.69           O1-
ANISOU 1076  OE2 GLU A 146     2652   2615   2213    -17   -141     46       O1-
ATOM   1077  N   PHE A 147      57.348  40.772  80.088  1.00 13.22           N  
ANISOU 1077  N   PHE A 147     1713   1801   1508     70     77      8       N  
ATOM   1078  CA  PHE A 147      56.563  39.545  80.028  1.00 12.20           C  
ANISOU 1078  CA  PHE A 147     1566   1696   1372     47     86     36       C  
ATOM   1079  C   PHE A 147      57.481  38.351  79.819  1.00 16.00           C  
ANISOU 1079  C   PHE A 147     2068   2157   1856     30     27     77       C  
ATOM   1080  O   PHE A 147      58.489  38.439  79.114  1.00 17.79           O  
ANISOU 1080  O   PHE A 147     2285   2359   2117     53    -16     82       O  
ATOM   1081  CB  PHE A 147      55.524  39.594  78.883  1.00 14.07           C  
ANISOU 1081  CB  PHE A 147     1735   1949   1661     76    110     34       C  
ATOM   1082  CG  PHE A 147      54.590  40.751  78.995  1.00 14.01           C  
ANISOU 1082  CG  PHE A 147     1696   1958   1668    112    164     -1       C  
ATOM   1083  CD1 PHE A 147      53.560  40.736  79.914  1.00 15.63           C  
ANISOU 1083  CD1 PHE A 147     1894   2203   1843     94    224    -24       C  
ATOM   1084  CD2 PHE A 147      54.788  41.886  78.226  1.00 16.70           C  
ANISOU 1084  CD2 PHE A 147     2021   2271   2055    165    157    -12       C  
ATOM   1085  CE1 PHE A 147      52.712  41.825  80.043  1.00 16.40           C  
ANISOU 1085  CE1 PHE A 147     1955   2311   1964    139    279    -64       C  
ATOM   1086  CE2 PHE A 147      53.951  42.974  78.348  1.00 17.71           C  
ANISOU 1086  CE2 PHE A 147     2124   2398   2206    211    205    -43       C  
ATOM   1087  CZ  PHE A 147      52.910  42.948  79.251  1.00 17.85           C  
ANISOU 1087  CZ  PHE A 147     2124   2455   2202    204    267    -72       C  
ATOM   1088  N   THR A 148      57.124  37.227  80.411  1.00 13.16           N  
ANISOU 1088  N   THR A 148     1734   1803   1463    -11     28    106       N  
ATOM   1089  CA  THR A 148      57.918  36.008  80.282  1.00 15.09           C  
ANISOU 1089  CA  THR A 148     2004   2013   1717    -20    -26    149       C  
ATOM   1090  C   THR A 148      57.172  35.002  79.425  1.00 13.50           C  
ANISOU 1090  C   THR A 148     1779   1802   1549    -33    -12    161       C  
ATOM   1091  O   THR A 148      55.973  35.151  79.157  1.00 14.48           O  
ANISOU 1091  O   THR A 148     1867   1961   1674    -48     36    144       O  
ATOM   1092  CB  THR A 148      58.207  35.388  81.650  1.00 17.17           C  
ANISOU 1092  CB  THR A 148     2335   2274   1913    -62    -48    185       C  
ATOM   1093  OG1 THR A 148      56.962  34.938  82.216  1.00 18.75           O  
ANISOU 1093  OG1 THR A 148     2552   2501   2071   -113      6    191       O  
ATOM   1094  CG2 THR A 148      58.886  36.400  82.565  1.00 20.81           C  
ANISOU 1094  CG2 THR A 148     2823   2756   2327    -64    -61    166       C  
ATOM   1095  N   ARG A 149      57.902  33.963  78.996  1.00 14.31           N  
ANISOU 1095  N   ARG A 149     1899   1859   1681    -27    -55    187       N  
ATOM   1096  CA  ARG A 149      57.283  32.918  78.178  1.00 15.87           C  
ANISOU 1096  CA  ARG A 149     2086   2037   1908    -49    -42    192       C  
ATOM   1097  C   ARG A 149      56.082  32.299  78.883  1.00 13.76           C  
ANISOU 1097  C   ARG A 149     1843   1789   1598   -114     -1    209       C  
ATOM   1098  O   ARG A 149      55.050  32.032  78.244  1.00 16.43           O  
ANISOU 1098  O   ARG A 149     2143   2151   1947   -145     34    193       O  
ATOM   1099  CB  ARG A 149      58.309  31.839  77.816  1.00 16.51           C  
ANISOU 1099  CB  ARG A 149     2196   2051   2028    -30    -89    214       C  
ATOM   1100  CG  ARG A 149      57.742  30.695  76.980  1.00 16.40           C  
ANISOU 1100  CG  ARG A 149     2185   2002   2043    -60    -72    210       C  
ATOM   1101  CD  ARG A 149      58.847  29.738  76.573  1.00 18.82           C  
ANISOU 1101  CD  ARG A 149     2518   2232   2400    -26   -111    220       C  
ATOM   1102  NE  ARG A 149      59.601  30.320  75.479  1.00 19.76           N  
ANISOU 1102  NE  ARG A 149     2582   2364   2562     22   -119    179       N  
ATOM   1103  CZ  ARG A 149      60.778  29.886  75.063  1.00 20.94           C  
ANISOU 1103  CZ  ARG A 149     2728   2468   2760     70   -149    171       C  
ATOM   1104  NH1 ARG A 149      61.370  28.857  75.673  1.00 20.43           N  
ANISOU 1104  NH1 ARG A 149     2713   2334   2716     89   -182    208       N  
ATOM   1105  NH2 ARG A 149      61.359  30.486  74.035  1.00 21.34           N  
ANISOU 1105  NH2 ARG A 149     2726   2544   2840     99   -144    129       N  
ATOM   1106  N   SER A 150      56.179  32.083  80.200  1.00 16.17           N  
ANISOU 1106  N   SER A 150     2207   2091   1845   -145     -5    241       N  
ATOM   1107  CA ASER A 150      55.044  31.528  80.934  0.60 16.56           C  
ANISOU 1107  CA ASER A 150     2284   2166   1843   -220     42    256       C  
ATOM   1108  CA BSER A 150      55.046  31.529  80.934  0.40 16.87           C  
ANISOU 1108  CA BSER A 150     2323   2205   1882   -220     42    257       C  
ATOM   1109  C   SER A 150      53.799  32.393  80.771  1.00 15.46           C  
ANISOU 1109  C   SER A 150     2073   2104   1697   -231    109    210       C  
ATOM   1110  O   SER A 150      52.681  31.870  80.629  1.00 15.43           O  
ANISOU 1110  O   SER A 150     2045   2131   1687   -286    152    205       O  
ATOM   1111  CB ASER A 150      55.403  31.378  82.411  0.60 19.77           C  
ANISOU 1111  CB ASER A 150     2768   2570   2174   -254     28    297       C  
ATOM   1112  CB BSER A 150      55.408  31.381  82.410  0.40 19.78           C  
ANISOU 1112  CB BSER A 150     2770   2572   2176   -254     27    297       C  
ATOM   1113  OG ASER A 150      56.476  30.472  82.564  0.60 23.15           O  
ANISOU 1113  OG ASER A 150     3257   2925   2614   -238    -42    351       O  
ATOM   1114  OG BSER A 150      54.314  30.866  83.138  0.40 22.02           O  
ANISOU 1114  OG BSER A 150     3081   2885   2400   -337     81    312       O  
ATOM   1115  N   GLN A 151      53.964  33.721  80.801  1.00 13.28           N  
ANISOU 1115  N   GLN A 151     1760   1859   1425   -180    119    173       N  
ATOM   1116  CA  GLN A 151      52.809  34.597  80.601  1.00 12.83           C  
ANISOU 1116  CA  GLN A 151     1630   1867   1377   -171    179    130       C  
ATOM   1117  C   GLN A 151      52.310  34.529  79.165  1.00 12.55           C  
ANISOU 1117  C   GLN A 151     1521   1844   1404   -149    174    118       C  
ATOM   1118  O   GLN A 151      51.093  34.499  78.932  1.00 15.18           O  
ANISOU 1118  O   GLN A 151     1791   2233   1742   -173    217    102       O  
ATOM   1119  CB  GLN A 151      53.146  36.043  80.945  1.00 13.07           C  
ANISOU 1119  CB  GLN A 151     1652   1909   1406   -116    190     94       C  
ATOM   1120  CG  GLN A 151      53.282  36.319  82.439  1.00 14.86           C  
ANISOU 1120  CG  GLN A 151     1940   2151   1557   -151    216     87       C  
ATOM   1121  CD  GLN A 151      53.822  37.697  82.685  1.00 20.18           C  
ANISOU 1121  CD  GLN A 151     2618   2818   2233   -102    219     46       C  
ATOM   1122  OE1 GLN A 151      54.951  37.998  82.308  1.00 20.14           O  
ANISOU 1122  OE1 GLN A 151     2629   2772   2250    -69    162     54       O  
ATOM   1123  NE2 GLN A 151      53.026  38.544  83.325  1.00 19.79           N  
ANISOU 1123  NE2 GLN A 151     2552   2808   2160   -101    289     -3       N  
ATOM   1124  N   LEU A 152      53.229  34.521  78.197  1.00 12.87           N  
ANISOU 1124  N   LEU A 152     1562   1841   1488   -108    122    124       N  
ATOM   1125  CA  LEU A 152      52.807  34.439  76.802  1.00 12.61           C  
ANISOU 1125  CA  LEU A 152     1467   1824   1499    -96    114    113       C  
ATOM   1126  C   LEU A 152      52.104  33.117  76.521  1.00 13.61           C  
ANISOU 1126  C   LEU A 152     1595   1956   1621   -168    124    123       C  
ATOM   1127  O   LEU A 152      51.192  33.060  75.686  1.00 14.56           O  
ANISOU 1127  O   LEU A 152     1650   2125   1758   -186    136    109       O  
ATOM   1128  CB  LEU A 152      54.013  34.627  75.871  1.00 14.70           C  
ANISOU 1128  CB  LEU A 152     1741   2043   1800    -51     64    113       C  
ATOM   1129  CG  LEU A 152      54.708  35.973  76.003  1.00 14.35           C  
ANISOU 1129  CG  LEU A 152     1696   1994   1764      7     54    101       C  
ATOM   1130  CD1 LEU A 152      55.916  35.972  75.079  1.00 18.97           C  
ANISOU 1130  CD1 LEU A 152     2288   2541   2380     35     11    101       C  
ATOM   1131  CD2 LEU A 152      53.787  37.125  75.646  1.00 16.13           C  
ANISOU 1131  CD2 LEU A 152     1861   2264   2004     41     82     83       C  
ATOM   1132  N   ASN A 153      52.526  32.038  77.191  1.00 14.32           N  
ANISOU 1132  N   ASN A 153     1760   1993   1688   -212    115    151       N  
ATOM   1133  CA  ASN A 153      51.844  30.758  77.010  1.00 14.51           C  
ANISOU 1133  CA  ASN A 153     1800   2007   1705   -291    130    161       C  
ATOM   1134  C   ASN A 153      50.389  30.835  77.470  1.00 14.92           C  
ANISOU 1134  C   ASN A 153     1802   2142   1725   -352    188    150       C  
ATOM   1135  O   ASN A 153      49.494  30.278  76.817  1.00 15.95           O  
ANISOU 1135  O   ASN A 153     1889   2308   1864   -408    205    137       O  
ATOM   1136  CB  ASN A 153      52.577  29.655  77.776  1.00 15.16           C  
ANISOU 1136  CB  ASN A 153     1986   2005   1770   -321    108    203       C  
ATOM   1137  CG  ASN A 153      53.937  29.332  77.186  1.00 14.65           C  
ANISOU 1137  CG  ASN A 153     1956   1861   1750   -264     53    209       C  
ATOM   1138  OD1 ASN A 153      54.257  29.722  76.070  1.00 16.38           O  
ANISOU 1138  OD1 ASN A 153     2128   2088   2010   -222     39    178       O  
ATOM   1139  ND2 ASN A 153      54.753  28.601  77.957  1.00 17.78           N  
ANISOU 1139  ND2 ASN A 153     2434   2184   2138   -261     21    252       N  
ATOM   1140  N   ILE A 154      50.131  31.500  78.603  1.00 13.68           N  
ANISOU 1140  N   ILE A 154     1648   2022   1529   -348    223    149       N  
ATOM   1141  CA  ILE A 154      48.738  31.700  79.028  1.00 14.35           C  
ANISOU 1141  CA  ILE A 154     1667   2197   1590   -396    290    128       C  
ATOM   1142  C   ILE A 154      47.999  32.562  78.009  1.00 16.19           C  
ANISOU 1142  C   ILE A 154     1781   2500   1870   -346    296     93       C  
ATOM   1143  O   ILE A 154      46.866  32.261  77.627  1.00 16.44           O  
ANISOU 1143  O   ILE A 154     1737   2601   1907   -395    323     79       O  
ATOM   1144  CB  ILE A 154      48.679  32.327  80.431  1.00 15.82           C  
ANISOU 1144  CB  ILE A 154     1881   2409   1721   -397    334    122       C  
ATOM   1145  CG1 ILE A 154      49.267  31.367  81.462  1.00 18.40           C  
ANISOU 1145  CG1 ILE A 154     2326   2678   1988   -462    323    169       C  
ATOM   1146  CG2 ILE A 154      47.225  32.674  80.790  1.00 15.70           C  
ANISOU 1146  CG2 ILE A 154     1777   2497   1690   -433    414     86       C  
ATOM   1147  CD1 ILE A 154      49.591  32.034  82.798  1.00 20.34           C  
ANISOU 1147  CD1 ILE A 154     2621   2938   2169   -457    345    167       C  
ATOM   1148  N   ALA A 155      48.639  33.638  77.544  1.00 14.95           N  
ANISOU 1148  N   ALA A 155     1607   2326   1748   -252    265     83       N  
ATOM   1149  CA  ALA A 155      48.007  34.511  76.553  1.00 15.98           C  
ANISOU 1149  CA  ALA A 155     1635   2512   1923   -195    259     63       C  
ATOM   1150  C   ALA A 155      47.646  33.743  75.287  1.00 15.61           C  
ANISOU 1150  C   ALA A 155     1549   2487   1896   -236    226     69       C  
ATOM   1151  O   ALA A 155      46.572  33.953  74.711  1.00 16.82           O  
ANISOU 1151  O   ALA A 155     1604   2722   2066   -242    235     58       O  
ATOM   1152  CB  ALA A 155      48.933  35.682  76.215  1.00 15.10           C  
ANISOU 1152  CB  ALA A 155     1538   2358   1841   -100    226     61       C  
ATOM   1153  N   ILE A 156      48.531  32.849  74.839  1.00 13.18           N  
ANISOU 1153  N   ILE A 156     1314   2107   1586   -265    189     83       N  
ATOM   1154  CA  ILE A 156      48.231  32.034  73.658  1.00 14.39           C  
ANISOU 1154  CA  ILE A 156     1444   2275   1750   -317    164     77       C  
ATOM   1155  C   ILE A 156      47.001  31.168  73.904  1.00 15.32           C  
ANISOU 1155  C   ILE A 156     1526   2451   1844   -418    202     70       C  
ATOM   1156  O   ILE A 156      46.111  31.054  73.044  1.00 19.00           O  
ANISOU 1156  O   ILE A 156     1910   2992   2317   -454    195     56       O  
ATOM   1157  CB  ILE A 156      49.462  31.187  73.282  1.00 14.10           C  
ANISOU 1157  CB  ILE A 156     1501   2138   1719   -325    129     84       C  
ATOM   1158  CG1 ILE A 156      50.519  32.078  72.621  1.00 15.40           C  
ANISOU 1158  CG1 ILE A 156     1668   2274   1910   -239     91     82       C  
ATOM   1159  CG2 ILE A 156      49.065  30.057  72.348  1.00 16.85           C  
ANISOU 1159  CG2 ILE A 156     1849   2487   2067   -407    122     68       C  
ATOM   1160  CD1 ILE A 156      51.938  31.471  72.642  1.00 15.93           C  
ANISOU 1160  CD1 ILE A 156     1821   2242   1987   -223     66     87       C  
ATOM   1161  N   ASN A 157      46.914  30.571  75.094  1.00 16.50           N  
ANISOU 1161  N   ASN A 157     1734   2574   1961   -473    241     82       N  
ATOM   1162  CA  ASN A 157      45.780  29.722  75.427  1.00 16.97           C  
ANISOU 1162  CA  ASN A 157     1768   2687   1993   -585    286     77       C  
ATOM   1163  C   ASN A 157      44.469  30.501  75.421  1.00 18.87           C  
ANISOU 1163  C   ASN A 157     1871   3059   2239   -579    322     53       C  
ATOM   1164  O   ASN A 157      43.423  29.941  75.080  1.00 22.34           O  
ANISOU 1164  O   ASN A 157     2243   3574   2672   -664    340     39       O  
ATOM   1165  CB  ASN A 157      46.008  29.080  76.797  1.00 21.93           C  
ANISOU 1165  CB  ASN A 157     2495   3262   2576   -640    321    103       C  
ATOM   1166  CG  ASN A 157      44.989  28.006  77.117  1.00 29.36           C  
ANISOU 1166  CG  ASN A 157     3437   4237   3482   -777    367    104       C  
ATOM   1167  OD1 ASN A 157      44.936  26.965  76.456  1.00 35.86           O  
ANISOU 1167  OD1 ASN A 157     4294   5020   4312   -851    351    104       O  
ATOM   1168  ND2 ASN A 157      44.177  28.251  78.133  1.00 28.66           N  
ANISOU 1168  ND2 ASN A 157     3313   4222   3355   -818    431    100       N  
ATOM   1169  N   ARG A 158      44.509  31.786  75.782  1.00 18.25           N  
ANISOU 1169  N   ARG A 158     1748   3009   2178   -478    333     45       N  
ATOM   1170  CA  ARG A 158      43.313  32.618  75.873  1.00 17.39           C  
ANISOU 1170  CA  ARG A 158     1505   3015   2087   -449    372     21       C  
ATOM   1171  C   ARG A 158      43.103  33.493  74.634  1.00 20.20           C  
ANISOU 1171  C   ARG A 158     1766   3415   2494   -363    320     20       C  
ATOM   1172  O   ARG A 158      42.151  34.283  74.613  1.00 20.58           O  
ANISOU 1172  O   ARG A 158     1695   3552   2571   -315    341      5       O  
ATOM   1173  CB  ARG A 158      43.384  33.495  77.147  1.00 21.01           C  
ANISOU 1173  CB  ARG A 158     1978   3471   2532   -394    429      6       C  
ATOM   1174  CG  ARG A 158      43.654  32.688  78.457  1.00 22.10           C  
ANISOU 1174  CG  ARG A 158     2223   3569   2604   -483    475     16       C  
ATOM   1175  CD  ARG A 158      43.640  33.548  79.751  1.00 21.74           C  
ANISOU 1175  CD  ARG A 158     2192   3538   2530   -445    538     -8       C  
ATOM   1176  NE  ARG A 158      42.300  34.050  80.026  1.00 23.78           N  
ANISOU 1176  NE  ARG A 158     2322   3914   2800   -445    612    -51       N  
ATOM   1177  CZ  ARG A 158      41.560  33.748  81.089  1.00 23.80           C  
ANISOU 1177  CZ  ARG A 158     2313   3980   2750   -526    697    -72       C  
ATOM   1178  NH1 ARG A 158      42.016  32.951  82.057  1.00 26.77           N  
ANISOU 1178  NH1 ARG A 158     2812   4310   3048   -619    718    -47       N  
ATOM   1179  NH2 ARG A 158      40.352  34.270  81.187  1.00 23.74           N  
ANISOU 1179  NH2 ARG A 158     2166   4086   2768   -512    763   -118       N  
ATOM   1180  N   ASN A 159      43.955  33.353  73.606  1.00 18.64           N  
ANISOU 1180  N   ASN A 159     1617   3157   2307   -344    253     37       N  
ATOM   1181  CA  ASN A 159      43.959  34.220  72.410  1.00 18.05           C  
ANISOU 1181  CA  ASN A 159     1478   3112   2268   -264    196     47       C  
ATOM   1182  C   ASN A 159      44.034  35.700  72.794  1.00 23.60           C  
ANISOU 1182  C   ASN A 159     2151   3809   3007   -141    207     48       C  
ATOM   1183  O   ASN A 159      43.393  36.558  72.183  1.00 25.11           O  
ANISOU 1183  O   ASN A 159     2246   4061   3236    -73    185     56       O  
ATOM   1184  CB  ASN A 159      42.741  33.948  71.510  1.00 23.38           C  
ANISOU 1184  CB  ASN A 159     2031   3904   2948   -313    175     44       C  
ATOM   1185  CG  ASN A 159      42.789  32.579  70.835  1.00 29.89           C  
ANISOU 1185  CG  ASN A 159     2896   4722   3739   -435    153     36       C  
ATOM   1186  OD1 ASN A 159      43.842  31.948  70.749  1.00 35.29           O  
ANISOU 1186  OD1 ASN A 159     3697   5305   4408   -459    141     37       O  
ATOM   1187  ND2 ASN A 159      41.644  32.136  70.312  1.00 27.46           N  
ANISOU 1187  ND2 ASN A 159     2487   4524   3422   -511    147     26       N  
ATOM   1188  N   ASP A 160      44.819  36.003  73.834  1.00 20.32           N  
ANISOU 1188  N   ASP A 160     1822   3318   2580   -112    239     42       N  
ATOM   1189  CA  ASP A 160      44.935  37.355  74.395  1.00 21.52           C  
ANISOU 1189  CA  ASP A 160     1966   3451   2761     -9    263     31       C  
ATOM   1190  C   ASP A 160      46.127  38.039  73.729  1.00 20.76           C  
ANISOU 1190  C   ASP A 160     1934   3271   2682     57    208     52       C  
ATOM   1191  O   ASP A 160      47.283  37.753  74.051  1.00 18.53           O  
ANISOU 1191  O   ASP A 160     1753   2911   2376     40    197     55       O  
ATOM   1192  CB  ASP A 160      45.099  37.283  75.913  1.00 21.10           C  
ANISOU 1192  CB  ASP A 160     1973   3372   2672    -34    331      6       C  
ATOM   1193  CG  ASP A 160      45.225  38.654  76.576  1.00 27.12           C  
ANISOU 1193  CG  ASP A 160     2738   4109   3458     61    366    -20       C  
ATOM   1194  OD1 ASP A 160      45.322  39.689  75.880  1.00 22.76           O  
ANISOU 1194  OD1 ASP A 160     2155   3538   2955    153    334    -12       O  
ATOM   1195  OD2 ASP A 160      45.240  38.697  77.830  1.00 26.46           O1-
ANISOU 1195  OD2 ASP A 160     2696   4019   3337     39    426    -48       O1-
ATOM   1196  N   GLY A 161      45.846  38.929  72.778  1.00 21.36           N  
ANISOU 1196  N   GLY A 161     1948   3368   2798    130    170     69       N  
ATOM   1197  CA  GLY A 161      46.900  39.639  72.079  1.00 23.50           C  
ANISOU 1197  CA  GLY A 161     2279   3568   3082    183    121     92       C  
ATOM   1198  C   GLY A 161      47.256  40.977  72.681  1.00 27.23           C  
ANISOU 1198  C   GLY A 161     2780   3981   3584    271    144     83       C  
ATOM   1199  O   GLY A 161      48.062  41.713  72.098  1.00 28.02           O  
ANISOU 1199  O   GLY A 161     2926   4023   3698    314    107    103       O  
ATOM   1200  N   SER A 162      46.726  41.285  73.864  1.00 20.95           N  
ANISOU 1200  N   SER A 162     1970   3197   2793    289    210     47       N  
ATOM   1201  CA  SER A 162      46.764  42.637  74.409  1.00 24.94           C  
ANISOU 1201  CA  SER A 162     2488   3655   3335    378    243     26       C  
ATOM   1202  C   SER A 162      48.011  42.922  75.231  1.00 20.31           C  
ANISOU 1202  C   SER A 162     2019   2981   2717    365    257      5       C  
ATOM   1203  O   SER A 162      48.215  44.074  75.634  1.00 21.08           O  
ANISOU 1203  O   SER A 162     2146   3024   2841    429    282    -17       O  
ATOM   1204  CB  SER A 162      45.523  42.893  75.271  1.00 24.13           C  
ANISOU 1204  CB  SER A 162     2302   3614   3251    405    317    -15       C  
ATOM   1205  OG  SER A 162      45.645  42.277  76.549  1.00 27.62           O  
ANISOU 1205  OG  SER A 162     2794   4063   3639    334    379    -54       O  
ATOM   1206  N   LEU A 163      48.840  41.916  75.498  1.00 17.71           N  
ANISOU 1206  N   LEU A 163     1756   2637   2337    286    241     10       N  
ATOM   1207  CA  LEU A 163      50.001  42.156  76.351  1.00 18.24           C  
ANISOU 1207  CA  LEU A 163     1922   2636   2371    271    248     -7       C  
ATOM   1208  C   LEU A 163      50.932  43.145  75.673  1.00 20.32           C  
ANISOU 1208  C   LEU A 163     2227   2831   2663    320    208      6       C  
ATOM   1209  O   LEU A 163      51.423  44.091  76.302  1.00 19.90           O  
ANISOU 1209  O   LEU A 163     2225   2724   2611    347    229    -21       O  
ATOM   1210  CB  LEU A 163      50.723  40.839  76.650  1.00 19.75           C  
ANISOU 1210  CB  LEU A 163     2169   2823   2512    189    226      8       C  
ATOM   1211  CG  LEU A 163      50.155  39.908  77.730  1.00 24.25           C  
ANISOU 1211  CG  LEU A 163     2746   3435   3034    122    271     -4       C  
ATOM   1212  CD1 LEU A 163      48.705  39.544  77.463  1.00 35.16           C  
ANISOU 1212  CD1 LEU A 163     4032   4896   4431    109    304     -9       C  
ATOM   1213  CD2 LEU A 163      50.976  38.642  77.809  1.00 21.99           C  
ANISOU 1213  CD2 LEU A 163     2522   3123   2712     55    233     25       C  
ATOM   1214  N   SER A 164      51.108  42.986  74.365  1.00 17.95           N  
ANISOU 1214  N   SER A 164     1904   2535   2383    325    154     45       N  
ATOM   1215  CA  SER A 164      52.028  43.807  73.602  1.00 15.84           C  
ANISOU 1215  CA  SER A 164     1677   2208   2133    354    115     65       C  
ATOM   1216  C   SER A 164      51.667  43.624  72.137  1.00 19.42           C  
ANISOU 1216  C   SER A 164     2079   2697   2603    361     68    108       C  
ATOM   1217  O   SER A 164      51.618  42.488  71.665  1.00 24.88           O  
ANISOU 1217  O   SER A 164     2750   3431   3271    307     47    117       O  
ATOM   1218  CB  SER A 164      53.468  43.374  73.864  1.00 18.96           C  
ANISOU 1218  CB  SER A 164     2147   2564   2495    303     94     59       C  
ATOM   1219  OG  SER A 164      54.360  44.132  73.089  1.00 22.41           O  
ANISOU 1219  OG  SER A 164     2615   2954   2945    317     63     75       O  
ATOM   1220  N   GLN A 165      51.402  44.719  71.432  1.00 17.24           N  
ANISOU 1220  N   GLN A 165     1788   2400   2363    422     49    135       N  
ATOM   1221  CA  GLN A 165      51.030  44.646  70.021  1.00 17.25           C  
ANISOU 1221  CA  GLN A 165     1744   2441   2369    427     -4    183       C  
ATOM   1222  C   GLN A 165      52.136  45.187  69.127  1.00 19.00           C  
ANISOU 1222  C   GLN A 165     2028   2611   2581    417    -42    213       C  
ATOM   1223  O   GLN A 165      52.792  46.177  69.460  1.00 21.52           O  
ANISOU 1223  O   GLN A 165     2406   2855   2914    444    -29    208       O  
ATOM   1224  CB  GLN A 165      49.744  45.429  69.745  1.00 20.75           C  
ANISOU 1224  CB  GLN A 165     2110   2913   2859    507     -8    209       C  
ATOM   1225  CG  GLN A 165      48.605  45.088  70.684  1.00 30.37           C  
ANISOU 1225  CG  GLN A 165     3256   4188   4094    522     42    172       C  
ATOM   1226  CD  GLN A 165      47.260  45.053  69.984  1.00 53.30           C  
ANISOU 1226  CD  GLN A 165     6044   7180   7027    558     15    204       C  
ATOM   1227  OE1 GLN A 165      47.061  45.707  68.958  1.00 58.27           O  
ANISOU 1227  OE1 GLN A 165     6652   7811   7679    607    -40    257       O  
ATOM   1228  NE2 GLN A 165      46.324  44.288  70.541  1.00 61.28           N  
ANISOU 1228  NE2 GLN A 165     6979   8272   8034    529     51    174       N  
ATOM   1229  N   ASP A 166      52.312  44.555  67.972  1.00 17.08           N  
ANISOU 1229  N   ASP A 166     1771   2410   2307    372    -83    239       N  
ATOM   1230  CA  ASP A 166      53.176  45.090  66.922  1.00 15.44           C  
ANISOU 1230  CA  ASP A 166     1610   2172   2084    357   -118    273       C  
ATOM   1231  C   ASP A 166      52.289  45.831  65.933  1.00 17.76           C  
ANISOU 1231  C   ASP A 166     1865   2492   2390    404   -161    335       C  
ATOM   1232  O   ASP A 166      51.623  45.213  65.097  1.00 20.11           O  
ANISOU 1232  O   ASP A 166     2107   2868   2664    379   -197    358       O  
ATOM   1233  CB  ASP A 166      53.966  43.975  66.242  1.00 16.57           C  
ANISOU 1233  CB  ASP A 166     1768   2348   2181    277   -131    258       C  
ATOM   1234  CG  ASP A 166      54.894  44.506  65.176  1.00 19.28           C  
ANISOU 1234  CG  ASP A 166     2156   2670   2499    251   -155    286       C  
ATOM   1235  OD1 ASP A 166      55.009  45.747  65.056  1.00 16.54           O  
ANISOU 1235  OD1 ASP A 166     1842   2273   2169    289   -163    320       O  
ATOM   1236  OD2 ASP A 166      55.494  43.677  64.463  1.00 19.36           O1-
ANISOU 1236  OD2 ASP A 166     2172   2711   2472    189   -162    270       O1-
ATOM   1237  N   ASN A 167      52.265  47.160  66.027  1.00 20.42           N  
ANISOU 1237  N   ASN A 167     2233   2759   2764    470   -162    364       N  
ATOM   1238  CA  ASN A 167      51.385  47.929  65.161  1.00 23.03           C  
ANISOU 1238  CA  ASN A 167     2529   3105   3117    531   -211    434       C  
ATOM   1239  C   ASN A 167      52.042  48.365  63.860  1.00 20.19           C  
ANISOU 1239  C   ASN A 167     2223   2732   2717    496   -260    495       C  
ATOM   1240  O   ASN A 167      51.337  48.838  62.963  1.00 22.77           O  
ANISOU 1240  O   ASN A 167     2521   3087   3045    532   -316    566       O  
ATOM   1241  CB  ASN A 167      50.847  49.157  65.895  1.00 30.60           C  
ANISOU 1241  CB  ASN A 167     3492   3988   4148    635   -187    438       C  
ATOM   1242  CG  ASN A 167      49.984  48.780  67.075  1.00 34.73           C  
ANISOU 1242  CG  ASN A 167     3948   4543   4706    672   -135    381       C  
ATOM   1243  OD1 ASN A 167      50.266  49.158  68.211  1.00 37.54           O  
ANISOU 1243  OD1 ASN A 167     4343   4835   5084    691    -77    327       O  
ATOM   1244  ND2 ASN A 167      48.948  47.990  66.816  1.00 34.04           N  
ANISOU 1244  ND2 ASN A 167     3759   4560   4613    668   -153    388       N  
ATOM   1245  N   ILE A 168      53.356  48.219  63.733  1.00 17.77           N  
ANISOU 1245  N   ILE A 168     1988   2392   2372    424   -243    471       N  
ATOM   1246  CA  ILE A 168      54.064  48.549  62.502  1.00 22.49           C  
ANISOU 1246  CA  ILE A 168     2637   2987   2919    372   -277    521       C  
ATOM   1247  C   ILE A 168      54.284  47.315  61.648  1.00 19.27           C  
ANISOU 1247  C   ILE A 168     2204   2674   2446    285   -292    504       C  
ATOM   1248  O   ILE A 168      53.993  47.319  60.453  1.00 22.74           O  
ANISOU 1248  O   ILE A 168     2635   3168   2837    257   -341    557       O  
ATOM   1249  CB  ILE A 168      55.406  49.248  62.810  1.00 25.88           C  
ANISOU 1249  CB  ILE A 168     3158   3326   3349    340   -244    502       C  
ATOM   1250  CG1 ILE A 168      55.179  50.528  63.617  1.00 31.76           C  
ANISOU 1250  CG1 ILE A 168     3943   3966   4159    419   -226    513       C  
ATOM   1251  CG2 ILE A 168      56.156  49.544  61.504  1.00 26.96           C  
ANISOU 1251  CG2 ILE A 168     3347   3472   3426    271   -271    551       C  
ATOM   1252  CD1 ILE A 168      56.401  51.432  63.663  1.00 38.62           C  
ANISOU 1252  CD1 ILE A 168     4909   4743   5022    378   -204    511       C  
ATOM   1253  N   GLY A 169      54.826  46.253  62.243  1.00 17.56           N  
ANISOU 1253  N   GLY A 169     1977   2472   2221    240   -252    430       N  
ATOM   1254  CA  GLY A 169      55.012  44.997  61.550  1.00 16.95           C  
ANISOU 1254  CA  GLY A 169     1877   2470   2092    164   -255    400       C  
ATOM   1255  C   GLY A 169      56.451  44.633  61.264  1.00 14.01           C  
ANISOU 1255  C   GLY A 169     1554   2081   1687     96   -226    359       C  
ATOM   1256  O   GLY A 169      56.710  43.478  60.904  1.00 17.07           O  
ANISOU 1256  O   GLY A 169     1926   2514   2045     41   -213    314       O  
ATOM   1257  N   THR A 170      57.393  45.569  61.404  1.00 15.85           N  
ANISOU 1257  N   THR A 170     1843   2250   1929     97   -210    368       N  
ATOM   1258  CA  THR A 170      58.781  45.238  61.081  1.00 16.45           C  
ANISOU 1258  CA  THR A 170     1949   2325   1977     30   -180    327       C  
ATOM   1259  C   THR A 170      59.368  44.269  62.103  1.00 14.91           C  
ANISOU 1259  C   THR A 170     1734   2118   1812     30   -144    254       C  
ATOM   1260  O   THR A 170      60.133  43.368  61.740  1.00 13.79           O  
ANISOU 1260  O   THR A 170     1585   2004   1652    -17   -124    207       O  
ATOM   1261  CB  THR A 170      59.629  46.513  60.958  1.00 17.51           C  
ANISOU 1261  CB  THR A 170     2144   2399   2109     17   -173    357       C  
ATOM   1262  OG1 THR A 170      59.438  47.354  62.107  1.00 18.86           O  
ANISOU 1262  OG1 THR A 170     2335   2494   2337     79   -166    361       O  
ATOM   1263  CG2 THR A 170      59.260  47.295  59.698  1.00 19.99           C  
ANISOU 1263  CG2 THR A 170     2490   2729   2376     -3   -211    435       C  
ATOM   1264  N   GLY A 171      59.002  44.406  63.380  1.00 13.14           N  
ANISOU 1264  N   GLY A 171     1504   1854   1635     83   -136    243       N  
ATOM   1265  CA  GLY A 171      59.504  43.457  64.365  1.00 13.01           C  
ANISOU 1265  CA  GLY A 171     1475   1829   1640     82   -112    187       C  
ATOM   1266  C   GLY A 171      58.998  42.050  64.103  1.00 14.27           C  
ANISOU 1266  C   GLY A 171     1598   2036   1788     62   -112    161       C  
ATOM   1267  O   GLY A 171      59.734  41.068  64.266  1.00 13.63           O  
ANISOU 1267  O   GLY A 171     1514   1954   1711     39    -95    117       O  
ATOM   1268  N   THR A 172      57.736  41.936  63.680  1.00 13.38           N  
ANISOU 1268  N   THR A 172     1456   1965   1665     70   -133    189       N  
ATOM   1269  CA  THR A 172      57.193  40.633  63.313  1.00 13.02           C  
ANISOU 1269  CA  THR A 172     1380   1967   1601     34   -134    164       C  
ATOM   1270  C   THR A 172      57.884  40.074  62.077  1.00 12.87           C  
ANISOU 1270  C   THR A 172     1372   1978   1540    -28   -130    139       C  
ATOM   1271  O   THR A 172      58.211  38.882  62.035  1.00 13.06           O  
ANISOU 1271  O   THR A 172     1395   2004   1564    -59   -109     89       O  
ATOM   1272  CB  THR A 172      55.688  40.755  63.110  1.00 13.93           C  
ANISOU 1272  CB  THR A 172     1450   2131   1711     49   -161    200       C  
ATOM   1273  OG1 THR A 172      55.111  41.181  64.358  1.00 14.59           O  
ANISOU 1273  OG1 THR A 172     1520   2186   1838    107   -149    207       O  
ATOM   1274  CG2 THR A 172      55.079  39.397  62.700  1.00 14.02           C  
ANISOU 1274  CG2 THR A 172     1433   2196   1699     -5   -162    170       C  
ATOM   1275  N   LEU A 173      58.167  40.927  61.093  1.00 12.16           N  
ANISOU 1275  N   LEU A 173     1300   1907   1413    -48   -144    172       N  
ATOM   1276  CA  LEU A 173      58.897  40.466  59.909  1.00 12.64           C  
ANISOU 1276  CA  LEU A 173     1375   2004   1425   -115   -130    142       C  
ATOM   1277  C   LEU A 173      60.271  39.926  60.284  1.00 13.59           C  
ANISOU 1277  C   LEU A 173     1505   2087   1571   -123    -86     80       C  
ATOM   1278  O   LEU A 173      60.684  38.851  59.826  1.00 12.54           O  
ANISOU 1278  O   LEU A 173     1367   1970   1426   -160    -59     22       O  
ATOM   1279  CB  LEU A 173      59.044  41.605  58.904  1.00 14.80           C  
ANISOU 1279  CB  LEU A 173     1675   2299   1649   -139   -152    197       C  
ATOM   1280  CG  LEU A 173      59.390  41.103  57.509  1.00 18.93           C  
ANISOU 1280  CG  LEU A 173     2209   2886   2098   -222   -142    173       C  
ATOM   1281  CD1 LEU A 173      58.084  40.874  56.704  1.00 21.33           C  
ANISOU 1281  CD1 LEU A 173     2493   3263   2350   -248   -191    209       C  
ATOM   1282  CD2 LEU A 173      60.312  42.107  56.822  1.00 25.43           C  
ANISOU 1282  CD2 LEU A 173     3074   3707   2882   -258   -132    201       C  
ATOM   1283  N   VAL A 174      60.999  40.674  61.111  1.00 10.55           N  
ANISOU 1283  N   VAL A 174     1133   1654   1222    -89    -78     88       N  
ATOM   1284  CA  VAL A 174      62.316  40.231  61.571  1.00 11.57           C  
ANISOU 1284  CA  VAL A 174     1258   1756   1382    -89    -46     35       C  
ATOM   1285  C   VAL A 174      62.210  38.900  62.302  1.00 11.03           C  
ANISOU 1285  C   VAL A 174     1172   1667   1351    -66    -37     -7       C  
ATOM   1286  O   VAL A 174      62.958  37.956  62.023  1.00 12.32           O  
ANISOU 1286  O   VAL A 174     1326   1831   1526    -80    -11    -61       O  
ATOM   1287  CB  VAL A 174      62.951  41.306  62.468  1.00 12.89           C  
ANISOU 1287  CB  VAL A 174     1440   1881   1578    -62    -49     55       C  
ATOM   1288  CG1 VAL A 174      64.221  40.761  63.108  1.00 14.05           C  
ANISOU 1288  CG1 VAL A 174     1567   2010   1761    -56    -28      4       C  
ATOM   1289  CG2 VAL A 174      63.288  42.533  61.636  1.00 13.63           C  
ANISOU 1289  CG2 VAL A 174     1561   1982   1635    -99    -49     91       C  
ATOM   1290  N   SER A 175      61.276  38.810  63.249  1.00 11.87           N  
ANISOU 1290  N   SER A 175     1278   1753   1479    -30    -56     18       N  
ATOM   1291  CA  SER A 175      61.146  37.601  64.057  1.00 11.29           C  
ANISOU 1291  CA  SER A 175     1200   1652   1437    -14    -50    -10       C  
ATOM   1292  C   SER A 175      60.858  36.383  63.187  1.00 11.69           C  
ANISOU 1292  C   SER A 175     1247   1722   1472    -55    -36    -48       C  
ATOM   1293  O   SER A 175      61.371  35.285  63.458  1.00 13.95           O  
ANISOU 1293  O   SER A 175     1540   1973   1789    -50    -18    -89       O  
ATOM   1294  CB  SER A 175      60.037  37.808  65.086  1.00 13.97           C  
ANISOU 1294  CB  SER A 175     1539   1981   1786     15    -66     25       C  
ATOM   1295  OG  SER A 175      60.401  38.863  65.964  1.00 14.87           O  
ANISOU 1295  OG  SER A 175     1665   2069   1915     49    -71     47       O  
ATOM   1296  N   GLY A 176      60.068  36.567  62.122  1.00 12.12           N  
ANISOU 1296  N   GLY A 176     1297   1830   1479    -96    -45    -36       N  
ATOM   1297  CA  GLY A 176      59.769  35.462  61.222  1.00 12.63           C  
ANISOU 1297  CA  GLY A 176     1363   1919   1517   -150    -30    -81       C  
ATOM   1298  C   GLY A 176      60.975  35.003  60.414  1.00 12.27           C  
ANISOU 1298  C   GLY A 176     1326   1871   1465   -175      8   -142       C  
ATOM   1299  O   GLY A 176      61.141  33.804  60.155  1.00 12.74           O  
ANISOU 1299  O   GLY A 176     1395   1909   1536   -196     36   -201       O  
ATOM   1300  N   ILE A 177      61.834  35.944  60.005  1.00 11.27           N  
ANISOU 1300  N   ILE A 177     1197   1763   1324   -176     16   -133       N  
ATOM   1301  CA  ILE A 177      63.071  35.573  59.312  1.00 11.67           C  
ANISOU 1301  CA  ILE A 177     1243   1819   1373   -198     62   -197       C  
ATOM   1302  C   ILE A 177      63.932  34.711  60.219  1.00 11.44           C  
ANISOU 1302  C   ILE A 177     1202   1725   1421   -144     82   -240       C  
ATOM   1303  O   ILE A 177      64.476  33.683  59.794  1.00 13.29           O  
ANISOU 1303  O   ILE A 177     1433   1943   1674   -151    122   -309       O  
ATOM   1304  CB  ILE A 177      63.838  36.822  58.845  1.00 12.13           C  
ANISOU 1304  CB  ILE A 177     1299   1910   1401   -217     68   -173       C  
ATOM   1305  CG1 ILE A 177      63.040  37.544  57.755  1.00 13.45           C  
ANISOU 1305  CG1 ILE A 177     1487   2138   1484   -274     45   -127       C  
ATOM   1306  CG2 ILE A 177      65.250  36.437  58.309  1.00 12.50           C  
ANISOU 1306  CG2 ILE A 177     1326   1967   1458   -235    125   -247       C  
ATOM   1307  CD1 ILE A 177      63.563  38.964  57.487  1.00 15.43           C  
ANISOU 1307  CD1 ILE A 177     1751   2403   1707   -289     39    -76       C  
ATOM   1308  N   LEU A 178      64.039  35.106  61.486  1.00 12.33           N  
ANISOU 1308  N   LEU A 178     1309   1799   1577    -89     54   -199       N  
ATOM   1309  CA  LEU A 178      64.888  34.383  62.422  1.00 12.90           C  
ANISOU 1309  CA  LEU A 178     1369   1815   1718    -34     58   -224       C  
ATOM   1310  C   LEU A 178      64.293  33.028  62.791  1.00 13.33           C  
ANISOU 1310  C   LEU A 178     1446   1817   1801    -22     59   -241       C  
ATOM   1311  O   LEU A 178      65.035  32.047  62.935  1.00 14.55           O  
ANISOU 1311  O   LEU A 178     1597   1925   2007      9     78   -285       O  
ATOM   1312  CB  LEU A 178      65.086  35.213  63.696  1.00 13.84           C  
ANISOU 1312  CB  LEU A 178     1483   1915   1859      7     23   -172       C  
ATOM   1313  CG  LEU A 178      65.747  36.583  63.503  1.00 13.30           C  
ANISOU 1313  CG  LEU A 178     1401   1883   1770     -8     22   -154       C  
ATOM   1314  CD1 LEU A 178      65.922  37.267  64.870  1.00 12.75           C  
ANISOU 1314  CD1 LEU A 178     1335   1788   1723     28    -11   -115       C  
ATOM   1315  CD2 LEU A 178      67.078  36.456  62.810  1.00 16.50           C  
ANISOU 1315  CD2 LEU A 178     1769   2312   2188    -22     58   -208       C  
ATOM   1316  N   ALA A 179      62.958  32.958  62.979  1.00 12.38           N  
ANISOU 1316  N   ALA A 179     1349   1703   1653    -46     38   -207       N  
ATOM   1317  CA  ALA A 179      62.414  31.841  63.742  1.00 13.05           C  
ANISOU 1317  CA  ALA A 179     1460   1729   1768    -35     33   -205       C  
ATOM   1318  C   ALA A 179      60.985  31.437  63.401  1.00 14.19           C  
ANISOU 1318  C   ALA A 179     1622   1896   1874    -92     30   -199       C  
ATOM   1319  O   ALA A 179      60.444  30.576  64.102  1.00 15.91           O  
ANISOU 1319  O   ALA A 179     1866   2067   2112    -94     27   -191       O  
ATOM   1320  CB  ALA A 179      62.486  32.169  65.253  1.00 13.81           C  
ANISOU 1320  CB  ALA A 179     1561   1792   1893     16      0   -152       C  
ATOM   1321  N   GLY A 180      60.345  31.983  62.369  1.00 12.95           N  
ANISOU 1321  N   GLY A 180     1450   1811   1660   -142     27   -197       N  
ATOM   1322  CA  GLY A 180      58.997  31.528  62.051  1.00 12.92           C  
ANISOU 1322  CA  GLY A 180     1450   1839   1620   -200     18   -193       C  
ATOM   1323  C   GLY A 180      58.994  30.053  61.675  1.00 13.18           C  
ANISOU 1323  C   GLY A 180     1517   1825   1664   -242     49   -258       C  
ATOM   1324  O   GLY A 180      59.898  29.566  60.993  1.00 15.32           O  
ANISOU 1324  O   GLY A 180     1803   2073   1946   -246     83   -319       O  
ATOM   1325  N   ASN A 181      57.978  29.324  62.141  1.00 12.99           N  
ANISOU 1325  N   ASN A 181     1509   1785   1642   -278     44   -250       N  
ATOM   1326  CA  ASN A 181      57.957  27.879  61.923  1.00 14.40           C  
ANISOU 1326  CA  ASN A 181     1735   1897   1839   -321     75   -309       C  
ATOM   1327  C   ASN A 181      57.109  27.442  60.730  1.00 14.18           C  
ANISOU 1327  C   ASN A 181     1710   1929   1750   -423     84   -355       C  
ATOM   1328  O   ASN A 181      56.894  26.233  60.553  1.00 16.52           O  
ANISOU 1328  O   ASN A 181     2053   2170   2056   -476    111   -408       O  
ATOM   1329  CB  ASN A 181      57.500  27.160  63.193  1.00 14.46           C  
ANISOU 1329  CB  ASN A 181     1776   1833   1886   -313     71   -277       C  
ATOM   1330  CG  ASN A 181      56.060  27.474  63.553  1.00 14.29           C  
ANISOU 1330  CG  ASN A 181     1725   1879   1825   -363     48   -232       C  
ATOM   1331  OD1 ASN A 181      55.274  27.873  62.710  1.00 15.47           O  
ANISOU 1331  OD1 ASN A 181     1836   2120   1923   -416     36   -236       O  
ATOM   1332  ND2 ASN A 181      55.712  27.294  64.826  1.00 17.08           N  
ANISOU 1332  ND2 ASN A 181     2094   2194   2202   -345     42   -186       N  
ATOM   1333  N   GLY A 182      56.625  28.380  59.911  1.00 13.67           N  
ANISOU 1333  N   GLY A 182     1602   1972   1620   -454     58   -334       N  
ATOM   1334  CA  GLY A 182      55.845  28.033  58.729  1.00 14.02           C  
ANISOU 1334  CA  GLY A 182     1643   2090   1592   -556     55   -373       C  
ATOM   1335  C   GLY A 182      54.512  27.359  58.999  1.00 17.20           C  
ANISOU 1335  C   GLY A 182     2041   2513   1981   -629     41   -368       C  
ATOM   1336  O   GLY A 182      54.034  26.576  58.163  1.00 18.12           O  
ANISOU 1336  O   GLY A 182     2177   2654   2052   -727     52   -427       O  
ATOM   1337  N   ARG A 183      53.896  27.625  60.153  1.00 15.07           N  
ANISOU 1337  N   ARG A 183     1746   2237   1744   -593     21   -306       N  
ATOM   1338  CA  ARG A 183      52.655  26.931  60.489  1.00 14.87           C  
ANISOU 1338  CA  ARG A 183     1712   2232   1708   -670     16   -304       C  
ATOM   1339  C   ARG A 183      51.563  27.186  59.457  1.00 19.60           C  
ANISOU 1339  C   ARG A 183     2253   2963   2231   -757    -20   -306       C  
ATOM   1340  O   ARG A 183      50.874  26.253  59.029  1.00 20.70           O  
ANISOU 1340  O   ARG A 183     2406   3120   2339   -864    -12   -353       O  
ATOM   1341  CB  ARG A 183      52.172  27.349  61.880  1.00 15.32           C  
ANISOU 1341  CB  ARG A 183     1740   2280   1802   -618      6   -237       C  
ATOM   1342  CG  ARG A 183      50.846  26.706  62.238  1.00 21.16           C  
ANISOU 1342  CG  ARG A 183     2458   3056   2526   -705      6   -234       C  
ATOM   1343  CD  ARG A 183      51.058  25.344  62.845  1.00 29.11           C  
ANISOU 1343  CD  ARG A 183     3550   3943   3567   -747     47   -267       C  
ATOM   1344  NE  ARG A 183      51.806  25.426  64.103  1.00 33.63           N  
ANISOU 1344  NE  ARG A 183     4162   4421   4194   -658     59   -226       N  
ATOM   1345  CZ  ARG A 183      52.560  24.439  64.569  1.00 33.70           C  
ANISOU 1345  CZ  ARG A 183     4258   4299   4246   -646     85   -245       C  
ATOM   1346  NH1 ARG A 183      52.652  23.305  63.889  1.00 39.77           N  
ANISOU 1346  NH1 ARG A 183     5087   5006   5018   -715    112   -309       N  
ATOM   1347  NH2 ARG A 183      53.228  24.581  65.703  1.00 20.83           N  
ANISOU 1347  NH2 ARG A 183     2657   2599   2657   -566     84   -199       N  
ATOM   1348  N   ILE A 184      51.363  28.444  59.062  1.00 15.94           N  
ANISOU 1348  N   ILE A 184     1727   2594   1737   -716    -64   -252       N  
ATOM   1349  CA  ILE A 184      50.301  28.727  58.099  1.00 16.72           C  
ANISOU 1349  CA  ILE A 184     1764   2825   1764   -790   -112   -240       C  
ATOM   1350  C   ILE A 184      50.716  28.276  56.698  1.00 16.97           C  
ANISOU 1350  C   ILE A 184     1837   2885   1726   -873   -106   -306       C  
ATOM   1351  O   ILE A 184      49.950  27.600  55.990  1.00 22.51           O  
ANISOU 1351  O   ILE A 184     2531   3651   2369   -986   -118   -347       O  
ATOM   1352  CB  ILE A 184      49.927  30.220  58.131  1.00 17.15           C  
ANISOU 1352  CB  ILE A 184     1743   2960   1813   -712   -166   -153       C  
ATOM   1353  CG1 ILE A 184      49.443  30.610  59.529  1.00 22.63           C  
ANISOU 1353  CG1 ILE A 184     2397   3630   2572   -639   -161   -104       C  
ATOM   1354  CG2 ILE A 184      48.841  30.535  57.115  1.00 20.75           C  
ANISOU 1354  CG2 ILE A 184     2128   3558   2196   -778   -229   -129       C  
ATOM   1355  CD1 ILE A 184      49.010  32.045  59.613  1.00 23.56           C  
ANISOU 1355  CD1 ILE A 184     2443   3813   2696   -556   -207    -26       C  
ATOM   1356  N   ASN A 185      51.919  28.655  56.268  1.00 17.57           N  
ANISOU 1356  N   ASN A 185     1955   2922   1801   -825    -84   -322       N  
ATOM   1357  CA  ASN A 185      52.438  28.268  54.958  1.00 20.35           C  
ANISOU 1357  CA  ASN A 185     2350   3300   2083   -901    -64   -392       C  
ATOM   1358  C   ASN A 185      53.855  27.746  55.165  1.00 17.40           C  
ANISOU 1358  C   ASN A 185     2044   2802   1764   -853      7   -456       C  
ATOM   1359  O   ASN A 185      54.767  28.527  55.451  1.00 17.79           O  
ANISOU 1359  O   ASN A 185     2090   2822   1847   -764     14   -424       O  
ATOM   1360  CB  ASN A 185      52.410  29.456  53.998  1.00 17.42           C  
ANISOU 1360  CB  ASN A 185     1944   3040   1636   -901   -116   -338       C  
ATOM   1361  CG  ASN A 185      52.727  29.060  52.573  1.00 22.60           C  
ANISOU 1361  CG  ASN A 185     2642   3751   2194  -1005   -100   -408       C  
ATOM   1362  OD1 ASN A 185      53.505  28.136  52.340  1.00 23.92           O  
ANISOU 1362  OD1 ASN A 185     2871   3844   2371  -1036    -30   -506       O  
ATOM   1363  ND2 ASN A 185      52.120  29.750  51.613  1.00 23.95           N  
ANISOU 1363  ND2 ASN A 185     2779   4052   2270  -1057   -164   -361       N  
ATOM   1364  N   SER A 186      54.037  26.432  54.991  1.00 19.50           N  
ANISOU 1364  N   SER A 186     2370   2998   2043   -914     59   -550       N  
ATOM   1365  CA  SER A 186      55.314  25.814  55.341  1.00 19.60           C  
ANISOU 1365  CA  SER A 186     2438   2879   2129   -851    126   -609       C  
ATOM   1366  C   SER A 186      56.457  26.346  54.485  1.00 19.53           C  
ANISOU 1366  C   SER A 186     2435   2894   2092   -828    155   -643       C  
ATOM   1367  O   SER A 186      57.612  26.360  54.930  1.00 21.58           O  
ANISOU 1367  O   SER A 186     2706   3073   2421   -740    193   -657       O  
ATOM   1368  CB  SER A 186      55.206  24.296  55.204  1.00 25.94           C  
ANISOU 1368  CB  SER A 186     3311   3595   2951   -924    177   -705       C  
ATOM   1369  OG  SER A 186      55.019  23.916  53.850  1.00 31.72           O  
ANISOU 1369  OG  SER A 186     4066   4393   3593  -1038    195   -787       O  
ATOM   1370  N   GLN A 187      56.152  26.805  53.273  1.00 18.74           N  
ANISOU 1370  N   GLN A 187     2323   2910   1886   -908    136   -651       N  
ATOM   1371  CA  GLN A 187      57.182  27.342  52.386  1.00 21.42           C  
ANISOU 1371  CA  GLN A 187     2670   3286   2182   -905    168   -681       C  
ATOM   1372  C   GLN A 187      57.848  28.588  52.945  1.00 17.46           C  
ANISOU 1372  C   GLN A 187     2130   2784   1718   -802    146   -596       C  
ATOM   1373  O   GLN A 187      58.952  28.942  52.500  1.00 19.74           O  
ANISOU 1373  O   GLN A 187     2426   3075   2001   -782    188   -626       O  
ATOM   1374  CB  GLN A 187      56.587  27.693  51.026  1.00 24.71           C  
ANISOU 1374  CB  GLN A 187     3085   3841   2462  -1021    137   -686       C  
ATOM   1375  CG  GLN A 187      56.050  26.512  50.239  1.00 32.20           C  
ANISOU 1375  CG  GLN A 187     4078   4807   3349  -1148    165   -788       C  
ATOM   1376  CD  GLN A 187      55.432  26.930  48.909  1.00 40.64           C  
ANISOU 1376  CD  GLN A 187     5142   6030   4269  -1269    121   -781       C  
ATOM   1377  N   TYR A 188      57.196  29.278  53.877  1.00 15.65           N  
ANISOU 1377  N   TYR A 188     1863   2560   1525   -743     87   -497       N  
ATOM   1378  CA  TYR A 188      57.655  30.589  54.318  1.00 15.78           C  
ANISOU 1378  CA  TYR A 188     1848   2586   1563   -661     59   -414       C  
ATOM   1379  C   TYR A 188      58.434  30.556  55.635  1.00 17.13           C  
ANISOU 1379  C   TYR A 188     2015   2650   1842   -555     81   -403       C  
ATOM   1380  O   TYR A 188      58.784  31.616  56.150  1.00 17.89           O  
ANISOU 1380  O   TYR A 188     2090   2746   1962   -491     59   -338       O  
ATOM   1381  CB  TYR A 188      56.462  31.541  54.435  1.00 17.18           C  
ANISOU 1381  CB  TYR A 188     1981   2840   1705   -659    -20   -312       C  
ATOM   1382  CG  TYR A 188      55.748  31.842  53.123  1.00 16.26           C  
ANISOU 1382  CG  TYR A 188     1857   2845   1474   -752    -61   -296       C  
ATOM   1383  CD1 TYR A 188      56.341  31.594  51.887  1.00 17.33           C  
ANISOU 1383  CD1 TYR A 188     2031   3025   1529   -832    -27   -360       C  
ATOM   1384  CD2 TYR A 188      54.479  32.409  53.135  1.00 16.14           C  
ANISOU 1384  CD2 TYR A 188     1793   2907   1431   -758   -138   -215       C  
ATOM   1385  CE1 TYR A 188      55.670  31.899  50.694  1.00 19.27           C  
ANISOU 1385  CE1 TYR A 188     2274   3390   1656   -925    -74   -337       C  
ATOM   1386  CE2 TYR A 188      53.819  32.722  51.967  1.00 17.60           C  
ANISOU 1386  CE2 TYR A 188     1967   3210   1511   -838   -190   -188       C  
ATOM   1387  CZ  TYR A 188      54.408  32.460  50.751  1.00 19.00           C  
ANISOU 1387  CZ  TYR A 188     2191   3432   1597   -926   -162   -246       C  
ATOM   1388  OH  TYR A 188      53.730  32.776  49.605  1.00 22.25           O  
ANISOU 1388  OH  TYR A 188     2595   3968   1892  -1012   -222   -212       O  
ATOM   1389  N   ARG A 189      58.745  29.370  56.157  1.00 16.48           N  
ANISOU 1389  N   ARG A 189     2080   2151   2030   -507   -496   -670       N  
ATOM   1390  CA  ARG A 189      59.451  29.224  57.431  1.00 15.43           C  
ANISOU 1390  CA  ARG A 189     1945   1953   1964   -469   -379   -609       C  
ATOM   1391  C   ARG A 189      60.785  29.972  57.456  1.00 14.52           C  
ANISOU 1391  C   ARG A 189     1885   1866   1766   -384   -322   -550       C  
ATOM   1392  O   ARG A 189      61.433  30.181  56.420  1.00 16.66           O  
ANISOU 1392  O   ARG A 189     2226   2177   1927   -361   -337   -577       O  
ATOM   1393  CB  ARG A 189      59.692  27.747  57.693  1.00 17.51           C  
ANISOU 1393  CB  ARG A 189     2259   2108   2286   -508   -315   -671       C  
ATOM   1394  CG  ARG A 189      60.765  27.248  56.711  1.00 25.97           C  
ANISOU 1394  CG  ARG A 189     3445   3168   3256   -482   -292   -734       C  
ATOM   1395  CD  ARG A 189      61.313  25.857  56.885  1.00 40.24           C  
ANISOU 1395  CD  ARG A 189     5322   4859   5107   -494   -214   -792       C  
ATOM   1396  NE  ARG A 189      60.514  24.862  56.174  0.80 53.93           N  
ANISOU 1396  NE  ARG A 189     7079   6549   6863   -583   -265   -904       N  
ATOM   1397  CZ  ARG A 189      60.324  24.829  54.850  0.80 56.50           C  
ANISOU 1397  CZ  ARG A 189     7455   6923   7089   -613   -342   -992       C  
ATOM   1398  NH1 ARG A 189      59.570  23.870  54.336  0.80 55.85           N  
ANISOU 1398  NH1 ARG A 189     7390   6792   7039   -703   -391  -1100       N  
ATOM   1399  NH2 ARG A 189      60.885  25.712  54.040  0.80 57.69           N  
ANISOU 1399  NH2 ARG A 189     7646   7168   7107   -560   -370   -976       N  
ATOM   1400  N   GLY A 190      61.198  30.367  58.666  1.00 13.46           N  
ANISOU 1400  N   GLY A 190     1719   1711   1685   -343   -253   -473       N  
ATOM   1401  CA  GLY A 190      62.447  31.080  58.906  1.00 12.58           C  
ANISOU 1401  CA  GLY A 190     1639   1621   1521   -271   -198   -416       C  
ATOM   1402  C   GLY A 190      63.626  30.142  59.077  1.00 12.55           C  
ANISOU 1402  C   GLY A 190     1699   1552   1517   -243   -118   -439       C  
ATOM   1403  O   GLY A 190      63.572  28.963  58.718  1.00 16.54           O  
ANISOU 1403  O   GLY A 190     2249   1998   2039   -274   -106   -509       O  
ATOM   1404  N   ILE A 191      64.714  30.686  59.632  1.00 11.78           N  
ANISOU 1404  N   ILE A 191     1605   1464   1407   -182    -64   -382       N  
ATOM   1405  CA  ILE A 191      66.034  30.051  59.523  1.00 13.17           C  
ANISOU 1405  CA  ILE A 191     1833   1603   1568   -137      3   -402       C  
ATOM   1406  C   ILE A 191      66.300  29.057  60.657  1.00 15.34           C  
ANISOU 1406  C   ILE A 191     2111   1790   1928   -121     56   -387       C  
ATOM   1407  O   ILE A 191      66.809  27.954  60.417  1.00 16.44           O  
ANISOU 1407  O   ILE A 191     2300   1863   2082   -109     97   -434       O  
ATOM   1408  CB  ILE A 191      67.125  31.138  59.467  1.00 13.03           C  
ANISOU 1408  CB  ILE A 191     1807   1643   1500    -83     29   -352       C  
ATOM   1409  CG1 ILE A 191      66.988  31.949  58.186  1.00 13.74           C  
ANISOU 1409  CG1 ILE A 191     1921   1806   1495    -95     -8   -367       C  
ATOM   1410  CG2 ILE A 191      68.533  30.499  59.515  1.00 14.17           C  
ANISOU 1410  CG2 ILE A 191     1980   1751   1652    -29    103   -366       C  
ATOM   1411  CD1 ILE A 191      67.837  33.231  58.170  1.00 16.41           C  
ANISOU 1411  CD1 ILE A 191     2242   2199   1793    -57     16   -306       C  
ATOM   1412  N   THR A 192      65.971  29.417  61.895  1.00 14.37           N  
ANISOU 1412  N   THR A 192     1944   1660   1856   -116     60   -320       N  
ATOM   1413  CA  THR A 192      66.217  28.567  63.053  1.00 12.44           C  
ANISOU 1413  CA  THR A 192     1712   1337   1677    -95    108   -289       C  
ATOM   1414  C   THR A 192      64.916  27.912  63.498  1.00 14.65           C  
ANISOU 1414  C   THR A 192     1982   1561   2023   -161    105   -298       C  
ATOM   1415  O   THR A 192      63.823  28.451  63.286  1.00 16.01           O  
ANISOU 1415  O   THR A 192     2107   1774   2201   -212     61   -305       O  
ATOM   1416  CB  THR A 192      66.803  29.357  64.236  1.00 13.31           C  
ANISOU 1416  CB  THR A 192     1794   1474   1790    -45    122   -208       C  
ATOM   1417  OG1 THR A 192      65.794  30.207  64.817  1.00 15.44           O  
ANISOU 1417  OG1 THR A 192     2017   1779   2069    -77     97   -171       O  
ATOM   1418  CG2 THR A 192      68.010  30.195  63.809  1.00 13.72           C  
ANISOU 1418  CG2 THR A 192     1836   1590   1789      5    122   -199       C  
ATOM   1419  N   THR A 193      65.046  26.735  64.113  1.00 15.79           N  
ANISOU 1419  N   THR A 193     2167   1608   2224   -158    154   -295       N  
ATOM   1420  CA  THR A 193      63.903  26.046  64.696  1.00 16.64           C  
ANISOU 1420  CA  THR A 193     2268   1649   2406   -222    172   -293       C  
ATOM   1421  C   THR A 193      63.983  25.934  66.206  1.00 18.34           C  
ANISOU 1421  C   THR A 193     2492   1821   2655   -193    223   -207       C  
ATOM   1422  O   THR A 193      62.941  25.753  66.835  1.00 18.26           O  
ANISOU 1422  O   THR A 193     2461   1781   2698   -248    245   -186       O  
ATOM   1423  CB  THR A 193      63.730  24.626  64.117  1.00 21.68           C  
ANISOU 1423  CB  THR A 193     2961   2185   3090   -264    194   -366       C  
ATOM   1424  OG1 THR A 193      64.890  23.830  64.390  1.00 24.87           O  
ANISOU 1424  OG1 THR A 193     3432   2516   3501   -195    246   -353       O  
ATOM   1425  CG2 THR A 193      63.493  24.662  62.603  1.00 22.67           C  
ANISOU 1425  CG2 THR A 193     3090   2352   3172   -305    138   -464       C  
ATOM   1426  N   GLU A 194      65.177  26.048  66.806  1.00 14.47           N  
ANISOU 1426  N   GLU A 194     2031   1333   2133   -111    241   -156       N  
ATOM   1427  CA  GLU A 194      65.298  25.864  68.254  1.00 15.75           C  
ANISOU 1427  CA  GLU A 194     2219   1454   2310    -78    281    -73       C  
ATOM   1428  C   GLU A 194      65.954  27.042  68.970  1.00 16.68           C  
ANISOU 1428  C   GLU A 194     2312   1656   2370    -21    258    -16       C  
ATOM   1429  O   GLU A 194      66.243  26.939  70.173  1.00 19.96           O  
ANISOU 1429  O   GLU A 194     2760   2048   2777     17    281     52       O  
ATOM   1430  CB  GLU A 194      66.058  24.569  68.569  1.00 20.52           C  
ANISOU 1430  CB  GLU A 194     2898   1953   2946    -31    323    -58       C  
ATOM   1431  CG  GLU A 194      65.364  23.302  68.078  1.00 26.35           C  
ANISOU 1431  CG  GLU A 194     3675   2583   3754    -94    358   -111       C  
ATOM   1432  CD  GLU A 194      64.069  22.995  68.806  0.50 26.34           C  
ANISOU 1432  CD  GLU A 194     3670   2530   3807   -172    398    -83       C  
ATOM   1433  OE1 GLU A 194      63.848  23.522  69.921  0.50 23.55           O  
ANISOU 1433  OE1 GLU A 194     3309   2202   3435   -159    418     -7       O  
ATOM   1434  OE2 GLU A 194      63.270  22.204  68.262  0.50 28.77           O1-
ANISOU 1434  OE2 GLU A 194     3983   2769   4178   -251    415   -142       O1-
ATOM   1435  N   SER A 195      66.191  28.158  68.287  1.00 16.40           N  
ANISOU 1435  N   SER A 195     2228   1712   2292    -16    214    -40       N  
ATOM   1436  CA  SER A 195      66.646  29.366  68.962  1.00 14.74           C  
ANISOU 1436  CA  SER A 195     1990   1574   2035     20    193      6       C  
ATOM   1437  C   SER A 195      65.478  30.064  69.650  1.00 15.09           C  
ANISOU 1437  C   SER A 195     2007   1641   2086    -22    202     33       C  
ATOM   1438  O   SER A 195      64.322  29.962  69.222  1.00 20.83           O  
ANISOU 1438  O   SER A 195     2705   2360   2851    -82    206      5       O  
ATOM   1439  CB  SER A 195      67.307  30.337  67.976  1.00 13.83           C  
ANISOU 1439  CB  SER A 195     1837   1538   1879     35    154    -25       C  
ATOM   1440  OG  SER A 195      68.385  29.717  67.285  1.00 15.92           O  
ANISOU 1440  OG  SER A 195     2121   1786   2142     75    161    -55       O  
ATOM   1441  N   ASP A 196      65.783  30.772  70.736  1.00 16.65           N  
ANISOU 1441  N   ASP A 196     2211   1867   2249     11    205     83       N  
ATOM   1442  CA  ASP A 196      64.791  31.526  71.503  1.00 18.84           C  
ANISOU 1442  CA  ASP A 196     2468   2165   2526    -17    226    108       C  
ATOM   1443  C   ASP A 196      64.864  33.001  71.139  1.00 17.00           C  
ANISOU 1443  C   ASP A 196     2186   2011   2264    -11    187     95       C  
ATOM   1444  O   ASP A 196      65.958  33.544  70.970  1.00 17.98           O  
ANISOU 1444  O   ASP A 196     2311   2172   2350     27    154     95       O  
ATOM   1445  CB  ASP A 196      65.049  31.413  73.007  1.00 18.36           C  
ANISOU 1445  CB  ASP A 196     2462   2081   2431     16    259    167       C  
ATOM   1446  CG  ASP A 196      64.754  30.039  73.565  0.75 28.04           C  
ANISOU 1446  CG  ASP A 196     3749   3220   3687      7    313    198       C  
ATOM   1447  OD1 ASP A 196      63.728  29.433  73.196  0.75 29.42           O  
ANISOU 1447  OD1 ASP A 196     3906   3349   3923    -52    349    178       O  
ATOM   1448  OD2 ASP A 196      65.573  29.568  74.383  0.75 32.03           O1-
ANISOU 1448  OD2 ASP A 196     4317   3697   4155     59    314    244       O1-
ATOM   1449  N   LEU A 197      63.709  33.665  71.070  1.00 13.05           N  
ANISOU 1449  N   LEU A 197     1640   1531   1789    -47    195     89       N  
ATOM   1450  CA  LEU A 197      63.674  35.099  70.802  1.00 12.60           C  
ANISOU 1450  CA  LEU A 197     1543   1534   1710    -37    165     84       C  
ATOM   1451  C   LEU A 197      63.587  35.903  72.099  1.00 12.02           C  
ANISOU 1451  C   LEU A 197     1486   1469   1611    -18    196    116       C  
ATOM   1452  O   LEU A 197      62.795  35.588  72.997  1.00 14.28           O  
ANISOU 1452  O   LEU A 197     1785   1726   1915    -33    251    136       O  
ATOM   1453  CB  LEU A 197      62.473  35.479  69.928  1.00 12.94           C  
ANISOU 1453  CB  LEU A 197     1522   1598   1798    -74    146     60       C  
ATOM   1454  CG  LEU A 197      62.420  34.864  68.532  1.00 14.39           C  
ANISOU 1454  CG  LEU A 197     1692   1784   1992    -99    103     17       C  
ATOM   1455  CD1 LEU A 197      61.138  35.300  67.835  1.00 17.27           C  
ANISOU 1455  CD1 LEU A 197     1989   2176   2398   -133     71     -2       C  
ATOM   1456  CD2 LEU A 197      63.650  35.285  67.725  1.00 17.87           C  
ANISOU 1456  CD2 LEU A 197     2157   2260   2375    -67     67      7       C  
ATOM   1457  N   ILE A 198      64.384  36.971  72.170  1.00 13.69           N  
ANISOU 1457  N   ILE A 198     1700   1719   1782     10    167    117       N  
ATOM   1458  CA  ILE A 198      64.228  38.018  73.178  1.00 14.32           C  
ANISOU 1458  CA  ILE A 198     1792   1811   1836     23    187    130       C  
ATOM   1459  C   ILE A 198      63.788  39.262  72.427  1.00 14.76           C  
ANISOU 1459  C   ILE A 198     1798   1897   1914     18    167    115       C  
ATOM   1460  O   ILE A 198      64.518  39.755  71.564  1.00 14.83           O  
ANISOU 1460  O   ILE A 198     1794   1930   1910     24    124    105       O  
ATOM   1461  CB  ILE A 198      65.527  38.285  73.953  1.00 14.88           C  
ANISOU 1461  CB  ILE A 198     1911   1896   1847     54    164    139       C  
ATOM   1462  CG1 ILE A 198      66.049  37.006  74.611  1.00 16.87           C  
ANISOU 1462  CG1 ILE A 198     2214   2118   2076     73    171    164       C  
ATOM   1463  CG2 ILE A 198      65.300  39.393  75.004  1.00 17.94           C  
ANISOU 1463  CG2 ILE A 198     2321   2293   2201     61    185    140       C  
ATOM   1464  CD1 ILE A 198      67.511  37.136  75.044  1.00 18.72           C  
ANISOU 1464  CD1 ILE A 198     2474   2377   2264    110    120    169       C  
ATOM   1465  N   VAL A 199      62.615  39.786  72.752  1.00 12.43           N  
ANISOU 1465  N   VAL A 199     1473   1595   1653     10    203    117       N  
ATOM   1466  CA  VAL A 199      62.018  40.860  71.965  1.00 11.96           C  
ANISOU 1466  CA  VAL A 199     1361   1556   1628     14    181    110       C  
ATOM   1467  C   VAL A 199      61.873  42.107  72.829  1.00 13.13           C  
ANISOU 1467  C   VAL A 199     1522   1698   1767     36    214    112       C  
ATOM   1468  O   VAL A 199      61.393  42.031  73.961  1.00 14.70           O  
ANISOU 1468  O   VAL A 199     1744   1879   1963     38    274    115       O  
ATOM   1469  CB  VAL A 199      60.658  40.438  71.389  1.00 13.90           C  
ANISOU 1469  CB  VAL A 199     1539   1798   1942     -9    185    105       C  
ATOM   1470  CG1 VAL A 199      60.017  41.607  70.617  1.00 16.31           C  
ANISOU 1470  CG1 VAL A 199     1789   2125   2282      9    152    107       C  
ATOM   1471  CG2 VAL A 199      60.830  39.202  70.483  1.00 14.84           C  
ANISOU 1471  CG2 VAL A 199     1655   1917   2067    -37    149     90       C  
ATOM   1472  N   VAL A 200      62.301  43.252  72.301  1.00 12.52           N  
ANISOU 1472  N   VAL A 200     1441   1632   1683     50    181    109       N  
ATOM   1473  CA  VAL A 200      62.000  44.539  72.915  1.00 12.54           C  
ANISOU 1473  CA  VAL A 200     1452   1618   1694     71    212    105       C  
ATOM   1474  C   VAL A 200      61.201  45.353  71.914  1.00 14.05           C  
ANISOU 1474  C   VAL A 200     1587   1811   1942     87    191    116       C  
ATOM   1475  O   VAL A 200      61.637  45.520  70.768  1.00 15.37           O  
ANISOU 1475  O   VAL A 200     1745   1994   2100     85    137    126       O  
ATOM   1476  CB  VAL A 200      63.269  45.301  73.334  1.00 12.83           C  
ANISOU 1476  CB  VAL A 200     1544   1653   1679     73    196     92       C  
ATOM   1477  CG1 VAL A 200      62.905  46.640  74.010  1.00 14.20           C  
ANISOU 1477  CG1 VAL A 200     1736   1797   1864     91    234     77       C  
ATOM   1478  CG2 VAL A 200      64.128  44.448  74.268  1.00 13.96           C  
ANISOU 1478  CG2 VAL A 200     1738   1803   1762     65    195     85       C  
ATOM   1479  N   LYS A 201      60.038  45.843  72.339  1.00 11.20           N  
ANISOU 1479  N   LYS A 201     1189   1432   1635    107    235    116       N  
ATOM   1480  CA  LYS A 201      59.289  46.837  71.580  1.00 13.55           C  
ANISOU 1480  CA  LYS A 201     1435   1723   1989    139    215    132       C  
ATOM   1481  C   LYS A 201      59.700  48.221  72.077  1.00 16.27           C  
ANISOU 1481  C   LYS A 201     1827   2031   2325    165    242    125       C  
ATOM   1482  O   LYS A 201      59.446  48.571  73.234  1.00 15.45           O  
ANISOU 1482  O   LYS A 201     1749   1899   2222    176    309    103       O  
ATOM   1483  CB  LYS A 201      57.787  46.616  71.723  1.00 15.42           C  
ANISOU 1483  CB  LYS A 201     1589   1959   2309    152    248    134       C  
ATOM   1484  CG  LYS A 201      56.980  47.763  71.144  1.00 15.99           C  
ANISOU 1484  CG  LYS A 201     1606   2020   2449    202    230    153       C  
ATOM   1485  CD  LYS A 201      55.511  47.473  71.264  1.00 17.72           C  
ANISOU 1485  CD  LYS A 201     1721   2245   2764    215    258    153       C  
ATOM   1486  CE  LYS A 201      54.701  48.581  70.597  1.00 30.37           C  
ANISOU 1486  CE  LYS A 201     3259   3839   4443    276    225    178       C  
ATOM   1487  NZ  LYS A 201      53.248  48.394  70.827  1.00 38.65           N  
ANISOU 1487  NZ  LYS A 201     4187   4894   5603    295    259    174       N  
ATOM   1488  N   LEU A 202      60.358  48.998  71.217  1.00 14.07           N  
ANISOU 1488  N   LEU A 202     1568   1746   2033    171    195    142       N  
ATOM   1489  CA  LEU A 202      60.842  50.317  71.610  1.00 13.74           C  
ANISOU 1489  CA  LEU A 202     1575   1656   1988    186    219    133       C  
ATOM   1490  C   LEU A 202      59.714  51.340  71.640  1.00 16.44           C  
ANISOU 1490  C   LEU A 202     1885   1957   2406    239    251    145       C  
ATOM   1491  O   LEU A 202      58.728  51.250  70.893  1.00 16.76           O  
ANISOU 1491  O   LEU A 202     1855   2011   2500    269    224    175       O  
ATOM   1492  CB  LEU A 202      61.921  50.804  70.646  1.00 16.43           C  
ANISOU 1492  CB  LEU A 202     1948   1997   2299    169    172    153       C  
ATOM   1493  CG  LEU A 202      63.191  49.973  70.560  1.00 13.77           C  
ANISOU 1493  CG  LEU A 202     1636   1696   1899    124    145    140       C  
ATOM   1494  CD1 LEU A 202      64.007  50.601  69.470  1.00 21.77           C  
ANISOU 1494  CD1 LEU A 202     2667   2704   2901    113    116    166       C  
ATOM   1495  CD2 LEU A 202      63.939  50.052  71.891  1.00 16.31           C  
