CNRS Nantes University US2B US2B
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***  H3N2  ***

elNémo ID: 2410211853501393066

Job options:

ID        	=	 2410211853501393066
JOBID     	=	 H3N2
USERID    	=	 lupuga_al
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 H3N2

HEADER    VIRAL PROTEIN                           19-JUN-12   4FNK              
TITLE     CRYSTAL STRUCTURE OF THE A/HONG KONG/1/1968 (H3N2) INFLUENZA VIRUS    
TITLE    2 HEMAGGLUTININ                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEMAGGLUTININ HA1 CHAIN;                                   
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 27-345;                                       
COMPND   5 SYNONYM: HEMAGGLUTININ RECEPTOR BINDING SUBUNIT HA1;                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HEMAGGLUTININ HA2 CHAIN;                                   
COMPND   9 CHAIN: B, D, F;                                                      
COMPND  10 FRAGMENT: UNP RESIDUES 346-519;                                      
COMPND  11 SYNONYM: HEMAGGLUTININ FUSION SUBUNIT HA2;                           
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;                              
SOURCE   3 ORGANISM_TAXID: 506350;                                              
SOURCE   4 STRAIN: A/HONG KONG/1/1968 H3N2;                                     
SOURCE   5 GENE: HA;                                                            
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HIGH FIVE;                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;                              
SOURCE  13 ORGANISM_TAXID: 506350;                                              
SOURCE  14 STRAIN: A/HONG KONG/1/1968 H3N2;                                     
SOURCE  15 GENE: HA;                                                            
SOURCE  16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  17 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: HIGH FIVE;                                 
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    VIRAL FUSION PROTEIN, VIRUS ATTACHMENT AND ENTRY, VIRAL PROTEIN       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.C.EKIERT,I.A.WILSON                                                 
REVDAT   5   13-SEP-23 4FNK    1       HETSYN                                   
REVDAT   4   29-JUL-20 4FNK    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   10-OCT-12 4FNK    1       JRNL                                     
REVDAT   2   03-OCT-12 4FNK    1       JRNL                                     
REVDAT   1   19-SEP-12 4FNK    0                                                
JRNL        AUTH   D.C.EKIERT,A.K.KASHYAP,J.STEEL,A.RUBRUM,G.BHABHA,R.KHAYAT,   
JRNL        AUTH 2 J.H.LEE,M.A.DILLON,R.E.O'NEIL,A.M.FAYNBOYM,M.HOROWITZ,       
JRNL        AUTH 3 L.HOROWITZ,A.B.WARD,P.PALESE,R.WEBBY,R.A.LERNER,R.R.BHATT,   
JRNL        AUTH 4 I.A.WILSON                                                   
JRNL        TITL   CROSS-NEUTRALIZATION OF INFLUENZA A VIRUSES MEDIATED BY A    
JRNL        TITL 2 SINGLE ANTIBODY LOOP.                                        
JRNL        REF    NATURE                        V. 489   526 2012              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   22982990                                                     
JRNL        DOI    10.1038/NATURE11414                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)                    
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 215391                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10817                           
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 43.0749 -  5.9026    1.00     7206   383  0.2231 0.2337        
REMARK   3     2  5.9026 -  4.6869    1.00     7037   354  0.1626 0.1738        
REMARK   3     3  4.6869 -  4.0950    1.00     6948   357  0.1325 0.1475        
REMARK   3     4  4.0950 -  3.7208    1.00     6934   355  0.1432 0.1650        
REMARK   3     5  3.7208 -  3.4542    1.00     6930   351  0.1512 0.1719        
REMARK   3     6  3.4542 -  3.2506    1.00     6884   367  0.1463 0.1771        
REMARK   3     7  3.2506 -  3.0879    1.00     6847   368  0.1453 0.1791        
REMARK   3     8  3.0879 -  2.9535    1.00     6902   357  0.1417 0.1618        
REMARK   3     9  2.9535 -  2.8398    1.00     6845   385  0.1459 0.1850        
REMARK   3    10  2.8398 -  2.7419    1.00     6862   338  0.1479 0.1893        
REMARK   3    11  2.7419 -  2.6561    1.00     6797   384  0.1455 0.1727        
REMARK   3    12  2.6561 -  2.5802    1.00     6852   361  0.1455 0.1873        
REMARK   3    13  2.5802 -  2.5123    1.00     6829   340  0.1454 0.1829        
REMARK   3    14  2.5123 -  2.4510    1.00     6787   397  0.1477 0.1875        
REMARK   3    15  2.4510 -  2.3953    1.00     6791   359  0.1546 0.1836        
REMARK   3    16  2.3953 -  2.3443    1.00     6809   379  0.1477 0.1894        
REMARK   3    17  2.3443 -  2.2974    1.00     6772   343  0.1493 0.1869        
REMARK   3    18  2.2974 -  2.2541    1.00     6833   349  0.1543 0.1903        
REMARK   3    19  2.2541 -  2.2138    1.00     6797   358  0.1587 0.1927        
REMARK   3    20  2.2138 -  2.1763    1.00     6782   373  0.1621 0.1997        
REMARK   3    21  2.1763 -  2.1412    1.00     6770   340  0.1637 0.1955        
REMARK   3    22  2.1412 -  2.1083    1.00     6819   338  0.1681 0.1923        
REMARK   3    23  2.1083 -  2.0773    1.00     6831   336  0.1770 0.2258        
REMARK   3    24  2.0773 -  2.0480    1.00     6718   387  0.1843 0.2113        
REMARK   3    25  2.0480 -  2.0203    1.00     6774   376  0.1904 0.2041        
REMARK   3    26  2.0203 -  1.9941    0.99     6763   336  0.2047 0.2256        
REMARK   3    27  1.9941 -  1.9692    0.99     6723   388  0.2164 0.2404        
REMARK   3    28  1.9692 -  1.9454    0.99     6700   349  0.2372 0.2550        
REMARK   3    29  1.9454 -  1.9228    0.97     6601   354  0.2578 0.2740        
REMARK   3    30  1.9228 -  1.9012    0.94     6431   355  0.2769 0.2940        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.73                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 60.12                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.810           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.53380                                              
REMARK   3    B22 (A**2) : -4.53090                                             
REMARK   3    B33 (A**2) : 1.99710                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.014          12805                                  
REMARK   3   ANGLE     :  1.422          17463                                  
REMARK   3   CHIRALITY :  0.088           1967                                  
REMARK   3   PLANARITY :  0.007           2252                                  
REMARK   3   DIHEDRAL  : 19.779           4849                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 31                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 9:33)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3916   5.2908 -35.8540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0995 T22:   0.0939                                     
REMARK   3      T33:   0.1420 T12:  -0.0207                                     
REMARK   3      T13:  -0.0021 T23:   0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4925 L22:   2.0271                                     
REMARK   3      L33:   1.9481 L12:   1.7092                                     
REMARK   3      L13:   0.9384 L23:   1.2194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0962 S12:   0.0956 S13:   0.0851                       
REMARK   3      S21:  -0.3001 S22:   0.0833 S23:   0.0402                       
REMARK   3      S31:  -0.2961 S32:   0.0571 S33:   0.0553                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 34:89)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8287 -38.6047 -41.1062              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1287 T22:   0.1468                                     
REMARK   3      T33:   0.2173 T12:   0.0317                                     
REMARK   3      T13:  -0.0488 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2331 L22:   2.1647                                     
REMARK   3      L33:   0.0848 L12:  -0.6743                                     
REMARK   3      L13:  -0.0838 L23:   0.3451                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0044 S12:  -0.0175 S13:   0.0840                       
REMARK   3      S21:   0.1646 S22:   0.0785 S23:  -0.5443                       
REMARK   3      S31:   0.0435 S32:   0.0996 S33:  -0.0642                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 90:288)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5232 -61.2680 -46.5073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0958 T22:   0.1401                                     
REMARK   3      T33:   0.1439 T12:   0.0238                                     
REMARK   3      T13:  -0.0367 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9698 L22:   1.7610                                     
REMARK   3      L33:   1.0794 L12:   0.0308                                     
REMARK   3      L13:   0.0126 L23:   0.0490                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0313 S12:   0.0519 S13:  -0.1905                       
REMARK   3      S21:   0.0098 S22:  -0.0358 S23:  -0.0716                       
REMARK   3      S31:   0.1946 S32:  -0.1641 S33:   0.0140                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 289:326)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9189 -15.1280 -39.6419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0715 T22:   0.1143                                     
REMARK   3      T33:   0.1426 T12:   0.0052                                     
REMARK   3      T13:   0.0083 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4456 L22:   4.8284                                     
REMARK   3      L33:   0.9944 L12:  -0.1335                                     
REMARK   3      L13:   0.0208 L23:   2.0814                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0134 S12:   0.0187 S13:   0.0212                       
REMARK   3      S21:  -0.0984 S22:   0.0666 S23:  -0.3218                       
REMARK   3      S31:  -0.0443 S32:   0.1274 S33:  -0.0275                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 1:30)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4362  12.6868 -27.5147              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1074 T22:   0.1559                                     
REMARK   3      T33:   0.2230 T12:  -0.0449                                     
REMARK   3      T13:   0.0163 T23:  -0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9158 L22:   1.9262                                     
REMARK   3      L33:   1.6309 L12:   0.8393                                     
REMARK   3      L13:   0.7069 L23:   0.4479                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0518 S12:  -0.0953 S13:   0.2679                       
REMARK   3      S21:   0.0339 S22:  -0.0041 S23:  -0.1272                       
REMARK   3      S31:  -0.1730 S32:   0.1349 S33:   0.0337                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 31:55)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5531  -1.1361 -23.0078              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0913 T22:   0.1383                                     
REMARK   3      T33:   0.1499 T12:  -0.0051                                     
REMARK   3      T13:  -0.0117 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0025 L22:   6.6585                                     
REMARK   3      L33:   1.3555 L12:   3.9454                                     
REMARK   3      L13:   0.8912 L23:   1.5233                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0178 S12:  -0.0216 S13:  -0.0358                       
REMARK   3      S21:   0.2553 S22:   0.1352 S23:  -0.3574                       
REMARK   3      S31:   0.0274 S32:   0.1487 S33:  -0.0961                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 56:75)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0559 -35.1309 -42.4556              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1849 T22:   0.1772                                     
REMARK   3      T33:   0.1726 T12:   0.0521                                     
REMARK   3      T13:  -0.0342 T23:  -0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9009 L22:   2.2543                                     
REMARK   3      L33:   1.1451 L12:   0.8079                                     
REMARK   3      L13:   0.6466 L23:  -0.3832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1312 S12:  -0.1798 S13:   0.0731                       
REMARK   3      S21:   0.3694 S22:   0.0671 S23:  -0.2409                       
REMARK   3      S31:  -0.0772 S32:   0.1202 S33:  -0.1522                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 76:158)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0474   0.7889 -28.4141              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0739 T22:   0.1240                                     
REMARK   3      T33:   0.1293 T12:  -0.0083                                     
REMARK   3      T13:   0.0009 T23:  -0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2311 L22:   2.4481                                     
REMARK   3      L33:   1.0406 L12:   0.1919                                     
REMARK   3      L13:   0.1214 L23:   1.3001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0150 S12:  -0.0261 S13:   0.0937                       
REMARK   3      S21:  -0.0484 S22:   0.0492 S23:  -0.0405                       
REMARK   3      S31:  -0.1105 S32:   0.0764 S33:  -0.0336                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 159:172)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4644  30.1032 -10.6423              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2711 T22:   0.2514                                     
REMARK   3      T33:   0.4167 T12:  -0.0012                                     
REMARK   3      T13:  -0.0019 T23:  -0.1731                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9215 L22:   3.4792                                     
REMARK   3      L33:   7.1863 L12:   2.5659                                     
REMARK   3      L13:   0.3673 L23:  -0.1225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0445 S12:  -0.3628 S13:   0.7205                       
REMARK   3      S21:   0.4306 S22:  -0.0228 S23:   0.3792                       
REMARK   3      S31:  -0.9332 S32:  -0.0506 S33:   0.0631                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 9:33)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   9.3294  -3.8887 -11.8272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0808 T22:   0.1411                                     
REMARK   3      T33:   0.0576 T12:  -0.0020                                     
REMARK   3      T13:  -0.0282 T23:  -0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2803 L22:   1.9478                                     
REMARK   3      L33:   2.2987 L12:  -0.3881                                     
REMARK   3      L13:  -0.5882 L23:   1.0652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0936 S12:  -0.1286 S13:   0.0431                       
REMARK   3      S21:   0.1777 S22:   0.1135 S23:  -0.1524                       
REMARK   3      S31:   0.0811 S32:   0.1306 S33:  -0.0366                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 34:89)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4879 -44.7026 -27.2103              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1577 T22:   0.1722                                     
REMARK   3      T33:   0.1742 T12:  -0.0659                                     
REMARK   3      T13:   0.0349 T23:  -0.0361                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1613 L22:   2.0552                                     
REMARK   3      L33:   0.2586 L12:   0.5664                                     
REMARK   3      L13:   0.1567 L23:   0.6374                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0995 S12:  -0.1061 S13:   0.0380                       
REMARK   3      S21:   0.3160 S22:  -0.2050 S23:   0.2966                       
REMARK   3      S31:   0.1441 S32:  -0.1661 S33:   0.0969                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 90:175)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.2557 -64.8352 -44.5074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2028 T22:   0.1857                                     
REMARK   3      T33:   0.1692 T12:  -0.0694                                     
REMARK   3      T13:  -0.0141 T23:  -0.0342                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6226 L22:   1.5270                                     
REMARK   3      L33:   0.9701 L12:   0.2963                                     
REMARK   3      L13:   0.2732 L23:   0.5941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0534 S12:   0.1998 S13:  -0.1051                       
REMARK   3      S21:   0.0027 S22:  -0.1200 S23:   0.1930                       
REMARK   3      S31:   0.2674 S32:  -0.1633 S33:   0.0534                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 176:195)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2472 -72.1214 -48.6703              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2573 T22:   0.2350                                     
REMARK   3      T33:   0.1988 T12:  -0.0036                                     
REMARK   3      T13:  -0.0138 T23:  -0.0897                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9815 L22:   1.8281                                     
REMARK   3      L33:   1.8943 L12:  -0.2026                                     
REMARK   3      L13:   0.3920 L23:   1.0720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1724 S12:   0.3521 S13:  -0.5139                       
REMARK   3      S21:  -0.0036 S22:  -0.0059 S23:  -0.1498                       
REMARK   3      S31:   0.4668 S32:   0.2995 S33:  -0.1563                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 196:249)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.4378 -65.2577 -51.9610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1244 T22:   0.2870                                     
REMARK   3      T33:   0.1271 T12:  -0.0022                                     
REMARK   3      T13:   0.0144 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0522 L22:   2.8517                                     
REMARK   3      L33:   1.5140 L12:  -0.1459                                     
REMARK   3      L13:   0.2321 L23:   0.0919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1769 S12:   0.5384 S13:   0.0422                       
REMARK   3      S21:  -0.2676 S22:  -0.1905 S23:  -0.0781                       
REMARK   3      S31:   0.1006 S32:   0.2301 S33:  -0.0242                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 250:300)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7884 -43.6674 -31.9724              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1197 T22:   0.1571                                     
REMARK   3      T33:   0.1717 T12:  -0.0328                                     
REMARK   3      T13:   0.0159 T23:  -0.0310                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5972 L22:   1.7022                                     
REMARK   3      L33:   0.0761 L12:   0.9040                                     
REMARK   3      L13:   0.1938 L23:   0.2195                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0460 S12:  -0.0021 S13:   0.1774                       
REMARK   3      S21:   0.1644 S22:  -0.1164 S23:   0.3569                       
REMARK   3      S31:   0.0513 S32:  -0.1006 S33:   0.0761                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 301:325)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0459 -20.2931 -20.8098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1204 T22:   0.1145                                     
REMARK   3      T33:   0.0785 T12:  -0.0064                                     
REMARK   3      T13:  -0.0054 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3583 L22:   4.1005                                     
REMARK   3      L33:   1.6665 L12:  -0.1834                                     
REMARK   3      L13:  -0.2692 L23:   1.8495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0212 S12:  -0.0930 S13:   0.0011                       
REMARK   3      S21:   0.2984 S22:   0.0584 S23:  -0.0177                       
REMARK   3      S31:   0.1650 S32:   0.0612 S33:  -0.0978                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 1:10)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7066   3.2345 -16.9182              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1275 T22:   0.1402                                     
REMARK   3      T33:   0.1497 T12:  -0.0030                                     
REMARK   3      T13:   0.0139 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3208 L22:   4.6552                                     
REMARK   3      L33:   5.3935 L12:   0.4558                                     
REMARK   3      L13:  -1.2350 L23:   1.9459                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0237 S12:  -0.0045 S13:   0.1320                       
REMARK   3      S21:  -0.0371 S22:  -0.0903 S23:  -0.1984                       
REMARK   3      S31:  -0.0335 S32:   0.1908 S33:   0.0659                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 11:22)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2683  -0.7150  -7.0781              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2006 T22:   0.1526                                     
REMARK   3      T33:   0.0640 T12:   0.0045                                     
REMARK   3      T13:   0.0089 T23:  -0.0309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6350 L22:   3.8372                                     
REMARK   3      L33:   6.0261 L12:  -0.8917                                     
REMARK   3      L13:   1.7628 L23:   0.9131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0088 S12:  -0.4831 S13:   0.0538                       
REMARK   3      S21:   0.3898 S22:  -0.0073 S23:   0.0735                       
REMARK   3      S31:  -0.1175 S32:  -0.0720 S33:   0.0403                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 23:55)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0621   0.6178 -13.4761              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1063 T22:   0.1744                                     
REMARK   3      T33:   0.1048 T12:   0.0014                                     
REMARK   3      T13:   0.0179 T23:  -0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8413 L22:   4.5525                                     
REMARK   3      L33:   5.6462 L12:   0.1257                                     
REMARK   3      L13:   0.4268 L23:   4.3632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0532 S12:  -0.1359 S13:   0.1068                       
REMARK   3      S21:   0.1079 S22:  -0.2036 S23:   0.3325                       
REMARK   3      S31:  -0.0511 S32:  -0.2839 S33:   0.2157                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 56:75)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1107 -38.3613 -35.1197              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1479 T22:   0.1461                                     
REMARK   3      T33:   0.2042 T12:  -0.0230                                     
REMARK   3      T13:   0.0002 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5076 L22:   1.5995                                     
REMARK   3      L33:   3.3640 L12:   0.6264                                     
REMARK   3      L13:  -0.2782 L23:   0.7933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0426 S12:  -0.0876 S13:   0.0871                       
REMARK   3      S21:   0.1752 S22:  -0.1070 S23:   0.4883                       
REMARK   3      S31:  -0.1207 S32:  -0.3065 S33:   0.1246                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 76:137)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0118  -9.2006 -25.6661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0811 T22:   0.1203                                     
REMARK   3      T33:   0.0856 T12:  -0.0056                                     
REMARK   3      T13:  -0.0023 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4053 L22:   4.6748                                     
REMARK   3      L33:   1.3261 L12:  -0.8511                                     
REMARK   3      L13:  -0.4026 L23:   2.2835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0208 S12:  -0.0367 S13:   0.0723                       
REMARK   3      S21:   0.0426 S22:   0.0115 S23:  -0.0987                       
REMARK   3      S31:  -0.0294 S32:  -0.0044 S33:  -0.0303                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 138:171)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6035  23.0029  -7.9579              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1974 T22:   0.1825                                     
REMARK   3      T33:   0.2832 T12:   0.0587                                     
REMARK   3      T13:  -0.0312 T23:  -0.0938                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9689 L22:   4.3320                                     
REMARK   3      L33:   1.8221 L12:  -0.3699                                     
REMARK   3      L13:  -0.5386 L23:  -0.0656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0555 S12:  -0.1810 S13:   0.4997                       
REMARK   3      S21:   0.1474 S22:  -0.0015 S23:   0.2707                       
REMARK   3      S31:  -0.2845 S32:  -0.0679 S33:  -0.0487                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESSEQ 10:153)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9755 -31.7270 -65.3631              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1756 T22:   0.1820                                     
REMARK   3      T33:   0.0337 T12:   0.0475                                     
REMARK   3      T13:  -0.0459 T23:  -0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1775 L22:   0.3835                                     
REMARK   3      L33:   0.3383 L12:   0.0313                                     
REMARK   3      L13:   0.0071 L23:   0.2249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0102 S12:   0.1199 S13:   0.0427                       
REMARK   3      S21:  -0.1552 S22:  -0.0265 S23:   0.0412                       
REMARK   3      S31:   0.0038 S32:  -0.0136 S33:   0.0400                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESSEQ 154:249)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2348 -58.9297 -70.0990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2720 T22:   0.2245                                     
REMARK   3      T33:   0.1220 T12:   0.0726                                     
REMARK   3      T13:  -0.0190 T23:  -0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9608 L22:   1.3421                                     
REMARK   3      L33:   1.6999 L12:   0.4891                                     
REMARK   3      L13:  -0.4328 L23:   0.1518                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0505 S12:  -0.0162 S13:  -0.2791                       
REMARK   3      S21:   0.0353 S22:   0.0200 S23:  -0.1888                       
REMARK   3      S31:   0.3767 S32:   0.1535 S33:   0.0109                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESSEQ 250:288)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9626 -32.7372 -68.2631              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2034 T22:   0.2073                                     
REMARK   3      T33:   0.0989 T12:   0.0266                                     
REMARK   3      T13:  -0.0284 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4808 L22:   1.3989                                     
REMARK   3      L33:   1.3794 L12:  -0.1997                                     
REMARK   3      L13:  -0.2116 L23:   0.8461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0782 S12:   0.1089 S13:   0.0858                       
REMARK   3      S21:  -0.2743 S22:  -0.0387 S23:  -0.0099                       
REMARK   3      S31:  -0.2657 S32:   0.0335 S33:  -0.0364                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESSEQ 289:326)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.4797 -11.7932 -47.4562              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0866 T22:   0.1276                                     
REMARK   3      T33:   0.1179 T12:   0.0257                                     
REMARK   3      T13:  -0.0321 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1816 L22:   4.1383                                     
REMARK   3      L33:   1.1365 L12:  -0.3742                                     
REMARK   3      L13:  -0.0171 L23:   1.7533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0138 S12:   0.0472 S13:   0.0309                       
REMARK   3      S21:  -0.1618 S22:  -0.1147 S23:   0.2849                       
REMARK   3      S31:  -0.1126 S32:  -0.1194 S33:   0.0907                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESSEQ 1:30)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5386  16.4334 -36.1025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1480 T22:   0.1449                                     
REMARK   3      T33:   0.2059 T12:   0.0468                                     
REMARK   3      T13:  -0.0693 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5300 L22:   3.5809                                     
REMARK   3      L33:   0.7187 L12:  -0.0451                                     
REMARK   3      L13:  -0.5222 L23:  -0.4058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1055 S12:  -0.0200 S13:   0.2624                       
REMARK   3      S21:  -0.0322 S22:  -0.1029 S23:   0.0040                       
REMARK   3      S31:  -0.2692 S32:  -0.1322 S33:   0.1040                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESSEQ 31:55)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4115   8.5916 -44.3144              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1240 T22:   0.1116                                     
REMARK   3      T33:   0.1238 T12:   0.0139                                     
REMARK   3      T13:  -0.0143 T23:   0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0086 L22:   7.2338                                     
REMARK   3      L33:   0.8664 L12:  -2.9726                                     
REMARK   3      L13:  -0.5472 L23:   1.0771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0896 S12:   0.0380 S13:   0.1744                       
REMARK   3      S21:  -0.5555 S22:  -0.0636 S23:  -0.0364                       
REMARK   3      S31:  -0.2535 S32:  -0.0484 S33:  -0.0214                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESSEQ 56:75)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8120 -30.4507 -54.5205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2070 T22:   0.1589                                     
REMARK   3      T33:   0.1258 T12:   0.0065                                     
REMARK   3      T13:  -0.0256 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7735 L22:   1.5904                                     
REMARK   3      L33:   2.2780 L12:  -1.0451                                     
REMARK   3      L13:  -0.0345 L23:  -0.1587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0237 S12:   0.1275 S13:   0.2463                       
REMARK   3      S21:  -0.5210 S22:  -0.0327 S23:   0.0465                       
REMARK   3      S31:  -0.1613 S32:   0.0215 S33:   0.0418                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESSEQ 76:132)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3924  -6.2707 -36.8074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0892 T22:   0.1149                                     
REMARK   3      T33:   0.1199 T12:   0.0127                                     
REMARK   3      T13:  -0.0179 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1348 L22:   6.0160                                     
REMARK   3      L33:   0.4995 L12:   0.1758                                     
REMARK   3      L13:   0.0543 L23:   1.4604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0095 S12:  -0.0008 S13:   0.0733                       
REMARK   3      S21:   0.0405 S22:  -0.0459 S23:   0.0789                       
REMARK   3      S31:  -0.0248 S32:  -0.0457 S33:   0.0308                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESSEQ 133:171)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1681  31.3372 -29.8129              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2834 T22:   0.1339                                     
REMARK   3      T33:   0.3156 T12:  -0.0021                                     
REMARK   3      T13:  -0.0801 T23:  -0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7962 L22:   3.3368                                     
REMARK   3      L33:   1.6282 L12:   0.2921                                     
REMARK   3      L13:  -1.0018 L23:   0.0506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0132 S12:  -0.0602 S13:   0.4765                       
REMARK   3      S21:   0.0045 S22:   0.0043 S23:   0.0779                       
REMARK   3      S31:  -0.5127 S32:   0.0414 S33:  -0.0162                       
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 4FNK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073122.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-09                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.066                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 215875                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.15000                            
REMARK 200   FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.65000                            
REMARK 200   FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2VIU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, 100 MM SODIUM    
REMARK 280  CACODYLATE, PH 6.5, 200 MM SODIUM CHLORIDE, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
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      173.87550            
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      173.87550            
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       52.57450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       75.72900            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       52.57450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       75.72900            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      173.87550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       52.57450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       75.72900            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      173.87550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       52.57450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       75.72900            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 41460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 57230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O                         
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 D 515  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     GLN A   327                                                      
REMARK 465     THR A   328                                                      
REMARK 465     ARG A   329                                                      
REMARK 465     ILE B   173                                                      
REMARK 465     LYS B   174                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     LYS C   326                                                      
REMARK 465     GLN C   327                                                      
REMARK 465     THR C   328                                                      
REMARK 465     ARG C   329                                                      
REMARK 465     GLN D   172                                                      
REMARK 465     ILE D   173                                                      
REMARK 465     LYS D   174                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     ASP E     8                                                      
REMARK 465     GLN E   327                                                      
REMARK 465     THR E   328                                                      
REMARK 465     ARG E   329                                                      
REMARK 465     GLN F   172                                                      
REMARK 465     ILE F   173                                                      
REMARK 465     LYS F   174                                                      
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   OE1  GLU C   325     O    HOH C   848              2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL A 323   CB    VAL A 323   CG2    -0.130                       
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    ILE A  62     -114.41     50.42                                   
REMARK 500    ASN A  96       43.62   -145.57                                   
REMARK 500    CYS A  97     -155.40   -138.05                                   
REMARK 500    VAL A 196      -57.73     67.68                                   
REMARK 500    THR A 206     -167.89   -119.13                                   
REMARK 500    ALA B   5      -66.31    -93.38                                   
REMARK 500    LYS B  58       75.10     51.39                                   
REMARK 500    PHE B  63     -108.79   -120.08                                   
REMARK 500    GLN B  65     -141.08   -127.53                                   
REMARK 500    ARG B 127     -124.21     52.53                                   
REMARK 500    TYR B 141       38.52    -96.01                                   
REMARK 500    ILE C  62     -113.14     48.62                                   
REMARK 500    ASN C  96       39.00   -147.10                                   
REMARK 500    CYS C  97     -153.67   -133.26                                   
REMARK 500    VAL C 196      -57.29     67.32                                   
REMARK 500    ARG C 201      142.15   -172.99                                   
REMARK 500    ARG C 201      127.55   -177.62                                   
REMARK 500    ALA D   5      -67.46    -96.29                                   
REMARK 500    LYS D  58       82.70     40.68                                   
REMARK 500    PHE D  63     -109.00   -122.43                                   
REMARK 500    GLN D  65     -134.36   -125.76                                   
REMARK 500    ARG D 127     -126.09     48.24                                   
REMARK 500    TYR D 141       35.86    -95.63                                   
REMARK 500    ILE E  62     -111.44     49.96                                   
REMARK 500    ASN E  96       44.16   -146.28                                   
REMARK 500    CYS E  97     -159.28   -137.60                                   
REMARK 500    VAL E 196      -56.67     65.48                                   
REMARK 500    ALA F   5      -66.37    -96.17                                   
REMARK 500    LYS F  58       92.65     49.22                                   
REMARK 500    ASN F  60      154.87    -39.44                                   
REMARK 500    PHE F  63     -108.52   -121.61                                   
REMARK 500    GLN F  65     -136.53   -126.50                                   
REMARK 500    ARG F 127     -123.60     60.13                                   
REMARK 500    TYR F 141       36.38    -90.55                                   
REMARK 500    ASP F 145     -169.19    -73.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FNL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FP8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FQR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: EMD-2138   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-2139   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-2140   RELATED DB: EMDB                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 HEMAGGLUTININ HA2 RESIDUE GLY 468 IS CORRECT (ALSO PRESENT IN PDB    
REMARK 999 ENTRIES 3SDY AND 4FQL).                                              
DBREF  4FNK A   11   329  UNP    Q91MA7   HEMA_I68A4      27    345             
DBREF  4FNK B    1   174  UNP    Q91MA7   HEMA_I68A4     346    519             
DBREF  4FNK C   11   329  UNP    Q91MA7   HEMA_I68A4      27    345             
DBREF  4FNK D    1   174  UNP    Q91MA7   HEMA_I68A4     346    519             
DBREF  4FNK E   11   329  UNP    Q91MA7   HEMA_I68A4      27    345             
DBREF  4FNK F    1   174  UNP    Q91MA7   HEMA_I68A4     346    519             
SEQADV 4FNK ALA A    7  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK ASP A    8  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK PRO A    9  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK GLY A   10  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK GLY B  123  UNP  Q91MA7    ARG   468 SEE REMARK 999                 
SEQADV 4FNK ALA C    7  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK ASP C    8  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK PRO C    9  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK GLY C   10  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK GLY D  123  UNP  Q91MA7    ARG   468 SEE REMARK 999                 
SEQADV 4FNK ALA E    7  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK ASP E    8  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK PRO E    9  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK GLY E   10  UNP  Q91MA7              EXPRESSION TAG                 
SEQADV 4FNK GLY F  123  UNP  Q91MA7    ARG   468 SEE REMARK 999                 
SEQRES   1 A  323  ALA ASP PRO GLY ALA THR LEU CYS LEU GLY HIS HIS ALA          
SEQRES   2 A  323  VAL PRO ASN GLY THR LEU VAL LYS THR ILE THR ASP ASP          
SEQRES   3 A  323  GLN ILE GLU VAL THR ASN ALA THR GLU LEU VAL GLN SER          
SEQRES   4 A  323  SER SER THR GLY LYS ILE CYS ASN ASN PRO HIS ARG ILE          
SEQRES   5 A  323  LEU ASP GLY ILE ASP CYS THR LEU ILE ASP ALA LEU LEU          
SEQRES   6 A  323  GLY ASP PRO HIS CYS ASP VAL PHE GLN ASN GLU THR TRP          
SEQRES   7 A  323  ASP LEU PHE VAL GLU ARG SER LYS ALA PHE SER ASN CYS          
SEQRES   8 A  323  TYR PRO TYR ASP VAL PRO ASP TYR ALA SER LEU ARG SER          
SEQRES   9 A  323  LEU VAL ALA SER SER GLY THR LEU GLU PHE ILE THR GLU          
SEQRES  10 A  323  GLY PHE THR TRP THR GLY VAL THR GLN ASN GLY GLY SER          
SEQRES  11 A  323  ASN ALA CYS LYS ARG GLY PRO GLY SER GLY PHE PHE SER          
SEQRES  12 A  323  ARG LEU ASN TRP LEU THR LYS SER GLY SER THR TYR PRO          
SEQRES  13 A  323  VAL LEU ASN VAL THR MET PRO ASN ASN ASP ASN PHE ASP          
SEQRES  14 A  323  LYS LEU TYR ILE TRP GLY VAL HIS HIS PRO SER THR ASN          
SEQRES  15 A  323  GLN GLU GLN THR SER LEU TYR VAL GLN ALA SER GLY ARG          
SEQRES  16 A  323  VAL THR VAL SER THR ARG ARG SER GLN GLN THR ILE ILE          
SEQRES  17 A  323  PRO ASN ILE GLY SER ARG PRO TRP VAL ARG GLY LEU SER          
SEQRES  18 A  323  SER ARG ILE SER ILE TYR TRP THR ILE VAL LYS PRO GLY          
SEQRES  19 A  323  ASP VAL LEU VAL ILE ASN SER ASN GLY ASN LEU ILE ALA          
SEQRES  20 A  323  PRO ARG GLY TYR PHE LYS MET ARG THR GLY LYS SER SER          
SEQRES  21 A  323  ILE MET ARG SER ASP ALA PRO ILE ASP THR CYS ILE SER          
SEQRES  22 A  323  GLU CYS ILE THR PRO ASN GLY SER ILE PRO ASN ASP LYS          
SEQRES  23 A  323  PRO PHE GLN ASN VAL ASN LYS ILE THR TYR GLY ALA CYS          
SEQRES  24 A  323  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR          
SEQRES  25 A  323  GLY MET ARG ASN VAL PRO GLU LYS GLN THR ARG                  
SEQRES   1 B  174  GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY          
SEQRES   2 B  174  TRP GLU GLY MET ILE ASP GLY TRP TYR GLY PHE ARG HIS          
SEQRES   3 B  174  GLN ASN SER GLU GLY THR GLY GLN ALA ALA ASP LEU LYS          
SEQRES   4 B  174  SER THR GLN ALA ALA ILE ASP GLN ILE ASN GLY LYS LEU          
SEQRES   5 B  174  ASN ARG VAL ILE GLU LYS THR ASN GLU LYS PHE HIS GLN          
SEQRES   6 B  174  ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN          
SEQRES   7 B  174  ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU          
SEQRES   8 B  174  TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN          
SEQRES   9 B  174  GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS          
SEQRES  10 B  174  LEU PHE GLU LYS THR GLY ARG GLN LEU ARG GLU ASN ALA          
SEQRES  11 B  174  GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS          
SEQRES  12 B  174  CYS ASP ASN ALA CYS ILE GLU SER ILE ARG ASN GLY THR          
SEQRES  13 B  174  TYR ASP HIS ASP VAL TYR ARG ASP GLU ALA LEU ASN ASN          
SEQRES  14 B  174  ARG PHE GLN ILE LYS                                          
SEQRES   1 C  323  ALA ASP PRO GLY ALA THR LEU CYS LEU GLY HIS HIS ALA          
SEQRES   2 C  323  VAL PRO ASN GLY THR LEU VAL LYS THR ILE THR ASP ASP          
SEQRES   3 C  323  GLN ILE GLU VAL THR ASN ALA THR GLU LEU VAL GLN SER          
SEQRES   4 C  323  SER SER THR GLY LYS ILE CYS ASN ASN PRO HIS ARG ILE          
SEQRES   5 C  323  LEU ASP GLY ILE ASP CYS THR LEU ILE ASP ALA LEU LEU          
SEQRES   6 C  323  GLY ASP PRO HIS CYS ASP VAL PHE GLN ASN GLU THR TRP          
SEQRES   7 C  323  ASP LEU PHE VAL GLU ARG SER LYS ALA PHE SER ASN CYS          
SEQRES   8 C  323  TYR PRO TYR ASP VAL PRO ASP TYR ALA SER LEU ARG SER          
SEQRES   9 C  323  LEU VAL ALA SER SER GLY THR LEU GLU PHE ILE THR GLU          
SEQRES  10 C  323  GLY PHE THR TRP THR GLY VAL THR GLN ASN GLY GLY SER          
SEQRES  11 C  323  ASN ALA CYS LYS ARG GLY PRO GLY SER GLY PHE PHE SER          
SEQRES  12 C  323  ARG LEU ASN TRP LEU THR LYS SER GLY SER THR TYR PRO          
SEQRES  13 C  323  VAL LEU ASN VAL THR MET PRO ASN ASN ASP ASN PHE ASP          
SEQRES  14 C  323  LYS LEU TYR ILE TRP GLY VAL HIS HIS PRO SER THR ASN          
SEQRES  15 C  323  GLN GLU GLN THR SER LEU TYR VAL GLN ALA SER GLY ARG          
SEQRES  16 C  323  VAL THR VAL SER THR ARG ARG SER GLN GLN THR ILE ILE          
SEQRES  17 C  323  PRO ASN ILE GLY SER ARG PRO TRP VAL ARG GLY LEU SER          
SEQRES  18 C  323  SER ARG ILE SER ILE TYR TRP THR ILE VAL LYS PRO GLY          
SEQRES  19 C  323  ASP VAL LEU VAL ILE ASN SER ASN GLY ASN LEU ILE ALA          
SEQRES  20 C  323  PRO ARG GLY TYR PHE LYS MET ARG THR GLY LYS SER SER          
SEQRES  21 C  323  ILE MET ARG SER ASP ALA PRO ILE ASP THR CYS ILE SER          
SEQRES  22 C  323  GLU CYS ILE THR PRO ASN GLY SER ILE PRO ASN ASP LYS          
SEQRES  23 C  323  PRO PHE GLN ASN VAL ASN LYS ILE THR TYR GLY ALA CYS          
SEQRES  24 C  323  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR          
SEQRES  25 C  323  GLY MET ARG ASN VAL PRO GLU LYS GLN THR ARG                  
SEQRES   1 D  174  GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY          
SEQRES   2 D  174  TRP GLU GLY MET ILE ASP GLY TRP TYR GLY PHE ARG HIS          
SEQRES   3 D  174  GLN ASN SER GLU GLY THR GLY GLN ALA ALA ASP LEU LYS          
SEQRES   4 D  174  SER THR GLN ALA ALA ILE ASP GLN ILE ASN GLY LYS LEU          
SEQRES   5 D  174  ASN ARG VAL ILE GLU LYS THR ASN GLU LYS PHE HIS GLN          
SEQRES   6 D  174  ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN          
SEQRES   7 D  174  ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU          
SEQRES   8 D  174  TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN          
SEQRES   9 D  174  GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS          
SEQRES  10 D  174  LEU PHE GLU LYS THR GLY ARG GLN LEU ARG GLU ASN ALA          
SEQRES  11 D  174  GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS          
SEQRES  12 D  174  CYS ASP ASN ALA CYS ILE GLU SER ILE ARG ASN GLY THR          
SEQRES  13 D  174  TYR ASP HIS ASP VAL TYR ARG ASP GLU ALA LEU ASN ASN          
SEQRES  14 D  174  ARG PHE GLN ILE LYS                                          
SEQRES   1 E  323  ALA ASP PRO GLY ALA THR LEU CYS LEU GLY HIS HIS ALA          
SEQRES   2 E  323  VAL PRO ASN GLY THR LEU VAL LYS THR ILE THR ASP ASP          
SEQRES   3 E  323  GLN ILE GLU VAL THR ASN ALA THR GLU LEU VAL GLN SER          
SEQRES   4 E  323  SER SER THR GLY LYS ILE CYS ASN ASN PRO HIS ARG ILE          
SEQRES   5 E  323  LEU ASP GLY ILE ASP CYS THR LEU ILE ASP ALA LEU LEU          
SEQRES   6 E  323  GLY ASP PRO HIS CYS ASP VAL PHE GLN ASN GLU THR TRP          
SEQRES   7 E  323  ASP LEU PHE VAL GLU ARG SER LYS ALA PHE SER ASN CYS          
SEQRES   8 E  323  TYR PRO TYR ASP VAL PRO ASP TYR ALA SER LEU ARG SER          
SEQRES   9 E  323  LEU VAL ALA SER SER GLY THR LEU GLU PHE ILE THR GLU          
SEQRES  10 E  323  GLY PHE THR TRP THR GLY VAL THR GLN ASN GLY GLY SER          
SEQRES  11 E  323  ASN ALA CYS LYS ARG GLY PRO GLY SER GLY PHE PHE SER          
SEQRES  12 E  323  ARG LEU ASN TRP LEU THR LYS SER GLY SER THR TYR PRO          
SEQRES  13 E  323  VAL LEU ASN VAL THR MET PRO ASN ASN ASP ASN PHE ASP          
SEQRES  14 E  323  LYS LEU TYR ILE TRP GLY VAL HIS HIS PRO SER THR ASN          
SEQRES  15 E  323  GLN GLU GLN THR SER LEU TYR VAL GLN ALA SER GLY ARG          
SEQRES  16 E  323  VAL THR VAL SER THR ARG ARG SER GLN GLN THR ILE ILE          
SEQRES  17 E  323  PRO ASN ILE GLY SER ARG PRO TRP VAL ARG GLY LEU SER          
SEQRES  18 E  323  SER ARG ILE SER ILE TYR TRP THR ILE VAL LYS PRO GLY          
SEQRES  19 E  323  ASP VAL LEU VAL ILE ASN SER ASN GLY ASN LEU ILE ALA          
SEQRES  20 E  323  PRO ARG GLY TYR PHE LYS MET ARG THR GLY LYS SER SER          
SEQRES  21 E  323  ILE MET ARG SER ASP ALA PRO ILE ASP THR CYS ILE SER          
SEQRES  22 E  323  GLU CYS ILE THR PRO ASN GLY SER ILE PRO ASN ASP LYS          
SEQRES  23 E  323  PRO PHE GLN ASN VAL ASN LYS ILE THR TYR GLY ALA CYS          
SEQRES  24 E  323  PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR          
SEQRES  25 E  323  GLY MET ARG ASN VAL PRO GLU LYS GLN THR ARG                  
SEQRES   1 F  174  GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY          
SEQRES   2 F  174  TRP GLU GLY MET ILE ASP GLY TRP TYR GLY PHE ARG HIS          
SEQRES   3 F  174  GLN ASN SER GLU GLY THR GLY GLN ALA ALA ASP LEU LYS          
SEQRES   4 F  174  SER THR GLN ALA ALA ILE ASP GLN ILE ASN GLY LYS LEU          
SEQRES   5 F  174  ASN ARG VAL ILE GLU LYS THR ASN GLU LYS PHE HIS GLN          
SEQRES   6 F  174  ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN          
SEQRES   7 F  174  ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU          
SEQRES   8 F  174  TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN          
SEQRES   9 F  174  GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS          
SEQRES  10 F  174  LEU PHE GLU LYS THR GLY ARG GLN LEU ARG GLU ASN ALA          
SEQRES  11 F  174  GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS          
SEQRES  12 F  174  CYS ASP ASN ALA CYS ILE GLU SER ILE ARG ASN GLY THR          
SEQRES  13 F  174  TYR ASP HIS ASP VAL TYR ARG ASP GLU ALA LEU ASN ASN          
SEQRES  14 F  174  ARG PHE GLN ILE LYS                                          
MODRES 4FNK ASN C  285  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN E  285  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN A  285  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN E  165  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN E   38  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN E   81  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN C   81  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN C  165  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN A   38  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN B  154  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN A  165  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN A   22  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN D  154  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN A   81  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN F  154  ASN  GLYCOSYLATION SITE                                 
MODRES 4FNK ASN C   38  ASN  GLYCOSYLATION SITE                                 
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    BMA  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    BMA  K   3      11                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    NAG  M   1      14                                                       
HET    NAG  M   2      14                                                       
HET    NAG  N   1      14                                                       
HET    NAG  N   2      14                                                       
HET    BMA  N   3      11                                                       
HET    MAN  N   4      11                                                       
HET    MAN  N   5      11                                                       
HET    NAG  O   1      14                                                       
HET    NAG  O   2      14                                                       
HET    NAG  A 401      14                                                       
HET    NAG  A 402      14                                                       
HET    NAG  A 403      14                                                       
HET    SO4  A 410       5                                                       
HET    NAG  B 201      14                                                       
HET    SO4  B 202       5                                                       
HET    GOL  C 510       6                                                       
HET    SO4  D 203       5                                                       
HET    SO4  D 204       5                                                       
HET    NAG  E 501      14                                                       
HET    NAG  E 502      14                                                       
HET    SO4  E 510       5                                                       
HET    GOL  E 511       6                                                       
HET    NAG  F 201      14                                                       
HET    SO4  F 202       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  NAG    25(C8 H15 N O6)                                              
FORMUL   7  BMA    3(C6 H12 O6)                                                 
FORMUL   7  MAN    3(C6 H12 O6)                                                 
FORMUL  19  SO4    6(O4 S 2-)                                                   
FORMUL  22  GOL    2(C3 H8 O3)                                                  
FORMUL  31  HOH   *1707(H2 O)                                                   
HELIX    1   1 THR A   65  GLN A   80  1                                  16
HELIX    2   2 ASP A  104  GLY A  116  1                                  13
HELIX    3   3 THR A  187  VAL A  196  1                                  10
HELIX    4   4 ASP B   37  GLU B   57  1                                  21
HELIX    5   5 GLY B   75  ARG B  127  1                                  53
HELIX    6   6 ASP B  145  ASN B  154  1                                  10
HELIX    7   7 ASP B  158  GLN B  172  1                                  15
HELIX    8   8 THR C   65  GLN C   80  1                                  16
HELIX    9   9 ASP C  104  GLY C  116  1                                  13
HELIX   10  10 THR C  187  VAL C  196  1                                  10
HELIX   11  11 ASP D   37  GLU D   57  1                                  21
HELIX   12  12 GLY D   75  ARG D  127  1                                  53
HELIX   13  13 ASP D  145  ASN D  154  1                                  10
HELIX   14  14 ASP D  158  PHE D  171  1                                  14
HELIX   15  15 THR E   65  GLN E   80  1                                  16
HELIX   16  16 ASP E  104  GLY E  116  1                                  13
HELIX   17  17 THR E  187  VAL E  196  1                                  10
HELIX   18  18 ASP F   37  GLU F   57  1                                  21
HELIX   19  19 GLY F   75  ARG F  127  1                                  53
HELIX   20  20 ASP F  145  ASN F  154  1                                  10
HELIX   21  21 ASP F  158  PHE F  171  1                                  14
SHEET    1   1 1 ALA A  11  HIS A  17  0
SHEET    2   2 1 THR A  24  VAL A  26  0
SHEET    3   3 1 ILE A  34  VAL A  36  0
SHEET    4   4 1 ALA A  39  GLU A  41  0
SHEET    5   5 1 VAL A  43  GLN A  44  0
SHEET    6   6 1 ILE A  51  ASN A  54  0
SHEET    7   7 1 ILE A  58  ASP A  60  0
SHEET    8   8 1 LEU A  86  GLU A  89  0
SHEET    9   9 1 TYR A 100  ASP A 101  0
SHEET   10  10 1 PHE A 120  THR A 122  0
SHEET   11  11 1 VAL A 130  THR A 131  0
SHEET   12  12 1 SER A 136  ARG A 141  0
SHEET   13  13 1 GLY A 144  GLY A 146  0
SHEET   14  14 1 LEU A 151  TRP A 153  0
SHEET   15  15 1 THR A 155  LYS A 156  0
SHEET   16  16 1 LEU A 164  PRO A 169  0
SHEET   17  17 1 LYS A 176  HIS A 184  0
SHEET   18  18 1 VAL A 202  SER A 205  0
SHEET   19  19 1 GLN A 210  ILE A 213  0
SHEET   20  20 1 ARG A 229  VAL A 237  0
SHEET   21  21 1 VAL A 242  SER A 247  0
SHEET   22  22 1 LEU A 251  PRO A 254  0
SHEET   23  23 1 GLY A 256  LYS A 259  0
SHEET   24  24 1 SER A 266  ARG A 269  0
SHEET   25  25 1 ILE A 274  ILE A 278  0
SHEET   26  26 1 CYS A 281  THR A 283  0
SHEET   27  27 1 GLY A 286  ILE A 288  0
SHEET   28  28 1 PHE A 294  GLN A 295  0
SHEET   29  29 1 TYR A 302  ALA A 304  0
SHEET   30  30 1 LYS A 307  TYR A 308  0
SHEET   31  31 1 LYS A 315  ALA A 317  0
SHEET   32  32 1 TYR B  22  ASN B  28  0
SHEET   33  33 1 GLY B  31  ALA B  36  0
SHEET   34  34 1 GLU B  61  LYS B  62  0
SHEET   35  35 1 ALA B 130  ASP B 132  0
SHEET   36  36 1 CYS B 137  ILE B 140  0
SHEET   37  37 1 ALA C  11  HIS C  17  0
SHEET   38  38 1 THR C  24  VAL C  26  0
SHEET   39  39 1 ILE C  34  VAL C  36  0
SHEET   40  40 1 ALA C  39  GLU C  41  0
SHEET   41  41 1 VAL C  43  GLN C  44  0
SHEET   42  42 1 ILE C  51  ASN C  54  0
SHEET   43  43 1 ILE C  58  ASP C  60  0
SHEET   44  44 1 LEU C  86  GLU C  89  0
SHEET   45  45 1 TYR C 100  ASP C 101  0
SHEET   46  46 1 PHE C 120  THR C 122  0
SHEET   47  47 1 VAL C 130  GLY C 134  0
SHEET   48  48 1 SER C 136  ARG C 141  0
SHEET   49  49 1 GLY C 144  GLY C 146  0
SHEET   50  50 1 LEU C 151  LYS C 156  0
SHEET   51  51 1 LEU C 164  PRO C 169  0
SHEET   52  52 1 LYS C 176  HIS C 184  0
SHEET   53  53 1 ARG C 201  SER C 205  0
SHEET   54  54 1 GLN C 210  ILE C 213  0
SHEET   55  55 1 ARG C 229  VAL C 237  0
SHEET   56  56 1 VAL C 242  GLY C 249  0
SHEET   57  57 1 LEU C 251  PRO C 254  0
SHEET   58  58 1 GLY C 256  LYS C 259  0
SHEET   59  59 1 SER C 266  ARG C 269  0
SHEET   60  60 1 ILE C 274  ILE C 278  0
SHEET   61  61 1 CYS C 281  THR C 283  0
SHEET   62  62 1 GLY C 286  ILE C 288  0
SHEET   63  63 1 PHE C 294  GLN C 295  0
SHEET   64  64 1 TYR C 302  CYS C 305  0
SHEET   65  65 1 LYS C 307  TYR C 308  0
SHEET   66  66 1 LYS C 315  ALA C 317  0
SHEET   67  67 1 TYR D  22  ASN D  28  0
SHEET   68  68 1 GLY D  31  ALA D  36  0
SHEET   69  69 1 ASN D  60  LYS D  62  0
SHEET   70  70 1 ALA D 130  ASP D 132  0
SHEET   71  71 1 CYS D 137  ILE D 140  0
SHEET   72  72 1 ALA E  11  HIS E  17  0
SHEET   73  73 1 THR E  24  VAL E  26  0
SHEET   74  74 1 ILE E  34  VAL E  36  0
SHEET   75  75 1 ALA E  39  GLU E  41  0
SHEET   76  76 1 VAL E  43  GLN E  44  0
SHEET   77  77 1 ILE E  51  ASN E  54  0
SHEET   78  78 1 ILE E  58  ASP E  60  0
SHEET   79  79 1 LEU E  86  GLU E  89  0
SHEET   80  80 1 TYR E 100  ASP E 101  0
SHEET   81  81 1 PHE E 120  THR E 122  0
SHEET   82  82 1 VAL E 130  THR E 131  0
SHEET   83  83 1 SER E 136  ARG E 141  0
SHEET   84  84 1 GLY E 144  GLY E 146  0
SHEET   85  85 1 LEU E 151  TRP E 153  0
SHEET   86  86 1 THR E 155  LYS E 156  0
SHEET   87  87 1 LEU E 164  PRO E 169  0
SHEET   88  88 1 LYS E 176  HIS E 184  0
SHEET   89  89 1 ARG E 201  SER E 205  0
SHEET   90  90 1 GLN E 210  ILE E 213  0
SHEET   91  91 1 ARG E 229  VAL E 237  0
SHEET   92  92 1 VAL E 242  GLY E 249  0
SHEET   93  93 1 LEU E 251  PRO E 254  0
SHEET   94  94 1 GLY E 256  LYS E 259  0
SHEET   95  95 1 SER E 266  ARG E 269  0
SHEET   96  96 1 ILE E 274  ILE E 278  0
SHEET   97  97 1 CYS E 281  THR E 283  0
SHEET   98  98 1 GLY E 286  ILE E 288  0
SHEET   99  99 1 PHE E 294  GLN E 295  0
SHEET  100 100 1 TYR E 302  ALA E 304  0
SHEET  101 101 1 LYS E 307  TYR E 308  0
SHEET  102 102 1 LYS E 315  ALA E 317  0
SHEET  103 103 1 TYR F  22  ASN F  28  0
SHEET  104 104 1 GLY F  31  ALA F  36  0
SHEET  105 105 1 GLU F  61  LYS F  62  0
SHEET  106 106 1 ALA F 130  ASP F 132  0
SHEET  107 107 1 CYS F 137  ILE F 140  0
SSBOND   1 CYS A   14    CYS B  137                          1555   1555  2.15  
SSBOND   2 CYS A   52    CYS A  277                          1555   1555  2.07  
SSBOND   3 CYS A   64    CYS A   76                          1555   1555  2.25  
SSBOND   4 CYS A   97    CYS A  139                          1555   1555  2.05  
SSBOND   5 CYS A  281    CYS A  305                          1555   1555  2.10  
SSBOND   6 CYS B  144    CYS B  148                          1555   1555  2.20  
SSBOND   7 CYS C   14    CYS D  137                          1555   1555  2.17  
SSBOND   8 CYS C   52    CYS C  277                          1555   1555  2.09  
SSBOND   9 CYS C   64    CYS C   76                          1555   1555  2.25  
SSBOND  10 CYS C   97    CYS C  139                          1555   1555  2.06  
SSBOND  11 CYS C  281    CYS C  305                          1555   1555  2.11  
SSBOND  12 CYS D  144    CYS D  148                          1555   1555  2.26  
SSBOND  13 CYS E   14    CYS F  137                          1555   1555  2.13  
SSBOND  14 CYS E   52    CYS E  277                          1555   1555  2.11  
SSBOND  15 CYS E   64    CYS E   76                          1555   1555  2.22  
SSBOND  16 CYS E   97    CYS E  139                          1555   1555  2.07  
SSBOND  17 CYS E  281    CYS E  305                          1555   1555  2.10  
SSBOND  18 CYS F  144    CYS F  148                          1555   1555  2.19  
LINK         ND2 ASN A  22                 C1  NAG A 401     1555   1555  1.46  
LINK         ND2 ASN A  38                 C1  NAG A 402     1555   1555  1.45  
LINK         ND2 ASN A  81                 C1  NAG A 403     1555   1555  1.46  
LINK         ND2 ASN A 165                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN A 285                 C1  NAG H   1     1555   1555  1.44  
LINK         ND2 ASN B 154                 C1  NAG B 201     1555   1555  1.45  
LINK         ND2 ASN C  38                 C1  NAG I   1     1555   1555  1.47  
LINK         ND2 ASN C  81                 C1  NAG J   1     1555   1555  1.45  
LINK         ND2 ASN C 165                 C1  NAG K   1     1555   1555  1.45  
LINK         ND2 ASN C 285                 C1  NAG L   1     1555   1555  1.42  
LINK         ND2 ASN D 154                 C1  NAG M   1     1555   1555  1.46  
LINK         ND2 ASN E  38                 C1  NAG E 501     1555   1555  1.45  
LINK         ND2 ASN E  81                 C1  NAG E 502     1555   1555  1.45  
LINK         ND2 ASN E 165                 C1  NAG N   1     1555   1555  1.44  
LINK         ND2 ASN E 285                 C1  NAG O   1     1555   1555  1.43  
LINK         ND2 ASN F 154                 C1  NAG F 201     1555   1555  1.46  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.43  
LINK         O4  NAG G   2                 C1  BMA G   3     1555   1555  1.44  
LINK         O6  BMA G   3                 C1  MAN G   4     1555   1555  1.44  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.44  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.44  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.45  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.42  
LINK         O4  NAG K   2                 C1  BMA K   3     1555   1555  1.44  
LINK         O4  NAG L   1                 C1  NAG L   2     1555   1555  1.44  
LINK         O4  NAG M   1                 C1  NAG M   2     1555   1555  1.45  
LINK         O4  NAG N   1                 C1  NAG N   2     1555   1555  1.43  
LINK         O4  NAG N   2                 C1  BMA N   3     1555   1555  1.45  
LINK         O3  BMA N   3                 C1  MAN N   4     1555   1555  1.45  
LINK         O6  BMA N   3                 C1  MAN N   5     1555   1555  1.44  
LINK         O4  NAG O   1                 C1  NAG O   2     1555   1555  1.44  
CISPEP   1 ASN A   54    PRO A   55          0         4.80                     
CISPEP   2 ASN C   54    PRO C   55          0         5.01                     
CISPEP   3 ASN E   54    PRO E   55          0         3.04                     
CRYST1  105.149  151.458  347.751  90.00  90.00  90.00 C 2 2 21     24          
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      0.009510  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006602  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002876        0.00000                         
ATOM      1  N   PRO A   9      26.920  34.569 -17.924  1.00 63.27           N
ANISOU    1  N   PRO A   9     9194   5883   8962   -425   -108  -1396       N
ATOM      2  CA  PRO A   9      27.868  33.656 -17.268  1.00 59.52           C
ANISOU    2  CA  PRO A   9     8566   5660   8391   -579     19  -1339       C
ATOM      3  C   PRO A   9      27.229  32.293 -16.928  1.00 51.16           C
ANISOU    3  C   PRO A   9     7282   4815   7341   -561    156  -1390       C
ATOM      4  O   PRO A   9      26.402  32.173 -15.999  1.00 51.94           O
ANISOU    4  O   PRO A   9     7210   5016   7510   -529    262  -1560       O
ATOM      5  CB  PRO A   9      28.294  34.414 -15.995  1.00 63.67           C
ANISOU    5  CB  PRO A   9     9065   6239   8888   -677    127  -1437       C
ATOM      6  CG  PRO A   9      27.348  35.595 -15.877  1.00 67.67           C
ANISOU    6  CG  PRO A   9     9652   6535   9525   -538     35  -1593       C
ATOM      7  CD  PRO A   9      26.871  35.889 -17.273  1.00 67.46           C
ANISOU    7  CD  PRO A   9     9817   6281   9534   -420   -120  -1507       C
ATOM      8  HA  PRO A   9      28.735  33.504 -17.911  1.00  0.00           H
ATOM      9  HB2 PRO A   9      28.204  33.768 -15.122  1.00  0.00           H
ATOM     10  HB3 PRO A   9      29.321  34.766 -16.096  1.00  0.00           H
ATOM     11  HG2 PRO A   9      26.505  35.341 -15.235  1.00  0.00           H
ATOM     12  HG3 PRO A   9      27.877  36.458 -15.474  1.00  0.00           H
ATOM     13  HD2 PRO A   9      27.533  36.597 -17.772  1.00  0.00           H
ATOM     14  HD3 PRO A   9      25.849  36.268 -17.256  1.00  0.00           H
ATOM     15  N   GLY A  10      27.608  31.278 -17.704  1.00 40.78           N
ANISOU   15  N   GLY A  10     5961   3572   5963   -591    147  -1247       N
ATOM     16  CA  GLY A  10      27.106  29.941 -17.485  1.00 34.17           C
ANISOU   16  CA  GLY A  10     4937   2923   5124   -587    251  -1272       C
ATOM     17  C   GLY A  10      27.965  28.880 -18.136  1.00 30.12           C
ANISOU   17  C   GLY A  10     4439   2511   4493   -675    269  -1092       C
ATOM     18  O   GLY A  10      29.180  29.019 -18.284  1.00 30.76           O
ANISOU   18  O   GLY A  10     4612   2622   4455   -793    281   -958       O
ATOM     19  H   GLY A  10      28.258  31.446 -18.459  1.00  0.00           H
ATOM     20  HA2 GLY A  10      27.073  29.753 -16.412  1.00  0.00           H
ATOM     21  HA3 GLY A  10      26.095  29.873 -17.887  1.00  0.00           H
ATOM     22  N   ALA A  11      27.331  27.789 -18.520  1.00 23.91           N
ANISOU   22  N   ALA A  11     3545   1798   3741   -615    279  -1092       N
ATOM     23  CA  ALA A  11      28.054  26.698 -19.111  1.00 21.19           C
ANISOU   23  CA  ALA A  11     3201   1556   3295   -688    301   -937       C
ATOM     24  C   ALA A  11      27.113  25.976 -20.058  1.00 21.23           C
ANISOU   24  C   ALA A  11     3156   1516   3393   -558    228   -941       C
ATOM     25  O   ALA A  11      25.913  26.274 -20.107  1.00 21.99           O
ANISOU   25  O   ALA A  11     3192   1539   3625   -414    173  -1065       O
ATOM     26  CB  ALA A  11      28.545  25.778 -18.003  1.00 20.11           C
ANISOU   26  CB  ALA A  11     2942   1654   3047   -820    446   -928       C
ATOM     27  H   ALA A  11      26.331  27.720 -18.398  1.00  0.00           H
ATOM     28  HA  ALA A  11      28.907  27.085 -19.669  1.00  0.00           H
ATOM     29  HB1 ALA A  11      29.096  24.945 -18.439  1.00  0.00           H
ATOM     30  HB2 ALA A  11      27.691  25.395 -17.444  1.00  0.00           H
ATOM     31  HB3 ALA A  11      29.199  26.335 -17.332  1.00  0.00           H
ATOM     32  N   THR A  12      27.665  25.050 -20.835  1.00 22.25           N
ANISOU   32  N   THR A  12     3302   1702   3449   -602    225   -803       N
ATOM     33  CA  THR A  12      26.894  24.212 -21.735  1.00 24.19           C
ANISOU   33  CA  THR A  12     3496   1930   3766   -499    168   -790       C
ATOM     34  C   THR A  12      27.334  22.798 -21.472  1.00 21.99           C
ANISOU   34  C   THR A  12     3108   1852   3395   -589    266   -725       C
ATOM     35  O   THR A  12      28.529  22.553 -21.248  1.00 22.05           O
ANISOU   35  O   THR A  12     3145   1958   3274   -715    318   -621       O
ATOM     36  CB  THR A  12      27.203  24.565 -23.197  1.00 30.68           C
ANISOU   36  CB  THR A  12     4491   2593   4575   -474     38   -657       C
ATOM     37  OG1 THR A  12      27.002  25.968 -23.383  1.00 36.47           O
ANISOU   37  OG1 THR A  12     5369   3130   5358   -420    -79   -685       O
ATOM     38  CG2 THR A  12      26.270  23.862 -24.125  1.00 33.16           C
ANISOU   38  CG2 THR A  12     4750   2891   4959   -340    -52   -635       C
ATOM     39  H   THR A  12      28.666  24.924 -20.798  1.00  0.00           H
ATOM     40  HA  THR A  12      25.828  24.321 -21.535  1.00  0.00           H
ATOM     41  HB  THR A  12      28.234  24.301 -23.434  1.00  0.00           H
ATOM     42  HG1 THR A  12      27.718  26.452 -22.966  1.00  0.00           H
ATOM     43 HG21 THR A  12      26.510  24.129 -25.154  1.00  0.00           H
ATOM     44 HG22 THR A  12      25.245  24.159 -23.903  1.00  0.00           H
ATOM     45 HG23 THR A  12      26.373  22.785 -23.996  1.00  0.00           H
ATOM     46  N   LEU A  13      26.368  21.870 -21.458  1.00 19.86           N
ANISOU   46  N   LEU A  13     2701   1664   3181   -509    271   -777       N
ATOM     47  CA  LEU A  13      26.647  20.480 -21.231  1.00 18.30           C
ANISOU   47  CA  LEU A  13     2409   1646   2900   -576    331   -709       C
ATOM     48  C   LEU A  13      25.916  19.715 -22.331  1.00 18.90           C
ANISOU   48  C   LEU A  13     2449   1710   3024   -454    254   -662       C
ATOM     49  O   LEU A  13      24.696  19.786 -22.419  1.00 20.63           O
ANISOU   49  O   LEU A  13     2597   1890   3353   -340    218   -771       O
ATOM     50  CB  LEU A  13      26.104  20.072 -19.859  1.00 18.55           C
ANISOU   50  CB  LEU A  13     2311   1808   2928   -646    431   -841       C
ATOM     51  CG  LEU A  13      26.300  18.587 -19.538  1.00 18.51           C
ANISOU   51  CG  LEU A  13     2227   1973   2834   -724    466   -764       C
ATOM     52  CD1 LEU A  13      27.797  18.233 -19.545  1.00 17.65           C
ANISOU   52  CD1 LEU A  13     2181   1930   2594   -792    450   -586       C
ATOM     53  CD2 LEU A  13      25.679  18.269 -18.197  1.00 19.63           C
ANISOU   53  CD2 LEU A  13     2278   2256   2926   -786    545   -863       C
ATOM     54  H   LEU A  13      25.412  22.158 -21.612  1.00  0.00           H
ATOM     55  HA  LEU A  13      27.719  20.293 -21.286  1.00  0.00           H
ATOM     56  HB2 LEU A  13      25.037  20.292 -19.832  1.00  0.00           H
ATOM     57  HB3 LEU A  13      26.604  20.665 -19.093  1.00  0.00           H
ATOM     58  HG  LEU A  13      25.798  17.995 -20.304  1.00  0.00           H
ATOM     59 HD21 LEU A  13      25.820  17.212 -17.972  1.00  0.00           H
ATOM     60 HD22 LEU A  13      26.156  18.872 -17.424  1.00  0.00           H
ATOM     61 HD23 LEU A  13      24.613  18.495 -18.228  1.00  0.00           H
ATOM     62 HD11 LEU A  13      27.922  17.175 -19.315  1.00  0.00           H
ATOM     63 HD12 LEU A  13      28.315  18.831 -18.795  1.00  0.00           H
ATOM     64 HD13 LEU A  13      28.215  18.443 -20.529  1.00  0.00           H
ATOM     65  N   CYS A  14      26.674  19.067 -23.208  1.00 17.75           N
ANISOU   65  N   CYS A  14     2351   1592   2803   -480    228   -515       N
ATOM     66  CA  CYS A  14      26.118  18.362 -24.362  1.00 18.66           C
ANISOU   66  CA  CYS A  14     2453   1692   2943   -385    156   -458       C
ATOM     67  C   CYS A  14      26.181  16.872 -24.150  1.00 17.00           C
ANISOU   67  C   CYS A  14     2134   1640   2687   -419    205   -421       C
ATOM     68  O   CYS A  14      27.202  16.350 -23.666  1.00 17.86           O
ANISOU   68  O   CYS A  14     2229   1840   2717   -526    257   -364       O
ATOM     69  CB  CYS A  14      26.911  18.686 -25.631  1.00 21.03           C
ANISOU   69  CB  CYS A  14     2898   1910   3183   -408     94   -333       C
ATOM     70  SG  CYS A  14      26.859  20.488 -26.093  1.00 31.33           S
ANISOU   70  SG  CYS A  14     4392   2986   4527   -385    -10   -344       S
ATOM     71  H   CYS A  14      27.675  19.061 -23.072  1.00  0.00           H
ATOM     72  HA  CYS A  14      25.079  18.662 -24.501  1.00  0.00           H
ATOM     73  HB2 CYS A  14      26.496  18.106 -26.455  1.00  0.00           H
ATOM     74  HB3 CYS A  14      27.950  18.391 -25.481  1.00  0.00           H
ATOM     75  N   LEU A  15      25.104  16.181 -24.509  1.00 14.54           N
ANISOU   75  N   LEU A  15     1746   1349   2428   -330    172   -453       N
ATOM     76  CA  LEU A  15      25.104  14.716 -24.476  1.00 14.18           C
ANISOU   76  CA  LEU A  15     1618   1430   2339   -358    196   -407       C
ATOM     77  C   LEU A  15      25.353  14.171 -25.869  1.00 15.49           C
ANISOU   77  C   LEU A  15     1832   1569   2486   -313    139   -302       C
ATOM     78  O   LEU A  15      24.964  14.772 -26.870  1.00 17.04           O
ANISOU   78  O   LEU A  15     2100   1657   2716   -239     67   -287       O
ATOM     79  CB  LEU A  15      23.754  14.189 -23.969  1.00 15.38           C
ANISOU   79  CB  LEU A  15     1654   1646   2544   -318    210   -516       C
ATOM     80  CG  LEU A  15      23.444  14.285 -22.483  1.00 20.67           C
ANISOU   80  CG  LEU A  15     2252   2402   3201   -412    294   -636       C
ATOM     81  CD1 LEU A  15      24.308  13.318 -21.751  1.00 23.80           C
ANISOU   81  CD1 LEU A  15     2646   2907   3490   -553    331   -556       C
ATOM     82  CD2 LEU A  15      23.643  15.713 -21.953  1.00 22.55           C
ANISOU   82  CD2 LEU A  15     2534   2558   3476   -421    318   -719       C
ATOM     83  H   LEU A  15      24.274  16.672 -24.809  1.00  0.00           H
ATOM     84  HA  LEU A  15      25.896  14.373 -23.810  1.00  0.00           H
ATOM     85  HB2 LEU A  15      23.699  13.135 -24.241  1.00  0.00           H
ATOM     86  HB3 LEU A  15      22.966  14.715 -24.509  1.00  0.00           H
ATOM     87  HG  LEU A  15      22.403  14.002 -22.329  1.00  0.00           H
ATOM     88 HD11 LEU A  15      24.096  13.376 -20.683  1.00  0.00           H
ATOM     89 HD12 LEU A  15      25.356  13.562 -21.927  1.00  0.00           H
ATOM     90 HD13 LEU A  15      24.105  12.308 -22.107  1.00  0.00           H
ATOM     91 HD21 LEU A  15      23.173  15.806 -20.974  1.00  0.00           H
ATOM     92 HD22 LEU A  15      24.709  15.923 -21.866  1.00  0.00           H
ATOM     93 HD23 LEU A  15      23.188  16.423 -22.643  1.00  0.00           H
ATOM     94  N   GLY A  16      26.054  13.057 -25.941  1.00 14.68           N
ANISOU   94  N   GLY A  16     1696   1554   2329   -367    163   -234       N
ATOM     95  CA  GLY A  16      26.312  12.466 -27.217  1.00 14.45           C
ANISOU   95  CA  GLY A  16     1697   1515   2280   -338    128   -160       C
ATOM     96  C   GLY A  16      26.677  11.010 -27.129  1.00 12.85           C
ANISOU   96  C   GLY A  16     1418   1409   2056   -366    143   -126       C
ATOM     97  O   GLY A  16      26.645  10.408 -26.050  1.00 11.30           O
ANISOU   97  O   GLY A  16     1157   1281   1855   -411    161   -145       O
ATOM     98  H   GLY A  16      26.407  12.624 -25.100  1.00  0.00           H
ATOM     99  HA2 GLY A  16      27.136  13.002 -27.688  1.00  0.00           H
ATOM    100  HA3 GLY A  16      25.423  12.569 -27.839  1.00  0.00           H
ATOM    101  N   HIS A  17      27.021  10.460 -28.281  1.00 13.27           N
ANISOU  101  N   HIS A  17     1490   1459   2092   -350    127    -78       N
ATOM    102  CA  HIS A  17      27.379   9.049 -28.407  1.00 12.67           C
ANISOU  102  CA  HIS A  17     1346   1452   2017   -358    126    -55       C
ATOM    103  C   HIS A  17      28.510   8.919 -29.392  1.00 12.54           C
ANISOU  103  C   HIS A  17     1351   1439   1975   -394    147    -33       C
ATOM    104  O   HIS A  17      28.787   9.837 -30.150  1.00 13.53           O
ANISOU  104  O   HIS A  17     1562   1519   2062   -421    158    -23       O
ATOM    105  CB  HIS A  17      26.180   8.227 -28.887  1.00 12.44           C
ANISOU  105  CB  HIS A  17     1288   1430   2007   -289     90    -60       C
ATOM    106  CG  HIS A  17      25.629   8.700 -30.180  1.00 12.69           C
ANISOU  106  CG  HIS A  17     1388   1400   2033   -238     59    -46       C
ATOM    107  ND1 HIS A  17      26.095   8.242 -31.388  1.00 13.48           N
ANISOU  107  ND1 HIS A  17     1521   1500   2101   -252     59    -13       N
ATOM    108  CD2 HIS A  17      24.693   9.633 -30.466  1.00 13.33           C
ANISOU  108  CD2 HIS A  17     1518   1409   2139   -183     13    -64       C
ATOM    109  CE1 HIS A  17      25.445   8.846 -32.365  1.00 14.83           C
ANISOU  109  CE1 HIS A  17     1775   1604   2257   -224     11      6       C
ATOM    110  NE2 HIS A  17      24.609   9.716 -31.836  1.00 14.61           N
ANISOU  110  NE2 HIS A  17     1759   1521   2272   -172    -31    -20       N
ATOM    111  H   HIS A  17      27.037  11.039 -29.108  1.00  0.00           H
ATOM    112  HA  HIS A  17      27.705   8.674 -27.437  1.00  0.00           H
ATOM    113  HB2 HIS A  17      25.395   8.287 -28.133  1.00  0.00           H
ATOM    114  HB3 HIS A  17      26.487   7.187 -28.994  1.00  0.00           H
ATOM    115  HD2 HIS A  17      24.119  10.206 -29.752  1.00  0.00           H
ATOM    116  HE1 HIS A  17      25.576   8.659 -33.420  1.00  0.00           H
ATOM    117  HD1 HIS A  17      26.822   7.551 -31.510  1.00  0.00           H
ATOM    118  HE2 HIS A  17      24.006  10.341 -32.352  1.00  0.00           H
ATOM    119  N   HIS A  18      29.210   7.792 -29.359  1.00 12.02           N
ANISOU  119  N   HIS A  18     1208   1427   1931   -406    148    -35       N
ATOM    120  CA  HIS A  18      30.346   7.622 -30.248  1.00 12.90           C
ANISOU  120  CA  HIS A  18     1306   1561   2034   -447    184    -53       C
ATOM    121  C   HIS A  18      29.963   7.294 -31.691  1.00 14.35           C
ANISOU  121  C   HIS A  18     1528   1735   2189   -431    192    -56       C
ATOM    122  O   HIS A  18      28.807   7.039 -31.986  1.00 15.48           O
ANISOU  122  O   HIS A  18     1698   1851   2331   -372    154    -33       O
ATOM    123  CB  HIS A  18      31.298   6.540 -29.707  1.00 13.66           C
ANISOU  123  CB  HIS A  18     1313   1712   2167   -431    153    -70       C
ATOM    124  CG  HIS A  18      30.786   5.139 -29.824  1.00 15.72           C
ANISOU  124  CG  HIS A  18     1527   1977   2470   -370    103    -69       C
ATOM    125  ND1 HIS A  18      31.590   4.032 -29.600  1.00 19.03           N
ANISOU  125  ND1 HIS A  18     1884   2414   2931   -342     57    -91       N
ATOM    126  CD2 HIS A  18      29.555   4.652 -30.135  1.00 15.37           C
ANISOU  126  CD2 HIS A  18     1491   1911   2436   -334     85    -53       C
ATOM    127  CE1 HIS A  18      30.870   2.931 -29.770  1.00 19.72           C
ANISOU  127  CE1 HIS A  18     1961   2484   3046   -295     12    -83       C
ATOM    128  NE2 HIS A  18      29.639   3.280 -30.099  1.00 16.72           N
ANISOU  128  NE2 HIS A  18     1623   2092   2640   -293     32    -59       N
ATOM    129  H   HIS A  18      28.954   7.055 -28.718  1.00  0.00           H
ATOM    130  HA  HIS A  18      30.895   8.564 -30.261  1.00  0.00           H
ATOM    131  HB2 HIS A  18      32.235   6.606 -30.260  1.00  0.00           H
ATOM    132  HB3 HIS A  18      31.500   6.749 -28.656  1.00  0.00           H
ATOM    133  HD2 HIS A  18      28.675   5.234 -30.367  1.00  0.00           H
ATOM    134  HE1 HIS A  18      31.230   1.919 -29.658  1.00  0.00           H
ATOM    135  HD1 HIS A  18      32.568   4.059 -29.348  1.00  0.00           H
ATOM    136  HE2 HIS A  18      28.881   2.641 -30.293  1.00  0.00           H
ATOM    137  N   ALA A  19      30.969   7.327 -32.565  1.00 15.68           N
ANISOU  137  N   ALA A  19     1695   1935   2327   -500    247    -94       N
ATOM    138  CA  ALA A  19      30.855   6.910 -33.961  1.00 16.04           C
ANISOU  138  CA  ALA A  19     1771   1991   2331   -524    272   -114       C
ATOM    139  C   ALA A  19      32.249   6.514 -34.415  1.00 16.65           C
ANISOU  139  C   ALA A  19     1768   2143   2416   -593    344   -204       C
ATOM    140  O   ALA A  19      33.223   6.817 -33.720  1.00 17.39           O
ANISOU  140  O   ALA A  19     1823   2265   2521   -594    346   -224       O
ATOM    141  CB  ALA A  19      30.304   8.059 -34.825  1.00 15.91           C
ANISOU  141  CB  ALA A  19     1919   1914   2214   -579    259    -64       C
ATOM    142  H   ALA A  19      31.866   7.661 -32.242  1.00  0.00           H
ATOM    143  HA  ALA A  19      30.190   6.049 -34.032  1.00  0.00           H
ATOM    144  HB1 ALA A  19      30.226   7.730 -35.861  1.00  0.00           H
ATOM    145  HB2 ALA A  19      30.978   8.914 -34.765  1.00  0.00           H
ATOM    146  HB3 ALA A  19      29.318   8.347 -34.460  1.00  0.00           H
ATOM    147  N   VAL A  20      32.348   5.836 -35.562  1.00 16.87           N
ANISOU  147  N   VAL A  20     1784   2204   2421   -619    382   -258       N
ATOM    148  CA  VAL A  20      33.635   5.467 -36.147  1.00 19.99           C
ANISOU  148  CA  VAL A  20     2118   2672   2807   -654    442   -365       C
ATOM    149  C   VAL A  20      33.631   5.869 -37.615  1.00 21.73           C
ANISOU  149  C   VAL A  20     2442   2918   2895   -783    511   -395       C
ATOM    150  O   VAL A  20      32.566   6.048 -38.205  1.00 20.76           O
ANISOU  150  O   VAL A  20     2424   2750   2713   -819    489   -326       O
ATOM    151  CB  VAL A  20      33.892   3.947 -36.013  1.00 21.12           C
ANISOU  151  CB  VAL A  20     2127   2830   3068   -551    414   -436       C
ATOM    152  CG1 VAL A  20      34.008   3.569 -34.563  1.00 22.15           C
ANISOU  152  CG1 VAL A  20     2192   2928   3298   -452    324   -394       C
ATOM    153  CG2 VAL A  20      32.756   3.142 -36.683  1.00 18.55           C
ANISOU  153  CG2 VAL A  20     1818   2481   2751   -524    400   -419       C
ATOM    154  H   VAL A  20      31.501   5.568 -36.043  1.00  0.00           H
ATOM    155  HA  VAL A  20      34.428   6.009 -35.632  1.00  0.00           H
ATOM    156  HB  VAL A  20      34.831   3.707 -36.512  1.00  0.00           H
ATOM    157 HG21 VAL A  20      32.681   3.424 -37.733  1.00  0.00           H
ATOM    158 HG22 VAL A  20      31.813   3.358 -36.181  1.00  0.00           H
ATOM    159 HG23 VAL A  20      32.972   2.076 -36.607  1.00  0.00           H
ATOM    160 HG11 VAL A  20      34.812   4.142 -34.101  1.00  0.00           H
ATOM    161 HG12 VAL A  20      33.068   3.786 -34.055  1.00  0.00           H
ATOM    162 HG13 VAL A  20      34.228   2.504 -34.481  1.00  0.00           H
ATOM    163  N   PRO A  21      34.815   6.015 -38.230  1.00 25.93           N
ANISOU  163  N   PRO A  21     2959   3522   3369   -865    585   -501       N
ATOM    164  CA  PRO A  21      34.857   6.502 -39.615  1.00 27.42           C
ANISOU  164  CA  PRO A  21     3278   3743   3397  -1019    644   -529       C
ATOM    165  C   PRO A  21      34.097   5.609 -40.618  1.00 29.44           C
ANISOU  165  C   PRO A  21     3551   4003   3634  -1030    654   -546       C
ATOM    166  O   PRO A  21      33.412   6.113 -41.512  1.00 33.98           O
ANISOU  166  O   PRO A  21     4285   4551   4075  -1134    640   -479       O
ATOM    167  CB  PRO A  21      36.358   6.547 -39.922  1.00 27.76           C
ANISOU  167  CB  PRO A  21     3257   3879   3411  -1092    727   -682       C
ATOM    168  CG  PRO A  21      37.000   6.725 -38.559  1.00 28.47           C
ANISOU  168  CG  PRO A  21     3246   3960   3613   -998    692   -672       C
ATOM    169  CD  PRO A  21      36.157   5.923 -37.624  1.00 27.96           C
ANISOU  169  CD  PRO A  21     3103   3829   3690   -840    607   -594       C
ATOM    170  HA  PRO A  21      34.451   7.513 -39.654  1.00  0.00           H
ATOM    171  HB2 PRO A  21      36.687   5.618 -40.388  1.00  0.00           H
ATOM    172  HB3 PRO A  21      36.589   7.397 -40.564  1.00  0.00           H
ATOM    173  HG2 PRO A  21      36.998   7.776 -38.270  1.00  0.00           H
ATOM    174  HG3 PRO A  21      38.020   6.340 -38.570  1.00  0.00           H
ATOM    175  HD2 PRO A  21      36.165   6.352 -36.622  1.00  0.00           H
ATOM    176  HD3 PRO A  21      36.495   4.887 -37.598  1.00  0.00           H
ATOM    177  N   ASN A  22      34.168   4.300 -40.440  1.00 25.79           N
ANISOU  177  N   ASN A  22     2940   3557   3302   -922    657   -623       N
ATOM    178  CA  ASN A  22      33.252   3.409 -41.191  1.00 29.50           C
ANISOU  178  CA  ASN A  22     3423   4016   3772   -912    652   -620       C
ATOM    179  C   ASN A  22      32.882   2.190 -40.380  1.00 24.40           C
ANISOU  179  C   ASN A  22     2637   3334   3299   -745    592   -626       C
ATOM    180  O   ASN A  22      33.732   1.551 -39.743  1.00 23.79           O
ANISOU  180  O   ASN A  22     2434   3264   3343   -653    578   -707       O
ATOM    181  CB  ASN A  22      33.856   3.009 -42.548  1.00 42.26           C
ANISOU  181  CB  ASN A  22     5052   5709   5295  -1031    747   -763       C
ATOM    182  CG  ASN A  22      32.789   2.841 -43.628  1.00 52.56           C
ANISOU  182  CG  ASN A  22     6482   7001   6486  -1114    741   -706       C
ATOM    183  OD1 ASN A  22      31.845   2.061 -43.465  1.00 50.34           O
ANISOU  183  OD1 ASN A  22     6166   6677   6282  -1025    693   -655       O
ATOM    184  ND2 ASN A  22      32.917   3.593 -44.716  1.00 65.07           N
ANISOU  184  ND2 ASN A  22     8226   8618   7879  -1293    775   -707       N
ATOM    185  H   ASN A  22      34.842   3.910 -39.797  1.00  0.00           H
ATOM    186  HA  ASN A  22      32.336   3.966 -41.388  1.00  0.00           H
ATOM    187  HB2 ASN A  22      34.555   3.784 -42.863  1.00  0.00           H
ATOM    188  HB3 ASN A  22      34.396   2.069 -42.433  1.00  0.00           H
ATOM    189 HD21 ASN A  22      32.233   3.531 -45.456  1.00  0.00           H
ATOM    190 HD22 ASN A  22      33.699   4.227 -44.803  1.00  0.00           H
ATOM    191  N   GLY A  23      31.596   1.901 -40.322  1.00 21.58           N
ANISOU  191  N   GLY A  23     2319   2927   2955   -706    534   -530       N
ATOM    192  CA  GLY A  23      31.142   0.805 -39.517  1.00 18.62           C
ANISOU  192  CA  GLY A  23     1839   2512   2723   -560    460   -521       C
ATOM    193  C   GLY A  23      30.873  -0.359 -40.426  1.00 20.40           C
ANISOU  193  C   GLY A  23     2034   2752   2964   -556    484   -597       C
ATOM    194  O   GLY A  23      31.614  -0.652 -41.354  1.00 22.97           O
ANISOU  194  O   GLY A  23     2344   3130   3255   -622    566   -720       O
ATOM    195  H   GLY A  23      30.931   2.452 -40.845  1.00  0.00           H
ATOM    196  HA2 GLY A  23      31.909   0.537 -38.791  1.00  0.00           H
ATOM    197  HA3 GLY A  23      30.226   1.085 -38.997  1.00  0.00           H
ATOM    198  N  ATHR A  24      29.781  -1.050 -40.147  0.63 18.88           N
ANISOU  198  N  ATHR A  24     1866   2505   2801   -458    395   -516       N
ATOM    199  N  BTHR A  24      29.760  -1.009 -40.183  0.37 18.88           N
ANISOU  199  N  BTHR A  24     1873   2506   2795   -462    396   -514       N
ATOM    200  CA ATHR A  24      29.384  -2.255 -40.838  0.63 19.13           C
ANISOU  200  CA ATHR A  24     1876   2535   2858   -436    396   -572       C
ATOM    201  CA BTHR A  24      29.437  -2.158 -40.967  0.37 18.92           C
ANISOU  201  CA BTHR A  24     1857   2516   2817   -453    409   -578       C
ATOM    202  C  ATHR A  24      27.936  -2.143 -41.238  0.63 16.76           C
ANISOU  202  C  ATHR A  24     1704   2208   2457   -435    339   -449       C
ATOM    203  C  BTHR A  24      27.947  -2.231 -41.197  0.37 16.63           C
ANISOU  203  C  BTHR A  24     1679   2190   2449   -428    337   -453       C
ATOM    204  O  ATHR A  24      27.120  -1.614 -40.492  0.63 14.99           O
ANISOU  204  O  ATHR A  24     1529   1946   2219   -380    260   -331       O
ATOM    205  O  BTHR A  24      27.143  -1.875 -40.323  0.37 14.91           O
ANISOU  205  O  BTHR A  24     1496   1932   2237   -359    251   -339       O
ATOM    206  CB ATHR A  24      29.504  -3.464 -39.916  0.63 22.16           C
ANISOU  206  CB ATHR A  24     2149   2866   3405   -307    313   -602       C
ATOM    207  CB BTHR A  24      29.969  -3.407 -40.291  0.37 21.98           C
ANISOU  207  CB BTHR A  24     2101   2869   3381   -343    363   -665       C
ATOM    208  OG1ATHR A  24      30.875  -3.653 -39.559  0.63 24.15           O
ANISOU  208  OG1ATHR A  24     2294   3123   3759   -280    330   -715       O
ATOM    209  OG1BTHR A  24      29.789  -4.525 -41.159  0.37 24.03           O
ANISOU  209  OG1BTHR A  24     2336   3129   3664   -344    387   -755       O
ATOM    210  CG2ATHR A  24      28.985  -4.727 -40.600  0.63 23.49           C
ANISOU  210  CG2ATHR A  24     2312   3015   3598   -282    302   -651       C
ATOM    211  CG2BTHR A  24      29.281  -3.624 -38.955  0.37 21.02           C
ANISOU  211  CG2BTHR A  24     1991   2679   3316   -236    232   -539       C
ATOM    212  H  ATHR A  24      29.186  -0.714 -39.403  0.63  0.00           H
ATOM    213  H  BTHR A  24      29.138  -0.700 -39.449  0.37  0.00           H
ATOM    214  HA ATHR A  24      30.005  -2.398 -41.723  0.63  0.00           H
ATOM    215  HA BTHR A  24      29.927  -2.059 -41.935  0.37  0.00           H
ATOM    216  HB ATHR A  24      28.922  -3.283 -39.012  0.63  0.00           H
ATOM    217  HB BTHR A  24      31.036  -3.276 -40.113  0.37  0.00           H
ATOM    218  HG1ATHR A  24      31.157  -2.940 -38.981  0.63  0.00           H
ATOM    219  HG1BTHR A  24      30.488  -4.536 -41.817  0.37  0.00           H
ATOM    220 HG21ATHR A  24      28.087  -5.075 -40.089  0.63  0.00           H
ATOM    221 HG21BTHR A  24      29.802  -4.404 -38.400  0.37  0.00           H
ATOM    222 HG22ATHR A  24      29.750  -5.503 -40.559  0.63  0.00           H
ATOM    223 HG22BTHR A  24      28.248  -3.928 -39.124  0.37  0.00           H
ATOM    224 HG23ATHR A  24      28.748  -4.505 -41.641  0.63  0.00           H
ATOM    225 HG23BTHR A  24      29.298  -2.697 -38.383  0.37  0.00           H
ATOM    226  N   LEU A  25      27.597  -2.688 -42.392  1.00 16.09           N
ANISOU  226  N   LEU A  25     1660   2146   2308   -497    377   -491       N
ATOM    227  CA  LEU A  25      26.231  -2.689 -42.858  1.00 15.12           C
ANISOU  227  CA  LEU A  25     1646   2003   2097   -498    312   -386       C
ATOM    228  C   LEU A  25      25.522  -3.960 -42.383  1.00 14.43           C
ANISOU  228  C   LEU A  25     1505   1883   2095   -392    245   -377       C
ATOM    229  O   LEU A  25      26.060  -5.074 -42.482  1.00 15.29           O
ANISOU  229  O   LEU A  25     1532   1988   2289   -368    272   -483       O
ATOM    230  CB  LEU A  25      26.205  -2.621 -44.389  1.00 17.92           C
ANISOU  230  CB  LEU A  25     2092   2400   2315   -648    380   -427       C
ATOM    231  CG  LEU A  25      26.704  -1.309 -45.000  1.00 21.58           C
ANISOU  231  CG  LEU A  25     2663   2889   2647   -798    425   -409       C
ATOM    232  CD1 LEU A  25      26.755  -1.400 -46.528  1.00 24.74           C
ANISOU  232  CD1 LEU A  25     3165   3342   2895   -985    496   -462       C
ATOM    233  CD2 LEU A  25      25.791  -0.163 -44.533  1.00 21.11           C
ANISOU  233  CD2 LEU A  25     2712   2761   2547   -753    303   -245       C
ATOM    234  H  ALEU A  25      28.312  -3.115 -42.963  0.63  0.00           H
ATOM    235  H  BLEU A  25      28.316  -3.050 -43.001  0.37  0.00           H
ATOM    236  HA  LEU A  25      25.714  -1.819 -42.453  1.00  0.00           H
ATOM    237  HB2 LEU A  25      25.176  -2.772 -44.714  1.00  0.00           H
ATOM    238  HB3 LEU A  25      26.813  -3.436 -44.780  1.00  0.00           H
ATOM    239  HG  LEU A  25      27.712  -1.119 -44.632  1.00  0.00           H
ATOM    240 HD11 LEU A  25      27.113  -0.455 -46.937  1.00  0.00           H
ATOM    241 HD12 LEU A  25      27.432  -2.202 -46.822  1.00  0.00           H
ATOM    242 HD13 LEU A  25      25.757  -1.608 -46.913  1.00  0.00           H
ATOM    243 HD21 LEU A  25      26.138   0.777 -44.963  1.00  0.00           H
ATOM    244 HD22 LEU A  25      25.819  -0.097 -43.445  1.00  0.00           H
ATOM    245 HD23 LEU A  25      24.769  -0.357 -44.859  1.00  0.00           H
ATOM    246  N   VAL A  26      24.332  -3.769 -41.855  1.00 13.26           N
ANISOU  246  N   VAL A  26     1402   1709   1929   -335    155   -263       N
ATOM    247  CA  VAL A  26      23.425  -4.840 -41.453  1.00 13.41           C
ANISOU  247  CA  VAL A  26     1400   1707   1987   -270     87   -237       C
ATOM    248  C   VAL A  26      22.000  -4.648 -41.986  1.00 14.44           C
ANISOU  248  C   VAL A  26     1608   1849   2028   -284     33   -158       C
ATOM    249  O   VAL A  26      21.632  -3.577 -42.474  1.00 15.76           O
ANISOU  249  O   VAL A  26     1849   2020   2121   -321     16   -104       O
ATOM    250  CB  VAL A  26      23.306  -4.906 -39.922  1.00 13.05           C
ANISOU  250  CB  VAL A  26     1303   1635   2022   -193     20   -193       C
ATOM    251  CG1 VAL A  26      24.688  -5.146 -39.260  1.00 15.11           C
ANISOU  251  CG1 VAL A  26     1482   1872   2388   -169     38   -262       C
ATOM    252  CG2 VAL A  26      22.597  -3.669 -39.355  1.00 13.83           C
ANISOU  252  CG2 VAL A  26     1437   1741   2079   -181    -14   -110       C
ATOM    253  H   VAL A  26      24.025  -2.816 -41.719  1.00  0.00           H
ATOM    254  HA  VAL A  26      23.815  -5.790 -41.819  1.00  0.00           H
ATOM    255  HB  VAL A  26      22.683  -5.769 -39.686  1.00  0.00           H
ATOM    256 HG21 VAL A  26      22.532  -3.752 -38.270  1.00  0.00           H
ATOM    257 HG22 VAL A  26      23.162  -2.775 -39.617  1.00  0.00           H
ATOM    258 HG23 VAL A  26      21.593  -3.601 -39.775  1.00  0.00           H
ATOM    259 HG11 VAL A  26      24.570  -5.188 -38.177  1.00  0.00           H
ATOM    260 HG12 VAL A  26      25.362  -4.330 -39.521  1.00  0.00           H
ATOM    261 HG13 VAL A  26      25.103  -6.089 -39.617  1.00  0.00           H
ATOM    262  N   LYS A  27      21.183  -5.694 -41.847  1.00 12.75           N
ANISOU  262  N   LYS A  27     1381   1634   1829   -256    -12   -150       N
ATOM    263  CA  LYS A  27      19.799  -5.667 -42.299  1.00 12.90           C
ANISOU  263  CA  LYS A  27     1449   1674   1778   -265    -69    -90       C
ATOM    264  C   LYS A  27      18.872  -5.538 -41.119  1.00 13.39           C
ANISOU  264  C   LYS A  27     1470   1745   1874   -207   -137    -43       C
ATOM    265  O   LYS A  27      19.177  -6.059 -40.051  1.00 13.90           O
ANISOU  265  O   LYS A  27     1487   1797   1999   -181   -143    -56       O
ATOM    266  CB  LYS A  27      19.480  -6.997 -43.002  1.00 15.09           C
ANISOU  266  CB  LYS A  27     1738   1959   2036   -297    -61   -130       C
ATOM    267  CG  LYS A  27      20.469  -7.388 -44.073  1.00 22.91           C
ANISOU  267  CG  LYS A  27     2745   2951   3009   -364     26   -221       C
ATOM    268  CD  LYS A  27      19.898  -8.576 -44.803  1.00 31.44           C
ANISOU  268  CD  LYS A  27     3849   4038   4057   -399     25   -253       C
ATOM    269  CE  LYS A  27      20.016  -8.469 -46.286  1.00 36.93           C
ANISOU  269  CE  LYS A  27     4617   4769   4647   -514     87   -293       C
ATOM    270  NZ  LYS A  27      19.414  -9.692 -46.923  1.00 36.97           N
ANISOU  270  NZ  LYS A  27     4644   4779   4623   -549     85   -329       N
ATOM    271  H   LYS A  27      21.537  -6.534 -41.413  1.00  0.00           H
ATOM    272  HA  LYS A  27      19.647  -4.835 -42.987  1.00  0.00           H
ATOM    273  HB2 LYS A  27      19.463  -7.785 -42.249  1.00  0.00           H
ATOM    274  HB3 LYS A  27      18.490  -6.924 -43.452  1.00  0.00           H
ATOM    275  HG2 LYS A  27      21.424  -7.654 -43.619  1.00  0.00           H
ATOM    276  HG3 LYS A  27      20.608  -6.560 -44.768  1.00  0.00           H
ATOM    277  HD2 LYS A  27      20.429  -9.470 -44.477  1.00  0.00           H
ATOM    278  HD3 LYS A  27      18.845  -8.677 -44.540  1.00  0.00           H
ATOM    279  HE2 LYS A  27      19.486  -7.581 -46.630  1.00  0.00           H
ATOM    280  HE3 LYS A  27      21.068  -8.395 -46.563  1.00  0.00           H
ATOM    281  HZ1 LYS A  27      18.441  -9.764 -46.660  1.00  0.00           H
ATOM    282  HZ2 LYS A  27      19.909 -10.514 -46.609  1.00  0.00           H
ATOM    283  HZ3 LYS A  27      19.487  -9.619 -47.928  1.00  0.00           H
ATOM    284  N   THR A  28      17.752  -4.849 -41.298  1.00 13.53           N
ANISOU  284  N   THR A  28     1505   1782   1855   -195   -193      1       N
ATOM    285  CA  THR A  28      16.757  -4.714 -40.252  1.00 13.58           C
ANISOU  285  CA  THR A  28     1450   1817   1892   -154   -242     10       C
ATOM    286  C   THR A  28      15.394  -5.060 -40.843  1.00 14.06           C
ANISOU  286  C   THR A  28     1510   1919   1912   -163   -299     18       C
ATOM    287  O   THR A  28      15.305  -5.554 -41.957  1.00 15.53           O
ANISOU  287  O   THR A  28     1751   2105   2045   -204   -301     26       O
ATOM    288  CB  THR A  28      16.700  -3.302 -39.659  1.00 14.72           C
ANISOU  288  CB  THR A  28     1575   1947   2071   -108   -263     22       C
ATOM    289  OG1 THR A  28      16.261  -2.385 -40.673  1.00 16.55           O
ANISOU  289  OG1 THR A  28     1865   2151   2273   -101   -320     54       O
ATOM    290  CG2 THR A  28      18.079  -2.878 -39.145  1.00 13.92           C
ANISOU  290  CG2 THR A  28     1480   1811   2000   -111   -207     17       C
ATOM    291  H   THR A  28      17.588  -4.405 -42.190  1.00  0.00           H
ATOM    292  HA  THR A  28      16.985  -5.422 -39.455  1.00  0.00           H
ATOM    293  HB  THR A  28      15.990  -3.289 -38.832  1.00  0.00           H
ATOM    294  HG1 THR A  28      15.560  -1.831 -40.322  1.00  0.00           H
ATOM    295 HG21 THR A  28      18.018  -1.873 -38.728  1.00  0.00           H
ATOM    296 HG22 THR A  28      18.792  -2.887 -39.969  1.00  0.00           H
ATOM    297 HG23 THR A  28      18.408  -3.573 -38.373  1.00  0.00           H
ATOM    298  N   ILE A  29      14.336  -4.787 -40.091  1.00 13.87           N
ANISOU  298  N   ILE A  29     1416   1940   1915   -134   -340      2       N
ATOM    299  CA  ILE A  29      12.964  -4.960 -40.566  1.00 15.80           C
ANISOU  299  CA  ILE A  29     1629   2234   2139   -134   -404     -8       C
ATOM    300  C   ILE A  29      12.646  -3.979 -41.700  1.00 16.07           C
ANISOU  300  C   ILE A  29     1714   2227   2165   -105   -484     28       C
ATOM    301  O   ILE A  29      11.963  -4.299 -42.685  1.00 14.30           O
ANISOU  301  O   ILE A  29     1521   2016   1895   -130   -541     47       O
ATOM    302  CB  ILE A  29      11.992  -4.714 -39.399  1.00 20.69           C
ANISOU  302  CB  ILE A  29     2135   2922   2804   -114   -417    -69       C
ATOM    303  CG1 ILE A  29      12.159  -5.820 -38.353  1.00 23.20           C
ANISOU  303  CG1 ILE A  29     2437   3283   3095   -188   -360    -91       C
ATOM    304  CG2 ILE A  29      10.567  -4.693 -39.891  1.00 23.00           C
ANISOU  304  CG2 ILE A  29     2365   3273   3100   -101   -490   -103       C
ATOM    305  CD1 ILE A  29      11.930  -7.232 -38.989  1.00 30.24           C
ANISOU  305  CD1 ILE A  29     3380   4189   3921   -256   -363    -74       C
ATOM    306  H   ILE A  29      14.484  -4.446 -39.152  1.00  0.00           H
ATOM    307  HA  ILE A  29      12.837  -5.980 -40.929  1.00  0.00           H
ATOM    308  HB  ILE A  29      12.224  -3.753 -38.940  1.00  0.00           H
ATOM    309 HG12 ILE A  29      11.434  -5.667 -37.554  1.00  0.00           H
ATOM    310 HG13 ILE A  29      13.166  -5.772 -37.938  1.00  0.00           H
ATOM    311 HG21 ILE A  29      10.451  -3.905 -40.635  1.00  0.00           H
ATOM    312 HG22 ILE A  29       9.896  -4.503 -39.053  1.00  0.00           H
ATOM    313 HG23 ILE A  29      10.323  -5.656 -40.340  1.00  0.00           H
ATOM    314 HD11 ILE A  29      11.547  -7.915 -38.231  1.00  0.00           H
ATOM    315 HD12 ILE A  29      11.209  -7.151 -39.803  1.00  0.00           H
ATOM    316 HD13 ILE A  29      12.875  -7.613 -39.377  1.00  0.00           H
ATOM    317  N  ATHR A  30      13.186  -2.787 -41.583  0.83 18.06           N
ANISOU  317  N  ATHR A  30     1992   2419   2453    -64   -500     46       N
ATOM    318  N  BTHR A  30      13.198  -2.791 -41.575  0.17 18.11           N
ANISOU  318  N  BTHR A  30     1998   2425   2459    -64   -499     46       N
ATOM    319  CA ATHR A  30      12.823  -1.717 -42.507  0.83 20.92           C
ANISOU  319  CA ATHR A  30     2419   2718   2813    -40   -612     89       C
ATOM    320  CA BTHR A  30      12.862  -1.710 -42.472  0.17 20.93           C
ANISOU  320  CA BTHR A  30     2419   2718   2814    -40   -608     88       C
ATOM    321  C  ATHR A  30      13.906  -1.370 -43.514  0.83 20.62           C
ANISOU  321  C  ATHR A  30     2526   2616   2694   -114   -595    151       C
ATOM    322  C  BTHR A  30      13.867  -1.588 -43.607  0.17 21.13           C
ANISOU  322  C  BTHR A  30     2590   2690   2747   -124   -588    149       C
ATOM    323  O  ATHR A  30      13.633  -0.634 -44.462  0.83 23.23           O
ANISOU  323  O  ATHR A  30     2952   2887   2987   -136   -702    205       O
ATOM    324  O  BTHR A  30      13.507  -1.295 -44.745  0.17 23.18           O
ANISOU  324  O  BTHR A  30     2944   2915   2947   -167   -678    200       O
ATOM    325  CB ATHR A  30      12.463  -0.416 -41.770  0.83 22.51           C
ANISOU  325  CB ATHR A  30     2562   2876   3114     54   -679     61       C
ATOM    326  CB BTHR A  30      12.821  -0.409 -41.679  0.17 22.19           C
ANISOU  326  CB BTHR A  30     2536   2830   3065     43   -651     66       C
ATOM    327  OG1ATHR A  30      13.586   0.054 -41.004  0.83 22.53           O
ANISOU  327  OG1ATHR A  30     2578   2849   3132     52   -595     59       O
ATOM    328  OG1BTHR A  30      11.870  -0.545 -40.615  0.17 22.85           O
ANISOU  328  OG1BTHR A  30     2470   2985   3229     99   -649    -21       O
ATOM    329  CG2ATHR A  30      11.254  -0.638 -40.855  0.83 23.74           C
ANISOU  329  CG2ATHR A  30     2556   3113   3350    111   -694    -33       C
ATOM    330  CG2BTHR A  30      12.446   0.750 -42.565  0.17 22.76           C
ANISOU  330  CG2BTHR A  30     2691   2806   3151     74   -801    116       C
ATOM    331  H  ATHR A  30      13.857  -2.610 -40.849  0.83  0.00           H
ATOM    332  H  BTHR A  30      13.870  -2.632 -40.838  0.17  0.00           H
ATOM    333  HA ATHR A  30      11.943  -2.040 -43.062  0.83  0.00           H
ATOM    334  HA BTHR A  30      11.875  -1.897 -42.894  0.17  0.00           H
ATOM    335  HB ATHR A  30      12.205   0.342 -42.509  0.83  0.00           H
ATOM    336  HB BTHR A  30      13.806  -0.224 -41.252  0.17  0.00           H
ATOM    337  HG1ATHR A  30      14.402  -0.207 -41.438  0.83  0.00           H
ATOM    338  HG1BTHR A  30      12.321  -0.473 -39.771  0.17  0.00           H
ATOM    339 HG21ATHR A  30      10.357  -0.766 -41.461  0.83  0.00           H
ATOM    340 HG21BTHR A  30      13.197   1.535 -42.475  0.17  0.00           H
ATOM    341 HG22ATHR A  30      11.415  -1.531 -40.251  0.83  0.00           H
ATOM    342 HG22BTHR A  30      11.475   1.140 -42.260  0.17  0.00           H
ATOM    343 HG23ATHR A  30      11.130   0.225 -40.201  0.83  0.00           H
ATOM    344 HG23BTHR A  30      12.394   0.414 -43.601  0.17  0.00           H
ATOM    345  N   ASP A  31      15.127  -1.842 -43.285  1.00 19.06           N
ANISOU  345  N   ASP A  31     2344   2427   2470   -162   -472    134       N
ATOM    346  CA  ASP A  31      16.241  -1.502 -44.164  1.00 20.17           C
ANISOU  346  CA  ASP A  31     2600   2530   2532   -253   -427    159       C
ATOM    347  C   ASP A  31      17.037  -2.717 -44.604  1.00 19.30           C
ANISOU  347  C   ASP A  31     2495   2463   2376   -330   -312    112       C
ATOM    348  O   ASP A  31      17.424  -3.541 -43.789  1.00 18.52           O
ANISOU  348  O   ASP A  31     2311   2389   2336   -294   -244     63       O
ATOM    349  CB  ASP A  31      17.223  -0.581 -43.442  1.00 26.43           C
ANISOU  349  CB  ASP A  31     3393   3285   3363   -236   -384    155       C
ATOM    350  CG  ASP A  31      16.665   0.795 -43.180  1.00 36.11           C
ANISOU  350  CG  ASP A  31     4643   4443   4633   -173   -498    193       C
ATOM    351  OD1 ASP A  31      16.875   1.663 -44.053  1.00 41.05           O
ANISOU  351  OD1 ASP A  31     5402   5001   5193   -237   -565    249       O
ATOM    352  OD2 ASP A  31      16.059   1.017 -42.099  1.00 38.84           O
ANISOU  352  OD2 ASP A  31     4884   4798   5076    -74   -522    159       O
ATOM    353  H  AASP A  31      15.286  -2.445 -42.491  0.83  0.00           H
ATOM    354  H  BASP A  31      15.323  -2.287 -42.400  0.17  0.00           H
ATOM    355  HA  ASP A  31      15.855  -0.990 -45.046  1.00  0.00           H
ATOM    356  HB2 ASP A  31      18.118  -0.480 -44.056  1.00  0.00           H
ATOM    357  HB3 ASP A  31      17.498  -1.036 -42.491  1.00  0.00           H
ATOM    358  N  AASP A  32      17.311  -2.805 -45.895  0.72 21.50           N
ANISOU  358  N  AASP A  32     2878   2742   2550   -443   -298    121       N
ATOM    359  N  BASP A  32      17.298  -2.797 -45.902  0.28 21.54           N
ANISOU  359  N  BASP A  32     2884   2747   2554   -443   -300    122       N
ATOM    360  CA AASP A  32      18.150  -3.882 -46.420  0.72 23.80           C
ANISOU  360  CA AASP A  32     3166   3072   2805   -523   -178     44       C
ATOM    361  CA BASP A  32      18.145  -3.844 -46.459  0.28 23.95           C
ANISOU  361  CA BASP A  32     3189   3090   2820   -526   -180     46       C
ATOM    362  C  AASP A  32      19.620  -3.662 -46.040  0.72 23.34           C
ANISOU  362  C  AASP A  32     3076   3012   2781   -542    -68    -22       C
ATOM    363  C  BASP A  32      19.592  -3.661 -45.999  0.28 23.38           C
ANISOU  363  C  BASP A  32     3078   3016   2789   -538    -70    -20       C
ATOM    364  O  AASP A  32      20.396  -4.617 -45.943  0.72 24.72           O
ANISOU  364  O  AASP A  32     3183   3209   3001   -547     26   -115       O
ATOM    365  O  BASP A  32      20.318  -4.635 -45.803  0.28 24.55           O
ANISOU  365  O  BASP A  32     3152   3185   2991   -531     17   -110       O
ATOM    366  CB AASP A  32      18.002  -3.972 -47.948  0.72 27.49           C
ANISOU  366  CB AASP A  32     3757   3553   3133   -668   -183     56       C
ATOM    367  CB BASP A  32      18.076  -3.806 -47.991  0.28 28.26           C
ANISOU  367  CB BASP A  32     3868   3647   3224   -677   -185     61       C
ATOM    368  CG AASP A  32      18.803  -5.115 -48.537  0.72 32.62           C
ANISOU  368  CG AASP A  32     4390   4248   3755   -754    -49    -56       C
ATOM    369  CG BASP A  32      18.637  -2.524 -48.565  0.28 32.86           C
ANISOU  369  CG BASP A  32     4575   4195   3717   -782   -205    106       C
ATOM    370  OD1AASP A  32      18.356  -6.278 -48.423  0.72 35.93           O
ANISOU  370  OD1AASP A  32     4752   4685   4214   -713    -40    -92       O
ATOM    371  OD1BASP A  32      19.249  -2.573 -49.659  0.28 35.67           O
ANISOU  371  OD1BASP A  32     5030   4579   3946   -953   -137     72       O
ATOM    372  OD2AASP A  32      19.879  -4.850 -49.114  0.72 32.99           O
ANISOU  372  OD2AASP A  32     4477   4313   3743   -868     49   -120       O
ATOM    373  OD2BASP A  32      18.481  -1.460 -47.918  0.28 34.33           O
ANISOU  373  OD2BASP A  32     4767   4326   3952   -709   -285    166       O
ATOM    374  H  AASP A  32      16.934  -2.116 -46.530  0.72  0.00           H
ATOM    375  H  BASP A  32      16.897  -2.110 -46.524  0.28  0.00           H
ATOM    376  HA AASP A  32      17.817  -4.824 -45.984  0.72  0.00           H
ATOM    377  HA BASP A  32      17.784  -4.812 -46.113  0.28  0.00           H
ATOM    378  HB2AASP A  32      16.950  -4.120 -48.190  0.72  0.00           H
ATOM    379  HB2BASP A  32      17.034  -3.899 -48.296  0.28  0.00           H
ATOM    380  HB3AASP A  32      18.340  -3.036 -48.393  0.72  0.00           H
ATOM    381  HB3BASP A  32      18.639  -4.649 -48.392  0.28  0.00           H
ATOM    382  N   GLN A  33      20.004  -2.409 -45.824  1.00 21.48           N
ANISOU  382  N   GLN A  33     2884   2745   2534   -552    -89     19       N
ATOM    383  CA  GLN A  33      21.372  -2.097 -45.439  1.00 21.46           C
ANISOU  383  CA  GLN A  33     2846   2750   2560   -578     11    -43       C
ATOM    384  C   GLN A  33      21.412  -0.825 -44.613  1.00 21.27           C
ANISOU  384  C   GLN A  33     2833   2678   2570   -524    -44     18       C
ATOM    385  O   GLN A  33      21.032   0.247 -45.083  1.00 22.84           O
ANISOU  385  O   GLN A  33     3146   2831   2701   -568   -125     92       O
ATOM    386  CB  GLN A  33      22.283  -1.938 -46.677  1.00 24.51           C
ANISOU  386  CB  GLN A  33     3317   3170   2825   -757    104   -102       C
ATOM    387  CG  GLN A  33      22.532  -3.290 -47.456  1.00 37.16           C
ANISOU  387  CG  GLN A  33     4882   4828   4411   -819    197   -214       C
ATOM    388  CD  GLN A  33      23.463  -4.334 -46.724  1.00 32.30           C
ANISOU  388  CD  GLN A  33     4102   4228   3941   -735    288   -347       C
ATOM    389  OE1 GLN A  33      23.103  -4.950 -45.692  1.00 28.24           O
ANISOU  389  OE1 GLN A  33     3502   3682   3546   -593    233   -328       O
ATOM    390  NE2 GLN A  33      24.662  -4.530 -47.291  1.00 34.05           N
ANISOU  390  NE2 GLN A  33     4285   4500   4152   -837    418   -490       N
ATOM    391  H  AGLN A  33      19.335  -1.660 -45.929  0.72  0.00           H
ATOM    392  H  BGLN A  33      19.349  -1.653 -45.962  0.28  0.00           H
ATOM    393  HA  GLN A  33      21.755  -2.916 -44.831  1.00  0.00           H
ATOM    394  HB2 GLN A  33      23.246  -1.547 -46.348  1.00  0.00           H
ATOM    395  HB3 GLN A  33      21.827  -1.220 -47.358  1.00  0.00           H
ATOM    396  HG2 GLN A  33      22.990  -3.046 -48.415  1.00  0.00           H
ATOM    397  HG3 GLN A  33      21.568  -3.761 -47.645  1.00  0.00           H
ATOM    398 HE21 GLN A  33      24.916  -4.020 -48.125  1.00  0.00           H
ATOM    399 HE22 GLN A  33      25.312  -5.188 -46.884  1.00  0.00           H
ATOM    400  N   ILE A  34      21.878  -0.930 -43.379  1.00 16.99           N
ANISOU  400  N   ILE A  34     2265   2166   2026   -276    505     -3       N
ATOM    401  CA  ILE A  34      22.019   0.277 -42.550  1.00 16.38           C
ANISOU  401  CA  ILE A  34     2147   2078   1999   -308    465    -15       C
ATOM    402  C   ILE A  34      23.304   0.152 -41.711  1.00 15.10           C
ANISOU  402  C   ILE A  34     1872   1870   1996   -323    407    -43       C
ATOM    403  O   ILE A  34      23.655  -0.947 -41.304  1.00 14.20           O
ANISOU  403  O   ILE A  34     1733   1758   1902   -312    346    -55       O
ATOM    404  CB  ILE A  34      20.784   0.504 -41.718  1.00 17.78           C
ANISOU  404  CB  ILE A  34     2386   2311   2061   -319    375    -17       C
ATOM    405  CG1 ILE A  34      20.873   1.834 -40.982  1.00 23.34           C
ANISOU  405  CG1 ILE A  34     3062   3003   2804   -347    343    -28       C
ATOM    406  CG2 ILE A  34      20.536  -0.578 -40.739  1.00 15.07           C
ANISOU  406  CG2 ILE A  34     2047   1994   1684   -316    271    -29       C
ATOM    407  CD1 ILE A  34      19.480   2.285 -40.545  1.00 27.02           C
ANISOU  407  CD1 ILE A  34     3608   3518   3141   -355    300    -22       C
ATOM    408  H   ILE A  34      22.135  -1.834 -43.008  1.00  0.00           H
ATOM    409  HA  ILE A  34      22.136   1.131 -43.217  1.00  0.00           H
ATOM    410  HB  ILE A  34      19.929   0.550 -42.392  1.00  0.00           H
ATOM    411 HG12 ILE A  34      21.304   2.585 -41.645  1.00  0.00           H
ATOM    412 HG13 ILE A  34      21.508   1.720 -40.104  1.00  0.00           H
ATOM    413 HG21 ILE A  34      20.471  -1.533 -41.261  1.00  0.00           H
ATOM    414 HG22 ILE A  34      21.355  -0.612 -40.020  1.00  0.00           H
ATOM    415 HG23 ILE A  34      19.600  -0.386 -40.215  1.00  0.00           H
ATOM    416 HD11 ILE A  34      19.554   3.237 -40.019  1.00  0.00           H
ATOM    417 HD12 ILE A  34      18.845   2.403 -41.423  1.00  0.00           H
ATOM    418 HD13 ILE A  34      19.047   1.536 -39.881  1.00  0.00           H
ATOM    419  N   GLU A  35      24.021   1.257 -41.514  1.00 14.98           N
ANISOU  419  N   GLU A  35     1787   1805   2100   -343    426    -57       N
ATOM    420  CA  GLU A  35      25.334   1.184 -40.905  1.00 15.34           C
ANISOU  420  CA  GLU A  35     1713   1788   2328   -350    375    -92       C
ATOM    421  C   GLU A  35      25.302   1.275 -39.393  1.00 14.19           C
ANISOU  421  C   GLU A  35     1554   1652   2187   -357    205   -127       C
ATOM    422  O   GLU A  35      24.769   2.222 -38.833  1.00 13.33           O
ANISOU  422  O   GLU A  35     1475   1558   2030   -371    161   -130       O
ATOM    423  CB  GLU A  35      26.248   2.289 -41.461  1.00 16.23           C
ANISOU  423  CB  GLU A  35     1741   1820   2605   -366    483    -97       C
ATOM    424  CG  GLU A  35      27.686   2.010 -41.227  1.00 16.80           C
ANISOU  424  CG  GLU A  35     1676   1808   2898   -368    468   -134       C
ATOM    425  CD  GLU A  35      28.581   3.140 -41.812  1.00 30.26           C
ANISOU  425  CD  GLU A  35     3288   3419   4793   -385    597   -139       C
ATOM    426  OE1 GLU A  35      28.296   3.614 -42.934  1.00 35.80           O
ANISOU  426  OE1 GLU A  35     4072   4122   5410   -357    731    -98       O
ATOM    427  OE2 GLU A  35      29.528   3.574 -41.149  1.00 25.78           O
ANISOU  427  OE2 GLU A  35     2614   2787   4394   -384    521   -184       O
ATOM    428  H   GLU A  35      23.647   2.153 -41.791  1.00  0.00           H
ATOM    429  HA  GLU A  35      25.773   0.223 -41.172  1.00  0.00           H
ATOM    430  HB2 GLU A  35      26.079   2.375 -42.534  1.00  0.00           H
ATOM    431  HB3 GLU A  35      25.989   3.235 -40.985  1.00  0.00           H
ATOM    432  HG2 GLU A  35      27.947   1.066 -41.705  1.00  0.00           H
ATOM    433  HG3 GLU A  35      27.865   1.930 -40.155  1.00  0.00           H
ATOM    434  N   VAL A  36      25.917   0.287 -38.740  1.00 13.98           N
ANISOU  434  N   VAL A  36     1488   1607   2215   -341    108   -154       N
ATOM    435  CA  VAL A  36      26.124   0.308 -37.309  1.00 14.05           C
ANISOU  435  CA  VAL A  36     1491   1603   2244   -332    -61   -194       C
ATOM    436  C   VAL A  36      27.601   0.316 -36.960  1.00 14.04           C
ANISOU  436  C   VAL A  36     1359   1512   2465   -325   -124   -247       C
ATOM    437  O   VAL A  36      28.465   0.102 -37.817  1.00 14.71           O
ANISOU  437  O   VAL A  36     1352   1547   2691   -330    -28   -249       O
ATOM    438  CB  VAL A  36      25.389  -0.897 -36.619  1.00 12.69           C
ANISOU  438  CB  VAL A  36     1418   1484   1921   -306   -148   -186       C
ATOM    439  CG1 VAL A  36      23.848  -0.781 -36.779  1.00 13.28           C
ANISOU  439  CG1 VAL A  36     1611   1633   1801   -314   -101   -144       C
ATOM    440  CG2 VAL A  36      25.827  -2.254 -37.217  1.00 13.37           C
ANISOU  440  CG2 VAL A  36     1479   1569   2033   -290   -111   -179       C
ATOM    441  H   VAL A  36      26.251  -0.507 -39.266  1.00  0.00           H
ATOM    442  HA  VAL A  36      25.686   1.229 -36.923  1.00  0.00           H
ATOM    443  HB  VAL A  36      25.631  -0.890 -35.556  1.00  0.00           H
ATOM    444 HG11 VAL A  36      23.510   0.169 -36.365  1.00  0.00           H
ATOM    445 HG12 VAL A  36      23.588  -0.829 -37.836  1.00  0.00           H
ATOM    446 HG13 VAL A  36      23.365  -1.601 -36.248  1.00  0.00           H
ATOM    447 HG21 VAL A  36      26.907  -2.363 -37.119  1.00  0.00           H
ATOM    448 HG22 VAL A  36      25.330  -3.064 -36.683  1.00  0.00           H
ATOM    449 HG23 VAL A  36      25.553  -2.292 -38.271  1.00  0.00           H
ATOM    450  N   THR A  37      27.933   0.540 -35.690  1.00 13.37           N
ANISOU  450  N   THR A  37     1266   1394   2422   -309   -290   -295       N
ATOM    451  CA  THR A  37      29.340   0.663 -35.361  1.00 14.64           C
ANISOU  451  CA  THR A  37     1290   1455   2817   -300   -366   -357       C
ATOM    452  C   THR A  37      30.058  -0.677 -35.421  1.00 15.32           C
ANISOU  452  C   THR A  37     1334   1517   2972   -275   -400   -375       C
ATOM    453  O   THR A  37      31.236  -0.691 -35.600  1.00 16.92           O
ANISOU  453  O   THR A  37     1403   1635   3391   -275   -405   -417       O
ATOM    454  CB  THR A  37      29.574   1.252 -33.982  1.00 16.08           C
ANISOU  454  CB  THR A  37     1481   1595   3035   -277   -557   -413       C
ATOM    455  OG1 THR A  37      28.943   0.403 -33.019  1.00 16.93           O
ANISOU  455  OG1 THR A  37     1722   1745   2966   -238   -680   -411       O
ATOM    456  CG2 THR A  37      28.958   2.652 -33.911  1.00 14.78           C
ANISOU  456  CG2 THR A  37     1346   1447   2823   -303   -525   -399       C
ATOM    457  H   THR A  37      27.224   0.622 -34.975  1.00  0.00           H
ATOM    458  HA  THR A  37      29.801   1.326 -36.093  1.00  0.00           H
ATOM    459  HB  THR A  37      30.644   1.308 -33.781  1.00  0.00           H
ATOM    460  HG1 THR A  37      28.764   0.903 -32.219  1.00  0.00           H
ATOM    461 HG21 THR A  37      29.127   3.074 -32.920  1.00  0.00           H
ATOM    462 HG22 THR A  37      27.887   2.587 -34.100  1.00  0.00           H
ATOM    463 HG23 THR A  37      29.422   3.292 -34.662  1.00  0.00           H
ATOM    464  N   ASN A  38      29.358  -1.795 -35.255  1.00 13.84           N
ANISOU  464  N   ASN A  38     1253   1395   2611   -255   -423   -346       N
ATOM    465  CA  ASN A  38      30.040  -3.096 -35.166  1.00 15.48           C
ANISOU  465  CA  ASN A  38     1427   1577   2875   -227   -476   -368       C
ATOM    466  C   ASN A  38      28.988  -4.177 -35.374  1.00 15.19           C
ANISOU  466  C   ASN A  38     1515   1628   2627   -218   -433   -315       C
ATOM    467  O   ASN A  38      27.822  -3.950 -35.085  1.00 15.64           O
ANISOU  467  O   ASN A  38     1687   1748   2507   -221   -430   -283       O
ATOM    468  CB  ASN A  38      30.668  -3.273 -33.791  1.00 17.45           C
ANISOU  468  CB  ASN A  38     1675   1767   3187   -184   -691   -435       C
ATOM    469  CG  ASN A  38      31.735  -4.391 -33.738  1.00 23.01           C
ANISOU  469  CG  ASN A  38     2302   2415   4025   -154   -756   -474       C
ATOM    470  OD1 ASN A  38      32.184  -4.901 -34.775  1.00 20.96           O
ANISOU  470  OD1 ASN A  38     1959   2147   3856   -174   -631   -458       O
ATOM    471  ND2 ASN A  38      32.133  -4.750 -32.522  1.00 34.41           N
ANISOU  471  ND2 ASN A  38     3809   3825   5442    -85   -914   -506       N
ATOM    472  H   ASN A  38      28.351  -1.751 -35.190  1.00  0.00           H
ATOM    473  HA  ASN A  38      30.806  -3.168 -35.938  1.00  0.00           H
ATOM    474  HB2 ASN A  38      31.139  -2.333 -33.504  1.00  0.00           H
ATOM    475  HB3 ASN A  38      29.881  -3.505 -33.073  1.00  0.00           H
ATOM    476 HD21 ASN A  38      31.738  -4.301 -31.708  1.00  0.00           H
ATOM    477 HD22 ASN A  38      32.830  -5.472 -32.412  1.00  0.00           H
ATOM    478  N   ALA A  39      29.400  -5.339 -35.857  1.00 13.77           N
ANISOU  478  N   ALA A  39     1307   1447   2479   -206   -402   -311       N
ATOM    479  CA  ALA A  39      28.510  -6.457 -35.974  1.00 14.00           C
ANISOU  479  CA  ALA A  39     1442   1546   2332   -193   -379   -271       C
ATOM    480  C   ALA A  39      29.339  -7.738 -35.941  1.00 15.71           C
ANISOU  480  C   ALA A  39     1613   1732   2625   -166   -426   -294       C
ATOM    481  O   ALA A  39      30.585  -7.698 -36.005  1.00 17.76           O
ANISOU  481  O   ALA A  39     1750   1915   3083   -162   -455   -337       O
ATOM    482  CB  ALA A  39      27.730  -6.412 -37.260  1.00 14.19           C
ANISOU  482  CB  ALA A  39     1496   1626   2270   -218   -209   -216       C
ATOM    483  H   ALA A  39      30.362  -5.440 -36.149  1.00  0.00           H
ATOM    484  HA  ALA A  39      27.817  -6.455 -35.133  1.00  0.00           H
ATOM    485  HB1 ALA A  39      26.981  -7.204 -37.259  1.00  0.00           H
ATOM    486  HB2 ALA A  39      27.235  -5.445 -37.351  1.00  0.00           H
ATOM    487  HB3 ALA A  39      28.408  -6.554 -38.101  1.00  0.00           H
ATOM    488  N   THR A  40      28.649  -8.870 -35.843  1.00 14.81           N
ANISOU  488  N   THR A  40     1592   1670   2367   -148   -432   -266       N
ATOM    489  CA  THR A  40      29.348 -10.137 -35.821  1.00 16.65           C
ANISOU  489  CA  THR A  40     1792   1879   2655   -122   -474   -284       C
ATOM    490  C   THR A  40      28.627 -11.108 -36.765  1.00 16.77           C
ANISOU  490  C   THR A  40     1856   1957   2559   -128   -357   -234       C
ATOM    491  O   THR A  40      27.413 -11.029 -36.987  1.00 17.31           O
ANISOU  491  O   THR A  40     2016   2087   2476   -139   -299   -194       O
ATOM    492  CB  THR A  40      29.511 -10.652 -34.368  1.00 30.76           C
ANISOU  492  CB  THR A  40     3646   3636   4404    -76   -657   -321       C
ATOM    493  OG1 THR A  40      30.462 -11.718 -34.365  1.00 34.28           O
ANISOU  493  OG1 THR A  40     4033   4041   4950    -50   -710   -351       O
ATOM    494  CG2 THR A  40      28.227 -11.144 -33.834  1.00 27.58           C
ANISOU  494  CG2 THR A  40     3397   3293   3788    -62   -662   -282       C
ATOM    495  H   THR A  40      27.641  -8.846 -35.784  1.00  0.00           H
ATOM    496  HA  THR A  40      30.347  -9.968 -36.224  1.00  0.00           H
ATOM    497  HB  THR A  40      29.876  -9.841 -33.737  1.00  0.00           H
ATOM    498  HG1 THR A  40      30.043 -12.521 -34.047  1.00  0.00           H
ATOM    499 HG21 THR A  40      28.370 -11.499 -32.813  1.00  0.00           H
ATOM    500 HG22 THR A  40      27.498 -10.334 -33.838  1.00  0.00           H
ATOM    501 HG23 THR A  40      27.864 -11.962 -34.456  1.00  0.00           H
ATOM    502  N   GLU A  41      29.407 -11.989 -37.370  1.00 15.18           N
ANISOU  502  N   GLU A  41     1586   1732   2449   -119   -323   -241       N
ATOM    503  CA  GLU A  41      28.941 -12.864 -38.426  1.00 13.08           C
ANISOU  503  CA  GLU A  41     1348   1510   2110   -121   -209   -201       C
ATOM    504  C   GLU A  41      28.255 -14.052 -37.808  1.00 13.65           C
ANISOU  504  C   GLU A  41     1516   1622   2049    -96   -277   -190       C
ATOM    505  O   GLU A  41      28.811 -14.718 -36.908  1.00 15.75           O
ANISOU  505  O   GLU A  41     1781   1856   2346    -68   -395   -221       O
ATOM    506  CB  GLU A  41      30.189 -13.322 -39.244  1.00 18.33           C
ANISOU  506  CB  GLU A  41     1898   2120   2945   -117   -146   -217       C
ATOM    507  CG  GLU A  41      29.893 -14.339 -40.355  1.00 18.97           C
ANISOU  507  CG  GLU A  41     2009   2235   2963   -109    -36   -181       C
ATOM    508  CD  GLU A  41      28.837 -13.830 -41.326  1.00 18.99           C
ANISOU  508  CD  GLU A  41     2086   2286   2842   -121     86   -137       C
ATOM    509  OE1 GLU A  41      29.109 -12.859 -42.055  1.00 19.77           O
ANISOU  509  OE1 GLU A  41     2152   2357   3004   -134    188   -129       O
ATOM    510  OE2 GLU A  41      27.737 -14.389 -41.336  1.00 17.07           O
ANISOU  510  OE2 GLU A  41     1938   2102   2447   -113     77   -114       O
ATOM    511  H   GLU A  41      30.373 -12.054 -37.082  1.00  0.00           H
ATOM    512  HA  GLU A  41      28.247 -12.329 -39.074  1.00  0.00           H
ATOM    513  HB2 GLU A  41      30.636 -12.440 -39.702  1.00  0.00           H
ATOM    514  HB3 GLU A  41      30.913 -13.760 -38.557  1.00  0.00           H
ATOM    515  HG2 GLU A  41      29.537 -15.263 -39.900  1.00  0.00           H
ATOM    516  HG3 GLU A  41      30.812 -14.544 -40.904  1.00  0.00           H
ATOM    517  N   LEU A  42      27.087 -14.411 -38.306  1.00 12.67           N
ANISOU  517  N   LEU A  42     1473   1558   1785   -102   -207   -150       N
ATOM    518  CA  LEU A  42      26.409 -15.574 -37.726  1.00 13.57           C
ANISOU  518  CA  LEU A  42     1671   1699   1787    -80   -257   -139       C
ATOM    519  C   LEU A  42      26.455 -16.816 -38.610  1.00 14.22           C
ANISOU  519  C   LEU A  42     1742   1797   1864    -69   -197   -125       C
ATOM    520  O   LEU A  42      25.935 -17.866 -38.183  1.00 13.32           O
ANISOU  520  O   LEU A  42     1690   1700   1670    -51   -231   -116       O
ATOM    521  CB  LEU A  42      24.952 -15.273 -37.412  1.00 13.02           C
ANISOU  521  CB  LEU A  42     1703   1672   1573    -88   -239   -112       C
ATOM    522  CG  LEU A  42      24.692 -14.192 -36.367  1.00 14.81           C
ANISOU  522  CG  LEU A  42     1971   1886   1771    -93   -304   -122       C
ATOM    523  CD1 LEU A  42      23.168 -14.149 -36.134  1.00 16.78           C
ANISOU  523  CD1 LEU A  42     2321   2173   1882   -100   -267    -91       C
ATOM    524  CD2 LEU A  42      25.480 -14.436 -35.068  1.00 15.12           C
ANISOU  524  CD2 LEU A  42     2026   1874   1843    -59   -441   -156       C
ATOM    525  H   LEU A  42      26.670 -13.897 -39.069  1.00  0.00           H
ATOM    526  HA  LEU A  42      26.908 -15.816 -36.788  1.00  0.00           H
ATOM    527  HB2 LEU A  42      24.471 -14.961 -38.339  1.00  0.00           H
ATOM    528  HB3 LEU A  42      24.478 -16.195 -37.075  1.00  0.00           H
ATOM    529  HG  LEU A  42      25.003 -13.233 -36.781  1.00  0.00           H
ATOM    530 HD11 LEU A  42      22.935 -13.387 -35.391  1.00  0.00           H
ATOM    531 HD12 LEU A  42      22.828 -15.121 -35.776  1.00  0.00           H
ATOM    532 HD13 LEU A  42      22.664 -13.910 -37.070  1.00  0.00           H
ATOM    533 HD21 LEU A  42      24.975 -13.942 -34.238  1.00  0.00           H
ATOM    534 HD22 LEU A  42      25.536 -15.507 -34.873  1.00  0.00           H
ATOM    535 HD23 LEU A  42      26.487 -14.032 -35.173  1.00  0.00           H
ATOM    536  N   VAL A  43      27.002 -16.682 -39.820  1.00 15.20           N
ANISOU  536  N   VAL A  43     1799   1911   2064    -77   -100   -120       N
ATOM    537  CA  VAL A  43      27.099 -17.814 -40.739  1.00 15.93           C
ANISOU  537  CA  VAL A  43     1887   2014   2153    -61    -39   -107       C
ATOM    538  C   VAL A  43      28.538 -18.265 -40.891  1.00 15.34           C
ANISOU  538  C   VAL A  43     1714   1885   2229    -51    -47   -132       C
ATOM    539  O   VAL A  43      29.400 -17.505 -41.317  1.00 15.17           O
ANISOU  539  O   VAL A  43     1612   1819   2333    -62      4   -144       O
ATOM    540  CB  VAL A  43      26.499 -17.525 -42.117  1.00 16.44           C
ANISOU  540  CB  VAL A  43     1981   2100   2166    -64     86    -80       C
ATOM    541  CG1 VAL A  43      26.629 -18.754 -43.030  1.00 16.13           C
ANISOU  541  CG1 VAL A  43     1946   2064   2117    -39    137    -71       C
ATOM    542  CG2 VAL A  43      25.039 -17.112 -42.005  1.00 16.63           C
ANISOU  542  CG2 VAL A  43     2092   2169   2056    -72     85    -63       C
ATOM    543  H   VAL A  43      27.356 -15.780 -40.106  1.00  0.00           H
ATOM    544  HA  VAL A  43      26.539 -18.641 -40.303  1.00  0.00           H
ATOM    545  HB  VAL A  43      27.055 -16.703 -42.568  1.00  0.00           H
ATOM    546 HG11 VAL A  43      27.677 -19.043 -43.104  1.00  0.00           H
ATOM    547 HG12 VAL A  43      26.248 -18.511 -44.022  1.00  0.00           H
ATOM    548 HG13 VAL A  43      26.054 -19.580 -42.612  1.00  0.00           H
ATOM    549 HG21 VAL A  43      24.956 -16.240 -41.356  1.00  0.00           H
ATOM    550 HG22 VAL A  43      24.460 -17.934 -41.584  1.00  0.00           H
ATOM    551 HG23 VAL A  43      24.654 -16.866 -42.995  1.00  0.00           H
ATOM    552  N   GLN A  44      28.807 -19.500 -40.484  1.00 13.66           N
ANISOU  552  N   GLN A  44     1505   1670   2015    -29   -110   -142       N
ATOM    553  CA  GLN A  44      30.114 -20.085 -40.731  1.00 14.39           C
ANISOU  553  CA  GLN A  44     1503   1712   2252    -17   -113   -167       C
ATOM    554  C   GLN A  44      30.215 -20.476 -42.178  1.00 14.71           C
ANISOU  554  C   GLN A  44     1530   1756   2304    -13     26   -142       C
ATOM    555  O   GLN A  44      29.464 -21.359 -42.648  1.00 15.15           O
ANISOU  555  O   GLN A  44     1653   1853   2248      1     54   -119       O
ATOM    556  CB  GLN A  44      30.312 -21.336 -39.860  1.00 14.89           C
ANISOU  556  CB  GLN A  44     1588   1771   2297     11   -226   -184       C
ATOM    557  CG  GLN A  44      31.742 -21.946 -39.967  1.00 17.22           C
ANISOU  557  CG  GLN A  44     1777   2006   2761     26   -253   -219       C
ATOM    558  CD  GLN A  44      32.809 -21.003 -39.391  1.00 19.00           C
ANISOU  558  CD  GLN A  44     1904   2159   3156     22   -322   -266       C
ATOM    559  OE1 GLN A  44      32.567 -20.305 -38.404  1.00 20.00           O
ANISOU  559  OE1 GLN A  44     2066   2280   3252     23   -420   -284       O
ATOM    560  NE2 GLN A  44      33.970 -20.999 -39.999  1.00 18.85           N
ANISOU  560  NE2 GLN A  44     1763   2077   3321     19   -271   -290       N
ATOM    561  H   GLN A  44      28.100 -20.035 -40.001  1.00  0.00           H
ATOM    562  HA  GLN A  44      30.888 -19.354 -40.498  1.00  0.00           H
ATOM    563  HB2 GLN A  44      30.129 -21.065 -38.820  1.00  0.00           H
ATOM    564  HB3 GLN A  44      29.585 -22.091 -40.159  1.00  0.00           H
ATOM    565  HG2 GLN A  44      31.967 -22.134 -41.017  1.00  0.00           H
ATOM    566  HG3 GLN A  44      31.769 -22.890 -39.422  1.00  0.00           H
ATOM    567 HE21 GLN A  44      34.713 -20.403 -39.664  1.00  0.00           H
ATOM    568 HE22 GLN A  44      34.121 -21.592 -40.802  1.00  0.00           H
ATOM    569  N   SER A  45      31.151 -19.876 -42.895  1.00 15.37           N
ANISOU  569  N   SER A  45     1529   1785   2526    -20    116   -149       N
ATOM    570  CA  SER A  45      31.234 -20.096 -44.329  1.00 19.51           C
ANISOU  570  CA  SER A  45     2064   2301   3049     -8    267   -121       C
ATOM    571  C   SER A  45      32.558 -20.699 -44.787  1.00 23.08           C
ANISOU  571  C   SER A  45     2419   2686   3666      5    319   -137       C
ATOM    572  O   SER A  45      32.760 -20.935 -45.960  1.00 24.56           O
ANISOU  572  O   SER A  45     2620   2853   3861     22    453   -114       O
ATOM    573  CB  SER A  45      30.957 -18.788 -45.100  1.00 23.11           C
ANISOU  573  CB  SER A  45     2543   2745   3494    -19    385   -100       C
ATOM    574  OG  SER A  45      31.889 -17.780 -44.731  1.00 26.37           O
ANISOU  574  OG  SER A  45     2853   3093   4072    -41    389   -124       O
ATOM    575  H   SER A  45      31.812 -19.261 -42.443  1.00  0.00           H
ATOM    576  HA  SER A  45      30.447 -20.802 -44.595  1.00  0.00           H
ATOM    577  HB2 SER A  45      31.041 -18.979 -46.170  1.00  0.00           H
ATOM    578  HB3 SER A  45      29.947 -18.444 -44.874  1.00  0.00           H
ATOM    579  HG  SER A  45      31.460 -17.142 -44.156  1.00  0.00           H
ATOM    580  N   SER A  46      33.458 -20.947 -43.869  1.00 26.08           N
ANISOU  580  N   SER A  46     2707   3024   4178      2    213   -179       N
ATOM    581  CA  SER A  46      34.741 -21.537 -44.234  1.00 28.38           C
ANISOU  581  CA  SER A  46     2892   3244   4649     14    253   -201       C
ATOM    582  C   SER A  46      35.051 -22.773 -43.409  1.00 28.10           C
ANISOU  582  C   SER A  46     2840   3214   4622     33    112   -230       C
ATOM    583  O   SER A  46      34.534 -22.953 -42.296  1.00 25.48           O
ANISOU  583  O   SER A  46     2561   2920   4200     37    -34   -243       O
ATOM    584  CB  SER A  46      35.864 -20.503 -44.060  1.00 30.48           C
ANISOU  584  CB  SER A  46     3022   3416   5143     -4    272   -238       C
ATOM    585  OG  SER A  46      35.959 -20.077 -42.710  1.00 32.40           O
ANISOU  585  OG  SER A  46     3235   3652   5422    -12     97   -282       O
ATOM    586  H   SER A  46      33.263 -20.728 -42.902  1.00  0.00           H
ATOM    587  HA  SER A  46      34.700 -21.826 -45.284  1.00  0.00           H
ATOM    588  HB2 SER A  46      36.811 -20.952 -44.359  1.00  0.00           H
ATOM    589  HB3 SER A  46      35.659 -19.641 -44.695  1.00  0.00           H
ATOM    590  HG  SER A  46      36.666 -19.433 -42.626  1.00  0.00           H
ATOM    591  N   SER A  47      35.912 -23.618 -43.988  1.00 29.48           N
ANISOU  591  N   SER A  47     2951   3346   4906     48    167   -237       N
ATOM    592  CA  SER A  47      36.484 -24.774 -43.326  1.00 28.46           C
ANISOU  592  CA  SER A  47     2784   3202   4829     69     46   -271       C
ATOM    593  C   SER A  47      37.989 -24.813 -43.638  1.00 27.49           C
ANISOU  593  C   SER A  47     2505   2973   4966     71     91   -309       C
ATOM    594  O   SER A  47      38.406 -24.338 -44.698  1.00 25.62           O
ANISOU  594  O   SER A  47     2222   2689   4823     63    264   -290       O
ATOM    595  CB  SER A  47      35.851 -26.064 -43.861  1.00 28.31           C
ANISOU  595  CB  SER A  47     2854   3243   4659     89     79   -236       C
ATOM    596  OG  SER A  47      36.532 -27.219 -43.331  1.00 27.87           O
ANISOU  596  OG  SER A  47     2754   3164   4670    111    -21   -267       O
ATOM    597  H   SER A  47      36.180 -23.439 -44.945  1.00  0.00           H
ATOM    598  HA  SER A  47      36.329 -24.702 -42.250  1.00  0.00           H
ATOM    599  HB2 SER A  47      34.803 -26.099 -43.564  1.00  0.00           H
ATOM    600  HB3 SER A  47      35.918 -26.074 -44.949  1.00  0.00           H
ATOM    601  HG  SER A  47      36.501 -27.197 -42.372  1.00  0.00           H
ATOM    602  N   THR A  48      38.784 -25.395 -42.738  1.00 30.10           N
ANISOU  602  N   THR A  48     2762   3259   5415     87    -59   -364       N
ATOM    603  CA  THR A  48      40.189 -25.695 -43.024  1.00 33.71           C
ANISOU  603  CA  THR A  48     3067   3614   6129     94    -29   -406       C
ATOM    604  C   THR A  48      40.338 -26.690 -44.160  1.00 31.90           C
ANISOU  604  C   THR A  48     2848   3389   5883    106    117   -370       C
ATOM    605  O   THR A  48      41.385 -26.762 -44.809  1.00 33.83           O
ANISOU  605  O   THR A  48     3026   3547   6281     96    216   -378       O
ATOM    606  CB  THR A  48      40.891 -26.368 -41.835  1.00 39.62           C
ANISOU  606  CB  THR A  48     3776   4320   6959    118   -240   -472       C
ATOM    607  OG1 THR A  48      40.263 -27.627 -41.541  1.00 42.12           O
ANISOU  607  OG1 THR A  48     4189   4712   7105    146   -316   -453       O
ATOM    608  CG2 THR A  48      40.864 -25.486 -40.604  1.00 41.58           C
ANISOU  608  CG2 THR A  48     4040   4547   7213    118   -407   -516       C
ATOM    609  H   THR A  48      38.406 -25.636 -41.833  1.00  0.00           H
ATOM    610  HA  THR A  48      40.712 -24.773 -43.279  1.00  0.00           H
ATOM    611  HB  THR A  48      41.930 -26.554 -42.106  1.00  0.00           H
ATOM    612  HG1 THR A  48      40.796 -28.109 -40.904  1.00  0.00           H
ATOM    613 HG21 THR A  48      41.369 -25.993 -39.782  1.00  0.00           H
ATOM    614 HG22 THR A  48      41.373 -24.547 -40.819  1.00  0.00           H
ATOM    615 HG23 THR A  48      39.830 -25.283 -40.325  1.00  0.00           H
ATOM    616  N   GLY A  49      39.320 -27.518 -44.363  1.00 27.80           N
ANISOU  616  N   GLY A  49     2464   2965   5132    119    116   -326       N
ATOM    617  CA  GLY A  49      39.397 -28.531 -45.389  1.00 25.91           C
ANISOU  617  CA  GLY A  49     2250   2733   4860    137    233   -295       C
ATOM    618  C   GLY A  49      39.878 -29.856 -44.838  1.00 25.64           C
ANISOU  618  C   GLY A  49     2187   2695   4860    161    112   -325       C
ATOM    619  O   GLY A  49      40.110 -30.789 -45.591  1.00 26.54           O
ANISOU  619  O   GLY A  49     2304   2805   4974    178    193   -308       O
ATOM    620  H   GLY A  49      38.487 -27.439 -43.797  1.00  0.00           H
ATOM    621  HA2 GLY A  49      38.407 -28.669 -45.823  1.00  0.00           H
ATOM    622  HA3 GLY A  49      40.084 -28.198 -46.167  1.00  0.00           H
ATOM    623  N   LYS A  50      40.027 -29.953 -43.531  1.00 25.63           N
ANISOU  623  N   LYS A  50     2169   2689   4881    167    -82   -371       N
ATOM    624  CA  LYS A  50      40.462 -31.211 -42.932  1.00 28.35           C
ANISOU  624  CA  LYS A  50     2501   3024   5246    196   -210   -403       C
ATOM    625  C   LYS A  50      39.490 -31.645 -41.865  1.00 24.81           C
ANISOU  625  C   LYS A  50     2185   2649   4593    212   -363   -396       C
ATOM    626  O   LYS A  50      38.978 -30.829 -41.119  1.00 24.44           O
ANISOU  626  O   LYS A  50     2186   2619   4481    205   -437   -402       O
ATOM    627  CB  LYS A  50      41.849 -31.047 -42.319  1.00 34.51           C
ANISOU  627  CB  LYS A  50     3154   3696   6264    198   -309   -475       C
ATOM    628  CG  LYS A  50      42.889 -30.718 -43.382  1.00 41.93           C
ANISOU  628  CG  LYS A  50     4010   4548   7375    166   -138   -472       C
ATOM    629  CD  LYS A  50      44.032 -29.922 -42.841  1.00 50.72           C
ANISOU  629  CD  LYS A  50     5044   5543   8684    142   -201   -532       C
ATOM    630  CE  LYS A  50      45.120 -29.769 -43.891  1.00 56.34           C
ANISOU  630  CE  LYS A  50     5679   6153   9576    112    -32   -529       C
ATOM    631  NZ  LYS A  50      45.639 -31.068 -44.373  1.00 57.72           N
ANISOU  631  NZ  LYS A  50     5840   6315   9775    123      2   -525       N
ATOM    632  H   LYS A  50      39.839 -29.154 -42.943  1.00  0.00           H
ATOM    633  HA  LYS A  50      40.504 -31.977 -43.706  1.00  0.00           H
ATOM    634  HB2 LYS A  50      42.130 -31.976 -41.823  1.00  0.00           H
ATOM    635  HB3 LYS A  50      41.822 -30.243 -41.584  1.00  0.00           H
ATOM    636  HG2 LYS A  50      43.276 -31.651 -43.792  1.00  0.00           H
ATOM    637  HG3 LYS A  50      42.411 -30.152 -44.182  1.00  0.00           H
ATOM    638  HD2 LYS A  50      44.444 -30.432 -41.970  1.00  0.00           H
ATOM    639  HD3 LYS A  50      43.676 -28.935 -42.545  1.00  0.00           H
ATOM    640  HE2 LYS A  50      44.710 -29.221 -44.740  1.00  0.00           H
ATOM    641  HE3 LYS A  50      45.944 -29.196 -43.465  1.00  0.00           H
ATOM    642  HZ1 LYS A  50      45.266 -31.259 -45.292  1.00  0.00           H
ATOM    643  HZ2 LYS A  50      45.358 -31.800 -43.736  1.00  0.00           H
ATOM    644  HZ3 LYS A  50      46.647 -31.031 -44.420  1.00  0.00           H
ATOM    645  N   ILE A  51      39.251 -32.944 -41.804  1.00 20.27           N
ANISOU  645  N   ILE A  51     1670   2110   3923    236   -399   -384       N
ATOM    646  CA  ILE A  51      38.455 -33.535 -40.752  1.00 20.74           C
ANISOU  646  CA  ILE A  51     1852   2219   3810    257   -535   -380       C
ATOM    647  C   ILE A  51      39.317 -33.787 -39.527  1.00 24.07           C
ANISOU  647  C   ILE A  51     2240   2573   4334    293   -727   -446       C
ATOM    648  O   ILE A  51      40.339 -34.495 -39.615  1.00 26.12           O
ANISOU  648  O   ILE A  51     2410   2776   4740    313   -764   -484       O
ATOM    649  CB  ILE A  51      37.879 -34.870 -41.235  1.00 20.47           C
ANISOU  649  CB  ILE A  51     1893   2240   3646    270   -487   -342       C
ATOM    650  CG1 ILE A  51      36.891 -34.617 -42.381  1.00 20.50           C
ANISOU  650  CG1 ILE A  51     1953   2307   3530    247   -325   -284       C
ATOM    651  CG2 ILE A  51      37.192 -35.627 -40.092  1.00 19.51           C
ANISOU  651  CG2 ILE A  51     1892   2149   3371    298   -619   -340       C
ATOM    652  CD1 ILE A  51      36.408 -35.934 -43.066  1.00 25.25           C
ANISOU  652  CD1 ILE A  51     2612   2953   4031    262   -269   -252       C
ATOM    653  H   ILE A  51      39.638 -33.545 -42.518  1.00  0.00           H
ATOM    654  HA  ILE A  51      37.640 -32.861 -40.490  1.00  0.00           H
ATOM    655  HB  ILE A  51      38.697 -35.483 -41.613  1.00  0.00           H
ATOM    656 HG12 ILE A  51      36.022 -34.093 -41.982  1.00  0.00           H
ATOM    657 HG13 ILE A  51      37.371 -33.986 -43.129  1.00  0.00           H
ATOM    658 HG21 ILE A  51      37.907 -35.798 -39.287  1.00  0.00           H
ATOM    659 HG22 ILE A  51      36.357 -35.036 -39.716  1.00  0.00           H
ATOM    660 HG23 ILE A  51      36.823 -36.584 -40.460  1.00  0.00           H
ATOM    661 HD11 ILE A  51      35.711 -35.692 -43.869  1.00  0.00           H
ATOM    662 HD12 ILE A  51      35.909 -36.564 -42.330  1.00  0.00           H
ATOM    663 HD13 ILE A  51      37.266 -36.465 -43.477  1.00  0.00           H
ATOM    664  N   CYS A  52      38.925 -33.194 -38.398  1.00 24.75           N
ANISOU  664  N   CYS A  52     2401   2657   4348    306   -853   -463       N
ATOM    665  CA  CYS A  52      39.622 -33.399 -37.122  1.00 23.88           C
ANISOU  665  CA  CYS A  52     2301   2477   4296    353  -1055   -528       C
ATOM    666  C   CYS A  52      39.333 -34.754 -36.496  1.00 21.88           C
ANISOU  666  C   CYS A  52     2167   2240   3904    395  -1135   -520       C
ATOM    667  O   CYS A  52      38.165 -35.130 -36.387  1.00 21.29           O
ANISOU  667  O   CYS A  52     2218   2236   3635    398  -1101   -467       O
ATOM    668  CB  CYS A  52      39.199 -32.329 -36.141  1.00 24.68           C
ANISOU  668  CB  CYS A  52     2484   2568   4325    358  -1141   -540       C
ATOM    669  SG  CYS A  52      39.696 -30.648 -36.683  1.00 30.33           S
ANISOU  669  SG  CYS A  52     3062   3242   5219    310  -1064   -560       S
ATOM    670  H   CYS A  52      38.121 -32.583 -38.422  1.00  0.00           H
ATOM    671  HA  CYS A  52      40.695 -33.314 -37.292  1.00  0.00           H
ATOM    672  HB2 CYS A  52      38.114 -32.357 -36.038  1.00  0.00           H
ATOM    673  HB3 CYS A  52      39.652 -32.537 -35.172  1.00  0.00           H
ATOM    674  N   ASN A  53      40.388 -35.447 -36.028  1.00 23.26           N
ANISOU  674  N   ASN A  53     2333   2342   4164    416  -1217   -570       N
ATOM    675  CA  ASN A  53      40.252 -36.789 -35.470  1.00 26.24           C
ANISOU  675  CA  ASN A  53     2817   2725   4427    456  -1283   -567       C
ATOM    676  C   ASN A  53      39.822 -36.845 -34.013  1.00 26.96           C
ANISOU  676  C   ASN A  53     3088   2792   4364    501  -1405   -579       C
ATOM    677  O   ASN A  53      39.712 -37.925 -33.437  1.00 27.55           O
ANISOU  677  O   ASN A  53     3268   2858   4340    538  -1454   -577       O
ATOM    678  CB  ASN A  53      41.555 -37.605 -35.683  1.00 35.57           C
ANISOU  678  CB  ASN A  53     3911   3838   5766    460  -1308   -616       C
ATOM    679  CG  ASN A  53      42.768 -37.095 -34.870  1.00 39.67           C
ANISOU  679  CG  ASN A  53     4402   4239   6433    473  -1427   -700       C
ATOM    680  OD1 ASN A  53      43.836 -37.700 -34.943  1.00 46.39           O
ANISOU  680  OD1 ASN A  53     5187   5022   7417    477  -1461   -747       O
ATOM    681  ND2 ASN A  53      42.626 -36.021 -34.127  1.00 37.39           N
ANISOU  681  ND2 ASN A  53     4159   3918   6128    481  -1492   -722       N
ATOM    682  H   ASN A  53      41.305 -35.024 -36.064  1.00  0.00           H
ATOM    683  HA  ASN A  53      39.473 -37.289 -36.045  1.00  0.00           H
ATOM    684  HB2 ASN A  53      41.813 -37.565 -36.741  1.00  0.00           H
ATOM    685  HB3 ASN A  53      41.364 -38.643 -35.410  1.00  0.00           H
ATOM    686 HD21 ASN A  53      43.407 -35.671 -33.591  1.00  0.00           H
ATOM    687 HD22 ASN A  53      41.736 -35.546 -34.092  1.00  0.00           H
ATOM    688  N   ASN A  54      39.580 -35.683 -33.414  1.00 25.44           N
ANISOU  688  N   ASN A  54     2936   2580   4149    501  -1442   -590       N
ATOM    689  CA  ASN A  54      39.002 -35.621 -32.086  1.00 26.20           C
ANISOU  689  CA  ASN A  54     3219   2655   4083    546  -1525   -591       C
ATOM    690  C   ASN A  54      37.907 -34.583 -32.075  1.00 26.54           C
ANISOU  690  C   ASN A  54     3311   2754   4021    524  -1470   -545       C
ATOM    691  O   ASN A  54      37.967 -33.614 -32.841  1.00 27.19           O
ANISOU  691  O   ASN A  54     3271   2859   4200    480  -1413   -542       O
ATOM    692  CB  ASN A  54      40.043 -35.229 -31.049  1.00 30.63           C
ANISOU  692  CB  ASN A  54     3804   3099   4735    585  -1661   -671       C
ATOM    693  CG  ASN A  54      40.819 -36.417 -30.543  1.00 38.39           C
ANISOU  693  CG  ASN A  54     4828   4016   5740    629  -1747   -716       C
ATOM    694  OD1 ASN A  54      42.043 -36.436 -30.643  1.00 45.05           O
ANISOU  694  OD1 ASN A  54     5568   4782   6766    630  -1808   -782       O
ATOM    695  ND2 ASN A  54      40.114 -37.430 -30.014  1.00 38.43           N
ANISOU  695  ND2 ASN A  54     4986   4048   5569    665  -1747   -682       N
ATOM    696  H   ASN A  54      39.804 -34.824 -33.895  1.00  0.00           H
ATOM    697  HA  ASN A  54      38.582 -36.593 -31.828  1.00  0.00           H
ATOM    698  HB2 ASN A  54      40.739 -34.522 -31.501  1.00  0.00           H
ATOM    699  HB3 ASN A  54      39.543 -34.747 -30.209  1.00  0.00           H
ATOM    700 HD21 ASN A  54      40.591 -38.251 -29.669  1.00  0.00           H
ATOM    701 HD22 ASN A  54      39.107 -37.371 -29.961  1.00  0.00           H
ATOM    702  N   PRO A  55      36.905 -34.763 -31.212  1.00 27.59           N
ANISOU  702  N   PRO A  55     3622   2901   3960    553  -1475   -511       N
ATOM    703  CA  PRO A  55      36.768 -35.797 -30.193  1.00 28.56           C
ANISOU  703  CA  PRO A  55     3905   2982   3962    609  -1526   -514       C
ATOM    704  C   PRO A  55      36.098 -37.077 -30.712  1.00 26.43           C
ANISOU  704  C   PRO A  55     3669   2775   3600    605  -1445   -460       C
ATOM    705  O   PRO A  55      36.005 -38.046 -29.968  1.00 29.05           O
ANISOU  705  O   PRO A  55     4124   3072   3841    648  -1473   -461       O
ATOM    706  CB  PRO A  55      35.849 -35.130 -29.172  1.00 30.32           C
ANISOU  706  CB  PRO A  55     4292   3193   4035    633  -1524   -491       C
ATOM    707  CG  PRO A  55      34.880 -34.308 -30.060  1.00 29.07           C
ANISOU  707  CG  PRO A  55     4073   3126   3845    573  -1414   -435       C
ATOM    708  CD  PRO A  55      35.732 -33.852 -31.241  1.00 28.08           C
ANISOU  708  CD  PRO A  55     3738   3020   3909    528  -1407   -461       C
ATOM    709  HA  PRO A  55      37.736 -36.025 -29.746  1.00  0.00           H
ATOM    710  HB2 PRO A  55      36.413 -34.481 -28.503  1.00  0.00           H
ATOM    711  HB3 PRO A  55      35.301 -35.881 -28.603  1.00  0.00           H
ATOM    712  HG2 PRO A  55      34.491 -33.450 -29.512  1.00  0.00           H
ATOM    713  HG3 PRO A  55      34.060 -34.937 -30.407  1.00  0.00           H
ATOM    714  HD2 PRO A  55      35.184 -33.957 -32.177  1.00  0.00           H
ATOM    715  HD3 PRO A  55      36.051 -32.819 -31.102  1.00  0.00           H
ATOM    716  N   HIS A  56      35.610 -37.072 -31.943  1.00 20.90           N
ANISOU  716  N   HIS A  56     2866   2156   2918    558  -1347   -417       N
ATOM    717  CA  HIS A  56      34.855 -38.218 -32.454  1.00 19.75           C
ANISOU  717  CA  HIS A  56     2757   2065   2681    557  -1269   -365       C
ATOM    718  C   HIS A  56      35.812 -39.295 -32.947  1.00 21.02           C
ANISOU  718  C   HIS A  56     2829   2210   2946    567  -1293   -391       C
ATOM    719  O   HIS A  56      36.857 -38.989 -33.512  1.00 23.14           O
ANISOU  719  O   HIS A  56     2952   2458   3384    549  -1315   -432       O
ATOM    720  CB  HIS A  56      33.979 -37.779 -33.619  1.00 19.29           C
ANISOU  720  CB  HIS A  56     2631   2090   2608    500  -1133   -315       C
ATOM    721  CG  HIS A  56      33.002 -36.710 -33.255  1.00 20.67           C
ANISOU  721  CG  HIS A  56     2881   2285   2688    481  -1091   -288       C
ATOM    722  ND1 HIS A  56      32.035 -36.890 -32.286  1.00 21.83           N
ANISOU  722  ND1 HIS A  56     3199   2419   2676    512  -1092   -258       N
ATOM    723  CD2 HIS A  56      32.842 -35.445 -33.730  1.00 21.60           C
ANISOU  723  CD2 HIS A  56     2929   2430   2850    435  -1039   -286       C
ATOM    724  CE1 HIS A  56      31.320 -35.777 -32.183  1.00 23.90           C
ANISOU  724  CE1 HIS A  56     3487   2701   2892    484  -1045   -239       C
ATOM    725  NE2 HIS A  56      31.803 -34.880 -33.035  1.00 22.54           N
ANISOU  725  NE2 HIS A  56     3171   2556   2839    437  -1020   -257       N
ATOM    726  H   HIS A  56      35.760 -36.269 -32.536  1.00  0.00           H
ATOM    727  HA  HIS A  56      34.228 -38.624 -31.660  1.00  0.00           H
ATOM    728  HB2 HIS A  56      34.623 -37.402 -34.413  1.00  0.00           H
ATOM    729  HB3 HIS A  56      33.431 -38.644 -33.992  1.00  0.00           H
ATOM    730  HD2 HIS A  56      33.424 -34.974 -34.508  1.00  0.00           H
ATOM    731  HE1 HIS A  56      30.484 -35.626 -31.517  1.00  0.00           H
ATOM    732  HE2 HIS A  56      31.461 -33.937 -33.152  1.00  0.00           H
ATOM    733  HD1 HIS A  56      31.895 -37.731 -31.744  1.00  0.00           H
ATOM    734  N   ARG A  57      35.444 -40.552 -32.787  1.00 20.08           N
ANISOU  734  N   ARG A  57     2794   2098   2737    591  -1274   -367       N
ATOM    735  CA  ARG A  57      36.286 -41.610 -33.320  1.00 20.57           C
ANISOU  735  CA  ARG A  57     2773   2152   2893    597  -1288   -388       C
ATOM    736  C   ARG A  57      36.049 -41.749 -34.821  1.00 20.25           C
ANISOU  736  C   ARG A  57     2599   2180   2913    558  -1179   -354       C
ATOM    737  O   ARG A  57      34.972 -42.166 -35.257  1.00 19.93           O
ANISOU  737  O   ARG A  57     2612   2196   2766    532  -1062   -300       O
ATOM    738  CB  ARG A  57      36.005 -42.918 -32.606  1.00 21.37           C
ANISOU  738  CB  ARG A  57     3011   2230   2879    638  -1303   -375       C
ATOM    739  CG  ARG A  57      36.794 -44.136 -33.161  1.00 28.43           C
ANISOU  739  CG  ARG A  57     3828   3120   3855    645  -1314   -393       C
ATOM    740  CD  ARG A  57      36.272 -45.443 -32.508  1.00 38.06           C
ANISOU  740  CD  ARG A  57     5194   4326   4941    683  -1308   -369       C
ATOM    741  NE  ARG A  57      36.714 -45.536 -31.123  1.00 43.81           N
ANISOU  741  NE  ARG A  57     6052   4971   5622    731  -1407   -413       N
ATOM    742  CZ  ARG A  57      37.864 -46.086 -30.751  1.00 49.77           C
ANISOU  742  CZ  ARG A  57     6791   5665   6454    758  -1505   -474       C
ATOM    743  NH1 ARG A  57      38.686 -46.612 -31.663  1.00 50.84           N
ANISOU  743  NH1 ARG A  57     6780   5815   6721    737  -1505   -492       N
ATOM    744  NH2 ARG A  57      38.191 -46.114 -29.462  1.00 52.91           N
ANISOU  744  NH2 ARG A  57     7323   5979   6799    811  -1600   -519       N
ATOM    745  H   ARG A  57      34.588 -40.776 -32.300  1.00  0.00           H
ATOM    746  HA  ARG A  57      37.329 -41.341 -33.156  1.00  0.00           H
ATOM    747  HB2 ARG A  57      34.940 -43.133 -32.695  1.00  0.00           H
ATOM    748  HB3 ARG A  57      36.248 -42.797 -31.550  1.00  0.00           H
ATOM    749  HG2 ARG A  57      36.659 -44.193 -34.241  1.00  0.00           H
ATOM    750  HG3 ARG A  57      37.853 -44.015 -32.934  1.00  0.00           H
ATOM    751  HD2 ARG A  57      36.655 -46.299 -33.064  1.00  0.00           H
ATOM    752  HD3 ARG A  57      35.182 -45.451 -32.540  1.00  0.00           H
ATOM    753  HE  ARG A  57      36.111 -45.161 -30.405  1.00  0.00           H
ATOM    754 HH11 ARG A  57      39.559 -47.031 -31.375  1.00  0.00           H
ATOM    755 HH12 ARG A  57      38.435 -46.591 -32.641  1.00  0.00           H
ATOM    756 HH21 ARG A  57      39.063 -46.532 -29.171  1.00  0.00           H
ATOM    757 HH22 ARG A  57      37.567 -45.717 -28.774  1.00  0.00           H
ATOM    758  N   ILE A  58      37.070 -41.406 -35.605  1.00 20.72           N
ANISOU  758  N   ILE A  58     2498   2227   3149    535  -1172   -388       N
ATOM    759  CA  ILE A  58      36.946 -41.420 -37.050  1.00 22.51           C
ANISOU  759  CA  ILE A  58     2620   2506   3426    482  -1014   -358       C
ATOM    760  C   ILE A  58      37.580 -42.693 -37.577  1.00 22.75           C
ANISOU  760  C   ILE A  58     2596   2528   3519    497  -1006   -366       C
ATOM    761  O   ILE A  58      38.667 -43.039 -37.156  1.00 24.63           O
ANISOU  761  O   ILE A  58     2782   2705   3870    531  -1118   -417       O
ATOM    762  CB  ILE A  58      37.709 -40.271 -37.694  1.00 26.44           C
ANISOU  762  CB  ILE A  58     2976   2983   4087    449   -978   -385       C
ATOM    763  CG1 ILE A  58      37.323 -38.931 -37.069  1.00 26.42           C
ANISOU  763  CG1 ILE A  58     3011   2975   4053    439  -1012   -389       C
ATOM    764  CG2 ILE A  58      37.459 -40.256 -39.207  1.00 27.77           C
ANISOU  764  CG2 ILE A  58     3074   3200   4276    405   -799   -346       C
ATOM    765  CD1 ILE A  58      35.867 -38.583 -37.179  1.00 23.29           C
ANISOU  765  CD1 ILE A  58     2719   2647   3484    411   -917   -331       C
ATOM    766  H   ILE A  58      37.947 -41.131 -35.185  1.00  0.00           H
ATOM    767  HA  ILE A  58      35.895 -41.379 -37.336  1.00  0.00           H
ATOM    768  HB  ILE A  58      38.774 -40.432 -37.526  1.00  0.00           H
ATOM    769 HG12 ILE A  58      37.897 -38.148 -37.564  1.00  0.00           H
ATOM    770 HG13 ILE A  58      37.597 -38.948 -36.014  1.00  0.00           H
ATOM    771 HG21 ILE A  58      38.009 -39.430 -39.659  1.00  0.00           H
ATOM    772 HG22 ILE A  58      36.393 -40.129 -39.398  1.00  0.00           H
ATOM    773 HG23 ILE A  58      37.796 -41.198 -39.640  1.00  0.00           H
ATOM    774 HD11 ILE A  58      35.687 -37.616 -36.708  1.00  0.00           H
ATOM    775 HD12 ILE A  58      35.584 -38.533 -38.230  1.00  0.00           H
ATOM    776 HD13 ILE A  58      35.272 -39.347 -36.679  1.00  0.00           H
ATOM    777  N   LEU A  59      36.901 -43.413 -38.461  1.00 20.84           N
ANISOU  777  N   LEU A  59     2369   2343   3208    477   -887   -321       N
ATOM    778  CA  LEU A  59      37.522 -44.564 -39.107  1.00 20.65           C
ANISOU  778  CA  LEU A  59     2285   2313   3250    488   -865   -328       C
ATOM    779  C   LEU A  59      37.551 -44.261 -40.595  1.00 20.73           C
ANISOU  779  C   LEU A  59     2203   2353   3318    449   -712   -306       C
ATOM    780  O   LEU A  59      36.494 -44.141 -41.235  1.00 19.76           O
ANISOU  780  O   LEU A  59     2130   2286   3090    426   -610   -264       O
ATOM    781  CB  LEU A  59      36.717 -45.823 -38.839  1.00 20.07           C
ANISOU  781  CB  LEU A  59     2322   2267   3038    509   -863   -297       C
ATOM    782  CG  LEU A  59      37.292 -47.121 -39.414  1.00 21.38           C
ANISOU  782  CG  LEU A  59     2440   2429   3256    525   -851   -302       C
ATOM    783  CD1 LEU A  59      38.716 -47.306 -38.884  1.00 25.00           C
ANISOU  783  CD1 LEU A  59     2826   2815   3858    560   -977   -362       C
ATOM    784  CD2 LEU A  59      36.403 -48.308 -39.028  1.00 19.54           C
ANISOU  784  CD2 LEU A  59     2324   2216   2884    546   -850   -271       C
ATOM    785  H   LEU A  59      35.949 -43.163 -38.688  1.00  0.00           H
ATOM    786  HA  LEU A  59      38.539 -44.691 -38.736  1.00  0.00           H
ATOM    787  HB2 LEU A  59      35.724 -45.681 -39.265  1.00  0.00           H
ATOM    788  HB3 LEU A  59      36.614 -45.941 -37.760  1.00  0.00           H
ATOM    789  HG  LEU A  59      37.326 -47.043 -40.501  1.00  0.00           H
ATOM    790 HD11 LEU A  59      39.137 -48.227 -39.286  1.00  0.00           H
ATOM    791 HD12 LEU A  59      39.331 -46.461 -39.193  1.00  0.00           H
ATOM    792 HD13 LEU A  59      38.694 -47.361 -37.796  1.00  0.00           H
ATOM    793 HD21 LEU A  59      36.821 -49.226 -39.442  1.00  0.00           H
ATOM    794 HD22 LEU A  59      35.400 -48.155 -39.425  1.00  0.00           H
ATOM    795 HD23 LEU A  59      36.355 -48.388 -37.942  1.00  0.00           H
ATOM    796  N   ASP A  60      38.748 -44.114 -41.140  1.00 21.70           N
ANISOU  796  N   ASP A  60     2200   2431   3614    448   -696   -338       N
ATOM    797  CA  ASP A  60      38.936 -43.830 -42.558  1.00 20.73           C
ANISOU  797  CA  ASP A  60     2001   2318   3557    422   -539   -319       C
ATOM    798  C   ASP A  60      38.856 -45.129 -43.333  1.00 18.69           C
ANISOU  798  C   ASP A  60     1757   2083   3262    436   -479   -298       C
ATOM    799  O   ASP A  60      39.656 -46.012 -43.139  1.00 19.16           O
ANISOU  799  O   ASP A  60     1773   2108   3400    460   -536   -324       O
ATOM    800  CB  ASP A  60      40.300 -43.205 -42.738  1.00 22.00           C
ANISOU  800  CB  ASP A  60     2020   2403   3937    418   -538   -363       C
ATOM    801  CG  ASP A  60      40.538 -42.662 -44.111  1.00 22.66           C
ANISOU  801  CG  ASP A  60     2038   2478   4095    395   -360   -341       C
ATOM    802  OD1 ASP A  60      39.832 -43.027 -45.070  1.00 23.28           O
ANISOU  802  OD1 ASP A  60     2178   2605   4063    393   -246   -297       O
ATOM    803  OD2 ASP A  60      41.437 -41.814 -44.216  1.00 23.29           O
ANISOU  803  OD2 ASP A  60     2008   2492   4349    384   -336   -371       O
ATOM    804  H   ASP A  60      39.563 -44.202 -40.551  1.00  0.00           H
ATOM    805  HA  ASP A  60      38.164 -43.143 -42.905  1.00  0.00           H
ATOM    806  HB2 ASP A  60      41.055 -43.964 -42.533  1.00  0.00           H
ATOM    807  HB3 ASP A  60      40.412 -42.395 -42.017  1.00  0.00           H
ATOM    808  N   GLY A  61      37.910 -45.228 -44.246  1.00 16.32           N
ANISOU  808  N   GLY A  61     1515   1836   2850    425   -368   -255       N
ATOM    809  CA  GLY A  61      37.692 -46.445 -44.992  1.00 17.26           C
ANISOU  809  CA  GLY A  61     1660   1977   2919    442   -317   -236       C
ATOM    810  C   GLY A  61      38.760 -46.699 -46.028  1.00 19.73           C
ANISOU  810  C   GLY A  61     1883   2249   3364    451   -227   -245       C
ATOM    811  O   GLY A  61      38.906 -47.824 -46.493  1.00 21.46           O
ANISOU  811  O   GLY A  61     2108   2471   3575    472   -209   -241       O
ATOM    812  H   GLY A  61      37.320 -44.429 -44.429  1.00  0.00           H
ATOM    813  HA2 GLY A  61      36.728 -46.376 -45.496  1.00  0.00           H
ATOM    814  HA3 GLY A  61      37.667 -47.285 -44.298  1.00  0.00           H
ATOM    815  N   ILE A  62      39.520 -45.657 -46.377  1.00 21.10           N
ANISOU  815  N   ILE A  62     1974   2376   3668    437   -165   -259       N
ATOM    816  CA  ILE A  62      40.560 -45.775 -47.392  1.00 21.92           C
ANISOU  816  CA  ILE A  62     1992   2424   3914    446    -50   -264       C
ATOM    817  C   ILE A  62      40.042 -46.424 -48.675  1.00 19.45           C
ANISOU  817  C   ILE A  62     1750   2141   3500    466     74   -226       C
ATOM    818  O   ILE A  62      39.248 -45.833 -49.351  1.00 18.82           O
ANISOU  818  O   ILE A  62     1743   2089   3320    464    156   -196       O
ATOM    819  CB  ILE A  62      41.806 -46.553 -46.896  1.00 35.21           C
ANISOU  819  CB  ILE A  62     3572   4047   5761    462   -130   -309       C
ATOM    820  CG1 ILE A  62      42.194 -46.128 -45.499  1.00 38.64           C
ANISOU  820  CG1 ILE A  62     3965   4451   6266    458   -295   -355       C
ATOM    821  CG2 ILE A  62      42.992 -46.250 -47.792  1.00 35.49           C
ANISOU  821  CG2 ILE A  62     3494   4002   5989    461      0   -321       C
ATOM    822  CD1 ILE A  62      42.598 -44.713 -45.435  1.00 41.19           C
ANISOU  822  CD1 ILE A  62     4214   4729   6706    435   -266   -373       C
ATOM    823  H   ILE A  62      39.370 -44.765 -45.927  1.00  0.00           H
ATOM    824  HA  ILE A  62      40.885 -44.766 -47.645  1.00  0.00           H
ATOM    825  HB  ILE A  62      41.600 -47.623 -46.910  1.00  0.00           H
ATOM    826 HG12 ILE A  62      41.341 -46.279 -44.838  1.00  0.00           H
ATOM    827 HG13 ILE A  62      43.022 -46.749 -45.157  1.00  0.00           H
ATOM    828 HG21 ILE A  62      42.988 -46.931 -48.643  1.00  0.00           H
ATOM    829 HG22 ILE A  62      43.916 -46.380 -47.228  1.00  0.00           H
ATOM    830 HG23 ILE A  62      42.925 -45.222 -48.148  1.00  0.00           H
ATOM    831 HD11 ILE A  62      43.588 -44.597 -45.875  1.00  0.00           H
ATOM    832 HD12 ILE A  62      42.623 -44.389 -44.394  1.00  0.00           H
ATOM    833 HD13 ILE A  62      41.881 -44.105 -45.987  1.00  0.00           H
ATOM    834  N   ASP A  63      40.524 -47.612 -49.031  1.00 18.52           N
ANISOU  834  N   ASP A  63     1615   2008   3413    491     82   -231       N
ATOM    835  CA  ASP A  63      40.096 -48.267 -50.275  1.00 20.02           C
ANISOU  835  CA  ASP A  63     1879   2217   3511    519    192   -199       C
ATOM    836  C   ASP A  63      38.789 -49.045 -50.137  1.00 19.36           C
ANISOU  836  C   ASP A  63     1907   2207   3244    528    124   -182       C
ATOM    837  O   ASP A  63      38.407 -49.744 -51.072  1.00 20.91           O
ANISOU  837  O   ASP A  63     2165   2415   3364    557    183   -164       O
ATOM    838  CB  ASP A  63      41.181 -49.241 -50.744  1.00 23.60           C
ANISOU  838  CB  ASP A  63     2266   2620   4083    543    234   -212       C
ATOM    839  CG  ASP A  63      42.434 -48.538 -51.177  1.00 29.83           C
ANISOU  839  CG  ASP A  63     2944   3319   5069    539    345   -226       C
ATOM    840  OD1 ASP A  63      42.309 -47.371 -51.623  1.00 31.51           O
ANISOU  840  OD1 ASP A  63     3169   3514   5290    528    443   -211       O
ATOM    841  OD2 ASP A  63      43.528 -49.147 -51.070  1.00 32.54           O
ANISOU  841  OD2 ASP A  63     3213   3618   5533    530    327   -248       O
ATOM    842  H   ASP A  63      41.197 -48.072 -48.435  1.00  0.00           H
ATOM    843  HA  ASP A  63      39.964 -47.502 -51.040  1.00  0.00           H
ATOM    844  HB2 ASP A  63      40.794 -49.817 -51.585  1.00  0.00           H
ATOM    845  HB3 ASP A  63      41.421 -49.923 -49.929  1.00  0.00           H
ATOM    846  N   CYS A  64      38.140 -48.974 -48.977  1.00 16.23           N
ANISOU  846  N   CYS A  64     1535   1846   2785    508      2   -188       N
ATOM    847  CA  CYS A  64      36.992 -49.811 -48.706  1.00 16.79           C
ANISOU  847  CA  CYS A  64     1694   1969   2715    516    -59   -176       C
ATOM    848  C   CYS A  64      35.718 -49.061 -48.410  1.00 16.21           C
ANISOU  848  C   CYS A  64     1693   1936   2528    497    -75   -160       C
ATOM    849  O   CYS A  64      35.712 -48.091 -47.643  1.00 16.71           O
ANISOU  849  O   CYS A  64     1742   1998   2610    472   -112   -166       O
ATOM    850  CB  CYS A  64      37.283 -50.698 -47.495  1.00 19.46           C
ANISOU  850  CB  CYS A  64     2015   2303   3074    519   -185   -195       C
ATOM    851  SG  CYS A  64      38.726 -51.778 -47.784  1.00 24.17           S
ANISOU  851  SG  CYS A  64     2524   2852   3807    544   -185   -218       S
ATOM    852  H   CYS A  64      38.455 -48.323 -48.272  1.00  0.00           H
ATOM    853  HA  CYS A  64      36.821 -50.453 -49.570  1.00  0.00           H
ATOM    854  HB2 CYS A  64      37.484 -50.063 -46.632  1.00  0.00           H
ATOM    855  HB3 CYS A  64      36.410 -51.317 -47.288  1.00  0.00           H
ATOM    856  N   THR A  65      34.621 -49.558 -48.955  1.00 15.17           N
ANISOU  856  N   THR A  65     1639   1837   2288    510    -57   -145       N
ATOM    857  CA  THR A  65      33.297 -49.153 -48.485  1.00 14.80           C
ANISOU  857  CA  THR A  65     1656   1823   2143    493    -93   -136       C
ATOM    858  C   THR A  65      32.960 -49.915 -47.205  1.00 14.75           C
ANISOU  858  C   THR A  65     1667   1824   2113    486   -189   -140       C
ATOM    859  O   THR A  65      33.561 -50.940 -46.898  1.00 14.64           O
ANISOU  859  O   THR A  65     1632   1796   2134    501   -229   -148       O
ATOM    860  CB  THR A  65      32.224 -49.527 -49.510  1.00 16.36           C
ANISOU  860  CB  THR A  65     1924   2039   2255    516    -54   -129       C
ATOM    861  OG1 THR A  65      32.238 -50.958 -49.714  1.00 16.69           O
ANISOU  861  OG1 THR A  65     1972   2078   2290    541    -77   -134       O
ATOM    862  CG2 THR A  65      32.458 -48.807 -50.811  1.00 18.90           C
ANISOU  862  CG2 THR A  65     2263   2345   2574    537     44   -124       C
ATOM    863  H   THR A  65      34.699 -50.227 -49.707  1.00  0.00           H
ATOM    864  HA  THR A  65      33.278 -48.079 -48.298  1.00  0.00           H
ATOM    865  HB  THR A  65      31.249 -49.238 -49.119  1.00  0.00           H
ATOM    866  HG1 THR A  65      31.606 -51.190 -50.399  1.00  0.00           H
ATOM    867 HG21 THR A  65      31.684 -49.087 -51.526  1.00  0.00           H
ATOM    868 HG22 THR A  65      32.424 -47.731 -50.642  1.00  0.00           H
ATOM    869 HG23 THR A  65      33.436 -49.082 -51.207  1.00  0.00           H
ATOM    870  N   LEU A  66      31.979 -49.426 -46.471  1.00 14.85           N
ANISOU  870  N   LEU A  66     1727   1852   2064    467   -219   -132       N
ATOM    871  CA  LEU A  66      31.551 -50.088 -45.258  1.00 14.53           C
ANISOU  871  CA  LEU A  66     1727   1807   1989    466   -289   -129       C
ATOM    872  C   LEU A  66      30.978 -51.460 -45.555  1.00 13.47           C
ANISOU  872  C   LEU A  66     1621   1674   1824    485   -287   -126       C
ATOM    873  O   LEU A  66      31.234 -52.397 -44.815  1.00 13.90           O
ANISOU  873  O   LEU A  66     1688   1712   1882    498   -335   -127       O
ATOM    874  CB  LEU A  66      30.540 -49.213 -44.515  1.00 14.99           C
ANISOU  874  CB  LEU A  66     1835   1871   1989    443   -297   -118       C
ATOM    875  CG  LEU A  66      29.958 -49.882 -43.265  1.00 15.62           C
ANISOU  875  CG  LEU A  66     1979   1932   2022    448   -344   -109       C
ATOM    876  CD1 LEU A  66      31.049 -50.225 -42.241  1.00 16.10           C
ANISOU  876  CD1 LEU A  66     2042   1964   2113    468   -423   -121       C
ATOM    877  CD2 LEU A  66      28.865 -48.933 -42.689  1.00 14.62           C
ANISOU  877  CD2 LEU A  66     1904   1808   1842    426   -327    -96       C
ATOM    878  H   LEU A  66      31.519 -48.575 -46.761  1.00  0.00           H
ATOM    879  HA  LEU A  66      32.423 -50.217 -44.617  1.00  0.00           H
ATOM    880  HB2 LEU A  66      31.037 -48.291 -44.213  1.00  0.00           H
ATOM    881  HB3 LEU A  66      29.724 -48.966 -45.194  1.00  0.00           H
ATOM    882  HG  LEU A  66      29.475 -50.810 -43.570  1.00  0.00           H
ATOM    883 HD11 LEU A  66      30.595 -50.698 -41.370  1.00  0.00           H
ATOM    884 HD12 LEU A  66      31.768 -50.909 -42.692  1.00  0.00           H
ATOM    885 HD13 LEU A  66      31.559 -49.312 -41.934  1.00  0.00           H
ATOM    886 HD21 LEU A  66      28.429 -49.380 -41.796  1.00  0.00           H
ATOM    887 HD22 LEU A  66      28.086 -48.781 -43.436  1.00  0.00           H
ATOM    888 HD23 LEU A  66      29.315 -47.974 -42.432  1.00  0.00           H
ATOM    889  N   ILE A  67      30.240 -51.601 -46.648  1.00 12.83           N
ANISOU  889  N   ILE A  67     1552   1606   1716    492   -237   -125       N
ATOM    890  CA  ILE A  67      29.695 -52.929 -46.995  1.00 13.32           C
ANISOU  890  CA  ILE A  67     1635   1664   1764    513   -242   -129       C
ATOM    891  C   ILE A  67      30.811 -53.908 -47.358  1.00 13.50           C
ANISOU  891  C   ILE A  67     1621   1679   1831    538   -249   -135       C
ATOM    892  O   ILE A  67      30.741 -55.054 -46.954  1.00 14.65           O
ANISOU  892  O   ILE A  67     1777   1813   1976    550   -281   -136       O
ATOM    893  CB  ILE A  67      28.649 -52.829 -48.135  1.00 14.79           C
ANISOU  893  CB  ILE A  67     1846   1856   1918    525   -207   -137       C
ATOM    894  CG1 ILE A  67      27.443 -52.018 -47.640  1.00 15.51           C
ANISOU  894  CG1 ILE A  67     1966   1947   1978    500   -208   -134       C
ATOM    895  CG2 ILE A  67      28.244 -54.196 -48.678  1.00 15.81           C
ANISOU  895  CG2 ILE A  67     1985   1973   2049    554   -218   -149       C
ATOM    896  CD1 ILE A  67      26.724 -52.622 -46.510  1.00 17.79           C
ANISOU  896  CD1 ILE A  67     2277   2217   2266    487   -230   -126       C
ATOM    897  H   ILE A  67      30.052 -50.804 -47.240  1.00  0.00           H
ATOM    898  HA  ILE A  67      29.187 -53.319 -46.113  1.00  0.00           H
ATOM    899  HB  ILE A  67      29.106 -52.272 -48.953  1.00  0.00           H
ATOM    900 HG12 ILE A  67      27.798 -51.035 -47.331  1.00  0.00           H
ATOM    901 HG13 ILE A  67      26.746 -51.891 -48.468  1.00  0.00           H
ATOM    902 HG21 ILE A  67      29.132 -54.731 -49.016  1.00  0.00           H
ATOM    903 HG22 ILE A  67      27.753 -54.768 -47.891  1.00  0.00           H
ATOM    904 HG23 ILE A  67      27.558 -54.066 -49.515  1.00  0.00           H
ATOM    905 HD11 ILE A  67      25.888 -51.982 -46.227  1.00  0.00           H
ATOM    906 HD12 ILE A  67      26.348 -53.603 -46.801  1.00  0.00           H
ATOM    907 HD13 ILE A  67      27.402 -52.730 -45.664  1.00  0.00           H
ATOM    908  N   ASP A  68      31.837 -53.493 -48.091  1.00 13.56           N
ANISOU  908  N   ASP A  68     1586   1683   1882    547   -213   -140       N
ATOM    909  CA  ASP A  68      32.962 -54.410 -48.356  1.00 14.98           C
ANISOU  909  CA  ASP A  68     1724   1846   2120    569   -216   -148       C
ATOM    910  C   ASP A  68      33.708 -54.812 -47.099  1.00 15.47           C
ANISOU  910  C   ASP A  68     1760   1892   2226    564   -291   -155       C
ATOM    911  O   ASP A  68      34.182 -55.968 -46.994  1.00 16.34           O
ANISOU  911  O   ASP A  68     1858   1990   2359    584   -321   -161       O
ATOM    912  CB  ASP A  68      33.903 -53.835 -49.429  1.00 14.94           C
ANISOU  912  CB  ASP A  68     1680   1828   2170    581   -140   -151       C
ATOM    913  CG  ASP A  68      33.303 -53.984 -50.847  1.00 21.61           C
ANISOU  913  CG  ASP A  68     2578   2676   2958    613    -74   -147       C
ATOM    914  OD1 ASP A  68      32.415 -54.863 -51.025  1.00 22.32           O
ANISOU  914  OD1 ASP A  68     2711   2776   2995    629   -104   -152       O
ATOM    915  OD2 ASP A  68      33.701 -53.248 -51.769  1.00 20.37           O
ANISOU  915  OD2 ASP A  68     2426   2503   2811    627      7   -143       O
ATOM    916  H   ASP A  68      31.847 -52.555 -48.465  1.00  0.00           H
ATOM    917  HA  ASP A  68      32.533 -55.322 -48.771  1.00  0.00           H
ATOM    918  HB2 ASP A  68      34.853 -54.367 -49.389  1.00  0.00           H
ATOM    919  HB3 ASP A  68      34.076 -52.779 -49.223  1.00  0.00           H
ATOM    920  N   ALA A  69      33.823 -53.897 -46.141  1.00 14.18           N
ANISOU  920  N   ALA A  69     1595   1723   2070    544   -329   -156       N
ATOM    921  CA  ALA A  69      34.446 -54.226 -44.848  1.00 15.29           C
ANISOU  921  CA  ALA A  69     1737   1837   2237    551   -420   -168       C
ATOM    922  C   ALA A  69      33.543 -55.213 -44.096  1.00 15.78           C
ANISOU  922  C   ALA A  69     1878   1898   2221    562   -454   -154       C
ATOM    923  O   ALA A  69      34.022 -56.204 -43.567  1.00 15.40           O
ANISOU  923  O   ALA A  69     1839   1827   2184    585   -507   -161       O
ATOM    924  CB  ALA A  69      34.692 -52.969 -44.010  1.00 15.31           C
ANISOU  924  CB  ALA A  69     1735   1827   2256    535   -460   -175       C
ATOM    925  H   ALA A  69      33.478 -52.962 -46.303  1.00  0.00           H
ATOM    926  HA  ALA A  69      35.405 -54.709 -45.038  1.00  0.00           H
ATOM    927  HB1 ALA A  69      35.153 -53.248 -43.062  1.00  0.00           H
ATOM    928  HB2 ALA A  69      33.743 -52.469 -43.819  1.00  0.00           H
ATOM    929  HB3 ALA A  69      35.355 -52.295 -44.552  1.00  0.00           H
ATOM    930  N   LEU A  70      32.231 -54.972 -44.134  1.00 15.67           N
ANISOU  930  N   LEU A  70     1916   1900   2138    546   -416   -136       N
ATOM    931  CA  LEU A  70      31.257 -55.847 -43.468  1.00 15.87           C
ANISOU  931  CA  LEU A  70     2011   1911   2108    553   -422   -122       C
ATOM    932  C   LEU A  70      31.375 -57.279 -43.996  1.00 16.76           C
ANISOU  932  C   LEU A  70     2111   2019   2236    575   -418   -126       C
ATOM    933  O   LEU A  70      31.571 -58.252 -43.243  1.00 16.33           O
ANISOU  933  O   LEU A  70     2091   1938   2173    596   -457   -123       O
ATOM    934  CB  LEU A  70      29.843 -55.332 -43.711  1.00 15.29           C
ANISOU  934  CB  LEU A  70     1969   1848   1993    531   -368   -110       C
ATOM    935  CG  LEU A  70      28.709 -56.217 -43.172  1.00 15.44           C
ANISOU  935  CG  LEU A  70     2045   1839   1982    535   -350    -97       C
ATOM    936  CD1 LEU A  70      28.493 -56.026 -41.683  1.00 15.90           C
ANISOU  936  CD1 LEU A  70     2182   1861   1997    538   -368    -80       C
ATOM    937  CD2 LEU A  70      27.441 -55.897 -43.978  1.00 14.87           C
ANISOU  937  CD2 LEU A  70     1963   1775   1911    518   -298   -100       C
ATOM    938  H   LEU A  70      31.897 -54.162 -44.637  1.00  0.00           H
ATOM    939  HA  LEU A  70      31.455 -55.847 -42.396  1.00  0.00           H
ATOM    940  HB2 LEU A  70      29.757 -54.354 -43.238  1.00  0.00           H
ATOM    941  HB3 LEU A  70      29.702 -55.208 -44.785  1.00  0.00           H
ATOM    942  HG  LEU A  70      28.974 -57.259 -43.349  1.00  0.00           H
ATOM    943 HD11 LEU A  70      29.413 -56.262 -41.149  1.00  0.00           H
ATOM    944 HD12 LEU A  70      27.696 -56.688 -41.344  1.00  0.00           H
ATOM    945 HD13 LEU A  70      28.214 -54.991 -41.486  1.00  0.00           H
ATOM    946 HD21 LEU A  70      26.616 -56.511 -43.618  1.00  0.00           H
ATOM    947 HD22 LEU A  70      27.618 -56.109 -45.032  1.00  0.00           H
ATOM    948 HD23 LEU A  70      27.189 -54.843 -43.856  1.00  0.00           H
ATOM    949  N   LEU A  71      31.318 -57.426 -45.306  1.00 17.74           N
ANISOU  949  N   LEU A  71     2194   2165   2380    578   -374   -133       N
ATOM    950  CA  LEU A  71      31.312 -58.767 -45.920  1.00 17.58           C
ANISOU  950  CA  LEU A  71     2167   2141   2373    601   -369   -138       C
ATOM    951  C   LEU A  71      32.662 -59.482 -45.762  1.00 16.97           C
ANISOU  951  C   LEU A  71     2053   2051   2342    622   -409   -148       C
ATOM    952  O   LEU A  71      32.719 -60.706 -45.691  1.00 16.16           O
ANISOU  952  O   LEU A  71     1961   1937   2242    641   -427   -149       O
ATOM    953  CB  LEU A  71      30.974 -58.691 -47.411  1.00 17.67           C
ANISOU  953  CB  LEU A  71     2159   2169   2384    610   -320   -148       C
ATOM    954  CG  LEU A  71      29.640 -58.047 -47.804  1.00 19.92           C
ANISOU  954  CG  LEU A  71     2473   2459   2634    598   -293   -149       C
ATOM    955  CD1 LEU A  71      29.515 -57.973 -49.322  1.00 20.69           C
ANISOU  955  CD1 LEU A  71     2571   2565   2726    624   -261   -164       C
ATOM    956  CD2 LEU A  71      28.472 -58.801 -47.194  1.00 21.41           C
ANISOU  956  CD2 LEU A  71     2694   2625   2816    593   -303   -147       C
ATOM    957  H   LEU A  71      31.278 -56.608 -45.897  1.00  0.00           H
ATOM    958  HA  LEU A  71      30.547 -59.366 -45.426  1.00  0.00           H
ATOM    959  HB2 LEU A  71      31.767 -58.121 -47.896  1.00  0.00           H
ATOM    960  HB3 LEU A  71      30.991 -59.704 -47.813  1.00  0.00           H
ATOM    961  HG  LEU A  71      29.627 -57.030 -47.413  1.00  0.00           H
ATOM    962 HD11 LEU A  71      28.563 -57.513 -49.587  1.00  0.00           H
ATOM    963 HD12 LEU A  71      29.561 -58.979 -49.740  1.00  0.00           H
ATOM    964 HD13 LEU A  71      30.332 -57.374 -49.725  1.00  0.00           H
ATOM    965 HD21 LEU A  71      27.537 -58.324 -47.488  1.00  0.00           H
ATOM    966 HD22 LEU A  71      28.560 -58.789 -46.108  1.00  0.00           H
ATOM    967 HD23 LEU A  71      28.481 -59.832 -47.548  1.00  0.00           H
ATOM    968  N   GLY A  72      33.755 -58.719 -45.740  1.00 16.19           N
ANISOU  968  N   GLY A  72     1907   1951   2295    619   -422   -158       N
ATOM    969  CA  GLY A  72      35.075 -59.288 -45.560  1.00 16.43           C
ANISOU  969  CA  GLY A  72     1890   1960   2394    638   -465   -175       C
ATOM    970  C   GLY A  72      35.794 -59.536 -46.883  1.00 17.35           C
ANISOU  970  C   GLY A  72     1944   2079   2569    651   -407   -184       C
ATOM    971  O   GLY A  72      36.472 -60.543 -47.037  1.00 19.11           O
ANISOU  971  O   GLY A  72     2140   2287   2832    672   -424   -193       O
ATOM    972  H   GLY A  72      33.660 -57.720 -45.852  1.00  0.00           H
ATOM    973  HA2 GLY A  72      35.673 -58.600 -44.962  1.00  0.00           H
ATOM    974  HA3 GLY A  72      34.983 -60.233 -45.025  1.00  0.00           H
ATOM    975  N   ASP A  73      35.601 -58.634 -47.844  1.00 15.10           N
ANISOU  975  N   ASP A  73     1648   1808   2283    641   -332   -178       N
ATOM    976  CA  ASP A  73      36.470 -58.538 -49.021  1.00 15.19           C
ANISOU  976  CA  ASP A  73     1609   1805   2357    657   -258   -184       C
ATOM    977  C   ASP A  73      37.915 -58.565 -48.502  1.00 17.56           C
ANISOU  977  C   ASP A  73     1827   2068   2776    658   -294   -205       C
ATOM    978  O   ASP A  73      38.254 -57.828 -47.577  1.00 20.22           O
ANISOU  978  O   ASP A  73     2139   2390   3152    641   -349   -216       O
ATOM    979  CB  ASP A  73      36.089 -57.215 -49.778  1.00 19.63           C
ANISOU  979  CB  ASP A  73     2186   2376   2896    646   -179   -174       C
ATOM    980  CG  ASP A  73      36.795 -57.043 -51.118  1.00 20.98           C
ANISOU  980  CG  ASP A  73     2339   2523   3111    670    -75   -173       C
ATOM    981  OD1 ASP A  73      37.857 -57.641 -51.327  1.00 21.51           O
ANISOU  981  OD1 ASP A  73     2352   2561   3262    686    -58   -182       O
ATOM    982  OD2 ASP A  73      36.340 -56.243 -51.962  1.00 20.88           O
ANISOU  982  OD2 ASP A  73     2369   2512   3053    677     -2   -162       O
ATOM    983  H   ASP A  73      34.826 -57.992 -47.759  1.00  0.00           H
ATOM    984  HA  ASP A  73      36.299 -59.395 -49.673  1.00  0.00           H
ATOM    985  HB2 ASP A  73      35.014 -57.219 -49.955  1.00  0.00           H
ATOM    986  HB3 ASP A  73      36.335 -56.365 -49.142  1.00  0.00           H
ATOM    987  N   PRO A  74      38.783 -59.461 -49.035  1.00 16.74           N
ANISOU  987  N   PRO A  74     1680   1941   2739    682   -274   -215       N
ATOM    988  CA  PRO A  74      40.093 -59.570 -48.385  1.00 17.44           C
ANISOU  988  CA  PRO A  74     1685   1987   2956    685   -332   -243       C
ATOM    989  C   PRO A  74      40.852 -58.250 -48.180  1.00 18.77           C
ANISOU  989  C   PRO A  74     1779   2120   3232    666   -319   -260       C
ATOM    990  O   PRO A  74      41.446 -58.078 -47.117  1.00 19.51           O
ANISOU  990  O   PRO A  74     1834   2184   3395    664   -420   -288       O
ATOM    991  CB  PRO A  74      40.885 -60.527 -49.311  1.00 16.67           C
ANISOU  991  CB  PRO A  74     1543   1865   2924    712   -275   -249       C
ATOM    992  CG  PRO A  74      39.813 -61.407 -49.954  1.00 16.03           C
ANISOU  992  CG  PRO A  74     1550   1825   2717    729   -248   -226       C
ATOM    993  CD  PRO A  74      38.569 -60.487 -50.069  1.00 16.27           C
ANISOU  993  CD  PRO A  74     1649   1890   2642    711   -223   -206       C
ATOM    994  HA  PRO A  74      39.962 -60.051 -47.416  1.00  0.00           H
ATOM    995  HB2 PRO A  74      41.585 -61.131 -48.733  1.00  0.00           H
ATOM    996  HB3 PRO A  74      41.417 -59.960 -50.075  1.00  0.00           H
ATOM    997  HG2 PRO A  74      40.133 -61.746 -50.939  1.00  0.00           H
ATOM    998  HG3 PRO A  74      39.593 -62.262 -49.314  1.00  0.00           H
ATOM    999  HD2 PRO A  74      38.514 -60.033 -51.058  1.00  0.00           H
ATOM   1000  HD3 PRO A  74      37.660 -61.051 -49.860  1.00  0.00           H
ATOM   1001  N   HIS A  75      40.866 -57.336 -49.146  1.00 18.92           N
ANISOU 1001  N   HIS A  75     1784   2133   3271    657   -201   -247       N
ATOM   1002  CA  HIS A  75      41.652 -56.106 -48.933  1.00 19.00           C
ANISOU 1002  CA  HIS A  75     1713   2100   3406    637   -183   -265       C
ATOM   1003  C   HIS A  75      40.982 -55.180 -47.927  1.00 18.57           C
ANISOU 1003  C   HIS A  75     1695   2069   3291    613   -262   -265       C
ATOM   1004  O   HIS A  75      41.575 -54.205 -47.511  1.00 19.20           O
ANISOU 1004  O   HIS A  75     1710   2113   3470    597   -280   -287       O
ATOM   1005  CB  HIS A  75      41.945 -55.375 -50.240  1.00 19.75           C
ANISOU 1005  CB  HIS A  75     1788   2169   3548    639    -20   -248       C
ATOM   1006  CG  HIS A  75      40.826 -54.513 -50.707  1.00 20.32           C
ANISOU 1006  CG  HIS A  75     1948   2282   3491    629     40   -218       C
ATOM   1007  ND1 HIS A  75      39.644 -55.026 -51.201  1.00 22.72           N
ANISOU 1007  ND1 HIS A  75     2359   2636   3636    645     48   -194       N
ATOM   1008  CD2 HIS A  75      40.702 -53.162 -50.753  1.00 19.32           C
ANISOU 1008  CD2 HIS A  75     1816   2148   3378    608     88   -212       C
ATOM   1009  CE1 HIS A  75      38.845 -54.027 -51.551  1.00 22.34           C
ANISOU 1009  CE1 HIS A  75     2368   2608   3510    635     95   -177       C
ATOM   1010  NE2 HIS A  75      39.463 -52.886 -51.278  1.00 21.66           N
ANISOU 1010  NE2 HIS A  75     2219   2492   3520    612    123   -185       N
ATOM   1011  H   HIS A  75      40.352 -57.480 -50.003  1.00  0.00           H
ATOM   1012  HA  HIS A  75      42.610 -56.405 -48.508  1.00  0.00           H
ATOM   1013  HB2 HIS A  75      42.152 -56.118 -51.011  1.00  0.00           H
ATOM   1014  HB3 HIS A  75      42.831 -54.755 -50.104  1.00  0.00           H
ATOM   1015  HD2 HIS A  75      41.439 -52.439 -50.436  1.00  0.00           H
ATOM   1016  HE1 HIS A  75      37.860 -54.126 -51.984  1.00  0.00           H
ATOM   1017  HD1 HIS A  75      39.422 -56.008 -51.283  1.00  0.00           H
ATOM   1018  HE2 HIS A  75      39.084 -51.963 -51.431  1.00  0.00           H
ATOM   1019  N   CYS A  76      39.775 -55.526 -47.490  1.00 18.01           N
ANISOU 1019  N   CYS A  76     1724   2051   3069    611   -310   -245       N
ATOM   1020  CA  CYS A  76      39.094 -54.773 -46.448  1.00 18.65           C
ANISOU 1020  CA  CYS A  76     1853   2149   3085    592   -382   -243       C
ATOM   1021  C   CYS A  76      39.132 -55.465 -45.073  1.00 16.76           C
ANISOU 1021  C   CYS A  76     1649   1897   2820    608   -520   -260       C
ATOM   1022  O   CYS A  76      38.590 -54.920 -44.133  1.00 16.20           O
ANISOU 1022  O   CYS A  76     1635   1833   2689    600   -580   -257       O
ATOM   1023  CB  CYS A  76      37.643 -54.483 -46.846  1.00 21.10           C
ANISOU 1023  CB  CYS A  76     2252   2511   3254    579   -329   -210       C
ATOM   1024  SG  CYS A  76      37.566 -53.595 -48.443  1.00 23.79           S
ANISOU 1024  SG  CYS A  76     2582   2855   3601    575   -177   -193       S
ATOM   1025  H   CYS A  76      39.319 -56.333 -47.892  1.00  0.00           H
ATOM   1026  HA  CYS A  76      39.605 -53.815 -46.348  1.00  0.00           H
ATOM   1027  HB2 CYS A  76      37.103 -55.426 -46.936  1.00  0.00           H
ATOM   1028  HB3 CYS A  76      37.174 -53.873 -46.074  1.00  0.00           H
ATOM   1029  N   ASP A  77      39.751 -56.643 -44.955  1.00 16.48           N
ANISOU 1029  N   ASP A  77     1595   1842   2825    634   -566   -275       N
ATOM   1030  CA  ASP A  77      39.713 -57.380 -43.692  1.00 17.44           C
ANISOU 1030  CA  ASP A  77     1778   1947   2903    659   -691   -287       C
ATOM   1031  C   ASP A  77      40.530 -56.715 -42.573  1.00 17.16           C
ANISOU 1031  C   ASP A  77     1725   1862   2933    660   -801   -325       C
ATOM   1032  O   ASP A  77      40.435 -57.106 -41.427  1.00 17.45           O
ANISOU 1032  O   ASP A  77     1847   1881   2903    674   -894   -333       O
ATOM   1033  CB  ASP A  77      40.149 -58.857 -43.887  1.00 16.47           C
ANISOU 1033  CB  ASP A  77     1648   1814   2795    684   -708   -293       C
ATOM   1034  CG  ASP A  77      38.962 -59.772 -44.268  1.00 22.47           C
ANISOU 1034  CG  ASP A  77     2489   2619   3431    688   -658   -257       C
ATOM   1035  OD1 ASP A  77      37.802 -59.485 -43.873  1.00 21.00           O
ANISOU 1035  OD1 ASP A  77     2385   2456   3138    675   -647   -232       O
ATOM   1036  OD2 ASP A  77      39.192 -60.756 -45.001  1.00 23.29           O
ANISOU 1036  OD2 ASP A  77     2569   2727   3554    701   -622   -255       O
ATOM   1037  H   ASP A  77      40.249 -57.028 -45.745  1.00  0.00           H
ATOM   1038  HA  ASP A  77      38.674 -57.395 -43.363  1.00  0.00           H
ATOM   1039  HB2 ASP A  77      40.894 -58.901 -44.681  1.00  0.00           H
ATOM   1040  HB3 ASP A  77      40.595 -59.221 -42.961  1.00  0.00           H
ATOM   1041  N  AVAL A  78      41.311 -55.698 -42.919  0.43 16.31           N
ANISOU 1041  N  AVAL A  78     1522   1728   2948    638   -774   -348       N
ATOM   1042  N  BVAL A  78      41.353 -55.731 -42.932  0.57 16.31           N
ANISOU 1042  N  BVAL A  78     1519   1726   2951    638   -774   -349       N
ATOM   1043  CA AVAL A  78      42.011 -54.913 -41.926  0.43 16.80           C
ANISOU 1043  CA AVAL A  78     1571   1741   3070    628   -870   -388       C
ATOM   1044  CA BVAL A  78      42.002 -54.890 -41.948  0.57 16.74           C
ANISOU 1044  CA BVAL A  78     1562   1734   3063    628   -867   -387       C
ATOM   1045  C  AVAL A  78      41.008 -54.133 -41.063  0.43 16.78           C
ANISOU 1045  C  AVAL A  78     1667   1758   2952    634   -917   -372       C
ATOM   1046  C  BVAL A  78      40.970 -54.303 -40.995  0.57 16.77           C
ANISOU 1046  C  BVAL A  78     1676   1757   2937    637   -924   -371       C
ATOM   1047  O  AVAL A  78      41.361 -53.589 -40.020  0.43 17.32           O
ANISOU 1047  O  AVAL A  78     1767   1786   3027    635  -1014   -404       O
ATOM   1048  O  BVAL A  78      41.275 -54.057 -39.825  0.57 17.14           O
ANISOU 1048  O  BVAL A  78     1779   1765   2970    646  -1031   -401       O
ATOM   1049  CB AVAL A  78      43.033 -53.972 -42.606  0.43 18.46           C
ANISOU 1049  CB AVAL A  78     1649   1912   3453    599   -810   -413       C
ATOM   1050  CB BVAL A  78      42.824 -53.739 -42.600  0.57 19.04           C
ANISOU 1050  CB BVAL A  78     1730   1993   3511    598   -804   -408       C
ATOM   1051  CG1AVAL A  78      42.324 -52.866 -43.366  0.43 18.71           C
ANISOU 1051  CG1AVAL A  78     1658   1976   3473    585   -704   -383       C
ATOM   1052  CG1BVAL A  78      44.172 -54.232 -43.059  0.57 19.25           C
ANISOU 1052  CG1BVAL A  78     1658   1967   3690    587   -785   -440       C
ATOM   1053  CG2AVAL A  78      43.987 -53.395 -41.590  0.43 20.61           C
ANISOU 1053  CG2AVAL A  78     1898   2116   3817    590   -925   -470       C
ATOM   1054  CG2BVAL A  78      42.065 -53.100 -43.760  0.57 18.50           C
ANISOU 1054  CG2BVAL A  78     1638   1967   3423    590   -664   -368       C
ATOM   1055  H  AVAL A  78      41.418 -55.468 -43.897  0.43  0.00           H
ATOM   1056  H  BVAL A  78      41.528 -55.568 -43.913  0.57  0.00           H
ATOM   1057  HA AVAL A  78      42.558 -55.596 -41.277  0.43  0.00           H
ATOM   1058  HA BVAL A  78      42.686 -55.510 -41.369  0.57  0.00           H
ATOM   1059  HB AVAL A  78      43.611 -54.558 -43.320  0.43  0.00           H
ATOM   1060  HB BVAL A  78      42.987 -52.972 -41.843  0.57  0.00           H
ATOM   1061 HG11AVAL A  78      42.540 -51.906 -42.897  0.43  0.00           H
ATOM   1062 HG11BVAL A  78      44.067 -54.738 -44.019  0.57  0.00           H
ATOM   1063 HG12AVAL A  78      42.674 -52.853 -44.398  0.43  0.00           H
ATOM   1064 HG12BVAL A  78      44.574 -54.929 -42.323  0.57  0.00           H
ATOM   1065 HG13AVAL A  78      41.249 -53.045 -43.349  0.43  0.00           H
ATOM   1066 HG13BVAL A  78      44.851 -53.386 -43.167  0.57  0.00           H
ATOM   1067 HG21AVAL A  78      43.421 -52.933 -40.781  0.43  0.00           H
ATOM   1068 HG21BVAL A  78      41.646 -53.881 -44.395  0.57  0.00           H
ATOM   1069 HG22AVAL A  78      44.616 -52.644 -42.068  0.43  0.00           H
ATOM   1070 HG22BVAL A  78      41.259 -52.479 -43.369  0.57  0.00           H
ATOM   1071 HG23AVAL A  78      44.614 -54.191 -41.187  0.43  0.00           H
ATOM   1072 HG23BVAL A  78      42.747 -52.483 -44.345  0.57  0.00           H
ATOM   1073  N   PHE A  79      39.753 -54.101 -41.496  1.00 16.69           N
ANISOU 1073  N   PHE A  79     1709   1801   2831    635   -847   -327       N
ATOM   1074  CA  PHE A  79      38.656 -53.491 -40.727  1.00 17.37           C
ANISOU 1074  CA  PHE A  79     1905   1908   2785    628   -862   -303       C
ATOM   1075  C   PHE A  79      37.850 -54.452 -39.851  1.00 17.58           C
ANISOU 1075  C   PHE A  79     2068   1937   2676    656   -906   -281       C
ATOM   1076  O   PHE A  79      36.911 -54.038 -39.201  1.00 17.40           O
ANISOU 1076  O   PHE A  79     2142   1922   2547    653   -903   -258       O
ATOM   1077  CB  PHE A  79      37.691 -52.793 -41.663  1.00 17.74           C
ANISOU 1077  CB  PHE A  79     1953   2010   2776    586   -730   -265       C
ATOM   1078  CG  PHE A  79      38.283 -51.579 -42.320  1.00 20.75           C
ANISOU 1078  CG  PHE A  79     2235   2383   3264    559   -678   -278       C
ATOM   1079  CD1 PHE A  79      38.515 -50.437 -41.596  1.00 26.06           C
ANISOU 1079  CD1 PHE A  79     2900   3031   3972    553   -738   -299       C
ATOM   1080  CD2 PHE A  79      38.654 -51.603 -43.653  1.00 19.23           C
ANISOU 1080  CD2 PHE A  79     1966   2200   3143    547   -567   -272       C
ATOM   1081  CE1 PHE A  79      39.087 -49.279 -42.219  1.00 27.79           C
ANISOU 1081  CE1 PHE A  79     3020   3234   4306    527   -679   -312       C
ATOM   1082  CE2 PHE A  79      39.259 -50.488 -44.261  1.00 20.60           C
ANISOU 1082  CE2 PHE A  79     2053   2351   3424    526   -501   -282       C
ATOM   1083  CZ  PHE A  79      39.481 -49.333 -43.543  1.00 24.37           C
ANISOU 1083  CZ  PHE A  79     2509   2803   3947    514   -555   -303       C
ATOM   1084  H  APHE A  79      39.542 -54.514 -42.393  0.43  0.00           H
ATOM   1085  H  BPHE A  79      39.574 -54.380 -42.450  0.57  0.00           H
ATOM   1086  HA  PHE A  79      39.090 -52.734 -40.074  1.00  0.00           H
ATOM   1087  HB2 PHE A  79      36.815 -52.486 -41.092  1.00  0.00           H
ATOM   1088  HB3 PHE A  79      37.380 -53.495 -42.436  1.00  0.00           H
ATOM   1089  HD1 PHE A  79      38.264 -50.410 -40.546  1.00  0.00           H
ATOM   1090  HD2 PHE A  79      38.476 -52.494 -44.237  1.00  0.00           H
ATOM   1091  HE1 PHE A  79      39.210 -48.366 -41.655  1.00  0.00           H
ATOM   1092  HE2 PHE A  79      39.552 -50.538 -45.299  1.00  0.00           H
ATOM   1093  HZ  PHE A  79      39.956 -48.482 -44.008  1.00  0.00           H
ATOM   1094  N   GLN A  80      38.256 -55.715 -39.783  1.00 18.33           N
ANISOU 1094  N   GLN A  80     2171   2015   2780    685   -941   -289       N
ATOM   1095  CA  GLN A  80      37.550 -56.671 -38.944  1.00 18.33           C
ANISOU 1095  CA  GLN A  80     2303   2004   2656    712   -966   -267       C
ATOM   1096  C   GLN A  80      37.457 -56.191 -37.510  1.00 18.13           C
ANISOU 1096  C   GLN A  80     2395   1937   2557    729  -1046   -278       C
ATOM   1097  O   GLN A  80      38.444 -55.750 -36.933  1.00 17.65           O
ANISOU 1097  O   GLN A  80     2316   1835   2557    732  -1129   -324       O
ATOM   1098  CB  GLN A  80      38.220 -58.051 -38.992  1.00 19.19           C
ANISOU 1098  CB  GLN A  80     2404   2096   2790    727   -989   -281       C
ATOM   1099  CG  GLN A  80      37.799 -58.873 -40.214  1.00 17.99           C
ANISOU 1099  CG  GLN A  80     2201   1987   2648    722   -899   -256       C
ATOM   1100  CD  GLN A  80      38.299 -60.298 -40.122  1.00 18.21           C
ANISOU 1100  CD  GLN A  80     2242   1998   2680    739   -923   -264       C
ATOM   1101  OE1 GLN A  80      38.997 -60.645 -39.181  1.00 20.30           O
ANISOU 1101  OE1 GLN A  80     2550   2219   2945    755  -1008   -291       O
ATOM   1102  NE2 GLN A  80      37.895 -61.133 -41.061  1.00 16.32           N
ANISOU 1102  NE2 GLN A  80     1976   1789   2436    739   -853   -244       N
ATOM   1103  H   GLN A  80      39.060 -56.013 -40.317  1.00  0.00           H
ATOM   1104  HA  GLN A  80      36.536 -56.775 -39.331  1.00  0.00           H
ATOM   1105  HB2 GLN A  80      37.948 -58.602 -38.092  1.00  0.00           H
ATOM   1106  HB3 GLN A  80      39.302 -57.918 -39.011  1.00  0.00           H
ATOM   1107  HG2 GLN A  80      38.211 -58.410 -41.111  1.00  0.00           H
ATOM   1108  HG3 GLN A  80      36.711 -58.880 -40.283  1.00  0.00           H
ATOM   1109 HE21 GLN A  80      37.300 -60.804 -41.808  1.00  0.00           H
ATOM   1110 HE22 GLN A  80      38.181 -62.101 -41.033  1.00  0.00           H
ATOM   1111  N   ASN A  81      36.228 -56.238 -36.971  1.00 18.50           N
ANISOU 1111  N   ASN A  81     2564   1987   2479    743  -1012   -237       N
ATOM   1112  CA  ASN A  81      35.933 -55.876 -35.581  1.00 19.07           C
ANISOU 1112  CA  ASN A  81     2779   2012   2453    767  -1061   -239       C
ATOM   1113  C   ASN A  81      36.168 -54.408 -35.269  1.00 18.41           C
ANISOU 1113  C   ASN A  81     2676   1923   2398    752  -1101   -261       C
ATOM   1114  O   ASN A  81      36.246 -54.050 -34.106  1.00 18.64           O
ANISOU 1114  O   ASN A  81     2812   1904   2368    775  -1161   -279       O
ATOM   1115  CB  ASN A  81      36.723 -56.745 -34.580  1.00 22.61           C
ANISOU 1115  CB  ASN A  81     3308   2402   2882    804  -1148   -274       C
ATOM   1116  CG  ASN A  81      35.978 -58.048 -34.193  1.00 29.42           C
ANISOU 1116  CG  ASN A  81     4289   3248   3642    833  -1102   -238       C
ATOM   1117  OD1 ASN A  81      35.098 -58.529 -34.931  1.00 24.53           O
ANISOU 1117  OD1 ASN A  81     3651   2664   3007    822  -1010   -193       O
ATOM   1118  ND2 ASN A  81      36.359 -58.628 -33.029  1.00 42.85           N
ANISOU 1118  ND2 ASN A  81     6114   4888   5280    875  -1168   -262       N
ATOM   1119  H   ASN A  81      35.463 -56.540 -37.557  1.00  0.00           H
ATOM   1120  HA  ASN A  81      34.874 -56.075 -35.414  1.00  0.00           H
ATOM   1121  HB2 ASN A  81      36.897 -56.162 -33.675  1.00  0.00           H
ATOM   1122  HB3 ASN A  81      37.685 -57.006 -35.022  1.00  0.00           H
ATOM   1123 HD21 ASN A  81      37.084 -58.204 -32.467  1.00  0.00           H
ATOM   1124 HD22 ASN A  81      35.918 -59.484 -32.723  1.00  0.00           H
ATOM   1125  N   GLU A  82      36.258 -53.553 -36.283  1.00 17.76           N
ANISOU 1125  N   GLU A  82     2465   1882   2400    717  -1063   -260       N
ATOM   1126  CA  GLU A  82      36.563 -52.147 -36.017  1.00 20.13           C
ANISOU 1126  CA  GLU A  82     2735   2173   2742    702  -1100   -284       C
ATOM   1127  C   GLU A  82      35.285 -51.458 -35.518  1.00 19.34           C
ANISOU 1127  C   GLU A  82     2745   2084   2520    702  -1060   -243       C
ATOM   1128  O   GLU A  82      34.167 -51.981 -35.711  1.00 17.95           O
ANISOU 1128  O   GLU A  82     2627   1934   2259    687   -958   -198       O
ATOM   1129  CB  GLU A  82      37.034 -51.438 -37.294  1.00 22.31           C
ANISOU 1129  CB  GLU A  82     2843   2485   3150    665  -1052   -294       C
ATOM   1130  CG  GLU A  82      38.522 -51.435 -37.457  1.00 28.06           C
ANISOU 1130  CG  GLU A  82     3459   3174   4029    659  -1107   -348       C
ATOM   1131  CD  GLU A  82      39.145 -50.416 -36.541  1.00 34.79           C
ANISOU 1131  CD  GLU A  82     4324   3974   4923    660  -1199   -393       C
ATOM   1132  OE1 GLU A  82      38.404 -49.861 -35.702  1.00 33.98           O
ANISOU 1132  OE1 GLU A  82     4333   3866   4710    671  -1222   -379       O
ATOM   1133  OE2 GLU A  82      40.362 -50.184 -36.657  1.00 40.04           O
ANISOU 1133  OE2 GLU A  82     4888   4594   5732    650  -1243   -444       O
ATOM   1134  H   GLU A  82      36.117 -53.872 -37.231  1.00  0.00           H
ATOM   1135  HA  GLU A  82      37.338 -52.079 -35.253  1.00  0.00           H
ATOM   1136  HB2 GLU A  82      36.688 -50.405 -37.263  1.00  0.00           H
ATOM   1137  HB3 GLU A  82      36.587 -51.933 -38.156  1.00  0.00           H
ATOM   1138  HG2 GLU A  82      38.912 -52.423 -37.214  1.00  0.00           H
ATOM   1139  HG3 GLU A  82      38.772 -51.192 -38.490  1.00  0.00           H
ATOM   1140  N   THR A  83      35.463 -50.301 -34.890  1.00 18.79           N
ANISOU 1140  N   THR A  83     2695   1992   2451    697  -1107   -264       N
ATOM   1141  CA  THR A  83      34.353 -49.485 -34.403  1.00 16.81           C
ANISOU 1141  CA  THR A  83     2543   1749   2097    694  -1068   -230       C
ATOM   1142  C   THR A  83      34.591 -48.040 -34.811  1.00 17.69           C
ANISOU 1142  C   THR A  83     2558   1882   2281    655  -1066   -247       C
ATOM   1143  O   THR A  83      35.697 -47.678 -35.142  1.00 18.29           O
ANISOU 1143  O   THR A  83     2519   1945   2485    651  -1125   -290       O
ATOM   1144  CB  THR A  83      34.214 -49.530 -32.857  1.00 19.97           C
ANISOU 1144  CB  THR A  83     3116   2083   2390    732  -1117   -240       C
ATOM   1145  OG1 THR A  83      35.320 -48.864 -32.257  1.00 20.71           O
ANISOU 1145  OG1 THR A  83     3188   2131   2551    742  -1226   -302       O
ATOM   1146  CG2 THR A  83      34.085 -50.960 -32.312  1.00 20.69           C
ANISOU 1146  CG2 THR A  83     3312   2139   2409    769  -1110   -230       C
ATOM   1147  H   THR A  83      36.406 -49.971 -34.743  1.00  0.00           H
ATOM   1148  HA  THR A  83      33.426 -49.836 -34.856  1.00  0.00           H
ATOM   1149  HB  THR A  83      33.309 -48.986 -32.586  1.00  0.00           H
ATOM   1150  HG1 THR A  83      36.131 -49.328 -32.477  1.00  0.00           H
ATOM   1151 HG21 THR A  83      33.991 -50.929 -31.227  1.00  0.00           H
ATOM   1152 HG22 THR A  83      34.972 -51.533 -32.583  1.00  0.00           H
ATOM   1153 HG23 THR A  83      33.201 -51.433 -32.740  1.00  0.00           H
ATOM   1154  N   TRP A  84      33.546 -47.203 -34.774  1.00 17.64           N
ANISOU 1154  N   TRP A  84     2596   1904   2203    624   -988   -214       N
ATOM   1155  CA  TRP A  84      33.683 -45.822 -35.186  1.00 18.34           C
ANISOU 1155  CA  TRP A  84     2601   2016   2354    584   -973   -226       C
ATOM   1156  C   TRP A  84      32.523 -45.020 -34.614  1.00 18.33           C
ANISOU 1156  C   TRP A  84     2702   2020   2241    573   -926   -194       C
ATOM   1157  O   TRP A  84      31.432 -45.571 -34.373  1.00 18.78           O
ANISOU 1157  O   TRP A  84     2856   2081   2198    575   -852   -154       O
ATOM   1158  CB  TRP A  84      33.626 -45.680 -36.733  1.00 14.57           C
ANISOU 1158  CB  TRP A  84     1985   1599   1953    527   -857   -214       C
ATOM   1159  CG  TRP A  84      32.349 -46.246 -37.315  1.00 14.52           C
ANISOU 1159  CG  TRP A  84     2017   1637   1863    502   -737   -169       C
ATOM   1160  CD1 TRP A  84      31.159 -45.557 -37.563  1.00 15.47           C
ANISOU 1160  CD1 TRP A  84     2165   1789   1922    468   -649   -139       C
ATOM   1161  CD2 TRP A  84      32.102 -47.611 -37.677  1.00 13.75           C
ANISOU 1161  CD2 TRP A  84     1931   1546   1746    513   -701   -154       C
ATOM   1162  NE1 TRP A  84      30.209 -46.435 -38.062  1.00 15.03           N
ANISOU 1162  NE1 TRP A  84     2132   1755   1823    459   -568   -111       N
ATOM   1163  CE2 TRP A  84      30.769 -47.689 -38.160  1.00 14.80           C
ANISOU 1163  CE2 TRP A  84     2093   1713   1818    485   -596   -119       C
ATOM   1164  CE3 TRP A  84      32.887 -48.770 -37.679  1.00 14.56           C
ANISOU 1164  CE3 TRP A  84     2017   1629   1887    544   -750   -170       C
ATOM   1165  CZ2 TRP A  84      30.204 -48.890 -38.611  1.00 15.21           C
ANISOU 1165  CZ2 TRP A  84     2156   1773   1852    488   -543   -102       C
ATOM   1166  CZ3 TRP A  84      32.306 -49.983 -38.125  1.00 15.03           C
ANISOU 1166  CZ3 TRP A  84     2095   1703   1913    546   -689   -147       C
ATOM   1167  CH2 TRP A  84      30.993 -50.028 -38.578  1.00 15.57           C
ANISOU 1167  CH2 TRP A  84     2189   1800   1926    518   -589   -115       C
ATOM   1168  H   TRP A  84      32.649 -47.540 -34.454  1.00  0.00           H
ATOM   1169  HA  TRP A  84      34.626 -45.420 -34.815  1.00  0.00           H
ATOM   1170  HB2 TRP A  84      33.690 -44.623 -36.990  1.00  0.00           H
ATOM   1171  HB3 TRP A  84      34.477 -46.203 -37.169  1.00  0.00           H
ATOM   1172  HD1 TRP A  84      31.003 -44.502 -37.392  1.00  0.00           H
ATOM   1173  HE3 TRP A  84      33.914 -48.740 -37.347  1.00  0.00           H
ATOM   1174  HZ2 TRP A  84      29.187 -48.927 -38.972  1.00  0.00           H
ATOM   1175  HZ3 TRP A  84      32.894 -50.889 -38.113  1.00  0.00           H
ATOM   1176  HH2 TRP A  84      30.580 -50.969 -38.911  1.00  0.00           H
ATOM   1177  HE1 TRP A  84      29.261 -46.194 -38.313  1.00  0.00           H
ATOM   1178  N   ASP A  85      32.768 -43.729 -34.441  1.00 16.70           N
ANISOU 1178  N   ASP A  85     2467   1810   2069    560   -961   -213       N
ATOM   1179  CA  ASP A  85      31.667 -42.783 -34.336  1.00 17.01           C
ANISOU 1179  CA  ASP A  85     2556   1874   2033    529   -886   -182       C
ATOM   1180  C   ASP A  85      31.293 -42.352 -35.746  1.00 16.82           C
ANISOU 1180  C   ASP A  85     2411   1916   2063    466   -769   -166       C
ATOM   1181  O   ASP A  85      30.120 -42.275 -36.085  1.00 16.89           O
ANISOU 1181  O   ASP A  85     2451   1958   2009    437   -670   -131       O
ATOM   1182  CB  ASP A  85      32.045 -41.566 -33.520  1.00 18.67           C
ANISOU 1182  CB  ASP A  85     2797   2050   2249    545   -977   -209       C
ATOM   1183  CG  ASP A  85      32.209 -41.878 -32.066  1.00 20.91           C
ANISOU 1183  CG  ASP A  85     3235   2259   2450    612  -1079   -225       C
ATOM   1184  OD1 ASP A  85      31.522 -42.773 -31.539  1.00 20.06           O
ANISOU 1184  OD1 ASP A  85     3250   2132   2240    636  -1032   -194       O
ATOM   1185  OD2 ASP A  85      33.070 -41.234 -31.456  1.00 23.31           O
ANISOU 1185  OD2 ASP A  85     3529   2516   2811    626  -1169   -274       O
ATOM   1186  H   ASP A  85      33.721 -43.401 -34.382  1.00  0.00           H
ATOM   1187  HA  ASP A  85      30.813 -43.276 -33.872  1.00  0.00           H
ATOM   1188  HB2 ASP A  85      32.986 -41.169 -33.900  1.00  0.00           H
ATOM   1189  HB3 ASP A  85      31.270 -40.808 -33.634  1.00  0.00           H
ATOM   1190  N   LEU A  86      32.302 -42.039 -36.560  1.00 16.50           N
ANISOU 1190  N   LEU A  86     2239   1885   2146    449   -780   -194       N
ATOM   1191  CA  LEU A  86      32.057 -41.700 -37.958  1.00 15.06           C
ANISOU 1191  CA  LEU A  86     1962   1754   2008    402   -665   -179       C
ATOM   1192  C   LEU A  86      32.943 -42.503 -38.914  1.00 15.50           C
ANISOU 1192  C   LEU A  86     1919   1811   2159    405   -645   -193       C
ATOM   1193  O   LEU A  86      34.140 -42.385 -38.857  1.00 15.87           O
ANISOU 1193  O   LEU A  86     1891   1823   2318    417   -705   -229       O
ATOM   1194  CB  LEU A  86      32.263 -40.207 -38.197  1.00 15.50           C
ANISOU 1194  CB  LEU A  86     1959   1815   2115    373   -651   -190       C
ATOM   1195  CG  LEU A  86      31.783 -39.713 -39.572  1.00 16.48           C
ANISOU 1195  CG  LEU A  86     2025   1986   2252    333   -525   -168       C
ATOM   1196  CD1 LEU A  86      30.240 -39.822 -39.754  1.00 15.29           C
ANISOU 1196  CD1 LEU A  86     1953   1874   1982    317   -453   -131       C
ATOM   1197  CD2 LEU A  86      32.315 -38.274 -39.842  1.00 16.54           C
ANISOU 1197  CD2 LEU A  86     1960   1985   2340    309   -512   -184       C
ATOM   1198  H   LEU A  86      33.247 -42.037 -36.204  1.00  0.00           H
ATOM   1199  HA  LEU A  86      31.017 -41.937 -38.184  1.00  0.00           H
ATOM   1200  HB2 LEU A  86      33.328 -39.991 -38.110  1.00  0.00           H
ATOM   1201  HB3 LEU A  86      31.731 -39.654 -37.423  1.00  0.00           H
ATOM   1202  HG  LEU A  86      32.237 -40.364 -40.319  1.00  0.00           H
ATOM   1203 HD11 LEU A  86      29.921 -40.845 -39.554  1.00  0.00           H
ATOM   1204 HD12 LEU A  86      29.975 -39.553 -40.776  1.00  0.00           H
ATOM   1205 HD13 LEU A  86      29.743 -39.144 -39.059  1.00  0.00           H
ATOM   1206 HD21 LEU A  86      31.969 -37.935 -40.818  1.00  0.00           H
ATOM   1207 HD22 LEU A  86      31.944 -37.599 -39.071  1.00  0.00           H
ATOM   1208 HD23 LEU A  86      33.405 -38.280 -39.825  1.00  0.00           H
ATOM   1209  N   PHE A  87      32.332 -43.291 -39.799  1.00 16.73           N
ANISOU 1209  N   PHE A  87     2076   2003   2279    395   -560   -168       N
ATOM   1210  CA  PHE A  87      33.045 -44.018 -40.851  1.00 16.71           C
ANISOU 1210  CA  PHE A  87     1991   2004   2354    398   -520   -176       C
ATOM   1211  C   PHE A  87      33.113 -43.091 -42.058  1.00 16.50           C
ANISOU 1211  C   PHE A  87     1896   1998   2375    370   -423   -170       C
ATOM   1212  O   PHE A  87      32.096 -42.558 -42.472  1.00 15.76           O
ANISOU 1212  O   PHE A  87     1841   1937   2210    351   -360   -148       O
ATOM   1213  CB  PHE A  87      32.279 -45.296 -41.220  1.00 16.20           C
ANISOU 1213  CB  PHE A  87     1974   1962   2220    408   -480   -153       C
ATOM   1214  CG  PHE A  87      33.064 -46.266 -42.097  1.00 17.77           C
ANISOU 1214  CG  PHE A  87     2107   2157   2486    422   -458   -163       C
ATOM   1215  CD1 PHE A  87      33.170 -46.072 -43.447  1.00 17.77           C
ANISOU 1215  CD1 PHE A  87     2054   2177   2522    412   -366   -157       C
ATOM   1216  CD2 PHE A  87      33.682 -47.392 -41.540  1.00 18.97           C
ANISOU 1216  CD2 PHE A  87     2266   2283   2660    453   -528   -177       C
ATOM   1217  CE1 PHE A  87      33.898 -46.953 -44.238  1.00 16.95           C
ANISOU 1217  CE1 PHE A  87     1899   2063   2477    429   -338   -165       C
ATOM   1218  CE2 PHE A  87      34.381 -48.263 -42.323  1.00 18.60           C
ANISOU 1218  CE2 PHE A  87     2159   2232   2677    465   -506   -186       C
ATOM   1219  CZ  PHE A  87      34.472 -48.050 -43.697  1.00 16.85           C
ANISOU 1219  CZ  PHE A  87     1881   2029   2491    453   -405   -178       C
ATOM   1220  H   PHE A  87      31.329 -43.391 -39.741  1.00  0.00           H
ATOM   1221  HA  PHE A  87      34.051 -44.269 -40.516  1.00  0.00           H
ATOM   1222  HB2 PHE A  87      31.373 -45.009 -41.754  1.00  0.00           H
ATOM   1223  HB3 PHE A  87      31.994 -45.809 -40.301  1.00  0.00           H
ATOM   1224  HD1 PHE A  87      32.682 -45.224 -43.904  1.00  0.00           H
ATOM   1225  HD2 PHE A  87      33.604 -47.573 -40.478  1.00  0.00           H
ATOM   1226  HE1 PHE A  87      34.006 -46.759 -45.295  1.00  0.00           H