ANISOU 1495  CD2 LEU A 202     2005   2005   2188    103    174     97       C  
ATOM   1496  N   LYS A 203      59.873  52.331  72.521  1.00 14.61           N  
ANISOU 1496  N   LYS A 203     1703   1671   2179    252    305    117       N  
ATOM   1497  CA  LYS A 203      58.997  53.492  72.499  1.00 16.07           C  
ANISOU 1497  CA  LYS A 203     1868   1798   2438    310    340    127       C  
ATOM   1498  C   LYS A 203      59.071  54.160  71.136  1.00 15.25           C  
ANISOU 1498  C   LYS A 203     1753   1681   2360    334    278    182       C  
ATOM   1499  O   LYS A 203      60.138  54.250  70.533  1.00 17.30           O  
ANISOU 1499  O   LYS A 203     2057   1945   2570    298    238    196       O  
ATOM   1500  CB  LYS A 203      59.408  54.489  73.582  1.00 20.32           C  
ANISOU 1500  CB  LYS A 203     2484   2271   2966    311    404     78       C  
ATOM   1501  CG  LYS A 203      59.128  54.018  74.993  1.00 22.02           C  
ANISOU 1501  CG  LYS A 203     2725   2493   3151    302    477     26       C  
ATOM   1502  CD  LYS A 203      60.042  54.718  76.004  1.00 26.28           C  
ANISOU 1502  CD  LYS A 203     3365   2989   3630    275    508    -33       C  
ATOM   1503  CE  LYS A 203      59.982  56.229  75.891  1.00 27.91           C  
ANISOU 1503  CE  LYS A 203     3605   3108   3893    306    534    -46       C  
ATOM   1504  NZ  LYS A 203      61.047  56.864  76.731  1.00 30.18           N  
ANISOU 1504  NZ  LYS A 203     3990   3355   4120    261    543   -111       N  
ATOM   1505  N   SER A 204      57.933  54.628  70.646  1.00 17.75           N  
ANISOU 1505  N   SER A 204     2009   1981   2755    397    271    217       N  
ATOM   1506  CA  SER A 204      57.936  55.284  69.349  1.00 21.72           C  
ANISOU 1506  CA  SER A 204     2511   2469   3271    429    207    281       C  
ATOM   1507  C   SER A 204      57.490  56.737  69.475  1.00 20.45           C  
ANISOU 1507  C   SER A 204     2369   2216   3183    496    246    299       C  
ATOM   1508  O   SER A 204      56.801  57.144  70.424  1.00 20.74           O  
ANISOU 1508  O   SER A 204     2389   2211   3281    534    318    264       O  
ATOM   1509  CB  SER A 204      57.063  54.518  68.344  1.00 24.96           C  
ANISOU 1509  CB  SER A 204     2835   2948   3701    450    130    320       C  
ATOM   1510  OG  SER A 204      55.707  54.565  68.699  1.00 28.49           O  
ANISOU 1510  OG  SER A 204     3190   3391   4241    505    152    318       O  
ATOM   1511  N   TYR A 205      57.900  57.518  68.482  1.00 18.98           N  
ANISOU 1511  N   TYR A 205     2226   1995   2990    512    205    356       N  
ATOM   1512  CA  TYR A 205      57.672  58.948  68.410  1.00 19.77           C  
ANISOU 1512  CA  TYR A 205     2365   1993   3154    572    235    386       C  
ATOM   1513  C   TYR A 205      57.230  59.265  66.985  1.00 22.88           C  
ANISOU 1513  C   TYR A 205     2741   2394   3559    629    153    481       C  
ATOM   1514  O   TYR A 205      57.686  58.630  66.032  1.00 22.08           O  
ANISOU 1514  O   TYR A 205     2647   2359   3384    592     85    514       O  
ATOM   1515  CB  TYR A 205      58.946  59.737  68.762  1.00 21.62           C  
ANISOU 1515  CB  TYR A 205     2707   2154   3354    517    281    360       C  
ATOM   1516  CG  TYR A 205      59.638  59.314  70.060  1.00 21.92           C  
ANISOU 1516  CG  TYR A 205     2776   2203   3351    448    334    267       C  
ATOM   1517  CD1 TYR A 205      60.480  58.214  70.096  1.00 20.10           C  
ANISOU 1517  CD1 TYR A 205     2545   2055   3039    374    303    243       C  
ATOM   1518  CD2 TYR A 205      59.461  60.037  71.235  1.00 29.43           C  
ANISOU 1518  CD2 TYR A 205     3764   3079   4339    462    414    205       C  
ATOM   1519  CE1 TYR A 205      61.115  57.824  71.286  1.00 23.63           C  
ANISOU 1519  CE1 TYR A 205     3022   2514   3441    320    339    167       C  
ATOM   1520  CE2 TYR A 205      60.090  59.657  72.420  1.00 29.61           C  
ANISOU 1520  CE2 TYR A 205     3826   3118   4307    402    451    121       C  
ATOM   1521  CZ  TYR A 205      60.922  58.553  72.434  1.00 31.32           C  
ANISOU 1521  CZ  TYR A 205     4037   3421   4440    332    408    107       C  
ATOM   1522  OH  TYR A 205      61.562  58.172  73.601  1.00 30.98           O  
ANISOU 1522  OH  TYR A 205     4036   3396   4337    280    432     33       O  
ATOM   1523  N   THR A 206      56.343  60.238  66.833  1.00 22.48           N  
ANISOU 1523  N   THR A 206     2670   2275   3597    722    159    524       N  
ATOM   1524  CA ATHR A 206      55.799  60.567  65.523  0.48 23.07           C  
ANISOU 1524  CA ATHR A 206     2733   2372   3663    773     66    604       C  
ATOM   1525  CA BTHR A 206      55.801  60.568  65.521  0.52 22.98           C  
ANISOU 1525  CA BTHR A 206     2722   2360   3651    772     66    604       C  
ATOM   1526  C   THR A 206      56.069  62.022  65.171  1.00 22.68           C  
ANISOU 1526  C   THR A 206     2776   2217   3624    802     85    646       C  
ATOM   1527  O   THR A 206      56.177  62.885  66.048  1.00 22.87           O  
ANISOU 1527  O   THR A 206     2841   2150   3700    807    168    604       O  
ATOM   1528  CB ATHR A 206      54.284  60.299  65.454  0.48 28.28           C  
ANISOU 1528  CB ATHR A 206     3277   3088   4382    833     18    596       C  
ATOM   1529  CB BTHR A 206      54.286  60.320  65.438  0.52 28.41           C  
ANISOU 1529  CB BTHR A 206     3294   3102   4398    833     17    597       C  
ATOM   1530  OG1ATHR A 206      53.936  59.246  66.362  0.48 30.54           O  
ANISOU 1530  OG1ATHR A 206     3481   3431   4693    800     56    529       O  
ATOM   1531  OG1BTHR A 206      53.617  61.075  66.456  0.52 26.53           O  
ANISOU 1531  OG1BTHR A 206     3036   2799   4245    875     99    551       O  
ATOM   1532  CG2ATHR A 206      53.875  59.900  64.038  0.48 25.58           C  
ANISOU 1532  CG2ATHR A 206     2907   2823   3990    853   -110    657       C  
ATOM   1533  CG2BTHR A 206      53.972  58.843  65.595  0.52 28.70           C  
ANISOU 1533  CG2BTHR A 206     3237   3244   4422    793    -12    561       C  
ATOM   1534  N   ASP A 207      56.174  62.277  63.863  1.00 23.45           N  
ANISOU 1534  N   ASP A 207     2914   2328   3668    818      7    726       N  
ATOM   1535  CA  ASP A 207      56.230  63.628  63.300  1.00 25.14           C  
ANISOU 1535  CA  ASP A 207     3212   2449   3892    857      8    782       C  
ATOM   1536  C   ASP A 207      57.468  64.401  63.732  1.00 20.83           C  
ANISOU 1536  C   ASP A 207     2773   1802   3341    795     99    768       C  
ATOM   1537  O   ASP A 207      57.425  65.631  63.831  1.00 26.97           O  
ANISOU 1537  O   ASP A 207     3607   2475   4164    821    137    779       O  
ATOM   1538  CB  ASP A 207      54.985  64.446  63.666  1.00 29.51           C  
ANISOU 1538  CB  ASP A 207     3717   2955   4541    947     12    772       C  
ATOM   1539  CG  ASP A 207      53.694  63.794  63.229  1.00 39.19           C  
ANISOU 1539  CG  ASP A 207     4829   4276   5787   1008    -80    781       C  
ATOM   1540  OD1 ASP A 207      53.726  62.780  62.499  1.00 36.46           O  
ANISOU 1540  OD1 ASP A 207     4451   4029   5372    982   -160    799       O  
ATOM   1541  OD2 ASP A 207      52.631  64.313  63.623  1.00 45.62           O1-
ANISOU 1541  OD2 ASP A 207     5583   5063   6686   1081    -71    764       O1-
ATOM   1542  N   THR A 208      58.583  63.715  63.988  1.00 21.21           N  
ANISOU 1542  N   THR A 208     2846   1874   3338    709    133    740       N  
ATOM   1543  CA  THR A 208      59.779  64.432  64.420  1.00 19.21           C  
ANISOU 1543  CA  THR A 208     2684   1528   3087    639    215    714       C  
ATOM   1544  C   THR A 208      60.262  65.390  63.336  1.00 23.66           C  
ANISOU 1544  C   THR A 208     3338   2033   3619    631    205    794       C  
ATOM   1545  O   THR A 208      60.545  66.563  63.610  1.00 23.77           O  
ANISOU 1545  O   THR A 208     3416   1937   3679    622    260    786       O  
ATOM   1546  CB  THR A 208      60.869  63.439  64.810  1.00 18.29           C  
ANISOU 1546  CB  THR A 208     2568   1463   2919    547    240    668       C  
ATOM   1547  OG1 THR A 208      60.432  62.706  65.967  1.00 24.91           O  
ANISOU 1547  OG1 THR A 208     3336   2354   3777    541    254    574       O  
ATOM   1548  CG2 THR A 208      62.168  64.153  65.135  1.00 20.77           C  
ANISOU 1548  CG2 THR A 208     2967   1692   3234    459    311    637       C  
ATOM   1549  N   TYR A 209      60.330  64.920  62.091  1.00 21.80           N  
ANISOU 1549  N   TYR A 209     3114   1869   3301    634    136    868       N  
ATOM   1550  CA  TYR A 209      60.650  65.789  60.965  1.00 20.22           C  
ANISOU 1550  CA  TYR A 209     3002   1621   3059    635    123    951       C  
ATOM   1551  C   TYR A 209      59.535  65.910  59.943  1.00 21.72           C  
ANISOU 1551  C   TYR A 209     3181   1847   3225    726     21   1025       C  
ATOM   1552  O   TYR A 209      59.395  66.969  59.331  1.00 25.29           O  
ANISOU 1552  O   TYR A 209     3700   2224   3685    760     13   1088       O  
ATOM   1553  CB  TYR A 209      61.905  65.295  60.221  1.00 20.21           C  
ANISOU 1553  CB  TYR A 209     3056   1663   2961    546    139    979       C  
ATOM   1554  CG  TYR A 209      63.098  65.040  61.111  1.00 19.75           C  
ANISOU 1554  CG  TYR A 209     3000   1583   2920    447    225    906       C  
ATOM   1555  CD1 TYR A 209      63.751  66.089  61.746  1.00 22.99           C  
ANISOU 1555  CD1 TYR A 209     3460   1881   3396    398    304    870       C  
ATOM   1556  CD2 TYR A 209      63.573  63.753  61.308  1.00 20.51           C  
ANISOU 1556  CD2 TYR A 209     3050   1773   2970    402    219    871       C  
ATOM   1557  CE1 TYR A 209      64.848  65.852  62.564  1.00 21.97           C  
ANISOU 1557  CE1 TYR A 209     3328   1737   3284    301    368    795       C  
ATOM   1558  CE2 TYR A 209      64.666  63.506  62.125  1.00 21.47           C  
ANISOU 1558  CE2 TYR A 209     3167   1885   3106    308    283    795       C  
ATOM   1559  CZ  TYR A 209      65.300  64.561  62.743  1.00 24.90           C  
ANISOU 1559  CZ  TYR A 209     3649   2202   3609    260    358    763       C  
ATOM   1560  OH  TYR A 209      66.392  64.315  63.549  1.00 23.50           O  
ANISOU 1560  OH  TYR A 209     3456   2033   3441    159    400    673       O  
ATOM   1561  N   TYR A 210      58.746  64.857  59.738  1.00 24.03           N  
ANISOU 1561  N   TYR A 210     3389   2250   3491    763    -60   1016       N  
ATOM   1562  CA  TYR A 210      57.775  64.812  58.659  1.00 23.83           C  
ANISOU 1562  CA  TYR A 210     3352   2275   3427    837   -175   1078       C  
ATOM   1563  C   TYR A 210      56.519  64.120  59.160  1.00 22.07           C  
ANISOU 1563  C   TYR A 210     2999   2123   3263    897   -232   1028       C  
ATOM   1564  O   TYR A 210      56.600  63.119  59.871  1.00 23.63           O  
ANISOU 1564  O   TYR A 210     3123   2384   3471    858   -211    963       O  
ATOM   1565  CB  TYR A 210      58.348  64.074  57.446  1.00 23.50           C  
ANISOU 1565  CB  TYR A 210     3361   2319   3250    792   -231   1123       C  
ATOM   1566  CG  TYR A 210      57.492  64.131  56.211  1.00 25.21           C  
ANISOU 1566  CG  TYR A 210     3594   2577   3409    857   -355   1189       C  
ATOM   1567  CD1 TYR A 210      57.202  65.343  55.607  1.00 29.89           C  
ANISOU 1567  CD1 TYR A 210     4258   3083   4014    910   -378   1265       C  
ATOM   1568  CD2 TYR A 210      56.980  62.973  55.644  1.00 28.62           C  
ANISOU 1568  CD2 TYR A 210     3971   3130   3772    863   -456   1173       C  
ATOM   1569  CE1 TYR A 210      56.421  65.408  54.463  1.00 32.35           C  
ANISOU 1569  CE1 TYR A 210     4591   3431   4271    971   -504   1330       C  
ATOM   1570  CE2 TYR A 210      56.200  63.024  54.498  1.00 28.01           C  
ANISOU 1570  CE2 TYR A 210     3915   3090   3638    919   -582   1226       C  
ATOM   1571  CZ  TYR A 210      55.923  64.246  53.918  1.00 31.17           C  
ANISOU 1571  CZ  TYR A 210     4389   3404   4051    974   -609   1307       C  
ATOM   1572  OH  TYR A 210      55.145  64.327  52.782  1.00 36.21           O  
ANISOU 1572  OH  TYR A 210     5051   4074   4634   1031   -745   1367       O  
ATOM   1573  N   ALA A 211      55.361  64.659  58.779  1.00 25.26           N  
ANISOU 1573  N   ALA A 211     3373   2514   3710    991   -304   1060       N  
ATOM   1574  CA  ALA A 211      54.096  64.163  59.303  1.00 28.05           C  
ANISOU 1574  CA  ALA A 211     3592   2925   4139   1050   -345   1009       C  
ATOM   1575  C   ALA A 211      53.900  62.698  58.951  1.00 28.12           C  
ANISOU 1575  C   ALA A 211     3527   3070   4086   1015   -419    980       C  
ATOM   1576  O   ALA A 211      54.101  62.287  57.803  1.00 32.35           O  
ANISOU 1576  O   ALA A 211     4110   3665   4517   1002   -504   1022       O  
ATOM   1577  CB  ALA A 211      52.937  64.995  58.754  1.00 31.35           C  
ANISOU 1577  CB  ALA A 211     3994   3313   4604   1160   -423   1056       C  
ATOM   1578  N   GLY A 212      53.502  61.912  59.951  1.00 29.34           N  
ANISOU 1578  N   GLY A 212     3572   3270   4305    996   -384    903       N  
ATOM   1579  CA  GLY A 212      53.181  60.516  59.760  1.00 29.53           C  
ANISOU 1579  CA  GLY A 212     3511   3416   4294    961   -447    864       C  
ATOM   1580  C   GLY A 212      54.339  59.559  59.910  1.00 29.31           C  
ANISOU 1580  C   GLY A 212     3516   3429   4193    864   -409    841       C  
ATOM   1581  O   GLY A 212      54.117  58.343  59.910  1.00 34.59           O  
ANISOU 1581  O   GLY A 212     4112   4189   4842    826   -450    798       O  
ATOM   1582  N   ARG A 213      55.566  60.057  60.042  1.00 23.30           N  
ANISOU 1582  N   ARG A 213     2858   2600   3394    821   -332    863       N  
ATOM   1583  CA  ARG A 213      56.724  59.182  60.142  1.00 19.07           C  
ANISOU 1583  CA  ARG A 213     2353   2104   2787    735   -296    844       C  
ATOM   1584  C   ARG A 213      57.026  58.851  61.597  1.00 20.89           C  
ANISOU 1584  C   ARG A 213     2537   2309   3090    700   -201    775       C  
ATOM   1585  O   ARG A 213      56.897  59.702  62.484  1.00 23.74           O  
ANISOU 1585  O   ARG A 213     2905   2584   3532    725   -127    753       O  
ATOM   1586  CB  ARG A 213      57.946  59.823  59.480  1.00 19.30           C  
ANISOU 1586  CB  ARG A 213     2515   2082   2735    698   -258    900       C  
ATOM   1587  CG  ARG A 213      57.703  60.196  58.013  1.00 20.46           C  
ANISOU 1587  CG  ARG A 213     2731   2247   2797    731   -345    971       C  
ATOM   1588  CD  ARG A 213      57.500  58.956  57.137  1.00 23.54           C  
ANISOU 1588  CD  ARG A 213     3096   2759   3088    710   -441    961       C  
ATOM   1589  NE  ARG A 213      57.312  59.327  55.730  1.00 26.61           N  
ANISOU 1589  NE  ARG A 213     3568   3160   3383    739   -525   1026       N  
ATOM   1590  CZ  ARG A 213      58.298  59.644  54.892  1.00 29.04           C  
ANISOU 1590  CZ  ARG A 213     3996   3447   3589    698   -496   1078       C  
ATOM   1591  NH1 ARG A 213      59.554  59.631  55.316  1.00 26.53           N  
ANISOU 1591  NH1 ARG A 213     3722   3101   3257    627   -384   1067       N  
ATOM   1592  NH2 ARG A 213      58.027  59.990  53.632  1.00 25.84           N  
ANISOU 1592  NH2 ARG A 213     3668   3051   3101    723   -578   1141       N  
ATOM   1593  N   ILE A 214      57.436  57.609  61.829  1.00 19.50           N  
ANISOU 1593  N   ILE A 214     2332   2213   2863    626   -202    712       N  
ATOM   1594  CA  ILE A 214      57.684  57.087  63.170  1.00 19.88           C  
ANISOU 1594  CA  ILE A 214     2348   2260   2947    574   -125    621       C  
ATOM   1595  C   ILE A 214      59.177  56.890  63.364  1.00 18.86           C  
ANISOU 1595  C   ILE A 214     2298   2125   2744    486    -71    587       C  
ATOM   1596  O   ILE A 214      59.856  56.320  62.500  1.00 20.74           O  
ANISOU 1596  O   ILE A 214     2572   2416   2894    444   -105    603       O  
ATOM   1597  CB  ILE A 214      56.944  55.757  63.390  1.00 24.12           C  
ANISOU 1597  CB  ILE A 214     2784   2887   3495    556   -165    571       C  
ATOM   1598  CG1 ILE A 214      55.438  55.966  63.219  1.00 31.53           C  
ANISOU 1598  CG1 ILE A 214     3620   3835   4525    640   -219    599       C  
ATOM   1599  CG2 ILE A 214      57.245  55.207  64.773  1.00 27.42           C  
ANISOU 1599  CG2 ILE A 214     3185   3299   3933    504    -80    488       C  
ATOM   1600  CD1 ILE A 214      54.643  54.679  63.247  1.00 40.20           C  
ANISOU 1600  CD1 ILE A 214     4611   5021   5642    615   -267    556       C  
ATOM   1601  N   ASN A 215      59.682  57.304  64.526  1.00 17.24           N  
ANISOU 1601  N   ASN A 215     2115   1860   2574    458     12    535       N  
ATOM   1602  CA  ASN A 215      61.061  57.015  64.882  1.00 15.21           C  
ANISOU 1602  CA  ASN A 215     1909   1608   2261    374     54    491       C  
ATOM   1603  C   ASN A 215      61.142  56.465  66.304  1.00 14.76           C  
ANISOU 1603  C   ASN A 215     1824   1561   2224    341    101    406       C  
ATOM   1604  O   ASN A 215      60.182  56.494  67.082  1.00 16.89           O  
ANISOU 1604  O   ASN A 215     2048   1817   2552    381    123    381       O  
ATOM   1605  CB  ASN A 215      61.978  58.251  64.724  1.00 17.69           C  
ANISOU 1605  CB  ASN A 215     2309   1832   2580    355    101    519       C  
ATOM   1606  CG  ASN A 215      61.642  59.376  65.695  1.00 18.05           C  
ANISOU 1606  CG  ASN A 215     2373   1775   2710    386    161    496       C  
ATOM   1607  OD1 ASN A 215      60.805  60.232  65.406  1.00 20.56           O  
ANISOU 1607  OD1 ASN A 215     2694   2032   3085    462    158    547       O  
ATOM   1608  ND2 ASN A 215      62.303  59.381  66.857  1.00 18.50           N  
ANISOU 1608  ND2 ASN A 215     2447   1811   2773    332    214    416       N  
ATOM   1609  N   TYR A 216      62.316  55.925  66.606  1.00 14.63           N  
ANISOU 1609  N   TYR A 216     1834   1571   2153    270    116    365       N  
ATOM   1610  CA  TYR A 216      62.729  55.504  67.940  1.00 14.87           C  
ANISOU 1610  CA  TYR A 216     1863   1606   2179    232    156    290       C  
ATOM   1611  C   TYR A 216      63.820  56.452  68.431  1.00 13.09           C  
ANISOU 1611  C   TYR A 216     1700   1316   1957    189    197    264       C  
ATOM   1612  O   TYR A 216      64.200  57.402  67.745  1.00 15.65           O  
ANISOU 1612  O   TYR A 216     2065   1585   2296    187    205    304       O  
ATOM   1613  CB  TYR A 216      63.205  54.049  67.897  1.00 15.54           C  
ANISOU 1613  CB  TYR A 216     1922   1776   2206    190    127    266       C  
ATOM   1614  CG  TYR A 216      62.215  53.144  67.183  1.00 15.96           C  
ANISOU 1614  CG  TYR A 216     1918   1887   2257    218     79    292       C  
ATOM   1615  CD1 TYR A 216      60.998  52.812  67.772  1.00 16.77           C  
ANISOU 1615  CD1 TYR A 216     1966   1997   2409    252     88    277       C  
ATOM   1616  CD2 TYR A 216      62.485  52.653  65.906  1.00 21.54           C  
ANISOU 1616  CD2 TYR A 216     2629   2640   2916    208     29    326       C  
ATOM   1617  CE1 TYR A 216      60.072  51.992  67.120  1.00 18.78           C  
ANISOU 1617  CE1 TYR A 216     2158   2304   2674    269     38    294       C  
ATOM   1618  CE2 TYR A 216      61.572  51.829  65.249  1.00 23.68           C  
ANISOU 1618  CE2 TYR A 216     2851   2964   3184    227    -25    339       C  
ATOM   1619  CZ  TYR A 216      60.373  51.503  65.855  1.00 24.89           C  
ANISOU 1619  CZ  TYR A 216     2939   3123   3396    254    -24    322       C  
ATOM   1620  OH  TYR A 216      59.461  50.696  65.195  1.00 25.59           O  
ANISOU 1620  OH  TYR A 216     2969   3263   3492    264    -84    328       O  
ATOM   1621  N   SER A 217      64.340  56.191  69.631  1.00 14.31           N  
ANISOU 1621  N   SER A 217     1866   1476   2097    151    221    194       N  
ATOM   1622  CA  SER A 217      65.314  57.094  70.231  1.00 17.20           C  
ANISOU 1622  CA  SER A 217     2284   1780   2471    105    251    153       C  
ATOM   1623  C   SER A 217      66.489  56.312  70.791  1.00 16.48           C  
ANISOU 1623  C   SER A 217     2188   1745   2327     41    231    103       C  
ATOM   1624  O   SER A 217      66.297  55.241  71.375  1.00 16.37           O  
ANISOU 1624  O   SER A 217     2150   1791   2277     46    216     79       O  
ATOM   1625  CB  SER A 217      64.675  57.922  71.350  1.00 20.69           C  
ANISOU 1625  CB  SER A 217     2758   2150   2952    132    301    106       C  
ATOM   1626  OG  SER A 217      65.467  59.064  71.611  1.00 27.88           O  
ANISOU 1626  OG  SER A 217     3726   2979   3887     91    327     76       O  
ATOM   1627  N   VAL A 218      67.696  56.878  70.641  1.00 13.84           N  
ANISOU 1627  N   VAL A 218     1875   1384   1998    -18    233     90       N  
ATOM   1628  CA  VAL A 218      68.923  56.205  71.089  1.00 13.64           C  
ANISOU 1628  CA  VAL A 218     1831   1414   1937    -76    205     46       C  
ATOM   1629  C   VAL A 218      68.827  55.771  72.554  1.00 15.68           C  
ANISOU 1629  C   VAL A 218     2102   1694   2161    -75    195    -22       C  
ATOM   1630  O   VAL A 218      69.201  54.651  72.905  1.00 14.04           O  
ANISOU 1630  O   VAL A 218     1869   1557   1908    -81    161    -35       O  
ATOM   1631  CB  VAL A 218      70.146  57.112  70.865  1.00 14.15           C  
ANISOU 1631  CB  VAL A 218     1907   1433   2034   -144    217     31       C  
ATOM   1632  CG1 VAL A 218      71.359  56.622  71.671  1.00 16.15           C  
ANISOU 1632  CG1 VAL A 218     2134   1735   2267   -201    180    -33       C  
ATOM   1633  CG2 VAL A 218      70.494  57.149  69.394  1.00 16.50           C  
ANISOU 1633  CG2 VAL A 218     2191   1737   2341   -152    229    102       C  
ATOM   1634  N   SER A 219      68.377  56.660  73.444  1.00 15.18           N  
ANISOU 1634  N   SER A 219     2088   1566   2114    -68    226    -66       N  
ATOM   1635  CA ASER A 219      68.368  56.325  74.868  0.59 16.71           C  
ANISOU 1635  CA ASER A 219     2312   1779   2257    -72    221   -133       C  
ATOM   1636  CA BSER A 219      68.368  56.325  74.869  0.41 16.83           C  
ANISOU 1636  CA BSER A 219     2328   1795   2273    -72    221   -133       C  
ATOM   1637  C   SER A 219      67.575  55.049  75.125  1.00 17.02           C  
ANISOU 1637  C   SER A 219     2328   1885   2254    -27    219   -111       C  
ATOM   1638  O   SER A 219      68.023  54.160  75.865  1.00 16.12           O  
ANISOU 1638  O   SER A 219     2219   1827   2080    -39    188   -135       O  
ATOM   1639  CB ASER A 219      67.792  57.487  75.675  0.59 16.01           C  
ANISOU 1639  CB ASER A 219     2288   1604   2190    -60    272   -183       C  
ATOM   1640  CB BSER A 219      67.795  57.485  75.685  0.41 16.43           C  
ANISOU 1640  CB BSER A 219     2341   1657   2243    -60    272   -184       C  
ATOM   1641  OG ASER A 219      66.495  57.806  75.203  0.59 15.03           O  
ANISOU 1641  OG ASER A 219     2156   1441   2115      7    321   -137       O  
ATOM   1642  OG BSER A 219      68.671  58.596  75.680  0.41 21.14           O  
ANISOU 1642  OG BSER A 219     2969   2188   2875   -118    270   -221       O  
ATOM   1643  N   ASP A 220      66.389  54.940  74.513  1.00 14.14           N  
ANISOU 1643  N   ASP A 220     1937   1512   1924     26    249    -62       N  
ATOM   1644  CA  ASP A 220      65.547  53.759  74.715  1.00 14.88           C  
ANISOU 1644  CA  ASP A 220     2001   1658   1993     60    255    -43       C  
ATOM   1645  C   ASP A 220      66.189  52.521  74.115  1.00 13.54           C  
ANISOU 1645  C   ASP A 220     1793   1560   1793     40    204    -14       C  
ATOM   1646  O   ASP A 220      66.068  51.415  74.661  1.00 14.58           O  
ANISOU 1646  O   ASP A 220     1921   1735   1884     45    198    -18       O  
ATOM   1647  CB  ASP A 220      64.169  53.955  74.074  1.00 15.70           C  
ANISOU 1647  CB  ASP A 220     2067   1741   2158    115    286      1       C  
ATOM   1648  CG  ASP A 220      63.462  55.215  74.535  1.00 18.71           C  
ANISOU 1648  CG  ASP A 220     2479   2042   2587    149    343    -21       C  
ATOM   1649  OD1 ASP A 220      63.601  55.598  75.710  1.00 19.24           O  
ANISOU 1649  OD1 ASP A 220     2602   2081   2626    139    380    -81       O  
ATOM   1650  OD2 ASP A 220      62.722  55.800  73.713  1.00 21.65           O1-
ANISOU 1650  OD2 ASP A 220     2822   2380   3025    191    351     23       O1-
ATOM   1651  N   PHE A 221      66.852  52.691  72.966  1.00 13.17           N  
ANISOU 1651  N   PHE A 221     1721   1518   1764     21    175     16       N  
ATOM   1652  CA  PHE A 221      67.586  51.603  72.334  1.00 12.86           C  
ANISOU 1652  CA  PHE A 221     1648   1540   1699      4    136     35       C  
ATOM   1653  C   PHE A 221      68.720  51.105  73.217  1.00 14.61           C  
ANISOU 1653  C   PHE A 221     1879   1792   1879    -26    107     -5       C  
ATOM   1654  O   PHE A 221      68.913  49.892  73.362  1.00 13.47           O  
ANISOU 1654  O   PHE A 221     1719   1695   1704    -19     85      1       O  
ATOM   1655  CB  PHE A 221      68.134  52.089  70.998  1.00 11.94           C  
ANISOU 1655  CB  PHE A 221     1516   1415   1606    -13    128     71       C  
ATOM   1656  CG  PHE A 221      69.172  51.192  70.403  1.00 12.16           C  
ANISOU 1656  CG  PHE A 221     1514   1496   1610    -36    102     77       C  
ATOM   1657  CD1 PHE A 221      68.808  49.974  69.848  1.00 15.30           C  
ANISOU 1657  CD1 PHE A 221     1888   1939   1986    -15     87     98       C  
ATOM   1658  CD2 PHE A 221      70.499  51.580  70.370  1.00 16.81           C  
ANISOU 1658  CD2 PHE A 221     2094   2084   2207    -81     97     58       C  
ATOM   1659  CE1 PHE A 221      69.767  49.132  69.285  1.00 14.99           C  
ANISOU 1659  CE1 PHE A 221     1825   1942   1929    -30     72     98       C  
ATOM   1660  CE2 PHE A 221      71.458  50.756  69.804  1.00 17.25           C  
ANISOU 1660  CE2 PHE A 221     2114   2189   2252    -95     83     63       C  
ATOM   1661  CZ  PHE A 221      71.089  49.529  69.279  1.00 16.63           C  
ANISOU 1661  CZ  PHE A 221     2020   2152   2147    -66     73     82       C  
ATOM   1662  N   LEU A 222      69.493  52.022  73.800  1.00 12.77           N  
ANISOU 1662  N   LEU A 222     1671   1531   1650    -61    101    -46       N  
ATOM   1663  CA  LEU A 222      70.574  51.591  74.688  1.00 13.57           C  
ANISOU 1663  CA  LEU A 222     1775   1669   1712    -88     55    -87       C  
ATOM   1664  C   LEU A 222      70.036  50.838  75.900  1.00 13.90           C  
ANISOU 1664  C   LEU A 222     1857   1732   1692    -59     53   -104       C  
ATOM   1665  O   LEU A 222      70.673  49.897  76.391  1.00 13.47           O  
ANISOU 1665  O   LEU A 222     1799   1725   1595    -57     11   -107       O  
ATOM   1666  CB  LEU A 222      71.400  52.799  75.123  1.00 14.47           C  
ANISOU 1666  CB  LEU A 222     1907   1744   1845   -138     44   -139       C  
ATOM   1667  CG  LEU A 222      72.092  53.496  73.944  1.00 14.20           C  
ANISOU 1667  CG  LEU A 222     1835   1686   1874   -176     55   -117       C  
ATOM   1668  CD1 LEU A 222      72.781  54.749  74.395  1.00 16.70           C  
ANISOU 1668  CD1 LEU A 222     2173   1950   2224   -234     53   -171       C  
ATOM   1669  CD2 LEU A 222      73.059  52.554  73.223  1.00 18.36           C  
ANISOU 1669  CD2 LEU A 222     2296   2276   2404   -186     26    -93       C  
ATOM   1670  N   ALA A 223      68.888  51.270  76.429  1.00 13.26           N  
ANISOU 1670  N   ALA A 223     1819   1614   1607    -35    105   -112       N  
ATOM   1671  CA  ALA A 223      68.249  50.530  77.517  1.00 13.35           C  
ANISOU 1671  CA  ALA A 223     1873   1643   1558     -8    125   -119       C  
ATOM   1672  C   ALA A 223      67.844  49.129  77.062  1.00 13.05           C  
ANISOU 1672  C   ALA A 223     1798   1643   1518     17    125    -68       C  
ATOM   1673  O   ALA A 223      67.997  48.158  77.813  1.00 13.17           O  
ANISOU 1673  O   ALA A 223     1841   1688   1477     26    112    -64       O  
ATOM   1674  CB  ALA A 223      67.037  51.315  78.035  1.00 13.87           C  
ANISOU 1674  CB  ALA A 223     1977   1657   1636     16    199   -138       C  
ATOM   1675  N   ALA A 224      67.357  48.998  75.814  1.00 12.92           N  
ANISOU 1675  N   ALA A 224     1727   1624   1559     25    135    -30       N  
ATOM   1676  CA  ALA A 224      67.056  47.671  75.271  1.00 13.29           C  
ANISOU 1676  CA  ALA A 224     1739   1702   1608     39    129      8       C  
ATOM   1677  C   ALA A 224      68.305  46.799  75.182  1.00 13.38           C  
ANISOU 1677  C   ALA A 224     1741   1751   1591     29     76     10       C  
ATOM   1678  O   ALA A 224      68.246  45.593  75.462  1.00 13.85           O  
ANISOU 1678  O   ALA A 224     1808   1829   1627     43     72     28       O  
ATOM   1679  CB  ALA A 224      66.406  47.794  73.892  1.00 11.86           C  
ANISOU 1679  CB  ALA A 224     1508   1516   1484     46    135     39       C  
ATOM   1680  N   ILE A 225      69.444  47.382  74.781  1.00 11.82           N  
ANISOU 1680  N   ILE A 225     1523   1561   1406      5     40     -5       N  
ATOM   1681  CA  ILE A 225      70.697  46.629  74.752  1.00 14.34           C  
ANISOU 1681  CA  ILE A 225     1819   1919   1712      1     -9     -6       C  
ATOM   1682  C   ILE A 225      71.040  46.113  76.142  1.00 12.87           C  
ANISOU 1682  C   ILE A 225     1676   1748   1464     14    -40    -21       C  
ATOM   1683  O   ILE A 225      71.447  44.955  76.306  1.00 14.23           O  
ANISOU 1683  O   ILE A 225     1844   1945   1618     37    -65     -2       O  
ATOM   1684  CB  ILE A 225      71.841  47.498  74.187  1.00 12.26           C  
ANISOU 1684  CB  ILE A 225     1517   1658   1483    -34    -31    -25       C  
ATOM   1685  CG1 ILE A 225      71.562  47.868  72.732  1.00 15.81           C  
ANISOU 1685  CG1 ILE A 225     1938   2094   1976    -42      2      2       C  
ATOM   1686  CG2 ILE A 225      73.185  46.782  74.368  1.00 15.58           C  
ANISOU 1686  CG2 ILE A 225     1899   2121   1898    -34    -84    -34       C  
ATOM   1687  CD1 ILE A 225      71.669  46.676  71.780  1.00 17.06           C  
ANISOU 1687  CD1 ILE A 225     2065   2282   2136    -23      2     29       C  
ATOM   1688  N   THR A 226      70.881  46.965  77.164  1.00 12.20           N  
ANISOU 1688  N   THR A 226     1643   1649   1345      3    -37    -56       N  
ATOM   1689  CA  THR A 226      71.115  46.548  78.538  1.00 12.87           C  
ANISOU 1689  CA  THR A 226     1787   1750   1350     17    -67    -70       C  
ATOM   1690  C   THR A 226      70.211  45.386  78.918  1.00 12.51           C  
ANISOU 1690  C   THR A 226     1780   1703   1271     52    -27    -28       C  
ATOM   1691  O   THR A 226      70.667  44.407  79.519  1.00 13.19           O  
ANISOU 1691  O   THR A 226     1893   1811   1308     75    -62     -7       O  
ATOM   1692  CB  THR A 226      70.875  47.725  79.483  1.00 16.84           C  
ANISOU 1692  CB  THR A 226     2353   2229   1816     -3    -55   -122       C  
ATOM   1693  OG1 THR A 226      71.656  48.848  79.050  1.00 19.54           O  
ANISOU 1693  OG1 THR A 226     2659   2559   2205    -45    -84   -161       O  
ATOM   1694  CG2 THR A 226      71.259  47.351  80.898  1.00 17.88           C  
ANISOU 1694  CG2 THR A 226     2559   2388   1846      9    -98   -140       C  
ATOM   1695  N   TYR A 227      68.936  45.463  78.537  1.00 13.21           N  
ANISOU 1695  N   TYR A 227     1865   1761   1392     56     47    -12       N  
ATOM   1696  CA  TYR A 227      67.993  44.416  78.912  1.00 14.01           C  
ANISOU 1696  CA  TYR A 227     1996   1853   1475     77     98     24       C  
ATOM   1697  C   TYR A 227      68.356  43.081  78.266  1.00 10.97           C  
ANISOU 1697  C   TYR A 227     1577   1480   1111     90     73     62       C  
ATOM   1698  O   TYR A 227      68.406  42.053  78.951  1.00 12.75           O  
ANISOU 1698  O   TYR A 227     1847   1705   1292    110     74     90       O  
ATOM   1699  CB  TYR A 227      66.568  44.830  78.530  1.00 12.25           C  
ANISOU 1699  CB  TYR A 227     1750   1599   1305     75    176     27       C  
ATOM   1700  CG  TYR A 227      65.571  43.729  78.799  1.00 13.42           C  
ANISOU 1700  CG  TYR A 227     1909   1735   1455     85    235     62       C  
ATOM   1701  CD1 TYR A 227      65.236  43.394  80.104  1.00 14.21           C  
ANISOU 1701  CD1 TYR A 227     2088   1827   1485     95    281     69       C  
ATOM   1702  CD2 TYR A 227      64.987  43.015  77.756  1.00 13.99           C  
ANISOU 1702  CD2 TYR A 227     1918   1802   1596     79    245     87       C  
ATOM   1703  CE1 TYR A 227      64.340  42.376  80.386  1.00 15.28           C  
ANISOU 1703  CE1 TYR A 227     2235   1944   1627     96    349    105       C  
ATOM   1704  CE2 TYR A 227      64.078  41.995  78.021  1.00 15.61           C  
ANISOU 1704  CE2 TYR A 227     2128   1989   1814     77    302    115       C  
ATOM   1705  CZ  TYR A 227      63.750  41.690  79.328  1.00 15.35           C  
ANISOU 1705  CZ  TYR A 227     2169   1943   1721     84    359    126       C  
ATOM   1706  OH  TYR A 227      62.857  40.671  79.632  1.00 17.81           O  
ANISOU 1706  OH  TYR A 227     2488   2228   2050     74    429    158       O  
ATOM   1707  N   VAL A 228      68.609  43.070  76.950  1.00 12.28           N  
ANISOU 1707  N   VAL A 228     1674   1651   1340     80     55     64       N  
ATOM   1708  CA  VAL A 228      68.801  41.774  76.293  1.00 10.47           C  
ANISOU 1708  CA  VAL A 228     1420   1424   1134     93     46     92       C  
ATOM   1709  C   VAL A 228      70.126  41.159  76.730  1.00 12.70           C  
ANISOU 1709  C   VAL A 228     1712   1728   1384    116    -14     98       C  
ATOM   1710  O   VAL A 228      70.234  39.931  76.859  1.00 12.95           O  
ANISOU 1710  O   VAL A 228     1762   1749   1410    142    -15    127       O  
ATOM   1711  CB  VAL A 228      68.679  41.870  74.753  1.00 11.74           C  
ANISOU 1711  CB  VAL A 228     1518   1587   1356     79     47     89       C  
ATOM   1712  CG1 VAL A 228      67.326  42.502  74.373  1.00 12.55           C  
ANISOU 1712  CG1 VAL A 228     1605   1671   1491     65     91     88       C  
ATOM   1713  CG2 VAL A 228      69.850  42.645  74.118  1.00 12.86           C  
ANISOU 1713  CG2 VAL A 228     1622   1752   1511     68      8     70       C  
ATOM   1714  N   THR A 229      71.142  41.983  77.005  1.00 13.34           N  
ANISOU 1714  N   THR A 229     1781   1836   1452    109    -65     70       N  
ATOM   1715  CA  THR A 229      72.397  41.419  77.498  1.00 12.71           C  
ANISOU 1715  CA  THR A 229     1697   1785   1349    137   -134     76       C  
ATOM   1716  C   THR A 229      72.273  40.948  78.943  1.00 12.41           C  
ANISOU 1716  C   THR A 229     1743   1746   1226    164   -151     95       C  
ATOM   1717  O   THR A 229      72.898  39.944  79.307  1.00 16.69           O  
ANISOU 1717  O   THR A 229     2298   2295   1748    205   -192    127       O  
ATOM   1718  CB  THR A 229      73.551  42.414  77.340  1.00 12.38           C  
ANISOU 1718  CB  THR A 229     1601   1775   1329    113   -189     36       C  
ATOM   1719  OG1 THR A 229      73.262  43.650  78.020  1.00 17.19           O  
ANISOU 1719  OG1 THR A 229     2247   2379   1905     81   -188      0       O  
ATOM   1720  CG2 THR A 229      73.834  42.661  75.832  1.00 12.88           C  
ANISOU 1720  CG2 THR A 229     1587   1839   1469     92   -164     30       C  
ATOM   1721  N   ASN A 230      71.469  41.634  79.772  1.00 12.89           N  
ANISOU 1721  N   ASN A 230     1868   1796   1235    147   -116     81       N  
ATOM   1722  CA  ASN A 230      71.155  41.122  81.108  1.00 14.61           C  
ANISOU 1722  CA  ASN A 230     2184   2008   1358    172   -109    106       C  
ATOM   1723  C   ASN A 230      70.566  39.720  81.016  1.00 13.26           C  
ANISOU 1723  C   ASN A 230     2038   1804   1195    198    -61    165       C  
ATOM   1724  O   ASN A 230      70.905  38.826  81.802  1.00 16.72           O  
ANISOU 1724  O   ASN A 230     2538   2240   1574    236    -86    207       O  
ATOM   1725  CB  ASN A 230      70.143  42.033  81.819  1.00 16.29           C  
ANISOU 1725  CB  ASN A 230     2459   2205   1525    149    -44     79       C  
ATOM   1726  CG  ASN A 230      70.745  43.308  82.384  1.00 19.89           C  
ANISOU 1726  CG  ASN A 230     2933   2683   1940    127    -94     17       C  
ATOM   1727  OD1 ASN A 230      71.954  43.502  82.396  1.00 19.47           O  
ANISOU 1727  OD1 ASN A 230     2847   2664   1885    125   -187     -4       O  
ATOM   1728  ND2 ASN A 230      69.872  44.179  82.892  1.00 21.68           N  
ANISOU 1728  ND2 ASN A 230     3210   2887   2139    110    -29    -15       N  
ATOM   1729  N   ILE A 231      69.636  39.525  80.078  1.00 14.28           N  
ANISOU 1729  N   ILE A 231     2124   1903   1398    177      8    170       N  
ATOM   1730  CA  ILE A 231      68.987  38.225  79.954  1.00 15.00           C  
ANISOU 1730  CA  ILE A 231     2236   1952   1510    188     61    217       C  
ATOM   1731  C   ILE A 231      70.003  37.172  79.549  1.00 15.99           C  
ANISOU 1731  C   ILE A 231     2343   2076   1658    224      6    242       C  
ATOM   1732  O   ILE A 231      70.019  36.066  80.094  1.00 17.68           O  
ANISOU 1732  O   ILE A 231     2614   2257   1845    255     15    290       O  
ATOM   1733  CB  ILE A 231      67.826  38.301  78.942  1.00 16.69           C  
ANISOU 1733  CB  ILE A 231     2394   2142   1806    151    128    205       C  
ATOM   1734  CG1 ILE A 231      66.680  39.180  79.486  1.00 17.84           C  
ANISOU 1734  CG1 ILE A 231     2559   2281   1939    128    197    189       C  
ATOM   1735  CG2 ILE A 231      67.361  36.890  78.577  1.00 17.39           C  
ANISOU 1735  CG2 ILE A 231     2488   2185   1935    152    166    240       C  
ATOM   1736  CD1 ILE A 231      65.980  38.672  80.762  1.00 18.79           C  
ANISOU 1736  CD1 ILE A 231     2768   2375   1996    134    267    223       C  
ATOM   1737  N   ALA A 232      70.875  37.500  78.583  1.00 13.69           N  
ANISOU 1737  N   ALA A 232     1972   1812   1419    224    -45    211       N  
ATOM   1738  CA  ALA A 232      71.889  36.541  78.149  1.00 16.85           C  
ANISOU 1738  CA  ALA A 232     2342   2209   1850    265    -88    229       C  
ATOM   1739  C   ALA A 232      72.820  36.146  79.286  1.00 17.88           C  
ANISOU 1739  C   ALA A 232     2519   2357   1918    318   -158    260       C  
ATOM   1740  O   ALA A 232      73.213  34.977  79.403  1.00 20.40           O  
ANISOU 1740  O   ALA A 232     2860   2647   2245    368   -171    302       O  
ATOM   1741  CB  ALA A 232      72.693  37.123  76.984  1.00 18.34           C  
ANISOU 1741  CB  ALA A 232     2437   2432   2101    253   -117    187       C  
ATOM   1742  N   ARG A 233      73.184  37.105  80.137  1.00 17.13           N  
ANISOU 1742  N   ARG A 233     2443   2305   1760    311   -208    239       N  
ATOM   1743  CA  ARG A 233      74.024  36.800  81.293  1.00 18.47           C  
ANISOU 1743  CA  ARG A 233     2663   2501   1854    360   -291    267       C  
ATOM   1744  C   ARG A 233      73.322  35.839  82.250  1.00 22.79           C  
ANISOU 1744  C   ARG A 233     3328   3003   2326    391   -250    333       C  
ATOM   1745  O   ARG A 233      73.938  34.894  82.759  1.00 29.74           O  
ANISOU 1745  O   ARG A 233     4248   3875   3178    453   -300    386       O  
ATOM   1746  CB  ARG A 233      74.400  38.099  82.005  1.00 20.46           C  
ANISOU 1746  CB  ARG A 233     2922   2805   2046    332   -350    218       C  
ATOM   1747  CG  ARG A 233      75.564  37.957  82.961  1.00 33.78           C  
ANISOU 1747  CG  ARG A 233     4627   4539   3670    378   -471    228       C  
ATOM   1748  CD  ARG A 233      75.794  39.236  83.753  0.60 34.55           C  
ANISOU 1748  CD  ARG A 233     4749   4682   3697    338   -526    168       C  
ATOM   1749  NE  ARG A 233      76.350  40.312  82.934  0.60 33.42           N  
ANISOU 1749  NE  ARG A 233     4495   4563   3639    286   -546    100       N  
ATOM   1750  CZ  ARG A 233      75.661  41.361  82.501  0.60 36.12           C  
ANISOU 1750  CZ  ARG A 233     4830   4887   4008    225   -478     54       C  
ATOM   1751  NH1 ARG A 233      74.379  41.487  82.813  0.60 40.22           N  
ANISOU 1751  NH1 ARG A 233     5433   5368   4482    212   -386     63       N  
ATOM   1752  NH2 ARG A 233      76.257  42.294  81.767  0.60 29.07           N  
ANISOU 1752  NH2 ARG A 233     3844   4009   3193    180   -496      2       N  
ATOM   1753  N   THR A 234      72.031  36.060  82.494  1.00 17.58           N  
ANISOU 1753  N   THR A 234     2725   2313   1640    350   -155    334       N  
ATOM   1754  CA  THR A 234      71.251  35.195  83.376  1.00 19.36           C  
ANISOU 1754  CA  THR A 234     3064   2491   1801    367    -91    398       C  
ATOM   1755  C   THR A 234      71.067  33.804  82.784  1.00 18.96           C  
ANISOU 1755  C   THR A 234     3009   2374   1821    388    -48    448       C  
ATOM   1756  O   THR A 234      71.234  32.791  83.479  1.00 23.39           O  
ANISOU 1756  O   THR A 234     3654   2898   2336    436    -52    517       O  
ATOM   1757  CB  THR A 234      69.881  35.834  83.619  1.00 22.76           C  
ANISOU 1757  CB  THR A 234     3528   2906   2215    312     16    377       C  
ATOM   1758  OG1 THR A 234      70.053  37.097  84.271  1.00 33.40           O  
ANISOU 1758  OG1 THR A 234     4897   4302   3490    297    -16    328       O  
ATOM   1759  CG2 THR A 234      69.018  34.917  84.484  1.00 32.66           C  
ANISOU 1759  CG2 THR A 234     4893   4105   3412    320    105    445       C  
ATOM   1760  N   GLU A 235      70.684  33.734  81.503  1.00 18.33           N  
ANISOU 1760  N   GLU A 235     2842   2273   1848    353     -7    414       N  
ATOM   1761  CA  GLU A 235      70.439  32.449  80.864  1.00 18.31           C  
ANISOU 1761  CA  GLU A 235     2838   2201   1917    362     38    445       C  
ATOM   1762  C   GLU A 235      71.732  31.712  80.531  1.00 22.58           C  
ANISOU 1762  C   GLU A 235     3351   2739   2491    429    -38    461       C  
ATOM   1763  O   GLU A 235      71.686  30.506  80.279  1.00 23.64           O  
ANISOU 1763  O   GLU A 235     3512   2803   2668    455     -7    497       O  
ATOM   1764  CB  GLU A 235      69.606  32.630  79.586  1.00 21.49           C  
ANISOU 1764  CB  GLU A 235     3162   2588   2413    302     96    395       C  
ATOM   1765  CG  GLU A 235      68.245  33.316  79.814  1.00 26.06           C  
ANISOU 1765  CG  GLU A 235     3748   3167   2986    241    173    379       C  
ATOM   1766  CD  GLU A 235      67.210  32.444  80.534  1.00 34.08           C  
ANISOU 1766  CD  GLU A 235     4842   4116   3990    224    267    431       C  
ATOM   1767  OE1 GLU A 235      66.980  31.301  80.087  1.00 38.21           O  
ANISOU 1767  OE1 GLU A 235     5370   4574   4572    219    300    452       O  
ATOM   1768  OE2 GLU A 235      66.620  32.903  81.546  1.00 36.61           O1-
ANISOU 1768  OE2 GLU A 235     5221   4445   4243    213    315    447       O1-
ATOM   1769  N   ASN A 236      72.873  32.407  80.523  1.00 19.21           N  
ANISOU 1769  N   ASN A 236     2867   2381   2053    457   -131    433       N  
ATOM   1770  CA  ASN A 236      74.174  31.797  80.230  1.00 19.11           C  
ANISOU 1770  CA  ASN A 236     2805   2373   2081    526   -204    445       C  
ATOM   1771  C   ASN A 236      74.151  31.051  78.894  1.00 21.49           C  
ANISOU 1771  C   ASN A 236     3050   2625   2488    524   -154    423       C  
ATOM   1772  O   ASN A 236      74.563  29.893  78.788  1.00 24.60           O  
ANISOU 1772  O   ASN A 236     3463   2964   2921    582   -153    459       O  
ATOM   1773  CB  ASN A 236      74.616  30.881  81.370  1.00 27.97           C  
ANISOU 1773  CB  ASN A 236     4019   3468   3140    604   -249    525       C  
ATOM   1774  CG  ASN A 236      74.932  31.656  82.629  1.00 36.37           C  
ANISOU 1774  CG  ASN A 236     5134   4597   4087    615   -325    535       C  
ATOM   1775  OD1 ASN A 236      75.649  32.656  82.583  1.00 39.26           O  
ANISOU 1775  OD1 ASN A 236     5428   5039   4451    602   -400    482       O  
ATOM   1776  ND2 ASN A 236      74.386  31.214  83.757  1.00 42.93           N  
ANISOU 1776  ND2 ASN A 236     6081   5398   4833    617   -297    590       N  
ATOM   1777  N   LYS A 237      73.661  31.736  77.864  1.00 15.73           N  
ANISOU 1777  N   LYS A 237     2258   1915   1803    459   -113    362       N  
ATOM   1778  CA  LYS A 237      73.667  31.246  76.496  1.00 18.47           C  
ANISOU 1778  CA  LYS A 237     2551   2232   2234    449    -73    326       C  
ATOM   1779  C   LYS A 237      74.225  32.316  75.570  1.00 16.38           C  
ANISOU 1779  C   LYS A 237     2191   2036   1999    421    -95    266       C  
ATOM   1780  O   LYS A 237      74.138  33.513  75.867  1.00 16.99           O  
ANISOU 1780  O   LYS A 237     2249   2166   2040    385   -118    247       O  
ATOM   1781  CB  LYS A 237      72.252  30.867  76.025  1.00 20.72           C  
ANISOU 1781  CB  LYS A 237     2872   2461   2541    387     10    317       C  
ATOM   1782  CG  LYS A 237      71.591  29.747  76.819  1.00 26.76           C  
ANISOU 1782  CG  LYS A 237     3731   3143   3292    399     56    375       C  
ATOM   1783  CD  LYS A 237      70.286  29.303  76.163  1.00 29.31           C  
ANISOU 1783  CD  LYS A 237     4063   3410   3664    330    135    353       C  
ATOM   1784  CE  LYS A 237      69.441  28.451  77.107  1.00 47.15           C  
ANISOU 1784  CE  LYS A 237     6414   5592   5908    320    197    413       C  
ATOM   1785  NZ  LYS A 237      70.246  27.413  77.809  1.00 54.55           N  
ANISOU 1785  NZ  LYS A 237     7423   6472   6830    398    179    479       N  
ATOM   1786  N   PRO A 238      74.786  31.915  74.434  1.00 14.81           N  
ANISOU 1786  N   PRO A 238     1936   1828   1862    436    -80    234       N  
ATOM   1787  CA  PRO A 238      75.236  32.908  73.454  1.00 14.80           C  
ANISOU 1787  CA  PRO A 238     1854   1884   1885    403    -81    183       C  
ATOM   1788  C   PRO A 238      74.071  33.760  72.971  1.00 15.27           C  
ANISOU 1788  C   PRO A 238     1922   1954   1924    327    -44    158       C  
ATOM   1789  O   PRO A 238      72.933  33.302  72.907  1.00 16.51           O  
ANISOU 1789  O   PRO A 238     2127   2068   2078    299     -4    164       O  
ATOM   1790  CB  PRO A 238      75.796  32.053  72.313  1.00 14.74           C  
ANISOU 1790  CB  PRO A 238     1814   1849   1939    434    -46    157       C  
ATOM   1791  CG  PRO A 238      76.091  30.724  72.909  1.00 20.25           C  
ANISOU 1791  CG  PRO A 238     2556   2484   2655    504    -52    197       C  
ATOM   1792  CD  PRO A 238      75.057  30.536  74.000  1.00 17.03           C  
ANISOU 1792  CD  PRO A 238     2236   2042   2194    485    -51    244       C  
ATOM   1793  N   LEU A 239      74.383  34.989  72.563  1.00 13.84           N  
ANISOU 1793  N   LEU A 239     1689   1828   1742    294    -58    130       N  
ATOM   1794  CA  LEU A 239      73.379  35.967  72.171  1.00 11.72           C  
ANISOU 1794  CA  LEU A 239     1424   1572   1457    234    -33    113       C  
ATOM   1795  C   LEU A 239      73.827  36.650  70.893  1.00 11.09           C  
ANISOU 1795  C   LEU A 239     1290   1524   1399    210    -19     80       C  
ATOM   1796  O   LEU A 239      74.962  37.120  70.812  1.00 12.49           O  
ANISOU 1796  O   LEU A 239     1416   1736   1595    221    -38     70       O  
ATOM   1797  CB  LEU A 239      73.190  37.014  73.282  1.00 12.70           C  
ANISOU 1797  CB  LEU A 239     1564   1721   1539    217    -62    123       C  
ATOM   1798  CG  LEU A 239      72.332  38.213  72.893  1.00 15.37           C  
ANISOU 1798  CG  LEU A 239     1897   2071   1872    166    -39    105       C  
ATOM   1799  CD1 LEU A 239      70.883  37.773  72.704  1.00 16.33           C  
ANISOU 1799  CD1 LEU A 239     2052   2157   1996    145      4    114       C  
ATOM   1800  CD2 LEU A 239      72.461  39.330  73.952  1.00 16.30           C  
ANISOU 1800  CD2 LEU A 239     2028   2211   1955    153    -68    101       C  
ATOM   1801  N   ILE A 240      72.944  36.714  69.899  1.00 11.93           N  
ANISOU 1801  N   ILE A 240     1407   1620   1505    177     15     65       N  
ATOM   1802  CA  ILE A 240      73.190  37.542  68.720  1.00 10.46           C  
ANISOU 1802  CA  ILE A 240     1189   1464   1321    150     31     44       C  
ATOM   1803  C   ILE A 240      72.184  38.683  68.765  1.00 12.03           C  
ANISOU 1803  C   ILE A 240     1399   1672   1501    110     28     51       C  
ATOM   1804  O   ILE A 240      70.968  38.447  68.840  1.00 13.33           O  
ANISOU 1804  O   ILE A 240     1591   1815   1659     96     34     57       O  
ATOM   1805  CB  ILE A 240      73.048  36.756  67.405  1.00 11.89           C  
ANISOU 1805  CB  ILE A 240     1381   1633   1505    149     64     18       C  
ATOM   1806  CG1 ILE A 240      73.877  35.475  67.414  1.00 14.71           C  
ANISOU 1806  CG1 ILE A 240     1737   1964   1890    197     78      8       C  
ATOM   1807  CG2 ILE A 240      73.453  37.653  66.226  1.00 14.45           C  
ANISOU 1807  CG2 ILE A 240     1683   1992   1814    126     86      5       C  
ATOM   1808  CD1 ILE A 240      73.579  34.537  66.216  1.00 19.05           C  
ANISOU 1808  CD1 ILE A 240     2316   2485   2437    194    114    -28       C  
ATOM   1809  N   ILE A 241      72.686  39.915  68.727  1.00 11.61           N  
ANISOU 1809  N   ILE A 241     1320   1643   1446     92     22     51       N  
ATOM   1810  CA  ILE A 241      71.851  41.112  68.706  1.00 11.82           C  
ANISOU 1810  CA  ILE A 241     1358   1670   1463     62     23     60       C  
ATOM   1811  C   ILE A 241      71.784  41.600  67.271  1.00  9.91           C  
ANISOU 1811  C   ILE A 241     1111   1439   1215     44     44     60       C  
ATOM   1812  O   ILE A 241      72.819  41.930  66.687  1.00 13.59           O  
ANISOU 1812  O   ILE A 241     1554   1924   1687     38     61     55       O  
ATOM   1813  CB  ILE A 241      72.426  42.211  69.612  1.00 14.33           C  
ANISOU 1813  CB  ILE A 241     1664   1995   1786     51      6     58       C  
ATOM   1814  CG1 ILE A 241      72.566  41.704  71.052  1.00 12.64           C  
ANISOU 1814  CG1 ILE A 241     1468   1777   1557     72    -23     59       C  
ATOM   1815  CG2 ILE A 241      71.550  43.448  69.552  1.00 15.31           C  
ANISOU 1815  CG2 ILE A 241     1804   2105   1907     27     16     66       C  
ATOM   1816  CD1 ILE A 241      73.298  42.704  71.943  1.00 15.92           C  
ANISOU 1816  CD1 ILE A 241     1874   2206   1970     58    -53     44       C  
ATOM   1817  N   ASN A 242      70.571  41.666  66.722  1.00 11.86           N  
ANISOU 1817  N   ASN A 242     1379   1679   1448     35     42     67       N  
ATOM   1818  CA  ASN A 242      70.343  42.003  65.317  1.00 12.86           C  
ANISOU 1818  CA  ASN A 242     1516   1819   1551     24     50     72       C  
ATOM   1819  C   ASN A 242      69.856  43.451  65.267  1.00 13.71           C  
ANISOU 1819  C   ASN A 242     1629   1922   1660     12     45     99       C  
ATOM   1820  O   ASN A 242      68.774  43.763  65.778  1.00 17.83           O  
ANISOU 1820  O   ASN A 242     2150   2427   2195     16     29    109       O  
ATOM   1821  CB  ASN A 242      69.319  41.024  64.743  1.00 12.88           C  
ANISOU 1821  CB  ASN A 242     1535   1818   1540     24     34     58       C  
ATOM   1822  CG  ASN A 242      68.962  41.306  63.308  1.00 14.85           C  
ANISOU 1822  CG  ASN A 242     1807   2088   1747     14     26     61       C  
ATOM   1823  OD1 ASN A 242      69.718  41.935  62.570  1.00 16.07           O  
ANISOU 1823  OD1 ASN A 242     1973   2258   1874     11     48     72       O  
ATOM   1824  ND2 ASN A 242      67.772  40.861  62.918  1.00 17.11           N  
ANISOU 1824  ND2 ASN A 242     2098   2374   2027      7     -8     52       N  
ATOM   1825  N   LEU A 243      70.666  44.348  64.710  1.00 13.20           N  
ANISOU 1825  N   LEU A 243     1565   1862   1589     -1     67    113       N  
ATOM   1826  CA  LEU A 243      70.275  45.756  64.616  1.00 14.77           C  
ANISOU 1826  CA  LEU A 243     1777   2041   1795    -10     69    143       C  
ATOM   1827  C   LEU A 243      69.526  45.984  63.309  1.00 13.95           C  
ANISOU 1827  C   LEU A 243     1703   1945   1650     -4     59    172       C  
ATOM   1828  O   LEU A 243      70.129  46.016  62.228  1.00 13.89           O  
ANISOU 1828  O   LEU A 243     1718   1954   1604    -12     83    182       O  
ATOM   1829  CB  LEU A 243      71.480  46.684  64.714  1.00 14.72           C  
ANISOU 1829  CB  LEU A 243     1760   2024   1808    -36    101    147       C  
ATOM   1830  CG  LEU A 243      72.328  46.609  65.993  1.00 15.37           C  
ANISOU 1830  CG  LEU A 243     1808   2105   1927    -46     94    116       C  
ATOM   1831  CD1 LEU A 243      73.273  47.811  66.051  1.00 16.94           C  
ANISOU 1831  CD1 LEU A 243     1993   2285   2158    -83    119    117       C  
ATOM   1832  CD2 LEU A 243      71.485  46.496  67.246  1.00 19.08           C  
ANISOU 1832  CD2 LEU A 243     2287   2559   2403    -30     65    104       C  
ATOM   1833  N   THR A 244      68.210  46.152  63.420  1.00 12.89           N  
ANISOU 1833  N   THR A 244     1569   1802   1525     13     24    185       N  
ATOM   1834  CA  THR A 244      67.308  46.375  62.296  1.00 11.11           C  
ANISOU 1834  CA  THR A 244     1366   1589   1265     27    -10    214       C  
ATOM   1835  C   THR A 244      66.781  47.801  62.285  1.00 13.34           C  
ANISOU 1835  C   THR A 244     1660   1840   1569     44    -14    261       C  
ATOM   1836  O   THR A 244      65.867  48.122  61.510  1.00 14.41           O  
ANISOU 1836  O   THR A 244     1807   1983   1685     68    -55    295       O  
ATOM   1837  CB  THR A 244      66.158  45.370  62.347  1.00 17.38           C  
ANISOU 1837  CB  THR A 244     2136   2401   2068     36    -54    191       C  
ATOM   1838  OG1 THR A 244      65.491  45.478  63.615  1.00 17.55           O  
ANISOU 1838  OG1 THR A 244     2120   2397   2150     44    -51    184       O  
ATOM   1839  CG2 THR A 244      66.703  43.955  62.207  1.00 15.41           C  
ANISOU 1839  CG2 THR A 244     1889   2169   1796     20    -45    146       C  
ATOM   1840  N   ILE A 245      67.351  48.655  63.138  1.00 14.54           N  
ANISOU 1840  N   ILE A 245     1810   1954   1761     34     22    263       N  
ATOM   1841  CA  ILE A 245      67.104  50.087  63.197  1.00 12.82           C  
ANISOU 1841  CA  ILE A 245     1612   1687   1572     46     35    302       C  
ATOM   1842  C   ILE A 245      68.464  50.758  63.259  1.00 13.91           C  
ANISOU 1842  C   ILE A 245     1769   1800   1716      8     86    303       C  
ATOM   1843  O   ILE A 245      69.472  50.129  63.594  1.00 15.03           O  
ANISOU 1843  O   ILE A 245     1889   1964   1856    -21    105    265       O  
ATOM   1844  CB  ILE A 245      66.255  50.456  64.425  1.00 12.96           C  
ANISOU 1844  CB  ILE A 245     1605   1671   1650     67     32    286       C  
ATOM   1845  CG1 ILE A 245      66.973  49.993  65.685  1.00 15.67           C  
ANISOU 1845  CG1 ILE A 245     1931   2014   2007     41     55    233       C  
ATOM   1846  CG2 ILE A 245      64.895  49.781  64.342  1.00 13.74           C  
ANISOU 1846  CG2 ILE A 245     1667   1795   1757     99    -11    285       C  
ATOM   1847  CD1 ILE A 245      66.322  50.503  66.955  1.00 17.86           C  
ANISOU 1847  CD1 ILE A 245     2202   2254   2329     56     70    213       C  
ATOM   1848  N   GLY A 246      68.502  52.034  62.907  1.00 14.21           N  
ANISOU 1848  N   GLY A 246     1843   1788   1768      8    109    347       N  
ATOM   1849  CA  GLY A 246      69.766  52.754  62.902  1.00 14.23           C  
ANISOU 1849  CA  GLY A 246     1859   1758   1788    -39    163    348       C  
ATOM   1850  C   GLY A 246      69.578  54.238  63.099  1.00 15.74           C  
ANISOU 1850  C   GLY A 246     2086   1868   2027    -40    188    381       C  
ATOM   1851  O   GLY A 246      68.521  54.792  62.784  1.00 14.96           O  
ANISOU 1851  O   GLY A 246     2014   1739   1931      7    167    425       O  
ATOM   1852  N   VAL A 247      70.622  54.888  63.628  1.00 14.47           N  
ANISOU 1852  N   VAL A 247     1921   1666   1909    -93    231    355       N  
ATOM   1853  CA  VAL A 247      70.682  56.345  63.686  1.00 14.90           C  
ANISOU 1853  CA  VAL A 247     2019   1629   2013   -109    269    384       C  
ATOM   1854  C   VAL A 247      71.009  56.879  62.303  1.00 16.67           C  
ANISOU 1854  C   VAL A 247     2295   1832   2206   -119    311    461       C  
ATOM   1855  O   VAL A 247      71.063  56.123  61.317  1.00 16.88           O  
ANISOU 1855  O   VAL A 247     2329   1921   2163   -106    305    489       O  
ATOM   1856  CB  VAL A 247      71.727  56.841  64.701  1.00 16.49           C  
ANISOU 1856  CB  VAL A 247     2198   1794   2275   -176    296    321       C  
ATOM   1857  CG1 VAL A 247      71.252  56.608  66.108  1.00 17.31           C  
ANISOU 1857  CG1 VAL A 247     2279   1900   2397   -159    259    254       C  
ATOM   1858  CG2 VAL A 247      73.029  56.125  64.506  1.00 18.20           C  
ANISOU 1858  CG2 VAL A 247     2363   2069   2482   -228    312    293       C  
ATOM   1859  N   LYS A 248      71.264  58.182  62.215  1.00 16.95           N  
ANISOU 1859  N   LYS A 248     2378   1775   2289   -143    360    496       N  
ATOM   1860  CA  LYS A 248      71.632  58.727  60.919  1.00 17.25           C  
ANISOU 1860  CA  LYS A 248     2477   1784   2291   -156    412    579       C  
ATOM   1861  C   LYS A 248      72.999  58.204  60.473  1.00 15.86           C  
ANISOU 1861  C   LYS A 248     2270   1658   2098   -225    467    560       C  
ATOM   1862  O   LYS A 248      73.779  57.644  61.252  1.00 17.22           O  
ANISOU 1862  O   LYS A 248     2368   1868   2307   -268    465    483       O  
ATOM   1863  CB  LYS A 248      71.602  60.261  60.926  1.00 27.40           C  
ANISOU 1863  CB  LYS A 248     3827   2944   3640   -169    461    626       C  
ATOM   1864  CG  LYS A 248      72.613  60.948  61.796  1.00 29.09           C  
ANISOU 1864  CG  LYS A 248     4017   3092   3943   -255    512    566       C  
ATOM   1865  CD  LYS A 248      72.870  62.384  61.299  1.00 33.83           C  
ANISOU 1865  CD  LYS A 248     4697   3565   4593   -287    587    634       C  
ATOM   1866  CE  LYS A 248      71.575  63.121  60.971  1.00 36.29           C  
ANISOU 1866  CE  LYS A 248     5086   3804   4898   -196    564    712       C  
ATOM   1867  NZ  LYS A 248      71.765  64.593  60.789  1.00 36.49           N  
ANISOU 1867  NZ  LYS A 248     5171   3717   4977   -218    605    739       N  
ATOM   1868  N   SER A 249      73.248  58.329  59.176  1.00 15.00           N  
ANISOU 1868  N   SER A 249     2218   1553   1927   -228    516    633       N  
ATOM   1869  CA  SER A 249      74.509  57.886  58.607  1.00 14.73           C  
ANISOU 1869  CA  SER A 249     2158   1561   1875   -288    589    623       C  
ATOM   1870  C   SER A 249      75.655  58.797  59.038  1.00 17.84           C  
ANISOU 1870  C   SER A 249     2524   1885   2370   -378    668    605       C  
ATOM   1871  O   SER A 249      75.458  59.936  59.473  1.00 19.55           O  
ANISOU 1871  O   SER A 249     2774   2003   2651   -395    679    620       O  
ATOM   1872  CB  SER A 249      74.425  57.843  57.073  1.00 17.92           C  
ANISOU 1872  CB  SER A 249     2650   1986   2173   -267    631    710       C  
ATOM   1873  OG  SER A 249      73.510  56.821  56.688  1.00 19.19           O  
ANISOU 1873  OG  SER A 249     2822   2227   2243   -197    550    705       O  
ATOM   1874  N   SER A 250      76.872  58.284  58.897  1.00 18.67           N  
ANISOU 1874  N   SER A 250     2563   2038   2494   -436    724    567       N  
ATOM   1875  CA ASER A 250      78.058  59.049  59.260  0.48 22.46           C  
ANISOU 1875  CA ASER A 250     2990   2471   3074   -526    783    535       C  
ATOM   1876  CA BSER A 250      78.060  59.047  59.255  0.52 22.31           C  
ANISOU 1876  CA BSER A 250     2970   2451   3054   -526    783    535       C  
ATOM   1877  C   SER A 250      79.249  58.529  58.467  1.00 25.81           C  
ANISOU 1877  C   SER A 250     3362   2961   3482   -560    846    525       C  
ATOM   1878  O   SER A 250      79.206  57.454  57.869  1.00 31.33           O  
ANISOU 1878  O   SER A 250     4058   3740   4106   -520    850    527       O  
ATOM   1879  CB ASER A 250      78.319  58.977  60.771  0.48 27.54           C  
ANISOU 1879  CB ASER A 250     3546   3107   3811   -560    730    441       C  
ATOM   1880  CB BSER A 250      78.351  58.962  60.753  0.52 27.70           C  
ANISOU 1880  CB BSER A 250     3564   3128   3831   -561    732    441       C  
ATOM   1881  OG ASER A 250      79.378  59.839  61.154  0.48 28.38           O  
ANISOU 1881  OG ASER A 250     3605   3163   4014   -647    767    404       O  
ATOM   1882  OG BSER A 250      79.096  57.786  61.027  0.52 29.34           O  
ANISOU 1882  OG BSER A 250     3671   3435   4042   -565    711    377       O  
ATOM   1883  N   ALA A 251      80.317  59.318  58.475  1.00 25.16           N  
ANISOU 1883  N   ALA A 251     3239   2843   3477   -632    896    510       N  
ATOM   1884  CA  ALA A 251      81.574  58.937  57.859  1.00 34.17           C  
ANISOU 1884  CA  ALA A 251     4313   4039   4630   -670    963    494       C  
ATOM   1885  C   ALA A 251      82.565  58.420  58.890  1.00 42.54           C  
ANISOU 1885  C   ALA A 251     5230   5143   5789   -712    937    402       C  
ATOM   1886  O   ALA A 251      83.577  57.817  58.516  1.00 44.09           O  
ANISOU 1886  O   ALA A 251     5349   5402   6003   -726    979    378       O  
ATOM   1887  CB  ALA A 251      82.177  60.128  57.103  1.00 33.08           C  
ANISOU 1887  CB  ALA A 251     4217   3837   4514   -722   1041    545       C  
ATOM   1888  N   VAL A 252      82.282  58.639  60.176  1.00 43.76           N  
ANISOU 1888  N   VAL A 252     5351   5268   6009   -728    865    348       N  
ATOM   1889  CA  VAL A 252      83.152  58.150  61.235  1.00 55.23           C  
ANISOU 1889  CA  VAL A 252     6671   6767   7546   -763    816    259       C  
ATOM   1890  C   VAL A 252      83.110  56.629  61.269  1.00 57.04           C  
ANISOU 1890  C   VAL A 252     6845   7094   7734   -703    787    233       C  
ATOM   1891  O   VAL A 252      82.060  56.011  61.067  1.00 64.55           O  
ANISOU 1891  O   VAL A 252     7860   8061   8605   -640    770    260       O  
ATOM   1892  CB  VAL A 252      82.744  58.773  62.582  1.00 61.21           C  
ANISOU 1892  CB  VAL A 252     7427   7468   8362   -792    739    206       C  
ATOM   1893  CG1 VAL A 252      81.408  58.228  63.054  1.00 63.18           C  
ANISOU 1893  CG1 VAL A 252     7734   7719   8554   -727    685    209       C  
ATOM   1894  CG2 VAL A 252      83.809  58.523  63.622  1.00 63.38           C  
ANISOU 1894  CG2 VAL A 252     7571   7787   8724   -839    680    115       C  
ATOM   1895  N   ALA A 253      84.272  56.015  61.479  1.00 54.18           N  
ANISOU 1895  N   ALA A 253     6362   6796   7428   -718    784    182       N  
ATOM   1896  CA  ALA A 253      84.395  54.564  61.507  1.00 49.40           C  
ANISOU 1896  CA  ALA A 253     5696   6278   6796   -656    760    154       C  
ATOM   1897  C   ALA A 253      84.864  54.058  62.861  1.00 45.81           C  
ANISOU 1897  C   ALA A 253     5128   5864   6414   -658    662     76       C  
ATOM   1898  O   ALA A 253      85.196  52.878  62.991  1.00 52.21           O  
ANISOU 1898  O   ALA A 253     5870   6744   7224   -606    635     49       O  
ATOM   1899  CB  ALA A 253      85.350  54.093  60.411  1.00 48.82           C  
ANISOU 1899  CB  ALA A 253     5587   6251   6714   -647    846    170       C  
ATOM   1900  N   THR A 254      84.903  54.917  63.869  1.00 38.63           N  
ANISOU 1900  N   THR A 254     4205   4911   5563   -712    601     39       N  
ATOM   1901  CA  THR A 254      85.368  54.496  65.174  1.00 43.69           C  
ANISOU 1901  CA  THR A 254     4749   5595   6256   -713    492    -36       C  
ATOM   1902  C   THR A 254      84.210  53.862  65.938  1.00 39.12           C  
ANISOU 1902  C   THR A 254     4231   5030   5604   -645    404    -48       C  
ATOM   1903  O   THR A 254      83.075  53.773  65.455  1.00 42.37           O  
ANISOU 1903  O   THR A 254     4754   5418   5925   -594    421      1       O  
ATOM   1904  CB  THR A 254      85.975  55.677  65.931  1.00 47.90           C  
ANISOU 1904  CB  THR A 254     5254   6081   6864   -797    453    -77       C  
ATOM   1905  OG1 THR A 254      85.137  56.829  65.781  1.00 50.32           O  
ANISOU 1905  OG1 THR A 254     5675   6291   7154   -833    491    -49       O  
ATOM   1906  CG2 THR A 254      87.366  55.998  65.399  1.00 49.55           C  
ANISOU 1906  CG2 THR A 254     5377   6305   7145   -845    506    -75       C  
ATOM   1907  N   THR A 255      84.501  53.403  67.144  1.00 38.33           N  
ANISOU 1907  N   THR A 255     4071   4973   5521   -629    293   -108       N  
ATOM   1908  CA  THR A 255      83.474  52.767  67.943  1.00 35.01           C  
ANISOU 1908  CA  THR A 255     3725   4568   5011   -553    204   -113       C  
ATOM   1909  C   THR A 255      82.469  53.800  68.441  1.00 34.71           C  
ANISOU 1909  C   THR A 255     3795   4455   4937   -574    187   -114       C  
ATOM   1910  O   THR A 255      82.752  54.996  68.547  1.00 42.82           O  
ANISOU 1910  O   THR A 255     4826   5421   6022   -652    211   -133       O  
ATOM   1911  CB  THR A 255      84.098  52.024  69.121  1.00 44.72           C  
ANISOU 1911  CB  THR A 255     4873   5861   6258   -529     91   -168       C  
ATOM   1912  OG1 THR A 255      85.007  52.897  69.801  1.00 51.69           O  
ANISOU 1912  OG1 THR A 255     5680   6734   7225   -614     50   -227       O  
ATOM   1913  CG2 THR A 255      84.856  50.802  68.624  1.00 49.16           C  
ANISOU 1913  CG2 THR A 255     5341   6491   6845   -476    107   -158       C  
ATOM   1914  N   SER A 256      81.288  53.315  68.759  1.00 25.66           N  