ATOM   1227  HE2 PHE A  87      34.865 -49.119 -41.877  1.00  0.00           H
ATOM   1228  HZ  PHE A  87      34.997 -48.756 -44.324  1.00  0.00           H
ATOM   1229  N   VAL A  88      34.304 -42.910 -42.634  1.00 17.13           N
ANISOU 1229  N   VAL A  88     1879   2051   2580    372   -405   -192       N
ATOM   1230  CA  VAL A  88      34.501 -42.029 -43.778  1.00 17.62           C
ANISOU 1230  CA  VAL A  88     1886   2115   2694    353   -297   -185       C
ATOM   1231  C   VAL A  88      34.772 -42.835 -45.033  1.00 17.65           C
ANISOU 1231  C   VAL A  88     1865   2121   2720    367   -208   -175       C
ATOM   1232  O   VAL A  88      35.795 -43.538 -45.134  1.00 18.70           O
ANISOU 1232  O   VAL A  88     1935   2220   2950    383   -222   -194       O
ATOM   1233  CB  VAL A  88      35.630 -41.008 -43.561  1.00 19.42           C
ANISOU 1233  CB  VAL A  88     2021   2294   3065    343   -314   -214       C
ATOM   1234  CG1 VAL A  88      35.763 -40.126 -44.797  1.00 19.80           C
ANISOU 1234  CG1 VAL A  88     2028   2337   3159    326   -177   -200       C
ATOM   1235  CG2 VAL A  88      35.312 -40.148 -42.359  1.00 20.46           C
ANISOU 1235  CG2 VAL A  88     2189   2422   3164    334   -406   -226       C
ATOM   1236  H   VAL A  88      35.102 -43.404 -42.261  1.00  0.00           H
ATOM   1237  HA  VAL A  88      33.576 -41.474 -43.933  1.00  0.00           H
ATOM   1238  HB  VAL A  88      36.568 -41.536 -43.390  1.00  0.00           H
ATOM   1239 HG11 VAL A  88      35.992 -40.746 -45.664  1.00  0.00           H
ATOM   1240 HG12 VAL A  88      34.826 -39.596 -44.967  1.00  0.00           H
ATOM   1241 HG13 VAL A  88      36.566 -39.405 -44.644  1.00  0.00           H
ATOM   1242 HG21 VAL A  88      35.217 -40.779 -41.475  1.00  0.00           H
ATOM   1243 HG22 VAL A  88      36.115 -39.427 -42.206  1.00  0.00           H
ATOM   1244 HG23 VAL A  88      34.375 -39.618 -42.529  1.00  0.00           H
ATOM   1245  N   GLU A  89      33.823 -42.824 -45.961  1.00 16.89           N
ANISOU 1245  N   GLU A  89     1825   2059   2532    367   -127   -149       N
ATOM   1246  CA  GLU A  89      34.017 -43.513 -47.227  1.00 18.87           C
ANISOU 1246  CA  GLU A  89     2075   2306   2788    391    -42   -141       C
ATOM   1247  C   GLU A  89      34.627 -42.602 -48.268  1.00 18.38           C
ANISOU 1247  C   GLU A  89     1978   2214   2792    392     74   -136       C
ATOM   1248  O   GLU A  89      34.163 -41.462 -48.488  1.00 18.31           O
ANISOU 1248  O   GLU A  89     1994   2212   2750    377    117   -125       O
ATOM   1249  CB  GLU A  89      32.710 -44.055 -47.784  1.00 20.64           C
ANISOU 1249  CB  GLU A  89     2388   2570   2886    404    -24   -123       C
ATOM   1250  CG  GLU A  89      32.172 -45.243 -47.080  1.00 21.43           C
ANISOU 1250  CG  GLU A  89     2520   2686   2936    410   -102   -125       C
ATOM   1251  CD  GLU A  89      30.891 -45.811 -47.694  1.00 19.99           C
ANISOU 1251  CD  GLU A  89     2407   2528   2659    424    -84   -116       C
ATOM   1252  OE1 GLU A  89      30.017 -45.045 -48.228  1.00 19.17           O
ANISOU 1252  OE1 GLU A  89     2346   2438   2501    421    -48   -110       O
ATOM   1253  OE2 GLU A  89      30.735 -47.047 -47.581  1.00 18.08           O
ANISOU 1253  OE2 GLU A  89     2177   2287   2405    440   -116   -118       O
ATOM   1254  H   GLU A  89      32.958 -42.333 -45.786  1.00  0.00           H
ATOM   1255  HA  GLU A  89      34.695 -44.351 -47.063  1.00  0.00           H
ATOM   1256  HB2 GLU A  89      31.964 -43.262 -47.727  1.00  0.00           H
ATOM   1257  HB3 GLU A  89      32.861 -44.313 -48.832  1.00  0.00           H
ATOM   1258  HG2 GLU A  89      31.961 -44.962 -46.048  1.00  0.00           H
ATOM   1259  HG3 GLU A  89      32.934 -46.023 -47.080  1.00  0.00           H
ATOM   1260  N   ARG A  90      35.644 -43.140 -48.925  1.00 15.34           N
ANISOU 1260  N   ARG A  90     1503   1861   2464    526   -133   -150       N
ATOM   1261  CA  ARG A  90      36.423 -42.421 -49.936  1.00 17.78           C
ANISOU 1261  CA  ARG A  90     1787   2125   2844    532    -63   -124       C
ATOM   1262  C   ARG A  90      35.983 -42.753 -51.357  1.00 20.97           C
ANISOU 1262  C   ARG A  90     2226   2576   3166    558     14   -103       C
ATOM   1263  O   ARG A  90      35.621 -43.896 -51.676  1.00 19.73           O
ANISOU 1263  O   ARG A  90     2065   2470   2960    572     18   -126       O
ATOM   1264  CB  ARG A  90      37.919 -42.781 -49.792  1.00 17.14           C
ANISOU 1264  CB  ARG A  90     1621   1999   2891    491    -46   -127       C
ATOM   1265  CG  ARG A  90      38.468 -42.583 -48.397  1.00 17.55           C
ANISOU 1265  CG  ARG A  90     1651   2014   3004    451   -135   -146       C
ATOM   1266  CD  ARG A  90      38.212 -41.149 -47.898  1.00 18.78           C
ANISOU 1266  CD  ARG A  90     1839   2115   3180    451   -172   -142       C
ATOM   1267  NE  ARG A  90      39.065 -40.849 -46.750  1.00 18.03           N
ANISOU 1267  NE  ARG A  90     1703   1964   3182    409   -252   -164       N
ATOM   1268  CZ  ARG A  90      39.181 -39.636 -46.231  1.00 18.12           C
ANISOU 1268  CZ  ARG A  90     1744   1915   3225    385   -287   -167       C
ATOM   1269  NH1 ARG A  90      38.493 -38.627 -46.752  1.00 17.24           N
ANISOU 1269  NH1 ARG A  90     1703   1787   3061    404   -243   -144       N
ATOM   1270  NH2 ARG A  90      39.994 -39.419 -45.209  1.00 19.69           N
ANISOU 1270  NH2 ARG A  90     1907   2064   3509    342   -370   -192       N
ATOM   1271  H   ARG A  90      35.895 -44.096 -48.718  1.00  0.00           H
ATOM   1272  HA  ARG A  90      36.303 -41.350 -49.774  1.00  0.00           H
ATOM   1273  HB2 ARG A  90      38.490 -42.154 -50.477  1.00  0.00           H
ATOM   1274  HB3 ARG A  90      38.056 -43.824 -50.077  1.00  0.00           H
ATOM   1275  HG2 ARG A  90      37.983 -43.287 -47.721  1.00  0.00           H
ATOM   1276  HG3 ARG A  90      39.541 -42.774 -48.404  1.00  0.00           H
ATOM   1277  HD2 ARG A  90      38.430 -40.445 -48.701  1.00  0.00           H
ATOM   1278  HD3 ARG A  90      37.167 -41.050 -47.606  1.00  0.00           H
ATOM   1279  HE  ARG A  90      39.591 -41.603 -46.332  1.00  0.00           H
ATOM   1280 HH11 ARG A  90      37.878 -38.787 -47.537  1.00  0.00           H
ATOM   1281 HH12 ARG A  90      38.585 -37.699 -46.364  1.00  0.00           H
ATOM   1282 HH21 ARG A  90      40.525 -40.183 -44.815  1.00  0.00           H
ATOM   1283 HH22 ARG A  90      40.083 -38.490 -44.823  1.00  0.00           H
ATOM   1284  N   SER A  91      36.079 -41.774 -52.248  1.00 23.88           N
ANISOU 1284  N   SER A  91     2634   2919   3520    560     76    -58       N
ATOM   1285  CA  SER A  91      35.675 -42.010 -53.633  1.00 24.30           C
ANISOU 1285  CA  SER A  91     2738   3016   3479    585    145    -35       C
ATOM   1286  C   SER A  91      36.581 -43.044 -54.324  1.00 23.75           C
ANISOU 1286  C   SER A  91     2628   2957   3440    567    221    -49       C
ATOM   1287  O   SER A  91      36.183 -43.640 -55.335  1.00 25.13           O
ANISOU 1287  O   SER A  91     2845   3179   3524    588    265    -52       O
ATOM   1288  CB  SER A  91      35.687 -40.677 -54.424  1.00 26.09           C
ANISOU 1288  CB  SER A  91     3028   3203   3683    588    198     27       C
ATOM   1289  OG  SER A  91      37.024 -40.221 -54.559  1.00 28.54           O
ANISOU 1289  OG  SER A  91     3297   3446   4102    540    267     51       O
ATOM   1290  H   SER A  91      36.430 -40.869 -51.970  1.00  0.00           H
ATOM   1291  HA  SER A  91      34.656 -42.396 -53.630  1.00  0.00           H
ATOM   1292  HB2 SER A  91      35.101 -39.931 -53.888  1.00  0.00           H
ATOM   1293  HB3 SER A  91      35.256 -40.837 -55.412  1.00  0.00           H
ATOM   1294  HG  SER A  91      37.103 -39.343 -54.179  1.00  0.00           H
ATOM   1295  N   LYS A  92      37.793 -43.254 -53.812  1.00 21.19           N
ANISOU 1295  N   LYS A  92     2220   2587   3243    532    236    -61       N
ATOM   1296  CA  LYS A  92      38.707 -44.225 -54.422  1.00 21.56           C
ANISOU 1296  CA  LYS A  92     2217   2639   3338    524    315    -78       C
ATOM   1297  C   LYS A  92      38.466 -45.667 -54.007  1.00 20.86           C
ANISOU 1297  C   LYS A  92     2101   2585   3240    542    267   -131       C
ATOM   1298  O   LYS A  92      39.195 -46.547 -54.444  1.00 21.20           O
ANISOU 1298  O   LYS A  92     2102   2626   3329    544    327   -153       O
ATOM   1299  CB  LYS A  92      40.144 -43.909 -54.077  1.00 23.57           C
ANISOU 1299  CB  LYS A  92     2376   2830   3752    483    349    -69       C
ATOM   1300  CG  LYS A  92      40.472 -44.137 -52.593  1.00 26.80           C
ANISOU 1300  CG  LYS A  92     2713   3212   4259    468    235    -99       C
ATOM   1301  CD  LYS A  92      41.901 -43.674 -52.269  1.00 33.75           C
ANISOU 1301  CD  LYS A  92     3491   4027   5305    421    254    -88       C
ATOM   1302  CE  LYS A  92      42.121 -43.628 -50.767  1.00 39.54           C
ANISOU 1302  CE  LYS A  92     4205   4739   6080    388    116   -109       C
ATOM   1303  NZ  LYS A  92      43.521 -43.289 -50.424  1.00 44.47           N
ANISOU 1303  NZ  LYS A  92     4730   5305   6860    337    115   -103       N
ATOM   1304  H   LYS A  92      38.086 -42.738 -52.994  1.00  0.00           H
ATOM   1305  HA  LYS A  92      38.596 -44.161 -55.504  1.00  0.00           H
ATOM   1306  HB2 LYS A  92      40.337 -42.864 -54.318  1.00  0.00           H
ATOM   1307  HB3 LYS A  92      40.798 -44.536 -54.683  1.00  0.00           H
ATOM   1308  HG2 LYS A  92      40.382 -45.199 -52.367  1.00  0.00           H
ATOM   1309  HG3 LYS A  92      39.766 -43.578 -51.979  1.00  0.00           H
ATOM   1310  HD2 LYS A  92      42.612 -44.370 -52.714  1.00  0.00           H
ATOM   1311  HD3 LYS A  92      42.061 -42.680 -52.687  1.00  0.00           H
ATOM   1312  HE2 LYS A  92      41.461 -42.875 -50.337  1.00  0.00           H
ATOM   1313  HE3 LYS A  92      41.876 -44.601 -50.341  1.00  0.00           H
ATOM   1314  HZ1 LYS A  92      43.791 -42.444 -50.907  1.00  0.00           H
ATOM   1315  HZ2 LYS A  92      44.129 -44.045 -50.704  1.00  0.00           H
ATOM   1316  HZ3 LYS A  92      43.599 -43.147 -49.427  1.00  0.00           H
ATOM   1317  N   ALA A  93      37.470 -45.915 -53.166  1.00 19.71           N
ANISOU 1317  N   ALA A  93     1978   2467   3042    556    166   -152       N
ATOM   1318  CA  ALA A  93      37.214 -47.272 -52.697  1.00 19.52           C
ANISOU 1318  CA  ALA A  93     1950   2471   2994    555    118   -186       C
ATOM   1319  C   ALA A  93      36.897 -48.166 -53.890  1.00 21.08           C
ANISOU 1319  C   ALA A  93     2173   2705   3130    585    184   -216       C
ATOM   1320  O   ALA A  93      36.326 -47.716 -54.862  1.00 22.95           O
ANISOU 1320  O   ALA A  93     2476   2974   3271    597    225   -199       O
ATOM   1321  CB  ALA A  93      36.042 -47.285 -51.690  1.00 17.44           C
ANISOU 1321  CB  ALA A  93     1732   2235   2661    545     23   -186       C
ATOM   1322  H   ALA A  93      36.884 -45.157 -52.848  1.00  0.00           H
ATOM   1323  HA  ALA A  93      38.109 -47.649 -52.202  1.00  0.00           H
ATOM   1324  HB1 ALA A  93      35.865 -48.306 -51.351  1.00  0.00           H
ATOM   1325  HB2 ALA A  93      36.291 -46.656 -50.835  1.00  0.00           H
ATOM   1326  HB3 ALA A  93      35.143 -46.902 -52.173  1.00  0.00           H
ATOM   1327  N   PHE A  94      37.241 -49.452 -53.802  1.00 18.95           N
ANISOU 1327  N   PHE A  94     1894   2432   2873    572    183   -237       N
ATOM   1328  CA  PHE A  94      36.932 -50.393 -54.863  1.00 19.00           C
ANISOU 1328  CA  PHE A  94     1933   2467   2820    598    239   -279       C
ATOM   1329  C   PHE A  94      36.658 -51.761 -54.207  1.00 18.98           C
ANISOU 1329  C   PHE A  94     1939   2457   2816    577    177   -299       C
ATOM   1330  O   PHE A  94      37.133 -52.036 -53.100  1.00 16.88           O
ANISOU 1330  O   PHE A  94     1644   2160   2609    549    120   -279       O
ATOM   1331  CB  PHE A  94      38.116 -50.494 -55.858  1.00 19.04           C
ANISOU 1331  CB  PHE A  94     1913   2447   2873    606    362   -284       C
ATOM   1332  CG  PHE A  94      39.411 -50.970 -55.226  1.00 21.87           C
ANISOU 1332  CG  PHE A  94     2210   2764   3335    578    349   -271       C
ATOM   1333  CD1 PHE A  94      39.723 -52.323 -55.172  1.00 23.18           C
ANISOU 1333  CD1 PHE A  94     2374   2918   3515    582    342   -299       C
ATOM   1334  CD2 PHE A  94      40.315 -50.063 -54.696  1.00 24.39           C
ANISOU 1334  CD2 PHE A  94     2471   3050   3747    549    342   -237       C
ATOM   1335  CE1 PHE A  94      40.915 -52.759 -54.582  1.00 25.80           C
ANISOU 1335  CE1 PHE A  94     2645   3210   3947    565    325   -290       C
ATOM   1336  CE2 PHE A  94      41.488 -50.480 -54.111  1.00 25.96           C
ANISOU 1336  CE2 PHE A  94     2607   3212   4045    524    322   -233       C
ATOM   1337  CZ  PHE A  94      41.799 -51.829 -54.052  1.00 27.04           C
ANISOU 1337  CZ  PHE A  94     2741   3342   4191    536    313   -258       C
ATOM   1338  H   PHE A  94      37.727 -49.778 -52.979  1.00  0.00           H
ATOM   1339  HA  PHE A  94      36.040 -50.060 -55.394  1.00  0.00           H
ATOM   1340  HB2 PHE A  94      37.842 -51.194 -56.648  1.00  0.00           H
ATOM   1341  HB3 PHE A  94      38.284 -49.513 -56.303  1.00  0.00           H
ATOM   1342  HD1 PHE A  94      39.038 -53.046 -55.590  1.00  0.00           H
ATOM   1343  HD2 PHE A  94      40.094 -49.007 -54.743  1.00  0.00           H
ATOM   1344  HE1 PHE A  94      41.146 -53.813 -54.539  1.00  0.00           H
ATOM   1345  HE2 PHE A  94      42.170 -49.753 -53.696  1.00  0.00           H
ATOM   1346  HZ  PHE A  94      42.723 -52.155 -53.597  1.00  0.00           H
ATOM   1347  N   SER A  95      35.866 -52.572 -54.888  1.00 20.36           N
ANISOU 1347  N   SER A  95     2157   2665   2913    593    183   -346       N
ATOM   1348  CA  SER A  95      35.613 -53.972 -54.514  1.00 20.05           C
ANISOU 1348  CA  SER A  95     2127   2613   2879    580    143   -379       C
ATOM   1349  C   SER A  95      36.589 -54.880 -55.237  1.00 19.51           C
ANISOU 1349  C   SER A  95     2053   2507   2855    595    223   -407       C
ATOM   1350  O   SER A  95      37.008 -54.590 -56.375  1.00 19.61           O
ANISOU 1350  O   SER A  95     2081   2527   2843    619    320   -421       O
ATOM   1351  CB  SER A  95      34.200 -54.366 -54.950  1.00 21.01           C
ANISOU 1351  CB  SER A  95     2298   2794   2890    591    105   -425       C
ATOM   1352  OG  SER A  95      33.222 -53.591 -54.295  1.00 20.66           O
ANISOU 1352  OG  SER A  95     2257   2790   2803    582     34   -398       O
ATOM   1353  H   SER A  95      35.409 -52.209 -55.712  1.00  0.00           H
ATOM   1354  HA  SER A  95      35.718 -54.095 -53.436  1.00  0.00           H
ATOM   1355  HB2 SER A  95      34.036 -55.417 -54.712  1.00  0.00           H
ATOM   1356  HB3 SER A  95      34.106 -54.224 -56.027  1.00  0.00           H
ATOM   1357  HG  SER A  95      33.394 -53.589 -53.351  1.00  0.00           H
ATOM   1358  N   ASN A  96      36.992 -55.973 -54.600  1.00 19.41           N
ANISOU 1358  N   ASN A  96     2023   2452   2902    585    191   -413       N
ATOM   1359  CA  ASN A  96      37.894 -56.880 -55.280  1.00 20.47           C
ANISOU 1359  CA  ASN A  96     2155   2549   3075    607    264   -441       C
ATOM   1360  C   ASN A  96      37.637 -58.323 -54.912  1.00 20.78           C
ANISOU 1360  C   ASN A  96     2212   2553   3133    605    221   -479       C
ATOM   1361  O   ASN A  96      38.576 -59.100 -54.719  1.00 21.78           O
ANISOU 1361  O   ASN A  96     2311   2629   3334    617    235   -478       O
ATOM   1362  CB  ASN A  96      39.346 -56.509 -54.967  1.00 22.59           C
ANISOU 1362  CB  ASN A  96     2357   2787   3437    608    289   -399       C
ATOM   1363  CG  ASN A  96      40.307 -57.081 -55.972  1.00 27.63           C
ANISOU 1363  CG  ASN A  96     2989   3407   4103    638    388   -428       C
ATOM   1364  OD1 ASN A  96      39.917 -57.406 -57.092  1.00 30.12           O
ANISOU 1364  OD1 ASN A  96     3361   3738   4344    660    460   -473       O
ATOM   1365  ND2 ASN A  96      41.562 -57.227 -55.583  1.00 28.75           N
ANISOU 1365  ND2 ASN A  96     3063   3515   4344    638    392   -410       N
ATOM   1366  H   ASN A  96      36.676 -56.168 -53.661  1.00  0.00           H
ATOM   1367  HA  ASN A  96      37.740 -56.771 -56.353  1.00  0.00           H
ATOM   1368  HB2 ASN A  96      39.439 -55.423 -54.971  1.00  0.00           H
ATOM   1369  HB3 ASN A  96      39.603 -56.884 -53.976  1.00  0.00           H
ATOM   1370 HD21 ASN A  96      42.246 -57.613 -56.218  1.00  0.00           H
ATOM   1371 HD22 ASN A  96      41.837 -56.952 -54.651  1.00  0.00           H
ATOM   1372  N   CYS A  97      36.374 -58.700 -54.868  1.00 19.65           N
ANISOU 1372  N   CYS A  97     2110   2435   2922    594    169   -518       N
ATOM   1373  CA  CYS A  97      36.017 -60.046 -54.460  1.00 19.80           C
ANISOU 1373  CA  CYS A  97     2146   2415   2962    590    123   -558       C
ATOM   1374  C   CYS A  97      34.918 -60.516 -55.398  1.00 19.14           C
ANISOU 1374  C   CYS A  97     2128   2366   2779    592    132   -636       C
ATOM   1375  O   CYS A  97      34.851 -60.071 -56.544  1.00 20.19           O
ANISOU 1375  O   CYS A  97     2299   2537   2836    605    196   -661       O
ATOM   1376  CB  CYS A  97      35.600 -60.052 -52.978  1.00 19.68           C
ANISOU 1376  CB  CYS A  97     2106   2394   2979    564     20   -520       C
ATOM   1377  SG  CYS A  97      35.477 -61.670 -52.132  1.00 24.24           S
ANISOU 1377  SG  CYS A  97     2694   2896   3619    560    -42   -545       S
ATOM   1378  H   CYS A  97      35.648 -58.045 -55.121  1.00  0.00           H
ATOM   1379  HA  CYS A  97      36.885 -60.693 -54.584  1.00  0.00           H
ATOM   1380  HB2 CYS A  97      34.621 -59.577 -52.914  1.00  0.00           H
ATOM   1381  HB3 CYS A  97      36.310 -59.436 -52.426  1.00  0.00           H
ATOM   1382  N   TYR A  98      34.099 -61.457 -54.960  1.00 16.93           N
ANISOU 1382  N   TYR A  98     1869   2069   2493    577     68   -679       N
ATOM   1383  CA  TYR A  98      33.103 -62.016 -55.856  1.00 16.65           C
ANISOU 1383  CA  TYR A  98     1910   2063   2353    548     65   -735       C
ATOM   1384  C   TYR A  98      32.103 -60.896 -56.177  1.00 17.11           C
ANISOU 1384  C   TYR A  98     1983   2219   2301    527     35   -708       C
ATOM   1385  O   TYR A  98      31.737 -60.113 -55.284  1.00 16.85           O
ANISOU 1385  O   TYR A  98     1906   2218   2278    516    -16   -653       O
ATOM   1386  CB  TYR A  98      32.408 -63.212 -55.213  1.00 17.02           C
ANISOU 1386  CB  TYR A  98     1979   2068   2419    507     -3   -756       C
ATOM   1387  CG  TYR A  98      31.850 -64.207 -56.218  1.00 19.24           C
ANISOU 1387  CG  TYR A  98     2338   2335   2636    484      9   -836       C
ATOM   1388  CD1 TYR A  98      30.636 -63.978 -56.835  1.00 20.90           C
ANISOU 1388  CD1 TYR A  98     2589   2620   2731    442    -29   -859       C
ATOM   1389  CD2 TYR A  98      32.575 -65.345 -56.595  1.00 19.71           C
ANISOU 1389  CD2 TYR A  98     2431   2305   2754    509     56   -894       C
ATOM   1390  CE1 TYR A  98      30.124 -64.862 -57.764  1.00 21.40           C
ANISOU 1390  CE1 TYR A  98     2727   2672   2731    415    -31   -937       C
ATOM   1391  CE2 TYR A  98      32.059 -66.251 -57.556  1.00 21.61           C
ANISOU 1391  CE2 TYR A  98     2755   2526   2928    485     66   -978       C
ATOM   1392  CZ  TYR A  98      30.841 -65.986 -58.129  1.00 22.03           C
ANISOU 1392  CZ  TYR A  98     2850   2659   2861    434     19   -999       C
ATOM   1393  OH  TYR A  98      30.283 -66.824 -59.057  1.00 22.30           O
ANISOU 1393  OH  TYR A  98     2969   2679   2825    403     13  -1085       O
ATOM   1394  H   TYR A  98      34.166 -61.785 -54.007  1.00  0.00           H
ATOM   1395  HA  TYR A  98      33.589 -62.337 -56.777  1.00  0.00           H
ATOM   1396  HB2 TYR A  98      33.129 -63.730 -54.580  1.00  0.00           H
ATOM   1397  HB3 TYR A  98      31.591 -62.849 -54.589  1.00  0.00           H
ATOM   1398  HD1 TYR A  98      30.075 -63.089 -56.586  1.00  0.00           H
ATOM   1399  HD2 TYR A  98      33.540 -65.535 -56.148  1.00  0.00           H
ATOM   1400  HE1 TYR A  98      29.158 -64.674 -58.208  1.00  0.00           H
ATOM   1401  HE2 TYR A  98      32.615 -67.135 -57.832  1.00  0.00           H
ATOM   1402  HH  TYR A  98      30.172 -66.354 -59.887  1.00  0.00           H
ATOM   1403  N   PRO A  99      31.687 -60.782 -57.450  1.00 18.36           N
ANISOU 1403  N   PRO A  99     2205   2421   2352    527     66   -747       N
ATOM   1404  CA  PRO A  99      30.746 -59.689 -57.774  1.00 17.93           C
ANISOU 1404  CA  PRO A  99     2162   2455   2196    517     28   -715       C
ATOM   1405  C   PRO A  99      29.369 -59.920 -57.162  1.00 17.75           C
ANISOU 1405  C   PRO A  99     2126   2472   2145    469    -71   -714       C
ATOM   1406  O   PRO A  99      28.859 -61.041 -57.223  1.00 18.76           O
ANISOU 1406  O   PRO A  99     2281   2578   2270    433   -102   -764       O
ATOM   1407  CB  PRO A  99      30.695 -59.698 -59.310  1.00 19.65           C
ANISOU 1407  CB  PRO A  99     2464   2702   2302    529     78   -760       C
ATOM   1408  CG  PRO A  99      31.315 -60.978 -59.731  1.00 21.82           C
ANISOU 1408  CG  PRO A  99     2777   2907   2607    533    131   -832       C
ATOM   1409  CD  PRO A  99      32.246 -61.417 -58.656  1.00 20.83           C
ANISOU 1409  CD  PRO A  99     2580   2704   2630    549    147   -812       C
ATOM   1410  HA  PRO A  99      31.150 -58.739 -57.424  1.00  0.00           H
ATOM   1411  HB2 PRO A  99      31.256 -58.855 -59.713  1.00  0.00           H
ATOM   1412  HB3 PRO A  99      29.660 -59.654 -59.650  1.00  0.00           H
ATOM   1413  HG2 PRO A  99      30.542 -61.731 -59.880  1.00  0.00           H
ATOM   1414  HG3 PRO A  99      31.868 -60.831 -60.659  1.00  0.00           H
ATOM   1415  HD2 PRO A  99      33.260 -61.066 -58.849  1.00  0.00           H
ATOM   1416  HD3 PRO A  99      32.231 -62.502 -58.558  1.00  0.00           H
ATOM   1417  N   TYR A 100      28.792 -58.875 -56.569  1.00 16.98           N
ANISOU 1417  N   TYR A 100     1987   2428   2037    470   -114   -659       N
ATOM   1418  CA  TYR A 100      27.635 -59.020 -55.720  1.00 18.50           C
ANISOU 1418  CA  TYR A 100     2145   2653   2232    429   -190   -648       C
ATOM   1419  C   TYR A 100      26.707 -57.818 -55.876  1.00 19.67           C
ANISOU 1419  C   TYR A 100     2276   2884   2314    441   -229   -614       C
ATOM   1420  O   TYR A 100      27.117 -56.751 -56.365  1.00 19.62           O
ANISOU 1420  O   TYR A 100     2282   2896   2278    482   -197   -582       O
ATOM   1421  CB  TYR A 100      28.033 -59.187 -54.254  1.00 18.22           C
ANISOU 1421  CB  TYR A 100     2061   2570   2293    421   -202   -612       C
ATOM   1422  CG  TYR A 100      28.587 -57.931 -53.604  1.00 18.29           C
ANISOU 1422  CG  TYR A 100     2031   2585   2333    456   -190   -553       C
ATOM   1423  CD1 TYR A 100      29.933 -57.640 -53.668  1.00 18.80           C
ANISOU 1423  CD1 TYR A 100     2087   2601   2456    491   -137   -538       C
ATOM   1424  CD2 TYR A 100      27.741 -57.034 -52.930  1.00 19.03           C
ANISOU 1424  CD2 TYR A 100     2094   2732   2405    453   -230   -517       C
ATOM   1425  CE1 TYR A 100      30.448 -56.501 -53.089  1.00 20.78           C
ANISOU 1425  CE1 TYR A 100     2304   2851   2742    514   -132   -490       C
ATOM   1426  CE2 TYR A 100      28.242 -55.887 -52.350  1.00 19.24           C
ANISOU 1426  CE2 TYR A 100     2095   2755   2459    482   -221   -472       C
ATOM   1427  CZ  TYR A 100      29.577 -55.608 -52.449  1.00 21.06           C
ANISOU 1427  CZ  TYR A 100     2322   2934   2744    509   -176   -458       C
ATOM   1428  OH  TYR A 100      30.090 -54.486 -51.851  1.00 22.39           O
ANISOU 1428  OH  TYR A 100     2472   3090   2946    522   -173   -413       O
ATOM   1429  H   TYR A 100      29.177 -57.953 -56.719  1.00  0.00           H
ATOM   1430  HA  TYR A 100      27.093 -59.913 -56.031  1.00  0.00           H
ATOM   1431  HB2 TYR A 100      27.150 -59.498 -53.695  1.00  0.00           H
ATOM   1432  HB3 TYR A 100      28.784 -59.974 -54.185  1.00  0.00           H
ATOM   1433  HD1 TYR A 100      30.597 -58.319 -54.182  1.00  0.00           H
ATOM   1434  HD2 TYR A 100      26.684 -57.246 -52.865  1.00  0.00           H
ATOM   1435  HE1 TYR A 100      31.508 -56.299 -53.128  1.00  0.00           H
ATOM   1436  HE2 TYR A 100      27.584 -55.214 -51.821  1.00  0.00           H
ATOM   1437  HH  TYR A 100      31.047 -54.489 -51.932  1.00  0.00           H
ATOM   1438  N   ASP A 101      25.466 -57.988 -55.486  1.00 20.72           N
ANISOU 1438  N   ASP A 101     2379   3063   2431    405   -293   -619       N
ATOM   1439  CA  ASP A 101      24.620 -56.802 -55.272  1.00 23.85           C
ANISOU 1439  CA  ASP A 101     2737   3529   2797    426   -329   -578       C
ATOM   1440  C   ASP A 101      23.893 -56.992 -53.958  1.00 21.77           C
ANISOU 1440  C   ASP A 101     2412   3274   2585    392   -360   -563       C
ATOM   1441  O   ASP A 101      23.838 -58.097 -53.421  1.00 23.18           O
ANISOU 1441  O   ASP A 101     2588   3417   2804    344   -365   -585       O
ATOM   1442  CB  ASP A 101      23.655 -56.563 -56.435  1.00 30.50           C
ANISOU 1442  CB  ASP A 101     3600   4442   3547    429   -376   -599       C
ATOM   1443  CG  ASP A 101      22.452 -57.479 -56.397  1.00 36.67           C
ANISOU 1443  CG  ASP A 101     4353   5257   4323    370   -441   -642       C
ATOM   1444  OD1 ASP A 101      22.667 -58.673 -56.535  1.00 37.97           O
ANISOU 1444  OD1 ASP A 101     4548   5377   4503    327   -435   -689       O
ATOM   1445  OD2 ASP A 101      21.293 -57.006 -56.252  1.00 40.20           O
ANISOU 1445  OD2 ASP A 101     4744   5771   4757    367   -498   -630       O
ATOM   1446  H   ASP A 101      25.097 -58.916 -55.335  1.00  0.00           H
ATOM   1447  HA  ASP A 101      25.269 -55.931 -55.181  1.00  0.00           H
ATOM   1448  HB2 ASP A 101      23.308 -55.531 -56.393  1.00  0.00           H
ATOM   1449  HB3 ASP A 101      24.188 -56.718 -57.373  1.00  0.00           H
ATOM   1450  N   VAL A 102      23.368 -55.901 -53.414  1.00 17.79           N
ANISOU 1450  N   VAL A 102     1867   2814   2080    418   -375   -524       N
ATOM   1451  CA  VAL A 102      22.622 -55.950 -52.188  1.00 16.49           C
ANISOU 1451  CA  VAL A 102     1647   2666   1952    392   -391   -510       C
ATOM   1452  C   VAL A 102      21.309 -55.257 -52.482  1.00 18.03           C
ANISOU 1452  C   VAL A 102     1824   2911   2117    390   -402   -490       C
ATOM   1453  O   VAL A 102      21.305 -54.035 -52.646  1.00 18.59           O
ANISOU 1453  O   VAL A 102     1907   2986   2171    435   -387   -454       O
ATOM   1454  CB  VAL A 102      23.345 -55.178 -51.094  1.00 16.95           C
ANISOU 1454  CB  VAL A 102     1713   2677   2050    413   -351   -462       C
ATOM   1455  CG1 VAL A 102      22.611 -55.317 -49.775  1.00 16.29           C
ANISOU 1455  CG1 VAL A 102     1607   2593   1990    374   -344   -443       C
ATOM   1456  CG2 VAL A 102      24.790 -55.665 -50.971  1.00 19.66           C
ANISOU 1456  CG2 VAL A 102     2082   2951   2436    422   -329   -466       C
ATOM   1457  H   VAL A 102      23.497 -55.012 -53.875  1.00  0.00           H
ATOM   1458  HA  VAL A 102      22.452 -56.982 -51.882  1.00  0.00           H
ATOM   1459  HB  VAL A 102      23.360 -54.124 -51.370  1.00  0.00           H
ATOM   1460 HG11 VAL A 102      23.141 -54.759 -49.003  1.00  0.00           H
ATOM   1461 HG12 VAL A 102      21.600 -54.923 -49.879  1.00  0.00           H
ATOM   1462 HG13 VAL A 102      22.563 -56.369 -49.495  1.00  0.00           H
ATOM   1463 HG21 VAL A 102      25.297 -55.105 -50.185  1.00  0.00           H
ATOM   1464 HG22 VAL A 102      24.796 -56.726 -50.722  1.00  0.00           H
ATOM   1465 HG23 VAL A 102      25.307 -55.511 -51.918  1.00  0.00           H
ATOM   1466  N   PRO A 103      20.221 -56.023 -52.633  1.00 20.55           N
ANISOU 1466  N   PRO A 103     2112   3260   2435    340   -432   -514       N
ATOM   1467  CA  PRO A 103      18.924 -55.353 -52.697  1.00 22.66           C
ANISOU 1467  CA  PRO A 103     2342   3571   2697    341   -444   -491       C
ATOM   1468  C   PRO A 103      18.796 -54.462 -51.427  1.00 22.21           C
ANISOU 1468  C   PRO A 103     2267   3501   2672    360   -401   -449       C
ATOM   1469  O   PRO A 103      19.060 -54.853 -50.284  1.00 22.22           O
ANISOU 1469  O   PRO A 103     2258   3479   2704    335   -376   -445       O
ATOM   1470  CB  PRO A 103      17.915 -56.502 -52.679  1.00 23.78           C
ANISOU 1470  CB  PRO A 103     2440   3737   2859    270   -477   -523       C
ATOM   1471  CG  PRO A 103      18.739 -57.743 -53.155  1.00 23.38           C
ANISOU 1471  CG  PRO A 103     2432   3654   2799    235   -494   -575       C
ATOM   1472  CD  PRO A 103      20.119 -57.498 -52.698  1.00 21.23           C
ANISOU 1472  CD  PRO A 103     2195   3337   2536    276   -458   -565       C
ATOM   1473  HA  PRO A 103      18.831 -54.760 -53.607  1.00  0.00           H
ATOM   1474  HB2 PRO A 103      17.526 -56.659 -51.673  1.00  0.00           H
ATOM   1475  HB3 PRO A 103      17.099 -56.300 -53.373  1.00  0.00           H
ATOM   1476  HG2 PRO A 103      18.707 -57.828 -54.241  1.00  0.00           H
ATOM   1477  HG3 PRO A 103      18.348 -58.651 -52.696  1.00  0.00           H
ATOM   1478  HD2 PRO A 103      20.286 -57.941 -51.716  1.00  0.00           H
ATOM   1479  HD3 PRO A 103      20.833 -57.896 -53.419  1.00  0.00           H
ATOM   1480  N   ASP A 104      18.362 -53.252 -51.624  1.00 23.27           N
ANISOU 1480  N   ASP A 104     2400   3649   2793    403   -397   -420       N
ATOM   1481  CA  ASP A 104      18.333 -52.304 -50.495  1.00 20.57           C
ANISOU 1481  CA  ASP A 104     2055   3287   2472    425   -358   -390       C
ATOM   1482  C   ASP A 104      19.703 -52.080 -49.813  1.00 17.70           C
ANISOU 1482  C   ASP A 104     1742   2866   2117    436   -326   -376       C
ATOM   1483  O   ASP A 104      19.809 -51.979 -48.574  1.00 18.00           O
ANISOU 1483  O   ASP A 104     1776   2887   2175    427   -302   -368       O
ATOM   1484  CB  ASP A 104      17.293 -52.676 -49.447  1.00 20.15           C
ANISOU 1484  CB  ASP A 104     1939   3267   2451    392   -347   -395       C
ATOM   1485  CG  ASP A 104      16.678 -51.393 -48.751  1.00 38.50           C
ANISOU 1485  CG  ASP A 104     4245   5599   4784    433   -321   -372       C
ATOM   1486  OD1 ASP A 104      17.108 -50.199 -49.038  1.00 35.09           O
ANISOU 1486  OD1 ASP A 104     3857   5139   4339    483   -317   -350       O
ATOM   1487  OD2 ASP A 104      15.770 -51.588 -47.909  1.00 39.75           O
ANISOU 1487  OD2 ASP A 104     4342   5794   4967    416   -304   -380       O
ATOM   1488  H   ASP A 104      18.048 -52.965 -52.540  1.00  0.00           H
ATOM   1489  HA  ASP A 104      18.029 -51.341 -50.906  1.00  0.00           H
ATOM   1490  HB2 ASP A 104      16.491 -53.235 -49.929  1.00  0.00           H
ATOM   1491  HB3 ASP A 104      17.760 -53.304 -48.688  1.00  0.00           H
ATOM   1492  N   TYR A 105      20.730 -51.971 -50.649  1.00 15.79           N
ANISOU 1492  N   TYR A 105     1542   2599   1858    458   -330   -376       N
ATOM   1493  CA  TYR A 105      22.080 -51.605 -50.236  1.00 13.93           C
ANISOU 1493  CA  TYR A 105     1346   2307   1639    471   -305   -360       C
ATOM   1494  C   TYR A 105      22.058 -50.423 -49.281  1.00 13.62           C
ANISOU 1494  C   TYR A 105     1320   2242   1614    485   -283   -330       C
ATOM   1495  O   TYR A 105      22.706 -50.429 -48.252  1.00 14.20           O
ANISOU 1495  O   TYR A 105     1406   2277   1710    473   -269   -323       O
ATOM   1496  CB  TYR A 105      22.865 -51.225 -51.474  1.00 14.11           C
ANISOU 1496  CB  TYR A 105     1398   2327   1637    509   -308   -358       C
ATOM   1497  CG  TYR A 105      24.321 -50.928 -51.235  1.00 14.17           C
ANISOU 1497  CG  TYR A 105     1434   2276   1675    519   -281   -341       C
ATOM   1498  CD1 TYR A 105      24.720 -49.690 -50.739  1.00 14.65           C
ANISOU 1498  CD1 TYR A 105     1514   2298   1754    531   -262   -305       C
ATOM   1499  CD2 TYR A 105      25.298 -51.860 -51.548  1.00 15.56           C
ANISOU 1499  CD2 TYR A 105     1609   2431   1871    517   -277   -365       C
ATOM   1500  CE1 TYR A 105      26.053 -49.409 -50.513  1.00 16.90           C
ANISOU 1500  CE1 TYR A 105     1814   2526   2079    530   -241   -289       C
ATOM   1501  CE2 TYR A 105      26.656 -51.579 -51.356  1.00 17.33           C
ANISOU 1501  CE2 TYR A 105     1848   2595   2141    522   -246   -346       C
ATOM   1502  CZ  TYR A 105      27.022 -50.331 -50.824  1.00 17.27           C
ANISOU 1502  CZ  TYR A 105     1857   2553   2154    524   -231   -305       C
ATOM   1503  OH  TYR A 105      28.334 -50.021 -50.594  1.00 16.24           O
ANISOU 1503  OH  TYR A 105     1728   2363   2077    520   -207   -286       O
ATOM   1504  H   TYR A 105      20.566 -52.152 -51.629  1.00  0.00           H
ATOM   1505  HA  TYR A 105      22.556 -52.457 -49.750  1.00  0.00           H
ATOM   1506  HB2 TYR A 105      22.800 -52.051 -52.183  1.00  0.00           H
ATOM   1507  HB3 TYR A 105      22.401 -50.346 -51.922  1.00  0.00           H
ATOM   1508  HD1 TYR A 105      23.975 -48.937 -50.528  1.00  0.00           H
ATOM   1509  HD2 TYR A 105      25.006 -52.820 -51.947  1.00  0.00           H
ATOM   1510  HE1 TYR A 105      26.336 -48.457 -50.088  1.00  0.00           H
ATOM   1511  HE2 TYR A 105      27.409 -52.309 -51.612  1.00  0.00           H
ATOM   1512  HH  TYR A 105      28.896 -50.675 -51.015  1.00  0.00           H
ATOM   1513  N   ALA A 106      21.275 -49.388 -49.594  1.00 13.31           N
ANISOU 1513  N   ALA A 106     1274   2224   1559    515   -286   -315       N
ATOM   1514  CA  ALA A 106      21.331 -48.189 -48.774  1.00 13.24           C
ANISOU 1514  CA  ALA A 106     1281   2187   1564    536   -268   -294       C
ATOM   1515  C   ALA A 106      20.907 -48.466 -47.345  1.00 13.68           C
ANISOU 1515  C   ALA A 106     1315   2250   1632    518   -254   -307       C
ATOM   1516  O   ALA A 106      21.454 -47.880 -46.418  1.00 14.38           O
ANISOU 1516  O   ALA A 106     1427   2305   1732    527   -243   -302       O
ATOM   1517  CB  ALA A 106      20.447 -47.105 -49.375  1.00 12.73           C
ANISOU 1517  CB  ALA A 106     1207   2143   1486    578   -278   -279       C
ATOM   1518  H   ALA A 106      20.653 -49.437 -50.388  1.00  0.00           H
ATOM   1519  HA  ALA A 106      22.359 -47.827 -48.764  1.00  0.00           H
ATOM   1520  HB1 ALA A 106      20.495 -46.210 -48.754  1.00  0.00           H
ATOM   1521  HB2 ALA A 106      20.795 -46.868 -50.380  1.00  0.00           H
ATOM   1522  HB3 ALA A 106      19.417 -47.460 -49.421  1.00  0.00           H
ATOM   1523  N   SER A 107      19.914 -49.339 -47.176  1.00 12.22           N
ANISOU 1523  N   SER A 107     1082   2115   1447    497   -259   -326       N
ATOM   1524  CA  SER A 107      19.432 -49.643 -45.851  1.00 11.93           C
ANISOU 1524  CA  SER A 107     1015   2102   1417    485   -242   -339       C
ATOM   1525  C   SER A 107      20.434 -50.475 -45.075  1.00 12.03           C
ANISOU 1525  C   SER A 107     1049   2086   1436    459   -243   -345       C
ATOM   1526  O   SER A 107      20.620 -50.266 -43.899  1.00 12.86           O
ANISOU 1526  O   SER A 107     1159   2190   1537    470   -233   -350       O
ATOM   1527  CB  SER A 107      18.106 -50.402 -45.913  1.00 12.12           C
ANISOU 1527  CB  SER A 107      966   2191   1448    462   -243   -356       C
ATOM   1528  OG  SER A 107      17.050 -49.504 -46.180  1.00 13.64           O
ANISOU 1528  OG  SER A 107     1125   2412   1645    495   -241   -351       O
ATOM   1529  H   SER A 107      19.498 -49.789 -47.979  1.00  0.00           H
ATOM   1530  HA  SER A 107      19.271 -48.706 -45.317  1.00  0.00           H
ATOM   1531  HB2 SER A 107      18.154 -51.149 -46.705  1.00  0.00           H
ATOM   1532  HB3 SER A 107      17.927 -50.897 -44.959  1.00  0.00           H
ATOM   1533  HG  SER A 107      16.221 -49.987 -46.215  1.00  0.00           H
ATOM   1534  N   LEU A 108      21.076 -51.455 -45.706  1.00 12.07           N
ANISOU 1534  N   LEU A 108     1065   2072   1450    431   -260   -348       N
ATOM   1535  CA  LEU A 108      22.073 -52.245 -44.951  1.00 11.95           C
ANISOU 1535  CA  LEU A 108     1069   2021   1451    412   -271   -350       C
ATOM   1536  C   LEU A 108      23.229 -51.348 -44.516  1.00 12.28           C
ANISOU 1536  C   LEU A 108     1160   2004   1503    436   -271   -332       C
ATOM   1537  O   LEU A 108      23.720 -51.417 -43.373  1.00 12.70           O
ANISOU 1537  O   LEU A 108     1226   2039   1559    438   -284   -332       O
ATOM   1538  CB  LEU A 108      22.596 -53.403 -45.815  1.00 11.06           C
ANISOU 1538  CB  LEU A 108      957   1889   1354    387   -290   -361       C
ATOM   1539  CG  LEU A 108      23.685 -54.271 -45.141  1.00 12.91           C
ANISOU 1539  CG  LEU A 108     1211   2075   1618    372   -311   -360       C
ATOM   1540  CD1 LEU A 108      23.214 -54.812 -43.831  1.00 12.05           C
ANISOU 1540  CD1 LEU A 108     1087   1988   1501    348   -321   -360       C
ATOM   1541  CD2 LEU A 108      24.133 -55.411 -46.080  1.00 15.35           C
ANISOU 1541  CD2 LEU A 108     1516   2366   1950    357   -329   -382       C
ATOM   1542  H   LEU A 108      20.887 -51.655 -46.678  1.00  0.00           H
ATOM   1543  HA  LEU A 108      21.595 -52.658 -44.063  1.00  0.00           H
ATOM   1544  HB2 LEU A 108      23.015 -52.982 -46.729  1.00  0.00           H
ATOM   1545  HB3 LEU A 108      21.756 -54.045 -46.081  1.00  0.00           H
ATOM   1546  HG  LEU A 108      24.549 -53.635 -44.950  1.00  0.00           H
ATOM   1547 HD11 LEU A 108      22.904 -53.989 -43.188  1.00  0.00           H
ATOM   1548 HD12 LEU A 108      24.025 -55.361 -43.352  1.00  0.00           H
ATOM   1549 HD13 LEU A 108      22.370 -55.481 -43.997  1.00  0.00           H
ATOM   1550 HD21 LEU A 108      24.471 -54.991 -47.027  1.00  0.00           H
ATOM   1551 HD22 LEU A 108      23.294 -56.084 -46.260  1.00  0.00           H
ATOM   1552 HD23 LEU A 108      24.949 -55.964 -45.616  1.00  0.00           H
ATOM   1553  N   ARG A 109      23.697 -50.526 -45.442  1.00 12.14           N
ANISOU 1553  N   ARG A 109     1166   1959   1488    452   -264   -318       N
ATOM   1554  CA  ARG A 109      24.777 -49.560 -45.157  1.00 11.53           C
ANISOU 1554  CA  ARG A 109     1123   1827   1430    467   -264   -302       C
ATOM   1555  C   ARG A 109      24.387 -48.648 -44.015  1.00 12.82           C
ANISOU 1555  C   ARG A 109     1294   1997   1580    490   -263   -308       C
ATOM   1556  O   ARG A 109      25.159 -48.386 -43.102  1.00 13.36           O
ANISOU 1556  O   ARG A 109     1384   2031   1661    495   -280   -311       O
ATOM   1557  CB  ARG A 109      25.052 -48.737 -46.392  1.00 11.24           C
ANISOU 1557  CB  ARG A 109     1098   1778   1394    484   -252   -285       C
ATOM   1558  CG  ARG A 109      26.114 -47.591 -46.211  1.00 12.69           C
ANISOU 1558  CG  ARG A 109     1306   1908   1608    497   -250   -266       C
ATOM   1559  CD  ARG A 109      26.403 -46.917 -47.548  1.00 12.86           C
ANISOU 1559  CD  ARG A 109     1332   1923   1630    519   -236   -246       C
ATOM   1560  NE  ARG A 109      27.279 -45.743 -47.477  1.00 13.23           N
ANISOU 1560  NE  ARG A 109     1393   1921   1712    534   -231   -226       N
ATOM   1561  CZ  ARG A 109      26.897 -44.521 -47.103  1.00 13.29           C
ANISOU 1561  CZ  ARG A 109     1415   1917   1718    561   -232   -220       C
ATOM   1562  NH1 ARG A 109      25.650 -44.277 -46.711  1.00 13.55           N
ANISOU 1562  NH1 ARG A 109     1447   1986   1717    577   -235   -232       N
ATOM   1563  NH2 ARG A 109      27.781 -43.516 -47.118  1.00 12.65           N
ANISOU 1563  NH2 ARG A 109     1345   1785   1678    575   -229   -204       N
ATOM   1564  H   ARG A 109      23.304 -50.561 -46.372  1.00  0.00           H
ATOM   1565  HA  ARG A 109      25.680 -50.106 -44.884  1.00  0.00           H
ATOM   1566  HB2 ARG A 109      24.114 -48.280 -46.708  1.00  0.00           H
ATOM   1567  HB3 ARG A 109      25.395 -49.404 -47.182  1.00  0.00           H
ATOM   1568  HG2 ARG A 109      27.037 -48.016 -45.816  1.00  0.00           H
ATOM   1569  HG3 ARG A 109      25.729 -46.851 -45.510  1.00  0.00           H
ATOM   1570  HD2 ARG A 109      26.875 -47.651 -48.201  1.00  0.00           H
ATOM   1571  HD3 ARG A 109      25.456 -46.615 -47.995  1.00  0.00           H
ATOM   1572  HE  ARG A 109      28.248 -45.870 -47.731  1.00  0.00           H
ATOM   1573 HH11 ARG A 109      25.382 -43.344 -46.431  1.00  0.00           H
ATOM   1574 HH12 ARG A 109      24.971 -45.024 -46.693  1.00  0.00           H
ATOM   1575 HH21 ARG A 109      27.497 -42.589 -46.835  1.00  0.00           H
ATOM   1576 HH22 ARG A 109      28.732 -43.685 -47.412  1.00  0.00           H
ATOM   1577  N   SER A 110      23.159 -48.158 -44.057  1.00 14.02           N
ANISOU 1577  N   SER A 110     1424   2195   1708    511   -247   -315       N
ATOM   1578  CA  SER A 110      22.694 -47.263 -43.008  1.00 15.19           C
ANISOU 1578  CA  SER A 110     1575   2356   1842    546   -239   -330       C
ATOM   1579  C   SER A 110      22.666 -47.937 -41.623  1.00 16.07           C
ANISOU 1579  C   SER A 110     1678   2493   1935    550   -247   -355       C
ATOM   1580  O   SER A 110      23.115 -47.362 -40.607  1.00 15.07           O
ANISOU 1580  O   SER A 110     1581   2348   1798    581   -260   -372       O
ATOM   1581  CB  SER A 110      21.279 -46.760 -43.312  1.00 14.36           C
ANISOU 1581  CB  SER A 110     1434   2300   1724    570   -217   -333       C
ATOM   1582  OG  SER A 110      20.826 -46.012 -42.186  1.00 15.48           O
ANISOU 1582  OG  SER A 110     1575   2454   1852    610   -199   -355       O
ATOM   1583  H   SER A 110      22.543 -48.405 -44.818  1.00  0.00           H
ATOM   1584  HA  SER A 110      23.364 -46.405 -42.962  1.00  0.00           H
ATOM   1585  HB2 SER A 110      20.615 -47.607 -43.485  1.00  0.00           H
ATOM   1586  HB3 SER A 110      21.298 -46.121 -44.195  1.00  0.00           H
ATOM   1587  HG  SER A 110      19.879 -45.868 -42.256  1.00  0.00           H
ATOM   1588  N   LEU A 111      22.102 -49.140 -41.566  1.00 15.39           N
ANISOU 1588  N   LEU A 111     1551   2454   1842    523   -243   -361       N
ATOM   1589  CA  LEU A 111      21.884 -49.762 -40.274  1.00 14.10           C
ANISOU 1589  CA  LEU A 111     1394   2316   1649    507   -235   -371       C
ATOM   1590  C   LEU A 111      23.210 -50.225 -39.673  1.00 13.01           C
ANISOU 1590  C   LEU A 111     1325   2107   1513    477   -277   -354       C
ATOM   1591  O   LEU A 111      23.404 -50.126 -38.467  1.00 13.31           O
ANISOU 1591  O   LEU A 111     1422   2124   1511    465   -278   -354       O
ATOM   1592  CB  LEU A 111      20.838 -50.880 -40.360  1.00 14.68           C
ANISOU 1592  CB  LEU A 111     1419   2443   1717    458   -206   -371       C
ATOM   1593  CG  LEU A 111      21.201 -52.190 -41.033  1.00 15.60           C
ANISOU 1593  CG  LEU A 111     1528   2541   1858    407   -234   -359       C
ATOM   1594  CD1 LEU A 111      21.885 -53.145 -40.067  1.00 17.25           C
ANISOU 1594  CD1 LEU A 111     1804   2697   2052    355   -245   -337       C
ATOM   1595  CD2 LEU A 111      19.936 -52.830 -41.646  1.00 15.81           C
ANISOU 1595  CD2 LEU A 111     1479   2634   1896    376   -213   -371       C
ATOM   1596  H   LEU A 111      21.828 -49.616 -42.414  1.00  0.00           H
ATOM   1597  HA  LEU A 111      21.481 -48.995 -39.612  1.00  0.00           H
ATOM   1598  HB2 LEU A 111      20.544 -51.119 -39.338  1.00  0.00           H
ATOM   1599  HB3 LEU A 111      19.963 -50.477 -40.870  1.00  0.00           H
ATOM   1600  HG  LEU A 111      21.897 -51.973 -41.843  1.00  0.00           H
ATOM   1601 HD21 LEU A 111      20.201 -53.771 -42.128  1.00  0.00           H
ATOM   1602 HD22 LEU A 111      19.207 -53.019 -40.858  1.00  0.00           H
ATOM   1603 HD23 LEU A 111      19.507 -52.152 -42.384  1.00  0.00           H
ATOM   1604 HD11 LEU A 111      22.130 -54.072 -40.585  1.00  0.00           H
ATOM   1605 HD12 LEU A 111      22.799 -52.687 -39.690  1.00  0.00           H
ATOM   1606 HD13 LEU A 111      21.216 -53.360 -39.234  1.00  0.00           H
ATOM   1607  N   VAL A 112      24.161 -50.647 -40.510  1.00 12.75           N
ANISOU 1607  N   VAL A 112     1284   2035   1524    471   -315   -343       N
ATOM   1608  CA  VAL A 112      25.492 -50.970 -40.019  1.00 13.33           C
ANISOU 1608  CA  VAL A 112     1405   2040   1619    454   -362   -327       C
ATOM   1609  C   VAL A 112      26.233 -49.684 -39.574  1.00 13.79           C
ANISOU 1609  C   VAL A 112     1495   2060   1684    488   -387   -334       C
ATOM   1610  O   VAL A 112      26.850 -49.622 -38.477  1.00 13.33           O
ANISOU 1610  O   VAL A 112     1493   1962   1608    474   -424   -331       O
ATOM   1611  CB  VAL A 112      26.307 -51.746 -41.050  1.00 14.21           C
ANISOU 1611  CB  VAL A 112     1499   2114   1786    436   -375   -314       C
ATOM   1612  CG1 VAL A 112      27.700 -52.053 -40.529  1.00 16.51           C
ANISOU 1612  CG1 VAL A 112     1824   2333   2117    424   -422   -296       C
ATOM   1613  CG2 VAL A 112      25.566 -53.062 -41.406  1.00 13.39           C
ANISOU 1613  CG2 VAL A 112     1368   2045   1676    405   -365   -318       C
ATOM   1614  H   VAL A 112      23.954 -50.743 -41.494  1.00  0.00           H
ATOM   1615  HA  VAL A 112      25.376 -51.606 -39.141  1.00  0.00           H
ATOM   1616  HB  VAL A 112      26.397 -51.141 -41.952  1.00  0.00           H
ATOM   1617 HG11 VAL A 112      28.210 -51.122 -40.283  1.00  0.00           H
ATOM   1618 HG12 VAL A 112      27.625 -52.673 -39.636  1.00  0.00           H
ATOM   1619 HG13 VAL A 112      28.265 -52.585 -41.294  1.00  0.00           H
ATOM   1620 HG21 VAL A 112      26.146 -53.618 -42.142  1.00  0.00           H
ATOM   1621 HG22 VAL A 112      24.585 -52.826 -41.819  1.00  0.00           H
ATOM   1622 HG23 VAL A 112      25.446 -53.666 -40.507  1.00  0.00           H
ATOM   1623  N   ALA A 113      26.087 -48.618 -40.364  1.00 11.61           N
ANISOU 1623  N   ALA A 113     1206   1782   1425    513   -356   -338       N
ATOM   1624  CA  ALA A 113      26.793 -47.368 -40.044  1.00 11.56           C
ANISOU 1624  CA  ALA A 113     1231   1728   1435    535   -375   -346       C
ATOM   1625  C   ALA A 113      26.336 -46.844 -38.672  1.00 12.80           C
ANISOU 1625  C   ALA A 113     1430   1897   1536    560   -388   -375       C
ATOM   1626  O   ALA A 113      27.142 -46.370 -37.847  1.00 13.51           O
ANISOU 1626  O   ALA A 113     1574   1936   1625    553   -431   -383       O
ATOM   1627  CB  ALA A 113      26.526 -46.321 -41.100  1.00 10.98           C
ANISOU 1627  CB  ALA A 113     1149   1648   1376    547   -334   -336       C
ATOM   1628  H   ALA A 113      25.493 -48.670 -41.179  1.00  0.00           H
ATOM   1629  HA  ALA A 113      27.864 -47.567 -40.007  1.00  0.00           H
ATOM   1630  HB1 ALA A 113      25.463 -46.309 -41.340  1.00  0.00           H
ATOM   1631  HB2 ALA A 113      27.098 -46.556 -41.997  1.00  0.00           H
ATOM   1632  HB3 ALA A 113      26.825 -45.342 -40.725  1.00  0.00           H
ATOM   1633  N   SER A 114      25.041 -46.974 -38.431  1.00 12.69           N
ANISOU 1633  N   SER A 114     1405   1943   1474    569   -335   -386       N
ATOM   1634  CA  SER A 114      24.389 -46.513 -37.210  1.00 14.26           C
ANISOU 1634  CA  SER A 114     1655   2156   1607    577   -305   -412       C
ATOM   1635  C   SER A 114      24.753 -47.380 -36.006  1.00 17.01           C
ANISOU 1635  C   SER A 114     2072   2489   1902    526   -329   -402       C
ATOM   1636  O   SER A 114      24.831 -46.871 -34.886  1.00 19.59           O
ANISOU 1636  O   SER A 114     2476   2797   2172    528   -333   -423       O
ATOM   1637  CB  SER A 114      22.869 -46.555 -37.388  1.00 16.12           C
ANISOU 1637  CB  SER A 114     1838   2467   1821    598   -231   -423       C
ATOM   1638  OG  SER A 114      22.229 -45.971 -36.294  1.00 19.47           O
ANISOU 1638  OG  SER A 114     2307   2904   2188    616   -185   -453       O
ATOM   1639  H   SER A 114      24.470 -47.419 -39.135  1.00  0.00           H
ATOM   1640  HA  SER A 114      24.694 -45.486 -37.012  1.00  0.00           H
ATOM   1641  HB2 SER A 114      22.599 -46.010 -38.293  1.00  0.00           H
ATOM   1642  HB3 SER A 114      22.546 -47.592 -37.482  1.00  0.00           H
ATOM   1643  HG  SER A 114      21.278 -46.006 -36.423  1.00  0.00           H
ATOM   1644  N   SER A 115      24.903 -48.692 -36.238  1.00 17.76           N
ANISOU 1644  N   SER A 115     2148   2591   2009    483   -342   -371       N
ATOM   1645  CA  SER A 115      25.333 -49.614 -35.194  1.00 19.15           C
ANISOU 1645  CA  SER A 115     2393   2742   2140    436   -375   -348       C
ATOM   1646  C   SER A 115      26.750 -49.260 -34.716  1.00 18.11           C
ANISOU 1646  C   SER A 115     2314   2539   2026    435   -465   -346       C
ATOM   1647  O   SER A 115      27.060 -49.374 -33.534  1.00 19.93           O
ANISOU 1647  O   SER A 115     2631   2747   2195    415   -502   -342       O
ATOM   1648  CB  SER A 115      25.279 -51.047 -35.702  1.00 20.93           C
ANISOU 1648  CB  SER A 115     2584   2974   2394    395   -376   -315       C
ATOM   1649  OG  SER A 115      25.681 -51.979 -34.702  1.00 21.83           O
ANISOU 1649  OG  SER A 115     2772   3056   2466    353   -411   -285       O
ATOM   1650  H   SER A 115      24.713 -49.052 -37.162  1.00  0.00           H
ATOM   1651  HA  SER A 115      24.651 -49.521 -34.349  1.00  0.00           H
ATOM   1652  HB2 SER A 115      25.944 -51.142 -36.560  1.00  0.00           H
ATOM   1653  HB3 SER A 115      24.260 -51.276 -36.014  1.00  0.00           H
ATOM   1654  HG  SER A 115      26.584 -51.792 -34.435  1.00  0.00           H
ATOM   1655  N   GLY A 116      27.622 -48.870 -35.647  1.00 14.65           N
ANISOU 1655  N   GLY A 116     1825   2066   1674    454   -502   -345       N
ATOM   1656  CA  GLY A 116      28.906 -48.289 -35.281  1.00 12.70           C
ANISOU 1656  CA  GLY A 116     1607   1755   1463    455   -583   -350       C
ATOM   1657  C   GLY A 116      29.974 -49.343 -34.967  1.00 12.93           C
ANISOU 1657  C   GLY A 116     1646   1741   1527    425   -662   -317       C
ATOM   1658  O   GLY A 116      30.987 -49.029 -34.378  1.00 13.27           O
ANISOU 1658  O   GLY A 116     1719   1734   1590    418   -741   -318       O
ATOM   1659  H   GLY A 116      27.387 -48.980 -36.623  1.00  0.00           H
ATOM   1660  HA2 GLY A 116      28.765 -47.664 -34.399  1.00  0.00           H
ATOM   1661  HA3 GLY A 116      29.258 -47.665 -36.103  1.00  0.00           H
ATOM   1662  N   THR A 117      29.743 -50.589 -35.350  1.00 14.23           N
ANISOU 1662  N   THR A 117     1784   1920   1702    408   -643   -289       N
ATOM   1663  CA  THR A 117      30.747 -51.608 -35.091  1.00 16.30           C
ANISOU 1663  CA  THR A 117     2055   2132   2007    389   -716   -255       C
ATOM   1664  C   THR A 117      30.650 -52.717 -36.120  1.00 17.16           C
ANISOU 1664  C   THR A 117     2104   2244   2172    383   -680   -237       C
ATOM   1665  O   THR A 117      29.568 -52.992 -36.646  1.00 17.67           O
ANISOU 1665  O   THR A 117     2147   2359   2208    379   -610   -245       O
ATOM   1666  CB  THR A 117      30.553 -52.233 -33.683  1.00 23.09           C
ANISOU 1666  CB  THR A 117     3016   2985   2772    361   -756   -232       C
ATOM   1667  OG1 THR A 117      31.471 -53.286 -33.520  1.00 23.62           O
ANISOU 1667  OG1 THR A 117     3087   2998   2890    347   -822   -192       O
ATOM   1668  CG2 THR A 117      29.147 -52.850 -33.512  1.00 22.93           C
ANISOU 1668  CG2 THR A 117     3022   3019   2672    337   -667   -224       C
ATOM   1669  H   THR A 117      28.880 -50.829 -35.816  1.00  0.00           H
ATOM   1670  HA  THR A 117      31.737 -51.155 -35.147  1.00  0.00           H
ATOM   1671  HB  THR A 117      30.720 -51.476 -32.917  1.00  0.00           H
ATOM   1672  HG1 THR A 117      31.843 -53.252 -32.636  1.00  0.00           H
ATOM   1673 HG21 THR A 117      29.055 -53.276 -32.513  1.00  0.00           H
ATOM   1674 HG22 THR A 117      28.392 -52.076 -33.648  1.00  0.00           H
ATOM   1675 HG23 THR A 117      29.001 -53.634 -34.255  1.00  0.00           H
ATOM   1676  N   LEU A 118      31.788 -53.359 -36.407  1.00 16.93           N
ANISOU 1676  N   LEU A 118     2051   2156   2225    371   -701   -213       N
ATOM   1677  CA  LEU A 118      31.805 -54.581 -37.195  1.00 16.63           C
ANISOU 1677  CA  LEU A 118     1976   2107   2234    368   -682   -199       C
ATOM   1678  C   LEU A 118      32.143 -55.813 -36.302  1.00 17.92           C
ANISOU 1678  C   LEU A 118     2192   2225   2391    355   -755   -162       C
ATOM   1679  O   LEU A 118      32.613 -56.844 -36.803  1.00 17.68           O
ANISOU 1679  O   LEU A 118     2137   2154   2426    358   -760   -148       O
ATOM   1680  CB  LEU A 118      32.865 -54.479 -38.294  1.00 16.79           C
ANISOU 1680  CB  LEU A 118     1936   2094   2351    371   -645   -203       C
ATOM   1681  CG  LEU A 118      32.490 -53.478 -39.404  1.00 19.43           C
ANISOU 1681  CG  LEU A 118     2231   2466   2686    379   -570   -227       C
ATOM   1682  CD1 LEU A 118      33.575 -53.339 -40.383  1.00 20.14           C
ANISOU 1682  CD1 LEU A 118     2276   2525   2850    378   -538   -224       C
ATOM   1683  CD2 LEU A 118      31.192 -53.877 -40.131  1.00 22.30           C
ANISOU 1683  CD2 LEU A 118     2580   2885   3008    386   -523   -242       C
ATOM   1684  H   LEU A 118      32.662 -52.984 -36.066  1.00  0.00           H
ATOM   1685  HA  LEU A 118      30.826 -54.727 -37.652  1.00  0.00           H
ATOM   1686  HB2 LEU A 118      32.994 -55.463 -38.744  1.00  0.00           H
ATOM   1687  HB3 LEU A 118      33.809 -54.170 -37.845  1.00  0.00           H
ATOM   1688  HG  LEU A 118      32.330 -52.505 -38.939  1.00  0.00           H
ATOM   1689 HD11 LEU A 118      34.494 -53.057 -39.870  1.00  0.00           H
ATOM   1690 HD12 LEU A 118      33.723 -54.288 -40.898  1.00  0.00           H
ATOM   1691 HD13 LEU A 118      33.313 -52.569 -41.109  1.00  0.00           H
ATOM   1692 HD21 LEU A 118      30.385 -53.981 -39.405  1.00  0.00           H
ATOM   1693 HD22 LEU A 118      30.931 -53.107 -40.857  1.00  0.00           H
ATOM   1694 HD23 LEU A 118      31.341 -54.826 -40.646  1.00  0.00           H
ATOM   1695  N   GLU A 119      31.959 -55.685 -34.994  1.00 16.91           N
ANISOU 1695  N   GLU A 119     2146   2097   2182    343   -811   -145       N
ATOM   1696  CA  GLU A 119      32.239 -56.813 -34.114  1.00 19.63           C
ANISOU 1696  CA  GLU A 119     2559   2393   2504    328   -881    -98       C
ATOM   1697  C   GLU A 119      31.474 -58.021 -34.580  1.00 17.98           C
ANISOU 1697  C   GLU A 119     2352   2185   2294    304   -821    -81       C
ATOM   1698  O   GLU A 119      30.254 -57.982 -34.666  1.00 17.73           O
ANISOU 1698  O   GLU A 119     2331   2209   2198    275   -738    -93       O
ATOM   1699  CB  GLU A 119      31.795 -56.534 -32.702  1.00 28.57           C
ANISOU 1699  CB  GLU A 119     3803   3541   3510    304   -908    -81       C
ATOM   1700  CG  GLU A 119      32.664 -55.620 -31.941  1.00 40.05           C
ANISOU 1700  CG  GLU A 119     5283   4974   4961    308   -960    -89       C
ATOM   1701  CD  GLU A 119      31.905 -55.041 -30.752  1.00 45.14           C
ANISOU 1701  CD  GLU A 119     6040   5655   5456    292   -967    -96       C
ATOM   1702  OE1 GLU A 119      31.585 -55.835 -29.829  1.00 46.23           O
ANISOU 1702  OE1 GLU A 119     6281   5783   5501    269   -996    -53       O
ATOM   1703  OE2 GLU A 119      31.601 -53.819 -30.793  1.00 44.54           O
ANISOU 1703  OE2 GLU A 119     5955   5613   5354    304   -933   -143       O
ATOM   1704  H   GLU A 119      31.627 -54.812 -34.611  1.00  0.00           H
ATOM   1705  HA  GLU A 119      33.307 -57.030 -34.126  1.00  0.00           H
ATOM   1706  HB2 GLU A 119      30.798 -56.096 -32.742  1.00  0.00           H
ATOM   1707  HB3 GLU A 119      31.735 -57.481 -32.165  1.00  0.00           H
ATOM   1708  HG2 GLU A 119      32.989 -54.808 -32.591  1.00  0.00           H
ATOM   1709  HG3 GLU A 119      33.536 -56.166 -31.582  1.00  0.00           H
ATOM   1710  N   PHE A 120      32.190 -59.115 -34.791  1.00 18.24           N
ANISOU 1710  N   PHE A 120     2376   2150   2402    313   -866    -54       N
ATOM   1711  CA  PHE A 120      31.644 -60.311 -35.366  1.00 17.82           C
ANISOU 1711  CA  PHE A 120     2321   2078   2370    290   -815    -45       C
ATOM   1712  C   PHE A 120      31.977 -61.523 -34.459  1.00 16.95           C
ANISOU 1712  C   PHE A 120     2297   1892   2253    275   -881     17       C
ATOM   1713  O   PHE A 120      33.051 -61.608 -33.895  1.00 18.87           O
ANISOU 1713  O   PHE A 120     2557   2080   2532    307   -980     46       O
ATOM   1714  CB  PHE A 120      32.224 -60.495 -36.777  1.00 18.12           C
ANISOU 1714  CB  PHE A 120     2264   2098   2523    325   -791    -81       C
ATOM   1715  CG  PHE A 120      31.664 -61.691 -37.522  1.00 18.09           C
ANISOU 1715  CG  PHE A 120     2258   2071   2544    301   -739    -88       C
ATOM   1716  CD1 PHE A 120      30.524 -61.570 -38.314  1.00 17.54           C
ANISOU 1716  CD1 PHE A 120     2161   2065   2439    272   -654   -124       C
ATOM   1717  CD2 PHE A 120      32.297 -62.940 -37.427  1.00 19.52           C
ANISOU 1717  CD2 PHE A 120     2465   2161   2790    311   -783    -58       C
ATOM   1718  CE1 PHE A 120      29.996 -62.645 -38.999  1.00 18.51           C
ANISOU 1718  CE1 PHE A 120     2284   2165   2584    242   -615   -138       C
ATOM   1719  CE2 PHE A 120      31.767 -64.026 -38.110  1.00 21.14           C
ANISOU 1719  CE2 PHE A 120     2677   2337   3019    285   -735    -71       C
ATOM   1720  CZ  PHE A 120      30.633 -63.869 -38.922  1.00 20.27           C
ANISOU 1720  CZ  PHE A 120     2539   2292   2869    248   -652   -114       C
ATOM   1721  H   PHE A 120      33.167 -59.107 -34.535  1.00  0.00           H
ATOM   1722  HA  PHE A 120      30.561 -60.208 -35.438  1.00  0.00           H
ATOM   1723  HB2 PHE A 120      32.007 -59.598 -37.357  1.00  0.00           H
ATOM   1724  HB3 PHE A 120      33.305 -60.607 -36.698  1.00  0.00           H
ATOM   1725  HD1 PHE A 120      30.040 -60.608 -38.394  1.00  0.00           H
ATOM   1726  HD2 PHE A 120      33.188 -63.055 -36.828  1.00  0.00           H
ATOM   1727  HE1 PHE A 120      29.097 -62.532 -39.587  1.00  0.00           H
ATOM   1728  HE2 PHE A 120      32.230 -64.997 -38.016  1.00  0.00           H
ATOM   1729  HZ  PHE A 120      30.257 -64.708 -39.489  1.00  0.00           H
ATOM   1730  N   ILE A 121      31.022 -62.423 -34.294  1.00 18.43           N
ANISOU 1730  N   ILE A 121     2537   2075   2392    225   -830     41       N
ATOM   1731  CA  ILE A 121      31.165 -63.574 -33.427  1.00 21.35           C
ANISOU 1731  CA  ILE A 121     3002   2368   2741    203   -880    108       C
ATOM   1732  C   ILE A 121      30.844 -64.777 -34.306  1.00 20.46           C
ANISOU 1732  C   ILE A 121     2868   2207   2698    183   -833    102       C
ATOM   1733  O   ILE A 121      29.732 -64.920 -34.824  1.00 19.71           O
ANISOU 1733  O   ILE A 121     2754   2158   2578    135   -743     75       O
ATOM   1734  CB  ILE A 121      30.217 -63.527 -32.192  1.00 28.06           C
ANISOU 1734  CB  ILE A 121     3962   3252   3447    146   -851    149       C
ATOM   1735  CG1 ILE A 121      30.603 -62.385 -31.241  1.00 30.57           C
ANISOU 1735  CG1 ILE A 121     4323   3606   3687    168   -907    149       C
ATOM   1736  CG2 ILE A 121      30.265 -64.866 -31.428  1.00 27.02           C
ANISOU 1736  CG2 ILE A 121     3939   3033   3295    115   -889    228       C
ATOM   1737  CD1 ILE A 121      30.103 -61.037 -31.697  1.00 31.59           C
ANISOU 1737  CD1 ILE A 121     4382   3827   3795    177   -841     82       C
ATOM   1738  H   ILE A 121      30.154 -62.302 -34.795  1.00  0.00           H
ATOM   1739  HA  ILE A 121      32.198 -63.642 -33.086  1.00  0.00           H
ATOM   1740  HB  ILE A 121      29.198 -63.361 -32.541  1.00  0.00           H
ATOM   1741 HG12 ILE A 121      30.182 -62.596 -30.258  1.00  0.00           H
ATOM   1742 HG13 ILE A 121      31.689 -62.348 -31.158  1.00  0.00           H
ATOM   1743 HD11 ILE A 121      29.753 -60.468 -30.836  1.00  0.00           H
ATOM   1744 HD12 ILE A 121      29.281 -61.173 -32.400  1.00  0.00           H
ATOM   1745 HD13 ILE A 121      30.913 -60.495 -32.185  1.00  0.00           H
ATOM   1746 HG21 ILE A 121      29.991 -65.679 -32.101  1.00  0.00           H
ATOM   1747 HG22 ILE A 121      31.274 -65.032 -31.049  1.00  0.00           H
ATOM   1748 HG23 ILE A 121      29.564 -64.834 -30.594  1.00  0.00           H
ATOM   1749  N   THR A 122      31.841 -65.634 -34.485  1.00 19.44           N
ANISOU 1749  N   THR A 122     2739   1983   2665    223   -899    123       N
ATOM   1750  CA  THR A 122      31.673 -66.820 -35.270  1.00 20.58           C
ANISOU 1750  CA  THR A 122     2876   2063   2880    211   -864    114       C
ATOM   1751  C   THR A 122      30.795 -67.781 -34.473  1.00 20.93           C
ANISOU 1751  C   THR A 122     3029   2069   2855    138   -844    173       C
ATOM   1752  O   THR A 122      30.939 -67.893 -33.247  1.00 22.48           O
ANISOU 1752  O   THR A 122     3320   2240   2983    128   -900    243       O
ATOM   1753  CB  THR A 122      33.036 -67.499 -35.529  1.00 25.46           C
ANISOU 1753  CB  THR A 122     3472   2577   3625    282   -942    125       C
ATOM   1754  OG1 THR A 122      33.831 -66.669 -36.397  1.00 27.86           O
ANISOU 1754  OG1 THR A 122     3664   2915   4005    342   -940     67       O
ATOM   1755  CG2 THR A 122      32.833 -68.854 -36.184  1.00 27.40           C
ANISOU 1755  CG2 THR A 122     3737   2737   3938    268   -909    118       C
ATOM   1756  H   THR A 122      32.737 -65.446 -34.059  1.00  0.00           H
ATOM   1757  HA  THR A 122      31.193 -66.575 -36.217  1.00  0.00           H
ATOM   1758  HB  THR A 122      33.558 -67.632 -34.581  1.00  0.00           H
ATOM   1759  HG1 THR A 122      33.810 -67.025 -37.288  1.00  0.00           H
ATOM   1760 HG21 THR A 122      33.802 -69.321 -36.361  1.00  0.00           H
ATOM   1761 HG22 THR A 122      32.314 -68.724 -37.134  1.00  0.00           H
ATOM   1762 HG23 THR A 122      32.237 -69.489 -35.528  1.00  0.00           H
ATOM   1763  N   GLU A 123      29.884 -68.459 -35.166  1.00 20.85           N
ANISOU 1763  N   GLU A 123     3008   2055   2857     83   -766    147       N
ATOM   1764  CA  GLU A 123      29.106 -69.511 -34.543  1.00 22.46           C
ANISOU 1764  CA  GLU A 123     3307   2206   3020      7   -741    203       C
ATOM   1765  C   GLU A 123      29.360 -70.867 -35.237  1.00 24.16           C
ANISOU 1765  C   GLU A 123     3536   2304   3340      6   -747    198       C
ATOM   1766  O   GLU A 123      29.697 -70.934 -36.423  1.00 22.21           O
ANISOU 1766  O   GLU A 123     3211   2048   3178     43   -733    128       O
ATOM   1767  CB  GLU A 123      27.614 -69.145 -34.557  1.00 22.26           C
ANISOU 1767  CB  GLU A 123     3265   2279   2914    -77   -638    182       C
ATOM   1768  CG  GLU A 123      27.285 -67.930 -33.669  1.00 23.13           C
ANISOU 1768  CG  GLU A 123     3386   2489   2913    -78   -623    195       C
ATOM   1769  CD  GLU A 123      25.832 -67.504 -33.785  1.00 24.63           C
ANISOU 1769  CD  GLU A 123     3535   2780   3043   -147   -515    165       C
ATOM   1770  OE1 GLU A 123      25.376 -67.309 -34.936  1.00 24.17           O
ANISOU 1770  OE1 GLU A 123     3377   2768   3036   -150   -474     97       O
ATOM   1771  OE2 GLU A 123      25.144 -67.386 -32.732  1.00 25.59           O
ANISOU 1771  OE2 GLU A 123     3723   2935   3067   -197   -472    210       O
ATOM   1772  H   GLU A 123      29.733 -68.238 -36.140  1.00  0.00           H
ATOM   1773  HA  GLU A 123      29.424 -69.597 -33.504  1.00  0.00           H
ATOM   1774  HB2 GLU A 123      27.322 -68.915 -35.582  1.00  0.00           H
ATOM   1775  HB3 GLU A 123      27.037 -70.002 -34.210  1.00  0.00           H
ATOM   1776  HG2 GLU A 123      27.919 -67.096 -33.969  1.00  0.00           H
ATOM   1777  HG3 GLU A 123      27.499 -68.182 -32.630  1.00  0.00           H
ATOM   1778  N   GLY A 124      29.170 -71.944 -34.480  1.00 29.14           N
ANISOU 1778  N   GLY A 124     4275   2841   3956    -40   -763    272       N
ATOM   1779  CA  GLY A 124      29.477 -73.269 -34.979  1.00 31.98           C
ANISOU 1779  CA  GLY A 124     4666   3068   4416    -37   -779    274       C
ATOM   1780  C   GLY A 124      28.307 -73.857 -35.733  1.00 34.02           C
ANISOU 1780  C   GLY A 124     4910   3331   4686   -128   -689    228       C
ATOM   1781  O   GLY A 124      27.718 -74.824 -35.281  1.00 37.33           O
ANISOU 1781  O   GLY A 124     5413   3675   5094   -204   -669    279       O
ATOM   1782  H   GLY A 124      28.806 -71.837 -33.544  1.00  0.00           H
ATOM   1783  HA2 GLY A 124      29.719 -73.918 -34.137  1.00  0.00           H
ATOM   1784  HA3 GLY A 124      30.338 -73.210 -35.644  1.00  0.00           H
ATOM   1785  N   PHE A 125      27.957 -73.268 -36.875  1.00 31.44           N
ANISOU 1785  N   PHE A 125     4478   3090   4379   -124   -639    133       N
ATOM   1786  CA  PHE A 125      26.964 -73.872 -37.742  1.00 31.47           C
ANISOU 1786  CA  PHE A 125     4459   3092   4408   -203   -574     77       C
ATOM   1787  C   PHE A 125      27.479 -75.250 -38.181  1.00 32.95           C
ANISOU 1787  C   PHE A 125     4703   3120   4695   -194   -601     71       C
ATOM   1788  O   PHE A 125      28.672 -75.435 -38.395  1.00 33.41           O
ANISOU 1788  O   PHE A 125     4762   3106   4826    -98   -655     66       O
ATOM   1789  CB  PHE A 125      26.706 -73.005 -38.981  1.00 29.99           C
ANISOU 1789  CB  PHE A 125     4156   3014   4224   -182   -538    -24       C
ATOM   1790  CG  PHE A 125      25.947 -71.751 -38.701  1.00 28.15           C
ANISOU 1790  CG  PHE A 125     3864   2928   3902   -203   -500    -28       C
ATOM   1791  CD1 PHE A 125      24.563 -71.732 -38.774  1.00 27.23           C
ANISOU 1791  CD1 PHE A 125     3720   2883   3746   -297   -437    -44       C
ATOM   1792  CD2 PHE A 125      26.607 -70.579 -38.388  1.00 27.59           C
ANISOU 1792  CD2 PHE A 125     3761   2925   3798   -127   -527    -21       C
ATOM   1793  CE1 PHE A 125      23.840 -70.567 -38.526  1.00 26.84           C
ANISOU 1793  CE1 PHE A 125     3608   2967   3623   -307   -398    -51       C
ATOM   1794  CE2 PHE A 125      25.889 -69.409 -38.128  1.00 26.97           C
ANISOU 1794  CE2 PHE A 125     3633   2973   3640   -142   -489    -29       C
ATOM   1795  CZ  PHE A 125      24.504 -69.402 -38.194  1.00 26.33           C
ANISOU 1795  CZ  PHE A 125     3524   2961   3520   -227   -422    -44       C
ATOM   1796  H   PHE A 125      28.387 -72.393 -37.139  1.00  0.00           H
ATOM   1797  HA  PHE A 125      26.032 -73.996 -37.190  1.00  0.00           H
ATOM   1798  HB2 PHE A 125      27.668 -72.733 -39.414  1.00  0.00           H
ATOM   1799  HB3 PHE A 125      26.149 -73.594 -39.710  1.00  0.00           H
ATOM   1800  HD1 PHE A 125      24.034 -72.639 -39.028  1.00  0.00           H
ATOM   1801  HD2 PHE A 125      27.686 -70.567 -38.344  1.00  0.00           H
ATOM   1802  HE1 PHE A 125      22.762 -70.575 -38.593  1.00  0.00           H
ATOM   1803  HE2 PHE A 125      26.417 -68.502 -37.873  1.00  0.00           H
ATOM   1804  HZ  PHE A 125      23.951 -68.497 -37.988  1.00  0.00           H
ATOM   1805  N   THR A 126      26.567 -76.202 -38.313  1.00 33.93           N
ANISOU 1805  N   THR A 126     4870   3188   4832   -293   -562     69       N
ATOM   1806  CA  THR A 126      26.892 -77.509 -38.860  1.00 34.41           C
ANISOU 1806  CA  THR A 126     4987   3096   4992   -295   -577     46       C
ATOM   1807  C   THR A 126      26.227 -77.643 -40.231  1.00 32.56           C
ANISOU 1807  C   THR A 126     4690   2896   4787   -339   -531    -68       C
ATOM   1808  O   THR A 126      25.036 -77.409 -40.378  1.00 33.32           O
ANISOU 1808  O   THR A 126     4747   3078   4836   -434   -483    -91       O
ATOM   1809  CB  THR A 126      26.440 -78.621 -37.886  1.00 37.46           C
ANISOU 1809  CB  THR A 126     5494   3364   5375   -381   -577    140       C
ATOM   1810  OG1 THR A 126      27.079 -78.407 -36.617  1.00 39.55           O
ANISOU 1810  OG1 THR A 126     5826   3609   5593   -334   -630    248       O
ATOM   1811  CG2 THR A 126      26.812 -80.011 -38.417  1.00 37.87           C
ANISOU 1811  CG2 THR A 126     5615   3236   5537   -378   -597    119       C
ATOM   1812  H   THR A 126      25.617 -76.014 -38.025  1.00  0.00           H
ATOM   1813  HA  THR A 126      27.972 -77.575 -38.988  1.00  0.00           H
ATOM   1814  HB  THR A 126      25.359 -78.565 -37.756  1.00  0.00           H
ATOM   1815  HG1 THR A 126      26.825 -77.548 -36.272  1.00  0.00           H
ATOM   1816 HG21 THR A 126      26.481 -80.771 -37.710  1.00  0.00           H
ATOM   1817 HG22 THR A 126      27.893 -80.075 -38.540  1.00  0.00           H
ATOM   1818 HG23 THR A 126      26.327 -80.174 -39.379  1.00  0.00           H
ATOM   1819  N   TRP A 127      27.017 -77.963 -41.246  1.00 30.61           N
ANISOU 1819  N   TRP A 127     4429   2587   4615   -264   -546   -144       N
ATOM   1820  CA  TRP A 127      26.499 -78.038 -42.607  1.00 29.01           C
ANISOU 1820  CA  TRP A 127     4178   2418   4426   -294   -511   -259       C
ATOM   1821  C   TRP A 127      26.725 -79.448 -43.097  1.00 30.98           C
ANISOU 1821  C   TRP A 127     4507   2497   4766   -307   -518   -297       C
ATOM   1822  O   TRP A 127      27.760 -79.770 -43.679  1.00 31.83           O
ANISOU 1822  O   TRP A 127     4626   2525   4942   -210   -531   -341       O
ATOM   1823  CB  TRP A 127      27.208 -77.030 -43.525  1.00 26.30           C
ANISOU 1823  CB  TRP A 127     3750   2168   4076   -192   -506   -331       C
ATOM   1824  CG  TRP A 127      27.105 -75.612 -43.049  1.00 24.59           C
ANISOU 1824  CG  TRP A 127     3461   2102   3780   -169   -503   -295       C
ATOM   1825  CD1 TRP A 127      28.120 -74.848 -42.555  1.00 23.97           C
ANISOU 1825  CD1 TRP A 127     3357   2049   3702    -74   -532   -253       C
ATOM   1826  CD2 TRP A 127      25.929 -74.777 -43.039  1.00 25.76           C
ANISOU 1826  CD2 TRP A 127     3549   2392   3846   -240   -472   -303       C
ATOM   1827  NE1 TRP A 127      27.654 -73.587 -42.232  1.00 24.14           N
ANISOU 1827  NE1 TRP A 127     3318   2212   3640    -84   -519   -236       N
ATOM   1828  CE2 TRP A 127      26.315 -73.519 -42.517  1.00 25.32           C
ANISOU 1828  CE2 TRP A 127     3445   2435   3739   -179   -479   -266       C
ATOM   1829  CE3 TRP A 127      24.597 -74.966 -43.419  1.00 28.01           C
ANISOU 1829  CE3 TRP A 127     3811   2728   4103   -346   -442   -340       C
ATOM   1830  CZ2 TRP A 127      25.412 -72.471 -42.350  1.00 25.56           C
ANISOU 1830  CZ2 TRP A 127     3413   2606   3692   -215   -452   -264       C
ATOM   1831  CZ3 TRP A 127      23.699 -73.911 -43.252  1.00 28.30           C
ANISOU 1831  CZ3 TRP A 127     3773   2912   4068   -380   -418   -336       C
ATOM   1832  CH2 TRP A 127      24.116 -72.682 -42.732  1.00 26.70           C
ANISOU 1832  CH2 TRP A 127     3530   2798   3815   -310   -420   -298       C
ATOM   1833  H   TRP A 127      27.993 -78.158 -41.074  1.00  0.00           H
ATOM   1834  HA  TRP A 127      25.430 -77.827 -42.598  1.00  0.00           H
ATOM   1835  HB2 TRP A 127      26.762 -77.094 -44.517  1.00  0.00           H
ATOM   1836  HB3 TRP A 127      28.261 -77.301 -43.596  1.00  0.00           H
ATOM   1837  HD1 TRP A 127      29.141 -75.180 -42.433  1.00  0.00           H
ATOM   1838  HE3 TRP A 127      24.270 -75.908 -43.833  1.00  0.00           H
ATOM   1839  HZ2 TRP A 127      25.725 -71.525 -41.933  1.00  0.00           H
ATOM   1840  HZ3 TRP A 127      22.664 -74.046 -43.529  1.00  0.00           H
ATOM   1841  HH2 TRP A 127      23.398 -71.881 -42.630  1.00  0.00           H
ATOM   1842  HE1 TRP A 127      28.211 -72.837 -41.848  1.00  0.00           H
ATOM   1843  N   THR A 128      25.766 -80.305 -42.812  1.00 33.13           N
ANISOU 1843  N   THR A 128     4836   2707   5044   -428   -504   -277       N
ATOM   1844  CA  THR A 128      25.972 -81.726 -43.034  1.00 35.31           C
ANISOU 1844  CA  THR A 128     5210   2795   5410   -449   -516   -294       C
ATOM   1845  C   THR A 128      25.760 -82.030 -44.498  1.00 34.36           C
ANISOU 1845  C   THR A 128     5070   2666   5318   -461   -498   -433       C
ATOM   1846  O   THR A 128      24.745 -81.655 -45.087  1.00 35.09           O
ANISOU 1846  O   THR A 128     5105   2865   5360   -544   -477   -494       O
ATOM   1847  CB  THR A 128      25.012 -82.565 -42.182  1.00 38.02           C
ANISOU 1847  CB  THR A 128     5629   3063   5755   -586   -504   -218       C
ATOM   1848  OG1 THR A 128      25.250 -82.299 -40.795  1.00 37.44           O
ANISOU 1848  OG1 THR A 128     5593   2995   5638   -572   -520    -85       O
ATOM   1849  CG2 THR A 128      25.208 -84.066 -42.448  1.00 41.26           C
ANISOU 1849  CG2 THR A 128     6149   3262   6265   -612   -518   -237       C
ATOM   1850  H   THR A 128      24.888 -79.974 -42.439  1.00  0.00           H
ATOM   1851  HA  THR A 128      26.997 -81.981 -42.765  1.00  0.00           H
ATOM   1852  HB  THR A 128      23.986 -82.291 -42.427  1.00  0.00           H
ATOM   1853  HG1 THR A 128      26.136 -82.585 -40.561  1.00  0.00           H
ATOM   1854 HG21 THR A 128      24.515 -84.638 -41.831  1.00  0.00           H
ATOM   1855 HG22 THR A 128      26.232 -84.348 -42.201  1.00  0.00           H
ATOM   1856 HG23 THR A 128      25.017 -84.277 -43.500  1.00  0.00           H
ATOM   1857  N   GLY A 129      26.751 -82.676 -45.091  1.00 32.84           N
ANISOU 1857  N   GLY A 129     4924   2349   5204   -370   -508   -486       N
ATOM   1858  CA  GLY A 129      26.608 -83.218 -46.425  1.00 33.22           C
ANISOU 1858  CA  GLY A 129     4991   2352   5282   -383   -490   -621       C
ATOM   1859  C   GLY A 129      26.897 -82.255 -47.545  1.00 31.44           C
ANISOU 1859  C   GLY A 129     4684   2259   5004   -312   -467   -717       C
ATOM   1860  O   GLY A 129      26.510 -82.540 -48.674  1.00 30.08           O
ANISOU 1860  O   GLY A 129     4524   2089   4817   -346   -451   -829       O
ATOM   1861  H   GLY A 129      27.627 -82.793 -44.602  1.00  0.00           H
ATOM   1862  HA2 GLY A 129      25.582 -83.568 -46.538  1.00  0.00           H
ATOM   1863  HA3 GLY A 129      27.277 -84.073 -46.524  1.00  0.00           H
ATOM   1864  N   VAL A 130      27.569 -81.133 -47.238  1.00 31.12           N
ANISOU 1864  N   VAL A 130     4568   2327   4929   -218   -465   -671       N
ATOM   1865  CA  VAL A 130      28.032 -80.205 -48.267  1.00 30.53           C
ANISOU 1865  CA  VAL A 130     4424   2363   4813   -138   -437   -750       C
ATOM   1866  C   VAL A 130      29.506 -79.898 -48.076  1.00 30.58           C
ANISOU 1866  C   VAL A 130     4405   2336   4877      7   -434   -720       C
ATOM   1867  O   VAL A 130      30.051 -80.096 -46.996  1.00 31.27           O
ANISOU 1867  O   VAL A 130     4509   2359   5015     42   -468   -624       O
ATOM   1868  CB  VAL A 130      27.253 -78.848 -48.265  1.00 28.85           C
ANISOU 1868  CB  VAL A 130     4118   2350   4493   -178   -433   -735       C
ATOM   1869  CG1 VAL A 130      25.840 -79.034 -48.769  1.00 29.79           C
ANISOU 1869  CG1 VAL A 130     4235   2523   4562   -306   -436   -789       C
ATOM   1870  CG2 VAL A 130      27.241 -78.206 -46.874  1.00 28.39           C
ANISOU 1870  CG2 VAL A 130     4027   2346   4414   -179   -454   -610       C
ATOM   1871  H   VAL A 130      27.760 -80.925 -46.268  1.00  0.00           H
ATOM   1872  HA  VAL A 130      27.901 -80.677 -49.241  1.00  0.00           H
ATOM   1873  HB  VAL A 130      27.765 -78.166 -48.945  1.00  0.00           H
ATOM   1874 HG21 VAL A 130      28.265 -78.078 -46.523  1.00  0.00           H
ATOM   1875 HG22 VAL A 130      26.698 -78.850 -46.182  1.00  0.00           H
ATOM   1876 HG23 VAL A 130      26.751 -77.234 -46.927  1.00  0.00           H
ATOM   1877 HG11 VAL A 130      25.864 -79.491 -49.758  1.00  0.00           H
ATOM   1878 HG12 VAL A 130      25.345 -78.065 -48.829  1.00  0.00           H
ATOM   1879 HG13 VAL A 130      25.292 -79.680 -48.083  1.00  0.00           H
ATOM   1880  N   THR A 131      30.155 -79.410 -49.125  1.00 31.01           N
ANISOU 1880  N   THR A 131     4419   2438   4925     88   -392   -802       N
ATOM   1881  CA  THR A 131      31.538 -78.935 -49.027  1.00 31.45           C
ANISOU 1881  CA  THR A 131     4421   2499   5030    220   -376   -772       C
ATOM   1882  C   THR A 131      31.547 -77.460 -48.591  1.00 27.95           C
ANISOU 1882  C   THR A 131     3885   2207   4526    236   -388   -718       C
ATOM   1883  O   THR A 131      30.803 -76.686 -49.148  1.00 27.53           O
ANISOU 1883  O   THR A 131     3799   2281   4380    189   -368   -754       O
ATOM   1884  CB  THR A 131      32.223 -79.023 -50.388  1.00 34.81           C
ANISOU 1884  CB  THR A 131     4839   2946   5442    288   -296   -862       C
ATOM   1885  OG1 THR A 131      32.173 -80.375 -50.874  1.00 37.37           O
ANISOU 1885  OG1 THR A 131     5254   3155   5791    268   -271   -908       O
ATOM   1886  CG2 THR A 131      33.670 -78.557 -50.294  1.00 35.94           C
ANISOU 1886  CG2 THR A 131     4910   3113   5634    409   -266   -819       C
ATOM   1887  H   THR A 131      29.683 -79.365 -50.017  1.00  0.00           H
ATOM   1888  HA  THR A 131      32.084 -79.537 -48.300  1.00  0.00           H
ATOM   1889  HB  THR A 131      31.693 -78.379 -51.089  1.00  0.00           H
ATOM   1890  HG1 THR A 131      31.523 -80.439 -51.577  1.00  0.00           H
ATOM   1891 HG21 THR A 131      34.140 -78.628 -51.275  1.00  0.00           H
ATOM   1892 HG22 THR A 131      33.697 -77.522 -49.953  1.00  0.00           H
ATOM   1893 HG23 THR A 131      34.209 -79.187 -49.587  1.00  0.00           H
ATOM   1894  N   GLN A 132      32.386 -77.068 -47.630  1.00 26.05           N
ANISOU 1894  N   GLN A 132     3606   1959   4332    302   -423   -631       N
ATOM   1895  CA  GLN A 132      32.413 -75.678 -47.156  1.00 26.21           C
ANISOU 1895  CA  GLN A 132     3546   2121   4290    311   -436   -577       C
ATOM   1896  C   GLN A 132      33.576 -74.902 -47.752  1.00 25.05           C
ANISOU 1896  C   GLN A 132     3321   2015   4183    417   -400   -608       C
ATOM   1897  O   GLN A 132      34.438 -75.473 -48.430  1.00 25.31           O
ANISOU 1897  O   GLN A 132     3352   1990   4274    480   -355   -648       O
ATOM   1898  CB  GLN A 132      32.528 -75.615 -45.640  1.00 29.47           C
ANISOU 1898  CB  GLN A 132     3972   2513   4713    304   -505   -461       C
ATOM   1899  CG  GLN A 132      31.353 -76.193 -44.908  1.00 32.69           C
ANISOU 1899  CG  GLN A 132     4451   2899   5069    193   -528   -413       C
ATOM   1900  CD  GLN A 132      31.501 -76.061 -43.406  1.00 33.07           C
ANISOU 1900  CD  GLN A 132     4524   2934   5106    189   -590   -296       C
ATOM   1901  OE1 GLN A 132      31.824 -74.977 -42.890  1.00 32.29           O
ANISOU 1901  OE1 GLN A 132     4371   2928   4970    221   -611   -256       O
ATOM   1902  NE2 GLN A 132      31.267 -77.171 -42.687  1.00 32.78           N
ANISOU 1902  NE2 GLN A 132     4581   2777   5099    146   -621   -239       N
ATOM   1903  H   GLN A 132      33.016 -77.742 -47.220  1.00  0.00           H
ATOM   1904  HA  GLN A 132      31.484 -75.192 -47.453  1.00  0.00           H
ATOM   1905  HB2 GLN A 132      33.420 -76.166 -45.342  1.00  0.00           H
ATOM   1906  HB3 GLN A 132      32.646 -74.573 -45.342  1.00  0.00           H
ATOM   1907  HG2 GLN A 132      31.265 -77.249 -45.162  1.00  0.00           H
ATOM   1908  HG3 GLN A 132      30.447 -75.675 -45.223  1.00  0.00           H
ATOM   1909 HE21 GLN A 132      31.008 -78.029 -43.153  1.00  0.00           H
ATOM   1910 HE22 GLN A 132      31.350 -77.148 -41.681  1.00  0.00           H
ATOM   1911  N   ASN A 133      33.572 -73.595 -47.529  1.00 24.51           N
ANISOU 1911  N   ASN A 133     3184   2073   4057    421   -403   -575       N
ATOM   1912  CA  ASN A 133      34.730 -72.744 -47.807  1.00 25.38           C
ANISOU 1912  CA  ASN A 133     3209   2219   4213    511   -379   -578       C
ATOM   1913  C   ASN A 133      35.097 -72.604 -49.270  1.00 26.61           C
ANISOU 1913  C   ASN A 133     3344   2414   4353    543   -285   -662       C
ATOM   1914  O   ASN A 133      36.283 -72.548 -49.603  1.00 28.20           O
ANISOU 1914  O   ASN A 133     3498   2623   4593    601   -238   -648       O
ATOM   1915  CB  ASN A 133      35.965 -73.277 -47.071  1.00 26.31           C
ANISOU 1915  CB  ASN A 133     3308   2273   4416    569   -410   -508       C
ATOM   1916  CG  ASN A 133      35.703 -73.516 -45.597  1.00 30.27           C
ANISOU 1916  CG  ASN A 133     3849   2723   4929    544   -508   -419       C
ATOM   1917  OD1 ASN A 133      35.130 -72.674 -44.898  1.00 32.53           O
ANISOU 1917  OD1 ASN A 133     4129   3073   5157    508   -551   -379       O
ATOM   1918  ND2 ASN A 133      36.080 -74.689 -45.121  1.00 32.82           N
ANISOU 1918  ND2 ASN A 133     4224   2942   5306    556   -537   -382       N
ATOM   1919  H   ASN A 133      32.737 -73.170 -47.152  1.00  0.00           H
ATOM   1920  HA  ASN A 133      34.514 -71.748 -47.420  1.00  0.00           H
ATOM   1921  HB2 ASN A 133      36.266 -74.219 -47.530  1.00  0.00           H
ATOM   1922  HB3 ASN A 133      36.777 -72.557 -47.174  1.00  0.00           H
ATOM   1923 HD21 ASN A 133      36.531 -75.359 -45.728  1.00  0.00           H
ATOM   1924 HD22 ASN A 133      35.917 -74.916 -44.150  1.00  0.00           H
ATOM   1925  N   GLY A 134      34.105 -72.544 -50.140  1.00 25.02           N
ANISOU 1925  N   GLY A 134     3180   2254   4070    492   -254   -735       N
ATOM   1926  CA  GLY A 134      34.366 -72.367 -51.549  1.00 26.38           C
ANISOU 1926  CA  GLY A 134     3351   2465   4205    519   -168   -815       C
ATOM   1927  C   GLY A 134      35.058 -71.037 -51.802  1.00 26.63           C
ANISOU 1927  C   GLY A 134     3302   2602   4215    562   -126   -785       C
ATOM   1928  O   GLY A 134      34.864 -70.089 -51.043  1.00 25.96           O
ANISOU 1928  O   GLY A 134     3170   2575   4120    554   -172   -733       O
ATOM   1929  H   GLY A 134      33.152 -72.623 -49.816  1.00  0.00           H
ATOM   1930  HA2 GLY A 134      33.422 -72.389 -52.094  1.00  0.00           H
ATOM   1931  HA3 GLY A 134      35.004 -73.178 -51.902  1.00  0.00           H
ATOM   1932  N   GLY A 135      35.874 -70.969 -52.849  1.00 27.12           N
ANISOU 1932  N   GLY A 135     3354   2681   4268    603    -37   -813       N
ATOM   1933  CA  GLY A 135      36.562 -69.726 -53.164  1.00 27.54           C
ANISOU 1933  CA  GLY A 135     3339   2824   4301    631     11   -779       C
ATOM   1934  C   GLY A 135      36.672 -69.514 -54.662  1.00 26.38           C
ANISOU 1934  C   GLY A 135     3225   2717   4081    644    111   -842       C
ATOM   1935  O   GLY A 135      36.268 -70.371 -55.441  1.00 26.26           O
ANISOU 1935  O   GLY A 135     3287   2661   4029    634    139   -915       O
ATOM   1936  H   GLY A 135      36.017 -71.784 -53.429  1.00  0.00           H
ATOM   1937  HA2 GLY A 135      36.008 -68.895 -52.729  1.00  0.00           H
ATOM   1938  HA3 GLY A 135      37.563 -69.753 -52.733  1.00  0.00           H
ATOM   1939  N   SER A 136      37.264 -68.395 -55.050  1.00 25.17           N
ANISOU 1939  N   SER A 136     3022   2636   3905    664    163   -810       N
ATOM   1940  CA  SER A 136      37.269 -67.947 -56.430  1.00 26.84           C
ANISOU 1940  CA  SER A 136     3272   2899   4028    674    255   -857       C
ATOM   1941  C   SER A 136      38.506 -67.112 -56.705  1.00 25.98           C
ANISOU 1941  C   SER A 136     3099   2822   3949    714    327   -806       C
ATOM   1942  O   SER A 136      38.983 -66.377 -55.830  1.00 24.94           O
ANISOU 1942  O   SER A 136     2890   2713   3873    712    287   -733       O
ATOM   1943  CB  SER A 136      36.033 -67.069 -56.681  1.00 30.05           C
ANISOU 1943  CB  SER A 136     3700   3393   4324    630    223   -878       C
ATOM   1944  OG  SER A 136      36.014 -66.588 -58.008  1.00 34.06           O
ANISOU 1944  OG  SER A 136     4256   3952   4732    639    305   -917       O
ATOM   1945  H   SER A 136      37.732 -67.829 -54.356  1.00  0.00           H
ATOM   1946  HA  SER A 136      37.250 -68.809 -57.097  1.00  0.00           H
ATOM   1947  HB2 SER A 136      36.053 -66.222 -55.995  1.00  0.00           H
ATOM   1948  HB3 SER A 136      35.133 -67.656 -56.499  1.00  0.00           H
ATOM   1949  HG  SER A 136      36.006 -67.330 -58.617  1.00  0.00           H
ATOM   1950  N   ASN A 137      39.018 -67.198 -57.927  1.00 27.83           N
ANISOU 1950  N   ASN A 137     3371   3061   4141    747    429   -846       N
ATOM   1951  CA  ASN A 137      40.123 -66.336 -58.321  1.00 28.83           C
ANISOU 1951  CA  ASN A 137     3439   3226   4287    780    503   -806       C
ATOM   1952  C   ASN A 137      39.699 -64.888 -58.586  1.00 30.09           C
ANISOU 1952  C   ASN A 137     3589   3473   4370    754    515   -775       C
ATOM   1953  O   ASN A 137      40.559 -64.038 -58.856  1.00 29.98           O
ANISOU 1953  O   ASN A 137     3524   3493   4374    772    570   -738       O
ATOM   1954  CB  ASN A 137      40.860 -66.914 -59.515  1.00 31.07           C
ANISOU 1954  CB  ASN A 137     3763   3489   4552    829    610   -861       C
ATOM   1955  CG  ASN A 137      41.723 -68.093 -59.117  1.00 37.13           C
ANISOU 1955  CG  ASN A 137     4503   4173   5433    870    606   -869       C
ATOM   1956  OD1 ASN A 137      42.345 -68.095 -58.038  1.00 38.83           O
ANISOU 1956  OD1 ASN A 137     4633   4364   5756    875    548   -810       O
ATOM   1957  ND2 ASN A 137      41.759 -69.111 -59.971  1.00 41.04           N
ANISOU 1957  ND2 ASN A 137     5074   4620   5897    902    661   -944       N
ATOM   1958  H   ASN A 137      38.640 -67.864 -58.586  1.00  0.00           H
ATOM   1959  HA  ASN A 137      40.827 -66.317 -57.489  1.00  0.00           H
ATOM   1960  HB2 ASN A 137      40.131 -67.243 -60.256  1.00  0.00           H
ATOM   1961  HB3 ASN A 137      41.491 -66.141 -59.954  1.00  0.00           H
ATOM   1962 HD21 ASN A 137      41.233 -69.067 -60.832  1.00  0.00           H
ATOM   1963 HD22 ASN A 137      42.312 -69.929 -59.759  1.00  0.00           H
ATOM   1964  N   ALA A 138      38.394 -64.621 -58.475  1.00 30.39           N
ANISOU 1964  N   ALA A 138     3671   3546   4330    712    458   -794       N
ATOM   1965  CA  ALA A 138      37.858 -63.256 -58.486  1.00 30.74           C
ANISOU 1965  CA  ALA A 138     3700   3669   4312    689    445   -759       C
ATOM   1966  C   ALA A 138      38.071 -62.583 -57.128  1.00 28.41           C
ANISOU 1966  C   ALA A 138     3318   3380   4098    672    365   -681       C
ATOM   1967  O   ALA A 138      37.937 -61.360 -57.001  1.00 27.88           O
ANISOU 1967  O   ALA A 138     3223   3365   4005    660    358   -638       O
ATOM   1968  CB  ALA A 138      36.366 -63.269 -58.811  1.00 31.35           C
ANISOU 1968  CB  ALA A 138     3846   3791   4273    653    393   -815       C
ATOM   1969  H   ALA A 138      37.749 -65.393 -58.379  1.00  0.00           H
ATOM   1970  HA  ALA A 138      38.379 -62.679 -59.250  1.00  0.00           H
ATOM   1971  HB1 ALA A 138      35.986 -62.248 -58.815  1.00  0.00           H
ATOM   1972  HB2 ALA A 138      35.835 -63.851 -58.058  1.00  0.00           H
ATOM   1973  HB3 ALA A 138      36.212 -63.718 -59.792  1.00  0.00           H
ATOM   1974  N   CYS A 139      38.383 -63.390 -56.122  1.00 25.06           N
ANISOU 1974  N   CYS A 139     2859   2898   3764    672    303   -664       N
ATOM   1975  CA  CYS A 139      38.534 -62.925 -54.759  1.00 23.67           C
ANISOU 1975  CA  CYS A 139     2621   2723   3649    652    216   -596       C
ATOM   1976  C   CYS A 139      39.760 -63.534 -54.076  1.00 26.42           C
ANISOU 1976  C   CYS A 139     2917   3012   4109    673    201   -563       C
ATOM   1977  O   CYS A 139      39.627 -64.266 -53.092  1.00 29.14           O
ANISOU 1977  O   CYS A 139     3259   3312   4501    665    123   -551       O
ATOM   1978  CB  CYS A 139      37.268 -63.244 -53.976  1.00 23.23           C
ANISOU 1978  CB  CYS A 139     2592   2671   3564    620    120   -610       C
ATOM   1979  SG  CYS A 139      37.282 -62.625 -52.276  1.00 25.87           S
ANISOU 1979  SG  CYS A 139     2873   3012   3942    593     14   -531       S
ATOM   1980  H   CYS A 139      38.521 -64.372 -56.315  1.00  0.00           H
ATOM   1981  HA  CYS A 139      38.658 -61.842 -54.780  1.00  0.00           H
ATOM   1982  HB2 CYS A 139      37.147 -64.327 -53.946  1.00  0.00           H
ATOM   1983  HB3 CYS A 139      36.415 -62.811 -54.499  1.00  0.00           H
ATOM   1984  N   LYS A 140      40.951 -63.185 -54.565  1.00 28.49           N
ANISOU 1984  N   LYS A 140     3135   3277   4413    699    270   -548       N
ATOM   1985  CA  LYS A 140      42.191 -63.752 -54.025  1.00 32.26           C
ANISOU 1985  CA  LYS A 140     3553   3704   5001    724    256   -527       C
ATOM   1986  C   LYS A 140      42.473 -63.274 -52.614  1.00 29.32           C
ANISOU 1986  C   LYS A 140     3127   3331   4680    696    155   -465       C
ATOM   1987  O   LYS A 140      42.242 -62.106 -52.269  1.00 28.62           O
ANISOU 1987  O   LYS A 140     3025   3291   4560    664    129   -431       O
ATOM   1988  CB  LYS A 140      43.368 -63.411 -54.927  1.00 38.83           C
ANISOU 1988  CB  LYS A 140     4339   4547   5868    755    356   -534       C
ATOM   1989  CG  LYS A 140      43.236 -63.987 -56.341  1.00 47.12           C
ANISOU 1989  CG  LYS A 140     5450   5593   6860    789    463   -601       C
ATOM   1990  CD  LYS A 140      44.345 -63.462 -57.245  1.00 54.59           C
ANISOU 1990  CD  LYS A 140     6348   6562   7831    813    569   -606       C
ATOM   1991  CE  LYS A 140      44.045 -63.666 -58.725  1.00 59.39           C
ANISOU 1991  CE  LYS A 140     7035   7190   8341    837    679   -670       C
ATOM   1992  NZ  LYS A 140      44.103 -65.102 -59.096  1.00 62.66           N
ANISOU 1992  NZ  LYS A 140     7498   7544   8765    877    702   -731       N
ATOM   1993  H   LYS A 140      41.000 -62.518 -55.322  1.00  0.00           H
ATOM   1994  HA  LYS A 140      42.085 -64.837 -54.001  1.00  0.00           H
ATOM   1995  HB2 LYS A 140      43.444 -62.326 -55.001  1.00  0.00           H
ATOM   1996  HB3 LYS A 140      44.281 -63.797 -54.474  1.00  0.00           H
ATOM   1997  HG2 LYS A 140      42.270 -63.698 -56.756  1.00  0.00           H
ATOM   1998  HG3 LYS A 140      43.296 -65.074 -56.293  1.00  0.00           H
ATOM   1999  HD2 LYS A 140      45.270 -63.985 -57.002  1.00  0.00           H
ATOM   2000  HD3 LYS A 140      44.481 -62.397 -57.056  1.00  0.00           H
ATOM   2001  HE2 LYS A 140      43.047 -63.284 -58.940  1.00  0.00           H
ATOM   2002  HE3 LYS A 140      44.775 -63.114 -59.317  1.00  0.00           H
ATOM   2003  HZ1 LYS A 140      43.900 -65.204 -60.080  1.00  0.00           H
ATOM   2004  HZ2 LYS A 140      45.027 -65.462 -58.904  1.00  0.00           H
ATOM   2005  HZ3 LYS A 140      43.422 -65.617 -58.557  1.00  0.00           H
ATOM   2006  N   ARG A 141      42.986 -64.184 -51.804  1.00 25.86           N
ANISOU 2006  N   ARG A 141     2670   2836   4321    711     97   -453       N
ATOM   2007  CA  ARG A 141      43.365 -63.882 -50.442  1.00 26.63           C
ANISOU 2007  CA  ARG A 141     2728   2925   4467    689     -3   -401       C
ATOM   2008  C   ARG A 141      44.806 -64.347 -50.362  1.00 30.93           C
ANISOU 2008  C   ARG A 141     3202   3428   5122    726      8   -394       C
ATOM   2009  O   ARG A 141      45.089 -65.546 -50.362  1.00 34.08           O
ANISOU 2009  O   ARG A 141     3609   3768   5572    764      6   -412       O
ATOM   2010  CB  ARG A 141      42.463 -64.628 -49.459  1.00 27.97           C
ANISOU 2010  CB  ARG A 141     2949   3061   4617    674    -95   -392       C
ATOM   2011  CG  ARG A 141      42.745 -64.316 -48.008  1.00 28.79           C
ANISOU 2011  CG  ARG A 141     3031   3159   4749    651   -202   -339       C
ATOM   2012  CD  ARG A 141      41.797 -65.068 -47.087  1.00 26.46           C
ANISOU 2012  CD  ARG A 141     2797   2829   4427    637   -286   -328       C
ATOM   2013  NE  ARG A 141      40.441 -64.496 -47.143  1.00 23.39           N
ANISOU 2013  NE  ARG A 141     2454   2488   3943    602   -290   -339       N
ATOM   2014  CZ  ARG A 141      40.072 -63.357 -46.576  1.00 21.30           C
ANISOU 2014  CZ  ARG A 141     2189   2278   3625    568   -323   -313       C
ATOM   2015  NH1 ARG A 141      40.946 -62.619 -45.896  1.00 21.55           N
ANISOU 2015  NH1 ARG A 141     2182   2320   3687    557   -358   -277       N
ATOM   2016  NH2 ARG A 141      38.829 -62.940 -46.728  1.00 19.11           N
ANISOU 2016  NH2 ARG A 141     1948   2043   3268    546   -321   -329       N
ATOM   2017  H   ARG A 141      43.118 -65.124 -52.149  1.00  0.00           H
ATOM   2018  HA  ARG A 141      43.306 -62.808 -50.265  1.00  0.00           H
ATOM   2019  HB2 ARG A 141      42.601 -65.698 -49.612  1.00  0.00           H
ATOM   2020  HB3 ARG A 141      41.425 -64.375 -49.676  1.00  0.00           H
ATOM   2021  HG2 ARG A 141      43.770 -64.605 -47.775  1.00  0.00           H
ATOM   2022  HG3 ARG A 141      42.629 -63.245 -47.843  1.00  0.00           H
ATOM   2023  HD2 ARG A 141      42.169 -65.004 -46.064  1.00  0.00           H
ATOM   2024  HD3 ARG A 141      41.758 -66.114 -47.390  1.00  0.00           H
ATOM   2025  HE  ARG A 141      39.738 -65.012 -47.653  1.00  0.00           H
ATOM   2026 HH11 ARG A 141      41.901 -62.933 -45.794  1.00  0.00           H
ATOM   2027 HH12 ARG A 141      40.655 -61.745 -45.482  1.00  0.00           H
ATOM   2028 HH21 ARG A 141      38.171 -63.495 -47.257  1.00  0.00           H
ATOM   2029 HH22 ARG A 141      38.535 -62.066 -46.315  1.00  0.00           H
ATOM   2030  N   GLY A 142      45.742 -63.410 -50.366  1.00 34.77           N
ANISOU 2030  N   GLY A 142     3617   3939   5654    718     24   -373       N
ATOM   2031  CA  GLY A 142      47.129 -63.794 -50.555  1.00 39.11           C
ANISOU 2031  CA  GLY A 142     4088   4456   6318    757     56   -378       C
ATOM   2032  C   GLY A 142      47.292 -64.377 -51.955  1.00 41.08           C
ANISOU 2032  C   GLY A 142     4350   4697   6561    801    179   -429       C
ATOM   2033  O   GLY A 142      46.645 -63.928 -52.912  1.00 38.88           O
ANISOU 2033  O   GLY A 142     4118   4459   6195    792    255   -454       O
ATOM   2034  H   GLY A 142      45.494 -62.439 -50.239  1.00  0.00           H
ATOM   2035  HA2 GLY A 142      47.406 -64.542 -49.812  1.00  0.00           H
ATOM   2036  HA3 GLY A 142      47.769 -62.918 -50.447  1.00  0.00           H
ATOM   2037  N   PRO A 143      48.157 -65.382 -52.101  1.00 44.59           N
ANISOU 2037  N   PRO A 143     4758   5089   7095    853    202   -448       N
ATOM   2038  CA  PRO A 143      48.379 -65.797 -53.491  1.00 47.08           C
ANISOU 2038  CA  PRO A 143     5089   5402   7398    895    332   -503       C
ATOM   2039  C   PRO A 143      47.241 -66.642 -54.091  1.00 47.32           C
ANISOU 2039  C   PRO A 143     5232   5414   7334    908    359   -550       C
ATOM   2040  O   PRO A 143      47.048 -66.608 -55.305  1.00 50.80           O
ANISOU 2040  O   PRO A 143     5714   5876   7712    922    463   -597       O
ATOM   2041  CB  PRO A 143      49.703 -66.567 -53.422  1.00 49.39           C
ANISOU 2041  CB  PRO A 143     5300   5642   7825    951    348   -511       C
ATOM   2042  CG  PRO A 143      49.801 -67.059 -52.005  1.00 49.35           C
ANISOU 2042  CG  PRO A 143     5278   5592   7879    949    212   -469       C
ATOM   2043  CD  PRO A 143      49.005 -66.105 -51.136  1.00 46.31           C
ANISOU 2043  CD  PRO A 143     4921   5250   7424    881    122   -425       C
ATOM   2044  HA  PRO A 143      48.520 -64.908 -54.106  1.00  0.00           H
ATOM   2045  HB2 PRO A 143      49.693 -67.406 -54.118  1.00  0.00           H
ATOM   2046  HB3 PRO A 143      50.537 -65.902 -53.647  1.00  0.00           H
ATOM   2047  HG2 PRO A 143      50.843 -67.071 -51.686  1.00  0.00           H
ATOM   2048  HG3 PRO A 143      49.381 -68.062 -51.933  1.00  0.00           H
ATOM   2049  HD2 PRO A 143      49.665 -65.418 -50.607  1.00  0.00           H
ATOM   2050  HD3 PRO A 143      48.388 -66.660 -50.429  1.00  0.00           H
ATOM   2051  N   GLY A 144      46.468 -67.343 -53.271  1.00 43.14           N
ANISOU 2051  N   GLY A 144     4756   4846   6790    897    269   -540       N
ATOM   2052  CA  GLY A 144      45.435 -68.229 -53.796  1.00 40.10           C
ANISOU 2052  CA  GLY A 144     4473   4428   6334    904    290   -590       C
ATOM   2053  C   GLY A 144      44.013 -67.670 -53.929  1.00 35.26           C
ANISOU 2053  C   GLY A 144     3932   3862   5603    851    273   -598       C
ATOM   2054  O   GLY A 144      43.696 -66.540 -53.480  1.00 33.81           O
ANISOU 2054  O   GLY A 144     3724   3737   5384    808    235   -557       O
ATOM   2055  H   GLY A 144      46.596 -67.262 -52.272  1.00  0.00           H
ATOM   2056  HA2 GLY A 144      45.383 -69.095 -53.136  1.00  0.00           H
ATOM   2057  HA3 GLY A 144      45.755 -68.574 -54.779  1.00  0.00           H
ATOM   2058  N   SER A 145      43.156 -68.466 -54.569  1.00 31.08           N
ANISOU 2058  N   SER A 145     3493   3303   5015    854    302   -656       N
ATOM   2059  CA  SER A 145      41.726 -68.196 -54.621  1.00 29.22           C
ANISOU 2059  CA  SER A 145     3324   3097   4680    805    271   -676       C
ATOM   2060  C   SER A 145      41.187 -68.053 -53.207  1.00 25.67           C
ANISOU 2060  C   SER A 145     2858   2643   4253    766    151   -622       C
ATOM   2061  O   SER A 145      41.690 -68.661 -52.254  1.00 25.61           O
ANISOU 2061  O   SER A 145     2823   2581   4325    780     87   -586       O
ATOM   2062  CB  SER A 145      40.987 -69.336 -55.347  1.00 33.13           C
ANISOU 2062  CB  SER A 145     3919   3538   5132    810    301   -754       C
ATOM   2063  OG  SER A 145      41.084 -70.534 -54.587  1.00 36.17           O
ANISOU 2063  OG  SER A 145     4317   3831   5593    823    241   -749       O
ATOM   2064  H   SER A 145      43.512 -69.288 -55.036  1.00  0.00           H
ATOM   2065  HA  SER A 145      41.560 -67.264 -55.161  1.00  0.00           H
ATOM   2066  HB2 SER A 145      41.437 -69.492 -56.327  1.00  0.00           H
ATOM   2067  HB3 SER A 145      39.937 -69.068 -55.469  1.00  0.00           H
ATOM   2068  HG  SER A 145      40.622 -71.241 -55.043  1.00  0.00           H
ATOM   2069  N   GLY A 146      40.148 -67.244 -53.044  1.00 21.82           N
ANISOU 2069  N   GLY A 146     2387   2213   3689    721    118   -616       N
ATOM   2070  CA  GLY A 146      39.573 -67.048 -51.728  1.00 21.11           C
ANISOU 2070  CA  GLY A 146     2287   2125   3607    686      9   -569       C
ATOM   2071  C   GLY A 146      38.138 -66.519 -51.801  1.00 20.93           C
ANISOU 2071  C   GLY A 146     2304   2155   3492    644    -17   -594       C
ATOM   2072  O   GLY A 146      37.487 -66.586 -52.845  1.00 21.74           O
ANISOU 2072  O   GLY A 146     2454   2279   3527    639     35   -657       O
ATOM   2073  H   GLY A 146      39.756 -66.763 -53.841  1.00  0.00           H
ATOM   2074  HA2 GLY A 146      40.185 -66.331 -51.180  1.00  0.00           H
ATOM   2075  HA3 GLY A 146      39.575 -67.998 -51.194  1.00  0.00           H
ATOM   2076  N   PHE A 147      37.644 -65.981 -50.690  1.00 19.09           N
ANISOU 2076  N   PHE A 147     2056   1946   3250    616   -101   -548       N
ATOM   2077  CA  PHE A 147      36.267 -65.542 -50.625  1.00 18.19           C
ANISOU 2077  CA  PHE A 147     1971   1881   3058    584   -135   -572       C
ATOM   2078  C   PHE A 147      36.153 -64.559 -49.465  1.00 20.47           C
ANISOU 2078  C   PHE A 147     2227   2214   3336    563   -203   -505       C
ATOM   2079  O   PHE A 147      37.110 -64.386 -48.696  1.00 21.99           O
ANISOU 2079  O   PHE A 147     2387   2389   3581    567   -231   -449       O
ATOM   2080  CB  PHE A 147      35.377 -66.756 -50.376  1.00 16.93           C
ANISOU 2080  CB  PHE A 147     1872   1654   2908    570   -180   -615       C
ATOM   2081  CG  PHE A 147      33.930 -66.566 -50.717  1.00 17.90           C
ANISOU 2081  CG  PHE A 147     2040   1844   2917    510   -190   -645       C
ATOM   2082  CD1 PHE A 147      33.520 -66.414 -52.038  1.00 20.44           C
ANISOU 2082  CD1 PHE A 147     2390   2213   3162    504   -130   -708       C
ATOM   2083  CD2 PHE A 147      32.959 -66.641 -49.736  1.00 17.85           C
ANISOU 2083  CD2 PHE A 147     2055   1857   2869    451   -256   -602       C
ATOM   2084  CE1 PHE A 147      32.152 -66.284 -52.374  1.00 20.27           C
ANISOU 2084  CE1 PHE A 147     2407   2263   3033    440   -152   -727       C
ATOM   2085  CE2 PHE A 147      31.586 -66.521 -50.069  1.00 19.15           C
ANISOU 2085  CE2 PHE A 147     2250   2093   2933    385   -263   -622       C
ATOM   2086  CZ  PHE A 147      31.198 -66.338 -51.390  1.00 19.29           C
ANISOU 2086  CZ  PHE A 147     2285   2160   2885    382   -218   -685       C
ATOM   2087  H   PHE A 147      38.238 -65.877 -49.880  1.00  0.00           H
ATOM   2088  HA  PHE A 147      35.984 -65.055 -51.558  1.00  0.00           H
ATOM   2089  HB2 PHE A 147      35.444 -67.012 -49.319  1.00  0.00           H
ATOM   2090  HB3 PHE A 147      35.762 -67.593 -50.959  1.00  0.00           H
ATOM   2091  HD1 PHE A 147      34.261 -66.395 -52.823  1.00  0.00           H
ATOM   2092  HD2 PHE A 147      33.249 -66.792 -48.707  1.00  0.00           H
ATOM   2093  HE1 PHE A 147      31.859 -66.142 -53.404  1.00  0.00           H
ATOM   2094  HE2 PHE A 147      30.838 -66.572 -49.292  1.00  0.00           H
ATOM   2095  HZ  PHE A 147      30.152 -66.239 -51.641  1.00  0.00           H
ATOM   2096  N   PHE A 148      34.988 -63.912 -49.365  1.00 21.03           N
ANISOU 2096  N   PHE A 148     2309   2346   3334    541   -229   -517       N
ATOM   2097  CA  PHE A 148      34.663 -63.027 -48.246  1.00 19.94           C
ANISOU 2097  CA  PHE A 148     2155   2250   3170    520   -291   -462       C
ATOM   2098  C   PHE A 148      34.914 -63.761 -46.939  1.00 19.44           C
ANISOU 2098  C   PHE A 148     2106   2119   3161    517   -368   -419       C
ATOM   2099  O   PHE A 148      34.503 -64.936 -46.786  1.00 20.28           O
ANISOU 2099  O   PHE A 148     2259   2167   3278    503   -387   -430       O
ATOM   2100  CB  PHE A 148      33.182 -62.685 -48.289  1.00 18.98           C
ANISOU 2100  CB  PHE A 148     2066   2203   2941    473   -301   -471       C
ATOM   2101  CG  PHE A 148      32.750 -61.988 -49.542  1.00 17.36           C
ANISOU 2101  CG  PHE A 148     1861   2069   2667    475   -243   -508       C
ATOM   2102  CD1 PHE A 148      33.074 -60.659 -49.742  1.00 17.72           C
ANISOU 2102  CD1 PHE A 148     1870   2164   2700    498   -221   -489       C
ATOM   2103  CD2 PHE A 148      32.024 -62.662 -50.513  1.00 16.14           C
ANISOU 2103  CD2 PHE A 148     1749   1926   2458    452   -216   -561       C
ATOM   2104  CE1 PHE A 148      32.676 -60.003 -50.889  1.00 17.60           C
ANISOU 2104  CE1 PHE A 148     1865   2209   2613    503   -172   -513       C
ATOM   2105  CE2 PHE A 148      31.620 -62.030 -51.663  1.00 17.32           C
ANISOU 2105  CE2 PHE A 148     1909   2141   2532    456   -174   -591       C
ATOM   2106  CZ  PHE A 148      31.949 -60.678 -51.845  1.00 17.45           C
ANISOU 2106  CZ  PHE A 148     1892   2207   2531    484   -152   -562       C
ATOM   2107  H   PHE A 148      34.301 -64.040 -50.094  1.00  0.00           H
ATOM   2108  HA  PHE A 148      35.264 -62.119 -48.293  1.00  0.00           H
ATOM   2109  HB2 PHE A 148      32.614 -63.611 -48.200  1.00  0.00           H
ATOM   2110  HB3 PHE A 148      32.946 -62.048 -47.436  1.00  0.00           H
ATOM   2111  HD1 PHE A 148      33.644 -60.129 -48.993  1.00  0.00           H
ATOM   2112  HD2 PHE A 148      31.772 -63.701 -50.362  1.00  0.00           H