ANISOU 1914  N   SER A 256     2734   3310   3704   -503    150    -96       N  
ATOM   1915  CA  SER A 256      80.202  54.153  69.223  1.00 25.95           C  
ANISOU 1915  CA  SER A 256     2872   3281   3706   -503    141    -95       C  
ATOM   1916  C   SER A 256      80.068  54.021  70.732  1.00 21.89           C  
ANISOU 1916  C   SER A 256     2367   2782   3167   -492     45   -157       C  
ATOM   1917  O   SER A 256      80.862  53.346  71.396  1.00 20.99           O  
ANISOU 1917  O   SER A 256     2183   2730   3062   -489    -23   -196       O  
ATOM   1918  CB  SER A 256      78.901  53.744  68.549  1.00 24.34           C  
ANISOU 1918  CB  SER A 256     2750   3069   3429   -432    171    -35       C  
ATOM   1919  OG  SER A 256      78.457  52.506  69.083  1.00 23.31           O  
ANISOU 1919  OG  SER A 256     2620   2996   3242   -364    114    -43       O  
ATOM   1920  N   ILE A 257      79.012  54.625  71.276  1.00 19.33           N  
ANISOU 1920  N   ILE A 257     2137   2405   2805   -479     40   -164       N  
ATOM   1921  CA  ILE A 257      78.742  54.485  72.698  1.00 21.52           C  
ANISOU 1921  CA  ILE A 257     2446   2695   3036   -463    -38   -220       C  
ATOM   1922  C   ILE A 257      78.406  53.049  73.075  1.00 19.57           C  
ANISOU 1922  C   ILE A 257     2196   2520   2720   -386    -84   -203       C  
ATOM   1923  O   ILE A 257      78.451  52.703  74.260  1.00 21.49           O  
ANISOU 1923  O   ILE A 257     2455   2792   2917   -371   -154   -244       O  
ATOM   1924  CB  ILE A 257      77.638  55.489  73.085  1.00 26.70           C  
ANISOU 1924  CB  ILE A 257     3203   3268   3672   -461     -9   -229       C  
ATOM   1925  CG1 ILE A 257      77.727  55.844  74.572  1.00 30.44           C  
ANISOU 1925  CG1 ILE A 257     3713   3736   4116   -483    -75   -311       C  
ATOM   1926  CG2 ILE A 257      76.270  54.964  72.675  1.00 27.97           C  
ANISOU 1926  CG2 ILE A 257     3421   3427   3779   -381     26   -170       C  
ATOM   1927  CD1 ILE A 257      77.005  57.128  74.921  1.00 34.08           C  
ANISOU 1927  CD1 ILE A 257     4263   4099   4589   -504    -34   -341       C  
ATOM   1928  N   LEU A 258      78.129  52.180  72.094  1.00 19.16           N  
ANISOU 1928  N   LEU A 258     2128   2495   2655   -339    -46   -145       N  
ATOM   1929  CA  LEU A 258      77.978  50.761  72.399  1.00 20.95           C  
ANISOU 1929  CA  LEU A 258     2345   2781   2833   -274    -85   -132       C  
ATOM   1930  C   LEU A 258      79.241  50.168  73.004  1.00 21.16           C  
ANISOU 1930  C   LEU A 258     2292   2867   2882   -278   -155   -166       C  
ATOM   1931  O   LEU A 258      79.167  49.138  73.686  1.00 22.31           O  
ANISOU 1931  O   LEU A 258     2445   3052   2981   -225   -208   -163       O  
ATOM   1932  CB  LEU A 258      77.598  49.975  71.142  1.00 22.01           C  
ANISOU 1932  CB  LEU A 258     2475   2930   2960   -234    -31    -76       C  
ATOM   1933  CG  LEU A 258      76.176  50.225  70.649  1.00 20.10           C  
ANISOU 1933  CG  LEU A 258     2308   2647   2683   -208     12    -38       C  
ATOM   1934  CD1 LEU A 258      75.972  49.610  69.266  1.00 25.92           C  
ANISOU 1934  CD1 LEU A 258     3038   3400   3412   -184     58      8       C  
ATOM   1935  CD2 LEU A 258      75.127  49.688  71.638  1.00 22.97           C  
ANISOU 1935  CD2 LEU A 258     2724   3011   2991   -163    -19    -44       C  
ATOM   1936  N   ASP A 259      80.396  50.799  72.784  1.00 23.38           N  
ANISOU 1936  N   ASP A 259     2494   3152   3238   -340   -157   -194       N  
ATOM   1937  CA  ASP A 259      81.640  50.301  73.353  1.00 26.38           C  
ANISOU 1937  CA  ASP A 259     2777   3591   3653   -344   -233   -229       C  
ATOM   1938  C   ASP A 259      81.707  50.454  74.868  1.00 23.96           C  
ANISOU 1938  C   ASP A 259     2502   3301   3299   -348   -338   -281       C  
ATOM   1939  O   ASP A 259      82.636  49.917  75.482  1.00 26.06           O  
ANISOU 1939  O   ASP A 259     2697   3625   3579   -335   -425   -305       O  
ATOM   1940  CB  ASP A 259      82.829  51.009  72.702  1.00 24.19           C  
ANISOU 1940  CB  ASP A 259     2395   3313   3483   -419   -201   -250       C  
ATOM   1941  N   THR A 260      80.753  51.159  75.487  1.00 20.30           N  
ANISOU 1941  N   THR A 260     2145   2790   2779   -360   -334   -300       N  
ATOM   1942  CA  THR A 260      80.731  51.237  76.945  1.00 22.06           C  
ANISOU 1942  CA  THR A 260     2420   3030   2933   -358   -426   -351       C  
ATOM   1943  C   THR A 260      80.258  49.944  77.598  1.00 19.97           C  
ANISOU 1943  C   THR A 260     2203   2809   2578   -271   -467   -317       C  
ATOM   1944  O   THR A 260      80.493  49.753  78.799  1.00 24.57           O  
ANISOU 1944  O   THR A 260     2818   3424   3094   -259   -558   -349       O  
ATOM   1945  CB  THR A 260      79.849  52.396  77.425  1.00 22.30           C  
ANISOU 1945  CB  THR A 260     2555   2989   2930   -394   -393   -388       C  
ATOM   1946  OG1 THR A 260      78.506  52.233  76.948  1.00 21.30           O  
ANISOU 1946  OG1 THR A 260     2504   2823   2768   -346   -308   -334       O  
ATOM   1947  CG2 THR A 260      80.411  53.729  76.951  1.00 25.12           C  
ANISOU 1947  CG2 THR A 260     2875   3291   3379   -487   -360   -428       C  
ATOM   1948  N   PHE A 261      79.596  49.065  76.851  1.00 19.32           N  
ANISOU 1948  N   PHE A 261     2132   2723   2485   -214   -405   -252       N  
ATOM   1949  CA  PHE A 261      79.130  47.787  77.385  1.00 19.86           C  
ANISOU 1949  CA  PHE A 261     2246   2819   2480   -137   -430   -214       C  
ATOM   1950  C   PHE A 261      80.260  46.768  77.317  1.00 22.47           C  
ANISOU 1950  C   PHE A 261     2486   3207   2845    -98   -492   -198       C  
ATOM   1951  O   PHE A 261      80.589  46.277  76.233  1.00 23.83           O  
ANISOU 1951  O   PHE A 261     2589   3384   3081    -83   -445   -170       O  
ATOM   1952  CB  PHE A 261      77.933  47.268  76.593  1.00 20.76           C  
ANISOU 1952  CB  PHE A 261     2407   2900   2582   -100   -340   -159       C  
ATOM   1953  CG  PHE A 261      76.682  48.061  76.780  1.00 17.90           C  
ANISOU 1953  CG  PHE A 261     2130   2485   2185   -115   -284   -165       C  
ATOM   1954  CD1 PHE A 261      76.386  49.113  75.935  1.00 17.47           C  
ANISOU 1954  CD1 PHE A 261     2068   2386   2182   -157   -223   -169       C  
ATOM   1955  CD2 PHE A 261      75.790  47.742  77.793  1.00 19.84           C  
ANISOU 1955  CD2 PHE A 261     2465   2724   2349    -83   -285   -162       C  
ATOM   1956  CE1 PHE A 261      75.203  49.846  76.090  1.00 18.76           C  
ANISOU 1956  CE1 PHE A 261     2305   2497   2326   -159   -171   -172       C  
ATOM   1957  CE2 PHE A 261      74.617  48.468  77.956  1.00 19.30           C  
ANISOU 1957  CE2 PHE A 261     2465   2607   2261    -91   -223   -170       C  
ATOM   1958  CZ  PHE A 261      74.333  49.525  77.106  1.00 19.79           C  
ANISOU 1958  CZ  PHE A 261     2510   2623   2384   -125   -170   -176       C  
ATOM   1959  N   ASN A 262      80.821  46.410  78.472  1.00 21.76           N  
ANISOU 1959  N   ASN A 262     2401   3160   2707    -74   -598   -216       N  
ATOM   1960  CA  ASN A 262      81.875  45.399  78.480  1.00 26.74           C  
ANISOU 1960  CA  ASN A 262     2943   3843   3375    -22   -665   -195       C  
ATOM   1961  C   ASN A 262      81.368  44.056  77.971  1.00 20.62           C  
ANISOU 1961  C   ASN A 262     2191   3055   2588     56   -613   -128       C  
ATOM   1962  O   ASN A 262      82.128  43.293  77.370  1.00 22.28           O  
ANISOU 1962  O   ASN A 262     2314   3287   2866     96   -614   -108       O  
ATOM   1963  CB  ASN A 262      82.448  45.241  79.885  1.00 30.59           C  
ANISOU 1963  CB  ASN A 262     3449   4379   3795      0   -801   -218       C  
ATOM   1964  CG  ASN A 262      83.486  46.300  80.217  1.00 43.93           C  
ANISOU 1964  CG  ASN A 262     5056   6100   5535    -75   -882   -293       C  
ATOM   1965  OD1 ASN A 262      83.754  46.567  81.384  1.00 54.77           O  
ANISOU 1965  OD1 ASN A 262     6468   7504   6837    -84   -991   -332       O  
ATOM   1966  ND2 ASN A 262      84.081  46.898  79.189  1.00 44.73           N  
ANISOU 1966  ND2 ASN A 262     5046   6192   5757   -133   -829   -315       N  
ATOM   1967  N   ILE A 263      80.087  43.759  78.184  1.00 19.97           N  
ANISOU 1967  N   ILE A 263     2223   2935   2431     77   -560    -98       N  
ATOM   1968  CA  ILE A 263      79.536  42.476  77.754  1.00 20.12           C  
ANISOU 1968  CA  ILE A 263     2271   2932   2442    140   -510    -40       C  
ATOM   1969  C   ILE A 263      79.578  42.339  76.236  1.00 21.42           C  
ANISOU 1969  C   ILE A 263     2371   3080   2689    130   -426    -33       C  
ATOM   1970  O   ILE A 263      79.647  41.221  75.711  1.00 21.32           O  
ANISOU 1970  O   ILE A 263     2343   3060   2700    182   -401     -1       O  
ATOM   1971  CB  ILE A 263      78.106  42.310  78.309  1.00 21.55           C  
ANISOU 1971  CB  ILE A 263     2578   3073   2536    148   -463    -16       C  
ATOM   1972  CG1 ILE A 263      77.549  40.922  78.007  1.00 28.68           C  
ANISOU 1972  CG1 ILE A 263     3515   3949   3433    206   -419     40       C  
ATOM   1973  CG2 ILE A 263      77.176  43.371  77.740  1.00 25.08           C  
ANISOU 1973  CG2 ILE A 263     3049   3485   2995     90   -385    -38       C  
ATOM   1974  CD1 ILE A 263      78.248  39.814  78.700  1.00 32.35           C  
ANISOU 1974  CD1 ILE A 263     3984   4431   3876    276   -489     75       C  
ATOM   1975  N   LEU A 264      79.570  43.457  75.508  1.00 19.16           N  
ANISOU 1975  N   LEU A 264     2052   2783   2444     65   -380    -62       N  
ATOM   1976  CA  LEU A 264      79.642  43.360  74.054  1.00 19.87           C  
ANISOU 1976  CA  LEU A 264     2093   2862   2596     55   -300    -51       C  
ATOM   1977  C   LEU A 264      81.045  43.016  73.557  1.00 25.85           C  
ANISOU 1977  C   LEU A 264     2732   3655   3433     69   -313    -62       C  
ATOM   1978  O   LEU A 264      81.217  42.835  72.348  1.00 25.62           O  
ANISOU 1978  O   LEU A 264     2665   3620   3449     67   -239    -55       O  
ATOM   1979  CB  LEU A 264      79.138  44.657  73.402  1.00 19.54           C  
ANISOU 1979  CB  LEU A 264     2067   2791   2566    -12   -240    -66       C  
ATOM   1980  CG  LEU A 264      77.648  45.001  73.598  1.00 22.12           C  
ANISOU 1980  CG  LEU A 264     2494   3076   2834    -18   -206    -53       C  
ATOM   1981  CD1 LEU A 264      77.240  46.277  72.855  1.00 23.17           C  
ANISOU 1981  CD1 LEU A 264     2637   3177   2991    -72   -151    -59       C  
ATOM   1982  CD2 LEU A 264      76.692  43.851  73.247  1.00 17.89           C  
ANISOU 1982  CD2 LEU A 264     2004   2525   2267     30   -171    -15       C  
ATOM   1983  N   SER A 265      82.037  42.900  74.445  1.00 22.44           N  
ANISOU 1983  N   SER A 265     2242   3264   3020     86   -405    -78       N  
ATOM   1984  CA  SER A 265      83.354  42.385  74.096  1.00 23.09           C  
ANISOU 1984  CA  SER A 265     2200   3385   3189    117   -425    -85       C  
ATOM   1985  C   SER A 265      83.579  40.975  74.629  1.00 27.40           C  
ANISOU 1985  C   SER A 265     2750   3940   3720    215   -478    -50       C  
ATOM   1986  O   SER A 265      84.712  40.491  74.630  1.00 35.19           O  
ANISOU 1986  O   SER A 265     3631   4962   4779    258   -519    -54       O  
ATOM   1987  CB  SER A 265      84.442  43.325  74.621  1.00 30.84           C  
ANISOU 1987  CB  SER A 265     3083   4408   4226     63   -499   -131       C  
ATOM   1988  OG  SER A 265      84.363  44.579  73.970  1.00 36.61           O  
ANISOU 1988  OG  SER A 265     3803   5117   4992    -28   -432   -159       O  
ATOM   1989  N   SER A 266      82.533  40.319  75.101  1.00 24.43           N  
ANISOU 1989  N   SER A 266     2493   3531   3261    252   -476    -15       N  
ATOM   1990  CA ASER A 266      82.693  38.985  75.647  0.51 24.07           C  
ANISOU 1990  CA ASER A 266     2468   3479   3198    344   -521     26       C  
ATOM   1991  CA BSER A 266      82.626  38.981  75.665  0.49 24.28           C  
ANISOU 1991  CA BSER A 266     2501   3503   3220    344   -520     27       C  
ATOM   1992  C   SER A 266      82.436  37.931  74.575  1.00 23.40           C  
ANISOU 1992  C   SER A 266     2389   3352   3150    388   -430     48       C  
ATOM   1993  O   SER A 266      81.802  38.182  73.543  1.00 20.82           O  
ANISOU 1993  O   SER A 266     2084   3000   2828    346   -338     37       O  
ATOM   1994  CB ASER A 266      81.756  38.775  76.837  0.51 24.66           C  
ANISOU 1994  CB ASER A 266     2674   3534   3162    360   -563     56       C  
ATOM   1995  CB BSER A 266      81.573  38.800  76.767  0.49 23.37           C  
ANISOU 1995  CB BSER A 266     2523   3364   2992    354   -550     57       C  
ATOM   1996  OG ASER A 266      80.410  38.825  76.417  0.51 20.78           O  
ANISOU 1996  OG ASER A 266     2274   2994   2628    328   -473     66       O  
ATOM   1997  OG BSER A 266      81.368  37.434  77.084  0.49 25.55           O  
ANISOU 1997  OG BSER A 266     2854   3609   3246    436   -555    110       O  
ATOM   1998  N   ALA A 267      82.970  36.741  74.825  1.00 22.14           N  
ANISOU 1998  N   ALA A 267     2211   3184   3017    477   -462     79       N  
ATOM   1999  CA  ALA A 267      82.701  35.623  73.936  1.00 22.82           C  
ANISOU 1999  CA  ALA A 267     2319   3218   3132    523   -379     94       C  
ATOM   2000  C   ALA A 267      81.216  35.285  73.978  1.00 21.68           C  
ANISOU 2000  C   ALA A 267     2310   3017   2912    502   -330    117       C  
ATOM   2001  O   ALA A 267      80.566  35.396  75.020  1.00 24.94           O  
ANISOU 2001  O   ALA A 267     2804   3422   3249    496   -373    143       O  
ATOM   2002  CB  ALA A 267      83.534  34.408  74.343  1.00 27.07           C  
ANISOU 2002  CB  ALA A 267     2823   3746   3717    631   -428    128       C  
ATOM   2003  N   GLY A 268      80.677  34.894  72.833  1.00 21.70           N  
ANISOU 2003  N   GLY A 268     2334   2980   2933    488   -237    103       N  
ATOM   2004  CA  GLY A 268      79.282  34.514  72.776  1.00 21.83           C  
ANISOU 2004  CA  GLY A 268     2458   2943   2894    464   -192    119       C  
ATOM   2005  C   GLY A 268      78.293  35.655  72.790  1.00 25.27           C  
ANISOU 2005  C   GLY A 268     2931   3392   3278    383   -177    105       C  
ATOM   2006  O   GLY A 268      77.116  35.427  73.071  1.00 29.22           O  
ANISOU 2006  O   GLY A 268     3513   3855   3733    365   -155    123       O  
ATOM   2007  N   VAL A 269      78.725  36.886  72.527  1.00 17.51           N  
ANISOU 2007  N   VAL A 269     2617   2239   1797    324   -495    216       N  
ATOM   2008  CA  VAL A 269      77.809  38.015  72.379  1.00 15.37           C  
ANISOU 2008  CA  VAL A 269     2337   1992   1511    274   -453    182       C  
ATOM   2009  C   VAL A 269      78.205  38.726  71.097  1.00 15.89           C  
ANISOU 2009  C   VAL A 269     2306   2065   1666    280   -406    180       C  
ATOM   2010  O   VAL A 269      79.315  39.267  71.006  1.00 16.78           O  
ANISOU 2010  O   VAL A 269     2339   2180   1858    295   -444    183       O  
ATOM   2011  CB  VAL A 269      77.842  38.974  73.575  1.00 17.31           C  
ANISOU 2011  CB  VAL A 269     2595   2249   1731    244   -517    154       C  
ATOM   2012  CG1 VAL A 269      76.902  40.127  73.331  1.00 20.74           C  
ANISOU 2012  CG1 VAL A 269     3018   2702   2159    202   -467    119       C  
ATOM   2013  CG2 VAL A 269      77.480  38.232  74.884  1.00 20.06           C  
ANISOU 2013  CG2 VAL A 269     3054   2589   1978    236   -562    159       C  
ATOM   2014  N   VAL A 270      77.321  38.711  70.100  1.00 12.81           N  
ANISOU 2014  N   VAL A 270     1924   1681   1264    264   -326    177       N  
ATOM   2015  CA  VAL A 270      77.667  39.144  68.754  1.00 12.52           C  
ANISOU 2015  CA  VAL A 270     1815   1646   1297    273   -274    183       C  
ATOM   2016  C   VAL A 270      76.642  40.168  68.295  1.00 15.36           C  
ANISOU 2016  C   VAL A 270     2170   2021   1644    233   -230    161       C  
ATOM   2017  O   VAL A 270      75.434  39.949  68.449  1.00 16.39           O  
ANISOU 2017  O   VAL A 270     2359   2159   1709    210   -204    149       O  
ATOM   2018  CB  VAL A 270      77.722  37.951  67.778  1.00 13.99           C  
ANISOU 2018  CB  VAL A 270     2019   1814   1481    303   -220    206       C  
ATOM   2019  CG1 VAL A 270      78.054  38.434  66.374  1.00 16.62           C  
ANISOU 2019  CG1 VAL A 270     2289   2150   1875    307   -160    211       C  
ATOM   2020  CG2 VAL A 270      78.749  36.920  68.270  1.00 18.53           C  
ANISOU 2020  CG2 VAL A 270     2599   2367   2075    352   -266    228       C  
ATOM   2021  N   VAL A 271      77.109  41.282  67.726  1.00 13.02           N  
ANISOU 2021  N   VAL A 271     1804   1727   1414    225   -222    157       N  
ATOM   2022  CA  VAL A 271      76.226  42.311  67.179  1.00 13.15           C  
ANISOU 2022  CA  VAL A 271     1815   1751   1429    196   -184    142       C  
ATOM   2023  C   VAL A 271      76.301  42.281  65.653  1.00 13.24           C  
ANISOU 2023  C   VAL A 271     1799   1760   1473    204   -121    163       C  
ATOM   2024  O   VAL A 271      77.389  42.370  65.074  1.00 13.99           O  
ANISOU 2024  O   VAL A 271     1839   1846   1630    220   -111    179       O  
ATOM   2025  CB  VAL A 271      76.568  43.713  67.723  1.00 13.08           C  
ANISOU 2025  CB  VAL A 271     1767   1741   1462    175   -222    120       C  
ATOM   2026  CG1 VAL A 271      75.630  44.758  67.143  1.00 16.27           C  
ANISOU 2026  CG1 VAL A 271     2170   2146   1867    153   -184    107       C  
ATOM   2027  CG2 VAL A 271      76.496  43.733  69.264  1.00 15.30           C  
ANISOU 2027  CG2 VAL A 271     2089   2025   1700    165   -286     96       C  
ATOM   2028  N   VAL A 272      75.139  42.146  65.012  1.00 11.49           N  
ANISOU 2028  N   VAL A 272     1615   1545   1205    190    -78    161       N  
ATOM   2029  CA  VAL A 272      74.992  42.183  63.558  1.00 12.47           C  
ANISOU 2029  CA  VAL A 272     1730   1666   1340    191    -22    178       C  
ATOM   2030  C   VAL A 272      74.092  43.364  63.237  1.00 14.47           C  
ANISOU 2030  C   VAL A 272     1978   1926   1593    168    -13    168       C  
ATOM   2031  O   VAL A 272      73.031  43.506  63.850  1.00 18.84           O  
ANISOU 2031  O   VAL A 272     2559   2491   2106    153    -26    147       O  
ATOM   2032  CB  VAL A 272      74.367  40.880  63.019  1.00 12.15           C  
ANISOU 2032  CB  VAL A 272     1746   1627   1243    197     12    186       C  
ATOM   2033  CG1 VAL A 272      74.281  40.899  61.494  1.00 13.57           C  
ANISOU 2033  CG1 VAL A 272     1927   1802   1426    196     67    203       C  
ATOM   2034  CG2 VAL A 272      75.173  39.680  63.462  1.00 14.20           C  
ANISOU 2034  CG2 VAL A 272     2022   1873   1501    226      0    196       C  
ATOM   2035  N   SER A 273      74.499  44.211  62.286  1.00 11.53           N  
ANISOU 2035  N   SER A 273     1572   1543   1266    164     11    183       N  
ATOM   2036  CA  SER A 273      73.692  45.371  61.912  1.00 10.47           C  
ANISOU 2036  CA  SER A 273     1437   1407   1136    148     16    179       C  
ATOM   2037  C   SER A 273      73.518  45.451  60.407  1.00 10.74           C  
ANISOU 2037  C   SER A 273     1481   1436   1166    147     61    206       C  
ATOM   2038  O   SER A 273      74.444  45.153  59.646  1.00 11.50           O  
ANISOU 2038  O   SER A 273     1563   1522   1284    154     95    228       O  
ATOM   2039  CB  SER A 273      74.331  46.696  62.375  1.00 13.61           C  
ANISOU 2039  CB  SER A 273     1792   1786   1594    138    -10    170       C  
ATOM   2040  OG  SER A 273      73.496  47.804  62.047  1.00 13.79           O  
ANISOU 2040  OG  SER A 273     1821   1798   1620    128     -7    166       O  
ATOM   2041  N   GLY A 274      72.349  45.908  59.968  1.00 10.52           N  
ANISOU 2041  N   GLY A 274     1474   1414   1110    139     62    205       N  
ATOM   2042  CA  GLY A 274      72.247  46.353  58.588  1.00 11.63           C  
ANISOU 2042  CA  GLY A 274     1626   1543   1250    136     93    233       C  
ATOM   2043  C   GLY A 274      73.187  47.515  58.321  1.00 12.04           C  
ANISOU 2043  C   GLY A 274     1645   1567   1364    130    101    249       C  
ATOM   2044  O   GLY A 274      73.484  48.321  59.204  1.00 12.96           O  
ANISOU 2044  O   GLY A 274     1730   1671   1522    124     72    232       O  
ATOM   2045  N   ALA A 275      73.650  47.616  57.072  1.00 10.63           N  
ANISOU 2045  N   ALA A 275     1477   1375   1187    125    144    281       N  
ATOM   2046  CA  ALA A 275      74.587  48.681  56.731  1.00 11.09           C  
ANISOU 2046  CA  ALA A 275     1505   1404   1305    111    163    301       C  
ATOM   2047  C   ALA A 275      73.935  50.050  56.704  1.00 14.23           C  
ANISOU 2047  C   ALA A 275     1910   1777   1718    102    138    304       C  
ATOM   2048  O   ALA A 275      74.649  51.055  56.779  1.00 12.72           O  
ANISOU 2048  O   ALA A 275     1694   1556   1583     85    140    312       O  
ATOM   2049  CB  ALA A 275      75.225  48.413  55.369  1.00 11.65           C  
ANISOU 2049  CB  ALA A 275     1595   1467   1367    106    227    335       C  
ATOM   2050  N   GLY A 276      72.611  50.110  56.561  1.00 12.64           N  
ANISOU 2050  N   GLY A 276     1744   1587   1474    113    114    300       N  
ATOM   2051  CA  GLY A 276      71.940  51.373  56.296  1.00 13.80           C  
ANISOU 2051  CA  GLY A 276     1903   1705   1634    115     93    311       C  
ATOM   2052  C   GLY A 276      71.248  51.347  54.950  1.00 12.91           C  
ANISOU 2052  C   GLY A 276     1838   1592   1474    119    105    346       C  
ATOM   2053  O   GLY A 276      71.680  50.641  54.030  1.00 11.50           O  
ANISOU 2053  O   GLY A 276     1686   1421   1262    111    143    369       O  
ATOM   2054  N   ASN A 277      70.175  52.119  54.817  1.00 13.14           N  
ANISOU 2054  N   ASN A 277     1882   1610   1499    133     69    349       N  
ATOM   2055  CA  ASN A 277      69.391  52.144  53.590  1.00 12.44           C  
ANISOU 2055  CA  ASN A 277     1841   1523   1363    140     62    383       C  
ATOM   2056  C   ASN A 277      69.513  53.490  52.889  1.00 14.17           C  
ANISOU 2056  C   ASN A 277     2087   1691   1608    140     59    422       C  
ATOM   2057  O   ASN A 277      68.559  53.966  52.258  1.00 16.36           O  
ANISOU 2057  O   ASN A 277     2395   1959   1863    158     25    444       O  
ATOM   2058  CB  ASN A 277      67.922  51.845  53.881  1.00 13.23           C  
ANISOU 2058  CB  ASN A 277     1934   1656   1438    161     16    360       C  
ATOM   2059  CG  ASN A 277      67.687  50.437  54.390  1.00 15.64           C  
ANISOU 2059  CG  ASN A 277     2227   2008   1705    154     22    329       C  
ATOM   2060  OD1 ASN A 277      68.582  49.597  54.437  1.00 14.12           O  
ANISOU 2060  OD1 ASN A 277     2039   1824   1502    140     57    326       O  
ATOM   2061  ND2 ASN A 277      66.437  50.160  54.721  1.00 17.28           N  
ANISOU 2061  ND2 ASN A 277     2422   2248   1897    165    -12    306       N  
ATOM   2062  N   GLN A 278      70.699  54.107  52.950  1.00 14.68           N  
ANISOU 2062  N   GLN A 278     2143   1718   1718    118     94    434       N  
ATOM   2063  CA  GLN A 278      70.881  55.443  52.392  1.00 13.98           C  
ANISOU 2063  CA  GLN A 278     2082   1570   1658    111     94    472       C  
ATOM   2064  C   GLN A 278      71.754  55.438  51.139  1.00 14.42           C  
ANISOU 2064  C   GLN A 278     2184   1607   1690     82    152    521       C  
ATOM   2065  O   GLN A 278      72.323  56.478  50.768  1.00 17.27           O  
ANISOU 2065  O   GLN A 278     2564   1915   2084     61    172    553       O  
ATOM   2066  CB  GLN A 278      71.448  56.398  53.452  1.00 13.49           C  
ANISOU 2066  CB  GLN A 278     1981   1470   1673    102     86    446       C  
ATOM   2067  CG  GLN A 278      70.658  56.419  54.759  1.00 13.53           C  
ANISOU 2067  CG  GLN A 278     1950   1494   1698    129     39    392       C  
ATOM   2068  CD  GLN A 278      69.149  56.622  54.586  1.00 15.70           C  
ANISOU 2068  CD  GLN A 278     2242   1776   1947    170     -5    391       C  
ATOM   2069  OE1 GLN A 278      68.695  57.506  53.856  1.00 15.73           O  
ANISOU 2069  OE1 GLN A 278     2282   1739   1955    185    -22    426       O  
ATOM   2070  NE2 GLN A 278      68.364  55.811  55.297  1.00 15.45           N  
ANISOU 2070  NE2 GLN A 278     2181   1795   1894    188    -24    351       N  
ATOM   2071  N   GLY A 279      71.816  54.304  50.437  1.00 15.29           N  
ANISOU 2071  N   GLY A 279     2318   1755   1738     77    182    529       N  
ATOM   2072  CA  GLY A 279      72.660  54.223  49.253  1.00 15.99           C  
ANISOU 2072  CA  GLY A 279     2453   1827   1797     49    249    572       C  
ATOM   2073  C   GLY A 279      72.221  55.095  48.091  1.00 19.08           C  
ANISOU 2073  C   GLY A 279     2924   2178   2149     45    242    627       C  
ATOM   2074  O   GLY A 279      73.048  55.453  47.251  1.00 22.08           O  
ANISOU 2074  O   GLY A 279     3342   2526   2519     14    302    666       O  
ATOM   2075  N   ASN A 280      70.926  55.424  47.999  1.00 16.72           N  
ANISOU 2075  N   ASN A 280     2651   1878   1823     76    169    632       N  
ATOM   2076  CA  ASN A 280      70.434  56.222  46.880  1.00 18.29           C  
ANISOU 2076  CA  ASN A 280     2933   2038   1980     79    148    689       C  
ATOM   2077  C   ASN A 280      69.467  57.309  47.330  1.00 18.69           C  
ANISOU 2077  C   ASN A 280     2975   2056   2072    116     72    691       C  
ATOM   2078  O   ASN A 280      68.707  57.832  46.512  1.00 21.49           O  
ANISOU 2078  O   ASN A 280     3391   2386   2388    135     28    734       O  
ATOM   2079  CB  ASN A 280      69.779  55.339  45.815  1.00 19.72           C  
ANISOU 2079  CB  ASN A 280     3178   2254   2061     83    135    707       C  
ATOM   2080  CG  ASN A 280      68.494  54.686  46.293  1.00 20.70           C  
ANISOU 2080  CG  ASN A 280     3269   2428   2169    116     60    670       C  
ATOM   2081  OD1 ASN A 280      68.230  54.592  47.484  1.00 20.16           O  
ANISOU 2081  OD1 ASN A 280     3124   2379   2157    134     38    624       O  
ATOM   2082  ND2 ASN A 280      67.670  54.257  45.343  1.00 26.42           N  
ANISOU 2082  ND2 ASN A 280     4053   3172   2813    122     21    692       N  
ATOM   2083  N   THR A 281      69.497  57.679  48.607  1.00 18.88           N  
ANISOU 2083  N   THR A 281     2927   2073   2172    128     56    647       N  
ATOM   2084  CA  THR A 281      68.536  58.625  49.154  1.00 15.98           C  
ANISOU 2084  CA  THR A 281     2546   1677   1848    170    -10    638       C  
ATOM   2085  C   THR A 281      69.043  60.056  49.180  1.00 18.09           C  
ANISOU 2085  C   THR A 281     2839   1861   2172    160     -2    665       C  
ATOM   2086  O   THR A 281      68.270  60.962  49.518  1.00 20.51           O  
ANISOU 2086  O   THR A 281     3147   2129   2516    200    -54    662       O  
ATOM   2087  CB  THR A 281      68.157  58.209  50.573  1.00 16.52           C  
ANISOU 2087  CB  THR A 281     2533   1785   1959    190    -31    568       C  
ATOM   2088  OG1 THR A 281      69.355  58.136  51.353  1.00 18.17           O  
ANISOU 2088  OG1 THR A 281     2703   1988   2212    155     17    541       O  
ATOM   2089  CG2 THR A 281      67.465  56.845  50.556  1.00 17.13           C  
ANISOU 2089  CG2 THR A 281     2591   1938   1981    199    -45    544       C  
ATOM   2090  N   ASP A 282      70.319  60.276  48.851  1.00 17.91           N  
ANISOU 2090  N   ASP A 282     2835   1808   2162    109     64    688       N  
ATOM   2091  CA  ASP A 282      70.874  61.617  48.678  1.00 17.43           C  
ANISOU 2091  CA  ASP A 282     2811   1662   2148     87     80    723       C  
ATOM   2092  C   ASP A 282      70.867  62.406  49.983  1.00 19.38           C  
ANISOU 2092  C   ASP A 282     3007   1875   2481     98     52    675       C  
ATOM   2093  O   ASP A 282      70.700  63.626  49.978  1.00 19.37           O  
ANISOU 2093  O   ASP A 282     3043   1798   2519    106     31    695       O  
ATOM   2094  CB  ASP A 282      70.143  62.395  47.575  1.00 19.84           C  
ANISOU 2094  CB  ASP A 282     3210   1916   2413    110     43    788       C  
ATOM   2095  CG  ASP A 282      70.187  61.685  46.243  1.00 29.81           C  
ANISOU 2095  CG  ASP A 282     4540   3208   3580     93     70    837       C  
ATOM   2096  OD1 ASP A 282      71.013  60.756  46.083  1.00 25.18           O  
ANISOU 2096  OD1 ASP A 282     3934   2666   2968     56    135    825       O  
ATOM   2097  OD2 ASP A 282      69.402  62.063  45.345  1.00 34.05           O1-
ANISOU 2097  OD2 ASP A 282     5152   3720   4065    120     23    886       O1-
ATOM   2098  N   ILE A 283      71.080  61.719  51.111  1.00 18.19           N  
ANISOU 2098  N   ILE A 283     2780   1776   2358     96     54    612       N  
ATOM   2099  CA  ILE A 283      71.130  62.407  52.397  1.00 17.22           C  
ANISOU 2099  CA  ILE A 283     2615   1622   2306    102     30    561       C  
ATOM   2100  C   ILE A 283      72.555  62.733  52.834  1.00 15.67           C  
ANISOU 2100  C   ILE A 283     2390   1398   2166     39     74    550       C  
ATOM   2101  O   ILE A 283      72.749  63.232  53.951  1.00 17.08           O  
ANISOU 2101  O   ILE A 283     2535   1554   2400     33     54    503       O  
ATOM   2102  CB  ILE A 283      70.391  61.608  53.497  1.00 17.01           C  
ANISOU 2102  CB  ILE A 283     2529   1661   2274    138     -4    495       C  
ATOM   2103  CG1 ILE A 283      70.901  60.161  53.633  1.00 15.56           C  
ANISOU 2103  CG1 ILE A 283     2302   1555   2054    118     26    476       C  
ATOM   2104  CG2 ILE A 283      68.885  61.588  53.175  1.00 19.27           C  
ANISOU 2104  CG2 ILE A 283     2833   1962   2528    200    -54    502       C  
ATOM   2105  CD1 ILE A 283      72.280  59.974  54.342  1.00 17.60           C  
ANISOU 2105  CD1 ILE A 283     2513   1817   2356     69     61    451       C  
ATOM   2106  N   HIS A 284      73.557  62.485  51.992  1.00 17.25           N  
ANISOU 2106  N   HIS A 284     2602   1600   2354     -9    134    591       N  
ATOM   2107  CA  HIS A 284      74.955  62.717  52.336  1.00 18.15           C  
ANISOU 2107  CA  HIS A 284     2674   1695   2527    -72    178    582       C  
ATOM   2108  C   HIS A 284      75.616  63.623  51.307  1.00 18.60           C  
ANISOU 2108  C   HIS A 284     2787   1682   2597   -120    228    645       C  
ATOM   2109  O   HIS A 284      75.499  63.387  50.099  1.00 18.69           O  
ANISOU 2109  O   HIS A 284     2856   1697   2548   -121    262    699       O  
ATOM   2110  CB  HIS A 284      75.707  61.384  52.430  1.00 18.22           C  
ANISOU 2110  CB  HIS A 284     2621   1781   2522    -87    217    564       C  
ATOM   2111  CG  HIS A 284      77.196  61.519  52.507  1.00 18.62           C  
ANISOU 2111  CG  HIS A 284     2621   1820   2633   -151    270    566       C  
ATOM   2112  ND1 HIS A 284      78.049  60.775  51.718  1.00 20.77           N  
ANISOU 2112  ND1 HIS A 284     2876   2125   2889   -177    342    593       N  
ATOM   2113  CD2 HIS A 284      77.987  62.305  53.277  1.00 18.02           C  
ANISOU 2113  CD2 HIS A 284     2504   1705   2637   -194    263    543       C  
ATOM   2114  CE1 HIS A 284      79.299  61.092  52.004  1.00 20.17           C  
ANISOU 2114  CE1 HIS A 284     2742   2035   2888   -232    378    587       C  
ATOM   2115  NE2 HIS A 284      79.290  62.025  52.939  1.00 18.43           N  
ANISOU 2115  NE2 HIS A 284     2506   1770   2725   -247    327    558       N  
ATOM   2116  N   TYR A 285      76.326  64.645  51.788  1.00 17.01           N  
ANISOU 2116  N   TYR A 285     2575   1417   2470   -166    233    637       N  
ATOM   2117  CA  TYR A 285      77.151  65.510  50.950  1.00 20.98           C  
ANISOU 2117  CA  TYR A 285     3122   1852   2998   -229    290    693       C  
ATOM   2118  C   TYR A 285      78.609  65.349  51.355  1.00 19.00           C  
ANISOU 2118  C   TYR A 285     2788   1616   2814   -300    340    672       C  
ATOM   2119  O   TYR A 285      78.928  65.395  52.549  1.00 19.59           O  
ANISOU 2119  O   TYR A 285     2796   1700   2946   -309    302    614       O  
ATOM   2120  CB  TYR A 285      76.736  66.980  51.088  1.00 21.22           C  
ANISOU 2120  CB  TYR A 285     3217   1779   3066   -229    253    706       C  
ATOM   2121  CG  TYR A 285      77.561  67.935  50.251  1.00 20.96           C  
ANISOU 2121  CG  TYR A 285     3240   1666   3060   -301    312    766       C  
ATOM   2122  CD1 TYR A 285      78.716  68.523  50.757  1.00 20.12           C  
ANISOU 2122  CD1 TYR A 285     3088   1521   3037   -379    342    749       C  
ATOM   2123  CD2 TYR A 285      77.181  68.247  48.952  1.00 22.95           C  
ANISOU 2123  CD2 TYR A 285     3592   1879   3249   -294    336    842       C  
ATOM   2124  CE1 TYR A 285      79.465  69.396  49.989  1.00 25.83           C  
ANISOU 2124  CE1 TYR A 285     3861   2168   3785   -452    403    805       C  
ATOM   2125  CE2 TYR A 285      77.922  69.113  48.183  1.00 25.30           C  
ANISOU 2125  CE2 TYR A 285     3950   2099   3564   -364    396    901       C  
ATOM   2126  CZ  TYR A 285      79.060  69.685  48.707  1.00 29.52           C  
ANISOU 2126  CZ  TYR A 285     4434   2595   4186   -444    433    882       C  
ATOM   2127  OH  TYR A 285      79.794  70.555  47.933  1.00 30.81           O  
ANISOU 2127  OH  TYR A 285     4653   2688   4366   -520    493    937       O  
ATOM   2128  N   SER A 286      79.491  65.167  50.370  1.00 19.36           N  
ANISOU 2128  N   SER A 286     2839   1665   2853   -350    424    719       N  
ATOM   2129  CA  SER A 286      80.929  65.171  50.612  1.00 23.67           C  
ANISOU 2129  CA  SER A 286     3301   2217   3475   -423    480    707       C  
ATOM   2130  C   SER A 286      81.565  66.339  49.870  1.00 24.53           C  
ANISOU 2130  C   SER A 286     3462   2239   3618   -498    538    761       C  
ATOM   2131  O   SER A 286      81.226  66.617  48.716  1.00 25.00           O  
ANISOU 2131  O   SER A 286     3618   2265   3617   -498    578    824       O  
ATOM   2132  CB  SER A 286      81.584  63.846  50.193  1.00 28.54           C  
ANISOU 2132  CB  SER A 286     3857   2917   4068   -422    544    707       C  
ATOM   2133  OG  SER A 286      81.503  63.649  48.798  1.00 37.71           O  
ANISOU 2133  OG  SER A 286     5094   4075   5158   -426    616    767       O  
ATOM   2134  N   GLY A 287      82.480  67.039  50.546  1.00 22.87           N  
ANISOU 2134  N   GLY A 287     3193   1992   3504   -565    540    738       N  
ATOM   2135  CA  GLY A 287      83.133  68.192  49.967  1.00 25.96           C  
ANISOU 2135  CA  GLY A 287     3628   2296   3939   -647    595    784       C  
ATOM   2136  C   GLY A 287      84.592  68.237  50.375  1.00 25.30           C  
ANISOU 2136  C   GLY A 287     3432   2226   3957   -734    641    762       C  
ATOM   2137  O   GLY A 287      85.044  67.455  51.217  1.00 24.64           O  
ANISOU 2137  O   GLY A 287     3237   2213   3912   -723    613    707       O  
ATOM   2138  N   ARG A 288      85.325  69.158  49.759  1.00 26.36           N  
ANISOU 2138  N   ARG A 288     3593   2289   4134   -821    709    807       N  
ATOM   2139  CA  ARG A 288      86.738  69.321  50.081  1.00 28.59           C  
ANISOU 2139  CA  ARG A 288     3763   2588   4513   -910    747    782       C  
ATOM   2140  C   ARG A 288      87.151  70.764  49.845  1.00 30.46           C  
ANISOU 2140  C   ARG A 288     4055   2740   4777   -989    749    800       C  
ATOM   2141  O   ARG A 288      87.015  71.277  48.729  1.00 29.68           O  
ANISOU 2141  O   ARG A 288     4054   2612   4610  -1000    788    855       O  
ATOM   2142  CB  ARG A 288      87.604  68.372  49.248  1.00 32.59           C  
ANISOU 2142  CB  ARG A 288     4203   3183   4996   -920    840    796       C  
ATOM   2143  CG  ARG A 288      89.071  68.746  49.236  1.00 44.42           C  
ANISOU 2143  CG  ARG A 288     5604   4696   6579  -1012    890    784       C  
ATOM   2144  CD  ARG A 288      89.929  67.606  48.724  1.00 52.53           C  
ANISOU 2144  CD  ARG A 288     6535   5819   7606  -1004    971    779       C  
ATOM   2145  NE  ARG A 288      90.511  66.833  49.816  1.00 56.76           N  
ANISOU 2145  NE  ARG A 288     6920   6412   8233   -995    937    724       N  
ATOM   2146  N   PHE A 289      87.658  71.410  50.897  1.00 26.20           N  
ANISOU 2146  N   PHE A 289     3458   2162   4335  -1045    700    754       N  
ATOM   2147  CA  PHE A 289      88.303  72.705  50.774  1.00 28.73           C  
ANISOU 2147  CA  PHE A 289     3809   2411   4696  -1137    706    764       C  
ATOM   2148  C   PHE A 289      89.752  72.530  50.338  1.00 34.98           C  
ANISOU 2148  C   PHE A 289     4496   3260   5533  -1218    784    769       C  
ATOM   2149  O   PHE A 289      90.446  71.616  50.794  1.00 36.89           O  
ANISOU 2149  O   PHE A 289     4605   3585   5828  -1218    796    732       O  
ATOM   2150  CB  PHE A 289      88.286  73.455  52.108  1.00 30.06           C  
ANISOU 2150  CB  PHE A 289     3959   2517   4946  -1167    617    705       C  
ATOM   2151  CG  PHE A 289      86.924  73.892  52.554  1.00 29.10           C  
ANISOU 2151  CG  PHE A 289     3945   2320   4789  -1094    543    696       C  
ATOM   2152  CD1 PHE A 289      86.313  74.994  51.980  1.00 31.31           C  
ANISOU 2152  CD1 PHE A 289     4366   2506   5026  -1091    535    737       C  
ATOM   2153  CD2 PHE A 289      86.276  73.229  53.578  1.00 28.28           C  
ANISOU 2153  CD2 PHE A 289     3802   2249   4696  -1025    472    643       C  
ATOM   2154  CE1 PHE A 289      85.064  75.406  52.408  1.00 31.87           C  
ANISOU 2154  CE1 PHE A 289     4529   2509   5070  -1015    466    725       C  
ATOM   2155  CE2 PHE A 289      85.030  73.637  54.004  1.00 29.20           C  
ANISOU 2155  CE2 PHE A 289     4013   2319   4764   -946    397    622       C  
ATOM   2156  CZ  PHE A 289      84.427  74.728  53.420  1.00 29.87           C  
ANISOU 2156  CZ  PHE A 289     4229   2289   4830   -945    405    669       C  
ATOM   2157  N   SER A 290      90.218  73.423  49.471  1.00 35.15           N  
ANISOU 2157  N   SER A 290     4577   3238   5541  -1285    834    815       N  
ATOM   2158  CA  SER A 290      91.621  73.416  49.087  1.00 38.71           C  
ANISOU 2158  CA  SER A 290     4930   3735   6045  -1370    909    819       C  
ATOM   2159  C   SER A 290      92.431  74.516  49.764  1.00 40.22           C  
ANISOU 2159  C   SER A 290     5082   3871   6329  -1474    875    793       C  
ATOM   2160  O   SER A 290      93.660  74.511  49.649  1.00 40.18           O  
ANISOU 2160  O   SER A 290     4973   3908   6385  -1549    925    786       O  
ATOM   2161  CB  SER A 290      91.760  73.532  47.561  1.00 43.16           C  
ANISOU 2161  CB  SER A 290     5569   4302   6530  -1382   1001    891       C  
ATOM   2162  OG  SER A 290      91.337  74.797  47.095  1.00 51.01           O  
ANISOU 2162  OG  SER A 290     6694   5194   7493  -1415    983    940       O  
ATOM   2163  N   SER A 291      91.787  75.442  50.473  1.00 37.53           N  
ANISOU 2163  N   SER A 291     4822   3437   6001  -1479    792    775       N  
ATOM   2164  CA  SER A 291      92.516  76.498  51.163  1.00 42.23           C  
ANISOU 2164  CA  SER A 291     5392   3976   6679  -1580    753    744       C  
ATOM   2165  C   SER A 291      91.698  76.995  52.349  1.00 42.11           C  
ANISOU 2165  C   SER A 291     5430   3889   6681  -1550    645    690       C  
ATOM   2166  O   SER A 291      90.506  76.700  52.483  1.00 43.34           O  
ANISOU 2166  O   SER A 291     5659   4026   6783  -1454    607    689       O  
ATOM   2167  CB  SER A 291      92.854  77.659  50.222  1.00 46.28           C  
ANISOU 2167  CB  SER A 291     5994   4414   7177  -1658    800    808       C  
ATOM   2168  OG  SER A 291      91.698  78.419  49.921  1.00 48.56           O  
ANISOU 2168  OG  SER A 291     6444   4603   7404  -1610    760    846       O  
ATOM   2169  N   VAL A 292      92.369  77.748  53.220  1.00 40.09           N  
ANISOU 2169  N   VAL A 292     5135   3597   6502  -1635    595    641       N  
ATOM   2170  CA  VAL A 292      91.726  78.400  54.356  1.00 42.36           C  
ANISOU 2170  CA  VAL A 292     5483   3806   6806  -1622    495    583       C  
ATOM   2171  C   VAL A 292      91.046  79.673  53.875  1.00 39.75           C  
ANISOU 2171  C   VAL A 292     5321   3347   6434  -1630    487    626       C  
ATOM   2172  O   VAL A 292      91.564  80.379  53.003  1.00 43.11           O  
ANISOU 2172  O   VAL A 292     5786   3736   6860  -1699    537    685       O  
ATOM   2173  CB  VAL A 292      92.760  78.694  55.460  1.00 44.79           C  
ANISOU 2173  CB  VAL A 292     5686   4129   7204  -1713    441    510       C  
ATOM   2174  CG1 VAL A 292      92.125  79.445  56.620  1.00 42.53           C  
ANISOU 2174  CG1 VAL A 292     5476   3757   6925  -1705    342    444       C  
ATOM   2175  CG2 VAL A 292      93.395  77.399  55.950  1.00 45.43           C  
ANISOU 2175  CG2 VAL A 292     5595   4338   7327  -1692    433    472       C  
ATOM   2176  N   GLY A 293      89.874  79.972  54.438  1.00 40.16           N  
ANISOU 2176  N   GLY A 293     5471   3331   6456  -1553    420    599       N  
ATOM   2177  CA  GLY A 293      89.108  81.119  53.998  1.00 38.46           C  
ANISOU 2177  CA  GLY A 293     5415   2994   6205  -1537    401    642       C  
ATOM   2178  C   GLY A 293      88.248  80.867  52.782  1.00 40.67           C  
ANISOU 2178  C   GLY A 293     5775   3273   6405  -1452    439    725       C  
ATOM   2179  O   GLY A 293      87.509  81.768  52.364  1.00 44.38           O  
ANISOU 2179  O   GLY A 293     6366   3645   6853  -1418    412    769       O  
ATOM   2180  N   GLU A 294      88.321  79.672  52.204  1.00 37.44           N  
ANISOU 2180  N   GLU A 294     5298   2970   5959  -1412    496    749       N  
ATOM   2181  CA  GLU A 294      87.489  79.331  51.063  1.00 35.64           C  
ANISOU 2181  CA  GLU A 294     5146   2753   5644  -1330    529    822       C  
ATOM   2182  C   GLU A 294      86.034  79.217  51.495  1.00 34.84           C  
ANISOU 2182  C   GLU A 294     5120   2616   5500  -1211    460    803       C  
ATOM   2183  O   GLU A 294      85.731  78.739  52.594  1.00 34.50           O  
ANISOU 2183  O   GLU A 294     5029   2596   5484  -1174    415    731       O  
ATOM   2184  CB  GLU A 294      87.973  78.020  50.448  1.00 34.21           C  
ANISOU 2184  CB  GLU A 294     4870   2696   5431  -1320    605    839       C  
ATOM   2185  CG  GLU A 294      87.198  77.541  49.238  1.00 34.57           C  
ANISOU 2185  CG  GLU A 294     4990   2769   5377  -1241    640    908       C  
ATOM   2186  CD  GLU A 294      87.740  76.232  48.713  1.00 41.36           C  
ANISOU 2186  CD  GLU A 294     5757   3750   6208  -1233    716    914       C  
ATOM   2187  OE1 GLU A 294      88.731  75.731  49.290  1.00 41.16           O  
ANISOU 2187  OE1 GLU A 294     5602   3786   6250  -1285    740    868       O  
ATOM   2188  OE2 GLU A 294      87.178  75.704  47.728  1.00 47.46           O1-
ANISOU 2188  OE2 GLU A 294     6584   4557   6891  -1173    747    962       O1-
ATOM   2189  N   VAL A 295      85.129  79.663  50.628  1.00 33.08           N  
ANISOU 2189  N   VAL A 295     4873   3467   4229  -1075   -155    583       N  
ATOM   2190  CA  VAL A 295      83.691  79.584  50.875  1.00 36.11           C  
ANISOU 2190  CA  VAL A 295     5340   3778   4603   -915   -138    595       C  
ATOM   2191  C   VAL A 295      83.079  78.610  49.878  1.00 28.91           C  
ANISOU 2191  C   VAL A 295     4339   2889   3757   -794   -111    653       C  
ATOM   2192  O   VAL A 295      83.310  78.723  48.667  1.00 32.41           O  
ANISOU 2192  O   VAL A 295     4784   3306   4225   -826    -76    674       O  
ATOM   2193  CB  VAL A 295      83.020  80.965  50.773  1.00 38.49           C  
ANISOU 2193  CB  VAL A 295     5859   3908   4856   -918    -98    564       C  
ATOM   2194  CG1 VAL A 295      81.520  80.838  50.973  1.00 36.79           C  
ANISOU 2194  CG1 VAL A 295     5702   3631   4645   -739    -75    584       C  
ATOM   2195  CG2 VAL A 295      83.616  81.920  51.790  1.00 42.42           C  
ANISOU 2195  CG2 VAL A 295     6463   4372   5281  -1052   -117    492       C  
ATOM   2196  N   GLN A 296      82.299  77.653  50.383  1.00 28.08           N  
ANISOU 2196  N   GLN A 296     4162   2834   3672   -665   -124    677       N  
ATOM   2197  CA  GLN A 296      81.569  76.717  49.539  1.00 27.07           C  
ANISOU 2197  CA  GLN A 296     3963   2722   3599   -554    -99    724       C  
ATOM   2198  C   GLN A 296      80.106  76.711  49.945  1.00 31.31           C  
ANISOU 2198  C   GLN A 296     4562   3210   4125   -417    -91    735       C  
ATOM   2199  O   GLN A 296      79.782  76.725  51.136  1.00 33.17           O  
ANISOU 2199  O   GLN A 296     4817   3457   4329   -383   -108    716       O  
ATOM   2200  CB  GLN A 296      82.160  75.301  49.628  1.00 26.56           C  
ANISOU 2200  CB  GLN A 296     3716   2782   3594   -539   -114    749       C  
ATOM   2201  CG  GLN A 296      83.597  75.237  49.106  1.00 29.66           C  
ANISOU 2201  CG  GLN A 296     4021   3233   4015   -660   -110    744       C  
ATOM   2202  CD  GLN A 296      84.199  73.839  49.090  1.00 31.19           C  
ANISOU 2202  CD  GLN A 296     4033   3535   4282   -627   -110    774       C  
ATOM   2203  OE1 GLN A 296      83.606  72.876  49.570  1.00 30.02           O  
ANISOU 2203  OE1 GLN A 296     3828   3419   4161   -524   -120    800       O  
ATOM   2204  NE2 GLN A 296      85.389  73.727  48.513  1.00 28.92           N  
ANISOU 2204  NE2 GLN A 296     3656   3300   4034   -715    -91    772       N  
ATOM   2205  N   ASP A 297      79.222  76.691  48.952  1.00 26.24           N  
ANISOU 2205  N   ASP A 297     3947   2519   3503   -343    -65    768       N  
ATOM   2206  CA  ASP A 297      77.787  76.658  49.191  1.00 26.04           C  
ANISOU 2206  CA  ASP A 297     3957   2458   3478   -209    -55    789       C  
ATOM   2207  C   ASP A 297      77.261  75.256  48.922  1.00 27.54           C  
ANISOU 2207  C   ASP A 297     4013   2733   3719   -135    -57    824       C  
ATOM   2208  O   ASP A 297      77.526  74.677  47.863  1.00 29.31           O  
ANISOU 2208  O   ASP A 297     4177   2986   3972   -160    -50    843       O  
ATOM   2209  CB  ASP A 297      77.065  77.685  48.316  1.00 32.58           C  
ANISOU 2209  CB  ASP A 297     4908   3177   4293   -172    -34    811       C  
ATOM   2210  CG  ASP A 297      77.364  79.113  48.737  1.00 48.43           C  
ANISOU 2210  CG  ASP A 297     7074   5073   6255   -227    -19    775       C  
ATOM   2211  OD1 ASP A 297      77.392  79.377  49.959  1.00 48.90           O  
ANISOU 2211  OD1 ASP A 297     7172   5125   6285   -229    -18    729       O  
ATOM   2212  OD2 ASP A 297      77.577  79.971  47.852  1.00 56.22           O1-
ANISOU 2212  OD2 ASP A 297     8158   5976   7229   -275     -4    790       O1-
ATOM   2213  N   VAL A 298      76.531  74.709  49.889  1.00 24.77           N  
ANISOU 2213  N   VAL A 298     3624   2416   3372    -52    -60    828       N  
ATOM   2214  CA  VAL A 298      75.960  73.371  49.798  1.00 24.04           C  
ANISOU 2214  CA  VAL A 298     3415   2394   3326     13    -58    859       C  
ATOM   2215  C   VAL A 298      74.452  73.528  49.667  1.00 26.12           C  
ANISOU 2215  C   VAL A 298     3704   2627   3592    121    -43    884       C  
ATOM   2216  O   VAL A 298      73.811  74.166  50.510  1.00 27.33           O  
ANISOU 2216  O   VAL A 298     3921   2743   3718    178    -31    873       O  
ATOM   2217  CB  VAL A 298      76.346  72.520  51.018  1.00 23.92           C  
ANISOU 2217  CB  VAL A 298     3323   2451   3315     15    -72    857       C  
ATOM   2218  CG1 VAL A 298      75.696  71.143  50.948  1.00 27.00           C  
ANISOU 2218  CG1 VAL A 298     3608   2895   3756     80    -60    892       C  
ATOM   2219  CG2 VAL A 298      77.864  72.404  51.108  1.00 24.33           C  
ANISOU 2219  CG2 VAL A 298     3329   2545   3369    -87    -95    843       C  
ATOM   2220  N   ILE A 299      73.885  72.954  48.609  1.00 23.64           N  
ANISOU 2220  N   ILE A 299     3339   2333   3310    145    -42    915       N  
ATOM   2221  CA  ILE A 299      72.499  73.194  48.221  1.00 25.19           C  
ANISOU 2221  CA  ILE A 299     3548   2512   3512    236    -40    949       C  
ATOM   2222  C   ILE A 299      71.622  72.077  48.774  1.00 25.84           C  
ANISOU 2222  C   ILE A 299     3528   2662   3627    299    -32    965       C  
ATOM   2223  O   ILE A 299      71.835  70.897  48.467  1.00 25.25           O  
ANISOU 2223  O   ILE A 299     3368   2643   3584    267    -32    969       O  
ATOM   2224  CB  ILE A 299      72.356  73.282  46.694  1.00 28.67           C  
ANISOU 2224  CB  ILE A 299     3996   2945   3951    211    -55    978       C  
ATOM   2225  CG1 ILE A 299      73.366  74.277  46.109  1.00 33.60           C  
ANISOU 2225  CG1 ILE A 299     4720   3506   4542    129    -56    966       C  
ATOM   2226  CG2 ILE A 299      70.920  73.628  46.315  1.00 32.05           C  
ANISOU 2226  CG2 ILE A 299     4428   3366   4382    308    -68   1025       C  
ATOM   2227  CD1 ILE A 299      73.326  75.651  46.747  1.00 38.29           C  
ANISOU 2227  CD1 ILE A 299     5436   4006   5107    153    -47    955       C  
ATOM   2228  N   ILE A 300      70.610  72.447  49.552  1.00 23.76           N  
ANISOU 2228  N   ILE A 300     3280   2388   3359    388    -14    973       N  
ATOM   2229  CA  ILE A 300      69.663  71.496  50.121  1.00 24.35           C  
ANISOU 2229  CA  ILE A 300     3263   2527   3463    446      3    992       C  
ATOM   2230  C   ILE A 300      68.281  71.834  49.599  1.00 28.93           C  
ANISOU 2230  C   ILE A 300     3821   3109   4060    531      3   1031       C  
ATOM   2231  O   ILE A 300      67.814  72.969  49.757  1.00 31.77           O  
ANISOU 2231  O   ILE A 300     4252   3411   4406    599     17   1036       O  
ATOM   2232  CB  ILE A 300      69.666  71.526  51.655  1.00 28.62           C  
ANISOU 2232  CB  ILE A 300     3822   3073   3979    474     33    970       C  
ATOM   2233  CG1 ILE A 300      71.033  71.113  52.196  1.00 30.82           C  
ANISOU 2233  CG1 ILE A 300     4102   3369   4238    390     17    945       C  
ATOM   2234  CG2 ILE A 300      68.563  70.628  52.197  1.00 30.86           C  
ANISOU 2234  CG2 ILE A 300     4017   3419   4290    535     61    995       C  
ATOM   2235  CD1 ILE A 300      71.184  71.374  53.678  1.00 33.61           C  
ANISOU 2235  CD1 ILE A 300     4502   3728   4541    399     33    921       C  
ATOM   2236  N   GLN A 301      67.622  70.856  48.987  1.00 23.78           N  
ANISOU 2236  N   GLN A 301     3070   2525   3442    528    -10   1058       N  
ATOM   2237  CA  GLN A 301      66.212  70.982  48.653  1.00 27.03           C  
ANISOU 2237  CA  GLN A 301     3425   2970   3876    607    -15   1102       C  
ATOM   2238  C   GLN A 301      65.397  70.424  49.808  1.00 28.05           C  
ANISOU 2238  C   GLN A 301     3485   3146   4028    663     30   1104       C  
ATOM   2239  O   GLN A 301      65.678  69.327  50.296  1.00 28.40           O  
ANISOU 2239  O   GLN A 301     3478   3230   4083    615     46   1091       O  
ATOM   2240  CB  GLN A 301      65.869  70.235  47.365  1.00 26.67           C  
ANISOU 2240  CB  GLN A 301     3308   2983   3842    556    -58   1128       C  
ATOM   2241  CG  GLN A 301      64.394  70.345  46.985  0.60 30.48           C  
ANISOU 2241  CG  GLN A 301     3713   3523   4347    628    -79   1181       C  
ATOM   2242  CD  GLN A 301      63.988  69.396  45.876  0.60 35.04           C  
ANISOU 2242  CD  GLN A 301     4209   4179   4927    555   -124   1198       C  
ATOM   2243  OE1 GLN A 301      64.744  68.502  45.498  0.60 39.12           O  
ANISOU 2243  OE1 GLN A 301     4727   4701   5437    456   -121   1162       O  
ATOM   2244  NE2 GLN A 301      62.781  69.587  45.349  0.60 35.26           N  
ANISOU 2244  NE2 GLN A 301     4164   4268   4964    604   -163   1252       N  
ATOM   2245  N   ASP A 302      64.410  71.180  50.265  1.00 25.23           N  
ANISOU 2245  N   ASP A 302     3127   2781   3679    768     58   1123       N  
ATOM   2246  CA  ASP A 302      63.495  70.685  51.283  1.00 26.44           C  
ANISOU 2246  CA  ASP A 302     3206   2988   3853    824    112   1129       C  
ATOM   2247  C   ASP A 302      62.129  70.437  50.661  1.00 29.14           C  
ANISOU 2247  C   ASP A 302     3427   3405   4242    875     98   1182       C  
ATOM   2248  O   ASP A 302      61.618  71.284  49.923  1.00 29.12           O  
ANISOU 2248  O   ASP A 302     3428   3387   4249    938     68   1218       O  
ATOM   2249  CB  ASP A 302      63.364  71.662  52.450  1.00 29.85           C  
ANISOU 2249  CB  ASP A 302     3719   3363   4259    906    176   1101       C  
ATOM   2250  CG  ASP A 302      62.690  71.025  53.647  1.00 36.34           C  
ANISOU 2250  CG  ASP A 302     4480   4243   5085    937    243   1097       C  
ATOM   2251  OD1 ASP A 302      63.307  70.124  54.250  1.00 38.07           O  
ANISOU 2251  OD1 ASP A 302     4694   4490   5282    864    248   1081       O  
ATOM   2252  OD2 ASP A 302      61.552  71.412  53.981  1.00 42.82           O1-
ANISOU 2252  OD2 ASP A 302     5255   5083   5931   1037    295   1116       O1-
ATOM   2253  N   GLY A 303      61.552  69.271  50.951  1.00 28.28           N  
ANISOU 2253  N   GLY A 303     3208   3377   4159    844    116   1192       N  
ATOM   2254  CA  GLY A 303      60.146  69.022  50.696  1.00 35.26           C  
ANISOU 2254  CA  GLY A 303     3960   4349   5088    892    117   1238       C  
ATOM   2255  C   GLY A 303      59.298  69.598  51.811  1.00 35.61           C  
ANISOU 2255  C   GLY A 303     3984   4399   5149   1009    198   1244       C  
ATOM   2256  O   GLY A 303      59.684  70.562  52.483  1.00 42.64           O  
ANISOU 2256  O   GLY A 303     4983   5208   6011   1073    240   1215       O  
ATOM   2257  N   ASP A 304      58.138  68.995  52.040  1.00 38.84           N  
ANISOU 2257  N   ASP A 304     4254   4902   5600   1030    228   1275       N  
ATOM   2258  CA  ASP A 304      57.220  69.530  53.047  1.00 40.39           C  
ANISOU 2258  CA  ASP A 304     4414   5115   5818   1148    319   1282       C  
ATOM   2259  C   ASP A 304      57.556  69.033  54.453  1.00 35.19           C  
ANISOU 2259  C   ASP A 304     3804   4446   5122   1121    406   1240       C  
ATOM   2260  O   ASP A 304      56.698  68.507  55.161  1.00 37.93           O  
ANISOU 2260  O   ASP A 304     4058   4863   5490   1138    476   1253       O  
ATOM   2261  CB  ASP A 304      55.783  69.183  52.677  1.00 47.51           C  
ANISOU 2261  CB  ASP A 304     5131   6136   6785   1186    317   1341       C  
ATOM   2262  N   ASP A 305      58.810  69.193  54.874  1.00 32.52           N  
ANISOU 2262  N   ASP A 305     3606   4025   4723   1074    400   1193       N  
ATOM   2263  CA  ASP A 305      59.179  68.813  56.232  1.00 34.17           C  
ANISOU 2263  CA  ASP A 305     3873   4229   4881   1049    471   1161       C  
ATOM   2264  C   ASP A 305      58.627  69.815  57.234  1.00 35.15           C  
ANISOU 2264  C   ASP A 305     4048   4326   4982   1161    568   1136       C  
ATOM   2265  O   ASP A 305      58.422  70.992  56.921  1.00 36.37           O  
ANISOU 2265  O   ASP A 305     4248   4421   5150   1254    575   1128       O  
ATOM   2266  CB  ASP A 305      60.697  68.741  56.397  1.00 31.59           C  
ANISOU 2266  CB  ASP A 305     3671   3837   4495    966    426   1124       C  
ATOM   2267  CG  ASP A 305      61.301  67.559  55.686  1.00 34.41           C  
ANISOU 2267  CG  ASP A 305     3982   4218   4874    857    361   1143       C  
ATOM   2268  OD1 ASP A 305      60.824  66.428  55.890  1.00 35.59           O  
ANISOU 2268  OD1 ASP A 305     4045   4428   5049    816    383   1169       O  
ATOM   2269  OD2 ASP A 305      62.261  67.772  54.919  1.00 37.19           O1-
ANISOU 2269  OD2 ASP A 305     4389   4522   5218    812    295   1128       O1-
ATOM   2270  N   TYR A 306      58.383  69.330  58.453  1.00 31.97           N  
ANISOU 2270  N   TYR A 306     3644   3962   4542   1153    652   1123       N  
ATOM   2271  CA  TYR A 306      58.146  70.234  59.571  1.00 32.39           C  
ANISOU 2271  CA  TYR A 306     3787   3976   4544   1235    755   1078       C  
ATOM   2272  C   TYR A 306      59.468  70.725  60.147  1.00 31.83           C  
ANISOU 2272  C   TYR A 306     3894   3823   4377   1181    734   1019       C  
ATOM   2273  O   TYR A 306      59.607  71.909  60.476  1.00 34.30           O  
ANISOU 2273  O   TYR A 306     4323   4055   4654   1241    776    969       O  
ATOM   2274  CB  TYR A 306      57.313  69.538  60.651  1.00 34.98           C  
ANISOU 2274  CB  TYR A 306     4046   4387   4857   1241    861   1089       C  
ATOM   2275  N   ALA A 307      60.460  69.839  60.239  1.00 29.86           N  
ANISOU 2275  N   ALA A 307     3665   3590   4090   1066    669   1027       N  
ATOM   2276  CA  ALA A 307      61.732  70.169  60.865  1.00 29.03           C  
ANISOU 2276  CA  ALA A 307     3705   3435   3892   1001    640    980       C  
ATOM   2277  C   ALA A 307      62.833  69.371  60.187  1.00 29.42           C  
ANISOU 2277  C   ALA A 307     3734   3490   3955    899    533   1007       C  
ATOM   2278  O   ALA A 307      62.572  68.398  59.478  1.00 27.26           O  
ANISOU 2278  O   ALA A 307     3349   3260   3749    872    500   1055       O  
ATOM   2279  CB  ALA A 307      61.702  69.888  62.372  1.00 29.72           C  
ANISOU 2279  CB  ALA A 307     3848   3561   3883    982    716    962       C  
ATOM   2280  N   LEU A 308      64.076  69.794  60.414  1.00 27.56           N  
ANISOU 2280  N   LEU A 308     3607   3209   3656    839    483    971       N  
ATOM   2281  CA  LEU A 308      65.232  69.132  59.829  1.00 26.59           C  
ANISOU 2281  CA  LEU A 308     3466   3090   3548    750    390    992       C  
ATOM   2282  C   LEU A 308      66.422  69.306  60.760  1.00 32.72           C  
ANISOU 2282  C   LEU A 308     4341   3862   4228    681    360    964       C  
ATOM   2283  O   LEU A 308      66.600  70.377  61.347  1.00 33.77           O  
ANISOU 2283  O   LEU A 308     4588   3955   4290    688    384    906       O  
ATOM   2284  CB  LEU A 308      65.546  69.707  58.438  1.00 26.13           C  
ANISOU 2284  CB  LEU A 308     3406   2976   3546    749    333    984       C  
ATOM   2285  CG  LEU A 308      66.272  68.821  57.429  1.00 32.67           C  
ANISOU 2285  CG  LEU A 308     4168   3819   4428    679    261   1015       C  
ATOM   2286  CD1 LEU A 308      65.483  67.547  57.165  1.00 31.88           C  
ANISOU 2286  CD1 LEU A 308     3946   3778   4388    680    277   1065       C  
ATOM   2287  CD2 LEU A 308      66.506  69.598  56.131  1.00 29.69           C  
ANISOU 2287  CD2 LEU A 308     3811   3385   4083    678    217   1003       C  
ATOM   2288  N   ASP A 309      67.211  68.239  60.913  1.00 27.32           N  
ANISOU 2288  N   ASP A 309     3613   3223   3544    616    309   1006       N  
ATOM   2289  CA  ASP A 309      68.485  68.266  61.625  1.00 28.86           C  
ANISOU 2289  CA  ASP A 309     3871   3434   3660    542    253    998       C  
ATOM   2290  C   ASP A 309      69.599  67.984  60.625  1.00 33.54           C  
ANISOU 2290  C   ASP A 309     4420   4011   4311    488    171   1013       C  
ATOM   2291  O   ASP A 309      69.527  67.008  59.872  1.00 36.91           O  
ANISOU 2291  O   ASP A 309     4753   4448   4823    489    160   1058       O  
ATOM   2292  CB  ASP A 309      68.545  67.225  62.753  1.00 29.71           C  
ANISOU 2292  CB  ASP A 309     3959   3613   3715    521    262   1052       C  
ATOM   2293  CG  ASP A 309      67.637  67.558  63.933  1.00 33.23           C  
ANISOU 2293  CG  ASP A 309     4469   4084   4074    556    349   1031       C  
ATOM   2294  OD1 ASP A 309      67.224  68.729  64.087  1.00 36.68           O  
ANISOU 2294  OD1 ASP A 309     4987   4477   4471    590    397    961       O  
ATOM   2295  OD2 ASP A 309      67.347  66.633  64.723  1.00 38.15           O1-
ANISOU 2295  OD2 ASP A 309     5065   4763   4666    550    376   1085       O1-
ATOM   2296  N   ILE A 310      70.624  68.828  60.621  1.00 26.46           N  
ANISOU 2296  N   ILE A 310     3593   3090   3369    433    122    971       N  
ATOM   2297  CA  ILE A 310      71.754  68.702  59.706  1.00 25.28           C  
ANISOU 2297  CA  ILE A 310     3405   2931   3271    376     54    978       C  
ATOM   2298  C   ILE A 310      73.018  68.566  60.541  1.00 27.98           C  
ANISOU 2298  C   ILE A 310     3760   3326   3546    301    -10    988       C  
ATOM   2299  O   ILE A 310      73.231  69.355  61.468  1.00 30.39           O  
ANISOU 2299  O   ILE A 310     4159   3638   3748    266    -16    946       O  
ATOM   2300  CB  ILE A 310      71.858  69.917  58.770  1.00 27.40           C  
ANISOU 2300  CB  ILE A 310     3734   3124   3553    367     51    924       C  
ATOM   2301  CG1 ILE A 310      70.541  70.143  58.021  1.00 33.27           C  
ANISOU 2301  CG1 ILE A 310     4463   3826   4353    451    104    925       C  
ATOM   2302  CG2 ILE A 310      73.005  69.744  57.792  1.00 26.46           C  
ANISOU 2302  CG2 ILE A 310     3569   3001   3485    302     -6    932       C  
ATOM   2303  CD1 ILE A 310      70.514  71.433  57.235  1.00 35.42           C  
ANISOU 2303  CD1 ILE A 310     4814   4015   4629    458    106    884       C  
ATOM   2304  N   THR A 311      73.849  67.568  60.224  1.00 25.40           N  
ANISOU 2304  N   THR A 311     3339   3036   3277    277    -56   1043       N  
ATOM   2305  CA  THR A 311      75.105  67.319  60.934  1.00 25.96           C  
ANISOU 2305  CA  THR A 311     3389   3172   3301    215   -129   1073       C  
ATOM   2306  C   THR A 311      76.278  67.508  59.978  1.00 25.71           C  
ANISOU 2306  C   THR A 311     3307   3132   3328    160   -178   1062       C  
ATOM   2307  O   THR A 311      76.304  66.905  58.901  1.00 27.00           O  
ANISOU 2307  O   THR A 311     3398   3268   3594    184   -159   1081       O  
ATOM   2308  CB  THR A 311      75.151  65.899  61.517  1.00 28.85           C  
ANISOU 2308  CB  THR A 311     3677   3594   3690    245   -137   1164       C  
ATOM   2309  OG1 THR A 311      74.037  65.697  62.399  1.00 34.92           O  
ANISOU 2309  OG1 THR A 311     4491   4374   4401    288    -81   1177       O  
ATOM   2310  CG2 THR A 311      76.446  65.675  62.295  1.00 34.04           C  
ANISOU 2310  CG2 THR A 311     4305   4331   4298    191   -224   1210       C  
ATOM   2311  N   LEU A 312      77.252  68.328  60.372  1.00 26.38           N  
ANISOU 2311  N   LEU A 312     3433   3244   3345     78   -235   1029       N  
ATOM   2312  CA  LEU A 312      78.482  68.503  59.604  1.00 26.38           C  
ANISOU 2312  CA  LEU A 312     3373   3254   3395     12   -281   1023       C  
ATOM   2313  C   LEU A 312      79.659  67.943  60.388  1.00 28.24           C  
ANISOU 2313  C   LEU A 312     3529   3594   3608    -33   -362   1081       C  
ATOM   2314  O   LEU A 312      79.855  68.299  61.556  1.00 29.53           O  
ANISOU 2314  O   LEU A 312     3745   3815   3659    -79   -408   1078       O  
ATOM   2315  CB  LEU A 312      78.732  69.977  59.264  1.00 26.66           C  
ANISOU 2315  CB  LEU A 312     3511   3238   3383    -63   -283    939       C  
ATOM   2316  CG  LEU A 312      80.040  70.210  58.489  1.00 39.02           C  
ANISOU 2316  CG  LEU A 312     5013   4820   4993   -147   -325    932       C  
ATOM   2317  CD1 LEU A 312      79.812  71.099  57.286  1.00 42.03           C  
ANISOU 2317  CD1 LEU A 312     5457   5105   5407   -165   -280    878       C  
ATOM   2318  CD2 LEU A 312      81.135  70.786  59.383  1.00 41.87           C  
ANISOU 2318  CD2 LEU A 312     5387   5255   5267   -261   -403    915       C  
ATOM   2319  N   ASN A 313      80.440  67.074  59.744  1.00 27.16           N  
ANISOU 2319  N   ASN A 313     3263   3482   3574    -19   -377   1136       N  
ATOM   2320  CA  ASN A 313      81.630  66.463  60.321  1.00 33.76           C  
ANISOU 2320  CA  ASN A 313     3992   4418   4416    -43   -455   1207       C  
ATOM   2321  C   ASN A 313      82.826  66.741  59.417  1.00 36.37           C  
ANISOU 2321  C   ASN A 313     4236   4765   4817   -104   -477   1191       C  
ATOM   2322  O   ASN A 313      82.720  66.645  58.192  1.00 33.72           O  
ANISOU 2322  O   ASN A 313     3878   4362   4571    -83   -415   1165       O  
ATOM   2323  CB  ASN A 313      81.467  64.945  60.481  1.00 42.45           C  
ANISOU 2323  CB  ASN A 313     5001   5532   5596     54   -438   1307       C  
ATOM   2324  CG  ASN A 313      80.061  64.540  60.896  1.00 56.99           C  
ANISOU 2324  CG  ASN A 313     6918   7327   7409    122   -378   1316       C  
ATOM   2325  OD1 ASN A 313      79.191  64.310  60.053  1.00 56.39           O  
ANISOU 2325  OD1 ASN A 313     6856   7171   7398    169   -301   1289       O  
ATOM   2326  ND2 ASN A 313      79.841  64.424  62.198  1.00 62.14           N  
ANISOU 2326  ND2 ASN A 313     7613   8039   7959    122   -412   1356       N  
ATOM   2327  N   THR A 314      83.974  67.055  60.011  1.00 37.92           N  
ANISOU 2327  N   THR A 314     4379   5059   4968   -185   -564   1209       N  
ATOM   2328  CA  THR A 314      85.128  67.489  59.232  1.00 44.40           C  
ANISOU 2328  CA  THR A 314     5119   5907   5844   -263   -583   1185       C  
ATOM   2329  C   THR A 314      86.235  66.447  59.104  1.00 55.41           C  
ANISOU 2329  C   THR A 314     6325   7385   7344   -227   -615   1276       C  
ATOM   2330  O   THR A 314      87.245  66.733  58.454  1.00 60.31           O  
ANISOU 2330  O   THR A 314     6856   8039   8019   -288   -623   1262       O  
ATOM   2331  CB  THR A 314      85.706  68.774  59.826  1.00 48.07           C  
ANISOU 2331  CB  THR A 314     5652   6422   6191   -407   -653   1124       C  
ATOM   2332  OG1 THR A 314      85.776  68.643  61.249  1.00 53.33           O  
ANISOU 2332  OG1 THR A 314     6334   7182   6748   -426   -736   1165       O  
ATOM   2333  CG2 THR A 314      84.825  69.959  59.477  1.00 43.62           C  
ANISOU 2333  CG2 THR A 314     5267   5743   5566   -444   -593   1021       C  
ATOM   2334  N   ASN A 315      86.084  65.263  59.698  1.00 62.48           N  
ANISOU 2334  N   ASN A 315     7157   8310   8273   -127   -628   1372       N  
ATOM   2335  CA  ASN A 315      87.013  64.139  59.520  1.00 69.39           C  
ANISOU 2335  CA  ASN A 315     7855   9239   9270    -58   -640   1470       C  
ATOM   2336  C   ASN A 315      88.472  64.575  59.692  1.00 74.89           C  
ANISOU 2336  C   ASN A 315     8424  10062   9968   -147   -729   1491       C  
ATOM   2337  O   ASN A 315      89.262  64.618  58.748  1.00 77.26           O  
ANISOU 2337  O   ASN A 315     8624  10367  10367   -167   -693   1473       O  
ATOM   2338  CB  ASN A 315      86.816  63.477  58.152  1.00 70.52           C  
ANISOU 2338  CB  ASN A 315     7960   9279   9556     16   -523   1452       C  
ATOM   2339  N   GLY A 316      88.809  64.892  60.937  1.00 73.17           N  
ANISOU 2339  N   GLY A 316     8210   9957   9633   -208   -844   1529       N  
ATOM   2340  CA  GLY A 316      90.135  65.352  61.266  1.00 68.85           C  
ANISOU 2340  CA  GLY A 316     7542   9552   9065   -312   -949   1551       C  
ATOM   2341  C   GLY A 316      90.100  66.652  62.039  1.00 61.71           C  
ANISOU 2341  C   GLY A 316     6763   8697   7986   -470  -1026   1471       C  
ATOM   2342  O   GLY A 316      89.063  67.057  62.571  1.00 62.76           O  
ANISOU 2342  O   GLY A 316     7072   8768   8006   -477  -1008   1420       O  
ATOM   2343  N   PRO A 317      91.241  67.340  62.112  1.00 52.93           N  
ANISOU 2343  N   PRO A 317     5565   7696   6849   -604  -1107   1455       N  
ATOM   2344  CA  PRO A 317      91.300  68.603  62.855  1.00 53.80           C  
ANISOU 2344  CA  PRO A 317     5803   7850   6788   -776  -1181   1370       C  
ATOM   2345  C   PRO A 317      90.694  69.784  62.121  1.00 53.38           C  
ANISOU 2345  C   PRO A 317     5925   7654   6701   -856  -1089   1228       C  
ATOM   2346  O   PRO A 317      90.654  70.882  62.688  1.00 54.08           O  
ANISOU 2346  O   PRO A 317     6148   7747   6652   -995  -1129   1144       O  
ATOM   2347  CB  PRO A 317      92.805  68.805  63.048  1.00 54.62           C  
ANISOU 2347  CB  PRO A 317     5724   8127   6902   -894  -1295   1412       C  
ATOM   2348  CG  PRO A 317      93.400  68.191  61.838  1.00 53.55           C  
ANISOU 2348  CG  PRO A 317     5416   7972   6959   -814  -1220   1450       C  
ATOM   2349  CD  PRO A 317      92.533  67.005  61.490  1.00 52.67           C  
ANISOU 2349  CD  PRO A 317     5313   7752   6948   -612  -1125   1508       C  
ATOM   2350  N   ASP A 318      90.232  69.592  60.887  1.00 50.40           N  
ANISOU 2350  N   ASP A 318     5558   7149   6443   -773   -968   1200       N  
ATOM   2351  CA  ASP A 318      89.745  70.708  60.088  1.00 48.18           C  
ANISOU 2351  CA  ASP A 318     5430   6735   6140   -842   -886   1083       C  
ATOM   2352  C   ASP A 318      88.589  71.414  60.788  1.00 43.06           C  
ANISOU 2352  C   ASP A 318     5002   6002   5358   -852   -870   1013       C  
ATOM   2353  O   ASP A 318      87.723  70.775  61.393  1.00 41.97           O  
ANISOU 2353  O   ASP A 318     4907   5849   5190   -745   -859   1051       O  
ATOM   2354  CB  ASP A 318      89.310  70.218  58.704  1.00 47.20           C  
ANISOU 2354  CB  ASP A 318     5283   6499   6153   -735   -765   1081       C  
ATOM   2355  CG  ASP A 318      90.389  69.406  58.007  1.00 55.99           C  
ANISOU 2355  CG  ASP A 318     6182   7686   7407   -704   -757   1148       C  
ATOM   2356  OD1 ASP A 318      90.782  68.349  58.547  1.00 59.39           O  
ANISOU 2356  OD1 ASP A 318     6472   8206   7886   -621   -805   1247       O  
ATOM   2357  OD2 ASP A 318      90.836  69.816  56.914  1.00 57.52           O1-
ANISOU 2357  OD2 ASP A 318     6348   7842   7663   -758   -696   1104       O1-
ATOM   2358  N   LYS A 319      88.598  72.744  60.719  1.00 37.37           N  
ANISOU 2358  N   LYS A 319     4422   5222   4556   -985   -860    910       N  
ATOM   2359  CA  LYS A 319      87.581  73.588  61.332  1.00 40.75           C  
ANISOU 2359  CA  LYS A 319     5068   5554   4860  -1002   -829    828       C  
ATOM   2360  C   LYS A 319      86.848  74.348  60.236  1.00 38.44           C  
ANISOU 2360  C   LYS A 319     4905   5090   4612   -980   -718    756       C  
ATOM   2361  O   LYS A 319      87.484  74.913  59.340  1.00 37.50           O  
ANISOU 2361  O   LYS A 319     4767   4940   4542  -1063   -698    725       O  
ATOM   2362  CB  LYS A 319      88.206  74.567  62.328  1.00 45.23           C  
ANISOU 2362  CB  LYS A 319     5717   6189   5278  -1185   -915    765       C  
ATOM   2363  CG  LYS A 319      88.855  73.898  63.525  1.00 53.13           C  
ANISOU 2363  CG  LYS A 319     6608   7372   6206  -1216  -1041    840       C  
ATOM   2364  CD  LYS A 319      87.991  74.051  64.768  1.00 55.35           C  
ANISOU 2364  CD  LYS A 319     7051   7647   6333  -1205  -1049    811       C  
ATOM   2365  CE  LYS A 319      88.580  73.283  65.939  1.00 58.01           C  
ANISOU 2365  CE  LYS A 319     7281   8172   6590  -1225  -1179    905       C  
ATOM   2366  NZ  LYS A 319      88.787  71.845  65.597  1.00 58.38           N  
ANISOU 2366  NZ  LYS A 319     7124   8282   6776  -1071  -1192   1046       N  
ATOM   2367  N   VAL A 320      85.517  74.361  60.308  1.00 36.17           N  
ANISOU 2367  N   VAL A 320     4741   4696   4306   -867   -646    735       N  
ATOM   2368  CA  VAL A 320      84.677  74.959  59.270  1.00 37.33           C  
ANISOU 2368  CA  VAL A 320     4997   4686   4500   -815   -545    689       C  
ATOM   2369  C   VAL A 320      83.584  75.789  59.934  1.00 39.96           C  
ANISOU 2369  C   VAL A 320     5530   4919   4735   -792   -499    619       C  
ATOM   2370  O   VAL A 320      82.932  75.323  60.875  1.00 42.19           O  
ANISOU 2370  O   VAL A 320     5834   5235   4962   -723   -502    636       O  
ATOM   2371  CB  VAL A 320      84.055  73.885  58.353  1.00 38.45           C  
ANISOU 2371  CB  VAL A 320     5043   4802   4765   -662   -488    754       C  
ATOM   2372  CG1 VAL A 320      83.130  74.526  57.329  1.00 36.59           C  
ANISOU 2372  CG1 VAL A 320     4921   4420   4563   -611   -400    714       C  
ATOM   2373  CG2 VAL A 320      85.142  73.073  57.645  1.00 36.63           C  
ANISOU 2373  CG2 VAL A 320     4625   4656   4638   -677   -513    813       C  
ATOM   2374  N   GLY A 321      83.396  77.034  59.455  1.00 34.81           N  
ANISOU 2374  N   GLY A 321     5027   4136   4061   -849   -447    543       N  
ATOM   2375  CA  GLY A 321      82.268  77.845  59.870  1.00 34.29           C  
ANISOU 2375  CA  GLY A 321     5151   3947   3932   -798   -378    479       C  
ATOM   2376  C   GLY A 321      81.056  77.625  58.970  1.00 34.56           C  
ANISOU 2376  C   GLY A 321     5196   3882   4055   -635   -293    509       C  
ATOM   2377  O   GLY A 321      81.147  77.013  57.909  1.00 32.05           O  
ANISOU 2377  O   GLY A 321     4766   3575   3837   -587   -287    565       O  
ATOM   2378  N   ALA A 322      79.901  78.129  59.406  1.00 31.21           N  
ANISOU 2378  N   ALA A 322     4905   3365   3589   -551   -226    471       N  
ATOM   2379  CA  ALA A 322      78.684  77.824  58.668  1.00 32.29           C  
ANISOU 2379  CA  ALA A 322     5027   3434   3808   -391   -158    510       C  
ATOM   2380  C   ALA A 322      77.625  78.899  58.852  1.00 30.99           C  
ANISOU 2380  C   ALA A 322     5037   3127   3611   -324    -73    454       C  
ATOM   2381  O   ALA A 322      77.504  79.510  59.917  1.00 31.86           O  
ANISOU 2381  O   ALA A 322     5270   3211   3624   -359    -51    386       O  
ATOM   2382  CB  ALA A 322      78.106  76.473  59.085  1.00 29.37           C  
ANISOU 2382  CB  ALA A 322     4531   3165   3465   -284   -164    576       C  
ATOM   2383  N   GLN A 323      76.839  79.091  57.793  1.00 30.54           N  
ANISOU 2383  N   GLN A 323     4986   2982   3635   -221    -23    485       N  
ATOM   2384  CA  GLN A 323      75.726  80.025  57.753  1.00 30.77           C  
ANISOU 2384  CA  GLN A 323     5152   2874   3665   -121     61    456       C  
ATOM   2385  C   GLN A 323      74.597  79.386  56.958  1.00 30.35           C  
ANISOU 2385  C   GLN A 323     5001   2826   3704     36     89    531       C  
ATOM   2386  O   GLN A 323      74.854  78.701  55.964  1.00 31.54           O  
ANISOU 2386  O   GLN A 323     5036   3028   3921     33     50    590       O  
ATOM   2387  CB  GLN A 323      76.153  81.353  57.104  1.00 31.62           C  
ANISOU 2387  CB  GLN A 323     5406   2837   3769   -194     82    416       C  
ATOM   2388  CG  GLN A 323      75.107  82.453  57.126  1.00 34.37           C  
ANISOU 2388  CG  GLN A 323     5917   3021   4121    -89    174    385       C  
ATOM   2389  CD  GLN A 323      75.648  83.771  56.590  1.00 35.47           C  
ANISOU 2389  CD  GLN A 323     6220   3006   4250   -178    196    347       C  
ATOM   2390  OE1 GLN A 323      76.293  83.808  55.539  1.00 35.96           O  
ANISOU 2390  OE1 GLN A 323     6246   3065   4353   -245    158    387       O  
ATOM   2391  NE2 GLN A 323      75.395  84.856  57.314  1.00 35.04           N  
ANISOU 2391  NE2 GLN A 323     6356   2818   4140   -185    266    265       N  
ATOM   2392  N   ILE A 324      73.352  79.599  57.403  1.00 30.15           N  
ANISOU 2392  N   ILE A 324     5020   2755   3680    166    160    524       N  
ATOM   2393  CA  ILE A 324      72.159  79.098  56.717  1.00 29.50           C  
ANISOU 2393  CA  ILE A 324     4844   2682   3681    313    187    593       C  
ATOM   2394  C   ILE A 324      71.500  80.238  55.961  1.00 30.19           C  
ANISOU 2394  C   ILE A 324     5036   2627   3809    394    237    600       C  
ATOM   2395  O   ILE A 324      71.323  81.338  56.505  1.00 31.41           O  
ANISOU 2395  O   ILE A 324     5346   2664   3924    409    298    541       O  
ATOM   2396  CB  ILE A 324      71.144  78.482  57.699  1.00 32.65           C  
ANISOU 2396  CB  ILE A 324     5194   3144   4068    412    237    597       C  
ATOM   2397  CG1 ILE A 324      71.805  77.464  58.621  1.00 39.99           C  
ANISOU 2397  CG1 ILE A 324     6050   4202   4942    332    192    594       C  
ATOM   2398  CG2 ILE A 324      69.948  77.903  56.932  1.00 29.70           C  
ANISOU 2398  CG2 ILE A 324     4701   2798   3785    546    255    671       C  
ATOM   2399  CD1 ILE A 324      71.329  77.599  60.055  1.00 42.42           C  
ANISOU 2399  CD1 ILE A 324     6429   4523   5164    356    251    544       C  
ATOM   2400  N   ILE A 325      71.093  79.969  54.720  1.00 29.57           N  
ANISOU 2400  N   ILE A 325     4877   2554   3805    451    213    675       N  
ATOM   2401  CA  ILE A 325      70.436  80.959  53.876  1.00 31.72           C  
ANISOU 2401  CA  ILE A 325     5230   2703   4119    540    245    708       C  
ATOM   2402  C   ILE A 325      69.098  80.397  53.412  1.00 33.95           C  
ANISOU 2402  C   ILE A 325     5389   3039   4470    690    254    782       C  
ATOM   2403  O   ILE A 325      69.039  79.294  52.855  1.00 30.63           O  
ANISOU 2403  O   ILE A 325     4823   2734   4082    677    203    831       O  
ATOM   2404  CB  ILE A 325      71.314  81.347  52.674  1.00 30.50           C  
ANISOU 2404  CB  ILE A 325     5112   2502   3973    443    196    734       C  
ATOM   2405  CG1 ILE A 325      72.740  81.639  53.153  1.00 34.36           C  
ANISOU 2405  CG1 ILE A 325     5675   2982   4398    270    175    663       C  
ATOM   2406  CG2 ILE A 325      70.714  82.546  51.953  1.00 31.18           C  
ANISOU 2406  CG2 ILE A 325     5319   2439   4088    528    232    770       C  
ATOM   2407  CD1 ILE A 325      73.663  82.152  52.074  1.00 34.70           C  
ANISOU 2407  CD1 ILE A 325     5769   2971   4443    160    144    680       C  
ATOM   2408  N   SER A 326      68.034  81.158  53.640  1.00 34.95           N  
ANISOU 2408  N   SER A 326     5573   3083   4624    829    323    790       N  
ATOM   2409  CA  SER A 326      66.683  80.742  53.298  1.00 31.08           C  
ANISOU 2409  CA  SER A 326     4959   2649   4202    978    336    862       C  
ATOM   2410  C   SER A 326      66.414  80.966  51.812  1.00 31.09           C  
ANISOU 2410  C   SER A 326     4929   2630   4252   1014    280    951       C  
ATOM   2411  O   SER A 326      67.145  81.702  51.147  1.00 32.78           O  
ANISOU 2411  O   SER A 326     5254   2752   4449    948    257    955       O  
ATOM   2412  CB  SER A 326      65.679  81.512  54.155  1.00 33.77           C  
ANISOU 2412  CB  SER A 326     5365   2909   4556   1121    440    836       C  
ATOM   2413  OG  SER A 326      65.434  82.797  53.611  1.00 34.75           O  
ANISOU 2413  OG  SER A 326     5616   2877   4709   1200    472    858       O  
ATOM   2414  N   PRO A 327      65.371  80.329  51.260  1.00 30.91           N  
ANISOU 2414  N   PRO A 327     4758   2701   4285   1106    256   1027       N  
ATOM   2415  CA  PRO A 327      65.088  80.512  49.824  1.00 35.81           C  
ANISOU 2415  CA  PRO A 327     5349   3321   4938   1132    191   1119       C  
ATOM   2416  C   PRO A 327      64.869  81.962  49.430  1.00 35.70           C  
ANISOU 2416  C   PRO A 327     5479   3146   4939   1219    220   1154       C  
ATOM   2417  O   PRO A 327      65.086  82.319  48.264  1.00 38.08           O  
ANISOU 2417  O   PRO A 327     5816   3415   5238   1195    164   1219       O  
ATOM   2418  CB  PRO A 327      63.819  79.674  49.604  1.00 39.41           C  
ANISOU 2418  CB  PRO A 327     5619   3906   5448   1229    172   1183       C  
ATOM   2419  CG  PRO A 327      63.816  78.675  50.714  1.00 38.52           C  
ANISOU 2419  CG  PRO A 327     5425   3886   5324   1193    208   1123       C  
ATOM   2420  CD  PRO A 327      64.455  79.355  51.887  1.00 34.16           C  
ANISOU 2420  CD  PRO A 327     5019   3235   4725   1170    279   1035       C  
ATOM   2421  N   SER A 328      64.441  82.808  50.368  1.00 36.07           N  
ANISOU 2421  N   SER A 328     5620   3085   4999   1320    312   1114       N  
ATOM   2422  CA ASER A 328      64.217  84.221  50.101  0.13 39.31           C  
ANISOU 2422  CA ASER A 328     6187   3317   5433   1415    358   1143       C  
ATOM   2423  CA BSER A 328      64.220  84.220  50.089  0.87 38.30           C  
ANISOU 2423  CA BSER A 328     6058   3189   5304   1415    357   1144       C  
ATOM   2424  C   SER A 328      65.462  85.074  50.307  1.00 39.83           C  
ANISOU 2424  C   SER A 328     6458   3236   5439   1286    383   1068       C  
ATOM   2425  O   SER A 328      65.422  86.277  50.031  1.00 37.48           O  
ANISOU 2425  O   SER A 328     6316   2768   5156   1342    422   1089       O  
ATOM   2426  CB ASER A 328      63.085  84.753  50.988  0.13 41.33           C  
ANISOU 2426  CB ASER A 328     6449   3514   5741   1600    464   1133       C  
ATOM   2427  CB BSER A 328      63.074  84.760  50.951  0.87 41.84           C  
ANISOU 2427  CB BSER A 328     6512   3578   5807   1602    462   1136       C  
ATOM   2428  OG ASER A 328      62.017  83.826  51.069  0.13 41.35           O  
ANISOU 2428  OG ASER A 328     6243   3675   5792   1691    453   1180       O  
ATOM   2429  OG BSER A 328      63.436  84.805  52.320  0.87 40.97           O  
ANISOU 2429  OG BSER A 328     6482   3436   5650   1556    547   1014       O  
ATOM   2430  N   GLY A 329      66.555  84.493  50.794  1.00 37.25           N  
ANISOU 2430  N   GLY A 329     6136   2971   5049   1116    361    984       N  
ATOM   2431  CA  GLY A 329      67.789  85.226  50.959  1.00 34.66           C  
ANISOU 2431  CA  GLY A 329     5979   2529   4662    969    372    914       C  
ATOM   2432  C   GLY A 329      68.107  85.682  52.366  1.00 39.03           C  
ANISOU 2432  C   GLY A 329     6653   3012   5166    932    452    795       C  
ATOM   2433  O   GLY A 329      69.175  86.270  52.575  1.00 36.87           O  
ANISOU 2433  O   GLY A 329     6519   2655   4836    788    456    727       O  
ATOM   2434  N   GLU A 330      67.220  85.452  53.329  1.00 35.67           N  
ANISOU 2434  N   GLU A 330     6182   2618   4751   1046    517    765       N  
ATOM   2435  CA  GLU A 330      67.542  85.781  54.712  1.00 36.80           C  
ANISOU 2435  CA  GLU A 330     6440   2715   4827    994    592    644       C  
ATOM   2436  C   GLU A 330      68.636  84.847  55.213  1.00 35.76           C  
ANISOU 2436  C   GLU A 330     6245   2723   4620    812    523    591       C  
ATOM   2437  O   GLU A 330      68.652  83.658  54.884  1.00 34.36           O  
ANISOU 2437  O   GLU A 330     5890   2705   4461    793    453    642       O  
ATOM   2438  CB  GLU A 330      66.300  85.673  55.596  1.00 37.27           C  
ANISOU 2438  CB  GLU A 330     6455   2792   4912   1160    686    630       C  
ATOM   2439  N   VAL A 331      69.565  85.389  56.001  1.00 36.26           N  
ANISOU 2439  N   VAL A 331     6453   2725   4600    675    542    490       N  
ATOM   2440  CA  VAL A 331      70.711  84.613  56.464  1.00 34.75           C  
ANISOU 2440  CA  VAL A 331     6203   2664   4337    498    467    447       C  
ATOM   2441  C   VAL A 331      70.682  84.497  57.982  1.00 39.82           C  
ANISOU 2441  C   VAL A 331     6894   3344   4893    470    515    355       C  
ATOM   2442  O   VAL A 331      70.098  85.327  58.688  1.00 36.73           O  
ANISOU 2442  O   VAL A 331     6643   2836   4476    539    617    291       O  
ATOM   2443  CB  VAL A 331      72.057  85.215  55.997  1.00 34.97           C  
ANISOU 2443  CB  VAL A 331     6329   2630   4329    316    418    417       C  
ATOM   2444  CG1 VAL A 331      72.106  85.301  54.479  1.00 35.99           C  
ANISOU 2444  CG1 VAL A 331     6417   2730   4530    335    376    511       C  
ATOM   2445  CG2 VAL A 331      72.282  86.582  56.628  1.00 40.23           C  
ANISOU 2445  CG2 VAL A 331     7232   3116   4938    265    496    320       C  
ATOM   2446  N   SER A 332      71.325  83.442  58.476  1.00 35.13           N  
ANISOU 2446  N   SER A 332     6185   2913   4250    370    444    352       N  
ATOM   2447  CA  SER A 332      71.511  83.190  59.894  1.00 35.68           C  
ANISOU 2447  CA  SER A 332     6291   3050   4217    310    463    277       C  
ATOM   2448  C   SER A 332      72.804  83.836  60.385  1.00 35.70           C  
ANISOU 2448  C   SER A 332     6427   3020   4119    113    426    189       C  
ATOM   2449  O   SER A 332      73.537  84.475  59.628  1.00 35.89           O  
ANISOU 2449  O   SER A 332     6510   2964   4161     23    394    186       O  
ATOM   2450  CB  SER A 332      71.558  81.688  60.151  1.00 35.75           C  
ANISOU 2450  CB  SER A 332     6105   3252   4226    306    397    335       C  
ATOM   2451  OG  SER A 332      72.799  81.174  59.688  1.00 32.71           O  
ANISOU 2451  OG  SER A 332     5640   2949   3839    166    289    362       O  
ATOM   2452  N   HIS A 333      73.102  83.651  61.672  1.00 36.33           N  
ANISOU 2452  N   HIS A 333     6549   3170   4084     32    426    120       N  
ATOM   2453  CA  HIS A 333      74.440  83.949  62.161  1.00 37.83           C  
ANISOU 2453  CA  HIS A 333     6809   3391   4172   -179    356     53       C  
ATOM   2454  C   HIS A 333      75.455  83.148  61.358  1.00 38.39           C  
ANISOU 2454  C   HIS A 333     6709   3583   4293   -269    233    131       C  
ATOM   2455  O   HIS A 333      75.205  81.997  60.989  1.00 36.71           O  
ANISOU 2455  O   HIS A 333     6316   3488   4147   -191    193    221       O  
ATOM   2456  CB  HIS A 333      74.566  83.606  63.651  1.00 47.61           C  
ANISOU 2456  CB  HIS A 333     8083   4734   5274   -246    352     -8       C  
ATOM   2457  CG  HIS A 333      73.688  84.426  64.547  1.00 67.93           C  
ANISOU 2457  CG  HIS A 333    10841   7191   7778   -181    486   -105       C  
ATOM   2458  ND1 HIS A 333      72.518  83.939  65.090  1.00 72.93           N  
ANISOU 2458  ND1 HIS A 333    11435   7859   8417    -26    569    -87       N  
ATOM   2459  CD2 HIS A 333      73.818  85.692  65.009  1.00 74.88           C  
ANISOU 2459  CD2 HIS A 333    11952   7917   8583   -253    560   -225       C  
ATOM   2460  CE1 HIS A 333      71.961  84.873  65.841  1.00 75.67           C  
ANISOU 2460  CE1 HIS A 333    11973   8081   8696      4    695   -192       C  
ATOM   2461  NE2 HIS A 333      72.729  85.947  65.808  1.00 75.79           N  
ANISOU 2461  NE2 HIS A 333    12163   7974   8661   -131    693   -280       N  
ATOM   2462  N   ASP A 334      76.591  83.775  61.054  1.00 37.32           N  
ANISOU 2462  N   ASP A 334     6635   3414   4132   -435    183     95       N  
ATOM   2463  CA  ASP A 334      77.719  83.087  60.423  1.00 37.55           C  
ANISOU 2463  CA  ASP A 334     6506   3566   4196   -542     74    154       C  
ATOM   2464  C   ASP A 334      78.613  82.587  61.550  1.00 39.55           C  
ANISOU 2464  C   ASP A 334     6711   3974   4341   -679     -9    125       C  
ATOM   2465  O   ASP A 334      79.472  83.308  62.061  1.00 43.35           O  
ANISOU 2465  O   ASP A 334     7294   4444   4732   -851    -40     48       O  
ATOM   2466  CB  ASP A 334      78.462  84.018  59.475  1.00 42.41           C  
ANISOU 2466  CB  ASP A 334     7198   4073   4843   -651     69    137       C  
ATOM   2467  CG  ASP A 334      79.367  83.272  58.517  1.00 49.95           C  
ANISOU 2467  CG  ASP A 334     7972   5137   5868   -712    -13    214       C  
ATOM   2468  OD1 ASP A 334      79.291  82.025  58.471  1.00 49.56           O  
ANISOU 2468  OD1 ASP A 334     7742   5227   5860   -643    -57    285       O  
ATOM   2469  OD2 ASP A 334      80.157  83.932  57.810  1.00 53.53           O1-
ANISOU 2469  OD2 ASP A 334     8470   5533   6337   -831    -24    202       O1-
ATOM   2470  N   ILE A 335      78.404  81.343  61.957  1.00 36.18           N  
ANISOU 2470  N   ILE A 335     6131   3695   3922   -609    -49    191       N  
ATOM   2471  CA  ILE A 335      79.016  80.864  63.192  1.00 38.94           C  
ANISOU 2471  CA  ILE A 335     6451   4188   4155   -709   -121    175       C  
ATOM   2472  C   ILE A 335      80.455  80.436  62.938  1.00 39.31           C  
ANISOU 2472  C   ILE A 335     6361   4363   4211   -853   -242    215       C  
ATOM   2473  O   ILE A 335      80.819  79.971  61.849  1.00 42.07           O  
ANISOU 2473  O   ILE A 335     6577   4733   4676   -829   -267    283       O  
ATOM   2474  CB  ILE A 335      78.190  79.719  63.803  1.00 46.82           C  
ANISOU 2474  CB  ILE A 335     7354   5285   5151   -576   -109    238       C  
ATOM   2475  CG1 ILE A 335      78.277  78.475  62.929  1.00 53.89           C  
ANISOU 2475  CG1 ILE A 335     8036   6266   6173   -495   -154    355       C  
ATOM   2476  CG2 ILE A 335      76.741  80.142  63.984  1.00 54.14           C  
ANISOU 2476  CG2 ILE A 335     8393   6093   6083   -427     20    203       C  
ATOM   2477  CD1 ILE A 335      77.624  77.308  63.550  1.00 58.60           C  
ANISOU 2477  CD1 ILE A 335     8539   6960   6766   -392   -150    420       C  
ATOM   2478  N   ARG A 336      81.287  80.611  63.961  1.00 37.39           N  
ANISOU 2478  N   ARG A 336     6280   3767   4161   -381   -550    104       N  
ATOM   2479  CA  ARG A 336      82.678  80.193  63.940  1.00 38.13           C  
ANISOU 2479  CA  ARG A 336     6268   3969   4252   -499   -621     84       C  
ATOM   2480  C   ARG A 336      82.986  79.469  65.241  1.00 39.14           C  
ANISOU 2480  C   ARG A 336     6354   4174   4343   -442   -638    111       C  
ATOM   2481  O   ARG A 336      82.257  79.591  66.228  1.00 39.32           O  
ANISOU 2481  O   ARG A 336     6474   4156   4310   -344   -605    129       O  
ATOM   2482  CB  ARG A 336      83.634  81.383  63.768  1.00 40.51           C  
ANISOU 2482  CB  ARG A 336     6685   4252   4454   -662   -688     15       C  
ATOM   2483  CG  ARG A 336      83.413  82.187  62.502  1.00 42.39           C  
ANISOU 2483  CG  ARG A 336     6985   4407   4712   -732   -677    -12       C  
ATOM   2484  CD  ARG A 336      84.033  81.495  61.308  1.00 47.10           C  
ANISOU 2484  CD  ARG A 336     7406   5077   5414   -813   -691    -12       C  
ATOM   2485  NE  ARG A 336      83.957  82.319  60.105  1.00 50.27           N  
ANISOU 2485  NE  ARG A 336     7876   5405   5819   -903   -690    -42       N  
ATOM   2486  CZ  ARG A 336      82.904  82.352  59.296  1.00 54.52           C  
ANISOU 2486  CZ  ARG A 336     8424   5870   6422   -831   -637    -10       C  
ATOM   2487  NH1 ARG A 336      81.840  81.606  59.563  1.00 54.63           N  
ANISOU 2487  NH1 ARG A 336     8376   5878   6502   -672   -577     46       N  
ATOM   2488  NH2 ARG A 336      82.915  83.129  58.222  1.00 55.29           N  
ANISOU 2488  NH2 ARG A 336     8592   5904   6513   -920   -645    -34       N  
ATOM   2489  N   TYR A 337      84.081  78.714  65.235  1.00 45.63           N  
ANISOU 2489  N   TYR A 337     7033   5110   5196   -504   -691    115       N  
ATOM   2490  CA  TYR A 337      84.489  77.999  66.436  1.00 52.78           C  
ANISOU 2490  CA  TYR A 337     7891   6097   6064   -455   -720    146       C  
ATOM   2491  C   TYR A 337      84.725  78.979  67.576  1.00 49.42           C  
ANISOU 2491  C   TYR A 337     7641   5654   5482   -494   -762    111       C  
ATOM   2492  O   TYR A 337      85.380  80.011  67.402  1.00 48.65           O  
ANISOU 2492  O   TYR A 337     7636   5544   5304   -624   -811     50       O  
ATOM   2493  CB  TYR A 337      85.753  77.184  66.165  1.00 60.98           C  
ANISOU 2493  CB  TYR A 337     8752   7262   7157   -525   -781    149       C  
ATOM   2494  N   SER A 338      84.160  78.661  68.742  1.00 46.13           N  
ANISOU 2494  N   SER A 338     7275   5233   5018   -387   -736    148       N  
ATOM   2495  CA  SER A 338      84.328  79.440  69.953  1.00 48.64           C  
ANISOU 2495  CA  SER A 338     7754   5542   5185   -415   -768    120       C  
ATOM   2496  C   SER A 338      84.291  78.455  71.112  1.00 47.68           C  
ANISOU 2496  C   SER A 338     7579   5492   5046   -321   -771    178       C  
ATOM   2497  O   SER A 338      83.479  77.519  71.088  1.00 45.27           O  
ANISOU 2497  O   SER A 338     7198   5175   4829   -196   -706    236       O  
ATOM   2498  CB  SER A 338      83.232  80.499  70.118  1.00 50.12           C  
ANISOU 2498  CB  SER A 338     8137   5591   5313   -370   -704     92       C  
ATOM   2499  OG  SER A 338      83.553  81.417  71.145  1.00 56.21           O  
ANISOU 2499  OG  SER A 338     9077   6348   5932   -431   -737     48       O  
ATOM   2500  N   PRO A 339      85.145  78.619  72.118  1.00 51.64           N  
ANISOU 2500  N   PRO A 339     8118   6069   5433   -383   -846    166       N  
ATOM   2501  CA  PRO A 339      85.167  77.668  73.247  1.00 54.73           C  
ANISOU 2501  CA  PRO A 339     8463   6534   5800   -297   -857    228       C  
ATOM   2502  C   PRO A 339      84.054  77.931  74.258  1.00 58.22           C  
ANISOU 2502  C   PRO A 339     9059   6897   6165   -201   -789    240       C  
ATOM   2503  O   PRO A 339      84.296  78.270  75.419  1.00 61.95           O  
ANISOU 2503  O   PRO A 339     9637   7397   6506   -225   -824    231       O  
ATOM   2504  CB  PRO A 339      86.569  77.886  73.839  1.00 54.23           C  
ANISOU 2504  CB  PRO A 339     8383   6589   5634   -418   -972    203       C  
ATOM   2505  CG  PRO A 339      87.239  78.961  73.004  1.00 59.23           C  
ANISOU 2505  CG  PRO A 339     9057   7207   6241   -572  -1012    123       C  
ATOM   2506  CD  PRO A 339      86.167  79.665  72.254  1.00 54.93           C  
ANISOU 2506  CD  PRO A 339     8620   6517   5735   -542   -926     96       C  
ATOM   2507  N   ASP A 340      82.809  77.773  73.810  1.00 57.38           N  
ANISOU 2507  N   ASP A 340     8965   6697   6139    -95   -689    258       N  
ATOM   2508  CA  ASP A 340      81.649  77.912  74.679  1.00 58.84           C  
ANISOU 2508  CA  ASP A 340     9275   6809   6271      9   -610    270       C  
ATOM   2509  C   ASP A 340      80.512  77.067  74.119  1.00 49.65           C  
ANISOU 2509  C   ASP A 340     8022   5603   5239    139   -513    319       C  
ATOM   2510  O   ASP A 340      80.567  76.585  72.984  1.00 45.35           O  
ANISOU 2510  O   ASP A 340     7345   5068   4818    138   -504    333       O  
ATOM   2511  CB  ASP A 340      81.233  79.382  74.834  1.00 66.86           C  
ANISOU 2511  CB  ASP A 340    10495   7721   7189    -33   -587    199       C  
ATOM   2512  CG  ASP A 340      80.668  79.974  73.556  1.00 75.55           C  
ANISOU 2512  CG  ASP A 340    11605   8727   8373    -32   -541    170       C  
ATOM   2513  OD1 ASP A 340      81.008  79.485  72.459  1.00 77.51           O  
ANISOU 2513  OD1 ASP A 340    11710   9008   8733    -57   -558    186       O  
ATOM   2514  OD2 ASP A 340      79.885  80.942  73.653  1.00 80.97           O  
ANISOU 2514  OD2 ASP A 340    12447   9305   9012     -5   -487    132       O  
ATOM   2515  N   PHE A 341      79.471  76.888  74.937  1.00 44.66           N  
ANISOU 2515  N   PHE A 341     7465   4928   4575    245   -437    341       N  
ATOM   2516  CA  PHE A 341      78.316  76.079  74.564  1.00 46.17           C  
ANISOU 2516  CA  PHE A 341     7579   5086   4875    367   -337    384       C  
ATOM   2517  C   PHE A 341      77.177  76.909  73.983  1.00 49.33           C  
ANISOU 2517  C   PHE A 341     8062   5378   5302    414   -258    347       C  
ATOM   2518  O   PHE A 341      76.006  76.529  74.117  1.00 46.51           O  
ANISOU 2518  O   PHE A 341     7702   4985   4985    523   -165    370       O  
ATOM   2519  CB  PHE A 341      77.825  75.276  75.769  1.00 46.85           C  
ANISOU 2519  CB  PHE A 341     7684   5200   4919    456   -294    433       C  
ATOM   2520  CG  PHE A 341      78.709  74.114  76.121  1.00 50.21           C  
ANISOU 2520  CG  PHE A 341     7988   5728   5362    449   -353    494       C  
ATOM   2521  CD1 PHE A 341      78.616  72.919  75.422  1.00 52.87           C  
ANISOU 2521  CD1 PHE A 341     8160   6095   5833    499   -323    547       C  
ATOM   2522  CD2 PHE A 341      79.632  74.217  77.151  1.00 51.58           C  
ANISOU 2522  CD2 PHE A 341     8213   5967   5417    394   -438    498       C  
ATOM   2523  CE1 PHE A 341      79.428  71.846  75.743  1.00 56.63           C  
ANISOU 2523  CE1 PHE A 341     8529   6657   6330    504   -374    605       C  
ATOM   2524  CE2 PHE A 341      80.448  73.150  77.479  1.00 56.33           C  
ANISOU 2524  CE2 PHE A 341     8701   6665   6036    398   -497    560       C  
ATOM   2525  CZ  PHE A 341      80.347  71.961  76.775  1.00 58.97           C  
ANISOU 2525  CZ  PHE A 341     8875   7020   6510    458   -464    615       C  
ATOM   2526  N   TYR A 342      77.490  78.024  73.333  1.00 50.13           N  
ANISOU 2526  N   TYR A 342     8237   5429   5382    334   -293    292       N  
ATOM   2527  CA  TYR A 342      76.451  78.931  72.873  1.00 51.37           C  
ANISOU 2527  CA  TYR A 342     8493   5477   5549    383   -226    258       C  
ATOM   2528  C   TYR A 342      75.595  78.289  71.788  1.00 43.31           C  
ANISOU 2528  C   TYR A 342     7341   4443   4671    460   -161    292       C  
ATOM   2529  O   TYR A 342      76.105  77.622  70.884  1.00 40.85           O  
ANISOU 2529  O   TYR A 342     6884   4185   4453    418   -191    315       O  
ATOM   2530  CB  TYR A 342      77.066  80.223  72.347  1.00 55.23           C  
ANISOU 2530  CB  TYR A 342     9090   5912   5985    272   -282    196       C  
ATOM   2531  CG  TYR A 342      76.054  81.335  72.273  1.00 57.65           C  
ANISOU 2531  CG  TYR A 342     9550   6093   6260    328   -218    158       C  
ATOM   2532  CD1 TYR A 342      75.438  81.807  73.421  1.00 58.28           C  
ANISOU 2532  CD1 TYR A 342     9777   6123   6244    389   -167    137       C  
ATOM   2533  CD2 TYR A 342      75.689  81.887  71.054  1.00 55.02           C  
ANISOU 2533  CD2 TYR A 342     9216   5693   5996    327   -205    145       C  
ATOM   2534  CE1 TYR A 342      74.501  82.814  73.366  1.00 57.19           C  
ANISOU 2534  CE1 TYR A 342     9778   5868   6085    452   -103    102       C  
ATOM   2535  CE2 TYR A 342      74.750  82.894  70.983  1.00 53.64           C  
ANISOU 2535  CE2 TYR A 342     9181   5402   5798    392   -147    116       C  
ATOM   2536  CZ  TYR A 342      74.161  83.352  72.143  1.00 57.18           C  
ANISOU 2536  CZ  TYR A 342     9770   5800   6156    459    -95     93       C  
ATOM   2537  OH  TYR A 342      73.226  84.355  72.078  1.00 63.90           O  
ANISOU 2537  OH  TYR A 342    10759   6532   6988    533    -34     63       O  
ATOM   2538  N   ILE A 343      74.283  78.494  71.890  1.00 36.96           N  
ANISOU 2538  N   ILE A 343     6588   3573   3882    570    -70    292       N  
ATOM   2539  CA  ILE A 343      73.323  78.071  70.877  1.00 35.12           C  
ANISOU 2539  CA  ILE A 343     6249   3324   3770    644     -5    317       C  
ATOM   2540  C   ILE A 343      72.851  79.318  70.145  1.00 36.06           C  
ANISOU 2540  C   ILE A 343     6468   3347   3887    645      4    276       C  
ATOM   2541  O   ILE A 343      72.167  80.169  70.731  1.00 37.78           O  
ANISOU 2541  O   ILE A 343     6829   3489   4037    704     46    246       O  
ATOM   2542  CB  ILE A 343      72.135  77.317  71.486  1.00 41.54           C  
ANISOU 2542  CB  ILE A 343     7029   4146   4609    772     95    350       C  
ATOM   2543  CG1 ILE A 343      72.615  76.163  72.367  1.00 41.91           C  
ANISOU 2543  CG1 ILE A 343     7011   4275   4639    772     86    392       C  
ATOM   2544  CG2 ILE A 343      71.205  76.820  70.380  1.00 39.11           C  
ANISOU 2544  CG2 ILE A 343     6595   3838   4427    835    158    374       C  
ATOM   2545  CD1 ILE A 343      71.506  75.501  73.158  1.00 42.12           C  
ANISOU 2545  CD1 ILE A 343     7035   4305   4664    884    186    418       C  
ATOM   2546  N   TYR A 344      73.204  79.428  68.867  1.00 34.68           N  
ANISOU 2546  N   TYR A 344     6221   3172   3783    582    -34    276       N  
ATOM   2547  CA  TYR A 344      72.766  80.551  68.052  1.00 34.83           C  
ANISOU 2547  CA  TYR A 344     6329   3100   3806    583    -30    247       C  
ATOM   2548  C   TYR A 344      71.370  80.277  67.514  1.00 35.60           C  
ANISOU 2548  C   TYR A 344     6361   3176   3989    708     54    275       C  
ATOM   2549  O   TYR A 344      71.129  79.239  66.893  1.00 33.55           O  
ANISOU 2549  O   TYR A 344     5937   2982   3828    726     78    314       O  
ATOM   2550  CB  TYR A 344      73.738  80.792  66.899  1.00 36.79           C  
ANISOU 2550  CB  TYR A 344     6532   3359   4086    454   -106    235       C  
ATOM   2551  CG  TYR A 344      75.168  81.014  67.339  1.00 46.19           C  
ANISOU 2551  CG  TYR A 344     7766   4588   5198    320   -192    205       C  
ATOM   2552  CD1 TYR A 344      75.681  82.295  67.469  1.00 50.51           C  
ANISOU 2552  CD1 TYR A 344     8481   5065   5645    238   -237    152       C  
ATOM   2553  CD2 TYR A 344      76.010  79.939  67.605  1.00 46.22           C  
ANISOU 2553  CD2 TYR A 344     7637   4698   5225    275   -229    230       C  
ATOM   2554  CE1 TYR A 344      76.989  82.502  67.864  1.00 55.87           C  
ANISOU 2554  CE1 TYR A 344     9191   5790   6247    107   -316    120       C  
ATOM   2555  CE2 TYR A 344      77.317  80.136  67.998  1.00 47.79           C  
ANISOU 2555  CE2 TYR A 344     7860   4945   5353    155   -312    203       C  
ATOM   2556  CZ  TYR A 344      77.802  81.417  68.126  1.00 54.69           C  
ANISOU 2556  CZ  TYR A 344     8897   5759   6125     67   -356    146       C  
ATOM   2557  OH  TYR A 344      79.107  81.612  68.519  1.00 58.74           O  
ANISOU 2557  OH  TYR A 344     9427   6330   6561    -61   -438    116       O  
ATOM   2558  N   ARG A 345      70.455  81.209  67.753  1.00 36.08           N  
ANISOU 2558  N   ARG A 345     6549   3149   4012    794    101    253       N  
ATOM   2559  CA  ARG A 345      69.061  81.046  67.377  1.00 37.87           C  
ANISOU 2559  CA  ARG A 345     6720   3360   4309    924    182    275       C  
ATOM   2560  C   ARG A 345      68.610  82.246  66.561  1.00 36.75           C  
ANISOU 2560  C   ARG A 345     6673   3121   4169    947    175    257       C  
ATOM   2561  O   ARG A 345      69.163  83.344  66.668  1.00 36.08           O  
ANISOU 2561  O   ARG A 345     6745   2957   4006    890    130    219       O  
ATOM   2562  CB  ARG A 345      68.157  80.890  68.610  1.00 36.16           C  
ANISOU 2562  CB  ARG A 345     6552   3137   4049   1041    266    271       C  
ATOM   2563  CG  ARG A 345      68.561  79.766  69.546  1.00 37.91           C  
ANISOU 2563  CG  ARG A 345     6707   3444   4254   1024    275    292       C  
ATOM   2564  CD  ARG A 345      67.663  79.731  70.768  1.00 41.60           C  
ANISOU 2564  CD  ARG A 345     7242   3896   4666   1129    360    282       C  
ATOM   2565  NE  ARG A 345      67.971  78.609  71.651  1.00 42.28           N  
ANISOU 2565  NE  ARG A 345     7267   4062   4734   1118    372    309       N  
ATOM   2566  CZ  ARG A 345      67.629  77.348  71.407  1.00 46.07           C  
ANISOU 2566  CZ  ARG A 345     7590   4617   5297   1147    412    354       C  
ATOM   2567  NH1 ARG A 345      66.960  77.037  70.304  1.00 48.05           N  
ANISOU 2567  NH1 ARG A 345     7721   4882   5652   1182    445    374       N  
ATOM   2568  NH2 ARG A 345      67.952  76.396  72.269  1.00 50.88           N  
ANISOU 2568  NH2 ARG A 345     8166   5286   5879   1137    421    381       N  
ATOM   2569  N   GLY A 346      67.586  82.025  65.750  1.00 34.91           N  
ANISOU 2569  N   GLY A 346     6346   2895   4022   1032    220    286       N  
ATOM   2570  CA  GLY A 346      67.005  83.117  64.999  1.00 35.38           C  
ANISOU 2570  CA  GLY A 346     6491   2865   4087   1079    218    279       C  
ATOM   2571  C   GLY A 346      65.839  82.637  64.170  1.00 34.94           C  
ANISOU 2571  C   GLY A 346     6297   2849   4131   1176    268    318       C  
ATOM   2572  O   GLY A 346      65.402  81.488  64.272  1.00 34.33           O  
ANISOU 2572  O   GLY A 346     6069   2864   4113   1211    317    344       O  
ATOM   2573  N   LYS A 347      65.358  83.535  63.320  1.00 38.91           N  
ANISOU 2573  N   LYS A 347     6854   3282   4649   1215    254    322       N  
ATOM   2574  CA  LYS A 347      64.128  83.313  62.581  1.00 43.42           C  
ANISOU 2574  CA  LYS A 347     7315   3882   5299   1323    300    357       C  
ATOM   2575  C   LYS A 347      64.283  83.879  61.181  1.00 42.43           C  
ANISOU 2575  C   LYS A 347     7191   3723   5206   1272    237    377       C  
ATOM   2576  O   LYS A 347      64.738  85.013  61.015  1.00 42.44           O  
ANISOU 2576  O   LYS A 347     7355   3621   5150   1236    189    357       O  
ATOM   2577  CB  LYS A 347      62.952  83.973  63.307  1.00 51.19           C  
ANISOU 2577  CB  LYS A 347     8386   4806   6257   1489    372    342       C  
ATOM   2578  CG  LYS A 347      61.576  83.610  62.802  1.00 55.46           C  
ANISOU 2578  CG  LYS A 347     8795   5401   6878   1617    433    374       C  
ATOM   2579  CD  LYS A 347      60.539  83.980  63.850  1.00 59.04           C  
ANISOU 2579  CD  LYS A 347     9313   5820   7301   1772    520    350       C  
ATOM   2580  CE  LYS A 347      59.179  84.205  63.232  1.00 60.25           C  
ANISOU 2580  CE  LYS A 347     9390   5986   7516   1915    562    374       C  
ATOM   2581  N   PHE A 348      63.931  83.077  60.182  1.00 38.76           N  
ANISOU 2581  N   PHE A 348     6553   3345   4827   1259    239    415       N  
ATOM   2582  CA  PHE A 348      63.800  83.547  58.809  1.00 38.47           C  
ANISOU 2582  CA  PHE A 348     6501   3288   4826   1231    191    443       C  
ATOM   2583  C   PHE A 348      62.385  84.091  58.653  1.00 41.97           C  
ANISOU 2583  C   PHE A 348     6954   3703   5291   1399    235    464       C  
ATOM   2584  O   PHE A 348      61.417  83.326  58.622  1.00 41.15           O  
ANISOU 2584  O   PHE A 348     6703   3686   5246   1484    295    485       O  
ATOM   2585  CB  PHE A 348      64.099  82.418  57.826  1.00 34.24           C  
ANISOU 2585  CB  PHE A 348     5777   2864   4368   1131    175    470       C  
ATOM   2586  CG  PHE A 348      65.452  81.790  58.024  1.00 32.37           C  
ANISOU 2586  CG  PHE A 348     5513   2666   4121    981    139    450       C  
ATOM   2587  CD1 PHE A 348      66.596  82.418  57.559  1.00 38.39           C  
ANISOU 2587  CD1 PHE A 348     6367   3376   4842    848     62    430       C  
ATOM   2588  CD2 PHE A 348      65.583  80.573  58.677  1.00 33.47           C  
ANISOU 2588  CD2 PHE A 348     5536   2892   4289    974    184    450       C  
ATOM   2589  CE1 PHE A 348      67.844  81.843  57.742  1.00 36.66           C  
ANISOU 2589  CE1 PHE A 348     6112   3202   4615    715     27    409       C  
ATOM   2590  CE2 PHE A 348      66.829  79.993  58.862  1.00 34.35           C  
ANISOU 2590  CE2 PHE A 348     5617   3041   4394    849    148    436       C  
ATOM   2591  CZ  PHE A 348      67.960  80.630  58.390  1.00 36.54           C  
ANISOU 2591  CZ  PHE A 348     5975   3275   4634    721     69    414       C  
ATOM   2592  N   ASN A 349      62.270  85.419  58.565  1.00 43.72           N  
ANISOU 2592  N   ASN A 349     7349   3801   5462   1448    207    456       N  
ATOM   2593  CA  ASN A 349      60.986  86.077  58.780  1.00 44.95           C  
ANISOU 2593  CA  ASN A 349     7548   3909   5622   1631    257    465       C  
ATOM   2594  C   ASN A 349      59.966  85.696  57.713  1.00 43.11           C  
ANISOU 2594  C   ASN A 349     7154   3756   5471   1701    264    516       C  
ATOM   2595  O   ASN A 349      58.833  85.319  58.035  1.00 43.00           O  
ANISOU 2595  O   ASN A 349     7041   3802   5495   1833    334    525       O  
ATOM   2596  CB  ASN A 349      61.184  87.590  58.826  1.00 54.58           C  
ANISOU 2596  CB  ASN A 349     8998   4968   6772   1659    223    448       C  
ATOM   2597  CG  ASN A 349      62.220  88.003  59.851  1.00 61.60           C  
ANISOU 2597  CG  ASN A 349    10051   5782   7571   1574    213    394       C  
ATOM   2598  OD1 ASN A 349      62.230  87.503  60.974  1.00 59.07           O  
ANISOU 2598  OD1 ASN A 349     9715   5498   7229   1594    265    364       O  
ATOM   2599  ND2 ASN A 349      63.101  88.918  59.466  1.00 68.69           N  
ANISOU 2599  ND2 ASN A 349    11107   6579   8411   1473    147    379       N  
ATOM   2600  N   LEU A 350      60.342  85.796  56.437  1.00 41.23           N  
ANISOU 2600  N   LEU A 350     6886   3525   5255   1608    194    548       N  
ATOM   2601  CA  LEU A 350      59.393  85.482  55.374  1.00 43.48           C  
ANISOU 2601  CA  LEU A 350     7023   3890   5609   1664    193    599       C  
ATOM   2602  C   LEU A 350      58.944  84.027  55.461  1.00 45.07           C  
ANISOU 2602  C   LEU A 350     7002   4246   5876   1658    253    605       C  
ATOM   2603  O   LEU A 350      57.747  83.726  55.391  1.00 44.82           O  
ANISOU 2603  O   LEU A 350     6856   4285   5888   1778    304    626       O  
ATOM   2604  CB  LEU A 350      60.010  85.785  54.009  1.00 46.15           C  
ANISOU 2604  CB  LEU A 350     7374   4211   5950   1540    105    629       C  
ATOM   2605  CG  LEU A 350      59.086  85.613  52.803  1.00 51.44           C  
ANISOU 2605  CG  LEU A 350     7912   4957   6678   1587     89    685       C  
ATOM   2606  CD1 LEU A 350      57.740  86.283  53.050  1.00 54.92           C  
ANISOU 2606  CD1 LEU A 350     8375   5367   7125   1798    124    707       C  
ATOM   2607  CD2 LEU A 350      59.737  86.170  51.548  1.00 52.45           C  
ANISOU 2607  CD2 LEU A 350     8104   5038   6788   1467     -1    713       C  
ATOM   2608  N   GLU A 351      59.895  83.110  55.641  1.00 39.63           N  
ANISOU 2608  N   GLU A 351     6254   3612   5194   1519    251    586       N  
ATOM   2609  CA  GLU A 351      59.555  81.698  55.736  1.00 37.99           C  
ANISOU 2609  CA  GLU A 351     5851   3539   5046   1502    312    592       C  
ATOM   2610  C   GLU A 351      58.877  81.344  57.055  1.00 38.84           C  
ANISOU 2610  C   GLU A 351     5947   3667   5144   1618    402    569       C  
ATOM   2611  O   GLU A 351      58.180  80.326  57.119  1.00 40.52           O  
ANISOU 2611  O   GLU A 351     6001   3988   5406   1648    467    578       O  
ATOM   2612  CB  GLU A 351      60.811  80.847  55.564  1.00 35.59           C  
ANISOU 2612  CB  GLU A 351     5495   3275   4752   1328    285    580       C  
ATOM   2613  CG  GLU A 351      61.344  80.808  54.144  1.00 40.01           C  
ANISOU 2613  CG  GLU A 351     6005   3857   5341   1199    218    602       C  
ATOM   2614  CD  GLU A 351      62.139  82.046  53.775  1.00 41.11           C  
ANISOU 2614  CD  GLU A 351     6322   3878   5421   1139    134    594       C  
ATOM   2615  OE1 GLU A 351      62.559  82.791  54.688  1.00 39.15           O  
ANISOU 2615  OE1 GLU A 351     6233   3535   5107   1164    126    564       O  
ATOM   2616  OE2 GLU A 351      62.348  82.275  52.563  1.00 41.14           O1-
ANISOU 2616  OE2 GLU A 351     6310   3884   5438   1059     79    617       O1-
ATOM   2617  N   ASN A 352      59.062  82.156  58.099  1.00 38.84           N  
ANISOU 2617  N   ASN A 352     6115   3567   5077   1677    410    536       N  
ATOM   2618  CA  ASN A 352      58.599  81.825  59.448  1.00 38.89           C  
ANISOU 2618  CA  ASN A 352     6130   3586   5061   1765    494    508       C  
ATOM   2619  C   ASN A 352      59.251  80.534  59.940  1.00 38.27           C  
ANISOU 2619  C   ASN A 352     5958   3588   4995   1664    519    500       C  
ATOM   2620  O   ASN A 352      58.627  79.713  60.613  1.00 47.53           O  
ANISOU 2620  O   ASN A 352     7043   4831   6185   1718    600    495       O  
ATOM   2621  CB  ASN A 352      57.071  81.729  59.511  1.00 48.84           C  
ANISOU 2621  CB  ASN A 352     7294   4902   6360   1924    570    519       C  
ATOM   2622  CG  ASN A 352      56.529  81.947  60.907  1.00 56.26           C  
ANISOU 2622  CG  ASN A 352     8311   5809   7257   2040    650    481       C  
ATOM   2623  OD1 ASN A 352      56.933  82.877  61.601  1.00 59.78           O  
ANISOU 2623  OD1 ASN A 352     8937   6141   7636   2062    636    451       O  
ATOM   2624  ND2 ASN A 352      55.613  81.082  61.331  1.00 57.56           N  
ANISOU 2624  ND2 ASN A 352     8341   6073   7455   2105    738    479       N  
ATOM   2625  N   THR A 353      60.518  80.346  59.581  1.00 37.29           N  
ANISOU 2625  N   THR A 353     5852   3454   4861   1516    452    498       N  
ATOM   2626  CA  THR A 353      61.317  79.209  60.014  1.00 32.90           C  
ANISOU 2626  CA  THR A 353     5224   2963   4316   1417    463    493       C  
ATOM   2627  C   THR A 353      62.302  79.677  61.079  1.00 32.84           C  
ANISOU 2627  C   THR A 353     5371   2881   4224   1377    433    460       C  
ATOM   2628  O   THR A 353      62.881  80.762  60.966  1.00 33.81           O  
ANISOU 2628  O   THR A 353     5639   2913   4295   1344    371    442       O  
ATOM   2629  CB  THR A 353      62.069  78.590  58.826  1.00 32.97           C  
ANISOU 2629  CB  THR A 353     5124   3024   4378   1277    411    514       C  
ATOM   2630  OG1 THR A 353      61.132  78.185  57.817  1.00 33.62           O  
ANISOU 2630  OG1 THR A 353     5066   3179   4531   1307    437    544       O  
ATOM   2631  CG2 THR A 353      62.905  77.385  59.253  1.00 30.76           C  
ANISOU 2631  CG2 THR A 353     4764   2807   4115   1185    424    511       C  
ATOM   2632  N   THR A 354      62.479  78.875  62.121  1.00 32.67           N  
ANISOU 2632  N   THR A 354     5326   2900   4185   1377    478    451       N  
ATOM   2633  CA  THR A 354      63.455  79.180  63.154  1.00 32.96           C  
ANISOU 2633  CA  THR A 354     5493   2888   4140   1328    447    422       C  
ATOM   2634  C   THR A 354      64.628  78.217  63.051  1.00 35.36           C  
ANISOU 2634  C   THR A 354     5718   3253   4464   1198    406    433       C  
ATOM   2635  O   THR A 354      64.509  77.118  62.498  1.00 31.33           O  
ANISOU 2635  O   THR A 354     5049   2825   4029   1169    432    460       O  
ATOM   2636  CB  THR A 354      62.827  79.126  64.554  1.00 36.02           C  
ANISOU 2636  CB  THR A 354     5942   3268   4477   1429    522    403       C  
ATOM   2637  OG1 THR A 354      62.464  77.780  64.876  1.00 38.86           O  
ANISOU 2637  OG1 THR A 354     6162   3723   4881   1442    588    425       O  
ATOM   2638  CG2 THR A 354      61.590  80.004  64.614  1.00 39.80           C  
ANISOU 2638  CG2 THR A 354     6480   3693   4948   1570    573    392       C  
ATOM   2639  N   TYR A 355      65.782  78.655  63.548  1.00 32.49           N  
ANISOU 2639  N   TYR A 355     5463   2850   4033   1116    342    409       N  
ATOM   2640  CA  TYR A 355      66.971  77.821  63.529  1.00 31.65           C  
ANISOU 2640  CA  TYR A 355     5286   2801   3940    999    298    416       C  
ATOM   2641  C   TYR A 355      67.640  77.830  64.889  1.00 32.14           C  
ANISOU 2641  C   TYR A 355     5442   2853   3915    986    285    398       C  
ATOM   2642  O   TYR A 355      67.503  78.772  65.671  1.00 32.99           O  
ANISOU 2642  O   TYR A 355     5704   2892   3939   1026    286    368       O  
ATOM   2643  CB  TYR A 355      67.993  78.265  62.457  1.00 31.32           C  
ANISOU 2643  CB  TYR A 355     5249   2743   3910    871    210    408       C  
ATOM   2644  CG  TYR A 355      68.677  79.600  62.712  1.00 32.07           C  
ANISOU 2644  CG  TYR A 355     5526   2749   3912    821    145    370       C  
ATOM   2645  CD1 TYR A 355      68.186  80.765  62.142  1.00 32.59           C  
ANISOU 2645  CD1 TYR A 355     5694   2729   3959    853    132    359       C  
ATOM   2646  CD2 TYR A 355      69.827  79.688  63.494  1.00 32.33           C  
ANISOU 2646  CD2 TYR A 355     5627   2784   3874    739     94    345       C  
ATOM   2647  CE1 TYR A 355      68.806  81.987  62.355  1.00 33.34           C  
ANISOU 2647  CE1 TYR A 355     5967   2733   3966    801     79    322       C  
ATOM   2648  CE2 TYR A 355      70.453  80.914  63.718  1.00 33.08           C  
ANISOU 2648  CE2 TYR A 355     5892   2799   3878    681     38    305       C  
ATOM   2649  CZ  TYR A 355      69.936  82.055  63.144  1.00 33.57           C  
ANISOU 2649  CZ  TYR A 355     6064   2768   3923    710     34    292       C  
ATOM   2650  OH  TYR A 355      70.540  83.274  63.346  1.00 37.73           O  
ANISOU 2650  OH  TYR A 355     6770   3207   4359    648    -14    251       O  
ATOM   2651  N   ALA A 356      68.362  76.748  65.153  1.00 31.64           N  
ANISOU 2651  N   ALA A 356     5287   2862   3873    929    275    417       N  
ATOM   2652  CA  ALA A 356      69.258  76.648  66.295  1.00 32.05           C  
ANISOU 2652  CA  ALA A 356     5408   2923   3846    890    240    407       C  
ATOM   2653  C   ALA A 356      70.517  75.967  65.793  1.00 31.46           C  
ANISOU 2653  C   ALA A 356     5234   2908   3810    774    174    419       C  
ATOM   2654  O   ALA A 356      70.444  74.858  65.255  1.00 33.64           O  
ANISOU 2654  O   ALA A 356     5361   3245   4175    768    203    451       O  
ATOM   2655  CB  ALA A 356      68.627  75.854  67.442  1.00 32.71           C  
ANISOU 2655  CB  ALA A 356     5478   3040   3911    977    315    426       C  
ATOM   2656  N   MET A 357      71.659  76.628  65.930  1.00 31.81           N  
ANISOU 2656  N   MET A 357     5360   2936   3791    678     89    391       N  
ATOM   2657  CA  MET A 357      72.915  76.015  65.523  1.00 35.28           C  
ANISOU 2657  CA  MET A 357     5702   3439   4263    569     25    397       C  
ATOM   2658  C   MET A 357      73.875  76.034  66.699  1.00 34.67           C  
ANISOU 2658  C   MET A 357     5691   3387   4094    530    -28    388       C  
ATOM   2659  O   MET A 357      73.886  76.975  67.499  1.00 32.84           O  
ANISOU 2659  O   MET A 357     5613   3106   3759    535    -45    357       O  
ATOM   2660  CB  MET A 357      73.526  76.697  64.278  1.00 39.77           C  
ANISOU 2660  CB  MET A 357     6268   3987   4856    462    -35    371       C  
ATOM   2661  CG  MET A 357      73.579  78.214  64.285  1.00 49.10           C  
ANISOU 2661  CG  MET A 357     7626   5080   5951    432    -74    327       C  
ATOM   2662  SD  MET A 357      73.542  78.921  62.610  1.00 52.38           S  
ANISOU 2662  SD  MET A 357     8032   5451   6418    361   -101    314       S  
ATOM   2663  CE  MET A 357      74.619  77.785  61.731  1.00 43.48           C  
ANISOU 2663  CE  MET A 357     6714   4425   5382    245   -137    326       C  
ATOM   2664  N   ARG A 358      74.651  74.965  66.821  1.00 31.73           N  
ANISOU 2664  N   ARG A 358     5203   3094   3761    496    -51    416       N  
ATOM   2665  CA  ARG A 358      75.543  74.816  67.958  1.00 32.57           C  
ANISOU 2665  CA  ARG A 358     5350   3240   3784    468   -104    418       C  
ATOM   2666  C   ARG A 358      76.556  73.737  67.624  1.00 37.15           C  
ANISOU 2666  C   ARG A 358     5777   3906   4433    413   -144    446       C  
ATOM   2667  O   ARG A 358      76.316  72.875  66.774  1.00 36.59           O  
ANISOU 2667  O   ARG A 358     5572   3859   4473    426   -103    471       O  
ATOM   2668  CB  ARG A 358      74.774  74.465  69.238  1.00 35.06           C  
ANISOU 2668  CB  ARG A 358     5726   3550   4046    573    -45    442       C  
ATOM   2669  CG  ARG A 358      74.640  72.971  69.506  1.00 39.77           C  
ANISOU 2669  CG  ARG A 358     6194   4209   4708    629      0    500       C  
ATOM   2670  CD  ARG A 358      73.624  72.684  70.602  1.00 48.92           C  
ANISOU 2670  CD  ARG A 358     7417   5350   5819    735     78    521       C  
ATOM   2671  NE  ARG A 358      72.273  73.061  70.194  1.00 62.35           N  
ANISOU 2671  NE  ARG A 358     9141   6996   7553    808    164    507       N  
ATOM   2672  CZ  ARG A 358      71.184  72.881  70.937  1.00 70.72           C  
ANISOU 2672  CZ  ARG A 358    10246   8039   8587    904    249    516       C  
ATOM   2673  NH1 ARG A 358      71.282  72.323  72.136  1.00 75.40           N  
ANISOU 2673  NH1 ARG A 358    10873   8657   9116    933    262    541       N  
ATOM   2674  NH2 ARG A 358      69.997  73.258  70.478  1.00 69.67           N  
ANISOU 2674  NH2 ARG A 358    10118   7864   8488    970    322    500       N  
ATOM   2675  N   PHE A 359      77.699  73.804  68.293  1.00 37.48           N  
ANISOU 2675  N   PHE A 359     5840   3996   4407    351   -224    438       N  
ATOM   2676  CA  PHE A 359      78.692  72.754  68.170  1.00 35.14           C  
ANISOU 2676  CA  PHE A 359     5400   3784   4167    316   -264    468       C  
ATOM   2677  C   PHE A 359      78.408  71.672  69.202  1.00 33.90           C  
ANISOU 2677  C   PHE A 359     5213   3660   4006    411   -227    527       C  
ATOM   2678  O   PHE A 359      78.062  71.962  70.350  1.00 35.41           O  
ANISOU 2678  O   PHE A 359     5519   3835   4099    458   -220    532       O  
ATOM   2679  CB  PHE A 359      80.103  73.322  68.326  1.00 37.73           C  
ANISOU 2679  CB  PHE A 359     5748   4161   4428    199   -374    433       C  
ATOM   2680  CG  PHE A 359      80.541  74.155  67.152  1.00 39.27           C  
ANISOU 2680  CG  PHE A 359     5942   4335   4645     89   -409    380       C  
ATOM   2681  CD1 PHE A 359      81.056  73.555  66.012  1.00 36.49           C  
ANISOU 2681  CD1 PHE A 359     5440   4023   4401     35   -415    381       C  
ATOM   2682  CD2 PHE A 359      80.405  75.533  67.172  1.00 44.76           C  
ANISOU 2682  CD2 PHE A 359     6794   4963   5251     39   -430    328       C  
ATOM   2683  CE1 PHE A 359      81.446  74.315  64.926  1.00 40.89           C  
ANISOU 2683  CE1 PHE A 359     6001   4560   4973    -73   -444    332       C  
ATOM   2684  CE2 PHE A 359      80.794  76.299  66.088  1.00 46.86           C  
ANISOU 2684  CE2 PHE A 359     7071   5202   5531    -65   -461    283       C  
ATOM   2685  CZ  PHE A 359      81.316  75.690  64.964  1.00 45.21           C  
ANISOU 2685  CZ  PHE A 359     6711   5041   5428   -124   -469    285       C  
ATOM   2686  N   ILE A 360      78.502  70.423  68.757  1.00 32.88           N  
ANISOU 2686  N   ILE A 360     4937   3572   3984    438   -194    570       N  
ATOM   2687  CA  ILE A 360      78.196  69.239  69.548  1.00 41.11           C  
ANISOU 2687  CA  ILE A 360     5939   4639   5042    529   -147    631       C  
ATOM   2688  C   ILE A 360      79.503  68.507  69.793  1.00 32.59           C  
ANISOU 2688  C   ILE A 360     4768   3639   3977    497   -222    661       C  
ATOM   2689  O   ILE A 360      80.422  68.566  68.971  1.00 32.41           O  
ANISOU 2689  O   ILE A 360     4658   3652   4004    416   -276    637       O  
ATOM   2690  CB  ILE A 360      77.183  68.333  68.809  1.00 47.68           C  
ANISOU 2690  CB  ILE A 360     6678   5448   5990    590    -39    658       C  
ATOM   2691  CG1 ILE A 360      75.869  69.074  68.581  1.00 54.99           C  
ANISOU 2691  CG1 ILE A 360     7685   6308   6902    629     31    631       C  
ATOM   2692  CG2 ILE A 360      76.936  67.026  69.559  1.00 54.84           C  
ANISOU 2692  CG2 ILE A 360     7542   6377   6918    673     15    723       C  
ATOM   2693  CD1 ILE A 360      74.898  68.955  69.726  1.00 56.47           C  
ANISOU 2693  CD1 ILE A 360     7964   6470   7022    724     95    653       C  
ATOM   2694  N   TYR A 361      79.595  67.820  70.932  1.00 33.21           N  
ANISOU 2694  N   TYR A 361     4865   3745   4008    561   -226    713       N  
ATOM   2695  CA  TYR A 361      80.764  67.014  71.273  1.00 33.71           C  
ANISOU 2695  CA  TYR A 361     4839   3885   4085    554   -294    754       C  
ATOM   2696  C   TYR A 361      80.327  65.569  71.487  1.00 38.71           C  
ANISOU 2696  C   TYR A 361     5400   4517   4792    650   -219    826       C  
ATOM   2697  O   TYR A 361      80.265  65.087  72.627  1.00 34.83           O  
ANISOU 2697  O   TYR A 361     4960   4038   4235    713   -222    877       O  
ATOM   2698  CB  TYR A 361      81.464  67.587  72.505  1.00 34.84           C  
ANISOU 2698  CB  TYR A 361     5081   4072   4086    531   -389    754       C  
ATOM   2699  CG  TYR A 361      81.806  69.039  72.292  1.00 35.05           C  
ANISOU 2699  CG  TYR A 361     5195   4088   4034    430   -450    678       C  
ATOM   2700  CD1 TYR A 361      82.906  69.403  71.525  1.00 35.05           C  
ANISOU 2700  CD1 TYR A 361     5118   4137   4061    327   -527    638       C  
ATOM   2701  CD2 TYR A 361      81.002  70.047  72.809  1.00 40.27           C  
ANISOU 2701  CD2 TYR A 361     6017   4687   4598    435   -422    643       C  
ATOM   2702  CE1 TYR A 361      83.217  70.729  71.312  1.00 42.24           C  
ANISOU 2702  CE1 TYR A 361     6119   5032   4897    226   -578    568       C  
ATOM   2703  CE2 TYR A 361      81.304  71.379  72.594  1.00 45.76           C  
ANISOU 2703  CE2 TYR A 361     6804   5360   5222    343   -471    574       C  
ATOM   2704  CZ  TYR A 361      82.412  71.714  71.845  1.00 49.46           C  
ANISOU 2704  CZ  TYR A 361     7203   5877   5714    235   -549    537       C  
ATOM   2705  OH  TYR A 361      82.717  73.040  71.627  1.00 57.21           O  
ANISOU 2705  OH  TYR A 361     8286   6832   6620    135   -594    467       O  
ATOM   2706  N   PRO A 362      80.020  64.847  70.407  1.00 40.63           N  
ANISOU 2706  N   PRO A 362     5529   4742   5166    658   -148    831       N  
ATOM   2707  CA  PRO A 362      79.515  63.482  70.567  1.00 46.00           C  
ANISOU 2707  CA  PRO A 362     6152   5409   5916    744    -62    894       C  
ATOM   2708  C   PRO A 362      80.598  62.542  71.065  1.00 42.31           C  
ANISOU 2708  C   PRO A 362     5613   4998   5465    771   -120    952       C  
ATOM   2709  O   PRO A 362      81.792  62.727  70.809  1.00 33.56           O  
ANISOU 2709  O   PRO A 362     4438   3947   4367    715   -212    936       O  
ATOM   2710  CB  PRO A 362      79.049  63.103  69.156  1.00 50.93           C  
ANISOU 2710  CB  PRO A 362     6673   6007   6674    720     17    871       C  
ATOM   2711  CG  PRO A 362      79.858  63.947  68.251  1.00 49.30           C  
ANISOU 2711  CG  PRO A 362     6424   5824   6485    618    -57    811       C  
ATOM   2712  CD  PRO A 362      80.153  65.229  68.989  1.00 42.80           C  
ANISOU 2712  CD  PRO A 362     5726   5008   5527    581   -143    778       C  
ATOM   2713  N   TYR A 363      80.156  61.521  71.799  1.00 39.21           N  
ANISOU 2713  N   TYR A 363     5236   4589   5072    860    -63   1020       N  
ATOM   2714  CA  TYR A 363      81.086  60.547  72.358  1.00 39.89           C  
ANISOU 2714  CA  TYR A 363     5265   4719   5171    906   -111   1087       C  
ATOM   2715  C   TYR A 363      81.953  59.915  71.273  1.00 38.15           C  
ANISOU 2715  C   TYR A 363     4884   4527   5084    879   -122   1083       C  
ATOM   2716  O   TYR A 363      83.141  59.653  71.493  1.00 35.76           O  
ANISOU 2716  O   TYR A 363     4515   4287   4785    878   -212   1106       O  
ATOM   2717  CB  TYR A 363      80.302  59.479  73.121  1.00 42.89           C  
ANISOU 2717  CB  TYR A 363     5691   5059   5545   1003    -24   1160       C  
ATOM   2718  CG  TYR A 363      81.134  58.327  73.624  1.00 41.76           C  
ANISOU 2718  CG  TYR A 363     5492   4946   5430   1066    -57   1241       C  
ATOM   2719  CD1 TYR A 363      81.207  57.139  72.910  1.00 39.91           C  
ANISOU 2719  CD1 TYR A 363     5148   4687   5329   1101     13   1272       C  
ATOM   2720  CD2 TYR A 363      81.832  58.416  74.823  1.00 41.28           C  
ANISOU 2720  CD2 TYR A 363     5489   4936   5258   1093   -158   1287       C  
ATOM   2721  CE1 TYR A 363      81.962  56.076  73.365  1.00 36.00           C  
ANISOU 2721  CE1 TYR A 363     4606   4211   4864   1170    -15   1350       C  
ATOM   2722  CE2 TYR A 363      82.590  57.353  75.289  1.00 43.92           C  
ANISOU 2722  CE2 TYR A 363     5771   5298   5617   1162   -194   1369       C  
ATOM   2723  CZ  TYR A 363      82.646  56.184  74.555  1.00 40.74           C  
ANISOU 2723  CZ  TYR A 363     5262   4863   5354   1205   -121   1401       C  
ATOM   2724  OH  TYR A 363      83.395  55.119  75.000  1.00 44.61           O  
ANISOU 2724  OH  TYR A 363     5704   5372   5875   1283   -153   1485       O  
ATOM   2725  N   ILE A 364      81.384  59.687  70.087  1.00 36.92           N  
ANISOU 2725  N   ILE A 364     4660   4330   5036    852    -33   1049       N  
ATOM   2726  CA  ILE A 364      82.094  58.905  69.080  1.00 42.96           C  
ANISOU 2726  CA  ILE A 364     5276   5113   5936    834    -19   1048       C  
ATOM   2727  C   ILE A 364      83.309  59.650  68.529  1.00 42.14           C  
ANISOU 2727  C   ILE A 364     5102   5074   5837    744   -127    995       C  
ATOM   2728  O   ILE A 364      84.301  59.018  68.142  1.00 42.40           O  
ANISOU 2728  O   ILE A 364     5014   5148   5948    741   -157   1006       O  
ATOM   2729  CB  ILE A 364      81.136  58.469  67.954  1.00 46.62           C  
ANISOU 2729  CB  ILE A 364     5690   5519   6505    818    108   1023       C  
ATOM   2730  CG1 ILE A 364      81.899  57.602  66.954  1.00 51.72           C  
ANISOU 2730  CG1 ILE A 364     6186   6179   7288    797    129   1020       C  
ATOM   2731  CG2 ILE A 364      80.500  59.687  67.271  1.00 43.27           C  
ANISOU 2731  CG2 ILE A 364     5311   5078   6054    740    113    950       C  
ATOM   2732  CD1 ILE A 364      81.077  56.587  66.264  1.00 53.87           C  
ANISOU 2732  CD1 ILE A 364     6410   6396   7663    818    266   1032       C  
ATOM   2733  N   THR A 365      83.277  60.983  68.494  1.00 37.05           N  
ANISOU 2733  N   THR A 365     4530   4439   5108    668   -184    935       N  
ATOM   2734  CA  THR A 365      84.390  61.740  67.928  1.00 39.19           C  
ANISOU 2734  CA  THR A 365     4743   4770   5377    568   -280    877       C  
ATOM   2735  C   THR A 365      85.419  62.175  68.974  1.00 40.10           C  
ANISOU 2735  C   THR A 365     4890   4961   5384    560   -407    890       C  
ATOM   2736  O   THR A 365      86.328  62.946  68.648  1.00 37.32           O  
ANISOU 2736  O   THR A 365     4508   4667   5007    466   -493    837       O  
ATOM   2737  CB  THR A 365      83.874  62.959  67.156  1.00 41.43           C  
ANISOU 2737  CB  THR A 365     5086   5020   5637    476   -271    801       C  
ATOM   2738  OG1 THR A 365      82.982  63.720  67.974  1.00 40.38           O  
ANISOU 2738  OG1 THR A 365     5108   4845   5390    503   -263    801       O  
ATOM   2739  CG2 THR A 365      83.148  62.517  65.889  1.00 44.26           C  
ANISOU 2739  CG2 THR A 365     5374   5329   6115    461   -164    782       C  
ATOM   2740  N   SER A 366      85.285  61.709  70.218  1.00 41.03           N  
ANISOU 2740  N   SER A 366     5072   5085   5432    648   -421    959       N  
ATOM   2741  CA  SER A 366      86.362  61.757  71.212  1.00 43.73           C  
ANISOU 2741  CA  SER A 366     5413   5513   5690    658   -540    991       C  
ATOM   2742  C   SER A 366      86.805  63.181  71.550  1.00 42.36           C  
ANISOU 2742  C   SER A 366     5323   5382   5387    558   -639    929       C  
ATOM   2743  O   SER A 366      87.966  63.415  71.897  1.00 39.93           O  
ANISOU 2743  O   SER A 366     4971   5168   5032    516   -750    924       O  
ATOM   2744  CB  SER A 366      87.564  60.925  70.752  1.00 48.49           C  
ANISOU 2744  CB  SER A 366     5846   6184   6393    666   -584   1011       C  
ATOM   2745  OG  SER A 366      87.145  59.666  70.252  0.60 49.33           O  
ANISOU 2745  OG  SER A 366     5876   6237   6629    744   -480   1055       O  
ATOM   2746  N   GLY A 367      85.895  64.148  71.482  1.00 35.94           N  
ANISOU 2746  N   GLY A 367     4636   4506   4515    519   -599    881       N  
ATOM   2747  CA  GLY A 367      86.196  65.519  71.836  1.00 36.38           C  
ANISOU 2747  CA  GLY A 367     4795   4584   4443    426   -677    821       C  
ATOM   2748  C   GLY A 367      86.233  66.463  70.658  1.00 40.21           C  
ANISOU 2748  C   GLY A 367     5272   5045   4962    316   -672    736       C  
ATOM   2749  O   GLY A 367      86.159  67.685  70.853  1.00 35.87           O  
ANISOU 2749  O   GLY A 367     4840   4479   4309    243   -708    681       O  
ATOM   2750  N   LYS A 368      86.370  65.933  69.446  1.00 34.92           N  
ANISOU 2750  N   LYS A 368     4472   4369   4428    298   -629    722       N  
ATOM   2751  CA  LYS A 368      86.243  66.748  68.249  1.00 34.17           C  
ANISOU 2751  CA  LYS A 368     4375   4240   4369    199   -610    648       C  
ATOM   2752  C   LYS A 368      84.807  67.242  68.115  1.00 35.22           C  
ANISOU 2752  C   LYS A 368     4628   4269   4483    230   -522    637       C  