ATOM   2113  HE1 PHE A 148      32.933 -58.965 -51.037  1.00  0.00           H
ATOM   2114  HE2 PHE A 148      31.058 -62.564 -52.415  1.00  0.00           H
ATOM   2115  HZ  PHE A 148      31.630 -60.164 -52.740  1.00  0.00           H
ATOM   2116  N   SER A 149      35.498 -63.068 -45.978  1.00 18.35           N
ANISOU 2116  N   SER A 149     1951   1995   3025    505   -407   -360       N
ATOM   2117  CA  SER A 149      35.889 -63.715 -44.733  1.00 18.81           C
ANISOU 2117  CA  SER A 149     2031   1992   3124    504   -485   -314       C
ATOM   2118  C   SER A 149      34.658 -64.070 -43.892  1.00 16.70           C
ANISOU 2118  C   SER A 149     1818   1719   2807    480   -546   -299       C
ATOM   2119  O   SER A 149      34.711 -64.991 -43.108  1.00 16.92           O
ANISOU 2119  O   SER A 149     1892   1681   2856    472   -597   -264       O
ATOM   2120  CB  SER A 149      36.825 -62.805 -43.930  1.00 20.40           C
ANISOU 2120  CB  SER A 149     2209   2215   3328    492   -513   -266       C
ATOM   2121  OG  SER A 149      36.123 -61.635 -43.503  1.00 19.34           O
ANISOU 2121  OG  SER A 149     2085   2148   3116    465   -523   -256       O
ATOM   2122  H   SER A 149      35.675 -62.082 -46.107  1.00  0.00           H
ATOM   2123  HA  SER A 149      36.422 -64.635 -44.973  1.00  0.00           H
ATOM   2124  HB2 SER A 149      37.191 -63.345 -43.057  1.00  0.00           H
ATOM   2125  HB3 SER A 149      37.669 -62.513 -44.555  1.00  0.00           H
ATOM   2126  HG  SER A 149      36.482 -60.865 -43.950  1.00  0.00           H
ATOM   2127  N   ARG A 150      33.539 -63.359 -44.067  1.00 14.53           N
ANISOU 2127  N   ARG A 150     1556   1532   2433    438   -514   -310       N
ATOM   2128  CA  ARG A 150      32.384 -63.568 -43.181  1.00 14.74           C
ANISOU 2128  CA  ARG A 150     1640   1584   2376    378   -537   -280       C
ATOM   2129  C   ARG A 150      31.329 -64.499 -43.779  1.00 17.27           C
ANISOU 2129  C   ARG A 150     1995   1904   2663    329   -499   -312       C
ATOM   2130  O   ARG A 150      30.309 -64.787 -43.158  1.00 20.52           O
ANISOU 2130  O   ARG A 150     2445   2335   3016    271   -504   -291       O
ATOM   2131  CB  ARG A 150      31.774 -62.219 -42.756  1.00 12.88           C
ANISOU 2131  CB  ARG A 150     1391   1439   2062    363   -534   -269       C
ATOM   2132  CG  ARG A 150      32.744 -61.276 -42.002  1.00 14.93           C
ANISOU 2132  CG  ARG A 150     1629   1694   2349    399   -585   -240       C
ATOM   2133  CD  ARG A 150      33.553 -61.980 -40.912  1.00 15.25           C
ANISOU 2133  CD  ARG A 150     1703   1656   2437    410   -665   -193       C
ATOM   2134  NE  ARG A 150      34.206 -60.981 -40.057  1.00 14.88           N
ANISOU 2134  NE  ARG A 150     1654   1623   2377    413   -706   -168       N
ATOM   2135  CZ  ARG A 150      35.006 -61.287 -39.048  1.00 16.59           C
ANISOU 2135  CZ  ARG A 150     1903   1789   2612    412   -771   -127       C
ATOM   2136  NH1 ARG A 150      35.356 -62.571 -38.833  1.00 18.58           N
ANISOU 2136  NH1 ARG A 150     2179   1964   2917    426   -814   -103       N
ATOM   2137  NH2 ARG A 150      35.506 -60.314 -38.317  1.00 17.11           N
ANISOU 2137  NH2 ARG A 150     1975   1876   2650    400   -792   -115       N
ATOM   2138  H   ARG A 150      33.487 -62.677 -44.810  1.00  0.00           H
ATOM   2139  HA  ARG A 150      32.758 -64.048 -42.277  1.00  0.00           H
ATOM   2140  HB2 ARG A 150      30.924 -62.422 -42.105  1.00  0.00           H
ATOM   2141  HB3 ARG A 150      31.414 -61.705 -43.647  1.00  0.00           H
ATOM   2142  HG2 ARG A 150      33.438 -60.846 -42.724  1.00  0.00           H
ATOM   2143  HG3 ARG A 150      32.168 -60.471 -41.547  1.00  0.00           H
ATOM   2144  HD2 ARG A 150      34.311 -62.612 -41.375  1.00  0.00           H
ATOM   2145  HD3 ARG A 150      32.888 -62.596 -40.307  1.00  0.00           H
ATOM   2146  HE  ARG A 150      34.035 -60.004 -40.250  1.00  0.00           H
ATOM   2147 HH11 ARG A 150      34.985 -63.302 -39.423  1.00  0.00           H
ATOM   2148 HH12 ARG A 150      35.990 -62.802 -38.081  1.00  0.00           H
ATOM   2149 HH21 ARG A 150      35.254 -59.355 -38.512  1.00  0.00           H
ATOM   2150 HH22 ARG A 150      36.141 -60.526 -37.561  1.00  0.00           H
ATOM   2151  N   LEU A 151      31.588 -64.993 -44.981  1.00 16.05           N
ANISOU 2151  N   LEU A 151     1827   1724   2546    348   -458   -365       N
ATOM   2152  CA  LEU A 151      30.646 -65.819 -45.681  1.00 16.32           C
ANISOU 2152  CA  LEU A 151     1892   1757   2550    300   -428   -407       C
ATOM   2153  C   LEU A 151      31.284 -67.171 -46.029  1.00 17.86           C
ANISOU 2153  C   LEU A 151     2122   1839   2825    317   -427   -430       C
ATOM   2154  O   LEU A 151      32.500 -67.286 -46.129  1.00 18.26           O
ANISOU 2154  O   LEU A 151     2151   1832   2956    383   -429   -430       O
ATOM   2155  CB  LEU A 151      30.207 -65.123 -46.954  1.00 15.46           C
ANISOU 2155  CB  LEU A 151     1753   1728   2392    304   -380   -462       C
ATOM   2156  CG  LEU A 151      29.379 -63.828 -46.713  1.00 19.72           C
ANISOU 2156  CG  LEU A 151     2262   2377   2854    288   -380   -443       C
ATOM   2157  CD1 LEU A 151      29.158 -63.054 -48.011  1.00 19.03           C
ANISOU 2157  CD1 LEU A 151     2147   2358   2723    309   -341   -487       C
ATOM   2158  CD2 LEU A 151      28.048 -64.151 -46.058  1.00 18.85           C
ANISOU 2158  CD2 LEU A 151     2170   2300   2693    216   -394   -427       C
ATOM   2159  H   LEU A 151      32.474 -64.782 -45.417  1.00  0.00           H
ATOM   2160  HA  LEU A 151      29.776 -65.987 -45.046  1.00  0.00           H
ATOM   2161  HB2 LEU A 151      31.097 -64.859 -47.525  1.00  0.00           H
ATOM   2162  HB3 LEU A 151      29.607 -65.817 -47.543  1.00  0.00           H
ATOM   2163  HG  LEU A 151      29.943 -63.190 -46.033  1.00  0.00           H
ATOM   2164 HD11 LEU A 151      30.121 -62.830 -48.469  1.00  0.00           H
ATOM   2165 HD12 LEU A 151      28.562 -63.657 -48.696  1.00  0.00           H
ATOM   2166 HD13 LEU A 151      28.633 -62.124 -47.794  1.00  0.00           H
ATOM   2167 HD21 LEU A 151      28.222 -64.703 -45.134  1.00  0.00           H
ATOM   2168 HD22 LEU A 151      27.448 -64.758 -46.736  1.00  0.00           H
ATOM   2169 HD23 LEU A 151      27.519 -63.225 -45.834  1.00  0.00           H
ATOM   2170  N   ASN A 152      30.437 -68.164 -46.259  1.00 17.95           N
ANISOU 2170  N   ASN A 152     2181   1819   2820    259   -421   -455       N
ATOM   2171  CA  ASN A 152      30.872 -69.546 -46.392  1.00 18.66           C
ANISOU 2171  CA  ASN A 152     2320   1785   2983    265   -426   -472       C
ATOM   2172  C   ASN A 152      30.159 -70.135 -47.607  1.00 19.85           C
ANISOU 2172  C   ASN A 152     2497   1939   3108    226   -387   -554       C
ATOM   2173  O   ASN A 152      28.981 -70.442 -47.565  1.00 19.06           O
ANISOU 2173  O   ASN A 152     2420   1865   2958    145   -393   -562       O
ATOM   2174  CB  ASN A 152      30.512 -70.319 -45.120  1.00 19.38           C
ANISOU 2174  CB  ASN A 152     2468   1812   3082    217   -473   -404       C
ATOM   2175  CG  ASN A 152      31.117 -71.708 -45.085  1.00 21.57           C
ANISOU 2175  CG  ASN A 152     2803   1944   3450    236   -489   -406       C
ATOM   2176  OD1 ASN A 152      31.682 -72.205 -46.080  1.00 21.64           O
ANISOU 2176  OD1 ASN A 152     2810   1897   3514    280   -458   -471       O
ATOM   2177  ND2 ASN A 152      31.000 -72.350 -43.936  1.00 23.26           N
ANISOU 2177  ND2 ASN A 152     3074   2089   3674    205   -535   -333       N
ATOM   2178  H   ASN A 152      29.453 -67.954 -46.345  1.00  0.00           H
ATOM   2179  HA  ASN A 152      31.950 -69.578 -46.548  1.00  0.00           H
ATOM   2180  HB2 ASN A 152      29.427 -70.410 -45.064  1.00  0.00           H
ATOM   2181  HB3 ASN A 152      30.865 -69.758 -44.254  1.00  0.00           H
ATOM   2182 HD21 ASN A 152      31.378 -73.282 -43.837  1.00  0.00           H
ATOM   2183 HD22 ASN A 152      30.533 -71.909 -43.156  1.00  0.00           H
ATOM   2184  N   TRP A 153      30.886 -70.269 -48.702  1.00 22.42           N
ANISOU 2184  N   TRP A 153     2818   2238   3465    282   -345   -618       N
ATOM   2185  CA  TRP A 153      30.320 -70.729 -49.936  1.00 22.27           C
ANISOU 2185  CA  TRP A 153     2831   2223   3406    252   -311   -704       C
ATOM   2186  C   TRP A 153      30.216 -72.261 -49.919  1.00 21.91           C
ANISOU 2186  C   TRP A 153     2859   2049   3418    220   -322   -733       C
ATOM   2187  O   TRP A 153      31.231 -72.961 -50.008  1.00 20.54           O
ANISOU 2187  O   TRP A 153     2706   1768   3330    283   -307   -747       O
ATOM   2188  CB  TRP A 153      31.199 -70.260 -51.076  1.00 22.58           C
ANISOU 2188  CB  TRP A 153     2850   2282   3449    327   -251   -759       C
ATOM   2189  CG  TRP A 153      30.654 -70.546 -52.410  1.00 24.74           C
ANISOU 2189  CG  TRP A 153     3166   2576   3657    303   -217   -850       C
ATOM   2190  CD1 TRP A 153      29.492 -71.197 -52.701  1.00 25.79           C
ANISOU 2190  CD1 TRP A 153     3346   2710   3741    220   -245   -891       C
ATOM   2191  CD2 TRP A 153      31.242 -70.194 -53.664  1.00 26.45           C
ANISOU 2191  CD2 TRP A 153     3388   2818   3844    357   -150   -913       C
ATOM   2192  NE1 TRP A 153      29.314 -71.267 -54.055  1.00 26.94           N
ANISOU 2192  NE1 TRP A 153     3531   2881   3824    221   -212   -979       N
ATOM   2193  CE2 TRP A 153      30.371 -70.659 -54.674  1.00 27.47           C
ANISOU 2193  CE2 TRP A 153     3580   2964   3894    306   -149   -993       C
ATOM   2194  CE3 TRP A 153      32.418 -69.521 -54.035  1.00 27.38           C
ANISOU 2194  CE3 TRP A 153     3463   2946   3993    440    -88   -909       C
ATOM   2195  CZ2 TRP A 153      30.644 -70.494 -56.029  1.00 28.44           C
ANISOU 2195  CZ2 TRP A 153     3741   3113   3954    339    -89  -1069       C
ATOM   2196  CZ3 TRP A 153      32.687 -69.360 -55.372  1.00 28.42           C
ANISOU 2196  CZ3 TRP A 153     3626   3103   4071    470    -15   -980       C
ATOM   2197  CH2 TRP A 153      31.803 -69.842 -56.359  1.00 28.93           C
ANISOU 2197  CH2 TRP A 153     3768   3184   4041    422    -16  -1059       C
ATOM   2198  H   TRP A 153      31.869 -70.041 -48.669  1.00  0.00           H
ATOM   2199  HA  TRP A 153      29.323 -70.304 -50.054  1.00  0.00           H
ATOM   2200  HB2 TRP A 153      31.332 -69.182 -50.985  1.00  0.00           H
ATOM   2201  HB3 TRP A 153      32.173 -70.741 -50.986  1.00  0.00           H
ATOM   2202  HD1 TRP A 153      28.810 -71.600 -51.967  1.00  0.00           H
ATOM   2203  HE3 TRP A 153      33.095 -69.139 -53.286  1.00  0.00           H
ATOM   2204  HZ2 TRP A 153      29.971 -70.864 -56.788  1.00  0.00           H
ATOM   2205  HZ3 TRP A 153      33.593 -68.855 -55.673  1.00  0.00           H
ATOM   2206  HH2 TRP A 153      32.045 -69.694 -57.401  1.00  0.00           H
ATOM   2207  HE1 TRP A 153      28.529 -71.698 -54.522  1.00  0.00           H
ATOM   2208  N   LEU A 154      28.983 -72.759 -49.789  1.00 22.16           N
ANISOU 2208  N   LEU A 154     2923   2087   3408    123   -347   -740       N
ATOM   2209  CA  LEU A 154      28.732 -74.205 -49.702  1.00 22.35           C
ANISOU 2209  CA  LEU A 154     3024   1984   3486     73   -361   -763       C
ATOM   2210  C   LEU A 154      28.443 -74.785 -51.068  1.00 22.78           C
ANISOU 2210  C   LEU A 154     3122   2015   3518     54   -335   -875       C
ATOM   2211  O   LEU A 154      27.671 -74.199 -51.823  1.00 22.43           O
ANISOU 2211  O   LEU A 154     3056   2077   3388     16   -333   -920       O
ATOM   2212  CB  LEU A 154      27.504 -74.460 -48.829  1.00 21.68           C
ANISOU 2212  CB  LEU A 154     2948   1916   3373    -37   -395   -711       C
ATOM   2213  CG  LEU A 154      27.516 -73.837 -47.447  1.00 21.40           C
ANISOU 2213  CG  LEU A 154     2883   1921   3328    -36   -418   -604       C
ATOM   2214  CD1 LEU A 154      26.222 -74.191 -46.709  1.00 24.02           C
ANISOU 2214  CD1 LEU A 154     3229   2268   3629   -153   -430   -564       C
ATOM   2215  CD2 LEU A 154      28.740 -74.202 -46.647  1.00 20.02           C
ANISOU 2215  CD2 LEU A 154     2735   1642   3230     38   -439   -544       C
ATOM   2216  H   LEU A 154      28.200 -72.123 -49.749  1.00  0.00           H
ATOM   2217  HA  LEU A 154      29.600 -74.702 -49.269  1.00  0.00           H
ATOM   2218  HB2 LEU A 154      26.634 -74.072 -49.359  1.00  0.00           H
ATOM   2219  HB3 LEU A 154      27.383 -75.537 -48.717  1.00  0.00           H
ATOM   2220  HG  LEU A 154      27.527 -72.755 -47.580  1.00  0.00           H
ATOM   2221 HD11 LEU A 154      26.235 -73.741 -45.716  1.00  0.00           H
ATOM   2222 HD12 LEU A 154      26.142 -75.274 -46.616  1.00  0.00           H
ATOM   2223 HD13 LEU A 154      25.368 -73.810 -47.269  1.00  0.00           H
ATOM   2224 HD21 LEU A 154      29.635 -73.933 -47.208  1.00  0.00           H
ATOM   2225 HD22 LEU A 154      28.729 -73.662 -45.700  1.00  0.00           H
ATOM   2226 HD23 LEU A 154      28.741 -75.275 -46.453  1.00  0.00           H
ATOM   2227  N   THR A 155      29.035 -75.942 -51.373  1.00 23.55           N
ANISOU 2227  N   THR A 155     3286   1971   3689     80   -321   -922       N
ATOM   2228  CA  THR A 155      28.730 -76.663 -52.606  1.00 24.22           C
ANISOU 2228  CA  THR A 155     3436   2014   3753     53   -300  -1038       C
ATOM   2229  C   THR A 155      28.480 -78.155 -52.320  1.00 27.11           C
ANISOU 2229  C   THR A 155     3888   2221   4193     -4   -322  -1056       C
ATOM   2230  O   THR A 155      28.538 -78.623 -51.169  1.00 27.04           O
ANISOU 2230  O   THR A 155     3890   2135   4248    -22   -352   -970       O
ATOM   2231  CB  THR A 155      29.843 -76.486 -53.669  1.00 23.88           C
ANISOU 2231  CB  THR A 155     3400   1959   3716    160   -233  -1111       C
ATOM   2232  OG1 THR A 155      31.096 -76.921 -53.136  1.00 26.13           O
ANISOU 2232  OG1 THR A 155     3679   2144   4104    250   -209  -1062       O
ATOM   2233  CG2 THR A 155      30.000 -74.992 -54.083  1.00 25.23           C
ANISOU 2233  CG2 THR A 155     3496   2286   3804    203   -206  -1095       C
ATOM   2234  H   THR A 155      29.713 -76.330 -50.733  1.00  0.00           H
ATOM   2235  HA  THR A 155      27.810 -76.245 -53.016  1.00  0.00           H
ATOM   2236  HB  THR A 155      29.599 -77.081 -54.549  1.00  0.00           H
ATOM   2237  HG1 THR A 155      31.492 -76.210 -52.626  1.00  0.00           H
ATOM   2238 HG21 THR A 155      30.789 -74.902 -54.830  1.00  0.00           H
ATOM   2239 HG22 THR A 155      30.260 -74.398 -53.207  1.00  0.00           H
ATOM   2240 HG23 THR A 155      29.061 -74.630 -54.501  1.00  0.00           H
ATOM   2241  N   LYS A 156      28.179 -78.908 -53.371  1.00 29.72           N
ANISOU 2241  N   LYS A 156     4287   2506   4500    -37   -306  -1156       N
ATOM   2242  CA  LYS A 156      27.875 -80.316 -53.203  1.00 31.60           C
ANISOU 2242  CA  LYS A 156     4610   2609   4787   -101   -317  -1162       C
ATOM   2243  C   LYS A 156      29.063 -81.043 -52.585  1.00 33.37           C
ANISOU 2243  C   LYS A 156     4866   2703   5112    -13   -292  -1103       C
ATOM   2244  O   LYS A 156      30.208 -80.603 -52.687  1.00 32.63           O
ANISOU 2244  O   LYS A 156     4733   2624   5041    103   -253  -1086       O
ATOM   2245  CB  LYS A 156      27.553 -80.960 -54.543  1.00 33.10           C
ANISOU 2245  CB  LYS A 156     4876   2788   4914   -135   -291  -1268       C
ATOM   2246  CG  LYS A 156      28.759 -81.040 -55.472  1.00 34.80           C
ANISOU 2246  CG  LYS A 156     5123   2979   5119    -16   -214  -1316       C
ATOM   2247  CD  LYS A 156      28.434 -81.823 -56.730  1.00 39.03           C
ANISOU 2247  CD  LYS A 156     5760   3480   5589    -54   -192  -1421       C
ATOM   2248  CE  LYS A 156      29.673 -81.986 -57.611  1.00 41.97           C
ANISOU 2248  CE  LYS A 156     6175   3818   5953     64   -104  -1465       C
ATOM   2249  NZ  LYS A 156      29.257 -82.312 -58.990  1.00 44.00           N
ANISOU 2249  NZ  LYS A 156     6527   4089   6104     30    -86  -1571       N
ATOM   2250  H   LYS A 156      28.162 -78.498 -54.294  1.00  0.00           H
ATOM   2251  HA  LYS A 156      27.013 -80.418 -52.543  1.00  0.00           H
ATOM   2252  HB2 LYS A 156      27.186 -81.970 -54.363  1.00  0.00           H
ATOM   2253  HB3 LYS A 156      26.769 -80.382 -55.032  1.00  0.00           H
ATOM   2254  HG2 LYS A 156      29.578 -81.533 -54.949  1.00  0.00           H
ATOM   2255  HG3 LYS A 156      29.066 -80.031 -55.748  1.00  0.00           H
ATOM   2256  HD2 LYS A 156      28.064 -82.809 -56.450  1.00  0.00           H
ATOM   2257  HD3 LYS A 156      27.662 -81.296 -57.291  1.00  0.00           H
ATOM   2258  HE2 LYS A 156      30.294 -82.791 -57.219  1.00  0.00           H
ATOM   2259  HE3 LYS A 156      30.242 -81.056 -57.613  1.00  0.00           H
ATOM   2260  HZ1 LYS A 156      28.252 -82.239 -59.065  1.00  0.00           H
ATOM   2261  HZ2 LYS A 156      29.691 -81.666 -59.634  1.00  0.00           H
ATOM   2262  HZ3 LYS A 156      29.543 -83.254 -59.214  1.00  0.00           H
ATOM   2263  N   SER A 157      28.767 -82.160 -51.936  1.00 36.19           N
ANISOU 2263  N   SER A 157     5288   2934   5528    -71   -316  -1067       N
ATOM   2264  CA  SER A 157      29.784 -83.091 -51.482  1.00 38.88           C
ANISOU 2264  CA  SER A 157     5677   3138   5957      5   -297  -1020       C
ATOM   2265  C   SER A 157      29.513 -84.447 -52.154  1.00 38.57           C
ANISOU 2265  C   SER A 157     5747   2981   5927    -44   -272  -1090       C
ATOM   2266  O   SER A 157      28.409 -84.975 -52.077  1.00 36.86           O
ANISOU 2266  O   SER A 157     5574   2735   5694   -170   -301  -1105       O
ATOM   2267  CB  SER A 157      29.738 -83.209 -49.960  1.00 41.42           C
ANISOU 2267  CB  SER A 157     5994   3406   6339    -16   -350   -895       C
ATOM   2268  OG  SER A 157      30.682 -84.158 -49.503  1.00 43.91           O
ANISOU 2268  OG  SER A 157     6358   3590   6735     57   -341   -844       O
ATOM   2269  H   SER A 157      27.797 -82.371 -51.750  1.00  0.00           H
ATOM   2270  HA  SER A 157      30.766 -82.728 -51.786  1.00  0.00           H
ATOM   2271  HB2 SER A 157      28.739 -83.523 -49.656  1.00  0.00           H
ATOM   2272  HB3 SER A 157      29.961 -82.238 -49.517  1.00  0.00           H
ATOM   2273  HG  SER A 157      30.638 -84.218 -48.546  1.00  0.00           H
ATOM   2274  N   GLY A 158      30.517 -84.983 -52.837  1.00 42.74           N
ANISOU 2274  N   GLY A 158     6315   3445   6479     54   -215  -1135       N
ATOM   2275  CA  GLY A 158      30.297 -86.122 -53.717  1.00 48.42           C
ANISOU 2275  CA  GLY A 158     7144   4065   7187     18   -183  -1225       C
ATOM   2276  C   GLY A 158      29.343 -85.749 -54.841  1.00 48.88           C
ANISOU 2276  C   GLY A 158     7217   4220   7134    -66   -186  -1327       C
ATOM   2277  O   GLY A 158      29.603 -84.813 -55.599  1.00 49.64           O
ANISOU 2277  O   GLY A 158     7268   4433   7160    -14   -159  -1369       O
ATOM   2278  H   GLY A 158      31.445 -84.596 -52.745  1.00  0.00           H
ATOM   2279  HA2 GLY A 158      31.250 -86.435 -54.144  1.00  0.00           H
ATOM   2280  HA3 GLY A 158      29.872 -86.945 -53.142  1.00  0.00           H
ATOM   2281  N   SER A 159      28.224 -86.457 -54.936  1.00 46.12           N
ANISOU 2281  N   SER A 159     6930   3826   6766   -198   -221  -1362       N
ATOM   2282  CA  SER A 159      27.284 -86.217 -56.023  1.00 44.54           C
ANISOU 2282  CA  SER A 159     6750   3714   6459   -283   -238  -1458       C
ATOM   2283  C   SER A 159      25.935 -85.670 -55.552  1.00 41.43           C
ANISOU 2283  C   SER A 159     6288   3421   6034   -416   -307  -1428       C
ATOM   2284  O   SER A 159      24.974 -85.673 -56.314  1.00 42.96           O
ANISOU 2284  O   SER A 159     6498   3674   6150   -510   -339  -1497       O
ATOM   2285  CB  SER A 159      27.068 -87.512 -56.821  1.00 47.69           C
ANISOU 2285  CB  SER A 159     7282   3991   6849   -334   -222  -1547       C
ATOM   2286  OG  SER A 159      26.548 -88.534 -55.994  1.00 50.11           O
ANISOU 2286  OG  SER A 159     7631   4173   7234   -427   -245  -1505       O
ATOM   2287  H   SER A 159      28.022 -87.169 -54.248  1.00  0.00           H
ATOM   2288  HA  SER A 159      27.728 -85.481 -56.693  1.00  0.00           H
ATOM   2289  HB2 SER A 159      28.022 -87.839 -57.235  1.00  0.00           H
ATOM   2290  HB3 SER A 159      26.370 -87.319 -57.636  1.00  0.00           H
ATOM   2291  HG  SER A 159      26.421 -89.332 -56.512  1.00  0.00           H
ATOM   2292  N   THR A 160      25.870 -85.156 -54.321  1.00 36.31           N
ANISOU 2292  N   THR A 160     5561   2798   5437   -420   -332  -1325       N
ATOM   2293  CA  THR A 160      24.600 -84.696 -53.791  1.00 36.18           C
ANISOU 2293  CA  THR A 160     5479   2869   5400   -545   -388  -1290       C
ATOM   2294  C   THR A 160      24.748 -83.413 -53.004  1.00 34.71           C
ANISOU 2294  C   THR A 160     5185   2794   5212   -498   -404  -1213       C
ATOM   2295  O   THR A 160      25.822 -83.093 -52.496  1.00 34.75           O
ANISOU 2295  O   THR A 160     5172   2772   5259   -385   -382  -1159       O
ATOM   2296  CB  THR A 160      23.971 -85.715 -52.843  1.00 38.47           C
ANISOU 2296  CB  THR A 160     5811   3042   5766   -657   -404  -1231       C
ATOM   2297  OG1 THR A 160      24.929 -86.064 -51.842  1.00 38.27           O
ANISOU 2297  OG1 THR A 160     5809   2907   5826   -575   -384  -1140       O
ATOM   2298  CG2 THR A 160      23.548 -86.969 -53.597  1.00 40.86           C
ANISOU 2298  CG2 THR A 160     6215   3242   6068   -737   -396  -1313       C
ATOM   2299  H   THR A 160      26.706 -85.087 -53.758  1.00  0.00           H
ATOM   2300  HA  THR A 160      23.916 -84.521 -54.622  1.00  0.00           H
ATOM   2301  HB  THR A 160      23.098 -85.271 -52.366  1.00  0.00           H
ATOM   2302  HG1 THR A 160      24.976 -85.365 -51.186  1.00  0.00           H
ATOM   2303 HG21 THR A 160      23.103 -87.680 -52.901  1.00  0.00           H
ATOM   2304 HG22 THR A 160      22.818 -86.704 -54.362  1.00  0.00           H
ATOM   2305 HG23 THR A 160      24.420 -87.421 -54.069  1.00  0.00           H
ATOM   2306  N   TYR A 161      23.644 -82.688 -52.902  1.00 33.69           N
ANISOU 2306  N   TYR A 161     4979   2789   5033   -588   -445  -1208       N
ATOM   2307  CA  TYR A 161      23.554 -81.519 -52.047  1.00 32.63           C
ANISOU 2307  CA  TYR A 161     4745   2756   4897   -570   -463  -1135       C
ATOM   2308  C   TYR A 161      22.217 -81.694 -51.358  1.00 37.45           C
ANISOU 2308  C   TYR A 161     5318   3390   5521   -720   -497  -1093       C
ATOM   2309  O   TYR A 161      21.180 -81.562 -51.997  1.00 34.12           O
ANISOU 2309  O   TYR A 161     4858   3059   5046   -807   -521  -1146       O
ATOM   2310  CB  TYR A 161      23.585 -80.263 -52.905  1.00 29.68           C
ANISOU 2310  CB  TYR A 161     4301   2543   4431   -510   -463  -1187       C
ATOM   2311  CG  TYR A 161      23.602 -78.929 -52.159  1.00 27.17           C
ANISOU 2311  CG  TYR A 161     3881   2368   4074   -467   -458  -1091       C
ATOM   2312  CD1 TYR A 161      22.543 -78.546 -51.341  1.00 27.01           C
ANISOU 2312  CD1 TYR A 161     3793   2432   4038   -558   -477  -1020       C
ATOM   2313  CD2 TYR A 161      24.661 -78.037 -52.327  1.00 25.76           C
ANISOU 2313  CD2 TYR A 161     3674   2243   3871   -338   -425  -1075       C
ATOM   2314  CE1 TYR A 161      22.543 -77.299 -50.679  1.00 26.90           C
ANISOU 2314  CE1 TYR A 161     3692   2548   3980   -514   -466   -938       C
ATOM   2315  CE2 TYR A 161      24.677 -76.786 -51.661  1.00 24.86           C
ANISOU 2315  CE2 TYR A 161     3472   2257   3717   -301   -421   -990       C
ATOM   2316  CZ  TYR A 161      23.616 -76.430 -50.838  1.00 25.83           C
ANISOU 2316  CZ  TYR A 161     3538   2456   3819   -387   -443   -924       C
ATOM   2317  OH  TYR A 161      23.603 -75.206 -50.207  1.00 25.56           O
ANISOU 2317  OH  TYR A 161     3427   2541   3743   -349   -436   -851       O
ATOM   2318  H   TYR A 161      22.834 -82.959 -53.440  1.00  0.00           H
ATOM   2319  HA  TYR A 161      24.365 -81.510 -51.319  1.00  0.00           H
ATOM   2320  HB2 TYR A 161      22.701 -80.275 -53.542  1.00  0.00           H
ATOM   2321  HB3 TYR A 161      24.467 -80.308 -53.544  1.00  0.00           H
ATOM   2322  HD1 TYR A 161      21.706 -79.215 -51.210  1.00  0.00           H
ATOM   2323  HD2 TYR A 161      25.482 -78.304 -52.975  1.00  0.00           H
ATOM   2324  HE1 TYR A 161      21.710 -77.021 -50.050  1.00  0.00           H
ATOM   2325  HE2 TYR A 161      25.511 -76.112 -51.793  1.00  0.00           H
ATOM   2326  HH  TYR A 161      24.338 -74.675 -50.523  1.00  0.00           H
ATOM   2327  N   PRO A 162      22.235 -82.055 -50.070  1.00 49.26           N
ANISOU 2327  N   PRO A 162     6828   4812   7076   -751   -491   -984       N
ATOM   2328  CA  PRO A 162      21.006 -82.356 -49.323  1.00 52.53           C
ANISOU 2328  CA  PRO A 162     7215   5238   7506   -899   -499   -928       C
ATOM   2329  C   PRO A 162      20.241 -81.103 -48.955  1.00 48.17           C
ANISOU 2329  C   PRO A 162     6539   4882   6883   -921   -493   -879       C
ATOM   2330  O   PRO A 162      20.731 -80.005 -49.180  1.00 47.91           O
ANISOU 2330  O   PRO A 162     6450   4963   6788   -818   -487   -877       O
ATOM   2331  CB  PRO A 162      21.518 -83.015 -48.039  1.00 57.15           C
ANISOU 2331  CB  PRO A 162     7871   5688   8155   -893   -481   -811       C
ATOM   2332  CG  PRO A 162      22.992 -83.286 -48.266  1.00 59.26           C
ANISOU 2332  CG  PRO A 162     8209   5847   8462   -746   -479   -826       C
ATOM   2333  CD  PRO A 162      23.444 -82.288 -49.262  1.00 55.85           C
ANISOU 2333  CD  PRO A 162     7714   5542   7966   -647   -473   -903       C
ATOM   2334  HA  PRO A 162      20.373 -83.044 -49.883  1.00  0.00           H
ATOM   2335  HB2 PRO A 162      21.383 -82.345 -47.190  1.00  0.00           H
ATOM   2336  HB3 PRO A 162      20.989 -83.952 -47.863  1.00  0.00           H
ATOM   2337  HG2 PRO A 162      23.546 -83.169 -47.335  1.00  0.00           H
ATOM   2338  HG3 PRO A 162      23.130 -84.294 -48.658  1.00  0.00           H
ATOM   2339  HD2 PRO A 162      24.254 -82.685 -49.874  1.00  0.00           H
ATOM   2340  HD3 PRO A 162      23.755 -81.368 -48.767  1.00  0.00           H
ATOM   2341  N   VAL A 163      19.052 -81.263 -48.391  1.00 42.99           N
ANISOU 2341  N   VAL A 163     5836   4260   6239  -1055   -489   -839       N
ATOM   2342  CA  VAL A 163      18.330 -80.125 -47.874  1.00 41.12           C
ANISOU 2342  CA  VAL A 163     5481   4196   5946  -1070   -472   -783       C
ATOM   2343  C   VAL A 163      19.041 -79.724 -46.573  1.00 40.32           C
ANISOU 2343  C   VAL A 163     5402   4086   5831   -998   -435   -659       C
ATOM   2344  O   VAL A 163      19.127 -80.512 -45.630  1.00 44.69           O
ANISOU 2344  O   VAL A 163     6028   4524   6427  -1045   -415   -581       O
ATOM   2345  CB  VAL A 163      16.848 -80.452 -47.616  1.00 43.19           C
ANISOU 2345  CB  VAL A 163     5677   4495   6237  -1235   -468   -778       C
ATOM   2346  CG1 VAL A 163      16.129 -79.235 -47.106  1.00 44.03           C
ANISOU 2346  CG1 VAL A 163     5655   4782   6291  -1236   -443   -726       C
ATOM   2347  CG2 VAL A 163      16.163 -80.954 -48.899  1.00 43.78           C
ANISOU 2347  CG2 VAL A 163     5737   4565   6331  -1316   -524   -906       C
ATOM   2348  H   VAL A 163      18.649 -82.187 -48.323  1.00  0.00           H
ATOM   2349  HA  VAL A 163      18.397 -79.303 -48.587  1.00  0.00           H
ATOM   2350  HB  VAL A 163      16.790 -81.235 -46.860  1.00  0.00           H
ATOM   2351 HG11 VAL A 163      16.615 -78.880 -46.197  1.00  0.00           H
ATOM   2352 HG12 VAL A 163      16.159 -78.452 -47.863  1.00  0.00           H
ATOM   2353 HG13 VAL A 163      15.092 -79.490 -46.888  1.00  0.00           H
ATOM   2354 HG21 VAL A 163      16.685 -81.837 -49.269  1.00  0.00           H
ATOM   2355 HG22 VAL A 163      16.193 -80.171 -49.657  1.00  0.00           H
ATOM   2356 HG23 VAL A 163      15.126 -81.210 -48.681  1.00  0.00           H
ATOM   2357  N   LEU A 164      19.647 -78.547 -46.560  1.00 34.37           N
ANISOU 2357  N   LEU A 164     4602   3440   5019   -881   -431   -642       N
ATOM   2358  CA  LEU A 164      20.209 -78.006 -45.340  1.00 31.71           C
ANISOU 2358  CA  LEU A 164     4274   3119   4657   -819   -406   -532       C
ATOM   2359  C   LEU A 164      19.089 -77.462 -44.508  1.00 30.45           C
ANISOU 2359  C   LEU A 164     4040   3067   4461   -902   -371   -472       C
ATOM   2360  O   LEU A 164      18.202 -76.792 -45.024  1.00 30.35           O
ANISOU 2360  O   LEU A 164     3926   3184   4420   -935   -370   -519       O
ATOM   2361  CB  LEU A 164      21.202 -76.879 -45.657  1.00 32.25           C
ANISOU 2361  CB  LEU A 164     4310   3265   4680   -674   -416   -543       C
ATOM   2362  CG  LEU A 164      22.311 -77.277 -46.628  1.00 32.83           C
ANISOU 2362  CG  LEU A 164     4435   3251   4787   -584   -436   -615       C
ATOM   2363  CD1 LEU A 164      23.139 -76.069 -47.010  1.00 29.72           C
ANISOU 2363  CD1 LEU A 164     3992   2953   4349   -459   -434   -627       C
ATOM   2364  CD2 LEU A 164      23.151 -78.381 -45.984  1.00 34.67           C
ANISOU 2364  CD2 LEU A 164     4773   3307   5092   -563   -442   -565       C
ATOM   2365  H   LEU A 164      19.719 -78.017 -47.417  1.00  0.00           H
ATOM   2366  HA  LEU A 164      20.719 -78.798 -44.791  1.00  0.00           H
ATOM   2367  HB2 LEU A 164      20.648 -76.048 -46.093  1.00  0.00           H
ATOM   2368  HB3 LEU A 164      21.658 -76.544 -44.725  1.00  0.00           H
ATOM   2369  HG  LEU A 164      21.850 -77.678 -47.531  1.00  0.00           H
ATOM   2370 HD11 LEU A 164      23.925 -76.371 -47.703  1.00  0.00           H
ATOM   2371 HD12 LEU A 164      23.589 -75.640 -46.115  1.00  0.00           H
ATOM   2372 HD13 LEU A 164      22.500 -75.326 -47.487  1.00  0.00           H
ATOM   2373 HD21 LEU A 164      23.948 -78.676 -46.666  1.00  0.00           H
ATOM   2374 HD22 LEU A 164      23.586 -78.011 -45.055  1.00  0.00           H
ATOM   2375 HD23 LEU A 164      22.518 -79.242 -45.771  1.00  0.00           H
ATOM   2376  N   ASN A 165      19.171 -77.690 -43.205  1.00 30.67           N
ANISOU 2376  N   ASN A 165     4120   3048   4485   -925   -340   -366       N
ATOM   2377  CA  ASN A 165      18.140 -77.270 -42.280  1.00 30.63           C
ANISOU 2377  CA  ASN A 165     4060   3134   4445  -1005   -287   -303       C
ATOM   2378  C   ASN A 165      18.800 -77.087 -40.919  1.00 31.52           C
ANISOU 2378  C   ASN A 165     4248   3214   4514   -958   -266   -189       C
ATOM   2379  O   ASN A 165      18.948 -78.072 -40.150  1.00 32.54           O
ANISOU 2379  O   ASN A 165     4481   3214   4668  -1009   -256   -117       O
ATOM   2380  CB  ASN A 165      17.055 -78.363 -42.192  1.00 32.20           C
ANISOU 2380  CB  ASN A 165     4265   3266   4702  -1167   -260   -301       C
ATOM   2381  CG  ASN A 165      15.891 -77.946 -41.330  1.00 36.12           C
ANISOU 2381  CG  ASN A 165     4687   3866   5171  -1259   -189   -244       C
ATOM   2382  OD1 ASN A 165      15.354 -76.851 -41.508  1.00 35.42           O
ANISOU 2382  OD1 ASN A 165     4482   3932   5043  -1232   -174   -271       O
ATOM   2383  ND2 ASN A 165      15.524 -78.787 -40.359  1.00 42.76           N
ANISOU 2383  ND2 ASN A 165     5597   4618   6032  -1361   -137   -161       N
ATOM   2384  H   ASN A 165      19.981 -78.174 -42.845  1.00  0.00           H
ATOM   2385  HA  ASN A 165      17.699 -76.330 -42.612  1.00  0.00           H
ATOM   2386  HB2 ASN A 165      16.689 -78.575 -43.197  1.00  0.00           H
ATOM   2387  HB3 ASN A 165      17.497 -79.269 -41.777  1.00  0.00           H
ATOM   2388 HD21 ASN A 165      14.762 -78.544 -39.742  1.00  0.00           H
ATOM   2389 HD22 ASN A 165      16.008 -79.665 -40.242  1.00  0.00           H
ATOM   2390  N   VAL A 166      19.211 -75.851 -40.609  1.00 31.34           N
ANISOU 2390  N   VAL A 166     4184   3298   4425   -861   -265   -172       N
ATOM   2391  CA  VAL A 166      19.973 -75.615 -39.394  1.00 33.06           C
ANISOU 2391  CA  VAL A 166     4481   3487   4595   -803   -265    -76       C
ATOM   2392  C   VAL A 166      19.386 -74.459 -38.611  1.00 32.55           C
ANISOU 2392  C   VAL A 166     4358   3562   4447   -803   -215    -39       C
ATOM   2393  O   VAL A 166      18.740 -73.575 -39.168  1.00 31.87           O
ANISOU 2393  O   VAL A 166     4160   3603   4344   -797   -197    -96       O
ATOM   2394  CB  VAL A 166      21.455 -75.332 -39.715  1.00 35.59           C
ANISOU 2394  CB  VAL A 166     4834   3762   4927   -664   -330    -90       C
ATOM   2395  CG1 VAL A 166      22.010 -76.466 -40.581  1.00 36.46           C
ANISOU 2395  CG1 VAL A 166     4995   3734   5125   -656   -368   -140       C
ATOM   2396  CG2 VAL A 166      21.613 -73.983 -40.412  1.00 35.28           C
ANISOU 2396  CG2 VAL A 166     4693   3859   4853   -581   -338   -152       C
ATOM   2397  H   VAL A 166      18.991 -75.079 -41.222  1.00  0.00           H
ATOM   2398  HA  VAL A 166      19.920 -76.511 -38.776  1.00  0.00           H
ATOM   2399  HB  VAL A 166      22.013 -75.306 -38.779  1.00  0.00           H
ATOM   2400 HG21 VAL A 166      21.211 -73.195 -39.775  1.00  0.00           H
ATOM   2401 HG22 VAL A 166      22.670 -73.793 -40.601  1.00  0.00           H
ATOM   2402 HG23 VAL A 166      21.072 -73.997 -41.358  1.00  0.00           H
ATOM   2403 HG11 VAL A 166      23.057 -76.270 -40.810  1.00  0.00           H
ATOM   2404 HG12 VAL A 166      21.441 -76.527 -41.509  1.00  0.00           H
ATOM   2405 HG13 VAL A 166      21.927 -77.409 -40.041  1.00  0.00           H
ATOM   2406  N   THR A 167      19.595 -74.483 -37.303  1.00 34.97           N
ANISOU 2406  N   THR A 167     4749   3841   4698   -807   -195     57       N
ATOM   2407  CA  THR A 167      19.064 -73.441 -36.450  1.00 36.64           C
ANISOU 2407  CA  THR A 167     4926   4174   4821   -806   -138     91       C
ATOM   2408  C   THR A 167      20.147 -72.919 -35.514  1.00 35.01           C
ANISOU 2408  C   THR A 167     4806   3949   4546   -712   -178    153       C
ATOM   2409  O   THR A 167      21.089 -73.635 -35.166  1.00 35.58           O
ANISOU 2409  O   THR A 167     4984   3901   4636   -681   -236    203       O
ATOM   2410  CB  THR A 167      17.870 -73.950 -35.629  1.00 40.77           C
ANISOU 2410  CB  THR A 167     5463   4705   5324   -938    -45    147       C
ATOM   2411  OG1 THR A 167      17.310 -72.879 -34.860  1.00 47.00           O
ANISOU 2411  OG1 THR A 167     6211   5619   6028   -930     22    168       O
ATOM   2412  CG2 THR A 167      18.286 -75.047 -34.711  1.00 38.12           C
ANISOU 2412  CG2 THR A 167     5278   4226   4978   -982    -49    244       C
ATOM   2413  H   THR A 167      20.131 -75.237 -36.897  1.00  0.00           H
ATOM   2414  HA  THR A 167      18.725 -72.618 -37.079  1.00  0.00           H
ATOM   2415  HB  THR A 167      17.109 -74.330 -36.311  1.00  0.00           H
ATOM   2416  HG1 THR A 167      17.187 -72.111 -35.422  1.00  0.00           H
ATOM   2417 HG21 THR A 167      17.423 -75.391 -34.140  1.00  0.00           H
ATOM   2418 HG22 THR A 167      19.050 -74.678 -34.027  1.00  0.00           H
ATOM   2419 HG23 THR A 167      18.690 -75.875 -35.294  1.00  0.00           H
ATOM   2420  N   MET A 168      19.989 -71.667 -35.109  1.00 32.31           N
ANISOU 2420  N   MET A 168     4419   3726   4131   -667   -153    148       N
ATOM   2421  CA  MET A 168      20.933 -71.012 -34.220  1.00 29.17           C
ANISOU 2421  CA  MET A 168     4095   3328   3661   -583   -195    195       C
ATOM   2422  C   MET A 168      20.108 -70.082 -33.331  1.00 27.21           C
ANISOU 2422  C   MET A 168     3832   3194   3314   -606   -114    214       C
ATOM   2423  O   MET A 168      19.623 -69.052 -33.775  1.00 25.27           O
ANISOU 2423  O   MET A 168     3481   3060   3061   -577    -83    153       O
ATOM   2424  CB  MET A 168      21.953 -70.217 -35.032  1.00 28.71           C
ANISOU 2424  CB  MET A 168     3981   3292   3637   -467   -270    135       C
ATOM   2425  CG  MET A 168      23.143 -69.716 -34.213  1.00 29.09           C
ANISOU 2425  CG  MET A 168     4104   3313   3637   -381   -340    180       C
ATOM   2426  SD  MET A 168      24.136 -71.071 -33.490  1.00 32.93           S
ANISOU 2426  SD  MET A 168     4737   3629   4147   -379   -417    271       S
ATOM   2427  CE  MET A 168      24.779 -71.887 -34.954  1.00 35.38           C
ANISOU 2427  CE  MET A 168     4994   3849   4600   -342   -463    206       C
ATOM   2428  H   MET A 168      19.183 -71.150 -35.430  1.00  0.00           H
ATOM   2429  HA  MET A 168      21.444 -71.755 -33.608  1.00  0.00           H
ATOM   2430  HB2 MET A 168      22.331 -70.857 -35.829  1.00  0.00           H
ATOM   2431  HB3 MET A 168      21.451 -69.359 -35.480  1.00  0.00           H
ATOM   2432  HG2 MET A 168      22.768 -69.090 -33.403  1.00  0.00           H
ATOM   2433  HG3 MET A 168      23.784 -69.113 -34.856  1.00  0.00           H
ATOM   2434  HE1 MET A 168      25.401 -72.731 -34.656  1.00  0.00           H
ATOM   2435  HE2 MET A 168      25.377 -71.181 -35.530  1.00  0.00           H
ATOM   2436  HE3 MET A 168      23.950 -72.244 -35.565  1.00  0.00           H
ATOM   2437  N   PRO A 169      19.928 -70.455 -32.065  1.00 29.73           N
ANISOU 2437  N   PRO A 169     4263   3479   3552   -656    -75    299       N
ATOM   2438  CA  PRO A 169      19.120 -69.632 -31.162  1.00 30.74           C
ANISOU 2438  CA  PRO A 169     4390   3711   3579   -680     18    315       C
ATOM   2439  C   PRO A 169      19.890 -68.409 -30.690  1.00 30.14           C
ANISOU 2439  C   PRO A 169     4341   3686   3426   -576    -30    303       C
ATOM   2440  O   PRO A 169      21.119 -68.455 -30.595  1.00 30.21           O
ANISOU 2440  O   PRO A 169     4416   3626   3437   -506   -136    322       O
ATOM   2441  CB  PRO A 169      18.856 -70.566 -29.982  1.00 33.24           C
ANISOU 2441  CB  PRO A 169     4846   3956   3828   -767     68    417       C
ATOM   2442  CG  PRO A 169      20.016 -71.466 -29.959  1.00 34.46           C
ANISOU 2442  CG  PRO A 169     5108   3970   4016   -735    -43    466       C
ATOM   2443  CD  PRO A 169      20.491 -71.634 -31.395  1.00 32.52           C
ANISOU 2443  CD  PRO A 169     4761   3696   3900   -687   -115    387       C
ATOM   2444  HA  PRO A 169      18.185 -69.339 -31.639  1.00  0.00           H
ATOM   2445  HB2 PRO A 169      17.935 -71.129 -30.135  1.00  0.00           H
ATOM   2446  HB3 PRO A 169      18.801 -69.996 -29.054  1.00  0.00           H
ATOM   2447  HG2 PRO A 169      19.729 -72.433 -29.546  1.00  0.00           H
ATOM   2448  HG3 PRO A 169      20.811 -71.028 -29.356  1.00  0.00           H
ATOM   2449  HD2 PRO A 169      20.104 -72.555 -31.831  1.00  0.00           H
ATOM   2450  HD3 PRO A 169      21.580 -71.617 -31.442  1.00  0.00           H
ATOM   2451  N   ASN A 170      19.176 -67.318 -30.438  1.00 29.12           N
ANISOU 2451  N   ASN A 170     4152   3674   3241   -565     46    267       N
ATOM   2452  CA  ASN A 170      19.763 -66.175 -29.787  1.00 29.33           C
ANISOU 2452  CA  ASN A 170     4224   3742   3179   -483     15    260       C
ATOM   2453  C   ASN A 170      19.463 -66.241 -28.298  1.00 31.49           C
ANISOU 2453  C   ASN A 170     4633   4016   3315   -527     79    330       C
ATOM   2454  O   ASN A 170      18.366 -65.916 -27.870  1.00 32.85           O
ANISOU 2454  O   ASN A 170     4777   4266   3437   -574    204    323       O
ATOM   2455  CB  ASN A 170      19.216 -64.879 -30.351  1.00 29.36           C
ANISOU 2455  CB  ASN A 170     4098   3861   3195   -434     58    177       C
ATOM   2456  CG  ASN A 170      19.947 -63.683 -29.819  1.00 28.64           C
ANISOU 2456  CG  ASN A 170     4053   3798   3031   -346     11    159       C
ATOM   2457  OD1 ASN A 170      20.762 -63.799 -28.888  1.00 30.41           O
ANISOU 2457  OD1 ASN A 170     4410   3966   3178   -330    -47    210       O
ATOM   2458  ND2 ASN A 170      19.663 -62.519 -30.383  1.00 26.02           N
ANISOU 2458  ND2 ASN A 170     3618   3547   2720   -290     30     89       N
ATOM   2459  H   ASN A 170      18.203 -67.289 -30.708  1.00  0.00           H
ATOM   2460  HA  ASN A 170      20.843 -66.198 -29.933  1.00  0.00           H
ATOM   2461  HB2 ASN A 170      19.315 -64.898 -31.436  1.00  0.00           H
ATOM   2462  HB3 ASN A 170      18.161 -64.795 -30.091  1.00  0.00           H
ATOM   2463 HD21 ASN A 170      20.120 -61.678 -30.062  1.00  0.00           H
ATOM   2464 HD22 ASN A 170      18.989 -62.473 -31.134  1.00  0.00           H
ATOM   2465  N   ASN A 171      20.440 -66.674 -27.518  1.00 33.66           N
ANISOU 2465  N   ASN A 171     5055   4204   3529   -509     -6    397       N
ATOM   2466  CA  ASN A 171      20.276 -66.765 -26.076  1.00 37.43           C
ANISOU 2466  CA  ASN A 171     5689   4676   3857   -546     40    470       C
ATOM   2467  C   ASN A 171      21.027 -65.669 -25.366  1.00 38.81           C
ANISOU 2467  C   ASN A 171     5938   4881   3929   -465    -25    454       C
ATOM   2468  O   ASN A 171      21.251 -65.741 -24.152  1.00 42.29           O
ANISOU 2468  O   ASN A 171     6538   5298   4232   -477    -33    516       O
ATOM   2469  CB  ASN A 171      20.738 -68.127 -25.571  1.00 39.73           C
ANISOU 2469  CB  ASN A 171     6119   4842   4136   -595    -11    572       C
ATOM   2470  CG  ASN A 171      19.856 -69.237 -26.049  1.00 42.57           C
ANISOU 2470  CG  ASN A 171     6432   5165   4578   -697     73    595       C
ATOM   2471  OD1 ASN A 171      20.345 -70.296 -26.465  1.00 44.93           O
ANISOU 2471  OD1 ASN A 171     6756   5353   4960   -712      3    630       O
ATOM   2472  ND2 ASN A 171      18.538 -69.007 -26.017  1.00 42.75           N
ANISOU 2472  ND2 ASN A 171     6377   5276   4588   -768    224    571       N
ATOM   2473  H   ASN A 171      21.319 -66.947 -27.933  1.00  0.00           H
ATOM   2474  HA  ASN A 171      19.216 -66.657 -25.846  1.00  0.00           H
ATOM   2475  HB2 ASN A 171      21.752 -68.307 -25.927  1.00  0.00           H
ATOM   2476  HB3 ASN A 171      20.740 -68.119 -24.481  1.00  0.00           H
ATOM   2477 HD21 ASN A 171      18.188 -68.123 -25.675  1.00  0.00           H
ATOM   2478 HD22 ASN A 171      17.894 -69.717 -26.334  1.00  0.00           H
ATOM   2479  N   ASP A 172      21.407 -64.664 -26.141  1.00 36.59           N
ANISOU 2479  N   ASP A 172     5544   4647   3711   -386    -74    371       N
ATOM   2480  CA  ASP A 172      22.067 -63.479 -25.635  1.00 37.94           C
ANISOU 2480  CA  ASP A 172     5759   4850   3807   -310   -135    337       C
ATOM   2481  C   ASP A 172      21.031 -62.405 -25.382  1.00 38.58           C
ANISOU 2481  C   ASP A 172     5794   5041   3824   -309     -6    279       C
ATOM   2482  O   ASP A 172      19.856 -62.593 -25.675  1.00 38.41           O
ANISOU 2482  O   ASP A 172     5689   5072   3831   -362    121    266       O
ATOM   2483  CB  ASP A 172      23.121 -63.014 -26.648  1.00 37.82           C
ANISOU 2483  CB  ASP A 172     5649   4813   3909   -228   -258    285       C
ATOM   2484  CG  ASP A 172      24.353 -63.933 -26.647  1.00 37.95           C
ANISOU 2484  CG  ASP A 172     5729   4716   3974   -209   -397    342       C
ATOM   2485  OD1 ASP A 172      25.051 -63.943 -25.607  1.00 38.05           O
ANISOU 2485  OD1 ASP A 172     5876   4687   3893   -194   -478    392       O
ATOM   2486  OD2 ASP A 172      24.612 -64.657 -27.636  1.00 37.27           O
ANISOU 2486  OD2 ASP A 172     5566   4581   4015   -208   -428    338       O
ATOM   2487  H   ASP A 172      21.228 -64.728 -27.133  1.00  0.00           H
ATOM   2488  HA  ASP A 172      22.562 -63.723 -24.695  1.00  0.00           H
ATOM   2489  HB2 ASP A 172      22.679 -63.017 -27.644  1.00  0.00           H
ATOM   2490  HB3 ASP A 172      23.432 -62.000 -26.399  1.00  0.00           H
ATOM   2491  N   ASN A 173      21.456 -61.287 -24.815  1.00 39.74           N
ANISOU 2491  N   ASN A 173     5994   5218   3888   -250    -40    242       N
ATOM   2492  CA  ASN A 173      20.521 -60.212 -24.531  1.00 40.88           C
ANISOU 2492  CA  ASN A 173     6104   5456   3971   -236     82    181       C
ATOM   2493  C   ASN A 173      20.759 -59.017 -25.423  1.00 36.89           C
ANISOU 2493  C   ASN A 173     5474   4991   3551   -156     44     93       C
ATOM   2494  O   ASN A 173      20.408 -57.906 -25.057  1.00 38.34           O
ANISOU 2494  O   ASN A 173     5662   5230   3676   -117     98     39       O
ATOM   2495  CB  ASN A 173      20.616 -59.787 -23.060  1.00 46.41           C
ANISOU 2495  CB  ASN A 173     6984   6164   4488   -237    101    200       C
ATOM   2496  CG  ASN A 173      21.988 -59.246 -22.700  1.00 49.99           C
ANISOU 2496  CG  ASN A 173     7528   6566   4902   -174    -66    192       C
ATOM   2497  OD1 ASN A 173      22.823 -58.993 -23.572  1.00 48.19           O
ANISOU 2497  OD1 ASN A 173     7211   6308   4791   -123   -178    162       O
ATOM   2498  ND2 ASN A 173      22.226 -59.056 -21.407  1.00 54.61           N
ANISOU 2498  ND2 ASN A 173     8291   7141   5318   -180    -81    217       N
ATOM   2499  H   ASN A 173      22.432 -61.181 -24.579  1.00  0.00           H
ATOM   2500  HA  ASN A 173      19.512 -60.580 -24.715  1.00  0.00           H
ATOM   2501  HB2 ASN A 173      19.874 -59.011 -22.871  1.00  0.00           H
ATOM   2502  HB3 ASN A 173      20.397 -60.648 -22.428  1.00  0.00           H
ATOM   2503 HD21 ASN A 173      23.120 -58.695 -21.106  1.00  0.00           H
ATOM   2504 HD22 ASN A 173      21.513 -59.273 -20.725  1.00  0.00           H
ATOM   2505  N   PHE A 174      21.361 -59.244 -26.590  1.00 32.32           N
ANISOU 2505  N   PHE A 174     4793   4378   3107   -129    -44     81       N
ATOM   2506  CA  PHE A 174      21.453 -58.222 -27.630  1.00 30.07           C
ANISOU 2506  CA  PHE A 174     4378   4131   2915    -63    -64      6       C
ATOM   2507  C   PHE A 174      20.955 -58.811 -28.948  1.00 28.54           C
ANISOU 2507  C   PHE A 174     4041   3951   2852    -83    -40     -5       C
ATOM   2508  O   PHE A 174      20.838 -60.034 -29.082  1.00 28.56           O
ANISOU 2508  O   PHE A 174     4053   3914   2886   -143    -37     42       O
ATOM   2509  CB  PHE A 174      22.892 -57.730 -27.796  1.00 30.27           C
ANISOU 2509  CB  PHE A 174     4429   4101   2972     -1   -210     -6       C
ATOM   2510  CG  PHE A 174      23.893 -58.849 -27.902  1.00 31.41           C
ANISOU 2510  CG  PHE A 174     4615   4158   3163    -17   -319     53       C
ATOM   2511  CD1 PHE A 174      24.102 -59.494 -29.110  1.00 31.06           C
ANISOU 2511  CD1 PHE A 174     4467   4086   3247    -16   -344     51       C
ATOM   2512  CD2 PHE A 174      24.594 -59.272 -26.788  1.00 33.17           C
ANISOU 2512  CD2 PHE A 174     4983   4324   3296    -29   -394    109       C
ATOM   2513  CE1 PHE A 174      25.012 -60.544 -29.210  1.00 31.11           C
ANISOU 2513  CE1 PHE A 174     4510   4006   3306    -23   -436    101       C
ATOM   2514  CE2 PHE A 174      25.501 -60.317 -26.869  1.00 34.29           C
ANISOU 2514  CE2 PHE A 174     5159   4380   3491    -35   -497    167       C
ATOM   2515  CZ  PHE A 174      25.717 -60.951 -28.091  1.00 33.13           C
ANISOU 2515  CZ  PHE A 174     4900   4201   3485    -29   -515    160       C
ATOM   2516  H   PHE A 174      21.767 -60.153 -26.761  1.00  0.00           H
ATOM   2517  HA  PHE A 174      20.819 -57.379 -27.356  1.00  0.00           H
ATOM   2518  HB2 PHE A 174      23.150 -57.116 -26.933  1.00  0.00           H
ATOM   2519  HB3 PHE A 174      22.953 -57.117 -28.695  1.00  0.00           H
ATOM   2520  HD1 PHE A 174      23.553 -59.179 -29.985  1.00  0.00           H
ATOM   2521  HD2 PHE A 174      24.432 -58.781 -25.840  1.00  0.00           H
ATOM   2522  HE1 PHE A 174      25.167 -61.039 -30.158  1.00  0.00           H
ATOM   2523  HE2 PHE A 174      26.038 -60.638 -25.989  1.00  0.00           H
ATOM   2524  HZ  PHE A 174      26.432 -61.757 -28.164  1.00  0.00           H
ATOM   2525  N   ASP A 175      20.662 -57.938 -29.905  1.00 27.86           N
ANISOU 2525  N   ASP A 175     3833   3916   2838    -34    -25    -68       N
ATOM   2526  CA  ASP A 175      20.267 -58.341 -31.254  1.00 27.40           C
ANISOU 2526  CA  ASP A 175     3642   3874   2895    -43    -21    -88       C
ATOM   2527  C   ASP A 175      21.459 -58.799 -32.097  1.00 24.47           C
ANISOU 2527  C   ASP A 175     3261   3431   2605    -20   -135    -81       C
ATOM   2528  O   ASP A 175      22.536 -58.198 -32.086  1.00 26.12           O
ANISOU 2528  O   ASP A 175     3500   3607   2818     35   -216    -90       O
ATOM   2529  CB  ASP A 175      19.603 -57.180 -31.989  1.00 30.22           C
ANISOU 2529  CB  ASP A 175     3883   4308   3292     11     22   -152       C
ATOM   2530  CG  ASP A 175      18.248 -56.804 -31.400  1.00 36.04           C
ANISOU 2530  CG  ASP A 175     4589   5124   3982     -8    150   -168       C
ATOM   2531  OD1 ASP A 175      17.743 -57.542 -30.523  1.00 39.89           O
ANISOU 2531  OD1 ASP A 175     5136   5611   4411    -76    218   -129       O
ATOM   2532  OD2 ASP A 175      17.692 -55.771 -31.834  1.00 36.59           O
ANISOU 2532  OD2 ASP A 175     4574   5252   4078     47    184   -219       O
ATOM   2533  H   ASP A 175      20.714 -56.952 -29.692  1.00  0.00           H
ATOM   2534  HA  ASP A 175      19.554 -59.162 -31.180  1.00  0.00           H
ATOM   2535  HB2 ASP A 175      20.260 -56.312 -31.933  1.00  0.00           H
ATOM   2536  HB3 ASP A 175      19.469 -57.455 -33.035  1.00  0.00           H
ATOM   2537  N   LYS A 176      21.235 -59.838 -32.879  1.00 20.09           N
ANISOU 2537  N   LYS A 176     2657   2855   2121    -63   -135    -70       N
ATOM   2538  CA  LYS A 176      22.253 -60.351 -33.770  1.00 18.90           C
ANISOU 2538  CA  LYS A 176     2490   2639   2053    -40   -223    -71       C
ATOM   2539  C   LYS A 176      21.912 -59.988 -35.206  1.00 18.18           C
ANISOU 2539  C   LYS A 176     2277   2592   2040    -14   -215   -126       C
ATOM   2540  O   LYS A 176      20.812 -60.235 -35.662  1.00 20.91           O
ANISOU 2540  O   LYS A 176     2552   2988   2403    -54   -156   -145       O
ATOM   2541  CB  LYS A 176      22.285 -61.877 -33.692  1.00 19.56           C
ANISOU 2541  CB  LYS A 176     2618   2651   2161   -106   -232    -24       C
ATOM   2542  CG  LYS A 176      22.693 -62.479 -32.379  1.00 20.57           C
ANISOU 2542  CG  LYS A 176     2880   2717   2217   -135   -254     45       C
ATOM   2543  CD  LYS A 176      22.627 -64.006 -32.484  1.00 22.34           C
ANISOU 2543  CD  LYS A 176     3141   2863   2483   -200   -258     90       C
ATOM   2544  CE  LYS A 176      23.110 -64.677 -31.194  1.00 26.45           C
ANISOU 2544  CE  LYS A 176     3809   3310   2931   -225   -292    172       C
ATOM   2545  NZ  LYS A 176      23.147 -66.175 -31.396  1.00 28.34           N
ANISOU 2545  NZ  LYS A 176     4087   3454   3228   -281   -305    217       N
ATOM   2546  H   LYS A 176      20.330 -60.286 -32.855  1.00  0.00           H
ATOM   2547  HA  LYS A 176      23.227 -59.942 -33.501  1.00  0.00           H
ATOM   2548  HB2 LYS A 176      21.284 -62.240 -33.924  1.00  0.00           H
ATOM   2549  HB3 LYS A 176      22.966 -62.243 -34.460  1.00  0.00           H
ATOM   2550  HG2 LYS A 176      23.711 -62.174 -32.139  1.00  0.00           H
ATOM   2551  HG3 LYS A 176      22.016 -62.138 -31.596  1.00  0.00           H
ATOM   2552  HD2 LYS A 176      23.258 -64.332 -33.311  1.00  0.00           H
ATOM   2553  HD3 LYS A 176      21.598 -64.307 -32.680  1.00  0.00           H
ATOM   2554  HE2 LYS A 176      22.426 -64.436 -30.380  1.00  0.00           H
ATOM   2555  HE3 LYS A 176      24.109 -64.318 -30.949  1.00  0.00           H
ATOM   2556  HZ1 LYS A 176      23.559 -66.384 -32.294  1.00  0.00           H
ATOM   2557  HZ2 LYS A 176      23.700 -66.600 -30.665  1.00  0.00           H
ATOM   2558  HZ3 LYS A 176      22.207 -66.542 -31.364  1.00  0.00           H
ATOM   2559  N   LEU A 177      22.894 -59.519 -35.945  1.00 14.85           N
ANISOU 2559  N   LEU A 177     1831   2146   1666     47   -279   -149       N
ATOM   2560  CA  LEU A 177      22.738 -59.302 -37.378  1.00 15.09           C
ANISOU 2560  CA  LEU A 177     1768   2206   1761     71   -280   -194       C
ATOM   2561  C   LEU A 177      23.458 -60.406 -38.162  1.00 16.32           C
ANISOU 2561  C   LEU A 177     1927   2289   1984     59   -325   -192       C
ATOM   2562  O   LEU A 177      24.663 -60.565 -38.042  1.00 17.04           O
ANISOU 2562  O   LEU A 177     2059   2314   2102     91   -382   -175       O
ATOM   2563  CB  LEU A 177      23.319 -57.964 -37.762  1.00 15.55           C
ANISOU 2563  CB  LEU A 177     1798   2285   1826    146   -305   -222       C
ATOM   2564  CG  LEU A 177      23.413 -57.640 -39.249  1.00 16.06           C
ANISOU 2564  CG  LEU A 177     1787   2369   1945    181   -314   -260       C
ATOM   2565  CD1 LEU A 177      22.067 -57.505 -39.882  1.00 17.10           C
ANISOU 2565  CD1 LEU A 177     1844   2578   2074    164   -267   -287       C
ATOM   2566  CD2 LEU A 177      24.223 -56.366 -39.415  1.00 15.03           C
ANISOU 2566  CD2 LEU A 177     1653   2236   1822    248   -341   -272       C
ATOM   2567  H   LEU A 177      23.779 -59.304 -35.508  1.00  0.00           H
ATOM   2568  HA  LEU A 177      21.677 -59.318 -37.629  1.00  0.00           H
ATOM   2569  HB2 LEU A 177      24.328 -57.916 -37.353  1.00  0.00           H
ATOM   2570  HB3 LEU A 177      22.723 -57.187 -37.284  1.00  0.00           H
ATOM   2571  HG  LEU A 177      23.945 -58.452 -39.744  1.00  0.00           H
ATOM   2572 HD11 LEU A 177      21.508 -58.431 -39.749  1.00  0.00           H
ATOM   2573 HD12 LEU A 177      22.185 -57.302 -40.946  1.00  0.00           H
ATOM   2574 HD13 LEU A 177      21.526 -56.683 -39.413  1.00  0.00           H
ATOM   2575 HD21 LEU A 177      24.300 -56.119 -40.474  1.00  0.00           H
ATOM   2576 HD22 LEU A 177      25.221 -56.514 -39.003  1.00  0.00           H
ATOM   2577 HD23 LEU A 177      23.729 -55.550 -38.887  1.00  0.00           H
ATOM   2578  N   TYR A 178      22.689 -61.171 -38.937  1.00 16.80           N
ANISOU 2578  N   TYR A 178     1944   2363   2075     13   -299   -212       N
ATOM   2579  CA  TYR A 178      23.194 -62.178 -39.867  1.00 16.40           C
ANISOU 2579  CA  TYR A 178     1894   2250   2088      3   -330   -227       C
ATOM   2580  C   TYR A 178      23.216 -61.674 -41.297  1.00 16.74           C
ANISOU 2580  C   TYR A 178     1868   2331   2160     43   -336   -281       C
ATOM   2581  O   TYR A 178      22.201 -61.182 -41.823  1.00 17.52           O
ANISOU 2581  O   TYR A 178     1904   2510   2244     35   -310   -310       O
ATOM   2582  CB  TYR A 178      22.331 -63.435 -39.789  1.00 16.55           C
ANISOU 2582  CB  TYR A 178     1924   2246   2119    -84   -303   -218       C
ATOM   2583  CG  TYR A 178      22.512 -64.197 -38.523  1.00 17.09           C
ANISOU 2583  CG  TYR A 178     2082   2250   2164   -126   -303   -155       C
ATOM   2584  CD1 TYR A 178      21.660 -63.982 -37.435  1.00 18.75           C
ANISOU 2584  CD1 TYR A 178     2312   2505   2309   -170   -249   -122       C
ATOM   2585  CD2 TYR A 178      23.550 -65.094 -38.382  1.00 16.45           C
ANISOU 2585  CD2 TYR A 178     2069   2062   2120   -116   -354   -127       C
ATOM   2586  CE1 TYR A 178      21.831 -64.663 -36.236  1.00 19.48           C
ANISOU 2586  CE1 TYR A 178     2502   2536   2361   -210   -246    -57       C
ATOM   2587  CE2 TYR A 178      23.746 -65.785 -37.175  1.00 19.23           C
ANISOU 2587  CE2 TYR A 178     2516   2348   2442   -150   -364    -59       C
ATOM   2588  CZ  TYR A 178      22.877 -65.568 -36.115  1.00 20.16           C
ANISOU 2588  CZ  TYR A 178     2665   2513   2483   -200   -310    -22       C
ATOM   2589  OH  TYR A 178      23.027 -66.273 -34.958  1.00 20.79           O
ANISOU 2589  OH  TYR A 178     2852   2529   2520   -238   -316     50       O
ATOM   2590  H   TYR A 178      21.689 -61.046 -38.877  1.00  0.00           H
ATOM   2591  HA  TYR A 178      24.212 -62.438 -39.576  1.00  0.00           H
ATOM   2592  HB2 TYR A 178      22.591 -64.085 -40.624  1.00  0.00           H
ATOM   2593  HB3 TYR A 178      21.283 -63.148 -39.880  1.00  0.00           H
ATOM   2594  HD1 TYR A 178      20.852 -63.272 -37.529  1.00  0.00           H
ATOM   2595  HD2 TYR A 178      24.221 -65.267 -39.210  1.00  0.00           H
ATOM   2596  HE1 TYR A 178      21.159 -64.491 -35.409  1.00  0.00           H
ATOM   2597  HE2 TYR A 178      24.567 -66.480 -37.073  1.00  0.00           H
ATOM   2598  HH  TYR A 178      23.815 -66.819 -35.015  1.00  0.00           H
ATOM   2599  N   ILE A 179      24.381 -61.773 -41.935  1.00 15.32           N
ANISOU 2599  N   ILE A 179     1700   2097   2023     90   -371   -293       N
ATOM   2600  CA  ILE A 179      24.526 -61.459 -43.357  1.00 14.41           C
ANISOU 2600  CA  ILE A 179     1540   2006   1929    125   -370   -341       C
ATOM   2601  C   ILE A 179      24.718 -62.769 -44.105  1.00 16.04           C
ANISOU 2601  C   ILE A 179     1768   2149   2178     95   -378   -367       C
ATOM   2602  O   ILE A 179      25.542 -63.581 -43.703  1.00 17.07           O
ANISOU 2602  O   ILE A 179     1946   2192   2349     97   -397   -346       O
ATOM   2603  CB  ILE A 179      25.746 -60.611 -43.592  1.00 14.79           C
ANISOU 2603  CB  ILE A 179     1586   2037   1997    197   -387   -339       C
ATOM   2604  CG1 ILE A 179      25.735 -59.372 -42.659  1.00 16.05           C
ANISOU 2604  CG1 ILE A 179     1743   2234   2120    224   -389   -313       C
ATOM   2605  CG2 ILE A 179      25.843 -60.251 -45.045  1.00 15.67           C
ANISOU 2605  CG2 ILE A 179     1663   2176   2115    229   -374   -382       C
ATOM   2606  CD1 ILE A 179      24.470 -58.477 -42.846  1.00 19.73           C
ANISOU 2606  CD1 ILE A 179     2165   2795   2538    222   -356   -329       C
ATOM   2607  H   ILE A 179      25.194 -62.076 -41.418  1.00  0.00           H
ATOM   2608  HA  ILE A 179      23.636 -60.946 -43.721  1.00  0.00           H
ATOM   2609  HB  ILE A 179      26.621 -61.210 -43.339  1.00  0.00           H
ATOM   2610 HG12 ILE A 179      25.767 -59.716 -41.625  1.00  0.00           H
ATOM   2611 HG13 ILE A 179      26.623 -58.773 -42.859  1.00  0.00           H
ATOM   2612 HG21 ILE A 179      26.728 -59.637 -45.209  1.00  0.00           H
ATOM   2613 HG22 ILE A 179      25.917 -61.161 -45.640  1.00  0.00           H
ATOM   2614 HG23 ILE A 179      24.954 -59.694 -45.341  1.00  0.00           H
ATOM   2615 HD11 ILE A 179      24.715 -57.444 -42.597  1.00  0.00           H
ATOM   2616 HD12 ILE A 179      24.137 -58.531 -43.882  1.00  0.00           H
ATOM   2617 HD13 ILE A 179      23.675 -58.830 -42.190  1.00  0.00           H
ATOM   2618  N   TRP A 180      23.945 -62.975 -45.169  1.00 16.38           N
ANISOU 2618  N   TRP A 180     1778   2232   2212     70   -369   -414       N
ATOM   2619  CA  TRP A 180      23.978 -64.193 -45.928  1.00 16.28           C
ANISOU 2619  CA  TRP A 180     1792   2161   2232     36   -375   -451       C
ATOM   2620  C   TRP A 180      23.709 -63.857 -47.384  1.00 17.52           C
ANISOU 2620  C   TRP A 180     1920   2370   2366     55   -376   -510       C
ATOM   2621  O   TRP A 180      23.475 -62.713 -47.716  1.00 18.81           O
ANISOU 2621  O   TRP A 180     2044   2610   2492     93   -373   -511       O
ATOM   2622  CB  TRP A 180      22.944 -65.191 -45.388  1.00 16.77           C
ANISOU 2622  CB  TRP A 180     1864   2209   2300    -56   -371   -443       C
ATOM   2623  CG  TRP A 180      21.552 -64.660 -45.182  1.00 18.43           C
ANISOU 2623  CG  TRP A 180     2011   2518   2474   -100   -354   -442       C
ATOM   2624  CD1 TRP A 180      21.067 -64.021 -44.065  1.00 19.59           C
ANISOU 2624  CD1 TRP A 180     2139   2712   2592   -107   -329   -398       C
ATOM   2625  CD2 TRP A 180      20.466 -64.738 -46.102  1.00 20.42           C
ANISOU 2625  CD2 TRP A 180     2207   2833   2718   -142   -363   -492       C
ATOM   2626  NE1 TRP A 180      19.734 -63.681 -44.256  1.00 20.88           N
ANISOU 2626  NE1 TRP A 180     2227   2966   2741   -145   -311   -417       N
ATOM   2627  CE2 TRP A 180      19.346 -64.122 -45.494  1.00 20.59           C
ANISOU 2627  CE2 TRP A 180     2163   2941   2721   -168   -340   -472       C
ATOM   2628  CE3 TRP A 180      20.330 -65.240 -47.395  1.00 21.84           C
ANISOU 2628  CE3 TRP A 180     2387   3007   2903   -156   -390   -554       C
ATOM   2629  CZ2 TRP A 180      18.114 -64.037 -46.126  1.00 19.82           C
ANISOU 2629  CZ2 TRP A 180     1987   2922   2624   -209   -350   -509       C
ATOM   2630  CZ3 TRP A 180      19.106 -65.143 -48.025  1.00 21.69           C
ANISOU 2630  CZ3 TRP A 180     2303   3067   2872   -200   -410   -591       C
ATOM   2631  CH2 TRP A 180      18.019 -64.533 -47.394  1.00 20.01           C
ANISOU 2631  CH2 TRP A 180     2010   2939   2653   -224   -393   -567       C
ATOM   2632  H   TRP A 180      23.309 -62.244 -45.454  1.00  0.00           H
ATOM   2633  HA  TRP A 180      24.971 -64.634 -45.845  1.00  0.00           H
ATOM   2634  HB2 TRP A 180      22.882 -66.020 -46.093  1.00  0.00           H
ATOM   2635  HB3 TRP A 180      23.307 -65.578 -44.436  1.00  0.00           H
ATOM   2636  HD1 TRP A 180      21.638 -63.814 -43.172  1.00  0.00           H
ATOM   2637  HE3 TRP A 180      21.170 -65.698 -47.896  1.00  0.00           H
ATOM   2638  HZ2 TRP A 180      17.261 -63.595 -45.633  1.00  0.00           H
ATOM   2639  HZ3 TRP A 180      18.987 -65.545 -49.020  1.00  0.00           H
ATOM   2640  HH2 TRP A 180      17.081 -64.452 -47.922  1.00  0.00           H
ATOM   2641  HE1 TRP A 180      19.149 -63.191 -43.594  1.00  0.00           H
ATOM   2642  N   GLY A 181      23.748 -64.848 -48.261  1.00 17.45           N
ANISOU 2642  N   GLY A 181     1941   2315   2375     30   -382   -559       N
ATOM   2643  CA  GLY A 181      23.640 -64.573 -49.676  1.00 17.32           C
ANISOU 2643  CA  GLY A 181     1918   2340   2322     52   -385   -617       C
ATOM   2644  C   GLY A 181      23.078 -65.729 -50.456  1.00 20.29           C
ANISOU 2644  C   GLY A 181     2323   2686   2701    -10   -403   -678       C
ATOM   2645  O   GLY A 181      22.879 -66.834 -49.937  1.00 21.27           O
ANISOU 2645  O   GLY A 181     2474   2740   2868    -70   -408   -677       O
ATOM   2646  H   GLY A 181      23.854 -65.800 -47.940  1.00  0.00           H
ATOM   2647  HA2 GLY A 181      22.987 -63.711 -49.814  1.00  0.00           H
ATOM   2648  HA3 GLY A 181      24.629 -64.332 -50.065  1.00  0.00           H
ATOM   2649  N   VAL A 182      22.863 -65.458 -51.733  1.00 22.65           N
ANISOU 2649  N   VAL A 182     2625   3031   2950      5   -414   -732       N
ATOM   2650  CA  VAL A 182      22.333 -66.413 -52.664  1.00 22.83           C
ANISOU 2650  CA  VAL A 182     2682   3035   2959    -49   -440   -804       C
ATOM   2651  C   VAL A 182      23.180 -66.274 -53.928  1.00 22.24           C
ANISOU 2651  C   VAL A 182     2662   2947   2842     13   -420   -854       C
ATOM   2652  O   VAL A 182      23.380 -65.175 -54.438  1.00 23.43           O
ANISOU 2652  O   VAL A 182     2798   3165   2940     71   -411   -842       O
ATOM   2653  CB  VAL A 182      20.852 -66.130 -52.990  1.00 24.34           C
ANISOU 2653  CB  VAL A 182     2813   3323   3111   -106   -490   -823       C
ATOM   2654  CG1 VAL A 182      20.295 -67.196 -53.938  1.00 27.39           C
ANISOU 2654  CG1 VAL A 182     3238   3684   3487   -174   -531   -905       C
ATOM   2655  CG2 VAL A 182      20.016 -66.090 -51.730  1.00 24.18           C
ANISOU 2655  CG2 VAL A 182     2727   3330   3131   -160   -490   -770       C
ATOM   2656  H   VAL A 182      23.083 -64.532 -52.070  1.00  0.00           H
ATOM   2657  HA  VAL A 182      22.436 -67.420 -52.259  1.00  0.00           H
ATOM   2658  HB  VAL A 182      20.785 -65.160 -53.482  1.00  0.00           H
ATOM   2659 HG11 VAL A 182      20.897 -67.225 -54.846  1.00  0.00           H
ATOM   2660 HG12 VAL A 182      20.328 -68.170 -53.449  1.00  0.00           H
ATOM   2661 HG13 VAL A 182      19.264 -66.952 -54.193  1.00  0.00           H
ATOM   2662 HG21 VAL A 182      20.412 -65.331 -51.055  1.00  0.00           H
ATOM   2663 HG22 VAL A 182      20.049 -67.064 -51.241  1.00  0.00           H
ATOM   2664 HG23 VAL A 182      18.985 -65.846 -51.986  1.00  0.00           H
ATOM   2665  N   HIS A 183      23.683 -67.394 -54.422  1.00 22.22           N
ANISOU 2665  N   HIS A 183     2727   2852   2862      1   -407   -911       N
ATOM   2666  CA  HIS A 183      24.490 -67.403 -55.615  1.00 23.06           C
ANISOU 2666  CA  HIS A 183     2895   2939   2927     56   -372   -966       C
ATOM   2667  C   HIS A 183      23.598 -67.548 -56.853  1.00 23.85           C
ANISOU 2667  C   HIS A 183     3030   3094   2939     16   -417  -1041       C
ATOM   2668  O   HIS A 183      22.734 -68.425 -56.881  1.00 24.85           O
ANISOU 2668  O   HIS A 183     3165   3201   3077    -65   -466  -1083       O
ATOM   2669  CB  HIS A 183      25.460 -68.583 -55.544  1.00 23.83           C
ANISOU 2669  CB  HIS A 183     3053   2905   3097     69   -333   -999       C
ATOM   2670  CG  HIS A 183      26.430 -68.632 -56.685  1.00 25.16           C
ANISOU 2670  CG  HIS A 183     3282   3044   3234    134   -274  -1057       C
ATOM   2671  ND1 HIS A 183      26.804 -69.805 -57.302  1.00 24.73           N
ANISOU 2671  ND1 HIS A 183     3305   2892   3197    129   -251  -1137       N
ATOM   2672  CD2 HIS A 183      27.120 -67.647 -57.307  1.00 26.59           C
ANISOU 2672  CD2 HIS A 183     3460   3275   3368    205   -224  -1047       C
ATOM   2673  CE1 HIS A 183      27.654 -69.535 -58.277  1.00 25.44           C
ANISOU 2673  CE1 HIS A 183     3437   2982   3246    197   -184  -1178       C
ATOM   2674  NE2 HIS A 183      27.874 -68.234 -58.292  1.00 25.70           N
ANISOU 2674  NE2 HIS A 183     3420   3104   3240    241   -165  -1120       N
ATOM   2675  H   HIS A 183      23.496 -68.267 -53.949  1.00  0.00           H
ATOM   2676  HA  HIS A 183      25.054 -66.472 -55.680  1.00  0.00           H
ATOM   2677  HB2 HIS A 183      26.025 -68.509 -54.615  1.00  0.00           H
ATOM   2678  HB3 HIS A 183      24.885 -69.509 -55.532  1.00  0.00           H
ATOM   2679  HD2 HIS A 183      27.084 -66.594 -57.071  1.00  0.00           H
ATOM   2680  HE1 HIS A 183      28.094 -70.257 -58.948  1.00  0.00           H
ATOM   2681  HE2 HIS A 183      28.495 -67.750 -58.924  1.00  0.00           H
ATOM   2682  HD1 HIS A 183      26.479 -70.727 -57.049  1.00  0.00           H
ATOM   2683  N   HIS A 184      23.808 -66.690 -57.856  1.00 23.14           N
ANISOU 2683  N   HIS A 184     2961   3069   2760     70   -405  -1055       N
ATOM   2684  CA  HIS A 184      23.181 -66.839 -59.163  1.00 24.24           C
ANISOU 2684  CA  HIS A 184     3158   3254   2799     46   -448  -1130       C
ATOM   2685  C   HIS A 184      24.205 -67.238 -60.209  1.00 24.74           C
ANISOU 2685  C   HIS A 184     3324   3260   2818     93   -382  -1195       C
ATOM   2686  O   HIS A 184      24.985 -66.392 -60.664  1.00 24.29           O
ANISOU 2686  O   HIS A 184     3284   3230   2717    166   -322  -1170       O
ATOM   2687  CB  HIS A 184      22.574 -65.513 -59.621  1.00 24.76           C
ANISOU 2687  CB  HIS A 184     3188   3441   2778     74   -487  -1094       C
ATOM   2688  CG  HIS A 184      21.664 -64.871 -58.629  1.00 27.06           C
ANISOU 2688  CG  HIS A 184     3372   3799   3112     51   -534  -1026       C
ATOM   2689  ND1 HIS A 184      20.294 -65.034 -58.664  1.00 30.15           N
ANISOU 2689  ND1 HIS A 184     3714   4242   3499    -17   -609  -1025       N
ATOM   2690  CD2 HIS A 184      21.913 -63.999 -57.623  1.00 26.85           C
ANISOU 2690  CD2 HIS A 184     3278   3792   3134     89   -504   -945       C
ATOM   2691  CE1 HIS A 184      19.746 -64.325 -57.693  1.00 30.06           C
ANISOU 2691  CE1 HIS A 184     3607   4283   3533    -16   -620   -960       C
ATOM   2692  NE2 HIS A 184      20.708 -63.688 -57.048  1.00 28.18           N
ANISOU 2692  NE2 HIS A 184     3361   4027   3318     48   -561   -918       N
ATOM   2693  H   HIS A 184      24.426 -65.906 -57.702  1.00  0.00           H
ATOM   2694  HA  HIS A 184      22.400 -67.598 -59.109  1.00  0.00           H
ATOM   2695  HB2 HIS A 184      23.389 -64.821 -59.832  1.00  0.00           H
ATOM   2696  HB3 HIS A 184      22.018 -65.685 -60.542  1.00  0.00           H
ATOM   2697  HD2 HIS A 184      22.880 -63.619 -57.329  1.00  0.00           H
ATOM   2698  HE1 HIS A 184      18.692 -64.275 -57.465  1.00  0.00           H
ATOM   2699  HE2 HIS A 184      20.576 -63.072 -56.259  1.00  0.00           H
ATOM   2700  N   PRO A 185      24.225 -68.526 -60.594  1.00 24.83           N
ANISOU 2700  N   PRO A 185     3406   3185   2843     51   -382  -1271       N
ATOM   2701  CA  PRO A 185      25.152 -69.003 -61.620  1.00 26.07           C
ANISOU 2701  CA  PRO A 185     3666   3281   2960     93   -304  -1323       C
ATOM   2702  C   PRO A 185      24.805 -68.443 -62.980  1.00 27.53           C
ANISOU 2702  C   PRO A 185     3917   3543   3000     97   -314  -1336       C
ATOM   2703  O   PRO A 185      23.664 -68.066 -63.256  1.00 27.08           O
ANISOU 2703  O   PRO A 185     3840   3567   2882     50   -402  -1320       O
ATOM   2704  CB  PRO A 185      24.942 -70.528 -61.618  1.00 27.01           C
ANISOU 2704  CB  PRO A 185     3841   3291   3129     28   -320  -1384       C
ATOM   2705  CG  PRO A 185      24.326 -70.815 -60.293  1.00 26.29           C
ANISOU 2705  CG  PRO A 185     3667   3182   3140    -28   -378  -1349       C
ATOM   2706  CD  PRO A 185      23.482 -69.638 -59.985  1.00 24.76           C
ANISOU 2706  CD  PRO A 185     3384   3116   2906    -39   -436  -1291       C
ATOM   2707  HA  PRO A 185      26.180 -68.756 -61.354  1.00  0.00           H
ATOM   2708  HB2 PRO A 185      24.274 -70.826 -62.426  1.00  0.00           H
ATOM   2709  HB3 PRO A 185      25.899 -71.042 -61.709  1.00  0.00           H
ATOM   2710  HG2 PRO A 185      25.098 -70.939 -59.533  1.00  0.00           H
ATOM   2711  HG3 PRO A 185      23.710 -71.713 -60.352  1.00  0.00           H
ATOM   2712  HD2 PRO A 185      23.383 -69.499 -58.908  1.00  0.00           H
ATOM   2713  HD3 PRO A 185      22.501 -69.740 -60.449  1.00  0.00           H
ATOM   2714  N   SER A 186      25.803 -68.351 -63.835  1.00 29.57           N
ANISOU 2714  N   SER A 186     4253   3776   3207    156   -220  -1358       N
ATOM   2715  CA  SER A 186      25.567 -67.807 -65.150  1.00 33.04           C
ANISOU 2715  CA  SER A 186     4772   4282   3500    160   -219  -1367       C
ATOM   2716  C   SER A 186      24.996 -68.863 -66.120  1.00 32.00           C
ANISOU 2716  C   SER A 186     4748   4114   3297     92   -257  -1446       C
ATOM   2717  O   SER A 186      24.357 -68.495 -67.098  1.00 31.47           O
ANISOU 2717  O   SER A 186     4736   4113   3108     66   -305  -1453       O
ATOM   2718  CB  SER A 186      26.860 -67.196 -65.678  1.00 39.14           C
ANISOU 2718  CB  SER A 186     5583   5046   4241    243    -90  -1352       C
ATOM   2719  OG  SER A 186      27.864 -68.185 -65.780  1.00 44.47           O
ANISOU 2719  OG  SER A 186     6307   5612   4977    265      8  -1403       O
ATOM   2720  H   SER A 186      26.728 -68.660 -63.571  1.00  0.00           H
ATOM   2721  HA  SER A 186      24.833 -67.007 -65.055  1.00  0.00           H
ATOM   2722  HB2 SER A 186      26.678 -66.765 -66.663  1.00  0.00           H
ATOM   2723  HB3 SER A 186      27.193 -66.412 -64.997  1.00  0.00           H
ATOM   2724  HG  SER A 186      28.178 -68.415 -64.902  1.00  0.00           H
ATOM   2725  N   THR A 187      25.214 -70.157 -65.837  1.00 32.18           N
ANISOU 2725  N   THR A 187     4801   4028   3397     62   -239  -1503       N
ATOM   2726  CA  THR A 187      24.731 -71.247 -66.704  1.00 34.85           C
ANISOU 2726  CA  THR A 187     5248   4316   3676     -6   -270  -1586       C
ATOM   2727  C   THR A 187      24.138 -72.424 -65.907  1.00 34.09           C
ANISOU 2727  C   THR A 187     5126   4140   3688    -81   -334  -1613       C
ATOM   2728  O   THR A 187      24.386 -72.579 -64.700  1.00 33.36           O
ANISOU 2728  O   THR A 187     4949   4004   3722    -69   -326  -1576       O
ATOM   2729  CB  THR A 187      25.857 -71.847 -67.606  1.00 38.26           C
ANISOU 2729  CB  THR A 187     5805   4665   4068     38   -143  -1651       C
ATOM   2730  OG1 THR A 187      26.825 -72.524 -66.787  1.00 37.13           O
ANISOU 2730  OG1 THR A 187     5634   4410   4062     86    -67  -1652       O
ATOM   2731  CG2 THR A 187      26.540 -70.773 -68.444  1.00 38.58           C
ANISOU 2731  CG2 THR A 187     5879   4774   4006    103    -56  -1626       C
ATOM   2732  H   THR A 187      25.728 -70.392 -65.000  1.00  0.00           H
ATOM   2733  HA  THR A 187      23.951 -70.847 -67.352  1.00  0.00           H
ATOM   2734  HB  THR A 187      25.407 -72.575 -68.280  1.00  0.00           H
ATOM   2735  HG1 THR A 187      27.449 -72.991 -67.348  1.00  0.00           H
ATOM   2736 HG21 THR A 187      27.317 -71.229 -69.058  1.00  0.00           H
ATOM   2737 HG22 THR A 187      26.988 -70.029 -67.785  1.00  0.00           H
ATOM   2738 HG23 THR A 187      25.804 -70.292 -69.088  1.00  0.00           H
ATOM   2739  N   ASN A 188      23.337 -73.235 -66.577  1.00 34.73           N
ANISOU 2739  N   ASN A 188     5281   4199   3715   -164   -398  -1675       N
ATOM   2740  CA  ASN A 188      22.801 -74.443 -65.946  1.00 38.02           C
ANISOU 2740  CA  ASN A 188     5692   4526   4229   -245   -449  -1705       C
ATOM   2741  C   ASN A 188      23.910 -75.434 -65.591  1.00 38.23           C
ANISOU 2741  C   ASN A 188     5770   4407   4348   -202   -353  -1739       C
ATOM   2742  O   ASN A 188      23.816 -76.127 -64.581  1.00 36.48           O
ANISOU 2742  O   ASN A 188     5504   4109   4249   -234   -371  -1724       O
ATOM   2743  CB  ASN A 188      21.770 -75.133 -66.842  1.00 42.50           C
ANISOU 2743  CB  ASN A 188     6337   5095   4717   -348   -534  -1770       C
ATOM   2744  CG  ASN A 188      20.467 -74.350 -66.959  1.00 44.47           C
ANISOU 2744  CG  ASN A 188     6507   5474   4915   -405   -654  -1726       C
ATOM   2745  OD1 ASN A 188      19.831 -74.001 -65.961  1.00 41.97           O
ANISOU 2745  OD1 ASN A 188     6065   5200   4682   -429   -707  -1662       O
ATOM   2746  ND2 ASN A 188      20.056 -74.085 -68.199  1.00 48.67           N
ANISOU 2746  ND2 ASN A 188     7114   6070   5309   -428   -692  -1761       N
ATOM   2747  H   ASN A 188      23.092 -73.019 -67.533  1.00  0.00           H
ATOM   2748  HA  ASN A 188      22.303 -74.149 -65.022  1.00  0.00           H
ATOM   2749  HB2 ASN A 188      21.549 -76.115 -66.425  1.00  0.00           H
ATOM   2750  HB3 ASN A 188      22.196 -75.260 -67.837  1.00  0.00           H
ATOM   2751 HD21 ASN A 188      20.604 -74.394 -68.989  1.00  0.00           H
ATOM   2752 HD22 ASN A 188      19.197 -73.575 -68.348  1.00  0.00           H
ATOM   2753  N   GLN A 189      24.950 -75.502 -66.423  1.00 39.90           N
ANISOU 2753  N   GLN A 189     6077   4579   4504   -130   -248  -1780       N
ATOM   2754  CA  GLN A 189      26.089 -76.365 -66.136  1.00 42.35           C
ANISOU 2754  CA  GLN A 189     6430   4753   4908    -69   -150  -1803       C
ATOM   2755  C   GLN A 189      26.729 -75.987 -64.805  1.00 37.91           C
ANISOU 2755  C   GLN A 189     5744   4176   4483     -9   -122  -1723       C
ATOM   2756  O   GLN A 189      27.047 -76.852 -64.001  1.00 37.04           O
ANISOU 2756  O   GLN A 189     5622   3956   4495     -8   -113  -1718       O
ATOM   2757  CB  GLN A 189      27.138 -76.296 -67.252  1.00 50.36           C
ANISOU 2757  CB  GLN A 189     7550   5745   5838     10    -28  -1847       C
ATOM   2758  CG  GLN A 189      28.451 -77.017 -66.902  1.00 59.71           C
ANISOU 2758  CG  GLN A 189     8757   6799   7132    104     78  -1851       C
ATOM   2759  CD  GLN A 189      29.493 -76.971 -68.028  1.00 69.94           C
ANISOU 2759  CD  GLN A 189    10145   8079   8349    198    196  -1881       C
ATOM   2760  OE1 GLN A 189      29.489 -76.064 -68.869  1.00 74.06           O
ANISOU 2760  OE1 GLN A 189    10685   8701   8753    204    231  -1873       O
ATOM   2761  NE2 GLN A 189      30.389 -77.959 -68.047  1.00 73.53           N
ANISOU 2761  NE2 GLN A 189    10646   8415   8875    279    248  -1910       N
ATOM   2762  H   GLN A 189      24.948 -74.946 -67.266  1.00  0.00           H
ATOM   2763  HA  GLN A 189      25.731 -77.392 -66.065  1.00  0.00           H
ATOM   2764  HB2 GLN A 189      27.362 -75.248 -67.451  1.00  0.00           H
ATOM   2765  HB3 GLN A 189      26.721 -76.744 -68.154  1.00  0.00           H
ATOM   2766  HG2 GLN A 189      28.224 -78.061 -66.684  1.00  0.00           H
ATOM   2767  HG3 GLN A 189      28.877 -76.557 -66.010  1.00  0.00           H
ATOM   2768 HE21 GLN A 189      30.358 -78.683 -67.343  1.00  0.00           H
ATOM   2769 HE22 GLN A 189      31.099 -77.983 -68.765  1.00  0.00           H
ATOM   2770  N   GLU A 190      26.917 -74.692 -64.577  1.00 36.15           N
ANISOU 2770  N   GLU A 190     5435   4060   4241     39   -110  -1659       N
ATOM   2771  CA  GLU A 190      27.460 -74.224 -63.313  1.00 35.54           C
ANISOU 2771  CA  GLU A 190     5241   3979   4284     88    -94  -1584       C
ATOM   2772  C   GLU A 190      26.497 -74.592 -62.178  1.00 33.28           C
ANISOU 2772  C   GLU A 190     4886   3680   4081      6   -194  -1555       C
ATOM   2773  O   GLU A 190      26.909 -75.103 -61.125  1.00 31.40           O
ANISOU 2773  O   GLU A 190     4608   3354   3968     17   -185  -1524       O
ATOM   2774  CB  GLU A 190      27.681 -72.707 -63.367  1.00 37.26           C
ANISOU 2774  CB  GLU A 190     5389   4319   4448    142    -73  -1525       C
ATOM   2775  CG  GLU A 190      28.330 -72.096 -62.128  1.00 40.59           C
ANISOU 2775  CG  GLU A 190     5696   4741   4985    197    -52  -1449       C
ATOM   2776  CD  GLU A 190      28.542 -70.577 -62.261  1.00 43.26           C
ANISOU 2776  CD  GLU A 190     5977   5196   5264    247    -30  -1394       C
ATOM   2777  OE1 GLU A 190      28.371 -70.061 -63.395  1.00 46.04           O
ANISOU 2777  OE1 GLU A 190     6390   5616   5488    250    -12  -1413       O
ATOM   2778  OE2 GLU A 190      28.874 -69.911 -61.240  1.00 41.47           O
ANISOU 2778  OE2 GLU A 190     5653   4986   5116    280    -32  -1330       O
ATOM   2779  H   GLU A 190      26.679 -74.022 -65.294  1.00  0.00           H
ATOM   2780  HA  GLU A 190      28.417 -74.714 -63.137  1.00  0.00           H
ATOM   2781  HB2 GLU A 190      28.320 -72.491 -64.223  1.00  0.00           H
ATOM   2782  HB3 GLU A 190      26.717 -72.223 -63.525  1.00  0.00           H
ATOM   2783  HG2 GLU A 190      27.688 -72.285 -61.268  1.00  0.00           H
ATOM   2784  HG3 GLU A 190      29.295 -72.575 -61.961  1.00  0.00           H
ATOM   2785  N   GLN A 191      25.214 -74.324 -62.383  1.00 32.07           N
ANISOU 2785  N   GLN A 191     4716   3612   3858    -77   -288  -1558       N
ATOM   2786  CA  GLN A 191      24.226 -74.612 -61.342  1.00 31.40           C
ANISOU 2786  CA  GLN A 191     4557   3525   3847   -163   -372  -1525       C
ATOM   2787  C   GLN A 191      24.305 -76.082 -60.894  1.00 31.80           C
ANISOU 2787  C   GLN A 191     4662   3426   3996   -211   -369  -1554       C
ATOM   2788  O   GLN A 191      24.343 -76.404 -59.698  1.00 29.89           O
ANISOU 2788  O   GLN A 191     4368   3124   3864   -229   -378  -1507       O
ATOM   2789  CB  GLN A 191      22.827 -74.283 -61.866  1.00 31.58           C
ANISOU 2789  CB  GLN A 191     4563   3655   3783   -248   -468  -1531       C
ATOM   2790  CG  GLN A 191      21.683 -74.758 -60.991  1.00 30.73           C
ANISOU 2790  CG  GLN A 191     4388   3541   3747   -355   -547  -1505       C
ATOM   2791  CD  GLN A 191      21.576 -74.005 -59.689  1.00 29.29           C
ANISOU 2791  CD  GLN A 191     4083   3407   3637   -343   -552  -1423       C
ATOM   2792  OE1 GLN A 191      21.820 -72.805 -59.628  1.00 28.53           O
ANISOU 2792  OE1 GLN A 191     3932   3406   3503   -276   -538  -1382       O
ATOM   2793  NE2 GLN A 191      21.226 -74.712 -58.626  1.00 29.99           N
ANISOU 2793  NE2 GLN A 191     4139   3428   3829   -410   -568  -1398       N
ATOM   2794  H   GLN A 191      24.918 -73.920 -63.260  1.00  0.00           H
ATOM   2795  HA  GLN A 191      24.433 -73.975 -60.482  1.00  0.00           H
ATOM   2796  HB2 GLN A 191      22.717 -74.746 -62.847  1.00  0.00           H
ATOM   2797  HB3 GLN A 191      22.747 -73.202 -61.983  1.00  0.00           H
ATOM   2798  HG2 GLN A 191      20.751 -74.631 -61.541  1.00  0.00           H
ATOM   2799  HG3 GLN A 191      21.822 -75.817 -60.774  1.00  0.00           H
ATOM   2800 HE21 GLN A 191      21.145 -74.263 -57.725  1.00  0.00           H
ATOM   2801 HE22 GLN A 191      21.040 -75.701 -58.716  1.00  0.00           H
ATOM   2802  N   THR A 192      24.357 -76.995 -61.850  1.00 33.67           N
ANISOU 2802  N   THR A 192     5013   3593   4188   -233   -355  -1630       N
ATOM   2803  CA  THR A 192      24.278 -78.402 -61.489  1.00 35.88           C
ANISOU 2803  CA  THR A 192     5351   3729   4553   -289   -362  -1658       C
ATOM   2804  C   THR A 192      25.638 -78.908 -60.998  1.00 36.62           C
ANISOU 2804  C   THR A 192     5468   3699   4746   -195   -273  -1643       C
ATOM   2805  O   THR A 192      25.687 -79.746 -60.108  1.00 37.61           O
ANISOU 2805  O   THR A 192     5594   3716   4981   -222   -282  -1617       O
ATOM   2806  CB  THR A 192      23.683 -79.279 -62.615  1.00 38.25           C
ANISOU 2806  CB  THR A 192     5769   3991   4774   -363   -393  -1747       C
ATOM   2807  OG1 THR A 192      24.412 -79.091 -63.834  1.00 41.02           O
ANISOU 2807  OG1 THR A 192     6212   4352   5023   -289   -326  -1804       O
ATOM   2808  CG2 THR A 192      22.230 -78.924 -62.832  1.00 37.05           C
ANISOU 2808  CG2 THR A 192     5570   3947   4559   -470   -500  -1744       C
ATOM   2809  H   THR A 192      24.450 -76.719 -62.817  1.00  0.00           H
ATOM   2810  HA  THR A 192      23.594 -78.471 -60.643  1.00  0.00           H
ATOM   2811  HB  THR A 192      23.751 -80.326 -62.321  1.00  0.00           H
ATOM   2812  HG1 THR A 192      24.576 -78.155 -63.968  1.00  0.00           H
ATOM   2813 HG21 THR A 192      21.818 -79.546 -63.627  1.00  0.00           H
ATOM   2814 HG22 THR A 192      21.673 -79.096 -61.911  1.00  0.00           H
ATOM   2815 HG23 THR A 192      22.151 -77.874 -63.114  1.00  0.00           H
ATOM   2816  N   SER A 193      26.734 -78.351 -61.510  1.00 36.80           N
ANISOU 2816  N   SER A 193     5501   3742   4739    -84   -189  -1646       N
ATOM   2817  CA  SER A 193      28.070 -78.785 -61.085  1.00 38.27           C
ANISOU 2817  CA  SER A 193     5693   3821   5028     15   -105  -1624       C
ATOM   2818  C   SER A 193      28.244 -78.466 -59.616  1.00 35.27           C
ANISOU 2818  C   SER A 193     5205   3431   4764     28   -131  -1531       C
ATOM   2819  O   SER A 193      28.820 -79.247 -58.860  1.00 36.06           O
ANISOU 2819  O   SER A 193     5312   3413   4976     54   -116  -1499       O
ATOM   2820  CB  SER A 193      29.172 -78.057 -61.854  1.00 42.48           C
ANISOU 2820  CB  SER A 193     6230   4401   5510    126     -7  -1630       C
ATOM   2821  OG  SER A 193      29.323 -78.594 -63.155  1.00 48.87           O
ANISOU 2821  OG  SER A 193     7164   5178   6227    136     39  -1714       O
ATOM   2822  H   SER A 193      26.644 -77.619 -62.201  1.00  0.00           H
ATOM   2823  HA  SER A 193      28.169 -79.860 -61.238  1.00  0.00           H
ATOM   2824  HB2 SER A 193      28.914 -77.001 -61.932  1.00  0.00           H
ATOM   2825  HB3 SER A 193      30.113 -78.157 -61.313  1.00  0.00           H
ATOM   2826  HG  SER A 193      28.771 -78.105 -63.769  1.00  0.00           H
ATOM   2827  N   LEU A 194      27.739 -77.300 -59.221  1.00 31.82           N
ANISOU 2827  N   LEU A 194     4677   3119   4294     12   -172  -1486       N
ATOM   2828  CA  LEU A 194      27.905 -76.833 -57.857  1.00 30.63           C
ANISOU 2828  CA  LEU A 194     4432   2971   4236     28   -197  -1400       C
ATOM   2829  C   LEU A 194      26.878 -77.426 -56.882  1.00 30.48           C
ANISOU 2829  C   LEU A 194     4401   2909   4272    -79   -276  -1370       C
ATOM   2830  O   LEU A 194      27.223 -77.784 -55.757  1.00 30.77           O
ANISOU 2830  O   LEU A 194     4418   2862   4411    -70   -284  -1307       O
ATOM   2831  CB  LEU A 194      27.778 -75.315 -57.834  1.00 30.61           C
ANISOU 2831  CB  LEU A 194     4343   3115   4171     57   -205  -1366       C
ATOM   2832  CG  LEU A 194      28.875 -74.514 -58.555  1.00 33.56           C
ANISOU 2832  CG  LEU A 194     4708   3537   4505    163   -119  -1367       C
ATOM   2833  CD1 LEU A 194      28.615 -73.023 -58.426  1.00 32.08           C
ANISOU 2833  CD1 LEU A 194     4441   3488   4258    179   -137  -1326       C
ATOM   2834  CD2 LEU A 194      30.279 -74.839 -58.028  1.00 36.85           C
ANISOU 2834  CD2 LEU A 194     5105   3858   5038    254    -53  -1324       C
ATOM   2835  H   LEU A 194      27.231 -76.730 -59.882  1.00  0.00           H
ATOM   2836  HA  LEU A 194      28.904 -77.103 -57.516  1.00  0.00           H
ATOM   2837  HB2 LEU A 194      26.825 -75.057 -58.296  1.00  0.00           H
ATOM   2838  HB3 LEU A 194      27.750 -74.992 -56.793  1.00  0.00           H
ATOM   2839  HG  LEU A 194      28.843 -74.773 -59.613  1.00  0.00           H
ATOM   2840 HD11 LEU A 194      27.617 -72.794 -58.801  1.00  0.00           H
ATOM   2841 HD12 LEU A 194      28.685 -72.732 -57.378  1.00  0.00           H
ATOM   2842 HD13 LEU A 194      29.356 -72.473 -59.006  1.00  0.00           H
ATOM   2843 HD21 LEU A 194      30.464 -75.909 -58.121  1.00  0.00           H
ATOM   2844 HD22 LEU A 194      30.350 -74.548 -56.980  1.00  0.00           H
ATOM   2845 HD23 LEU A 194      31.021 -74.290 -58.608  1.00  0.00           H
ATOM   2846  N   TYR A 195      25.618 -77.496 -57.306  1.00 29.85           N
ANISOU 2846  N   TYR A 195     4329   2890   4122   -183   -334  -1406       N
ATOM   2847  CA  TYR A 195      24.496 -77.644 -56.367  1.00 30.56           C
ANISOU 2847  CA  TYR A 195     4371   2991   4250   -292   -403  -1363       C
ATOM   2848  C   TYR A 195      23.606 -78.862 -56.668  1.00 32.12           C
ANISOU 2848  C   TYR A 195     4636   3117   4453   -408   -439  -1407       C
ATOM   2849  O   TYR A 195      22.673 -79.146 -55.901  1.00 32.71           O
ANISOU 2849  O   TYR A 195     4673   3186   4569   -511   -485  -1369       O
ATOM   2850  CB  TYR A 195      23.636 -76.376 -56.389  1.00 30.41           C
ANISOU 2850  CB  TYR A 195     4258   3142   4156   -319   -446  -1342       C
ATOM   2851  CG  TYR A 195      24.445 -75.125 -56.129  1.00 27.95           C
ANISOU 2851  CG  TYR A 195     3884   2910   3824   -212   -406  -1282       C
ATOM   2852  CD1 TYR A 195      25.270 -75.031 -55.011  1.00 25.08           C
ANISOU 2852  CD1 TYR A 195     3492   2497   3540   -157   -374  -1191       C
ATOM   2853  CD2 TYR A 195      24.433 -74.063 -57.024  1.00 27.20           C
ANISOU 2853  CD2 TYR A 195     3770   2938   3628   -166   -400  -1306       C
ATOM   2854  CE1 TYR A 195      26.047 -73.896 -54.785  1.00 22.92           C
ANISOU 2854  CE1 TYR A 195     3161   2294   3252    -65   -339  -1131       C
ATOM   2855  CE2 TYR A 195      25.205 -72.920 -56.798  1.00 25.06           C
ANISOU 2855  CE2 TYR A 195     3447   2734   3343    -74   -355  -1240       C
ATOM   2856  CZ  TYR A 195      26.016 -72.854 -55.677  1.00 23.99           C
ANISOU 2856  CZ  TYR A 195     3274   2545   3294    -26   -325  -1157       C
ATOM   2857  OH  TYR A 195      26.817 -71.749 -55.426  1.00 24.76           O
ANISOU 2857  OH  TYR A 195     3319   2701   3389     58   -287  -1096       O
ATOM   2858  H   TYR A 195      25.428 -77.446 -58.297  1.00  0.00           H
ATOM   2859  HA  TYR A 195      24.905 -77.761 -55.363  1.00  0.00           H
ATOM   2860  HB2 TYR A 195      22.867 -76.461 -55.621  1.00  0.00           H
ATOM   2861  HB3 TYR A 195      23.155 -76.291 -57.364  1.00  0.00           H
ATOM   2862  HD1 TYR A 195      25.308 -75.850 -54.308  1.00  0.00           H
ATOM   2863  HD2 TYR A 195      23.817 -74.121 -57.909  1.00  0.00           H
ATOM   2864  HE1 TYR A 195      26.674 -73.837 -53.907  1.00  0.00           H
ATOM   2865  HE2 TYR A 195      25.169 -72.094 -57.493  1.00  0.00           H
ATOM   2866  HH  TYR A 195      26.333 -71.119 -54.887  1.00  0.00           H
ATOM   2867  N   VAL A 196      23.906 -79.550 -57.775  1.00 32.78           N
ANISOU 2867  N   VAL A 196     4818   3145   4492   -394   -414  -1485       N
ATOM   2868  CA  VAL A 196      23.195 -80.760 -58.223  1.00 34.02           C
ANISOU 2868  CA  VAL A 196     5059   3220   4647   -496   -445  -1541       C
ATOM   2869  C   VAL A 196      21.768 -80.432 -58.651  1.00 34.94           C
ANISOU 2869  C   VAL A 196     5133   3451   4689   -607   -525  -1559       C
ATOM   2870  O   VAL A 196      21.375 -80.690 -59.795  1.00 35.40           O
ANISOU 2870  O   VAL A 196     5258   3530   4663   -640   -551  -1632       O
ATOM   2871  CB  VAL A 196      23.176 -81.835 -57.140  1.00 34.34           C
ANISOU 2871  CB  VAL A 196     5124   3116   4808   -550   -446  -1495       C
ATOM   2872  CG1 VAL A 196      22.407 -83.093 -57.626  1.00 38.50           C
ANISOU 2872  CG1 VAL A 196     5741   3554   5333   -665   -477  -1555       C
ATOM   2873  CG2 VAL A 196      24.610 -82.196 -56.749  1.00 34.37           C
ANISOU 2873  CG2 VAL A 196     5167   3003   4888   -429   -376  -1469       C
ATOM   2874  H   VAL A 196      24.672 -79.217 -58.343  1.00  0.00           H
ATOM   2875  HA  VAL A 196      23.723 -81.161 -59.088  1.00  0.00           H
ATOM   2876  HB  VAL A 196      22.667 -81.435 -56.263  1.00  0.00           H
ATOM   2877 HG21 VAL A 196      24.594 -82.964 -55.976  1.00  0.00           H
ATOM   2878 HG22 VAL A 196      25.141 -82.573 -57.623  1.00  0.00           H
ATOM   2879 HG23 VAL A 196      25.117 -81.309 -56.370  1.00  0.00           H
ATOM   2880 HG11 VAL A 196      21.389 -82.814 -57.899  1.00  0.00           H
ATOM   2881 HG12 VAL A 196      22.379 -83.833 -56.826  1.00  0.00           H
ATOM   2882 HG13 VAL A 196      22.913 -83.516 -58.494  1.00  0.00           H
ATOM   2883  N   GLN A 197      20.989 -79.855 -57.748  1.00 35.93           N
ANISOU 2883  N   GLN A 197     5149   3655   4846   -662   -566  -1491       N
ATOM   2884  CA  GLN A 197      19.641 -79.424 -58.098  1.00 38.97           C
ANISOU 2884  CA  GLN A 197     5470   4165   5174   -754   -641  -1494       C
ATOM   2885  C   GLN A 197      19.668 -78.409 -59.254  1.00 40.17           C
ANISOU 2885  C   GLN A 197     5617   4446   5199   -689   -655  -1528       C
ATOM   2886  O   GLN A 197      20.570 -77.543 -59.332  1.00 39.27           O
ANISOU 2886  O   GLN A 197     5491   4376   5055   -577   -605  -1513       O
ATOM   2887  CB  GLN A 197      18.951 -78.803 -56.878  1.00 37.36           C
ANISOU 2887  CB  GLN A 197     5137   4033   5026   -800   -660  -1407       C
ATOM   2888  CG  GLN A 197      18.327 -79.802 -55.919  1.00 37.72           C
ANISOU 2888  CG  GLN A 197     5178   3982   5172   -918   -669  -1371       C
ATOM   2889  CD  GLN A 197      19.345 -80.634 -55.133  1.00 37.38           C
ANISOU 2889  CD  GLN A 197     5212   3773   5219   -883   -612  -1345       C
ATOM   2890  OE1 GLN A 197      19.565 -81.816 -55.417  1.00 37.06           O
ANISOU 2890  OE1 GLN A 197     5276   3598   5209   -913   -602  -1384       O
ATOM   2891  NE2 GLN A 197      19.918 -80.040 -54.113  1.00 37.25           N
ANISOU 2891  NE2 GLN A 197     5146   3760   5248   -823   -580  -1274       N
ATOM   2892  H   GLN A 197      21.332 -79.712 -56.809  1.00  0.00           H
ATOM   2893  HA  GLN A 197      19.069 -80.296 -58.415  1.00  0.00           H
ATOM   2894  HB2 GLN A 197      19.693 -78.224 -56.328  1.00  0.00           H
ATOM   2895  HB3 GLN A 197      18.172 -78.126 -57.228  1.00  0.00           H
ATOM   2896  HG2 GLN A 197      17.700 -80.483 -56.494  1.00  0.00           H
ATOM   2897  HG3 GLN A 197      17.698 -79.261 -55.212  1.00  0.00           H
ATOM   2898 HE21 GLN A 197      20.581 -80.544 -53.542  1.00  0.00           H
ATOM   2899 HE22 GLN A 197      19.696 -79.078 -53.899  1.00  0.00           H
ATOM   2900  N   ALA A 198      18.670 -78.501 -60.129  1.00 40.13           N
ANISOU 2900  N   ALA A 198     5624   4501   5124   -763   -726  -1568       N
ATOM   2901  CA  ALA A 198      18.566 -77.624 -61.304  1.00 41.50           C
ANISOU 2901  CA  ALA A 198     5810   4789   5169   -716   -751  -1596       C
ATOM   2902  C   ALA A 198      18.164 -76.197 -60.946  1.00 41.79           C
ANISOU 2902  C   ALA A 198     5720   4977   5182   -676   -773  -1524       C
ATOM   2903  O   ALA A 198      18.443 -75.255 -61.692  1.00 40.04           O
ANISOU 2903  O   ALA A 198     5507   4842   4865   -602   -767  -1524       O
ATOM   2904  CB  ALA A 198      17.558 -78.205 -62.319  1.00 43.73           C
ANISOU 2904  CB  ALA A 198     6147   5081   5386   -814   -835  -1658       C
ATOM   2905  H   ALA A 198      17.957 -79.200 -59.980  1.00  0.00           H
ATOM   2906  HA  ALA A 198      19.544 -77.588 -61.784  1.00  0.00           H
ATOM   2907  HB1 ALA A 198      17.491 -77.545 -63.184  1.00  0.00           H
ATOM   2908  HB2 ALA A 198      16.578 -78.289 -61.850  1.00  0.00           H
ATOM   2909  HB3 ALA A 198      17.893 -79.191 -62.640  1.00  0.00           H
ATOM   2910  N   SER A 199      17.481 -76.060 -59.816  1.00 44.42           N
ANISOU 2910  N   SER A 199     5941   5337   5599   -731   -793  -1460       N
ATOM   2911  CA  SER A 199      17.096 -74.769 -59.299  1.00 44.39           C
ANISOU 2911  CA  SER A 199     5813   5464   5588   -694   -803  -1387       C
ATOM   2912  C   SER A 199      17.219 -74.829 -57.784  1.00 40.42           C
ANISOU 2912  C   SER A 199     5238   4925   5194   -710   -762  -1325       C
ATOM   2913  O   SER A 199      16.749 -75.781 -57.158  1.00 40.95           O
ANISOU 2913  O   SER A 199     5302   4915   5341   -805   -769  -1321       O
ATOM   2914  CB  SER A 199      15.662 -74.444 -59.695  1.00 48.82           C
ANISOU 2914  CB  SER A 199     6299   6128   6120   -765   -892  -1373       C
ATOM   2915  OG  SER A 199      15.369 -73.091 -59.379  1.00 52.46           O
ANISOU 2915  OG  SER A 199     6654   6717   6563   -706   -896  -1306       O
ATOM   2916  H   SER A 199      17.222 -76.889 -59.300  1.00  0.00           H
ATOM   2917  HA  SER A 199      17.766 -74.004 -59.690  1.00  0.00           H
ATOM   2918  HB2 SER A 199      15.539 -74.600 -60.767  1.00  0.00           H
ATOM   2919  HB3 SER A 199      14.979 -75.099 -59.153  1.00  0.00           H
ATOM   2920  HG  SER A 199      15.991 -72.515 -59.829  1.00  0.00           H
ATOM   2921  N   GLY A 200      17.868 -73.831 -57.193  1.00 34.77           N
ANISOU 2921  N   GLY A 200     4474   4259   4479   -621   -718  -1277       N
ATOM   2922  CA  GLY A 200      18.058 -73.829 -55.751  1.00 33.04           C
ANISOU 2922  CA  GLY A 200     4198   4006   4351   -633   -680  -1219       C
ATOM   2923  C   GLY A 200      17.013 -73.003 -55.054  1.00 34.05           C
ANISOU 2923  C   GLY A 200     4195   4252   4489   -669   -701  -1154       C
ATOM   2924  O   GLY A 200      16.084 -72.488 -55.679  1.00 33.02           O
ANISOU 2924  O   GLY A 200     4013   4224   4310   -684   -749  -1151       O
ATOM   2925  H   GLY A 200      18.231 -73.070 -57.748  1.00  0.00           H
ATOM   2926  HA2 GLY A 200      17.999 -74.854 -55.386  1.00  0.00           H
ATOM   2927  HA3 GLY A 200      19.044 -73.424 -55.522  1.00  0.00           H
ATOM   2928  N   ARG A 201      17.191 -72.824 -53.751  1.00 35.66           N
ANISOU 2928  N   ARG A 201     4352   4441   4754   -672   -659  -1091       N
ATOM   2929  CA  ARG A 201      16.285 -72.004 -52.968  1.00 33.70           C
ANISOU 2929  CA  ARG A 201     3984   4304   4516   -695   -655  -1025       C
ATOM   2930  C   ARG A 201      16.947 -71.732 -51.634  1.00 30.41           C
ANISOU 2930  C   ARG A 201     3572   3854   4128   -650   -583   -927       C
ATOM   2931  O   ARG A 201      17.575 -72.615 -51.074  1.00 30.61           O
ANISOU 2931  O   ARG A 201     3672   3758   4201   -665   -552   -905       O
ATOM   2932  CB  ARG A 201      14.969 -72.746 -52.716  1.00 36.61           C
ANISOU 2932  CB  ARG A 201     4294   4674   4943   -831   -682  -1028       C
ATOM   2933  CG  ARG A 201      14.014 -72.033 -51.743  1.00 37.86           C
ANISOU 2933  CG  ARG A 201     4320   4935   5130   -864   -659   -962       C
ATOM   2934  CD  ARG A 201      12.793 -72.933 -51.394  1.00 42.02           C
ANISOU 2934  CD  ARG A 201     4794   5440   5730  -1004   -665   -952       C
ATOM   2935  NE  ARG A 201      13.205 -74.264 -50.949  1.00 44.48           N
ANISOU 2935  NE  ARG A 201     5196   5601   6104  -1087   -640   -964       N
ATOM   2936  CZ  ARG A 201      13.625 -74.567 -49.716  1.00 48.09           C
ANISOU 2936  CZ  ARG A 201     5688   5986   6597  -1101   -566   -889       C
ATOM   2937  NH1 ARG A 201      13.696 -73.635 -48.753  1.00 48.05           N
ANISOU 2937  NH1 ARG A 201     5634   6053   6568  -1042   -509   -805       N
ATOM   2938  NH2 ARG A 201      13.991 -75.813 -49.442  1.00 50.74           N
ANISOU 2938  NH2 ARG A 201     6123   6169   6985  -1163   -551   -887       N
ATOM   2939  H   ARG A 201      17.975 -73.268 -53.294  1.00  0.00           H
ATOM   2940  HA  ARG A 201      16.090 -71.065 -53.486  1.00  0.00           H
ATOM   2941  HB2 ARG A 201      15.204 -73.728 -52.305  1.00  0.00           H
ATOM   2942  HB3 ARG A 201      14.458 -72.882 -53.669  1.00  0.00           H
ATOM   2943  HG2 ARG A 201      14.553 -71.794 -50.826  1.00  0.00           H
ATOM   2944  HG3 ARG A 201      13.659 -71.110 -52.201  1.00  0.00           H
ATOM   2945  HD2 ARG A 201      12.167 -73.036 -52.280  1.00  0.00           H
ATOM   2946  HD3 ARG A 201      12.214 -72.456 -50.603  1.00  0.00           H
ATOM   2947  HE  ARG A 201      13.170 -75.013 -51.626  1.00  0.00           H
ATOM   2948 HH11 ARG A 201      13.425 -72.683 -48.951  1.00  0.00           H
ATOM   2949 HH12 ARG A 201      14.021 -73.886 -47.830  1.00  0.00           H
ATOM   2950 HH21 ARG A 201      13.946 -76.522 -50.160  1.00  0.00           H
ATOM   2951 HH22 ARG A 201      14.314 -76.052 -48.516  1.00  0.00           H
ATOM   2952  N   VAL A 202      16.800 -70.516 -51.123  1.00 29.47           N
ANISOU 2952  N   VAL A 202     3379   3838   3980   -593   -563   -869       N
ATOM   2953  CA  VAL A 202      17.262 -70.195 -49.761  1.00 28.66           C
ANISOU 2953  CA  VAL A 202     3277   3715   3895   -561   -502   -777       C
ATOM   2954  C   VAL A 202      16.130 -69.565 -48.974  1.00 27.80           C
ANISOU 2954  C   VAL A 202     3062   3708   3793   -603   -483   -731       C
ATOM   2955  O   VAL A 202      15.555 -68.582 -49.395  1.00 29.09           O
ANISOU 2955  O   VAL A 202     3143   3984   3924   -569   -505   -744       O
ATOM   2956  CB  VAL A 202      18.457 -69.232 -49.778  1.00 29.08           C
ANISOU 2956  CB  VAL A 202     3361   3781   3907   -433   -482   -750       C
ATOM   2957  CG1 VAL A 202      18.862 -68.856 -48.347  1.00 28.71           C
ANISOU 2957  CG1 VAL A 202     3316   3721   3872   -407   -434   -661       C
ATOM   2958  CG2 VAL A 202      19.620 -69.874 -50.502  1.00 30.14           C
ANISOU 2958  CG2 VAL A 202     3591   3814   4046   -388   -484   -793       C
ATOM   2959  H   VAL A 202      16.362 -69.796 -51.679  1.00  0.00           H
ATOM   2960  HA  VAL A 202      17.562 -71.118 -49.266  1.00  0.00           H
ATOM   2961  HB  VAL A 202      18.169 -68.326 -50.311  1.00  0.00           H
ATOM   2962 HG11 VAL A 202      18.015 -68.395 -47.838  1.00  0.00           H
ATOM   2963 HG12 VAL A 202      19.165 -69.754 -47.808  1.00  0.00           H
ATOM   2964 HG13 VAL A 202      19.694 -68.153 -48.378  1.00  0.00           H
ATOM   2965 HG21 VAL A 202      20.466 -69.187 -50.512  1.00  0.00           H
ATOM   2966 HG22 VAL A 202      19.904 -70.793 -49.989  1.00  0.00           H
ATOM   2967 HG23 VAL A 202      19.328 -70.105 -51.526  1.00  0.00           H
ATOM   2968  N   THR A 203      15.818 -70.113 -47.817  1.00 27.25           N
ANISOU 2968  N   THR A 203     2993   3595   3764   -673   -437   -676       N
ATOM   2969  CA  THR A 203      14.776 -69.546 -46.975  1.00 29.17           C
ANISOU 2969  CA  THR A 203     3138   3930   4014   -712   -397   -631       C
ATOM   2970  C   THR A 203      15.411 -69.351 -45.604  1.00 26.83           C
ANISOU 2970  C   THR A 203     2896   3595   3702   -679   -333   -546       C
ATOM   2971  O   THR A 203      15.917 -70.288 -45.005  1.00 26.46           O
ANISOU 2971  O   THR A 203     2938   3438   3678   -716   -315   -511       O
ATOM   2972  CB  THR A 203      13.535 -70.458 -46.829  1.00 33.32           C
ANISOU 2972  CB  THR A 203     3604   4451   4603   -854   -392   -645       C
ATOM   2973  OG1 THR A 203      12.863 -70.599 -48.086  1.00 35.61           O
ANISOU 2973  OG1 THR A 203     3836   4786   4907   -890   -466   -728       O
ATOM   2974  CG2 THR A 203      12.543 -69.844 -45.845  1.00 33.41           C
ANISOU 2974  CG2 THR A 203     3511   4557   4626   -886   -327   -593       C
ATOM   2975  H   THR A 203      16.310 -70.940 -47.510  1.00  0.00           H
ATOM   2976  HA  THR A 203      14.471 -68.579 -47.375  1.00  0.00           H
ATOM   2977  HB  THR A 203      13.845 -71.439 -46.469  1.00  0.00           H
ATOM   2978  HG1 THR A 203      12.377 -69.795 -48.281  1.00  0.00           H
ATOM   2979 HG21 THR A 203      11.674 -70.495 -45.751  1.00  0.00           H
ATOM   2980 HG22 THR A 203      13.020 -69.732 -44.871  1.00  0.00           H
ATOM   2981 HG23 THR A 203      12.227 -68.867 -46.210  1.00  0.00           H
ATOM   2982  N   VAL A 204      15.400 -68.120 -45.122  1.00 24.88           N
ANISOU 2982  N   VAL A 204     2605   3436   3414   -606   -306   -514       N
ATOM   2983  CA  VAL A 204      15.934 -67.816 -43.825  1.00 24.39           C
ANISOU 2983  CA  VAL A 204     2595   3349   3323   -574   -254   -440       C
ATOM   2984  C   VAL A 204      14.824 -67.141 -43.045  1.00 25.75           C
ANISOU 2984  C   VAL A 204     2677   3622   3485   -602   -194   -412       C
ATOM   2985  O   VAL A 204      14.190 -66.218 -43.545  1.00 26.98           O
ANISOU 2985  O   VAL A 204     2735   3882   3636   -565   -204   -444       O
ATOM   2986  CB  VAL A 204      17.130 -66.858 -43.959  1.00 24.28           C
ANISOU 2986  CB  VAL A 204     2622   3338   3266   -448   -275   -434       C
ATOM   2987  CG1 VAL A 204      17.674 -66.500 -42.613  1.00 24.11           C
ANISOU 2987  CG1 VAL A 204     2656   3294   3210   -418   -236   -363       C
ATOM   2988  CG2 VAL A 204      18.210 -67.490 -44.810  1.00 25.38           C
ANISOU 2988  CG2 VAL A 204     2835   3386   3424   -415   -322   -467       C
ATOM   2989  H   VAL A 204      15.006 -67.376 -45.680  1.00  0.00           H
ATOM   2990  HA  VAL A 204      16.242 -68.733 -43.322  1.00  0.00           H
ATOM   2991  HB  VAL A 204      16.791 -65.946 -44.450  1.00  0.00           H
ATOM   2992 HG11 VAL A 204      16.887 -66.046 -42.011  1.00  0.00           H
ATOM   2993 HG12 VAL A 204      18.037 -67.400 -42.117  1.00  0.00           H
ATOM   2994 HG13 VAL A 204      18.495 -65.793 -42.729  1.00  0.00           H
ATOM   2995 HG21 VAL A 204      17.800 -67.746 -45.787  1.00  0.00           H
ATOM   2996 HG22 VAL A 204      18.575 -68.394 -44.322  1.00  0.00           H
ATOM   2997 HG23 VAL A 204      19.033 -66.786 -44.934  1.00  0.00           H
ATOM   2998  N   SER A 205      14.587 -67.581 -41.821  1.00 27.15           N
ANISOU 2998  N   SER A 205     2890   3767   3658   -662   -128   -352       N
ATOM   2999  CA  SER A 205      13.457 -67.063 -41.070  1.00 30.91           C
ANISOU 2999  CA  SER A 205     3279   4336   4129   -699    -52   -330       C
ATOM   3000  C   SER A 205      13.756 -66.968 -39.595  1.00 31.68           C
ANISOU 3000  C   SER A 205     3459   4406   4171   -698     21   -255       C
ATOM   3001  O   SER A 205      14.687 -67.613 -39.095  1.00 32.71           O
ANISOU 3001  O   SER A 205     3715   4434   4281   -700      7   -212       O
ATOM   3002  CB  SER A 205      12.255 -67.982 -41.250  1.00 33.78           C
ANISOU 3002  CB  SER A 205     3566   4707   4563   -831    -28   -346       C
ATOM   3003  OG  SER A 205      12.592 -69.303 -40.877  1.00 33.70           O
ANISOU 3003  OG  SER A 205     3656   4573   4574   -916    -21   -312       O
ATOM   3004  H   SER A 205      15.191 -68.277 -41.408  1.00  0.00           H
ATOM   3005  HA  SER A 205      13.205 -66.071 -41.446  1.00  0.00           H
ATOM   3006  HB2 SER A 205      11.435 -67.629 -40.624  1.00  0.00           H
ATOM   3007  HB3 SER A 205      11.944 -67.970 -42.295  1.00  0.00           H
ATOM   3008  HG  SER A 205      12.992 -69.755 -41.624  1.00  0.00           H
ATOM   3009  N   THR A 206      12.950 -66.148 -38.923  1.00 30.87           N
ANISOU 3009  N   THR A 206     3287   4398   4044   -692     96   -243       N
ATOM   3010  CA  THR A 206      12.870 -66.096 -37.475  1.00 30.76           C
ANISOU 3010  CA  THR A 206     3338   4377   3970   -714    187   -178       C
ATOM   3011  C   THR A 206      11.422 -66.459 -37.090  1.00 30.35           C
ANISOU 3011  C   THR A 206     3187   4383   3960   -823    286   -171       C
ATOM   3012  O   THR A 206      10.632 -66.932 -37.924  1.00 31.92           O
ANISOU 3012  O   THR A 206     3279   4606   4243   -890    265   -212       O
ATOM   3013  CB  THR A 206      13.265 -64.722 -36.928  1.00 31.05           C
ANISOU 3013  CB  THR A 206     3392   4471   3933   -603    204   -175       C
ATOM   3014  OG1 THR A 206      12.349 -63.713 -37.377  1.00 33.26           O
ANISOU 3014  OG1 THR A 206     3531   4867   4239   -562    228   -224       O
ATOM   3015  CG2 THR A 206      14.670 -64.319 -37.395  1.00 28.82           C
ANISOU 3015  CG2 THR A 206     3187   4137   3627   -503    107   -186       C
ATOM   3016  H   THR A 206      12.358 -65.524 -39.453  1.00  0.00           H
ATOM   3017  HA  THR A 206      13.543 -66.846 -37.059  1.00  0.00           H
ATOM   3018  HB  THR A 206      13.249 -64.756 -35.839  1.00  0.00           H
ATOM   3019  HG1 THR A 206      12.546 -63.484 -38.288  1.00  0.00           H
ATOM   3020 HG21 THR A 206      14.921 -63.339 -36.990  1.00  0.00           H
ATOM   3021 HG22 THR A 206      15.394 -65.054 -37.043  1.00  0.00           H
ATOM   3022 HG23 THR A 206      14.693 -64.279 -38.484  1.00  0.00           H
ATOM   3023  N  AARG A 207      11.073 -66.277 -35.824  0.48 29.29           N
ANISOU 3023  N  AARG A 207     3089   4271   3770   -847    393   -119       N
ATOM   3024  N  BARG A 207      11.058 -66.235 -35.834  0.52 29.28           N
ANISOU 3024  N  BARG A 207     3084   4273   3768   -844    394   -121       N
ATOM   3025  CA AARG A 207       9.737 -66.626 -35.391  0.48 29.65           C
ANISOU 3025  CA AARG A 207     3038   4370   3858   -953    505   -108       C
ATOM   3026  CA BARG A 207       9.746 -66.655 -35.387  0.52 29.67           C
ANISOU 3026  CA BARG A 207     3042   4370   3861   -955    505   -107       C
ATOM   3027  C  AARG A 207       8.742 -65.852 -36.225  0.48 28.74           C
ANISOU 3027  C  AARG A 207     2730   4374   3817   -925    501   -177       C
ATOM   3028  C  BARG A 207       8.656 -65.756 -35.937  0.52 28.94           C
ANISOU 3028  C  BARG A 207     2759   4408   3828   -925    530   -167       C
ATOM   3029  O  AARG A 207       7.774 -66.406 -36.718  0.48 27.05           O
ANISOU 3029  O  AARG A 207     2394   4189   3696  -1016    512   -201       O
ATOM   3030  O  BARG A 207       7.499 -66.136 -35.920  0.52 27.61           O
ANISOU 3030  O  BARG A 207     2470   4287   3732  -1019    599   -173       O
ATOM   3031  CB AARG A 207       9.527 -66.306 -33.918  0.48 31.32           C
ANISOU 3031  CB AARG A 207     3318   4603   3980   -962    635    -50       C
ATOM   3032  CB BARG A 207       9.660 -66.730 -33.864  0.52 31.74           C
ANISOU 3032  CB BARG A 207     3406   4620   4035   -992    628    -33       C
ATOM   3033  CG AARG A 207       9.981 -67.386 -32.963  0.48 33.96           C
ANISOU 3033  CG AARG A 207     3818   4828   4258  -1044    671     35       C
ATOM   3034  CG BARG A 207       9.630 -68.147 -33.329  0.52 34.67           C
ANISOU 3034  CG BARG A 207     3874   4888   4412  -1122    666     35       C
ATOM   3035  CD AARG A 207       9.732 -66.960 -31.513  0.48 34.94           C
ANISOU 3035  CD AARG A 207     4018   4986   4272  -1047    803     89       C
ATOM   3036  CD BARG A 207       9.516 -68.181 -31.808  0.52 37.10           C
ANISOU 3036  CD BARG A 207     4295   5188   4615  -1158    793    114       C
ATOM   3037  NE AARG A 207       8.307 -66.906 -31.170  0.48 33.70           N
ANISOU 3037  NE AARG A 207     3729   4918   4157  -1127    951     84       N
ATOM   3038  NE BARG A 207      10.398 -69.186 -31.217  0.52 40.62           N
ANISOU 3038  NE BARG A 207     4931   5499   5005  -1199    760    193       N
ATOM   3039  CZ AARG A 207       7.583 -67.956 -30.802  0.48 32.51           C
ANISOU 3039  CZ AARG A 207     3570   4735   4046  -1269   1041    132       C
ATOM   3040  CZ BARG A 207      11.269 -68.947 -30.241  0.52 40.78           C
ANISOU 3040  CZ BARG A 207     5117   5478   4901  -1142    754    249       C
ATOM   3041  NH1AARG A 207       8.137 -69.163 -30.758  0.48 33.35           N
ANISOU 3041  NH1AARG A 207     3801   4716   4155  -1346    991    188       N
ATOM   3042  NH1BARG A 207      11.384 -67.735 -29.708  0.52 39.30           N
ANISOU 3042  NH1BARG A 207     4937   5369   4624  -1049    786    230       N
ATOM   3043  NH2AARG A 207       6.301 -67.806 -30.487  0.48 30.99           N
ANISOU 3043  NH2AARG A 207     3242   4633   3900  -1335   1183    124       N
ATOM   3044  NH2BARG A 207      12.021 -69.936 -29.784  0.52 41.68           N
ANISOU 3044  NH2BARG A 207     5393   5464   4978  -1180    711    324       N
ATOM   3045  H  AARG A 207      11.737 -65.896 -35.165  0.48  0.00           H
ATOM   3046  H  BARG A 207      11.691 -65.775 -35.195  0.52  0.00           H
ATOM   3047  HA AARG A 207       9.579 -67.693 -35.549  0.48  0.00           H
ATOM   3048  HA BARG A 207       9.572 -67.658 -35.776  0.52  0.00           H
ATOM   3049  HB2AARG A 207      10.080 -65.395 -33.687  0.48  0.00           H
ATOM   3050  HB2BARG A 207       8.750 -66.222 -33.545  0.52  0.00           H
ATOM   3051  HB3AARG A 207       8.466 -66.120 -33.752  0.48  0.00           H
ATOM   3052  HB3BARG A 207      10.519 -66.212 -33.438  0.52  0.00           H
ATOM   3053  HG2AARG A 207       9.427 -68.302 -33.168  0.48  0.00           H
ATOM   3054  HG2BARG A 207       8.773 -68.667 -33.758  0.52  0.00           H
ATOM   3055  HG3AARG A 207      11.046 -67.570 -33.107  0.48  0.00           H
ATOM   3056  HG3BARG A 207      10.544 -68.660 -33.629  0.52  0.00           H
ATOM   3057  HD2AARG A 207      10.163 -65.970 -31.363  0.48  0.00           H
ATOM   3058  HD2BARG A 207       8.486 -68.413 -31.537  0.52  0.00           H
ATOM   3059  HD3AARG A 207      10.229 -67.666 -30.848  0.48  0.00           H
ATOM   3060  HD3BARG A 207       9.776 -67.200 -31.410  0.52  0.00           H
ATOM   3061  HE AARG A 207       7.845 -66.009 -31.217  0.48  0.00           H
ATOM   3062  HE BARG A 207      10.342 -70.129 -31.575  0.52  0.00           H
ATOM   3063 HH11AARG A 207       9.110 -69.281 -31.001  0.48  0.00           H
ATOM   3064 HH11BARG A 207      10.809 -66.977 -30.048  0.52  0.00           H
ATOM   3065 HH12AARG A 207       7.585 -69.962 -30.482  0.48  0.00           H
ATOM   3066 HH12BARG A 207      12.046 -67.572 -28.963  0.52  0.00           H
ATOM   3067 HH21AARG A 207       5.876 -66.891 -30.523  0.48  0.00           H
ATOM   3068 HH21BARG A 207      11.935 -70.861 -30.180  0.52  0.00           H
ATOM   3069 HH22AARG A 207       5.752 -68.607 -30.211  0.48  0.00           H
ATOM   3070 HH22BARG A 207      12.681 -69.766 -29.039  0.52  0.00           H
ATOM   3071  N   ARG A 208       9.011 -64.571 -36.424  1.00 33.28           N
ANISOU 3071  N   ARG A 208     3276   5012   4356   -797    473   -210       N
ATOM   3072  CA  ARG A 208       8.002 -63.682 -37.011  1.00 40.82           C
ANISOU 3072  CA  ARG A 208     4052   6086   5373   -754    482   -265       C
ATOM   3073  C   ARG A 208       8.381 -63.071 -38.357  1.00 38.00           C
ANISOU 3073  C   ARG A 208     3646   5749   5041   -662    350   -322       C
ATOM   3074  O   ARG A 208       7.681 -62.208 -38.854  1.00 41.82           O
ANISOU 3074  O   ARG A 208     3999   6325   5566   -604    340   -362       O
ATOM   3075  CB  ARG A 208       7.596 -62.586 -36.010  1.00 48.31           C
ANISOU 3075  CB  ARG A 208     4979   7108   6270   -688    596   -257       C
ATOM   3076  CG  ARG A 208       6.766 -63.100 -34.815  1.00 55.81           C
ANISOU 3076  CG  ARG A 208     5920   8073   7211   -790    754   -213       C
ATOM   3077  CD  ARG A 208       6.679 -62.063 -33.682  1.00 60.13           C
ANISOU 3077  CD  ARG A 208     6507   8670   7671   -715    869   -203       C
ATOM   3078  NE  ARG A 208       6.021 -62.593 -32.484  1.00 65.29           N
ANISOU 3078  NE  ARG A 208     7185   9329   8292   -812   1031   -154       N
ATOM   3079  CZ  ARG A 208       6.626 -63.291 -31.518  1.00 69.14           C
ANISOU 3079  CZ  ARG A 208     7853   9736   8683   -870   1073    -86       C
ATOM   3080  NH1 ARG A 208       7.924 -63.564 -31.586  1.00 70.37           N
ANISOU 3080  NH1 ARG A 208     8169   9795   8772   -838    959    -61       N
ATOM   3081  NH2 ARG A 208       5.925 -63.723 -30.473  1.00 70.99           N
ANISOU 3081  NH2 ARG A 208     8103   9983   8885   -961   1231    -41       N
ATOM   3082  H  AARG A 208       9.917 -64.203 -36.170  0.48  0.00           H
ATOM   3083  H  BARG A 208       9.978 -64.282 -36.390  0.52  0.00           H
ATOM   3084  HA  ARG A 208       7.114 -64.290 -37.184  1.00  0.00           H
ATOM   3085  HB2 ARG A 208       7.005 -61.839 -36.541  1.00  0.00           H
ATOM   3086  HB3 ARG A 208       8.499 -62.110 -35.629  1.00  0.00           H
ATOM   3087  HG2 ARG A 208       5.758 -63.329 -35.160  1.00  0.00           H
ATOM   3088  HG3 ARG A 208       7.225 -64.010 -34.429  1.00  0.00           H
ATOM   3089  HD2 ARG A 208       7.689 -61.750 -33.416  1.00  0.00           H
ATOM   3090  HD3 ARG A 208       6.122 -61.196 -34.038  1.00  0.00           H
ATOM   3091  HE  ARG A 208       5.032 -62.417 -32.380  1.00  0.00           H
ATOM   3092 HH11 ARG A 208       8.467 -63.242 -32.375  1.00  0.00           H
ATOM   3093 HH12 ARG A 208       8.368 -64.093 -30.849  1.00  0.00           H
ATOM   3094 HH21 ARG A 208       6.381 -64.251 -29.743  1.00  0.00           H
ATOM   3095 HH22 ARG A 208       4.937 -63.523 -30.410  1.00  0.00           H
ATOM   3096  N   SER A 209       9.437 -63.569 -38.978  1.00 30.71           N
ANISOU 3096  N   SER A 209     2827   4741   4100   -651    251   -324       N
ATOM   3097  CA  SER A 209       9.846 -63.071 -40.289  1.00 30.45           C
ANISOU 3097  CA  SER A 209     2766   4723   4081   -571    135   -374       C
ATOM   3098  C   SER A 209      10.358 -64.211 -41.149  1.00 29.68           C
ANISOU 3098  C   SER A 209     2725   4542   4011   -631     50   -391       C
ATOM   3099  O   SER A 209      10.812 -65.219 -40.633  1.00 28.61           O
ANISOU 3099  O   SER A 209     2689   4314   3867   -700     69   -356       O
ATOM   3100  CB  SER A 209      10.954 -62.012 -40.166  1.00 32.53           C
ANISOU 3100  CB  SER A 209     3120   4972   4270   -443    107   -367       C
ATOM   3101  OG  SER A 209      12.277 -62.581 -40.045  1.00 34.94           O
ANISOU 3101  OG  SER A 209     3574   5170   4533   -439     66   -341       O
ATOM   3102  H   SER A 209       9.970 -64.306 -38.539  1.00  0.00           H
ATOM   3103  HA  SER A 209       8.983 -62.621 -40.779  1.00  0.00           H
ATOM   3104  HB2 SER A 209      10.756 -61.405 -39.282  1.00  0.00           H
ATOM   3105  HB3 SER A 209      10.926 -61.370 -41.047  1.00  0.00           H
ATOM   3106  HG  SER A 209      12.934 -61.890 -40.157  1.00  0.00           H
ATOM   3107  N   GLN A 210      10.312 -64.025 -42.461  1.00 31.55           N
ANISOU 3107  N   GLN A 210     2908   4807   4274   -598    -46   -446       N
ATOM   3108  CA  GLN A 210      10.865 -64.997 -43.380  1.00 34.59           C
ANISOU 3108  CA  GLN A 210     3356   5113   4674   -638   -127   -475       C
ATOM   3109  C   GLN A 210      11.209 -64.322 -44.710  1.00 35.21           C
ANISOU 3109  C   GLN A 210     3418   5226   4733   -549   -224   -526       C
ATOM   3110  O   GLN A 210      10.530 -63.384 -45.149  1.00 34.07           O
ANISOU 3110  O   GLN A 210     3169   5178   4597   -497   -246   -547       O
ATOM   3111  CB  GLN A 210       9.868 -66.110 -43.620  1.00 38.05           C
ANISOU 3111  CB  GLN A 210     3725   5545   5189   -774   -130   -497       C
ATOM   3112  CG  GLN A 210       8.695 -65.640 -44.433  1.00 41.18           C
ANISOU 3112  CG  GLN A 210     3957   6052   5637   -780   -175   -548       C
ATOM   3113  CD  GLN A 210       7.647 -66.684 -44.591  1.00 43.29           C
ANISOU 3113  CD  GLN A 210     4140   6317   5992   -921   -177   -569       C
ATOM   3114  OE1 GLN A 210       7.747 -67.770 -44.034  1.00 46.01           O
ANISOU 3114  OE1 GLN A 210     4547   6575   6358  -1024   -132   -544       O
ATOM   3115  NE2 GLN A 210       6.607 -66.353 -45.317  1.00 41.65           N
ANISOU 3115  NE2 GLN A 210     3841   6160   5825   -895   -227   -580       N
ATOM   3116  H   GLN A 210       9.882 -63.187 -42.827  1.00  0.00           H
ATOM   3117  HA  GLN A 210      11.773 -65.419 -42.949  1.00  0.00           H
ATOM   3118  HB2 GLN A 210       9.508 -66.475 -42.658  1.00  0.00           H
ATOM   3119  HB3 GLN A 210      10.364 -66.925 -44.147  1.00  0.00           H
ATOM   3120  HG2 GLN A 210       8.253 -64.775 -43.938  1.00  0.00           H
ATOM   3121  HG3 GLN A 210       9.047 -65.341 -45.420  1.00  0.00           H
ATOM   3122 HE21 GLN A 210       5.853 -67.012 -45.449  1.00  0.00           H
ATOM   3123 HE22 GLN A 210       6.560 -65.439 -45.745  1.00  0.00           H
ATOM   3124  N   GLN A 211      12.279 -64.809 -45.331  1.00 35.53           N
ANISOU 3124  N   GLN A 211     3567   5183   4749   -530   -278   -541       N
ATOM   3125  CA  GLN A 211      12.716 -64.346 -46.641  1.00 34.48           C
ANISOU 3125  CA  GLN A 211     3445   5068   4588   -457   -360   -588       C
ATOM   3126  C   GLN A 211      13.056 -65.574 -47.445  1.00 32.68           C
ANISOU 3126  C   GLN A 211     3282   4758   4376   -521   -412   -631       C
ATOM   3127  O   GLN A 211      13.873 -66.386 -46.999  1.00 31.66           O
ANISOU 3127  O   GLN A 211     3254   4524   4250   -544   -388   -610       O
ATOM   3128  CB  GLN A 211      13.971 -63.488 -46.515  1.00 35.17           C
ANISOU 3128  CB  GLN A 211     3615   5129   4618   -344   -353   -562       C
ATOM   3129  CG  GLN A 211      13.810 -62.237 -45.703  1.00 37.98           C
ANISOU 3129  CG  GLN A 211     3932   5547   4952   -273   -304   -524       C
ATOM   3130  CD  GLN A 211      15.165 -61.634 -45.289  1.00 40.49           C
ANISOU 3130  CD  GLN A 211     4349   5812   5225   -188   -290   -492       C
ATOM   3131  OE1 GLN A 211      15.764 -60.855 -46.036  1.00 40.30           O
ANISOU 3131  OE1 GLN A 211     4341   5798   5173   -107   -326   -505       O
ATOM   3132  NE2 GLN A 211      15.638 -61.995 -44.085  1.00 42.43           N
ANISOU 3132  NE2 GLN A 211     4660   6000   5462   -212   -240   -448       N
ATOM   3133  H   GLN A 211      12.813 -65.533 -44.873  1.00  0.00           H
ATOM   3134  HA  GLN A 211      11.920 -63.783 -47.128  1.00  0.00           H
ATOM   3135  HB2 GLN A 211      14.285 -63.201 -47.518  1.00  0.00           H
ATOM   3136  HB3 GLN A 211      14.759 -64.092 -46.066  1.00  0.00           H
ATOM   3137  HG2 GLN A 211      13.265 -61.502 -46.295  1.00  0.00           H
ATOM   3138  HG3 GLN A 211      13.235 -62.467 -44.806  1.00  0.00           H
ATOM   3139 HE21 GLN A 211      15.111 -62.633 -43.506  1.00  0.00           H
ATOM   3140 HE22 GLN A 211      16.521 -61.628 -43.759  1.00  0.00           H
ATOM   3141  N   THR A 212      12.436 -65.739 -48.616  1.00 32.56           N
ANISOU 3141  N   THR A 212     3216   4784   4371   -547   -488   -692       N
ATOM   3142  CA  THR A 212      12.826 -66.835 -49.534  1.00 33.85           C
ANISOU 3142  CA  THR A 212     3457   4867   4536   -596   -543   -749       C
ATOM   3143  C   THR A 212      13.282 -66.217 -50.838  1.00 33.24           C
ANISOU 3143  C   THR A 212     3433   4805   4391   -499   -597   -770       C
ATOM   3144  O   THR A 212      12.596 -65.346 -51.408  1.00 32.85           O
ANISOU 3144  O   THR A 212     3335   4830   4318   -449   -625   -753       O
ATOM   3145  CB  THR A 212      11.693 -67.825 -49.826  1.00 36.86           C
ANISOU 3145  CB  THR A 212     3795   5235   4975   -713   -571   -771       C
ATOM   3146  OG1 THR A 212      11.328 -68.506 -48.625  1.00 37.07           O
ANISOU 3146  OG1 THR A 212     3786   5232   5065   -817   -505   -746       O
ATOM   3147  CG2 THR A 212      12.133 -68.885 -50.857  1.00 38.76           C
ANISOU 3147  CG2 THR A 212     4136   5384   5205   -750   -629   -832       C
ATOM   3148  H   THR A 212      11.692 -65.109 -48.879  1.00  0.00           H
ATOM   3149  HA  THR A 212      13.661 -67.379 -49.094  1.00  0.00           H
ATOM   3150  HB  THR A 212      10.829 -67.283 -50.211  1.00  0.00           H
ATOM   3151  HG1 THR A 212      10.425 -68.824 -48.699  1.00  0.00           H
ATOM   3152 HG21 THR A 212      11.309 -69.574 -51.045  1.00  0.00           H
ATOM   3153 HG22 THR A 212      12.987 -69.438 -50.467  1.00  0.00           H
ATOM   3154 HG23 THR A 212      12.414 -68.392 -51.788  1.00  0.00           H
ATOM   3155  N   ILE A 213      14.460 -66.642 -51.281  1.00 33.55           N
ANISOU 3155  N   ILE A 213     3576   4770   4402   -473   -606   -805       N
ATOM   3156  CA  ILE A 213      15.062 -66.161 -52.496  1.00 33.77           C
ANISOU 3156  CA  ILE A 213     3668   4802   4359   -390   -639   -828       C
ATOM   3157  C   ILE A 213      15.291 -67.357 -53.423  1.00 34.54           C
ANISOU 3157  C   ILE A 213     3850   4822   4451   -443   -676   -897       C
ATOM   3158  O   ILE A 213      15.829 -68.397 -53.022  1.00 34.75           O
ANISOU 3158  O   ILE A 213     3931   4753   4521   -494   -658   -926       O
ATOM   3159  CB  ILE A 213      16.401 -65.462 -52.221  1.00 33.86           C
ANISOU 3159  CB  ILE A 213     3731   4795   4340   -292   -600   -809       C
ATOM   3160  CG1 ILE A 213      16.271 -64.430 -51.100  1.00 34.92           C
ANISOU 3160  CG1 ILE A 213     3803   4980   4485   -248   -554   -737       C
ATOM   3161  CG2 ILE A 213      16.931 -64.819 -53.479  1.00 34.32           C
ANISOU 3161  CG2 ILE A 213     3843   4873   4325   -211   -622   -827       C
ATOM   3162  CD1 ILE A 213      15.218 -63.408 -51.338  1.00 37.40           C
ANISOU 3162  CD1 ILE A 213     4037   5391   4783   -218   -569   -710       C
ATOM   3163  H   ILE A 213      14.956 -67.335 -50.740  1.00  0.00           H
ATOM   3164  HA  ILE A 213      14.383 -65.458 -52.979  1.00  0.00           H
ATOM   3165  HB  ILE A 213      17.117 -66.219 -51.901  1.00  0.00           H
ATOM   3166 HG12 ILE A 213      16.035 -64.957 -50.175  1.00  0.00           H
ATOM   3167 HG13 ILE A 213      17.228 -63.923 -50.979  1.00  0.00           H
ATOM   3168 HG21 ILE A 213      17.881 -64.328 -53.265  1.00  0.00           H
ATOM   3169 HG22 ILE A 213      17.081 -65.583 -54.242  1.00  0.00           H
ATOM   3170 HG23 ILE A 213      16.214 -64.081 -53.840  1.00  0.00           H
ATOM   3171 HD11 ILE A 213      15.483 -62.485 -50.822  1.00  0.00           H
ATOM   3172 HD12 ILE A 213      15.135 -63.215 -52.407  1.00  0.00           H
ATOM   3173 HD13 ILE A 213      14.264 -63.775 -50.960  1.00  0.00           H
ATOM   3174  N   ILE A 214      14.844 -67.216 -54.662  1.00 35.06           N
ANISOU 3174  N   ILE A 214     3934   4923   4464   -432   -730   -922       N
ATOM   3175  CA  ILE A 214      15.065 -68.243 -55.682  1.00 35.00           C
ANISOU 3175  CA  ILE A 214     4020   4847   4431   -472   -766   -993       C
ATOM   3176  C   ILE A 214      16.161 -67.710 -56.590  1.00 33.14           C
ANISOU 3176  C   ILE A 214     3872   4607   4112   -375   -754  -1015       C
ATOM   3177  O   ILE A 214      16.025 -66.621 -57.130  1.00 35.65           O
ANISOU 3177  O   ILE A 214     4172   5003   4372   -308   -768   -986       O
ATOM   3178  CB  ILE A 214      13.815 -68.484 -56.541  1.00 37.66           C
ANISOU 3178  CB  ILE A 214     4327   5226   4754   -534   -844  -1011       C
ATOM   3179  CG1 ILE A 214      12.615 -68.870 -55.668  1.00 40.04           C
ANISOU 3179  CG1 ILE A 214     4520   5546   5145   -629   -852   -983       C
ATOM   3180  CG2 ILE A 214      14.092 -69.596 -57.583  1.00 36.21           C
ANISOU 3180  CG2 ILE A 214     4258   4965   4536   -580   -880  -1090       C
ATOM   3181  CD1 ILE A 214      12.819 -70.151 -54.860  1.00 41.28           C
ANISOU 3181  CD1 ILE A 214     4704   5601   5378   -723   -818  -1003       C
ATOM   3182  H   ILE A 214      14.337 -66.378 -54.910  1.00  0.00           H
ATOM   3183  HA  ILE A 214      15.385 -69.174 -55.214  1.00  0.00           H
ATOM   3184  HB  ILE A 214      13.576 -67.563 -57.072  1.00  0.00           H
ATOM   3185 HG12 ILE A 214      12.421 -68.054 -54.972  1.00  0.00           H
ATOM   3186 HG13 ILE A 214      11.743 -68.997 -56.309  1.00  0.00           H
ATOM   3187 HG21 ILE A 214      14.946 -69.313 -58.199  1.00  0.00           H
ATOM   3188 HG22 ILE A 214      13.215 -69.726 -58.217  1.00  0.00           H
ATOM   3189 HG23 ILE A 214      14.310 -70.531 -57.067  1.00  0.00           H
ATOM   3190 HD11 ILE A 214      11.926 -70.355 -54.269  1.00  0.00           H
ATOM   3191 HD12 ILE A 214      13.674 -70.028 -54.195  1.00  0.00           H
ATOM   3192 HD13 ILE A 214      13.003 -70.983 -55.539  1.00  0.00           H
ATOM   3193  N   PRO A 215      17.258 -68.450 -56.743  1.00 31.00           N
ANISOU 3193  N   PRO A 215     3695   4241   3842   -363   -720  -1064       N
ATOM   3194  CA  PRO A 215      18.276 -67.904 -57.638  1.00 32.30           C
ANISOU 3194  CA  PRO A 215     3936   4407   3928   -270   -696  -1085       C
ATOM   3195  C   PRO A 215      17.767 -67.823 -59.076  1.00 34.99           C
ANISOU 3195  C   PRO A 215     4327   4790   4178   -274   -748  -1118       C
ATOM   3196  O   PRO A 215      16.890 -68.610 -59.483  1.00 34.58           O
ANISOU 3196  O   PRO A 215     4283   4726   4130   -358   -805  -1151       O
ATOM   3197  CB  PRO A 215      19.413 -68.928 -57.562  1.00 32.62           C
ANISOU 3197  CB  PRO A 215     4066   4323   4004   -266   -648  -1140       C
ATOM   3198  CG  PRO A 215      19.038 -69.930 -56.492  1.00 32.93           C
ANISOU 3198  CG  PRO A 215     4078   4289   4145   -354   -650  -1136       C
ATOM   3199  CD  PRO A 215      17.570 -69.806 -56.271  1.00 32.12           C
ANISOU 3199  CD  PRO A 215     3885   4264   4054   -432   -702  -1103       C
ATOM   3200  HA  PRO A 215      18.612 -66.927 -57.291  1.00  0.00           H
ATOM   3201  HB2 PRO A 215      20.347 -68.431 -57.298  1.00  0.00           H
ATOM   3202  HB3 PRO A 215      19.521 -69.434 -58.522  1.00  0.00           H
ATOM   3203  HG2 PRO A 215      19.282 -70.939 -56.823  1.00  0.00           H
ATOM   3204  HG3 PRO A 215      19.572 -69.704 -55.569  1.00  0.00           H
ATOM   3205  HD2 PRO A 215      17.326 -69.915 -55.214  1.00  0.00           H
ATOM   3206  HD3 PRO A 215      17.033 -70.547 -56.863  1.00  0.00           H
ATOM   3207  N   ASN A 216      18.360 -66.925 -59.851  1.00 36.76           N
ANISOU 3207  N   ASN A 216     4595   5055   4318   -190   -730  -1111       N
ATOM   3208  CA  ASN A 216      18.010 -66.739 -61.241  1.00 38.86           C
ANISOU 3208  CA  ASN A 216     4925   5360   4482   -186   -776  -1136       C
ATOM   3209  C   ASN A 216      19.257 -66.980 -62.123  1.00 33.02           C
ANISOU 3209  C   ASN A 216     4312   4564   3670   -133   -715  -1189       C
ATOM   3210  O   ASN A 216      20.255 -66.253 -62.030  1.00 32.40           O
ANISOU 3210  O   ASN A 216     4247   4490   3575    -51   -648  -1166       O
ATOM   3211  CB  ASN A 216      17.458 -65.328 -61.384  1.00 48.10           C
ANISOU 3211  CB  ASN A 216     6032   6633   5613   -133   -807  -1065       C
ATOM   3212  CG  ASN A 216      16.644 -65.126 -62.652  1.00 57.13           C
ANISOU 3212  CG  ASN A 216     7214   7827   6667   -150   -887  -1075       C
ATOM   3213  OD1 ASN A 216      17.136 -65.390 -63.750  1.00 67.73           O
ANISOU 3213  OD1 ASN A 216     8671   9148   7917   -141   -883  -1123       O
ATOM   3214  ND2 ASN A 216      15.395 -64.652 -62.513  1.00 52.33           N
ANISOU 3214  ND2 ASN A 216     6512   7285   6085   -175   -958  -1031       N
ATOM   3215  H   ASN A 216      19.087 -66.347 -59.453  1.00  0.00           H
ATOM   3216  HA  ASN A 216      17.235 -67.456 -61.514  1.00  0.00           H
ATOM   3217  HB2 ASN A 216      18.294 -64.629 -61.395  1.00  0.00           H
ATOM   3218  HB3 ASN A 216      16.827 -65.108 -60.523  1.00  0.00           H
ATOM   3219 HD21 ASN A 216      15.032 -64.447 -61.593  1.00  0.00           H
ATOM   3220 HD22 ASN A 216      14.819 -64.500 -63.328  1.00  0.00           H
ATOM   3221  N   ILE A 217      19.231 -68.025 -62.949  1.00 31.21           N
ANISOU 3221  N   ILE A 217     4178   4278   3403   -182   -729  -1262       N
ATOM   3222  CA  ILE A 217      20.415 -68.382 -63.752  1.00 31.93           C
ANISOU 3222  CA  ILE A 217     4394   4305   3435   -135   -652  -1317       C
ATOM   3223  C   ILE A 217      20.505 -67.502 -64.990  1.00 32.28           C
ANISOU 3223  C   ILE A 217     4506   4417   3344    -88   -654  -1308       C
ATOM   3224  O   ILE A 217      19.491 -67.227 -65.638  1.00 35.68           O
ANISOU 3224  O   ILE A 217     4936   4913   3710   -125   -741  -1299       O
ATOM   3225  CB  ILE A 217      20.394 -69.858 -64.160  1.00 34.78           C
ANISOU 3225  CB  ILE A 217     4842   4567   3805   -203   -656  -1401       C
ATOM   3226  CG1 ILE A 217      20.432 -70.744 -62.911  1.00 35.44           C
ANISOU 3226  CG1 ILE A 217     4872   4566   4026   -246   -645  -1403       C
ATOM   3227  CG2 ILE A 217      21.589 -70.201 -65.119  1.00 36.60           C
ANISOU 3227  CG2 ILE A 217     5208   4733   3966   -149   -563  -1461       C
ATOM   3228  CD1 ILE A 217      19.836 -72.158 -63.141  1.00 40.50           C
ANISOU 3228  CD1 ILE A 217     5569   5125   4693   -348   -689  -1467       C
ATOM   3229  H   ILE A 217      18.390 -68.579 -63.026  1.00  0.00           H
ATOM   3230  HA  ILE A 217      21.304 -68.209 -63.145  1.00  0.00           H
ATOM   3231  HB  ILE A 217      19.462 -70.054 -64.690  1.00  0.00           H
ATOM   3232 HG12 ILE A 217      21.470 -70.853 -62.597  1.00  0.00           H
ATOM   3233 HG13 ILE A 217      19.873 -70.253 -62.114  1.00  0.00           H
ATOM   3234 HG21 ILE A 217      21.544 -69.561 -66.000  1.00  0.00           H
ATOM   3235 HG22 ILE A 217      22.532 -70.035 -64.598  1.00  0.00           H
ATOM   3236 HG23 ILE A 217      21.521 -71.245 -65.425  1.00  0.00           H
ATOM   3237 HD11 ILE A 217      19.895 -72.732 -62.216  1.00  0.00           H
ATOM   3238 HD12 ILE A 217      20.401 -72.668 -63.921  1.00  0.00           H
ATOM   3239 HD13 ILE A 217      18.794 -72.068 -63.447  1.00  0.00           H
ATOM   3240  N   GLY A 218      21.706 -67.036 -65.312  1.00 29.32           N
ANISOU 3240  N   GLY A 218     4185   4026   2928     -7   -556  -1306       N
ATOM   3241  CA  GLY A 218      21.927 -66.320 -66.568  1.00 28.28           C
ANISOU 3241  CA  GLY A 218     4143   3944   2659     32   -538  -1301       C
ATOM   3242  C   GLY A 218      23.117 -65.394 -66.459  1.00 27.57           C
ANISOU 3242  C   GLY A 218     4054   3860   2562    125   -432  -1258       C
ATOM   3243  O   GLY A 218      23.594 -65.153 -65.345  1.00 27.15           O
ANISOU 3243  O   GLY A 218     3914   3790   2611    159   -395  -1225       O
ATOM   3244  H   GLY A 218      22.480 -67.178 -64.679  1.00  0.00           H
ATOM   3245  HA2 GLY A 218      21.039 -65.734 -66.805  1.00  0.00           H
ATOM   3246  HA3 GLY A 218      22.105 -67.041 -67.366  1.00  0.00           H
ATOM   3247  N   SER A 219      23.614 -64.858 -67.578  1.00 27.67           N
ANISOU 3247  N   SER A 219     4161   3895   2456    162   -378  -1256       N
ATOM   3248  CA  SER A 219      24.772 -63.937 -67.507  1.00 28.57           C
ANISOU 3248  CA  SER A 219     4275   4013   2569    245   -266  -1209       C
ATOM   3249  C   SER A 219      24.455 -62.513 -67.117  1.00 28.06           C
ANISOU 3249  C   SER A 219     4136   4029   2497    287   -303  -1117       C
ATOM   3250  O   SER A 219      23.448 -61.942 -67.554  1.00 30.67           O
ANISOU 3250  O   SER A 219     4465   4429   2759    269   -399  -1083       O
ATOM   3251  CB  SER A 219      25.464 -63.809 -68.851  1.00 33.34           C
ANISOU 3251  CB  SER A 219     5008   4613   3048    266   -176  -1233       C
ATOM   3252  OG  SER A 219      25.959 -65.025 -69.323  1.00 36.27           O
ANISOU 3252  OG  SER A 219     5458   4904   3418    240   -112  -1320       O
ATOM   3253  H   SER A 219      23.200 -65.081 -68.472  1.00  0.00           H
ATOM   3254  HA  SER A 219      25.487 -64.339 -66.789  1.00  0.00           H
ATOM   3255  HB2 SER A 219      26.295 -63.111 -68.749  1.00  0.00           H
ATOM   3256  HB3 SER A 219      24.755 -63.411 -69.577  1.00  0.00           H
ATOM   3257  HG  SER A 219      26.909 -64.958 -69.447  1.00  0.00           H
ATOM   3258  N   ARG A 220      25.346 -61.961 -66.300  1.00 25.94           N
ANISOU 3258  N   ARG A 220     3805   3744   2306    343   -226  -1078       N
ATOM   3259  CA  ARG A 220      25.445 -60.555 -66.041  1.00 26.01           C
ANISOU 3259  CA  ARG A 220     3769   3810   2302    396   -220   -995       C
ATOM   3260  C   ARG A 220      26.769 -60.100 -66.657  1.00 27.87           C
ANISOU 3260  C   ARG A 220     4071   4018   2499    450    -79   -980       C
ATOM   3261  O   ARG A 220      27.541 -60.923 -67.142  1.00 27.47           O
ANISOU 3261  O   ARG A 220     4083   3906   2449    445     10  -1036       O
ATOM   3262  CB  ARG A 220      25.431 -60.298 -64.544  1.00 25.23           C
ANISOU 3262  CB  ARG A 220     3544   3710   2331    409   -240   -963       C
ATOM   3263  CG  ARG A 220      24.086 -60.576 -63.854  1.00 24.07           C
ANISOU 3263  CG  ARG A 220     3315   3598   2231    353   -364   -960       C
ATOM   3264  CD  ARG A 220      23.800 -62.058 -63.627  1.00 22.85           C
ANISOU 3264  CD  ARG A 220     3164   3385   2132    286   -389  -1032       C
ATOM   3265  NE  ARG A 220      22.672 -62.184 -62.721  1.00 24.56           N
ANISOU 3265  NE  ARG A 220     3281   3631   2419    236   -480  -1012       N
ATOM   3266  CZ  ARG A 220      21.919 -63.269 -62.549  1.00 27.11           C
ANISOU 3266  CZ  ARG A 220     3592   3928   2783    159   -535  -1054       C
ATOM   3267  NH1 ARG A 220      22.194 -64.392 -63.178  1.00 27.80           N
ANISOU 3267  NH1 ARG A 220     3763   3949   2849    125   -516  -1126       N
ATOM   3268  NH2 ARG A 220      20.895 -63.235 -61.698  1.00 27.40           N
ANISOU 3268  NH2 ARG A 220     3529   3997   2886    116   -599  -1022       N
ATOM   3269  H   ARG A 220      25.997 -62.574 -65.830  1.00  0.00           H
ATOM   3270  HA  ARG A 220      24.615 -60.031 -66.515  1.00  0.00           H
ATOM   3271  HB2 ARG A 220      26.186 -60.935 -64.084  1.00  0.00           H
ATOM   3272  HB3 ARG A 220      25.702 -59.257 -64.368  1.00  0.00           H
ATOM   3273  HG2 ARG A 220      24.087 -60.075 -62.886  1.00  0.00           H
ATOM   3274  HG3 ARG A 220      23.287 -60.155 -64.464  1.00  0.00           H
ATOM   3275  HD2 ARG A 220      23.561 -62.535 -64.578  1.00  0.00           H
ATOM   3276  HD3 ARG A 220      24.676 -62.536 -63.189  1.00  0.00           H
ATOM   3277  HE  ARG A 220      22.436 -61.372 -62.169  1.00  0.00           H
ATOM   3278 HH11 ARG A 220      21.622 -65.210 -63.024  1.00  0.00           H
ATOM   3279 HH12 ARG A 220      22.977 -64.436 -63.814  1.00  0.00           H
ATOM   3280 HH21 ARG A 220      20.331 -64.060 -61.553  1.00  0.00           H
ATOM   3281 HH22 ARG A 220      20.683 -62.384 -61.197  1.00  0.00           H
ATOM   3282  N   PRO A 221      27.038 -58.793 -66.651  1.00 31.15           N
ANISOU 3282  N   PRO A 221     4474   4474   2887    499    -50   -904       N
ATOM   3283  CA  PRO A 221      28.327 -58.403 -67.231  1.00 32.19           C
ANISOU 3283  CA  PRO A 221     4662   4573   2996    538     98   -886       C
ATOM   3284  C   PRO A 221      29.531 -59.025 -66.514  1.00 28.85           C
ANISOU 3284  C   PRO A 221     4179   4070   2714    555    207   -914       C
ATOM   3285  O   PRO A 221      29.604 -59.123 -65.286  1.00 26.69           O
ANISOU 3285  O   PRO A 221     3799   3774   2569    559    179   -901       O
ATOM   3286  CB  PRO A 221      28.339 -56.885 -67.071  1.00 32.96           C
ANISOU 3286  CB  PRO A 221     4736   4719   3069    584     99   -791       C
ATOM   3287  CG  PRO A 221      26.886 -56.506 -66.981  1.00 32.97           C
ANISOU 3287  CG  PRO A 221     4717   4788   3023    566    -58   -767       C
ATOM   3288  CD  PRO A 221      26.225 -57.635 -66.257  1.00 31.63           C
ANISOU 3288  CD  PRO A 221     4481   4604   2934    518   -139   -830       C
ATOM   3289  HA  PRO A 221      28.351 -58.664 -68.289  1.00  0.00           H
ATOM   3290  HB2 PRO A 221      28.869 -56.597 -66.163  1.00  0.00           H
ATOM   3291  HB3 PRO A 221      28.798 -56.417 -67.942  1.00  0.00           H
ATOM   3292  HG2 PRO A 221      26.768 -55.576 -66.425  1.00  0.00           H
ATOM   3293  HG3 PRO A 221      26.463 -56.402 -67.980  1.00  0.00           H
ATOM   3294  HD2 PRO A 221      26.257 -57.482 -65.178  1.00  0.00           H
ATOM   3295  HD3 PRO A 221      25.196 -57.757 -66.596  1.00  0.00           H
ATOM   3296  N   TRP A 222      30.487 -59.427 -67.329  1.00 27.88           N
ANISOU 3296  N   TRP A 222     4121   3901   2571    560    331   -944       N
ATOM   3297  CA  TRP A 222      31.739 -59.993 -66.871  1.00 29.30           C
ANISOU 3297  CA  TRP A 222     4246   3999   2887    580    447   -965       C
ATOM   3298  C   TRP A 222      32.417 -59.041 -65.884  1.00 27.99           C
ANISOU 3298  C   TRP A 222     3969   3829   2839    618    482   -889       C
ATOM   3299  O   TRP A 222      32.679 -57.881 -66.218  1.00 29.07           O
ANISOU 3299  O   TRP A 222     4117   4001   2928    640    529   -824       O
ATOM   3300  CB  TRP A 222      32.583 -60.180 -68.127  1.00 35.30           C
ANISOU 3300  CB  TRP A 222     5093   4739   3582    579    584   -997       C
ATOM   3301  CG  TRP A 222      33.852 -60.940 -68.021  1.00 42.20           C
ANISOU 3301  CG  TRP A 222     5919   5533   4582    594    710  -1040       C
ATOM   3302  CD1 TRP A 222      34.050 -62.257 -68.344  1.00 44.89           C
ANISOU 3302  CD1 TRP A 222     6292   5819   4947    577    738  -1133       C
ATOM   3303  CD2 TRP A 222      35.133 -60.420 -67.638  1.00 46.37           C
ANISOU 3303  CD2 TRP A 222     6344   6037   5236    628    817   -999       C
ATOM   3304  NE1 TRP A 222      35.371 -62.591 -68.169  1.00 46.75           N
ANISOU 3304  NE1 TRP A 222     6431   6018   5315    621    836  -1158       N
ATOM   3305  CE2 TRP A 222      36.060 -61.486 -67.737  1.00 47.89           C
ANISOU 3305  CE2 TRP A 222     6491   6184   5523    654    877  -1071       C
ATOM   3306  CE3 TRP A 222      35.584 -59.163 -67.208  1.00 48.24           C
ANISOU 3306  CE3 TRP A 222     6514   6297   5520    650    846   -907       C
ATOM   3307  CZ2 TRP A 222      37.416 -61.333 -67.423  1.00 50.38           C
ANISOU 3307  CZ2 TRP A 222     6706   6475   5960    714    950  -1030       C
ATOM   3308  CZ3 TRP A 222      36.925 -59.011 -66.881  1.00 50.33           C
ANISOU 3308  CZ3 TRP A 222     6669   6529   5923    679    934   -884       C
ATOM   3309  CH2 TRP A 222      37.831 -60.092 -67.001  1.00 51.64           C
ANISOU 3309  CH2 TRP A 222     6799   6654   6170    713    979   -939       C
ATOM   3310  H   TRP A 222      30.338 -59.335 -68.324  1.00  0.00           H
ATOM   3311  HA  TRP A 222      31.560 -60.957 -66.395  1.00  0.00           H
ATOM   3312  HB2 TRP A 222      32.834 -59.186 -68.497  1.00  0.00           H
ATOM   3313  HB3 TRP A 222      31.962 -60.669 -68.877  1.00  0.00           H
ATOM   3314  HD1 TRP A 222      33.280 -62.933 -68.686  1.00  0.00           H
ATOM   3315  HE3 TRP A 222      34.901 -58.330 -67.133  1.00  0.00           H
ATOM   3316  HZ2 TRP A 222      38.109 -62.157 -67.509  1.00  0.00           H
ATOM   3317  HZ3 TRP A 222      37.282 -58.054 -66.530  1.00  0.00           H
ATOM   3318  HH2 TRP A 222      38.871 -59.939 -66.756  1.00  0.00           H
ATOM   3319  HE1 TRP A 222      35.771 -63.504 -68.332  1.00  0.00           H
ATOM   3320  N   VAL A 223      32.646 -59.498 -64.653  1.00 27.97           N
ANISOU 3320  N   VAL A 223     3861   3781   2985    621    451   -891       N
ATOM   3321  CA  VAL A 223      33.395 -58.711 -63.651  1.00 31.11           C
ANISOU 3321  CA  VAL A 223     4145   4158   3518    640    477   -817       C
ATOM   3322  C   VAL A 223      34.435 -59.618 -63.002  1.00 34.00           C
ANISOU 3322  C   VAL A 223     4439   4435   4044    651    531   -841       C
ATOM   3323  O   VAL A 223      34.092 -60.675 -62.496  1.00 32.86           O
ANISOU 3323  O   VAL A 223     4287   4253   3947    634    469   -884       O
ATOM   3324  CB  VAL A 223      32.480 -58.155 -62.559  1.00 30.98           C
ANISOU 3324  CB  VAL A 223     4060   4175   3536    616    348   -760       C
ATOM   3325  CG1 VAL A 223      33.313 -57.541 -61.422  1.00 31.63           C
ANISOU 3325  CG1 VAL A 223     4031   4220   3766    628    366   -696       C
ATOM   3326  CG2 VAL A 223      31.539 -57.131 -63.134  1.00 30.27           C
ANISOU 3326  CG2 VAL A 223     4023   4163   3314    612    295   -718       C
ATOM   3327  H   VAL A 223      32.297 -60.410 -64.397  1.00  0.00           H
ATOM   3328  HA  VAL A 223      33.901 -57.885 -64.150  1.00  0.00           H
ATOM   3329  HB  VAL A 223      31.890 -58.976 -62.151  1.00  0.00           H
ATOM   3330 HG11 VAL A 223      33.988 -58.295 -61.017  1.00  0.00           H
ATOM   3331 HG12 VAL A 223      33.894 -56.704 -61.809  1.00  0.00           H
ATOM   3332 HG13 VAL A 223      32.648 -57.188 -60.634  1.00  0.00           H
ATOM   3333 HG21 VAL A 223      30.895 -56.745 -62.344  1.00  0.00           H
ATOM   3334 HG22 VAL A 223      30.927 -57.594 -63.908  1.00  0.00           H
ATOM   3335 HG23 VAL A 223      32.114 -56.312 -63.567  1.00  0.00           H
ATOM   3336  N   ARG A 224      35.705 -59.226 -63.060  1.00 36.04           N
ANISOU 3336  N   ARG A 224     4650   4654   4391    673    643   -804       N
ATOM   3337  CA  ARG A 224      36.794 -60.055 -62.549  1.00 36.37           C
ANISOU 3337  CA  ARG A 224     4631   4609   4578    694    688   -800       C
ATOM   3338  C   ARG A 224      36.632 -61.502 -62.965  1.00 36.46           C
ANISOU 3338  C   ARG A 224     4712   4574   4566    695    688   -876       C
ATOM   3339  O   ARG A 224      36.723 -62.424 -62.148  1.00 37.62           O
ANISOU 3339  O   ARG A 224     4817   4665   4810    693    631   -886       O
ATOM   3340  CB  ARG A 224      36.885 -59.919 -61.031  1.00 37.06           C
ANISOU 3340  CB  ARG A 224     4606   4674   4799    683    593   -747       C
ATOM   3341  CG  ARG A 224      37.294 -58.519 -60.588  1.00 37.34           C
ANISOU 3341  CG  ARG A 224     4572   4738   4878    685    601   -669       C
ATOM   3342  CD  ARG A 224      37.510 -58.408 -59.072  1.00 35.64           C
ANISOU 3342  CD  ARG A 224     4261   4494   4787    670    506   -613       C
ATOM   3343  NE  ARG A 224      36.256 -58.297 -58.326  1.00 31.95           N
ANISOU 3343  NE  ARG A 224     3796   4061   4280    644    389   -618       N
ATOM   3344  CZ  ARG A 224      35.428 -57.271 -58.385  1.00 30.17           C
ANISOU 3344  CZ  ARG A 224     3585   3903   3974    642    351   -601       C
ATOM   3345  NH1 ARG A 224      35.721 -56.243 -59.145  1.00 32.97           N
ANISOU 3345  NH1 ARG A 224     3959   4288   4281    655    422   -574       N
ATOM   3346  NH2 ARG A 224      34.301 -57.255 -57.686  1.00 28.01           N
ANISOU 3346  NH2 ARG A 224     3315   3664   3664    619    244   -594       N
ATOM   3347  H   ARG A 224      35.923 -58.329 -63.469  1.00  0.00           H
ATOM   3348  HA  ARG A 224      37.726 -59.685 -62.976  1.00  0.00           H
ATOM   3349  HB2 ARG A 224      35.910 -60.149 -60.602  1.00  0.00           H
ATOM   3350  HB3 ARG A 224      37.615 -60.636 -60.655  1.00  0.00           H
ATOM   3351  HG2 ARG A 224      38.224 -58.253 -61.091  1.00  0.00           H
ATOM   3352  HG3 ARG A 224      36.518 -57.814 -60.886  1.00  0.00           H
ATOM   3353  HD2 ARG A 224      38.041 -59.297 -58.730  1.00  0.00           H
ATOM   3354  HD3 ARG A 224      38.122 -57.530 -58.866  1.00  0.00           H
ATOM   3355  HE  ARG A 224      36.005 -59.064 -57.719  1.00  0.00           H
ATOM   3356 HH11 ARG A 224      36.576 -56.240 -59.682  1.00  0.00           H
ATOM   3357 HH12 ARG A 224      35.091 -55.455 -59.193  1.00  0.00           H
ATOM   3358 HH21 ARG A 224      33.682 -56.459 -57.744  1.00  0.00           H
ATOM   3359 HH22 ARG A 224      34.062 -58.039 -57.095  1.00  0.00           H
ATOM   3360  N   GLY A 225      36.400 -61.693 -64.262  1.00 37.35           N
ANISOU 3360  N   GLY A 225     4941   4705   4543    695    752   -928       N
ATOM   3361  CA  GLY A 225      36.341 -63.009 -64.848  1.00 37.92           C
ANISOU 3361  CA  GLY A 225     5100   4732   4577    705    763  -1004       C
ATOM   3362  C   GLY A 225      35.023 -63.738 -64.762  1.00 35.94           C
ANISOU 3362  C   GLY A 225     4902   4486   4269    641    652  -1068       C
ATOM   3363  O   GLY A 225      34.929 -64.834 -65.293  1.00 38.96           O
ANISOU 3363  O   GLY A 225     5365   4818   4618    637    664  -1135       O
ATOM   3364  H   GLY A 225      36.260 -60.888 -64.856  1.00  0.00           H
ATOM   3365  HA2 GLY A 225      37.090 -63.624 -64.350  1.00  0.00           H
ATOM   3366  HA3 GLY A 225      36.615 -62.925 -65.900  1.00  0.00           H
ATOM   3367  N   LEU A 226      34.015 -63.148 -64.115  1.00 29.26           N
ANISOU 3367  N   LEU A 226     4015   3705   3399    610    533  -1043       N
ATOM   3368  CA  LEU A 226      32.788 -63.873 -63.770  1.00 28.02           C
ANISOU 3368  CA  LEU A 226     3879   3557   3209    564    404  -1089       C
ATOM   3369  C   LEU A 226      31.522 -63.192 -64.278  1.00 26.22           C
ANISOU 3369  C   LEU A 226     3701   3430   2831    532    314  -1087       C
ATOM   3370  O   LEU A 226      31.355 -61.961 -64.160  1.00 26.42           O
ANISOU 3370  O   LEU A 226     3694   3525   2821    550    299  -1025       O
ATOM   3371  CB  LEU A 226      32.637 -63.993 -62.242  1.00 28.68           C
ANISOU 3371  CB  LEU A 226     3854   3617   3426    558    322  -1054       C
ATOM   3372  CG  LEU A 226      33.686 -64.858 -61.539  1.00 33.02           C
ANISOU 3372  CG  LEU A 226     4352   4062   4132    583    365  -1047       C
ATOM   3373  CD1 LEU A 226      33.450 -64.901 -60.062  1.00 33.63           C
ANISOU 3373  CD1 LEU A 226     4339   4121   4317    570    275  -1006       C
ATOM   3374  CD2 LEU A 226      33.662 -66.251 -62.110  1.00 36.52           C
ANISOU 3374  CD2 LEU A 226     4879   4432   4563    571    384  -1124       C
ATOM   3375  H   LEU A 226      34.100 -62.175 -63.856  1.00  0.00           H
ATOM   3376  HA  LEU A 226      32.842 -64.875 -64.196  1.00  0.00           H
ATOM   3377  HB2 LEU A 226      31.656 -64.421 -62.035  1.00  0.00           H
ATOM   3378  HB3 LEU A 226      32.673 -62.992 -61.813  1.00  0.00           H
ATOM   3379  HG  LEU A 226      34.670 -64.426 -61.720  1.00  0.00           H
ATOM   3380 HD11 LEU A 226      33.470 -63.888 -59.661  1.00  0.00           H
ATOM   3381 HD12 LEU A 226      34.231 -65.495 -59.587  1.00  0.00           H
ATOM   3382 HD13 LEU A 226      32.478 -65.352 -59.862  1.00  0.00           H
ATOM   3383 HD21 LEU A 226      33.835 -66.206 -63.185  1.00  0.00           H
ATOM   3384 HD22 LEU A 226      34.443 -66.849 -61.641  1.00  0.00           H
ATOM   3385 HD23 LEU A 226      32.691 -66.706 -61.917  1.00  0.00           H
ATOM   3386  N  ASER A 227      30.621 -63.999 -64.824  0.54 25.60           N
ANISOU 3386  N  ASER A 227     3700   3354   2672    485    248  -1150       N
ATOM   3387  N  BSER A 227      30.605 -63.991 -64.808  0.46 25.57           N
ANISOU 3387  N  BSER A 227     3695   3351   2668    485    246  -1149       N
ATOM   3388  CA ASER A 227      29.347 -63.494 -65.306  0.54 25.25           C
ANISOU 3388  CA ASER A 227     3695   3399   2498    448    143  -1144       C
ATOM   3389  CA BSER A 227      29.311 -63.466 -65.221  0.46 25.04           C
ANISOU 3389  CA BSER A 227     3661   3375   2477    448    137  -1141       C
ATOM   3390  C  ASER A 227      28.216 -63.885 -64.358  0.54 24.29           C
ANISOU 3390  C  ASER A 227     3509   3293   2426    399      9  -1151       C
ATOM   3391  C  BSER A 227      28.244 -63.749 -64.162  0.46 23.99           C
ANISOU 3391  C  BSER A 227     3453   3260   2403    404      7  -1140       C
ATOM   3392  O  ASER A 227      27.047 -63.596 -64.622  0.54 24.37           O
ANISOU 3392  O  ASER A 227     3528   3374   2358    360    -92  -1143       O
ATOM   3393  O  BSER A 227      27.169 -63.151 -64.178  0.46 23.92           O
ANISOU 3393  O  BSER A 227     3427   3331   2331    379    -90  -1113       O
ATOM   3394  CB ASER A 227      29.091 -64.005 -66.723  0.54 26.98           C
ANISOU 3394  CB ASER A 227     4047   3620   2584    418    158  -1203       C
ATOM   3395  CB BSER A 227      28.914 -64.035 -66.583  0.46 27.12           C
ANISOU 3395  CB BSER A 227     4054   3642   2609    412    136  -1202       C
ATOM   3396  OG ASER A 227      29.857 -63.268 -67.661  0.54 26.39           O
ANISOU 3396  OG ASER A 227     4032   3566   2431    453    268  -1180       O
ATOM   3397  OG BSER A 227      28.892 -65.447 -66.572  0.46 28.21           O
ANISOU 3397  OG BSER A 227     4228   3698   2792    377    132  -1279       O
ATOM   3398  H  ASER A 227      30.825 -64.985 -64.906  0.54  0.00           H
ATOM   3399  H  BSER A 227      30.806 -64.974 -64.926  0.46  0.00           H
ATOM   3400  HA ASER A 227      29.402 -62.406 -65.341  0.54  0.00           H
ATOM   3401  HA BSER A 227      29.404 -62.385 -65.323  0.46  0.00           H
ATOM   3402  HB2ASER A 227      28.032 -63.895 -66.958  0.54  0.00           H
ATOM   3403  HB2BSER A 227      29.633 -63.699 -67.330  0.46  0.00           H
ATOM   3404  HB3ASER A 227      29.366 -65.058 -66.782  0.54  0.00           H
ATOM   3405  HB3BSER A 227      27.924 -63.665 -66.849  0.46  0.00           H
ATOM   3406  HG ASER A 227      29.270 -62.752 -68.219  0.54  0.00           H
ATOM   3407  HG BSER A 227      29.542 -65.773 -65.945  0.46  0.00           H
ATOM   3408  N  ASER A 228      28.584 -64.534 -63.251  0.54 24.08           N
ANISOU 3408  N  ASER A 228     3413   3198   2536    399     13  -1158       N
ATOM   3409  N  BSER A 228      28.554 -64.647 -63.228  0.46 24.12           N
ANISOU 3409  N  BSER A 228     3420   3198   2546    395      9  -1163       N
ATOM   3410  CA ASER A 228      27.652 -64.891 -62.184  0.54 23.74           C
ANISOU 3410  CA ASER A 228     3301   3158   2561    346    -91  -1146       C
ATOM   3411  CA BSER A 228      27.646 -64.953 -62.130  0.46 24.02           C
ANISOU 3411  CA BSER A 228     3335   3189   2603    344    -93  -1147       C
ATOM   3412  C  ASER A 228      27.681 -63.822 -61.083  0.54 21.29           C
ANISOU 3412  C  ASER A 228     2885   2885   2319    363   -106  -1042       C
ATOM   3413  C  BSER A 228      27.689 -63.850 -61.073  0.46 21.31           C
ANISOU 3413  C  BSER A 228     2888   2886   2323    363   -105  -1043       C
ATOM   3414  O  ASER A 228      28.533 -62.937 -61.107  0.54 20.71           O
ANISOU 3414  O  ASER A 228     2791   2820   2256    417    -37   -992       O
ATOM   3415  O  BSER A 228      28.541 -62.965 -61.124  0.46 20.72           O
ANISOU 3415  O  BSER A 228     2795   2821   2257    417    -36   -994       O
ATOM   3416  CB ASER A 228      28.059 -66.229 -61.589  0.54 24.90           C
ANISOU 3416  CB ASER A 228     3448   3193   2820    327    -75  -1190       C
ATOM   3417  CB BSER A 228      28.020 -66.284 -61.490  0.46 25.35           C
ANISOU 3417  CB BSER A 228     3499   3246   2885    323    -81  -1188       C
ATOM   3418  OG ASER A 228      29.414 -66.176 -61.173  0.54 26.62           O
ANISOU 3418  OG ASER A 228     3632   3346   3136    390     19  -1160       O
ATOM   3419  OG BSER A 228      28.114 -67.299 -62.467  0.46 26.18           O
ANISOU 3419  OG BSER A 228     3705   3297   2945    306    -53  -1268       O
ATOM   3420  H  ASER A 228      29.555 -64.791 -63.146  0.54  0.00           H
ATOM   3421  H  BSER A 228      29.441 -65.128 -63.282  0.46  0.00           H
ATOM   3422  HA ASER A 228      26.644 -64.966 -62.592  0.54  0.00           H
ATOM   3423  HA BSER A 228      26.632 -65.024 -62.522  0.46  0.00           H
ATOM   3424  HB2ASER A 228      27.425 -66.451 -60.731  0.54  0.00           H
ATOM   3425  HB2BSER A 228      27.256 -66.558 -60.762  0.46  0.00           H
ATOM   3426  HB3ASER A 228      27.940 -67.011 -62.339  0.54  0.00           H
ATOM   3427  HB3BSER A 228      28.980 -66.182 -60.983  0.46  0.00           H
ATOM   3428  HG ASER A 228      29.726 -65.269 -61.215  0.54  0.00           H
ATOM   3429  HG BSER A 228      27.396 -67.925 -62.348  0.46  0.00           H
ATOM   3430  N   ARG A 229      26.765 -63.927 -60.117  1.00 21.46           N
ANISOU 3430  N   ARG A 229     2842   2925   2388    315   -189  -1012       N
ATOM   3431  CA  ARG A 229      26.630 -62.935 -59.055  1.00 21.12           C
ANISOU 3431  CA  ARG A 229     2709   2921   2394    327   -209   -924       C
ATOM   3432  C   ARG A 229      26.185 -63.577 -57.769  1.00 21.11           C
ANISOU 3432  C   ARG A 229     2652   2884   2486    279   -255   -904       C
ATOM   3433  O   ARG A 229      25.574 -64.654 -57.772  1.00 23.92           O
ANISOU 3433  O   ARG A 229     3029   3209   2851    221   -294   -954       O
ATOM   3434  CB  ARG A 229      25.541 -61.894 -59.412  1.00 20.43           C
ANISOU 3434  CB  ARG A 229     2604   2941   2218    322   -274   -895       C
ATOM   3435  CG  ARG A 229      25.866 -60.959 -60.579  1.00 20.66           C
ANISOU 3435  CG  ARG A 229     2691   3017   2143    372   -239   -886       C
ATOM   3436  CD  ARG A 229      27.033 -60.080 -60.258  1.00 20.89           C
ANISOU 3436  CD  ARG A 229     2695   3022   2220    429   -155   -825       C
ATOM   3437  NE  ARG A 229      27.281 -59.059 -61.273  1.00 22.91           N
ANISOU 3437  NE  ARG A 229     3003   3322   2379    471   -117   -801       N
ATOM   3438  CZ  ARG A 229      28.034 -59.217 -62.361  1.00 25.07           C
ANISOU 3438  CZ  ARG A 229     3360   3577   2589    495    -37   -835       C
ATOM   3439  NH1 ARG A 229      28.670 -60.375 -62.627  1.00 22.89           N
ANISOU 3439  NH1 ARG A 229     3123   3235   2340    489     19   -904       N
ATOM   3440  NH2 ARG A 229      28.163 -58.189 -63.196  1.00 27.84           N
ANISOU 3440  NH2 ARG A 229     3761   3971   2845    528     -5   -797       N
ATOM   3441  H  AARG A 229      26.143 -64.722 -60.121  0.54  0.00           H
ATOM   3442  H  BARG A 229      26.127 -64.710 -60.127  0.46  0.00           H
ATOM   3443  HA  ARG A 229      27.584 -62.430 -58.902  1.00  0.00           H
ATOM   3444  HB2 ARG A 229      24.630 -62.437 -59.663  1.00  0.00           H
ATOM   3445  HB3 ARG A 229      25.345 -61.286 -58.529  1.00  0.00           H
ATOM   3446  HG2 ARG A 229      26.103 -61.557 -61.459  1.00  0.00           H
ATOM   3447  HG3 ARG A 229      24.997 -60.337 -60.792  1.00  0.00           H
ATOM   3448  HD2 ARG A 229      27.922 -60.704 -60.170  1.00  0.00           H
ATOM   3449  HD3 ARG A 229      26.851 -59.589 -59.302  1.00  0.00           H
ATOM   3450  HE  ARG A 229      26.845 -58.158 -61.139  1.00  0.00           H
ATOM   3451 HH11 ARG A 229      29.237 -60.460 -63.459  1.00  0.00           H
ATOM   3452 HH12 ARG A 229      28.580 -61.157 -61.995  1.00  0.00           H
ATOM   3453 HH21 ARG A 229      28.731 -58.281 -64.026  1.00  0.00           H
ATOM   3454 HH22 ARG A 229      27.692 -57.317 -63.000  1.00  0.00           H
ATOM   3455  N   ILE A 230      26.449 -62.881 -56.662  1.00 16.45           N
ANISOU 3455  N   ILE A 230     1994   2298   1957    299   -250   -831       N
ATOM   3456  CA  ILE A 230      25.869 -63.212 -55.387  1.00 16.07           C
ANISOU 3456  CA  ILE A 230     1896   2239   1971    254   -294   -798       C
ATOM   3457  C   ILE A 230      24.983 -62.044 -54.962  1.00 17.35           C
ANISOU 3457  C   ILE A 230     1999   2494   2100    254   -332   -748       C
ATOM   3458  O   ILE A 230      25.391 -60.890 -55.126  1.00 20.59           O
ANISOU 3458  O   ILE A 230     2396   2938   2487    307   -309   -711       O
ATOM   3459  CB  ILE A 230      26.978 -63.426 -54.340  1.00 18.11           C
ANISOU 3459  CB  ILE A 230     2135   2417   2327    281   -260   -757       C
ATOM   3460  CG1 ILE A 230      27.716 -64.732 -54.650  1.00 21.74           C
ANISOU 3460  CG1 ILE A 230     2647   2776   2838    281   -230   -809       C
ATOM   3461  CG2 ILE A 230      26.391 -63.496 -52.923  1.00 18.47           C
ANISOU 3461  CG2 ILE A 230     2138   2464   2416    240   -301   -707       C
ATOM   3462  CD1 ILE A 230      28.898 -64.964 -53.763  1.00 24.62           C
ANISOU 3462  CD1 ILE A 230     2992   3060   3305    320   -205   -770       C
ATOM   3463  H   ILE A 230      27.079 -62.093 -56.721  1.00  0.00           H
ATOM   3464  HA  ILE A 230      25.268 -64.117 -55.479  1.00  0.00           H
ATOM   3465  HB  ILE A 230      27.683 -62.597 -54.393  1.00  0.00           H
ATOM   3466 HG12 ILE A 230      28.060 -64.699 -55.684  1.00  0.00           H
ATOM   3467 HG13 ILE A 230      27.022 -65.564 -54.536  1.00  0.00           H
ATOM   3468 HG21 ILE A 230      25.865 -62.567 -52.701  1.00  0.00           H
ATOM   3469 HG22 ILE A 230      27.197 -63.639 -52.203  1.00  0.00           H
ATOM   3470 HG23 ILE A 230      25.694 -64.332 -52.859  1.00  0.00           H
ATOM   3471 HD11 ILE A 230      29.377 -65.905 -54.034  1.00  0.00           H
ATOM   3472 HD12 ILE A 230      29.609 -64.147 -53.884  1.00  0.00           H
ATOM   3473 HD13 ILE A 230      28.570 -65.009 -52.725  1.00  0.00           H
ATOM   3474  N   SER A 231      23.784 -62.324 -54.463  1.00 17.67           N
ANISOU 3474  N   SER A 231     2002   2571   2143    196   -384   -747       N
ATOM   3475  CA  SER A 231      22.919 -61.307 -53.849  1.00 19.61           C
ANISOU 3475  CA  SER A 231     2179   2895   2376    199   -412   -700       C
ATOM   3476  C   SER A 231      22.952 -61.476 -52.353  1.00 19.20           C
ANISOU 3476  C   SER A 231     2094   2812   2391    177   -401   -655       C
ATOM   3477  O   SER A 231      22.849 -62.578 -51.844  1.00 20.22           O
ANISOU 3477  O   SER A 231     2236   2886   2562    123   -404   -666       O
ATOM   3478  CB  SER A 231      21.476 -61.402 -54.347  1.00 22.86           C
ANISOU 3478  CB  SER A 231     2558   3383   2747    152   -473   -731       C
ATOM   3479  OG  SER A 231      21.419 -61.174 -55.739  1.00 24.11           O
ANISOU 3479  OG  SER A 231     2759   3576   2827    176   -496   -769       O
ATOM   3480  H   SER A 231      23.453 -63.277 -54.508  1.00  0.00           H
ATOM   3481  HA  SER A 231      23.310 -60.320 -54.097  1.00  0.00           H
ATOM   3482  HB2 SER A 231      21.086 -62.397 -54.130  1.00  0.00           H
ATOM   3483  HB3 SER A 231      20.868 -60.657 -53.834  1.00  0.00           H
ATOM   3484  HG  SER A 231      20.780 -60.482 -55.924  1.00  0.00           H
ATOM   3485  N   ILE A 232      23.126 -60.355 -51.657  1.00 17.86           N
ANISOU 3485  N   ILE A 232     1891   2670   2224    219   -388   -603       N
ATOM   3486  CA  ILE A 232      23.287 -60.318 -50.219  1.00 17.78           C
ANISOU 3486  CA  ILE A 232     1863   2632   2259    209   -376   -558       C
ATOM   3487  C   ILE A 232      22.008 -59.893 -49.519  1.00 19.41           C
ANISOU 3487  C   ILE A 232     2012   2909   2453    181   -390   -539       C
ATOM   3488  O   ILE A 232      21.332 -58.913 -49.921  1.00 20.12           O
ANISOU 3488  O   ILE A 232     2063   3075   2509    210   -403   -538       O
ATOM   3489  CB  ILE A 232      24.432 -59.335 -49.873  1.00 16.42           C
ANISOU 3489  CB  ILE A 232     1699   2437   2102    275   -352   -520       C
ATOM   3490  CG1 ILE A 232      25.753 -59.809 -50.485  1.00 17.02           C
ANISOU 3490  CG1 ILE A 232     1815   2442   2209    303   -327   -537       C
ATOM   3491  CG2 ILE A 232      24.547 -59.078 -48.393  1.00 16.69           C
ANISOU 3491  CG2 ILE A 232     1723   2455   2164    270   -351   -475       C
ATOM   3492  CD1 ILE A 232      26.337 -61.057 -49.877  1.00 18.45           C
ANISOU 3492  CD1 ILE A 232     2024   2537   2451    276   -327   -540       C
ATOM   3493  H   ILE A 232      23.147 -59.480 -52.161  1.00  0.00           H
ATOM   3494  HA  ILE A 232      23.563 -61.314 -49.871  1.00  0.00           H
ATOM   3495  HB  ILE A 232      24.187 -58.383 -50.343  1.00  0.00           H
ATOM   3496 HG12 ILE A 232      26.483 -59.007 -50.372  1.00  0.00           H
ATOM   3497 HG13 ILE A 232      25.596 -59.985 -51.549  1.00  0.00           H
ATOM   3498 HG21 ILE A 232      23.584 -58.744 -48.006  1.00  0.00           H
ATOM   3499 HG22 ILE A 232      25.297 -58.307 -48.216  1.00  0.00           H
ATOM   3500 HG23 ILE A 232      24.843 -59.997 -47.887  1.00  0.00           H
ATOM   3501 HD11 ILE A 232      27.270 -61.306 -50.382  1.00  0.00           H
ATOM   3502 HD12 ILE A 232      25.632 -61.880 -49.991  1.00  0.00           H
ATOM   3503 HD13 ILE A 232      26.531 -60.889 -48.818  1.00  0.00           H
ATOM   3504  N   TYR A 233      21.667 -60.631 -48.466  1.00 19.21           N
ANISOU 3504  N   TYR A 233     1984   2857   2458    125   -383   -523       N
ATOM   3505  CA  TYR A 233      20.496 -60.364 -47.643  1.00 18.05           C
ANISOU 3505  CA  TYR A 233     1782   2769   2306     91   -376   -504       C
ATOM   3506  C   TYR A 233      20.903 -60.327 -46.180  1.00 18.66           C
ANISOU 3506  C   TYR A 233     1885   2808   2396     87   -348   -456       C
ATOM   3507  O   TYR A 233      22.014 -60.746 -45.794  1.00 19.23           O
ANISOU 3507  O   TYR A 233     2016   2802   2489     99   -349   -438       O
ATOM   3508  CB  TYR A 233      19.435 -61.453 -47.878  1.00 17.81           C
ANISOU 3508  CB  TYR A 233     1725   2751   2293      5   -391   -535       C
ATOM   3509  CG  TYR A 233      18.949 -61.425 -49.309  1.00 19.64           C
ANISOU 3509  CG  TYR A 233     1934   3029   2501      8   -434   -586       C
ATOM   3510  CD1 TYR A 233      17.895 -60.599 -49.689  1.00 20.51           C
ANISOU 3510  CD1 TYR A 233     1968   3235   2591     23   -458   -593       C
ATOM   3511  CD2 TYR A 233      19.593 -62.168 -50.298  1.00 20.84           C
ANISOU 3511  CD2 TYR A 233     2146   3127   2646      3   -452   -628       C
ATOM   3512  CE1 TYR A 233      17.461 -60.548 -51.020  1.00 22.60           C
ANISOU 3512  CE1 TYR A 233     2238   3526   2824     30   -497   -621       C
ATOM   3513  CE2 TYR A 233      19.193 -62.123 -51.620  1.00 22.30           C
ANISOU 3513  CE2 TYR A 233     2329   3354   2791      7   -495   -677       C
ATOM   3514  CZ  TYR A 233      18.117 -61.302 -51.982  1.00 24.53           C
ANISOU 3514  CZ  TYR A 233     2545   3728   3047     19   -525   -672       C
ATOM   3515  OH  TYR A 233      17.729 -61.262 -53.298  1.00 26.88           O
ANISOU 3515  OH  TYR A 233     2864   4050   3300     25   -563   -698       O
ATOM   3516  H   TYR A 233      22.252 -61.418 -48.225  1.00  0.00           H
ATOM   3517  HA  TYR A 233      20.079 -59.396 -47.921  1.00  0.00           H
ATOM   3518  HB2 TYR A 233      18.591 -61.280 -47.210  1.00  0.00           H
ATOM   3519  HB3 TYR A 233      19.869 -62.430 -47.664  1.00  0.00           H
ATOM   3520  HD1 TYR A 233      17.404 -59.988 -48.946  1.00  0.00           H
ATOM   3521  HD2 TYR A 233      20.428 -62.796 -50.023  1.00  0.00           H
ATOM   3522  HE1 TYR A 233      16.622 -59.926 -51.295  1.00  0.00           H
ATOM   3523  HE2 TYR A 233      19.704 -62.714 -52.366  1.00  0.00           H
ATOM   3524  HH  TYR A 233      16.936 -60.727 -53.382  1.00  0.00           H
ATOM   3525  N  ATRP A 234      20.018 -59.832 -45.335  0.52 18.34           N
ANISOU 3525  N  ATRP A 234     1804   2822   2341     74   -325   -436       N
ATOM   3526  N  BTRP A 234      20.015 -59.798 -45.350  0.48 18.33           N
ANISOU 3526  N  BTRP A 234     1802   2822   2340     76   -325   -437       N
ATOM   3527  CA ATRP A 234      20.331 -59.807 -43.918  0.52 17.81           C
ANISOU 3527  CA ATRP A 234     1776   2723   2268     66   -297   -393       C
ATOM   3528  CA BTRP A 234      20.283 -59.719 -43.921  0.48 17.80           C
ANISOU 3528  CA BTRP A 234     1771   2727   2265     69   -296   -394       C
ATOM   3529  C  ATRP A 234      19.098 -60.067 -43.099  0.52 18.59           C
ANISOU 3529  C  ATRP A 234     1838   2867   2360      5   -257   -381       C
ATOM   3530  C  BTRP A 234      19.073 -60.124 -43.117  0.48 18.63           C
ANISOU 3530  C  BTRP A 234     1843   2871   2366      1   -257   -382       C
ATOM   3531  O  ATRP A 234      17.978 -59.845 -43.556  0.52 18.95           O
ANISOU 3531  O  ATRP A 234     1804   2985   2411    -10   -249   -406       O
ATOM   3532  O  BTRP A 234      17.941 -60.067 -43.604  0.48 19.00           O
ANISOU 3532  O  BTRP A 234     1811   2985   2422    -24   -251   -407       O
ATOM   3533  CB ATRP A 234      20.989 -58.497 -43.524  0.52 17.03           C
ANISOU 3533  CB ATRP A 234     1691   2633   2147    142   -295   -376       C
ATOM   3534  CB BTRP A 234      20.762 -58.330 -43.517  0.48 16.68           C
ANISOU 3534  CB BTRP A 234     1634   2605   2098    144   -291   -378       C
ATOM   3535  CG ATRP A 234      20.032 -57.342 -43.458  0.52 16.83           C
ANISOU 3535  CG ATRP A 234     1605   2691   2099    175   -273   -384       C
ATOM   3536  CG BTRP A 234      19.823 -57.180 -43.869  0.48 17.10           C
ANISOU 3536  CG BTRP A 234     1617   2745   2134    184   -279   -394       C
ATOM   3537  CD1ATRP A 234      19.295 -56.953 -42.379  0.52 17.72           C
ANISOU 3537  CD1ATRP A 234     1703   2842   2190    165   -230   -369       C
ATOM   3538  CD1BTRP A 234      19.732 -56.544 -45.074  0.48 16.66           C
ANISOU 3538  CD1BTRP A 234     1528   2726   2078    230   -304   -417       C
ATOM   3539  CD2ATRP A 234      19.733 -56.419 -44.505  0.52 16.63           C
ANISOU 3539  CD2ATRP A 234     1531   2718   2070    229   -290   -406       C
ATOM   3540  CD2BTRP A 234      18.898 -56.505 -42.989  0.48 17.07           C
ANISOU 3540  CD2BTRP A 234     1576   2798   2112    189   -237   -386       C
ATOM   3541  NE1ATRP A 234      18.539 -55.848 -42.694  0.52 17.63           N
ANISOU 3541  NE1ATRP A 234     1627   2900   2172    215   -218   -386       N
ATOM   3542  NE1BTRP A 234      18.797 -55.527 -45.006  0.48 17.06           N
ANISOU 3542  NE1BTRP A 234     1523   2843   2117    265   -288   -418       N
ATOM   3543  CE2ATRP A 234      18.797 -55.492 -43.991  0.52 17.78           C
ANISOU 3543  CE2ATRP A 234     1626   2927   2202    255   -261   -404       C
ATOM   3544  CE2BTRP A 234      18.266 -55.489 -43.742  0.48 17.95           C
ANISOU 3544  CE2BTRP A 234     1623   2975   2224    244   -245   -405       C
ATOM   3545  CE3ATRP A 234      20.168 -56.278 -45.826  0.52 16.23           C
ANISOU 3545  CE3ATRP A 234     1482   2664   2021    261   -324   -425       C
ATOM   3546  CE3BTRP A 234      18.527 -56.676 -41.651  0.48 18.49           C
ANISOU 3546  CE3BTRP A 234     1776   2978   2271    155   -189   -364       C
ATOM   3547  CZ2ATRP A 234      18.274 -54.449 -44.759  0.52 17.59           C
ANISOU 3547  CZ2ATRP A 234     1579   2932   2172    305   -262   -406       C
ATOM   3548  CZ2BTRP A 234      17.296 -54.642 -43.197  0.48 16.81           C
ANISOU 3548  CZ2BTRP A 234     1423   2891   2073    272   -207   -408       C
ATOM   3549  CZ3ATRP A 234      19.649 -55.243 -46.588  0.52 16.85           C
ANISOU 3549  CZ3ATRP A 234     1559   2762   2081    298   -313   -416       C
ATOM   3550  CZ3BTRP A 234      17.558 -55.836 -41.108  0.48 19.38           C
ANISOU 3550  CZ3BTRP A 234     1838   3157   2367    177   -140   -370       C
ATOM   3551  CH2ATRP A 234      18.707 -54.337 -46.048  0.52 17.10           C
ANISOU 3551  CH2ATRP A 234     1557   2836   2106    319   -287   -404       C
ATOM   3552  CH2BTRP A 234      16.951 -54.826 -41.878  0.48 18.52           C
ANISOU 3552  CH2BTRP A 234     1655   3109   2273    238   -149   -394       C
ATOM   3553  H  ATRP A 234      19.135 -59.475 -45.670  0.52  0.00           H
ATOM   3554  H  BTRP A 234      19.141 -59.445 -45.714  0.48  0.00           H
ATOM   3555  HA ATRP A 234      21.040 -60.610 -43.718  0.52  0.00           H
ATOM   3556  HA BTRP A 234      21.083 -60.424 -43.694  0.48  0.00           H
ATOM   3557  HB2ATRP A 234      21.760 -58.264 -44.258  0.52  0.00           H
ATOM   3558  HB2BTRP A 234      21.716 -58.147 -44.012  0.48  0.00           H
ATOM   3559  HB3ATRP A 234      21.459 -58.620 -42.548  0.52  0.00           H
ATOM   3560  HB3BTRP A 234      20.926 -58.323 -42.439  0.48  0.00           H
ATOM   3561  HD1ATRP A 234      19.304 -57.442 -41.416  0.52  0.00           H
ATOM   3562  HD1BTRP A 234      20.307 -56.798 -45.952  0.48  0.00           H
ATOM   3563  HE3ATRP A 234      20.893 -56.961 -46.244  0.52  0.00           H
ATOM   3564  HE3BTRP A 234      18.985 -57.447 -41.049  0.48  0.00           H
ATOM   3565  HZ2ATRP A 234      17.554 -53.757 -44.348  0.52  0.00           H
ATOM   3566  HZ2BTRP A 234      16.833 -53.869 -43.792  0.48  0.00           H
ATOM   3567  HZ3ATRP A 234      19.970 -55.126 -47.613  0.52  0.00           H
ATOM   3568  HZ3BTRP A 234      17.266 -55.962 -40.076  0.48  0.00           H
ATOM   3569  HH2ATRP A 234      18.323 -53.541 -46.668  0.52  0.00           H
ATOM   3570  HH2BTRP A 234      16.205 -54.188 -41.428  0.48  0.00           H
ATOM   3571  HE1ATRP A 234      17.899 -55.377 -42.071  0.52  0.00           H
ATOM   3572  HE1BTRP A 234      18.545 -54.911 -45.766  0.48  0.00           H
ATOM   3573  N   THR A 235      19.324 -60.550 -41.883  1.00 19.38           N
ANISOU 3573  N   THR A 235     1996   2921   2448    -30   -231   -342       N
ATOM   3574  CA  THR A 235      18.266 -60.920 -40.969  1.00 21.48           C
ANISOU 3574  CA  THR A 235     2243   3217   2702    -98   -176   -321       C
ATOM   3575  C   THR A 235      18.717 -60.561 -39.561  1.00 20.98           C
ANISOU 3575  C   THR A 235     2253   3130   2587    -83   -147   -277       C
ATOM   3576  O   THR A 235      19.810 -60.938 -39.156  1.00 19.00           O
ANISOU 3576  O   THR A 235     2088   2802   2330    -72   -182   -249       O
ATOM   3577  CB  THR A 235      18.065 -62.441 -40.966  1.00 23.13           C
ANISOU 3577  CB  THR A 235     2479   3366   2943   -191   -175   -312       C
ATOM   3578  OG1 THR A 235      17.829 -62.889 -42.296  1.00 23.93           O
ANISOU 3578  OG1 THR A 235     2534   3472   3086   -207   -215   -360       O
ATOM   3579  CG2 THR A 235      16.883 -62.846 -40.089  1.00 24.81           C
ANISOU 3579  CG2 THR A 235     2663   3613   3150   -273   -105   -288       C
ATOM   3580  H  ATHR A 235      20.281 -60.665 -41.582  0.52  0.00           H
ATOM   3581  H  BTHR A 235      20.283 -60.617 -41.574  0.48  0.00           H
ATOM   3582  HA  THR A 235      17.338 -60.407 -41.222  1.00  0.00           H
ATOM   3583  HB  THR A 235      18.969 -62.918 -40.586  1.00  0.00           H
ATOM   3584  HG1 THR A 235      17.287 -63.681 -42.275  1.00  0.00           H
ATOM   3585 HG21 THR A 235      16.769 -63.930 -40.110  1.00  0.00           H
ATOM   3586 HG22 THR A 235      17.062 -62.519 -39.065  1.00  0.00           H
ATOM   3587 HG23 THR A 235      15.974 -62.378 -40.466  1.00  0.00           H
ATOM   3588  N   ILE A 236      17.870 -59.883 -38.812  1.00 20.80           N
ANISOU 3588  N   ILE A 236     2200   3173   2530    -82    -86   -272       N
ATOM   3589  CA  ILE A 236      18.137 -59.588 -37.422  1.00 21.88           C
ANISOU 3589  CA  ILE A 236     2418   3293   2602    -77    -51   -235       C
ATOM   3590  C   ILE A 236      17.369 -60.527 -36.512  1.00 23.46           C
ANISOU 3590  C   ILE A 236     2645   3489   2781   -169     17   -199       C
ATOM   3591  O   ILE A 236      16.175 -60.802 -36.717  1.00 27.39           O
ANISOU 3591  O   ILE A 236     3057   4043   3309   -223     73   -213       O
ATOM   3592  CB  ILE A 236      17.778 -58.115 -37.103  1.00 23.41           C
ANISOU 3592  CB  ILE A 236     2579   3556   2761     -8    -16   -258       C
ATOM   3593  CG1 ILE A 236      18.705 -57.203 -37.900  1.00 27.07           C
ANISOU 3593  CG1 ILE A 236     3039   4005   3243     77    -84   -282       C
ATOM   3594  CG2 ILE A 236      17.897 -57.860 -35.645  1.00 22.51           C
ANISOU 3594  CG2 ILE A 236     2555   3430   2567    -12     29   -229       C
ATOM   3595  CD1 ILE A 236      18.412 -55.741 -37.752  1.00 31.26           C
ANISOU 3595  CD1 ILE A 236     3540   4586   3751    150    -59   -307       C
ATOM   3596  H   ILE A 236      17.006 -59.559 -39.223  1.00  0.00           H
ATOM   3597  HA  ILE A 236      19.202 -59.729 -37.240  1.00  0.00           H
ATOM   3598  HB  ILE A 236      16.749 -57.928 -37.411  1.00  0.00           H
ATOM   3599 HG12 ILE A 236      18.615 -57.464 -38.955  1.00  0.00           H
ATOM   3600 HG13 ILE A 236      19.731 -57.386 -37.582  1.00  0.00           H
ATOM   3601 HG21 ILE A 236      17.642 -56.821 -35.435  1.00  0.00           H
ATOM   3602 HG22 ILE A 236      18.921 -58.054 -35.325  1.00  0.00           H
ATOM   3603 HG23 ILE A 236      17.216 -58.518 -35.104  1.00  0.00           H
ATOM   3604 HD11 ILE A 236      19.118 -55.166 -38.352  1.00  0.00           H
ATOM   3605 HD12 ILE A 236      18.509 -55.456 -36.704  1.00  0.00           H
ATOM   3606 HD13 ILE A 236      17.396 -55.538 -38.092  1.00  0.00           H
ATOM   3607  N   VAL A 237      18.039 -61.036 -35.486  1.00 20.42           N
ANISOU 3607  N   VAL A 237     2378   3037   2345   -191     12   -149       N
ATOM   3608  CA  VAL A 237      17.410 -61.994 -34.604  1.00 21.38           C
ANISOU 3608  CA  VAL A 237     2544   3139   2438   -283     78   -102       C
ATOM   3609  C   VAL A 237      17.479 -61.420 -33.202  1.00 24.50           C
ANISOU 3609  C   VAL A 237     3032   3547   2730   -269    127    -70       C
ATOM   3610  O   VAL A 237      18.570 -61.182 -32.675  1.00 23.80           O
ANISOU 3610  O   VAL A 237     3044   3406   2593   -224     64    -49       O
ATOM   3611  CB  VAL A 237      18.153 -63.328 -34.615  1.00 21.95           C
ANISOU 3611  CB  VAL A 237     2702   3104   2535   -330     23    -59       C
ATOM   3612  CG1 VAL A 237      17.424 -64.366 -33.750  1.00 22.17           C
ANISOU 3612  CG1 VAL A 237     2781   3106   2538   -436     97     -4       C
ATOM   3613  CG2 VAL A 237      18.301 -63.835 -36.032  1.00 23.97           C
ANISOU 3613  CG2 VAL A 237     2888   3337   2884   -331    -34   -101       C
ATOM   3614  H   VAL A 237      18.994 -60.753 -35.320  1.00  0.00           H
ATOM   3615  HA  VAL A 237      16.370 -62.143 -34.896  1.00  0.00           H
ATOM   3616  HB  VAL A 237      19.148 -63.171 -34.199  1.00  0.00           H
ATOM   3617 HG11 VAL A 237      17.325 -63.987 -32.733  1.00  0.00           H
ATOM   3618 HG12 VAL A 237      16.434 -64.554 -34.165  1.00  0.00           H
ATOM   3619 HG13 VAL A 237      17.995 -65.294 -33.738  1.00  0.00           H
ATOM   3620 HG21 VAL A 237      18.832 -64.787 -36.024  1.00  0.00           H
ATOM   3621 HG22 VAL A 237      17.314 -63.974 -36.473  1.00  0.00           H
ATOM   3622 HG23 VAL A 237      18.863 -63.110 -36.621  1.00  0.00           H
ATOM   3623  N   LYS A 238      16.328 -61.243 -32.576  1.00 28.94           N
ANISOU 3623  N   LYS A 238     3562   4175   3257   -309    238    -69       N
ATOM   3624  CA  LYS A 238      16.286 -60.680 -31.236  1.00 31.98           C
ANISOU 3624  CA  LYS A 238     4041   4578   3530   -297    301    -46       C
ATOM   3625  C   LYS A 238      16.479 -61.722 -30.153  1.00 30.83           C
ANISOU 3625  C   LYS A 238     4035   4367   3312   -373    324     30       C
ATOM   3626  O   LYS A 238      16.295 -62.933 -30.379  1.00 28.46           O
ANISOU 3626  O   LYS A 238     3737   4018   3059   -452    326     68       O
ATOM   3627  CB  LYS A 238      14.946 -59.981 -31.007  1.00 36.90           C
ANISOU 3627  CB  LYS A 238     4569   5304   4148   -299    427    -81       C
ATOM   3628  CG  LYS A 238      14.762 -58.729 -31.825  1.00 40.40           C
ANISOU 3628  CG  LYS A 238     4900   5811   4641   -207    406   -150       C
ATOM   3629  CD  LYS A 238      13.313 -58.298 -31.762  1.00 45.69           C
ANISOU 3629  CD  LYS A 238     5445   6577   5337   -217    528   -181       C
ATOM   3630  CE  LYS A 238      13.038 -57.019 -32.555  1.00 47.18           C
ANISOU 3630  CE  LYS A 238     5521   6826   5577   -117    507   -245       C
ATOM   3631  NZ  LYS A 238      11.570 -56.747 -32.562  1.00 47.54           N
ANISOU 3631  NZ  LYS A 238     5425   6966   5672   -128    619   -273       N
ATOM   3632  H   LYS A 238      15.466 -61.502 -33.035  1.00  0.00           H
ATOM   3633  HA  LYS A 238      17.081 -59.939 -31.148  1.00  0.00           H
ATOM   3634  HB2 LYS A 238      14.148 -60.678 -31.262  1.00  0.00           H
ATOM   3635  HB3 LYS A 238      14.862 -59.724 -29.951  1.00  0.00           H
ATOM   3636  HG2 LYS A 238      15.038 -58.927 -32.861  1.00  0.00           H
ATOM   3637  HG3 LYS A 238      15.395 -57.937 -31.425  1.00  0.00           H
ATOM   3638  HD2 LYS A 238      12.694 -59.098 -32.167  1.00  0.00           H
ATOM   3639  HD3 LYS A 238      13.039 -58.133 -30.720  1.00  0.00           H
ATOM   3640  HE2 LYS A 238      13.390 -57.143 -33.579  1.00  0.00           H
ATOM   3641  HE3 LYS A 238      13.561 -56.183 -32.090  1.00  0.00           H
ATOM   3642  HZ1 LYS A 238      11.070 -57.590 -32.319  1.00  0.00           H
ATOM   3643  HZ2 LYS A 238      11.288 -56.443 -33.483  1.00  0.00           H
ATOM   3644  HZ3 LYS A 238      11.358 -56.024 -31.889  1.00  0.00           H
ATOM   3645  N   PRO A 239      16.805 -61.252 -28.940  1.00 33.25           N
ANISOU 3645  N   PRO A 239     4467   4669   3497   -351    346     55       N
ATOM   3646  CA  PRO A 239      16.953 -62.181 -27.814  1.00 34.06           C
ANISOU 3646  CA  PRO A 239     4721   4712   3508   -421    371    136       C
ATOM   3647  C   PRO A 239      15.710 -63.053 -27.671  1.00 33.73           C
ANISOU 3647  C   PRO A 239     4634   4694   3487   -529    500    167       C
ATOM   3648  O   PRO A 239      14.585 -62.571 -27.766  1.00 33.33           O
ANISOU 3648  O   PRO A 239     4472   4733   3458   -543    613    127       O
ATOM   3649  CB  PRO A 239      17.117 -61.247 -26.604  1.00 36.76           C
ANISOU 3649  CB  PRO A 239     5177   5083   3705   -378    404    133       C
ATOM   3650  CG  PRO A 239      17.637 -59.960 -27.183  1.00 36.26           C
ANISOU 3650  CG  PRO A 239     5051   5051   3676   -274    334     58       C
ATOM   3651  CD  PRO A 239      17.014 -59.849 -28.545  1.00 34.27           C
ANISOU 3651  CD  PRO A 239     4614   4845   3562   -265    348      7       C
ATOM   3652  HA  PRO A 239      17.841 -62.800 -27.943  1.00  0.00           H
ATOM   3653  HB2 PRO A 239      16.159 -61.087 -26.110  1.00  0.00           H
ATOM   3654  HB3 PRO A 239      17.839 -61.663 -25.901  1.00  0.00           H
ATOM   3655  HG2 PRO A 239      17.342 -59.116 -26.560  1.00  0.00           H
ATOM   3656  HG3 PRO A 239      18.723 -60.000 -27.270  1.00  0.00           H
ATOM   3657  HD2 PRO A 239      17.684 -59.344 -29.240  1.00  0.00           H
ATOM   3658  HD3 PRO A 239      16.061 -59.324 -28.486  1.00  0.00           H
ATOM   3659  N   GLY A 240      15.916 -64.345 -27.455  1.00 35.11           N
ANISOU 3659  N   GLY A 240     4891   4784   3667   -607    481    239       N
ATOM   3660  CA  GLY A 240      14.807 -65.267 -27.318  1.00 36.87           C
ANISOU 3660  CA  GLY A 240     5077   5012   3918   -724    599    276       C
ATOM   3661  C   GLY A 240      14.222 -65.748 -28.633  1.00 37.69           C
ANISOU 3661  C   GLY A 240     5015   5128   4178   -765    589    232       C
ATOM   3662  O   GLY A 240      13.413 -66.668 -28.643  1.00 39.02           O
ANISOU 3662  O   GLY A 240     5150   5282   4393   -873    663    262       O
ATOM   3663  H   GLY A 240      16.862 -64.692 -27.385  1.00  0.00           H
ATOM   3664  HA2 GLY A 240      15.155 -66.137 -26.762  1.00  0.00           H
ATOM   3665  HA3 GLY A 240      14.019 -64.780 -26.744  1.00  0.00           H
ATOM   3666  N   ASP A 241      14.635 -65.146 -29.746  1.00 35.87           N
ANISOU 3666  N   ASP A 241     4685   4919   4025   -683    495    162       N
ATOM   3667  CA  ASP A 241      14.207 -65.624 -31.053  1.00 35.34           C
ANISOU 3667  CA  ASP A 241     4481   4856   4091   -716    462    118       C
ATOM   3668  C   ASP A 241      15.273 -66.588 -31.555  1.00 33.26           C
ANISOU 3668  C   ASP A 241     4294   4472   3871   -718    343    142       C
ATOM   3669  O   ASP A 241      16.237 -66.892 -30.844  1.00 32.87           O
ANISOU 3669  O   ASP A 241     4390   4342   3757   -697    292    199       O
ATOM   3670  CB  ASP A 241      14.017 -64.456 -32.017  1.00 36.07           C
ANISOU 3670  CB  ASP A 241     4432   5037   4234   -627    431     32       C
ATOM   3671  CG  ASP A 241      12.969 -64.737 -33.105  1.00 39.85           C
ANISOU 3671  CG  ASP A 241     4742   5569   4829   -679    449    -17       C
ATOM   3672  OD1 ASP A 241      12.749 -65.900 -33.480  1.00 36.74           O
ANISOU 3672  OD1 ASP A 241     4342   5119   4498   -770    437     -1       O
ATOM   3673  OD2 ASP A 241      12.389 -63.761 -33.621  1.00 45.88           O
ANISOU 3673  OD2 ASP A 241     5381   6428   5624   -624    463    -75       O
ATOM   3674  H   ASP A 241      15.252 -64.349 -29.683  1.00  0.00           H
ATOM   3675  HA  ASP A 241      13.263 -66.158 -30.947  1.00  0.00           H
ATOM   3676  HB2 ASP A 241      13.699 -63.583 -31.446  1.00  0.00           H
ATOM   3677  HB3 ASP A 241      14.971 -64.235 -32.496  1.00  0.00           H
ATOM   3678  N   VAL A 242      15.109 -67.045 -32.784  1.00 33.71           N
ANISOU 3678  N   VAL A 242     4254   4517   4037   -737    295     96       N
ATOM   3679  CA  VAL A 242      15.953 -68.090 -33.314  1.00 39.31           C
ANISOU 3679  CA  VAL A 242     5028   5108   4800   -749    203    111       C
ATOM   3680  C   VAL A 242      16.030 -67.934 -34.834  1.00 39.32           C
ANISOU 3680  C   VAL A 242     4916   5130   4894   -710    132     28       C
ATOM   3681  O   VAL A 242      15.080 -67.474 -35.473  1.00 43.94           O
ANISOU 3681  O   VAL A 242     5369   5808   5520   -724    165    -27       O
ATOM   3682  CB  VAL A 242      15.381 -69.482 -32.937  1.00 45.39           C
ANISOU 3682  CB  VAL A 242     5848   5800   5597   -880    255    168       C
ATOM   3683  CG1 VAL A 242      13.954 -69.588 -33.354  1.00 46.58           C
ANISOU 3683  CG1 VAL A 242     5858   6027   5812   -970    341    131       C
ATOM   3684  CG2 VAL A 242      16.173 -70.593 -33.579  1.00 48.88           C
ANISOU 3684  CG2 VAL A 242     6350   6112   6110   -890    163    173       C
ATOM   3685  H   VAL A 242      14.379 -66.656 -33.364  1.00  0.00           H
ATOM   3686  HA  VAL A 242      16.953 -67.989 -32.893  1.00  0.00           H
ATOM   3687  HB  VAL A 242      15.436 -69.598 -31.855  1.00  0.00           H
ATOM   3688 HG11 VAL A 242      13.379 -68.786 -32.891  1.00  0.00           H
ATOM   3689 HG12 VAL A 242      13.554 -70.551 -33.037  1.00  0.00           H
ATOM   3690 HG13 VAL A 242      13.885 -69.505 -34.439  1.00  0.00           H
ATOM   3691 HG21 VAL A 242      17.217 -70.518 -33.276  1.00  0.00           H
ATOM   3692 HG22 VAL A 242      16.103 -70.509 -34.664  1.00  0.00           H
ATOM   3693 HG23 VAL A 242      15.771 -71.556 -33.262  1.00  0.00           H
ATOM   3694  N   LEU A 243      17.173 -68.300 -35.398  1.00 30.93           N
ANISOU 3694  N   LEU A 243     3908   3982   3863   -657     35     20       N
ATOM   3695  CA  LEU A 243      17.363 -68.266 -36.827  1.00 27.03           C
ANISOU 3695  CA  LEU A 243     3334   3494   3442   -622    -28    -55       C
ATOM   3696  C   LEU A 243      17.213 -69.700 -37.355  1.00 29.62           C
ANISOU 3696  C   LEU A 243     3685   3724   3844   -709    -46    -58       C
ATOM   3697  O   LEU A 243      17.738 -70.643 -36.743  1.00 30.02           O
ANISOU 3697  O   LEU A 243     3849   3662   3894   -739    -58      2       O
ATOM   3698  CB  LEU A 243      18.767 -67.765 -37.117  1.00 25.35           C
ANISOU 3698  CB  LEU A 243     3167   3245   3221   -509   -111    -65       C
ATOM   3699  CG  LEU A 243      19.133 -67.501 -38.579  1.00 26.32           C
ANISOU 3699  CG  LEU A 243     3220   3382   3399   -452   -168   -141       C
ATOM   3700  CD1 LEU A 243      18.439 -66.277 -39.089  1.00 25.78           C
ANISOU 3700  CD1 LEU A 243     3040   3439   3315   -416   -146   -190       C
ATOM   3701  CD2 LEU A 243      20.633 -67.356 -38.723  1.00 26.78           C
ANISOU 3701  CD2 LEU A 243     3338   3372   3464   -360   -237   -136       C
ATOM   3702  H   LEU A 243      17.932 -68.612 -34.810  1.00  0.00           H
ATOM   3703  HA  LEU A 243      16.625 -67.613 -37.291  1.00  0.00           H
ATOM   3704  HB2 LEU A 243      19.465 -68.510 -36.735  1.00  0.00           H
ATOM   3705  HB3 LEU A 243      18.919 -66.841 -36.558  1.00  0.00           H
ATOM   3706  HG  LEU A 243      18.810 -68.354 -39.175  1.00  0.00           H
ATOM   3707 HD11 LEU A 243      17.361 -66.397 -38.978  1.00  0.00           H
ATOM   3708 HD12 LEU A 243      18.768 -65.409 -38.518  1.00  0.00           H
ATOM   3709 HD13 LEU A 243      18.682 -66.133 -40.142  1.00  0.00           H
ATOM   3710 HD21 LEU A 243      21.123 -68.254 -38.348  1.00  0.00           H
ATOM   3711 HD22 LEU A 243      20.971 -66.492 -38.151  1.00  0.00           H
ATOM   3712 HD23 LEU A 243      20.885 -67.217 -39.774  1.00  0.00           H
ATOM   3713  N   VAL A 244      16.487 -69.862 -38.465  1.00 31.84           N
ANISOU 3713  N   VAL A 244     3865   4044   4187   -748    -54   -127       N
ATOM   3714  CA  VAL A 244      16.478 -71.112 -39.223  1.00 31.06           C
ANISOU 3714  CA  VAL A 244     3787   3850   4163   -814    -90   -154       C
ATOM   3715  C   VAL A 244      16.844 -70.794 -40.663  1.00 30.29           C
ANISOU 3715  C   VAL A 244     3637   3776   4097   -749   -160   -242       C
ATOM   3716  O   VAL A 244      16.374 -69.813 -41.252  1.00 30.79           O
ANISOU 3716  O   VAL A 244     3600   3953   4147   -711   -163   -289       O
ATOM   3717  CB  VAL A 244      15.125 -71.840 -39.194  1.00 30.03           C
ANISOU 3717  CB  VAL A 244     3597   3732   4080   -954    -35   -157       C
ATOM   3718  CG1 VAL A 244      15.208 -73.115 -40.018  1.00 29.65           C
ANISOU 3718  CG1 VAL A 244     3584   3572   4110  -1020    -83   -195       C
ATOM   3719  CG2 VAL A 244      14.702 -72.157 -37.754  1.00 30.47           C
ANISOU 3719  CG2 VAL A 244     3711   3767   4097  -1027     53    -65       C
ATOM   3720  H   VAL A 244      15.923 -69.091 -38.793  1.00  0.00           H
ATOM   3721  HA  VAL A 244      17.238 -71.775 -38.809  1.00  0.00           H
ATOM   3722  HB  VAL A 244      14.373 -71.189 -39.640  1.00  0.00           H
ATOM   3723 HG11 VAL A 244      14.246 -73.627 -39.994  1.00  0.00           H
ATOM   3724 HG12 VAL A 244      15.977 -73.767 -39.602  1.00  0.00           H
ATOM   3725 HG13 VAL A 244      15.461 -72.866 -41.048  1.00  0.00           H
ATOM   3726 HG21 VAL A 244      14.648 -71.233 -37.179  1.00  0.00           H
ATOM   3727 HG22 VAL A 244      13.724 -72.638 -37.760  1.00  0.00           H
ATOM   3728 HG23 VAL A 244      15.433 -72.826 -37.299  1.00  0.00           H
ATOM   3729  N   ILE A 245      17.750 -71.601 -41.176  1.00 28.66           N
ANISOU 3729  N   ILE A 245     3506   3456   3926   -728   -212   -258       N
ATOM   3730  CA  ILE A 245      18.223 -71.514 -42.532  1.00 27.28           C
ANISOU 3730  CA  ILE A 245     3309   3280   3777   -672   -269   -339       C
ATOM   3731  C   ILE A 245      17.902 -72.867 -43.174  1.00 28.91           C
ANISOU 3731  C   ILE A 245     3546   3390   4048   -762   -288   -381       C
ATOM   3732  O   ILE A 245      18.311 -73.911 -42.694  1.00 27.98           O
ANISOU 3732  O   ILE A 245     3522   3144   3964   -797   -287   -342       O
ATOM   3733  CB  ILE A 245      19.754 -71.294 -42.580  1.00 24.21           C
ANISOU 3733  CB  ILE A 245     2990   2829   3379   -555   -306   -329       C
ATOM   3734  CG1 ILE A 245      20.114 -69.961 -41.918  1.00 22.40           C
ANISOU 3734  CG1 ILE A 245     2737   2684   3089   -474   -295   -290       C
ATOM   3735  CG2 ILE A 245      20.258 -71.339 -44.012  1.00 22.58           C
ANISOU 3735  CG2 ILE A 245     2772   2610   3198   -504   -348   -413       C
ATOM   3736  CD1 ILE A 245      21.576 -69.652 -41.827  1.00 21.31           C
ANISOU 3736  CD1 ILE A 245     2651   2494   2952   -368   -332   -274       C
ATOM   3737  H   ILE A 245      18.135 -72.323 -40.583  1.00  0.00           H
ATOM   3738  HA  ILE A 245      17.709 -70.712 -43.062  1.00  0.00           H
ATOM   3739  HB  ILE A 245      20.235 -72.097 -42.021  1.00  0.00           H
ATOM   3740 HG12 ILE A 245      19.711 -69.971 -40.905  1.00  0.00           H
ATOM   3741 HG13 ILE A 245      19.627 -69.159 -42.473  1.00  0.00           H
ATOM   3742 HG21 ILE A 245      19.991 -72.295 -44.462  1.00  0.00           H
ATOM   3743 HG22 ILE A 245      21.342 -71.225 -44.019  1.00  0.00           H
ATOM   3744 HG23 ILE A 245      19.804 -70.529 -44.583  1.00  0.00           H
ATOM   3745 HD11 ILE A 245      21.714 -68.686 -41.342  1.00  0.00           H
ATOM   3746 HD12 ILE A 245      22.003 -69.619 -42.829  1.00  0.00           H
ATOM   3747 HD13 ILE A 245      22.075 -70.426 -41.244  1.00  0.00           H
ATOM   3748  N   ASN A 246      17.193 -72.820 -44.276  1.00 31.75           N
ANISOU 3748  N   ASN A 246     3833   3807   4425   -795   -313   -461       N
ATOM   3749  CA  ASN A 246      16.761 -74.019 -44.964  1.00 34.19           C
ANISOU 3749  CA  ASN A 246     4164   4035   4793   -890   -338   -516       C
ATOM   3750  C   ASN A 246      17.066 -73.807 -46.451  1.00 31.95           C
ANISOU 3750  C   ASN A 246     3867   3776   4498   -833   -396   -615       C
ATOM   3751  O   ASN A 246      16.574 -72.863 -47.048  1.00 32.07           O
ANISOU 3751  O   ASN A 246     3793   3915   4476   -804   -414   -652       O
ATOM   3752  CB  ASN A 246      15.268 -74.218 -44.693  1.00 37.49           C
ANISOU 3752  CB  ASN A 246     4492   4513   5238  -1020   -309   -512       C
ATOM   3753  CG  ASN A 246      14.707 -75.488 -45.324  1.00 39.97           C
ANISOU 3753  CG  ASN A 246     4823   4739   5622  -1140   -338   -569       C
ATOM   3754  OD1 ASN A 246      14.500 -75.546 -46.522  1.00 40.99           O
ANISOU 3754  OD1 ASN A 246     4924   4891   5759  -1144   -396   -660       O
ATOM   3755  ND2 ASN A 246      14.409 -76.481 -44.502  1.00 40.91           N
ANISOU 3755  ND2 ASN A 246     4995   4760   5789  -1244   -297   -514       N
ATOM   3756  H   ASN A 246      16.940 -71.919 -44.657  1.00  0.00           H
ATOM   3757  HA  ASN A 246      17.320 -74.878 -44.593  1.00  0.00           H
ATOM   3758  HB2 ASN A 246      14.726 -73.362 -45.096  1.00  0.00           H
ATOM   3759  HB3 ASN A 246      15.108 -74.260 -43.616  1.00  0.00           H
ATOM   3760 HD21 ASN A 246      14.577 -76.384 -43.511  1.00  0.00           H
ATOM   3761 HD22 ASN A 246      14.014 -77.336 -44.866  1.00  0.00           H
ATOM   3762  N   SER A 247      17.902 -74.644 -47.039  1.00 30.60           N
ANISOU 3762  N   SER A 247     3787   3484   4354   -810   -422   -657       N
ATOM   3763  CA  SER A 247      18.267 -74.465 -48.458  1.00 31.72           C
ANISOU 3763  CA  SER A 247     3935   3645   4472   -753   -465   -753       C
ATOM   3764  C   SER A 247      18.542 -75.793 -49.156  1.00 32.39           C
ANISOU 3764  C   SER A 247     4111   3591   4605   -796   -489   -823       C
ATOM   3765  O   SER A 247      19.108 -76.671 -48.557  1.00 35.39           O
ANISOU 3765  O   SER A 247     4574   3838   5036   -804   -472   -786       O
ATOM   3766  CB  SER A 247      19.542 -73.605 -48.561  1.00 31.88           C
ANISOU 3766  CB  SER A 247     3978   3683   4453   -609   -455   -737       C
ATOM   3767  OG  SER A 247      19.918 -73.400 -49.918  1.00 31.57           O
ANISOU 3767  OG  SER A 247     3951   3664   4381   -554   -481   -824       O
ATOM   3768  H   SER A 247      18.294 -75.412 -46.514  1.00  0.00           H
ATOM   3769  HA  SER A 247      17.452 -73.955 -48.973  1.00  0.00           H
ATOM   3770  HB2 SER A 247      20.355 -74.111 -48.040  1.00  0.00           H
ATOM   3771  HB3 SER A 247      19.361 -72.639 -48.090  1.00  0.00           H
ATOM   3772  HG  SER A 247      19.261 -72.852 -50.353  1.00  0.00           H
ATOM   3773  N   ASN A 248      18.181 -75.927 -50.428  1.00 31.21           N
ANISOU 3773  N   ASN A 248     3956   3466   4435   -816   -532   -925       N
ATOM   3774  CA  ASN A 248      18.595 -77.085 -51.220  1.00 32.66           C
ANISOU 3774  CA  ASN A 248     4241   3516   4651   -835   -553  -1007       C
ATOM   3775  C   ASN A 248      19.461 -76.652 -52.387  1.00 31.97           C
ANISOU 3775  C   ASN A 248     4192   3448   4505   -725   -561  -1081       C
ATOM   3776  O   ASN A 248      19.459 -77.283 -53.453  1.00 32.80           O
ANISOU 3776  O   ASN A 248     4360   3503   4601   -744   -589  -1183       O
ATOM   3777  CB  ASN A 248      17.396 -77.870 -51.753  1.00 35.73           C
ANISOU 3777  CB  ASN A 248     4617   3892   5069   -977   -600  -1079       C
ATOM   3778  CG  ASN A 248      16.640 -77.114 -52.804  1.00 37.02           C
ANISOU 3778  CG  ASN A 248     4708   4201   5159   -978   -653  -1139       C
ATOM   3779  OD1 ASN A 248      16.641 -75.892 -52.814  1.00 38.24           O
ANISOU 3779  OD1 ASN A 248     4786   4483   5261   -909   -652  -1118       O
ATOM   3780  ND2 ASN A 248      15.973 -77.837 -53.690  1.00 37.03           N
ANISOU 3780  ND2 ASN A 248     4744   4184   5143  -1048   -700  -1190       N
ATOM   3781  H   ASN A 248      17.609 -75.214 -50.857  1.00  0.00           H
ATOM   3782  HA  ASN A 248      19.182 -77.746 -50.582  1.00  0.00           H
ATOM   3783  HB2 ASN A 248      16.722 -78.085 -50.924  1.00  0.00           H
ATOM   3784  HB3 ASN A 248      17.748 -78.810 -52.177  1.00  0.00           H
ATOM   3785 HD21 ASN A 248      15.441 -77.380 -54.417  1.00  0.00           H
ATOM   3786 HD22 ASN A 248      15.996 -78.845 -53.639  1.00  0.00           H
ATOM   3787  N   GLY A 249      20.195 -75.555 -52.179  1.00 30.20           N
ANISOU 3787  N   GLY A 249     3937   3298   4240   -612   -532  -1031       N
ATOM   3788  CA  GLY A 249      21.220 -75.140 -53.121  1.00 29.87           C
ANISOU 3788  CA  GLY A 249     3936   3262   4153   -499   -516  -1082       C
ATOM   3789  C   GLY A 249      21.380 -73.644 -53.151  1.00 27.64           C
ANISOU 3789  C   GLY A 249     3580   3119   3805   -419   -505  -1041       C
ATOM   3790  O   GLY A 249      20.435 -72.907 -52.822  1.00 28.34           O
ANISOU 3790  O   GLY A 249     3583   3319   3865   -457   -526  -1005       O
ATOM   3791  H   GLY A 249      20.034 -75.003 -51.349  1.00  0.00           H
ATOM   3792  HA2 GLY A 249      20.944 -75.485 -54.117  1.00  0.00           H
ATOM   3793  HA3 GLY A 249      22.169 -75.594 -52.837  1.00  0.00           H
ATOM   3794  N   ASN A 250      22.571 -73.194 -53.543  1.00 25.20           N
ANISOU 3794  N   ASN A 250     3300   2799   3477   -308   -468  -1046       N
ATOM   3795  CA  ASN A 250      22.820 -71.771 -53.807  1.00 24.90           C
ANISOU 3795  CA  ASN A 250     3208   2881   3373   -229   -455  -1019       C
ATOM   3796  C   ASN A 250      22.974 -70.860 -52.572  1.00 24.05           C
ANISOU 3796  C   ASN A 250     3033   2824   3283   -196   -439   -914       C
ATOM   3797  O   ASN A 250      23.049 -69.638 -52.712  1.00 22.62           O
ANISOU 3797  O   ASN A 250     2803   2741   3052   -141   -432   -889       O
ATOM   3798  CB  ASN A 250      21.717 -71.219 -54.719  1.00 25.50           C
ANISOU 3798  CB  ASN A 250     3247   3075   3366   -269   -504  -1067       C
ATOM   3799  CG  ASN A 250      21.627 -71.974 -56.041  1.00 26.75           C
ANISOU 3799  CG  ASN A 250     3484   3195   3484   -294   -527  -1177       C
ATOM   3800  OD1 ASN A 250      21.160 -73.133 -56.093  1.00 28.34           O
ANISOU 3800  OD1 ASN A 250     3726   3317   3725   -378   -555  -1227       O
ATOM   3801  ND2 ASN A 250      22.049 -71.317 -57.120  1.00 25.53           N
ANISOU 3801  ND2 ASN A 250     3360   3096   3245   -225   -516  -1218       N
ATOM   3802  H   ASN A 250      23.327 -73.853 -53.662  1.00  0.00           H
ATOM   3803  HA  ASN A 250      23.754 -71.710 -54.365  1.00  0.00           H
ATOM   3804  HB2 ASN A 250      21.928 -70.170 -54.928  1.00  0.00           H
ATOM   3805  HB3 ASN A 250      20.760 -71.293 -54.203  1.00  0.00           H
ATOM   3806 HD21 ASN A 250      22.008 -71.758 -58.028  1.00  0.00           H
ATOM   3807 HD22 ASN A 250      22.410 -70.378 -57.030  1.00  0.00           H
ATOM   3808  N   LEU A 251      22.985 -71.454 -51.382  1.00 23.95           N
ANISOU 3808  N   LEU A 251     3025   2740   3333   -233   -434   -855       N
ATOM   3809  CA  LEU A 251      23.189 -70.704 -50.148  1.00 22.51           C
ANISOU 3809  CA  LEU A 251     2800   2593   3160   -205   -421   -761       C
ATOM   3810  C   LEU A 251      24.663 -70.253 -49.972  1.00 20.15           C
ANISOU 3810  C   LEU A 251     2516   2256   2883    -96   -395   -731       C
ATOM   3811  O   LEU A 251      25.595 -71.070 -50.091  1.00 19.39           O
ANISOU 3811  O   LEU A 251     2475   2048   2843    -62   -384   -748       O
ATOM   3812  CB  LEU A 251      22.764 -71.576 -48.953  1.00 23.39           C
ANISOU 3812  CB  LEU A 251     2932   2633   3322   -282   -424   -706       C
ATOM   3813  CG  LEU A 251      23.161 -71.004 -47.576  1.00 24.09           C
ANISOU 3813  CG  LEU A 251     3007   2730   3414   -250   -411   -608       C
ATOM   3814  CD1 LEU A 251      22.475 -69.670 -47.327  1.00 24.69           C
ANISOU 3814  CD1 LEU A 251     3004   2947   3431   -242   -404   -583       C
ATOM   3815  CD2 LEU A 251      22.804 -71.995 -46.507  1.00 25.29           C
ANISOU 3815  CD2 LEU A 251     3205   2800   3606   -327   -409   -554       C
ATOM   3816  H   LEU A 251      22.848 -72.453 -51.331  1.00  0.00           H
ATOM   3817  HA  LEU A 251      22.556 -69.817 -50.173  1.00  0.00           H
ATOM   3818  HB2 LEU A 251      23.230 -72.555 -49.063  1.00  0.00           H
ATOM   3819  HB3 LEU A 251      21.681 -71.700 -48.980  1.00  0.00           H
ATOM   3820  HG  LEU A 251      24.240 -70.849 -47.561  1.00  0.00           H
ATOM   3821 HD11 LEU A 251      22.749 -68.968 -48.114  1.00  0.00           H
ATOM   3822 HD12 LEU A 251      21.394 -69.812 -47.327  1.00  0.00           H
ATOM   3823 HD13 LEU A 251      22.790 -69.274 -46.361  1.00  0.00           H
ATOM   3824 HD21 LEU A 251      23.083 -71.595 -45.532  1.00  0.00           H
ATOM   3825 HD22 LEU A 251      23.340 -72.928 -46.683  1.00  0.00           H
ATOM   3826 HD23 LEU A 251      21.730 -72.183 -46.529  1.00  0.00           H
ATOM   3827  N   ILE A 252      24.863 -68.949 -49.748  1.00 18.55           N
ANISOU 3827  N   ILE A 252     2261   2144   2645    -42   -387   -692       N
ATOM   3828  CA  ILE A 252      26.141 -68.423 -49.306  1.00 18.16           C
ANISOU 3828  CA  ILE A 252     2208   2066   2626     44   -370   -650       C
ATOM   3829  C   ILE A 252      25.901 -68.195 -47.806  1.00 19.04           C
ANISOU 3829  C   ILE A 252     2306   2184   2745     20   -387   -567       C
ATOM   3830  O   ILE A 252      25.198 -67.267 -47.395  1.00 20.13           O
ANISOU 3830  O   ILE A 252     2398   2415   2834      6   -388   -539       O
ATOM   3831  CB  ILE A 252      26.522 -67.115 -50.024  1.00 18.25           C
ANISOU 3831  CB  ILE A 252     2179   2164   2592    111   -350   -661       C
ATOM   3832  CG1 ILE A 252      26.548 -67.322 -51.547  1.00 19.33           C
ANISOU 3832  CG1 ILE A 252     2343   2309   2694    124   -331   -743       C
ATOM   3833  CG2 ILE A 252      27.854 -66.576 -49.511  1.00 18.83           C
ANISOU 3833  CG2 ILE A 252     2238   2205   2713    189   -336   -617       C
ATOM   3834  CD1 ILE A 252      27.582 -68.372 -52.026  1.00 20.38           C
ANISOU 3834  CD1 ILE A 252     2532   2327   2887    157   -301   -787       C
ATOM   3835  H   ILE A 252      24.096 -68.307 -49.892  1.00  0.00           H
ATOM   3836  HA  ILE A 252      26.922 -69.169 -49.450  1.00  0.00           H
ATOM   3837  HB  ILE A 252      25.754 -66.375 -49.800  1.00  0.00           H
ATOM   3838 HG12 ILE A 252      26.786 -66.368 -52.018  1.00  0.00           H
ATOM   3839 HG13 ILE A 252      25.556 -67.635 -51.874  1.00  0.00           H
ATOM   3840 HG21 ILE A 252      28.099 -65.652 -50.035  1.00  0.00           H
ATOM   3841 HG22 ILE A 252      27.778 -66.378 -48.442  1.00  0.00           H
ATOM   3842 HG23 ILE A 252      28.637 -67.313 -49.689  1.00  0.00           H
ATOM   3843 HD11 ILE A 252      27.537 -68.458 -53.112  1.00  0.00           H
ATOM   3844 HD12 ILE A 252      28.583 -68.058 -51.728  1.00  0.00           H
ATOM   3845 HD13 ILE A 252      27.355 -69.338 -51.575  1.00  0.00           H
ATOM   3846  N   ALA A 253      26.463 -69.073 -46.992  1.00 19.52           N
ANISOU 3846  N   ALA A 253     2413   2140   2863     16   -400   -529       N
ATOM   3847  CA  ALA A 253      26.081 -69.147 -45.581  1.00 19.65           C
ANISOU 3847  CA  ALA A 253     2444   2150   2873    -26   -415   -452       C
ATOM   3848  C   ALA A 253      26.789 -68.121 -44.751  1.00 19.15           C
ANISOU 3848  C   ALA A 253     2360   2120   2797     35   -427   -397       C
ATOM   3849  O   ALA A 253      27.917 -67.761 -45.059  1.00 19.24           O
ANISOU 3849  O   ALA A 253     2358   2108   2843    112   -433   -404       O
ATOM   3850  CB  ALA A 253      26.392 -70.570 -45.035  1.00 20.01           C
ANISOU 3850  CB  ALA A 253     2565   2059   2980    -55   -432   -426       C
ATOM   3851  H   ALA A 253      27.167 -69.703 -47.350  1.00  0.00           H
ATOM   3852  HA  ALA A 253      25.008 -68.974 -45.504  1.00  0.00           H
ATOM   3853  HB1 ALA A 253      27.106 -71.065 -45.694  1.00  0.00           H
ATOM   3854  HB2 ALA A 253      26.817 -70.490 -44.034  1.00  0.00           H
ATOM   3855  HB3 ALA A 253      25.472 -71.152 -44.994  1.00  0.00           H
ATOM   3856  N   PRO A 254      26.150 -67.684 -43.655  1.00 20.52           N
ANISOU 3856  N   PRO A 254     2533   2340   2923     -1   -430   -342       N
ATOM   3857  CA  PRO A 254      26.824 -66.882 -42.649  1.00 20.31           C
ANISOU 3857  CA  PRO A 254     2510   2326   2882     46   -452   -287       C
ATOM   3858  C   PRO A 254      27.804 -67.742 -41.847  1.00 20.43           C
ANISOU 3858  C   PRO A 254     2590   2225   2949     66   -496   -236       C
ATOM   3859  O   PRO A 254      27.603 -68.961 -41.722  1.00 20.99           O
ANISOU 3859  O   PRO A 254     2714   2212   3049     23   -500   -225       O
ATOM   3860  CB  PRO A 254      25.680 -66.439 -41.738  1.00 20.01           C
ANISOU 3860  CB  PRO A 254     2470   2360   2771    -13   -431   -252       C
ATOM   3861  CG  PRO A 254      24.712 -67.579 -41.809  1.00 21.93           C
ANISOU 3861  CG  PRO A 254     2737   2572   3023   -102   -409   -257       C
ATOM   3862  CD  PRO A 254      24.800 -68.093 -43.214  1.00 22.76           C
ANISOU 3862  CD  PRO A 254     2821   2653   3172    -96   -409   -329       C
ATOM   3863  HA  PRO A 254      27.326 -66.025 -43.098  1.00  0.00           H
ATOM   3864  HB2 PRO A 254      25.225 -65.519 -42.104  1.00  0.00           H
ATOM   3865  HB3 PRO A 254      26.037 -66.306 -40.717  1.00  0.00           H
ATOM   3866  HG2 PRO A 254      24.990 -68.359 -41.100  1.00  0.00           H
ATOM   3867  HG3 PRO A 254      23.702 -67.226 -41.601  1.00  0.00           H
ATOM   3868  HD2 PRO A 254      24.033 -67.640 -43.842  1.00  0.00           H
ATOM   3869  HD3 PRO A 254      24.709 -69.179 -43.227  1.00  0.00           H
ATOM   3870  N   ARG A 255      28.813 -67.107 -41.274  1.00 18.90           N
ANISOU 3870  N   ARG A 255     2392   2023   2767    129   -534   -203       N
ATOM   3871  CA  ARG A 255      29.747 -67.799 -40.394  1.00 20.24           C
ANISOU 3871  CA  ARG A 255     2618   2091   2983    156   -594   -146       C
ATOM   3872  C   ARG A 255      29.464 -67.484 -38.942  1.00 21.16           C
ANISOU 3872  C   ARG A 255     2789   2226   3025    127   -624    -75       C
ATOM   3873  O   ARG A 255      30.119 -68.005 -38.047  1.00 22.26           O
ANISOU 3873  O   ARG A 255     2989   2288   3179    143   -685    -16       O
ATOM   3874  CB  ARG A 255      31.168 -67.401 -40.740  1.00 22.05           C
ANISOU 3874  CB  ARG A 255     2800   2290   3288    246   -629   -159       C
ATOM   3875  CG  ARG A 255      31.631 -67.915 -42.116  1.00 24.21           C
ANISOU 3875  CG  ARG A 255     3036   2523   3639    282   -592   -225       C
ATOM   3876  CD  ARG A 255      33.109 -67.773 -42.284  1.00 24.96           C
ANISOU 3876  CD  ARG A 255     3086   2568   3830    368   -622   -227       C
ATOM   3877  NE  ARG A 255      33.558 -68.285 -43.567  1.00 23.78           N
ANISOU 3877  NE  ARG A 255     2907   2379   3750    405   -571   -293       N
ATOM   3878  CZ  ARG A 255      34.023 -69.514 -43.764  1.00 23.59           C
ANISOU 3878  CZ  ARG A 255     2915   2244   3806    429   -577   -303       C
ATOM   3879  NH1 ARG A 255      34.124 -70.384 -42.770  1.00 24.51           N
ANISOU 3879  NH1 ARG A 255     3093   2271   3948    421   -639   -243       N
ATOM   3880  NH2 ARG A 255      34.415 -69.859 -44.952  1.00 23.46           N
ANISOU 3880  NH2 ARG A 255     2874   2199   3840    466   -520   -372       N
ATOM   3881  H   ARG A 255      28.939 -66.121 -41.450  1.00  0.00           H
ATOM   3882  HA  ARG A 255      29.639 -68.873 -40.546  1.00  0.00           H
ATOM   3883  HB2 ARG A 255      31.232 -66.313 -40.739  1.00  0.00           H
ATOM   3884  HB3 ARG A 255      31.838 -67.793 -39.975  1.00  0.00           H
ATOM   3885  HG2 ARG A 255      31.363 -68.968 -42.209  1.00  0.00           H
ATOM   3886  HG3 ARG A 255      31.126 -67.347 -42.898  1.00  0.00           H
ATOM   3887  HD2 ARG A 255      33.609 -68.326 -41.489  1.00  0.00           H
ATOM   3888  HD3 ARG A 255      33.377 -66.719 -42.208  1.00  0.00           H
ATOM   3889  HE  ARG A 255      33.514 -67.665 -44.363  1.00  0.00           H
ATOM   3890 HH11 ARG A 255      33.833 -70.123 -41.839  1.00  0.00           H
ATOM   3891 HH12 ARG A 255      34.492 -71.309 -42.944  1.00  0.00           H
ATOM   3892 HH21 ARG A 255      34.354 -69.200 -45.715  1.00  0.00           H
ATOM   3893 HH22 ARG A 255      34.781 -70.786 -45.113  1.00  0.00           H
ATOM   3894  N   GLY A 256      28.521 -66.583 -38.692  1.00 20.83           N
ANISOU 3894  N   GLY A 256     2728   2287   2899     92   -584    -81       N
ATOM   3895  CA  GLY A 256      28.298 -66.057 -37.343  1.00 20.15           C
ANISOU 3895  CA  GLY A 256     2695   2232   2729     74   -601    -26       C
ATOM   3896  C   GLY A 256      27.498 -64.758 -37.492  1.00 19.10           C
ANISOU 3896  C   GLY A 256     2506   2219   2533     69   -549    -62       C
ATOM   3897  O   GLY A 256      26.845 -64.592 -38.511  1.00 19.59           O
ANISOU 3897  O   GLY A 256     2504   2332   2607     57   -500   -114       O
ATOM   3898  H   GLY A 256      27.943 -66.252 -39.451  1.00  0.00           H
ATOM   3899  HA2 GLY A 256      27.734 -66.777 -36.750  1.00  0.00           H
ATOM   3900  HA3 GLY A 256      29.255 -65.850 -36.863  1.00  0.00           H
ATOM   3901  N   TYR A 257      27.538 -63.870 -36.506  1.00 17.92           N
ANISOU 3901  N   TYR A 257     2386   2110   2314     81   -564    -37       N
ATOM   3902  CA  TYR A 257      26.684 -62.660 -36.528  1.00 17.30           C
ANISOU 3902  CA  TYR A 257     2263   2136   2173     78   -509    -69       C
ATOM   3903  C   TYR A 257      27.486 -61.436 -36.107  1.00 18.92           C
ANISOU 3903  C   TYR A 257     2467   2360   2361    136   -554    -73       C
ATOM   3904  O   TYR A 257      28.517 -61.546 -35.434  1.00 20.83           O
ANISOU 3904  O   TYR A 257     2757   2543   2613    161   -629    -40       O
ATOM   3905  CB  TYR A 257      25.505 -62.809 -35.572  1.00 17.36           C
ANISOU 3905  CB  TYR A 257     2319   2184   2093     12   -451    -39       C
ATOM   3906  CG  TYR A 257      25.951 -62.902 -34.126  1.00 19.90           C
ANISOU 3906  CG  TYR A 257     2751   2466   2346      7   -493     22       C
ATOM   3907  CD1 TYR A 257      26.182 -64.146 -33.526  1.00 20.90           C