ATOM   2753  O   LYS A 368      83.854  66.476  68.287  1.00 34.96           O  
ANISOU 2753  O   LYS A 368     4599   4191   4495    328   -434    685       O  
ATOM   2754  CB  LYS A 368      86.660  65.928  67.026  1.00 35.97           C  
ANISOU 2754  CB  LYS A 368     4433   4486   4748    179   -573    642       C  
ATOM   2755  CG  LYS A 368      86.338  66.563  65.690  1.00 36.47           C  
ANISOU 2755  CG  LYS A 368     4489   4503   4863     87   -533    577       C  
ATOM   2756  CD  LYS A 368      87.059  67.883  65.534  0.80 43.53           C  
ANISOU 2756  CD  LYS A 368     5443   5428   5670    -43   -620    505       C  
ATOM   2757  CE  LYS A 368      86.712  68.524  64.208  0.80 46.14           C  
ANISOU 2757  CE  LYS A 368     5778   5706   6046   -133   -581    446       C  
ATOM   2758  NZ  LYS A 368      86.778  67.522  63.107  0.80 47.13           N  
ANISOU 2758  NZ  LYS A 368     5749   5839   6320   -132   -517    453       N  
ATOM   2759  N   GLU A 369      84.650  68.532  67.840  1.00 33.37           N  
ANISOU 2759  N   GLU A 369     4497   4002   4182    148   -544    574       N  
ATOM   2760  CA  GLU A 369      83.319  69.098  67.695  1.00 32.81           C  
ANISOU 2760  CA  GLU A 369     4539   3836   4092    182   -468    561       C  
ATOM   2761  C   GLU A 369      82.728  68.749  66.337  1.00 37.51           C  
ANISOU 2761  C   GLU A 369     5049   4390   4812    175   -388    551       C  
ATOM   2762  O   GLU A 369      83.442  68.546  65.351  1.00 34.77           O  
ANISOU 2762  O   GLU A 369     4590   4078   4543    102   -406    527       O  
ATOM   2763  CB  GLU A 369      83.348  70.618  67.859  1.00 44.60           C  
ANISOU 2763  CB  GLU A 369     6181   5296   5469    103   -516    500       C  
ATOM   2764  CG  GLU A 369      83.833  71.376  66.628  1.00 50.45           C  
ANISOU 2764  CG  GLU A 369     6898   6031   6241    -19   -544    436       C  
ATOM   2765  CD  GLU A 369      85.320  71.195  66.369  1.00 58.96           C  
ANISOU 2765  CD  GLU A 369     7863   7205   7334   -115   -630    415       C  
ATOM   2766  OE1 GLU A 369      86.051  70.808  67.308  1.00 62.03           O  
ANISOU 2766  OE1 GLU A 369     8225   7667   7676    -96   -689    441       O  
ATOM   2767  OE2 GLU A 369      85.758  71.441  65.226  1.00 61.90           O1-
ANISOU 2767  OE2 GLU A 369     8171   7585   7765   -209   -638    371       O1-
ATOM   2768  N   ASN A 370      81.407  68.657  66.304  1.00 31.24           N  
ANISOU 2768  N   ASN A 370     4306   3529   4035    251   -298    569       N  
ATOM   2769  CA  ASN A 370      80.657  68.629  65.063  1.00 30.32           C  
ANISOU 2769  CA  ASN A 370     4143   3369   4010    237   -227    552       C  
ATOM   2770  C   ASN A 370      79.639  69.750  65.122  1.00 30.27           C  
ANISOU 2770  C   ASN A 370     4279   3289   3935    252   -203    524       C  
ATOM   2771  O   ASN A 370      79.303  70.250  66.196  1.00 30.85           O  
ANISOU 2771  O   ASN A 370     4475   3339   3908    299   -212    529       O  
ATOM   2772  CB  ASN A 370      79.960  67.285  64.838  1.00 34.01           C  
ANISOU 2772  CB  ASN A 370     4510   3832   4580    319   -129    602       C  
ATOM   2773  CG  ASN A 370      80.941  66.155  64.612  1.00 48.37           C  
ANISOU 2773  CG  ASN A 370     6185   5711   6483    308   -143    627       C  
ATOM   2774  OD1 ASN A 370      82.060  66.372  64.143  1.00 54.01           O  
ANISOU 2774  OD1 ASN A 370     6838   6471   7213    222   -212    595       O  
ATOM   2775  ND2 ASN A 370      80.530  64.939  64.952  1.00 58.75           N  
ANISOU 2775  ND2 ASN A 370     7446   7024   7853    395    -73    682       N  
ATOM   2776  N   LEU A 371      79.150  70.152  63.960  1.00 29.65           N  
ANISOU 2776  N   LEU A 371     4184   3173   3908    212   -171    497       N  
ATOM   2777  CA  LEU A 371      78.176  71.225  63.890  1.00 29.65           C  
ANISOU 2777  CA  LEU A 371     4311   3101   3854    233   -148    473       C  
ATOM   2778  C   LEU A 371      76.779  70.649  63.696  1.00 33.01           C  
ANISOU 2778  C   LEU A 371     4707   3496   4338    331    -44    505       C  
ATOM   2779  O   LEU A 371      76.550  69.859  62.773  1.00 32.66           O  
ANISOU 2779  O   LEU A 371     4541   3471   4396    323      6    518       O  
ATOM   2780  CB  LEU A 371      78.514  72.186  62.758  1.00 29.97           C  
ANISOU 2780  CB  LEU A 371     4372   3117   3899    126   -189    423       C  
ATOM   2781  CG  LEU A 371      77.383  73.199  62.631  1.00 42.06           C  
ANISOU 2781  CG  LEU A 371     6028   4566   5387    168   -157    409       C  
ATOM   2782  CD1 LEU A 371      77.287  73.989  63.917  1.00 43.75           C  
ANISOU 2782  CD1 LEU A 371     6400   4745   5479    210   -181    398       C  
ATOM   2783  CD2 LEU A 371      77.592  74.097  61.452  1.00 45.71           C  
ANISOU 2783  CD2 LEU A 371     6516   4995   5856     71   -190    370       C  
ATOM   2784  N   GLU A 372      75.849  71.052  64.558  1.00 29.48           N  
ANISOU 2784  N   GLU A 372     4369   3007   3824    418     -7    512       N  
ATOM   2785  CA  GLU A 372      74.455  70.646  64.457  1.00 29.12           C  
ANISOU 2785  CA  GLU A 372     4306   2938   3820    511     92    536       C  
ATOM   2786  C   GLU A 372      73.592  71.851  64.117  1.00 32.67           C  
ANISOU 2786  C   GLU A 372     4857   3323   4232    531    103    505       C  
ATOM   2787  O   GLU A 372      73.660  72.886  64.790  1.00 29.89           O  
ANISOU 2787  O   GLU A 372     4645   2928   3783    536     65    480       O  
ATOM   2788  CB  GLU A 372      73.964  70.007  65.757  1.00 29.55           C  
ANISOU 2788  CB  GLU A 372     4393   3000   3834    608    141    572       C  
ATOM   2789  N   ILE A 373      72.765  71.705  63.092  1.00 28.66           N  
ANISOU 2789  N   ILE A 373     4281   2808   3799    544    156    509       N  
ATOM   2790  CA  ILE A 373      71.839  72.743  62.670  1.00 28.78           C  
ANISOU 2790  CA  ILE A 373     4376   2767   3794    578    171    490       C  
ATOM   2791  C   ILE A 373      70.436  72.172  62.767  1.00 28.62           C  
ANISOU 2791  C   ILE A 373     4307   2754   3812    684    272    515       C  
ATOM   2792  O   ILE A 373      70.144  71.127  62.172  1.00 30.90           O  
ANISOU 2792  O   ILE A 373     4463   3090   4187    680    325    539       O  
ATOM   2793  CB  ILE A 373      72.153  73.223  61.246  1.00 28.38           C  
ANISOU 2793  CB  ILE A 373     4288   2707   3788    485    131    470       C  
ATOM   2794  CG1 ILE A 373      73.550  73.842  61.220  1.00 32.98           C  
ANISOU 2794  CG1 ILE A 373     4925   3284   4321    373     35    438       C  
ATOM   2795  CG2 ILE A 373      71.093  74.201  60.767  1.00 30.32           C  
ANISOU 2795  CG2 ILE A 373     4607   2894   4018    536    150    461       C  
ATOM   2796  CD1 ILE A 373      73.927  74.434  59.886  1.00 35.39           C  
ANISOU 2796  CD1 ILE A 373     5217   3574   4654    270     -8    414       C  
ATOM   2797  N   ARG A 374      69.578  72.834  63.535  1.00 29.20           N  
ANISOU 2797  N   ARG A 374     4488   2784   3822    775    303    507       N  
ATOM   2798  CA  ARG A 374      68.183  72.436  63.672  1.00 29.19           C  
ANISOU 2798  CA  ARG A 374     4448   2793   3849    878    400    524       C  
ATOM   2799  C   ARG A 374      67.303  73.516  63.066  1.00 34.12           C  
ANISOU 2799  C   ARG A 374     5127   3371   4468    922    405    506       C  
ATOM   2800  O   ARG A 374      67.348  74.673  63.499  1.00 31.49           O  
ANISOU 2800  O   ARG A 374     4935   2972   4058    944    370    480       O  
ATOM   2801  CB  ARG A 374      67.808  72.199  65.135  1.00 29.77           C  
ANISOU 2801  CB  ARG A 374     4591   2864   3857    960    447    531       C  
ATOM   2802  CG  ARG A 374      68.644  71.135  65.809  1.00 33.73           C  
ANISOU 2802  CG  ARG A 374     5049   3409   4357    928    439    557       C  
ATOM   2803  CD  ARG A 374      68.124  70.833  67.200  1.00 45.52           C  
ANISOU 2803  CD  ARG A 374     6609   4901   5785   1009    495    568       C  
ATOM   2804  NE  ARG A 374      68.977  69.876  67.894  1.00 55.88           N  
ANISOU 2804  NE  ARG A 374     7893   6250   7086    983    477    599       N  
ATOM   2805  CZ  ARG A 374      68.678  69.328  69.067  1.00 63.41           C  
ANISOU 2805  CZ  ARG A 374     8888   7215   7991   1039    524    621       C  
ATOM   2806  NH1 ARG A 374      67.545  69.647  69.677  1.00 65.88           N  
ANISOU 2806  NH1 ARG A 374     9266   7505   8260   1120    597    608       N  
ATOM   2807  NH2 ARG A 374      69.512  68.466  69.630  1.00 64.85           N  
ANISOU 2807  NH2 ARG A 374     9045   7430   8165   1015    498    656       N  
ATOM   2808  N   LEU A 375      66.509  73.138  62.071  1.00 28.98           N  
ANISOU 2808  N   LEU A 375     4366   2752   3894    935    449    521       N  
ATOM   2809  CA  LEU A 375      65.537  74.030  61.454  1.00 29.27           C  
ANISOU 2809  CA  LEU A 375     4432   2756   3933    993    459    514       C  
ATOM   2810  C   LEU A 375      64.142  73.559  61.834  1.00 30.19           C  
ANISOU 2810  C   LEU A 375     4493   2908   4070   1106    560    526       C  
ATOM   2811  O   LEU A 375      63.826  72.375  61.683  1.00 28.99           O  
ANISOU 2811  O   LEU A 375     4214   2825   3976   1099    621    546       O  
ATOM   2812  CB  LEU A 375      65.696  74.049  59.935  1.00 28.71           C  
ANISOU 2812  CB  LEU A 375     4276   2705   3927    913    424    521       C  
ATOM   2813  CG  LEU A 375      67.074  74.503  59.458  1.00 33.42           C  
ANISOU 2813  CG  LEU A 375     4919   3274   4507    789    330    504       C  
ATOM   2814  CD1 LEU A 375      67.192  74.358  57.950  1.00 34.44           C  
ANISOU 2814  CD1 LEU A 375     4951   3432   4704    702    307    512       C  
ATOM   2815  CD2 LEU A 375      67.318  75.937  59.879  1.00 35.26           C  
ANISOU 2815  CD2 LEU A 375     5330   3417   4651    804    272    478       C  
ATOM   2816  N   ARG A 376      63.327  74.482  62.344  1.00 30.25           N  
ANISOU 2816  N   ARG A 376     4598   2867   4027   1208    581    510       N  
ATOM   2817  CA  ARG A 376      61.981  74.195  62.828  1.00 31.77           C  
ANISOU 2817  CA  ARG A 376     4752   3091   4228   1323    677    513       C  
ATOM   2818  C   ARG A 376      60.969  74.992  62.018  1.00 34.65           C  
ANISOU 2818  C   ARG A 376     5105   3445   4617   1394    683    512       C  
ATOM   2819  O   ARG A 376      61.189  76.169  61.726  1.00 34.59           O  
ANISOU 2819  O   ARG A 376     5204   3362   4575   1401    621    500       O  
ATOM   2820  CB  ARG A 376      61.834  74.534  64.316  1.00 34.23           C  
ANISOU 2820  CB  ARG A 376     5189   3361   4457   1397    710    491       C  
ATOM   2821  CG  ARG A 376      62.758  73.745  65.231  1.00 37.40           C  
ANISOU 2821  CG  ARG A 376     5606   3778   4824   1339    704    498       C  
ATOM   2822  CD  ARG A 376      62.408  72.271  65.224  1.00 40.92           C  
ANISOU 2822  CD  ARG A 376     5910   4307   5330   1331    778    526       C  
ATOM   2823  N   ASP A 377      59.857  74.344  61.666  1.00 30.93           N  
ANISOU 2823  N   ASP A 377     4503   3048   4200   1446    758    526       N  
ATOM   2824  CA  ASP A 377      58.833  74.947  60.808  1.00 34.56           C  
ANISOU 2824  CA  ASP A 377     4920   3520   4691   1515    763    533       C  
ATOM   2825  C   ASP A 377      59.431  75.338  59.458  1.00 35.47           C  
ANISOU 2825  C   ASP A 377     5018   3622   4838   1425    676    549       C  
ATOM   2826  O   ASP A 377      59.164  76.417  58.925  1.00 34.51           O  
ANISOU 2826  O   ASP A 377     4961   3449   4702   1467    629    551       O  
ATOM   2827  CB  ASP A 377      58.169  76.147  61.491  1.00 39.76           C  
ANISOU 2827  CB  ASP A 377     5707   4106   5293   1645    774    511       C  
ATOM   2828  CG  ASP A 377      56.723  76.336  61.069  1.00 57.58           C  
ANISOU 2828  CG  ASP A 377     7879   6411   7586   1760    828    518       C  
ATOM   2829  OD1 ASP A 377      56.278  75.640  60.131  1.00 61.83           O  
ANISOU 2829  OD1 ASP A 377     8264   7040   8189   1727    844    541       O  
ATOM   2830  OD2 ASP A 377      56.033  77.183  61.678  1.00 64.60           O1-
ANISOU 2830  OD2 ASP A 377     8854   7253   8439   1882    856    499       O1-
ATOM   2831  N   ILE A 378      60.256  74.444  58.907  1.00 29.96           N  
ANISOU 2831  N   ILE A 378     4235   2967   4180   1300    656    560       N  
ATOM   2832  CA  ILE A 378      60.935  74.703  57.645  1.00 30.89           C  
ANISOU 2832  CA  ILE A 378     4333   3078   4325   1195    578    570       C  
ATOM   2833  C   ILE A 378      59.920  74.691  56.508  1.00 37.60           C  
ANISOU 2833  C   ILE A 378     5073   3987   5226   1219    593    592       C  
ATOM   2834  O   ILE A 378      58.912  73.970  56.543  1.00 41.27           O  
ANISOU 2834  O   ILE A 378     5422   4533   5727   1272    671    600       O  
ATOM   2835  CB  ILE A 378      62.060  73.670  57.424  1.00 33.70           C  
ANISOU 2835  CB  ILE A 378     4619   3470   4716   1061    565    571       C  
ATOM   2836  CG1 ILE A 378      62.907  74.017  56.193  1.00 28.19           C  
ANISOU 2836  CG1 ILE A 378     3916   2757   4037    940    483    573       C  
ATOM   2837  CG2 ILE A 378      61.500  72.251  57.304  1.00 30.72           C  
ANISOU 2837  CG2 ILE A 378     4081   3189   4402   1050    653    585       C  
ATOM   2838  CD1 ILE A 378      64.164  73.152  56.047  1.00 29.08           C  
ANISOU 2838  CD1 ILE A 378     3976   2893   4179    812    464    567       C  
ATOM   2839  N   LYS A 379      60.174  75.513  55.498  1.00 31.20           N  
ANISOU 2839  N   LYS A 379     4301   3141   4414   1178    516    602       N  
ATOM   2840  CA  LYS A 379      59.266  75.611  54.372  1.00 33.60           C  
ANISOU 2840  CA  LYS A 379     4511   3500   4756   1198    515    627       C  
ATOM   2841  C   LYS A 379      59.926  75.062  53.112  1.00 30.65           C  
ANISOU 2841  C   LYS A 379     4047   3172   4427   1046    477    639       C  
ATOM   2842  O   LYS A 379      61.155  75.089  52.991  1.00 34.87           O  
ANISOU 2842  O   LYS A 379     4635   3665   4951    936    426    625       O  
ATOM   2843  CB  LYS A 379      58.842  77.065  54.148  1.00 38.46           C  
ANISOU 2843  CB  LYS A 379     5247   4036   5331   1289    459    637       C  
ATOM   2844  CG  LYS A 379      58.072  77.658  55.322  1.00 43.63           C  
ANISOU 2844  CG  LYS A 379     5987   4645   5946   1449    506    623       C  
ATOM   2845  CD  LYS A 379      56.996  76.696  55.810  1.00 48.84           C  
ANISOU 2845  CD  LYS A 379     6509   5407   6641   1523    608    621       C  
ATOM   2846  CE  LYS A 379      56.079  77.349  56.831  1.00 52.18           C  
ANISOU 2846  CE  LYS A 379     7003   5793   7028   1689    659    605       C  
ATOM   2847  NZ  LYS A 379      56.837  77.904  57.987  1.00 51.20           N  
ANISOU 2847  NZ  LYS A 379     7051   5563   6838   1700    648    575       N  
ATOM   2848  N   PRO A 380      59.145  74.553  52.158  1.00 31.44           N  
ANISOU 2848  N   PRO A 380     4008   3364   4575   1030    503    660       N  
ATOM   2849  CA  PRO A 380      59.747  73.927  50.975  1.00 31.03           C  
ANISOU 2849  CA  PRO A 380     3864   3361   4564    877    479    665       C  
ATOM   2850  C   PRO A 380      60.526  74.927  50.140  1.00 35.08           C  
ANISOU 2850  C   PRO A 380     4476   3803   5048    801    378    671       C  
ATOM   2851  O   PRO A 380      60.159  76.099  50.022  1.00 33.65           O  
ANISOU 2851  O   PRO A 380     4398   3561   4828    877    327    685       O  
ATOM   2852  CB  PRO A 380      58.539  73.389  50.196  1.00 35.49           C  
ANISOU 2852  CB  PRO A 380     4276   4038   5171    896    526    687       C  
ATOM   2853  CG  PRO A 380      57.404  73.390  51.166  1.00 33.36           C  
ANISOU 2853  CG  PRO A 380     3992   3792   4891   1050    595    686       C  
ATOM   2854  CD  PRO A 380      57.673  74.515  52.112  1.00 30.76           C  
ANISOU 2854  CD  PRO A 380     3836   3347   4503   1147    556    676       C  
ATOM   2855  N   GLY A 381      61.602  74.448  49.546  1.00 28.73           N  
ANISOU 2855  N   GLY A 381     3884   2908   4123    719   -204   1365       N  
ATOM   2856  CA  GLY A 381      62.398  75.255  48.656  1.00 32.24           C  
ANISOU 2856  CA  GLY A 381     4397   3314   4539    684   -215   1397       C  
ATOM   2857  C   GLY A 381      63.861  74.932  48.819  1.00 30.41           C  
ANISOU 2857  C   GLY A 381     4241   3047   4265    615   -203   1326       C  
ATOM   2858  O   GLY A 381      64.235  73.967  49.486  1.00 27.69           O  
ANISOU 2858  O   GLY A 381     3890   2725   3906    593   -198   1260       O  
ATOM   2859  N   VAL A 382      64.689  75.774  48.209  1.00 29.46           N  
ANISOU 2859  N   VAL A 382     4192   2869   4131    583   -193   1345       N  
ATOM   2860  CA  VAL A 382      66.133  75.579  48.184  1.00 30.22           C  
ANISOU 2860  CA  VAL A 382     4353   2933   4195    509   -180   1294       C  
ATOM   2861  C   VAL A 382      66.744  76.321  49.364  1.00 30.92           C  
ANISOU 2861  C   VAL A 382     4504   2905   4339    524   -116   1227       C  
ATOM   2862  O   VAL A 382      66.656  77.552  49.446  1.00 34.76           O  
ANISOU 2862  O   VAL A 382     5037   3302   4869    551    -78   1245       O  
ATOM   2863  CB  VAL A 382      66.731  76.069  46.857  1.00 29.62           C  
ANISOU 2863  CB  VAL A 382     4322   2859   4074    454   -197   1354       C  
ATOM   2864  CG1 VAL A 382      68.255  76.027  46.911  1.00 31.22           C  
ANISOU 2864  CG1 VAL A 382     4587   3013   4263    378   -167   1305       C  
ATOM   2865  CG2 VAL A 382      66.194  75.240  45.703  1.00 29.77           C  
ANISOU 2865  CG2 VAL A 382     4287   3000   4023    421   -261   1414       C  
ATOM   2866  N   TRP A 383      67.354  75.570  50.279  1.00 26.96           N  
ANISOU 2866  N   TRP A 383     4005   2402   3835    504   -102   1152       N  
ATOM   2867  CA  TRP A 383      68.091  76.109  51.412  1.00 23.96           C  
ANISOU 2867  CA  TRP A 383     3691   1922   3493    499    -47   1083       C  
ATOM   2868  C   TRP A 383      69.585  75.948  51.161  1.00 27.24           C  
ANISOU 2868  C   TRP A 383     4148   2318   3885    416    -42   1061       C  
ATOM   2869  O   TRP A 383      70.026  74.983  50.534  1.00 30.47           O  
ANISOU 2869  O   TRP A 383     4515   2818   4244    365    -83   1057       O  
ATOM   2870  CB  TRP A 383      67.684  75.399  52.709  1.00 27.45           C  
ANISOU 2870  CB  TRP A 383     4109   2376   3945    540    -30   1019       C  
ATOM   2871  CG  TRP A 383      66.270  75.702  53.110  1.00 30.56           C  
ANISOU 2871  CG  TRP A 383     4465   2770   4378    620    -12   1036       C  
ATOM   2872  CD1 TRP A 383      65.130  75.197  52.550  1.00 31.33           C  
ANISOU 2872  CD1 TRP A 383     4479   2953   4470    655    -49   1091       C  
ATOM   2873  CD2 TRP A 383      65.844  76.605  54.140  1.00 32.68           C  
ANISOU 2873  CD2 TRP A 383     4777   2944   4698    669     57   1002       C  
ATOM   2874  NE1 TRP A 383      64.019  75.733  53.167  1.00 32.23           N  
ANISOU 2874  NE1 TRP A 383     4571   3034   4639    729     -8   1100       N  
ATOM   2875  CE2 TRP A 383      64.433  76.594  54.151  1.00 34.44           C  
ANISOU 2875  CE2 TRP A 383     4931   3203   4953    740     62   1044       C  
ATOM   2876  CE3 TRP A 383      66.520  77.423  55.052  1.00 33.80           C  
ANISOU 2876  CE3 TRP A 383     5012   2971   4859    653    122    940       C  
ATOM   2877  CZ2 TRP A 383      63.684  77.369  55.040  1.00 37.94           C  
ANISOU 2877  CZ2 TRP A 383     5392   3571   5452    803    137   1029       C  
ATOM   2878  CZ3 TRP A 383      65.775  78.193  55.933  1.00 39.71           C  
ANISOU 2878  CZ3 TRP A 383     5791   3644   5653    709    195    917       C  
ATOM   2879  CH2 TRP A 383      64.372  78.158  55.922  1.00 41.19           C  
ANISOU 2879  CH2 TRP A 383     5904   3869   5876    787    205    963       C  
ATOM   2880  N   ILE A 384      70.370  76.902  51.647  1.00 28.93           N  
ANISOU 2880  N   ILE A 384     4438   2430   4124    383      6   1016       N  
ATOM   2881  CA  ILE A 384      71.801  76.925  51.376  1.00 26.15           C  
ANISOU 2881  CA  ILE A 384     4107   2088   3740    277     -1    959       C  
ATOM   2882  C   ILE A 384      72.563  76.891  52.688  1.00 25.93           C  
ANISOU 2882  C   ILE A 384     4104   2041   3707    236     13    845       C  
ATOM   2883  O   ILE A 384      72.280  77.675  53.601  1.00 30.14           O  
ANISOU 2883  O   ILE A 384     4701   2481   4270    262     59    813       O  
ATOM   2884  CB  ILE A 384      72.204  78.153  50.545  1.00 30.02           C  
ANISOU 2884  CB  ILE A 384     4663   2492   4253    242     34   1012       C  
ATOM   2885  CG1 ILE A 384      71.465  78.129  49.207  1.00 37.84           C  
ANISOU 2885  CG1 ILE A 384     5627   3518   5232    278      7   1135       C  
ATOM   2886  CG2 ILE A 384      73.712  78.170  50.331  1.00 28.38           C  
ANISOU 2886  CG2 ILE A 384     4467   2296   4021    126     34    948       C  
ATOM   2887  CD1 ILE A 384      71.557  79.421  48.428  1.00 44.05           C  
ANISOU 2887  CD1 ILE A 384     6473   4232   6033    260     33   1184       C  
ATOM   2888  N   LEU A 385      73.524  75.973  52.774  1.00 24.57           N  
ANISOU 2888  N   LEU A 385     3884   1956   3495    173    -24    788       N  
ATOM   2889  CA  LEU A 385      74.499  75.928  53.850  1.00 27.00           C  
ANISOU 2889  CA  LEU A 385     4203   2267   3788    113    -29    692       C  
ATOM   2890  C   LEU A 385      75.801  76.504  53.295  1.00 28.58           C  
ANISOU 2890  C   LEU A 385     4416   2451   3992      9    -23    675       C  
ATOM   2891  O   LEU A 385      76.434  75.901  52.420  1.00 30.01           O  
ANISOU 2891  O   LEU A 385     4542   2702   4158    -30    -41    697       O  
ATOM   2892  CB  LEU A 385      74.661  74.489  54.344  1.00 29.80           C  
ANISOU 2892  CB  LEU A 385     4483   2734   4107    125    -71    656       C  
ATOM   2893  CG  LEU A 385      75.556  74.175  55.533  1.00 41.45           C  
ANISOU 2893  CG  LEU A 385     5950   4241   5556     79    -94    571       C  
ATOM   2894  CD1 LEU A 385      75.239  75.108  56.686  1.00 43.69           C  
ANISOU 2894  CD1 LEU A 385     6320   4437   5844     82    -66    521       C  
ATOM   2895  CD2 LEU A 385      75.365  72.720  55.947  1.00 42.26           C  
ANISOU 2895  CD2 LEU A 385     5985   4442   5629    124   -124    563       C  
ATOM   2896  N   ARG A 386      76.173  77.690  53.774  1.00 23.87           N  
ANISOU 2896  N   ARG A 386     3897   1757   3417    -39     13    638       N  
ATOM   2897  CA  ARG A 386      77.357  78.403  53.308  1.00 27.35           C  
ANISOU 2897  CA  ARG A 386     4358   2167   3868   -147     28    620       C  
ATOM   2898  C   ARG A 386      78.493  78.133  54.287  1.00 25.78           C  
ANISOU 2898  C   ARG A 386     4129   2021   3647   -235     -7    528       C  
ATOM   2899  O   ARG A 386      78.435  78.563  55.444  1.00 25.69           O  
ANISOU 2899  O   ARG A 386     4172   1966   3624   -252     -3    463       O  
ATOM   2900  CB  ARG A 386      77.070  79.897  53.191  1.00 29.63           C  
ANISOU 2900  CB  ARG A 386     4756   2307   4194   -156     96    638       C  
ATOM   2901  CG  ARG A 386      78.286  80.738  52.872  1.00 31.44           C  
ANISOU 2901  CG  ARG A 386     5020   2489   4436   -280    122    607       C  
ATOM   2902  CD  ARG A 386      77.869  82.078  52.284  1.00 35.32           C  
ANISOU 2902  CD  ARG A 386     5616   2835   4969   -270    198    662       C  
ATOM   2903  NE  ARG A 386      77.391  81.928  50.914  1.00 33.71           N  
ANISOU 2903  NE  ARG A 386     5390   2649   4770   -214    199    774       N  
ATOM   2904  CZ  ARG A 386      76.734  82.868  50.239  1.00 31.57           C  
ANISOU 2904  CZ  ARG A 386     5191   2273   4531   -165    254    860       C  
ATOM   2905  NH1 ARG A 386      76.468  84.038  50.805  1.00 29.27           N  
ANISOU 2905  NH1 ARG A 386     5005   1837   4281   -158    327    844       N  
ATOM   2906  NH2 ARG A 386      76.344  82.632  48.993  1.00 33.64           N  
ANISOU 2906  NH2 ARG A 386     5427   2574   4781   -124    238    965       N  
ATOM   2907  N   LEU A 387      79.521  77.422  53.823  1.00 24.20           N  
ANISOU 2907  N   LEU A 387     3841   1916   3440   -290    -39    526       N  
ATOM   2908  CA  LEU A 387      80.612  76.949  54.666  1.00 26.20           C  
ANISOU 2908  CA  LEU A 387     4031   2249   3676   -361    -86    461       C  
ATOM   2909  C   LEU A 387      81.901  77.695  54.356  1.00 29.86           C  
ANISOU 2909  C   LEU A 387     4486   2698   4163   -489    -75    437       C  
ATOM   2910  O   LEU A 387      82.240  77.915  53.189  1.00 29.51           O  
ANISOU 2910  O   LEU A 387     4430   2637   4144   -515    -40    483       O  
ATOM   2911  CB  LEU A 387      80.834  75.450  54.466  1.00 23.11           C  
ANISOU 2911  CB  LEU A 387     3528   1982   3269   -317   -123    484       C  
ATOM   2912  CG  LEU A 387      79.565  74.617  54.633  1.00 24.37           C  
ANISOU 2912  CG  LEU A 387     3690   2162   3408   -200   -129    511       C  
ATOM   2913  CD1 LEU A 387      79.856  73.175  54.313  1.00 25.70           C  
ANISOU 2913  CD1 LEU A 387     3762   2437   3565   -168   -148    532       C  
ATOM   2914  CD2 LEU A 387      79.042  74.759  56.049  1.00 24.46           C  
ANISOU 2914  CD2 LEU A 387     3749   2151   3394   -171   -146    458       C  
ATOM   2915  N   THR A 388      82.626  78.062  55.408  1.00 27.90           N  
ANISOU 2915  N   THR A 388     4242   2460   3901   -576   -107    365       N  
ATOM   2916  CA  THR A 388      83.891  78.779  55.303  1.00 25.79           C  
ANISOU 2916  CA  THR A 388     3957   2187   3655   -715   -105    331       C  
ATOM   2917  C   THR A 388      84.945  77.995  56.065  1.00 32.52           C  
ANISOU 2917  C   THR A 388     4691   3175   4492   -771   -182    298       C  
ATOM   2918  O   THR A 388      84.761  77.699  57.249  1.00 35.27           O  
ANISOU 2918  O   THR A 388     5047   3562   4794   -760   -235    254       O  
ATOM   2919  CB  THR A 388      83.796  80.199  55.884  1.00 34.09           C  
ANISOU 2919  CB  THR A 388     5140   3112   4703   -795    -68    272       C  
ATOM   2920  OG1 THR A 388      82.639  80.866  55.369  1.00 39.87           O  
ANISOU 2920  OG1 THR A 388     5982   3715   5452   -714      5    314       O  
ATOM   2921  CG2 THR A 388      85.045  81.005  55.530  1.00 35.95           C  
ANISOU 2921  CG2 THR A 388     5362   3330   4969   -948    -51    246       C  
ATOM   2922  N   SER A 389      86.048  77.667  55.401  1.00 29.96           N  
ANISOU 2922  N   SER A 389     4256   2921   4204   -828   -187    323       N  
ATOM   2923  CA  SER A 389      87.093  76.902  56.063  1.00 31.93           C  
ANISOU 2923  CA  SER A 389     4373   3307   4452   -871   -260    310       C  
ATOM   2924  C   SER A 389      87.913  77.809  56.973  1.00 33.04           C  
ANISOU 2924  C   SER A 389     4526   3449   4576  -1021   -304    239       C  
ATOM   2925  O   SER A 389      88.170  78.971  56.649  1.00 34.31           O  
ANISOU 2925  O   SER A 389     4759   3519   4758  -1120   -259    211       O  
ATOM   2926  CB  SER A 389      87.991  76.214  55.035  1.00 33.93           C  
ANISOU 2926  CB  SER A 389     4496   3634   4761   -874   -235    367       C  
ATOM   2927  OG  SER A 389      88.669  77.161  54.242  1.00 36.47           O  
ANISOU 2927  OG  SER A 389     4831   3899   5127   -979   -183    366       O  
ATOM   2928  N   GLU A 390      88.303  77.271  58.129  1.00 36.92           N  
ANISOU 2928  N   GLU A 390     4956   4046   5027  -1040   -394    212       N  
ATOM   2929  CA  GLU A 390      89.132  77.978  59.099  1.00 40.80           C  
ANISOU 2929  CA  GLU A 390     5447   4570   5486  -1194   -458    145       C  
ATOM   2930  C   GLU A 390      90.495  77.336  59.308  1.00 39.23           C  
ANISOU 2930  C   GLU A 390     5060   4532   5313  -1260   -538    172       C  
ATOM   2931  O   GLU A 390      91.471  78.052  59.531  1.00 39.86           O  
ANISOU 2931  O   GLU A 390     5104   4640   5403  -1416   -571    136       O  
ATOM   2932  CB  GLU A 390      88.419  78.062  60.461  1.00 44.15           C  
ANISOU 2932  CB  GLU A 390     5976   4981   5819  -1184   -505     84       C  
ATOM   2933  CG  GLU A 390      87.110  78.845  60.458  1.00 48.96           C  
ANISOU 2933  CG  GLU A 390     6772   5425   6407  -1131   -422     51       C  
ATOM   2934  CD  GLU A 390      86.615  79.160  61.865  1.00 53.38           C  
ANISOU 2934  CD  GLU A 390     7449   5959   6875  -1161   -454    -26       C  
ATOM   2935  OE1 GLU A 390      85.716  78.447  62.362  1.00 51.10           O  
ANISOU 2935  OE1 GLU A 390     7186   5681   6547  -1040   -460    -13       O  
ATOM   2936  OE2 GLU A 390      87.125  80.124  62.474  1.00 54.37           O1-
ANISOU 2936  OE2 GLU A 390     7645   6049   6964  -1313   -466   -103       O1-
ATOM   2937  N   LEU A 391      90.579  76.008  59.254  1.00 39.94           N  
ANISOU 2937  N   LEU A 391     5029   4729   5419  -1146   -566    239       N  
ATOM   2938  CA  LEU A 391      91.839  75.284  59.309  1.00 41.03           C  
ANISOU 2938  CA  LEU A 391     4971   5017   5602  -1176   -625    289       C  
ATOM   2939  C   LEU A 391      91.635  73.986  58.549  1.00 37.89           C  
ANISOU 2939  C   LEU A 391     4490   4655   5253  -1019   -575    371       C  
ATOM   2940  O   LEU A 391      90.614  73.321  58.727  1.00 36.30           O  
ANISOU 2940  O   LEU A 391     4352   4428   5011   -894   -563    382       O  
ATOM   2941  CB  LEU A 391      92.274  75.017  60.760  1.00 51.29           C  
ANISOU 2941  CB  LEU A 391     6217   6437   6832  -1227   -754    269       C  
ATOM   2942  CG  LEU A 391      93.490  74.133  61.077  1.00 58.14           C  
ANISOU 2942  CG  LEU A 391     6869   7483   7738  -1236   -837    338       C  
ATOM   2943  CD1 LEU A 391      93.982  74.458  62.472  1.00 58.57           C  
ANISOU 2943  CD1 LEU A 391     6910   7636   7708  -1357   -972    297       C  
ATOM   2944  CD2 LEU A 391      93.209  72.628  60.978  1.00 59.93           C  
ANISOU 2944  CD2 LEU A 391     7013   7772   7986  -1055   -826    423       C  
ATOM   2945  N   ILE A 392      92.587  73.631  57.689  1.00 36.13           N  
ANISOU 2945  N   ILE A 392     4129   4483   5115  -1031   -536    426       N  
ATOM   2946  CA  ILE A 392      92.469  72.397  56.924  1.00 34.31           C  
ANISOU 2946  CA  ILE A 392     3828   4278   4931   -893   -472    499       C  
ATOM   2947  C   ILE A 392      93.795  71.649  56.938  1.00 33.86           C  
ANISOU 2947  C   ILE A 392     3563   4353   4949   -900   -494    564       C  
ATOM   2948  O   ILE A 392      94.871  72.243  57.058  1.00 37.60           O  
ANISOU 2948  O   ILE A 392     3940   4883   5464  -1025   -530    560       O  
ATOM   2949  CB  ILE A 392      92.002  72.650  55.465  1.00 39.85           C  
ANISOU 2949  CB  ILE A 392     4609   4867   5667   -866   -349    509       C  
ATOM   2950  CG1 ILE A 392      93.115  73.278  54.631  1.00 43.41           C  
ANISOU 2950  CG1 ILE A 392     4985   5316   6193   -978   -297    521       C  
ATOM   2951  CG2 ILE A 392      90.744  73.512  55.423  1.00 42.00           C  
ANISOU 2951  CG2 ILE A 392     5072   5010   5877   -862   -329    459       C  
ATOM   2952  CD1 ILE A 392      92.763  73.393  53.159  1.00 47.95           C  
ANISOU 2952  CD1 ILE A 392     5629   5794   6794   -949   -175    543       C  
ATOM   2953  N   ILE A 393      93.700  70.322  56.857  1.00 35.19           N  
ANISOU 2953  N   ILE A 393     3660   4572   5138   -765   -469    627       N  
ATOM   2954  CA  ILE A 393      94.820  69.503  56.412  1.00 40.97           C  
ANISOU 2954  CA  ILE A 393     4208   5392   5968   -734   -431    706       C  
ATOM   2955  C   ILE A 393      94.387  68.844  55.109  1.00 39.64           C  
ANISOU 2955  C   ILE A 393     4081   5144   5836   -637   -289    735       C  
ATOM   2956  O   ILE A 393      94.850  69.226  54.029  1.00 41.41           O  
ANISOU 2956  O   ILE A 393     4292   5325   6119   -688   -199    741       O  
ATOM   2957  CB  ILE A 393      95.253  68.467  57.464  1.00 47.19           C  
ANISOU 2957  CB  ILE A 393     4864   6310   6756   -660   -516    767       C  
ATOM   2958  CG1 ILE A 393      95.937  69.166  58.637  1.00 48.90           C  
ANISOU 2958  CG1 ILE A 393     5015   6627   6938   -786   -662    747       C  
ATOM   2959  CG2 ILE A 393      96.223  67.465  56.853  1.00 48.39           C  
ANISOU 2959  CG2 ILE A 393     4837   6527   7022   -588   -441    862       C  
ATOM   2960  CD1 ILE A 393      96.283  68.238  59.780  1.00 50.36           C  
ANISOU 2960  CD1 ILE A 393     5086   6947   7102   -720   -765    811       C  
ATOM   2961  N   SER A 394      93.474  67.871  55.193  1.00 37.69           N  
ANISOU 2961  N   SER A 394     3896   4875   5549   -508   -265    749       N  
ATOM   2962  CA  SER A 394      92.911  67.293  53.979  1.00 36.38           C  
ANISOU 2962  CA  SER A 394     3799   4628   5396   -434   -137    763       C  
ATOM   2963  C   SER A 394      91.820  68.166  53.383  1.00 33.95           C  
ANISOU 2963  C   SER A 394     3669   4205   5025   -469   -111    706       C  
ATOM   2964  O   SER A 394      91.574  68.090  52.175  1.00 38.53           O  
ANISOU 2964  O   SER A 394     4305   4720   5615   -459    -10    714       O  
ATOM   2965  CB  SER A 394      92.346  65.895  54.248  1.00 37.25           C  
ANISOU 2965  CB  SER A 394     3909   4755   5488   -294   -113    798       C  
ATOM   2966  OG  SER A 394      91.120  65.960  54.959  1.00 37.77           O  
ANISOU 2966  OG  SER A 394     4101   4788   5464   -257   -175    756       O  
ATOM   2967  N   GLY A 395      91.168  68.991  54.200  1.00 32.26           N  
ANISOU 2967  N   GLY A 395     3547   3965   4745   -508   -197    654       N  
ATOM   2968  CA  GLY A 395      90.076  69.818  53.741  1.00 28.31           C  
ANISOU 2968  CA  GLY A 395     3209   3355   4193   -524   -174    613       C  
ATOM   2969  C   GLY A 395      88.761  69.100  53.560  1.00 29.27           C  
ANISOU 2969  C   GLY A 395     3425   3434   4264   -414   -147    617       C  
ATOM   2970  O   GLY A 395      87.766  69.747  53.208  1.00 27.72           O  
ANISOU 2970  O   GLY A 395     3353   3154   4026   -416   -133    594       O  
ATOM   2971  N   GLU A 396      88.713  67.791  53.796  1.00 27.76           N  
ANISOU 2971  N   GLU A 396     3176   3296   4076   -320   -135    650       N  
ATOM   2972  CA  GLU A 396      87.518  67.019  53.498  1.00 28.86           C  
ANISOU 2972  CA  GLU A 396     3398   3396   4172   -228    -97    654       C  
ATOM   2973  C   GLU A 396      86.487  67.162  54.609  1.00 29.15           C  
ANISOU 2973  C   GLU A 396     3509   3422   4145   -190   -170    621       C  
ATOM   2974  O   GLU A 396      86.824  67.294  55.790  1.00 28.80           O  
ANISOU 2974  O   GLU A 396     3428   3427   4086   -202   -248    607       O  
ATOM   2975  CB  GLU A 396      87.877  65.549  53.289  1.00 35.08           C  
ANISOU 2975  CB  GLU A 396     4106   4231   4992   -146    -37    699       C  
ATOM   2976  CG  GLU A 396      88.794  65.335  52.095  1.00 46.24           C  
ANISOU 2976  CG  GLU A 396     5460   5641   6468   -175     63    730       C  
ATOM   2977  CD  GLU A 396      88.976  63.877  51.735  1.00 63.35           C  
ANISOU 2977  CD  GLU A 396     7581   7826   8664    -89    153    770       C  
ATOM   2978  OE1 GLU A 396      88.618  63.008  52.558  1.00 69.90           O  
ANISOU 2978  OE1 GLU A 396     8396   8685   9477     -7    126    782       O  
ATOM   2979  OE2 GLU A 396      89.472  63.599  50.623  1.00 69.44           O1-
ANISOU 2979  OE2 GLU A 396     8339   8573   9473   -104    261    788       O1-
ATOM   2980  N   TYR A 397      85.215  67.151  54.217  1.00 25.23           N  
ANISOU 2980  N   TYR A 397     3117   2862   3606   -147   -145    611       N  
ATOM   2981  CA  TYR A 397      84.136  67.208  55.195  1.00 24.29           C  
ANISOU 2981  CA  TYR A 397     3070   2725   3434   -101   -194    584       C  
ATOM   2982  C   TYR A 397      82.930  66.453  54.662  1.00 19.31           C  
ANISOU 2982  C   TYR A 397     2496   2064   2776    -26   -148    598       C  
ATOM   2983  O   TYR A 397      82.816  66.184  53.463  1.00 21.37           O  
ANISOU 2983  O   TYR A 397     2770   2305   3047    -29    -86    620       O  
ATOM   2984  CB  TYR A 397      83.758  68.654  55.543  1.00 23.53           C  
ANISOU 2984  CB  TYR A 397     3057   2565   3317   -161   -231    543       C  
ATOM   2985  CG  TYR A 397      83.258  69.486  54.374  1.00 21.12           C  
ANISOU 2985  CG  TYR A 397     2826   2179   3020   -190   -182    552       C  
ATOM   2986  CD1 TYR A 397      84.145  70.169  53.535  1.00 21.93           C  
ANISOU 2986  CD1 TYR A 397     2909   2264   3159   -272   -152    561       C  
ATOM   2987  CD2 TYR A 397      81.895  69.602  54.120  1.00 22.89           C  
ANISOU 2987  CD2 TYR A 397     3135   2346   3215   -136   -167    559       C  
ATOM   2988  CE1 TYR A 397      83.672  70.931  52.471  1.00 22.97           C  
ANISOU 2988  CE1 TYR A 397     3116   2321   3291   -296   -109    578       C  
ATOM   2989  CE2 TYR A 397      81.421  70.358  53.069  1.00 23.54           C  
ANISOU 2989  CE2 TYR A 397     3281   2362   3301   -157   -131    581       C  
ATOM   2990  CZ  TYR A 397      82.308  71.024  52.253  1.00 21.78           C  
ANISOU 2990  CZ  TYR A 397     3049   2120   3107   -235   -103    592       C  
ATOM   2991  OH  TYR A 397      81.811  71.775  51.213  1.00 25.80           O  
ANISOU 2991  OH  TYR A 397     3628   2563   3613   -252    -68    623       O  
ATOM   2992  N   ASP A 398      82.022  66.112  55.579  1.00 20.75           N  
ANISOU 2992  N   ASP A 398     2718   2246   2921     34   -178    583       N  
ATOM   2993  CA  ASP A 398      80.818  65.368  55.242  1.00 20.29           C  
ANISOU 2993  CA  ASP A 398     2706   2167   2837    100   -143    594       C  
ATOM   2994  C   ASP A 398      79.626  65.989  55.955  1.00 21.61           C  
ANISOU 2994  C   ASP A 398     2950   2289   2970    125   -175    569       C  
ATOM   2995  O   ASP A 398      79.751  66.462  57.088  1.00 25.11           O  
ANISOU 2995  O   ASP A 398     3408   2735   3398    118   -221    540       O  
ATOM   2996  CB  ASP A 398      80.956  63.888  55.629  1.00 22.02           C  
ANISOU 2996  CB  ASP A 398     2875   2436   3055    166   -119    611       C  
ATOM   2997  CG  ASP A 398      82.028  63.176  54.817  1.00 25.78           C  
ANISOU 2997  CG  ASP A 398     3279   2942   3573    156    -61    642       C  
ATOM   2998  OD1 ASP A 398      83.179  63.063  55.307  1.00 31.40           O  
ANISOU 2998  OD1 ASP A 398     3907   3704   4319    148    -81    657       O  
ATOM   2999  OD2 ASP A 398      81.722  62.738  53.687  1.00 25.76           O1-
ANISOU 2999  OD2 ASP A 398     3302   2915   3569    152      7    653       O1-
ATOM   3000  N   ILE A 399      78.477  66.005  55.285  1.00 19.94           N  
ANISOU 3000  N   ILE A 399     2790   2039   2747    150   -148    583       N  
ATOM   3001  CA  ILE A 399      77.248  66.534  55.862  1.00 18.62           C  
ANISOU 3001  CA  ILE A 399     2686   1828   2563    186   -163    571       C  
ATOM   3002  C   ILE A 399      76.160  65.486  55.700  1.00 18.47           C  
ANISOU 3002  C   ILE A 399     2669   1823   2526    246   -137    588       C  
ATOM   3003  O   ILE A 399      76.048  64.861  54.639  1.00 18.84           O  
ANISOU 3003  O   ILE A 399     2702   1886   2571    237   -106    613       O  
ATOM   3004  CB  ILE A 399      76.817  67.860  55.201  1.00 19.27           C  
ANISOU 3004  CB  ILE A 399     2821   1841   2658    155   -159    583       C  
ATOM   3005  CG1 ILE A 399      78.036  68.751  54.928  1.00 24.69           C  
ANISOU 3005  CG1 ILE A 399     3500   2514   3367     75   -167    572       C  
ATOM   3006  CG2 ILE A 399      75.805  68.576  56.085  1.00 19.37           C  
ANISOU 3006  CG2 ILE A 399     2894   1798   2667    194   -167    567       C  
ATOM   3007  CD1 ILE A 399      77.672  70.080  54.308  1.00 24.83           C  
ANISOU 3007  CD1 ILE A 399     3581   2454   3401     45   -154    589       C  
ATOM   3008  N   TYR A 400      75.338  65.311  56.739  1.00 17.58           N  
ANISOU 3008  N   TYR A 400     2580   1702   2398    299   -145    572       N  
ATOM   3009  CA  TYR A 400      74.277  64.308  56.719  1.00 17.56           C  
ANISOU 3009  CA  TYR A 400     2577   1714   2382    350   -119    584       C  
ATOM   3010  C   TYR A 400      72.935  64.906  57.118  1.00 18.24           C  
ANISOU 3010  C   TYR A 400     2703   1756   2471    389   -118    587       C  
ATOM   3011  O   TYR A 400      72.841  65.675  58.079  1.00 20.00           O  
ANISOU 3011  O   TYR A 400     2964   1942   2694    403   -129    561       O  
ATOM   3012  CB  TYR A 400      74.597  63.122  57.650  1.00 16.34           C  
ANISOU 3012  CB  TYR A 400     2399   1600   2209    390   -110    571       C  
ATOM   3013  CG  TYR A 400      75.789  62.336  57.161  1.00 17.08           C  
ANISOU 3013  CG  TYR A 400     2441   1736   2314    370    -92    583       C  
ATOM   3014  CD1 TYR A 400      77.069  62.668  57.577  1.00 18.29           C  
ANISOU 3014  CD1 TYR A 400     2559   1914   2478    344   -123    578       C  
ATOM   3015  CD2 TYR A 400      75.637  61.304  56.240  1.00 17.91           C  
ANISOU 3015  CD2 TYR A 400     2532   1853   2419    370    -40    601       C  
ATOM   3016  CE1 TYR A 400      78.170  61.982  57.117  1.00 18.87           C  
ANISOU 3016  CE1 TYR A 400     2571   2023   2574    334    -98    599       C  
ATOM   3017  CE2 TYR A 400      76.737  60.602  55.773  1.00 17.03           C  
ANISOU 3017  CE2 TYR A 400     2379   1767   2325    358     -4    614       C  
ATOM   3018  CZ  TYR A 400      78.003  60.954  56.213  1.00 18.44           C  
ANISOU 3018  CZ  TYR A 400     2509   1970   2526    346    -32    617       C  
ATOM   3019  OH  TYR A 400      79.113  60.280  55.758  1.00 19.17           O  
ANISOU 3019  OH  TYR A 400     2546   2088   2650    343     12    639       O  
ATOM   3020  N   LEU A 401      71.909  64.532  56.370  1.00 17.11           N  
ANISOU 3020  N   LEU A 401     2551   1618   2330    403   -102    618       N  
ATOM   3021  CA  LEU A 401      70.515  64.728  56.748  1.00 18.43           C  
ANISOU 3021  CA  LEU A 401     2732   1762   2510    453    -92    631       C  
ATOM   3022  C   LEU A 401      70.036  63.499  57.501  1.00 16.75           C  
ANISOU 3022  C   LEU A 401     2508   1579   2279    492    -66    614       C  
ATOM   3023  O   LEU A 401      70.721  62.471  57.514  1.00 18.02           O  
ANISOU 3023  O   LEU A 401     2651   1776   2419    482    -55    601       O  
ATOM   3024  CB  LEU A 401      69.671  64.968  55.495  1.00 16.02           C  
ANISOU 3024  CB  LEU A 401     2410   1463   2216    438    -98    685       C  
ATOM   3025  CG  LEU A 401      70.079  66.144  54.616  1.00 20.88           C  
ANISOU 3025  CG  LEU A 401     3041   2046   2844    401   -118    715       C  
ATOM   3026  CD1 LEU A 401      69.230  66.209  53.349  1.00 24.36           C  
ANISOU 3026  CD1 LEU A 401     3464   2511   3283    385   -133    780       C  
ATOM   3027  CD2 LEU A 401      69.963  67.442  55.396  1.00 30.31           C  
ANISOU 3027  CD2 LEU A 401     4278   3167   4072    431   -114    707       C  
ATOM   3028  N   PRO A 402      68.868  63.555  58.145  1.00 18.70           N  
ANISOU 3028  N   PRO A 402     2763   1805   2539    542    -47    617       N  
ATOM   3029  CA  PRO A 402      68.335  62.343  58.784  1.00 18.03           C  
ANISOU 3029  CA  PRO A 402     2668   1744   2437    574    -14    604       C  
ATOM   3030  C   PRO A 402      68.036  61.267  57.753  1.00 17.67           C  
ANISOU 3030  C   PRO A 402     2587   1745   2382    541     -1    624       C  
ATOM   3031  O   PRO A 402      67.966  61.518  56.547  1.00 17.60           O  
ANISOU 3031  O   PRO A 402     2560   1751   2375    497    -21    653       O  
ATOM   3032  CB  PRO A 402      67.049  62.817  59.465  1.00 18.41           C  
ANISOU 3032  CB  PRO A 402     2726   1756   2511    627     11    612       C  
ATOM   3033  CG  PRO A 402      67.169  64.298  59.545  1.00 19.26           C  
ANISOU 3033  CG  PRO A 402     2866   1809   2644    632     -3    616       C  
ATOM   3034  CD  PRO A 402      67.974  64.711  58.352  1.00 18.77           C  
ANISOU 3034  CD  PRO A 402     2790   1760   2582    575    -42    636       C  
ATOM   3035  N   ASN A 403      67.849  60.043  58.252  1.00 15.99           N  
ANISOU 3035  N   ASN A 403     2373   1550   2152    558     37    608       N  
ATOM   3036  CA  ASN A 403      67.496  58.934  57.371  1.00 16.65           C  
ANISOU 3036  CA  ASN A 403     2437   1667   2222    518     64    616       C  
ATOM   3037  C   ASN A 403      66.268  59.286  56.545  1.00 19.05           C  
ANISOU 3037  C   ASN A 403     2710   1988   2540    492     45    650       C  
ATOM   3038  O   ASN A 403      65.344  59.943  57.033  1.00 18.14           O  
ANISOU 3038  O   ASN A 403     2580   1857   2457    533     38    668       O  
ATOM   3039  CB  ASN A 403      67.221  57.672  58.178  1.00 15.75           C  
ANISOU 3039  CB  ASN A 403     2335   1554   2094    547    120    596       C  
ATOM   3040  CG  ASN A 403      68.457  57.148  58.876  1.00 16.59           C  
ANISOU 3040  CG  ASN A 403     2463   1657   2185    575    136    579       C  
ATOM   3041  OD1 ASN A 403      69.581  57.424  58.461  1.00 17.01           O  
ANISOU 3041  OD1 ASN A 403     2509   1716   2236    554    115    581       O  
ATOM   3042  ND2 ASN A 403      68.255  56.378  59.937  1.00 18.07           N  
ANISOU 3042  ND2 ASN A 403     2670   1835   2360    621    176    569       N  
ATOM   3043  N   LYS A 404      66.276  58.847  55.278  1.00 15.77           N  
ANISOU 3043  N   LYS A 404     2284   1607   2100    422     38    664       N  
ATOM   3044  CA  LYS A 404      65.243  59.259  54.330  1.00 16.21           C  
ANISOU 3044  CA  LYS A 404     2306   1696   2159    383      0    709       C  
ATOM   3045  C   LYS A 404      63.851  58.867  54.793  1.00 15.86           C  
ANISOU 3045  C   LYS A 404     2220   1669   2136    404     13    722       C  
ATOM   3046  O   LYS A 404      62.880  59.591  54.521  1.00 18.49           O  
ANISOU 3046  O   LYS A 404     2507   2019   2499    414    -24    772       O  
ATOM   3047  CB  LYS A 404      65.540  58.657  52.949  1.00 16.83           C  
ANISOU 3047  CB  LYS A 404     2396   1813   2186    289     -3    711       C  
ATOM   3048  CG  LYS A 404      64.693  59.236  51.795  1.00 19.47           C  
ANISOU 3048  CG  LYS A 404     2699   2194   2506    236    -64    769       C  
ATOM   3049  CD  LYS A 404      64.934  60.748  51.665  1.00 23.11           C  
ANISOU 3049  CD  LYS A 404     3155   2628   2998    274   -112    814       C  
ATOM   3050  CE  LYS A 404      64.416  61.311  50.371  1.00 37.36           C  
ANISOU 3050  CE  LYS A 404     4941   4478   4777    219   -173    881       C  
ATOM   3051  NZ  LYS A 404      65.481  62.090  49.676  1.00 39.06           N  
ANISOU 3051  NZ  LYS A 404     5199   4668   4974    195   -186    892       N  
ATOM   3052  N   ASN A 405      63.716  57.737  55.472  1.00 17.30           N  
ANISOU 3052  N   ASN A 405     2416   1848   2310    411     70    684       N  
ATOM   3053  CA  ASN A 405      62.383  57.321  55.884  1.00 20.45           C  
ANISOU 3053  CA  ASN A 405     2773   2264   2732    421     91    695       C  
ATOM   3054  C   ASN A 405      61.850  58.133  57.055  1.00 19.07           C  
ANISOU 3054  C   ASN A 405     2585   2051   2610    513    102    707       C  
ATOM   3055  O   ASN A 405      60.739  57.861  57.529  1.00 19.97           O  
ANISOU 3055  O   ASN A 405     2660   2173   2756    533    131    718       O  
ATOM   3056  CB  ASN A 405      62.349  55.816  56.183  1.00 16.50           C  
ANISOU 3056  CB  ASN A 405     2299   1765   2205    392    159    652       C  
ATOM   3057  CG  ASN A 405      63.233  55.403  57.356  1.00 17.77           C  
ANISOU 3057  CG  ASN A 405     2515   1876   2362    458    211    615       C  
ATOM   3058  OD1 ASN A 405      63.939  56.217  57.934  1.00 18.24           O  
ANISOU 3058  OD1 ASN A 405     2593   1908   2430    513    189    614       O  
ATOM   3059  ND2 ASN A 405      63.200  54.114  57.687  1.00 17.65           N  
ANISOU 3059  ND2 ASN A 405     2528   1851   2329    446    281    586       N  
ATOM   3060  N   LEU A 406      62.585  59.151  57.506  1.00 16.42           N  
ANISOU 3060  N   LEU A 406     2283   1671   2286    563     85    704       N  
ATOM   3061  CA  LEU A 406      62.082  60.084  58.503  1.00 18.93           C  
ANISOU 3061  CA  LEU A 406     2602   1941   2648    640    102    713       C  
ATOM   3062  C   LEU A 406      61.744  61.461  57.947  1.00 18.80           C  
ANISOU 3062  C   LEU A 406     2559   1910   2675    659     61    766       C  
ATOM   3063  O   LEU A 406      61.171  62.272  58.681  1.00 20.02           O  
ANISOU 3063  O   LEU A 406     2713   2016   2876    726     90    780       O  
ATOM   3064  CB  LEU A 406      63.099  60.246  59.647  1.00 16.22           C  
ANISOU 3064  CB  LEU A 406     2332   1549   2281    681    124    663       C  
ATOM   3065  CG  LEU A 406      63.348  59.001  60.473  1.00 17.04           C  
ANISOU 3065  CG  LEU A 406     2467   1657   2350    689    172    623       C  
ATOM   3066  CD1 LEU A 406      64.266  59.398  61.643  1.00 16.51           C  
ANISOU 3066  CD1 LEU A 406     2467   1551   2256    729    176    588       C  
ATOM   3067  CD2 LEU A 406      62.026  58.418  60.990  1.00 18.42           C  
ANISOU 3067  CD2 LEU A 406     2615   1833   2550    713    228    630       C  
ATOM   3068  N   ILE A 407      62.068  61.754  56.684  1.00 20.22           N  
ANISOU 3068  N   ILE A 407     2722   2123   2839    604      6    800       N  
ATOM   3069  CA  ILE A 407      61.929  63.096  56.139  1.00 19.66           C  
ANISOU 3069  CA  ILE A 407     2638   2030   2804    624    -31    857       C  
ATOM   3070  C   ILE A 407      61.123  63.031  54.843  1.00 21.37           C  
ANISOU 3070  C   ILE A 407     2783   2317   3020    577    -84    930       C  
ATOM   3071  O   ILE A 407      60.781  61.955  54.354  1.00 21.56           O  
ANISOU 3071  O   ILE A 407     2777   2405   3008    514    -94    923       O  
ATOM   3072  CB  ILE A 407      63.298  63.780  55.908  1.00 21.23           C  
ANISOU 3072  CB  ILE A 407     2899   2191   2977    603    -51    833       C  
ATOM   3073  CG1 ILE A 407      64.132  63.016  54.874  1.00 19.91           C  
ANISOU 3073  CG1 ILE A 407     2740   2075   2750    518    -79    819       C  
ATOM   3074  CG2 ILE A 407      64.090  63.870  57.225  1.00 17.81           C  
ANISOU 3074  CG2 ILE A 407     2529   1702   2536    639    -13    765       C  
ATOM   3075  CD1 ILE A 407      65.551  63.609  54.653  1.00 19.87           C  
ANISOU 3075  CD1 ILE A 407     2785   2037   2726    493    -91    795       C  
ATOM   3076  N   ALA A 408      60.827  64.209  54.292  1.00 22.75           N  
ANISOU 3076  N   ALA A 408     2936   2477   3232    603   -118   1002       N  
ATOM   3077  CA  ALA A 408      59.989  64.298  53.106  1.00 23.10           C  
ANISOU 3077  CA  ALA A 408     2907   2595   3276    566   -181   1089       C  
ATOM   3078  C   ALA A 408      60.654  63.613  51.911  1.00 28.32           C  
ANISOU 3078  C   ALA A 408     3593   3319   3849    455   -227   1075       C  
ATOM   3079  O   ALA A 408      61.882  63.606  51.789  1.00 25.18           O  
ANISOU 3079  O   ALA A 408     3267   2889   3410    425   -216   1024       O  
ATOM   3080  CB  ALA A 408      59.697  65.760  52.775  1.00 25.08           C  
ANISOU 3080  CB  ALA A 408     3142   2808   3579    623   -201   1168       C  
ATOM   3081  N   PRO A 409      59.860  63.034  51.007  1.00 30.92           N  
ANISOU 3081  N   PRO A 409     3864   3740   4145    385   -277   1120       N  
ATOM   3082  CA  PRO A 409      60.452  62.353  49.843  1.00 34.06           C  
ANISOU 3082  CA  PRO A 409     4301   4193   4447    268   -309   1100       C  
ATOM   3083  C   PRO A 409      61.383  63.230  49.021  1.00 28.61           C  
ANISOU 3083  C   PRO A 409     3666   3478   3726    250   -338   1126       C  
ATOM   3084  O   PRO A 409      62.390  62.730  48.506  1.00 33.45           O  
ANISOU 3084  O   PRO A 409     4347   4090   4274    179   -321   1073       O  
ATOM   3085  CB  PRO A 409      59.220  61.924  49.038  1.00 38.56           C  
ANISOU 3085  CB  PRO A 409     4789   4869   4993    201   -372   1165       C  
ATOM   3086  CG  PRO A 409      58.148  61.758  50.080  1.00 40.22           C  
ANISOU 3086  CG  PRO A 409     4921   5077   5284    272   -341   1174       C  
ATOM   3087  CD  PRO A 409      58.404  62.827  51.099  1.00 33.54           C  
ANISOU 3087  CD  PRO A 409     4092   4131   4521    401   -295   1179       C  
ATOM   3088  N   ASP A 410      61.103  64.526  48.907  1.00 29.13           N  
ANISOU 3088  N   ASP A 410     3710   3515   3843    314   -368   1207       N  
ATOM   3089  CA  ASP A 410      61.907  65.416  48.081  1.00 31.78           C  
ANISOU 3089  CA  ASP A 410     4101   3824   4152    294   -392   1242       C  
ATOM   3090  C   ASP A 410      63.002  66.143  48.851  1.00 27.92           C  
ANISOU 3090  C   ASP A 410     3678   3230   3702    349   -337   1189       C  
ATOM   3091  O   ASP A 410      63.678  66.995  48.274  1.00 28.36           O  
ANISOU 3091  O   ASP A 410     3779   3250   3748    338   -347   1217       O  
ATOM   3092  CB  ASP A 410      61.013  66.445  47.385  1.00 35.36           C  
ANISOU 3092  CB  ASP A 410     4498   4304   4632    327   -456   1373       C  
ATOM   3093  CG  ASP A 410      60.090  65.816  46.368  1.00 54.40           C  
ANISOU 3093  CG  ASP A 410     6847   6839   6982    245   -534   1437       C  
ATOM   3094  OD1 ASP A 410      60.475  64.784  45.779  1.00 60.24           O  
ANISOU 3094  OD1 ASP A 410     7626   7633   7629    134   -540   1378       O  
ATOM   3095  OD2 ASP A 410      58.983  66.355  46.154  1.00 60.06           O1-
ANISOU 3095  OD2 ASP A 410     7478   7600   7740    286   -579   1526       O1-
ATOM   3096  N   THR A 411      63.200  65.845  50.132  1.00 24.07           N  
ANISOU 3096  N   THR A 411     3199   2693   3253    401   -281   1115       N  
ATOM   3097  CA  THR A 411      64.259  66.517  50.876  1.00 23.92           C  
ANISOU 3097  CA  THR A 411     3243   2585   3259    436   -239   1063       C  
ATOM   3098  C   THR A 411      65.581  65.812  50.603  1.00 23.46           C  
ANISOU 3098  C   THR A 411     3233   2537   3142    363   -223    991       C  
ATOM   3099  O   THR A 411      65.701  64.609  50.851  1.00 23.96           O  
ANISOU 3099  O   THR A 411     3292   2636   3175    336   -202    938       O  
ATOM   3100  CB  THR A 411      63.934  66.534  52.368  1.00 24.65           C  
ANISOU 3100  CB  THR A 411     3334   2627   3406    515   -189   1018       C  
ATOM   3101  OG1 THR A 411      62.761  67.336  52.577  1.00 25.49           O  
ANISOU 3101  OG1 THR A 411     3398   2715   3572    581   -186   1070       O  
ATOM   3102  CG2 THR A 411      65.091  67.131  53.151  1.00 24.25           C  
ANISOU 3102  CG2 THR A 411     3352   2498   3363    528   -155    954       C  
ATOM   3103  N   ARG A 412      66.570  66.547  50.084  1.00 21.10           N  
ANISOU 3103  N   ARG A 412     3222   1901   2892    719    262    719       N  
ATOM   3104  CA AARG A 412      67.817  65.919  49.668  0.53 19.53           C  
ANISOU 3104  CA AARG A 412     3010   1740   2670    589    260    708       C  
ATOM   3105  CA BARG A 412      67.825  65.919  49.693  0.47 19.52           C  
ANISOU 3105  CA BARG A 412     3009   1738   2670    588    260    707       C  
ATOM   3106  C   ARG A 412      68.869  66.982  49.389  1.00 20.37           C  
ANISOU 3106  C   ARG A 412     3213   1702   2824    524    299    751       C  
ATOM   3107  O   ARG A 412      68.552  68.157  49.187  1.00 23.20           O  
ANISOU 3107  O   ARG A 412     3656   1942   3217    587    323    813       O  
ATOM   3108  CB AARG A 412      67.617  65.049  48.423  0.53 21.86           C  
ANISOU 3108  CB AARG A 412     3241   2179   2887    592    228    767       C  
ATOM   3109  CB BARG A 412      67.643  65.014  48.471  0.47 22.49           C  
ANISOU 3109  CB BARG A 412     3319   2260   2968    588    228    762       C  
ATOM   3110  CG AARG A 412      66.842  65.728  47.305  0.53 26.77           C  
ANISOU 3110  CG AARG A 412     3895   2801   3476    694    214    881       C  
ATOM   3111  CG BARG A 412      67.352  65.769  47.194  0.47 28.30           C  
ANISOU 3111  CG BARG A 412     4108   2975   3670    653    229    885       C  
ATOM   3112  CD AARG A 412      66.841  64.855  46.066  0.53 32.20           C  
ANISOU 3112  CD AARG A 412     4540   3624   4069    682    177    927       C  
ATOM   3113  CD BARG A 412      67.016  64.806  46.071  0.47 32.38           C  
ANISOU 3113  CD BARG A 412     4566   3646   4092    665    182    923       C  
ATOM   3114  NE AARG A 412      68.137  64.895  45.400  0.53 37.43           N  
ANISOU 3114  NE AARG A 412     5254   4259   4707    587    222    961       N  
ATOM   3115  NE BARG A 412      65.936  65.312  45.236  0.47 36.85           N  
ANISOU 3115  NE BARG A 412     5146   4236   4621    787    141   1015       N  
ATOM   3116  CZ AARG A 412      68.354  65.483  44.231  0.53 50.76           C  
ANISOU 3116  CZ AARG A 412     7015   5924   6347    608    244   1071       C  
ATOM   3117  CZ BARG A 412      66.119  65.907  44.064  0.47 46.82           C  
ANISOU 3117  CZ BARG A 412     6484   5475   5828    816    147   1125       C  
ATOM   3118  NH1 ARG A 412      67.350  66.072  43.585  1.00 54.28           N  
ANISOU 3118  NH1 ARG A 412     7494   6373   6757    726    208   1157       N  
ATOM   3119  NH2AARG A 412      69.572  65.477  43.707  0.53 53.91           N  
ANISOU 3119  NH2AARG A 412     7451   6300   6734    517    304   1100       N  
ATOM   3120  NH2BARG A 412      65.073  66.340  43.369  0.47 42.97           N  
ANISOU 3120  NH2BARG A 412     6007   5016   5305    938     95   1209       N  
ATOM   3121  N   PHE A 413      70.124  66.545  49.368  1.00 19.87           N  
ANISOU 3121  N   PHE A 413     3133   1646   2772    398    309    723       N  
ATOM   3122  CA  PHE A 413      71.191  67.378  48.829  1.00 20.75           C  
ANISOU 3122  CA  PHE A 413     3307   1646   2930    319    353    784       C  
ATOM   3123  C   PHE A 413      71.097  67.403  47.311  1.00 21.26           C  
ANISOU 3123  C   PHE A 413     3382   1765   2930    351    376    907       C  
ATOM   3124  O   PHE A 413      70.824  66.380  46.681  1.00 23.05           O  
ANISOU 3124  O   PHE A 413     3545   2141   3075    369    353    916       O  
ATOM   3125  CB  PHE A 413      72.564  66.843  49.237  1.00 20.20           C  
ANISOU 3125  CB  PHE A 413     3192   1582   2900    178    358    720       C  
ATOM   3126  CG  PHE A 413      72.904  67.087  50.671  1.00 20.12           C  
ANISOU 3126  CG  PHE A 413     3203   1486   2956    132    330    609       C  
ATOM   3127  CD1 PHE A 413      73.166  68.367  51.123  1.00 24.92           C  
ANISOU 3127  CD1 PHE A 413     3908   1916   3644    111    344    605       C  
ATOM   3128  CD2 PHE A 413      72.984  66.030  51.565  1.00 19.02           C  
ANISOU 3128  CD2 PHE A 413     2997   1436   2793    108    288    509       C  
ATOM   3129  CE1 PHE A 413      73.486  68.594  52.441  1.00 22.74           C  
ANISOU 3129  CE1 PHE A 413     3666   1560   3415     69    308    493       C  
ATOM   3130  CE2 PHE A 413      73.307  66.250  52.895  1.00 19.09           C  
ANISOU 3130  CE2 PHE A 413     3040   1370   2844     71    255    407       C  
ATOM   3131  CZ  PHE A 413      73.552  67.528  53.334  1.00 20.28           C  
ANISOU 3131  CZ  PHE A 413     3291   1350   3066     52    261    394       C  
ATOM   3132  N   LEU A 414      71.349  68.581  46.732  1.00 22.59           N  
ANISOU 3132  N   LEU A 414     3644   1806   3134    356    423   1003       N  
ATOM   3133  CA  LEU A 414      71.418  68.710  45.279  1.00 27.66           C  
ANISOU 3133  CA  LEU A 414     4319   2485   3707    380    457   1132       C  
ATOM   3134  C   LEU A 414      72.563  67.894  44.690  1.00 31.21           C  
ANISOU 3134  C   LEU A 414     4717   3016   4127    271    495   1136       C  
ATOM   3135  O   LEU A 414      72.434  67.327  43.596  1.00 28.71           O  
ANISOU 3135  O   LEU A 414     4392   2811   3706    303    501   1198       O  
ATOM   3136  CB  LEU A 414      71.573  70.181  44.906  1.00 28.93           C  
ANISOU 3136  CB  LEU A 414     4599   2468   3924    396    512   1235       C  
ATOM   3137  CG  LEU A 414      71.917  70.500  43.450  1.00 35.46           C  
ANISOU 3137  CG  LEU A 414     5460   3331   4684    385    547   1344       C  
ATOM   3138  CD1 LEU A 414      70.683  70.308  42.592  1.00 37.61           C  
ANISOU 3138  CD1 LEU A 414     5737   3714   4839    523    490   1402       C  
ATOM   3139  CD2 LEU A 414      72.474  71.915  43.282  1.00 33.65           C  
ANISOU 3139  CD2 LEU A 414     5309   2943   4534    334    591   1390       C  
ATOM   3140  N   ASP A 415      73.701  67.832  45.391  1.00 23.72           N  
ANISOU 3140  N   ASP A 415     3733   2013   3268    147    520   1071       N  
ATOM   3141  CA  ASP A 415      74.922  67.193  44.895  1.00 22.44           C  
ANISOU 3141  CA  ASP A 415     3513   1909   3106     42    572   1080       C  
ATOM   3142  C   ASP A 415      75.351  66.109  45.876  1.00 23.18           C  
ANISOU 3142  C   ASP A 415     3503   2080   3224    -20    525    950       C  
ATOM   3143  O   ASP A 415      76.343  66.276  46.599  1.00 24.48           O  
ANISOU 3143  O   ASP A 415     3635   2176   3490   -124    532    898       O  
ATOM   3144  CB  ASP A 415      76.036  68.216  44.714  1.00 24.94           C  
ANISOU 3144  CB  ASP A 415     3871   2077   3527    -59    652   1145       C  
ATOM   3145  CG  ASP A 415      75.666  69.302  43.739  1.00 31.09           C  
ANISOU 3145  CG  ASP A 415     4757   2779   4278     -1    697   1273       C  
ATOM   3146  OD1 ASP A 415      75.615  69.008  42.524  1.00 32.60           O  
ANISOU 3146  OD1 ASP A 415     4957   3068   4360     36    727   1348       O  
ATOM   3147  OD2 ASP A 415      75.420  70.446  44.183  1.00 34.64           O1-
ANISOU 3147  OD2 ASP A 415     5273   3092   4798      9    681   1271       O1-
ATOM   3148  N   PRO A 416      74.659  64.976  45.895  1.00 22.24           N  
ANISOU 3148  N   PRO A 416     3330   2102   3017     38    474    898       N  
ATOM   3149  CA  PRO A 416      74.903  63.955  46.918  1.00 24.24           C  
ANISOU 3149  CA  PRO A 416     3499   2421   3290     -4    426    778       C  
ATOM   3150  C   PRO A 416      76.080  63.049  46.574  1.00 24.30           C  
ANISOU 3150  C   PRO A 416     3431   2502   3300    -88    461    765       C  
ATOM   3151  O   PRO A 416      76.582  63.017  45.451  1.00 25.14           O  
ANISOU 3151  O   PRO A 416     3545   2636   3371   -102    528    845       O  
ATOM   3152  CB  PRO A 416      73.598  63.162  46.913  1.00 24.37           C  
ANISOU 3152  CB  PRO A 416     3494   2550   3216     95    368    749       C  
ATOM   3153  CG  PRO A 416      73.154  63.243  45.485  1.00 24.05           C  
ANISOU 3153  CG  PRO A 416     3492   2562   3084    155    389    851       C  
ATOM   3154  CD  PRO A 416      73.522  64.622  45.025  1.00 26.12           C  
ANISOU 3154  CD  PRO A 416     3840   2693   3392    148    447    948       C  
ATOM   3155  N   ASP A 417      76.496  62.289  47.585  1.00 20.10           N  
ANISOU 3155  N   ASP A 417     2829   2002   2806   -134    419    665       N  
ATOM   3156  CA  ASP A 417      77.537  61.274  47.469  1.00 22.94           C  
ANISOU 3156  CA  ASP A 417     3103   2438   3176   -198    439    636       C  
ATOM   3157  C   ASP A 417      77.012  60.003  48.122  1.00 21.85           C  
ANISOU 3157  C   ASP A 417     2917   2401   2986   -162    375    546       C  
ATOM   3158  O   ASP A 417      76.670  60.015  49.311  1.00 20.77           O  
ANISOU 3158  O   ASP A 417     2780   2234   2878   -157    317    474       O  
ATOM   3159  CB  ASP A 417      78.825  61.744  48.149  1.00 23.28           C  
ANISOU 3159  CB  ASP A 417     3103   2394   3347   -306    447    611       C  
ATOM   3160  CG  ASP A 417      79.993  60.803  47.920  1.00 32.97           C  
ANISOU 3160  CG  ASP A 417     4230   3697   4602   -366    480    598       C  
ATOM   3161  OD1 ASP A 417      79.854  59.825  47.151  1.00 28.65           O  
ANISOU 3161  OD1 ASP A 417     3661   3258   3967   -323    511    612       O  
ATOM   3162  OD2 ASP A 417      81.056  61.049  48.525  1.00 37.97           O1-
ANISOU 3162  OD2 ASP A 417     4803   4275   5347   -455    471    571       O1-
ATOM   3163  N   SER A 418      76.933  58.911  47.354  1.00 21.00           N  
ANISOU 3163  N   SER A 418     2777   2405   2798   -137    391    551       N  
ATOM   3164  CA  SER A 418      76.455  57.648  47.915  1.00 19.76           C  
ANISOU 3164  CA  SER A 418     2576   2334   2599   -110    337    471       C  
ATOM   3165  C   SER A 418      77.525  56.903  48.704  1.00 19.68           C  
ANISOU 3165  C   SER A 418     2493   2336   2649   -172    326    407       C  
ATOM   3166  O   SER A 418      77.186  56.006  49.485  1.00 19.91           O  
ANISOU 3166  O   SER A 418     2496   2408   2662   -156    276    338       O  
ATOM   3167  CB  SER A 418      75.923  56.733  46.803  1.00 23.22           C  
ANISOU 3167  CB  SER A 418     3017   2876   2929    -62    346    491       C  
ATOM   3168  OG  SER A 418      76.951  56.421  45.867  1.00 27.28           O  
ANISOU 3168  OG  SER A 418     3517   3420   3427    -94    418    527       O  
ATOM   3169  N   VAL A 419      78.805  57.230  48.504  1.00 18.23           N  
ANISOU 3169  N   VAL A 419     2271   2116   2538   -240    373    433       N  
ATOM   3170  CA  VAL A 419      79.861  56.644  49.325  1.00 19.89           C  
ANISOU 3170  CA  VAL A 419     2402   2333   2823   -296    349    376       C  
ATOM   3171  C   VAL A 419      79.735  57.178  50.751  1.00 19.18           C  
ANISOU 3171  C   VAL A 419     2329   2170   2788   -317    270    314       C  