ANISOU 3907  CD1 TYR A 257     2964   2507   2471    -29   -522     83       C
ATOM   3908  CD2 TYR A 257      26.181 -61.763 -33.369  1.00 21.59           C
ANISOU 3908  CD2 TYR A 257     2992   2720   2492     41   -510     18       C
ATOM   3909  CE1 TYR A 257      26.594 -64.244 -32.204  1.00 22.13           C
ANISOU 3909  CE1 TYR A 257     3233   2627   2550    -32   -570    145       C
ATOM   3910  CE2 TYR A 257      26.598 -61.856 -32.056  1.00 22.88           C
ANISOU 3910  CE2 TYR A 257     3267   2848   2577     35   -557     71       C
ATOM   3911  CZ  TYR A 257      26.809 -63.106 -31.488  1.00 23.80           C
ANISOU 3911  CZ  TYR A 257     3471   2886   2687     -1   -590    136       C
ATOM   3912  OH  TYR A 257      27.209 -63.210 -30.185  1.00 25.71           O
ANISOU 3912  OH  TYR A 257     3837   3094   2840     -6   -645    194       O
ATOM   3913  H   TYR A 257      28.162 -64.022 -35.727  1.00  0.00           H
ATOM   3914  HA  TYR A 257      26.306 -62.508 -37.539  1.00  0.00           H
ATOM   3915  HB2 TYR A 257      24.851 -61.944 -35.683  1.00  0.00           H
ATOM   3916  HB3 TYR A 257      24.949 -63.710 -35.831  1.00  0.00           H
ATOM   3917  HD1 TYR A 257      26.037 -65.047 -34.103  1.00  0.00           H
ATOM   3918  HD2 TYR A 257      26.032 -60.790 -33.813  1.00  0.00           H
ATOM   3919  HE1 TYR A 257      26.742 -65.212 -31.749  1.00  0.00           H
ATOM   3920  HE2 TYR A 257      26.759 -60.961 -31.473  1.00  0.00           H
ATOM   3921  HH  TYR A 257      26.925 -64.055 -29.829  1.00  0.00           H
ATOM   3922  N   PHE A 258      26.991 -60.271 -36.508  1.00 18.23           N
ANISOU 3922  N   PHE A 258     2323   2351   2251    155   -513   -115       N
ATOM   3923  CA  PHE A 258      27.514 -58.991 -36.062  1.00 17.12           C
ANISOU 3923  CA  PHE A 258     2187   2232   2085    199   -542   -125       C
ATOM   3924  C   PHE A 258      26.707 -58.561 -34.866  1.00 16.65           C
ANISOU 3924  C   PHE A 258     2191   2215   1921    173   -509   -110       C
ATOM   3925  O   PHE A 258      25.471 -58.716 -34.838  1.00 18.50           O
ANISOU 3925  O   PHE A 258     2413   2502   2114    134   -431   -116       O
ATOM   3926  CB  PHE A 258      27.421 -57.954 -37.191  1.00 17.01           C
ANISOU 3926  CB  PHE A 258     2087   2269   2108    239   -512   -175       C
ATOM   3927  CG  PHE A 258      28.286 -58.291 -38.376  1.00 16.80           C
ANISOU 3927  CG  PHE A 258     2007   2204   2174    267   -532   -191       C
ATOM   3928  CD1 PHE A 258      27.836 -59.132 -39.357  1.00 16.90           C
ANISOU 3928  CD1 PHE A 258     1987   2217   2217    248   -498   -208       C
ATOM   3929  CD2 PHE A 258      29.582 -57.819 -38.444  1.00 16.35           C
ANISOU 3929  CD2 PHE A 258     1935   2104   2173    310   -586   -190       C
ATOM   3930  CE1 PHE A 258      28.664 -59.487 -40.442  1.00 16.56           C
ANISOU 3930  CE1 PHE A 258     1906   2134   2251    277   -507   -229       C
ATOM   3931  CE2 PHE A 258      30.388 -58.123 -39.520  1.00 16.13           C
ANISOU 3931  CE2 PHE A 258     1854   2042   2232    338   -588   -206       C
ATOM   3932  CZ  PHE A 258      29.934 -58.952 -40.518  1.00 16.73           C
ANISOU 3932  CZ  PHE A 258     1908   2120   2328    324   -545   -227       C
ATOM   3933  H   PHE A 258      26.214 -60.275 -37.154  1.00  0.00           H
ATOM   3934  HA  PHE A 258      28.557 -59.111 -35.768  1.00  0.00           H
ATOM   3935  HB2 PHE A 258      26.385 -57.896 -37.524  1.00  0.00           H
ATOM   3936  HB3 PHE A 258      27.721 -56.981 -36.801  1.00  0.00           H
ATOM   3937  HD1 PHE A 258      26.833 -59.529 -39.300  1.00  0.00           H
ATOM   3938  HD2 PHE A 258      29.969 -57.204 -37.645  1.00  0.00           H
ATOM   3939  HE1 PHE A 258      28.310 -60.167 -41.202  1.00  0.00           H
ATOM   3940  HE2 PHE A 258      31.383 -57.707 -39.579  1.00  0.00           H
ATOM   3941  HZ  PHE A 258      30.570 -59.184 -41.360  1.00  0.00           H
ATOM   3942  N   LYS A 259      27.394 -58.091 -33.837  1.00 16.23           N
ANISOU 3942  N   LYS A 259     2207   2137   1822    189   -568    -92       N
ATOM   3943  CA  LYS A 259      26.707 -57.616 -32.665  1.00 20.19           C
ANISOU 3943  CA  LYS A 259     2784   2676   2211    169   -533    -85       C
ATOM   3944  C   LYS A 259      26.135 -56.228 -32.994  1.00 22.16           C
ANISOU 3944  C   LYS A 259     2980   2994   2446    202   -479   -140       C
ATOM   3945  O   LYS A 259      26.848 -55.370 -33.443  1.00 28.23           O
ANISOU 3945  O   LYS A 259     3712   3752   3261    246   -520   -167       O
ATOM   3946  CB  LYS A 259      27.662 -57.554 -31.476  1.00 24.42           C
ANISOU 3946  CB  LYS A 259     3424   3160   2694    177   -626    -52       C
ATOM   3947  CG  LYS A 259      26.983 -57.152 -30.199  1.00 31.11           C
ANISOU 3947  CG  LYS A 259     4373   4042   3405    153   -587    -45       C
ATOM   3948  CD  LYS A 259      27.917 -57.278 -29.006  1.00 40.40           C
ANISOU 3948  CD  LYS A 259     5672   5163   4515    154   -694     -7       C
ATOM   3949  CE  LYS A 259      27.238 -56.767 -27.744  1.00 49.54           C
ANISOU 3949  CE  LYS A 259     6945   6360   5519    133   -646     -9       C
ATOM   3950  NZ  LYS A 259      28.118 -56.910 -26.544  1.00 55.49           N
ANISOU 3950  NZ  LYS A 259     7835   7061   6188    131   -762     30       N
ATOM   3951  H   LYS A 259      28.403 -58.066 -33.874  1.00  0.00           H
ATOM   3952  HA  LYS A 259      25.887 -58.295 -32.431  1.00  0.00           H
ATOM   3953  HB2 LYS A 259      28.445 -56.828 -31.697  1.00  0.00           H
ATOM   3954  HB3 LYS A 259      28.119 -58.534 -31.339  1.00  0.00           H
ATOM   3955  HG2 LYS A 259      26.118 -57.796 -30.040  1.00  0.00           H
ATOM   3956  HG3 LYS A 259      26.648 -56.118 -30.283  1.00  0.00           H
ATOM   3957  HD2 LYS A 259      28.186 -58.325 -28.870  1.00  0.00           H
ATOM   3958  HD3 LYS A 259      28.819 -56.695 -29.191  1.00  0.00           H
ATOM   3959  HE2 LYS A 259      26.323 -57.336 -27.580  1.00  0.00           H
ATOM   3960  HE3 LYS A 259      26.984 -55.715 -27.877  1.00  0.00           H
ATOM   3961  HZ1 LYS A 259      27.635 -56.562 -25.728  1.00  0.00           H
ATOM   3962  HZ2 LYS A 259      28.967 -56.381 -26.684  1.00  0.00           H
ATOM   3963  HZ3 LYS A 259      28.347 -57.884 -26.409  1.00  0.00           H
ATOM   3964  N  AMET A 260      24.841 -56.043 -32.794  0.50 20.79           N
ANISOU 3964  N  AMET A 260     2797   2885   2217    180   -383   -153       N
ATOM   3965  N  BMET A 260      24.859 -56.019 -32.734  0.50 20.81           N
ANISOU 3965  N  BMET A 260     2804   2887   2215    181   -385   -153       N
ATOM   3966  CA AMET A 260      24.208 -54.740 -33.023  0.50 20.95           C
ANISOU 3966  CA AMET A 260     2769   2966   2224    220   -330   -203       C
ATOM   3967  CA BMET A 260      24.231 -54.733 -33.038  0.50 20.69           C
ANISOU 3967  CA BMET A 260     2736   2932   2193    221   -331   -204       C
ATOM   3968  C  AMET A 260      24.354 -53.849 -31.798  0.50 20.86           C
ANISOU 3968  C  AMET A 260     2851   2954   2120    237   -336   -216       C
ATOM   3969  C  BMET A 260      24.162 -53.807 -31.836  0.50 20.94           C
ANISOU 3969  C  BMET A 260     2854   2975   2129    236   -321   -220       C
ATOM   3970  O  AMET A 260      24.247 -54.317 -30.657  0.50 21.71           O
ANISOU 3970  O  AMET A 260     3059   3052   2139    202   -330   -187       O
ATOM   3971  O  BMET A 260      23.720 -54.210 -30.753  0.50 21.85           O
ANISOU 3971  O  BMET A 260     3053   3097   2152    200   -284   -197       O
ATOM   3972  CB AMET A 260      22.725 -54.911 -33.342  0.50 22.72           C
ANISOU 3972  CB AMET A 260     2928   3263   2442    196   -225   -217       C
ATOM   3973  CB BMET A 260      22.841 -54.967 -33.585  0.50 22.75           C
ANISOU 3973  CB BMET A 260     2918   3261   2465    199   -235   -217       C
ATOM   3974  CG AMET A 260      22.426 -55.557 -34.687  0.50 23.34           C
ANISOU 3974  CG AMET A 260     2908   3354   2608    183   -220   -222       C
ATOM   3975  CG BMET A 260      22.858 -55.544 -34.962  0.50 23.93           C
ANISOU 3975  CG BMET A 260     2977   3409   2705    195   -250   -222       C
ATOM   3976  SD AMET A 260      22.639 -54.489 -36.154  0.50 28.10           S
ANISOU 3976  SD AMET A 260     3412   3979   3287    252   -242   -266       S
ATOM   3977  SD BMET A 260      21.223 -55.483 -35.719  0.50 24.48           S
ANISOU 3977  SD BMET A 260     2937   3569   2796    181   -159   -252       S
ATOM   3978  CE AMET A 260      21.676 -53.038 -35.747  0.50 32.09           C
ANISOU 3978  CE AMET A 260     3896   4550   3747    299   -176   -304       C
ATOM   3979  CE BMET A 260      21.013 -53.715 -35.925  0.50 33.87           C
ANISOU 3979  CE BMET A 260     4087   4802   3980    264   -143   -297       C
ATOM   3980  H  AMET A 260      24.275 -56.817 -32.476  0.50  0.00           H
ATOM   3981  H  BMET A 260      24.308 -56.757 -32.319  0.50  0.00           H
ATOM   3982  HA AMET A 260      24.696 -54.256 -33.869  0.50  0.00           H
ATOM   3983  HA BMET A 260      24.821 -54.242 -33.811  0.50  0.00           H
ATOM   3984  HB2AMET A 260      22.281 -55.531 -32.563  0.50  0.00           H
ATOM   3985  HB2BMET A 260      22.311 -54.015 -33.612  0.50  0.00           H
ATOM   3986  HB3AMET A 260      22.250 -53.930 -33.316  0.50  0.00           H
ATOM   3987  HB3BMET A 260      22.310 -55.649 -32.922  0.50  0.00           H
ATOM   3988  HG2AMET A 260      21.391 -55.898 -34.670  0.50  0.00           H
ATOM   3989  HG2BMET A 260      23.185 -56.582 -34.908  0.50  0.00           H
ATOM   3990  HG3AMET A 260      23.072 -56.428 -34.800  0.50  0.00           H
ATOM   3991  HG3BMET A 260      23.559 -54.980 -35.578  0.50  0.00           H
ATOM   3992  HE1AMET A 260      22.346 -52.207 -35.527  0.50  0.00           H
ATOM   3993  HE1BMET A 260      20.006 -53.508 -36.288  0.50  0.00           H
ATOM   3994  HE2AMET A 260      21.038 -52.777 -36.592  0.50  0.00           H
ATOM   3995  HE2BMET A 260      21.162 -53.218 -34.967  0.50  0.00           H
ATOM   3996  HE3AMET A 260      21.056 -53.246 -34.875  0.50  0.00           H
ATOM   3997  HE3BMET A 260      21.743 -53.344 -36.645  0.50  0.00           H
ATOM   3998  N   ARG A 261      24.605 -52.564 -32.034  1.00 19.99           N
ANISOU 3998  N   ARG A 261     2719   2849   2027    289   -349   -260       N
ATOM   3999  CA  ARG A 261      24.636 -51.565 -30.960  1.00 20.35           C
ANISOU 3999  CA  ARG A 261     2852   2894   1986    309   -348   -288       C
ATOM   4000  C   ARG A 261      23.724 -50.398 -31.340  1.00 20.76           C
ANISOU 4000  C   ARG A 261     2846   2996   2045    355   -267   -341       C
ATOM   4001  O   ARG A 261      23.386 -50.233 -32.520  1.00 18.09           O
ANISOU 4001  O   ARG A 261     2402   2683   1788    379   -245   -350       O
ATOM   4002  CB  ARG A 261      26.061 -51.058 -30.766  1.00 21.73           C
ANISOU 4002  CB  ARG A 261     3069   3002   2185    328   -466   -293       C
ATOM   4003  CG  ARG A 261      26.928 -52.131 -30.100  1.00 27.85           C
ANISOU 4003  CG  ARG A 261     3917   3725   2938    291   -555   -241       C
ATOM   4004  CD  ARG A 261      28.337 -51.670 -29.825  1.00 34.32           C
ANISOU 4004  CD  ARG A 261     4768   4483   3790    307   -682   -246       C
ATOM   4005  NE  ARG A 261      29.148 -52.813 -29.402  1.00 40.22           N
ANISOU 4005  NE  ARG A 261     5560   5180   4543    281   -773   -190       N
ATOM   4006  CZ  ARG A 261      29.229 -53.259 -28.152  1.00 43.25           C
ANISOU 4006  CZ  ARG A 261     6069   5547   4817    255   -816   -158       C
ATOM   4007  NH1 ARG A 261      28.554 -52.641 -27.183  1.00 45.99           N
ANISOU 4007  NH1 ARG A 261     6514   5926   5033    247   -767   -184       N
ATOM   4008  NH2 ARG A 261      29.991 -54.324 -27.866  1.00 41.67           N
ANISOU 4008  NH2 ARG A 261     5903   5294   4635    239   -907   -100       N
ATOM   4009  H  AARG A 261      24.780 -52.267 -32.983  0.50  0.00           H
ATOM   4010  H  BARG A 261      24.930 -52.302 -32.954  0.50  0.00           H
ATOM   4011  HA  ARG A 261      24.282 -52.016 -30.033  1.00  0.00           H
ATOM   4012  HB2 ARG A 261      26.487 -50.805 -31.737  1.00  0.00           H
ATOM   4013  HB3 ARG A 261      26.044 -50.168 -30.138  1.00  0.00           H
ATOM   4014  HG2 ARG A 261      26.465 -52.412 -29.154  1.00  0.00           H
ATOM   4015  HG3 ARG A 261      26.964 -53.006 -30.748  1.00  0.00           H
ATOM   4016  HD2 ARG A 261      28.326 -50.919 -29.035  1.00  0.00           H
ATOM   4017  HD3 ARG A 261      28.762 -51.238 -30.731  1.00  0.00           H
ATOM   4018  HE  ARG A 261      29.683 -53.297 -30.109  1.00  0.00           H
ATOM   4019 HH11 ARG A 261      27.982 -51.838 -27.400  1.00  0.00           H
ATOM   4020 HH12 ARG A 261      28.615 -52.976 -26.232  1.00  0.00           H
ATOM   4021 HH21 ARG A 261      30.503 -54.790 -28.601  1.00  0.00           H
ATOM   4022 HH22 ARG A 261      30.053 -54.660 -26.916  1.00  0.00           H
ATOM   4023  N   THR A 262      23.338 -49.590 -30.356  1.00 24.53           N
ANISOU 4023  N   THR A 262     3400   3487   2436    373   -226   -375       N
ATOM   4024  CA  THR A 262      22.674 -48.310 -30.664  1.00 26.84           C
ANISOU 4024  CA  THR A 262     3647   3807   2744    432   -166   -430       C
ATOM   4025  C   THR A 262      23.571 -47.213 -30.111  1.00 27.70           C
ANISOU 4025  C   THR A 262     3840   3857   2826    461   -234   -467       C
ATOM   4026  O   THR A 262      24.318 -47.433 -29.159  1.00 28.01           O
ANISOU 4026  O   THR A 262     3986   3857   2798    432   -300   -458       O
ATOM   4027  CB  THR A 262      21.278 -48.185 -30.032  1.00 31.16           C
ANISOU 4027  CB  THR A 262     4198   4420   3222    437    -36   -453       C
ATOM   4028  OG1 THR A 262      21.423 -48.134 -28.628  1.00 36.31           O
ANISOU 4028  OG1 THR A 262     4989   5056   3750    417    -26   -461       O
ATOM   4029  CG2 THR A 262      20.406 -49.367 -30.363  1.00 30.44           C
ANISOU 4029  CG2 THR A 262     4034   4382   3150    390     28   -414       C
ATOM   4030  H   THR A 262      23.500 -49.854 -29.395  1.00  0.00           H
ATOM   4031  HA  THR A 262      22.592 -48.198 -31.745  1.00  0.00           H
ATOM   4032  HB  THR A 262      20.800 -47.270 -30.382  1.00  0.00           H
ATOM   4033  HG1 THR A 262      21.977 -47.387 -28.390  1.00  0.00           H
ATOM   4034 HG21 THR A 262      19.429 -49.240 -29.898  1.00  0.00           H
ATOM   4035 HG22 THR A 262      20.871 -50.278 -29.987  1.00  0.00           H
ATOM   4036 HG23 THR A 262      20.287 -49.439 -31.444  1.00  0.00           H
ATOM   4037  N   GLY A 263      23.521 -46.029 -30.697  1.00 28.40           N
ANISOU 4037  N   GLY A 263     3886   3934   2970    517   -227   -507       N
ATOM   4038  CA  GLY A 263      24.381 -44.944 -30.223  1.00 27.40           C
ANISOU 4038  CA  GLY A 263     3837   3743   2832    537   -294   -547       C
ATOM   4039  C   GLY A 263      24.503 -43.873 -31.296  1.00 25.82           C
ANISOU 4039  C   GLY A 263     3562   3517   2731    589   -300   -568       C
ATOM   4040  O   GLY A 263      23.610 -43.732 -32.131  1.00 26.46           O
ANISOU 4040  O   GLY A 263     3554   3642   2857    625   -231   -566       O
ATOM   4041  H   GLY A 263      22.890 -45.874 -31.470  1.00  0.00           H
ATOM   4042  HA2 GLY A 263      23.948 -44.506 -29.324  1.00  0.00           H
ATOM   4043  HA3 GLY A 263      25.370 -45.340 -29.993  1.00  0.00           H
ATOM   4044  N   LYS A 264      25.611 -43.147 -31.281  1.00 24.15           N
ANISOU 4044  N   LYS A 264     3387   3232   2556    589   -386   -583       N
ATOM   4045  CA  LYS A 264      25.737 -41.941 -32.085  1.00 24.21           C
ANISOU 4045  CA  LYS A 264     3354   3201   2643    636   -386   -606       C
ATOM   4046  C   LYS A 264      26.473 -42.152 -33.409  1.00 19.28           C
ANISOU 4046  C   LYS A 264     2636   2558   2131    627   -429   -562       C
ATOM   4047  O   LYS A 264      26.829 -41.176 -34.030  1.00 19.00           O
ANISOU 4047  O   LYS A 264     2582   2476   2161    653   -442   -571       O
ATOM   4048  CB  LYS A 264      26.523 -40.890 -31.280  1.00 30.58           C
ANISOU 4048  CB  LYS A 264     4262   3929   3430    634   -449   -656       C
ATOM   4049  CG  LYS A 264      25.871 -40.528 -29.928  1.00 39.32           C
ANISOU 4049  CG  LYS A 264     5484   5044   4411    646   -405   -713       C
ATOM   4050  CD  LYS A 264      26.813 -39.692 -29.031  1.00 46.90           C
ANISOU 4050  CD  LYS A 264     6560   5921   5338    627   -494   -765       C
ATOM   4051  CE  LYS A 264      26.138 -39.321 -27.695  1.00 54.08           C
ANISOU 4051  CE  LYS A 264     7585   6839   6124    631   -433   -810       C
ATOM   4052  NZ  LYS A 264      26.995 -38.414 -26.860  1.00 59.17           N
ANISOU 4052  NZ  LYS A 264     8325   7403   6755    599   -510   -845       N
ATOM   4053  H   LYS A 264      26.384 -43.437 -30.699  1.00  0.00           H
ATOM   4054  HA  LYS A 264      24.741 -41.552 -32.294  1.00  0.00           H
ATOM   4055  HB2 LYS A 264      26.598 -39.983 -31.880  1.00  0.00           H
ATOM   4056  HB3 LYS A 264      27.527 -41.271 -31.094  1.00  0.00           H
ATOM   4057  HG2 LYS A 264      24.965 -39.952 -30.118  1.00  0.00           H
ATOM   4058  HG3 LYS A 264      25.605 -41.446 -29.405  1.00  0.00           H
ATOM   4059  HD2 LYS A 264      27.712 -40.272 -28.824  1.00  0.00           H
ATOM   4060  HD3 LYS A 264      27.090 -38.779 -29.557  1.00  0.00           H
ATOM   4061  HE2 LYS A 264      25.944 -40.235 -27.134  1.00  0.00           H
ATOM   4062  HE3 LYS A 264      25.191 -38.823 -27.902  1.00  0.00           H
ATOM   4063  HZ1 LYS A 264      26.516 -38.197 -25.998  1.00  0.00           H
ATOM   4064  HZ2 LYS A 264      27.176 -37.560 -27.368  1.00  0.00           H
ATOM   4065  HZ3 LYS A 264      27.870 -38.874 -26.653  1.00  0.00           H
ATOM   4066  N   SER A 265      26.738 -43.395 -33.828  1.00 14.87           N
ANISOU 4066  N   SER A 265     2027   2028   1594    590   -448   -514       N
ATOM   4067  CA  SER A 265      27.566 -43.621 -35.012  1.00 14.71           C
ANISOU 4067  CA  SER A 265     1930   1985   1674    581   -485   -478       C
ATOM   4068  C   SER A 265      26.866 -43.288 -36.310  1.00 14.51           C
ANISOU 4068  C   SER A 265     1826   1992   1695    623   -425   -467       C
ATOM   4069  O   SER A 265      25.638 -43.417 -36.431  1.00 15.35           O
ANISOU 4069  O   SER A 265     1907   2160   1767    649   -358   -473       O
ATOM   4070  CB  SER A 265      28.114 -45.057 -35.057  1.00 15.69           C
ANISOU 4070  CB  SER A 265     2032   2120   1810    535   -524   -438       C
ATOM   4071  OG  SER A 265      28.815 -45.286 -33.851  1.00 15.44           O
ANISOU 4071  OG  SER A 265     2079   2053   1734    502   -596   -443       O
ATOM   4072  H   SER A 265      26.363 -44.184 -33.322  1.00  0.00           H
ATOM   4073  HA  SER A 265      28.425 -42.954 -34.933  1.00  0.00           H
ATOM   4074  HB2 SER A 265      27.291 -45.766 -35.149  1.00  0.00           H
ATOM   4075  HB3 SER A 265      28.791 -45.167 -35.904  1.00  0.00           H
ATOM   4076  HG  SER A 265      29.718 -44.974 -33.941  1.00  0.00           H
ATOM   4077  N   SER A 266      27.666 -42.904 -37.305  1.00 13.76           N
ANISOU 4077  N   SER A 266     1690   1858   1682    626   -449   -448       N
ATOM   4078  CA  SER A 266      27.138 -42.652 -38.619  1.00 13.27           C
ANISOU 4078  CA  SER A 266     1565   1822   1655    663   -404   -428       C
ATOM   4079  C   SER A 266      28.219 -42.866 -39.656  1.00 12.41           C
ANISOU 4079  C   SER A 266     1421   1678   1616    623   -419   -389       C
ATOM   4080  O   SER A 266      29.279 -43.432 -39.364  1.00 13.67           O
ANISOU 4080  O   SER A 266     1579   1806   1809    588   -468   -382       O
ATOM   4081  CB  SER A 266      26.562 -41.227 -38.698  1.00 15.53           C
ANISOU 4081  CB  SER A 266     1873   2086   1942    720   -374   -451       C
ATOM   4082  OG  SER A 266      25.882 -41.033 -39.929  1.00 16.58           O
ANISOU 4082  OG  SER A 266     1965   2249   2085    714   -323   -409       O
ATOM   4083  H   SER A 266      28.655 -42.789 -37.134  1.00  0.00           H
ATOM   4084  HA  SER A 266      26.332 -43.361 -38.809  1.00  0.00           H
ATOM   4085  HB2 SER A 266      27.376 -40.506 -38.621  1.00  0.00           H
ATOM   4086  HB3 SER A 266      25.866 -41.074 -37.874  1.00  0.00           H
ATOM   4087  HG  SER A 266      24.992 -41.388 -39.863  1.00  0.00           H
ATOM   4088  N   ILE A 267      27.924 -42.463 -40.879  1.00 11.89           N
ANISOU 4088  N   ILE A 267     1334   1620   1566    617   -368   -356       N
ATOM   4089  CA  ILE A 267      28.839 -42.645 -42.001  1.00 13.08           C
ANISOU 4089  CA  ILE A 267     1459   1745   1768    579   -356   -315       C
ATOM   4090  C   ILE A 267      28.767 -41.396 -42.869  1.00 13.96           C
ANISOU 4090  C   ILE A 267     1576   1827   1900    605   -328   -294       C
ATOM   4091  O   ILE A 267      27.734 -40.703 -42.900  1.00 14.21           O
ANISOU 4091  O   ILE A 267     1623   1877   1900    641   -307   -299       O
ATOM   4092  CB  ILE A 267      28.495 -43.945 -42.807  1.00 10.70           C
ANISOU 4092  CB  ILE A 267     1128   1492   1447    548   -325   -291       C
ATOM   4093  CG1 ILE A 267      29.521 -44.170 -43.903  1.00 11.35           C
ANISOU 4093  CG1 ILE A 267     1187   1548   1578    524   -309   -259       C
ATOM   4094  CG2 ILE A 267      27.078 -43.856 -43.459  1.00 11.63           C
ANISOU 4094  CG2 ILE A 267     1237   1664   1517    568   -286   -284       C
ATOM   4095  CD1 ILE A 267      29.581 -45.645 -44.447  1.00 11.86           C
ANISOU 4095  CD1 ILE A 267     1230   1639   1636    494   -295   -250       C
ATOM   4096  H   ILE A 267      27.035 -42.013 -41.043  1.00  0.00           H
ATOM   4097  HA  ILE A 267      29.852 -42.737 -41.610  1.00  0.00           H
ATOM   4098  HB  ILE A 267      28.516 -44.796 -42.126  1.00  0.00           H
ATOM   4099 HG12 ILE A 267      29.280 -43.510 -44.736  1.00  0.00           H
ATOM   4100 HG13 ILE A 267      30.505 -43.901 -43.519  1.00  0.00           H
ATOM   4101 HG21 ILE A 267      26.330 -43.694 -42.683  1.00  0.00           H
ATOM   4102 HG22 ILE A 267      27.055 -43.026 -44.165  1.00  0.00           H
ATOM   4103 HG23 ILE A 267      26.861 -44.786 -43.985  1.00  0.00           H
ATOM   4104 HD11 ILE A 267      29.196 -46.328 -43.690  1.00  0.00           H
ATOM   4105 HD12 ILE A 267      30.614 -45.905 -44.679  1.00  0.00           H
ATOM   4106 HD13 ILE A 267      28.975 -45.724 -45.350  1.00  0.00           H
ATOM   4107  N   MET A 268      29.861 -41.061 -43.554  1.00 14.63           N
ANISOU 4107  N   MET A 268     1647   1864   2046    591   -327   -270       N
ATOM   4108  CA  MET A 268      29.892 -39.872 -44.394  1.00 15.31           C
ANISOU 4108  CA  MET A 268     1745   1914   2158    621   -302   -244       C
ATOM   4109  C   MET A 268      30.779 -40.154 -45.600  1.00 14.67           C
ANISOU 4109  C   MET A 268     1633   1820   2121    607   -274   -206       C
ATOM   4110  O   MET A 268      31.784 -40.855 -45.476  1.00 15.87           O
ANISOU 4110  O   MET A 268     1753   1959   2317    572   -287   -210       O
ATOM   4111  CB  MET A 268      30.428 -38.682 -43.572  1.00 17.94           C
ANISOU 4111  CB  MET A 268     2111   2167   2539    639   -340   -273       C
ATOM   4112  CG  MET A 268      30.482 -37.368 -44.337  1.00 21.54           C
ANISOU 4112  CG  MET A 268     2591   2563   3031    673   -315   -246       C
ATOM   4113  SD  MET A 268      31.089 -35.987 -43.300  1.00 20.26           S
ANISOU 4113  SD  MET A 268     2481   2282   2934    684   -366   -291       S
ATOM   4114  CE  MET A 268      29.732 -35.891 -42.127  1.00 18.72           C
ANISOU 4114  CE  MET A 268     2331   2132   2650    722   -371   -343       C
ATOM   4115  H   MET A 268      30.684 -41.643 -43.489  1.00  0.00           H
ATOM   4116  HA  MET A 268      28.882 -39.647 -44.736  1.00  0.00           H
ATOM   4117  HB2 MET A 268      29.781 -38.546 -42.706  1.00  0.00           H
ATOM   4118  HB3 MET A 268      31.432 -38.924 -43.223  1.00  0.00           H
ATOM   4119  HG2 MET A 268      29.480 -37.127 -44.691  1.00  0.00           H
ATOM   4120  HG3 MET A 268      31.143 -37.484 -45.196  1.00  0.00           H
ATOM   4121  HE1 MET A 268      29.928 -35.095 -41.408  1.00  0.00           H
ATOM   4122  HE2 MET A 268      29.639 -36.841 -41.601  1.00  0.00           H
ATOM   4123  HE3 MET A 268      28.805 -35.679 -42.660  1.00  0.00           H
ATOM   4124  N   ARG A 269      30.426 -39.608 -46.773  1.00 12.92           N
ANISOU 4124  N   ARG A 269     1420   1601   1889    640   -238   -172       N
ATOM   4125  CA  ARG A 269      31.288 -39.690 -47.942  1.00 13.50           C
ANISOU 4125  CA  ARG A 269     1472   1656   2003    646   -205   -140       C
ATOM   4126  C   ARG A 269      32.127 -38.389 -48.005  1.00 14.74           C
ANISOU 4126  C   ARG A 269     1643   1717   2242    668   -206   -129       C
ATOM   4127  O   ARG A 269      31.580 -37.308 -48.000  1.00 15.04           O
ANISOU 4127  O   ARG A 269     1726   1720   2268    705   -209   -119       O
ATOM   4128  CB  ARG A 269      30.470 -39.829 -49.218  1.00 13.74           C
ANISOU 4128  CB  ARG A 269     1515   1735   1969    680   -175   -112       C
ATOM   4129  CG  ARG A 269      29.545 -41.102 -49.229  1.00 14.40           C
ANISOU 4129  CG  ARG A 269     1587   1901   1984    655   -184   -131       C
ATOM   4130  CD  ARG A 269      28.816 -41.267 -50.588  1.00 15.65           C
ANISOU 4130  CD  ARG A 269     1758   2109   2078    692   -170   -111       C
ATOM   4131  NE  ARG A 269      27.943 -42.429 -50.585  1.00 14.92           N
ANISOU 4131  NE  ARG A 269     1651   2084   1932    668   -186   -136       N
ATOM   4132  CZ  ARG A 269      26.674 -42.406 -50.199  1.00 16.08           C
ANISOU 4132  CZ  ARG A 269     1800   2268   2042    669   -207   -149       C
ATOM   4133  NH1 ARG A 269      26.125 -41.277 -49.802  1.00 16.51           N
ANISOU 4133  NH1 ARG A 269     1869   2302   2101    696   -214   -140       N
ATOM   4134  NH2 ARG A 269      25.951 -43.515 -50.214  1.00 17.34           N
ANISOU 4134  NH2 ARG A 269     1941   2482   2165    646   -218   -173       N
ATOM   4135  H   ARG A 269      29.540 -39.128 -46.847  1.00  0.00           H
ATOM   4136  HA  ARG A 269      31.954 -40.547 -47.843  1.00  0.00           H
ATOM   4137  HB2 ARG A 269      29.842 -38.944 -49.324  1.00  0.00           H
ATOM   4138  HB3 ARG A 269      31.150 -39.881 -50.068  1.00  0.00           H
ATOM   4139  HG2 ARG A 269      28.801 -41.005 -48.438  1.00  0.00           H
ATOM   4140  HG3 ARG A 269      30.153 -41.987 -49.041  1.00  0.00           H
ATOM   4141  HD2 ARG A 269      28.219 -40.376 -50.780  1.00  0.00           H
ATOM   4142  HD3 ARG A 269      29.557 -41.379 -51.380  1.00  0.00           H
ATOM   4143  HE  ARG A 269      28.327 -43.310 -50.897  1.00  0.00           H
ATOM   4144 HH11 ARG A 269      25.158 -41.261 -49.510  1.00  0.00           H
ATOM   4145 HH12 ARG A 269      26.671 -40.427 -49.790  1.00  0.00           H
ATOM   4146 HH21 ARG A 269      24.985 -43.492 -49.921  1.00  0.00           H
ATOM   4147 HH22 ARG A 269      26.366 -44.384 -50.519  1.00  0.00           H
ATOM   4148  N   SER A 270      33.433 -38.507 -48.061  1.00 16.15           N
ANISOU 4148  N   SER A 270     1784   1848   2505    622   -196   -125       N
ATOM   4149  CA  SER A 270      34.295 -37.328 -48.094  1.00 18.26           C
ANISOU 4149  CA  SER A 270     2065   2020   2853    591   -181   -102       C
ATOM   4150  C   SER A 270      35.637 -37.751 -48.626  1.00 21.34           C
ANISOU 4150  C   SER A 270     2395   2389   3326    536   -137    -82       C
ATOM   4151  O   SER A 270      36.087 -38.868 -48.340  1.00 20.75           O
ANISOU 4151  O   SER A 270     2262   2350   3273    517   -153   -107       O
ATOM   4152  CB  SER A 270      34.499 -36.772 -46.677  1.00 17.28           C
ANISOU 4152  CB  SER A 270     1953   1841   2771    570   -252   -148       C
ATOM   4153  OG  SER A 270      35.365 -35.639 -46.717  1.00 19.06           O
ANISOU 4153  OG  SER A 270     2190   1967   3085    529   -242   -130       O
ATOM   4154  H   SER A 270      33.849 -39.427 -48.082  1.00  0.00           H
ATOM   4155  HA  SER A 270      33.860 -36.563 -48.738  1.00  0.00           H
ATOM   4156  HB2 SER A 270      34.943 -37.543 -46.047  1.00  0.00           H
ATOM   4157  HB3 SER A 270      33.535 -36.476 -46.262  1.00  0.00           H
ATOM   4158  HG  SER A 270      34.871 -34.868 -47.005  1.00  0.00           H
ATOM   4159  N   ASP A 271      36.297 -36.854 -49.352  1.00 23.37           N
ANISOU 4159  N   ASP A 271     2663   2581   3637    510    -79    -37       N
ATOM   4160  CA  ASP A 271      37.696 -37.043 -49.682  1.00 24.63           C
ANISOU 4160  CA  ASP A 271     2751   2704   3903    449    -33    -22       C
ATOM   4161  C   ASP A 271      38.627 -36.127 -48.870  1.00 25.85           C
ANISOU 4161  C   ASP A 271     2881   2763   4179    389    -72    -33       C
ATOM   4162  O   ASP A 271      39.822 -36.050 -49.161  1.00 26.97           O
ANISOU 4162  O   ASP A 271     2956   2863   4430    332    -31    -16       O
ATOM   4163  CB  ASP A 271      37.917 -36.878 -51.188  1.00 26.46           C
ANISOU 4163  CB  ASP A 271     3002   2937   4113    450     79     39       C
ATOM   4164  CG  ASP A 271      37.419 -38.095 -51.988  1.00 30.19           C
ANISOU 4164  CG  ASP A 271     3476   3505   4492    489    116     36       C
ATOM   4165  OD1 ASP A 271      37.276 -39.184 -51.394  1.00 29.96           O
ANISOU 4165  OD1 ASP A 271     3403   3526   4454    498     67    -11       O
ATOM   4166  OD2 ASP A 271      37.172 -37.966 -53.206  1.00 33.55           O
ANISOU 4166  OD2 ASP A 271     3951   3948   4847    509    191     80       O
ATOM   4167  H   ASP A 271      35.816 -36.028 -49.679  1.00  0.00           H
ATOM   4168  HA  ASP A 271      37.952 -38.072 -49.428  1.00  0.00           H
ATOM   4169  HB2 ASP A 271      37.379 -35.992 -51.526  1.00  0.00           H
ATOM   4170  HB3 ASP A 271      38.982 -36.740 -51.377  1.00  0.00           H
ATOM   4171  N   ALA A 272      38.107 -35.475 -47.824  1.00 23.87           N
ANISOU 4171  N   ALA A 272     2678   2478   3912    399   -153    -68       N
ATOM   4172  CA  ALA A 272      38.934 -34.587 -47.011  1.00 22.28           C
ANISOU 4172  CA  ALA A 272     2465   2182   3818    339   -204    -89       C
ATOM   4173  C   ALA A 272      39.973 -35.359 -46.202  1.00 21.65           C
ANISOU 4173  C   ALA A 272     2292   2107   3828    288   -268   -127       C
ATOM   4174  O   ALA A 272      39.653 -36.359 -45.592  1.00 20.24           O
ANISOU 4174  O   ALA A 272     2099   1992   3599    314   -322   -161       O
ATOM   4175  CB  ALA A 272      38.052 -33.753 -46.044  1.00 18.72           C
ANISOU 4175  CB  ALA A 272     2104   1696   3314    371   -274   -129       C
ATOM   4176  H   ALA A 272      37.131 -35.598 -47.594  1.00  0.00           H
ATOM   4177  HA  ALA A 272      39.458 -33.901 -47.676  1.00  0.00           H
ATOM   4178  HB1 ALA A 272      38.686 -33.098 -45.447  1.00  0.00           H
ATOM   4179  HB2 ALA A 272      37.501 -34.424 -45.385  1.00  0.00           H
ATOM   4180  HB3 ALA A 272      37.349 -33.152 -46.621  1.00  0.00           H
ATOM   4181  N   PRO A 273      41.221 -34.854 -46.133  1.00 24.41           N
ANISOU 4181  N   PRO A 273     2577   2382   4317    214   -271   -121       N
ATOM   4182  CA  PRO A 273      42.182 -35.552 -45.267  1.00 25.25           C
ANISOU 4182  CA  PRO A 273     2589   2490   4514    172   -356   -159       C
ATOM   4183  C   PRO A 273      41.770 -35.436 -43.820  1.00 25.26           C
ANISOU 4183  C   PRO A 273     2646   2482   4468    177   -487   -220       C
ATOM   4184  O   PRO A 273      41.065 -34.479 -43.438  1.00 26.91           O
ANISOU 4184  O   PRO A 273     2953   2650   4621    191   -507   -238       O
ATOM   4185  CB  PRO A 273      43.532 -34.816 -45.516  1.00 28.61           C
ANISOU 4185  CB  PRO A 273     2932   2830   5109     86   -333   -140       C
ATOM   4186  CG  PRO A 273      43.250 -33.666 -46.316  1.00 29.76           C
ANISOU 4186  CG  PRO A 273     3145   2917   5245     77   -247    -95       C
ATOM   4187  CD  PRO A 273      41.820 -33.740 -46.882  1.00 27.69           C
ANISOU 4187  CD  PRO A 273     2992   2711   4816    165   -197    -74       C
ATOM   4188  HA  PRO A 273      42.262 -36.600 -45.556  1.00  0.00           H
ATOM   4189  HB2 PRO A 273      44.224 -35.474 -46.041  1.00  0.00           H
ATOM   4190  HB3 PRO A 273      43.966 -34.507 -44.565  1.00  0.00           H
ATOM   4191  HG2 PRO A 273      43.347 -32.770 -45.703  1.00  0.00           H
ATOM   4192  HG3 PRO A 273      43.962 -33.617 -47.140  1.00  0.00           H
ATOM   4193  HD2 PRO A 273      41.833 -33.950 -47.951  1.00  0.00           H
ATOM   4194  HD3 PRO A 273      41.282 -32.813 -46.682  1.00  0.00           H
ATOM   4195  N  AILE A 274      42.266 -36.354 -43.000  0.62 25.00           N
ANISOU 4195  N  AILE A 274     2556   2479   4462    166   -575   -252       N
ATOM   4196  N  BILE A 274      42.117 -36.449 -43.050  0.38 24.79           N
ANISOU 4196  N  BILE A 274     2537   2464   4419    176   -569   -251       N
ATOM   4197  CA AILE A 274      42.004 -36.395 -41.564  0.62 27.02           C
ANISOU 4197  CA AILE A 274     2868   2732   4667    166   -705   -309       C
ATOM   4198  CA BILE A 274      41.950 -36.409 -41.623  0.38 26.66           C
ANISOU 4198  CA BILE A 274     2823   2689   4616    170   -698   -306       C
ATOM   4199  C  AILE A 274      43.216 -35.934 -40.739  0.62 30.39           C
ANISOU 4199  C  AILE A 274     3240   3085   5222     89   -814   -339       C
ATOM   4200  C  BILE A 274      43.154 -35.636 -41.108  0.38 30.03           C
ANISOU 4200  C  BILE A 274     3200   3027   5184     88   -774   -327       C
ATOM   4201  O  AILE A 274      44.247 -36.610 -40.711  0.62 31.89           O
ANISOU 4201  O  AILE A 274     3316   3281   5518     59   -851   -332       O
ATOM   4202  O  BILE A 274      44.164 -35.494 -41.810  0.38 32.14           O
ANISOU 4202  O  BILE A 274     3365   3262   5587     40   -727   -295       O
ATOM   4203  CB AILE A 274      41.644 -37.792 -41.119  0.62 27.77           C
ANISOU 4203  CB AILE A 274     2955   2911   4687    208   -744   -318       C
ATOM   4204  CB BILE A 274      41.919 -37.813 -41.016  0.38 28.13           C
ANISOU 4204  CB BILE A 274     2981   2947   4759    196   -762   -321       C
ATOM   4205  CG1AILE A 274      40.267 -38.178 -41.649  0.62 27.44           C
ANISOU 4205  CG1AILE A 274     2981   2940   4505    278   -665   -304       C
ATOM   4206  CG1BILE A 274      40.884 -38.696 -41.726  0.38 27.45           C
ANISOU 4206  CG1BILE A 274     2921   2946   4562    263   -676   -296       C
ATOM   4207  CG2AILE A 274      41.668 -37.898 -39.603  0.62 28.93           C
ANISOU 4207  CG2AILE A 274     3151   3048   4794    195   -884   -370       C
ATOM   4208  CG2BILE A 274      41.619 -37.755 -39.533  0.38 28.93           C
ANISOU 4208  CG2BILE A 274     3161   3041   4789    193   -888   -374       C
ATOM   4209  CD1AILE A 274      40.030 -39.656 -41.609  0.62 27.94           C
ANISOU 4209  CD1AILE A 274     3016   3081   4520    310   -670   -299       C
ATOM   4210  CD1BILE A 274      39.491 -38.091 -41.829  0.38 26.34           C
ANISOU 4210  CD1BILE A 274     2890   2825   4294    310   -631   -302       C
ATOM   4211  H  AILE A 274      42.862 -37.069 -43.393  0.62  0.00           H
ATOM   4212  H  BILE A 274      42.511 -37.276 -43.475  0.38  0.00           H
ATOM   4213  HA AILE A 274      41.165 -35.735 -41.346  0.62  0.00           H
ATOM   4214  HA BILE A 274      41.033 -35.876 -41.372  0.38  0.00           H
ATOM   4215  HB AILE A 274      42.379 -38.486 -41.527  0.62  0.00           H
ATOM   4216  HB BILE A 274      42.902 -38.265 -41.149  0.38  0.00           H
ATOM   4217 HG12AILE A 274      39.508 -37.686 -41.041  0.62  0.00           H
ATOM   4218 HG12BILE A 274      40.806 -39.635 -41.177  0.38  0.00           H
ATOM   4219 HG13AILE A 274      40.174 -37.832 -42.679  0.62  0.00           H
ATOM   4220 HG13BILE A 274      41.244 -38.911 -42.732  0.38  0.00           H
ATOM   4221 HD11AILE A 274      39.089 -39.887 -42.108  0.62  0.00           H
ATOM   4222 HD11BILE A 274      39.040 -38.376 -42.780  0.38  0.00           H
ATOM   4223 HD12AILE A 274      40.847 -40.169 -42.118  0.62  0.00           H
ATOM   4224 HD12BILE A 274      38.874 -38.459 -41.010  0.38  0.00           H
ATOM   4225 HD13AILE A 274      39.982 -39.988 -40.572  0.62  0.00           H
ATOM   4226 HD13BILE A 274      39.561 -37.005 -41.771  0.38  0.00           H
ATOM   4227 HG21AILE A 274      42.548 -37.384 -39.216  0.62  0.00           H
ATOM   4228 HG21BILE A 274      41.316 -36.744 -39.262  0.38  0.00           H
ATOM   4229 HG22AILE A 274      40.769 -37.437 -39.193  0.62  0.00           H
ATOM   4230 HG22BILE A 274      40.813 -38.451 -39.298  0.38  0.00           H
ATOM   4231 HG23AILE A 274      41.703 -38.948 -39.313  0.62  0.00           H
ATOM   4232 HG23BILE A 274      42.512 -38.029 -38.971  0.38  0.00           H
ATOM   4233  N  AASP A 275      43.056 -34.790 -40.065  0.62 32.61           N
ANISOU 4233  N  AASP A 275     3603   3295   5492     62   -870   -378       N
ATOM   4234  N  BASP A 275      43.045 -35.115 -39.895  0.38 32.46           N
ANISOU 4234  N  BASP A 275     3578   3295   5459     69   -888   -382       N
ATOM   4235  CA AASP A 275      44.114 -34.106 -39.322  0.62 34.23           C
ANISOU 4235  CA AASP A 275     3776   3416   5816    -20   -977   -414       C
ATOM   4236  CA BASP A 275      44.192 -34.519 -39.258  0.38 33.95           C
ANISOU 4236  CA BASP A 275     3718   3405   5778    -13   -989   -412       C
ATOM   4237  C  AASP A 275      43.996 -34.366 -37.813  0.62 34.18           C
ANISOU 4237  C  AASP A 275     3836   3418   5735    -21  -1131   -479       C
ATOM   4238  C  BASP A 275      44.024 -34.510 -37.763  0.38 34.36           C
ANISOU 4238  C  BASP A 275     3852   3448   5755    -19  -1138   -479       C
ATOM   4239  O  AASP A 275      42.959 -34.828 -37.327  0.62 32.89           O
ANISOU 4239  O  AASP A 275     3765   3312   5418     41  -1136   -496       O
ATOM   4240  O  BASP A 275      42.976 -34.881 -37.230  0.38 32.95           O
ANISOU 4240  O  BASP A 275     3775   3322   5423     41  -1146   -500       O
ATOM   4241  CB AASP A 275      44.011 -32.607 -39.607  0.62 34.99           C
ANISOU 4241  CB AASP A 275     3935   3414   5947    -55   -935   -417       C
ATOM   4242  CB BASP A 275      44.448 -33.116 -39.787  0.38 35.67           C
ANISOU 4242  CB BASP A 275     3953   3525   6078    -64   -934   -402       C
ATOM   4243  CG AASP A 275      45.296 -31.836 -39.306  0.62 35.98           C
ANISOU 4243  CG AASP A 275     3990   3439   6240   -159  -1008   -437       C
ATOM   4244  CG BASP A 275      45.060 -33.128 -41.169  0.38 38.77           C
ANISOU 4244  CG BASP A 275     4239   3911   6579    -86   -804   -333       C
ATOM   4245  OD1AASP A 275      46.368 -32.468 -39.111  0.62 36.76           O
ANISOU 4245  OD1AASP A 275     3962   3554   6449   -202  -1071   -434       O
ATOM   4246  OD1BASP A 275      45.949 -33.968 -41.436  0.38 37.27           O
ANISOU 4246  OD1BASP A 275     3918   3755   6486   -106   -802   -313       O
ATOM   4247  OD2AASP A 275      45.210 -30.579 -39.271  0.62 34.89           O
ANISOU 4247  OD2AASP A 275     3924   3206   6128   -195  -1002   -454       O
ATOM   4248  OD2BASP A 275      44.638 -32.308 -42.004  0.38 42.62           O
ANISOU 4248  OD2BASP A 275     4780   4360   7052    -80   -699   -297       O
ATOM   4249  H  AASP A 275      42.138 -34.368 -40.069  0.62  0.00           H
ATOM   4250  H  BASP A 275      42.156 -35.136 -39.416  0.38  0.00           H
ATOM   4251  HA AASP A 275      45.082 -34.467 -39.669  0.62  0.00           H
ATOM   4252  HA BASP A 275      45.063 -35.131 -39.494  0.38  0.00           H
ATOM   4253  HB2AASP A 275      43.210 -32.194 -38.994  0.62  0.00           H
ATOM   4254  HB2BASP A 275      45.128 -32.604 -39.107  0.38  0.00           H
ATOM   4255  HB3AASP A 275      43.756 -32.467 -40.657  0.62  0.00           H
ATOM   4256  HB3BASP A 275      43.504 -32.572 -39.822  0.38  0.00           H
ATOM   4257  N   THR A 276      45.085 -34.098 -37.088  1.00 38.19           N
ANISOU 4257  N   THR A 276     4301   3882   6328    -81  -1234   -499       N
ATOM   4258  CA  THR A 276      45.113 -34.182 -35.639  1.00 38.83           C
ANISOU 4258  CA  THR A 276     4472   3979   6301    -71  -1345   -534       C
ATOM   4259  C   THR A 276      44.800 -32.787 -35.124  1.00 38.46           C
ANISOU 4259  C   THR A 276     4535   3858   6221   -101  -1372   -585       C
ATOM   4260  O   THR A 276      45.599 -31.851 -35.240  1.00 42.73           O
ANISOU 4260  O   THR A 276     5040   4327   6868   -164  -1382   -587       O
ATOM   4261  CB  THR A 276      46.476 -34.709 -35.119  1.00 55.53           C
ANISOU 4261  CB  THR A 276     6502   6103   8492    -98  -1413   -510       C
ATOM   4262  OG1 THR A 276      46.397 -34.951 -33.706  1.00 57.01           O
ANISOU 4262  OG1 THR A 276     6791   6311   8560    -85  -1517   -538       O
ATOM   4263  CG2 THR A 276      47.595 -33.720 -35.406  1.00 55.25           C
ANISOU 4263  CG2 THR A 276     6386   5995   8612   -173  -1420   -507       C
ATOM   4264  H  ATHR A 276      45.929 -33.824 -37.571  0.62  0.00           H
ATOM   4265  H  BTHR A 276      45.881 -33.723 -37.584  0.38  0.00           H
ATOM   4266  HA  THR A 276      44.326 -34.862 -35.312  1.00  0.00           H
ATOM   4267  HB  THR A 276      46.702 -35.649 -35.622  1.00  0.00           H
ATOM   4268  HG1 THR A 276      45.690 -35.575 -33.527  1.00  0.00           H
ATOM   4269 HG21 THR A 276      48.536 -34.258 -35.517  1.00  0.00           H
ATOM   4270 HG22 THR A 276      47.676 -33.013 -34.580  1.00  0.00           H
ATOM   4271 HG23 THR A 276      47.375 -33.179 -36.326  1.00  0.00           H
ATOM   4272  N   CYS A 277      43.596 -32.649 -34.613  1.00 34.24           N
ANISOU 4272  N   CYS A 277     4136   3339   5536    -51  -1369   -626       N
ATOM   4273  CA  CYS A 277      43.052 -31.357 -34.230  1.00 34.66           C
ANISOU 4273  CA  CYS A 277     4311   3322   5537    -57  -1364   -676       C
ATOM   4274  C   CYS A 277      41.716 -31.683 -33.586  1.00 30.45           C
ANISOU 4274  C   CYS A 277     3906   2842   4821     18  -1351   -713       C
ATOM   4275  O   CYS A 277      41.316 -32.835 -33.597  1.00 28.09           O
ANISOU 4275  O   CYS A 277     3588   2624   4460     60  -1344   -694       O
ATOM   4276  CB  CYS A 277      42.929 -30.438 -35.457  1.00 36.04           C
ANISOU 4276  CB  CYS A 277     4464   3414   5814    -73  -1263   -655       C
ATOM   4277  SG  CYS A 277      41.744 -30.961 -36.707  1.00 65.03           S
ANISOU 4277  SG  CYS A 277     8136   7141   9430     16  -1113   -603       S
ATOM   4278  H   CYS A 277      43.027 -33.473 -34.482  1.00  0.00           H
ATOM   4279  HA  CYS A 277      43.706 -30.892 -33.493  1.00  0.00           H
ATOM   4280  HB2 CYS A 277      42.632 -29.449 -35.107  1.00  0.00           H
ATOM   4281  HB3 CYS A 277      43.910 -30.357 -35.925  1.00  0.00           H
ATOM   4282  N   ILE A 278      41.018 -30.692 -33.026  1.00 27.64           N
ANISOU 4282  N   ILE A 278     3678   2443   4379     36  -1338   -765       N
ATOM   4283  CA  ILE A 278      39.814 -30.995 -32.267  1.00 27.28           C
ANISOU 4283  CA  ILE A 278     3750   2455   4159    105  -1318   -802       C
ATOM   4284  C   ILE A 278      38.662 -30.187 -32.863  1.00 24.57           C
ANISOU 4284  C   ILE A 278     3477   2074   3783    167  -1209   -819       C
ATOM   4285  O   ILE A 278      38.761 -28.969 -32.988  1.00 23.84           O
ANISOU 4285  O   ILE A 278     3424   1894   3738    148  -1189   -837       O
ATOM   4286  CB  ILE A 278      39.974 -30.587 -30.808  1.00 32.57           C
ANISOU 4286  CB  ILE A 278     4523   3118   4734     82  -1394   -851       C
ATOM   4287  CG1 ILE A 278      41.185 -31.272 -30.177  1.00 37.35           C
ANISOU 4287  CG1 ILE A 278     5066   3749   5377     27  -1504   -826       C
ATOM   4288  CG2 ILE A 278      38.712 -30.876 -30.000  1.00 32.28           C
ANISOU 4288  CG2 ILE A 278     4608   3141   4516    149  -1353   -887       C
ATOM   4289  CD1 ILE A 278      41.450 -30.808 -28.765  1.00 41.44           C
ANISOU 4289  CD1 ILE A 278     5688   4249   5809     -2  -1586   -875       C
ATOM   4290  H   ILE A 278      41.325 -29.735 -33.129  1.00  0.00           H
ATOM   4291  HA  ILE A 278      39.593 -32.060 -32.332  1.00  0.00           H
ATOM   4292  HB  ILE A 278      40.148 -29.511 -30.780  1.00  0.00           H
ATOM   4293 HG12 ILE A 278      41.008 -32.347 -30.163  1.00  0.00           H
ATOM   4294 HG13 ILE A 278      42.065 -31.067 -30.787  1.00  0.00           H
ATOM   4295 HG21 ILE A 278      37.860 -30.380 -30.465  1.00  0.00           H
ATOM   4296 HG22 ILE A 278      38.536 -31.951 -29.974  1.00  0.00           H
ATOM   4297 HG23 ILE A 278      38.838 -30.504 -28.983  1.00  0.00           H
ATOM   4298 HD11 ILE A 278      42.322 -31.329 -28.368  1.00  0.00           H
ATOM   4299 HD12 ILE A 278      41.637 -29.734 -28.765  1.00  0.00           H
ATOM   4300 HD13 ILE A 278      40.582 -31.025 -28.142  1.00  0.00           H
ATOM   4301  N   SER A 279      37.569 -30.841 -33.234  1.00 24.36           N
ANISOU 4301  N   SER A 279     3465   2114   3678    245  -1135   -810       N
ATOM   4302  CA  SER A 279      36.360 -30.084 -33.655  1.00 26.06           C
ANISOU 4302  CA  SER A 279     3747   2310   3845    324  -1027   -820       C
ATOM   4303  C   SER A 279      35.121 -30.953 -33.480  1.00 22.43           C
ANISOU 4303  C   SER A 279     3309   1959   3252    405   -964   -819       C
ATOM   4304  O   SER A 279      35.130 -32.076 -33.904  1.00 20.94           O
ANISOU 4304  O   SER A 279     3039   1860   3057    408   -946   -764       O
ATOM   4305  CB  SER A 279      36.449 -29.666 -35.118  1.00 29.71           C
ANISOU 4305  CB  SER A 279     4135   2736   4418    334   -944   -751       C
ATOM   4306  OG  SER A 279      35.243 -29.034 -35.532  1.00 30.09           O
ANISOU 4306  OG  SER A 279     4240   2777   4415    421   -847   -749       O
ATOM   4307  H   SER A 279      37.558 -31.851 -33.231  1.00  0.00           H
ATOM   4308  HA  SER A 279      36.262 -29.193 -33.034  1.00  0.00           H
ATOM   4309  HB2 SER A 279      37.279 -28.970 -35.242  1.00  0.00           H
ATOM   4310  HB3 SER A 279      36.623 -30.548 -35.734  1.00  0.00           H
ATOM   4311  HG  SER A 279      34.832 -29.552 -36.228  1.00  0.00           H
ATOM   4312  N   GLU A 280      34.071 -30.415 -32.874  1.00 21.76           N
ANISOU 4312  N   GLU A 280     3320   1882   3065    463   -912   -864       N
ATOM   4313  CA  GLU A 280      32.827 -31.152 -32.655  1.00 22.48           C
ANISOU 4313  CA  GLU A 280     3429   2074   3037    536   -842   -867       C
ATOM   4314  C   GLU A 280      32.054 -31.374 -33.942  1.00 22.81           C
ANISOU 4314  C   GLU A 280     3392   2166   3111    601   -742   -804       C
ATOM   4315  O   GLU A 280      31.309 -32.356 -34.059  1.00 23.54           O
ANISOU 4315  O   GLU A 280     3443   2363   3136    636   -694   -777       O
ATOM   4316  CB  GLU A 280      31.939 -30.382 -31.682  1.00 25.24           C
ANISOU 4316  CB  GLU A 280     3884   2421   3285    574   -793   -922       C
ATOM   4317  CG  GLU A 280      32.532 -30.253 -30.273  1.00 30.75           C
ANISOU 4317  CG  GLU A 280     4669   3099   3916    512   -875   -973       C
ATOM   4318  CD  GLU A 280      32.440 -31.545 -29.457  1.00 33.66           C
ANISOU 4318  CD  GLU A 280     5050   3563   4177    498   -905   -966       C
ATOM   4319  OE1 GLU A 280      31.759 -32.521 -29.899  1.00 32.82           O
ANISOU 4319  OE1 GLU A 280     4892   3539   4037    539   -851   -934       O
ATOM   4320  OE2 GLU A 280      33.065 -31.591 -28.366  1.00 35.57           O
ANISOU 4320  OE2 GLU A 280     5352   3795   4368    442   -983   -988       O
ATOM   4321  H   GLU A 280      34.133 -29.460 -32.551  1.00  0.00           H
ATOM   4322  HA  GLU A 280      33.066 -32.122 -32.218  1.00  0.00           H
ATOM   4323  HB2 GLU A 280      31.780 -29.380 -32.081  1.00  0.00           H
ATOM   4324  HB3 GLU A 280      30.976 -30.888 -31.612  1.00  0.00           H
ATOM   4325  HG2 GLU A 280      31.993 -29.469 -29.741  1.00  0.00           H
ATOM   4326  HG3 GLU A 280      33.580 -29.964 -30.357  1.00  0.00           H
ATOM   4327  N   CYS A 281      32.207 -30.463 -34.903  1.00 21.48           N
ANISOU 4327  N   CYS A 281     3201   1924   3037    613   -709   -773       N
ATOM   4328  CA  CYS A 281      31.377 -30.492 -36.130  1.00 18.99           C
ANISOU 4328  CA  CYS A 281     2826   1653   2737    681   -616   -709       C
ATOM   4329  C   CYS A 281      32.195 -30.913 -37.353  1.00 18.86           C
ANISOU 4329  C   CYS A 281     2710   1646   2811    638   -612   -625       C
ATOM   4330  O   CYS A 281      33.244 -30.336 -37.642  1.00 20.46           O
ANISOU 4330  O   CYS A 281     2902   1760   3109    577   -645   -611       O
ATOM   4331  CB  CYS A 281      30.720 -29.120 -36.384  1.00 19.79           C
ANISOU 4331  CB  CYS A 281     2977   1692   2849    728   -555   -707       C
ATOM   4332  SG  CYS A 281      29.681 -29.191 -37.882  1.00 23.00           S
ANISOU 4332  SG  CYS A 281     3309   2170   3261    801   -457   -615       S
ATOM   4333  H   CYS A 281      32.902 -29.739 -34.793  1.00  0.00           H
ATOM   4334  HA  CYS A 281      30.584 -31.225 -35.985  1.00  0.00           H
ATOM   4335  HB2 CYS A 281      31.497 -28.368 -36.520  1.00  0.00           H
ATOM   4336  HB3 CYS A 281      30.102 -28.851 -35.528  1.00  0.00           H
ATOM   4337  N   ILE A 282      31.722 -31.933 -38.068  1.00 17.53           N
ANISOU 4337  N   ILE A 282     2468   1581   2613    664   -567   -573       N
ATOM   4338  CA  ILE A 282      32.380 -32.490 -39.243  1.00 18.52           C
ANISOU 4338  CA  ILE A 282     2503   1731   2803    631   -549   -499       C
ATOM   4339  C   ILE A 282      31.449 -32.363 -40.448  1.00 17.83           C
ANISOU 4339  C   ILE A 282     2394   1681   2698    702   -471   -445       C
ATOM   4340  O   ILE A 282      30.230 -32.645 -40.326  1.00 17.05           O
ANISOU 4340  O   ILE A 282     2300   1660   2518    760   -435   -453       O
ATOM   4341  CB  ILE A 282      32.666 -33.987 -39.044  1.00 19.40           C
ANISOU 4341  CB  ILE A 282     2552   1935   2885    599   -574   -488       C
ATOM   4342  CG1 ILE A 282      33.537 -34.165 -37.804  1.00 21.87           C
ANISOU 4342  CG1 ILE A 282     2891   2215   3204    537   -667   -537       C
ATOM   4343  CG2 ILE A 282      33.240 -34.607 -40.343  1.00 22.93           C
ANISOU 4343  CG2 ILE A 282     2909   2411   3392    578   -539   -418       C
ATOM   4344  CD1 ILE A 282      33.907 -35.618 -37.480  1.00 22.22           C
ANISOU 4344  CD1 ILE A 282     2883   2334   3224    506   -706   -524       C
ATOM   4345  H   ILE A 282      30.849 -32.348 -37.776  1.00  0.00           H
ATOM   4346  HA  ILE A 282      33.311 -31.956 -39.435  1.00  0.00           H
ATOM   4347  HB  ILE A 282      31.713 -34.476 -38.844  1.00  0.00           H
ATOM   4348 HG12 ILE A 282      32.999 -33.754 -36.950  1.00  0.00           H
ATOM   4349 HG13 ILE A 282      34.456 -33.595 -37.941  1.00  0.00           H
ATOM   4350 HG21 ILE A 282      33.437 -35.667 -40.184  1.00  0.00           H
ATOM   4351 HG22 ILE A 282      32.518 -34.489 -41.151  1.00  0.00           H
ATOM   4352 HG23 ILE A 282      34.168 -34.101 -40.608  1.00  0.00           H
ATOM   4353 HD11 ILE A 282      34.526 -35.644 -36.583  1.00  0.00           H
ATOM   4354 HD12 ILE A 282      32.998 -36.195 -37.310  1.00  0.00           H
ATOM   4355 HD13 ILE A 282      34.459 -36.047 -38.316  1.00  0.00           H
ATOM   4356  N   THR A 283      31.983 -31.860 -41.571  1.00 16.91           N
ANISOU 4356  N   THR A 283     2257   1515   2654    687   -442   -386       N
ATOM   4357  CA  THR A 283      31.236 -31.810 -42.840  1.00 15.75           C
ANISOU 4357  CA  THR A 283     2092   1408   2483    745   -377   -322       C
ATOM   4358  C   THR A 283      32.108 -32.542 -43.858  1.00 16.57           C
ANISOU 4358  C   THR A 283     2129   1540   2628    697   -356   -265       C
ATOM   4359  O   THR A 283      33.285 -32.787 -43.577  1.00 17.48           O
ANISOU 4359  O   THR A 283     2210   1623   2808    621   -384   -271       O
ATOM   4360  CB  THR A 283      30.983 -30.399 -43.358  1.00 17.06           C
ANISOU 4360  CB  THR A 283     2319   1483   2679    778   -346   -293       C
ATOM   4361  OG1 THR A 283      32.134 -29.907 -44.075  1.00 17.93           O
ANISOU 4361  OG1 THR A 283     2427   1503   2883    724   -339   -248       O
ATOM   4362  CG2 THR A 283      30.552 -29.407 -42.243  1.00 19.56           C
ANISOU 4362  CG2 THR A 283     2711   1737   2983    796   -364   -356       C
ATOM   4363  H   THR A 283      32.928 -31.504 -41.546  1.00  0.00           H
ATOM   4364  HA  THR A 283      30.287 -32.334 -42.727  1.00  0.00           H
ATOM   4365  HB  THR A 283      30.161 -30.460 -44.071  1.00  0.00           H
ATOM   4366  HG1 THR A 283      32.923 -30.040 -43.545  1.00  0.00           H
ATOM   4367 HG21 THR A 283      30.387 -28.421 -42.677  1.00  0.00           H
ATOM   4368 HG22 THR A 283      31.336 -29.345 -41.489  1.00  0.00           H
ATOM   4369 HG23 THR A 283      29.630 -29.759 -41.780  1.00  0.00           H
ATOM   4370  N   PRO A 284      31.558 -32.902 -45.028  1.00 16.50           N
ANISOU 4370  N   PRO A 284     2097   1591   2581    737   -308   -210       N
ATOM   4371  CA  PRO A 284      32.429 -33.565 -46.009  1.00 17.82           C
ANISOU 4371  CA  PRO A 284     2210   1780   2780    689   -274   -161       C
ATOM   4372  C   PRO A 284      33.582 -32.665 -46.478  1.00 17.80           C
ANISOU 4372  C   PRO A 284     2218   1672   2873    633   -249   -123       C
ATOM   4373  O   PRO A 284      34.566 -33.187 -46.996  1.00 17.63           O
ANISOU 4373  O   PRO A 284     2141   1656   2901    577   -221    -96       O
ATOM   4374  CB  PRO A 284      31.483 -33.823 -47.178  1.00 18.60           C
ANISOU 4374  CB  PRO A 284     2313   1948   2806    752   -232   -113       C
ATOM   4375  CG  PRO A 284      30.126 -34.064 -46.468  1.00 17.57           C
ANISOU 4375  CG  PRO A 284     2189   1894   2593    785   -247   -148       C
ATOM   4376  CD  PRO A 284      30.145 -32.947 -45.453  1.00 16.52           C
ANISOU 4376  CD  PRO A 284     2110   1674   2494    794   -273   -189       C
ATOM   4377  HA  PRO A 284      32.812 -34.504 -45.610  1.00  0.00           H
ATOM   4378  HB2 PRO A 284      31.791 -34.700 -47.747  1.00  0.00           H
ATOM   4379  HB3 PRO A 284      31.426 -32.948 -47.825  1.00  0.00           H
ATOM   4380  HG2 PRO A 284      29.288 -33.966 -47.158  1.00  0.00           H
ATOM   4381  HG3 PRO A 284      30.112 -35.036 -45.975  1.00  0.00           H
ATOM   4382  HD2 PRO A 284      29.491 -33.173 -44.611  1.00  0.00           H
ATOM   4383  HD3 PRO A 284      29.856 -32.004 -45.918  1.00  0.00           H
ATOM   4384  N   ASN A 285      33.420 -31.357 -46.351  1.00 18.04           N
ANISOU 4384  N   ASN A 285     2316   1607   2930    649   -251   -118       N
ATOM   4385  CA  ASN A 285      34.479 -30.395 -46.717  1.00 20.09           C
ANISOU 4385  CA  ASN A 285     2591   1752   3289    587   -226    -83       C
ATOM   4386  C   ASN A 285      35.603 -30.326 -45.703  1.00 21.81           C
ANISOU 4386  C   ASN A 285     2776   1911   3600    502   -280   -134       C
ATOM   4387  O   ASN A 285      36.630 -29.681 -45.950  1.00 24.39           O
ANISOU 4387  O   ASN A 285     3092   2149   4028    431   -264   -109       O
ATOM   4388  CB  ASN A 285      33.931 -28.991 -46.780  1.00 21.62           C
ANISOU 4388  CB  ASN A 285     2878   1847   3490    631   -220    -68       C
ATOM   4389  CG  ASN A 285      32.760 -28.867 -47.730  1.00 24.61           C
ANISOU 4389  CG  ASN A 285     3296   2270   3784    725   -185    -15       C
ATOM   4390  OD1 ASN A 285      31.657 -29.414 -47.478  1.00 23.35           O
ANISOU 4390  OD1 ASN A 285     3128   2200   3543    796   -206    -45       O
ATOM   4391  ND2 ASN A 285      32.988 -28.161 -48.829  1.00 31.43           N
ANISOU 4391  ND2 ASN A 285     4203   3073   4667    724   -132     66       N
ATOM   4392  H   ASN A 285      32.544 -31.006 -45.992  1.00  0.00           H
ATOM   4393  HA  ASN A 285      34.889 -30.665 -47.690  1.00  0.00           H
ATOM   4394  HB2 ASN A 285      33.604 -28.699 -45.782  1.00  0.00           H
ATOM   4395  HB3 ASN A 285      34.723 -28.316 -47.104  1.00  0.00           H
ATOM   4396 HD21 ASN A 285      33.896 -27.746 -48.983  1.00  0.00           H
ATOM   4397 HD22 ASN A 285      32.254 -28.038 -49.512  1.00  0.00           H
ATOM   4398  N   GLY A 286      35.376 -30.907 -44.540  1.00 19.34           N
ANISOU 4398  N   GLY A 286     2454   1643   3252    506   -349   -204       N
ATOM   4399  CA  GLY A 286      36.249 -30.713 -43.397  1.00 19.43           C
ANISOU 4399  CA  GLY A 286     2457   1595   3330    437   -425   -262       C
ATOM   4400  C   GLY A 286      35.468 -30.294 -42.170  1.00 20.31           C
ANISOU 4400  C   GLY A 286     2649   1690   3379    477   -483   -337       C
ATOM   4401  O   GLY A 286      34.271 -29.954 -42.240  1.00 20.93           O
ANISOU 4401  O   GLY A 286     2786   1786   3382    559   -454   -341       O
ATOM   4402  H   GLY A 286      34.569 -31.506 -44.442  1.00  0.00           H
ATOM   4403  HA2 GLY A 286      36.768 -31.648 -43.185  1.00  0.00           H
ATOM   4404  HA3 GLY A 286      36.983 -29.943 -43.634  1.00  0.00           H
ATOM   4405  N   SER A 287      36.149 -30.286 -41.042  1.00 21.36           N
ANISOU 4405  N   SER A 287     2786   1787   3544    419   -566   -398       N
ATOM   4406  CA  SER A 287      35.546 -29.794 -39.825  1.00 22.33           C
ANISOU 4406  CA  SER A 287     2999   1880   3604    447   -619   -476       C
ATOM   4407  C   SER A 287      35.311 -28.306 -39.932  1.00 22.00           C
ANISOU 4407  C   SER A 287     3043   1717   3598    464   -599   -486       C
ATOM   4408  O   SER A 287      36.008 -27.593 -40.654  1.00 22.49           O
ANISOU 4408  O   SER A 287     3093   1692   3758    419   -575   -442       O
ATOM   4409  CB  SER A 287      36.423 -30.133 -38.622  1.00 23.09           C
ANISOU 4409  CB  SER A 287     3091   1963   3721    376   -725   -537       C
ATOM   4410  OG  SER A 287      36.486 -31.558 -38.454  1.00 23.20           O
ANISOU 4410  OG  SER A 287     3039   2088   3689    375   -744   -526       O
ATOM   4411  H   SER A 287      37.100 -30.626 -41.028  1.00  0.00           H
ATOM   4412  HA  SER A 287      34.582 -30.286 -39.696  1.00  0.00           H
ATOM   4413  HB2 SER A 287      35.998 -29.681 -37.726  1.00  0.00           H
ATOM   4414  HB3 SER A 287      37.428 -29.742 -38.784  1.00  0.00           H
ATOM   4415  HG  SER A 287      36.501 -31.770 -37.518  1.00  0.00           H
ATOM   4416  N   ILE A 288      34.315 -27.840 -39.197  1.00 18.96           N
ANISOU 4416  N   ILE A 288     2747   1322   3136    531   -603   -545       N
ATOM   4417  CA  ILE A 288      34.084 -26.417 -39.057  1.00 18.90           C
ANISOU 4417  CA  ILE A 288     2830   1200   3152    546   -589   -567       C
ATOM   4418  C   ILE A 288      33.831 -26.070 -37.613  1.00 20.76           C
ANISOU 4418  C   ILE A 288     3145   1424   3317    542   -636   -660       C
ATOM   4419  O   ILE A 288      33.367 -26.898 -36.858  1.00 19.00           O
ANISOU 4419  O   ILE A 288     2925   1291   3004    566   -656   -701       O
ATOM   4420  CB  ILE A 288      32.861 -25.932 -39.865  1.00 19.52           C
ANISOU 4420  CB  ILE A 288     2932   1303   3182    643   -498   -516       C
ATOM   4421  CG1 ILE A 288      31.600 -26.701 -39.419  1.00 18.09           C
ANISOU 4421  CG1 ILE A 288     2741   1255   2878    720   -471   -540       C
ATOM   4422  CG2 ILE A 288      33.105 -26.156 -41.361  1.00 19.96           C
ANISOU 4422  CG2 ILE A 288     2929   1365   3291    648   -449   -417       C
ATOM   4423  CD1 ILE A 288      30.276 -26.110 -40.012  1.00 18.33           C
ANISOU 4423  CD1 ILE A 288     2787   1312   2867    812   -392   -500       C
ATOM   4424  H   ILE A 288      33.703 -28.490 -38.724  1.00  0.00           H
ATOM   4425  HA  ILE A 288      34.969 -25.880 -39.399  1.00  0.00           H
ATOM   4426  HB  ILE A 288      32.713 -24.868 -39.683  1.00  0.00           H
ATOM   4427 HG12 ILE A 288      31.693 -27.737 -39.744  1.00  0.00           H
ATOM   4428 HG13 ILE A 288      31.540 -26.677 -38.331  1.00  0.00           H
ATOM   4429 HG21 ILE A 288      32.239 -25.812 -41.926  1.00  0.00           H
ATOM   4430 HG22 ILE A 288      33.987 -25.597 -41.673  1.00  0.00           H
ATOM   4431 HG23 ILE A 288      33.263 -27.218 -41.548  1.00  0.00           H
ATOM   4432 HD11 ILE A 288      29.427 -26.696 -39.660  1.00  0.00           H
ATOM   4433 HD12 ILE A 288      30.163 -25.075 -39.688  1.00  0.00           H
ATOM   4434 HD13 ILE A 288      30.317 -26.147 -41.101  1.00  0.00           H
ATOM   4435  N   PRO A 289      34.195 -24.854 -37.216  1.00 22.69           N
ANISOU 4435  N   PRO A 289     2117   2516   3986    485   -762   -668       N
ATOM   4436  CA  PRO A 289      33.856 -24.293 -35.902  1.00 24.18           C
ANISOU 4436  CA  PRO A 289     2446   2668   4075    533   -911   -632       C
ATOM   4437  C   PRO A 289      32.355 -24.275 -35.663  1.00 21.59           C
ANISOU 4437  C   PRO A 289     2265   2393   3544    541   -868   -480       C
ATOM   4438  O   PRO A 289      31.591 -24.103 -36.617  1.00 20.20           O
ANISOU 4438  O   PRO A 289     2026   2305   3346    491   -695   -416       O
ATOM   4439  CB  PRO A 289      34.341 -22.826 -36.002  1.00 25.42           C
ANISOU 4439  CB  PRO A 289     2480   2840   4338    478   -836   -686       C
ATOM   4440  CG  PRO A 289      35.395 -22.843 -36.991  1.00 26.97           C
ANISOU 4440  CG  PRO A 289     2502   3017   4729    424   -726   -803       C
ATOM   4441  CD  PRO A 289      35.036 -23.939 -38.003  1.00 25.90           C
ANISOU 4441  CD  PRO A 289     2356   2927   4557    407   -620   -759       C
ATOM   4442  HA  PRO A 289      34.374 -24.824 -35.103  1.00  0.00           H
ATOM   4443  HB2 PRO A 289      34.724 -22.484 -35.041  1.00  0.00           H
ATOM   4444  HB3 PRO A 289      33.526 -22.182 -36.332  1.00  0.00           H
ATOM   4445  HG2 PRO A 289      36.350 -23.068 -36.517  1.00  0.00           H
ATOM   4446  HG3 PRO A 289      35.448 -21.877 -37.493  1.00  0.00           H
ATOM   4447  HD2 PRO A 289      34.483 -23.527 -38.847  1.00  0.00           H
ATOM   4448  HD3 PRO A 289      35.935 -24.449 -38.349  1.00  0.00           H
ATOM   4449  N   ASN A 290      31.929 -24.401 -34.413  1.00 20.40           N
ANISOU 4449  N   ASN A 290     2334   2171   3247    599  -1015   -434       N
ATOM   4450  CA  ASN A 290      30.506 -24.361 -34.141  1.00 20.72           C
ANISOU 4450  CA  ASN A 290     2552   2234   3085    570   -922   -302       C
ATOM   4451  C   ASN A 290      30.126 -23.234 -33.188  1.00 21.48           C
ANISOU 4451  C   ASN A 290     2764   2316   3082    549   -938   -269       C
ATOM   4452  O   ASN A 290      29.093 -23.300 -32.529  1.00 22.09           O
ANISOU 4452  O   ASN A 290     3058   2364   2970    514   -872   -187       O
ATOM   4453  CB  ASN A 290      30.005 -25.713 -33.626  1.00 22.28           C
ANISOU 4453  CB  ASN A 290     2987   2345   3133    609   -974   -251       C
ATOM   4454  CG  ASN A 290      30.535 -26.032 -32.249  1.00 24.62           C
ANISOU 4454  CG  ASN A 290     3523   2493   3339    694  -1203   -284       C
ATOM   4455  OD1 ASN A 290      31.375 -25.294 -31.692  1.00 25.66           O
ANISOU 4455  OD1 ASN A 290     3613   2598   3540    711  -1319   -368       O
ATOM   4456  ND2 ASN A 290      30.051 -27.114 -31.681  1.00 25.15           N
ANISOU 4456  ND2 ASN A 290     3856   2461   3237    713  -1226   -233       N
ATOM   4457  H   ASN A 290      32.589 -24.524 -33.659  1.00  0.00           H
ATOM   4458  HA  ASN A 290      30.001 -24.168 -35.088  1.00  0.00           H
ATOM   4459  HB2 ASN A 290      28.916 -25.691 -33.586  1.00  0.00           H
ATOM   4460  HB3 ASN A 290      30.320 -26.495 -34.317  1.00  0.00           H
ATOM   4461 HD21 ASN A 290      30.361 -27.381 -30.758  1.00  0.00           H
ATOM   4462 HD22 ASN A 290      29.369 -27.678 -32.168  1.00  0.00           H
ATOM   4463  N   ASP A 291      30.920 -22.173 -33.178  1.00 21.80           N
ANISOU 4463  N   ASP A 291     2648   2373   3264    556   -992   -344       N
ATOM   4464  CA  ASP A 291      30.552 -20.977 -32.382  1.00 24.21           C
ANISOU 4464  CA  ASP A 291     3035   2677   3486    528   -992   -315       C
ATOM   4465  C   ASP A 291      29.393 -20.190 -33.001  1.00 23.89           C
ANISOU 4465  C   ASP A 291     2959   2745   3374    415   -752   -228       C
ATOM   4466  O   ASP A 291      28.635 -19.530 -32.294  1.00 28.90           O
ANISOU 4466  O   ASP A 291     3720   3372   3887    380   -712   -180       O
ATOM   4467  CB  ASP A 291      31.769 -20.062 -32.163  1.00 28.39           C
ANISOU 4467  CB  ASP A 291     3408   3181   4198    555  -1105   -435       C
ATOM   4468  CG  ASP A 291      32.382 -19.552 -33.474  1.00 35.30           C
ANISOU 4468  CG  ASP A 291     4004   4135   5275    483   -940   -496       C
ATOM   4469  OD1 ASP A 291      33.076 -20.321 -34.165  1.00 34.48           O
ANISOU 4469  OD1 ASP A 291     3803   4018   5280    480   -913   -560       O
ATOM   4470  OD2 ASP A 291      32.180 -18.352 -33.832  1.00 41.90           O
ANISOU 4470  OD2 ASP A 291     4740   5031   6148    420   -823   -482       O
ATOM   4471  H   ASP A 291      31.777 -22.179 -33.713  1.00  0.00           H
ATOM   4472  HA  ASP A 291      30.224 -21.325 -31.402  1.00  0.00           H
ATOM   4473  HB2 ASP A 291      32.530 -20.621 -31.619  1.00  0.00           H
ATOM   4474  HB3 ASP A 291      31.463 -19.206 -31.561  1.00  0.00           H
ATOM   4475  N   LYS A 292      29.230 -20.233 -34.312  1.00 16.04           N
ANISOU 4475  N   LYS A 292     1806   1836   2454    363   -600   -219       N
ATOM   4476  CA  LYS A 292      28.092 -19.534 -34.918  1.00 14.14           C
ANISOU 4476  CA  LYS A 292     1556   1672   2146    279   -421   -151       C
ATOM   4477  C   LYS A 292      26.878 -20.442 -35.026  1.00 15.65           C
ANISOU 4477  C   LYS A 292     1862   1864   2220    256   -336    -91       C
ATOM   4478  O   LYS A 292      27.019 -21.650 -35.115  1.00 16.49           O
ANISOU 4478  O   LYS A 292     2009   1939   2317    290   -368    -93       O
ATOM   4479  CB  LYS A 292      28.464 -19.018 -36.294  1.00 14.44           C
ANISOU 4479  CB  LYS A 292     1419   1772   2295    238   -309   -175       C
ATOM   4480  CG  LYS A 292      29.706 -18.149 -36.310  1.00 17.76           C
ANISOU 4480  CG  LYS A 292     1701   2175   2872    240   -343   -259       C
ATOM   4481  CD  LYS A 292      30.118 -17.802 -37.744  1.00 19.02           C
ANISOU 4481  CD  LYS A 292     1737   2364   3127    182   -182   -289       C
ATOM   4482  CE  LYS A 292      31.353 -16.887 -37.759  1.00 22.93           C
ANISOU 4482  CE  LYS A 292     2082   2821   3810    162   -168   -396       C
ATOM   4483  NZ  LYS A 292      32.525 -17.540 -37.184  1.00 28.97           N
ANISOU 4483  NZ  LYS A 292     2784   3516   4705    218   -306   -503       N
ATOM   4484  H   LYS A 292      29.883 -20.742 -34.891  1.00  0.00           H
ATOM   4485  HA  LYS A 292      27.833 -18.683 -34.288  1.00  0.00           H
ATOM   4486  HB2 LYS A 292      27.630 -18.431 -36.677  1.00  0.00           H
ATOM   4487  HB3 LYS A 292      28.625 -19.870 -36.955  1.00  0.00           H
ATOM   4488  HG2 LYS A 292      29.502 -17.227 -35.765  1.00  0.00           H
ATOM   4489  HG3 LYS A 292      30.522 -18.681 -35.821  1.00  0.00           H
ATOM   4490  HD2 LYS A 292      29.291 -17.292 -38.238  1.00  0.00           H
ATOM   4491  HD3 LYS A 292      30.346 -18.721 -38.284  1.00  0.00           H
ATOM   4492  HE2 LYS A 292      31.132 -15.989 -37.182  1.00  0.00           H
ATOM   4493  HE3 LYS A 292      31.573 -16.603 -38.788  1.00  0.00           H
ATOM   4494  HZ1 LYS A 292      33.310 -16.904 -37.207  1.00  0.00           H
ATOM   4495  HZ2 LYS A 292      32.746 -18.368 -37.719  1.00  0.00           H
ATOM   4496  HZ3 LYS A 292      32.330 -17.800 -36.228  1.00  0.00           H
ATOM   4497  N   PRO A 293      25.665 -19.856 -35.017  1.00 15.83           N
ANISOU 4497  N   PRO A 293     1924   1913   2177    198   -226    -53       N
ATOM   4498  CA  PRO A 293      24.414 -20.636 -35.018  1.00 14.02           C
ANISOU 4498  CA  PRO A 293     1783   1665   1880    167   -129    -30       C
ATOM   4499  C   PRO A 293      24.079 -21.230 -36.385  1.00 13.08           C
ANISOU 4499  C   PRO A 293     1560   1595   1814    163    -66    -33       C
ATOM   4500  O   PRO A 293      23.337 -22.204 -36.445  1.00 13.02           O
ANISOU 4500  O   PRO A 293     1603   1561   1783    154    -13    -33       O
ATOM   4501  CB  PRO A 293      23.349 -19.590 -34.597  1.00 14.68           C
ANISOU 4501  CB  PRO A 293     1892   1751   1937    110    -46    -30       C
ATOM   4502  CG  PRO A 293      23.982 -18.265 -34.942  1.00 14.47           C
ANISOU 4502  CG  PRO A 293     1754   1776   1966    112    -88    -35       C
ATOM   4503  CD  PRO A 293      25.439 -18.423 -34.731  1.00 15.77           C
ANISOU 4503  CD  PRO A 293     1893   1928   2172    164   -204    -52       C
ATOM   4504  HA  PRO A 293      24.470 -21.429 -34.272  1.00  0.00           H
ATOM   4505  HB2 PRO A 293      22.423 -19.734 -35.154  1.00  0.00           H
ATOM   4506  HB3 PRO A 293      23.160 -19.652 -33.525  1.00  0.00           H
ATOM   4507  HG2 PRO A 293      23.778 -18.011 -35.982  1.00  0.00           H
ATOM   4508  HG3 PRO A 293      23.594 -17.486 -34.286  1.00  0.00           H
ATOM   4509  HD2 PRO A 293      26.004 -17.793 -35.418  1.00  0.00           H
ATOM   4510  HD3 PRO A 293      25.702 -18.194 -33.698  1.00  0.00           H
ATOM   4511  N   PHE A 294      24.624 -20.660 -37.453  1.00 12.62           N
ANISOU 4511  N   PHE A 294     1380   1593   1821    167    -62    -43       N
ATOM   4512  CA  PHE A 294      24.342 -21.112 -38.811  1.00 13.11           C
ANISOU 4512  CA  PHE A 294     1386   1687   1908    168     -9    -47       C
ATOM   4513  C   PHE A 294      25.611 -21.350 -39.587  1.00 13.48           C
ANISOU 4513  C   PHE A 294     1356   1747   2018    187    -17    -70       C
ATOM   4514  O   PHE A 294      26.711 -20.863 -39.230  1.00 14.98           O
ANISOU 4514  O   PHE A 294     1493   1926   2271    193    -55    -99       O
ATOM   4515  CB  PHE A 294      23.475 -20.082 -39.560  1.00 13.71           C
ANISOU 4515  CB  PHE A 294     1447   1784   1978    144     34    -48       C
ATOM   4516  CG  PHE A 294      22.299 -19.620 -38.770  1.00 14.53           C
ANISOU 4516  CG  PHE A 294     1587   1867   2069    119     48    -58       C
ATOM   4517  CD1 PHE A 294      21.265 -20.499 -38.472  1.00 14.99           C
ANISOU 4517  CD1 PHE A 294     1671   1889   2134    108     89    -85       C
ATOM   4518  CD2 PHE A 294      22.237 -18.337 -38.293  1.00 15.37           C
ANISOU 4518  CD2 PHE A 294     1692   1975   2172     98     41    -56       C
ATOM   4519  CE1 PHE A 294      20.182 -20.092 -37.718  1.00 16.11           C
ANISOU 4519  CE1 PHE A 294     1833   1992   2297     69    141   -123       C
ATOM   4520  CE2 PHE A 294      21.130 -17.903 -37.527  1.00 14.84           C
ANISOU 4520  CE2 PHE A 294     1649   1879   2112     67     72    -84       C
ATOM   4521  CZ  PHE A 294      20.133 -18.775 -37.237  1.00 15.33           C
ANISOU 4521  CZ  PHE A 294     1731   1900   2195     50    130   -123       C
ATOM   4522  H   PHE A 294      25.257 -19.885 -37.320  1.00  0.00           H
ATOM   4523  HA  PHE A 294      23.791 -22.051 -38.755  1.00  0.00           H
ATOM   4524  HB2 PHE A 294      24.094 -19.217 -39.799  1.00  0.00           H
ATOM   4525  HB3 PHE A 294      23.121 -20.529 -40.489  1.00  0.00           H
ATOM   4526  HD1 PHE A 294      21.309 -21.515 -38.835  1.00  0.00           H
ATOM   4527  HD2 PHE A 294      23.043 -17.649 -38.504  1.00  0.00           H
ATOM   4528  HE1 PHE A 294      19.380 -20.782 -37.500  1.00  0.00           H
ATOM   4529  HE2 PHE A 294      21.079 -16.883 -37.175  1.00  0.00           H
ATOM   4530  HZ  PHE A 294      19.297 -18.454 -36.633  1.00  0.00           H
ATOM   4531  N   GLN A 295      25.475 -22.103 -40.673  1.00 12.08           N
ANISOU 4531  N   GLN A 295     1163   1581   1845    195     27    -76       N
ATOM   4532  CA  GLN A 295      26.598 -22.364 -41.551  1.00 12.44           C
ANISOU 4532  CA  GLN A 295     1142   1628   1959    199     63   -112       C
ATOM   4533  C   GLN A 295      26.112 -22.564 -42.991  1.00 12.05           C
ANISOU 4533  C   GLN A 295     1129   1586   1865    191    140   -108       C
ATOM   4534  O   GLN A 295      24.995 -23.054 -43.217  1.00 13.06           O
ANISOU 4534  O   GLN A 295     1306   1717   1939    208    121    -91       O
ATOM   4535  CB  GLN A 295      27.411 -23.580 -41.064  1.00 14.16           C
ANISOU 4535  CB  GLN A 295     1318   1819   2242    242     -7   -148       C
ATOM   4536  CG  GLN A 295      26.604 -24.895 -40.938  1.00 14.58           C
ANISOU 4536  CG  GLN A 295     1439   1863   2239    268    -32   -122       C
ATOM   4537  CD  GLN A 295      26.708 -25.833 -42.151  1.00 14.79           C
ANISOU 4537  CD  GLN A 295     1431   1901   2289    278     21   -143       C
ATOM   4538  OE1 GLN A 295      27.463 -25.594 -43.098  1.00 14.07           O
ANISOU 4538  OE1 GLN A 295     1278   1816   2250    263     88   -181       O
ATOM   4539  NE2 GLN A 295      25.981 -26.963 -42.076  1.00 14.73           N
ANISOU 4539  NE2 GLN A 295     1472   1880   2246    298      5   -127       N
ATOM   4540  H   GLN A 295      24.573 -22.501 -40.891  1.00  0.00           H
ATOM   4541  HA  GLN A 295      27.251 -21.492 -41.533  1.00  0.00           H
ATOM   4542  HB2 GLN A 295      27.824 -23.341 -40.084  1.00  0.00           H
ATOM   4543  HB3 GLN A 295      28.236 -23.745 -41.757  1.00  0.00           H
ATOM   4544  HG2 GLN A 295      26.966 -25.433 -40.062  1.00  0.00           H
ATOM   4545  HG3 GLN A 295      25.555 -24.645 -40.782  1.00  0.00           H
ATOM   4546 HE21 GLN A 295      25.395 -27.134 -41.271  1.00  0.00           H
ATOM   4547 HE22 GLN A 295      26.021 -27.640 -42.825  1.00  0.00           H
ATOM   4548  N   ASN A 296      26.984 -22.268 -43.947  1.00 11.35           N
ANISOU 4548  N   ASN A 296     1024   1482   1807    166    230   -139       N
ATOM   4549  CA  ASN A 296      26.671 -22.447 -45.372  1.00 13.32           C
ANISOU 4549  CA  ASN A 296     1363   1712   1984    161    307   -138       C
ATOM   4550  C   ASN A 296      27.739 -23.327 -46.057  1.00 12.89           C
ANISOU 4550  C   ASN A 296     1256   1638   2003    152    392   -195       C
ATOM   4551  O   ASN A 296      27.956 -23.263 -47.287  1.00 14.47           O
ANISOU 4551  O   ASN A 296     1545   1799   2154    125    509   -213       O
ATOM   4552  CB  ASN A 296      26.612 -21.048 -45.948  1.00 18.67           C
ANISOU 4552  CB  ASN A 296     2143   2356   2596    123    374   -123       C
ATOM   4553  CG  ASN A 296      26.306 -20.995 -47.369  1.00 23.38           C
ANISOU 4553  CG  ASN A 296     2904   2899   3080    123    437   -119       C
ATOM   4554  OD1 ASN A 296      27.054 -20.337 -48.139  1.00 26.25           O
ANISOU 4554  OD1 ASN A 296     3359   3201   3416     69    579   -136       O
ATOM   4555  ND2 ASN A 296      25.155 -21.566 -47.762  1.00 23.21           N
ANISOU 4555  ND2 ASN A 296     2953   2879   2988    180    337   -105       N
ATOM   4556  H   ASN A 296      27.891 -21.908 -43.687  1.00  0.00           H
ATOM   4557  HA  ASN A 296      25.694 -22.921 -45.471  1.00  0.00           H
ATOM   4558  HB2 ASN A 296      27.581 -20.573 -45.790  1.00  0.00           H
ATOM   4559  HB3 ASN A 296      25.854 -20.481 -45.407  1.00  0.00           H
ATOM   4560 HD21 ASN A 296      24.872 -21.518 -48.730  1.00  0.00           H
ATOM   4561 HD22 ASN A 296      24.573 -22.044 -47.089  1.00  0.00           H
ATOM   4562  N   VAL A 297      28.401 -24.170 -45.276  1.00 11.78           N
ANISOU 4562  N   VAL A 297      992   1509   1976    177    332   -233       N
ATOM   4563  CA  VAL A 297      29.478 -25.013 -45.821  1.00 13.07           C
ANISOU 4563  CA  VAL A 297     1068   1645   2254    174    400   -314       C
ATOM   4564  C   VAL A 297      28.905 -26.246 -46.523  1.00 14.45           C
ANISOU 4564  C   VAL A 297     1295   1829   2366    207    392   -298       C
ATOM   4565  O   VAL A 297      29.249 -26.521 -47.676  1.00 15.00           O
ANISOU 4565  O   VAL A 297     1400   1871   2427    182    513   -336       O
ATOM   4566  CB  VAL A 297      30.459 -25.414 -44.718  1.00 13.61           C
ANISOU 4566  CB  VAL A 297      986   1696   2487    208    294   -383       C
ATOM   4567  CG1 VAL A 297      31.521 -26.395 -45.230  1.00 15.11           C
ANISOU 4567  CG1 VAL A 297     1113   1848   2779    199    314   -464       C
ATOM   4568  CG2 VAL A 297      31.141 -24.142 -44.179  1.00 14.13           C
ANISOU 4568  CG2 VAL A 297     1000   1741   2627    169    303   -418       C
ATOM   4569  H   VAL A 297      28.164 -24.234 -44.296  1.00  0.00           H
ATOM   4570  HA  VAL A 297      30.023 -24.427 -46.561  1.00  0.00           H
ATOM   4571  HB  VAL A 297      29.904 -25.887 -43.908  1.00  0.00           H
ATOM   4572 HG11 VAL A 297      31.034 -27.293 -45.610  1.00  0.00           H
ATOM   4573 HG12 VAL A 297      32.093 -25.926 -46.030  1.00  0.00           H
ATOM   4574 HG13 VAL A 297      32.191 -26.663 -44.414  1.00  0.00           H
ATOM   4575 HG21 VAL A 297      31.844 -24.412 -43.391  1.00  0.00           H
ATOM   4576 HG22 VAL A 297      31.676 -23.646 -44.989  1.00  0.00           H
ATOM   4577 HG23 VAL A 297      30.385 -23.467 -43.776  1.00  0.00           H
ATOM   4578  N   ASN A 298      28.055 -26.986 -45.817  1.00 14.68           N
ANISOU 4578  N   ASN A 298     1340   1884   2354    255    268   -252       N
ATOM   4579  CA  ASN A 298      27.464 -28.195 -46.375  1.00 15.13           C
ANISOU 4579  CA  ASN A 298     1431   1944   2372    287    253   -246       C
ATOM   4580  C   ASN A 298      26.220 -28.594 -45.572  1.00 14.06           C
ANISOU 4580  C   ASN A 298     1341   1820   2181    314    158   -195       C
ATOM   4581  O   ASN A 298      26.224 -28.531 -44.344  1.00 14.14           O
ANISOU 4581  O   ASN A 298     1344   1822   2208    320     92   -177       O
ATOM   4582  CB  ASN A 298      28.492 -29.368 -46.349  1.00 12.21           C
ANISOU 4582  CB  ASN A 298      960   1555   2123    313    242   -311       C
ATOM   4583  CG  ASN A 298      28.174 -30.433 -47.377  1.00 15.17           C
ANISOU 4583  CG  ASN A 298     1368   1928   2466    329    282   -324       C
ATOM   4584  OD1 ASN A 298      27.047 -30.945 -47.418  1.00 14.83           O
ANISOU 4584  OD1 ASN A 298     1392   1898   2346    354    232   -281       O
ATOM   4585  ND2 ASN A 298      29.156 -30.761 -48.231  1.00 18.20           N
ANISOU 4585  ND2 ASN A 298     1702   2287   2925    309    383   -398       N
ATOM   4586  H   ASN A 298      27.815 -26.705 -44.877  1.00  0.00           H
ATOM   4587  HA  ASN A 298      27.172 -28.003 -47.407  1.00  0.00           H
ATOM   4588  HB2 ASN A 298      28.480 -29.822 -45.358  1.00  0.00           H
ATOM   4589  HB3 ASN A 298      29.488 -28.971 -46.546  1.00  0.00           H
ATOM   4590 HD21 ASN A 298      30.057 -30.309 -48.163  1.00  0.00           H
ATOM   4591 HD22 ASN A 298      28.994 -31.460 -48.942  1.00  0.00           H
ATOM   4592  N   LYS A 299      25.162 -29.001 -46.268  1.00 13.14           N
ANISOU 4592  N   LYS A 299     1282   1704   2008    329    159   -188       N
ATOM   4593  CA  LYS A 299      23.982 -29.517 -45.595  1.00 13.23           C
ANISOU 4593  CA  LYS A 299     1310   1704   2012    340    109   -175       C
ATOM   4594  C   LYS A 299      24.266 -30.853 -44.914  1.00 12.18           C
ANISOU 4594  C   LYS A 299     1160   1549   1921    359     82   -178       C
ATOM   4595  O   LYS A 299      23.518 -31.252 -44.024  1.00 11.89           O
ANISOU 4595  O   LYS A 299     1162   1478   1878    350     71   -166       O
ATOM   4596  CB  LYS A 299      22.797 -29.653 -46.543  1.00 13.30           C
ANISOU 4596  CB  LYS A 299     1357   1702   1996    360     97   -203       C
ATOM   4597  CG  LYS A 299      23.036 -30.578 -47.758  1.00 13.41           C
ANISOU 4597  CG  LYS A 299     1387   1709   2000    391    110   -233       C
ATOM   4598  CD  LYS A 299      21.914 -30.367 -48.804  1.00 15.48           C
ANISOU 4598  CD  LYS A 299     1719   1940   2222    428     56   -273       C
ATOM   4599  CE  LYS A 299      22.172 -31.172 -50.084  1.00 18.37           C
ANISOU 4599  CE  LYS A 299     2143   2288   2549    462     65   -303       C
ATOM   4600  NZ  LYS A 299      23.265 -30.547 -50.872  1.00 20.28           N
ANISOU 4600  NZ  LYS A 299     2476   2521   2708    438    153   -287       N
ATOM   4601  H   LYS A 299      25.179 -28.951 -47.277  1.00  0.00           H
ATOM   4602  HA  LYS A 299      23.705 -28.803 -44.820  1.00  0.00           H
ATOM   4603  HB2 LYS A 299      21.955 -30.050 -45.976  1.00  0.00           H
ATOM   4604  HB3 LYS A 299      22.531 -28.661 -46.910  1.00  0.00           H
ATOM   4605  HG2 LYS A 299      24.000 -30.342 -48.209  1.00  0.00           H
ATOM   4606  HG3 LYS A 299      23.034 -31.617 -47.429  1.00  0.00           H
ATOM   4607  HD2 LYS A 299      21.862 -29.308 -49.057  1.00  0.00           H
ATOM   4608  HD3 LYS A 299      20.962 -30.678 -48.373  1.00  0.00           H
ATOM   4609  HE2 LYS A 299      21.263 -31.194 -50.685  1.00  0.00           H
ATOM   4610  HE3 LYS A 299      22.455 -32.191 -49.819  1.00  0.00           H
ATOM   4611  HZ1 LYS A 299      23.164 -29.542 -50.850  1.00  0.00           H
ATOM   4612  HZ2 LYS A 299      23.218 -30.869 -51.828  1.00  0.00           H
ATOM   4613  HZ3 LYS A 299      24.157 -30.805 -50.474  1.00  0.00           H
ATOM   4614  N   ILE A 300      25.305 -31.553 -45.354  1.00 10.66           N
ANISOU 4614  N   ILE A 300      923   1356   1773    380     83   -204       N
ATOM   4615  CA  ILE A 300      25.720 -32.800 -44.672  1.00 10.99           C
ANISOU 4615  CA  ILE A 300      962   1357   1856    411     26   -212       C
ATOM   4616  C   ILE A 300      26.644 -32.463 -43.501  1.00 12.25           C
ANISOU 4616  C   ILE A 300     1123   1485   2047    427    -55   -212       C
ATOM   4617  O   ILE A 300      27.714 -31.887 -43.708  1.00 13.85           O
ANISOU 4617  O   ILE A 300     1241   1698   2324    429    -60   -254       O
ATOM   4618  CB  ILE A 300      26.430 -33.745 -45.628  1.00 11.28           C
ANISOU 4618  CB  ILE A 300      937   1395   1953    438     42   -261       C
ATOM   4619  CG1 ILE A 300      25.470 -34.180 -46.722  1.00 11.48           C
ANISOU 4619  CG1 ILE A 300      990   1437   1937    437     92   -267       C
ATOM   4620  CG2 ILE A 300      26.948 -35.026 -44.871  1.00 13.40           C
ANISOU 4620  CG2 ILE A 300     1212   1607   2274    484    -48   -276       C
ATOM   4621  CD1 ILE A 300      26.208 -34.789 -47.958  1.00 14.54           C
ANISOU 4621  CD1 ILE A 300     1344   1829   2350    445    142   -314       C
ATOM   4622  H   ILE A 300      25.818 -31.231 -46.163  1.00  0.00           H
ATOM   4623  HA  ILE A 300      24.832 -33.298 -44.284  1.00  0.00           H
ATOM   4624  HB  ILE A 300      27.277 -33.228 -46.079  1.00  0.00           H
ATOM   4625 HG12 ILE A 300      24.793 -34.931 -46.315  1.00  0.00           H
ATOM   4626 HG13 ILE A 300      24.888 -33.317 -47.047  1.00  0.00           H
ATOM   4627 HG21 ILE A 300      27.639 -34.728 -44.082  1.00  0.00           H
ATOM   4628 HG22 ILE A 300      26.102 -35.555 -44.432  1.00  0.00           H
ATOM   4629 HG23 ILE A 300      27.461 -35.681 -45.575  1.00  0.00           H
ATOM   4630 HD11 ILE A 300      25.476 -35.083 -48.710  1.00  0.00           H
ATOM   4631 HD12 ILE A 300      26.779 -35.663 -47.645  1.00  0.00           H
ATOM   4632 HD13 ILE A 300      26.884 -34.045 -48.380  1.00  0.00           H
ATOM   4633  N   THR A 301      26.237 -32.836 -42.288  1.00 12.84           N
ANISOU 4633  N   THR A 301     1308   1501   2070    436   -114   -177       N
ATOM   4634  CA  THR A 301      27.070 -32.624 -41.099  1.00 16.14           C
ANISOU 4634  CA  THR A 301     1779   1859   2493    472   -233   -182       C
ATOM   4635  C   THR A 301      26.933 -33.763 -40.109  1.00 16.08           C
ANISOU 4635  C   THR A 301     1939   1746   2424    509   -315   -161       C
ATOM   4636  O   THR A 301      26.005 -34.584 -40.189  1.00 17.09           O
ANISOU 4636  O   THR A 301     2146   1848   2501    484   -240   -135       O
ATOM   4637  CB  THR A 301      26.706 -31.303 -40.377  1.00 19.78           C
ANISOU 4637  CB  THR A 301     2287   2332   2895    435   -219   -148       C
ATOM   4638  OG1 THR A 301      25.399 -31.406 -39.830  1.00 21.61           O
ANISOU 4638  OG1 THR A 301     2647   2535   3030    392   -146   -102       O
ATOM   4639  CG2 THR A 301      26.712 -30.144 -41.362  1.00 20.72           C
ANISOU 4639  CG2 THR A 301     2283   2538   3052    394   -132   -159       C
ATOM   4640  H   THR A 301      25.333 -33.275 -42.185  1.00  0.00           H
ATOM   4641  HA  THR A 301      28.112 -32.567 -41.415  1.00  0.00           H
ATOM   4642  HB  THR A 301      27.424 -31.111 -39.579  1.00  0.00           H
ATOM   4643  HG1 THR A 301      25.449 -31.790 -38.952  1.00  0.00           H
ATOM   4644 HG21 THR A 301      26.454 -29.222 -40.841  1.00  0.00           H
ATOM   4645 HG22 THR A 301      27.704 -30.047 -41.802  1.00  0.00           H
ATOM   4646 HG23 THR A 301      25.982 -30.332 -42.149  1.00  0.00           H
ATOM   4647  N   TYR A 302      27.895 -33.835 -39.189  1.00 15.14           N
ANISOU 4647  N   TYR A 302     1888   1547   2319    574   -479   -186       N
ATOM   4648  CA  TYR A 302      27.897 -34.832 -38.142  1.00 14.67           C
ANISOU 4648  CA  TYR A 302     2056   1349   2169    625   -592   -166       C
ATOM   4649  C   TYR A 302      28.414 -34.126 -36.913  1.00 17.09           C
ANISOU 4649  C   TYR A 302     2499   1575   2419    667   -739   -168       C
ATOM   4650  O   TYR A 302      29.445 -33.438 -36.988  1.00 17.78           O
ANISOU 4650  O   TYR A 302     2436   1689   2632    711   -852   -238       O
ATOM   4651  CB  TYR A 302      28.798 -36.015 -38.483  1.00 14.61           C
ANISOU 4651  CB  TYR A 302     2001   1290   2260    707   -721   -228       C
ATOM   4652  CG  TYR A 302      28.877 -36.996 -37.357  1.00 15.98           C
ANISOU 4652  CG  TYR A 302     2456   1296   2320    771   -867   -207       C
ATOM   4653  CD1 TYR A 302      29.881 -36.912 -36.397  1.00 17.49           C
ANISOU 4653  CD1 TYR A 302     2732   1427   2488    809  -1064   -256       C
ATOM   4654  CD2 TYR A 302      27.898 -38.011 -37.209  1.00 16.06           C
ANISOU 4654  CD2 TYR A 302     2657   1234   2211    735   -761   -145       C
ATOM   4655  CE1 TYR A 302      29.968 -37.861 -35.338  1.00 19.06           C
ANISOU 4655  CE1 TYR A 302     3221   1486   2535    842  -1190   -245       C
ATOM   4656  CE2 TYR A 302      27.972 -38.933 -36.160  1.00 17.59           C
ANISOU 4656  CE2 TYR A 302     3149   1272   2263    766   -862   -122       C
ATOM   4657  CZ  TYR A 302      29.002 -38.834 -35.226  1.00 19.10           C
ANISOU 4657  CZ  TYR A 302     3433   1416   2410    816  -1078   -168       C
ATOM   4658  OH  TYR A 302      29.049 -39.735 -34.193  1.00 20.88           O
ANISOU 4658  OH  TYR A 302     3965   1505   2462    834  -1173   -156       O
ATOM   4659  H   TYR A 302      28.652 -33.167 -39.225  1.00  0.00           H
ATOM   4660  HA  TYR A 302      26.880 -35.182 -37.965  1.00  0.00           H
ATOM   4661  HB2 TYR A 302      29.800 -35.644 -38.699  1.00  0.00           H
ATOM   4662  HB3 TYR A 302      28.406 -36.518 -39.367  1.00  0.00           H
ATOM   4663  HD1 TYR A 302      30.606 -36.114 -36.456  1.00  0.00           H
ATOM   4664  HD2 TYR A 302      27.084 -38.073 -37.916  1.00  0.00           H
ATOM   4665  HE1 TYR A 302      30.783 -37.817 -34.631  1.00  0.00           H
ATOM   4666  HE2 TYR A 302      27.235 -39.718 -36.074  1.00  0.00           H
ATOM   4667  HH  TYR A 302      28.494 -40.490 -34.401  1.00  0.00           H
ATOM   4668  N   GLY A 303      27.679 -34.238 -35.807  1.00 19.28           N
ANISOU 4668  N   GLY A 303     3061   1746   2517    645   -719   -104       N
ATOM   4669  CA  GLY A 303      28.104 -33.709 -34.524  1.00 20.44           C
ANISOU 4669  CA  GLY A 303     3416   1783   2567    694   -875   -101       C
ATOM   4670  C   GLY A 303      27.346 -32.472 -34.092  1.00 20.58           C
ANISOU 4670  C   GLY A 303     3470   1846   2505    610   -740    -58       C
ATOM   4671  O   GLY A 303      26.243 -32.181 -34.590  1.00 21.82           O
ANISOU 4671  O   GLY A 303     3553   2085   2654    508   -515    -24       O
ATOM   4672  H   GLY A 303      26.788 -34.711 -35.864  1.00  0.00           H
ATOM   4673  HA2 GLY A 303      27.959 -34.482 -33.769  1.00  0.00           H
ATOM   4674  HA3 GLY A 303      29.166 -33.468 -34.579  1.00  0.00           H
ATOM   4675  N   ALA A 304      27.957 -31.700 -33.195  1.00 20.71           N
ANISOU 4675  N   ALA A 304     3581   1805   2484    660   -895    -76       N
ATOM   4676  CA  ALA A 304      27.338 -30.449 -32.719  1.00 22.94           C
ANISOU 4676  CA  ALA A 304     3895   2124   2696    587   -785    -43       C
ATOM   4677  C   ALA A 304      27.628 -29.309 -33.717  1.00 22.85           C
ANISOU 4677  C   ALA A 304     3535   2287   2861    556   -733    -79       C
ATOM   4678  O   ALA A 304      28.704 -28.712 -33.689  1.00 25.97           O
ANISOU 4678  O   ALA A 304     3804   2695   3370    617   -887   -143       O
ATOM   4679  CB  ALA A 304      27.872 -30.094 -31.340  1.00 25.84           C
ANISOU 4679  CB  ALA A 304     4528   2351   2938    654   -977    -52       C
ATOM   4680  H   ALA A 304      28.859 -31.976 -32.835  1.00  0.00           H
ATOM   4681  HA  ALA A 304      26.260 -30.593 -32.653  1.00  0.00           H
ATOM   4682  HB1 ALA A 304      27.409 -29.169 -30.998  1.00  0.00           H
ATOM   4683  HB2 ALA A 304      27.637 -30.898 -30.642  1.00  0.00           H
ATOM   4684  HB3 ALA A 304      28.953 -29.962 -31.392  1.00  0.00           H
ATOM   4685  N   CYS A 305      26.675 -29.038 -34.603  1.00 18.87           N
ANISOU 4685  N   CYS A 305     2890   1894   2385    464   -520    -51       N
ATOM   4686  CA  CYS A 305      26.931 -28.269 -35.796  1.00 17.43           C
ANISOU 4686  CA  CYS A 305     2427   1851   2346    440   -462    -80       C
ATOM   4687  C   CYS A 305      25.974 -27.092 -35.895  1.00 17.33           C
ANISOU 4687  C   CYS A 305     2376   1906   2304    359   -319    -51       C
ATOM   4688  O   CYS A 305      24.849 -27.197 -35.477  1.00 17.90           O
ANISOU 4688  O   CYS A 305     2567   1944   2289    304   -207    -21       O
ATOM   4689  CB  CYS A 305      26.713 -29.142 -37.016  1.00 17.14           C
ANISOU 4689  CB  CYS A 305     2268   1869   2375    429   -378    -88       C
ATOM   4690  SG  CYS A 305      28.047 -30.351 -37.250  1.00 23.49           S
ANISOU 4690  SG  CYS A 305     3022   2619   3284    527   -543   -153       S
ATOM   4691  H   CYS A 305      25.740 -29.382 -34.435  1.00  0.00           H
ATOM   4692  HA  CYS A 305      27.959 -27.906 -35.784  1.00  0.00           H
ATOM   4693  HB2 CYS A 305      25.771 -29.678 -36.899  1.00  0.00           H
ATOM   4694  HB3 CYS A 305      26.651 -28.507 -37.900  1.00  0.00           H
ATOM   4695  N   PRO A 306      26.452 -25.967 -36.432  1.00 16.11           N
ANISOU 4695  N   PRO A 306     2056   1831   2235    349   -320    -74       N
ATOM   4696  CA  PRO A 306      25.503 -24.906 -36.785  1.00 14.96           C
ANISOU 4696  CA  PRO A 306     1860   1748   2073    281   -195    -51       C
ATOM   4697  C   PRO A 306      24.484 -25.463 -37.815  1.00 17.08           C
ANISOU 4697  C   PRO A 306     2082   2056   2353    249    -79    -46       C
ATOM   4698  O   PRO A 306      24.775 -26.429 -38.540  1.00 15.27           O
ANISOU 4698  O   PRO A 306     1808   1834   2160    275    -85    -59       O
ATOM   4699  CB  PRO A 306      26.387 -23.817 -37.400  1.00 13.68           C
ANISOU 4699  CB  PRO A 306     1544   1647   2008    282   -214    -81       C
ATOM   4700  CG  PRO A 306      27.804 -24.128 -36.965  1.00 14.80           C
ANISOU 4700  CG  PRO A 306     1652   1741   2232    347   -359   -138       C
ATOM   4701  CD  PRO A 306      27.839 -25.644 -36.792  1.00 15.65           C
ANISOU 4701  CD  PRO A 306     1848   1790   2310    395   -419   -137       C
ATOM   4702  HA  PRO A 306      24.992 -24.534 -35.897  1.00  0.00           H
ATOM   4703  HB2 PRO A 306      26.086 -22.835 -37.034  1.00  0.00           H
ATOM   4704  HB3 PRO A 306      26.315 -23.848 -38.487  1.00  0.00           H
ATOM   4705  HG2 PRO A 306      28.034 -23.629 -36.023  1.00  0.00           H
ATOM   4706  HG3 PRO A 306      28.511 -23.821 -37.736  1.00  0.00           H
ATOM   4707  HD2 PRO A 306      28.128 -26.138 -37.720  1.00  0.00           H
ATOM   4708  HD3 PRO A 306      28.517 -25.921 -35.985  1.00  0.00           H
ATOM   4709  N   LYS A 307      23.325 -24.821 -37.904  1.00 18.10           N
ANISOU 4709  N   LYS A 307     2207   2201   2469    199     10    -45       N
ATOM   4710  CA  LYS A 307      22.281 -25.209 -38.864  1.00 19.68           C
ANISOU 4710  CA  LYS A 307     2351   2420   2708    182     84    -70       C
ATOM   4711  C   LYS A 307      22.612 -24.702 -40.257  1.00 16.36           C
ANISOU 4711  C   LYS A 307     1827   2063   2325    202     67    -78       C
ATOM   4712  O   LYS A 307      23.078 -23.546 -40.455  1.00 14.92           O
ANISOU 4712  O   LYS A 307     1615   1911   2143    197     53    -69       O
ATOM   4713  CB  LYS A 307      20.945 -24.653 -38.376  1.00 23.31           C
ANISOU 4713  CB  LYS A 307     2831   2847   3178    131    163   -101       C
ATOM   4714  CG  LYS A 307      20.643 -25.226 -36.978  1.00 29.91           C
ANISOU 4714  CG  LYS A 307     3824   3589   3952     93    227    -96       C
ATOM   4715  CD  LYS A 307      19.302 -24.894 -36.469  1.00 38.06           C
ANISOU 4715  CD  LYS A 307     4872   4564   5023     23    357   -154       C
ATOM   4716  CE  LYS A 307      19.069 -25.508 -35.060  1.00 48.09           C
ANISOU 4716  CE  LYS A 307     6361   5709   6200    -30    464   -149       C
ATOM   4717  NZ  LYS A 307      19.669 -24.663 -33.958  1.00 49.24           N
ANISOU 4717  NZ  LYS A 307     6645   5829   6234    -31    418   -105       N
ATOM   4718  H   LYS A 307      23.154 -24.038 -37.290  1.00  0.00           H
ATOM   4719  HA  LYS A 307      22.218 -26.297 -38.893  1.00  0.00           H
ATOM   4720  HB2 LYS A 307      20.154 -24.943 -39.068  1.00  0.00           H
ATOM   4721  HB3 LYS A 307      21.001 -23.566 -38.320  1.00  0.00           H
ATOM   4722  HG2 LYS A 307      21.381 -24.832 -36.280  1.00  0.00           H
ATOM   4723  HG3 LYS A 307      20.743 -26.311 -37.016  1.00  0.00           H
ATOM   4724  HD2 LYS A 307      19.204 -23.810 -36.405  1.00  0.00           H
ATOM   4725  HD3 LYS A 307      18.551 -25.282 -37.158  1.00  0.00           H
ATOM   4726  HE2 LYS A 307      19.524 -26.498 -35.030  1.00  0.00           H
ATOM   4727  HE3 LYS A 307      17.997 -25.605 -34.888  1.00  0.00           H
ATOM   4728  HZ1 LYS A 307      19.745 -25.214 -33.115  1.00  0.00           H
ATOM   4729  HZ2 LYS A 307      19.076 -23.864 -33.786  1.00  0.00           H
ATOM   4730  HZ3 LYS A 307      20.587 -24.346 -34.237  1.00  0.00           H
ATOM   4731  N   TYR A 308      22.370 -25.551 -41.235  1.00 13.39           N
ANISOU 4731  N   TYR A 308     1423   1695   1972    222     79    -97       N
ATOM   4732  CA  TYR A 308      22.677 -25.175 -42.594  1.00 12.21           C
ANISOU 4732  CA  TYR A 308     1237   1579   1824    241     77   -105       C
ATOM   4733  C   TYR A 308      21.656 -24.179 -43.104  1.00 11.81           C
ANISOU 4733  C   TYR A 308     1198   1522   1767    238     66   -126       C
ATOM   4734  O   TYR A 308      20.462 -24.409 -42.994  1.00 12.39           O
ANISOU 4734  O   TYR A 308     1259   1566   1881    239     60   -171       O
ATOM   4735  CB  TYR A 308      22.701 -26.389 -43.533  1.00 13.07           C
ANISOU 4735  CB  TYR A 308     1336   1686   1945    270     83   -125       C
ATOM   4736  CG  TYR A 308      23.100 -26.000 -44.954  1.00 13.82           C
ANISOU 4736  CG  TYR A 308     1449   1792   2010    284     99   -134       C
ATOM   4737  CD1 TYR A 308      24.430 -25.824 -45.302  1.00 14.50           C
ANISOU 4737  CD1 TYR A 308     1518   1886   2104    271    146   -132       C
ATOM   4738  CD2 TYR A 308      22.143 -25.782 -45.917  1.00 14.64           C
ANISOU 4738  CD2 TYR A 308     1605   1873   2083    309     69   -160       C
ATOM   4739  CE1 TYR A 308      24.800 -25.474 -46.578  1.00 16.82           C
ANISOU 4739  CE1 TYR A 308     1872   2163   2354    265    208   -144       C
ATOM   4740  CE2 TYR A 308      22.482 -25.413 -47.210  1.00 16.05           C
ANISOU 4740  CE2 TYR A 308     1875   2033   2193    323     85   -164       C
ATOM   4741  CZ  TYR A 308      23.800 -25.253 -47.542  1.00 17.76           C
ANISOU 4741  CZ  TYR A 308     2101   2254   2393    292    176   -149       C
ATOM   4742  OH  TYR A 308      24.130 -24.914 -48.831  1.00 18.96           O
ANISOU 4742  OH  TYR A 308     2386   2360   2459    289    236   -157       O
ATOM   4743  H   TYR A 308      21.973 -26.458 -41.035  1.00  0.00           H
ATOM   4744  HA  TYR A 308      23.660 -24.704 -42.610  1.00  0.00           H
ATOM   4745  HB2 TYR A 308      21.707 -26.837 -43.556  1.00  0.00           H
ATOM   4746  HB3 TYR A 308      23.413 -27.121 -43.151  1.00  0.00           H
ATOM   4747  HD1 TYR A 308      25.194 -25.965 -44.552  1.00  0.00           H
ATOM   4748  HD2 TYR A 308      21.101 -25.901 -45.660  1.00  0.00           H
ATOM   4749  HE1 TYR A 308      25.843 -25.370 -46.837  1.00  0.00           H
ATOM   4750  HE2 TYR A 308      21.711 -25.253 -47.950  1.00  0.00           H
ATOM   4751  HH  TYR A 308      25.026 -24.570 -48.852  1.00  0.00           H
ATOM   4752  N   VAL A 309      22.141 -23.080 -43.682  1.00 11.58           N
ANISOU 4752  N   VAL A 309     1194   1503   1702    235     64   -110       N
ATOM   4753  CA  VAL A 309      21.290 -22.106 -44.325  1.00 11.60           C
ANISOU 4753  CA  VAL A 309     1244   1480   1683    250     22   -131       C
ATOM   4754  C   VAL A 309      21.834 -21.720 -45.699  1.00 11.65           C
ANISOU 4754  C   VAL A 309     1353   1464   1611    267     33   -120       C
ATOM   4755  O   VAL A 309      23.011 -21.980 -46.046  1.00 13.10           O
ANISOU 4755  O   VAL A 309     1542   1659   1777    245    113   -101       O
ATOM   4756  CB  VAL A 309      21.126 -20.816 -43.468  1.00 14.07           C
ANISOU 4756  CB  VAL A 309     1548   1795   2002    221     15   -120       C
ATOM   4757  CG1 VAL A 309      20.481 -21.097 -42.110  1.00 14.75           C
ANISOU 4757  CG1 VAL A 309     1582   1877   2145    194     31   -139       C
ATOM   4758  CG2 VAL A 309      22.489 -20.071 -43.318  1.00 14.03           C
ANISOU 4758  CG2 VAL A 309     1551   1811   1968    190     63    -75       C
ATOM   4759  H   VAL A 309      23.139 -22.923 -43.670  1.00  0.00           H
ATOM   4760  HA  VAL A 309      20.305 -22.552 -44.462  1.00  0.00           H
ATOM   4761  HB  VAL A 309      20.454 -20.152 -44.012  1.00  0.00           H
ATOM   4762 HG11 VAL A 309      19.534 -21.617 -42.257  1.00  0.00           H
ATOM   4763 HG12 VAL A 309      21.148 -21.719 -41.513  1.00  0.00           H
ATOM   4764 HG13 VAL A 309      20.302 -20.155 -41.591  1.00  0.00           H
ATOM   4765 HG21 VAL A 309      22.349 -19.174 -42.716  1.00  0.00           H
ATOM   4766 HG22 VAL A 309      23.210 -20.727 -42.830  1.00  0.00           H
ATOM   4767 HG23 VAL A 309      22.861 -19.792 -44.304  1.00  0.00           H
ATOM   4768  N   LYS A 310      20.995 -21.067 -46.479  1.00 10.89           N
ANISOU 4768  N   LYS A 310     1352   1316   1472    305    -43   -146       N
ATOM   4769  CA  LYS A 310      21.368 -20.716 -47.834  1.00 13.15           C
ANISOU 4769  CA  LYS A 310     1812   1544   1642    325    -34   -136       C
ATOM   4770  C   LYS A 310      22.255 -19.475 -47.904  1.00 12.99           C
ANISOU 4770  C   LYS A 310     1876   1502   1557    274     53    -92       C
ATOM   4771  O   LYS A 310      22.989 -19.283 -48.855  1.00 14.02           O
ANISOU 4771  O   LYS A 310     2152   1580   1595    253    146    -78       O
ATOM   4772  CB  LYS A 310      20.103 -20.458 -48.643  1.00 18.82           C
ANISOU 4772  CB  LYS A 310     2643   2181   2326    406   -193   -191       C
ATOM   4773  CG  LYS A 310      19.398 -21.735 -49.032  1.00 25.15           C
ANISOU 4773  CG  LYS A 310     3398   2975   3184    460   -265   -253       C
ATOM   4774  CD  LYS A 310      18.135 -21.438 -49.832  1.00 31.98           C
ANISOU 4774  CD  LYS A 310     4361   3739   4051    558   -465   -342       C
ATOM   4775  CE  LYS A 310      17.219 -20.515 -49.075  1.00 37.20           C
ANISOU 4775  CE  LYS A 310     4931   4380   4822    569   -557   -397       C
ATOM   4776  NZ  LYS A 310      15.926 -20.281 -49.783  1.00 41.71           N
ANISOU 4776  NZ  LYS A 310     5556   4836   5454    681   -790   -523       N
ATOM   4777  H   LYS A 310      20.084 -20.809 -46.128  1.00  0.00           H
ATOM   4778  HA  LYS A 310      21.903 -21.555 -48.279  1.00  0.00           H
ATOM   4779  HB2 LYS A 310      20.372 -19.917 -49.550  1.00  0.00           H
ATOM   4780  HB3 LYS A 310      19.423 -19.844 -48.052  1.00  0.00           H
ATOM   4781  HG2 LYS A 310      20.070 -22.343 -49.638  1.00  0.00           H
ATOM   4782  HG3 LYS A 310      19.131 -22.286 -48.131  1.00  0.00           H
ATOM   4783  HD2 LYS A 310      18.413 -20.968 -50.775  1.00  0.00           H
ATOM   4784  HD3 LYS A 310      17.613 -22.372 -50.037  1.00  0.00           H
ATOM   4785  HE2 LYS A 310      17.722 -19.557 -48.941  1.00  0.00           H
ATOM   4786  HE3 LYS A 310      17.013 -20.946 -48.095  1.00  0.00           H
ATOM   4787  HZ1 LYS A 310      15.278 -21.021 -49.555  1.00  0.00           H
ATOM   4788  HZ2 LYS A 310      15.539 -19.394 -49.493  1.00  0.00           H
ATOM   4789  HZ3 LYS A 310      16.086 -20.269 -50.780  1.00  0.00           H
ATOM   4790  N   GLN A 311      22.096 -18.585 -46.948  1.00 12.84           N
ANISOU 4790  N   GLN A 311     1786   1506   1586    251     33    -81       N
ATOM   4791  CA  GLN A 311      22.802 -17.303 -46.975  1.00 14.17           C
ANISOU 4791  CA  GLN A 311     2030   1645   1708    204    106    -49       C
ATOM   4792  C   GLN A 311      24.289 -17.529 -46.735  1.00 15.05           C
ANISOU 4792  C   GLN A 311     2058   1787   1871    135    262    -41       C
ATOM   4793  O   GLN A 311      24.649 -18.378 -45.924  1.00 14.83           O
ANISOU 4793  O   GLN A 311     1872   1823   1939    131    261    -53       O
ATOM   4794  CB  GLN A 311      22.302 -16.427 -45.840  1.00 13.70           C
ANISOU 4794  CB  GLN A 311     1879   1614   1712    195     44    -49       C
ATOM   4795  CG  GLN A 311      20.873 -15.943 -46.010  1.00 14.07           C
ANISOU 4795  CG  GLN A 311     1978   1613   1757    258   -108    -88       C
ATOM   4796  CD  GLN A 311      19.881 -16.834 -45.218  1.00 14.00           C
ANISOU 4796  CD  GLN A 311     1809   1643   1867    280   -169   -145       C
ATOM   4797  OE1 GLN A 311      20.092 -18.060 -45.070  1.00 13.07           O
ANISOU 4797  OE1 GLN A 311     1620   1565   1781    274   -124   -146       O
ATOM   4798  NE2 GLN A 311      18.811 -16.213 -44.720  1.00 13.19           N
ANISOU 4798  NE2 GLN A 311     1657   1515   1842    300   -256   -202       N
ATOM   4799  H   GLN A 311      21.474 -18.791 -46.179  1.00  0.00           H
ATOM   4800  HA  GLN A 311      22.645 -16.806 -47.932  1.00  0.00           H
ATOM   4801  HB2 GLN A 311      22.952 -15.555 -45.770  1.00  0.00           H
ATOM   4802  HB3 GLN A 311      22.371 -16.989 -44.909  1.00  0.00           H
ATOM   4803  HG2 GLN A 311      20.799 -14.918 -45.646  1.00  0.00           H
ATOM   4804  HG3 GLN A 311      20.610 -15.967 -47.068  1.00  0.00           H
ATOM   4805 HE21 GLN A 311      18.688 -15.222 -44.869  1.00  0.00           H
ATOM   4806 HE22 GLN A 311      18.124 -16.734 -44.194  1.00  0.00           H
ATOM   4807  N   ASN A 312      25.150 -16.748 -47.375  1.00 17.90           N