ATOM   3172  O   VAL A 419      79.200  58.271  50.981  1.00 20.51           O  
ANISOU 3172  O   VAL A 419     2566   2257   2970   -310    258    328       O  
ATOM   3173  CB  VAL A 419      81.232  56.957  48.696  1.00 23.24           C  
ANISOU 3173  CB  VAL A 419     2766   2738   3327   -364    424    428       C  
ATOM   3174  CG1 VAL A 419      82.380  56.601  49.626  1.00 26.83           C  
ANISOU 3174  CG1 VAL A 419     3125   3185   3885   -427    384    375       C  
ATOM   3175  CG2 VAL A 419      81.362  56.204  47.387  1.00 25.39           C  
ANISOU 3175  CG2 VAL A 419     3030   3094   3522   -329    507    474       C  
ATOM   3176  N   ALA A 420      80.168  56.372  51.730  1.00 16.33           N  
ANISOU 3176  N   ALA A 420     1919   1838   2449   -332    213    244       N  
ATOM   3177  CA  ALA A 420      80.182  56.772  53.142  1.00 15.79           C  
ANISOU 3177  CA  ALA A 420     1876   1708   2418   -351    131    178       C  
ATOM   3178  C   ALA A 420      78.776  57.105  53.644  1.00 18.27           C  
ANISOU 3178  C   ALA A 420     2280   1999   2663   -283    108    156       C  
ATOM   3179  O   ALA A 420      78.525  58.172  54.211  1.00 17.58           O  
ANISOU 3179  O   ALA A 420     2257   1820   2601   -289     86    142       O  
ATOM   3180  CB  ALA A 420      81.148  57.940  53.375  1.00 18.78           C  
ANISOU 3180  CB  ALA A 420     2245   1985   2907   -436    120    186       C  
ATOM   3181  N   THR A 421      77.848  56.166  53.436  1.00 14.87           N  
ANISOU 3181  N   THR A 421     1850   1649   2151   -218    116    152       N  
ATOM   3182  CA  THR A 421      76.464  56.311  53.888  1.00 14.09           C  
ANISOU 3182  CA  THR A 421     1811   1547   1996   -149    104    137       C  
ATOM   3183  C   THR A 421      76.091  55.258  54.926  1.00 15.31           C  
ANISOU 3183  C   THR A 421     1958   1749   2111   -122     66     75       C  
ATOM   3184  O   THR A 421      74.899  55.050  55.182  1.00 15.66           O  
ANISOU 3184  O   THR A 421     2028   1816   2107    -63     71     69       O  
ATOM   3185  CB  THR A 421      75.488  56.270  52.707  1.00 16.50           C  
ANISOU 3185  CB  THR A 421     2124   1900   2247    -96    144    195       C  
ATOM   3186  OG1 THR A 421      75.869  55.242  51.773  1.00 16.99           O  
ANISOU 3186  OG1 THR A 421     2134   2045   2278   -106    168    213       O  
ATOM   3187  CG2 THR A 421      75.500  57.633  51.977  1.00 17.06           C  
ANISOU 3187  CG2 THR A 421     2241   1895   2345    -98    177    261       C  
ATOM   3188  N   ILE A 422      77.087  54.599  55.534  1.00 14.21           N  
ANISOU 3188  N   ILE A 422     1780   1623   1995   -162     31     37       N  
ATOM   3189  CA  ILE A 422      76.798  53.582  56.550  1.00 14.47           C  
ANISOU 3189  CA  ILE A 422     1818   1694   1986   -134     -3    -12       C  
ATOM   3190  C   ILE A 422      76.078  54.206  57.740  1.00 14.56           C  
ANISOU 3190  C   ILE A 422     1910   1652   1969   -100    -26    -51       C  
ATOM   3191  O   ILE A 422      76.463  55.276  58.236  1.00 16.06           O  
ANISOU 3191  O   ILE A 422     2149   1763   2192   -124    -54    -72       O  
ATOM   3192  CB  ILE A 422      78.105  52.918  57.018  1.00 13.53           C  
ANISOU 3192  CB  ILE A 422     1648   1590   1904   -177    -47    -39       C  
ATOM   3193  CG1 ILE A 422      78.850  52.277  55.846  1.00 16.14           C  
ANISOU 3193  CG1 ILE A 422     1898   1972   2263   -200     -7     -2       C  
ATOM   3194  CG2 ILE A 422      77.846  51.877  58.122  1.00 17.42           C  
ANISOU 3194  CG2 ILE A 422     2160   2113   2345   -143    -83    -81       C  
ATOM   3195  CD1 ILE A 422      78.107  51.093  55.196  1.00 15.35           C  
ANISOU 3195  CD1 ILE A 422     1786   1944   2103   -156     32      9       C  
ATOM   3196  N   THR A 423      75.044  53.520  58.231  1.00 13.04           N  
ANISOU 3196  N   THR A 423     1737   1498   1719    -45    -11    -62       N  
ATOM   3197  CA  THR A 423      74.405  53.949  59.474  1.00 13.09           C  
ANISOU 3197  CA  THR A 423     1824   1462   1687     -3    -19   -102       C  
ATOM   3198  C   THR A 423      75.400  53.832  60.633  1.00 14.51           C  
ANISOU 3198  C   THR A 423     2040   1613   1860    -32    -87   -157       C  
ATOM   3199  O   THR A 423      76.169  52.876  60.725  1.00 15.12           O  
ANISOU 3199  O   THR A 423     2070   1733   1941    -57   -119   -162       O  
ATOM   3200  CB  THR A 423      73.103  53.149  59.696  1.00 13.22           C  
ANISOU 3200  CB  THR A 423     1837   1533   1654     57     27    -91       C  
ATOM   3201  OG1 THR A 423      72.342  53.740  60.759  1.00 14.71           O  
ANISOU 3201  OG1 THR A 423     2105   1678   1806    111     46   -119       O  
ATOM   3202  CG2 THR A 423      73.352  51.669  60.000  1.00 13.98           C  
ANISOU 3202  CG2 THR A 423     1898   1689   1725     47     17    -99       C  
ATOM   3203  N   MET A 424      75.375  54.818  61.533  1.00 13.26           N  
ANISOU 3203  N   MET A 424     1971   1378   1688    -23   -114   -200       N  
ATOM   3204  CA AMET A 424      76.544  55.049  62.380  0.60 13.93           C  
ANISOU 3204  CA AMET A 424     2087   1421   1784    -71   -204   -254       C  
ATOM   3205  CA BMET A 424      76.495  55.079  62.438  0.40 14.77           C  
ANISOU 3205  CA BMET A 424     2200   1526   1887    -68   -203   -256       C  
ATOM   3206  C   MET A 424      76.888  53.852  63.263  1.00 17.41           C  
ANISOU 3206  C   MET A 424     2528   1917   2170    -57   -248   -277       C  
ATOM   3207  O   MET A 424      78.074  53.545  63.439  1.00 16.26           O  
ANISOU 3207  O   MET A 424     2340   1780   2059   -105   -324   -293       O  
ATOM   3208  CB AMET A 424      76.350  56.291  63.237  0.60 17.69           C  
ANISOU 3208  CB AMET A 424     2681   1799   2241    -59   -229   -308       C  
ATOM   3209  CB BMET A 424      76.098  56.234  63.349  0.40 18.50           C  
ANISOU 3209  CB BMET A 424     2797   1906   2326    -41   -217   -309       C  
ATOM   3210  CG AMET A 424      77.629  56.731  63.903  0.60 18.75           C  
ANISOU 3210  CG AMET A 424     2839   1879   2407   -128   -339   -366       C  
ATOM   3211  CG BMET A 424      77.056  57.355  63.430  0.40 26.76           C  
ANISOU 3211  CG BMET A 424     3871   2861   3438   -111   -286   -346       C  
ATOM   3212  SD AMET A 424      77.456  58.277  64.804  0.60 27.48           S  
ANISOU 3212  SD AMET A 424     4098   2848   3494   -124   -376   -443       S  
ATOM   3213  SD BMET A 424      78.483  56.686  64.224  0.40 37.26           S  
ANISOU 3213  SD BMET A 424     5168   4215   4773   -172   -410   -393       S  
ATOM   3214  CE AMET A 424      76.567  57.690  66.244  0.60 22.79           C  
ANISOU 3214  CE AMET A 424     3629   2282   2746    -23   -365   -493       C  
ATOM   3215  CE BMET A 424      77.707  56.046  65.707  0.40 17.35           C  
ANISOU 3215  CE BMET A 424     2769   1719   2103    -81   -418   -441       C  
ATOM   3216  N   TYR A 425      75.899  53.165  63.838  1.00 15.67           N  
ANISOU 3216  N   TYR A 425     2352   1731   1870      9   -201   -274       N  
ATOM   3217  CA  TYR A 425      76.279  52.061  64.717  1.00 15.70           C  
ANISOU 3217  CA  TYR A 425     2372   1776   1819     25   -242   -288       C  
ATOM   3218  C   TYR A 425      76.860  50.873  63.963  1.00 15.93           C  
ANISOU 3218  C   TYR A 425     2292   1871   1892     -1   -244   -248       C  
ATOM   3219  O   TYR A 425      77.437  49.981  64.596  1.00 19.15           O  
ANISOU 3219  O   TYR A 425     2702   2304   2271      7   -293   -255       O  
ATOM   3220  CB  TYR A 425      75.085  51.600  65.555  1.00 17.10           C  
ANISOU 3220  CB  TYR A 425     2627   1968   1902     99   -177   -286       C  
ATOM   3221  CG  TYR A 425      74.646  52.563  66.624  1.00 16.12           C  
ANISOU 3221  CG  TYR A 425     2636   1782   1708    142   -177   -336       C  
ATOM   3222  CD1 TYR A 425      75.538  53.429  67.235  1.00 22.74           C  
ANISOU 3222  CD1 TYR A 425     3544   2557   2539    111   -274   -399       C  
ATOM   3223  CD2 TYR A 425      73.322  52.601  67.018  1.00 21.68           C  
ANISOU 3223  CD2 TYR A 425     3394   2488   2355    213    -78   -324       C  
ATOM   3224  CE1 TYR A 425      75.110  54.308  68.231  1.00 27.33           C  
ANISOU 3224  CE1 TYR A 425     4267   3072   3044    156   -273   -456       C  
ATOM   3225  CE2 TYR A 425      72.889  53.462  67.998  1.00 22.62           C  
ANISOU 3225  CE2 TYR A 425     3644   2548   2403    265    -62   -372       C  
ATOM   3226  CZ  TYR A 425      73.776  54.314  68.599  1.00 24.00           C  
ANISOU 3226  CZ  TYR A 425     3906   2654   2557    239   -160   -442       C  
ATOM   3227  OH  TYR A 425      73.325  55.170  69.578  1.00 28.29           O  
ANISOU 3227  OH  TYR A 425     4599   3132   3019    296   -143   -500       O  
ATOM   3228  N   ALA A 426      76.712  50.828  62.640  1.00 14.10           N  
ANISOU 3228  N   ALA A 426     1976   1663   1720    -23   -192   -207       N  
ATOM   3229  CA  ALA A 426      77.265  49.767  61.819  1.00 13.24           C  
ANISOU 3229  CA  ALA A 426     1774   1609   1650    -42   -184   -177       C  
ATOM   3230  C   ALA A 426      78.648  50.108  61.295  1.00 13.47           C  
ANISOU 3230  C   ALA A 426     1730   1630   1759    -99   -232   -177       C  
ATOM   3231  O   ALA A 426      79.213  49.333  60.518  1.00 15.57           O  
ANISOU 3231  O   ALA A 426     1915   1936   2063   -112   -215   -152       O  
ATOM   3232  CB  ALA A 426      76.322  49.472  60.642  1.00 13.79           C  
ANISOU 3232  CB  ALA A 426     1800   1713   1726    -31   -103   -136       C  
ATOM   3233  N   ALA A 427      79.197  51.255  61.692  1.00 15.47           N  
ANISOU 3233  N   ALA A 427     2009   1826   2044   -136   -286   -206       N  
ATOM   3234  CA  ALA A 427      80.466  51.710  61.139  1.00 16.15           C  
ANISOU 3234  CA  ALA A 427     2012   1898   2227   -203   -322   -199       C  
ATOM   3235  C   ALA A 427      81.668  51.052  61.788  1.00 18.77           C  
ANISOU 3235  C   ALA A 427     2292   2251   2588   -218   -410   -219       C  
ATOM   3236  O   ALA A 427      82.756  51.087  61.199  1.00 21.74           O  
ANISOU 3236  O   ALA A 427     2564   2639   3059   -266   -424   -202       O  
ATOM   3237  CB  ALA A 427      80.604  53.225  61.293  1.00 20.33           C  
ANISOU 3237  CB  ALA A 427     2585   2343   2795   -248   -350   -222       C  
ATOM   3238  N   SER A 428      81.525  50.477  62.982  1.00 20.44           N  
ANISOU 3238  N   SER A 428     2571   2472   2725   -175   -469   -251       N  
ATOM   3239  CA  SER A 428      82.718  50.055  63.707  1.00 24.94           C  
ANISOU 3239  CA  SER A 428     3099   3055   3321   -187   -579   -272       C  
ATOM   3240  C   SER A 428      83.065  48.595  63.418  1.00 17.37           C  
ANISOU 3240  C   SER A 428     2069   2160   2369   -146   -558   -236       C  
ATOM   3241  O   SER A 428      82.207  47.778  63.068  1.00 16.63           O  
ANISOU 3241  O   SER A 428     1999   2094   2225   -101   -475   -209       O  
ATOM   3242  CB  SER A 428      82.558  50.272  65.218  1.00 30.65           C  
ANISOU 3242  CB  SER A 428     3945   3749   3951   -159   -673   -327       C  
ATOM   3243  OG  SER A 428      82.186  49.089  65.897  1.00 34.74           O  
ANISOU 3243  OG  SER A 428     4514   4306   4378    -88   -671   -314       O  
ATOM   3244  N   ASP A 429      84.355  48.280  63.547  1.00 21.08           N  
ANISOU 3244  N   ASP A 429     2444   2651   2913   -164   -637   -236       N  
ATOM   3245  CA  ASP A 429      84.788  46.904  63.329  1.00 22.24           C  
ANISOU 3245  CA  ASP A 429     2527   2849   3074   -115   -621   -203       C  
ATOM   3246  C   ASP A 429      84.366  45.972  64.456  1.00 20.40           C  
ANISOU 3246  C   ASP A 429     2392   2625   2735    -44   -663   -208       C  
ATOM   3247  O   ASP A 429      84.609  44.763  64.363  1.00 24.60           O  
ANISOU 3247  O   ASP A 429     2891   3186   3269      6   -647   -178       O  
ATOM   3248  CB  ASP A 429      86.302  46.849  63.138  1.00 27.08           C  
ANISOU 3248  CB  ASP A 429     2996   3484   3809   -145   -688   -195       C  
ATOM   3249  N   ASP A 430      83.705  46.483  65.492  1.00 19.67           N  
ANISOU 3249  N   ASP A 430     2427   2501   2545    -32   -703   -241       N  
ATOM   3250  CA  ASP A 430      83.178  45.625  66.541  1.00 19.98           C  
ANISOU 3250  CA  ASP A 430     2576   2546   2469     39   -719   -235       C  
ATOM   3251  C   ASP A 430      81.815  45.028  66.205  1.00 21.35           C  
ANISOU 3251  C   ASP A 430     2808   2722   2582     73   -586   -205       C  
ATOM   3252  O   ASP A 430      81.278  44.268  67.017  1.00 22.73           O  
ANISOU 3252  O   ASP A 430     3072   2896   2666    128   -575   -189       O  
ATOM   3253  CB  ASP A 430      83.090  46.408  67.846  1.00 22.22           C  
ANISOU 3253  CB  ASP A 430     2984   2798   2662     45   -814   -285       C  
ATOM   3254  CG  ASP A 430      84.463  46.745  68.417  1.00 41.55           C  
ANISOU 3254  CG  ASP A 430     5382   5247   5157     17   -978   -319       C  
ATOM   3255  OD1 ASP A 430      85.443  46.058  68.060  1.00 42.97           O  
ANISOU 3255  OD1 ASP A 430     5440   5463   5423     21  -1018   -290       O  
ATOM   3256  OD2 ASP A 430      84.554  47.690  69.227  1.00 51.34           O  
ANISOU 3256  OD2 ASP A 430     6705   6451   6350     -5  -1069   -376       O  
ATOM   3257  N   VAL A 431      81.250  45.353  65.041  1.00 14.65           N  
ANISOU 3257  N   VAL A 431     1909   1875   1782     40   -490   -193       N  
ATOM   3258  CA  VAL A 431      79.948  44.877  64.595  1.00 15.44           C  
ANISOU 3258  CA  VAL A 431     2043   1980   1844     60   -377   -168       C  
ATOM   3259  C   VAL A 431      80.148  44.158  63.270  1.00 14.77           C  
ANISOU 3259  C   VAL A 431     1860   1922   1830     47   -316   -140       C  
ATOM   3260  O   VAL A 431      81.045  44.509  62.497  1.00 17.46           O  
ANISOU 3260  O   VAL A 431     2111   2273   2250     14   -331   -141       O  
ATOM   3261  CB  VAL A 431      78.964  46.069  64.440  1.00 16.92           C  
ANISOU 3261  CB  VAL A 431     2275   2143   2010     41   -329   -184       C  
ATOM   3262  CG1 VAL A 431      77.682  45.684  63.713  1.00 25.77           C  
ANISOU 3262  CG1 VAL A 431     3391   3278   3121     52   -221   -156       C  
ATOM   3263  CG2 VAL A 431      78.658  46.687  65.824  1.00 17.39           C  
ANISOU 3263  CG2 VAL A 431     2457   2170   1980     69   -374   -218       C  
ATOM   3264  N   ILE A 432      79.330  43.146  63.006  1.00 12.39           N  
ANISOU 3264  N   ILE A 432     1577   1628   1502     72   -245   -117       N  
ATOM   3265  CA  ILE A 432      79.246  42.556  61.668  1.00 11.71           C  
ANISOU 3265  CA  ILE A 432     1423   1561   1465     58   -179   -102       C  
ATOM   3266  C   ILE A 432      78.206  43.347  60.895  1.00 12.94           C  
ANISOU 3266  C   ILE A 432     1580   1721   1615     29   -121   -103       C  
ATOM   3267  O   ILE A 432      77.028  43.336  61.251  1.00 14.04           O  
ANISOU 3267  O   ILE A 432     1772   1854   1710     40    -84    -99       O  
ATOM   3268  CB  ILE A 432      78.873  41.068  61.729  1.00 12.42           C  
ANISOU 3268  CB  ILE A 432     1536   1646   1536     91   -142    -84       C  
ATOM   3269  CG1 ILE A 432      79.968  40.279  62.467  1.00 14.00           C  
ANISOU 3269  CG1 ILE A 432     1735   1839   1744    132   -204    -74       C  
ATOM   3270  CG2 ILE A 432      78.600  40.505  60.302  1.00 13.84           C  
ANISOU 3270  CG2 ILE A 432     1667   1839   1753     73    -75    -83       C  
ATOM   3271  CD1 ILE A 432      79.618  38.809  62.745  1.00 15.94           C  
ANISOU 3271  CD1 ILE A 432     2027   2062   1969    172   -169    -49       C  
ATOM   3272  N   THR A 433      78.630  44.014  59.825  1.00 11.07           N  
ANISOU 3272  N   THR A 433     1284   1497   1427     -2   -108   -103       N  
ATOM   3273  CA  THR A 433      77.769  44.917  59.062  1.00  9.99           C  
ANISOU 3273  CA  THR A 433     1149   1362   1285    -23    -66    -97       C  
ATOM   3274  C   THR A 433      77.388  44.279  57.732  1.00 11.26           C  
ANISOU 3274  C   THR A 433     1276   1551   1451    -28    -10    -85       C  
ATOM   3275  O   THR A 433      78.264  43.802  57.010  1.00 12.13           O  
ANISOU 3275  O   THR A 433     1340   1677   1593    -31      1    -83       O  
ATOM   3276  CB  THR A 433      78.508  46.239  58.826  1.00 13.31           C  
ANISOU 3276  CB  THR A 433     1544   1765   1749    -57    -92    -99       C  
ATOM   3277  OG1 THR A 433      78.746  46.839  60.110  1.00 14.56           O  
ANISOU 3277  OG1 THR A 433     1751   1889   1892    -55   -155   -123       O  
ATOM   3278  CG2 THR A 433      77.681  47.192  57.974  1.00 13.61           C  
ANISOU 3278  CG2 THR A 433     1591   1799   1782    -69    -48    -82       C  
ATOM   3279  N   VAL A 434      76.092  44.280  57.419  1.00 10.40           N  
ANISOU 3279  N   VAL A 434     1189   1452   1312    -25     23    -79       N  
ATOM   3280  CA  VAL A 434      75.548  43.519  56.292  1.00  9.56           C  
ANISOU 3280  CA  VAL A 434     1064   1371   1197    -31     58    -77       C  
ATOM   3281  C   VAL A 434      74.826  44.461  55.340  1.00 10.36           C  
ANISOU 3281  C   VAL A 434     1158   1491   1288    -40     73    -62       C  
ATOM   3282  O   VAL A 434      73.861  45.122  55.729  1.00 12.72           O  
ANISOU 3282  O   VAL A 434     1473   1784   1576    -32     73    -53       O  
ATOM   3283  CB  VAL A 434      74.579  42.429  56.781  1.00 11.89           C  
ANISOU 3283  CB  VAL A 434     1383   1661   1475    -23     71    -82       C  
ATOM   3284  CG1 VAL A 434      74.124  41.547  55.630  1.00 12.93           C  
ANISOU 3284  CG1 VAL A 434     1499   1811   1604    -38     91    -93       C  
ATOM   3285  CG2 VAL A 434      75.222  41.597  57.899  1.00 13.40           C  
ANISOU 3285  CG2 VAL A 434     1599   1825   1667     -4     55    -85       C  
ATOM   3286  N   GLY A 435      75.250  44.466  54.074  1.00 10.72           N  
ANISOU 3286  N   GLY A 435     1183   1559   1331    -50     91    -56       N  
ATOM   3287  CA  GLY A 435      74.517  45.162  53.032  1.00 13.85           C  
ANISOU 3287  CA  GLY A 435     1582   1977   1702    -51    101    -36       C  
ATOM   3288  C   GLY A 435      73.531  44.241  52.339  1.00 14.07           C  
ANISOU 3288  C   GLY A 435     1612   2035   1698    -52     99    -51       C  
ATOM   3289  O   GLY A 435      73.419  43.062  52.651  1.00 12.85           O  
ANISOU 3289  O   GLY A 435     1460   1874   1547    -57     98    -78       O  
ATOM   3290  N   THR A 436      72.804  44.793  51.363  1.00 11.87           N  
ANISOU 3290  N   THR A 436     1336   1784   1389    -48     92    -34       N  
ATOM   3291  CA  THR A 436      71.680  44.082  50.752  1.00 11.15           C  
ANISOU 3291  CA  THR A 436     1241   1724   1272    -54     67    -50       C  
ATOM   3292  C   THR A 436      71.954  43.776  49.289  1.00 13.54           C  
ANISOU 3292  C   THR A 436     1567   2058   1518    -55     66    -60       C  
ATOM   3293  O   THR A 436      72.087  44.692  48.472  1.00 14.20           O  
ANISOU 3293  O   THR A 436     1668   2160   1568    -39     71    -27       O  
ATOM   3294  CB  THR A 436      70.386  44.883  50.868  1.00 11.64           C  
ANISOU 3294  CB  THR A 436     1280   1801   1340    -39     43    -23       C  
ATOM   3295  OG1 THR A 436      70.026  45.009  52.252  1.00 12.72           O  
ANISOU 3295  OG1 THR A 436     1405   1910   1520    -33     56    -20       O  
ATOM   3296  CG2 THR A 436      69.232  44.154  50.133  1.00 14.09           C  
ANISOU 3296  CG2 THR A 436     1568   2150   1634    -54      1    -41       C  
ATOM   3297  N   PHE A 437      72.012  42.487  48.973  1.00 11.65           N  
ANISOU 3297  N   PHE A 437     1342   1818   1265    -69     63   -105       N  
ATOM   3298  CA  PHE A 437      72.053  41.988  47.604  1.00 11.56           C  
ANISOU 3298  CA  PHE A 437     1372   1836   1186    -68     55   -132       C  
ATOM   3299  C   PHE A 437      70.634  41.771  47.088  1.00 13.05           C  
ANISOU 3299  C   PHE A 437     1554   2054   1350    -85    -14   -148       C  
ATOM   3300  O   PHE A 437      69.727  41.368  47.824  1.00 13.99           O  
ANISOU 3300  O   PHE A 437     1631   2162   1521   -109    -42   -157       O  
ATOM   3301  CB  PHE A 437      72.838  40.672  47.559  1.00 13.26           C  
ANISOU 3301  CB  PHE A 437     1613   2023   1403    -72     84   -181       C  
ATOM   3302  CG  PHE A 437      73.264  40.272  46.187  1.00 13.84           C  
ANISOU 3302  CG  PHE A 437     1745   2117   1397    -57    102   -210       C  
ATOM   3303  CD1 PHE A 437      72.647  39.222  45.528  1.00 18.23           C  
ANISOU 3303  CD1 PHE A 437     2344   2671   1911    -74     63   -271       C  
ATOM   3304  CD2 PHE A 437      74.279  40.962  45.544  1.00 13.93           C  
ANISOU 3304  CD2 PHE A 437     1773   2146   1375    -27    161   -178       C  
ATOM   3305  CE1 PHE A 437      73.052  38.869  44.240  1.00 18.32           C  
ANISOU 3305  CE1 PHE A 437     2430   2700   1831    -52     81   -305       C  
ATOM   3306  CE2 PHE A 437      74.688  40.613  44.251  1.00 18.39           C  
ANISOU 3306  CE2 PHE A 437     2404   2732   1851     -4    193   -201       C  
ATOM   3307  CZ  PHE A 437      74.067  39.568  43.612  1.00 18.47           C  
ANISOU 3307  CZ  PHE A 437     2471   2742   1804    -12    152   -268       C  
ATOM   3308  N   ASN A 438      70.443  42.031  45.789  1.00 12.83           N  
ANISOU 3308  N   ASN A 438     1566   2067   1241    -72    -41   -148       N  
ATOM   3309  CA  ASN A 438      69.147  41.880  45.137  1.00 16.28           C  
ANISOU 3309  CA  ASN A 438     1995   2543   1648    -85   -126   -164       C  
ATOM   3310  C   ASN A 438      69.233  40.683  44.192  1.00 16.62           C  
ANISOU 3310  C   ASN A 438     2100   2587   1626   -105   -153   -236       C  
ATOM   3311  O   ASN A 438      69.806  40.777  43.101  1.00 15.18           O  
ANISOU 3311  O   ASN A 438     1993   2427   1347    -78   -139   -243       O  
ATOM   3312  CB  ASN A 438      68.760  43.168  44.406  1.00 14.09           C  
ANISOU 3312  CB  ASN A 438     1726   2309   1318    -47   -155   -105       C  
ATOM   3313  CG  ASN A 438      67.363  43.107  43.797  1.00 14.61           C  
ANISOU 3313  CG  ASN A 438     1766   2423   1362    -54   -260   -114       C  
ATOM   3314  OD1 ASN A 438      66.795  42.028  43.609  1.00 18.51           O  
ANISOU 3314  OD1 ASN A 438     2252   2920   1860    -96   -317   -176       O  
ATOM   3315  ND2 ASN A 438      66.812  44.269  43.460  1.00 18.00           N  
ANISOU 3315  ND2 ASN A 438     2182   2886   1772    -13   -293    -52       N  
ATOM   3316  N   ASN A 439      68.653  39.552  44.607  1.00 14.52           N  
ANISOU 3316  N   ASN A 439     1813   2293   1411   -152   -187   -290       N  
ATOM   3317  CA  ASN A 439      68.706  38.360  43.761  1.00 17.90           C  
ANISOU 3317  CA  ASN A 439     2311   2706   1784   -175   -217   -370       C  
ATOM   3318  C   ASN A 439      67.944  38.529  42.457  1.00 21.19           C  
ANISOU 3318  C   ASN A 439     2768   3179   2105   -176   -312   -393       C  
ATOM   3319  O   ASN A 439      68.243  37.830  41.484  1.00 23.32           O  
ANISOU 3319  O   ASN A 439     3131   3446   2286   -174   -328   -458       O  
ATOM   3320  CB  ASN A 439      68.154  37.144  44.505  1.00 23.31           C  
ANISOU 3320  CB  ASN A 439     2964   3335   2557   -235   -237   -418       C  
ATOM   3321  CG  ASN A 439      69.210  36.427  45.320  1.00 28.88           C  
ANISOU 3321  CG  ASN A 439     3691   3973   3308   -225   -150   -427       C  
ATOM   3322  OD1 ASN A 439      70.406  36.465  45.004  1.00 29.78           O  
ANISOU 3322  OD1 ASN A 439     3857   4079   3377   -179    -85   -428       O  
ATOM   3323  ND2 ASN A 439      68.771  35.744  46.366  1.00 29.24           N  
ANISOU 3323  ND2 ASN A 439     3694   3969   3448   -266   -144   -429       N  
ATOM   3324  N   LYS A 440      66.978  39.444  42.405  1.00 16.17           N  
ANISOU 3324  N   LYS A 440     2070   2594   1480   -170   -378   -344       N  
ATOM   3325  CA  LYS A 440      66.203  39.629  41.185  1.00 19.92           C  
ANISOU 3325  CA  LYS A 440     2579   3129   1862   -165   -487   -360       C  
ATOM   3326  C   LYS A 440      67.014  40.300  40.088  1.00 19.72           C  
ANISOU 3326  C   LYS A 440     2659   3137   1694   -101   -454   -334       C  
ATOM   3327  O   LYS A 440      66.793  40.026  38.900  1.00 20.79           O  
ANISOU 3327  O   LYS A 440     2881   3308   1710    -92   -524   -376       O  
ATOM   3328  CB  LYS A 440      64.957  40.455  41.469  1.00 23.74           C  
ANISOU 3328  CB  LYS A 440     2956   3659   2406   -163   -565   -304       C  
ATOM   3329  CG  LYS A 440      63.932  39.746  42.326  1.00 29.19           C  
ANISOU 3329  CG  LYS A 440     3535   4328   3227   -231   -608   -330       C  
ATOM   3330  CD  LYS A 440      62.895  40.755  42.815  1.00 36.40           C  
ANISOU 3330  CD  LYS A 440     4329   5284   4217   -207   -642   -257       C  
ATOM   3331  CE  LYS A 440      61.766  40.078  43.569  1.00 41.80           C  
ANISOU 3331  CE  LYS A 440     4890   5958   5035   -274   -680   -275       C  
ATOM   3332  NZ  LYS A 440      60.661  41.028  43.874  1.00 41.48           N  
ANISOU 3332  NZ  LYS A 440     4726   5968   5065   -242   -718   -206       N  
ATOM   3333  N   THR A 441      67.923  41.199  40.454  1.00 18.35           N  
ANISOU 3333  N   THR A 441     2487   2954   1531    -57   -350   -263       N  
ATOM   3334  CA  THR A 441      68.771  41.876  39.474  1.00 20.40           C  
ANISOU 3334  CA  THR A 441     2841   3239   1672     -1   -293   -224       C  
ATOM   3335  C   THR A 441      70.186  41.333  39.454  1.00 20.08           C  
ANISOU 3335  C   THR A 441     2857   3159   1614     10   -172   -249       C  
ATOM   3336  O   THR A 441      71.009  41.826  38.676  1.00 19.08           O  
ANISOU 3336  O   THR A 441     2803   3048   1398     55    -99   -214       O  
ATOM   3337  CB  THR A 441      68.838  43.372  39.771  1.00 18.60           C  
ANISOU 3337  CB  THR A 441     2574   3021   1471     37   -258   -118       C  
ATOM   3338  OG1 THR A 441      69.471  43.555  41.041  1.00 18.15           O  
ANISOU 3338  OG1 THR A 441     2449   2913   1536     22   -174    -97       O  
ATOM   3339  CG2 THR A 441      67.445  43.984  39.807  1.00 19.97           C  
ANISOU 3339  CG2 THR A 441     2684   3232   1670     43   -370    -84       C  
ATOM   3340  N   ASP A 442      70.501  40.380  40.335  1.00 19.40           N  
ANISOU 3340  N   ASP A 442     2732   3019   1620    -24   -140   -299       N  
ATOM   3341  CA  ASP A 442      71.849  39.825  40.470  1.00 19.66           C  
ANISOU 3341  CA  ASP A 442     2797   3012   1662     -6    -27   -320       C  
ATOM   3342  C   ASP A 442      72.870  40.927  40.731  1.00 19.53           C  
ANISOU 3342  C   ASP A 442     2750   2997   1672     27     73   -235       C  
ATOM   3343  O   ASP A 442      73.996  40.901  40.219  1.00 21.05           O  
ANISOU 3343  O   ASP A 442     2987   3188   1823     61    170   -227       O  
ATOM   3344  CB  ASP A 442      72.249  38.995  39.251  1.00 22.20           C  
ANISOU 3344  CB  ASP A 442     3239   3338   1858     19     -9   -389       C  
ATOM   3345  CG  ASP A 442      73.470  38.136  39.522  1.00 27.28           C  
ANISOU 3345  CG  ASP A 442     3899   3929   2535     39     99   -425       C  
ATOM   3346  OD1 ASP A 442      73.583  37.646  40.668  0.70 25.41           O  
ANISOU 3346  OD1 ASP A 442     3590   3644   2419     13    107   -434       O  
ATOM   3347  OD2 ASP A 442      74.294  37.939  38.592  0.70 28.98           O1-
ANISOU 3347  OD2 ASP A 442     4202   4154   2655     87    177   -443       O1-
ATOM   3348  N   SER A 443      72.478  41.903  41.540  1.00 16.64           N  
ANISOU 3348  N   SER A 443     2309   2632   1384     16     52   -172       N  
ATOM   3349  CA  SER A 443      73.364  43.019  41.855  1.00 18.06           C  
ANISOU 3349  CA  SER A 443     2458   2802   1602     34    132    -95       C  
ATOM   3350  C   SER A 443      72.951  43.601  43.193  1.00 17.77           C  
ANISOU 3350  C   SER A 443     2336   2738   1680     11    105    -65       C  
ATOM   3351  O   SER A 443      71.942  43.211  43.774  1.00 14.52           O  
ANISOU 3351  O   SER A 443     1887   2324   1307    -11     36    -93       O  
ATOM   3352  CB  SER A 443      73.318  44.100  40.782  1.00 25.28           C  
ANISOU 3352  CB  SER A 443     3430   3754   2423     67    144    -30       C  
ATOM   3353  OG  SER A 443      72.070  44.754  40.810  1.00 28.43           O  
ANISOU 3353  OG  SER A 443     3811   4174   2816     68     50     -1       O  
ATOM   3354  N   MET A 444      73.750  44.545  43.683  1.00 16.40           N  
ANISOU 3354  N   MET A 444     2130   2540   1560     15    164     -9       N  
ATOM   3355  CA  MET A 444      73.414  45.182  44.949  1.00 13.77           C  
ANISOU 3355  CA  MET A 444     1735   2177   1321      0    141     14       C  
ATOM   3356  C   MET A 444      72.096  45.938  44.849  1.00 13.79           C  
ANISOU 3356  C   MET A 444     1733   2199   1308     12     73     45       C  
ATOM   3357  O   MET A 444      71.783  46.545  43.821  1.00 16.83           O  
ANISOU 3357  O   MET A 444     2161   2614   1620     38     59     83       O  
ATOM   3358  CB  MET A 444      74.518  46.148  45.374  1.00 18.31           C  
ANISOU 3358  CB  MET A 444     2288   2718   1952     -4    204     64       C  
ATOM   3359  CG  MET A 444      75.794  45.445  45.824  1.00 19.39           C  
ANISOU 3359  CG  MET A 444     2394   2833   2140    -15    258     37       C  
ATOM   3360  SD  MET A 444      75.514  44.404  47.261  1.00 17.28           S  
ANISOU 3360  SD  MET A 444     2086   2538   1940    -30    213    -20       S  
ATOM   3361  CE  MET A 444      75.023  45.639  48.476  1.00 17.29           C  
ANISOU 3361  CE  MET A 444     2057   2508   2003    -41    178     15       C  
ATOM   3362  N   TRP A 445      71.319  45.902  45.930  1.00 14.49           N  
ANISOU 3362  N   TRP A 445     1770   2272   1465      1     36     33       N  
ATOM   3363  CA  TRP A 445      70.135  46.741  46.010  1.00 14.23           C  
ANISOU 3363  CA  TRP A 445     1714   2251   1440     23    -14     70       C  
ATOM   3364  C   TRP A 445      70.539  48.207  45.954  1.00 16.90           C  
ANISOU 3364  C   TRP A 445     2074   2563   1786     49     21    138       C  
ATOM   3365  O   TRP A 445      71.512  48.622  46.591  1.00 17.25           O  
ANISOU 3365  O   TRP A 445     2115   2560   1877     35     73    148       O  
ATOM   3366  CB  TRP A 445      69.380  46.449  47.318  1.00 14.69           C  
ANISOU 3366  CB  TRP A 445     1712   2291   1579     10    -32     49       C  
ATOM   3367  CG  TRP A 445      68.208  47.350  47.574  1.00 15.58           C  
ANISOU 3367  CG  TRP A 445     1788   2412   1718     43    -65     88       C  
ATOM   3368  CD1 TRP A 445      67.183  47.629  46.711  1.00 18.27           C  
ANISOU 3368  CD1 TRP A 445     2117   2800   2026     69   -127    111       C  
ATOM   3369  CD2 TRP A 445      67.922  48.084  48.784  1.00 14.86           C  
ANISOU 3369  CD2 TRP A 445     1672   2282   1694     62    -39    107       C  
ATOM   3370  NE1 TRP A 445      66.280  48.481  47.300  1.00 17.53           N  
ANISOU 3370  NE1 TRP A 445     1977   2698   1984    108   -136    148       N  
ATOM   3371  CE2 TRP A 445      66.712  48.777  48.571  1.00 14.78           C  
ANISOU 3371  CE2 TRP A 445     1627   2295   1694    105    -76    144       C  
ATOM   3372  CE3 TRP A 445      68.566  48.209  50.031  1.00 14.67           C  
ANISOU 3372  CE3 TRP A 445     1653   2206   1714     53      8     94       C  
ATOM   3373  CZ2 TRP A 445      66.135  49.598  49.543  1.00 18.20           C  
ANISOU 3373  CZ2 TRP A 445     2035   2696   2183    143    -52    167       C  
ATOM   3374  CZ3 TRP A 445      67.993  49.032  50.997  1.00 16.54           C  
ANISOU 3374  CZ3 TRP A 445     1879   2412   1994     85     23    112       C  
ATOM   3375  CH2 TRP A 445      66.784  49.703  50.754  1.00 18.16           C  
ANISOU 3375  CH2 TRP A 445     2052   2637   2211    132      1    147       C  
ATOM   3376  N   ILE A 446      69.793  48.996  45.168  1.00 15.93           N  
ANISOU 3376  N   ILE A 446     1971   2464   1618     87    -15    187       N  
ATOM   3377  CA  ILE A 446      70.150  50.397  44.962  1.00 19.73           C  
ANISOU 3377  CA  ILE A 446     2486   2908   2101    114     21    259       C  
ATOM   3378  C   ILE A 446      70.137  51.199  46.255  1.00 17.84           C  
ANISOU 3378  C   ILE A 446     2218   2605   1955    115     41    269       C  
ATOM   3379  O   ILE A 446      70.836  52.214  46.359  1.00 19.29           O  
ANISOU 3379  O   ILE A 446     2432   2733   2165    114     86    311       O  
ATOM   3380  CB  ILE A 446      69.218  51.018  43.899  1.00 19.44           C  
ANISOU 3380  CB  ILE A 446     2482   2910   1995    167    -33    314       C  
ATOM   3381  CG1 ILE A 446      67.752  50.802  44.295  1.00 21.68           C  
ANISOU 3381  CG1 ILE A 446     2700   3227   2312    189   -114    296       C  
ATOM   3382  CG2 ILE A 446      69.491  50.376  42.543  1.00 23.65           C  
ANISOU 3382  CG2 ILE A 446     3076   3499   2413    168    -44    306       C  
ATOM   3383  CD1 ILE A 446      66.762  51.418  43.323  1.00 31.04           C  
ANISOU 3383  CD1 ILE A 446     3900   4455   3440    249   -186    352       C  
ATOM   3384  N   GLY A 447      69.377  50.760  47.258  1.00 16.73           N  
ANISOU 3384  N   GLY A 447     2026   2466   1864    114     14    230       N  
ATOM   3385  CA  GLY A 447      69.310  51.471  48.518  1.00 15.29           C  
ANISOU 3385  CA  GLY A 447     1832   2224   1753    124     36    230       C  
ATOM   3386  C   GLY A 447      70.373  51.113  49.530  1.00 15.86           C  
ANISOU 3386  C   GLY A 447     1905   2256   1866     80     70    189       C  
ATOM   3387  O   GLY A 447      70.425  51.743  50.591  1.00 15.05           O  
ANISOU 3387  O   GLY A 447     1809   2099   1809     86     83    183       O  
ATOM   3388  N   SER A 448      71.223  50.125  49.248  1.00 13.15           N  
ANISOU 3388  N   SER A 448     1557   1935   1505     42     82    158       N  
ATOM   3389  CA  SER A 448      72.159  49.641  50.262  1.00 12.00           C  
ANISOU 3389  CA  SER A 448     1401   1759   1401     10    101    119       C  
ATOM   3390  C   SER A 448      73.280  50.656  50.496  1.00 13.14           C  
ANISOU 3390  C   SER A 448     1562   1846   1584    -10    128    141       C  
ATOM   3391  O   SER A 448      73.954  51.078  49.548  1.00 15.50           O  
ANISOU 3391  O   SER A 448     1874   2144   1870    -21    159    177       O  
ATOM   3392  CB  SER A 448      72.730  48.287  49.825  1.00 14.21           C  
ANISOU 3392  CB  SER A 448     1668   2074   1657    -13    107     83       C  
ATOM   3393  OG  SER A 448      73.457  47.661  50.892  1.00 15.04           O  
ANISOU 3393  OG  SER A 448     1757   2155   1803    -33    113     48       O  
ATOM   3394  N   SER A 449      73.474  51.046  51.765  1.00 12.47           N  
ANISOU 3394  N   SER A 449     1481   1711   1544    -17    119    118       N  
ATOM   3395  CA  SER A 449      74.497  52.028  52.113  1.00 12.68           C  
ANISOU 3395  CA  SER A 449     1522   1675   1620    -46    128    129       C  
ATOM   3396  C   SER A 449      75.890  51.494  51.799  1.00 13.99           C  
ANISOU 3396  C   SER A 449     1651   1852   1811    -89    147    124       C  
ATOM   3397  O   SER A 449      76.143  50.288  51.864  1.00 15.88           O  
ANISOU 3397  O   SER A 449     1863   2134   2038    -90    144     93       O  
ATOM   3398  CB  SER A 449      74.416  52.376  53.608  1.00 14.35           C  
ANISOU 3398  CB  SER A 449     1756   1835   1860    -44    100     89       C  
ATOM   3399  OG  SER A 449      73.372  53.296  53.860  1.00 14.07           O  
ANISOU 3399  OG  SER A 449     1760   1765   1819     -2    101    103       O  
ATOM   3400  N   LYS A 450      76.805  52.408  51.478  1.00 13.76           N  
ANISOU 3400  N   LYS A 450     1620   1781   1828   -124    171    156       N  
ATOM   3401  CA  LYS A 450      78.163  52.060  51.088  1.00 13.77           C  
ANISOU 3401  CA  LYS A 450     1569   1793   1870   -164    203    163       C  
ATOM   3402  C   LYS A 450      79.162  52.566  52.115  1.00 14.36           C  
ANISOU 3402  C   LYS A 450     1614   1812   2031   -212    170    141       C  
ATOM   3403  O   LYS A 450      78.968  53.614  52.734  1.00 16.29           O  
ANISOU 3403  O   LYS A 450     1896   1989   2305   -227    141    137       O  
ATOM   3404  CB  LYS A 450      78.527  52.658  49.719  1.00 16.95           C  
ANISOU 3404  CB  LYS A 450     1980   2198   2263   -173    272    231       C  
ATOM   3405  CG  LYS A 450      77.646  52.188  48.585  1.00 20.21           C  
ANISOU 3405  CG  LYS A 450     2430   2670   2578   -125    294    253       C  
ATOM   3406  CD  LYS A 450      78.213  52.689  47.269  1.00 30.05           C  
ANISOU 3406  CD  LYS A 450     3694   3921   3803   -132    370    321       C  
ATOM   3407  CE  LYS A 450      77.135  53.035  46.270  1.00 40.81           C  
ANISOU 3407  CE  LYS A 450     5126   5308   5071    -83    370    365       C  
ATOM   3408  NZ  LYS A 450      77.735  53.806  45.134  1.00 36.36           N  
ANISOU 3408  NZ  LYS A 450     4596   4730   4488    -90    451    448       N  
ATOM   3409  N   GLY A 451      80.253  51.819  52.266  1.00 14.42           N  
ANISOU 3409  N   GLY A 451     1554   1844   2081   -235    169    124       N  
ATOM   3410  CA  GLY A 451      81.315  52.197  53.159  1.00 17.37           C  
ANISOU 3410  CA  GLY A 451     1882   2176   2543   -285    123    102       C  
ATOM   3411  C   GLY A 451      82.069  53.412  52.681  1.00 19.49           C  
ANISOU 3411  C   GLY A 451     2125   2387   2891   -346    156    147       C  
ATOM   3412  O   GLY A 451      81.946  53.838  51.529  1.00 19.21           O  
ANISOU 3412  O   GLY A 451     2104   2354   2839   -345    233    206       O  
ATOM   3413  N   PRO A 452      82.853  54.002  53.581  1.00 25.34           N  
ANISOU 3413  N   PRO A 452     2836   3074   3718   -402     95    120       N  
ATOM   3414  CA  PRO A 452      83.725  55.115  53.210  1.00 28.96           C  
ANISOU 3414  CA  PRO A 452     3255   3468   4280   -480    122    161       C  
ATOM   3415  C   PRO A 452      84.978  54.646  52.486  1.00 25.66           C  
ANISOU 3415  C   PRO A 452     2717   3094   3939   -512    185    200       C  
ATOM   3416  O   PRO A 452      85.409  53.496  52.599  1.00 27.66           O  
ANISOU 3416  O   PRO A 452     2907   3416   4188   -481    178    178       O  
ATOM   3417  CB  PRO A 452      84.084  55.732  54.566  1.00 31.30           C  
ANISOU 3417  CB  PRO A 452     3562   3694   4637   -529     12    100       C  
ATOM   3418  CG  PRO A 452      84.036  54.567  55.509  1.00 26.39           C  
ANISOU 3418  CG  PRO A 452     2928   3131   3966   -483    -62     39       C  
ATOM   3419  CD  PRO A 452      82.883  53.729  55.032  1.00 26.33           C  
ANISOU 3419  CD  PRO A 452     2976   3186   3843   -399    -10     50       C  
ATOM   3420  N   ILE A 453      85.577  55.582  51.751  1.00 25.03           N  
ANISOU 3420  N   ILE A 453     2605   2967   3936   -574    254    263       N  
ATOM   3421  CA  ILE A 453      86.843  55.314  51.073  1.00 41.57           C  
ANISOU 3421  CA  ILE A 453     4574   5095   6125   -612    331    309       C  
ATOM   3422  C   ILE A 453      88.012  55.504  52.030  1.00 46.43           C  
ANISOU 3422  C   ILE A 453     5075   5682   6886   -690    246    274       C  
ATOM   3423  O   ILE A 453      88.982  54.738  52.003  1.00 51.25           O  
ANISOU 3423  O   ILE A 453     5561   6350   7563   -690    257    275       O  
ATOM   3424  CB  ILE A 453      86.994  56.209  49.827  1.00 48.69           C  
ANISOU 3424  CB  ILE A 453     5492   5961   7048   -645    458    404       C  
ATOM   3425  CG1 ILE A 453      85.807  56.034  48.881  1.00 45.90           C  
ANISOU 3425  CG1 ILE A 453     5258   5643   6541   -563    522    438       C  
ATOM   3426  CG2 ILE A 453      88.304  55.913  49.110  1.00 52.92           C  
ANISOU 3426  CG2 ILE A 453     5891   6535   7681   -681    561    458       C  
ATOM   3427  CD1 ILE A 453      85.637  54.625  48.372  1.00 43.62           C  
ANISOU 3427  CD1 ILE A 453     4960   5459   6156   -484    558    419       C  
ATOM   3428  N   ARG A 454      87.941  56.527  52.884  1.00 48.96           N  
ANISOU 3428  N   ARG A 454     5436   5910   7257   -752    154    240       N  
ATOM   3429  CA  ARG A 454      88.981  56.734  53.885  1.00 55.50           C  
ANISOU 3429  CA  ARG A 454     6166   6707   8213   -830     43    193       C  
ATOM   3430  C   ARG A 454      89.017  55.588  54.887  1.00 59.17           C  
ANISOU 3430  C   ARG A 454     6611   7241   8630   -771    -66    121       C  
ATOM   3431  O   ARG A 454      90.096  55.147  55.304  1.00 60.50           O  
ANISOU 3431  O   ARG A 454     6649   7443   8897   -799   -123    106       O  
ATOM   3432  CB  ARG A 454      88.755  58.066  54.603  1.00 52.68           C  
ANISOU 3432  CB  ARG A 454     5891   6228   7898   -903    -40    157       C  
ATOM   3433  N   GLY A 455      87.849  55.093  55.281  1.00 59.84           N  
ANISOU 3433  N   GLY A 455     6819   7347   8570   -687    -92     83       N  
ATOM   3434  CA  GLY A 455      87.749  54.040  56.272  1.00 63.78           C  
ANISOU 3434  CA  GLY A 455     7325   7899   9010   -627   -187     23       C  
ATOM   3435  C   GLY A 455      86.891  54.465  57.445  1.00 62.50           C  
ANISOU 3435  C   GLY A 455     7296   7684   8765   -612   -288    -45       C  
ATOM   3436  O   GLY A 455      86.533  55.639  57.568  1.00 63.10           O  
ANISOU 3436  O   GLY A 455     7447   7676   8852   -655   -298    -54       O  
ATOM   3437  N   ILE A 458      86.982  48.495  55.727  1.00 25.37           N  
ANISOU 3437  N   ILE A 458     2791   3654   3194   -362      3    -86       N  
ATOM   3438  CA  ILE A 458      85.953  48.141  54.742  1.00 24.52           C  
ANISOU 3438  CA  ILE A 458     2712   3550   3054   -342     33    -69       C  
ATOM   3439  C   ILE A 458      84.612  47.884  55.426  1.00 17.87           C  
ANISOU 3439  C   ILE A 458     1933   2665   2193   -306      5    -41       C  
ATOM   3440  O   ILE A 458      84.507  47.070  56.346  1.00 21.59           O  
ANISOU 3440  O   ILE A 458     2405   3120   2680   -274    -38    -51       O  
ATOM   3441  CB  ILE A 458      86.383  46.905  53.907  1.00 24.37           C  
ANISOU 3441  CB  ILE A 458     2635   3573   3053   -317     48   -111       C  
ATOM   3442  CG1 ILE A 458      87.539  47.270  52.948  1.00 29.78           C  
ANISOU 3442  CG1 ILE A 458     3259   4309   3745   -362     95   -142       C  
ATOM   3443  CG2 ILE A 458      85.191  46.304  53.170  1.00 26.81           C  
ANISOU 3443  CG2 ILE A 458     2977   3885   3323   -295     65   -101       C  
ATOM   3444  CD1 ILE A 458      87.090  47.925  51.654  1.00 32.37           C  
ANISOU 3444  CD1 ILE A 458     3612   4671   4015   -407    150   -117       C  
ATOM   3445  N   LYS A 459      83.578  48.581  54.966  1.00 15.39           N  
ANISOU 3445  N   LYS A 459     1666   2333   1847   -315     30      0       N  
ATOM   3446  CA  LYS A 459      82.191  48.299  55.313  1.00 14.10           C  
ANISOU 3446  CA  LYS A 459     1553   2138   1666   -281     17     24       C  
ATOM   3447  C   LYS A 459      81.374  48.348  54.028  1.00 16.83           C  
ANISOU 3447  C   LYS A 459     1908   2509   1978   -282     47     56       C  
ATOM   3448  O   LYS A 459      81.709  49.113  53.120  1.00 17.31           O  
ANISOU 3448  O   LYS A 459     1959   2594   2025   -319     78     79       O  
ATOM   3449  CB  LYS A 459      81.644  49.311  56.333  1.00 14.45           C  
ANISOU 3449  CB  LYS A 459     1646   2127   1716   -293     11     45       C  
ATOM   3450  CG  LYS A 459      82.237  49.147  57.742  1.00 14.10           C  
ANISOU 3450  CG  LYS A 459     1602   2069   1687   -300    -26     14       C  
ATOM   3451  CD  LYS A 459      81.761  47.839  58.367  1.00 14.93           C  
ANISOU 3451  CD  LYS A 459     1713   2175   1784   -259    -66      5       C  
ATOM   3452  CE  LYS A 459      82.141  47.745  59.858  1.00 15.57           C  
ANISOU 3452  CE  LYS A 459     1805   2247   1865   -275   -109     -9       C  
ATOM   3453  NZ  LYS A 459      81.628  46.497  60.524  1.00 15.40           N  
ANISOU 3453  NZ  LYS A 459     1795   2222   1834   -241   -150     -4       N  
ATOM   3454  N   PRO A 460      80.314  47.522  53.902  1.00 16.06           N  
ANISOU 3454  N   PRO A 460     1828   2414   1861   -249     37     60       N  
ATOM   3455  CA  PRO A 460      79.901  46.484  54.854  1.00 13.59           C  
ANISOU 3455  CA  PRO A 460     1527   2077   1561   -211      3     37       C  
ATOM   3456  C   PRO A 460      80.909  45.346  54.855  1.00 15.09           C  
ANISOU 3456  C   PRO A 460     1669   2288   1777   -197     -9    -12       C  
ATOM   3457  O   PRO A 460      81.810  45.317  54.009  1.00 16.37           O  
ANISOU 3457  O   PRO A 460     1786   2489   1945   -216     16    -36       O  
ATOM   3458  CB  PRO A 460      78.547  46.009  54.302  1.00 13.34           C  
ANISOU 3458  CB  PRO A 460     1517   2054   1499   -192      8     56       C  
ATOM   3459  CG  PRO A 460      78.736  46.173  52.799  1.00 14.66           C  
ANISOU 3459  CG  PRO A 460     1658   2280   1634   -220     41     65       C  
ATOM   3460  CD  PRO A 460      79.493  47.487  52.672  1.00 16.56           C  
ANISOU 3460  CD  PRO A 460     1894   2515   1883   -256     58     91       C  
ATOM   3461  N   ASP A 461      80.757  44.411  55.787  1.00 13.95           N  
ANISOU 3461  N   ASP A 461     1531   2116   1653   -165    -45    -25       N  
ATOM   3462  CA  ASP A 461      81.646  43.252  55.793  1.00 12.77           C  
ANISOU 3462  CA  ASP A 461     1330   1973   1548   -143    -60    -64       C  
ATOM   3463  C   ASP A 461      81.248  42.250  54.717  1.00 13.43           C  
ANISOU 3463  C   ASP A 461     1396   2077   1628   -129    -29    -94       C  
ATOM   3464  O   ASP A 461      82.108  41.739  53.988  1.00 14.62           O  
ANISOU 3464  O   ASP A 461     1492   2254   1810   -130     -4   -139       O  
ATOM   3465  CB  ASP A 461      81.619  42.605  57.177  1.00 14.40           C  
ANISOU 3465  CB  ASP A 461     1551   2141   1779   -118   -114    -52       C  
ATOM   3466  CG  ASP A 461      82.175  43.521  58.246  1.00 22.04           C  
ANISOU 3466  CG  ASP A 461     2529   3102   2744   -144   -144    -34       C  
ATOM   3467  OD1 ASP A 461      83.393  43.820  58.192  1.00 24.47           O  
ANISOU 3467  OD1 ASP A 461     2787   3430   3079   -159   -149    -50       O  
ATOM   3468  OD2 ASP A 461      81.397  43.961  59.130  1.00 19.34           O1-
ANISOU 3468  OD2 ASP A 461     2242   2738   2370   -155   -159    -12       O1-
ATOM   3469  N   ILE A 462      79.954  41.954  54.616  1.00 13.48           N  
ANISOU 3469  N   ILE A 462     1444   2075   1601   -120    -27    -79       N  
ATOM   3470  CA  ILE A 462      79.405  41.062  53.595  1.00 12.55           C  
ANISOU 3470  CA  ILE A 462     1317   1983   1469   -118      3   -110       C  
ATOM   3471  C   ILE A 462      78.026  41.584  53.225  1.00 12.23           C  
ANISOU 3471  C   ILE A 462     1320   1959   1368   -133     10    -71       C  
ATOM   3472  O   ILE A 462      77.514  42.529  53.839  1.00 12.94           O  
ANISOU 3472  O   ILE A 462     1445   2027   1443   -134     -5    -24       O  
ATOM   3473  CB  ILE A 462      79.306  39.600  54.076  1.00 15.35           C  
ANISOU 3473  CB  ILE A 462     1664   2297   1873    -82    -15   -141       C  
ATOM   3474  CG1 ILE A 462      78.448  39.513  55.342  1.00 17.24           C  
ANISOU 3474  CG1 ILE A 462     1955   2489   2106    -63    -59    -98       C  
ATOM   3475  CG2 ILE A 462      80.683  38.962  54.318  1.00 16.92           C  
ANISOU 3475  CG2 ILE A 462     1803   2476   2149    -60    -24   -176       C  
ATOM   3476  CD1 ILE A 462      77.907  38.107  55.565  1.00 20.94           C  
ANISOU 3476  CD1 ILE A 462     2430   2922   2604    -38    -67   -116       C  
ATOM   3477  N   VAL A 463      77.390  40.956  52.235  1.00 12.50           N  
ANISOU 3477  N   VAL A 463     1348   2031   1371   -144     35    -94       N  
ATOM   3478  CA  VAL A 463      76.014  41.286  51.888  1.00 13.24           C  
ANISOU 3478  CA  VAL A 463     1474   2145   1412   -155     34    -55       C  
ATOM   3479  C   VAL A 463      75.204  39.998  51.845  1.00 13.57           C  
ANISOU 3479  C   VAL A 463     1522   2181   1454   -144     34    -90       C  
ATOM   3480  O   VAL A 463      75.750  38.897  51.776  1.00 16.07           O  
ANISOU 3480  O   VAL A 463     1815   2484   1808   -135     46   -148       O  
ATOM   3481  CB  VAL A 463      75.934  42.040  50.548  1.00 12.74           C  
ANISOU 3481  CB  VAL A 463     1397   2154   1290   -200     61    -32       C  
ATOM   3482  CG1 VAL A 463      76.781  43.308  50.609  1.00 13.68           C  
ANISOU 3482  CG1 VAL A 463     1512   2270   1417   -215     64      4       C  
ATOM   3483  CG2 VAL A 463      76.423  41.140  49.390  1.00 14.82           C  
ANISOU 3483  CG2 VAL A 463     1622   2478   1532   -231     99   -100       C  
ATOM   3484  N   ALA A 464      73.880  40.146  51.874  1.00 11.95           N  
ANISOU 3484  N   ALA A 464     1344   1983   1215   -146     24    -55       N  
ATOM   3485  CA  ALA A 464      72.982  39.002  51.843  1.00 13.22           C  
ANISOU 3485  CA  ALA A 464     1512   2140   1371   -143     25    -86       C  
ATOM   3486  C   ALA A 464      71.709  39.409  51.115  1.00 15.03           C  
ANISOU 3486  C   ALA A 464     1746   2424   1539   -167     26    -50       C  
ATOM   3487  O   ALA A 464      71.345  40.586  51.072  1.00 14.67           O  
ANISOU 3487  O   ALA A 464     1708   2392   1476   -169     15     12       O  
ATOM   3488  CB  ALA A 464      72.650  38.503  53.262  1.00 16.00           C  
ANISOU 3488  CB  ALA A 464     1896   2418   1765   -109     -2    -78       C  
ATOM   3489  N   SER A 465      71.025  38.410  50.565  1.00 14.72           N  
ANISOU 3489  N   SER A 465     1701   2416   1478   -187     38    -90       N  
ATOM   3490  CA  SER A 465      69.766  38.654  49.873  1.00 16.09           C  
ANISOU 3490  CA  SER A 465     1870   2651   1592   -214     31    -58       C  
ATOM   3491  C   SER A 465      68.782  39.364  50.801  1.00 14.94           C  
ANISOU 3491  C   SER A 465     1746   2466   1463   -183      3      6       C  
ATOM   3492  O   SER A 465      68.564  38.931  51.930  1.00 16.97           O  
ANISOU 3492  O   SER A 465     2029   2659   1761   -155     -4     -6       O  
ATOM   3493  CB  SER A 465      69.179  37.326  49.410  1.00 21.34           C  
ANISOU 3493  CB  SER A 465     2528   3341   2240   -240     48   -123       C  
ATOM   3494  OG  SER A 465      67.935  37.542  48.761  1.00 22.02           O  
ANISOU 3494  OG  SER A 465     2604   3497   2267   -271     35    -90       O  
ATOM   3495  N   GLY A 466      68.197  40.459  50.333  1.00 13.67           N  
ANISOU 3495  N   GLY A 466     1575   2343   1275   -191    -10     74       N  
ATOM   3496  CA  GLY A 466      67.283  41.195  51.187  1.00 12.94           C  
ANISOU 3496  CA  GLY A 466     1496   2207   1214   -159    -27    126       C  
ATOM   3497  C   GLY A 466      66.284  42.058  50.444  1.00 14.97           C  
ANISOU 3497  C   GLY A 466     1725   2515   1446   -168    -44    200       C  
ATOM   3498  O   GLY A 466      65.858  43.094  50.970  1.00 15.70           O  
ANISOU 3498  O   GLY A 466     1820   2566   1580   -139    -51    254       O  
ATOM   3499  N   VAL A 467      65.880  41.649  49.242  1.00 13.64           N  
ANISOU 3499  N   VAL A 467     1530   2438   1216   -210    -50    201       N  
ATOM   3500  CA  VAL A 467      64.869  42.375  48.473  1.00 13.36           C  
ANISOU 3500  CA  VAL A 467     1462   2463   1153   -222    -78    282       C  
ATOM   3501  C   VAL A 467      63.616  41.512  48.352  1.00 19.25           C  
ANISOU 3501  C   VAL A 467     2188   3252   1875   -237    -89    261       C  
ATOM   3502  O   VAL A 467      63.674  40.381  47.845  1.00 17.96           O  
ANISOU 3502  O   VAL A 467     2023   3138   1663   -278    -77    193       O  
ATOM   3503  CB  VAL A 467      65.406  42.793  47.096  1.00 13.63           C  
ANISOU 3503  CB  VAL A 467     1475   2587   1118   -273    -84    320       C  
ATOM   3504  CG1 VAL A 467      64.323  43.504  46.298  1.00 18.87           C  
ANISOU 3504  CG1 VAL A 467     2100   3318   1751   -288   -125    420       C  
ATOM   3505  CG2 VAL A 467      66.615  43.698  47.281  1.00 15.06           C  
ANISOU 3505  CG2 VAL A 467     1674   2720   1329   -260    -70    343       C  
ATOM   3506  N   ASP A 468      62.486  42.056  48.819  1.00 15.23           N  
ANISOU 3506  N   ASP A 468     1660   2720   1405   -205   -108    314       N  
ATOM   3507  CA  ASP A 468      61.165  41.404  48.752  1.00 14.73           C  
ANISOU 3507  CA  ASP A 468     1568   2699   1328   -218   -122    305       C  
ATOM   3508  C   ASP A 468      61.187  40.008  49.373  1.00 16.29           C  
ANISOU 3508  C   ASP A 468     1797   2868   1525   -230    -94    205       C  
ATOM   3509  O   ASP A 468      60.702  39.033  48.789  1.00 17.51           O  
ANISOU 3509  O   ASP A 468     1936   3086   1631   -274    -94    161       O  
ATOM   3510  CB  ASP A 468      60.648  41.334  47.306  1.00 18.76           C  
ANISOU 3510  CB  ASP A 468     2034   3337   1758   -274   -154    344       C  
ATOM   3511  CG  ASP A 468      60.276  42.684  46.748  1.00 27.88           C  
ANISOU 3511  CG  ASP A 468     3151   4520   2924   -260   -193    466       C  
ATOM   3512  OD1 ASP A 468      59.959  43.598  47.530  1.00 25.84           O  
ANISOU 3512  OD1 ASP A 468     2887   4180   2751   -201   -194    516       O  
ATOM   3513  OD2 ASP A 468      60.279  42.829  45.507  1.00 27.45           O1-
ANISOU 3513  OD2 ASP A 468     3068   4570   2792   -312   -222    513       O1-
ATOM   3514  N   ILE A 469      61.737  39.921  50.581  1.00 13.42           N  
ANISOU 3514  N   ILE A 469     1474   2408   1215   -193    -72    172       N  
ATOM   3515  CA  ILE A 469      61.793  38.656  51.310  1.00 12.94           C  
ANISOU 3515  CA  ILE A 469     1446   2306   1165   -200    -51     94       C  
ATOM   3516  C   ILE A 469      60.467  38.447  52.036  1.00 13.88           C  
ANISOU 3516  C   ILE A 469     1558   2409   1309   -192    -51     96       C  
ATOM   3517  O   ILE A 469      60.014  39.322  52.783  1.00 14.28           O  
ANISOU 3517  O   ILE A 469     1604   2418   1402   -157    -50    136       O  
ATOM   3518  CB  ILE A 469      62.969  38.643  52.303  1.00 14.67           C  
ANISOU 3518  CB  ILE A 469     1710   2438   1426   -171    -36     70       C  
ATOM   3519  CG1 ILE A 469      64.300  38.923  51.590  1.00 14.47           C  
ANISOU 3519  CG1 ILE A 469     1684   2430   1385   -179    -33     66       C  
ATOM   3520  CG2 ILE A 469      63.012  37.305  53.037  1.00 17.65           C  
ANISOU 3520  CG2 ILE A 469     2119   2769   1819   -178    -21      6       C  
ATOM   3521  CD1 ILE A 469      64.536  38.054  50.341  1.00 19.35           C  
ANISOU 3521  CD1 ILE A 469     2281   3122   1949   -227    -22     19       C  
ATOM   3522  N   ILE A 470      59.853  37.279  51.829  1.00 14.32           N  
ANISOU 3522  N   ILE A 470     1609   2495   1339   -229    -44     47       N  
ATOM   3523  CA  ILE A 470      58.564  36.944  52.445  1.00 13.52           C  
ANISOU 3523  CA  ILE A 470     1495   2387   1254   -232    -40     41       C  
ATOM   3524  C   ILE A 470      58.771  36.557  53.902  1.00 13.62           C  
ANISOU 3524  C   ILE A 470     1559   2306   1309   -213    -16     12       C  
ATOM   3525  O   ILE A 470      59.628  35.723  54.222  1.00 14.39           O  
ANISOU 3525  O   ILE A 470     1698   2359   1410   -220     -6    -30       O  
ATOM   3526  CB  ILE A 470      57.898  35.790  51.686  1.00 14.08           C  
ANISOU 3526  CB  ILE A 470     1546   2524   1281   -289    -38     -8       C  
ATOM   3527  CG1 ILE A 470      57.701  36.164  50.227  1.00 15.42           C  
ANISOU 3527  CG1 ILE A 470     1665   2804   1391   -322    -65     23       C  
ATOM   3528  CG2 ILE A 470      56.554  35.397  52.339  1.00 13.05           C  
ANISOU 3528  CG2 ILE A 470     1400   2390   1169   -299    -30    -18       C  
ATOM   3529  CD1 ILE A 470      57.458  34.965  49.328  1.00 17.06           C  
ANISOU 3529  CD1 ILE A 470     1860   3081   1540   -392    -57    -46       C  
ATOM   3530  N   SER A 471      57.956  37.119  54.792  1.00 12.29           N  
ANISOU 3530  N   SER A 471     1386   2110   1175   -193     -8     34       N  
ATOM   3531  CA  SER A 471      58.035  36.723  56.189  1.00 12.16           C  
ANISOU 3531  CA  SER A 471     1418   2019   1182   -190     14      8       C  
ATOM   3532  C   SER A 471      56.699  36.968  56.882  1.00 11.91           C  
ANISOU 3532  C   SER A 471     1364   1988   1173   -192     33     11       C  
ATOM   3533  O   SER A 471      55.752  37.517  56.312  1.00 13.74           O  
ANISOU 3533  O   SER A 471     1537   2270   1414   -186     26     38       O  
ATOM   3534  CB  SER A 471      59.173  37.468  56.893  1.00 13.67           C  
ANISOU 3534  CB  SER A 471     1647   2153   1395   -159     15     23       C  
ATOM   3535  OG  SER A 471      59.387  36.953  58.186  1.00 13.97           O  
ANISOU 3535  OG  SER A 471     1736   2132   1441   -168     29      1       O  
ATOM   3536  N   THR A 472      56.647  36.553  58.138  1.00 12.09           N  
ANISOU 3536  N   THR A 472     1432   1957   1203   -203     57    -14       N  
ATOM   3537  CA  THR A 472      55.466  36.789  58.963  1.00 12.03           C  
ANISOU 3537  CA  THR A 472     1409   1946   1217   -212     87    -22       C  
ATOM   3538  C   THR A 472      55.205  38.283  59.129  1.00 12.99           C  
ANISOU 3538  C   THR A 472     1494   2058   1384   -171     98      8       C  
ATOM   3539  O   THR A 472      56.133  39.089  59.248  1.00 14.75           O  
ANISOU 3539  O   THR A 472     1737   2249   1620   -144     93     27       O  
ATOM   3540  CB  THR A 472      55.691  36.178  60.339  1.00 14.20           C  
ANISOU 3540  CB  THR A 472     1749   2166   1482   -239    110    -48       C  
ATOM   3541  OG1 THR A 472      56.946  36.679  60.848  1.00 12.73           O  
ANISOU 3541  OG1 THR A 472     1606   1935   1296   -219    100    -35       O  
ATOM   3542  CG2 THR A 472      55.754  34.643  60.255  1.00 14.11           C  
ANISOU 3542  CG2 THR A 472     1769   2149   1443   -280    104    -73       C  
ATOM   3543  N   TYR A 473      53.927  38.650  59.200  1.00 14.40           N  
ANISOU 3543  N   TYR A 473     1617   2260   1596   -168    118      9       N  
ATOM   3544  CA  TYR A 473      53.543  40.042  59.365  1.00 13.59           C  
ANISOU 3544  CA  TYR A 473     1468   2137   1557   -126    135     35       C  
ATOM   3545  C   TYR A 473      52.370  40.113  60.335  1.00 15.36           C  
ANISOU 3545  C   TYR A 473     1669   2350   1817   -139    186     -2       C  
ATOM   3546  O   TYR A 473      51.874  39.093  60.827  1.00 18.94           O  
ANISOU 3546  O   TYR A 473     2143   2817   2236   -185    204    -40       O  
ATOM   3547  CB  TYR A 473      53.209  40.653  57.997  1.00 14.67           C  
ANISOU 3547  CB  TYR A 473     1531   2325   1716    -95     95     95       C  
ATOM   3548  CG  TYR A 473      53.110  42.159  57.939  1.00 14.39           C  
ANISOU 3548  CG  TYR A 473     1452   2255   1759    -42    102    141       C  
ATOM   3549  CD1 TYR A 473      54.221  42.966  58.147  1.00 17.70           C  
ANISOU 3549  CD1 TYR A 473     1911   2620   2193    -19    106    154       C  
ATOM   3550  CD2 TYR A 473      51.898  42.770  57.610  1.00 17.10           C  
ANISOU 3550  CD2 TYR A 473     1707   2621   2171    -14    102    175       C  
ATOM   3551  CE1 TYR A 473      54.119  44.356  58.060  1.00 19.42           C  
ANISOU 3551  CE1 TYR A 473     2089   2795   2494     27    115    197       C  
ATOM   3552  CE2 TYR A 473      51.792  44.146  57.524  1.00 19.42           C  
ANISOU 3552  CE2 TYR A 473     1955   2869   2553     39    108    223       C  
ATOM   3553  CZ  TYR A 473      52.913  44.927  57.734  1.00 20.23           C  
ANISOU 3553  CZ  TYR A 473     2106   2910   2672     58    116    233       C  
ATOM   3554  OH  TYR A 473      52.818  46.299  57.639  1.00 27.74           O  
ANISOU 3554  OH  TYR A 473     3013   3805   3721    109    127    281       O  
ATOM   3555  N   LYS A 474      51.907  41.325  60.611  1.00 15.99           N  
ANISOU 3555  N   LYS A 474     1702   2401   1972   -101    216      7       N  
ATOM   3556  CA  LYS A 474      50.950  41.439  61.704  1.00 17.19           C  
ANISOU 3556  CA  LYS A 474     1838   2533   2159   -118    279    -45       C  
ATOM   3557  C   LYS A 474      49.612  40.794  61.345  1.00 18.23           C  
ANISOU 3557  C   LYS A 474     1903   2724   2298   -137    281    -52       C  
ATOM   3558  O   LYS A 474      49.257  40.605  60.171  1.00 18.50           O  
ANISOU 3558  O   LYS A 474     1882   2815   2331   -124    231     -8       O  
ATOM   3559  CB  LYS A 474      50.774  42.898  62.113  1.00 29.39           C  
ANISOU 3559  CB  LYS A 474     3345   4023   3798    -74    322    -47       C  
ATOM   3560  CG  LYS A 474      50.887  43.903  61.015  1.00 33.58           C  
ANISOU 3560  CG  LYS A 474     3816   4548   4394    -11    282     26       C  
ATOM   3561  CD  LYS A 474      50.744  45.303  61.582  1.00 34.72           C  
ANISOU 3561  CD  LYS A 474     3929   4617   4646     29    336     15       C  
ATOM   3562  CE  LYS A 474      50.509  46.320  60.477  1.00 29.40           C  
ANISOU 3562  CE  LYS A 474     3175   3935   4062     95    298    101       C  
ATOM   3563  NZ  LYS A 474      49.736  47.491  60.995  1.00 34.10           N  
ANISOU 3563  NZ  LYS A 474     3702   4460   4795    139    360     84       N  
ATOM   3564  N   ASN A 475      48.886  40.403  62.399  1.00 18.64           N  
ANISOU 3564  N   ASN A 475     1963   2771   2349   -178    338   -111       N  
ATOM   3565  CA  ASN A 475      47.544  39.823  62.283  1.00 21.62           C  
ANISOU 3565  CA  ASN A 475     2275   3201   2739   -204    354   -131       C  
ATOM   3566  C   ASN A 475      47.555  38.488  61.540  1.00 16.86           C  
ANISOU 3566  C   ASN A 475     1690   2654   2061   -247    307   -121       C  
ATOM   3567  O   ASN A 475      46.629  38.173  60.796  1.00 19.26           O  
ANISOU 3567  O   ASN A 475     1920   3019   2377   -254    287   -110       O  
ATOM   3568  CB  ASN A 475      46.577  40.805  61.609  1.00 23.49           C  
ANISOU 3568  CB  ASN A 475     2390   3457   3076   -147    349    -96       C  
ATOM   3569  CG  ASN A 475      46.556  42.157  62.303  1.00 22.40           C  
ANISOU 3569  CG  ASN A 475     2229   3249   3033   -101    404   -111       C  
ATOM   3570  OD1 ASN A 475      46.736  43.202  61.665  1.00 28.99           O  
ANISOU 3570  OD1 ASN A 475     3016   4059   3940    -37    379    -56       O  
ATOM   3571  ND2 ASN A 475      46.337  42.142  63.608  1.00 22.96           N  
ANISOU 3571  ND2 ASN A 475     2333   3286   3103   -139    483   -188       N  
ATOM   3572  N   GLY A 476      48.588  37.679  61.772  1.00 16.89           N  
ANISOU 3572  N   GLY A 476     1789   2635   1993   -279    291   -129       N  
ATOM   3573  CA  GLY A 476      48.590  36.358  61.186  1.00 15.70           C  
ANISOU 3573  CA  GLY A 476     1660   2521   1785   -324    260   -134       C  
ATOM   3574  C   GLY A 476      48.775  36.328  59.687  1.00 17.09           C  
ANISOU 3574  C   GLY A 476     1792   2750   1951   -303    199    -94       C  
ATOM   3575  O   GLY A 476      48.407  35.342  59.049  1.00 20.40           O  
ANISOU 3575  O   GLY A 476     2200   3218   2334   -345    181   -108       O  
ATOM   3576  N   THR A 477      49.323  37.383  59.112  1.00 16.23           N  
ANISOU 3576  N   THR A 477     1661   2637   1870   -247    171    -47       N  
ATOM   3577  CA  THR A 477      49.516  37.474  57.674  1.00 17.75           C  
ANISOU 3577  CA  THR A 477     1811   2889   2043   -234    113     -2       C  
ATOM   3578  C   THR A 477      50.967  37.182  57.292  1.00 15.14           C  
ANISOU 3578  C   THR A 477     1551   2536   1665   -233     87      4       C  
ATOM   3579  O   THR A 477      51.846  36.935  58.127  1.00 14.26           O  
ANISOU 3579  O   THR A 477     1516   2360   1541   -237    107    -20       O  
ATOM   3580  CB  THR A 477      49.112  38.860  57.151  1.00 19.12           C  
ANISOU 3580  CB  THR A 477     1902   3078   2283   -175     93     61       C  
ATOM   3581  OG1 THR A 477      49.983  39.860  57.706  1.00 19.66           O  
ANISOU 3581  OG1 THR A 477     2010   3071   2390   -130    110     76       O  
ATOM   3582  CG2 THR A 477      47.653  39.190  57.508  1.00 21.85           C  
ANISOU 3582  CG2 THR A 477     2162   3443   2696   -167    121     55       C  
ATOM   3583  N   TYR A 478      51.221  37.207  55.987  1.00 16.11           N  
ANISOU 3583  N   TYR A 478     1644   2720   1759   -233     42     36       N  
ATOM   3584  CA  TYR A 478      52.572  37.284  55.450  1.00 15.00           C  
ANISOU 3584  CA  TYR A 478     1548   2566   1586   -223     19     50       C  
ATOM   3585  C   TYR A 478      52.690  38.561  54.636  1.00 14.23           C  
ANISOU 3585  C   TYR A 478     1399   2497   1511   -181    -14    124       C  
ATOM   3586  O   TYR A 478      51.705  39.037  54.066  1.00 16.96           O  
ANISOU 3586  O   TYR A 478     1668   2899   1879   -173    -37    167       O  
ATOM   3587  CB  TYR A 478      52.915  36.072  54.559  1.00 16.22           C  
ANISOU 3587  CB  TYR A 478     1718   2769   1675   -275      2     14       C  
ATOM   3588  CG  TYR A 478      52.933  34.765  55.314  1.00 16.11           C  
ANISOU 3588  CG  TYR A 478     1761   2712   1650   -315     33    -51       C  
ATOM   3589  CD1 TYR A 478      53.965  34.474  56.204  1.00 14.63           C  
ANISOU 3589  CD1 TYR A 478     1647   2439   1470   -304     51    -68       C  
ATOM   3590  CD2 TYR A 478      51.906  33.829  55.153  1.00 16.19           C  
ANISOU 3590  CD2 TYR A 478     1746   2763   1643   -367     43    -88       C  
ATOM   3591  CE1 TYR A 478      53.982  33.283  56.914  1.00 15.89           C  
ANISOU 3591  CE1 TYR A 478     1858   2553   1627   -340     74   -112       C  
ATOM   3592  CE2 TYR A 478      51.915  32.627  55.849  1.00 16.16           C  
ANISOU 3592  CE2 TYR A 478     1795   2709   1635   -407     73   -140       C  
ATOM   3593  CZ  TYR A 478      52.972  32.364  56.729  1.00 16.55           C  
ANISOU 3593  CZ  TYR A 478     1921   2670   1697   -391     87   -147       C  
ATOM   3594  OH  TYR A 478      53.009  31.176  57.427  1.00 16.67           O  
ANISOU 3594  OH  TYR A 478     1990   2630   1714   -430    110   -183       O  
ATOM   3595  N   ASN A 479      53.903  39.103  54.575  1.00 13.68           N  
ANISOU 3595  N   ASN A 479     1370   2389   1440   -157    -20    143       N  
ATOM   3596  CA  ASN A 479      54.203  40.291  53.784  1.00 14.48           C  
ANISOU 3596  CA  ASN A 479     1435   2508   1559   -123    -51    217       C  
ATOM   3597  C   ASN A 479      55.640  40.148  53.309  1.00 14.64           C  
ANISOU 3597  C   ASN A 479     1507   2524   1533   -133    -61    212       C  
ATOM   3598  O   ASN A 479      56.282  39.111  53.520  1.00 16.50           O  
ANISOU 3598  O   ASN A 479     1793   2746   1731   -162    -47    152       O  
ATOM   3599  CB  ASN A 479      53.966  41.570  54.605  1.00 16.31           C  
ANISOU 3599  CB  ASN A 479     1651   2667   1879    -69    -27    249       C  
ATOM   3600  CG  ASN A 479      53.578  42.765  53.745  1.00 17.59           C  
ANISOU 3600  CG  ASN A 479     1742   2855   2087    -33    -62    341       C  
ATOM   3601  OD1 ASN A 479      54.201  43.037  52.720  1.00 18.04           O  
ANISOU 3601  OD1 ASN A 479     1795   2953   2105    -40    -99    392       O  
ATOM   3602  ND2 ASN A 479      52.510  43.460  54.133  1.00 22.23           N  
ANISOU 3602  ND2 ASN A 479     2268   3420   2759      3    -49    366       N  
ATOM   3603  N   THR A 480      56.153  41.179  52.656  1.00 16.20           N  
ANISOU 3603  N   THR A 480     1686   2729   1739   -111    -83    276       N  
ATOM   3604  CA  THR A 480      57.542  41.167  52.222  1.00 13.61           C  
ANISOU 3604  CA  THR A 480     1400   2398   1373   -121    -87    271       C  
ATOM   3605  C   THR A 480      58.254  42.393  52.742  1.00 14.33           C  
ANISOU 3605  C   THR A 480     1510   2415   1519    -79    -76    307       C  
ATOM   3606  O   THR A 480      57.647  43.448  52.917  1.00 16.13           O  
ANISOU 3606  O   THR A 480     1703   2616   1811    -43    -77    360       O  
ATOM   3607  CB  THR A 480      57.697  41.163  50.692  1.00 18.01           C  
ANISOU 3607  CB  THR A 480     1925   3056   1864   -157   -124    311       C  
ATOM   3608  OG1 THR A 480      56.863  42.189  50.138  1.00 18.94           O  
ANISOU 3608  OG1 THR A 480     1979   3210   2009   -138   -158    404       O  
ATOM   3609  CG2 THR A 480      57.324  39.824  50.127  1.00 19.63           C  
ANISOU 3609  CG2 THR A 480     2123   3333   2001   -214   -126    252       C  
ATOM   3610  N   GLY A 481      59.561  42.249  52.938  1.00 13.87           N  
ANISOU 3610  N   GLY A 481     1503   2324   1444    -84    -64    276       N  
ATOM   3611  CA  GLY A 481      60.398  43.365  53.318  1.00 16.25           C  
ANISOU 3611  CA  GLY A 481     1824   2563   1787    -56    -54    304       C  
ATOM   3612  C   GLY A 481      61.637  43.471  52.453  1.00 14.23           C  
ANISOU 3612  C   GLY A 481     1581   2337   1490    -75    -66    317       C  
ATOM   3613  O   GLY A 481      62.140  42.485  51.915  1.00 14.20           O  
ANISOU 3613  O   GLY A 481     1588   2379   1429   -108    -69    275       O  
ATOM   3614  N   THR A 482      62.137  44.694  52.348  1.00 12.80           N  
ANISOU 3614  N   THR A 482     1397   2123   1344    -57    -66    370       N  
ATOM   3615  CA  THR A 482      63.383  44.971  51.637  1.00 12.68           C  
ANISOU 3615  CA  THR A 482     1394   2128   1296    -77    -71    383       C  
ATOM   3616  C   THR A 482      64.276  45.834  52.506  1.00 16.32           C  
ANISOU 3616  C   THR A 482     1887   2505   1810    -56    -48    378       C  
ATOM   3617  O   THR A 482      63.788  46.729  53.195  1.00 17.32           O  
ANISOU 3617  O   THR A 482     2010   2568   2004    -26    -35    401       O  
ATOM   3618  CB  THR A 482      63.089  45.703  50.324  1.00 16.82           C  
ANISOU 3618  CB  THR A 482     1876   2718   1797    -92   -100    474       C  
ATOM   3619  OG1 THR A 482      62.463  44.807  49.396  1.00 17.85           O  
ANISOU 3619  OG1 THR A 482     1979   2948   1856   -129   -123    469       O  
ATOM   3620  CG2 THR A 482      64.377  46.261  49.696  1.00 16.81           C  
ANISOU 3620  CG2 THR A 482     1889   2727   1771   -115    -97    497       C  
ATOM   3621  N   GLY A 483      65.578  45.567  52.483  1.00 13.83           N  
ANISOU 3621  N   GLY A 483     1597   2188   1469    -74    -41    341       N  
ATOM   3622  CA  GLY A 483      66.534  46.509  53.041  1.00 13.64           C  
ANISOU 3622  CA  GLY A 483     1594   2101   1486    -67    -25    346       C  
ATOM   3623  C   GLY A 483      67.566  45.836  53.915  1.00 13.25           C  
ANISOU 3623  C   GLY A 483     1579   2023   1430    -73    -15    274       C  
ATOM   3624  O   GLY A 483      67.573  44.623  54.104  1.00 12.56           O  
ANISOU 3624  O   GLY A 483     1501   1956   1316    -78    -20    225       O  
ATOM   3625  N   THR A 484      68.474  46.657  54.450  1.00 11.91           N  
ANISOU 3625  N   THR A 484     1520   1700   1305   -104     83    344       N  
ATOM   3626  CA  THR A 484      69.609  46.055  55.149  1.00 12.86           C  
ANISOU 3626  CA  THR A 484     1596   1826   1466   -155    104    295       C  
ATOM   3627  C   THR A 484      69.208  45.431  56.485  1.00 13.23           C  
ANISOU 3627  C   THR A 484     1635   1850   1542   -141     68    214       C  
ATOM   3628  O   THR A 484      69.942  44.573  56.985  1.00 12.57           O  
ANISOU 3628  O   THR A 484     1517   1788   1470   -160     66    171       O  
ATOM   3629  CB  THR A 484      70.768  47.057  55.331  1.00 12.49           C  
ANISOU 3629  CB  THR A 484     1542   1711   1494   -225    127    343       C  
ATOM   3630  OG1 THR A 484      70.353  48.171  56.136  1.00 12.79           O  
ANISOU 3630  OG1 THR A 484     1636   1637   1586   -230     88    343       O  
ATOM   3631  CG2 THR A 484      71.304  47.526  53.957  1.00 12.97           C  
ANISOU 3631  CG2 THR A 484     1608   1797   1521   -244    203    441       C  
ATOM   3632  N   GLY A 485      68.057  45.810  57.063  1.00 11.05           N  
ANISOU 3632  N   GLY A 485     1393   1527   1278    -97     53    201       N  
ATOM   3633  CA  GLY A 485      67.570  45.086  58.222  1.00 12.44           C  
ANISOU 3633  CA  GLY A 485     1574   1690   1461    -75     53    138       C  
ATOM   3634  C   GLY A 485      67.024  43.716  57.889  1.00 15.29           C  
ANISOU 3634  C   GLY A 485     1883   2122   1804    -56     57    109       C  
ATOM   3635  O   GLY A 485      66.946  42.854  58.773  1.00 15.67           O  
ANISOU 3635  O   GLY A 485     1934   2163   1857    -53     70     68       O  
ATOM   3636  N   VAL A 486      66.601  43.507  56.639  1.00 12.49           N  
ANISOU 3636  N   VAL A 486     1497   1824   1423    -44     39    131       N  
ATOM   3637  CA  VAL A 486      66.262  42.160  56.206  1.00 10.13           C  
ANISOU 3637  CA  VAL A 486     1160   1580   1109    -42     25     87       C  
ATOM   3638  C   VAL A 486      67.536  41.333  56.056  1.00 12.01           C  
ANISOU 3638  C   VAL A 486     1398   1848   1315    -69     47     59       C  
ATOM   3639  O   VAL A 486      67.637  40.218  56.578  1.00 14.06           O  
ANISOU 3639  O   VAL A 486     1644   2105   1594    -70     53     13       O  
ATOM   3640  CB  VAL A 486      65.464  42.204  54.885  1.00 12.01           C  
ANISOU 3640  CB  VAL A 486     1388   1865   1310    -20    -31    105       C  
ATOM   3641  CG1 VAL A 486      65.184  40.788  54.397  1.00 13.59           C  
ANISOU 3641  CG1 VAL A 486     1565   2106   1494    -30    -65     40       C  
ATOM   3642  CG2 VAL A 486      64.167  42.967  55.101  1.00 15.67           C  
ANISOU 3642  CG2 VAL A 486     1820   2293   1842     20    -61    139       C  
ATOM   3643  N   SER A 487      68.532  41.883  55.357  1.00 11.72           N  
ANISOU 3643  N   SER A 487     1372   1834   1246    -85     70     96       N  
ATOM   3644  CA  SER A 487      69.785  41.164  55.152  1.00 12.16           C  
ANISOU 3644  CA  SER A 487     1402   1919   1299    -98    111     77       C  
ATOM   3645  C   SER A 487      70.464  40.844  56.478  1.00 12.56           C  
ANISOU 3645  C   SER A 487     1426   1928   1419   -112     97     54       C  
ATOM   3646  O   SER A 487      71.046  39.759  56.652  1.00 11.52           O  
ANISOU 3646  O   SER A 487     1266   1807   1304   -100    106     19       O  
ATOM   3647  CB  SER A 487      70.706  42.005  54.257  1.00 11.36           C  
ANISOU 3647  CB  SER A 487     1301   1838   1176   -117    166    141       C  
ATOM   3648  OG  SER A 487      70.040  42.221  53.017  1.00 14.60           O  
ANISOU 3648  OG  SER A 487     1770   2289   1487    -91    168    168       O  
ATOM   3649  N   SER A 488      70.434  41.790  57.419  1.00 11.73           N  
ANISOU 3649  N   SER A 488     1344   1765   1347   -132     67     73       N  
ATOM   3650  CA ASER A 488      71.067  41.524  58.701  0.61 12.22           C  
ANISOU 3650  CA ASER A 488     1410   1786   1445   -141     26     48       C  
ATOM   3651  CA BSER A 488      71.035  41.559  58.728  0.39 12.78           C  
ANISOU 3651  CA BSER A 488     1484   1856   1516   -141     26     49       C  
ATOM   3652  C   SER A 488      70.329  40.428  59.463  1.00 11.39           C  
ANISOU 3652  C   SER A 488     1339   1670   1318   -106     24     11       C  
ATOM   3653  O   SER A 488      70.965  39.673  60.216  1.00 13.19           O  
ANISOU 3653  O   SER A 488     1569   1884   1558    -97     -5     -4       O  
ATOM   3654  CB ASER A 488      71.149  42.812  59.525  0.61 12.98           C  
ANISOU 3654  CB ASER A 488     1560   1813   1561   -169    -15     59       C  
ATOM   3655  CB BSER A 488      70.986  42.853  59.549  0.39 12.31           C  
ANISOU 3655  CB BSER A 488     1482   1724   1470   -165    -13     59       C  
ATOM   3656  OG ASER A 488      69.873  43.215  59.987  0.61  9.44           O  
ANISOU 3656  OG ASER A 488     1183   1326   1078   -136      0     50       O  
ATOM   3657  OG BSER A 488      71.571  42.700  60.834  0.39 14.99           O  
ANISOU 3657  OG BSER A 488     1860   2020   1817   -173    -79     28       O  
ATOM   3658  N   SER A 489      69.012  40.309  59.264  1.00 10.73           N  
ANISOU 3658  N   SER A 489     1272   1588   1217    -85     52      6       N  
ATOM   3659  CA  SER A 489      68.255  39.220  59.874  1.00 11.57           C  
ANISOU 3659  CA  SER A 489     1393   1676   1329    -65     72    -17       C  
ATOM   3660  C   SER A 489      68.632  37.881  59.256  1.00 12.10           C  
ANISOU 3660  C   SER A 489     1422   1769   1407    -62     74    -45       C  
ATOM   3661  O   SER A 489      68.693  36.858  59.953  1.00 13.22           O  
ANISOU 3661  O   SER A 489     1583   1877   1564    -50     80    -56       O  
ATOM   3662  CB  SER A 489      66.754  39.470  59.718  1.00 12.23           C  
ANISOU 3662  CB  SER A 489     1463   1750   1434    -52    103    -10       C  
ATOM   3663  OG  SER A 489      66.391  40.675  60.360  1.00 12.89           O  
ANISOU 3663  OG  SER A 489     1591   1794   1514    -36    120     10       O  
ATOM   3664  N   ILE A 490      68.841  37.847  57.937  1.00 11.72           N  
ANISOU 3664  N   ILE A 490     1340   1772   1343    -66     74    -56       N  
ATOM   3665  CA AILE A 490      69.304  36.621  57.287  0.73 11.93           C  
ANISOU 3665  CA AILE A 490     1351   1813   1369    -52     86    -99       C  
ATOM   3666  CA BILE A 490      69.281  36.600  57.330  0.27 12.13           C  
ANISOU 3666  CA BILE A 490     1378   1837   1396    -52     86    -99       C  
ATOM   3667  C   ILE A 490      70.642  36.186  57.882  1.00 14.44           C  
ANISOU 3667  C   ILE A 490     1651   2116   1721    -34     90    -94       C  
ATOM   3668  O   ILE A 490      70.859  35.010  58.204  1.00 13.82           O  
ANISOU 3668  O   ILE A 490     1577   2003   1671     -9     92   -118       O  
ATOM   3669  CB AILE A 490      69.423  36.835  55.765  0.73 12.88           C  
ANISOU 3669  CB AILE A 490     1472   1992   1429    -48     99   -112       C  
ATOM   3670  CB BILE A 490      69.285  36.735  55.802  0.27 12.48           C  
ANISOU 3670  CB BILE A 490     1424   1938   1382    -48     95   -117       C  
ATOM   3671  CG1AILE A 490      68.063  37.120  55.113  0.73 11.63           C  
ANISOU 3671  CG1AILE A 490     1330   1848   1240    -57     54   -119       C  
ATOM   3672  CG1BILE A 490      67.840  36.857  55.335  0.27 13.88           C  
ANISOU 3672  CG1BILE A 490     1611   2119   1545    -60     49   -129       C  
ATOM   3673  CG2AILE A 490      70.148  35.660  55.103  0.73 13.72           C  
ANISOU 3673  CG2AILE A 490     1584   2107   1523    -19    134   -167       C  
ATOM   3674  CG2BILE A 490      69.986  35.549  55.154  0.27 14.43           C  
ANISOU 3674  CG2BILE A 490     1676   2190   1616    -20    127   -173       C  
ATOM   3675  CD1AILE A 490      67.089  35.938  55.116  0.73 12.43           C  
ANISOU 3675  CD1AILE A 490     1426   1916   1382    -67     18   -178       C  
ATOM   3676  CD1BILE A 490      67.694  36.961  53.896  0.27 16.01           C  
ANISOU 3676  CD1BILE A 490     1914   2440   1727    -50     26   -148       C  
ATOM   3677  N   VAL A 491      71.570  37.138  58.031  1.00 12.06           N  
ANISOU 3677  N   VAL A 491     1319   1830   1432    -48     81    -57       N  
ATOM   3678  CA  VAL A 491      72.879  36.787  58.584  1.00 12.33           C  
ANISOU 3678  CA  VAL A 491     1304   1852   1528    -32     58    -48       C  
ATOM   3679  C   VAL A 491      72.759  36.363  60.041  1.00 13.81           C  
ANISOU 3679  C   VAL A 491     1545   1982   1721    -18     -6    -42       C  
ATOM   3680  O   VAL A 491      73.447  35.432  60.488  1.00 14.61           O  
ANISOU 3680  O   VAL A 491     1629   2059   1862     20    -34    -43       O  
ATOM   3681  CB  VAL A 491      73.870  37.952  58.398  1.00 12.77           C  
ANISOU 3681  CB  VAL A 491     1295   1927   1628    -68     52     -7       C  
ATOM   3682  CG1 VAL A 491      75.163  37.714  59.185  1.00 14.17           C  
ANISOU 3682  CG1 VAL A 491     1397   2084   1901    -60    -12      6       C  
ATOM   3683  CG2 VAL A 491      74.201  38.129  56.907  1.00 13.97           C  
ANISOU 3683  CG2 VAL A 491     1405   2136   1768    -67    150      3       C  
ATOM   3684  N   THR A 492      71.898  37.041  60.806  1.00 11.45           N  
ANISOU 3684  N   THR A 492     1322   1655   1374    -37    -24    -32       N  
ATOM   3685  CA  THR A 492      71.698  36.666  62.206  1.00 12.98           C  
ANISOU 3685  CA  THR A 492     1604   1793   1534    -16    -62    -21       C  
ATOM   3686  C   THR A 492      71.237  35.225  62.316  1.00 14.44           C  
ANISOU 3686  C   THR A 492     1811   1947   1728     16    -23    -25       C  
ATOM   3687  O   THR A 492      71.768  34.457  63.124  1.00 12.70           O  
ANISOU 3687  O   THR A 492     1630   1686   1509     51    -63     -5       O  
ATOM   3688  CB  THR A 492      70.688  37.604  62.863  1.00 13.32           C  
ANISOU 3688  CB  THR A 492     1736   1809   1518    -29    -42    -17       C  
ATOM   3689  OG1 THR A 492      71.281  38.900  62.965  1.00 14.51           O  
ANISOU 3689  OG1 THR A 492     1888   1957   1668    -59    -98    -17       O  
ATOM   3690  CG2 THR A 492      70.323  37.127  64.272  1.00 14.51           C  
ANISOU 3690  CG2 THR A 492     2010   1902   1602      3    -42     -1       C  
ATOM   3691  N   GLY A 493      70.244  34.839  61.508  1.00 12.77           N  
ANISOU 3691  N   GLY A 493     1578   1743   1530      2     43    -47       N  
ATOM   3692  CA  GLY A 493      69.756  33.469  61.592  1.00 13.26           C  
ANISOU 3692  CA  GLY A 493     1660   1753   1624     15     77    -55       C  
ATOM   3693  C   GLY A 493      70.818  32.468  61.182  1.00 14.19           C  
ANISOU 3693  C   GLY A 493     1744   1859   1787     54     58    -74       C  
ATOM   3694  O   GLY A 493      71.005  31.435  61.831  1.00 13.95           O  
ANISOU 3694  O   GLY A 493     1757   1763   1782     87     53    -55       O  
ATOM   3695  N   VAL A 494      71.522  32.753  60.089  1.00 14.46           N  
ANISOU 3695  N   VAL A 494     1709   1953   1834     59     62   -107       N  
ATOM   3696  CA  VAL A 494      72.560  31.839  59.630  1.00 14.49           C  
ANISOU 3696  CA  VAL A 494     1670   1944   1891    112     72   -130       C  
ATOM   3697  C   VAL A 494      73.680  31.742  60.658  1.00 16.65           C  
ANISOU 3697  C   VAL A 494     1923   2194   2208    156      5    -81       C  
ATOM   3698  O   VAL A 494      74.212  30.655  60.915  1.00 14.80           O  
ANISOU 3698  O   VAL A 494     1689   1905   2030    216     -5    -77       O  
ATOM   3699  CB  VAL A 494      73.057  32.279  58.240  1.00 15.73           C  
ANISOU 3699  CB  VAL A 494     1766   2173   2037    114    122   -167       C  
ATOM   3700  CG1 VAL A 494      74.362  31.592  57.862  1.00 22.98           C  
ANISOU 3700  CG1 VAL A 494     2618   3087   3025    184    158   -180       C  
ATOM   3701  CG2 VAL A 494      71.968  31.986  57.210  1.00 16.57           C  
ANISOU 3701  CG2 VAL A 494     1921   2286   2091     89    154   -227       C  
ATOM   3702  N   LEU A 495      74.016  32.863  61.306  1.00 14.13           N  
ANISOU 3702  N   LEU A 495     1595   1905   1867    128    -58    -44       N  
ATOM   3703  CA ALEU A 495      75.048  32.832  62.338  0.52 14.80           C  
ANISOU 3703  CA ALEU A 495     1668   1968   1989    162   -164     -3       C  
ATOM   3704  CA BLEU A 495      75.045  32.839  62.338  0.48 14.86           C  
ANISOU 3704  CA BLEU A 495     1675   1975   1996    162   -164     -3       C  
ATOM   3705  C   LEU A 495      74.625  31.985  63.531  1.00 14.40           C  
ANISOU 3705  C   LEU A 495     1742   1840   1891    199   -205     33       C  
ATOM   3706  O   LEU A 495      75.472  31.358  64.173  1.00 15.65           O  
ANISOU 3706  O   LEU A 495     1897   1960   2088    260   -289     68       O  
ATOM   3707  CB ALEU A 495      75.385  34.245  62.807  0.52 17.28           C  
ANISOU 3707  CB ALEU A 495     1972   2312   2283    110   -243     13       C  
ATOM   3708  CB BLEU A 495      75.363  34.263  62.787  0.48 17.22           C  
ANISOU 3708  CB BLEU A 495     1965   2306   2274    108   -240     12       C  
ATOM   3709  CG ALEU A 495      76.450  35.011  62.027  0.52 16.09           C  
ANISOU 3709  CG ALEU A 495     1670   2213   2229     82   -245     13       C  
ATOM   3710  CG BLEU A 495      76.555  34.457  63.719  0.48 17.71           C  
ANISOU 3710  CG BLEU A 495     1990   2351   2387    126   -392     42       C  
ATOM   3711  CD1ALEU A 495      76.549  36.408  62.579  0.52 17.37           C  
ANISOU 3711  CD1ALEU A 495     1854   2375   2373     14   -328     22       C  
ATOM   3712  CD1BLEU A 495      77.806  33.794  63.170  0.48 15.64           C  
ANISOU 3712  CD1BLEU A 495     1564   2104   2275    178   -400     52       C  
ATOM   3713  CD2ALEU A 495      77.819  34.322  62.075  0.52 14.52           C  
ANISOU 3713  CD2ALEU A 495     1341   2011   2165    140   -297     32       C  
ATOM   3714  CD2BLEU A 495      76.804  35.939  63.954  0.48 21.29           C  
ANISOU 3714  CD2BLEU A 495     2434   2821   2836     52   -464     37       C  
ATOM   3715  N   ALA A 496      73.326  31.951  63.849  1.00 14.08           N  
ANISOU 3715  N   ALA A 496     1808   1771   1773    169   -142     36       N  
ATOM   3716  CA  ALA A 496      72.888  31.087  64.933  1.00 16.57           C  
ANISOU 3716  CA  ALA A 496     2249   2003   2042    202   -142     86       C  
ATOM   3717  C   ALA A 496      73.130  29.627  64.585  1.00 15.61           C  
ANISOU 3717  C   ALA A 496     2110   1817   2006    252   -115     89       C  
ATOM   3718  O   ALA A 496      73.537  28.839  65.444  1.00 15.50           O  
ANISOU 3718  O   ALA A 496     2168   1733   1989    312   -166    147       O  
ATOM   3719  CB  ALA A 496      71.412  31.348  65.258  1.00 13.32           C  
ANISOU 3719  CB  ALA A 496     1925   1572   1563    156    -44     95       C  
ATOM   3720  N   LEU A 497      72.902  29.249  63.324  1.00 12.49           N  
ANISOU 3720  N   LEU A 497     1634   1433   1677    235    -42     25       N  
ATOM   3721  CA  LEU A 497      73.208  27.882  62.908  1.00 13.78           C  
ANISOU 3721  CA  LEU A 497     1790   1518   1926    289    -15      7       C  
ATOM   3722  C   LEU A 497      74.707  27.620  62.972  1.00 18.46           C  
ANISOU 3722  C   LEU A 497     2308   2116   2590    378    -85     23       C  
ATOM   3723  O   LEU A 497      75.134  26.547  63.407  1.00 17.92           O  
ANISOU 3723  O   LEU A 497     2272   1956   2579    453   -110     59       O  
ATOM   3724  CB  LEU A 497      72.677  27.622  61.494  1.00 12.87           C  
ANISOU 3724  CB  LEU A 497     1630   1416   1843    254     63    -86       C  
ATOM   3725  CG  LEU A 497      71.189  27.853  61.276  1.00 15.68           C  
ANISOU 3725  CG  LEU A 497     2021   1771   2168    166    109   -108       C  
ATOM   3726  CD1 LEU A 497      70.833  27.540  59.826  1.00 16.12           C  
ANISOU 3726  CD1 LEU A 497     2043   1837   2244    141    140   -209       C  
ATOM   3727  CD2 LEU A 497      70.331  26.988  62.227  1.00 18.80           C  
ANISOU 3727  CD2 LEU A 497     2504   2050   2590    146    141    -51       C  
ATOM   3728  N   LEU A 498      75.515  28.591  62.535  1.00 16.68           N  
ANISOU 3728  N   LEU A 498     1969   1986   2382    371   -115      6       N  
ATOM   3729  CA  LEU A 498      76.964  28.424  62.552  1.00 16.14           C  
ANISOU 3729  CA  LEU A 498     1782   1927   2421    450   -177     27       C  
ATOM   3730  C   LEU A 498      77.490  28.319  63.978  1.00 18.43           C  
ANISOU 3730  C   LEU A 498     2121   2177   2705    495   -330    110       C  
ATOM   3731  O   LEU A 498      78.416  27.548  64.247  1.00 20.18           O  
ANISOU 3731  O   LEU A 498     2290   2351   3027    590   -394    145       O  
ATOM   3732  CB  LEU A 498      77.627  29.587  61.820  1.00 18.32           C  
ANISOU 3732  CB  LEU A 498     1920   2309   2734    411   -162      4       C  
ATOM   3733  CG  LEU A 498      77.296  29.713  60.330  1.00 31.55           C  
ANISOU 3733  CG  LEU A 498     3561   4033   4395    386    -15    -67       C  
ATOM   3734  CD1 LEU A 498      77.785  31.047  59.786  1.00 35.55           C  
ANISOU 3734  CD1 LEU A 498     3964   4633   4911    329      4    -59       C  
ATOM   3735  CD2 LEU A 498      77.901  28.558  59.550  1.00 38.73           C  
ANISOU 3735  CD2 LEU A 498     4422   4899   5392    482     73   -110       C  
ATOM   3736  N   MET A 499      76.884  29.056  64.912  1.00 18.43           N  
ANISOU 3736  N   MET A 499     2236   2186   2578    438   -391    141       N  
ATOM   3737  CA  MET A 499      77.350  29.005  66.293  1.00 17.63           C  
ANISOU 3737  CA  MET A 499     2226   2048   2426    482   -551    214       C  
ATOM   3738  C   MET A 499      77.035  27.660  66.933  1.00 21.21           C  
ANISOU 3738  C   MET A 499     2812   2389   2858    556   -541    277       C  
ATOM   3739  O   MET A 499      77.856  27.126  67.689  1.00 23.06           O  
ANISOU 3739  O   MET A 499     3068   2576   3119    644   -676    344       O  
ATOM   3740  CB  MET A 499      76.749  30.173  67.083  1.00 19.35           C  
ANISOU 3740  CB  MET A 499     2565   2297   2490    410   -598    216       C  
ATOM   3741  CG  MET A 499      77.418  31.497  66.656  1.00 22.40           C  
ANISOU 3741  CG  MET A 499     2816   2767   2929    349   -662    172       C  
ATOM   3742  SD  MET A 499      76.694  33.040  67.238  1.00 31.98           S  
ANISOU 3742  SD  MET A 499     4152   4006   3991    258   -686    143       S  
ATOM   3743  CE  MET A 499      76.463  32.598  68.918  1.00 29.31           C  
ANISOU 3743  CE  MET A 499     4061   3596   3479    317   -795    202       C  
ATOM   3744  N   GLU A 500      75.867  27.083  66.632  1.00 18.84           N  
ANISOU 3744  N   GLU A 500     2598   2036   2526    521   -391    265       N  
ATOM   3745  CA  GLU A 500      75.586  25.747  67.138  1.00 21.51           C  
ANISOU 3745  CA  GLU A 500     3052   2245   2874    580   -362    331       C  
ATOM   3746  C   GLU A 500      76.507  24.718  66.500  1.00 23.17           C  
ANISOU 3746  C   GLU A 500     3157   2399   3249    676   -372    317       C  
ATOM   3747  O   GLU A 500      76.992  23.799  67.176  1.00 27.04           O  
ANISOU 3747  O   GLU A 500     3711   2790   3773    772   -443    396       O  
ATOM   3748  CB  GLU A 500      74.117  25.376  66.911  1.00 19.65           C  
ANISOU 3748  CB  GLU A 500     2902   1955   2610    502   -199    317       C  
ATOM   3749  CG  GLU A 500      73.803  24.041  67.586  1.00 25.62           C  
ANISOU 3749  CG  GLU A 500     3796   2557   3382    550   -163    407       C  
ATOM   3750  CD  GLU A 500      72.479  23.435  67.185  1.00 30.65           C  
ANISOU 3750  CD  GLU A 500     4469   3112   4063    467     -4    389       C  
ATOM   3751  OE1 GLU A 500      71.816  23.977  66.287  1.00 26.70           O  
ANISOU 3751  OE1 GLU A 500     3879   2680   3588    382     62    297       O  
ATOM   3752  OE2 GLU A 500      72.110  22.398  67.772  1.00 37.02           O1-
ANISOU 3752  OE2 GLU A 500     5394   3779   4893    485     46    473       O1-
ATOM   3753  N   TYR A 501      76.779  24.867  65.201  1.00 23.31           N  
ANISOU 3753  N   TYR A 501     3022   2471   3363    662   -298    220       N  
ATOM   3754  CA  TYR A 501      77.683  23.946  64.520  1.00 21.50           C  
ANISOU 3754  CA  TYR A 501     2692   2188   3289    767   -278    192       C  
ATOM   3755  C   TYR A 501      79.071  23.978  65.143  1.00 21.88           C  
ANISOU 3755  C   TYR A 501     2641   2249   3423    872   -432    260       C  
ATOM   3756  O   TYR A 501      79.695  22.929  65.346  1.00 24.93           O  
ANISOU 3756  O   TYR A 501     3019   2535   3917    993   -467    303       O  
ATOM   3757  CB  TYR A 501      77.752  24.308  63.040  1.00 22.32           C  
ANISOU 3757  CB  TYR A 501     2673   2369   3440    735   -159     76       C  
ATOM   3758  CG  TYR A 501      78.701  23.451  62.239  1.00 27.98           C  
ANISOU 3758  CG  TYR A 501     3287   3037   4306    852   -100     31       C  
ATOM   3759  CD1 TYR A 501      78.264  22.278  61.641  1.00 32.98           C  
ANISOU 3759  CD1 TYR A 501     4002   3549   4979    888      0    -31       C  
ATOM   3760  CD2 TYR A 501      80.030  23.822  62.063  1.00 27.72           C  
ANISOU 3760  CD2 TYR A 501     3071   3071   4389    928   -136     47       C  
ATOM   3761  CE1 TYR A 501      79.122  21.491  60.907  1.00 31.52           C  
ANISOU 3761  CE1 TYR A 501     3744   3307   4924   1011     72    -84       C  
ATOM   3762  CE2 TYR A 501      80.895  23.037  61.328  1.00 30.89           C  
ANISOU 3762  CE2 TYR A 501     3370   3426   4939   1052    -51      7       C  
ATOM   3763  CZ  TYR A 501      80.435  21.877  60.754  1.00 32.28           C  
ANISOU 3763  CZ  TYR A 501     3655   3479   5131   1100     57    -62       C  
ATOM   3764  OH  TYR A 501      81.291  21.093  60.022  1.00 38.78           O  
ANISOU 3764  OH  TYR A 501     4395   4243   6095   1239    157   -113       O  
ATOM   3765  N   LEU A 502      79.576  25.181  65.428  1.00 22.76           N  
ANISOU 3765  N   LEU A 502     2666   2474   3507    829   -536    269       N  
ATOM   3766  CA  LEU A 502      80.898  25.314  66.024  1.00 24.61           C  
ANISOU 3766  CA  LEU A 502     2779   2725   3845    911   -717    329       C  
ATOM   3767  C   LEU A 502      80.929  24.721  67.424  1.00 30.84           C  
ANISOU 3767  C   LEU A 502     3734   3425   4557    981   -881    438       C  
ATOM   3768  O   LEU A 502      81.897  24.048  67.796  1.00 35.09           O  
ANISOU 3768  O   LEU A 502     4206   3910   5218   1106  -1005    501       O  
ATOM   3769  CB  LEU A 502      81.308  26.780  66.064  1.00 25.78           C  
ANISOU 3769  CB  LEU A 502     2818   2995   3981    821   -804    308       C  
ATOM   3770  CG  LEU A 502      81.829  27.345  64.750  1.00 27.36           C  
ANISOU 3770  CG  LEU A 502     2802   3280   4313    789   -678    238       C  
ATOM   3771  CD1 LEU A 502      81.674  28.847  64.745  1.00 31.31           C  
ANISOU 3771  CD1 LEU A 502     3276   3875   4746    659   -712    214       C  
ATOM   3772  CD2 LEU A 502      83.280  26.957  64.578  1.00 33.31           C  
ANISOU 3772  CD2 LEU A 502     3325   4031   5300    899   -739    268       C  
ATOM   3773  N   GLU A 503      79.876  24.957  68.213  1.00 30.91           N  
ANISOU 3773  N   GLU A 503     3965   3415   4364    912   -876    470       N  
ATOM   3774  CA  GLU A 503      79.844  24.428  69.575  1.00 43.17           C  
ANISOU 3774  CA  GLU A 503     5720   4884   5800    980  -1011    585       C  
ATOM   3775  C   GLU A 503      79.789  22.904  69.579  1.00 48.10           C  
ANISOU 3775  C   GLU A 503     6413   5360   6505   1085   -949    649       C  
ATOM   3776  O   GLU A 503      80.417  22.257  70.427  1.00 51.27           O  
ANISOU 3776  O   GLU A 503     6866   5710   6904   1173  -1065    744       O  
ATOM   3777  CB  GLU A 503      78.654  25.010  70.338  1.00 43.19           C  
ANISOU 3777  CB  GLU A 503     5952   4895   5565    887   -961    603       C  
ATOM   3778  N   LYS A 504      79.048  22.310  68.642  1.00 62.26           N  
ANISOU 3778  N   LYS A 504     9385   4554   9719   -380    839    863       N  
ATOM   3779  CA  LYS A 504      78.944  20.856  68.601  1.00 63.71           C  
ANISOU 3779  CA  LYS A 504     9714   4441  10051   -353    862    887       C  
ATOM   3780  C   LYS A 504      80.261  20.222  68.169  1.00 68.52           C  
ANISOU 3780  C   LYS A 504    10347   4860  10828    -77    943    879       C  
ATOM   3781  O   LYS A 504      80.764  19.301  68.824  1.00 71.90           O  
ANISOU 3781  O   LYS A 504    10823   5116  11378     58    951   1073       O  
ATOM   3782  CB  LYS A 504      77.811  20.434  67.665  1.00 60.83           C  
ANISOU 3782  CB  LYS A 504     9431   4014   9668   -571    853    656       C  
ATOM   3783  CG  LYS A 504      76.419  20.654  68.234  1.00 57.18           C  
ANISOU 3783  CG  LYS A 504     8940   3694   9092   -824    758    726       C  
ATOM   3784  CD  LYS A 504      75.365  19.930  67.409  1.00 59.55           C  
ANISOU 3784  CD  LYS A 504     9313   3889   9423  -1001    725    568       C  
ATOM   3785  N   GLN A 505      80.834  20.699  67.069  1.00 69.00           N  
ANISOU 3785  N   GLN A 505    10362   4966  10889     10   1000    657       N  
ATOM   3786  CA  GLN A 505      82.079  20.144  66.550  1.00 69.27           C  
ANISOU 3786  CA  GLN A 505    10400   4852  11069    273   1081    630       C  
ATOM   3787  C   GLN A 505      82.859  21.185  65.759  1.00 64.85           C  
ANISOU 3787  C   GLN A 505     9710   4478  10452    394   1105    469       C  
ATOM   3788  O   GLN A 505      83.883  21.685  66.220  1.00 64.49           O  
ANISOU 3788  O   GLN A 505     9525   4545  10433    603   1085    629       O  
ATOM   3789  CB  GLN A 505      81.797  18.923  65.673  1.00 73.81           C  
ANISOU 3789  CB  GLN A 505    11146   5164  11735    228   1154    457       C  
ATOM   3790  N   PRO A 509      85.816  25.674  71.999  1.00 56.32           N  
ANISOU 3790  N   PRO A 509     7814   4839   8748    780    427   2040       N  
ATOM   3791  CA  PRO A 509      85.150  26.094  73.236  1.00 54.65           C  
ANISOU 3791  CA  PRO A 509     7635   4830   8299    574    321   2211       C  
ATOM   3792  C   PRO A 509      84.290  27.339  73.034  1.00 45.47           C  
ANISOU 3792  C   PRO A 509     6445   3922   6910    371    324   2069       C  
ATOM   3793  O   PRO A 509      84.666  28.225  72.264  1.00 43.56           O  
ANISOU 3793  O   PRO A 509     6078   3897   6574    420    311   1862       O  
ATOM   3794  CB  PRO A 509      86.321  26.379  74.182  1.00 56.47           C  
ANISOU 3794  CB  PRO A 509     7746   5299   8412    694    159   2434       C  
ATOM   3795  CG  PRO A 509      87.428  26.799  73.283  1.00 56.92           C  
ANISOU 3795  CG  PRO A 509     7642   5430   8553    913    161   2350       C  
ATOM   3796  CD  PRO A 509      87.235  26.071  71.971  1.00 58.16           C  
ANISOU 3796  CD  PRO A 509     7867   5253   8977   1008    341   2124       C  
ATOM   3797  N   ARG A 510      83.142  27.399  73.716  1.00 46.56           N  
ANISOU 3797  N   ARG A 510     6686   4094   6910    128    329   2100       N  
ATOM   3798  CA  ARG A 510      82.259  28.554  73.571  1.00 40.71           C  
ANISOU 3798  CA  ARG A 510     5912   3617   5939    -84    343   1944       C  
ATOM   3799  C   ARG A 510      82.970  29.846  73.944  1.00 37.03           C  
ANISOU 3799  C   ARG A 510     5305   3543   5221    -44    231   2001       C  
ATOM   3800  O   ARG A 510      82.633  30.916  73.424  1.00 33.33           O  
ANISOU 3800  O   ARG A 510     4755   3326   4584   -138    244   1786       O  
ATOM   3801  CB  ARG A 510      81.002  28.368  74.422  1.00 47.41           C  
ANISOU 3801  CB  ARG A 510     6891   4465   6658   -324    360   1964       C  
ATOM   3802  N   LEU A 511      83.982  29.762  74.806  1.00 41.21           N  
ANISOU 3802  N   LEU A 511     5801   4166   5691     85    108   2187       N  
ATOM   3803  CA  LEU A 511      84.748  30.935  75.206  1.00 43.94           C  
ANISOU 3803  CA  LEU A 511     6026   4877   5790    114    -11   2178       C  
ATOM   3804  C   LEU A 511      85.533  31.528  74.037  1.00 46.91           C  
ANISOU 3804  C   LEU A 511     6235   5359   6228    281    -16   2090       C  
ATOM   3805  O   LEU A 511      86.158  32.584  74.176  1.00 49.42           O  
ANISOU 3805  O   LEU A 511     6439   5992   6345    296   -108   2022       O  
ATOM   3806  CB  LEU A 511      85.687  30.566  76.359  1.00 53.19           C  
ANISOU 3806  CB  LEU A 511     7207   6078   6925    196   -131   2353       C  
ATOM   3807  CG  LEU A 511      86.482  31.703  76.995  1.00 57.96           C  
ANISOU 3807  CG  LEU A 511     7722   7008   7292    189   -245   2309       C  
ATOM   3808  CD1 LEU A 511      85.615  32.534  77.934  1.00 60.53           C  
ANISOU 3808  CD1 LEU A 511     8148   7490   7362    -11   -217   2189       C  
ATOM   3809  CD2 LEU A 511      87.695  31.141  77.703  1.00 60.17           C  
ANISOU 3809  CD2 LEU A 511     7967   7251   7641    317   -352   2494       C  
ATOM   3810  N   SER A 512      85.495  30.879  72.872  1.00 48.89           N  
ANISOU 3810  N   SER A 512     6485   5368   6723    385     92   1905       N  
ATOM   3811  CA  SER A 512      86.197  31.375  71.695  1.00 48.85           C  
ANISOU 3811  CA  SER A 512     6340   5464   6757    537    106   1662       C  
ATOM   3812  C   SER A 512      85.275  31.916  70.605  1.00 48.72           C  
ANISOU 3812  C   SER A 512     6322   5511   6680    389    204   1286       C  
ATOM   3813  O   SER A 512      85.770  32.305  69.542  1.00 55.03           O  
ANISOU 3813  O   SER A 512     7019   6380   7510    498    228   1058       O  
ATOM   3814  CB  SER A 512      87.088  30.269  71.111  1.00 56.80           C  
ANISOU 3814  CB  SER A 512     7341   6158   8081    793    162   1690       C  
ATOM   3815  OG  SER A 512      86.363  29.454  70.206  1.00 57.85           O  
ANISOU 3815  OG  SER A 512     7599   5986   8397    745    314   1452       O  
ATOM   3816  N   LEU A 513      83.959  31.971  70.831  1.00 37.81           N  
ANISOU 3816  N   LEU A 513     5040   4111   5214    140    260   1229       N  
ATOM   3817  CA  LEU A 513      83.014  32.441  69.807  1.00 32.87           C  
ANISOU 3817  CA  LEU A 513     4404   3537   4547    -22    344    903       C  
ATOM   3818  C   LEU A 513      82.866  33.963  69.859  1.00 27.65           C  
ANISOU 3818  C   LEU A 513     3614   3283   3608   -123    299    817       C  
ATOM   3819  O   LEU A 513      81.803  34.521  70.133  1.00 34.16           O  
ANISOU 3819  O   LEU A 513     4459   4227   4292   -344    337    787       O  
ATOM   3820  CB  LEU A 513      81.664  31.756  69.962  1.00 38.15           C  
ANISOU 3820  CB  LEU A 513     5223   3985   5287   -242    429    896       C  
ATOM   3821  CG  LEU A 513      81.582  30.254  69.692  1.00 51.80           C  
ANISOU 3821  CG  LEU A 513     7100   5289   7293   -188    500    914       C  
ATOM   3822  CD1 LEU A 513      80.236  29.921  69.070  1.00 53.29           C  
ANISOU 3822  CD1 LEU A 513     7387   5322   7539   -425    590    725       C  
ATOM   3823  CD2 LEU A 513      82.723  29.790  68.798  1.00 57.99           C  
ANISOU 3823  CD2 LEU A 513     7850   5929   8254     65    522    804       C  
ATOM   3824  N   PHE A 514      83.960  34.641  69.556  1.00 19.65           N  
ANISOU 3824  N   PHE A 514     2462   2477   2529     49    227    780       N  
ATOM   3825  CA  PHE A 514      83.942  36.092  69.489  1.00 16.58           C  
ANISOU 3825  CA  PHE A 514     1945   2468   1885    -24    188    678       C  
ATOM   3826  C   PHE A 514      83.475  36.560  68.114  1.00 17.86           C  
ANISOU 3826  C   PHE A 514     2034   2688   2064    -84    260    323       C  
ATOM   3827  O   PHE A 514      83.627  35.858  67.110  1.00 17.76           O  
ANISOU 3827  O   PHE A 514     2044   2457   2246     -1    313    150       O  
ATOM   3828  CB  PHE A 514      85.333  36.670  69.766  1.00 18.70           C  
ANISOU 3828  CB  PHE A 514     2090   2951   2065    174     66    801       C  
ATOM   3829  CG  PHE A 514      85.818  36.481  71.189  1.00 18.73           C  
ANISOU 3829  CG  PHE A 514     2149   2978   1989    195    -38   1169       C  
ATOM   3830  CD1 PHE A 514      85.465  37.382  72.178  1.00 23.14           C  
ANISOU 3830  CD1 PHE A 514     2738   3667   2388     22    -67   1096       C  
ATOM   3831  CD2 PHE A 514      86.630  35.412  71.529  1.00 20.93           C  
ANISOU 3831  CD2 PHE A 514     2459   3025   2471    375    -83   1390       C  
ATOM   3832  CE1 PHE A 514      85.930  37.224  73.483  1.00 22.72           C  
ANISOU 3832  CE1 PHE A 514     2758   3547   2326     16   -136   1224       C  
ATOM   3833  CE2 PHE A 514      87.104  35.246  72.831  1.00 22.61           C  
ANISOU 3833  CE2 PHE A 514     2723   3238   2630    351   -179   1604       C  
ATOM   3834  CZ  PHE A 514      86.741  36.143  73.809  1.00 27.69           C  
ANISOU 3834  CZ  PHE A 514     3415   4034   3072    156   -200   1484       C  
ATOM   3835  N   THR A 515      82.951  37.791  68.082  1.00 15.35           N  
ANISOU 3835  N   THR A 515     1822   2051   1959   -149   -124     48       N  
ATOM   3836  CA  THR A 515      82.550  38.412  66.818  1.00 13.96           C  
ANISOU 3836  CA  THR A 515     1619   1863   1821   -138    -87     24       C  
ATOM   3837  C   THR A 515      83.652  38.335  65.769  1.00 14.92           C  
ANISOU 3837  C   THR A 515     1686   2041   1943    -75   -103     18       C  
ATOM   3838  O   THR A 515      83.381  38.046  64.597  1.00 15.30           O  
ANISOU 3838  O   THR A 515     1731   2067   2017    -31    -97      7       O  
ATOM   3839  CB  THR A 515      82.167  39.870  67.067  1.00 14.44           C  
ANISOU 3839  CB  THR A 515     1669   1929   1887   -213    -32      7       C  
ATOM   3840  OG1 THR A 515      81.094  39.912  68.015  1.00 16.10           O  
ANISOU 3840  OG1 THR A 515     1925   2091   2099   -266     -9      6       O  
ATOM   3841  CG2 THR A 515      81.700  40.550  65.769  1.00 17.17           C  
ANISOU 3841  CG2 THR A 515     1996   2257   2269   -195      3     -7       C  
ATOM   3842  N   GLN A 516      84.898  38.604  66.171  1.00 15.92           N  
ANISOU 3842  N   GLN A 516     1765   2249   2035    -76   -121     22       N  
ATOM   3843  CA  GLN A 516      86.011  38.636  65.222  1.00 17.87           C  
ANISOU 3843  CA  GLN A 516     1945   2567   2276    -25   -129     10       C  
ATOM   3844  C   GLN A 516      86.200  37.292  64.526  1.00 18.96           C  
ANISOU 3844  C   GLN A 516     2092   2683   2430     78   -162     14       C  
ATOM   3845  O   GLN A 516      86.453  37.235  63.311  1.00 17.98           O  
ANISOU 3845  O   GLN A 516     1940   2572   2320    120   -148     -6       O  
ATOM   3846  CB  GLN A 516      87.274  39.043  65.975  1.00 21.73           C  
ANISOU 3846  CB  GLN A 516     2375   3163   2720    -52   -148     14       C  
ATOM   3847  CG  GLN A 516      88.513  39.209  65.142  1.00 24.79           C  
ANISOU 3847  CG  GLN A 516     2678   3648   3093    -16   -150     -2       C  
ATOM   3848  CD  GLN A 516      89.676  39.679  65.979  1.00 22.28           C  
ANISOU 3848  CD  GLN A 516     2293   3450   2723    -61   -170      0       C  
ATOM   3849  OE1 GLN A 516      89.726  39.440  67.195  1.00 26.41           O  
ANISOU 3849  OE1 GLN A 516     2831   3986   3217    -82   -204     23       O  
ATOM   3850  NE2 GLN A 516      90.617  40.376  65.347  1.00 28.72           N  
ANISOU 3850  NE2 GLN A 516     3033   4361   3518    -86   -148    -25       N  
ATOM   3851  N   VAL A 517      86.084  36.201  65.284  1.00 15.96           N  
ANISOU 3851  N   VAL A 517     1759   2262   2042    118   -202     39       N  
ATOM   3852  CA  VAL A 517      86.174  34.854  64.726  1.00 19.16           C  
ANISOU 3852  CA  VAL A 517     2197   2620   2461    216   -228     43       C  
ATOM   3853  C   VAL A 517      85.039  34.596  63.736  1.00 19.02           C  
ANISOU 3853  C   VAL A 517     2229   2520   2477    209   -199     21       C  
ATOM   3854  O   VAL A 517      85.256  34.101  62.621  1.00 17.32           O  
ANISOU 3854  O   VAL A 517     2008   2298   2274    269   -193     -1       O  
ATOM   3855  CB  VAL A 517      86.143  33.826  65.874  1.00 21.10           C  
ANISOU 3855  CB  VAL A 517     2507   2823   2688    245   -273     82       C  
ATOM   3856  CG1 VAL A 517      86.168  32.425  65.317  1.00 24.28           C  
ANISOU 3856  CG1 VAL A 517     2966   3154   3105    345   -292     85       C  
ATOM   3857  CG2 VAL A 517      87.304  34.067  66.852  1.00 28.93           C  
ANISOU 3857  CG2 VAL A 517     3441   3914   3637    254   -312    109       C  
ATOM   3858  N   LEU A 518      83.801  34.883  64.144  1.00 16.60           N  
ANISOU 3858  N   LEU A 518     1970   2156   2180    136   -179     23       N  
ATOM   3859  CA  LEU A 518      82.663  34.606  63.272  1.00 14.36           C  
ANISOU 3859  CA  LEU A 518     1723   1809   1922    123   -158      4       C  
ATOM   3860  C   LEU A 518      82.709  35.475  62.023  1.00 15.07           C  
ANISOU 3860  C   LEU A 518     1760   1941   2026    120   -128    -19       C  
ATOM   3861  O   LEU A 518      82.381  35.007  60.924  1.00 16.41           O  
ANISOU 3861  O   LEU A 518     1941   2088   2204    147   -123    -39       O  
ATOM   3862  CB  LEU A 518      81.359  34.813  64.036  1.00 17.35           C  
ANISOU 3862  CB  LEU A 518     2146   2139   2307     45   -141     11       C  
ATOM   3863  CG  LEU A 518      81.278  33.862  65.235  1.00 23.16           C  
ANISOU 3863  CG  LEU A 518     2949   2829   3020     39   -169     37       C  
ATOM   3864  CD1 LEU A 518      80.181  34.292  66.189  1.00 26.42           C  
ANISOU 3864  CD1 LEU A 518     3390   3218   3431    -51   -145     41       C  
ATOM   3865  CD2 LEU A 518      81.048  32.438  64.765  1.00 25.03           C  
ANISOU 3865  CD2 LEU A 518     3257   2993   3258     86   -188     34       C  
ATOM   3866  N   LYS A 519      83.131  36.734  62.167  1.00 15.20           N  
ANISOU 3866  N   LYS A 519     1724   2015   2036     82   -107    -18       N  
ATOM   3867  CA  LYS A 519      83.247  37.602  60.994  1.00 15.58           C  
ANISOU 3867  CA  LYS A 519     1731   2098   2090     76    -78    -34       C  
ATOM   3868  C   LYS A 519      84.259  37.041  60.006  1.00 16.49           C  
ANISOU 3868  C   LYS A 519     1814   2256   2194    143    -88    -52       C  
ATOM   3869  O   LYS A 519      84.030  37.056  58.791  1.00 16.30           O  
ANISOU 3869  O   LYS A 519     1788   2232   2174    155    -73    -68       O  
ATOM   3870  CB  LYS A 519      83.658  39.017  61.417  1.00 15.78           C  
ANISOU 3870  CB  LYS A 519     1722   2170   2105     17    -49    -30       C  
ATOM   3871  CG  LYS A 519      83.671  40.029  60.247  1.00 20.29           C  
ANISOU 3871  CG  LYS A 519     2270   2764   2678      0    -14    -38       C  
ATOM   3872  CD  LYS A 519      84.328  41.332  60.672  1.00 23.01           C  
ANISOU 3872  CD  LYS A 519     2590   3150   3002    -61     17    -38       C  
ATOM   3873  CE  LYS A 519      83.504  42.040  61.730  1.00 25.80           C  
ANISOU 3873  CE  LYS A 519     2980   3457   3367   -119     40    -29       C  
ATOM   3874  NZ  LYS A 519      84.097  43.360  62.083  1.00 31.80           N  
ANISOU 3874  NZ  LYS A 519     3733   4245   4105   -188     79    -35       N  
ATOM   3875  N   THR A 520      85.379  36.522  60.517  1.00 16.42           N  
ANISOU 3875  N   THR A 520     1780   2291   2169    189   -113    -49       N  
ATOM   3876  CA  THR A 520      86.411  35.941  59.666  1.00 15.60           C  
ANISOU 3876  CA  THR A 520     1637   2235   2057    265   -118    -70       C  
ATOM   3877  C   THR A 520      85.872  34.768  58.866  1.00 17.67           C  
ANISOU 3877  C   THR A 520     1956   2426   2332    320   -122    -87       C  
ATOM   3878  O   THR A 520      86.140  34.657  57.663  1.00 18.25           O  
ANISOU 3878  O   THR A 520     2012   2520   2401    348   -103   -116       O  
ATOM   3879  CB  THR A 520      87.592  35.512  60.534  1.00 18.07           C  
ANISOU 3879  CB  THR A 520     1908   2606   2351    317   -150    -57       C  
ATOM   3880  OG1 THR A 520      88.146  36.678  61.147  1.00 22.15           O  
ANISOU 3880  OG1 THR A 520     2367   3203   2845    248   -142    -50       O  
ATOM   3881  CG2 THR A 520      88.674  34.819  59.706  1.00 23.20           C  
ANISOU 3881  CG2 THR A 520     2511   3309   2995    413   -153    -81       C  
ATOM   3882  N   TYR A 521      85.087  33.894  59.509  1.00 16.18           N  
ANISOU 3882  N   TYR A 521     1843   2152   2154    324   -142    -73       N  
ATOM   3883  CA  TYR A 521      84.515  32.756  58.791  1.00 18.17           C  
ANISOU 3883  CA  TYR A 521     2162   2328   2412    358   -142    -94       C  
ATOM   3884  C   TYR A 521      83.509  33.200  57.732  1.00 16.70           C  
ANISOU 3884  C   TYR A 521     1984   2132   2231    302   -117   -114       C  
ATOM   3885  O   TYR A 521      83.486  32.643  56.625  1.00 17.24           O  
ANISOU 3885  O   TYR A 521     2070   2188   2293    329   -106   -146       O  
ATOM   3886  CB  TYR A 521      83.845  31.794  59.767  1.00 20.26           C  
ANISOU 3886  CB  TYR A 521     2514   2502   2680    354   -165    -72       C  
ATOM   3887  CG  TYR A 521      84.810  30.884  60.487  1.00 22.11           C  
ANISOU 3887  CG  TYR A 521     2769   2724   2907    441   -196    -52       C  
ATOM   3888  CD1 TYR A 521      85.782  30.167  59.793  1.00 25.13           C  
ANISOU 3888  CD1 TYR A 521     3141   3118   3289    545   -197    -74       C  
ATOM   3889  CD2 TYR A 521      84.740  30.736  61.865  1.00 27.91           C  
ANISOU 3889  CD2 TYR A 521     3536   3438   3631    425   -225    -11       C  
ATOM   3890  CE1 TYR A 521      86.666  29.329  60.462  1.00 34.12           C  
ANISOU 3890  CE1 TYR A 521     4295   4247   4423    642   -228    -50       C  
ATOM   3891  CE2 TYR A 521      85.620  29.906  62.543  1.00 29.38           C  
ANISOU 3891  CE2 TYR A 521     3742   3615   3805    513   -261     17       C  
ATOM   3892  CZ  TYR A 521      86.574  29.209  61.839  1.00 33.80           C  
ANISOU 3892  CZ  TYR A 521     4286   4185   4369    627   -264      0       C  
ATOM   3893  OH  TYR A 521      87.440  28.379  62.521  1.00 38.30           O  
ANISOU 3893  OH  TYR A 521     4874   4748   4929    731   -302     34       O  
ATOM   3894  N   LEU A 522      82.655  34.177  58.063  1.00 14.53           N  
ANISOU 3894  N   LEU A 522     1696   1860   1963    227   -107    -96       N  
ATOM   3895  CA  LEU A 522      81.696  34.691  57.087  1.00 14.54           C  
ANISOU 3895  CA  LEU A 522     1694   1864   1967    183    -90   -106       C  
ATOM   3896  C   LEU A 522      82.407  35.258  55.872  1.00 16.81           C  
ANISOU 3896  C   LEU A 522     1933   2214   2238    201    -72   -123       C  
ATOM   3897  O   LEU A 522      81.982  35.038  54.727  1.00 15.07           O  
ANISOU 3897  O   LEU A 522     1726   1995   2006    197    -65   -142       O  
ATOM   3898  CB  LEU A 522      80.824  35.768  57.736  1.00 15.74           C  
ANISOU 3898  CB  LEU A 522     1831   2016   2133    118    -79    -81       C  
ATOM   3899  CG  LEU A 522      79.830  35.307  58.800  1.00 18.02           C  
ANISOU 3899  CG  LEU A 522     2165   2249   2433     81    -88    -70       C  
ATOM   3900  CD1 LEU A 522      79.126  36.537  59.384  1.00 18.31           C  
ANISOU 3900  CD1 LEU A 522     2175   2297   2486     29    -66    -51       C  
ATOM   3901  CD2 LEU A 522      78.798  34.322  58.213  1.00 19.62           C  
ANISOU 3901  CD2 LEU A 522     2413   2408   2633     65    -96    -88       C  
ATOM   3902  N   ILE A 523      83.496  35.990  56.099  1.00 14.61           N  
ANISOU 3902  N   ILE A 523     1602   1997   1953    210    -62   -116       N  
ATOM   3903  CA  ILE A 523      84.234  36.576  54.982  1.00 14.28           C  
ANISOU 3903  CA  ILE A 523     1516   2022   1889    215    -38   -133       C  
ATOM   3904  C   ILE A 523      84.927  35.487  54.169  1.00 16.23           C  
ANISOU 3904  C   ILE A 523     1766   2279   2122    282    -37   -170       C  
ATOM   3905  O   ILE A 523      84.915  35.520  52.929  1.00 18.03           O  
ANISOU 3905  O   ILE A 523     1992   2530   2330    279    -19   -194       O  
ATOM   3906  CB  ILE A 523      85.223  37.641  55.507  1.00 14.30           C  
ANISOU 3906  CB  ILE A 523     1460   2091   1881    191    -24   -121       C  
ATOM   3907  CG1 ILE A 523      84.445  38.887  55.965  1.00 15.50           C  
ANISOU 3907  CG1 ILE A 523     1624   2223   2043    120     -9    -91       C  
ATOM   3908  CG2 ILE A 523      86.298  37.966  54.424  1.00 17.31           C  
ANISOU 3908  CG2 ILE A 523     1792   2554   2233    202      3   -146       C  
ATOM   3909  CD1 ILE A 523      85.282  39.895  56.763  1.00 17.04           C  
ANISOU 3909  CD1 ILE A 523     1782   2467   2226     78      8    -82       C  
ATOM   3910  N   LEU A 524      85.517  34.493  54.845  1.00 15.76           N  
ANISOU 3910  N   LEU A 524     1716   2200   2071    346    -56   -177       N  
ATOM   3911  CA  LEU A 524      86.207  33.416  54.136  1.00 16.51           C  
ANISOU 3911  CA  LEU A 524     1821   2295   2158    425    -49   -215       C  
ATOM   3912  C   LEU A 524      85.252  32.631  53.249  1.00 18.81           C  
ANISOU 3912  C   LEU A 524     2185   2517   2444    415    -43   -243       C  
ATOM   3913  O   LEU A 524      85.631  32.177  52.157  1.00 20.89           O  
ANISOU 3913  O   LEU A 524     2452   2796   2688    447    -20   -284       O  
ATOM   3914  CB  LEU A 524      86.875  32.474  55.134  1.00 22.35           C  
ANISOU 3914  CB  LEU A 524     2571   3009   2910    505    -74   -206       C  
ATOM   3915  CG  LEU A 524      88.371  32.598  55.346  1.00 39.71           C  
ANISOU 3915  CG  LEU A 524     4684   5304   5101    571    -74   -211       C  
ATOM   3916  CD1 LEU A 524      88.747  31.741  56.525  1.00 41.84           C  
ANISOU 3916  CD1 LEU A 524     4975   5540   5382    644   -113   -184       C  
ATOM   3917  CD2 LEU A 524      89.113  32.150  54.099  1.00 42.03           C  
ANISOU 3917  CD2 LEU A 524     4950   5638   5381    633    -41   -262       C  
ATOM   3918  N   GLY A 525      84.011  32.460  53.698  1.00 16.56           N  
ANISOU 3918  N   GLY A 525     1957   2164   2170    364    -60   -224       N  
ATOM   3919  CA  GLY A 525      83.033  31.704  52.937  1.00 17.47           C  
ANISOU 3919  CA  GLY A 525     2141   2224   2275    337    -57   -251       C  
ATOM   3920  C   GLY A 525      82.259  32.491  51.904  1.00 18.42           C  
ANISOU 3920  C   GLY A 525     2239   2385   2374    270    -48   -253       C  
ATOM   3921  O   GLY A 525      81.514  31.882  51.131  1.00 20.31           O  
ANISOU 3921  O   GLY A 525     2525   2599   2593    241    -47   -280       O  
ATOM   3922  N   ALA A 526      82.414  33.815  51.856  1.00 16.24           N  
ANISOU 3922  N   ALA A 526     1901   2173   2098    242    -42   -224       N  
ATOM   3923  CA  ALA A 526      81.557  34.626  50.995  1.00 16.96           C  
ANISOU 3923  CA  ALA A 526     1979   2296   2171    185    -40   -211       C  
ATOM   3924  C   ALA A 526      81.841  34.386  49.516  1.00 15.88           C  
ANISOU 3924  C   ALA A 526     1846   2198   1991    188    -24   -247       C  
ATOM   3925  O   ALA A 526      82.975  34.095  49.109  1.00 18.58           O  
ANISOU 3925  O   ALA A 526     2173   2568   2318    232     -1   -278       O  
ATOM   3926  CB  ALA A 526      81.721  36.113  51.300  1.00 15.18           C  
ANISOU 3926  CB  ALA A 526     1703   2113   1953    160    -31   -169       C  
ATOM   3927  N   THR A 527      80.780  34.523  48.716  1.00 15.29           N  
ANISOU 3927  N   THR A 527     1786   2133   1892    138    -35   -243       N  
ATOM   3928  CA  THR A 527      80.882  34.427  47.264  1.00 16.03           C  
ANISOU 3928  CA  THR A 527     1886   2272   1933    123    -23   -272       C  
ATOM   3929  C   THR A 527      81.366  35.742  46.676  1.00 15.65           C  
ANISOU 3929  C   THR A 527     1792   2292   1862    110     -9   -240       C  
ATOM   3930  O   THR A 527      80.775  36.795  46.932  1.00 16.98           O  
ANISOU 3930  O   THR A 527     1940   2470   2042     84    -21   -188       O  
ATOM   3931  CB  THR A 527      79.515  34.083  46.690  1.00 18.03           C  
ANISOU 3931  CB  THR A 527     2169   2522   2161     67    -49   -274       C  
ATOM   3932  OG1 THR A 527      79.115  32.789  47.156  1.00 22.13           O  
ANISOU 3932  OG1 THR A 527     2744   2973   2692     65    -55   -310       O  
ATOM   3933  CG2 THR A 527      79.545  34.097  45.150  1.00 18.20           C  
ANISOU 3933  CG2 THR A 527     2197   2602   2117     39    -41   -298       C  
ATOM   3934  N   LYS A 528      82.407  35.671  45.844  1.00 16.93           N  
ANISOU 3934  N   LYS A 528     1944   2500   1988    125     22   -274       N  
ATOM   3935  CA  LYS A 528      82.916  36.814  45.097  1.00 16.17           C  
ANISOU 3935  CA  LYS A 528     1818   2472   1855     99     43   -252       C  
ATOM   3936  C   LYS A 528      82.500  36.644  43.645  1.00 18.78           C  
ANISOU 3936  C   LYS A 528     2174   2841   2120     62     43   -269       C  
ATOM   3937  O   LYS A 528      82.840  35.638  43.016  1.00 24.15           O  
ANISOU 3937  O   LYS A 528     2878   3525   2773     74     61   -330       O  
ATOM   3938  CB  LYS A 528      84.437  36.918  45.209  1.00 19.69           C  
ANISOU 3938  CB  LYS A 528     2223   2960   2299    131     83   -279       C  
ATOM   3939  CG  LYS A 528      84.901  37.151  46.647  1.00 21.65           C  
ANISOU 3939  CG  LYS A 528     2439   3186   2600    159     78   -259       C  
ATOM   3940  CD  LYS A 528      86.349  37.568  46.698  1.00 28.31           C  
ANISOU 3940  CD  LYS A 528     3225   4100   3432    171    113   -277       C  
ATOM   3941  CE  LYS A 528      87.207  36.508  47.347  1.00 40.21           C  
ANISOU 3941  CE  LYS A 528     4708   5605   4966    248    115   -317       C  
ATOM   3942  NZ  LYS A 528      88.582  37.038  47.598  1.00 44.39           N  
ANISOU 3942  NZ  LYS A 528     5159   6220   5485    255    144   -327       N  
ATOM   3943  N   LEU A 529      81.741  37.606  43.139  1.00 17.07           N  
ANISOU 3943  N   LEU A 529     1958   2650   1877     20     23   -215       N  
ATOM   3944  CA  LEU A 529      81.290  37.546  41.762  1.00 18.55           C  
ANISOU 3944  CA  LEU A 529     2168   2886   1992    -21     14   -221       C  
ATOM   3945  C   LEU A 529      82.428  37.878  40.814  1.00 20.15           C  
ANISOU 3945  C   LEU A 529     2368   3151   2139    -35     59   -244       C  
ATOM   3946  O   LEU A 529      83.335  38.652  41.131  1.00 20.02           O  
ANISOU 3946  O   LEU A 529     2324   3151   2133    -30     89   -228       O  
ATOM   3947  CB  LEU A 529      80.123  38.501  41.535  1.00 18.44           C  
ANISOU 3947  CB  LEU A 529     2154   2887   1967    -50    -27   -146       C  
ATOM   3948  CG  LEU A 529      78.899  38.195  42.410  1.00 22.95           C  
ANISOU 3948  CG  LEU A 529     2718   3414   2589    -43    -68   -127       C  
ATOM   3949  CD1 LEU A 529      77.814  39.245  42.208  1.00 21.78           C  
ANISOU 3949  CD1 LEU A 529     2553   3288   2433    -53   -105    -50       C  
ATOM   3950  CD2 LEU A 529      78.342  36.789  42.170  1.00 20.16           C  
ANISOU 3950  CD2 LEU A 529     2390   3051   2220    -63    -84   -186       C  
ATOM   3951  N   GLU A 530      82.357  37.291  39.626  1.00 18.29           N  
ANISOU 3951  N   GLU A 530     2159   2954   1835    -64     66   -285       N  
ATOM   3952  CA  GLU A 530      83.433  37.450  38.664  1.00 19.26           C  
ANISOU 3952  CA  GLU A 530     2280   3142   1897    -83    115   -320       C  
ATOM   3953  C   GLU A 530      83.632  38.914  38.280  1.00 19.59           C  
ANISOU 3953  C   GLU A 530     2313   3226   1902   -123    121   -251       C  
ATOM   3954  O   GLU A 530      82.678  39.683  38.138  1.00 22.08           O  
ANISOU 3954  O   GLU A 530     2646   3538   2207   -146     80   -179       O  
ATOM   3955  CB  GLU A 530      83.165  36.616  37.414  1.00 21.15           C  
ANISOU 3955  CB  GLU A 530     2560   3417   2060   -119    121   -376       C  
ATOM   3956  CG  GLU A 530      84.400  36.563  36.521  1.00 25.28           C  
ANISOU 3956  CG  GLU A 530     3078   4004   2524   -130    186   -432       C  
ATOM   3957  CD  GLU A 530      84.361  35.471  35.484  0.50 26.88           C  
ANISOU 3957  CD  GLU A 530     3324   4227   2662   -153    209   -513       C  
ATOM   3958  OE1 GLU A 530      83.280  34.886  35.273  0.50 26.61           O  
ANISOU 3958  OE1 GLU A 530     3330   4168   2612   -181    168   -518       O  
ATOM   3959  OE2 GLU A 530      85.421  35.221  34.866  0.50 24.12           O1-
ANISOU 3959  OE2 GLU A 530     2967   3923   2274   -149    272   -577       O1-
ATOM   3960  N   ILE A 531      84.902  39.284  38.147  1.00 19.17           N  
ANISOU 3960  N   ILE A 531     2236   3216   1833   -128    176   -275       N  
ATOM   3961  CA  ILE A 531      85.448  40.481  37.509  1.00 19.54           C  
ANISOU 3961  CA  ILE A 531     2288   3316   1821   -183    205   -235       C  
ATOM   3962  C   ILE A 531      85.332  41.727  38.389  1.00 19.05           C  
ANISOU 3962  C   ILE A 531     2222   3214   1803   -189    195   -158       C  
ATOM   3963  O   ILE A 531      86.050  42.711  38.165  1.00 19.35           O  
ANISOU 3963  O   ILE A 531     2263   3283   1806   -235    232   -134       O  
ATOM   3964  CB  ILE A 531      84.850  40.716  36.100  1.00 22.13           C  
ANISOU 3964  CB  ILE A 531     2666   3690   2053   -241    190   -210       C  
ATOM   3965  CG1 ILE A 531      85.969  41.223  35.173  1.00 22.01           C  
ANISOU 3965  CG1 ILE A 531     2653   3752   1958   -298    252   -230       C  
ATOM   3966  CG2 ILE A 531      83.727  41.737  36.117  1.00 25.56           C  
ANISOU 3966  CG2 ILE A 531     3132   4095   2485   -256    135   -107       C  
ATOM   3967  CD1 ILE A 531      85.685  41.058  33.717  1.00 23.43           C  
ANISOU 3967  CD1 ILE A 531     2879   3992   2031   -355    252   -239       C  
ATOM   3968  N   TYR A 532      84.503  41.678  39.435  1.00 18.38           N  
ANISOU 3968  N   TYR A 532     2133   3060   1792   -148    152   -126       N  
ATOM   3969  CA  TYR A 532      84.514  42.750  40.417  1.00 17.96           C  
ANISOU 3969  CA  TYR A 532     2075   2962   1786   -149    154    -71       C  
ATOM   3970  C   TYR A 532      85.800  42.693  41.224  1.00 18.58           C  
ANISOU 3970  C   TYR A 532     2105   3059   1895   -142    198   -115       C  
ATOM   3971  O   TYR A 532      86.448  41.652  41.340  1.00 20.99           O  
ANISOU 3971  O   TYR A 532     2372   3390   2212   -108    213   -183       O  
ATOM   3972  CB  TYR A 532      83.329  42.647  41.385  1.00 17.34           C  
ANISOU 3972  CB  TYR A 532     1999   2812   1778   -108    105    -35       C  
ATOM   3973  CG  TYR A 532      81.966  42.884  40.752  1.00 17.67           C  
ANISOU 3973  CG  TYR A 532     2071   2846   1795   -110     55     20       C  
ATOM   3974  CD1 TYR A 532      81.602  44.132  40.266  1.00 29.39           C  
ANISOU 3974  CD1 TYR A 532     3592   4327   3247   -130     50     98       C  
ATOM   3975  CD2 TYR A 532      81.051  41.850  40.657  1.00 19.26           C  
ANISOU 3975  CD2 TYR A 532     2267   3046   2006    -91     14     -4       C  
ATOM   3976  CE1 TYR A 532      80.346  44.339  39.693  1.00 28.80           C  
ANISOU 3976  CE1 TYR A 532     3535   4258   3149   -120     -2    154       C  
ATOM   3977  CE2 TYR A 532      79.785  42.049  40.100  1.00 20.57           C  
ANISOU 3977  CE2 TYR A 532     2445   3225   2146    -96    -37     46       C  
ATOM   3978  CZ  TYR A 532      79.449  43.290  39.625  1.00 24.62           C  
ANISOU 3978  CZ  TYR A 532     2981   3744   2628   -103    -47    126       C  
ATOM   3979  OH  TYR A 532      78.201  43.461  39.057  1.00 29.44           O  
ANISOU 3979  OH  TYR A 532     3594   4381   3211    -97   -104    180       O  
ATOM   3980  N   THR A 533      86.142  43.829  41.814  1.00 19.06           N  
ANISOU 3980  N   THR A 533     2170   3104   1969   -174    219    -75       N  
ATOM   3981  CA  THR A 533      87.308  43.958  42.674  1.00 17.70           C  
ANISOU 3981  CA  THR A 533     1946   2959   1820   -182    255   -108       C  
ATOM   3982  C   THR A 533      86.858  43.901  44.127  1.00 20.11           C  
ANISOU 3982  C   THR A 533     2239   3197   2204   -144    227    -92       C  
ATOM   3983  O   THR A 533      85.966  44.655  44.523  1.00 20.49           O  
ANISOU 3983  O   THR A 533     2329   3179   2276   -151    208    -35       O  
ATOM   3984  CB  THR A 533      88.026  45.275  42.399  1.00 24.72           C  
ANISOU 3984  CB  THR A 533     2854   3878   2661   -265    303    -81       C  
ATOM   3985  OG1 THR A 533      88.497  45.278  41.049  1.00 26.32           O  
ANISOU 3985  OG1 THR A 533     3068   4150   2783   -307    334    -99       O  
ATOM   3986  CG2 THR A 533      89.202  45.443  43.336  1.00 27.28           C  
ANISOU 3986  CG2 THR A 533     3117   4245   3005   -286    337   -117       C  
ATOM   3987  N   TYR A 534      87.461  43.002  44.911  1.00 18.14           N  
ANISOU 3987  N   TYR A 534     1935   2965   1992   -100    224   -142       N  
ATOM   3988  CA  TYR A 534      87.094  42.853  46.310  1.00 21.49           C  
ANISOU 3988  CA  TYR A 534     2350   3333   2483    -68    197   -130       C  
ATOM   3989  C   TYR A 534      88.306  43.088  47.197  1.00 21.25           C  
ANISOU 3989  C   TYR A 534     2262   3352   2460    -84    222   -153       C  
ATOM   3990  O   TYR A 534      89.437  42.814  46.789  1.00 24.39           O  
ANISOU 3990  O   TYR A 534     2606   3835   2825    -86    251   -197       O  
ATOM   3991  CB  TYR A 534      86.534  41.461  46.624  1.00 18.63           C  
ANISOU 3991  CB  TYR A 534     1985   2933   2159      3    158   -157       C  
ATOM   3992  CG  TYR A 534      85.216  41.161  45.965  1.00 17.85           C  
ANISOU 3992  CG  TYR A 534     1936   2791   2057      9    126   -137       C  
ATOM   3993  CD1 TYR A 534      84.016  41.468  46.590  1.00 15.53           C  
ANISOU 3993  CD1 TYR A 534     1669   2432   1801     10     95    -92       C  
ATOM   3994  CD2 TYR A 534      85.170  40.577  44.710  1.00 18.05           C  
ANISOU 3994  CD2 TYR A 534     1974   2849   2033      9    129   -165       C  
ATOM   3995  CE1 TYR A 534      82.812  41.190  45.999  1.00 17.07           C  
ANISOU 3995  CE1 TYR A 534     1892   2605   1988     14     63    -74       C  
ATOM   3996  CE2 TYR A 534      83.971  40.290  44.101  1.00 20.17           C  
ANISOU 3996  CE2 TYR A 534     2282   3093   2290      5     96   -148       C  
ATOM   3997  CZ  TYR A 534      82.789  40.604  44.736  1.00 17.15           C  
ANISOU 3997  CZ  TYR A 534     1915   2656   1946      7     60   -101       C  
ATOM   3998  OH  TYR A 534      81.577  40.333  44.136  1.00 18.95           O  
ANISOU 3998  OH  TYR A 534     2166   2877   2158      0     24    -85       O  
ATOM   3999  N   PRO A 535      88.103  43.593  48.421  1.00 19.57           N  
ANISOU 3999  N   PRO A 535     2053   3097   2285    -98    212   -127       N  
ATOM   4000  CA  PRO A 535      86.816  44.083  48.928  1.00 16.81           C  
ANISOU 4000  CA  PRO A 535     1761   2654   1972   -100    190    -78       C  
ATOM   4001  C   PRO A 535      86.437  45.409  48.287  1.00 17.17           C  
ANISOU 4001  C   PRO A 535     1863   2673   1987   -156    216    -31       C  
ATOM   4002  O   PRO A 535      87.298  46.056  47.700  1.00 20.30           O  
ANISOU 4002  O   PRO A 535     2257   3121   2334   -212    255    -36       O  
ATOM   4003  CB  PRO A 535      87.075  44.259  50.424  1.00 20.72           C  
ANISOU 4003  CB  PRO A 535     2236   3134   2504   -108    187    -78       C  
ATOM   4004  CG  PRO A 535      88.531  44.565  50.499  1.00 22.68           C  
ANISOU 4004  CG  PRO A 535     2429   3474   2716   -151    219   -109       C  
ATOM   4005  CD  PRO A 535      89.171  43.728  49.429  1.00 23.58           C  
ANISOU 4005  CD  PRO A 535     2503   3659   2799   -115    225   -149       C  
ATOM   4006  N   ASN A 536      85.167  45.806  48.381  1.00 16.77           N  
ANISOU 4006  N   ASN A 536     1863   2547   1964   -140    195     16       N  
ATOM   4007  CA  ASN A 536      84.770  47.114  47.879  1.00 17.33           C  
ANISOU 4007  CA  ASN A 536     1996   2578   2011   -178    218     70       C  
ATOM   4008  C   ASN A 536      83.682  47.653  48.794  1.00 18.95           C  
ANISOU 4008  C   ASN A 536     2234   2696   2270   -155    209    108       C  
ATOM   4009  O   ASN A 536      83.123  46.925  49.614  1.00 18.14           O  
ANISOU 4009  O   ASN A 536     2106   2573   2215   -115    180     93       O  