ANISOU 4807  N   ASN A 312     2530   2087   2186     81    393    -37       N
ATOM   4808  CA  ASN A 312      26.576 -16.929 -47.112  1.00 22.34           C
ANISOU 4808  CA  ASN A 312     2966   2661   2859     14    543    -71       C
ATOM   4809  C   ASN A 312      27.079 -15.974 -46.044  1.00 20.40           C
ANISOU 4809  C   ASN A 312     2600   2439   2712    -25    549    -79       C
ATOM   4810  O   ASN A 312      28.173 -16.139 -45.522  1.00 19.55           O
ANISOU 4810  O   ASN A 312     2337   2345   2746    -60    613   -131       O
ATOM   4811  CB  ASN A 312      27.419 -16.877 -48.391  1.00 28.84           C
ANISOU 4811  CB  ASN A 312     3940   3390   3628    -45    741    -99       C
ATOM   4812  CG  ASN A 312      27.252 -15.603 -49.142  1.00 37.76           C
ANISOU 4812  CG  ASN A 312     5321   4410   4615    -77    812    -70       C
ATOM   4813  OD1 ASN A 312      27.127 -14.544 -48.553  1.00 41.32           O
ANISOU 4813  OD1 ASN A 312     5758   4861   5081    -91    779    -51       O
ATOM   4814  ND2 ASN A 312      27.243 -15.692 -50.475  1.00 43.35           N
ANISOU 4814  ND2 ASN A 312     6297   5008   5165    -87    909    -66       N
ATOM   4815  H   ASN A 312      24.828 -16.047 -48.027  1.00  0.00           H
ATOM   4816  HA  ASN A 312      26.691 -17.934 -46.707  1.00  0.00           H
ATOM   4817  HB2 ASN A 312      28.469 -16.986 -48.120  1.00  0.00           H
ATOM   4818  HB3 ASN A 312      27.133 -17.707 -49.036  1.00  0.00           H
ATOM   4819 HD21 ASN A 312      27.348 -16.592 -50.922  1.00  0.00           H
ATOM   4820 HD22 ASN A 312      27.131 -14.860 -51.036  1.00  0.00           H
ATOM   4821  N   THR A 313      26.245 -15.013 -45.669  1.00 17.80           N
ANISOU 4821  N   THR A 313     2328   2108   2327     -7    458    -42       N
ATOM   4822  CA  THR A 313      26.586 -14.111 -44.597  1.00 16.06           C
ANISOU 4822  CA  THR A 313     2000   1911   2189    -35    444    -47       C
ATOM   4823  C   THR A 313      25.306 -13.578 -43.975  1.00 14.47           C
ANISOU 4823  C   THR A 313     1821   1735   1941      9    298    -15       C
ATOM   4824  O   THR A 313      24.337 -13.274 -44.681  1.00 14.62           O
ANISOU 4824  O   THR A 313     1981   1709   1864     46    237      1       O
ATOM   4825  CB  THR A 313      27.461 -12.918 -45.116  1.00 19.34           C
ANISOU 4825  CB  THR A 313     2495   2245   2609   -112    603    -64       C
ATOM   4826  OG1 THR A 313      27.699 -11.994 -44.057  1.00 18.74           O
ANISOU 4826  OG1 THR A 313     2311   2192   2618   -132    568    -74       O
ATOM   4827  CG2 THR A 313      26.783 -12.178 -46.256  1.00 21.15           C
ANISOU 4827  CG2 THR A 313     2996   2378   2661   -109    625    -21       C
ATOM   4828  H   THR A 313      25.358 -14.912 -46.141  1.00  0.00           H
ATOM   4829  HA  THR A 313      27.147 -14.658 -43.839  1.00  0.00           H
ATOM   4830  HB  THR A 313      28.417 -13.307 -45.467  1.00  0.00           H
ATOM   4831  HG1 THR A 313      28.036 -12.464 -43.291  1.00  0.00           H
ATOM   4832 HG21 THR A 313      27.421 -11.359 -46.588  1.00  0.00           H
ATOM   4833 HG22 THR A 313      26.614 -12.865 -47.085  1.00  0.00           H
ATOM   4834 HG23 THR A 313      25.828 -11.780 -45.913  1.00  0.00           H
ATOM   4835  N   LEU A 314      25.325 -13.444 -42.657  1.00 12.54           N
ANISOU 4835  N   LEU A 314     1445   1544   1774      9    239    -21       N
ATOM   4836  CA  LEU A 314      24.273 -12.754 -41.916  1.00 13.17           C
ANISOU 4836  CA  LEU A 314     1527   1636   1839     28    143    -11       C
ATOM   4837  C   LEU A 314      24.900 -12.036 -40.718  1.00 14.26           C
ANISOU 4837  C   LEU A 314     1575   1796   2047     -2    141    -20       C
ATOM   4838  O   LEU A 314      25.478 -12.674 -39.806  1.00 15.42           O
ANISOU 4838  O   LEU A 314     1631   1974   2253      3    116    -38       O
ATOM   4839  CB  LEU A 314      23.223 -13.718 -41.385  1.00 14.14           C
ANISOU 4839  CB  LEU A 314     1609   1791   1971     68     65    -22       C
ATOM   4840  CG  LEU A 314      22.230 -14.346 -42.367  1.00 17.74           C
ANISOU 4840  CG  LEU A 314     2131   2219   2389    113     20    -38       C
ATOM   4841  CD1 LEU A 314      21.475 -15.526 -41.716  1.00 18.43           C
ANISOU 4841  CD1 LEU A 314     2144   2334   2527    131     -8    -67       C
ATOM   4842  CD2 LEU A 314      21.242 -13.315 -42.897  1.00 19.94           C
ANISOU 4842  CD2 LEU A 314     2499   2439   2638    144    -61    -57       C
ATOM   4843  H   LEU A 314      26.101 -13.836 -42.143  1.00  0.00           H
ATOM   4844  HA  LEU A 314      23.795 -12.021 -42.566  1.00  0.00           H
ATOM   4845  HB2 LEU A 314      22.638 -13.176 -40.642  1.00  0.00           H
ATOM   4846  HB3 LEU A 314      23.743 -14.528 -40.873  1.00  0.00           H
ATOM   4847  HG  LEU A 314      22.796 -14.735 -43.214  1.00  0.00           H
ATOM   4848 HD21 LEU A 314      21.788 -12.489 -43.353  1.00  0.00           H
ATOM   4849 HD22 LEU A 314      20.634 -12.938 -42.074  1.00  0.00           H
ATOM   4850 HD23 LEU A 314      20.597 -13.780 -43.642  1.00  0.00           H
ATOM   4851 HD11 LEU A 314      22.193 -16.255 -41.342  1.00  0.00           H
ATOM   4852 HD12 LEU A 314      20.831 -15.998 -42.458  1.00  0.00           H
ATOM   4853 HD13 LEU A 314      20.867 -15.157 -40.890  1.00  0.00           H
ATOM   4854  N   LYS A 315      24.776 -10.703 -40.704  1.00 13.33           N
ANISOU 4854  N   LYS A 315     1500   1649   1917    -24    146    -12       N
ATOM   4855  CA  LYS A 315      25.457  -9.917 -39.682  1.00 14.53           C
ANISOU 4855  CA  LYS A 315     1570   1811   2139    -53    145    -29       C
ATOM   4856  C   LYS A 315      24.498  -9.517 -38.553  1.00 13.65           C
ANISOU 4856  C   LYS A 315     1443   1724   2018    -36     56    -28       C
ATOM   4857  O   LYS A 315      23.428  -8.975 -38.808  1.00 14.36           O
ANISOU 4857  O   LYS A 315     1590   1795   2071    -24     22    -23       O
ATOM   4858  CB  LYS A 315      26.100  -8.661 -40.316  1.00 17.84           C
ANISOU 4858  CB  LYS A 315     2041   2171   2567   -104    238    -32       C
ATOM   4859  CG  LYS A 315      27.129  -8.974 -41.401  1.00 23.01           C
ANISOU 4859  CG  LYS A 315     2725   2774   3243   -146    383    -55       C
ATOM   4860  CD  LYS A 315      28.305  -9.661 -40.816  1.00 29.53           C
ANISOU 4860  CD  LYS A 315     3379   3623   4217   -156    403   -121       C
ATOM   4861  CE  LYS A 315      29.510  -9.724 -41.787  1.00 35.31           C
ANISOU 4861  CE  LYS A 315     4096   4284   5036   -222    592   -185       C
ATOM   4862  NZ  LYS A 315      29.828  -8.408 -42.391  1.00 39.54           N
ANISOU 4862  NZ  LYS A 315     4733   4731   5561   -299    743   -191       N
ATOM   4863  H   LYS A 315      24.210 -10.241 -41.402  1.00  0.00           H
ATOM   4864  HA  LYS A 315      26.252 -10.528 -39.254  1.00  0.00           H
ATOM   4865  HB2 LYS A 315      25.308  -8.056 -40.758  1.00  0.00           H
ATOM   4866  HB3 LYS A 315      26.585  -8.082 -39.530  1.00  0.00           H
ATOM   4867  HG2 LYS A 315      26.673  -9.619 -42.152  1.00  0.00           H
ATOM   4868  HG3 LYS A 315      27.451  -8.045 -41.871  1.00  0.00           H
ATOM   4869  HD2 LYS A 315      28.610  -9.124 -39.918  1.00  0.00           H
ATOM   4870  HD3 LYS A 315      28.020 -10.676 -40.541  1.00  0.00           H
ATOM   4871  HE2 LYS A 315      29.277 -10.427 -42.587  1.00  0.00           H
ATOM   4872  HE3 LYS A 315      30.384 -10.084 -41.243  1.00  0.00           H
ATOM   4873  HZ1 LYS A 315      30.830  -8.300 -42.454  1.00  0.00           H
ATOM   4874  HZ2 LYS A 315      29.446  -7.672 -41.815  1.00  0.00           H
ATOM   4875  HZ3 LYS A 315      29.425  -8.355 -43.316  1.00  0.00           H
ATOM   4876  N   LEU A 316      24.882  -9.813 -37.317  1.00 12.40           N
ANISOU 4876  N   LEU A 316     1224   1591   1897    -32     15    -45       N
ATOM   4877  CA  LEU A 316      24.182  -9.375 -36.133  1.00 12.48           C
ANISOU 4877  CA  LEU A 316     1245   1606   1891    -32    -34    -52       C
ATOM   4878  C   LEU A 316      24.805  -8.091 -35.612  1.00 12.88           C
ANISOU 4878  C   LEU A 316     1265   1645   1983    -55    -46    -66       C
ATOM   4879  O   LEU A 316      25.949  -8.084 -35.203  1.00 13.53           O
ANISOU 4879  O   LEU A 316     1294   1721   2128    -53    -68    -94       O
ATOM   4880  CB  LEU A 316      24.223 -10.461 -35.071  1.00 14.20           C
ANISOU 4880  CB  LEU A 316     1483   1826   2086    -11    -73    -60       C
ATOM   4881  CG  LEU A 316      23.430 -10.230 -33.803  1.00 15.50           C
ANISOU 4881  CG  LEU A 316     1712   1971   2207    -23    -85    -72       C
ATOM   4882  CD1 LEU A 316      21.968 -10.371 -34.063  1.00 15.34           C
ANISOU 4882  CD1 LEU A 316     1705   1942   2181    -40    -28    -89       C
ATOM   4883  CD2 LEU A 316      23.865 -11.155 -32.750  1.00 16.63           C
ANISOU 4883  CD2 LEU A 316     1936   2083   2299      0   -130    -76       C
ATOM   4884  H   LEU A 316      25.711 -10.377 -37.198  1.00  0.00           H
ATOM   4885  HA  LEU A 316      23.142  -9.179 -36.393  1.00  0.00           H
ATOM   4886  HB2 LEU A 316      25.266 -10.597 -34.783  1.00  0.00           H
ATOM   4887  HB3 LEU A 316      23.874 -11.389 -35.523  1.00  0.00           H
ATOM   4888  HG  LEU A 316      23.619  -9.212 -33.463  1.00  0.00           H
ATOM   4889 HD11 LEU A 316      21.669  -9.675 -34.847  1.00  0.00           H
ATOM   4890 HD12 LEU A 316      21.414 -10.150 -33.151  1.00  0.00           H
ATOM   4891 HD13 LEU A 316      21.752 -11.391 -34.381  1.00  0.00           H
ATOM   4892 HD21 LEU A 316      24.935 -11.034 -32.578  1.00  0.00           H
ATOM   4893 HD22 LEU A 316      23.661 -12.180 -33.060  1.00  0.00           H
ATOM   4894 HD23 LEU A 316      23.322 -10.939 -31.830  1.00  0.00           H
ATOM   4895  N   ALA A 317      24.043  -6.997 -35.615  1.00 12.49           N
ANISOU 4895  N   ALA A 317     1242   1583   1921    -70    -46    -62       N
ATOM   4896  CA  ALA A 317      24.561  -5.742 -35.085  1.00 12.32           C
ANISOU 4896  CA  ALA A 317     1193   1547   1939    -93    -56    -77       C
ATOM   4897  C   ALA A 317      25.015  -5.926 -33.638  1.00 12.15           C
ANISOU 4897  C   ALA A 317     1154   1533   1930    -81   -121   -105       C
ATOM   4898  O   ALA A 317      24.302  -6.527 -32.842  1.00 13.51           O
ANISOU 4898  O   ALA A 317     1383   1706   2043    -68   -142   -105       O
ATOM   4899  CB  ALA A 317      23.478  -4.640 -35.143  1.00 12.67           C
ANISOU 4899  CB  ALA A 317     1276   1573   1966   -101    -68    -76       C
ATOM   4900  H   ALA A 317      23.104  -7.038 -35.986  1.00  0.00           H
ATOM   4901  HA  ALA A 317      25.415  -5.430 -35.686  1.00  0.00           H
ATOM   4902  HB1 ALA A 317      23.883  -3.710 -34.743  1.00  0.00           H
ATOM   4903  HB2 ALA A 317      23.171  -4.487 -36.178  1.00  0.00           H
ATOM   4904  HB3 ALA A 317      22.616  -4.946 -34.550  1.00  0.00           H
ATOM   4905  N   THR A 318      26.170  -5.344 -33.277  1.00 11.33           N
ANISOU 4905  N   THR A 318      988   1412   1904    -85   -150   -141       N
ATOM   4906  CA  THR A 318      26.629  -5.365 -31.891  1.00 11.07           C
ANISOU 4906  CA  THR A 318      968   1363   1877    -55   -255   -180       C
ATOM   4907  C   THR A 318      27.006  -3.924 -31.455  1.00 14.41           C
ANISOU 4907  C   THR A 318     1345   1767   2364    -77   -275   -214       C
ATOM   4908  O   THR A 318      27.767  -3.732 -30.533  1.00 15.45           O
ANISOU 4908  O   THR A 318     1458   1869   2544    -48   -376   -269       O
ATOM   4909  CB  THR A 318      27.819  -6.327 -31.713  1.00 13.62           C
ANISOU 4909  CB  THR A 318     1245   1662   2269    -10   -335   -229       C
ATOM   4910  OG1 THR A 318      28.836  -5.992 -32.663  1.00 16.31           O
ANISOU 4910  OG1 THR A 318     1451   1991   2756    -36   -272   -275       O
ATOM   4911  CG2 THR A 318      27.376  -7.800 -31.965  1.00 16.83           C
ANISOU 4911  CG2 THR A 318     1719   2081   2595     15   -327   -193       C
ATOM   4912  H   THR A 318      26.732  -4.883 -33.978  1.00  0.00           H
ATOM   4913  HA  THR A 318      25.809  -5.712 -31.262  1.00  0.00           H
ATOM   4914  HB  THR A 318      28.217  -6.233 -30.703  1.00  0.00           H
ATOM   4915  HG1 THR A 318      29.584  -6.583 -32.552  1.00  0.00           H
ATOM   4916 HG21 THR A 318      28.230  -8.464 -31.835  1.00  0.00           H
ATOM   4917 HG22 THR A 318      26.994  -7.895 -32.981  1.00  0.00           H
ATOM   4918 HG23 THR A 318      26.594  -8.071 -31.256  1.00  0.00           H
ATOM   4919  N   GLY A 319      26.385  -2.922 -32.072  1.00 14.57           N
ANISOU 4919  N   GLY A 319     1366   1792   2379   -118   -198   -185       N
ATOM   4920  CA  GLY A 319      26.670  -1.538 -31.743  1.00 15.13           C
ANISOU 4920  CA  GLY A 319     1399   1841   2509   -143   -205   -212       C
ATOM   4921  C   GLY A 319      25.507  -0.731 -32.262  1.00 13.47           C
ANISOU 4921  C   GLY A 319     1244   1630   2244   -169   -154   -171       C
ATOM   4922  O   GLY A 319      24.622  -1.254 -32.987  1.00 13.04           O
ANISOU 4922  O   GLY A 319     1240   1584   2130   -161   -124   -137       O
ATOM   4923  H   GLY A 319      25.700  -3.129 -32.785  1.00  0.00           H
ATOM   4924  HA2 GLY A 319      26.761  -1.418 -30.663  1.00  0.00           H
ATOM   4925  HA3 GLY A 319      27.591  -1.221 -32.232  1.00  0.00           H
ATOM   4926  N   MET A 320      25.513   0.544 -31.916  1.00 10.89           N
ANISOU 4926  N   MET A 320      903   1282   1952   -190   -162   -189       N
ATOM   4927  CA  MET A 320      24.441   1.454 -32.325  1.00 10.73           C
ANISOU 4927  CA  MET A 320      934   1242   1901   -202   -147   -168       C
ATOM   4928  C   MET A 320      24.645   1.868 -33.802  1.00 12.40           C
ANISOU 4928  C   MET A 320     1198   1404   2111   -223    -77   -134       C
ATOM   4929  O   MET A 320      25.657   1.569 -34.426  1.00 13.51           O
ANISOU 4929  O   MET A 320     1324   1524   2286   -247     -4   -134       O
ATOM   4930  CB  MET A 320      24.495   2.673 -31.434  1.00 11.11           C
ANISOU 4930  CB  MET A 320      957   1276   1988   -217   -181   -201       C
ATOM   4931  CG  MET A 320      25.763   3.518 -31.625  1.00 13.65           C
ANISOU 4931  CG  MET A 320     1220   1561   2406   -250   -149   -225       C
ATOM   4932  SD  MET A 320      25.907   4.907 -30.449  1.00 13.30           S
ANISOU 4932  SD  MET A 320     1134   1499   2420   -262   -208   -276       S
ATOM   4933  CE  MET A 320      26.211   4.070 -28.909  1.00 12.98           C
ANISOU 4933  CE  MET A 320     1088   1490   2355   -214   -320   -323       C
ATOM   4934  H   MET A 320      26.275   0.899 -31.356  1.00  0.00           H
ATOM   4935  HA  MET A 320      23.476   0.959 -32.212  1.00  0.00           H
ATOM   4936  HB2 MET A 320      23.629   3.298 -31.652  1.00  0.00           H
ATOM   4937  HB3 MET A 320      24.442   2.350 -30.394  1.00  0.00           H
ATOM   4938  HG2 MET A 320      25.756   3.924 -32.637  1.00  0.00           H
ATOM   4939  HG3 MET A 320      26.634   2.872 -31.513  1.00  0.00           H
ATOM   4940  HE1 MET A 320      26.318   4.804 -28.111  1.00  0.00           H
ATOM   4941  HE2 MET A 320      25.375   3.408 -28.684  1.00  0.00           H
ATOM   4942  HE3 MET A 320      27.127   3.484 -28.989  1.00  0.00           H
ATOM   4943  N  AARG A 321      23.660   2.562 -34.336  0.48 13.07           N
ANISOU 4943  N  AARG A 321     1362   1448   2156   -212   -101   -119       N
ATOM   4944  N  BARG A 321      23.671   2.580 -34.331  0.52 13.07           N
ANISOU 4944  N  BARG A 321     1362   1447   2156   -212   -101   -119       N
ATOM   4945  CA AARG A 321      23.775   3.217 -35.626  0.48 13.66           C
ANISOU 4945  CA AARG A 321     1561   1437   2192   -226    -55    -86       C
ATOM   4946  CA BARG A 321      23.816   3.238 -35.615  0.52 13.55           C
ANISOU 4946  CA BARG A 321     1545   1422   2180   -228    -52    -86       C
ATOM   4947  C  AARG A 321      25.038   4.062 -35.670  0.48 14.27           C
ANISOU 4947  C  AARG A 321     1621   1468   2332   -290     47    -95       C
ATOM   4948  C  BARG A 321      25.072   4.060 -35.655  0.52 14.26           C
ANISOU 4948  C  BARG A 321     1618   1468   2335   -292     49    -96       C
ATOM   4949  O  AARG A 321      25.329   4.787 -34.720  0.48 14.15           O
ANISOU 4949  O  AARG A 321     1518   1468   2391   -307     24   -130       O
ATOM   4950  O  BARG A 321      25.386   4.774 -34.704  0.52 14.16           O
ANISOU 4950  O  BARG A 321     1514   1471   2396   -309     27   -132       O
ATOM   4951  CB AARG A 321      22.538   4.094 -35.830  0.48 16.09           C
ANISOU 4951  CB AARG A 321     1951   1690   2472   -188   -152    -93       C
ATOM   4952  CB BARG A 321      22.612   4.135 -35.863  0.52 15.98           C
ANISOU 4952  CB BARG A 321     1941   1673   2458   -191   -146    -91       C
ATOM   4953  CG AARG A 321      22.448   4.764 -37.158  0.48 18.30           C
ANISOU 4953  CG AARG A 321     2431   1850   2673   -180   -149    -57       C
ATOM   4954  CG BARG A 321      21.424   3.364 -36.303  0.52 17.40           C
ANISOU 4954  CG BARG A 321     2155   1852   2605   -128   -234   -105       C
ATOM   4955  CD AARG A 321      21.624   3.984 -38.125  0.48 23.18           C
ANISOU 4955  CD AARG A 321     3161   2432   3216   -115   -225    -50       C
ATOM   4956  CD BARG A 321      21.455   3.224 -37.785  0.52 21.87           C
ANISOU 4956  CD BARG A 321     2904   2330   3075   -105   -232    -65       C
ATOM   4957  NE AARG A 321      21.269   4.835 -39.245  0.48 27.37           N
ANISOU 4957  NE AARG A 321     3934   2815   3651    -82   -284    -28       N
ATOM   4958  NE BARG A 321      21.194   4.505 -38.426  0.52 25.37           N
ANISOU 4958  NE BARG A 321     3518   2650   3472    -90   -285    -54       N
ATOM   4959  CZ AARG A 321      22.105   5.186 -40.210  0.48 28.96           C
ANISOU 4959  CZ AARG A 321     4340   2912   3750   -127   -165     26       C
ATOM   4960  CZ BARG A 321      21.991   5.118 -39.291  0.52 28.24           C
ANISOU 4960  CZ BARG A 321     4067   2911   3751   -132   -188     -4       C
ATOM   4961  NH1AARG A 321      23.366   4.731 -40.208  0.48 30.55           N
ANISOU 4961  NH1AARG A 321     4481   3152   3975   -213     31     45       N
ATOM   4962  NH1BARG A 321      23.160   4.580 -39.656  0.52 29.67           N
ANISOU 4962  NH1BARG A 321     4257   3101   3915   -200    -13     26       N
ATOM   4963  NH2AARG A 321      21.678   5.990 -41.182  0.48 30.39           N
ANISOU 4963  NH2AARG A 321     4802   2931   3813    -87   -239     48       N
ATOM   4964  NH2BARG A 321      21.596   6.281 -39.807  0.52 29.27           N
ANISOU 4964  NH2BARG A 321     4387   2911   3823   -107   -259      4       N
ATOM   4965  H  AARG A 321      22.791   2.641 -33.827  0.48  0.00           H
ATOM   4966  H  BARG A 321      22.799   2.670 -33.829  0.52  0.00           H
ATOM   4967  HA AARG A 321      23.817   2.463 -36.412  0.48  0.00           H
ATOM   4968  HA BARG A 321      23.862   2.481 -36.398  0.52  0.00           H
ATOM   4969  HB2AARG A 321      22.542   4.867 -35.062  0.48  0.00           H
ATOM   4970  HB2BARG A 321      22.867   4.860 -36.636  0.52  0.00           H
ATOM   4971  HB3AARG A 321      21.650   3.476 -35.694  0.48  0.00           H
ATOM   4972  HB3BARG A 321      22.370   4.667 -34.943  0.52  0.00           H
ATOM   4973  HG2AARG A 321      23.453   4.876 -37.564  0.48  0.00           H
ATOM   4974  HG2BARG A 321      21.439   2.376 -35.843  0.52  0.00           H
ATOM   4975  HG3AARG A 321      22.005   5.751 -37.029  0.48  0.00           H
ATOM   4976  HG3BARG A 321      20.517   3.891 -36.006  0.52  0.00           H
ATOM   4977  HD2AARG A 321      22.196   3.129 -38.484  0.48  0.00           H
ATOM   4978  HD2BARG A 321      20.693   2.508 -38.093  0.52  0.00           H
ATOM   4979  HD3AARG A 321      20.717   3.634 -37.632  0.48  0.00           H
ATOM   4980  HD3BARG A 321      22.436   2.861 -38.092  0.52  0.00           H
ATOM   4981  HE AARG A 321      20.322   5.183 -39.292  0.48  0.00           H
ATOM   4982  HE BARG A 321      20.328   4.969 -38.191  0.52  0.00           H
ATOM   4983 HH11AARG A 321      24.001   4.999 -40.946  0.48  0.00           H
ATOM   4984 HH11BARG A 321      23.452   3.695 -39.267  0.52  0.00           H
ATOM   4985 HH12AARG A 321      23.681   4.120 -39.468  0.48  0.00           H
ATOM   4986 HH12BARG A 321      23.751   5.059 -40.321  0.52  0.00           H
ATOM   4987 HH21AARG A 321      22.306   6.263 -41.924  0.48  0.00           H
ATOM   4988 HH21BARG A 321      22.183   6.764 -40.472  0.52  0.00           H
ATOM   4989 HH22AARG A 321      20.726   6.327 -41.177  0.48  0.00           H
ATOM   4990 HH22BARG A 321      20.710   6.680 -39.533  0.52  0.00           H
ATOM   4991  N   ASN A 322      25.796   3.955 -36.758  1.00 14.33           N
ANISOU 4991  N   ASN A 322     1714   1406   2323   -333    174    -77       N
ATOM   4992  CA  ASN A 322      27.019   4.744 -36.943  1.00 14.79           C
ANISOU 4992  CA  ASN A 322     1756   1391   2472   -414    322   -111       C
ATOM   4993  C   ASN A 322      26.676   5.976 -37.743  1.00 16.54           C
ANISOU 4993  C   ASN A 322     2186   1488   2610   -440    368    -72       C
ATOM   4994  O   ASN A 322      26.385   5.878 -38.935  1.00 18.48           O
ANISOU 4994  O   ASN A 322     2653   1643   2727   -438    416    -24       O
ATOM   4995  CB  ASN A 322      28.100   3.964 -37.676  1.00 14.92           C
ANISOU 4995  CB  ASN A 322     1756   1375   2540   -466    483   -138       C
ATOM   4996  CG  ASN A 322      29.455   4.658 -37.615  1.00 16.14           C
ANISOU 4996  CG  ASN A 322     1813   1453   2866   -558    649   -223       C
ATOM   4997  OD1 ASN A 322      29.857   5.127 -36.551  1.00 15.80           O
ANISOU 4997  OD1 ASN A 322     1600   1445   2957   -556    582   -286       O
ATOM   4998  ND2 ASN A 322      30.130   4.772 -38.739  1.00 17.15           N
ANISOU 4998  ND2 ASN A 322     2058   1462   2997   -643    871   -236       N
ATOM   4999  H  AASN A 322      25.520   3.308 -37.482  0.48  0.00           H
ATOM   5000  H  BASN A 322      25.501   3.320 -37.486  0.52  0.00           H
ATOM   5001  HA  ASN A 322      27.398   5.047 -35.967  1.00  0.00           H
ATOM   5002  HB2 ASN A 322      27.808   3.857 -38.721  1.00  0.00           H
ATOM   5003  HB3 ASN A 322      28.188   2.974 -37.229  1.00  0.00           H
ATOM   5004 HD21 ASN A 322      29.755   4.389 -39.595  1.00  0.00           H
ATOM   5005 HD22 ASN A 322      31.024   5.243 -38.746  1.00  0.00           H
ATOM   5006  N   VAL A 323      26.732   7.116 -37.079  1.00 15.64           N
ANISOU 5006  N   VAL A 323     2026   1356   2561   -460    344    -96       N
ATOM   5007  CA  VAL A 323      26.293   8.392 -37.642  1.00 16.93           C
ANISOU 5007  CA  VAL A 323     2391   1396   2646   -472    350    -62       C
ATOM   5008  C   VAL A 323      27.412   9.415 -37.504  1.00 18.80           C
ANISOU 5008  C   VAL A 323     2591   1552   3000   -571    514   -108       C
ATOM   5009  O   VAL A 323      27.292  10.363 -36.751  1.00 20.46           O
ANISOU 5009  O   VAL A 323     2732   1768   3274   -571    451   -131       O
ATOM   5010  CB  VAL A 323      25.132   9.039 -36.837  1.00 21.48           C
ANISOU 5010  CB  VAL A 323     2930   2016   3217   -402    153    -65       C
ATOM   5011  CG1 VAL A 323      24.490  10.178 -37.631  1.00 24.95           C
ANISOU 5011  CG1 VAL A 323     3620   2307   3552   -384    109    -29       C
ATOM   5012  CG2 VAL A 323      24.163   8.107 -36.470  1.00 21.62           C
ANISOU 5012  CG2 VAL A 323     2876   2130   3208   -324     12    -68       C
ATOM   5013  H   VAL A 323      27.096   7.106 -36.137  1.00  0.00           H
ATOM   5014  HA  VAL A 323      26.012   8.272 -38.688  1.00  0.00           H
ATOM   5015  HB  VAL A 323      25.552   9.462 -35.925  1.00  0.00           H
ATOM   5016 HG11 VAL A 323      25.255  10.901 -37.913  1.00  0.00           H
ATOM   5017 HG12 VAL A 323      24.022   9.776 -38.529  1.00  0.00           H
ATOM   5018 HG13 VAL A 323      23.735  10.669 -37.017  1.00  0.00           H
ATOM   5019 HG21 VAL A 323      24.630   7.300 -35.905  1.00  0.00           H
ATOM   5020 HG22 VAL A 323      23.408   8.593 -35.852  1.00  0.00           H
ATOM   5021 HG23 VAL A 323      23.693   7.700 -37.365  1.00  0.00           H
ATOM   5022  N   PRO A 324      28.496   9.239 -38.249  1.00 20.89           N
ANISOU 5022  N   PRO A 324     2898   1729   3309   -661    739   -134       N
ATOM   5023  CA  PRO A 324      29.581  10.202 -38.045  1.00 23.94           C
ANISOU 5023  CA  PRO A 324     3204   2058   3835   -741    891   -207       C
ATOM   5024  C   PRO A 324      29.244  11.582 -38.597  1.00 26.80           C
ANISOU 5024  C   PRO A 324     3811   2288   4082   -764    934   -159       C
ATOM   5025  O   PRO A 324      29.753  12.585 -38.074  1.00 29.53           O
ANISOU 5025  O   PRO A 324     4062   2627   4532   -793    968   -209       O
ATOM   5026  CB  PRO A 324      30.758   9.573 -38.777  1.00 26.74           C
ANISOU 5026  CB  PRO A 324     3527   2400   4231   -778   1092   -268       C
ATOM   5027  CG  PRO A 324      30.202   8.613 -39.713  1.00 26.45           C
ANISOU 5027  CG  PRO A 324     3675   2339   4035   -762   1105   -195       C
ATOM   5028  CD  PRO A 324      28.873   8.140 -39.151  1.00 22.60           C
ANISOU 5028  CD  PRO A 324     3184   1925   3477   -681    860   -126       C
ATOM   5029  HA  PRO A 324      29.809  10.278 -36.982  1.00  0.00           H
ATOM   5030  HB2 PRO A 324      31.319  10.338 -39.313  1.00  0.00           H
ATOM   5031  HB3 PRO A 324      31.409   9.064 -38.066  1.00  0.00           H
ATOM   5032  HG2 PRO A 324      30.880   7.767 -39.824  1.00  0.00           H
ATOM   5033  HG3 PRO A 324      30.045   9.090 -40.681  1.00  0.00           H
ATOM   5034  HD2 PRO A 324      28.135   8.010 -39.943  1.00  0.00           H
ATOM   5035  HD3 PRO A 324      29.002   7.213 -38.592  1.00  0.00           H
ATOM   5036  N   GLU A 325      28.382  11.645 -39.602  1.00 28.67           N
ANISOU 5036  N   GLU A 325     4365   2424   4105   -732    900    -69       N
ATOM   5037  CA  GLU A 325      28.057  12.937 -40.210  1.00 37.25           C
ANISOU 5037  CA  GLU A 325     5719   3380   5055   -731    908    -24       C
ATOM   5038  C   GLU A 325      26.556  13.163 -40.092  1.00 41.93           C
ANISOU 5038  C   GLU A 325     6458   3935   5537   -628    638     35       C
ATOM   5039  O   GLU A 325      25.802  12.222 -39.983  1.00 38.34           O
ANISOU 5039  O   GLU A 325     5956   3562   5050   -549    481     49       O
ATOM   5040  CB  GLU A 325      28.494  12.975 -41.690  1.00 44.93           C
ANISOU 5040  CB  GLU A 325     6986   4242   5841   -758   1094      0       C
ATOM   5041  CG  GLU A 325      29.888  12.383 -41.979  1.00 52.45           C
ANISOU 5041  CG  GLU A 325     7801   5223   6904   -840   1362    -89       C
ATOM   5042  CD  GLU A 325      30.984  13.446 -42.164  1.00 61.73           C
ANISOU 5042  CD  GLU A 325     8981   6320   8154   -924   1602   -170       C
ATOM   5043  OE1 GLU A 325      30.807  14.347 -43.021  1.00 66.61           O
ANISOU 5043  OE1 GLU A 325     9916   6805   8589   -939   1680   -133       O
ATOM   5044  OE2 GLU A 325      32.030  13.367 -41.458  1.00 63.95           O
ANISOU 5044  OE2 GLU A 325     8955   6664   8679   -965   1702   -285       O
ATOM   5045  H   GLU A 325      27.949  10.801 -39.949  1.00  0.00           H
ATOM   5046  HA  GLU A 325      28.578  13.725 -39.666  1.00  0.00           H
ATOM   5047  HB2 GLU A 325      28.496  14.016 -42.014  1.00  0.00           H
ATOM   5048  HB3 GLU A 325      27.758  12.430 -42.282  1.00  0.00           H
ATOM   5049  HG2 GLU A 325      29.827  11.789 -42.891  1.00  0.00           H
ATOM   5050  HG3 GLU A 325      30.169  11.730 -41.153  1.00  0.00           H
ATOM   5051  N   LYS A 326      26.136  14.420 -40.122  1.00 55.80           N
ANISOU 5051  N   LYS A 326     8351   5607   7242   -606    564     52       N
ATOM   5052  CA  LYS A 326      24.719  14.781 -39.983  1.00 63.30           C
ANISOU 5052  CA  LYS A 326     9407   6524   8121   -487    277     73       C
ATOM   5053  C   LYS A 326      23.748  13.749 -40.565  1.00 66.38           C
ANISOU 5053  C   LYS A 326     9901   6927   8392   -377     98     97       C
ATOM   5054  O   LYS A 326      23.441  13.759 -41.761  1.00 70.11           O
ANISOU 5054  O   LYS A 326    10641   7322   8673   -322     66    135       O
ATOM   5055  CB  LYS A 326      24.466  16.130 -40.637  1.00 67.38           C
ANISOU 5055  CB  LYS A 326    10175   6915   8512   -460    246    103       C
ATOM   5056  CG  LYS A 326      25.561  17.154 -40.370  1.00 69.13           C
ANISOU 5056  CG  LYS A 326    10341   7102   8822   -576    463     81       C
ATOM   5057  CD  LYS A 326      25.842  17.316 -38.879  1.00 65.96           C
ANISOU 5057  CD  LYS A 326     9596   6801   8666   -621    448     15       C
ATOM   5058  CE  LYS A 326      25.053  18.489 -38.305  1.00 63.83           C
ANISOU 5058  CE  LYS A 326     9342   6485   8424   -570    269      3       C
ATOM   5059  NZ  LYS A 326      25.554  18.881 -36.956  1.00 62.46           N
ANISOU 5059  NZ  LYS A 326     8866   6396   8469   -633    302    -72       N
ATOM   5060  HA  LYS A 326      24.503  14.880 -38.919  1.00  0.00           H
ATOM   5061  HB2 LYS A 326      24.389  15.981 -41.714  1.00  0.00           H
ATOM   5062  HB3 LYS A 326      23.519  16.526 -40.269  1.00  0.00           H
ATOM   5063  HG2 LYS A 326      25.249  18.116 -40.776  1.00  0.00           H
ATOM   5064  HG3 LYS A 326      26.475  16.836 -40.872  1.00  0.00           H
ATOM   5065  HD2 LYS A 326      26.907  17.496 -38.733  1.00  0.00           H
ATOM   5066  HD3 LYS A 326      25.557  16.402 -38.358  1.00  0.00           H
ATOM   5067  HE2 LYS A 326      25.147  19.341 -38.978  1.00  0.00           H
ATOM   5068  HE3 LYS A 326      24.002  18.209 -38.228  1.00  0.00           H
ATOM   5069  HZ1 LYS A 326      25.589  18.066 -36.360  1.00  0.00           H
ATOM   5070  HZ2 LYS A 326      24.933  19.567 -36.552  1.00  0.00           H
ATOM   5071  HZ3 LYS A 326      26.480  19.275 -37.042  1.00  0.00           H
ATOM   5072  H   LYS A 326      26.816  15.157 -40.245  1.00  0.00           H
TER    5073      LYS A 326
ATOM   5074  N   GLY B   1      15.602   5.938 -35.402  1.00 24.65           N
ANISOU 5074  N   GLY B   1     2861   3049   3456   -170   -110    246       N
ATOM   5075  CA  GLY B   1      15.143   4.949 -34.355  1.00 22.06           C
ANISOU 5075  CA  GLY B   1     2497   2815   3071   -192   -105    212       C
ATOM   5076  C   GLY B   1      13.888   5.456 -33.686  1.00 19.37           C
ANISOU 5076  C   GLY B   1     2055   2503   2803   -183   -101    166       C
ATOM   5077  O   GLY B   1      13.518   6.628 -33.905  1.00 19.67           O
ANISOU 5077  O   GLY B   1     2044   2480   2949   -142   -105    146       O
ATOM   5078  HA2 GLY B   1      15.926   4.825 -33.607  1.00  0.00           H
ATOM   5079  HA3 GLY B   1      14.938   3.989 -34.829  1.00  0.00           H
ATOM   5080  H1  GLY B   1      16.449   5.600 -35.837  1.00  0.00           H
ATOM   5081  H2  GLY B   1      15.781   6.831 -34.966  1.00  0.00           H
ATOM   5082  H3  GLY B   1      14.883   6.045 -36.103  1.00  0.00           H
ATOM   5083  N   LEU B   2      13.267   4.632 -32.838  1.00 17.58           N
ANISOU 5083  N   LEU B   2     1794   2364   2521   -224    -92    140       N
ATOM   5084  CA  LEU B   2      11.987   4.999 -32.266  1.00 17.35           C
ANISOU 5084  CA  LEU B   2     1654   2380   2557   -224    -77     88       C
ATOM   5085  C   LEU B   2      12.013   6.232 -31.349  1.00 16.41           C
ANISOU 5085  C   LEU B   2     1449   2258   2529   -192    -11    -20       C
ATOM   5086  O   LEU B   2      10.977   6.908 -31.195  1.00 16.53           O
ANISOU 5086  O   LEU B   2     1360   2276   2646   -159     -2    -72       O
ATOM   5087  CB  LEU B   2      11.394   3.824 -31.500  1.00 17.39           C
ANISOU 5087  CB  LEU B   2     1652   2491   2464   -301    -68     80       C
ATOM   5088  CG  LEU B   2      10.970   2.651 -32.386  1.00 17.44           C
ANISOU 5088  CG  LEU B   2     1728   2501   2398   -335   -143    179       C
ATOM   5089  CD1 LEU B   2      10.659   1.479 -31.472  1.00 20.19           C
ANISOU 5089  CD1 LEU B   2     2097   2945   2629   -428   -135    170       C
ATOM   5090  CD2 LEU B   2       9.762   3.015 -33.273  1.00 16.94           C
ANISOU 5090  CD2 LEU B   2     1598   2411   2429   -307   -196    215       C
ATOM   5091  H   LEU B   2      13.692   3.749 -32.594  1.00  0.00           H
ATOM   5092  HA  LEU B   2      11.313   5.222 -33.093  1.00  0.00           H
ATOM   5093  HB2 LEU B   2      12.141   3.465 -30.792  1.00  0.00           H
ATOM   5094  HB3 LEU B   2      10.524   4.173 -30.943  1.00  0.00           H
ATOM   5095  HG  LEU B   2      11.807   2.379 -33.030  1.00  0.00           H
ATOM   5096 HD11 LEU B   2      10.352   0.622 -32.071  1.00  0.00           H
ATOM   5097 HD12 LEU B   2       9.853   1.753 -30.791  1.00  0.00           H
ATOM   5098 HD13 LEU B   2      11.548   1.221 -30.897  1.00  0.00           H
ATOM   5099 HD21 LEU B   2      10.022   3.858 -33.914  1.00  0.00           H
ATOM   5100 HD22 LEU B   2       8.916   3.286 -32.641  1.00  0.00           H
ATOM   5101 HD23 LEU B   2       9.494   2.158 -33.891  1.00  0.00           H
ATOM   5102  N   PHE B   3      13.171   6.493 -30.732  1.00 16.06           N
ANISOU 5102  N   PHE B   3     1443   2207   2451   -201     30    -60       N
ATOM   5103  CA  PHE B   3      13.273   7.524 -29.708  1.00 19.59           C
ANISOU 5103  CA  PHE B   3     1828   2657   2958   -187     94   -168       C
ATOM   5104  C   PHE B   3      13.723   8.873 -30.243  1.00 21.85           C
ANISOU 5104  C   PHE B   3     2114   2832   3356   -124     85   -178       C
ATOM   5105  O   PHE B   3      13.507   9.896 -29.612  1.00 25.15           O
ANISOU 5105  O   PHE B   3     2473   3227   3855    -94    123   -268       O
ATOM   5106  CB  PHE B   3      14.144   7.016 -28.560  1.00 20.58           C
ANISOU 5106  CB  PHE B   3     1996   2846   2977   -250    133   -211       C
ATOM   5107  CG  PHE B   3      13.503   5.871 -27.883  1.00 22.62           C
ANISOU 5107  CG  PHE B   3     2257   3208   3131   -324    141   -214       C
ATOM   5108  CD1 PHE B   3      13.708   4.594 -28.338  1.00 22.47           C
ANISOU 5108  CD1 PHE B   3     2318   3206   3015   -360     83   -126       C
ATOM   5109  CD2 PHE B   3      12.558   6.098 -26.904  1.00 26.17           C
ANISOU 5109  CD2 PHE B   3     2626   3733   3586   -360    206   -305       C
ATOM   5110  CE1 PHE B   3      13.012   3.536 -27.773  1.00 24.66           C
ANISOU 5110  CE1 PHE B   3     2609   3569   3193   -441     79   -119       C
ATOM   5111  CE2 PHE B   3      11.878   5.043 -26.338  1.00 27.30           C
ANISOU 5111  CE2 PHE B   3     2774   3975   3624   -450    217   -301       C
ATOM   5112  CZ  PHE B   3      12.097   3.783 -26.771  1.00 25.22           C
ANISOU 5112  CZ  PHE B   3     2601   3722   3260   -493    148   -203       C
ATOM   5113  H   PHE B   3      13.994   5.963 -30.982  1.00  0.00           H
ATOM   5114  HA  PHE B   3      12.271   7.665 -29.303  1.00  0.00           H
ATOM   5115  HB2 PHE B   3      14.291   7.821 -27.840  1.00  0.00           H
ATOM   5116  HB3 PHE B   3      15.112   6.705 -28.953  1.00  0.00           H
ATOM   5117  HD1 PHE B   3      14.412   4.412 -29.137  1.00  0.00           H
ATOM   5118  HD2 PHE B   3      12.351   7.107 -26.580  1.00  0.00           H
ATOM   5119  HE1 PHE B   3      13.185   2.526 -28.115  1.00  0.00           H
ATOM   5120  HE2 PHE B   3      11.167   5.224 -25.545  1.00  0.00           H
ATOM   5121  HZ  PHE B   3      11.551   2.962 -26.329  1.00  0.00           H
ATOM   5122  N   GLY B   4      14.305   8.891 -31.431  1.00 19.47           N
ANISOU 5122  N   GLY B   4     1887   2456   3056   -110     35    -88       N
ATOM   5123  CA  GLY B   4      14.587  10.164 -32.080  1.00 18.74           C
ANISOU 5123  CA  GLY B   4     1810   2248   3064    -67     12    -80       C
ATOM   5124  C   GLY B   4      15.803  10.885 -31.524  1.00 17.27           C
ANISOU 5124  C   GLY B   4     1648   2034   2881    -82     56   -130       C
ATOM   5125  O   GLY B   4      15.962  12.087 -31.748  1.00 17.35           O
ANISOU 5125  O   GLY B   4     1665   1950   2979    -55     44   -148       O
ATOM   5126  H   GLY B   4      14.553   8.024 -31.887  1.00  0.00           H
ATOM   5127  HA2 GLY B   4      13.719  10.811 -31.957  1.00  0.00           H
ATOM   5128  HA3 GLY B   4      14.742   9.987 -33.144  1.00  0.00           H
ATOM   5129  N   ALA B   5      16.668  10.170 -30.791  1.00 14.36           N
ANISOU 5129  N   ALA B   5     1298   1740   2419   -129     93   -152       N
ATOM   5130  CA  ALA B   5      17.876  10.783 -30.255  1.00 13.20           C
ANISOU 5130  CA  ALA B   5     1168   1574   2274   -151    124   -196       C
ATOM   5131  C   ALA B   5      19.059  10.582 -31.202  1.00 13.83           C
ANISOU 5131  C   ALA B   5     1310   1622   2321   -174    111   -125       C
ATOM   5132  O   ALA B   5      19.594  11.533 -31.785  1.00 14.80           O
ANISOU 5132  O   ALA B   5     1460   1666   2498   -179    109   -110       O
ATOM   5133  CB  ALA B   5      18.196  10.213 -28.840  1.00 14.24           C
ANISOU 5133  CB  ALA B   5     1283   1798   2331   -193    158   -268       C
ATOM   5134  H   ALA B   5      16.480   9.195 -30.608  1.00  0.00           H
ATOM   5135  HA  ALA B   5      17.698  11.854 -30.157  1.00  0.00           H
ATOM   5136  HB1 ALA B   5      19.101  10.682 -28.455  1.00  0.00           H
ATOM   5137  HB2 ALA B   5      17.364  10.423 -28.167  1.00  0.00           H
ATOM   5138  HB3 ALA B   5      18.346   9.135 -28.908  1.00  0.00           H
ATOM   5139  N   ILE B   6      19.477   9.331 -31.359  1.00 14.31           N
ANISOU 5139  N   ILE B   6     1397   1745   2293   -193    102    -86       N
ATOM   5140  CA  ILE B   6      20.580   9.009 -32.241  1.00 15.50           C
ANISOU 5140  CA  ILE B   6     1594   1882   2413   -210    104    -37       C
ATOM   5141  C   ILE B   6      20.076   9.201 -33.666  1.00 18.48           C
ANISOU 5141  C   ILE B   6     2022   2195   2805   -201     80     43       C
ATOM   5142  O   ILE B   6      19.008   8.700 -34.002  1.00 20.40           O
ANISOU 5142  O   ILE B   6     2273   2443   3034   -182     44     81       O
ATOM   5143  CB  ILE B   6      20.994   7.541 -32.063  1.00 13.80           C
ANISOU 5143  CB  ILE B   6     1396   1739   2108   -216     88    -24       C
ATOM   5144  CG1 ILE B   6      21.653   7.369 -30.689  1.00 13.48           C
ANISOU 5144  CG1 ILE B   6     1323   1751   2048   -235     91    -95       C
ATOM   5145  CG2 ILE B   6      21.927   7.142 -33.183  1.00 14.76           C
ANISOU 5145  CG2 ILE B   6     1557   1847   2204   -220     97     20       C
ATOM   5146  CD1 ILE B   6      22.174   5.940 -30.381  1.00 13.43           C
ANISOU 5146  CD1 ILE B   6     1343   1800   1962   -239     51    -86       C
ATOM   5147  H   ILE B   6      19.016   8.589 -30.853  1.00  0.00           H
ATOM   5148  HA  ILE B   6      21.426   9.668 -32.046  1.00  0.00           H
ATOM   5149  HB  ILE B   6      20.102   6.915 -32.107  1.00  0.00           H
ATOM   5150 HG12 ILE B   6      22.498   8.055 -30.632  1.00  0.00           H
ATOM   5151 HG13 ILE B   6      20.930   7.646 -29.922  1.00  0.00           H
ATOM   5152 HG21 ILE B   6      22.221   6.100 -33.058  1.00  0.00           H
ATOM   5153 HG22 ILE B   6      21.419   7.263 -34.140  1.00  0.00           H
ATOM   5154 HG23 ILE B   6      22.814   7.775 -33.160  1.00  0.00           H
ATOM   5155 HD11 ILE B   6      22.157   5.771 -29.304  1.00  0.00           H
ATOM   5156 HD12 ILE B   6      23.195   5.839 -30.749  1.00  0.00           H
ATOM   5157 HD13 ILE B   6      21.536   5.207 -30.874  1.00  0.00           H
ATOM   5158  N   ALA B   7      20.838   9.908 -34.484  1.00 19.28           N
ANISOU 5158  N   ALA B   7     2161   2238   2927   -227     96     70       N
ATOM   5159  CA  ALA B   7      20.416  10.282 -35.831  1.00 23.08           C
ANISOU 5159  CA  ALA B   7     2713   2641   3415   -237     66    149       C
ATOM   5160  C   ALA B   7      19.117  11.093 -35.757  1.00 25.10           C
ANISOU 5160  C   ALA B   7     2953   2829   3754   -198     11    152       C
ATOM   5161  O   ALA B   7      18.284  11.012 -36.655  1.00 27.38           O
ANISOU 5161  O   ALA B   7     3285   3071   4046   -187    -46    219       O
ATOM   5162  CB  ALA B   7      20.227   9.029 -36.705  1.00 24.22           C
ANISOU 5162  CB  ALA B   7     2912   2820   3472   -240     50    211       C
ATOM   5163  H   ALA B   7      21.750  10.201 -34.164  1.00  0.00           H
ATOM   5164  HA  ALA B   7      21.191  10.905 -36.278  1.00  0.00           H
ATOM   5165  HB1 ALA B   7      19.913   9.327 -37.705  1.00  0.00           H
ATOM   5166  HB2 ALA B   7      19.465   8.388 -36.261  1.00  0.00           H
ATOM   5167  HB3 ALA B   7      21.169   8.484 -36.768  1.00  0.00           H
ATOM   5168  N   GLY B   8      18.967  11.883 -34.692  1.00 22.72           N
ANISOU 5168  N   GLY B   8     2588   2518   3524   -175     24     74       N
ATOM   5169  CA  GLY B   8      17.758  12.669 -34.458  1.00 20.73           C
ANISOU 5169  CA  GLY B   8     2298   2207   3371   -121    -20     47       C
ATOM   5170  C   GLY B   8      18.107  13.995 -33.822  1.00 19.86           C
ANISOU 5170  C   GLY B   8     2172   2029   3345   -115     -6    -23       C
ATOM   5171  O   GLY B   8      18.854  14.762 -34.403  1.00 20.54           O
ANISOU 5171  O   GLY B   8     2324   2037   3445   -155    -15      9       O
ATOM   5172  H   GLY B   8      19.720  11.940 -34.021  1.00  0.00           H
ATOM   5173  HA2 GLY B   8      17.256  12.848 -35.409  1.00  0.00           H
ATOM   5174  HA3 GLY B   8      17.091  12.116 -33.797  1.00  0.00           H
ATOM   5175  N   PHE B   9      17.617  14.271 -32.618  1.00 18.64           N
ANISOU 5175  N   PHE B   9     1939   1905   3237    -78     20   -123       N
ATOM   5176  CA  PHE B   9      17.976  15.529 -31.977  1.00 19.00           C
ANISOU 5176  CA  PHE B   9     1982   1881   3358    -74     33   -199       C
ATOM   5177  C   PHE B   9      19.450  15.640 -31.641  1.00 19.54           C
ANISOU 5177  C   PHE B   9     2082   1970   3372   -145     77   -211       C
ATOM   5178  O   PHE B   9      20.000  16.759 -31.561  1.00 21.24           O
ANISOU 5178  O   PHE B   9     2330   2100   3640   -167     72   -236       O
ATOM   5179  CB  PHE B   9      17.042  15.894 -30.813  1.00 18.62           C
ANISOU 5179  CB  PHE B   9     1846   1853   3375    -17     57   -318       C
ATOM   5180  CG  PHE B   9      17.125  15.001 -29.601  1.00 19.23           C
ANISOU 5180  CG  PHE B   9     1872   2069   3366    -46    128   -386       C
ATOM   5181  CD1 PHE B   9      18.128  15.178 -28.655  1.00 19.94           C
ANISOU 5181  CD1 PHE B   9     1975   2189   3411    -95    172   -446       C
ATOM   5182  CD2 PHE B   9      16.150  14.065 -29.355  1.00 20.08           C
ANISOU 5182  CD2 PHE B   9     1922   2269   3440    -31    141   -394       C
ATOM   5183  CE1 PHE B   9      18.183  14.407 -27.514  1.00 18.80           C
ANISOU 5183  CE1 PHE B   9     1802   2159   3181   -131    219   -505       C
ATOM   5184  CE2 PHE B   9      16.195  13.296 -28.217  1.00 20.39           C
ANISOU 5184  CE2 PHE B   9     1932   2425   3389    -75    198   -453       C
ATOM   5185  CZ  PHE B   9      17.207  13.479 -27.293  1.00 18.93           C
ANISOU 5185  CZ  PHE B   9     1775   2262   3154   -124    233   -508       C
ATOM   5186  H   PHE B   9      17.004  13.617 -32.153  1.00  0.00           H
ATOM   5187  HA  PHE B   9      17.799  16.294 -32.733  1.00  0.00           H
ATOM   5188  HB2 PHE B   9      16.017  15.861 -31.183  1.00  0.00           H
ATOM   5189  HB3 PHE B   9      17.262  16.915 -30.503  1.00  0.00           H
ATOM   5190  HD1 PHE B   9      18.880  15.936 -28.818  1.00  0.00           H
ATOM   5191  HD2 PHE B   9      15.343  13.933 -30.060  1.00  0.00           H
ATOM   5192  HE1 PHE B   9      18.987  14.535 -26.805  1.00  0.00           H
ATOM   5193  HE2 PHE B   9      15.437  12.546 -28.044  1.00  0.00           H
ATOM   5194  HZ  PHE B   9      17.225  12.884 -26.392  1.00  0.00           H
ATOM   5195  N  AILE B  10      20.110  14.500 -31.485  0.42 18.72           N
ANISOU 5195  N  AILE B  10     1969   1972   3170   -182    111   -192       N
ATOM   5196  N  BILE B  10      20.096  14.491 -31.439  0.58 18.71           N
ANISOU 5196  N  BILE B  10     1966   1973   3169   -181    112   -195       N
ATOM   5197  CA AILE B  10      21.562  14.483 -31.472  0.42 18.26           C
ANISOU 5197  CA AILE B  10     1932   1935   3071   -247    141   -187       C
ATOM   5198  CA BILE B  10      21.552  14.416 -31.470  0.58 18.23           C
ANISOU 5198  CA BILE B  10     1927   1936   3064   -246    141   -186       C
ATOM   5199  C  AILE B  10      21.999  14.276 -32.920  0.42 17.97           C
ANISOU 5199  C  AILE B  10     1956   1868   3004   -280    131    -88       C
ATOM   5200  C  BILE B  10      21.899  14.317 -32.959  0.58 18.00           C
ANISOU 5200  C  BILE B  10     1962   1865   3012   -276    127    -86       C
ATOM   5201  O  AILE B  10      21.820  13.199 -33.505  0.42 18.09           O
ANISOU 5201  O  AILE B  10     1982   1935   2956   -271    128    -36       O
ATOM   5202  O  BILE B  10      21.569  13.331 -33.621  0.58 18.08           O
ANISOU 5202  O  BILE B  10     1988   1916   2967   -264    118    -29       O
ATOM   5203  CB AILE B  10      22.108  13.431 -30.506  0.42 19.20           C
ANISOU 5203  CB AILE B  10     2009   2170   3115   -263    168   -228       C
ATOM   5204  CB BILE B  10      22.126  13.181 -30.727  0.58 18.58           C
ANISOU 5204  CB BILE B  10     1936   2101   3023   -263    166   -210       C
ATOM   5205  CG1AILE B  10      21.590  13.762 -29.102  0.42 20.33           C
ANISOU 5205  CG1AILE B  10     2114   2337   3275   -249    181   -327       C
ATOM   5206  CG1BILE B  10      21.480  12.962 -29.345  0.58 19.69           C
ANISOU 5206  CG1BILE B  10     2033   2299   3150   -245    176   -292       C
ATOM   5207  CG2AILE B  10      23.650  13.399 -30.557  0.42 20.08           C
ANISOU 5207  CG2AILE B  10     2121   2305   3205   -321    187   -227       C
ATOM   5208  CG2BILE B  10      23.677  13.282 -30.633  0.58 20.31           C
ANISOU 5208  CG2BILE B  10     2150   2339   3227   -321    187   -220       C
ATOM   5209  CD1AILE B  10      22.029  12.849 -28.021  0.42 20.43           C
ANISOU 5209  CD1AILE B  10     2107   2449   3208   -277    191   -368       C
ATOM   5210  CD1BILE B  10      21.753  14.021 -28.320  0.58 20.97           C
ANISOU 5210  CD1BILE B  10     2182   2428   3356   -261    194   -383       C
ATOM   5211  H  AILE B  10      19.598  13.636 -31.374  0.42  0.00           H
ATOM   5212  H  BILE B  10      19.563  13.652 -31.260  0.58  0.00           H
ATOM   5213  HA AILE B  10      21.913  15.462 -31.145  0.42  0.00           H
ATOM   5214  HA BILE B  10      21.977  15.328 -31.052  0.58  0.00           H
ATOM   5215  HB AILE B  10      21.727  12.453 -30.800  0.42  0.00           H
ATOM   5216  HB BILE B  10      21.896  12.305 -31.333  0.58  0.00           H
ATOM   5217 HG12AILE B  10      21.928  14.767 -28.849  0.42  0.00           H
ATOM   5218 HG12BILE B  10      21.847  12.014 -28.951  0.58  0.00           H
ATOM   5219 HG13AILE B  10      20.500  13.763 -29.129  0.42  0.00           H
ATOM   5220 HG13BILE B  10      20.401  12.884 -29.479  0.58  0.00           H
ATOM   5221 HG21AILE B  10      24.050  14.255 -30.013  0.42  0.00           H
ATOM   5222 HG21BILE B  10      24.016  14.177 -31.155  0.58  0.00           H
ATOM   5223 HG22AILE B  10      24.009  12.477 -30.099  0.42  0.00           H
ATOM   5224 HG22BILE B  10      23.974  13.338 -29.586  0.58  0.00           H
ATOM   5225 HG23AILE B  10      23.980  13.442 -31.595  0.42  0.00           H
ATOM   5226 HG23BILE B  10      24.127  12.401 -31.092  0.58  0.00           H
ATOM   5227 HD11AILE B  10      22.097  11.833 -28.409  0.42  0.00           H
ATOM   5228 HD11BILE B  10      21.464  14.994 -28.717  0.58  0.00           H
ATOM   5229 HD12AILE B  10      21.307  12.879 -27.205  0.42  0.00           H
ATOM   5230 HD12BILE B  10      22.816  14.028 -28.080  0.58  0.00           H
ATOM   5231 HD13AILE B  10      23.006  13.164 -27.653  0.42  0.00           H
ATOM   5232 HD13BILE B  10      21.178  13.811 -27.418  0.58  0.00           H
ATOM   5233  N   GLU B  11      22.534  15.339 -33.502  1.00 17.43           N
ANISOU 5233  N   GLU B  11     1939   1710   2974   -326    125    -64       N
ATOM   5234  CA  GLU B  11      22.714  15.411 -34.939  1.00 20.96           C
ANISOU 5234  CA  GLU B  11     2467   2104   3393   -371    112     30       C
ATOM   5235  C   GLU B  11      23.680  14.380 -35.487  1.00 18.78           C
ANISOU 5235  C   GLU B  11     2189   1919   3028   -417    166     58       C
ATOM   5236  O   GLU B  11      23.511  13.926 -36.595  1.00 18.43           O
ANISOU 5236  O   GLU B  11     2204   1866   2932   -433    161    129       O
ATOM   5237  CB  GLU B  11      23.181  16.793 -35.334  1.00 30.13           C
ANISOU 5237  CB  GLU B  11     3695   3151   4603   -434     95     46       C
ATOM   5238  CG  GLU B  11      22.139  17.814 -35.034  1.00 41.98           C
ANISOU 5238  CG  GLU B  11     5213   4536   6201   -375     24     23       C
ATOM   5239  CD  GLU B  11      22.550  19.173 -35.538  1.00 53.46           C
ANISOU 5239  CD  GLU B  11     6760   5852   7699   -442    -14     53       C
ATOM   5240  OE1 GLU B  11      22.898  20.038 -34.694  1.00 57.45           O
ANISOU 5240  OE1 GLU B  11     7251   6316   8261   -450    -11    -17       O
ATOM   5241  OE2 GLU B  11      22.553  19.341 -36.784  1.00 57.39           O
ANISOU 5241  OE2 GLU B  11     7358   6284   8164   -497    -50    149       O
ATOM   5242  H  AGLU B  11      22.824  16.119 -32.930  0.42  0.00           H
ATOM   5243  H  BGLU B  11      22.897  16.075 -32.913  0.58  0.00           H
ATOM   5244  HA  GLU B  11      21.744  15.241 -35.406  1.00  0.00           H
ATOM   5245  HB2 GLU B  11      24.087  17.035 -34.779  1.00  0.00           H
ATOM   5246  HB3 GLU B  11      23.400  16.806 -36.402  1.00  0.00           H
ATOM   5247  HG2 GLU B  11      21.206  17.523 -35.517  1.00  0.00           H
ATOM   5248  HG3 GLU B  11      21.985  17.863 -33.956  1.00  0.00           H
ATOM   5249  N   ASN B  12      24.708  14.061 -34.723  1.00 17.33           N
ANISOU 5249  N   ASN B  12     1939   1814   2831   -437    213     -1       N
ATOM   5250  CA  ASN B  12      25.647  13.027 -35.138  1.00 16.33           C
ANISOU 5250  CA  ASN B  12     1789   1777   2640   -461    261      5       C
ATOM   5251  C   ASN B  12      26.406  12.502 -33.934  1.00 17.65           C
ANISOU 5251  C   ASN B  12     1866   2029   2812   -446    272    -72       C
ATOM   5252  O   ASN B  12      26.357  13.062 -32.829  1.00 19.01           O
ANISOU 5252  O   ASN B  12     2005   2191   3026   -440    254   -128       O
ATOM   5253  CB  ASN B  12      26.614  13.555 -36.206  1.00 17.53           C
ANISOU 5253  CB  ASN B  12     1981   1905   2774   -556    312     39       C
ATOM   5254  CG  ASN B  12      27.348  14.834 -35.771  1.00 21.91           C
ANISOU 5254  CG  ASN B  12     2523   2413   3386   -627    324      6       C
ATOM   5255  OD1 ASN B  12      26.865  15.938 -35.979  1.00 24.81           O
ANISOU 5255  OD1 ASN B  12     2961   2674   3792   -652    286     35       O
ATOM   5256  ND2 ASN B  12      28.488  14.674 -35.142  1.00 21.85           N
ANISOU 5256  ND2 ASN B  12     2429   2480   3392   -656    363    -56       N
ATOM   5257  H   ASN B  12      24.845  14.538 -33.843  1.00  0.00           H
ATOM   5258  HA  ASN B  12      25.079  12.203 -35.569  1.00  0.00           H
ATOM   5259  HB2 ASN B  12      27.355  12.784 -36.416  1.00  0.00           H
ATOM   5260  HB3 ASN B  12      26.054  13.763 -37.117  1.00  0.00           H
ATOM   5261 HD21 ASN B  12      28.848  13.745 -34.978  1.00  0.00           H
ATOM   5262 HD22 ASN B  12      29.006  15.480 -34.822  1.00  0.00           H
ATOM   5263  N   GLY B  13      27.102  11.396 -34.166  1.00 17.07           N
ANISOU 5263  N   GLY B  13     1759   2034   2694   -437    296    -79       N
ATOM   5264  CA  GLY B  13      27.971  10.813 -33.172  1.00 16.08           C
ANISOU 5264  CA  GLY B  13     1552   1982   2577   -424    288   -144       C
ATOM   5265  C   GLY B  13      29.328  11.523 -33.174  1.00 17.40           C
ANISOU 5265  C   GLY B  13     1661   2161   2789   -495    331   -182       C
ATOM   5266  O   GLY B  13      29.676  12.330 -34.075  1.00 18.09           O
ANISOU 5266  O   GLY B  13     1777   2210   2885   -565    380   -153       O
ATOM   5267  H   GLY B  13      27.021  10.948 -35.067  1.00  0.00           H
ATOM   5268  HA2 GLY B  13      27.513  10.916 -32.188  1.00  0.00           H
ATOM   5269  HA3 GLY B  13      28.116   9.756 -33.394  1.00  0.00           H
ATOM   5270  N   TRP B  14      30.102  11.183 -32.158  1.00 17.17           N
ANISOU 5270  N   TRP B  14     1554   2186   2783   -486    304   -244       N
ATOM   5271  CA  TRP B  14      31.408  11.760 -31.928  1.00 16.02           C
ANISOU 5271  CA  TRP B  14     1330   2065   2691   -551    327   -290       C
ATOM   5272  C   TRP B  14      32.496  10.724 -32.176  1.00 15.43           C
ANISOU 5272  C   TRP B  14     1164   2074   2625   -529    342   -326       C
ATOM   5273  O   TRP B  14      32.702   9.837 -31.348  1.00 14.47           O
ANISOU 5273  O   TRP B  14     1001   1993   2506   -471    275   -362       O
ATOM   5274  CB  TRP B  14      31.508  12.199 -30.463  1.00 14.91           C
ANISOU 5274  CB  TRP B  14     1166   1919   2581   -557    266   -343       C
ATOM   5275  CG  TRP B  14      30.637  13.358 -30.067  1.00 15.84           C
ANISOU 5275  CG  TRP B  14     1355   1955   2710   -579    257   -338       C
ATOM   5276  CD1 TRP B  14      30.197  14.391 -30.873  1.00 19.59           C
ANISOU 5276  CD1 TRP B  14     1895   2348   3202   -617    290   -296       C
ATOM   5277  CD2 TRP B  14      30.111  13.618 -28.758  1.00 14.82           C
ANISOU 5277  CD2 TRP B  14     1243   1809   2579   -563    209   -383       C
ATOM   5278  NE1 TRP B  14      29.406  15.271 -30.115  1.00 18.97           N
ANISOU 5278  NE1 TRP B  14     1862   2198   3146   -608    259   -321       N
ATOM   5279  CE2 TRP B  14      29.350  14.818 -28.825  1.00 16.02           C
ANISOU 5279  CE2 TRP B  14     1458   1870   2758   -578    221   -380       C
ATOM   5280  CE3 TRP B  14      30.203  12.954 -27.539  1.00 17.02           C
ANISOU 5280  CE3 TRP B  14     1501   2138   2830   -542    153   -429       C
ATOM   5281  CZ2 TRP B  14      28.698  15.360 -27.710  1.00 16.72           C
ANISOU 5281  CZ2 TRP B  14     1575   1926   2853   -567    195   -435       C
ATOM   5282  CZ3 TRP B  14      29.549  13.469 -26.432  1.00 18.28           C
ANISOU 5282  CZ3 TRP B  14     1701   2269   2975   -548    129   -475       C
ATOM   5283  CH2 TRP B  14      28.793  14.680 -26.527  1.00 18.21           C
ANISOU 5283  CH2 TRP B  14     1742   2178   3000   -557    160   -484       C
ATOM   5284  H   TRP B  14      29.765  10.486 -31.510  1.00  0.00           H
ATOM   5285  HA  TRP B  14      31.556  12.618 -32.584  1.00  0.00           H
ATOM   5286  HB2 TRP B  14      32.544  12.477 -30.267  1.00  0.00           H
ATOM   5287  HB3 TRP B  14      31.255  11.348 -29.831  1.00  0.00           H
ATOM   5288  HD1 TRP B  14      30.426  14.504 -31.922  1.00  0.00           H
ATOM   5289  HE3 TRP B  14      30.780  12.045 -27.457  1.00  0.00           H
ATOM   5290  HZ2 TRP B  14      28.140  16.282 -27.782  1.00  0.00           H
ATOM   5291  HZ3 TRP B  14      29.610  12.951 -25.487  1.00  0.00           H
ATOM   5292  HH2 TRP B  14      28.290  15.063 -25.651  1.00  0.00           H
ATOM   5293  HE1 TRP B  14      28.953  16.103 -30.465  1.00  0.00           H
ATOM   5294  N   GLU B  15      33.223  10.848 -33.272  1.00 16.36           N
ANISOU 5294  N   GLU B  15     1251   2217   2749   -579    425   -324       N
ATOM   5295  CA  GLU B  15      34.364   9.982 -33.499  1.00 18.15           C
ANISOU 5295  CA  GLU B  15     1368   2526   3004   -555    450   -380       C
ATOM   5296  C   GLU B  15      35.438  10.158 -32.408  1.00 18.99           C
ANISOU 5296  C   GLU B  15     1387   2666   3165   -551    385   -434       C
ATOM   5297  O   GLU B  15      36.249   9.240 -32.185  1.00 19.63           O
ANISOU 5297  O   GLU B  15     1381   2802   3277   -491    352   -483       O
ATOM   5298  CB  GLU B  15      34.932  10.207 -34.915  1.00 19.00           C
ANISOU 5298  CB  GLU B  15     1483   2656   3081   -615    560   -366       C
ATOM   5299  CG  GLU B  15      33.938   9.719 -36.003  1.00 22.05           C
ANISOU 5299  CG  GLU B  15     1972   3012   3393   -602    604   -310       C
ATOM   5300  CD  GLU B  15      34.470   9.772 -37.448  1.00 27.16           C
ANISOU 5300  CD  GLU B  15     2636   3689   3993   -675    724   -306       C
ATOM   5301  OE1 GLU B  15      35.490  10.371 -37.709  1.00 26.57           O
ANISOU 5301  OE1 GLU B  15     2519   3647   3929   -736    768   -328       O
ATOM   5302  OE2 GLU B  15      33.849   9.188 -38.358  1.00 33.57           O
ANISOU 5302  OE2 GLU B  15     3536   4487   4732   -657    753   -268       O
ATOM   5303  H   GLU B  15      32.983  11.551 -33.957  1.00  0.00           H
ATOM   5304  HA  GLU B  15      34.010   8.952 -33.447  1.00  0.00           H
ATOM   5305  HB2 GLU B  15      35.120  11.271 -35.057  1.00  0.00           H
ATOM   5306  HB3 GLU B  15      35.870   9.661 -35.016  1.00  0.00           H
ATOM   5307  HG2 GLU B  15      33.046  10.343 -35.949  1.00  0.00           H
ATOM   5308  HG3 GLU B  15      33.655   8.691 -35.776  1.00  0.00           H
ATOM   5309  N   GLY B  16      35.438  11.320 -31.724  1.00 17.79           N
ANISOU 5309  N   GLY B  16     1259   2471   3028   -613    360   -427       N
ATOM   5310  CA  GLY B  16      36.460  11.597 -30.718  1.00 18.38           C
ANISOU 5310  CA  GLY B  16     1262   2572   3149   -626    299   -471       C
ATOM   5311  C   GLY B  16      36.110  10.991 -29.349  1.00 18.13           C
ANISOU 5311  C   GLY B  16     1231   2536   3120   -570    185   -498       C
ATOM   5312  O   GLY B  16      36.894  11.072 -28.415  1.00 19.47           O
ANISOU 5312  O   GLY B  16     1352   2724   3323   -578    114   -531       O
ATOM   5313  H   GLY B  16      34.722  12.008 -31.910  1.00  0.00           H
ATOM   5314  HA2 GLY B  16      36.560  12.677 -30.608  1.00  0.00           H
ATOM   5315  HA3 GLY B  16      37.411  11.185 -31.056  1.00  0.00           H
ATOM   5316  N  AMET B  17      34.918  10.421 -29.224  0.50 16.55           N
ANISOU 5316  N  AMET B  17     1094   2312   2881   -525    163   -479       N
ATOM   5317  N  BMET B  17      34.941  10.364 -29.255  0.50 16.54           N
ANISOU 5317  N  BMET B  17     1091   2314   2881   -522    164   -479       N
ATOM   5318  CA AMET B  17      34.602   9.712 -27.998  0.50 16.52           C
ANISOU 5318  CA AMET B  17     1100   2313   2862   -484     55   -504       C
ATOM   5319  CA BMET B  17      34.521   9.703 -28.023  0.50 16.63           C
ANISOU 5319  CA BMET B  17     1119   2325   2874   -483     57   -501       C
ATOM   5320  C  AMET B  17      35.096   8.308 -28.222  0.50 17.28           C
ANISOU 5320  C  AMET B  17     1137   2456   2972   -405      9   -522       C
ATOM   5321  C  BMET B  17      35.016   8.267 -28.082  0.50 17.20           C
ANISOU 5321  C  BMET B  17     1133   2443   2957   -403     -3   -522       C
ATOM   5322  O  AMET B  17      34.471   7.497 -28.903  0.50 17.05           O
ANISOU 5322  O  AMET B  17     1157   2425   2897   -347     29   -490       O
ATOM   5323  O  BMET B  17      34.280   7.378 -28.498  0.50 16.88           O
ANISOU 5323  O  BMET B  17     1157   2397   2860   -341     -6   -488       O
ATOM   5324  CB AMET B  17      33.124   9.715 -27.676  0.50 17.88           C
ANISOU 5324  CB AMET B  17     1391   2442   2961   -466     45   -467       C
ATOM   5325  CB BMET B  17      33.001   9.717 -27.916  0.50 17.13           C
ANISOU 5325  CB BMET B  17     1303   2343   2861   -462     62   -457       C
ATOM   5326  CG AMET B  17      32.758   8.741 -26.557  0.50 19.85           C
ANISOU 5326  CG AMET B  17     1681   2704   3156   -425    -61   -476       C
ATOM   5327  CG BMET B  17      32.420   8.790 -26.858  0.50 18.20           C
ANISOU 5327  CG BMET B  17     1493   2488   2936   -420    -34   -460       C
ATOM   5328  SD AMET B  17      31.212   9.213 -25.748  0.50 24.68           S
ANISOU 5328  SD AMET B  17     2412   3278   3689   -445    -58   -463       S
ATOM   5329  SD BMET B  17      32.734   9.399 -25.200  0.50 22.60           S
ANISOU 5329  SD BMET B  17     2058   3037   3491   -481   -116   -513       S
ATOM   5330  CE AMET B  17      31.803  10.617 -24.834  0.50 25.00           C
ANISOU 5330  CE AMET B  17     2433   3292   3774   -528    -63   -520       C
ATOM   5331  CE BMET B  17      31.539  10.708 -25.121  0.50 26.09           C
ANISOU 5331  CE BMET B  17     2581   3422   3910   -521    -38   -508       C
ATOM   5332  H  AMET B  17      34.241  10.480 -29.971  0.50  0.00           H
ATOM   5333  H  BMET B  17      34.328  10.345 -30.057  0.50  0.00           H
ATOM   5334  HA AMET B  17      35.152  10.160 -27.170  0.50  0.00           H
ATOM   5335  HA BMET B  17      34.958  10.210 -27.163  0.50  0.00           H
ATOM   5336  HB2AMET B  17      32.572   9.437 -28.574  0.50  0.00           H
ATOM   5337  HB2BMET B  17      32.592   9.424 -28.883  0.50  0.00           H
ATOM   5338  HB3AMET B  17      32.830  10.721 -27.378  0.50  0.00           H
ATOM   5339  HB3BMET B  17      32.679  10.735 -27.698  0.50  0.00           H
ATOM   5340  HG2AMET B  17      32.646   7.742 -26.979  0.50  0.00           H
ATOM   5341  HG2BMET B  17      32.873   7.804 -26.964  0.50  0.00           H
ATOM   5342  HG3AMET B  17      33.559   8.729 -25.818  0.50  0.00           H
ATOM   5343  HG3BMET B  17      31.344   8.706 -27.009  0.50  0.00           H
ATOM   5344  HE1AMET B  17      32.513  10.285 -24.077  0.50  0.00           H
ATOM   5345  HE1BMET B  17      30.955  10.724 -26.041  0.50  0.00           H
ATOM   5346  HE2AMET B  17      32.296  11.312 -25.514  0.50  0.00           H
ATOM   5347  HE2BMET B  17      32.053  11.662 -25.001  0.50  0.00           H
ATOM   5348  HE3AMET B  17      30.963  11.116 -24.351  0.50  0.00           H
ATOM   5349  HE3BMET B  17      30.875  10.543 -24.272  0.50  0.00           H
ATOM   5350  N   ILE B  18      36.251   8.051 -27.673  1.00 19.32           N
ANISOU 5350  N   ILE B  18     1322   2742   3275   -390    -57   -559       N
ATOM   5351  CA  ILE B  18      36.902   6.782 -27.886  1.00 22.20           C
ANISOU 5351  CA  ILE B  18     1621   3140   3674   -305   -109   -589       C
ATOM   5352  C   ILE B  18      36.991   5.910 -26.624  1.00 25.46           C
ANISOU 5352  C   ILE B  18     2053   3540   4080   -261   -276   -603       C
ATOM   5353  O   ILE B  18      37.528   4.808 -26.706  1.00 28.77           O
ANISOU 5353  O   ILE B  18     2430   3969   4532   -179   -345   -627       O
ATOM   5354  CB  ILE B  18      38.293   6.958 -28.551  1.00 28.48           C
ANISOU 5354  CB  ILE B  18     2304   3979   4539   -305    -49   -625       C
ATOM   5355  CG1 ILE B  18      39.221   7.814 -27.701  1.00 29.25           C
ANISOU 5355  CG1 ILE B  18     2354   4083   4678   -366    -93   -642       C
ATOM   5356  CG2 ILE B  18      38.152   7.617 -29.936  1.00 28.84           C
ANISOU 5356  CG2 ILE B  18     2358   4036   4564   -355    110   -603       C
ATOM   5357  CD1 ILE B  18      40.608   7.971 -28.303  1.00 29.75           C
ANISOU 5357  CD1 ILE B  18     2295   4198   4812   -374    -38   -681       C
ATOM   5358  H  AILE B  18      36.694   8.748 -27.092  0.50  0.00           H
ATOM   5359  H  BILE B  18      36.752   8.790 -27.201  0.50  0.00           H
ATOM   5360  HA  ILE B  18      36.286   6.234 -28.598  1.00  0.00           H
ATOM   5361  HB  ILE B  18      38.745   5.974 -28.678  1.00  0.00           H
ATOM   5362 HG12 ILE B  18      39.320   7.349 -26.720  1.00  0.00           H
ATOM   5363 HG13 ILE B  18      38.776   8.802 -27.579  1.00  0.00           H
ATOM   5364 HG21 ILE B  18      37.490   7.016 -30.559  1.00  0.00           H
ATOM   5365 HG22 ILE B  18      39.132   7.684 -30.408  1.00  0.00           H
ATOM   5366 HG23 ILE B  18      37.735   8.617 -29.822  1.00  0.00           H
ATOM   5367 HD11 ILE B  18      41.341   8.085 -27.504  1.00  0.00           H
ATOM   5368 HD12 ILE B  18      40.850   7.087 -28.893  1.00  0.00           H
ATOM   5369 HD13 ILE B  18      40.628   8.853 -28.944  1.00  0.00           H
ATOM   5370  N   ASP B  19      36.439   6.366 -25.496  1.00 24.31           N
ANISOU 5370  N   ASP B  19     1987   3367   3884   -315   -340   -589       N
ATOM   5371  CA  ASP B  19      36.469   5.567 -24.265  1.00 26.55           C
ANISOU 5371  CA  ASP B  19     2326   3632   4129   -296   -501   -590       C
ATOM   5372  C   ASP B  19      35.079   5.263 -23.666  1.00 23.94           C
ANISOU 5372  C   ASP B  19     2133   3276   3685   -320   -539   -558       C
ATOM   5373  O   ASP B  19      34.961   4.961 -22.491  1.00 25.08           O
ANISOU 5373  O   ASP B  19     2359   3403   3766   -349   -651   -552       O
ATOM   5374  CB  ASP B  19      37.350   6.233 -23.209  1.00 33.43           C
ANISOU 5374  CB  ASP B  19     3181   4501   5020   -352   -568   -606       C
ATOM   5375  CG  ASP B  19      36.799   7.559 -22.732  1.00 39.95           C
ANISOU 5375  CG  ASP B  19     4065   5309   5805   -449   -508   -603       C
ATOM   5376  OD1 ASP B  19      35.902   8.133 -23.409  1.00 41.06           O
ANISOU 5376  OD1 ASP B  19     4234   5441   5928   -468   -395   -592       O
ATOM   5377  OD2 ASP B  19      37.279   8.035 -21.673  1.00 44.11           O
ANISOU 5377  OD2 ASP B  19     4614   5826   6320   -504   -580   -614       O
ATOM   5378  H   ASP B  19      35.995   7.273 -25.490  1.00  0.00           H
ATOM   5379  HA  ASP B  19      36.930   4.611 -24.513  1.00  0.00           H
ATOM   5380  HB2 ASP B  19      38.338   6.401 -23.637  1.00  0.00           H
ATOM   5381  HB3 ASP B  19      37.445   5.563 -22.355  1.00  0.00           H
ATOM   5382  N   GLY B  20      34.039   5.321 -24.471  1.00 20.80           N
ANISOU 5382  N   GLY B  20     1795   2872   3235   -308   -430   -516       N
ATOM   5383  CA  GLY B  20      32.696   5.039 -24.011  1.00 19.67           C
ANISOU 5383  CA  GLY B  20     1785   2712   2976   -326   -437   -475       C
ATOM   5384  C   GLY B  20      31.775   5.107 -25.204  1.00 18.33           C
ANISOU 5384  C   GLY B  20     1641   2539   2786   -298   -318   -433       C
ATOM   5385  O   GLY B  20      32.182   5.516 -26.286  1.00 19.02           O
ANISOU 5385  O   GLY B  20     1660   2631   2936   -281   -231   -435       O
ATOM   5386  H   GLY B  20      34.183   5.570 -25.439  1.00  0.00           H
ATOM   5387  HA2 GLY B  20      32.657   4.043 -23.569  1.00  0.00           H
ATOM   5388  HA3 GLY B  20      32.396   5.782 -23.272  1.00  0.00           H
ATOM   5389  N   TRP B  21      30.541   4.677 -25.023  1.00 15.29           N
ANISOU 5389  N   TRP B  21     1356   2147   2308   -303   -319   -394       N
ATOM   5390  CA  TRP B  21      29.575   4.697 -26.095  1.00 12.94           C
ANISOU 5390  CA  TRP B  21     1087   1841   1989   -280   -228   -349       C
ATOM   5391  C   TRP B  21      28.724   5.969 -26.008  1.00 12.74           C
ANISOU 5391  C   TRP B  21     1077   1802   1964   -326   -142   -352       C
ATOM   5392  O   TRP B  21      28.246   6.455 -27.034  1.00 12.29           O
ANISOU 5392  O   TRP B  21     1014   1724   1930   -313    -62   -323       O
ATOM   5393  CB  TRP B  21      28.640   3.478 -25.981  1.00 13.42           C
ANISOU 5393  CB  TRP B  21     1240   1903   1955   -262   -283   -306       C
ATOM   5394  CG  TRP B  21      29.257   2.192 -26.447  1.00 15.05           C
ANISOU 5394  CG  TRP B  21     1449   2104   2166   -197   -358   -295       C
ATOM   5395  CD1 TRP B  21      30.570   1.874 -26.520  1.00 16.79           C
ANISOU 5395  CD1 TRP B  21     1595   2324   2461   -152   -410   -335       C
ATOM   5396  CD2 TRP B  21      28.528   1.057 -26.934  1.00 14.90           C
ANISOU 5396  CD2 TRP B  21     1510   2073   2079   -165   -388   -247       C
ATOM   5397  NE1 TRP B  21      30.713   0.583 -27.019  1.00 16.88           N
ANISOU 5397  NE1 TRP B  21     1635   2318   2459    -82   -473   -322       N
ATOM   5398  CE2 TRP B  21      29.468   0.067 -27.271  1.00 15.97           C
ANISOU 5398  CE2 TRP B  21     1626   2193   2251    -94   -463   -264       C
ATOM   5399  CE3 TRP B  21      27.174   0.793 -27.086  1.00 15.04           C
ANISOU 5399  CE3 TRP B  21     1608   2092   2014   -192   -365   -196       C
ATOM   5400  CZ2 TRP B  21      29.090  -1.168 -27.789  1.00 17.09           C
ANISOU 5400  CZ2 TRP B  21     1843   2309   2341    -49   -514   -230       C
ATOM   5401  CZ3 TRP B  21      26.790  -0.453 -27.585  1.00 16.36           C
ANISOU 5401  CZ3 TRP B  21     1848   2241   2126   -160   -419   -154       C
ATOM   5402  CH2 TRP B  21      27.749  -1.397 -27.946  1.00 16.80           C
ANISOU 5402  CH2 TRP B  21     1899   2272   2214    -88   -491   -171       C
ATOM   5403  H   TRP B  21      30.267   4.327 -24.116  1.00  0.00           H
ATOM   5404  HA  TRP B  21      30.094   4.670 -27.053  1.00  0.00           H
ATOM   5405  HB2 TRP B  21      28.354   3.362 -24.936  1.00  0.00           H
ATOM   5406  HB3 TRP B  21      27.743   3.669 -26.570  1.00  0.00           H
ATOM   5407  HD1 TRP B  21      31.384   2.524 -26.234  1.00  0.00           H
ATOM   5408  HE3 TRP B  21      26.434   1.535 -26.824  1.00  0.00           H
ATOM   5409  HZ2 TRP B  21      29.823  -1.915 -28.056  1.00  0.00           H
ATOM   5410  HZ3 TRP B  21      25.741  -0.687 -27.692  1.00  0.00           H
ATOM   5411  HH2 TRP B  21      27.425  -2.339 -28.363  1.00  0.00           H
ATOM   5412  HE1 TRP B  21      31.590   0.105 -27.171  1.00  0.00           H
ATOM   5413  N   TYR B  22      28.505   6.446 -24.787  1.00 13.73           N
ANISOU 5413  N   TYR B  22     1229   1930   2059   -380   -166   -389       N
ATOM   5414  CA  TYR B  22      27.665   7.636 -24.537  1.00 15.64           C
ANISOU 5414  CA  TYR B  22     1485   2152   2306   -415    -92   -412       C
ATOM   5415  C   TYR B  22      28.468   8.526 -23.593  1.00 16.77           C
ANISOU 5415  C   TYR B  22     1606   2286   2480   -468   -112   -473       C
ATOM   5416  O   TYR B  22      29.266   8.018 -22.799  1.00 15.87           O
ANISOU 5416  O   TYR B  22     1494   2191   2346   -491   -200   -492       O
ATOM   5417  CB  TYR B  22      26.373   7.290 -23.836  1.00 14.50           C
ANISOU 5417  CB  TYR B  22     1407   2029   2073   -437    -89   -414       C
ATOM   5418  CG  TYR B  22      25.546   6.273 -24.569  1.00 12.71           C
ANISOU 5418  CG  TYR B  22     1211   1816   1802   -400    -91   -353       C
ATOM   5419  CD1 TYR B  22      24.777   6.639 -25.651  1.00 12.01           C
ANISOU 5419  CD1 TYR B  22     1107   1706   1751   -364    -25   -319       C
ATOM   5420  CD2 TYR B  22      25.572   4.939 -24.206  1.00 13.26           C
ANISOU 5420  CD2 TYR B  22     1333   1911   1792   -406   -173   -326       C
ATOM   5421  CE1 TYR B  22      24.023   5.684 -26.361  1.00 12.87           C
ANISOU 5421  CE1 TYR B  22     1248   1825   1816   -337    -35   -259       C
ATOM   5422  CE2 TYR B  22      24.828   3.993 -24.904  1.00 12.85           C
ANISOU 5422  CE2 TYR B  22     1319   1867   1697   -379   -181   -268       C
ATOM   5423  CZ  TYR B  22      24.062   4.363 -25.956  1.00 12.69           C
ANISOU 5423  CZ  TYR B  22     1277   1832   1712   -347   -110   -237       C
ATOM   5424  OH  TYR B  22      23.320   3.422 -26.644  1.00 11.78           O
ANISOU 5424  OH  TYR B  22     1203   1722   1550   -329   -126   -179       O
ATOM   5425  H   TYR B  22      28.929   5.977 -23.999  1.00  0.00           H
ATOM   5426  HA  TYR B  22      27.461   8.160 -25.471  1.00  0.00           H
ATOM   5427  HB2 TYR B  22      25.784   8.201 -23.729  1.00  0.00           H
ATOM   5428  HB3 TYR B  22      26.605   6.904 -22.843  1.00  0.00           H
ATOM   5429  HD1 TYR B  22      24.752   7.674 -25.960  1.00  0.00           H
ATOM   5430  HD2 TYR B  22      26.179   4.627 -23.369  1.00  0.00           H
ATOM   5431  HE1 TYR B  22      23.423   5.980 -27.209  1.00  0.00           H
ATOM   5432  HE2 TYR B  22      24.862   2.956 -24.604  1.00  0.00           H
ATOM   5433  HH  TYR B  22      22.408   3.716 -26.706  1.00  0.00           H
ATOM   5434  N   GLY B  23      28.234   9.841 -23.636  1.00 15.72           N
ANISOU 5434  N   GLY B  23     1464   2114   2394   -491    -45   -503       N
ATOM   5435  CA  GLY B  23      28.964  10.714 -22.736  1.00 15.81           C
ANISOU 5435  CA  GLY B  23     1467   2110   2429   -549    -66   -563       C
ATOM   5436  C   GLY B  23      28.591  12.174 -22.844  1.00 15.96           C
ANISOU 5436  C   GLY B  23     1491   2070   2502   -568      4   -597       C
ATOM   5437  O   GLY B  23      27.536  12.531 -23.432  1.00 15.91           O
ANISOU 5437  O   GLY B  23     1502   2034   2510   -532     65   -582       O
ATOM   5438  H   GLY B  23      27.560  10.221 -24.285  1.00  0.00           H
ATOM   5439  HA2 GLY B  23      30.027  10.617 -22.955  1.00  0.00           H
ATOM   5440  HA3 GLY B  23      28.788  10.384 -21.712  1.00  0.00           H
ATOM   5441  N   PHE B  24      29.481  13.008 -22.304  1.00 15.04           N
ANISOU 5441  N   PHE B  24     1361   1930   2423   -624    -17   -642       N
ATOM   5442  CA  PHE B  24      29.216  14.403 -22.099  1.00 15.47           C
ANISOU 5442  CA  PHE B  24     1441   1917   2518   -653     27   -690       C
ATOM   5443  C   PHE B  24      30.364  15.210 -22.684  1.00 16.79           C
ANISOU 5443  C   PHE B  24     1562   2047   2769   -695     26   -680       C
ATOM   5444  O   PHE B  24      31.545  14.821 -22.578  1.00 17.54           O
ANISOU 5444  O   PHE B  24     1600   2183   2881   -727    -24   -675       O
ATOM   5445  CB  PHE B  24      29.195  14.746 -20.607  1.00 15.85           C
ANISOU 5445  CB  PHE B  24     1542   1968   2512   -711     -4   -772       C
ATOM   5446  CG  PHE B  24      28.125  14.025 -19.804  1.00 16.53           C
ANISOU 5446  CG  PHE B  24     1684   2101   2497   -704      3   -798       C
ATOM   5447  CD1 PHE B  24      28.411  12.818 -19.171  1.00 17.13           C
ANISOU 5447  CD1 PHE B  24     1781   2242   2485   -728    -71   -779       C
ATOM   5448  CD2 PHE B  24      26.879  14.602 -19.614  1.00 17.73           C
ANISOU 5448  CD2 PHE B  24     1865   2229   2640   -682     79   -849       C
ATOM   5449  CE1 PHE B  24      27.421  12.151 -18.393  1.00 17.87           C
ANISOU 5449  CE1 PHE B  24     1940   2382   2467   -749    -61   -800       C
ATOM   5450  CE2 PHE B  24      25.889  13.965 -18.823  1.00 19.74           C
ANISOU 5450  CE2 PHE B  24     2162   2543   2796   -695    102   -885       C
ATOM   5451  CZ  PHE B  24      26.172  12.735 -18.224  1.00 19.42           C
ANISOU 5451  CZ  PHE B  24     2155   2571   2651   -738     35   -855       C
ATOM   5452  H   PHE B  24      30.381  12.641 -22.027  1.00  0.00           H
ATOM   5453  HA  PHE B  24      28.274  14.685 -22.568  1.00  0.00           H
ATOM   5454  HB2 PHE B  24      29.029  15.819 -20.508  1.00  0.00           H
ATOM   5455  HB3 PHE B  24      30.169  14.505 -20.182  1.00  0.00           H
ATOM   5456  HD1 PHE B  24      29.394  12.383 -19.271  1.00  0.00           H
ATOM   5457  HD2 PHE B  24      26.658  15.553 -20.076  1.00  0.00           H
ATOM   5458  HE1 PHE B  24      27.640  11.197 -17.937  1.00  0.00           H
ATOM   5459  HE2 PHE B  24      24.923  14.428 -18.685  1.00  0.00           H
ATOM   5460  HZ  PHE B  24      25.420  12.238 -17.629  1.00  0.00           H
ATOM   5461  N   ARG B  25      30.033  16.345 -23.270  1.00 16.57           N
ANISOU 5461  N   ARG B  25     1557   1941   2798   -700     76   -679       N
ATOM   5462  CA  ARG B  25      31.036  17.351 -23.572  1.00 17.40           C
ANISOU 5462  CA  ARG B  25     1643   1998   2969   -770     75   -682       C
ATOM   5463  C   ARG B  25      30.564  18.647 -22.928  1.00 19.03           C
ANISOU 5463  C   ARG B  25     1922   2113   3196   -797     81   -746       C
ATOM   5464  O   ARG B  25      29.368  18.910 -22.903  1.00 21.16           O
ANISOU 5464  O   ARG B  25     2239   2339   3462   -739    111   -766       O
ATOM   5465  CB  ARG B  25      31.173  17.560 -25.067  1.00 18.89           C
ANISOU 5465  CB  ARG B  25     1815   2160   3203   -768    121   -610       C
ATOM   5466  CG  ARG B  25      31.959  16.494 -25.739  1.00 19.91           C
ANISOU 5466  CG  ARG B  25     1864   2374   3326   -761    125   -566       C
ATOM   5467  CD  ARG B  25      32.068  16.725 -27.234  1.00 20.14           C
ANISOU 5467  CD  ARG B  25     1891   2380   3380   -776    185   -500       C
ATOM   5468  NE  ARG B  25      32.865  15.663 -27.837  1.00 19.46           N
ANISOU 5468  NE  ARG B  25     1728   2384   3281   -758    198   -474       N
ATOM   5469  CZ  ARG B  25      33.232  15.606 -29.120  1.00 19.07           C
ANISOU 5469  CZ  ARG B  25     1667   2347   3233   -778    257   -425       C
ATOM   5470  NH1 ARG B  25      32.881  16.559 -29.975  1.00 19.12           N
ANISOU 5470  NH1 ARG B  25     1740   2275   3249   -831    299   -384       N
ATOM   5471  NH2 ARG B  25      33.990  14.604 -29.526  1.00 19.00           N
ANISOU 5471  NH2 ARG B  25     1585   2422   3211   -748    268   -422       N
ATOM   5472  H   ARG B  25      29.068  16.517 -23.512  1.00  0.00           H
ATOM   5473  HA  ARG B  25      31.996  17.055 -23.150  1.00  0.00           H
ATOM   5474  HB2 ARG B  25      31.668  18.516 -25.239  1.00  0.00           H
ATOM   5475  HB3 ARG B  25      30.178  17.595 -25.510  1.00  0.00           H
ATOM   5476  HG2 ARG B  25      31.471  15.535 -25.566  1.00  0.00           H
ATOM   5477  HG3 ARG B  25      32.960  16.466 -25.309  1.00  0.00           H
ATOM   5478  HD2 ARG B  25      31.071  16.725 -27.674  1.00  0.00           H
ATOM   5479  HD3 ARG B  25      32.546  17.687 -27.419  1.00  0.00           H
ATOM   5480  HE  ARG B  25      33.164  14.909 -27.235  1.00  0.00           H
ATOM   5481 HH11 ARG B  25      32.315  17.335 -29.662  1.00  0.00           H
ATOM   5482 HH12 ARG B  25      33.180  16.509 -30.938  1.00  0.00           H
ATOM   5483 HH21 ARG B  25      34.271  13.886 -28.873  1.00  0.00           H
ATOM   5484 HH22 ARG B  25      34.289  14.555 -30.490  1.00  0.00           H
ATOM   5485  N   HIS B  26      31.492  19.451 -22.409  1.00 19.25           N
ANISOU 5485  N   HIS B  26     1956   2111   3245   -875     48   -780       N
ATOM   5486  CA  HIS B  26      31.079  20.629 -21.719  1.00 19.53           C
ANISOU 5486  CA  HIS B  26     2071   2056   3293   -897     47   -850       C
ATOM   5487  C   HIS B  26      31.966  21.786 -22.104  1.00 20.18           C
ANISOU 5487  C   HIS B  26     2175   2070   3423   -967     30   -823       C
ATOM   5488  O   HIS B  26      33.104  21.618 -22.563  1.00 20.40           O
ANISOU 5488  O   HIS B  26     2146   2148   3456  -1015     13   -765       O
ATOM   5489  CB  HIS B  26      31.114  20.456 -20.192  1.00 19.55           C
ANISOU 5489  CB  HIS B  26     2111   2098   3220   -917      8   -923       C
ATOM   5490  CG  HIS B  26      32.486  20.388 -19.629  1.00 21.05           C
ANISOU 5490  CG  HIS B  26     2279   2333   3385   -982    -64   -902       C
ATOM   5491  ND1 HIS B  26      33.168  19.199 -19.488  1.00 19.83           N
ANISOU 5491  ND1 HIS B  26     2061   2275   3197   -977   -114   -861       N
ATOM   5492  CD2 HIS B  26      33.314  21.357 -19.165  1.00 23.93           C
ANISOU 5492  CD2 HIS B  26     2675   2653   3763  -1053   -107   -917       C
ATOM   5493  CE1 HIS B  26      34.361  19.438 -18.984  1.00 21.40           C
ANISOU 5493  CE1 HIS B  26     2243   2487   3399  -1038   -185   -853       C
ATOM   5494  NE2 HIS B  26      34.478  20.740 -18.779  1.00 23.86           N
ANISOU 5494  NE2 HIS B  26     2611   2719   3735  -1090   -180   -884       N
ATOM   5495  H   HIS B  26      32.473  19.229 -22.503  1.00  0.00           H
ATOM   5496  HA  HIS B  26      30.057  20.863 -22.017  1.00  0.00           H
ATOM   5497  HB2 HIS B  26      30.598  21.302 -19.738  1.00  0.00           H
ATOM   5498  HB3 HIS B  26      30.583  19.541 -19.931  1.00  0.00           H
ATOM   5499  HD2 HIS B  26      33.098  22.414 -19.110  1.00  0.00           H
ATOM   5500  HE1 HIS B  26      35.117  18.696 -18.773  1.00  0.00           H
ATOM   5501  HD1 HIS B  26      32.809  18.287 -19.733  1.00  0.00           H
ATOM   5502  N   GLN B  27      31.407  22.959 -21.883  1.00 21.18           N
ANISOU 5502  N   GLN B  27     2385   2081   3582   -970     34   -873       N
ATOM   5503  CA  GLN B  27      32.175  24.167 -21.892  1.00 23.83           C
ANISOU 5503  CA  GLN B  27     2771   2339   3944  -1048      1   -865       C
ATOM   5504  C   GLN B  27      31.799  24.986 -20.660  1.00 24.36           C
ANISOU 5504  C   GLN B  27     2924   2338   3992  -1050    -23   -965       C
ATOM   5505  O   GLN B  27      30.607  25.209 -20.393  1.00 24.22           O
ANISOU 5505  O   GLN B  27     2951   2263   3987   -976      9  -1034       O
ATOM   5506  CB  GLN B  27      31.913  24.951 -23.173  1.00 26.86           C
ANISOU 5506  CB  GLN B  27     3198   2618   4392  -1056     18   -806       C
ATOM   5507  CG  GLN B  27      32.713  26.292 -23.155  1.00 42.41           C
ANISOU 5507  CG  GLN B  27     5238   4496   6379  -1154    -28   -795       C
ATOM   5508  CD  GLN B  27      32.979  26.879 -24.526  1.00 48.63           C
ANISOU 5508  CD  GLN B  27     6060   5217   7200  -1211    -25   -702       C
ATOM   5509  OE1 GLN B  27      34.075  27.406 -24.793  1.00 54.29           O
ANISOU 5509  OE1 GLN B  27     6778   5940   7911  -1320    -49   -655       O
ATOM   5510  NE2 GLN B  27      31.980  26.836 -25.392  1.00 49.38           N
ANISOU 5510  NE2 GLN B  27     6190   5245   7327  -1146     -3   -672       N
ATOM   5511  H   GLN B  27      30.414  23.007 -21.703  1.00  0.00           H
ATOM   5512  HA  GLN B  27      33.234  23.915 -21.841  1.00  0.00           H
ATOM   5513  HB2 GLN B  27      30.848  25.168 -23.251  1.00  0.00           H
ATOM   5514  HB3 GLN B  27      32.225  24.356 -24.031  1.00  0.00           H
ATOM   5515  HG2 GLN B  27      32.145  27.020 -22.577  1.00  0.00           H
ATOM   5516  HG3 GLN B  27      33.668  26.121 -22.658  1.00  0.00           H
ATOM   5517 HE21 GLN B  27      31.102  26.412 -25.129  1.00  0.00           H
ATOM   5518 HE22 GLN B  27      32.096  27.227 -26.316  1.00  0.00           H
ATOM   5519  N   ASN B  28      32.805  25.440 -19.909  1.00 25.95           N
ANISOU 5519  N   ASN B  28     3147   2548   4167  -1131    -78   -977       N
ATOM   5520  CA  ASN B  28      32.553  26.289 -18.757  1.00 27.35           C
ANISOU 5520  CA  ASN B  28     3420   2656   4318  -1144   -103  -1069       C
ATOM   5521  C   ASN B  28      33.695  27.289 -18.605  1.00 28.21           C
ANISOU 5521  C   ASN B  28     3570   2710   4440  -1250   -170  -1047       C
ATOM   5522  O   ASN B  28      34.503  27.494 -19.527  1.00 27.98           O
ANISOU 5522  O   ASN B  28     3500   2681   4451  -1311   -183   -964       O
ATOM   5523  CB  ASN B  28      32.369  25.465 -17.477  1.00 28.66           C
ANISOU 5523  CB  ASN B  28     3585   2913   4393  -1130   -109  -1131       C
ATOM   5524  CG  ASN B  28      33.618  24.614 -17.124  1.00 30.21           C
ANISOU 5524  CG  ASN B  28     3712   3219   4548  -1192   -176  -1074       C
ATOM   5525  OD1 ASN B  28      34.691  24.786 -17.719  1.00 31.68           O
ANISOU 5525  OD1 ASN B  28     3844   3415   4778  -1249   -212  -1005       O
ATOM   5526  ND2 ASN B  28      33.476  23.716 -16.140  1.00 27.12           N
ANISOU 5526  ND2 ASN B  28     3325   2907   4072  -1182   -198  -1104       N
ATOM   5527  H   ASN B  28      33.755  25.190 -20.145  1.00  0.00           H
ATOM   5528  HA  ASN B  28      31.634  26.846 -18.939  1.00  0.00           H
ATOM   5529  HB2 ASN B  28      31.519  24.796 -17.613  1.00  0.00           H
ATOM   5530  HB3 ASN B  28      32.157  26.141 -16.649  1.00  0.00           H
ATOM   5531 HD21 ASN B  28      34.259  23.142 -15.864  1.00  0.00           H
ATOM   5532 HD22 ASN B  28      32.586  23.613 -15.675  1.00  0.00           H
ATOM   5533  N   SER B  29      33.764  27.937 -17.455  1.00 31.54           N
ANISOU 5533  N   SER B  29     4073   3085   4824  -1280   -210  -1122       N
ATOM   5534  CA  SER B  29      34.774  28.961 -17.279  1.00 35.60           C
ANISOU 5534  CA  SER B  29     4636   3534   5356  -1383   -283  -1105       C
ATOM   5535  C   SER B  29      36.205  28.400 -17.231  1.00 34.89           C
ANISOU 5535  C   SER B  29     4447   3549   5260  -1468   -341  -1035       C
ATOM   5536  O   SER B  29      37.165  29.168 -17.307  1.00 34.68           O
ANISOU 5536  O   SER B  29     4427   3482   5266  -1562   -400  -1003       O
ATOM   5537  CB  SER B  29      34.481  29.720 -15.986  1.00 41.35           C
ANISOU 5537  CB  SER B  29     5480   4189   6041  -1389   -316  -1209       C
ATOM   5538  OG  SER B  29      34.515  28.784 -14.922  1.00 45.44           O
ANISOU 5538  OG  SER B  29     5974   4814   6477  -1380   -324  -1246       O
ATOM   5539  H   SER B  29      33.120  27.721 -16.707  1.00  0.00           H
ATOM   5540  HA  SER B  29      34.705  29.660 -18.112  1.00  0.00           H
ATOM   5541  HB2 SER B  29      33.496  30.183 -16.042  1.00  0.00           H
ATOM   5542  HB3 SER B  29      35.240  30.486 -15.828  1.00  0.00           H
ATOM   5543  HG  SER B  29      34.334  29.234 -14.094  1.00  0.00           H
ATOM   5544  N   GLU B  30      36.356  27.094 -17.054  1.00 34.90           N
ANISOU 5544  N   GLU B  30     4357   3678   5227  -1434   -335  -1015       N
ATOM   5545  CA  GLU B  30      37.676  26.474 -16.961  1.00 38.10           C
ANISOU 5545  CA  GLU B  30     4658   4180   5637  -1494   -400   -957       C
ATOM   5546  C   GLU B  30      38.088  25.786 -18.272  1.00 38.87           C
ANISOU 5546  C   GLU B  30     4630   4356   5781  -1479   -352   -874       C
ATOM   5547  O   GLU B  30      39.156  25.165 -18.335  1.00 42.13           O
ANISOU 5547  O   GLU B  30     4936   4859   6211  -1510   -392   -831       O
ATOM   5548  CB  GLU B  30      37.738  25.441 -15.842  1.00 40.40           C
ANISOU 5548  CB  GLU B  30     4937   4553   5861  -1469   -452   -986       C
ATOM   5549  CG  GLU B  30      37.276  25.893 -14.476  1.00 46.30           C
ANISOU 5549  CG  GLU B  30     5807   5244   6539  -1479   -489  -1073       C
ATOM   5550  CD  GLU B  30      37.824  24.980 -13.367  1.00 49.07           C
ANISOU 5550  CD  GLU B  30     6145   5668   6830  -1495   -585  -1076       C
ATOM   5551  OE1 GLU B  30      39.076  24.918 -13.229  1.00 55.50           O
ANISOU 5551  OE1 GLU B  30     6893   6506   7687  -1557   -681  -1033       O
ATOM   5552  OE2 GLU B  30      37.027  24.323 -12.642  1.00 43.09           O
ANISOU 5552  OE2 GLU B  30     5442   4941   5989  -1450   -569  -1119       O
ATOM   5553  H   GLU B  30      35.534  26.511 -16.981  1.00  0.00           H
ATOM   5554  HA  GLU B  30      38.404  27.255 -16.743  1.00  0.00           H
ATOM   5555  HB2 GLU B  30      37.117  24.596 -16.138  1.00  0.00           H
ATOM   5556  HB3 GLU B  30      38.768  25.093 -15.756  1.00  0.00           H
ATOM   5557  HG2 GLU B  30      36.187  25.873 -14.446  1.00  0.00           H
ATOM   5558  HG3 GLU B  30      37.619  26.913 -14.302  1.00  0.00           H
ATOM   5559  N   GLY B  31      37.252  25.891 -19.303  1.00 34.65           N
ANISOU 5559  N   GLY B  31     4359   3397   5407  -1423   -282   -804       N
ATOM   5560  CA  GLY B  31      37.588  25.373 -20.617  1.00 33.59           C
ANISOU 5560  CA  GLY B  31     4218   3336   5210  -1498   -323   -679       C
ATOM   5561  C   GLY B  31      36.539  24.386 -21.125  1.00 31.16           C
ANISOU 5561  C   GLY B  31     3900   3028   4914  -1429   -324   -609       C
ATOM   5562  O   GLY B  31      35.339  24.563 -20.899  1.00 31.65           O
ANISOU 5562  O   GLY B  31     3969   2948   5108  -1331   -332   -600       O
ATOM   5563  H   GLY B  31      36.359  26.344 -19.167  1.00  0.00           H
ATOM   5564  HA2 GLY B  31      37.657  26.206 -21.317  1.00  0.00           H
ATOM   5565  HA3 GLY B  31      38.554  24.871 -20.565  1.00  0.00           H
ATOM   5566  N   THR B  32      36.998  23.357 -21.822  1.00 26.99           N
ANISOU 5566  N   THR B  32     3318   2650   4287  -1449   -295   -577       N
ATOM   5567  CA  THR B  32      36.077  22.380 -22.388  1.00 27.14           C
ANISOU 5567  CA  THR B  32     3333   2677   4303  -1402   -302   -503       C
ATOM   5568  C   THR B  32      36.599  21.012 -22.048  1.00 25.86           C
ANISOU 5568  C   THR B  32     3062   2716   4047  -1328   -216   -591       C
ATOM   5569  O   THR B  32      37.750  20.857 -21.650  1.00 28.17           O
ANISOU 5569  O   THR B  32     3282   3120   4301  -1336   -181   -679       O
ATOM   5570  CB  THR B  32      36.004  22.500 -23.895  1.00 31.32           C
ANISOU 5570  CB  THR B  32     3933   3177   4789  -1509   -315   -379       C
ATOM   5571  OG1 THR B  32      37.288  22.181 -24.441  1.00 34.96           O
ANISOU 5571  OG1 THR B  32     4379   3805   5099  -1609   -219   -418       O
ATOM   5572  CG2 THR B  32      35.625  23.900 -24.302  1.00 32.05           C
ANISOU 5572  CG2 THR B  32     4142   3086   4950  -1577   -393   -295       C
ATOM   5573  H   THR B  32      37.992  23.249 -21.962  1.00  0.00           H
ATOM   5574  HA  THR B  32      35.085  22.515 -21.958  1.00  0.00           H
ATOM   5575  HB  THR B  32      35.263  21.798 -24.279  1.00  0.00           H
ATOM   5576  HG1 THR B  32      37.256  22.253 -25.398  1.00  0.00           H
ATOM   5577 HG21 THR B  32      35.579  23.963 -25.389  1.00  0.00           H
ATOM   5578 HG22 THR B  32      34.650  24.149 -23.882  1.00  0.00           H
ATOM   5579 HG23 THR B  32      36.371  24.601 -23.929  1.00  0.00           H
ATOM   5580  N   GLY B  33      35.742  20.019 -22.174  1.00 22.75           N
ANISOU 5580  N   GLY B  33     2645   2342   3658  -1249   -207   -563       N
ATOM   5581  CA  GLY B  33      36.181  18.670 -21.924  1.00 20.95           C
ANISOU 5581  CA  GLY B  33     2314   2275   3370  -1176   -159   -630       C
ATOM   5582  C   GLY B  33      35.147  17.669 -22.384  1.00 20.06           C
ANISOU 5582  C   GLY B  33     2206   2172   3242  -1101   -155   -553       C
ATOM   5583  O   GLY B  33      34.048  18.027 -22.829  1.00 19.82           O
ANISOU 5583  O   GLY B  33     2251   2019   3261  -1087   -206   -441       O
ATOM   5584  H   GLY B  33      34.786  20.202 -22.443  1.00  0.00           H
ATOM   5585  HA2 GLY B  33      36.349  18.543 -20.855  1.00  0.00           H
ATOM   5586  HA3 GLY B  33      37.115  18.492 -22.457  1.00  0.00           H
ATOM   5587  N   GLN B  34      35.517  16.407 -22.239  1.00 18.99           N
ANISOU 5587  N   GLN B  34     1981   2163   3072  -1036   -124   -606       N
ATOM   5588  CA  GLN B  34      34.669  15.298 -22.622  1.00 18.02           C
ANISOU 5588  CA  GLN B  34     1859   2073   2916   -952   -114   -539       C
ATOM   5589  C   GLN B  34      34.858  14.181 -21.606  1.00 18.25           C
ANISOU 5589  C   GLN B  34     1814   2177   2944   -817   -142   -605       C
ATOM   5590  O   GLN B  34      35.992  13.961 -21.140  1.00 20.56           O
ANISOU 5590  O   GLN B  34     2012   2518   3281   -832   -179   -700       O
ATOM   5591  CB  GLN B  34      35.103  14.810 -24.015  1.00 18.33           C
ANISOU 5591  CB  GLN B  34     1893   2177   2895  -1098    -36   -526       C
ATOM   5592  CG  GLN B  34      34.296  13.605 -24.536  1.00 18.13           C
ANISOU 5592  CG  GLN B  34     1874   2191   2825  -1044    -18   -466       C
ATOM   5593  CD  GLN B  34      34.807  13.135 -25.898  1.00 21.19           C
ANISOU 5593  CD  GLN B  34     2299   2640   3112  -1180     90   -466       C
ATOM   5594  OE1 GLN B  34      34.200  13.409 -26.910  1.00 22.55           O
ANISOU 5594  OE1 GLN B  34     2622   2765   3182  -1294     70   -345       O
ATOM   5595  NE2 GLN B  34      35.950  12.453 -25.910  1.00 23.67           N
ANISOU 5595  NE2 GLN B  34     2484   3037   3471  -1156    195   -608       N
ATOM   5596  H   GLN B  34      36.426  16.210 -21.846  1.00  0.00           H
ATOM   5597  HA  GLN B  34      33.626  15.613 -22.643  1.00  0.00           H
ATOM   5598  HB2 GLN B  34      36.154  14.523 -23.966  1.00  0.00           H
ATOM   5599  HB3 GLN B  34      34.998  15.633 -24.722  1.00  0.00           H
ATOM   5600  HG2 GLN B  34      33.249  13.894 -24.631  1.00  0.00           H
ATOM   5601  HG3 GLN B  34      34.377  12.785 -23.822  1.00  0.00           H
ATOM   5602 HE21 GLN B  34      36.430  12.257 -25.043  1.00  0.00           H
ATOM   5603 HE22 GLN B  34      36.337  12.131 -26.786  1.00  0.00           H
ATOM   5604  N   ALA B  35      33.795  13.445 -21.313  1.00 17.01           N
ANISOU 5604  N   ALA B  35     1696   2012   2755   -707   -149   -551       N
ATOM   5605  CA  ALA B  35      33.866  12.277 -20.452  1.00 18.02           C
ANISOU 5605  CA  ALA B  35     1802   2194   2849   -616   -202   -580       C
ATOM   5606  C   ALA B  35      32.831  11.258 -20.869  1.00 17.88           C
ANISOU 5606  C   ALA B  35     1803   2193   2798   -541   -170   -509       C
ATOM   5607  O   ALA B  35      31.681  11.581 -21.097  1.00 18.15           O
ANISOU 5607  O   ALA B  35     1892   2167   2839   -519   -128   -451       O
ATOM   5608  CB  ALA B  35      33.635  12.663 -18.982  1.00 18.87           C
ANISOU 5608  CB  ALA B  35     2015   2257   2896   -608   -246   -623       C
ATOM   5609  H   ALA B  35      32.901  13.706 -21.704  1.00  0.00           H
ATOM   5610  HA  ALA B  35      34.856  11.831 -20.546  1.00  0.00           H
ATOM   5611  HB1 ALA B  35      33.693  11.771 -18.358  1.00  0.00           H
ATOM   5612  HB2 ALA B  35      34.399  13.375 -18.669  1.00  0.00           H
ATOM   5613  HB3 ALA B  35      32.650  13.117 -18.876  1.00  0.00           H
ATOM   5614  N   ALA B  36      33.242  10.002 -20.938  1.00 17.59           N
ANISOU 5614  N   ALA B  36     1699   2217   2768   -498   -206   -523       N
ATOM   5615  CA  ALA B  36      32.309   8.904 -21.152  1.00 17.34           C
ANISOU 5615  CA  ALA B  36     1692   2203   2693   -426   -188   -462       C
ATOM   5616  C   ALA B  36      31.383   8.764 -19.954  1.00 17.50           C
ANISOU 5616  C   ALA B  36     1833   2188   2628   -382   -207   -446       C
ATOM   5617  O   ALA B  36      31.789   8.996 -18.825  1.00 18.52           O
ANISOU 5617  O   ALA B  36     2033   2300   2704   -416   -276   -490       O
ATOM   5618  CB  ALA B  36      33.106   7.571 -21.367  1.00 18.17           C
ANISOU 5618  CB  ALA B  36     1681   2350   2871   -392   -239   -505       C
ATOM   5619  H   ALA B  36      34.227   9.800 -20.840  1.00  0.00           H
ATOM   5620  HA  ALA B  36      31.713   9.111 -22.041  1.00  0.00           H
ATOM   5621  HB1 ALA B  36      33.929   7.520 -20.655  1.00  0.00           H
ATOM   5622  HB2 ALA B  36      33.502   7.544 -22.382  1.00  0.00           H
ATOM   5623  HB3 ALA B  36      32.441   6.721 -21.214  1.00  0.00           H
ATOM   5624  N   ASP B  37      30.138   8.391 -20.204  1.00 17.01           N
ANISOU 5624  N   ASP B  37     1807   2109   2546   -340   -138   -396       N
ATOM   5625  CA  ASP B  37      29.220   7.959 -19.143  1.00 18.51           C
ANISOU 5625  CA  ASP B  37     2105   2277   2652   -332   -104   -416       C
ATOM   5626  C   ASP B  37      29.272   6.448 -19.038  1.00 18.41           C
ANISOU 5626  C   ASP B  37     2115   2314   2567   -297   -177   -372       C
ATOM   5627  O   ASP B  37      28.846   5.739 -19.960  1.00 16.23           O
ANISOU 5627  O   ASP B  37     1777   2063   2328   -244   -149   -319       O
ATOM   5628  CB  ASP B  37      27.779   8.383 -19.419  1.00 18.31           C
ANISOU 5628  CB  ASP B  37     2064   2178   2715   -309     18   -417       C
ATOM   5629  CG  ASP B  37      26.828   8.026 -18.267  1.00 20.15           C
ANISOU 5629  CG  ASP B  37     2397   2382   2877   -347    128   -501       C
ATOM   5630  OD1 ASP B  37      26.874   8.716 -17.219  1.00 21.57           O
ANISOU 5630  OD1 ASP B  37     2666   2520   3010   -439    201   -615       O
ATOM   5631  OD2 ASP B  37      26.008   7.087 -18.412  1.00 19.75           O
ANISOU 5631  OD2 ASP B  37     2349   2346   2809   -318    167   -471       O
ATOM   5632  H   ASP B  37      29.808   8.404 -21.158  1.00  0.00           H
ATOM   5633  HA  ASP B  37      29.543   8.392 -18.196  1.00  0.00           H
ATOM   5634  HB2 ASP B  37      27.755   9.462 -19.569  1.00  0.00           H
ATOM   5635  HB3 ASP B  37      27.433   7.891 -20.328  1.00  0.00           H
ATOM   5636  N  ALEU B  38      29.747   5.946 -17.902  0.48 19.74           N
ANISOU 5636  N  ALEU B  38     2397   2476   2627   -348   -293   -383       N
ATOM   5637  N  BLEU B  38      29.738   5.947 -17.897  0.52 19.74           N
ANISOU 5637  N  BLEU B  38     2398   2476   2627   -349   -293   -383       N
ATOM   5638  CA ALEU B  38      29.998   4.511 -17.771  0.48 19.52           C
ANISOU 5638  CA ALEU B  38     2390   2454   2574   -320   -435   -325       C
ATOM   5639  CA BLEU B  38      30.010   4.514 -17.765  0.52 19.87           C
ANISOU 5639  CA BLEU B  38     2434   2498   2618   -321   -437   -325       C
ATOM   5640  C  ALEU B  38      28.715   3.699 -17.673  0.48 18.65           C
ANISOU 5640  C  ALEU B  38     2373   2349   2362   -319   -340   -291       C
ATOM   5641  C  BLEU B  38      28.731   3.683 -17.643  0.52 18.68           C
ANISOU 5641  C  BLEU B  38     2382   2353   2364   -321   -345   -291       C
ATOM   5642  O  ALEU B  38      28.610   2.644 -18.290  0.48 17.68           O
ANISOU 5642  O  ALEU B  38     2190   2242   2286   -249   -375   -240       O
ATOM   5643  O  BLEU B  38      28.640   2.598 -18.221  0.52 17.76           O
ANISOU 5643  O  BLEU B  38     2209   2249   2290   -253   -386   -239       O
ATOM   5644  CB ALEU B  38      30.903   4.213 -16.565  0.48 23.75           C
ANISOU 5644  CB ALEU B  38     3051   2938   3036   -409   -677   -309       C
ATOM   5645  CB BLEU B  38      30.953   4.241 -16.575  0.52 24.42           C
ANISOU 5645  CB BLEU B  38     3130   3023   3127   -408   -681   -310       C
ATOM   5646  CG ALEU B  38      31.181   2.722 -16.326  0.48 28.56           C
ANISOU 5646  CG ALEU B  38     3693   3496   3663   -389   -899   -228       C
ATOM   5647  CG BLEU B  38      32.311   4.960 -16.570  0.52 30.73           C
ANISOU 5647  CG BLEU B  38     3812   3799   4064   -415   -811   -352       C
ATOM   5648  CD1ALEU B  38      31.955   2.100 -17.494  0.48 28.58           C
ANISOU 5648  CD1ALEU B  38     3418   3492   3950   -248   -942   -250       C
ATOM   5649  CD1BLEU B  38      33.173   4.507 -15.387  0.52 34.07           C
ANISOU 5649  CD1BLEU B  38     4361   4135   4449   -512  -1138   -303       C
ATOM   5650  CD2ALEU B  38      31.919   2.523 -14.999  0.48 33.26           C
ANISOU 5650  CD2ALEU B  38     4479   3998   4161   -530  -1211   -173       C
ATOM   5651  CD2BLEU B  38      33.092   4.774 -17.886  0.52 33.81           C
ANISOU 5651  CD2BLEU B  38     3923   4211   4713   -306   -782   -394       C
ATOM   5652  H  ALEU B  38      29.936   6.561 -17.123  0.48  0.00           H
ATOM   5653  H  BLEU B  38      29.906   6.562 -17.113  0.52  0.00           H
ATOM   5654  HA ALEU B  38      30.526   4.186 -18.667  0.48  0.00           H
ATOM   5655  HA BLEU B  38      30.524   4.193 -18.671  0.52  0.00           H
ATOM   5656  HB2ALEU B  38      30.424   4.616 -15.673  0.48  0.00           H
ATOM   5657  HB2BLEU B  38      30.426   4.532 -15.667  0.52  0.00           H
ATOM   5658  HB3ALEU B  38      31.854   4.725 -16.710  0.48  0.00           H
ATOM   5659  HB3BLEU B  38      31.138   3.168 -16.529  0.52  0.00           H
ATOM   5660  HG ALEU B  38      30.221   2.211 -16.253  0.48  0.00           H
ATOM   5661  HG BLEU B  38      32.119   6.026 -16.449  0.52  0.00           H
ATOM   5662 HD11ALEU B  38      31.702   1.043 -17.577  0.48  0.00           H
ATOM   5663 HD11BLEU B  38      33.965   5.236 -15.214  0.52  0.00           H
ATOM   5664 HD12ALEU B  38      31.688   2.611 -18.419  0.48  0.00           H
ATOM   5665 HD12BLEU B  38      32.552   4.427 -14.495  0.52  0.00           H
ATOM   5666 HD13ALEU B  38      33.025   2.204 -17.317  0.48  0.00           H
ATOM   5667 HD13BLEU B  38      33.615   3.536 -15.610  0.52  0.00           H
ATOM   5668 HD21ALEU B  38      31.555   1.618 -14.512  0.48  0.00           H
ATOM   5669 HD21BLEU B  38      33.576   5.712 -18.157  0.52  0.00           H
ATOM   5670 HD22ALEU B  38      31.739   3.381 -14.351  0.48  0.00           H
ATOM   5671 HD22BLEU B  38      33.848   4.000 -17.753  0.52  0.00           H
ATOM   5672 HD23ALEU B  38      32.988   2.428 -15.189  0.48  0.00           H
ATOM   5673 HD23BLEU B  38      32.404   4.478 -18.678  0.52  0.00           H
ATOM   5674  N   LYS B  39      27.744   4.180 -16.907  1.00 19.08           N
ANISOU 5674  N   LYS B  39     2563   2385   2303   -410   -197   -348       N
ATOM   5675  CA  LYS B  39      26.506   3.416 -16.654  1.00 21.42           C
ANISOU 5675  CA  LYS B  39     2950   2679   2510   -447    -79   -351       C
ATOM   5676  C   LYS B  39      25.665   3.169 -17.920  1.00 17.91           C
ANISOU 5676  C   LYS B  39     2333   2250   2221   -320     21   -316       C
ATOM   5677  O   LYS B  39      25.197   2.042 -18.177  1.00 16.55           O
ANISOU 5677  O   LYS B  39     2177   2097   2014   -293      7   -260       O
ATOM   5678  CB  LYS B  39      25.677   4.128 -15.588  1.00 27.91           C
ANISOU 5678  CB  LYS B  39     3917   3460   3228   -607    121   -488       C
ATOM   5679  CG  LYS B  39      24.617   3.287 -14.865  1.00 35.13           C
ANISOU 5679  CG  LYS B  39     5003   4367   3978   -746    253   -535       C
ATOM   5680  CD  LYS B  39      23.970   4.122 -13.730  1.00 43.75           C
ANISOU 5680  CD  LYS B  39     6242   5409   4971   -967    511   -741       C
ATOM   5681  CE  LYS B  39      22.951   3.334 -12.910  1.00 50.91           C
ANISOU 5681  CE  LYS B  39     7355   6310   5680  -1183    699   -834       C
ATOM   5682  NZ  LYS B  39      21.822   2.771 -13.727  1.00 52.69           N
ANISOU 5682  NZ  LYS B  39     7383   6533   6104  -1049    831   -839       N
ATOM   5683  H  ALYS B  39      27.855   5.092 -16.486  0.48  0.00           H
ATOM   5684  H  BLYS B  39      27.842   5.104 -16.510  0.52  0.00           H
ATOM   5685  HA  LYS B  39      26.794   2.444 -16.254  1.00  0.00           H
ATOM   5686  HB2 LYS B  39      26.366   4.510 -14.835  1.00  0.00           H
ATOM   5687  HB3 LYS B  39      25.178   4.977 -16.055  1.00  0.00           H
ATOM   5688  HG2 LYS B  39      25.087   2.400 -14.439  1.00  0.00           H
ATOM   5689  HG3 LYS B  39      23.848   2.984 -15.576  1.00  0.00           H
ATOM   5690  HD2 LYS B  39      24.759   4.468 -13.062  1.00  0.00           H
ATOM   5691  HD3 LYS B  39      23.475   4.988 -14.169  1.00  0.00           H
ATOM   5692  HE2 LYS B  39      22.531   3.998 -12.154  1.00  0.00           H
ATOM   5693  HE3 LYS B  39      23.464   2.513 -12.409  1.00  0.00           H
ATOM   5694  HZ1 LYS B  39      21.047   2.546 -13.120  1.00  0.00           H
ATOM   5695  HZ2 LYS B  39      22.133   1.935 -14.200  1.00  0.00           H
ATOM   5696  HZ3 LYS B  39      21.527   3.454 -14.410  1.00  0.00           H
ATOM   5697  N  ASER B  40      25.473   4.215 -18.718  0.71 16.83           N
ANISOU 5697  N  ASER B  40     2053   2089   2253   -264     89   -333       N
ATOM   5698  N  BSER B  40      25.478   4.193 -18.736  0.29 16.77           N
ANISOU 5698  N  BSER B  40     2044   2082   2245   -263     87   -331       N
ATOM   5699  CA ASER B  40      24.733   4.078 -19.980  0.71 15.25           C
ANISOU 5699  CA ASER B  40     1725   1880   2191   -187    115   -268       C
ATOM   5700  CA BSER B  40      24.716   4.007 -19.966  0.29 15.30           C
ANISOU 5700  CA BSER B  40     1735   1888   2191   -187    115   -267       C
ATOM   5701  C  ASER B  40      25.486   3.178 -20.956  0.71 13.90           C
ANISOU 5701  C  ASER B  40     1512   1776   1993   -144     11   -182       C