ATOM   4010  CB  ASN A 536      84.316  47.053  46.409  1.00 19.67           C  
ANISOU 4010  CB  ASN A 536     2319   2895   2261   -169    204     94       C  
ATOM   4011  CG  ASN A 536      83.119  46.163  46.202  1.00 23.57           C  
ANISOU 4011  CG  ASN A 536     2803   3372   2780   -107    151    100       C  
ATOM   4012  OD1 ASN A 536      82.017  46.491  46.634  1.00 20.18           O  
ANISOU 4012  OD1 ASN A 536     2393   2886   2389    -78    129    139       O  
ATOM   4013  ND2 ASN A 536      83.311  45.048  45.490  1.00 22.03           N  
ANISOU 4013  ND2 ASN A 536     2581   3230   2560    -91    133     58       N  
ATOM   4014  N   VAL A 537      83.404  48.956  48.678  1.00 19.74           N  
ANISOU 4014  N   VAL A 537     2398   2741   2361   -183    239    156       N  
ATOM   4015  CA  VAL A 537      82.519  49.584  49.664  1.00 17.93           C  
ANISOU 4015  CA  VAL A 537     2202   2428   2184   -162    244    184       C  
ATOM   4016  C   VAL A 537      81.050  49.298  49.412  1.00 16.29           C  
ANISOU 4016  C   VAL A 537     1993   2188   2009    -88    201    220       C  
ATOM   4017  O   VAL A 537      80.200  49.744  50.192  1.00 17.36           O  
ANISOU 4017  O   VAL A 537     2145   2261   2192    -59    206    240       O  
ATOM   4018  CB  VAL A 537      82.720  51.110  49.724  1.00 23.77           C  
ANISOU 4018  CB  VAL A 537     3022   3102   2906   -211    300    221       C  
ATOM   4019  CG1 VAL A 537      84.126  51.442  50.237  1.00 28.81           C  
ANISOU 4019  CG1 VAL A 537     3655   3777   3514   -302    346    178       C  
ATOM   4020  CG2 VAL A 537      82.490  51.715  48.372  1.00 22.64           C  
ANISOU 4020  CG2 VAL A 537     2935   2952   2717   -207    301    275       C  
ATOM   4021  N   SER A 538      80.712  48.572  48.347  1.00 16.52           N  
ANISOU 4021  N   SER A 538     1999   2266   2011    -60    161    224       N  
ATOM   4022  CA ASER A 538      79.327  48.194  48.091  0.42 20.22           C  
ANISOU 4022  CA ASER A 538     2452   2729   2503      0    114    252       C  
ATOM   4023  CA BSER A 538      79.333  48.193  48.084  0.58 15.63           C  
ANISOU 4023  CA BSER A 538     1870   2147   1920      0    114    252       C  
ATOM   4024  C   SER A 538      79.015  46.785  48.573  1.00 16.06           C  
ANISOU 4024  C   SER A 538     1867   2230   2003     18     78    203       C  
ATOM   4025  O   SER A 538      78.052  46.587  49.330  1.00 16.12           O  
ANISOU 4025  O   SER A 538     1857   2209   2059     48     62    206       O  
ATOM   4026  CB ASER A 538      79.009  48.308  46.594  0.42 21.13           C  
ANISOU 4026  CB ASER A 538     2585   2882   2561      9     87    292       C  
ATOM   4027  CB BSER A 538      79.061  48.316  46.579  0.58 21.67           C  
ANISOU 4027  CB BSER A 538     2654   2952   2627      7     89    291       C  
ATOM   4028  OG ASER A 538      78.869  49.661  46.211  0.42 23.92           O  
ANISOU 4028  OG ASER A 538     3004   3189   2896     12    111    358       O  
ATOM   4029  OG BSER A 538      77.762  47.891  46.260  0.58 21.07           O  
ANISOU 4029  OG BSER A 538     2550   2891   2563     57     37    315       O  
ATOM   4030  N   GLN A 539      79.815  45.801  48.146  1.00 15.37           N  
ANISOU 4030  N   GLN A 539     1757   2197   1887      1     70    155       N  
ATOM   4031  CA  GLN A 539      79.613  44.401  48.497  1.00 14.65           C  
ANISOU 4031  CA  GLN A 539     1630   2122   1815     18     40    108       C  
ATOM   4032  C   GLN A 539      80.457  43.940  49.679  1.00 15.53           C  
ANISOU 4032  C   GLN A 539     1723   2221   1955     10     57     66       C  
ATOM   4033  O   GLN A 539      80.306  42.794  50.120  1.00 17.18           O  
ANISOU 4033  O   GLN A 539     1917   2429   2183     28     34     32       O  
ATOM   4034  CB  GLN A 539      79.940  43.506  47.297  1.00 16.63           C  
ANISOU 4034  CB  GLN A 539     1874   2429   2014     14     23     77       C  
ATOM   4035  CG  GLN A 539      79.128  43.741  46.059  1.00 21.05           C  
ANISOU 4035  CG  GLN A 539     2448   3019   2532     15     -3    113       C  
ATOM   4036  CD  GLN A 539      79.576  42.780  44.986  1.00 26.48           C  
ANISOU 4036  CD  GLN A 539     3134   3763   3165      0    -11     69       C  
ATOM   4037  OE1 GLN A 539      79.633  41.569  45.223  1.00 28.46           O  
ANISOU 4037  OE1 GLN A 539     3372   4014   3428      8    -21     16       O  
ATOM   4038  NE2 GLN A 539      79.962  43.309  43.835  1.00 29.41           N  
ANISOU 4038  NE2 GLN A 539     3526   4175   3474    -24      0     88       N  
ATOM   4039  N   GLY A 540      81.357  44.772  50.179  1.00 14.31           N  
ANISOU 4039  N   GLY A 540     1576   2062   1798    -20     94     68       N  
ATOM   4040  CA  GLY A 540      82.292  44.285  51.179  1.00 17.47           C  
ANISOU 4040  CA  GLY A 540     1950   2476   2212    -28    103     30       C  
ATOM   4041  C   GLY A 540      83.160  43.186  50.595  1.00 14.25           C  
ANISOU 4041  C   GLY A 540     1511   2126   1778    -10     93    -15       C  
ATOM   4042  O   GLY A 540      83.774  43.349  49.530  1.00 14.64           O  
ANISOU 4042  O   GLY A 540     1557   2223   1783    -24    109    -23       O  
ATOM   4043  N   TYR A 541      83.225  42.056  51.301  1.00 15.75           N  
ANISOU 4043  N   TYR A 541     1630   2691   1662   -504   -319    109       N  
ATOM   4044  CA  TYR A 541      83.970  40.884  50.847  1.00 15.92           C  
ANISOU 4044  CA  TYR A 541     1521   2787   1742   -395   -275     75       C  
ATOM   4045  C   TYR A 541      83.125  39.880  50.067  1.00 17.76           C  
ANISOU 4045  C   TYR A 541     1784   2992   1973   -318   -156    -29       C  
ATOM   4046  O   TYR A 541      83.647  38.827  49.676  1.00 20.12           O  
ANISOU 4046  O   TYR A 541     2012   3318   2315   -210   -104    -80       O  
ATOM   4047  CB  TYR A 541      84.615  40.189  52.044  1.00 15.43           C  
ANISOU 4047  CB  TYR A 541     1488   2649   1726   -325   -371    111       C  
ATOM   4048  CG  TYR A 541      85.781  40.954  52.583  1.00 19.47           C  
ANISOU 4048  CG  TYR A 541     1912   3223   2261   -397   -517    213       C  
ATOM   4049  CD1 TYR A 541      85.611  41.893  53.594  1.00 20.37           C  
ANISOU 4049  CD1 TYR A 541     2184   3249   2308   -505   -643    261       C  
ATOM   4050  CD2 TYR A 541      87.066  40.742  52.083  1.00 20.63           C  
ANISOU 4050  CD2 TYR A 541     1819   3513   2506   -360   -530    261       C  
ATOM   4051  CE1 TYR A 541      86.701  42.601  54.098  1.00 23.20           C  
ANISOU 4051  CE1 TYR A 541     2474   3652   2690   -599   -815    353       C  
ATOM   4052  CE2 TYR A 541      88.148  41.442  52.577  1.00 24.38           C  
ANISOU 4052  CE2 TYR A 541     2182   4050   3033   -449   -688    372       C  
ATOM   4053  CZ  TYR A 541      87.962  42.373  53.582  1.00 21.83           C  
ANISOU 4053  CZ  TYR A 541     2036   3621   2637   -575   -841    413       C  
ATOM   4054  OH  TYR A 541      89.050  43.074  54.061  1.00 27.65           O  
ANISOU 4054  OH  TYR A 541     2732   4342   3432   -640   -955    485       O  
ATOM   4055  N   GLY A 542      81.854  40.175  49.797  1.00 13.97           N  
ANISOU 4055  N   GLY A 542     1399   2453   1455   -368   -119    -61       N  
ATOM   4056  CA  GLY A 542      81.061  39.279  48.981  1.00 13.73           C  
ANISOU 4056  CA  GLY A 542     1391   2400   1426   -328    -43   -155       C  
ATOM   4057  C   GLY A 542      79.768  38.879  49.653  1.00 14.75           C  
ANISOU 4057  C   GLY A 542     1644   2370   1590   -333    -33   -172       C  
ATOM   4058  O   GLY A 542      79.359  39.439  50.679  1.00 14.80           O  
ANISOU 4058  O   GLY A 542     1732   2293   1599   -364    -54   -113       O  
ATOM   4059  N   ILE A 543      79.119  37.874  49.062  1.00 14.27           N  
ANISOU 4059  N   ILE A 543     1604   2262   1556   -306      9   -255       N  
ATOM   4060  CA  ILE A 543      77.762  37.468  49.410  1.00 13.46           C  
ANISOU 4060  CA  ILE A 543     1576   2026   1511   -338     28   -265       C  
ATOM   4061  C   ILE A 543      77.798  36.293  50.374  1.00 15.41           C  
ANISOU 4061  C   ILE A 543     1907   2130   1820   -271     47   -271       C  
ATOM   4062  O   ILE A 543      78.482  35.294  50.119  1.00 16.75           O  
ANISOU 4062  O   ILE A 543     2075   2283   2007   -192     50   -330       O  
ATOM   4063  CB  ILE A 543      76.964  37.091  48.147  1.00 15.98           C  
ANISOU 4063  CB  ILE A 543     1875   2367   1829   -383     25   -342       C  
ATOM   4064  CG1 ILE A 543      77.018  38.221  47.126  1.00 19.34           C  
ANISOU 4064  CG1 ILE A 543     2236   2939   2171   -446     -6   -319       C  
ATOM   4065  CG2 ILE A 543      75.521  36.756  48.531  1.00 21.03           C  
ANISOU 4065  CG2 ILE A 543     2547   2876   2568   -438     31   -326       C  
ATOM   4066  CD1 ILE A 543      76.601  37.776  45.701  1.00 23.31           C  
ANISOU 4066  CD1 ILE A 543     2745   3498   2616   -484    -32   -407       C  
ATOM   4067  N   LEU A 544      77.041  36.406  51.464  1.00 14.81           N  
ANISOU 4067  N   LEU A 544     1912   1942   1775   -296     74   -207       N  
ATOM   4068  CA  LEU A 544      76.860  35.330  52.434  1.00 16.27           C  
ANISOU 4068  CA  LEU A 544     2200   1974   2009   -255    103   -186       C  
ATOM   4069  C   LEU A 544      76.674  33.978  51.753  1.00 18.45           C  
ANISOU 4069  C   LEU A 544     2477   2175   2358   -231    108   -271       C  
ATOM   4070  O   LEU A 544      75.899  33.844  50.797  1.00 18.62           O  
ANISOU 4070  O   LEU A 544     2455   2206   2412   -294    109   -333       O  
ATOM   4071  CB  LEU A 544      75.643  35.643  53.307  1.00 14.83           C  
ANISOU 4071  CB  LEU A 544     2086   1694   1856   -310    180   -116       C  
ATOM   4072  CG  LEU A 544      75.236  34.564  54.307  1.00 14.75           C  
ANISOU 4072  CG  LEU A 544     2194   1520   1891   -294    237    -71       C  
ATOM   4073  CD1 LEU A 544      76.145  34.580  55.523  1.00 18.71           C  
ANISOU 4073  CD1 LEU A 544     2827   1986   2297   -233    205     -4       C  
ATOM   4074  CD2 LEU A 544      73.778  34.787  54.721  1.00 16.72           C  
ANISOU 4074  CD2 LEU A 544     2448   1696   2209   -364    355    -15       C  
ATOM   4075  N   ASN A 545      77.396  32.970  52.241  1.00 19.77           N  
ANISOU 4075  N   ASN A 545     2708   2255   2550   -141     95   -273       N  
ATOM   4076  CA  ASN A 545      77.256  31.614  51.700  1.00 19.49           C  
ANISOU 4076  CA  ASN A 545     2713   2102   2591   -107    102   -360       C  
ATOM   4077  C   ASN A 545      77.399  30.621  52.847  1.00 25.39           C  
ANISOU 4077  C   ASN A 545     3582   2672   3393    -48    104   -291       C  
ATOM   4078  O   ASN A 545      78.518  30.264  53.227  1.00 22.95           O  
ANISOU 4078  O   ASN A 545     3285   2355   3079     70     62   -269       O  
ATOM   4079  CB  ASN A 545      78.274  31.342  50.606  1.00 21.68           C  
ANISOU 4079  CB  ASN A 545     2927   2471   2839    -17     88   -469       C  
ATOM   4080  CG  ASN A 545      77.954  30.089  49.821  1.00 28.11           C  
ANISOU 4080  CG  ASN A 545     3814   3159   3709      2     99   -595       C  
ATOM   4081  OD1 ASN A 545      77.726  29.021  50.392  1.00 23.59           O  
ANISOU 4081  OD1 ASN A 545     3345   2394   3224     28     99   -586       O  
ATOM   4082  ND2 ASN A 545      77.919  30.217  48.504  1.00 35.11           N  
ANISOU 4082  ND2 ASN A 545     4671   4139   4532    -21    103   -713       N  
ATOM   4083  N   LEU A 546      76.258  30.166  53.369  1.00 26.91           N  
ANISOU 4083  N   LEU A 546     3853   2723   3650   -134    151   -244       N  
ATOM   4084  CA  LEU A 546      76.247  29.247  54.502  1.00 23.67           C  
ANISOU 4084  CA  LEU A 546     3583   2132   3280   -101    166   -152       C  
ATOM   4085  C   LEU A 546      77.052  27.985  54.208  1.00 23.33           C  
ANISOU 4085  C   LEU A 546     3592   1969   3302     16    117   -213       C  
ATOM   4086  O   LEU A 546      77.908  27.579  55.004  1.00 24.17           O  
ANISOU 4086  O   LEU A 546     3768   2016   3402    125     73   -138       O  
ATOM   4087  CB  LEU A 546      74.796  28.895  54.851  1.00 29.25           C  
ANISOU 4087  CB  LEU A 546     4333   2710   4070   -232    250    -97       C  
ATOM   4088  CG  LEU A 546      74.526  27.756  55.831  1.00 34.03           C  
ANISOU 4088  CG  LEU A 546     5093   3099   4739   -237    286      2       C  
ATOM   4089  CD1 LEU A 546      75.186  28.057  57.164  1.00 36.92           C  
ANISOU 4089  CD1 LEU A 546     5579   3466   4982   -164    287    131       C  
ATOM   4090  CD2 LEU A 546      73.021  27.566  56.003  1.00 34.81           C  
ANISOU 4090  CD2 LEU A 546     5176   3107   4942   -393    389     62       C  
ATOM   4091  N   LYS A 547      76.775  27.339  53.074  1.00 20.37           N  
ANISOU 4091  N   LYS A 547     3201   1545   2994      1    114   -348       N  
ATOM   4092  CA  LYS A 547      77.424  26.068  52.769  1.00 21.70           C  
ANISOU 4092  CA  LYS A 547     3450   1558   3236    122     89   -425       C  
ATOM   4093  C   LYS A 547      78.938  26.221  52.723  1.00 24.25           C  
ANISOU 4093  C   LYS A 547     3703   1987   3524    309     60   -434       C  
ATOM   4094  O   LYS A 547      79.675  25.408  53.295  1.00 24.79           O  
ANISOU 4094  O   LYS A 547     3835   1928   3657    445     28   -385       O  
ATOM   4095  CB  LYS A 547      76.904  25.521  51.439  1.00 28.95           C  
ANISOU 4095  CB  LYS A 547     4385   2424   4191     67     86   -598       C  
ATOM   4096  CG  LYS A 547      77.541  24.203  51.027  1.00 31.90           C  
ANISOU 4096  CG  LYS A 547     4873   2611   4637    204     76   -709       C  
ATOM   4097  CD  LYS A 547      77.022  23.729  49.668  1.00 33.64           C  
ANISOU 4097  CD  LYS A 547     5153   2778   4853    136     63   -905       C  
ATOM   4098  N   ASN A 548      79.424  27.260  52.044  1.00 22.50           N  
ANISOU 4098  N   ASN A 548     3339   1995   3217    315     67   -481       N  
ATOM   4099  CA AASN A 548      80.868  27.428  51.914  0.50 22.51           C  
ANISOU 4099  CA AASN A 548     3228   2113   3211    478     51   -480       C  
ATOM   4100  CA BASN A 548      80.866  27.420  51.914  0.50 22.51           C  
ANISOU 4100  CA BASN A 548     3230   2112   3212    479     51   -481       C  
ATOM   4101  C   ASN A 548      81.501  27.844  53.228  1.00 23.45           C  
ANISOU 4101  C   ASN A 548     3333   2258   3319    514    -28   -310       C  
ATOM   4102  O   ASN A 548      82.656  27.495  53.493  1.00 24.71           O  
ANISOU 4102  O   ASN A 548     3431   2420   3536    668    -78   -267       O  
ATOM   4103  CB AASN A 548      81.203  28.453  50.833  0.50 20.53           C  
ANISOU 4103  CB AASN A 548     2829   2102   2870    452     89   -555       C  
ATOM   4104  CB BASN A 548      81.176  28.416  50.800  0.50 20.57           C  
ANISOU 4104  CB BASN A 548     2838   2101   2876    451     91   -561       C  
ATOM   4105  CG AASN A 548      82.641  28.344  50.371  0.50 26.19           C  
ANISOU 4105  CG AASN A 548     3414   2923   3615    628    118   -586       C  
ATOM   4106  CG BASN A 548      80.873  27.849  49.427  0.50 29.19           C  
ANISOU 4106  CG BASN A 548     3971   3168   3950    457    156   -742       C  
ATOM   4107  OD1AASN A 548      83.431  29.282  50.504  0.50 26.93           O  
ANISOU 4107  OD1AASN A 548     3356   3199   3678    635     95   -508       O  
ATOM   4108  OD1BASN A 548      80.796  26.632  49.254  0.50 34.84           O  
ANISOU 4108  OD1BASN A 548     4806   3691   4739    531    171   -827       O  
ATOM   4109  ND2AASN A 548      82.997  27.180  49.852  0.50 25.50           N  
ANISOU 4109  ND2AASN A 548     3380   2708   3600    773    172   -695       N  
ATOM   4110  ND2BASN A 548      80.696  28.725  48.446  0.50 34.10           N  
ANISOU 4110  ND2BASN A 548     4521   3971   4463    376    184   -802       N  
ATOM   4111  N   THR A 549      80.759  28.576  54.065  1.00 19.97           N  
ANISOU 4111  N   THR A 549     2952   1830   2805    379    -44   -211       N  
ATOM   4112  CA  THR A 549      81.282  28.935  55.376  1.00 20.12           C  
ANISOU 4112  CA  THR A 549     3019   1851   2775    397   -132    -58       C  
ATOM   4113  C   THR A 549      81.458  27.698  56.250  1.00 25.54           C  
ANISOU 4113  C   THR A 549     3851   2324   3531    489   -179     27       C  
ATOM   4114  O   THR A 549      82.478  27.558  56.931  1.00 27.65           O  
ANISOU 4114  O   THR A 549     4108   2590   3808    594   -292    124       O  
ATOM   4115  CB  THR A 549      80.353  29.951  56.042  1.00 20.59           C  
ANISOU 4115  CB  THR A 549     3153   1948   2722    243   -104      7       C  
ATOM   4116  OG1 THR A 549      80.240  31.103  55.195  1.00 24.88           O  
ANISOU 4116  OG1 THR A 549     3563   2672   3217    171    -76    -60       O  
ATOM   4117  CG2 THR A 549      80.917  30.385  57.385  1.00 19.98           C  
ANISOU 4117  CG2 THR A 549     3170   1871   2549    252   -205    147       C  
ATOM   4118  N   ILE A 550      80.479  26.785  56.242  1.00 26.38           N  
ANISOU 4118  N   ILE A 550     4088   2241   3695    441   -109      4       N  
ATOM   4119  CA  ILE A 550      80.633  25.524  56.966  1.00 28.16           C  
ANISOU 4119  CA  ILE A 550     4464   2236   4000    526   -150     88       C  
ATOM   4120  C   ILE A 550      81.850  24.765  56.456  1.00 31.18           C  
ANISOU 4120  C   ILE A 550     4766   2583   4500    734   -206     36       C  
ATOM   4121  O   ILE A 550      82.629  24.206  57.240  1.00 31.76           O  
ANISOU 4121  O   ILE A 550     4887   2561   4620    862   -307    154       O  
ATOM   4122  CB  ILE A 550      79.353  24.675  56.849  1.00 30.18           C  
ANISOU 4122  CB  ILE A 550     4852   2289   4326    416    -60     61       C  
ATOM   4123  CG1 ILE A 550      78.194  25.333  57.610  1.00 36.75           C  
ANISOU 4123  CG1 ILE A 550     5755   3140   5068    237     17    158       C  
ATOM   4124  CG2 ILE A 550      79.610  23.255  57.362  1.00 29.24           C  
ANISOU 4124  CG2 ILE A 550     4890   1904   4316    516   -103    130       C  
ATOM   4125  CD1 ILE A 550      78.056  24.881  59.041  1.00 42.81           C  
ANISOU 4125  CD1 ILE A 550     6721   3758   5786    227     10    345       C  
ATOM   4126  N   GLN A 551      82.037  24.734  55.134  1.00 28.88           N  
ANISOU 4126  N   GLN A 551     4353   2365   4254    782   -138   -137       N  
ATOM   4127  CA  GLN A 551      83.182  24.029  54.569  1.00 31.21           C  
ANISOU 4127  CA  GLN A 551     4563   2631   4665   1002   -145   -202       C  
ATOM   4128  C   GLN A 551      84.494  24.681  54.993  1.00 34.58           C  
ANISOU 4128  C   GLN A 551     4808   3236   5095   1115   -238    -95       C  
ATOM   4129  O   GLN A 551      85.490  23.988  55.226  1.00 39.47           O  
ANISOU 4129  O   GLN A 551     5376   3782   5840   1312   -298    -41       O  
ATOM   4130  CB  GLN A 551      83.061  23.967  53.047  1.00 38.10           C  
ANISOU 4130  CB  GLN A 551     5373   3564   5539   1017    -28   -417       C  
ATOM   4131  CG  GLN A 551      82.063  22.914  52.579  1.00 53.29           C  
ANISOU 4131  CG  GLN A 551     7489   5246   7514    958     21   -535       C  
ATOM   4132  CD  GLN A 551      81.601  23.117  51.148  1.00 62.99           C  
ANISOU 4132  CD  GLN A 551     8701   6557   8674    887    104   -739       C  
ATOM   4133  OE1 GLN A 551      81.801  24.181  50.560  1.00 68.28           O  
ANISOU 4133  OE1 GLN A 551     9226   7478   9239    844    137   -772       O  
ATOM   4134  NE2 GLN A 551      80.966  22.095  50.583  1.00 64.89           N  
ANISOU 4134  NE2 GLN A 551     9111   6577   8967    861    124   -871       N  
ATOM   4135  N   GLN A 552      84.509  26.012  55.117  1.00 36.15           N  
ANISOU 4135  N   GLN A 552     4904   3657   5174    988   -265    -53       N  
ATOM   4136  CA  GLN A 552      85.683  26.696  55.656  1.00 37.75           C  
ANISOU 4136  CA  GLN A 552     4947   4017   5380   1047   -392     70       C  
ATOM   4137  C   GLN A 552      85.901  26.351  57.125  1.00 35.62           C  
ANISOU 4137  C   GLN A 552     4814   3619   5102   1068   -558    257       C  
ATOM   4138  O   GLN A 552      87.036  26.112  57.554  1.00 39.73           O  
ANISOU 4138  O   GLN A 552     5227   4152   5716   1209   -693    364       O  
ATOM   4139  CB  GLN A 552      85.539  28.208  55.491  1.00 41.60           C  
ANISOU 4139  CB  GLN A 552     5340   4732   5735    879   -393     70       C  
ATOM   4140  CG  GLN A 552      85.459  28.683  54.055  1.00 43.84           C  
ANISOU 4140  CG  GLN A 552     5484   5169   6005    854   -252    -83       C  
ATOM   4141  CD  GLN A 552      86.717  28.383  53.273  1.00 50.42           C  
ANISOU 4141  CD  GLN A 552     6099   6101   6959   1035   -208   -122       C  
ATOM   4142  OE1 GLN A 552      86.680  27.683  52.257  1.00 56.00           O  
ANISOU 4142  OE1 GLN A 552     6802   6765   7710   1135    -71   -265       O  
ATOM   4143  NE2 GLN A 552      87.841  28.918  53.738  1.00 42.35           N  
ANISOU 4143  NE2 GLN A 552     4892   5209   5990   1077   -322      4       N  
ATOM   4144  N   ILE A 553      84.830  26.352  57.919  1.00 34.54           N  
ANISOU 4144  N   ILE A 553     4909   3366   4850    927   -551    312       N  
ATOM   4145  CA  ILE A 553      84.950  25.973  59.324  1.00 37.51           C  
ANISOU 4145  CA  ILE A 553     5467   3609   5176    937   -693    495       C  
ATOM   4146  C   ILE A 553      85.469  24.546  59.446  1.00 44.50           C  
ANISOU 4146  C   ILE A 553     6394   4285   6229   1131   -744    544       C  
ATOM   4147  O   ILE A 553      86.314  24.247  60.298  1.00 45.41           O  
ANISOU 4147  O   ILE A 553     6524   4354   6375   1235   -923    702       O  
ATOM   4148  CB  ILE A 553      83.596  26.149  60.034  1.00 35.70           C  
ANISOU 4148  CB  ILE A 553     5484   3287   4795    757   -610    534       C  
ATOM   4149  CG1 ILE A 553      83.241  27.633  60.103  1.00 35.46           C  
ANISOU 4149  CG1 ILE A 553     5422   3449   4603    600   -585    509       C  
ATOM   4150  CG2 ILE A 553      83.629  25.512  61.416  1.00 34.57           C  
ANISOU 4150  CG2 ILE A 553     5577   2970   4586    776   -721    722       C  
ATOM   4151  CD1 ILE A 553      82.041  27.947  60.950  1.00 40.40           C  
ANISOU 4151  CD1 ILE A 553     6275   4002   5074    449   -494    565       C  
ATOM   4152  N   ALA A 554      84.988  23.649  58.581  1.00 45.65           N  
ANISOU 4152  N   ALA A 554     6567   4290   6490   1184   -603    411       N  
ATOM   4153  CA  ALA A 554      85.385  22.247  58.664  1.00 47.88           C  
ANISOU 4153  CA  ALA A 554     6924   4327   6942   1372   -637    443       C  
ATOM   4154  C   ALA A 554      86.836  22.048  58.240  1.00 49.17           C  
ANISOU 4154  C   ALA A 554     6849   4565   7269   1616   -704    441       C  
ATOM   4155  O   ALA A 554      87.552  21.227  58.826  1.00 51.56           O  
ANISOU 4155  O   ALA A 554     7174   4718   7699   1792   -828    568       O  
ATOM   4156  CB  ALA A 554      84.452  21.389  57.808  1.00 46.41           C  
ANISOU 4156  CB  ALA A 554     6852   3954   6828   1342   -476    281       C  
ATOM   4157  N   ASN A 555      87.284  22.778  57.225  1.00 53.54           N  
ANISOU 4157  N   ASN A 555     7164   5347   7834   1634   -617    311       N  
ATOM   4158  CA  ASN A 555      88.646  22.627  56.724  1.00 65.26           C  
ANISOU 4158  CA  ASN A 555     8381   6924   9491   1866   -632    306       C  
ATOM   4159  C   ASN A 555      89.635  23.455  57.537  1.00 72.65           C  
ANISOU 4159  C   ASN A 555     9135   8046  10423   1863   -838    494       C  
ATOM   4160  O   ASN A 555      90.753  23.716  57.090  1.00 78.08           O  
ANISOU 4160  O   ASN A 555     9529   8894  11243   1998   -849    507       O  
ATOM   4161  CB  ASN A 555      88.721  23.023  55.248  1.00 69.06           C  
ANISOU 4161  CB  ASN A 555     8694   7572   9974   1882   -427     96       C  
ATOM   4162  CG  ASN A 555      87.929  22.090  54.352  1.00 75.31           C  
ANISOU 4162  CG  ASN A 555     9665   8166  10783   1912   -255   -104       C  
ATOM   4163  OD1 ASN A 555      87.190  21.227  54.830  1.00 78.04           O  
ANISOU 4163  OD1 ASN A 555    10256   8252  11144   1882   -284    -86       O  
ATOM   4164  ND2 ASN A 555      88.080  22.257  53.043  1.00 76.37           N  
ANISOU 4164  ND2 ASN A 555     9693   8417  10907   1959    -80   -293       N  
ATOM   4165  N   HIS A 560      96.917  32.157  57.706  1.00 61.11           N  
ANISOU 4165  N   HIS A 560     6478   6646  10095    -52  -1438    649       N  
ATOM   4166  CA  HIS A 560      97.223  32.674  56.377  1.00 62.76           C  
ANISOU 4166  CA  HIS A 560     6654   6874  10319    -61  -1387    706       C  
ATOM   4167  C   HIS A 560      95.951  32.944  55.586  1.00 59.54           C  
ANISOU 4167  C   HIS A 560     6337   6453   9833    -51  -1368    615       C  
ATOM   4168  O   HIS A 560      95.906  33.856  54.760  1.00 58.76           O  
ANISOU 4168  O   HIS A 560     6252   6341   9732    -83  -1394    640       O  
ATOM   4169  CB  HIS A 560      98.115  31.694  55.610  1.00 68.63           C  
ANISOU 4169  CB  HIS A 560     7326   7660  11090    -15  -1255    777       C  
ATOM   4170  N   HIS A 561      94.914  32.144  55.841  1.00 56.46           N  
ANISOU 4170  N   HIS A 561     6010   6060   9382    -13  -1331    510       N  
ATOM   4171  CA  HIS A 561      93.647  32.310  55.137  1.00 56.85           C  
ANISOU 4171  CA  HIS A 561     6136   6091   9375      1  -1324    413       C  
ATOM   4172  C   HIS A 561      92.890  33.561  55.566  1.00 51.78           C  
ANISOU 4172  C   HIS A 561     5527   5409   8739    -35  -1451    345       C  
ATOM   4173  O   HIS A 561      91.925  33.935  54.892  1.00 51.60           O  
ANISOU 4173  O   HIS A 561     5557   5359   8690    -26  -1473    272       O  
ATOM   4174  CB  HIS A 561      92.763  31.078  55.342  1.00 51.37           C  
ANISOU 4174  CB  HIS A 561     5486   5404   8630     45  -1252    322       C  
ATOM   4175  N   HIS A 562      93.302  34.212  56.653  1.00 51.98           N  
ANISOU 4175  N   HIS A 562     5529   5421   8800    -71  -1544    363       N  
ATOM   4176  CA  HIS A 562      92.618  35.407  57.126  1.00 51.98           C  
ANISOU 4176  CA  HIS A 562     5566   5379   8806    -97  -1670    291       C  
ATOM   4177  C   HIS A 562      92.664  36.509  56.070  1.00 52.33           C  
ANISOU 4177  C   HIS A 562     5626   5390   8866   -122  -1736    328       C  
ATOM   4178  O   HIS A 562      93.639  36.649  55.326  1.00 52.79           O  
ANISOU 4178  O   HIS A 562     5651   5461   8947   -147  -1710    446       O  
ATOM   4179  CB  HIS A 562      93.253  35.895  58.432  1.00 52.30           C  
ANISOU 4179  CB  HIS A 562     5591   5403   8877   -131  -1764    322       C  
ATOM   4180  CG  HIS A 562      92.416  36.893  59.167  1.00 52.32           C  
ANISOU 4180  CG  HIS A 562     5646   5364   8870   -142  -1877    219       C  
ATOM   4181  ND1 HIS A 562      92.454  38.243  58.896  1.00 52.70           N  
ANISOU 4181  ND1 HIS A 562     5709   5365   8950   -170  -2003    231       N  
ATOM   4182  CD2 HIS A 562      91.492  36.732  60.144  1.00 52.14           C  
ANISOU 4182  CD2 HIS A 562     5667   5335   8807   -126  -1877     96       C  
ATOM   4183  CE1 HIS A 562      91.601  38.874  59.683  1.00 52.73           C  
ANISOU 4183  CE1 HIS A 562     5762   5335   8939   -160  -2083    113       C  
ATOM   4184  NE2 HIS A 562      90.999  37.979  60.446  1.00 52.42           N  
ANISOU 4184  NE2 HIS A 562     5737   5325   8856   -134  -1998     28       N  
ATOM   4185  N   HIS A 563      91.595  37.306  56.012  1.00 52.23           N  
ANISOU 4185  N   HIS A 563     5666   5333   8845   -117  -1825    223       N  
ATOM   4186  CA  HIS A 563      91.492  38.323  54.970  1.00 52.61           C  
ANISOU 4186  CA  HIS A 563     5754   5334   8900   -139  -1905    246       C  
ATOM   4187  C   HIS A 563      92.479  39.470  55.150  1.00 53.26           C  
ANISOU 4187  C   HIS A 563     5822   5389   9027   -204  -2017    352       C  
ATOM   4188  O   HIS A 563      92.663  40.257  54.216  1.00 53.75           O  
ANISOU 4188  O   HIS A 563     5919   5414   9089   -240  -2072    407       O  
ATOM   4189  CB  HIS A 563      90.060  38.869  54.894  1.00 52.46           C  
ANISOU 4189  CB  HIS A 563     5792   5264   8876   -108  -1990     96       C  
ATOM   4190  CG  HIS A 563      89.508  39.340  56.205  1.00 52.43           C  
ANISOU 4190  CG  HIS A 563     5783   5244   8892    -98  -2068     -8       C  
ATOM   4191  ND1 HIS A 563      89.043  38.475  57.172  1.00 52.06           N  
ANISOU 4191  ND1 HIS A 563     5715   5238   8827    -71  -1986    -87       N  
ATOM   4192  CD2 HIS A 563      89.332  40.588  56.702  1.00 52.84           C  
ANISOU 4192  CD2 HIS A 563     5861   5242   8974   -111  -2218    -48       C  
ATOM   4193  CE1 HIS A 563      88.611  39.170  58.210  1.00 52.28           C  
ANISOU 4193  CE1 HIS A 563     5756   5241   8866    -69  -2069   -174       C  
ATOM   4194  NE2 HIS A 563      88.778  40.454  57.952  1.00 52.74           N  
ANISOU 4194  NE2 HIS A 563     5841   5241   8956    -87  -2214   -156       N  
ATOM   4195  N   HIS A 564      93.119  39.585  56.306  1.00 53.40           N  
ANISOU 4195  N   HIS A 564     5797   5414   9077   -225  -2059    384       N  
ATOM   4196  CA  HIS A 564      94.135  40.606  56.527  1.00 54.11           C  
ANISOU 4196  CA  HIS A 564     5866   5474   9221   -291  -2173    494       C  
ATOM   4197  C   HIS A 564      95.549  40.047  56.529  1.00 56.08           C  
ANISOU 4197  C   HIS A 564     6022   5770   9515   -323  -2096    640       C  
ATOM   4198  O   HIS A 564      96.502  40.808  56.727  1.00 55.24           O  
ANISOU 4198  O   HIS A 564     5877   5643   9469   -386  -2185    743       O  
ATOM   4199  CB  HIS A 564      93.877  41.335  57.853  1.00 54.21           C  
ANISOU 4199  CB  HIS A 564     5907   5441   9248   -296  -2313    426       C  
ATOM   4200  CG  HIS A 564      92.665  42.210  57.828  1.00 57.20           C  
ANISOU 4200  CG  HIS A 564     6364   5762   9608   -270  -2418    293       C  
ATOM   4201  ND1 HIS A 564      91.883  42.431  58.938  1.00 55.31           N  
ANISOU 4201  ND1 HIS A 564     6161   5501   9354   -234  -2475    162       N  
ATOM   4202  CD2 HIS A 564      92.095  42.914  56.820  1.00 54.34           C  
ANISOU 4202  CD2 HIS A 564     6051   5354   9242   -271  -2480    266       C  
ATOM   4203  CE1 HIS A 564      90.884  43.235  58.620  1.00 54.18           C  
ANISOU 4203  CE1 HIS A 564     6069   5305   9212   -207  -2565     54       C  
ATOM   4204  NE2 HIS A 564      90.991  43.545  57.341  1.00 54.76           N  
ANISOU 4204  NE2 HIS A 564     6155   5358   9294   -229  -2581    116       N  
ATOM   4205  N   HIS A 565      95.706  38.748  56.302  1.00 54.19           N  
ANISOU 4205  N   HIS A 565     5743   5590   9257   -280  -1943    648       N  
ATOM   4206  CA  HIS A 565      97.013  38.101  56.326  1.00 61.60           C  
ANISOU 4206  CA  HIS A 565     6581   6574  10251   -293  -1865    769       C  
ATOM   4207  C   HIS A 565      97.527  37.863  54.911  1.00 67.88           C  
ANISOU 4207  C   HIS A 565     7345   7406  11043   -301  -1742    853       C  
ATOM   4208  O   HIS A 565      98.331  38.640  54.397  1.00 71.85           O  
ANISOU 4208  O   HIS A 565     7808   7901  11590   -367  -1770    959       O  
ATOM   4209  CB  HIS A 565      96.941  36.779  57.092  1.00 55.58           C  
ANISOU 4209  CB  HIS A 565     5801   5845   9472   -235  -1784    724       C  
ATOM   4210  CG  HIS A 565      98.250  36.339  57.668  1.00 57.81           C  
ANISOU 4210  CG  HIS A 565     5985   6145   9834   -247  -1781    828       C  
ATOM   4211  ND1 HIS A 565      99.306  35.925  56.886  1.00 59.58           N  
ANISOU 4211  ND1 HIS A 565     6110   6412  10116   -248  -1683    936       N  
ATOM   4212  CD2 HIS A 565      98.673  36.248  58.952  1.00 58.53           C  
ANISOU 4212  CD2 HIS A 565     6065   6213   9962   -256  -1870    837       C  
ATOM   4213  CE1 HIS A 565     100.324  35.597  57.663  1.00 60.44           C  
ANISOU 4213  CE1 HIS A 565     6133   6523  10310   -254  -1717   1004       C  
ATOM   4214  NE2 HIS A 565      99.967  35.787  58.920  1.00 59.05           N  
ANISOU 4214  NE2 HIS A 565     6017   6302  10119   -260  -1839    949       N  
TER    4215      HIS A 565                                                      
HETATM 4216  S   SO4 A 601      49.774  47.951  56.809  0.74 66.86           S  
HETATM 4217  O1  SO4 A 601      51.192  48.194  56.556  0.74 66.55           O  
HETATM 4218  O2  SO4 A 601      48.965  48.736  55.881  0.74 68.46           O  
HETATM 4219  O3  SO4 A 601      49.478  46.535  56.620  0.74 64.37           O  
HETATM 4220  O4  SO4 A 601      49.449  48.346  58.177  0.74 65.93           O  
HETATM 4221  S   SO4 A 602      46.902  46.903  63.068  0.75 56.28           S  
HETATM 4222  O1  SO4 A 602      47.139  45.512  63.446  0.75 57.75           O  
HETATM 4223  O2  SO4 A 602      46.788  47.005  61.613  0.75 52.84           O  
HETATM 4224  O3  SO4 A 602      48.011  47.731  63.535  0.75 51.84           O  
HETATM 4225  O4  SO4 A 602      45.655  47.354  63.681  0.75 58.61           O  
HETATM 4226  S   SO4 A 603      39.624  32.022  84.819  0.66 23.85           S  
HETATM 4227  O1  SO4 A 603      39.853  33.214  84.013  0.66 23.84           O  
HETATM 4228  O2  SO4 A 603      39.675  30.815  84.003  0.66 28.04           O  
HETATM 4229  O3  SO4 A 603      40.640  31.959  85.876  0.66 31.74           O  
HETATM 4230  O4  SO4 A 603      38.300  32.117  85.429  0.66 21.00           O  
HETATM 4231  S   SO4 A 604      54.386  59.417  53.090  0.78 54.51           S  
HETATM 4232  O1  SO4 A 604      55.510  59.814  52.249  0.78 45.94           O  
HETATM 4233  O2  SO4 A 604      53.536  58.484  52.355  0.78 57.28           O  
HETATM 4234  O3  SO4 A 604      54.869  58.771  54.309  0.78 50.63           O  
HETATM 4235  O4  SO4 A 604      53.612  60.606  53.448  0.78 58.42           O  
HETATM 4236  S   SO4 A 605      66.374  73.316  70.803  0.78 80.75           S  
HETATM 4237  O1  SO4 A 605      67.581  73.375  69.983  0.78 80.21           O  
HETATM 4238  O2  SO4 A 605      65.197  73.358  69.941  0.78 80.79           O  
HETATM 4239  O3  SO4 A 605      66.371  72.078  71.575  0.78 80.92           O  
HETATM 4240  O4  SO4 A 605      66.348  74.455  71.715  0.78 82.48           O  
HETATM 4241  O   HOH A 701      49.813  38.827  68.755  1.00 28.55           O  
HETATM 4242  O   HOH A 702      80.622  79.846  68.440  1.00 48.08           O  
HETATM 4243  O   HOH A 703      81.035  31.055  48.596  1.00 29.65           O  
HETATM 4244  O   HOH A 704      76.674  38.175  38.621  1.00 28.52           O  
HETATM 4245  O   HOH A 705      84.012  48.706  77.613  1.00 49.49           O  
HETATM 4246  O   HOH A 706      85.275  34.283  49.781  1.00 36.47           O  
HETATM 4247  O   HOH A 707      75.037  55.785  91.352  1.00 47.28           O  
HETATM 4248  O   HOH A 708      78.964  55.684  59.828  1.00 29.89           O  
HETATM 4249  O   HOH A 709      60.265  63.113  72.659  1.00 56.19           O  
HETATM 4250  O   HOH A 710      99.835  35.307  54.585  1.00 56.71           O  
HETATM 4251  O   HOH A 711      64.068  76.617  66.338  1.00 47.75           O  
HETATM 4252  O   HOH A 712      55.074  49.838  83.662  1.00 38.88           O  
HETATM 4253  O   HOH A 713      85.302  44.407  56.701  1.00 33.28           O  
HETATM 4254  O   HOH A 714      92.295  66.686  57.430  1.00 47.67           O  
HETATM 4255  O   HOH A 715      56.750  50.952  69.358  1.00 36.42           O  
HETATM 4256  O   HOH A 716      83.706  69.107  62.612  1.00 48.34           O  
HETATM 4257  O   HOH A 717      64.447  27.813  75.810  1.00 41.26           O  
HETATM 4258  O   HOH A 718      78.065  76.151  70.230  1.00 38.47           O  
HETATM 4259  O   HOH A 719      74.841  57.177  69.912  1.00 27.72           O  
HETATM 4260  O   HOH A 720      64.987  29.736  80.247  1.00 44.89           O  
HETATM 4261  O   HOH A 721      63.148  47.486  61.325  1.00 25.32           O  
HETATM 4262  O   HOH A 722      62.429  27.028  59.929  1.00 41.75           O  
HETATM 4263  O   HOH A 723      46.153  30.982  70.248  1.00 25.55           O  
HETATM 4264  O   HOH A 724      70.101  20.889  67.301  1.00 34.65           O  
HETATM 4265  O   HOH A 725      76.668  60.598  68.022  1.00 42.23           O  
HETATM 4266  O   HOH A 726      76.035  47.793  50.893  1.00 20.41           O  
HETATM 4267  O   HOH A 727      64.225  39.722  83.916  1.00 22.16           O  
HETATM 4268  O   HOH A 728      85.714  33.818  32.714  1.00 30.64           O  
HETATM 4269  O   HOH A 729      54.791  43.357  70.658  1.00 20.42           O  
HETATM 4270  O   HOH A 730      49.899  45.237  78.243  1.00 28.80           O  
HETATM 4271  O   HOH A 731      50.785  40.487  52.124  1.00 48.75           O  
HETATM 4272  O   HOH A 732      84.362  45.216  60.154  1.00 23.70           O  
HETATM 4273  O   HOH A 733      80.513  61.746  59.800  1.00 46.16           O  
HETATM 4274  O   HOH A 734      65.945  54.037  48.598  1.00 26.74           O  
HETATM 4275  O   HOH A 735      71.605  69.116  73.247  1.00 56.36           O  
HETATM 4276  O   HOH A 736      52.422  26.277  50.872  1.00 44.49           O  
HETATM 4277  O   HOH A 737      82.091  33.791  41.323  1.00 34.55           O  
HETATM 4278  O   HOH A 738      64.879  38.845  45.817  1.00 26.63           O  
HETATM 4279  O   HOH A 739      76.414  41.322  39.309  1.00 33.36           O  
HETATM 4280  O   HOH A 740      56.367  46.627  46.230  1.00 46.06           O  
HETATM 4281  O   HOH A 741      48.904  44.355  65.004  1.00 34.22           O  
HETATM 4282  O   HOH A 742      56.748  54.152  78.218  1.00 33.46           O  
HETATM 4283  O   HOH A 743      73.176  47.983  42.120  1.00 33.38           O  
HETATM 4284  O   HOH A 744      47.338  43.713  67.267  1.00 42.21           O  
HETATM 4285  O   HOH A 745      79.910  55.639  56.100  1.00 20.98           O  
HETATM 4286  O   HOH A 746      85.448  64.925  50.619  1.00 48.87           O  
HETATM 4287  O   HOH A 747      59.877  50.091  62.667  1.00 24.74           O  
HETATM 4288  O   HOH A 748      59.183  60.754  63.263  1.00 20.93           O  
HETATM 4289  O   HOH A 749      60.678  81.426  50.711  1.00 46.33           O  
HETATM 4290  O   HOH A 750      60.548  46.820  87.939  1.00 40.52           O  
HETATM 4291  O   HOH A 751      60.693  71.161  47.450  1.00 45.87           O  
HETATM 4292  O   HOH A 752      68.441  79.502  49.488  1.00 40.65           O  
HETATM 4293  O   HOH A 753      76.558  64.508  43.267  1.00 42.69           O  
HETATM 4294  O   HOH A 754      60.659  59.464  76.318  1.00 37.07           O  
HETATM 4295  O   HOH A 755      54.478  33.209  70.397  1.00 15.60           O  
HETATM 4296  O   HOH A 756      75.908  35.471  76.072  1.00 33.15           O  
HETATM 4297  O   HOH A 757      63.118  41.823  85.802  1.00 24.14           O  
HETATM 4298  O   HOH A 758      54.320  56.616  67.753  1.00 45.87           O  
HETATM 4299  O   HOH A 759      73.063  64.481  70.093  1.00 48.87           O  
HETATM 4300  O   HOH A 760      45.267  40.283  65.174  1.00 26.65           O  
HETATM 4301  O   HOH A 761      50.321  40.984  69.900  1.00 34.85           O  
HETATM 4302  O   HOH A 762      63.181  87.404  52.818  1.00 50.68           O  
HETATM 4303  O   HOH A 763      75.814  49.197  47.514  1.00 31.97           O  
HETATM 4304  O   HOH A 764      87.226  40.221  75.460  1.00 34.89           O  
HETATM 4305  O   HOH A 765      73.859  44.071  80.580  1.00 23.40           O  
HETATM 4306  O   HOH A 766      64.363  57.145  87.783  1.00 31.04           O  
HETATM 4307  O   HOH A 767      64.366  63.522  85.118  1.00 30.39           O  
HETATM 4308  O   HOH A 768      71.615  43.993  37.247  1.00 26.26           O  
HETATM 4309  O   HOH A 769      60.630  27.690  50.850  1.00 37.81           O  
HETATM 4310  O   HOH A 770      49.468  49.171  78.504  1.00 39.81           O  
HETATM 4311  O   HOH A 771      88.614  35.901  56.598  1.00 27.86           O  
HETATM 4312  O   HOH A 772      79.771  42.230  68.153  1.00 19.23           O  
HETATM 4313  O   HOH A 773      61.980  29.553  70.446  1.00 40.72           O  
HETATM 4314  O   HOH A 774      83.798  63.753  57.817  1.00 46.79           O  
HETATM 4315  O   HOH A 775      61.268  29.858  53.768  1.00 16.38           O  
HETATM 4316  O   HOH A 776      53.046  49.325  58.955  1.00 44.06           O  
HETATM 4317  O   HOH A 777      52.927  62.837  55.459  1.00 40.18           O  
HETATM 4318  O   HOH A 778      82.309  46.580  74.202  1.00 30.70           O  
HETATM 4319  O   HOH A 779      64.602  28.356  55.996  1.00 31.04           O  
HETATM 4320  O   HOH A 780      49.603  27.950  75.348  1.00 24.53           O  
HETATM 4321  O   HOH A 781      66.102  43.536  65.702  1.00 17.56           O  
HETATM 4322  O   HOH A 782      68.947  51.318  86.535  1.00 39.60           O  
HETATM 4323  O   HOH A 783      78.819  50.789  67.053  1.00 34.79           O  
HETATM 4324  O   HOH A 784      67.542  46.422  66.380  1.00 16.31           O  
HETATM 4325  O   HOH A 785      82.264  55.230  85.515  1.00 27.93           O  
HETATM 4326  O   HOH A 786      47.825  37.612  65.235  1.00 40.41           O  
HETATM 4327  O   HOH A 787      54.386  29.866  85.636  1.00 41.28           O  
HETATM 4328  O   HOH A 788      37.534  33.406  87.668  1.00 28.21           O  
HETATM 4329  O   HOH A 789      97.916  42.770  55.531  1.00 49.17           O  
HETATM 4330  O   HOH A 790      57.111  31.184  59.390  1.00 13.79           O  
HETATM 4331  O   HOH A 791      62.732  54.491  71.244  1.00 19.19           O  
HETATM 4332  O   HOH A 792      70.020  60.054  64.266  1.00 26.53           O  
HETATM 4333  O   HOH A 793      80.152  80.469  56.427  1.00 35.47           O  
HETATM 4334  O   HOH A 794      58.530  63.484  67.736  1.00 40.13           O  
HETATM 4335  O   HOH A 795      71.520  55.536  58.255  1.00 16.61           O  
HETATM 4336  O   HOH A 796      83.391  64.920  70.754  1.00 31.96           O  
HETATM 4337  O   HOH A 797      78.746  65.416  47.524  1.00 23.73           O  
HETATM 4338  O   HOH A 798      50.802  27.435  65.677  1.00 30.27           O  
HETATM 4339  O   HOH A 799      61.814  46.051  47.070  1.00 22.15           O  
HETATM 4340  O   HOH A 800      86.021  38.740  41.529  1.00 25.16           O  
HETATM 4341  O   HOH A 801      64.333  35.543  44.038  1.00 52.33           O  
HETATM 4342  O   HOH A 802      73.662  66.668  72.165  1.00 40.67           O  
HETATM 4343  O   HOH A 803      74.341  25.761  70.864  1.00 32.76           O  
HETATM 4344  O   HOH A 804      88.612  42.588  37.250  1.00 28.84           O  
HETATM 4345  O   HOH A 805      61.615  27.591  61.939  1.00 23.34           O  
HETATM 4346  O   HOH A 806      60.636  25.900  68.772  1.00 33.28           O  
HETATM 4347  O   HOH A 807      79.196  42.007  70.716  1.00 19.69           O  
HETATM 4348  O   HOH A 808      79.591  33.547  54.165  1.00 18.84           O  
HETATM 4349  O   HOH A 809      63.909  29.133  66.475  1.00 16.26           O  
HETATM 4350  O   HOH A 810      54.891  33.208  47.170  1.00 31.86           O  
HETATM 4351  O   HOH A 811      59.694  33.052  53.650  1.00 14.82           O  
HETATM 4352  O   HOH A 812      72.957  58.837  46.163  1.00 41.68           O  
HETATM 4353  O   HOH A 813      57.654  25.706  66.404  1.00 22.15           O  
HETATM 4354  O   HOH A 814      71.879  39.418  84.287  1.00 52.73           O  
HETATM 4355  O   HOH A 815      73.927  27.293  74.610  1.00 34.00           O  
HETATM 4356  O   HOH A 816      59.921  62.390  61.125  1.00 21.56           O  
HETATM 4357  O   HOH A 817      75.662  71.645  46.636  1.00 31.15           O  
HETATM 4358  O   HOH A 818      44.326  45.724  68.756  0.50 48.48           O  
HETATM 4359  O   HOH A 819      45.332  40.582  79.820  1.00 39.01           O  
HETATM 4360  O   HOH A 820      72.553  53.106  44.412  1.00 39.68           O  
HETATM 4361  O   HOH A 821      88.105  31.771  51.039  1.00 47.51           O  
HETATM 4362  O   HOH A 822      66.026  53.493  51.311  1.00 25.10           O  
HETATM 4363  O   HOH A 823      85.048  49.948  60.205  1.00 34.80           O  
HETATM 4364  O   HOH A 824      59.601  50.614  58.109  1.00 24.14           O  
HETATM 4365  O   HOH A 825      67.121  39.612  47.147  1.00 19.89           O  
HETATM 4366  O   HOH A 826      91.807  40.051  68.886  1.00 19.05           O  
HETATM 4367  O   HOH A 827      60.976  33.165  80.224  1.00 18.54           O  
HETATM 4368  O   HOH A 828      83.056  60.992  52.029  1.00 47.68           O  
HETATM 4369  O   HOH A 829      43.436  36.928  78.924  1.00 22.33           O  
HETATM 4370  O   HOH A 830      86.831  45.275  38.807  1.00 21.53           O  
HETATM 4371  O   HOH A 831      59.649  27.793  72.685  1.00 39.27           O  
HETATM 4372  O   HOH A 832      66.699  53.686  87.555  1.00 31.08           O  
HETATM 4373  O   HOH A 833      73.002  52.897  63.302  1.00 13.63           O  
HETATM 4374  O   HOH A 834      73.820  50.306  46.898  1.00 30.68           O  
HETATM 4375  O   HOH A 835      64.804  38.335  37.991  1.00 24.67           O  
HETATM 4376  O   HOH A 836      90.063  43.505  39.615  1.00 35.17           O  
HETATM 4377  O   HOH A 837      71.823  35.767  50.913  1.00 27.04           O  
HETATM 4378  O   HOH A 838      77.034  52.635  88.743  1.00 36.37           O  
HETATM 4379  O   HOH A 839      51.596  47.161  72.730  1.00 37.25           O  
HETATM 4380  O   HOH A 840      54.547  48.624  67.053  1.00 26.07           O  
HETATM 4381  O   HOH A 841      60.175  57.653  79.247  1.00 35.33           O  
HETATM 4382  O   HOH A 842      80.424  82.463  65.843  1.00 37.79           O  
HETATM 4383  O   HOH A 843      65.750  78.472  67.805  1.00 32.79           O  
HETATM 4384  O   HOH A 844      59.901  55.501  58.732  1.00 31.25           O  
HETATM 4385  O   HOH A 845      67.450  26.532  72.645  1.00 33.30           O  
HETATM 4386  O   HOH A 846      78.256  72.267  46.370  1.00 35.39           O  
HETATM 4387  O   HOH A 847      59.619  42.804  85.716  1.00 34.00           O  
HETATM 4388  O   HOH A 848      69.896  46.206  41.794  1.00 24.00           O  
HETATM 4389  O   HOH A 849      58.483  30.245  84.487  1.00 46.00           O  
HETATM 4390  O   HOH A 850      85.628  37.031  50.469  1.00 24.58           O  
HETATM 4391  O   HOH A 851      73.731  31.360  52.675  1.00 30.85           O  
HETATM 4392  O   HOH A 852      82.068  38.794  70.829  1.00 18.54           O  
HETATM 4393  O   HOH A 853      64.193  21.178  63.848  1.00 45.98           O  
HETATM 4394  O   HOH A 854      80.801  52.791  87.707  1.00 35.91           O  
HETATM 4395  O   HOH A 855      76.358  62.146  60.931  1.00 29.19           O  
HETATM 4396  O   HOH A 856      92.229  69.684  49.841  1.00 42.62           O  
HETATM 4397  O   HOH A 857      80.881  50.574  68.380  1.00 44.98           O  
HETATM 4398  O   HOH A 858      75.173  46.477  81.353  1.00 29.81           O  
HETATM 4399  O   HOH A 859      41.405  28.018  75.326  1.00 34.26           O  
HETATM 4400  O   HOH A 860      61.103  23.150  66.765  1.00 38.38           O  
HETATM 4401  O   HOH A 861      63.274  82.085  46.139  1.00 53.18           O  
HETATM 4402  O   HOH A 862      76.442  33.203  48.121  1.00 31.23           O  
HETATM 4403  O   HOH A 863      58.098  79.368  63.346  1.00 50.01           O  
HETATM 4404  O   HOH A 864      49.508  41.424  64.938  1.00 33.47           O  
HETATM 4405  O   HOH A 865      85.676  47.424  58.874  1.00 31.22           O  
HETATM 4406  O   HOH A 866      78.231  67.768  75.496  1.00 37.14           O  
HETATM 4407  O   HOH A 867      68.079  29.416  73.121  1.00 33.55           O  
HETATM 4408  O   HOH A 868      52.892  24.012  57.973  1.00 36.37           O  
HETATM 4409  O   HOH A 869      91.459  42.822  52.627  1.00 46.69           O  
HETATM 4410  O   HOH A 870      79.663  81.851  47.654  1.00 44.45           O  
HETATM 4411  O   HOH A 871      64.881  70.141  64.762  1.00 58.58           O  
HETATM 4412  O   HOH A 872      57.279  23.412  52.237  1.00 54.57           O  
HETATM 4413  O   HOH A 873      72.862  35.512  46.021  1.00 35.82           O  
HETATM 4414  O   HOH A 874      58.765  33.157  58.517  1.00 15.56           O  
HETATM 4415  O   HOH A 875      85.114  42.007  64.721  1.00 41.42           O  
HETATM 4416  O   HOH A 876      74.995  28.350  50.662  1.00 45.44           O  
HETATM 4417  O   HOH A 877      66.818  53.942  57.963  1.00 25.84           O  
HETATM 4418  O   HOH A 878      56.573  73.404  58.426  1.00 39.08           O  
HETATM 4419  O   HOH A 879      67.887  26.759  50.479  1.00 43.91           O  
HETATM 4420  O   HOH A 880      80.110  52.814  65.261  1.00 23.03           O  
HETATM 4421  O   HOH A 881      87.374  48.040  45.685  1.00 43.64           O  
HETATM 4422  O   HOH A 882      54.942  56.229  58.219  1.00 39.20           O  
HETATM 4423  O   HOH A 883      50.437  25.398  67.715  1.00 27.31           O  
HETATM 4424  O   HOH A 884      43.699  38.300  69.972  1.00 31.51           O  
HETATM 4425  O   HOH A 885      65.790  57.226  91.323  1.00 55.68           O  
HETATM 4426  O   HOH A 886      55.400  52.455  81.443  1.00 36.19           O  
HETATM 4427  O   HOH A 887      44.446  42.152  70.615  1.00 47.76           O  
HETATM 4428  O   HOH A 888      74.221  69.512  47.631  1.00 24.34           O  
HETATM 4429  O   HOH A 889      89.476  41.341  43.773  1.00 37.80           O  
HETATM 4430  O   HOH A 890      57.787  50.347  55.330  1.00 31.62           O  
HETATM 4431  O   HOH A 891      72.309  50.220  63.306  1.00 15.17           O  
HETATM 4432  O   HOH A 892      74.545  58.924  72.129  1.00 31.82           O  
HETATM 4433  O   HOH A 893      64.693  59.309  91.242  1.00 54.99           O  
HETATM 4434  O   HOH A 894      50.537  42.341  67.622  1.00 24.45           O  
HETATM 4435  O   HOH A 895      69.411  53.203  87.509  1.00 34.58           O  
HETATM 4436  O   HOH A 896      61.950  52.072  55.974  1.00 28.61           O  
HETATM 4437  O   HOH A 897      84.415  64.096  52.335  1.00 45.59           O  
HETATM 4438  O   HOH A 898      52.160  29.516  84.453  1.00 48.10           O  
HETATM 4439  O   HOH A 899      80.021  46.169  43.727  1.00 45.47           O  
HETATM 4440  O   HOH A 900      72.655  58.365  48.635  1.00 27.41           O  
HETATM 4441  O   HOH A 901      71.197  59.597  57.507  1.00 18.27           O  
HETATM 4442  O   HOH A 902      63.157  48.540  88.126  1.00 47.83           O  
HETATM 4443  O   HOH A 903      55.263  67.234  57.507  1.00 39.01           O  
HETATM 4444  O   HOH A 904      75.164  73.846  73.512  1.00 47.68           O  
HETATM 4445  O   HOH A 905      49.876  24.781  56.768  1.00 50.58           O  
HETATM 4446  O   HOH A 906      87.341  37.809  38.536  1.00 27.06           O  
HETATM 4447  O   HOH A 907      88.651  37.273  68.756  0.50 28.02           O  
HETATM 4448  O   HOH A 908      64.179  44.690  42.373  1.00 25.00           O  
HETATM 4449  O   HOH A 909      84.609  51.094  54.008  1.00 36.22           O  
HETATM 4450  O   HOH A 910      65.516  55.386  55.194  1.00 20.69           O  
HETATM 4451  O   HOH A 911      51.898  50.467  72.331  1.00 35.73           O  
HETATM 4452  O   HOH A 912      84.876  58.344  52.198  1.00 38.13           O  
HETATM 4453  O   HOH A 913      52.149  29.226  81.663  1.00 21.50           O  
HETATM 4454  O   HOH A 914      89.957  47.609  40.164  1.00 48.83           O  
HETATM 4455  O   HOH A 915      44.356  31.319  82.544  1.00 24.43           O  
HETATM 4456  O   HOH A 916      61.940  31.954  46.797  1.00 22.16           O  
HETATM 4457  O   HOH A 917      88.582  40.262  39.955  1.00 42.51           O  
HETATM 4458  O   HOH A 918      47.049  27.495  56.053  1.00 46.79           O  
HETATM 4459  O   HOH A 919      68.333  62.356  62.635  1.00 29.38           O  
HETATM 4460  O   HOH A 920      68.004  59.659  61.128  1.00 22.08           O  
HETATM 4461  O   HOH A 921      49.022  49.151  70.841  1.00 42.20           O  
HETATM 4462  O   HOH A 922      73.042  33.557  51.273  1.00 48.77           O  
HETATM 4463  O   HOH A 923      60.125  25.892  65.472  1.00 25.78           O  
HETATM 4464  O   HOH A 924      53.971  27.563  80.563  1.00 33.15           O  
HETATM 4465  O   HOH A 925      63.411  60.421  74.308  1.00 40.71           O  
HETATM 4466  O   HOH A 926      69.599  53.783  57.145  1.00 14.73           O  
HETATM 4467  O   HOH A 927      83.710  70.574  47.771  1.00 48.32           O  
HETATM 4468  O   HOH A 928      77.628  47.227  43.415  1.00 40.12           O  
HETATM 4469  O   HOH A 929      57.278  27.121  78.008  1.00 29.62           O  
HETATM 4470  O   HOH A 930      70.048  46.639  84.470  1.00 36.50           O  
HETATM 4471  O   HOH A 931      53.867  48.870  49.316  1.00 52.45           O  
HETATM 4472  O   HOH A 932      52.811  29.335  48.791  1.00 38.63           O  
HETATM 4473  O   HOH A 933      57.280  55.726  59.583  1.00 23.98           O  
HETATM 4474  O   HOH A 934      61.068  54.035  61.107  1.00 22.60           O  
HETATM 4475  O   HOH A 935      58.541  65.873  49.411  1.00 36.78           O  
HETATM 4476  O   HOH A 936      61.639  43.723  89.059  1.00 57.48           O  
HETATM 4477  O   HOH A 937      63.848  49.763  46.259  1.00 32.03           O  
HETATM 4478  O   HOH A 938      73.822  60.665  49.647  1.00 19.46           O  
HETATM 4479  O   HOH A 939      60.812  44.015  68.165  1.00 22.25           O  
HETATM 4480  O   HOH A 940      76.698  45.802  40.013  1.00 36.83           O  
HETATM 4481  O   HOH A 941      71.063  72.927  67.387  1.00 48.76           O  
HETATM 4482  O   HOH A 942      68.888  29.456  47.393  1.00 36.62           O  
HETATM 4483  O   HOH A 943      69.418  49.298  83.788  1.00 33.35           O  
HETATM 4484  O   HOH A 944      66.459  36.371  39.635  1.00 36.21           O  
HETATM 4485  O   HOH A 945      71.287  36.131  42.199  1.00 27.92           O  
HETATM 4486  O   HOH A 946      55.595  61.562  69.375  1.00 37.75           O  
HETATM 4487  O   HOH A 947      71.250  83.601  69.314  1.00 52.88           O  
HETATM 4488  O   HOH A 948      77.619  56.775  69.780  1.00 26.69           O  
HETATM 4489  O   HOH A 949      84.462  46.271  41.655  1.00 28.88           O  
HETATM 4490  O   HOH A 950      70.060  33.609  47.981  1.00 26.70           O  
HETATM 4491  O   HOH A 951      59.508  77.466  64.826  1.00 49.48           O  
HETATM 4492  O   HOH A 952      43.508  29.088  72.225  1.00 36.10           O  
HETATM 4493  O   HOH A 953      85.566  50.141  47.002  1.00 30.86           O  
HETATM 4494  O   HOH A 954      60.679  59.654  52.308  1.00 31.48           O  
HETATM 4495  O   HOH A 955      61.418  36.913  43.584  1.00 45.49           O  
HETATM 4496  O   HOH A 956      51.739  40.912  49.356  1.00 26.07           O  
HETATM 4497  O   HOH A 957      49.211  27.846  53.103  1.00 38.61           O  
HETATM 4498  O   HOH A 958      87.156  33.819  36.862  1.00 48.79           O  
HETATM 4499  O   HOH A 959      74.691  35.621  42.574  1.00 42.81           O  
HETATM 4500  O   HOH A 960      83.857  33.067  45.533  1.00 31.86           O  
HETATM 4501  O   HOH A 961      56.818  50.770  66.607  1.00 30.64           O  
HETATM 4502  O   HOH A 962      65.029  61.043  69.400  1.00 35.74           O  
HETATM 4503  O   HOH A 963      75.723  35.429  39.410  1.00 43.84           O  
HETATM 4504  O   HOH A 964      85.605  35.552  41.829  1.00 44.65           O  
HETATM 4505  O   HOH A 965      58.946  31.710  81.339  1.00 22.41           O  
HETATM 4506  O   HOH A 966      73.111  56.438  44.398  1.00 37.65           O  
HETATM 4507  O   HOH A 967      53.105  54.574  76.237  1.00 42.85           O  
HETATM 4508  O   HOH A 968      72.192  60.213  70.608  1.00 27.46           O  
HETATM 4509  O   HOH A 969      70.465  58.673  43.958  1.00 45.11           O  
HETATM 4510  O   HOH A 970      76.367  45.297  42.363  1.00 26.78           O  
HETATM 4511  O   HOH A 971      50.119  41.720  55.312  1.00 30.87           O  
HETATM 4512  O   HOH A 972      52.513  50.984  69.124  1.00 45.44           O  
HETATM 4513  O   HOH A 973      83.144  43.112  69.121  1.00 37.93           O  
HETATM 4514  O   HOH A 974      78.197  59.512  69.887  1.00 34.96           O  
HETATM 4515  O   HOH A 975      64.897  66.371  66.510  1.00 42.54           O  
HETATM 4516  O   HOH A 976      67.687  31.125  83.782  1.00 39.10           O  
HETATM 4517  O   HOH A 977      89.381  35.393  54.043  1.00 34.63           O  
HETATM 4518  O   HOH A 978      51.405  40.139  46.761  1.00 35.99           O  
HETATM 4519  O   HOH A 979      68.178  55.331  42.516  1.00 36.61           O  
HETATM 4520  O   HOH A 980      72.951  46.015  83.864  1.00 38.28           O  
HETATM 4521  O   HOH A 981      80.323  76.361  46.096  1.00 41.69           O  
HETATM 4522  O   HOH A 982      74.595  59.242  63.755  1.00 31.41           O  
HETATM 4523  O   HOH A 983      45.269  29.525  80.727  1.00 47.90           O  
HETATM 4524  O   HOH A 984      65.728  63.476  72.811  1.00 33.08           O  
HETATM 4525  O   HOH A 985      58.575  32.417  83.758  1.00 33.16           O  
HETATM 4526  O   HOH A 986      62.636  61.517  69.085  1.00 33.98           O  
HETATM 4527  O   HOH A 987      67.885  47.248  43.444  1.00 19.05           O  
HETATM 4528  O   HOH A 988      68.955  28.932  80.496  1.00 57.34           O  
HETATM 4529  O   HOH A 989      58.630  25.858  75.373  1.00 40.79           O  
HETATM 4530  O   HOH A 990      82.773  52.459  58.400  1.00 29.32           O  
HETATM 4531  O   HOH A 991      62.700  67.780  65.510  1.00 42.57           O  
HETATM 4532  O   HOH A 992      57.101  60.063  78.654  1.00 52.51           O  
HETATM 4533  O   HOH A 993      85.875  19.364  60.713  1.00 52.67           O  
HETATM 4534  O   HOH A 994      55.762  27.535  81.609  1.00 43.41           O  
HETATM 4535  O   HOH A 995      48.404  37.195  54.523  1.00 28.31           O  
HETATM 4536  O   HOH A 996      56.342  72.697  55.150  1.00 37.93           O  
HETATM 4537  O   HOH A 997      74.543  87.501  59.732  1.00 54.54           O  
HETATM 4538  O   HOH A 998      46.843  46.356  77.392  1.00 49.51           O  
HETATM 4539  O   HOH A 999      58.346  28.939  80.455  1.00 39.54           O  
HETATM 4540  O   HOH A1000      85.941  80.896  47.770  1.00 47.33           O  
HETATM 4541  O   HOH A1001      47.470  26.823  74.479  1.00 37.87           O  
HETATM 4542  O   HOH A1002      79.782  45.571  69.552  1.00 32.29           O  
HETATM 4543  O   HOH A1003      64.532  53.507  45.271  1.00 50.01           O  
HETATM 4544  O   HOH A1004      61.115  27.928  78.757  1.00 38.99           O  
HETATM 4545  O   HOH A1005      43.649  42.379  79.094  1.00 50.03           O  
HETATM 4546  O   HOH A1006      81.345  54.585  58.237  1.00 37.25           O  
HETATM 4547  O   HOH A1007      76.971  43.117  42.541  1.00 35.99           O  
HETATM 4548  O   HOH A1008      66.235  86.573  64.149  1.00 52.89           O  
HETATM 4549  O   HOH A1009      66.767  43.260  83.483  1.00 42.07           O  
HETATM 4550  O   HOH A1010      62.471  59.602  47.480  1.00 49.13           O  
HETATM 4551  O   HOH A1011      87.844  44.510  57.185  1.00 49.46           O  
HETATM 4552  O   HOH A1012      93.483  40.940  66.941  1.00 27.70           O  
HETATM 4553  O   HOH A1013      86.188  70.527  45.594  1.00 52.45           O  
HETATM 4554  O   HOH A1014      95.621  78.016  52.446  1.00 54.14           O  
HETATM 4555  O   HOH A1015      81.970  49.627  44.778  1.00 47.07           O  
HETATM 4556  O   HOH A1016      43.059  36.992  81.644  1.00 27.05           O  
HETATM 4557  O   HOH A1017      68.691  46.569  89.207  1.00 43.76           O  
HETATM 4558  O   HOH A1018      79.959  63.991  45.411  1.00 41.32           O  
HETATM 4559  O   HOH A1019      47.210  40.029  68.252  1.00 45.17           O  
HETATM 4560  O   HOH A1020      72.708  34.408  48.185  1.00 39.86           O  
HETATM 4561  O   HOH A1021      83.206  31.151  47.134  1.00 49.11           O  
HETATM 4562  O   HOH A1022      60.129  56.861  53.162  1.00 40.15           O  
HETATM 4563  O   HOH A1023      63.259  31.356  83.143  1.00 39.72           O  
HETATM 4564  O   HOH A1024      41.668  29.038  68.535  1.00 34.19           O  
HETATM 4565  O   HOH A1025      58.630  56.073  54.960  1.00 50.93           O  
HETATM 4566  O   HOH A1026      69.242  78.314  75.058  1.00 47.44           O  
HETATM 4567  O   HOH A1027      56.893  51.999  85.972  1.00 54.66           O  
HETATM 4568  O   HOH A1028      85.392  42.475  67.350  1.00 41.00           O  
HETATM 4569  O   HOH A1029      57.622  68.022  79.717  1.00 56.33           O  
HETATM 4570  O   HOH A1030      59.199  39.508  40.511  1.00 55.71           O  
HETATM 4571  O   HOH A1031      47.505  28.145  79.972  1.00 40.92           O  
HETATM 4572  O   HOH A1032      86.028  48.314  43.373  1.00 39.56           O  
HETATM 4573  O   HOH A1033      64.354  55.243  52.604  1.00 37.01           O  
HETATM 4574  O   HOH A1034      58.088  56.468  79.176  1.00 46.41           O  
HETATM 4575  O   HOH A1035      49.939  27.966  80.142  1.00 40.37           O  
HETATM 4576  O   HOH A1036      50.969  48.501  48.367  1.00 53.53           O  
HETATM 4577  O   HOH A1037      69.818  47.717  39.732  1.00 34.29           O  
HETATM 4578  O   HOH A1038      64.999  58.606  48.020  1.00 45.15           O  
HETATM 4579  O   HOH A1039      73.943  59.244  68.362  1.00 36.00           O  
HETATM 4580  O   HOH A1040      59.048  73.856  46.611  1.00 52.67           O  
HETATM 4581  O   HOH A1041      85.081  51.569  57.311  1.00 53.06           O  
HETATM 4582  O   HOH A1042      40.550  28.393  70.940  1.00 45.16           O  
HETATM 4583  O   HOH A1043      81.666  53.566  44.786  1.00 52.24           O  
HETATM 4584  O   HOH A1044      49.510  23.168  66.507  1.00 46.19           O  
HETATM 4585  O   HOH A1045      68.456  31.642  86.129  1.00 50.16           O  
HETATM 4586  O   HOH A1046      61.808  56.377  87.643  1.00 51.73           O  
HETATM 4587  O   HOH A1047      57.176  49.878  57.422  1.00 41.52           O  
HETATM 4588  O   HOH A1048      91.790  69.772  47.295  1.00 49.97           O  
HETATM 4589  O   HOH A1049      60.128  25.233  62.858  1.00 37.59           O  
HETATM 4590  O   HOH A1050      65.776  48.085  42.180  1.00 30.41           O  
HETATM 4591  O   HOH A1051      64.361  56.160  48.150  1.00 38.74           O  
HETATM 4592  O   HOH A1052      84.557  51.206  45.288  1.00 49.61           O  
HETATM 4593  O   HOH A1053      59.161  51.908  60.759  1.00 26.03           O  
HETATM 4594  O   HOH A1054      58.354  75.346  65.505  1.00 55.54           O  
HETATM 4595  O   HOH A1055      63.821  48.786  43.850  1.00 52.28           O  
HETATM 4596  O   HOH A1056      85.256  47.320  39.118  1.00 42.53           O  
HETATM 4597  O   HOH A1057      77.733  61.691  65.494  1.00 53.71           O  
HETATM 4598  O   HOH A1058      75.679  61.761  63.386  1.00 33.82           O  
HETATM 4599  O   HOH A1059      61.269  58.779  49.882  1.00 36.78           O  
HETATM 4600  O   HOH A1060      73.131  59.955  65.726  1.00 38.42           O  
HETATM 4601  O   HOH A1061      61.771  55.117  52.581  1.00 41.41           O  
HETATM 4602  O   HOH A1062      62.833  33.241  44.554  1.00 28.89           O  
HETATM 4603  O   HOH A1063      62.527  30.778  80.978  1.00 47.19           O  
HETATM 4604  O   HOH A1064      62.781  46.268  44.388  1.00 39.24           O  
HETATM 4605  O   HOH A1065      79.144  66.202  43.185  1.00 54.40           O  
HETATM 4606  O   HOH A1066      88.730  38.037  36.264  1.00 29.87           O  
HETATM 4607  O   HOH A1067      56.438  58.319  77.413  1.00 51.83           O  
HETATM 4608  O   HOH A1068      74.203  29.067  43.476  1.00 53.78           O  
HETATM 4609  O   HOH A1069      59.831  52.961  54.511  1.00 39.55           O  
HETATM 4610  O   HOH A1070      63.619  22.648  59.990  1.00 71.12           O  
HETATM 4611  O   HOH A1071      47.945  27.217  70.137  1.00 54.99           O  
HETATM 4612  O   HOH A1072      56.699  53.143  60.117  1.00 29.99           O  
HETATM 4613  O   HOH A1073      46.052  41.650  54.776  1.00 39.73           O  
HETATM 4614  O   HOH A1074      53.954  52.863  60.547  1.00 44.72           O  
HETATM 4615  O   HOH A1075      66.118  49.714  40.137  1.00 42.27           O  
CONECT 4216 4217 4218 4219 4220                                                 
CONECT 4217 4216                                                                
CONECT 4218 4216                                                                
CONECT 4219 4216                                                                
CONECT 4220 4216                                                                
CONECT 4221 4222 4223 4224 4225                                                 
CONECT 4222 4221                                                                
CONECT 4223 4221                                                                
CONECT 4224 4221                                                                
CONECT 4225 4221                                                                
CONECT 4226 4227 4228 4229 4230                                                 
CONECT 4227 4226                                                                
CONECT 4228 4226                                                                
CONECT 4229 4226                                                                
CONECT 4230 4226                                                                
CONECT 4231 4232 4233 4234 4235                                                 
CONECT 4232 4231                                                                
CONECT 4233 4231                                                                
CONECT 4234 4231                                                                
CONECT 4235 4231                                                                
CONECT 4236 4237 4238 4239 4240                                                 
CONECT 4237 4236                                                                
CONECT 4238 4236                                                                
CONECT 4239 4236                                                                
CONECT 4240 4236                                                                
MASTER      600    0    5   19   37    0    6    6 4559    1   25   44          
END                                                                             



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