ATOM   5702  C  BSER B  40      25.487   3.151 -20.958  0.29 14.03           C
ANISOU 5702  C  BSER B  40     1528   1793   2008   -144     10   -181       C
ATOM   5703  O  ASER B  40      24.901   2.306 -21.629  0.71 13.06           O
ANISOU 5703  O  ASER B  40     1385   1687   1889   -117     18   -127       O
ATOM   5704  O  BSER B  40      24.916   2.290 -21.641  0.29 13.12           O
ANISOU 5704  O  BSER B  40     1393   1697   1896   -117     17   -127       O
ATOM   5705  CB ASER B  40      24.415   5.443 -20.593  0.71 14.71           C
ANISOU 5705  CB ASER B  40     1550   1726   2312   -176    137   -276       C
ATOM   5706  CB BSER B  40      24.362   5.348 -20.571  0.29 14.82           C
ANISOU 5706  CB BSER B  40     1568   1744   2320   -175    141   -276       C
ATOM   5707  OG ASER B  40      25.572   6.235 -20.819  0.71 14.46           O
ANISOU 5707  OG ASER B  40     1510   1709   2275   -196     67   -269       O
ATOM   5708  OG BSER B  40      23.523   6.045 -19.678  0.29 15.51           O
ANISOU 5708  OG BSER B  40     1650   1738   2505   -209    276   -403       O
ATOM   5709  H  ASER B  40      25.841   5.117 -18.453  0.71  0.00           H
ATOM   5710  H  BSER B  40      25.861   5.099 -18.509  0.29  0.00           H
ATOM   5711  HA ASER B  40      23.784   3.592 -19.752  0.71  0.00           H
ATOM   5712  HA BSER B  40      23.789   3.490 -19.718  0.29  0.00           H
ATOM   5713  HB2ASER B  40      23.910   5.286 -21.546  0.71  0.00           H
ATOM   5714  HB2BSER B  40      23.843   5.197 -21.518  0.29  0.00           H
ATOM   5715  HB3ASER B  40      23.744   5.982 -19.924  0.71  0.00           H
ATOM   5716  HB3BSER B  40      25.272   5.923 -20.741  0.29  0.00           H
ATOM   5717  HG ASER B  40      26.007   6.413 -19.982  0.71  0.00           H
ATOM   5718  HG BSER B  40      22.628   6.059 -20.024  0.29  0.00           H
ATOM   5719  N   THR B  41      26.785   3.392 -21.044  1.00 15.48           N
ANISOU 5719  N   THR B  41     1685   2003   2194   -152    -68   -197       N
ATOM   5720  CA  THR B  41      27.639   2.602 -21.918  1.00 16.23           C
ANISOU 5720  CA  THR B  41     1702   2141   2325   -135   -116   -187       C
ATOM   5721  C   THR B  41      27.518   1.106 -21.540  1.00 16.50           C
ANISOU 5721  C   THR B  41     1772   2176   2320    -94   -177   -166       C
ATOM   5722  O   THR B  41      27.274   0.271 -22.399  1.00 15.77           O
ANISOU 5722  O   THR B  41     1637   2104   2251    -76   -144   -147       O
ATOM   5723  CB  THR B  41      29.088   3.055 -21.804  1.00 15.52           C
ANISOU 5723  CB  THR B  41     1540   2052   2303   -157   -179   -253       C
ATOM   5724  OG1 THR B  41      29.240   4.381 -22.386  1.00 15.04           O
ANISOU 5724  OG1 THR B  41     1455   1989   2271   -218   -117   -264       O
ATOM   5725  CG2 THR B  41      30.002   2.082 -22.501  1.00 14.15           C
ANISOU 5725  CG2 THR B  41     1244   1892   2242   -144   -198   -309       C
ATOM   5726  H  ATHR B  41      27.199   4.126 -20.488  0.71  0.00           H
ATOM   5727  H  BTHR B  41      27.190   4.136 -20.494  0.29  0.00           H
ATOM   5728  HA  THR B  41      27.308   2.734 -22.948  1.00  0.00           H
ATOM   5729  HB  THR B  41      29.361   3.100 -20.750  1.00  0.00           H
ATOM   5730  HG1 THR B  41      28.847   5.034 -21.802  1.00  0.00           H
ATOM   5731 HG21 THR B  41      31.034   2.422 -22.409  1.00  0.00           H
ATOM   5732 HG22 THR B  41      29.732   2.022 -23.555  1.00  0.00           H
ATOM   5733 HG23 THR B  41      29.902   1.098 -22.043  1.00  0.00           H
ATOM   5734  N   GLN B  42      27.589   0.804 -20.257  1.00 16.97           N
ANISOU 5734  N   GLN B  42     1946   2203   2299   -112   -271   -163       N
ATOM   5735  CA  GLN B  42      27.578  -0.577 -19.788  1.00 18.68           C
ANISOU 5735  CA  GLN B  42     2234   2387   2475   -102   -390   -121       C
ATOM   5736  C   GLN B  42      26.163  -1.169 -19.926  1.00 18.23           C
ANISOU 5736  C   GLN B  42     2251   2350   2323   -109   -269    -82       C
ATOM   5737  O   GLN B  42      26.026  -2.335 -20.121  1.00 18.49           O
ANISOU 5737  O   GLN B  42     2296   2371   2359    -83   -321    -44       O
ATOM   5738  CB  GLN B  42      28.019  -0.651 -18.326  1.00 23.76           C
ANISOU 5738  CB  GLN B  42     3052   2968   3006   -189   -569   -100       C
ATOM   5739  CG  GLN B  42      28.352  -2.060 -17.874  1.00 30.32           C
ANISOU 5739  CG  GLN B  42     3958   3717   3846   -194   -799    -27       C
ATOM   5740  CD  GLN B  42      29.522  -2.630 -18.662  1.00 34.05           C
ANISOU 5740  CD  GLN B  42     4190   4132   4616    -76   -931    -62       C
ATOM   5741  OE1 GLN B  42      30.599  -2.042 -18.702  1.00 35.41           O
ANISOU 5741  OE1 GLN B  42     4229   4276   4950    -58  -1012   -121       O
ATOM   5742  NE2 GLN B  42      29.306  -3.765 -19.303  1.00 34.15           N
ANISOU 5742  NE2 GLN B  42     4128   4118   4729     -8   -925    -56       N
ATOM   5743  H   GLN B  42      27.653   1.551 -19.580  1.00  0.00           H
ATOM   5744  HA  GLN B  42      28.268  -1.163 -20.396  1.00  0.00           H
ATOM   5745  HB2 GLN B  42      27.212  -0.268 -17.701  1.00  0.00           H
ATOM   5746  HB3 GLN B  42      28.898  -0.021 -18.191  1.00  0.00           H
ATOM   5747  HG2 GLN B  42      27.480  -2.696 -18.023  1.00  0.00           H
ATOM   5748  HG3 GLN B  42      28.607  -2.045 -16.814  1.00  0.00           H
ATOM   5749 HE21 GLN B  42      30.045  -4.186 -19.848  1.00  0.00           H
ATOM   5750 HE22 GLN B  42      28.402  -4.212 -19.248  1.00  0.00           H
ATOM   5751  N   ALA B  43      25.126  -0.361 -19.809  1.00 18.39           N
ANISOU 5751  N   ALA B  43     2299   2382   2306   -146   -114   -108       N
ATOM   5752  CA  ALA B  43      23.774  -0.867 -19.958  1.00 17.85           C
ANISOU 5752  CA  ALA B  43     2253   2315   2214   -155      3    -96       C
ATOM   5753  C   ALA B  43      23.563  -1.338 -21.403  1.00 16.90           C
ANISOU 5753  C   ALA B  43     2008   2222   2191    -84      7    -40       C
ATOM   5754  O   ALA B  43      22.994  -2.410 -21.648  1.00 15.97           O
ANISOU 5754  O   ALA B  43     1914   2112   2041    -76     13     -3       O
ATOM   5755  CB  ALA B  43      22.751   0.200 -19.566  1.00 16.58           C
ANISOU 5755  CB  ALA B  43     2077   2117   2105   -203    170   -180       C
ATOM   5756  H   ALA B  43      25.275   0.619 -19.614  1.00  0.00           H
ATOM   5757  HA  ALA B  43      23.651  -1.723 -19.295  1.00  0.00           H
ATOM   5758  HB1 ALA B  43      21.744  -0.200 -19.685  1.00  0.00           H
ATOM   5759  HB2 ALA B  43      22.873   1.073 -20.207  1.00  0.00           H
ATOM   5760  HB3 ALA B  43      22.907   0.488 -18.526  1.00  0.00           H
ATOM   5761  N   ALA B  44      24.040  -0.550 -22.365  1.00 15.78           N
ANISOU 5761  N   ALA B  44     1765   2090   2139    -71      2    -35       N
ATOM   5762  CA  ALA B  44      23.919  -0.950 -23.758  1.00 15.04           C
ANISOU 5762  CA  ALA B  44     1614   2021   2078    -80      9     12       C
ATOM   5763  C   ALA B  44      24.776  -2.186 -24.052  1.00 15.84           C
ANISOU 5763  C   ALA B  44     1699   2149   2172    -63    -22    -18       C
ATOM   5764  O   ALA B  44      24.301  -3.145 -24.690  1.00 15.95           O
ANISOU 5764  O   ALA B  44     1719   2174   2168    -70      3      7       O
ATOM   5765  CB  ALA B  44      24.298   0.167 -24.698  1.00 12.82           C
ANISOU 5765  CB  ALA B  44     1290   1735   1846   -141      6     25       C
ATOM   5766  H   ALA B  44      24.485   0.325 -22.127  1.00  0.00           H
ATOM   5767  HA  ALA B  44      22.877  -1.210 -23.945  1.00  0.00           H
ATOM   5768  HB1 ALA B  44      24.194  -0.173 -25.728  1.00  0.00           H
ATOM   5769  HB2 ALA B  44      25.332   0.460 -24.515  1.00  0.00           H
ATOM   5770  HB3 ALA B  44      23.643   1.022 -24.530  1.00  0.00           H
ATOM   5771  N   ILE B  45      26.008  -2.165 -23.582  1.00 14.85           N
ANISOU 5771  N   ILE B  45     1532   2009   2101    -42    -87    -81       N
ATOM   5772  CA  ILE B  45      26.914  -3.278 -23.820  1.00 15.00           C
ANISOU 5772  CA  ILE B  45     1472   1999   2229    -12   -135   -144       C
ATOM   5773  C   ILE B  45      26.343  -4.543 -23.199  1.00 15.71           C
ANISOU 5773  C   ILE B  45     1645   2045   2279     31   -218    -89       C
ATOM   5774  O   ILE B  45      26.412  -5.605 -23.811  1.00 16.80           O
ANISOU 5774  O   ILE B  45     1732   2161   2490     47   -204   -118       O
ATOM   5775  CB  ILE B  45      28.305  -2.974 -23.266  1.00 16.37           C
ANISOU 5775  CB  ILE B  45     1552   2122   2545     11   -243   -223       C
ATOM   5776  CG1 ILE B  45      28.998  -1.973 -24.202  1.00 17.40           C
ANISOU 5776  CG1 ILE B  45     1579   2297   2733    -62   -116   -312       C
ATOM   5777  CG2 ILE B  45      29.137  -4.255 -23.133  1.00 18.24           C
ANISOU 5777  CG2 ILE B  45     1680   2258   2990     72   -370   -286       C
ATOM   5778  CD1 ILE B  45      30.332  -1.389 -23.613  1.00 22.21           C
ANISOU 5778  CD1 ILE B  45     2079   2861   3498    -50   -211   -398       C
ATOM   5779  H   ILE B  45      26.326  -1.367 -23.051  1.00  0.00           H
ATOM   5780  HA  ILE B  45      26.998  -3.430 -24.896  1.00  0.00           H
ATOM   5781  HB  ILE B  45      28.200  -2.519 -22.281  1.00  0.00           H
ATOM   5782 HG12 ILE B  45      28.313  -1.146 -24.392  1.00  0.00           H
ATOM   5783 HG13 ILE B  45      29.219  -2.470 -25.147  1.00  0.00           H
ATOM   5784 HG21 ILE B  45      28.629  -4.951 -22.466  1.00  0.00           H
ATOM   5785 HG22 ILE B  45      30.117  -4.010 -22.724  1.00  0.00           H
ATOM   5786 HG23 ILE B  45      29.257  -4.714 -24.114  1.00  0.00           H
ATOM   5787 HD11 ILE B  45      31.111  -2.150 -23.652  1.00  0.00           H
ATOM   5788 HD12 ILE B  45      30.640  -0.524 -24.200  1.00  0.00           H
ATOM   5789 HD13 ILE B  45      30.171  -1.087 -22.578  1.00  0.00           H
ATOM   5790  N   ASP B  46      25.764  -4.435 -22.011  1.00 15.19           N
ANISOU 5790  N   ASP B  46     1724   1961   2087     16   -283    -24       N
ATOM   5791  CA  ASP B  46      25.285  -5.619 -21.311  1.00 16.94           C
ANISOU 5791  CA  ASP B  46     2075   2131   2232      5   -376     36       C
ATOM   5792  C   ASP B  46      24.066  -6.193 -22.044  1.00 15.93           C
ANISOU 5792  C   ASP B  46     1956   2048   2048      0   -238     64       C
ATOM   5793  O   ASP B  46      23.888  -7.410 -22.125  1.00 14.38           O
ANISOU 5793  O   ASP B  46     1792   1812   1858     12   -288     91       O
ATOM   5794  CB  ASP B  46      24.886  -5.323 -19.866  1.00 18.27           C
ANISOU 5794  CB  ASP B  46     2451   2275   2216    -94   -430     76       C
ATOM   5795  CG  ASP B  46      26.079  -5.143 -18.950  1.00 20.68           C
ANISOU 5795  CG  ASP B  46     2813   2501   2545   -125   -659     87       C
ATOM   5796  OD1 ASP B  46      27.221  -5.473 -19.323  1.00 22.04           O
ANISOU 5796  OD1 ASP B  46     2832   2607   2935    -43   -812     64       O
ATOM   5797  OD2 ASP B  46      25.871  -4.675 -17.830  1.00 21.85           O
ANISOU 5797  OD2 ASP B  46     3157   2637   2508   -255   -686    102       O
ATOM   5798  H   ASP B  46      25.654  -3.524 -21.588  1.00  0.00           H
ATOM   5799  HA  ASP B  46      26.077  -6.368 -21.309  1.00  0.00           H
ATOM   5800  HB2 ASP B  46      24.285  -6.153 -19.495  1.00  0.00           H
ATOM   5801  HB3 ASP B  46      24.285  -4.414 -19.845  1.00  0.00           H
ATOM   5802  N   GLN B  47      23.195  -5.325 -22.555  1.00 15.30           N
ANISOU 5802  N   GLN B  47     1845   2026   1941    -22    -94     65       N
ATOM   5803  CA  GLN B  47      22.041  -5.818 -23.312  1.00 15.40           C
ANISOU 5803  CA  GLN B  47     1848   2063   1939    -36     -8    102       C
ATOM   5804  C   GLN B  47      22.472  -6.495 -24.623  1.00 14.97           C
ANISOU 5804  C   GLN B  47     1721   2026   1942    -33      0     91       C
ATOM   5805  O   GLN B  47      21.912  -7.533 -25.015  1.00 15.90           O
ANISOU 5805  O   GLN B  47     1865   2141   2036    -42     17    113       O
ATOM   5806  CB  GLN B  47      21.061  -4.661 -23.606  1.00 14.89           C
ANISOU 5806  CB  GLN B  47     1734   2005   1919    -62     75    112       C
ATOM   5807  CG  GLN B  47      20.327  -4.206 -22.361  1.00 20.20           C
ANISOU 5807  CG  GLN B  47     2461   2646   2568    -96    150     64       C
ATOM   5808  CD  GLN B  47      19.460  -2.985 -22.664  1.00 26.67           C
ANISOU 5808  CD  GLN B  47     3162   3418   3552    -99    216     38       C
ATOM   5809  OE1 GLN B  47      18.438  -3.085 -23.352  1.00 29.29           O
ANISOU 5809  OE1 GLN B  47     3411   3716   4000    -99    223     71       O
ATOM   5810  NE2 GLN B  47      19.903  -1.827 -22.199  1.00 28.11           N
ANISOU 5810  NE2 GLN B  47     3324   3575   3781   -102    231    -17       N
ATOM   5811  H   GLN B  47      23.329  -4.333 -22.422  1.00  0.00           H
ATOM   5812  HA  GLN B  47      21.523  -6.557 -22.701  1.00  0.00           H
ATOM   5813  HB2 GLN B  47      21.623  -3.819 -24.010  1.00  0.00           H
ATOM   5814  HB3 GLN B  47      20.333  -4.991 -24.347  1.00  0.00           H
ATOM   5815  HG2 GLN B  47      19.692  -5.016 -22.003  1.00  0.00           H
ATOM   5816  HG3 GLN B  47      21.052  -3.950 -21.589  1.00  0.00           H
ATOM   5817 HE21 GLN B  47      19.388  -0.978 -22.384  1.00  0.00           H
ATOM   5818 HE22 GLN B  47      20.756  -1.793 -21.659  1.00  0.00           H
ATOM   5819  N  AILE B  48      23.451  -5.911 -25.298  0.81 14.06           N
ANISOU 5819  N  AILE B  48     1525   1925   1891    -51     16     34       N
ATOM   5820  N  BILE B  48      23.478  -5.932 -25.288  0.19 14.06           N
ANISOU 5820  N  BILE B  48     1525   1925   1893    -50     15     32       N
ATOM   5821  CA AILE B  48      23.933  -6.464 -26.551  0.81 13.31           C
ANISOU 5821  CA AILE B  48     1377   1846   1835   -113     89    -32       C
ATOM   5822  CA BILE B  48      23.957  -6.475 -26.559  0.19 13.41           C
ANISOU 5822  CA BILE B  48     1388   1858   1849   -113     89    -35       C
ATOM   5823  C  AILE B  48      24.650  -7.801 -26.313  0.81 14.32           C
ANISOU 5823  C  AILE B  48     1449   1907   2086    -50     51   -115       C
ATOM   5824  C  BILE B  48      24.698  -7.789 -26.354  0.19 14.32           C
ANISOU 5824  C  BILE B  48     1443   1906   2090    -53     55   -121       C
ATOM   5825  O  AILE B  48      24.419  -8.774 -27.031  0.81 14.32           O
ANISOU 5825  O  AILE B  48     1447   1898   2098    -84    114   -151       O
ATOM   5826  O  BILE B  48      24.604  -8.701 -27.175  0.19 14.42           O
ANISOU 5826  O  BILE B  48     1440   1912   2127    -96    132   -175       O
ATOM   5827  CB AILE B  48      24.805  -5.446 -27.323  0.81 13.94           C
ANISOU 5827  CB AILE B  48     1403   1954   1938   -206    157   -103       C
ATOM   5828  CB BILE B  48      24.885  -5.495 -27.298  0.19 13.96           C
ANISOU 5828  CB BILE B  48     1400   1955   1951   -201    157   -112       C
ATOM   5829  CG1AILE B  48      23.891  -4.394 -27.935  0.81 13.23           C
ANISOU 5829  CG1AILE B  48     1395   1891   1743   -304    151     10       C
ATOM   5830  CG1BILE B  48      24.132  -4.214 -27.641  0.19 13.25           C
ANISOU 5830  CG1BILE B  48     1377   1888   1768   -276    141     -5       C
ATOM   5831  CG2AILE B  48      25.619  -6.150 -28.364  0.81 15.11           C
ANISOU 5831  CG2AILE B  48     1489   2103   2149   -304    284   -251       C
ATOM   5832  CG2BILE B  48      25.434  -6.135 -28.559  0.19 15.00           C
ANISOU 5832  CG2BILE B  48     1498   2098   2102   -330    296   -236       C
ATOM   5833  CD1AILE B  48      24.599  -3.118 -28.421  0.81 14.17           C
ANISOU 5833  CD1AILE B  48     1513   2020   1853   -410    171    -13       C
ATOM   5834  CD1BILE B  48      22.785  -4.446 -28.266  0.19 12.43           C
ANISOU 5834  CD1BILE B  48     1351   1783   1590   -336    116    109       C
ATOM   5835  H  AILE B  48      23.869  -5.067 -24.935  0.81  0.00           H
ATOM   5836  H  BILE B  48      23.922  -5.109 -24.906  0.19  0.00           H
ATOM   5837  HA AILE B  48      23.059  -6.673 -27.168  0.81  0.00           H
ATOM   5838  HA BILE B  48      23.092  -6.668 -27.194  0.19  0.00           H
ATOM   5839  HB AILE B  48      25.480  -4.958 -26.620  0.81  0.00           H
ATOM   5840  HB BILE B  48      25.719  -5.244 -26.643  0.19  0.00           H
ATOM   5841 HG12AILE B  48      23.382  -4.844 -28.788  0.81  0.00           H
ATOM   5842 HG12BILE B  48      24.739  -3.636 -28.338  0.19  0.00           H
ATOM   5843 HG13AILE B  48      23.142  -4.113 -27.194  0.81  0.00           H
ATOM   5844 HG13BILE B  48      23.999  -3.632 -26.729  0.19  0.00           H
ATOM   5845 HG21AILE B  48      26.585  -6.429 -27.943  0.81  0.00           H
ATOM   5846 HG21BILE B  48      24.688  -6.076 -29.351  0.19  0.00           H
ATOM   5847 HG22AILE B  48      25.772  -5.487 -29.215  0.81  0.00           H
ATOM   5848 HG22BILE B  48      25.673  -7.180 -28.362  0.19  0.00           H
ATOM   5849 HG23AILE B  48      25.093  -7.047 -28.692  0.81  0.00           H
ATOM   5850 HG23BILE B  48      26.336  -5.609 -28.870  0.19  0.00           H
ATOM   5851 HD11AILE B  48      24.330  -2.926 -29.460  0.81  0.00           H
ATOM   5852 HD11BILE B  48      22.015  -3.973 -27.657  0.19  0.00           H
ATOM   5853 HD12AILE B  48      24.291  -2.274 -27.804  0.81  0.00           H
ATOM   5854 HD12BILE B  48      22.770  -4.016 -29.267  0.19  0.00           H
ATOM   5855 HD13AILE B  48      25.678  -3.249 -28.344  0.81  0.00           H
ATOM   5856 HD13BILE B  48      22.593  -5.517 -28.328  0.19  0.00           H
ATOM   5857  N   ASN B  49      25.410  -7.905 -25.246  1.00 14.89           N
ANISOU 5857  N   ASN B  49     1489   1905   2261     34    -86   -131       N
ATOM   5858  CA  ASN B  49      26.088  -9.149 -24.941  1.00 15.99           C
ANISOU 5858  CA  ASN B  49     1562   1923   2591    101   -203   -187       C
ATOM   5859  C   ASN B  49      25.056 -10.194 -24.548  1.00 15.83           C
ANISOU 5859  C   ASN B  49     1682   1875   2458    109   -263    -81       C
ATOM   5860  O   ASN B  49      25.231 -11.374 -24.840  1.00 15.11           O
ANISOU 5860  O   ASN B  49     1545   1696   2501    136   -294   -127       O
ATOM   5861  CB  ASN B  49      27.109  -8.977 -23.836  1.00 19.06           C
ANISOU 5861  CB  ASN B  49     1910   2204   3128    163   -423   -189       C
ATOM   5862  CG  ASN B  49      28.406  -8.395 -24.358  1.00 25.04           C
ANISOU 5862  CG  ASN B  49     2452   2940   4122    167   -368   -354       C
ATOM   5863  OD1 ASN B  49      28.731  -8.544 -25.556  1.00 25.75           O
ANISOU 5863  OD1 ASN B  49     2409   3056   4319    113   -160   -510       O
ATOM   5864  ND2 ASN B  49      29.164  -7.743 -23.470  1.00 28.11           N
ANISOU 5864  ND2 ASN B  49     2817   3278   4585    194   -539   -337       N
ATOM   5865  H  AASN B  49      25.523  -7.110 -24.633  0.81  0.00           H
ATOM   5866  H  BASN B  49      25.482  -7.124 -24.610  0.19  0.00           H
ATOM   5867  HA  ASN B  49      26.603  -9.492 -25.838  1.00  0.00           H
ATOM   5868  HB2 ASN B  49      26.701  -8.307 -23.079  1.00  0.00           H
ATOM   5869  HB3 ASN B  49      27.311  -9.947 -23.382  1.00  0.00           H
ATOM   5870 HD21 ASN B  49      28.857  -7.656 -22.512  1.00  0.00           H
ATOM   5871 HD22 ASN B  49      30.043  -7.338 -23.758  1.00  0.00           H
ATOM   5872  N   GLY B  50      23.988  -9.750 -23.886  1.00 16.60           N
ANISOU 5872  N   GLY B  50     1937   2034   2336     72   -258     36       N
ATOM   5873  CA  GLY B  50      22.905 -10.635 -23.494  1.00 17.45           C
ANISOU 5873  CA  GLY B  50     2186   2129   2316     42   -272    121       C
ATOM   5874  C   GLY B  50      22.272 -11.241 -24.741  1.00 16.29           C
ANISOU 5874  C   GLY B  50     1990   2026   2172     22   -136     97       C
ATOM   5875  O   GLY B  50      22.055 -12.463 -24.824  1.00 17.16           O
ANISOU 5875  O   GLY B  50     2135   2076   2309     27   -171    105       O
ATOM   5876  H   GLY B  50      23.930  -8.770 -23.650  1.00  0.00           H
ATOM   5877  HA2 GLY B  50      23.297 -11.431 -22.861  1.00  0.00           H
ATOM   5878  HA3 GLY B  50      22.154 -10.069 -22.943  1.00  0.00           H
ATOM   5879  N  ALYS B  51      21.950 -10.418 -25.726  0.75 15.36           N
ANISOU 5879  N  ALYS B  51     1819   1999   2020    -27     -5     80       N
ATOM   5880  N  BLYS B  51      21.991 -10.393 -25.725  0.25 15.36           N
ANISOU 5880  N  BLYS B  51     1815   1998   2022    -26     -6     77       N
ATOM   5881  CA ALYS B  51      21.271 -10.983 -26.905  0.75 14.41           C
ANISOU 5881  CA ALYS B  51     1704   1914   1857    -99     90     80       C
ATOM   5882  CA BLYS B  51      21.337 -10.850 -26.951  0.25 15.03           C
ANISOU 5882  CA BLYS B  51     1776   1998   1938   -102     94     76       C
ATOM   5883  C  ALYS B  51      22.210 -11.810 -27.768  0.75 14.70           C
ANISOU 5883  C  ALYS B  51     1663   1909   2015   -123    153    -56       C
ATOM   5884  C  BLYS B  51      22.226 -11.844 -27.643  0.25 14.48           C
ANISOU 5884  C  BLYS B  51     1636   1874   1993   -111    139    -52       C
ATOM   5885  O  ALYS B  51      21.797 -12.785 -28.406  0.75 13.71           O
ANISOU 5885  O  ALYS B  51     1565   1771   1874   -172    208    -79       O
ATOM   5886  O  BLYS B  51      21.792 -12.922 -28.042  0.25 13.77           O
ANISOU 5886  O  BLYS B  51     1578   1758   1898   -136    168    -62       O
ATOM   5887  CB ALYS B  51      20.515  -9.914 -27.733  0.75 16.95           C
ANISOU 5887  CB ALYS B  51     2035   2308   2099   -192    142    139       C
ATOM   5888  CB BLYS B  51      21.059  -9.697 -27.920  0.25 17.73           C
ANISOU 5888  CB BLYS B  51     2107   2409   2221   -201    157     98       C
ATOM   5889  CG ALYS B  51      21.370  -8.941 -28.370  0.75 18.57           C
ANISOU 5889  CG ALYS B  51     2197   2538   2320   -254    178     86       C
ATOM   5890  CG BLYS B  51      20.653  -8.421 -27.257  0.25 17.97           C
ANISOU 5890  CG BLYS B  51     2134   2450   2245   -172    113    164       C
ATOM   5891  CD ALYS B  51      20.664  -8.137 -29.443  0.75 18.50           C
ANISOU 5891  CD ALYS B  51     2243   2559   2226   -400    169    170       C
ATOM   5892  CD BLYS B  51      19.542  -7.701 -28.007  0.25 17.47           C
ANISOU 5892  CD BLYS B  51     2082   2395   2163   -256     92    257       C
ATOM   5893  CE ALYS B  51      19.490  -7.355 -28.915  0.75 17.76           C
ANISOU 5893  CE ALYS B  51     2139   2437   2172   -352     75    288       C
ATOM   5894  CE BLYS B  51      19.868  -7.505 -29.463  0.25 17.78           C
ANISOU 5894  CE BLYS B  51     2166   2456   2135   -415    100    264       C
ATOM   5895  NZ ALYS B  51      18.666  -7.012 -30.013  0.75 17.26           N
ANISOU 5895  NZ ALYS B  51     2127   2353   2078   -493     -8    393       N
ATOM   5896  NZ BLYS B  51      18.734  -6.872 -30.147  0.25 17.47           N
ANISOU 5896  NZ BLYS B  51     2161   2380   2099   -514    -15    398       N
ATOM   5897  H  ALYS B  51      22.163  -9.432 -25.671  0.75  0.00           H
ATOM   5898  H  BLYS B  51      22.233  -9.418 -25.625  0.25  0.00           H
ATOM   5899  HA ALYS B  51      20.515 -11.671 -26.526  0.75  0.00           H
ATOM   5900  HA BLYS B  51      20.395 -11.334 -26.693  0.25  0.00           H
ATOM   5901  HB2ALYS B  51      19.943 -10.424 -28.508  0.75  0.00           H
ATOM   5902  HB2BLYS B  51      20.257 -10.002 -28.593  0.25  0.00           H
ATOM   5903  HB3ALYS B  51      19.821  -9.390 -27.075  0.75  0.00           H
ATOM   5904  HB3BLYS B  51      21.957  -9.513 -28.509  0.25  0.00           H
ATOM   5905  HG2ALYS B  51      22.210  -9.464 -28.826  0.75  0.00           H
ATOM   5906  HG2BLYS B  51      20.305  -8.647 -26.249  0.25  0.00           H
ATOM   5907  HG3ALYS B  51      21.751  -8.257 -27.611  0.75  0.00           H
ATOM   5908  HG3BLYS B  51      21.520  -7.764 -27.193  0.25  0.00           H
ATOM   5909  HD2ALYS B  51      21.378  -7.439 -29.880  0.75  0.00           H
ATOM   5910  HD2BLYS B  51      19.386  -6.724 -27.549  0.25  0.00           H
ATOM   5911  HD3ALYS B  51      20.314  -8.817 -30.220  0.75  0.00           H
ATOM   5912  HD3BLYS B  51      18.624  -8.282 -27.924  0.25  0.00           H
ATOM   5913  HE2ALYS B  51      18.928  -7.964 -28.207  0.75  0.00           H
ATOM   5914  HE2BLYS B  51      20.072  -8.473 -29.921  0.25  0.00           H
ATOM   5915  HE3ALYS B  51      19.843  -6.449 -28.423  0.75  0.00           H
ATOM   5916  HE3BLYS B  51      20.748  -6.868 -29.555  0.25  0.00           H
ATOM   5917  HZ1ALYS B  51      17.848  -6.522 -29.680  0.75  0.00           H
ATOM   5918  HZ1BLYS B  51      18.016  -6.649 -29.473  0.25  0.00           H
ATOM   5919  HZ2ALYS B  51      19.180  -6.417 -30.647  0.75  0.00           H
ATOM   5920  HZ2BLYS B  51      18.361  -7.507 -30.839  0.25  0.00           H
ATOM   5921  HZ3ALYS B  51      18.382  -7.852 -30.496  0.75  0.00           H
ATOM   5922  HZ3BLYS B  51      19.044  -6.025 -30.601  0.25  0.00           H
ATOM   5923  N   LEU B  52      23.484 -11.457 -27.778  1.00 14.51           N
ANISOU 5923  N   LEU B  52     1524   1849   2142    -99    162   -176       N
ATOM   5924  CA  LEU B  52      24.473 -12.222 -28.526  1.00 17.42           C
ANISOU 5924  CA  LEU B  52     1762   2145   2713   -129    265   -374       C
ATOM   5925  C   LEU B  52      24.621 -13.595 -27.913  1.00 17.36           C
ANISOU 5925  C   LEU B  52     1716   1989   2890    -17    136   -391       C
ATOM   5926  O   LEU B  52      24.660 -14.642 -28.609  1.00 18.22           O
ANISOU 5926  O   LEU B  52     1779   2036   3107    -53    232   -508       O
ATOM   5927  CB  LEU B  52      25.812 -11.448 -28.495  1.00 21.72           C
ANISOU 5927  CB  LEU B  52     2151   2663   3439   -121    295   -516       C
ATOM   5928  CG  LEU B  52      27.010 -12.065 -29.191  1.00 26.19           C
ANISOU 5928  CG  LEU B  52     2510   3129   4312   -161    445   -794       C
ATOM   5929  CD1 LEU B  52      26.701 -12.328 -30.651  1.00 26.45           C
ANISOU 5929  CD1 LEU B  52     2608   3235   4205   -385    723   -921       C
ATOM   5930  CD2 LEU B  52      28.221 -11.092 -29.035  1.00 33.57           C
ANISOU 5930  CD2 LEU B  52     3286   4049   5420   -160    467   -919       C
ATOM   5931  H  ALEU B  52      23.777 -10.642 -27.258  0.75  0.00           H
ATOM   5932  H  BLEU B  52      23.772 -10.592 -27.343  0.25  0.00           H
ATOM   5933  HA  LEU B  52      24.141 -12.324 -29.559  1.00  0.00           H
ATOM   5934  HB2 LEU B  52      26.082 -11.310 -27.448  1.00  0.00           H
ATOM   5935  HB3 LEU B  52      25.641 -10.463 -28.930  1.00  0.00           H
ATOM   5936  HG  LEU B  52      27.252 -13.010 -28.706  1.00  0.00           H
ATOM   5937 HD11 LEU B  52      27.572 -12.771 -31.133  1.00  0.00           H
ATOM   5938 HD12 LEU B  52      26.451 -11.389 -31.144  1.00  0.00           H
ATOM   5939 HD13 LEU B  52      25.857 -13.014 -30.726  1.00  0.00           H
ATOM   5940 HD21 LEU B  52      29.095 -11.517 -29.529  1.00  0.00           H
ATOM   5941 HD22 LEU B  52      27.977 -10.132 -29.491  1.00  0.00           H
ATOM   5942 HD23 LEU B  52      28.437 -10.947 -27.976  1.00  0.00           H
ATOM   5943  N   ASN B  53      24.690 -13.634 -26.597  1.00 16.62           N
ANISOU 5943  N   ASN B  53     1667   1820   2826     92    -95   -271       N
ATOM   5944  CA  ASN B  53      24.887 -14.922 -25.923  1.00 17.92           C
ANISOU 5944  CA  ASN B  53     1834   1803   3171    173   -297   -249       C
ATOM   5945  C   ASN B  53      23.649 -15.796 -26.070  1.00 16.71           C
ANISOU 5945  C   ASN B  53     1838   1679   2831    127   -260   -152       C
ATOM   5946  O   ASN B  53      23.763 -17.023 -26.107  1.00 18.79           O
ANISOU 5946  O   ASN B  53     2079   1799   3261    159   -336   -188       O
ATOM   5947  CB  ASN B  53      25.237 -14.735 -24.441  1.00 21.52           C
ANISOU 5947  CB  ASN B  53     2378   2158   3639    229   -597   -114       C
ATOM   5948  CG  ASN B  53      26.659 -14.178 -24.239  1.00 29.05           C
ANISOU 5948  CG  ASN B  53     3134   3017   4887    293   -706   -223       C
ATOM   5949  OD1 ASN B  53      26.953 -13.548 -23.218  1.00 31.93           O
ANISOU 5949  OD1 ASN B  53     3581   3359   5191    295   -900   -121       O
ATOM   5950  ND2 ASN B  53      27.531 -14.398 -25.210  1.00 32.50           N
ANISOU 5950  ND2 ASN B  53     3312   3393   5642    317   -561   -453       N
ATOM   5951  H   ASN B  53      24.608 -12.784 -26.057  1.00  0.00           H
ATOM   5952  HA  ASN B  53      25.721 -15.432 -26.406  1.00  0.00           H
ATOM   5953  HB2 ASN B  53      25.165 -15.700 -23.940  1.00  0.00           H
ATOM   5954  HB3 ASN B  53      24.520 -14.048 -23.991  1.00  0.00           H
ATOM   5955 HD21 ASN B  53      27.252 -14.914 -26.032  1.00  0.00           H
ATOM   5956 HD22 ASN B  53      28.476 -14.050 -25.129  1.00  0.00           H
ATOM   5957  N   ARG B  54      22.456 -15.201 -26.148  1.00 14.34           N
ANISOU 5957  N   ARG B  54     1677   1540   2232     53   -157    -38       N
ATOM   5958  CA  ARG B  54      21.250 -16.043 -26.419  1.00 15.36           C
ANISOU 5958  CA  ARG B  54     1924   1698   2217     -4   -104     31       C
ATOM   5959  C   ARG B  54      21.276 -16.651 -27.826  1.00 18.38           C
ANISOU 5959  C   ARG B  54     2232   2091   2662    -69     65    -98       C
ATOM   5960  O   ARG B  54      20.791 -17.763 -28.073  1.00 18.41           O
ANISOU 5960  O   ARG B  54     2283   2042   2669    -91     74   -100       O
ATOM   5961  CB  ARG B  54      19.949 -15.219 -26.248  1.00 14.27           C
ANISOU 5961  CB  ARG B  54     1889   1698   1836    -71    -33    148       C
ATOM   5962  CG  ARG B  54      19.651 -14.802 -24.787  1.00 14.96           C
ANISOU 5962  CG  ARG B  54     2096   1772   1817    -71   -132    241       C
ATOM   5963  CD  ARG B  54      18.186 -15.037 -24.468  1.00 16.02           C
ANISOU 5963  CD  ARG B  54     2341   1954   1793   -155    -56    309       C
ATOM   5964  NE  ARG B  54      17.904 -16.471 -24.561  1.00 18.41           N
ANISOU 5964  NE  ARG B  54     2721   2182   2092   -176   -101    333       N
ATOM   5965  CZ  ARG B  54      16.694 -16.987 -24.711  1.00 16.99           C
ANISOU 5965  CZ  ARG B  54     2599   2037   1821   -251    -17    366       C
ATOM   5966  NH1 ARG B  54      15.622 -16.207 -24.780  1.00 15.64           N
ANISOU 5966  NH1 ARG B  54     2387   1954   1599   -304    107    370       N
ATOM   5967  NH2 ARG B  54      16.563 -18.293 -24.828  1.00 16.43           N
ANISOU 5967  NH2 ARG B  54     2599   1887   1755   -270    -67    384       N
ATOM   5968  H   ARG B  54      22.370 -14.202 -26.026  1.00  0.00           H
ATOM   5969  HA  ARG B  54      21.234 -16.858 -25.696  1.00  0.00           H
ATOM   5970  HB2 ARG B  54      20.035 -14.315 -26.851  1.00  0.00           H
ATOM   5971  HB3 ARG B  54      19.111 -15.808 -26.620  1.00  0.00           H
ATOM   5972  HG2 ARG B  54      19.883 -13.745 -24.659  1.00  0.00           H
ATOM   5973  HG3 ARG B  54      20.268 -15.392 -24.109  1.00  0.00           H
ATOM   5974  HD2 ARG B  54      17.565 -14.495 -25.181  1.00  0.00           H
ATOM   5975  HD3 ARG B  54      17.972 -14.688 -23.458  1.00  0.00           H
ATOM   5976  HE  ARG B  54      18.685 -17.109 -24.507  1.00  0.00           H
ATOM   5977 HH11 ARG B  54      15.721 -15.205 -24.704  1.00  0.00           H
ATOM   5978 HH12 ARG B  54      14.707 -16.616 -24.908  1.00  0.00           H
ATOM   5979 HH21 ARG B  54      17.378 -18.888 -24.789  1.00  0.00           H
ATOM   5980 HH22 ARG B  54      15.647 -18.699 -24.956  1.00  0.00           H
ATOM   5981  N   VAL B  55      21.739 -15.862 -28.772  1.00 22.09           N
ANISOU 5981  N   VAL B  55     2621   2639   3132   -143    216   -203       N
ATOM   5982  CA  VAL B  55      21.787 -16.296 -30.173  1.00 26.08           C
ANISOU 5982  CA  VAL B  55     3110   3169   3629   -290    415   -347       C
ATOM   5983  C   VAL B  55      22.888 -17.320 -30.407  1.00 25.34           C
ANISOU 5983  C   VAL B  55     2858   2916   3856   -253    479   -578       C
ATOM   5984  O   VAL B  55      22.694 -18.227 -31.214  1.00 29.84           O
ANISOU 5984  O   VAL B  55     3441   3453   4445   -349    614   -692       O
ATOM   5985  CB  VAL B  55      21.993 -15.091 -31.090  1.00 28.62           C
ANISOU 5985  CB  VAL B  55     3448   3609   3818   -447    549   -388       C
ATOM   5986  CG1 VAL B  55      22.446 -15.502 -32.498  1.00 31.06           C
ANISOU 5986  CG1 VAL B  55     3760   3923   4120   -668    791   -602       C
ATOM   5987  CG2 VAL B  55      20.708 -14.276 -31.146  1.00 28.46           C
ANISOU 5987  CG2 VAL B  55     3567   3698   3550   -507    468   -171       C
ATOM   5988  H   VAL B  55      22.068 -14.939 -28.529  1.00  0.00           H
ATOM   5989  HA  VAL B  55      20.831 -16.757 -30.422  1.00  0.00           H
ATOM   5990  HB  VAL B  55      22.771 -14.464 -30.654  1.00  0.00           H
ATOM   5991 HG11 VAL B  55      23.366 -16.083 -32.429  1.00  0.00           H
ATOM   5992 HG12 VAL B  55      22.624 -14.609 -33.097  1.00  0.00           H
ATOM   5993 HG13 VAL B  55      21.669 -16.106 -32.968  1.00  0.00           H
ATOM   5994 HG21 VAL B  55      20.851 -13.415 -31.799  1.00  0.00           H
ATOM   5995 HG22 VAL B  55      20.452 -13.932 -30.144  1.00  0.00           H
ATOM   5996 HG23 VAL B  55      19.901 -14.897 -31.534  1.00  0.00           H
ATOM   5997  N   ILE B  56      24.037 -17.217 -29.749  1.00 44.85           N
ANISOU 5997  N   ILE B  56     7150   4471   5418   -142   -219  -2657       N
ATOM   5998  CA  ILE B  56      25.132 -18.115 -30.135  1.00 42.60           C
ANISOU 5998  CA  ILE B  56     6777   4293   5115   -223   -403  -2534       C
ATOM   5999  C   ILE B  56      25.242 -19.333 -29.215  1.00 47.75           C
ANISOU 5999  C   ILE B  56     7525   5187   5430   -274   -461  -2521       C
ATOM   6000  O   ILE B  56      26.137 -20.176 -29.384  1.00 48.28           O
ANISOU 6000  O   ILE B  56     7526   5358   5460   -327   -637  -2408       O
ATOM   6001  CB  ILE B  56      26.505 -17.423 -30.202  1.00 42.01           C
ANISOU 6001  CB  ILE B  56     6661   4117   5183   -349   -597  -2556       C
ATOM   6002  CG1 ILE B  56      26.943 -17.012 -28.817  1.00 45.63           C
ANISOU 6002  CG1 ILE B  56     7292   4614   5430   -469   -664  -2726       C
ATOM   6003  CG2 ILE B  56      26.480 -16.208 -31.169  1.00 42.17           C
ANISOU 6003  CG2 ILE B  56     6572   3899   5553   -319   -560  -2536       C
ATOM   6004  CD1 ILE B  56      28.261 -16.331 -28.799  1.00 50.88           C
ANISOU 6004  CD1 ILE B  56     7912   5190   6229   -600   -852  -2749       C
ATOM   6005  H   ILE B  56      24.154 -16.542 -29.007  1.00  0.00           H
ATOM   6006  HA  ILE B  56      24.908 -18.485 -31.135  1.00  0.00           H
ATOM   6007  HB  ILE B  56      27.228 -18.144 -30.584  1.00  0.00           H
ATOM   6008 HG12 ILE B  56      27.006 -17.905 -28.195  1.00  0.00           H
ATOM   6009 HG13 ILE B  56      26.194 -16.341 -28.396  1.00  0.00           H
ATOM   6010 HD11 ILE B  56      28.747 -16.504 -27.839  1.00  0.00           H
ATOM   6011 HD12 ILE B  56      28.119 -15.260 -28.946  1.00  0.00           H
ATOM   6012 HD13 ILE B  56      28.886 -16.728 -29.599  1.00  0.00           H
ATOM   6013 HG21 ILE B  56      25.752 -16.388 -31.960  1.00  0.00           H
ATOM   6014 HG22 ILE B  56      26.202 -15.310 -30.617  1.00  0.00           H
ATOM   6015 HG23 ILE B  56      27.468 -16.073 -31.608  1.00  0.00           H
ATOM   6016  N   GLU B  57      24.299 -19.420 -28.281  1.00 53.55           N
ANISOU 6016  N   GLU B  57     8411   6003   5934   -245   -319  -2611       N
ATOM   6017  CA  GLU B  57      24.139 -20.548 -27.378  1.00 58.72           C
ANISOU 6017  CA  GLU B  57     9151   6899   6260   -298   -329  -2582       C
ATOM   6018  C   GLU B  57      23.762 -21.848 -28.108  1.00 59.60           C
ANISOU 6018  C   GLU B  57     9139   7144   6363   -214   -320  -2396       C
ATOM   6019  O   GLU B  57      22.983 -21.830 -29.058  1.00 55.58           O
ANISOU 6019  O   GLU B  57     8545   6551   6021    -85   -191  -2328       O
ATOM   6020  CB  GLU B  57      23.046 -20.203 -26.362  1.00 63.25           C
ANISOU 6020  CB  GLU B  57     9883   7502   6648   -160   -225  -2691       C
ATOM   6021  CG  GLU B  57      22.734 -21.285 -25.359  1.00 66.83           C
ANISOU 6021  CG  GLU B  57    10313   8272   6806   -129   -265  -2695       C
ATOM   6022  CD  GLU B  57      21.640 -20.874 -24.378  1.00 71.97           C
ANISOU 6022  CD  GLU B  57    11093   8979   7275    -51    -90  -2839       C
ATOM   6023  OE1 GLU B  57      20.666 -20.218 -24.801  1.00 71.74           O
ANISOU 6023  OE1 GLU B  57    11049   8815   7394     55    113  -2881       O
ATOM   6024  OE2 GLU B  57      21.753 -21.198 -23.175  1.00 76.47           O
ANISOU 6024  OE2 GLU B  57    11750   9740   7563   -103   -147  -2906       O
ATOM   6025  H   GLU B  57      23.651 -18.651 -28.193  1.00  0.00           H
ATOM   6026  HA  GLU B  57      25.076 -20.705 -26.844  1.00  0.00           H
ATOM   6027  HB2 GLU B  57      22.132 -19.981 -26.913  1.00  0.00           H
ATOM   6028  HB3 GLU B  57      23.349 -19.307 -25.820  1.00  0.00           H
ATOM   6029  HG2 GLU B  57      22.406 -22.175 -25.896  1.00  0.00           H
ATOM   6030  HG3 GLU B  57      23.640 -21.522 -24.801  1.00  0.00           H
ATOM   6031  N   LYS B  58      24.334 -22.965 -27.659  1.00 67.01           N
ANISOU 6031  N   LYS B  58    10080   8271   7112   -273   -481  -2288       N
ATOM   6032  CA  LYS B  58      23.767 -24.304 -27.932  1.00 66.89           C
ANISOU 6032  CA  LYS B  58    10047   8387   6979   -202   -461  -2097       C
ATOM   6033  C   LYS B  58      23.456 -24.609 -29.376  1.00 60.46           C
ANISOU 6033  C   LYS B  58     9082   7478   6412    -88   -399  -1929       C
ATOM   6034  O   LYS B  58      22.293 -24.644 -29.743  1.00 58.45           O
ANISOU 6034  O   LYS B  58     8797   7217   6194      8   -201  -1895       O
ATOM   6035  CB  LYS B  58      22.417 -24.478 -27.202  1.00 72.58           C
ANISOU 6035  CB  LYS B  58    10830   9241   7506   -151   -248  -2148       C
ATOM   6036  CG  LYS B  58      22.466 -24.783 -25.697  1.00 78.76           C
ANISOU 6036  CG  LYS B  58    11706  10236   7984   -220   -307  -2206       C
ATOM   6037  CD  LYS B  58      21.048 -24.782 -25.088  1.00 81.94           C
ANISOU 6037  CD  LYS B  58    12166  10735   8235   -121    -86  -2249       C
ATOM   6038  CE  LYS B  58      20.401 -26.177 -25.100  1.00 81.77           C
ANISOU 6038  CE  LYS B  58    12132  10879   8060   -121    -38  -2023       C
ATOM   6039  NZ  LYS B  58      20.295 -26.792 -26.458  1.00 78.97           N
ANISOU 6039  NZ  LYS B  58    11687  10426   7891    -77    -25  -1847       N
ATOM   6040  H   LYS B  58      25.182 -22.895 -27.115  1.00  0.00           H
ATOM   6041  HA  LYS B  58      24.462 -25.057 -27.560  1.00  0.00           H
ATOM   6042  HB2 LYS B  58      21.886 -25.298 -27.685  1.00  0.00           H
ATOM   6043  HB3 LYS B  58      21.835 -23.567 -27.344  1.00  0.00           H
ATOM   6044  HG2 LYS B  58      22.918 -25.763 -25.546  1.00  0.00           H
ATOM   6045  HG3 LYS B  58      23.072 -24.027 -25.197  1.00  0.00           H
ATOM   6046  HD2 LYS B  58      20.421 -24.101 -25.664  1.00  0.00           H
ATOM   6047  HD3 LYS B  58      21.105 -24.427 -24.059  1.00  0.00           H
ATOM   6048  HE2 LYS B  58      21.000 -26.837 -24.472  1.00  0.00           H
ATOM   6049  HE3 LYS B  58      19.401 -26.101 -24.672  1.00  0.00           H
ATOM   6050  HZ1 LYS B  58      19.648 -27.567 -26.427  1.00  0.00           H
ATOM   6051  HZ2 LYS B  58      21.204 -27.123 -26.749  1.00  0.00           H
ATOM   6052  HZ3 LYS B  58      19.962 -26.101 -27.115  1.00  0.00           H
ATOM   6053  N   THR B  59      24.443 -24.878 -30.209  1.00 56.04           N
ANISOU 6053  N   THR B  59     8391   6867   6033   -105   -548  -1798       N
ATOM   6054  CA  THR B  59      24.087 -25.580 -31.447  1.00 54.06           C
ANISOU 6054  CA  THR B  59     7987   6610   5945    -15   -483  -1592       C
ATOM   6055  C   THR B  59      23.489 -26.947 -31.040  1.00 54.56           C
ANISOU 6055  C   THR B  59     8087   6841   5802      5   -472  -1456       C
ATOM   6056  O   THR B  59      23.797 -27.488 -29.971  1.00 56.70           O
ANISOU 6056  O   THR B  59     8465   7234   5842    -70   -585  -1467       O
ATOM   6057  CB  THR B  59      25.286 -25.794 -32.421  1.00 44.08           C
ANISOU 6057  CB  THR B  59     6567   5293   4887    -37   -634  -1474       C
ATOM   6058  OG1 THR B  59      26.271 -26.626 -31.786  1.00 45.36           O
ANISOU 6058  OG1 THR B  59     6748   5557   4930   -113   -843  -1425       O
ATOM   6059  CG2 THR B  59      25.900 -24.422 -32.888  1.00 52.23           C
ANISOU 6059  CG2 THR B  59     7546   6156   6142    -73   -650  -1580       C
ATOM   6060  H   THR B  59      25.396 -24.614 -30.005  1.00  0.00           H
ATOM   6061  HA  THR B  59      23.319 -25.005 -31.964  1.00  0.00           H
ATOM   6062  HB  THR B  59      24.917 -26.318 -33.303  1.00  0.00           H
ATOM   6063  HG1 THR B  59      27.011 -26.760 -32.383  1.00  0.00           H
ATOM   6064 HG21 THR B  59      26.733 -24.608 -33.566  1.00  0.00           H
ATOM   6065 HG22 THR B  59      25.136 -23.839 -33.403  1.00  0.00           H
ATOM   6066 HG23 THR B  59      26.255 -23.868 -32.019  1.00  0.00           H
ATOM   6067  N   ASN B  60      22.599 -27.448 -31.885  1.00 53.01           N
ANISOU 6067  N   ASN B  60     7803   6645   5692     98   -340  -1323       N
ATOM   6068  CA  ASN B  60      22.091 -28.799 -31.828  1.00 51.65           C
ANISOU 6068  CA  ASN B  60     7623   6597   5404    122   -343  -1156       C
ATOM   6069  C   ASN B  60      23.170 -29.853 -32.165  1.00 44.47           C
ANISOU 6069  C   ASN B  60     6632   5722   4543     92   -550  -1014       C
ATOM   6070  O   ASN B  60      24.062 -29.612 -32.962  1.00 43.11           O
ANISOU 6070  O   ASN B  60     6352   5469   4560     92   -628  -1004       O
ATOM   6071  CB  ASN B  60      20.915 -28.916 -32.822  1.00 53.51           C
ANISOU 6071  CB  ASN B  60     7768   6793   5771    225   -161  -1061       C
ATOM   6072  CG  ASN B  60      21.349 -28.782 -34.324  1.00 66.30           C
ANISOU 6072  CG  ASN B  60     9229   8306   7655    268   -181   -976       C
ATOM   6073  OD1 ASN B  60      20.596 -29.165 -35.219  1.00 61.22           O
ANISOU 6073  OD1 ASN B  60     8504   7652   7104    333    -90   -861       O
ATOM   6074  ND2 ASN B  60      22.551 -28.256 -34.587  1.00 69.53           N
ANISOU 6074  ND2 ASN B  60     9596   8649   8176    220   -300  -1028       N
ATOM   6075  H   ASN B  60      22.253 -26.845 -32.618  1.00  0.00           H
ATOM   6076  HA  ASN B  60      21.718 -28.990 -30.822  1.00  0.00           H
ATOM   6077  HB2 ASN B  60      20.443 -29.889 -32.685  1.00  0.00           H
ATOM   6078  HB3 ASN B  60      20.186 -28.138 -32.597  1.00  0.00           H
ATOM   6079 HD21 ASN B  60      22.862 -28.160 -35.543  1.00  0.00           H
ATOM   6080 HD22 ASN B  60      23.147 -27.955 -33.829  1.00  0.00           H
ATOM   6081  N   GLU B  61      23.095 -31.008 -31.531  1.00 38.22           N
ANISOU 6081  N   GLU B  61     5886   5047   3588     65   -637   -904       N
ATOM   6082  CA  GLU B  61      23.987 -32.107 -31.863  1.00 34.48           C
ANISOU 6082  CA  GLU B  61     5321   4588   3190     56   -824   -763       C
ATOM   6083  C   GLU B  61      23.180 -33.169 -32.598  1.00 27.60           C
ANISOU 6083  C   GLU B  61     4375   3733   2378    133   -755   -604       C
ATOM   6084  O   GLU B  61      22.231 -33.656 -32.051  1.00 27.32           O
ANISOU 6084  O   GLU B  61     4412   3776   2191    132   -685   -545       O
ATOM   6085  CB  GLU B  61      24.546 -32.705 -30.593  1.00 40.83           C
ANISOU 6085  CB  GLU B  61     6227   5498   3791    -42  -1012   -732       C
ATOM   6086  CG  GLU B  61      25.817 -33.445 -30.824  1.00 43.66           C
ANISOU 6086  CG  GLU B  61     6479   5832   4277    -63  -1242   -639       C
ATOM   6087  CD  GLU B  61      26.508 -33.822 -29.543  1.00 47.59           C
ANISOU 6087  CD  GLU B  61     7073   6418   4590   -176  -1460   -612       C
ATOM   6088  OE1 GLU B  61      25.812 -34.122 -28.535  1.00 49.05           O
ANISOU 6088  OE1 GLU B  61     7401   6721   4517   -230  -1442   -582       O
ATOM   6089  OE2 GLU B  61      27.762 -33.838 -29.568  1.00 48.87           O
ANISOU 6089  OE2 GLU B  61     7159   6539   4869   -215  -1653   -610       O
ATOM   6090  H   GLU B  61      22.406 -31.131 -30.803  1.00  0.00           H
ATOM   6091  HA  GLU B  61      24.799 -31.750 -32.497  1.00  0.00           H
ATOM   6092  HB2 GLU B  61      23.811 -33.394 -30.178  1.00  0.00           H
ATOM   6093  HB3 GLU B  61      24.727 -31.905 -29.875  1.00  0.00           H
ATOM   6094  HG2 GLU B  61      25.595 -34.355 -31.381  1.00  0.00           H
ATOM   6095  HG3 GLU B  61      26.486 -32.822 -31.417  1.00  0.00           H
ATOM   6096  N   LYS B  62      23.557 -33.516 -33.818  1.00 23.26           N
ANISOU 6096  N   LYS B  62     3682   3114   2041    190   -772   -541       N
ATOM   6097  CA  LYS B  62      22.893 -34.564 -34.570  1.00 22.81           C
ANISOU 6097  CA  LYS B  62     3554   3062   2050    256   -730   -406       C
ATOM   6098  C   LYS B  62      23.929 -35.603 -35.057  1.00 22.05           C
ANISOU 6098  C   LYS B  62     3346   2943   2089    268   -904   -326       C
ATOM   6099  O   LYS B  62      25.077 -35.277 -35.353  1.00 22.48           O
ANISOU 6099  O   LYS B  62     3324   2956   2260    254   -993   -381       O
ATOM   6100  CB  LYS B  62      22.207 -33.998 -35.793  1.00 23.05           C
ANISOU 6100  CB  LYS B  62     3509   3027   2221    324   -558   -418       C
ATOM   6101  CG  LYS B  62      21.160 -32.932 -35.504  1.00 24.99           C
ANISOU 6101  CG  LYS B  62     3828   3264   2404    334   -377   -497       C
ATOM   6102  CD  LYS B  62      20.048 -33.459 -34.598  1.00 26.37           C
ANISOU 6102  CD  LYS B  62     4098   3528   2395    329   -308   -444       C
ATOM   6103  CE  LYS B  62      18.955 -32.367 -34.449  1.00 25.81           C
ANISOU 6103  CE  LYS B  62     4067   3434   2304    360   -100   -535       C
ATOM   6104  NZ  LYS B  62      17.966 -32.720 -33.416  1.00 24.14           N
ANISOU 6104  NZ  LYS B  62     3948   3329   1894    344    -12   -512       N
ATOM   6105  H   LYS B  62      24.336 -33.033 -34.242  1.00  0.00           H
ATOM   6106  HA  LYS B  62      22.156 -35.056 -33.935  1.00  0.00           H
ATOM   6107  HB2 LYS B  62      21.718 -34.819 -36.318  1.00  0.00           H
ATOM   6108  HB3 LYS B  62      22.965 -33.570 -36.449  1.00  0.00           H
ATOM   6109  HG2 LYS B  62      21.643 -32.087 -35.014  1.00  0.00           H
ATOM   6110  HG3 LYS B  62      20.724 -32.597 -36.445  1.00  0.00           H
ATOM   6111  HD2 LYS B  62      20.459 -33.700 -33.618  1.00  0.00           H
ATOM   6112  HD3 LYS B  62      19.611 -34.354 -35.040  1.00  0.00           H
ATOM   6113  HE2 LYS B  62      19.432 -31.426 -34.174  1.00  0.00           H
ATOM   6114  HE3 LYS B  62      18.444 -32.242 -35.404  1.00  0.00           H
ATOM   6115  HZ1 LYS B  62      18.440 -32.890 -32.541  1.00  0.00           H
ATOM   6116  HZ2 LYS B  62      17.312 -31.959 -33.302  1.00  0.00           H
ATOM   6117  HZ3 LYS B  62      17.468 -33.553 -33.697  1.00  0.00           H
ATOM   6118  N   PHE B  63      23.499 -36.837 -35.175  1.00 20.82           N
ANISOU 6118  N   PHE B  63     3169   2805   1937    297   -945   -200       N
ATOM   6119  CA  PHE B  63      24.412 -37.909 -35.512  1.00 20.17           C
ANISOU 6119  CA  PHE B  63     2983   2687   1992    317  -1113   -133       C
ATOM   6120  C   PHE B  63      23.965 -38.561 -36.814  1.00 19.32           C
ANISOU 6120  C   PHE B  63     2773   2532   2035    398  -1037    -91       C
ATOM   6121  O   PHE B  63      24.122 -37.965 -37.866  1.00 17.99           O
ANISOU 6121  O   PHE B  63     2528   2331   1978    433   -937   -161       O
ATOM   6122  CB  PHE B  63      24.483 -38.842 -34.331  1.00 21.71           C
ANISOU 6122  CB  PHE B  63     3251   2933   2066    262  -1280    -23       C
ATOM   6123  CG  PHE B  63      24.986 -38.168 -33.098  1.00 23.46           C
ANISOU 6123  CG  PHE B  63     3579   3216   2118    168  -1365    -76       C
ATOM   6124  CD1 PHE B  63      26.262 -37.603 -33.080  1.00 24.58           C
ANISOU 6124  CD1 PHE B  63     3667   3324   2348    139  -1477   -162       C
ATOM   6125  CD2 PHE B  63      24.198 -38.088 -31.967  1.00 25.76           C
ANISOU 6125  CD2 PHE B  63     4023   3607   2158    101  -1331    -45       C
ATOM   6126  CE1 PHE B  63      26.740 -36.973 -31.956  1.00 28.87           C
ANISOU 6126  CE1 PHE B  63     4314   3921   2733     42  -1573   -220       C
ATOM   6127  CE2 PHE B  63      24.668 -37.475 -30.828  1.00 30.43           C
ANISOU 6127  CE2 PHE B  63     4727   4267   2569      4  -1413   -111       C
ATOM   6128  CZ  PHE B  63      25.943 -36.904 -30.815  1.00 32.19           C
ANISOU 6128  CZ  PHE B  63     4905   4446   2882    -28  -1544   -202       C
ATOM   6129  H   PHE B  63      22.521 -37.041 -35.029  1.00  0.00           H
ATOM   6130  HA  PHE B  63      25.401 -37.479 -35.667  1.00  0.00           H
ATOM   6131  HB2 PHE B  63      23.484 -39.232 -34.133  1.00  0.00           H
ATOM   6132  HB3 PHE B  63      25.145 -39.673 -34.575  1.00  0.00           H
ATOM   6133  HD1 PHE B  63      26.883 -37.662 -33.962  1.00  0.00           H
ATOM   6134  HD2 PHE B  63      23.204 -38.510 -31.976  1.00  0.00           H
ATOM   6135  HE1 PHE B  63      27.727 -36.534 -31.957  1.00  0.00           H
ATOM   6136  HE2 PHE B  63      24.050 -37.435 -29.943  1.00  0.00           H
ATOM   6137  HZ  PHE B  63      26.309 -36.412 -29.926  1.00  0.00           H
ATOM   6138  N   HIS B  64      23.443 -39.782 -36.777  1.00 20.33           N
ANISOU 6138  N   HIS B  64     2900   2656   2169    418  -1092     25       N
ATOM   6139  CA  HIS B  64      22.970 -40.410 -38.009  1.00 20.96           C
ANISOU 6139  CA  HIS B  64     2895   2687   2381    487  -1026     48       C
ATOM   6140  C   HIS B  64      21.639 -39.773 -38.451  1.00 21.04           C
ANISOU 6140  C   HIS B  64     2950   2722   2322    498   -829     51       C
ATOM   6141  O   HIS B  64      20.683 -39.674 -37.673  1.00 21.66           O
ANISOU 6141  O   HIS B  64     3122   2849   2260    468   -772    108       O
ATOM   6142  CB  HIS B  64      22.822 -41.933 -37.847  1.00 20.69           C
ANISOU 6142  CB  HIS B  64     2842   2616   2403    502  -1163    168       C
ATOM   6143  CG  HIS B  64      22.732 -42.659 -39.148  1.00 22.54           C
ANISOU 6143  CG  HIS B  64     2974   2784   2807    570  -1137    151       C
ATOM   6144  ND1 HIS B  64      23.686 -42.526 -40.131  1.00 24.10           N
ANISOU 6144  ND1 HIS B  64     3056   2947   3153    615  -1126     40       N
ATOM   6145  CD2 HIS B  64      21.781 -43.491 -39.652  1.00 23.83           C
ANISOU 6145  CD2 HIS B  64     3129   2922   3003    574  -1072    216       C
ATOM   6146  CE1 HIS B  64      23.337 -43.258 -41.184  1.00 24.89           C
ANISOU 6146  CE1 HIS B  64     3099   3009   3349    643  -1056     27       C
ATOM   6147  NE2 HIS B  64      22.200 -43.870 -40.909  1.00 24.55           N
ANISOU 6147  NE2 HIS B  64     3120   2964   3245    616  -1034    131       N
ATOM   6148  H   HIS B  64      23.373 -40.276 -35.899  1.00  0.00           H
ATOM   6149  HA  HIS B  64      23.709 -40.224 -38.788  1.00  0.00           H
ATOM   6150  HB2 HIS B  64      21.916 -42.134 -37.276  1.00  0.00           H
ATOM   6151  HB3 HIS B  64      23.679 -42.312 -37.291  1.00  0.00           H
ATOM   6152  HD2 HIS B  64      20.870 -43.797 -39.160  1.00  0.00           H
ATOM   6153  HE1 HIS B  64      23.890 -43.339 -42.108  1.00  0.00           H
ATOM   6154  HE2 HIS B  64      21.716 -44.512 -41.521  1.00  0.00           H
ATOM   6155  N   GLN B  65      21.616 -39.356 -39.706  1.00 18.80           N
ANISOU 6155  N   GLN B  65     2590   2411   2144    538   -730     -6       N
ATOM   6156  CA  GLN B  65      20.507 -38.649 -40.283  1.00 19.39           C
ANISOU 6156  CA  GLN B  65     2680   2494   2193    549   -562      0       C
ATOM   6157  C   GLN B  65      20.082 -39.359 -41.583  1.00 21.11           C
ANISOU 6157  C   GLN B  65     2822   2686   2511    590   -537     35       C
ATOM   6158  O   GLN B  65      20.064 -40.576 -41.628  1.00 26.74           O
ANISOU 6158  O   GLN B  65     3518   3377   3266    606   -632     87       O
ATOM   6159  CB  GLN B  65      20.908 -37.205 -40.533  1.00 19.46           C
ANISOU 6159  CB  GLN B  65     2679   2497   2218    536   -474    -97       C
ATOM   6160  CG  GLN B  65      21.273 -36.517 -39.238  1.00 23.80           C
ANISOU 6160  CG  GLN B  65     3316   3066   2662    489   -505   -152       C
ATOM   6161  CD  GLN B  65      22.145 -35.295 -39.489  1.00 27.69           C
ANISOU 6161  CD  GLN B  65     3776   3528   3219    467   -485   -259       C
ATOM   6162  OE1 GLN B  65      21.736 -34.372 -40.190  1.00 26.71           O
ANISOU 6162  OE1 GLN B  65     3627   3373   3149    476   -364   -282       O
ATOM   6163  NE2 GLN B  65      23.380 -35.305 -38.927  1.00 30.64           N
ANISOU 6163  NE2 GLN B  65     4139   3902   3602    431   -619   -309       N
ATOM   6164  H   GLN B  65      22.419 -39.544 -40.288  1.00  0.00           H
ATOM   6165  HA  GLN B  65      19.673 -38.668 -39.582  1.00  0.00           H
ATOM   6166  HB2 GLN B  65      21.767 -37.184 -41.203  1.00  0.00           H
ATOM   6167  HB3 GLN B  65      20.076 -36.677 -40.999  1.00  0.00           H
ATOM   6168  HG2 GLN B  65      20.360 -36.204 -38.733  1.00  0.00           H
ATOM   6169  HG3 GLN B  65      21.813 -37.217 -38.600  1.00  0.00           H
ATOM   6170 HE21 GLN B  65      24.006 -34.525 -39.069  1.00  0.00           H
ATOM   6171 HE22 GLN B  65      23.674 -36.092 -38.367  1.00  0.00           H
ATOM   6172  N   ILE B  66      19.723 -38.604 -42.604  1.00 15.47           N
ANISOU 6172  N   ILE B  66     2069   1972   1835    599   -419     10       N
ATOM   6173  CA  ILE B  66      19.398 -39.180 -43.893  1.00 14.08           C
ANISOU 6173  CA  ILE B  66     1830   1788   1730    622   -400     29       C
ATOM   6174  C   ILE B  66      20.477 -38.744 -44.858  1.00 15.03           C
ANISOU 6174  C   ILE B  66     1866   1918   1924    623   -384    -63       C
ATOM   6175  O   ILE B  66      21.206 -37.740 -44.605  1.00 14.06           O
ANISOU 6175  O   ILE B  66     1735   1801   1806    601   -361   -118       O
ATOM   6176  CB  ILE B  66      18.031 -38.699 -44.436  1.00 13.31           C
ANISOU 6176  CB  ILE B  66     1747   1700   1611    617   -283    101       C
ATOM   6177  CG1 ILE B  66      17.980 -37.167 -44.539  1.00 13.96           C
ANISOU 6177  CG1 ILE B  66     1830   1783   1692    601   -174     71       C
ATOM   6178  CG2 ILE B  66      16.899 -39.219 -43.565  1.00 13.37           C
ANISOU 6178  CG2 ILE B  66     1815   1709   1556    614   -283    201       C
ATOM   6179  CD1 ILE B  66      16.809 -36.683 -45.430  1.00 13.76           C
ANISOU 6179  CD1 ILE B  66     1781   1755   1692    598    -78    148       C
ATOM   6180  H   ILE B  66      19.674 -37.602 -42.484  1.00  0.00           H
ATOM   6181  HA  ILE B  66      19.397 -40.267 -43.816  1.00  0.00           H
ATOM   6182  HB  ILE B  66      17.902 -39.109 -45.438  1.00  0.00           H
ATOM   6183 HG12 ILE B  66      17.856 -36.751 -43.539  1.00  0.00           H
ATOM   6184 HG13 ILE B  66      18.919 -36.807 -44.960  1.00  0.00           H
ATOM   6185 HG21 ILE B  66      15.945 -38.871 -43.962  1.00  0.00           H
ATOM   6186 HG22 ILE B  66      16.915 -40.309 -43.562  1.00  0.00           H
ATOM   6187 HG23 ILE B  66      17.025 -38.851 -42.547  1.00  0.00           H
ATOM   6188 HD11 ILE B  66      16.812 -35.594 -45.474  1.00  0.00           H
ATOM   6189 HD12 ILE B  66      15.865 -37.027 -45.007  1.00  0.00           H
ATOM   6190 HD13 ILE B  66      16.926 -37.088 -46.435  1.00  0.00           H
ATOM   6191  N   GLU B  67      20.568 -39.497 -45.955  1.00 15.30           N
ANISOU 6191  N   GLU B  67     1839   1958   2014    643   -393    -83       N
ATOM   6192  CA  GLU B  67      21.433 -39.120 -47.059  1.00 14.44           C
ANISOU 6192  CA  GLU B  67     1645   1887   1956    636   -346   -164       C
ATOM   6193  C   GLU B  67      20.858 -37.887 -47.767  1.00 13.18           C
ANISOU 6193  C   GLU B  67     1488   1760   1759    595   -226   -123       C
ATOM   6194  O   GLU B  67      19.635 -37.679 -47.841  1.00 12.79           O
ANISOU 6194  O   GLU B  67     1486   1703   1671    586   -182    -36       O
ATOM   6195  CB  GLU B  67      21.590 -40.309 -48.018  1.00 14.74           C
ANISOU 6195  CB  GLU B  67     1628   1929   2043    667   -378   -215       C
ATOM   6196  CG  GLU B  67      22.170 -41.572 -47.324  1.00 15.54           C
ANISOU 6196  CG  GLU B  67     1713   1967   2226    715   -515   -248       C
ATOM   6197  CD  GLU B  67      23.577 -41.395 -46.776  1.00 19.83           C
ANISOU 6197  CD  GLU B  67     2190   2501   2842    728   -573   -317       C
ATOM   6198  OE1 GLU B  67      24.317 -40.484 -47.237  1.00 23.09           O
ANISOU 6198  OE1 GLU B  67     2542   2966   3264    705   -499   -374       O
ATOM   6199  OE2 GLU B  67      23.998 -42.170 -45.855  1.00 21.01           O
ANISOU 6199  OE2 GLU B  67     2340   2592   3052    754   -706   -303       O
ATOM   6200  H   GLU B  67      20.025 -40.346 -46.019  1.00  0.00           H
ATOM   6201  HA  GLU B  67      22.414 -38.865 -46.659  1.00  0.00           H
ATOM   6202  HB2 GLU B  67      20.611 -40.556 -48.428  1.00  0.00           H
ATOM   6203  HB3 GLU B  67      22.252 -40.019 -48.834  1.00  0.00           H
ATOM   6204  HG2 GLU B  67      21.513 -41.839 -46.496  1.00  0.00           H
ATOM   6205  HG3 GLU B  67      22.176 -42.392 -48.042  1.00  0.00           H
ATOM   6206  N   LYS B  68      21.761 -37.067 -48.285  1.00 13.09           N
ANISOU 6206  N   LYS B  68     1413   1782   1777    565   -181   -173       N
ATOM   6207  CA  LYS B  68      21.407 -35.798 -48.907  1.00 13.73           C
ANISOU 6207  CA  LYS B  68     1486   1882   1849    515    -87   -120       C
ATOM   6208  C   LYS B  68      22.024 -35.601 -50.302  1.00 14.47           C
ANISOU 6208  C   LYS B  68     1492   2056   1948    474    -30   -143       C
ATOM   6209  O   LYS B  68      21.665 -34.651 -50.988  1.00 14.23           O
ANISOU 6209  O   LYS B  68     1452   2049   1908    421     37    -71       O
ATOM   6210  CB  LYS B  68      21.822 -34.683 -47.970  1.00 13.89           C
ANISOU 6210  CB  LYS B  68     1528   1854   1895    495    -84   -135       C
ATOM   6211  CG  LYS B  68      21.120 -34.831 -46.638  1.00 15.50           C
ANISOU 6211  CG  LYS B  68     1828   2005   2056    525   -118   -119       C
ATOM   6212  CD  LYS B  68      21.638 -33.813 -45.631  1.00 18.72           C
ANISOU 6212  CD  LYS B  68     2270   2369   2473    502   -128   -169       C
ATOM   6213  CE  LYS B  68      20.900 -33.942 -44.319  1.00 18.69           C
ANISOU 6213  CE  LYS B  68     2370   2339   2393    522   -142   -163       C
ATOM   6214  NZ  LYS B  68      21.251 -32.804 -43.425  1.00 18.54           N
ANISOU 6214  NZ  LYS B  68     2398   2276   2370    493   -135   -232       N
ATOM   6215  H   LYS B  68      22.735 -37.333 -48.247  1.00  0.00           H
ATOM   6216  HA  LYS B  68      20.322 -35.765 -49.011  1.00  0.00           H
ATOM   6217  HB2 LYS B  68      21.556 -33.723 -48.413  1.00  0.00           H
ATOM   6218  HB3 LYS B  68      22.900 -34.723 -47.816  1.00  0.00           H
ATOM   6219  HG2 LYS B  68      20.050 -34.679 -46.780  1.00  0.00           H
ATOM   6220  HG3 LYS B  68      21.291 -35.836 -46.252  1.00  0.00           H
ATOM   6221  HD2 LYS B  68      22.701 -33.985 -45.463  1.00  0.00           H
ATOM   6222  HD3 LYS B  68      21.494 -32.808 -46.028  1.00  0.00           H
ATOM   6223  HE2 LYS B  68      19.826 -33.936 -44.507  1.00  0.00           H
ATOM   6224  HE3 LYS B  68      21.178 -34.880 -43.838  1.00  0.00           H
ATOM   6225  HZ1 LYS B  68      22.253 -32.681 -43.413  1.00  0.00           H
ATOM   6226  HZ2 LYS B  68      20.925 -32.998 -42.489  1.00  0.00           H
ATOM   6227  HZ3 LYS B  68      20.813 -31.960 -43.766  1.00  0.00           H
ATOM   6228  N   GLU B  69      22.927 -36.497 -50.715  1.00 13.65           N
ANISOU 6228  N   GLU B  69     1323   1998   1866    497    -54   -238       N
ATOM   6229  CA  GLU B  69      23.423 -36.541 -52.098  1.00 14.95           C
ANISOU 6229  CA  GLU B  69     1407   2266   2007    460     17   -277       C
ATOM   6230  C   GLU B  69      23.267 -37.960 -52.580  1.00 15.64           C
ANISOU 6230  C   GLU B  69     1492   2372   2079    508    -14   -354       C
ATOM   6231  O   GLU B  69      23.384 -38.884 -51.780  1.00 15.58           O
ANISOU 6231  O   GLU B  69     1499   2291   2129    573   -102   -399       O
ATOM   6232  CB  GLU B  69      24.902 -36.117 -52.194  1.00 17.05           C
ANISOU 6232  CB  GLU B  69     1564   2576   2339    440     43   -353       C
ATOM   6233  CG  GLU B  69      25.126 -34.629 -51.934  1.00 22.28           C
ANISOU 6233  CG  GLU B  69     2219   3218   3028    373     73   -280       C
ATOM   6234  CD  GLU B  69      26.614 -34.235 -52.015  1.00 27.40           C
ANISOU 6234  CD  GLU B  69     2745   3909   3756    342     90   -344       C
ATOM   6235  OE1 GLU B  69      27.409 -34.961 -52.659  1.00 29.45           O
ANISOU 6235  OE1 GLU B  69     2908   4250   4032    360    122   -434       O
ATOM   6236  OE2 GLU B  69      27.001 -33.221 -51.407  1.00 27.85           O
ANISOU 6236  OE2 GLU B  69     2797   3912   3871    302     69   -313       O
ATOM   6237  H   GLU B  69      23.282 -37.170 -50.051  1.00  0.00           H
ATOM   6238  HA  GLU B  69      22.818 -35.881 -52.719  1.00  0.00           H
ATOM   6239  HB2 GLU B  69      25.472 -36.685 -51.459  1.00  0.00           H
ATOM   6240  HB3 GLU B  69      25.273 -36.359 -53.190  1.00  0.00           H
ATOM   6241  HG2 GLU B  69      24.754 -34.388 -50.938  1.00  0.00           H
ATOM   6242  HG3 GLU B  69      24.566 -34.052 -52.670  1.00  0.00           H
ATOM   6243  N   PHE B  70      23.053 -38.127 -53.886  1.00 15.92           N
ANISOU 6243  N   PHE B  70     1508   2504   2039    468     51   -369       N
ATOM   6244  CA  PHE B  70      22.699 -39.435 -54.486  1.00 17.18           C
ANISOU 6244  CA  PHE B  70     1681   2674   2170    501     22   -450       C
ATOM   6245  C   PHE B  70      23.433 -39.627 -55.812  1.00 19.19           C
ANISOU 6245  C   PHE B  70     1860   3065   2368    468    114   -565       C
ATOM   6246  O   PHE B  70      23.552 -38.694 -56.597  1.00 21.34           O
ANISOU 6246  O   PHE B  70     2106   3446   2556    384    202   -509       O
ATOM   6247  CB  PHE B  70      21.190 -39.507 -54.723  1.00 17.31           C
ANISOU 6247  CB  PHE B  70     1791   2672   2113    471     -5   -333       C
ATOM   6248  CG  PHE B  70      20.411 -39.282 -53.480  1.00 16.94           C
ANISOU 6248  CG  PHE B  70     1810   2516   2112    499    -65   -223       C
ATOM   6249  CD1 PHE B  70      20.084 -38.005 -53.075  1.00 15.56           C
ANISOU 6249  CD1 PHE B  70     1653   2326   1934    465    -25   -113       C
ATOM   6250  CD2 PHE B  70      20.128 -40.348 -52.642  1.00 18.95           C
ANISOU 6250  CD2 PHE B  70     2100   2678   2421    561   -159   -241       C
ATOM   6251  CE1 PHE B  70      19.399 -37.785 -51.869  1.00 16.69           C
ANISOU 6251  CE1 PHE B  70     1855   2378   2110    495    -60    -38       C
ATOM   6252  CE2 PHE B  70      19.456 -40.153 -51.433  1.00 18.22           C
ANISOU 6252  CE2 PHE B  70     2068   2508   2349    579   -200   -142       C
ATOM   6253  CZ  PHE B  70      19.083 -38.885 -51.053  1.00 17.31           C
ANISOU 6253  CZ  PHE B  70     1973   2392   2212    549   -141    -52       C
ATOM   6254  H   PHE B  70      23.136 -37.325 -54.494  1.00  0.00           H
ATOM   6255  HA  PHE B  70      22.990 -40.231 -53.800  1.00  0.00           H
ATOM   6256  HB2 PHE B  70      20.913 -38.745 -55.452  1.00  0.00           H
ATOM   6257  HB3 PHE B  70      20.941 -40.489 -55.125  1.00  0.00           H
ATOM   6258  HD1 PHE B  70      20.358 -37.163 -53.693  1.00  0.00           H
ATOM   6259  HD2 PHE B  70      20.431 -41.344 -52.928  1.00  0.00           H
ATOM   6260  HE1 PHE B  70      19.119 -36.785 -51.573  1.00  0.00           H
ATOM   6261  HE2 PHE B  70      19.230 -40.997 -50.798  1.00  0.00           H
ATOM   6262  HZ  PHE B  70      18.547 -38.734 -50.127  1.00  0.00           H
ATOM   6263  N   SER B  71      23.924 -40.821 -56.052  1.00 19.71           N
ANISOU 6263  N   SER B  71     1886   3123   2480    531     96   -725       N
ATOM   6264  CA  SER B  71      24.695 -41.051 -57.246  1.00 22.38           C
ANISOU 6264  CA  SER B  71     2143   3597   2763    509    202   -867       C
ATOM   6265  C   SER B  71      23.864 -41.728 -58.349  1.00 23.07           C
ANISOU 6265  C   SER B  71     2296   3750   2718    473    214   -918       C
ATOM   6266  O   SER B  71      24.371 -41.906 -59.461  1.00 25.91           O
ANISOU 6266  O   SER B  71     2609   4250   2987    438    316  -1044       O
ATOM   6267  CB  SER B  71      25.906 -41.925 -56.902  1.00 24.31           C
ANISOU 6267  CB  SER B  71     2277   3792   3166    609    190  -1046       C
ATOM   6268  OG  SER B  71      25.443 -43.155 -56.401  1.00 24.67           O
ANISOU 6268  OG  SER B  71     2371   3698   3303    691     69  -1099       O
ATOM   6269  H   SER B  71      23.761 -41.576 -55.401  1.00  0.00           H
ATOM   6270  HA  SER B  71      25.053 -40.092 -57.619  1.00  0.00           H
ATOM   6271  HB2 SER B  71      26.516 -41.427 -56.148  1.00  0.00           H
ATOM   6272  HB3 SER B  71      26.501 -42.096 -57.799  1.00  0.00           H
ATOM   6273  HG  SER B  71      25.837 -43.873 -56.901  1.00  0.00           H
ATOM   6274  N   GLU B  72      22.640 -42.154 -58.034  1.00 19.90           N
ANISOU 6274  N   GLU B  72     1999   3254   2308    478    111   -832       N
ATOM   6275  CA  GLU B  72      21.771 -42.799 -59.033  1.00 22.53           C
ANISOU 6275  CA  GLU B  72     2401   3637   2523    432     95   -869       C
ATOM   6276  C   GLU B  72      20.375 -42.191 -58.960  1.00 20.01           C
ANISOU 6276  C   GLU B  72     2173   3298   2131    362     39   -652       C
ATOM   6277  O   GLU B  72      19.894 -41.912 -57.854  1.00 18.25           O
ANISOU 6277  O   GLU B  72     1976   2958   2000    397    -24   -524       O
ATOM   6278  CB  GLU B  72      21.589 -44.297 -58.732  1.00 28.89           C
ANISOU 6278  CB  GLU B  72     3229   4308   3441    520    -10  -1001       C
ATOM   6279  CG  GLU B  72      22.807 -45.149 -58.989  1.00 40.27           C
ANISOU 6279  CG  GLU B  72     4577   5748   4977    600     33  -1245       C
ATOM   6280  CD  GLU B  72      23.857 -45.061 -57.890  1.00 47.35           C
ANISOU 6280  CD  GLU B  72     5380   6555   6056    688     15  -1256       C
ATOM   6281  OE1 GLU B  72      23.473 -45.085 -56.691  1.00 49.38           O
ANISOU 6281  OE1 GLU B  72     5675   6676   6412    723    -99  -1126       O
ATOM   6282  OE2 GLU B  72      25.065 -44.995 -58.223  1.00 49.38           O
ANISOU 6282  OE2 GLU B  72     5521   6885   6356    717    111  -1395       O
ATOM   6283  H   GLU B  72      22.302 -42.032 -57.090  1.00  0.00           H
ATOM   6284  HA  GLU B  72      22.186 -42.665 -60.032  1.00  0.00           H
ATOM   6285  HB2 GLU B  72      21.319 -44.401 -57.681  1.00  0.00           H
ATOM   6286  HB3 GLU B  72      20.767 -44.675 -59.340  1.00  0.00           H
ATOM   6287  HG2 GLU B  72      22.488 -46.187 -59.078  1.00  0.00           H
ATOM   6288  HG3 GLU B  72      23.259 -44.839 -59.931  1.00  0.00           H
ATOM   6289  N   VAL B  73      19.709 -42.105 -60.110  1.00 19.42           N
ANISOU 6289  N   VAL B  73     2143   3336   1899    266     54   -622       N
ATOM   6290  CA  VAL B  73      18.292 -41.773 -60.147  1.00 19.43           C
ANISOU 6290  CA  VAL B  73     2219   3308   1856    205    -21   -427       C
ATOM   6291  C   VAL B  73      17.488 -42.927 -59.534  1.00 19.27           C
ANISOU 6291  C   VAL B  73     2249   3138   1935    266   -147   -443       C
ATOM   6292  O   VAL B  73      17.729 -44.082 -59.871  1.00 19.43           O
ANISOU 6292  O   VAL B  73     2278   3135   1969    299   -182   -618       O
ATOM   6293  CB  VAL B  73      17.808 -41.531 -61.623  1.00 23.81           C
ANISOU 6293  CB  VAL B  73     2808   4030   2208     74      0   -394       C
ATOM   6294  CG1 VAL B  73      16.277 -41.551 -61.714  1.00 23.06           C
ANISOU 6294  CG1 VAL B  73     2781   3885   2096     20   -113   -219       C
ATOM   6295  CG2 VAL B  73      18.357 -40.203 -62.125  1.00 25.07           C
ANISOU 6295  CG2 VAL B  73     2920   4327   2279     -9    105   -295       C
ATOM   6296  H   VAL B  73      20.199 -42.274 -60.977  1.00  0.00           H
ATOM   6297  HA  VAL B  73      18.122 -40.869 -59.562  1.00  0.00           H
ATOM   6298  HB  VAL B  73      18.203 -42.329 -62.252  1.00  0.00           H
ATOM   6299 HG11 VAL B  73      15.903 -42.508 -61.351  1.00  0.00           H
ATOM   6300 HG12 VAL B  73      15.973 -41.413 -62.752  1.00  0.00           H
ATOM   6301 HG13 VAL B  73      15.866 -40.746 -61.105  1.00  0.00           H
ATOM   6302 HG21 VAL B  73      18.022 -40.034 -63.148  1.00  0.00           H
ATOM   6303 HG22 VAL B  73      17.996 -39.396 -61.487  1.00  0.00           H
ATOM   6304 HG23 VAL B  73      19.446 -40.227 -62.099  1.00  0.00           H
ATOM   6305  N   GLU B  74      16.548 -42.604 -58.650  1.00 17.86           N
ANISOU 6305  N   GLU B  74     2098   2856   1831    278   -208   -264       N
ATOM   6306  CA  GLU B  74      15.714 -43.617 -58.018  1.00 18.81           C
ANISOU 6306  CA  GLU B  74     2259   2843   2046    320   -324   -240       C
ATOM   6307  C   GLU B  74      14.226 -43.299 -57.987  1.00 20.28           C
ANISOU 6307  C   GLU B  74     2479   3002   2223    263   -383    -34       C
ATOM   6308  O   GLU B  74      13.421 -44.196 -57.756  1.00 20.97           O
ANISOU 6308  O   GLU B  74     2597   3004   2368    268   -482     -7       O
ATOM   6309  CB  GLU B  74      16.149 -43.816 -56.566  1.00 17.20           C
ANISOU 6309  CB  GLU B  74     2035   2514   1984    416   -346   -237       C
ATOM   6310  CG  GLU B  74      17.557 -44.324 -56.396  1.00 19.59           C
ANISOU 6310  CG  GLU B  74     2288   2804   2351    487   -324   -425       C
ATOM   6311  CD  GLU B  74      17.930 -44.333 -54.895  1.00 21.42           C
ANISOU 6311  CD  GLU B  74     2506   2926   2706    561   -364   -379       C
ATOM   6312  OE1 GLU B  74      17.990 -43.228 -54.252  1.00 20.09           O
ANISOU 6312  OE1 GLU B  74     2333   2775   2525    552   -311   -276       O
ATOM   6313  OE2 GLU B  74      18.124 -45.455 -54.359  1.00 22.13           O
ANISOU 6313  OE2 GLU B  74     2595   2908   2907    621   -458   -442       O
ATOM   6314  H   GLU B  74      16.409 -41.632 -58.411  1.00  0.00           H
ATOM   6315  HA  GLU B  74      15.853 -44.558 -58.550  1.00  0.00           H
ATOM   6316  HB2 GLU B  74      16.070 -42.857 -56.053  1.00  0.00           H
ATOM   6317  HB3 GLU B  74      15.466 -44.521 -56.092  1.00  0.00           H
ATOM   6318  HG2 GLU B  74      18.245 -43.673 -56.936  1.00  0.00           H
ATOM   6319  HG3 GLU B  74      17.628 -45.336 -56.793  1.00  0.00           H
ATOM   6320  N   GLY B  75      13.835 -42.045 -58.168  1.00 19.22           N
ANISOU 6320  N   GLY B  75     2332   2928   2044    210   -329    120       N
ATOM   6321  CA  GLY B  75      12.410 -41.735 -58.162  1.00 20.25           C
ANISOU 6321  CA  GLY B  75     2472   3026   2195    163   -385    318       C
ATOM   6322  C   GLY B  75      11.853 -41.432 -56.761  1.00 19.13           C
ANISOU 6322  C   GLY B  75     2316   2770   2184    230   -379    437       C
ATOM   6323  O   GLY B  75      12.464 -40.667 -56.011  1.00 16.66           O
ANISOU 6323  O   GLY B  75     1984   2439   1907    276   -302    433       O
ATOM   6324  H   GLY B  75      14.516 -41.313 -58.308  1.00  0.00           H
ATOM   6325  HA2 GLY B  75      12.244 -40.863 -58.795  1.00  0.00           H
ATOM   6326  HA3 GLY B  75      11.865 -42.581 -58.581  1.00  0.00           H
ATOM   6327  N   ARG B  76      10.721 -42.058 -56.417  1.00 16.66           N
ANISOU 6327  N   ARG B  76     2415   2055   1859    113   -309   -194       N
ATOM   6328  CA  ARG B  76       9.837 -41.590 -55.324  1.00 15.25           C
ANISOU 6328  CA  ARG B  76     2157   1883   1756    101   -320   -200       C
ATOM   6329  C   ARG B  76      10.494 -41.375 -53.947  1.00 13.28           C
ANISOU 6329  C   ARG B  76     1866   1661   1521     97   -251   -170       C
ATOM   6330  O   ARG B  76      10.257 -40.341 -53.300  1.00 13.32           O
ANISOU 6330  O   ARG B  76     1830   1682   1552     93   -253   -160       O
ATOM   6331  CB  ARG B  76       8.703 -42.603 -55.156  1.00 15.28           C
ANISOU 6331  CB  ARG B  76     2125   1856   1824     79   -337   -245       C
ATOM   6332  CG  ARG B  76       7.615 -42.207 -54.194  1.00 15.23           C
ANISOU 6332  CG  ARG B  76     2033   1845   1908     52   -335   -278       C
ATOM   6333  CD  ARG B  76       6.521 -43.254 -54.161  1.00 15.91           C
ANISOU 6333  CD  ARG B  76     2084   1896   2065     18   -336   -341       C
ATOM   6334  NE  ARG B  76       5.393 -42.762 -53.379  1.00 15.60           N
ANISOU 6334  NE  ARG B  76     1951   1848   2128    -16   -328   -397       N
ATOM   6335  CZ  ARG B  76       4.181 -43.307 -53.386  1.00 16.58           C
ANISOU 6335  CZ  ARG B  76     2010   1940   2350    -53   -334   -483       C
ATOM   6336  NH1 ARG B  76       3.905 -44.355 -54.165  1.00 17.94           N
ANISOU 6336  NH1 ARG B  76     2207   2084   2525    -58   -362   -516       N
ATOM   6337  NH2 ARG B  76       3.241 -42.773 -52.643  1.00 16.85           N
ANISOU 6337  NH2 ARG B  76     1948   1967   2487    -88   -312   -547       N
ATOM   6338  H   ARG B  76      10.457 -42.889 -56.927  1.00  0.00           H
ATOM   6339  HA  ARG B  76       9.395 -40.643 -55.634  1.00  0.00           H
ATOM   6340  HB2 ARG B  76       9.138 -43.538 -54.804  1.00  0.00           H
ATOM   6341  HB3 ARG B  76       8.252 -42.780 -56.132  1.00  0.00           H
ATOM   6342  HG2 ARG B  76       7.189 -41.254 -54.509  1.00  0.00           H
ATOM   6343  HG3 ARG B  76       8.039 -42.099 -53.196  1.00  0.00           H
ATOM   6344  HD2 ARG B  76       6.192 -43.466 -55.178  1.00  0.00           H
ATOM   6345  HD3 ARG B  76       6.906 -44.167 -53.707  1.00  0.00           H
ATOM   6346  HE  ARG B  76       5.543 -41.953 -52.793  1.00  0.00           H
ATOM   6347 HH11 ARG B  76       4.626 -44.755 -54.748  1.00  0.00           H
ATOM   6348 HH12 ARG B  76       2.975 -44.748 -54.171  1.00  0.00           H
ATOM   6349 HH21 ARG B  76       3.448 -41.970 -52.066  1.00  0.00           H
ATOM   6350 HH22 ARG B  76       2.310 -43.165 -52.648  1.00  0.00           H
ATOM   6351  N  AILE B  77      11.282 -42.343 -53.487  0.60 12.56           N
ANISOU 6351  N  AILE B  77     1791   1567   1413    103   -204   -160       N
ATOM   6352  N  BILE B  77      11.285 -42.339 -53.483  0.40 12.53           N
ANISOU 6352  N  BILE B  77     1787   1564   1410    103   -204   -160       N
ATOM   6353  CA AILE B  77      11.872 -42.237 -52.155  0.60 12.05           C
ANISOU 6353  CA AILE B  77     1707   1513   1357    107   -162   -138       C
ATOM   6354  CA BILE B  77      11.862 -42.214 -52.147  0.40 12.16           C
ANISOU 6354  CA BILE B  77     1721   1528   1372    107   -162   -138       C
ATOM   6355  C  AILE B  77      12.964 -41.157 -52.112  0.60 12.44           C
ANISOU 6355  C  AILE B  77     1745   1600   1383    129   -148   -118       C
ATOM   6356  C  BILE B  77      12.948 -41.138 -52.119  0.40 12.40           C
ANISOU 6356  C  BILE B  77     1739   1595   1378    129   -149   -118       C
ATOM   6357  O  AILE B  77      13.054 -40.387 -51.154  0.60 11.50           O
ANISOU 6357  O  AILE B  77     1594   1496   1280    128   -136   -101       O
ATOM   6358  O  BILE B  77      13.021 -40.356 -51.177  0.40 11.51           O
ANISOU 6358  O  BILE B  77     1595   1498   1282    128   -137   -101       O
ATOM   6359  CB AILE B  77      12.445 -43.560 -51.664  0.60 13.81           C
ANISOU 6359  CB AILE B  77     1971   1708   1568    120   -140   -140       C
ATOM   6360  CB BILE B  77      12.430 -43.528 -51.601  0.40 14.05           C
ANISOU 6360  CB BILE B  77     2000   1739   1599    119   -139   -139       C
ATOM   6361  CG1AILE B  77      11.341 -44.618 -51.536  0.60 12.78           C
ANISOU 6361  CG1AILE B  77     1861   1533   1461     84   -135   -161       C
ATOM   6362  CG1BILE B  77      12.826 -43.369 -50.131  0.40 12.71           C
ANISOU 6362  CG1BILE B  77     1835   1562   1432    126   -117   -118       C
ATOM   6363  CG2AILE B  77      13.129 -43.374 -50.313  0.60 13.71           C
ANISOU 6363  CG2AILE B  77     1963   1695   1553    137   -120   -119       C
ATOM   6364  CG2BILE B  77      13.655 -43.946 -52.362  0.40 16.01           C
ANISOU 6364  CG2BILE B  77     2271   1997   1816    157   -138   -148       C
ATOM   6365  CD1AILE B  77      10.158 -44.156 -50.815  0.60 11.82           C
ANISOU 6365  CD1AILE B  77     1701   1402   1389     38   -118   -175       C
ATOM   6366  CD1BILE B  77      11.748 -42.826 -49.273  0.40 10.09           C
ANISOU 6366  CD1BILE B  77     1482   1222   1132     81    -97   -116       C
ATOM   6367  H  AILE B  77      11.473 -43.153 -54.060  0.60  0.00           H
ATOM   6368  H  BILE B  77      11.485 -43.151 -54.050  0.40  0.00           H
ATOM   6369  HA AILE B  77      11.083 -41.940 -51.464  0.60  0.00           H
ATOM   6370  HA BILE B  77      11.066 -41.895 -51.474  0.40  0.00           H
ATOM   6371  HB AILE B  77      13.184 -43.910 -52.385  0.60  0.00           H
ATOM   6372  HB BILE B  77      11.673 -44.308 -51.685  0.40  0.00           H
ATOM   6373 HG12AILE B  77      11.036 -44.918 -52.538  0.60  0.00           H
ATOM   6374 HG12BILE B  77      13.111 -44.348 -49.745  0.40  0.00           H
ATOM   6375 HG13AILE B  77      11.748 -45.487 -51.019  0.60  0.00           H
ATOM   6376 HG13BILE B  77      13.688 -42.705 -50.071  0.40  0.00           H
ATOM   6377 HG21AILE B  77      14.187 -43.621 -50.404  0.60  0.00           H
ATOM   6378 HG21BILE B  77      14.539 -43.785 -51.745  0.40  0.00           H
ATOM   6379 HG22AILE B  77      12.665 -44.031 -49.577  0.60  0.00           H
ATOM   6380 HG22BILE B  77      13.736 -43.354 -53.274  0.40  0.00           H
ATOM   6381 HG23AILE B  77      13.024 -42.338 -49.992  0.60  0.00           H
ATOM   6382 HG23BILE B  77      13.580 -45.002 -52.620  0.40  0.00           H
ATOM   6383 HD11AILE B  77       9.265 -44.584 -51.270  0.60  0.00           H
ATOM   6384 HD11BILE B  77      12.183 -42.194 -48.498  0.40  0.00           H
ATOM   6385 HD12AILE B  77      10.221 -44.471 -49.773  0.60  0.00           H
ATOM   6386 HD12BILE B  77      11.063 -42.235 -49.881  0.40  0.00           H
ATOM   6387 HD13AILE B  77      10.105 -43.068 -50.863  0.60  0.00           H
ATOM   6388 HD13BILE B  77      11.204 -43.649 -48.808  0.40  0.00           H
ATOM   6389  N   GLN B  78      13.782 -41.090 -53.148  1.00 13.59           N
ANISOU 6389  N   GLN B  78     1917   1755   1491    142   -141   -127       N
ATOM   6390  CA  GLN B  78      14.765 -40.020 -53.259  1.00 13.49           C
ANISOU 6390  CA  GLN B  78     1894   1771   1460    147   -112   -122       C
ATOM   6391  C   GLN B  78      14.111 -38.671 -53.413  1.00 13.32           C
ANISOU 6391  C   GLN B  78     1872   1757   1433    129   -135   -104       C
ATOM   6392  O   GLN B  78      14.641 -37.642 -52.882  1.00 14.24           O
ANISOU 6392  O   GLN B  78     1961   1896   1553    128   -113    -91       O
ATOM   6393  CB  GLN B  78      15.686 -40.262 -54.433  1.00 13.79           C
ANISOU 6393  CB  GLN B  78     1972   1808   1459    146    -77   -151       C
ATOM   6394  CG  GLN B  78      16.877 -39.293 -54.490  1.00 14.47           C
ANISOU 6394  CG  GLN B  78     2041   1919   1538    139    -19   -166       C
ATOM   6395  CD  GLN B  78      17.740 -39.562 -55.671  1.00 15.72           C
ANISOU 6395  CD  GLN B  78     2243   2069   1662    121     40   -209       C
ATOM   6396  OE1 GLN B  78      18.024 -38.652 -56.447  1.00 17.26           O
ANISOU 6396  OE1 GLN B  78     2490   2258   1809     84     84   -215       O
ATOM   6397  NE2 GLN B  78      18.155 -40.823 -55.846  1.00 14.84           N
ANISOU 6397  NE2 GLN B  78     2123   1947   1568    143     48   -245       N
ATOM   6398  H  AGLN B  78      13.725 -41.791 -53.873  0.60  0.00           H
ATOM   6399  H  BGLN B  78      13.736 -41.802 -53.863  0.40  0.00           H
ATOM   6400  HA  GLN B  78      15.365 -40.009 -52.349  1.00  0.00           H
ATOM   6401  HB2 GLN B  78      16.072 -41.279 -54.364  1.00  0.00           H
ATOM   6402  HB3 GLN B  78      15.112 -40.167 -55.355  1.00  0.00           H
ATOM   6403  HG2 GLN B  78      16.501 -38.272 -54.551  1.00  0.00           H
ATOM   6404  HG3 GLN B  78      17.470 -39.401 -53.582  1.00  0.00           H
ATOM   6405 HE21 GLN B  78      17.888 -41.539 -55.186  1.00  0.00           H
ATOM   6406 HE22 GLN B  78      18.735 -41.058 -56.638  1.00  0.00           H
ATOM   6407  N   ASP B  79      13.032 -38.606 -54.207  1.00 11.68           N
ANISOU 6407  N   ASP B  79     1698   1523   1215    119   -189   -109       N
ATOM   6408  CA  ASP B  79      12.301 -37.321 -54.347  1.00 11.97           C
ANISOU 6408  CA  ASP B  79     1740   1555   1255    115   -237   -100       C
ATOM   6409  C   ASP B  79      11.923 -36.795 -52.944  1.00 11.66           C
ANISOU 6409  C   ASP B  79     1620   1535   1277    113   -229    -90       C
ATOM   6410  O   ASP B  79      12.038 -35.576 -52.634  1.00 10.84           O
ANISOU 6410  O   ASP B  79     1504   1444   1172    113   -231    -75       O
ATOM   6411  CB  ASP B  79      10.985 -37.501 -55.117  1.00 13.68           C
ANISOU 6411  CB  ASP B  79     1981   1732   1484    119   -325   -126       C
ATOM   6412  CG  ASP B  79      11.178 -37.814 -56.611  1.00 16.36           C
ANISOU 6412  CG  ASP B  79     2431   2039   1748    121   -353   -135       C
ATOM   6413  OD1 ASP B  79      12.237 -37.457 -57.182  1.00 17.01           O
ANISOU 6413  OD1 ASP B  79     2584   2122   1758    109   -300   -121       O
ATOM   6414  OD2 ASP B  79      10.202 -38.370 -57.197  1.00 17.12           O
ANISOU 6414  OD2 ASP B  79     2542   2101   1862    130   -428   -166       O
ATOM   6415  H   ASP B  79      12.719 -39.426 -54.707  1.00  0.00           H
ATOM   6416  HA  ASP B  79      12.930 -36.592 -54.857  1.00  0.00           H
ATOM   6417  HB2 ASP B  79      10.408 -36.581 -55.031  1.00  0.00           H
ATOM   6418  HB3 ASP B  79      10.420 -38.313 -54.659  1.00  0.00           H
ATOM   6419  N   LEU B  80      11.365 -37.690 -52.144  1.00 11.23           N
ANISOU 6419  N   LEU B  80     1523   1475   1270    106   -219   -103       N
ATOM   6420  CA  LEU B  80      10.933 -37.322 -50.784  1.00 10.36           C
ANISOU 6420  CA  LEU B  80     1355   1372   1209     92   -196   -100       C
ATOM   6421  C   LEU B  80      12.116 -36.928 -49.858  1.00 14.94           C
ANISOU 6421  C   LEU B  80     1931   1978   1768    104   -150    -70       C
ATOM   6422  O   LEU B  80      12.031 -35.951 -49.099  1.00 12.69           O
ANISOU 6422  O   LEU B  80     1614   1707   1501     99   -142    -60       O
ATOM   6423  CB  LEU B  80      10.127 -38.475 -50.165  1.00 10.50           C
ANISOU 6423  CB  LEU B  80     1359   1363   1269     66   -174   -127       C
ATOM   6424  CG  LEU B  80       9.493 -38.250 -48.780  1.00 10.75           C
ANISOU 6424  CG  LEU B  80     1352   1386   1347     33   -130   -137       C
ATOM   6425  CD1 LEU B  80       8.546 -37.057 -48.807  1.00 10.43           C
ANISOU 6425  CD1 LEU B  80     1245   1352   1366     26   -163   -167       C
ATOM   6426  CD2 LEU B  80       8.685 -39.531 -48.428  1.00 12.19           C
ANISOU 6426  CD2 LEU B  80     1546   1526   1561     -9    -92   -173       C
ATOM   6427  H   LEU B  80      11.234 -38.637 -52.470  1.00  0.00           H
ATOM   6428  HA  LEU B  80      10.272 -36.459 -50.866  1.00  0.00           H
ATOM   6429  HB2 LEU B  80      10.797 -39.330 -50.080  1.00  0.00           H
ATOM   6430  HB3 LEU B  80       9.331 -38.740 -50.860  1.00  0.00           H
ATOM   6431  HG  LEU B  80      10.273 -38.088 -48.037  1.00  0.00           H
ATOM   6432 HD11 LEU B  80       9.105 -36.154 -49.053  1.00  0.00           H
ATOM   6433 HD12 LEU B  80       8.081 -36.940 -47.828  1.00  0.00           H
ATOM   6434 HD13 LEU B  80       7.774 -37.223 -49.559  1.00  0.00           H
ATOM   6435 HD21 LEU B  80       8.219 -39.410 -47.450  1.00  0.00           H
ATOM   6436 HD22 LEU B  80       7.913 -39.692 -49.181  1.00  0.00           H
ATOM   6437 HD23 LEU B  80       9.356 -40.390 -48.407  1.00  0.00           H
ATOM   6438  N   GLU B  81      13.206 -37.694 -49.885  1.00 12.97           N
ANISOU 6438  N   GLU B  81     1708   1732   1489    122   -126    -66       N
ATOM   6439  CA  GLU B  81      14.393 -37.338 -49.108  1.00 11.55           C
ANISOU 6439  CA  GLU B  81     1514   1571   1302    144   -103    -57       C
ATOM   6440  C   GLU B  81      14.901 -35.939 -49.461  1.00 11.42           C
ANISOU 6440  C   GLU B  81     1479   1584   1277    141    -94    -51       C
ATOM   6441  O   GLU B  81      15.266 -35.159 -48.568  1.00 11.13           O
ANISOU 6441  O   GLU B  81     1412   1563   1253    145    -84    -41       O
ATOM   6442  CB  GLU B  81      15.518 -38.380 -49.328  1.00 10.33           C
ANISOU 6442  CB  GLU B  81     1380   1411   1136    174    -95    -77       C
ATOM   6443  CG  GLU B  81      15.162 -39.724 -48.688  1.00 12.06           C
ANISOU 6443  CG  GLU B  81     1638   1588   1355    181   -106    -79       C
ATOM   6444  CD  GLU B  81      15.996 -40.924 -49.261  1.00 16.53           C
ANISOU 6444  CD  GLU B  81     2232   2138   1912    214   -114   -107       C
ATOM   6445  OE1 GLU B  81      16.355 -40.903 -50.464  1.00 15.79           O
ANISOU 6445  OE1 GLU B  81     2129   2060   1809    213   -100   -127       O
ATOM   6446  OE2 GLU B  81      16.227 -41.872 -48.491  1.00 17.09           O
ANISOU 6446  OE2 GLU B  81     2345   2171   1979    239   -133   -111       O
ATOM   6447  H   GLU B  81      13.213 -38.532 -50.449  1.00  0.00           H
ATOM   6448  HA  GLU B  81      14.123 -37.346 -48.052  1.00  0.00           H
ATOM   6449  HB2 GLU B  81      16.440 -38.007 -48.882  1.00  0.00           H
ATOM   6450  HB3 GLU B  81      15.670 -38.522 -50.398  1.00  0.00           H
ATOM   6451  HG2 GLU B  81      15.345 -39.656 -47.616  1.00  0.00           H
ATOM   6452  HG3 GLU B  81      14.103 -39.922 -48.852  1.00  0.00           H
ATOM   6453  N   LYS B  82      14.906 -35.620 -50.746  1.00  9.74           N
ANISOU 6453  N   LYS B  82     1298   1368   1034    130    -97    -57       N
ATOM   6454  CA  LYS B  82      15.451 -34.331 -51.180  1.00 10.33           C
ANISOU 6454  CA  LYS B  82     1385   1456   1085    116    -76    -52       C
ATOM   6455  C   LYS B  82      14.465 -33.204 -50.811  1.00 11.79           C
ANISOU 6455  C   LYS B  82     1558   1637   1283    109   -115    -31       C
ATOM   6456  O   LYS B  82      14.867 -32.085 -50.430  1.00 12.49           O
ANISOU 6456  O   LYS B  82     1633   1739   1372    102    -99    -21       O
ATOM   6457  CB  LYS B  82      15.664 -34.330 -52.683  1.00 10.97           C
ANISOU 6457  CB  LYS B  82     1543   1517   1109     98    -64    -65       C
ATOM   6458  CG  LYS B  82      16.860 -35.172 -53.115  1.00 13.84           C
ANISOU 6458  CG  LYS B  82     1908   1887   1465     98     -5   -101       C
ATOM   6459  CD  LYS B  82      16.971 -35.165 -54.666  1.00 21.98           C
ANISOU 6459  CD  LYS B  82     3040   2887   2426     68     20   -116       C
ATOM   6460  CE  LYS B  82      18.376 -35.570 -55.118  1.00 24.16           C
ANISOU 6460  CE  LYS B  82     3307   3171   2701     51    113   -171       C
ATOM   6461  NZ  LYS B  82      18.533 -35.479 -56.603  1.00 25.42           N
ANISOU 6461  NZ  LYS B  82     3587   3292   2778      7    160   -189       N
ATOM   6462  H   LYS B  82      14.534 -36.266 -51.428  1.00  0.00           H
ATOM   6463  HA  LYS B  82      16.404 -34.155 -50.680  1.00  0.00           H
ATOM   6464  HB2 LYS B  82      15.826 -33.303 -53.010  1.00  0.00           H
ATOM   6465  HB3 LYS B  82      14.767 -34.717 -53.167  1.00  0.00           H
ATOM   6466  HG2 LYS B  82      17.771 -34.756 -52.685  1.00  0.00           H
ATOM   6467  HG3 LYS B  82      16.728 -36.196 -52.765  1.00  0.00           H
ATOM   6468  HD2 LYS B  82      16.754 -34.162 -55.034  1.00  0.00           H
ATOM   6469  HD3 LYS B  82      16.245 -35.865 -55.081  1.00  0.00           H
ATOM   6470  HE2 LYS B  82      19.102 -34.908 -54.646  1.00  0.00           H
ATOM   6471  HE3 LYS B  82      18.570 -36.595 -54.802  1.00  0.00           H
ATOM   6472  HZ1 LYS B  82      17.772 -35.968 -57.052  1.00  0.00           H
ATOM   6473  HZ2 LYS B  82      18.523 -34.509 -56.884  1.00  0.00           H
ATOM   6474  HZ3 LYS B  82      19.410 -35.899 -56.876  1.00  0.00           H
ATOM   6475  N   TYR B  83      13.190 -33.499 -50.901  1.00 11.74           N
ANISOU 6475  N   TYR B  83     1551   1610   1301    110   -166    -36       N
ATOM   6476  CA  TYR B  83      12.167 -32.501 -50.571  1.00  9.89           C
ANISOU 6476  CA  TYR B  83     1290   1367   1101    109   -211    -36       C
ATOM   6477  C   TYR B  83      12.148 -32.177 -49.081  1.00 10.03           C
ANISOU 6477  C   TYR B  83     1242   1406   1163    104   -179    -30       C
ATOM   6478  O   TYR B  83      11.950 -31.031 -48.677  1.00 10.90           O
ANISOU 6478  O   TYR B  83     1331   1521   1289    103   -189    -24       O
ATOM   6479  CB  TYR B  83      10.790 -33.021 -50.958  1.00 10.13           C
ANISOU 6479  CB  TYR B  83     1308   1367   1173    112   -273    -69       C
ATOM   6480  CG  TYR B  83       9.657 -32.008 -50.840  1.00 11.15           C
ANISOU 6480  CG  TYR B  83     1401   1478   1357    120   -339    -95       C
ATOM   6481  CD1 TYR B  83       9.483 -31.023 -51.804  1.00 11.57           C
ANISOU 6481  CD1 TYR B  83     1520   1500   1375    140   -415    -94       C
ATOM   6482  CD2 TYR B  83       8.750 -32.081 -49.789  1.00 12.61           C
ANISOU 6482  CD2 TYR B  83     1498   1665   1627    106   -326   -129       C
ATOM   6483  CE1 TYR B  83       8.409 -30.113 -51.739  1.00 13.39           C
ANISOU 6483  CE1 TYR B  83     1718   1704   1666    162   -499   -130       C
ATOM   6484  CE2 TYR B  83       7.651 -31.165 -49.684  1.00 12.63           C
ANISOU 6484  CE2 TYR B  83     1448   1648   1704    117   -389   -175       C
ATOM   6485  CZ  TYR B  83       7.502 -30.194 -50.649  1.00 12.97           C
ANISOU 6485  CZ  TYR B  83     1545   1663   1721    152   -484   -175       C
ATOM   6486  OH  TYR B  83       6.441 -29.343 -50.595  1.00 12.80           O
ANISOU 6486  OH  TYR B  83     1472   1613   1777    176   -567   -230       O
ATOM   6487  H   TYR B  83      12.910 -34.422 -51.200  1.00  0.00           H
ATOM   6488  HA  TYR B  83      12.370 -31.587 -51.130  1.00  0.00           H
ATOM   6489  HB2 TYR B  83      10.555 -33.866 -50.311  1.00  0.00           H
ATOM   6490  HB3 TYR B  83      10.831 -33.375 -51.988  1.00  0.00           H
ATOM   6491  HD1 TYR B  83      10.186 -30.953 -52.621  1.00  0.00           H
ATOM   6492  HD2 TYR B  83       8.876 -32.844 -49.035  1.00  0.00           H
ATOM   6493  HE1 TYR B  83       8.277 -29.365 -52.507  1.00  0.00           H
ATOM   6494  HE2 TYR B  83       6.953 -31.236 -48.863  1.00  0.00           H
ATOM   6495  HH  TYR B  83       5.790 -29.681 -49.976  1.00  0.00           H
ATOM   6496  N   VAL B  84      12.326 -33.194 -48.261  1.00  9.67           N
ANISOU 6496  N   VAL B  84     1180   1363   1130    101   -143    -32       N
ATOM   6497  CA  VAL B  84      12.353 -33.032 -46.807  1.00 10.13           C
ANISOU 6497  CA  VAL B  84     1210   1427   1211     93   -111    -25       C
ATOM   6498  C   VAL B  84      13.545 -32.112 -46.462  1.00 11.43           C
ANISOU 6498  C   VAL B  84     1371   1620   1354    108    -96     -5       C
ATOM   6499  O   VAL B  84      13.389 -31.135 -45.719  1.00 12.17           O
ANISOU 6499  O   VAL B  84     1438   1721   1464    102    -91      2       O
ATOM   6500  CB  VAL B  84      12.500 -34.410 -46.132  1.00  9.45           C
ANISOU 6500  CB  VAL B  84     1154   1320   1117     90    -84    -28       C
ATOM   6501  CG1 VAL B  84      12.985 -34.275 -44.679  1.00 10.03           C
ANISOU 6501  CG1 VAL B  84     1242   1388   1180     92    -58    -14       C
ATOM   6502  CG2 VAL B  84      11.118 -35.131 -46.178  1.00  8.63           C
ANISOU 6502  CG2 VAL B  84     1043   1185   1051     56    -78    -58       C
ATOM   6503  H   VAL B  84      12.448 -34.118 -48.650  1.00  0.00           H
ATOM   6504  HA  VAL B  84      11.426 -32.563 -46.477  1.00  0.00           H
ATOM   6505  HB  VAL B  84      13.225 -35.001 -46.692  1.00  0.00           H
ATOM   6506 HG11 VAL B  84      13.951 -33.770 -44.663  1.00  0.00           H
ATOM   6507 HG12 VAL B  84      12.262 -33.694 -44.107  1.00  0.00           H
ATOM   6508 HG13 VAL B  84      13.086 -35.266 -44.236  1.00  0.00           H
ATOM   6509 HG21 VAL B  84      11.202 -36.109 -45.704  1.00  0.00           H
ATOM   6510 HG22 VAL B  84      10.808 -35.255 -47.215  1.00  0.00           H
ATOM   6511 HG23 VAL B  84      10.378 -34.532 -45.647  1.00  0.00           H
ATOM   6512  N   GLU B  85      14.698 -32.375 -47.066  1.00 11.06           N
ANISOU 6512  N   GLU B  85     1340   1583   1278    124    -85     -8       N
ATOM   6513  CA  GLU B  85      15.871 -31.540 -46.778  1.00 12.22           C
ANISOU 6513  CA  GLU B  85     1468   1754   1422    131    -63     -9       C
ATOM   6514  C   GLU B  85      15.746 -30.119 -47.307  1.00 11.98           C
ANISOU 6514  C   GLU B  85     1441   1730   1381    112    -61      0       C
ATOM   6515  O   GLU B  85      16.125 -29.177 -46.618  1.00 11.98           O
ANISOU 6515  O   GLU B  85     1414   1744   1392    110    -50      5       O
ATOM   6516  CB  GLU B  85      17.150 -32.208 -47.338  1.00 13.60           C
ANISOU 6516  CB  GLU B  85     1643   1935   1589    147    -40    -40       C
ATOM   6517  CG  GLU B  85      18.446 -31.528 -46.918  1.00 14.85           C
ANISOU 6517  CG  GLU B  85     1758   2115   1769    156    -15    -67       C
ATOM   6518  CD  GLU B  85      18.715 -31.596 -45.394  1.00 15.91           C
ANISOU 6518  CD  GLU B  85     1868   2248   1928    188    -47    -68       C
ATOM   6519  OE1 GLU B  85      17.959 -32.305 -44.659  1.00 16.34           O
ANISOU 6519  OE1 GLU B  85     1957   2279   1972    198    -75    -45       O
ATOM   6520  OE2 GLU B  85      19.706 -30.965 -44.953  1.00 15.79           O
ANISOU 6520  OE2 GLU B  85     1810   2249   1942    200    -41    -97       O
ATOM   6521  H   GLU B  85      14.768 -33.143 -47.718  1.00  0.00           H
ATOM   6522  HA  GLU B  85      15.976 -31.481 -45.695  1.00  0.00           H
ATOM   6523  HB2 GLU B  85      17.094 -32.194 -48.426  1.00  0.00           H
ATOM   6524  HB3 GLU B  85      17.176 -33.245 -47.004  1.00  0.00           H
ATOM   6525  HG2 GLU B  85      19.273 -32.013 -47.436  1.00  0.00           H
ATOM   6526  HG3 GLU B  85      18.407 -30.482 -47.221  1.00  0.00           H
ATOM   6527  N   ASP B  86      15.253 -29.961 -48.520  1.00 11.29           N
ANISOU 6527  N   ASP B  86     1401   1623   1264    100    -78      2       N
ATOM   6528  CA  ASP B  86      15.082 -28.647 -49.149  1.00 12.69           C
ANISOU 6528  CA  ASP B  86     1622   1787   1415     84    -90     13       C
ATOM   6529  C   ASP B  86      14.094 -27.809 -48.322  1.00 13.05           C
ANISOU 6529  C   ASP B  86     1629   1829   1499     91   -131     23       C
ATOM   6530  O   ASP B  86      14.317 -26.619 -48.084  1.00 12.69           O
ANISOU 6530  O   ASP B  86     1586   1785   1450     84   -126     32       O
ATOM   6531  CB  ASP B  86      14.542 -28.771 -50.569  1.00 14.64           C
ANISOU 6531  CB  ASP B  86     1956   1995   1614     78   -128     11       C
ATOM   6532  CG  ASP B  86      14.792 -27.517 -51.399  1.00 21.05           C
ANISOU 6532  CG  ASP B  86     2860   2773   2364     56   -127     21       C
ATOM   6533  OD1 ASP B  86      15.930 -26.987 -51.311  1.00 22.43           O
ANISOU 6533  OD1 ASP B  86     3039   2962   2521     28    -51     17       O
ATOM   6534  OD2 ASP B  86      13.849 -27.049 -52.117  1.00 25.25           O
ANISOU 6534  OD2 ASP B  86     3467   3257   2869     68   -206     27       O
ATOM   6535  H   ASP B  86      14.981 -30.783 -49.040  1.00  0.00           H
ATOM   6536  HA  ASP B  86      16.045 -28.137 -49.177  1.00  0.00           H
ATOM   6537  HB2 ASP B  86      13.468 -28.950 -50.520  1.00  0.00           H
ATOM   6538  HB3 ASP B  86      15.020 -29.620 -51.057  1.00  0.00           H
ATOM   6539  N   THR B  87      13.057 -28.476 -47.833  1.00 11.77           N
ANISOU 6539  N   THR B  87     1429   1662   1382    100   -159     11       N
ATOM   6540  CA  THR B  87      12.011 -27.856 -47.030  1.00 11.37           C
ANISOU 6540  CA  THR B  87     1328   1605   1386    101   -184     -1       C
ATOM   6541  C   THR B  87      12.626 -27.354 -45.705  1.00 10.66           C
ANISOU 6541  C   THR B  87     1202   1541   1306     94   -137     13       C
ATOM   6542  O   THR B  87      12.390 -26.216 -45.298  1.00  9.64           O
ANISOU 6542  O   THR B  87     1055   1413   1196     94   -147     14       O
ATOM   6543  CB  THR B  87      10.836 -28.835 -46.774  1.00 11.23           C
ANISOU 6543  CB  THR B  87     1272   1571   1422     95   -196    -35       C
ATOM   6544  OG1 THR B  87      10.155 -29.087 -48.009  1.00 13.64           O
ANISOU 6544  OG1 THR B  87     1604   1848   1729    107   -262    -57       O
ATOM   6545  CG2 THR B  87       9.843 -28.295 -45.730  1.00 14.21           C
ANISOU 6545  CG2 THR B  87     1583   1944   1871     82   -190    -66       C
ATOM   6546  H   THR B  87      12.989 -29.465 -48.027  1.00  0.00           H
ATOM   6547  HA  THR B  87      11.626 -26.995 -47.576  1.00  0.00           H
ATOM   6548  HB  THR B  87      11.245 -29.776 -46.407  1.00  0.00           H
ATOM   6549  HG1 THR B  87      10.776 -29.440 -48.651  1.00  0.00           H
ATOM   6550 HG21 THR B  87       9.535 -29.104 -45.068  1.00  0.00           H
ATOM   6551 HG22 THR B  87       8.968 -27.889 -46.237  1.00  0.00           H
ATOM   6552 HG23 THR B  87      10.322 -27.509 -45.146  1.00  0.00           H
ATOM   6553  N   LYS B  88      13.419 -28.201 -45.057  1.00 10.59           N
ANISOU 6553  N   LYS B  88     1192   1547   1285     96    -98     19       N
ATOM   6554  CA  LYS B  88      14.094 -27.893 -43.822  1.00 10.29           C
ANISOU 6554  CA  LYS B  88     1138   1523   1248     99    -71     26       C
ATOM   6555  C   LYS B  88      15.033 -26.700 -44.016  1.00  9.88           C
ANISOU 6555  C   LYS B  88     1080   1491   1184    101    -65     33       C
ATOM   6556  O   LYS B  88      15.054 -25.762 -43.206  1.00  9.57           O
ANISOU 6556  O   LYS B  88     1019   1459   1159     97    -60     38       O
ATOM   6557  CB  LYS B  88      14.921 -29.127 -43.372  1.00  9.02           C
ANISOU 6557  CB  LYS B  88      998   1359   1069    116    -60     23       C
ATOM   6558  CG  LYS B  88      15.747 -28.878 -42.132  1.00  9.45           C
ANISOU 6558  CG  LYS B  88     1053   1418   1120    132    -58     23       C
ATOM   6559  CD  LYS B  88      16.624 -30.084 -41.724  1.00 10.83           C
ANISOU 6559  CD  LYS B  88     1262   1575   1278    165    -76     10       C
ATOM   6560  CE  LYS B  88      17.509 -29.732 -40.560  1.00 12.81           C
ANISOU 6560  CE  LYS B  88     1519   1821   1527    193   -101      1       C
ATOM   6561  NZ  LYS B  88      18.557 -30.768 -40.379  1.00 15.05           N
ANISOU 6561  NZ  LYS B  88     1827   2084   1808    243   -145    -28       N
ATOM   6562  H   LYS B  88      13.557 -29.119 -45.456  1.00  0.00           H
ATOM   6563  HA  LYS B  88      13.356 -27.653 -43.056  1.00  0.00           H
ATOM   6564  HB2 LYS B  88      14.233 -29.948 -43.169  1.00  0.00           H
ATOM   6565  HB3 LYS B  88      15.587 -29.419 -44.184  1.00  0.00           H
ATOM   6566  HG2 LYS B  88      15.072 -28.648 -41.308  1.00  0.00           H
ATOM   6567  HG3 LYS B  88      16.393 -28.018 -42.307  1.00  0.00           H
ATOM   6568  HD2 LYS B  88      15.978 -30.916 -41.443  1.00  0.00           H
ATOM   6569  HD3 LYS B  88      17.244 -30.380 -42.570  1.00  0.00           H
ATOM   6570  HE2 LYS B  88      17.984 -28.769 -40.748  1.00  0.00           H
ATOM   6571  HE3 LYS B  88      16.906 -29.667 -39.655  1.00  0.00           H
ATOM   6572  HZ1 LYS B  88      19.375 -30.350 -39.959  1.00  0.00           H
ATOM   6573  HZ2 LYS B  88      18.207 -31.501 -39.778  1.00  0.00           H
ATOM   6574  HZ3 LYS B  88      18.803 -31.158 -41.277  1.00  0.00           H
ATOM   6575  N   ILE B  89      15.815 -26.721 -45.080  1.00  8.90           N
ANISOU 6575  N   ILE B  89      978   1371   1034     98    -53     28       N
ATOM   6576  CA  ILE B  89      16.823 -25.672 -45.290  1.00  9.64           C
ANISOU 6576  CA  ILE B  89     1070   1475   1117     84    -23     21       C
ATOM   6577  C   ILE B  89      16.110 -24.346 -45.523  1.00 10.43           C
ANISOU 6577  C   ILE B  89     1194   1559   1209     70    -43     39       C
ATOM   6578  O   ILE B  89      16.596 -23.304 -45.065  1.00 10.82           O
ANISOU 6578  O   ILE B  89     1231   1617   1265     60    -24     40       O
ATOM   6579  CB  ILE B  89      17.730 -26.012 -46.495  1.00 10.96           C
ANISOU 6579  CB  ILE B  89     1269   1640   1257     68     17     -1       C
ATOM   6580  CG1 ILE B  89      18.633 -27.219 -46.084  1.00 12.29           C
ANISOU 6580  CG1 ILE B  89     1393   1824   1452     93     28    -35       C
ATOM   6581  CG2 ILE B  89      18.564 -24.801 -46.960  1.00 12.37           C
ANISOU 6581  CG2 ILE B  89     1468   1816   1419     30     69    -16       C
ATOM   6582  CD1 ILE B  89      19.326 -27.909 -47.241  1.00 13.22           C
ANISOU 6582  CD1 ILE B  89     1532   1937   1555     80     68    -69       C
ATOM   6583  H   ILE B  89      15.719 -27.465 -45.756  1.00  0.00           H
ATOM   6584  HA  ILE B  89      17.440 -25.590 -44.395  1.00  0.00           H
ATOM   6585  HB  ILE B  89      17.095 -26.327 -47.323  1.00  0.00           H
ATOM   6586 HG12 ILE B  89      19.398 -26.854 -45.398  1.00  0.00           H
ATOM   6587 HG13 ILE B  89      18.018 -27.951 -45.561  1.00  0.00           H
ATOM   6588 HG21 ILE B  89      17.897 -23.984 -47.236  1.00  0.00           H
ATOM   6589 HG22 ILE B  89      19.218 -24.478 -46.150  1.00  0.00           H
ATOM   6590 HG23 ILE B  89      19.167 -25.085 -47.822  1.00  0.00           H
ATOM   6591 HD11 ILE B  89      19.983 -27.201 -47.746  1.00  0.00           H
ATOM   6592 HD12 ILE B  89      19.915 -28.746 -46.865  1.00  0.00           H
ATOM   6593 HD13 ILE B  89      18.579 -28.277 -47.944  1.00  0.00           H
ATOM   6594  N   ASP B  90      15.025 -24.368 -46.283  1.00 11.13           N
ANISOU 6594  N   ASP B  90     1323   1619   1288     73    -89     47       N
ATOM   6595  CA  ASP B  90      14.308 -23.121 -46.580  1.00 13.69           C
ANISOU 6595  CA  ASP B  90     1682   1914   1607     73   -133     55       C
ATOM   6596  C   ASP B  90      13.671 -22.543 -45.295  1.00 13.09           C
ANISOU 6596  C   ASP B  90     1537   1850   1588     84   -145     51       C
ATOM   6597  O   ASP B  90      13.687 -21.334 -45.081  1.00 12.45           O
ANISOU 6597  O   ASP B  90     1464   1760   1508     81   -154     57       O
ATOM   6598  CB  ASP B  90      13.254 -23.342 -47.643  1.00 15.82           C
ANISOU 6598  CB  ASP B  90     2007   2141   1865     89   -205     49       C
ATOM   6599  CG  ASP B  90      13.838 -23.426 -49.046  1.00 18.40           C
ANISOU 6599  CG  ASP B  90     2446   2436   2111     71   -196     56       C
ATOM   6600  OD1 ASP B  90      15.039 -23.143 -49.226  1.00 17.60           O
ANISOU 6600  OD1 ASP B  90     2373   2343   1970     38   -120     60       O
ATOM   6601  OD2 ASP B  90      13.054 -23.752 -49.963  1.00 21.45           O
ANISOU 6601  OD2 ASP B  90     2891   2781   2477     88   -265     49       O
ATOM   6602  H   ASP B  90      14.690 -25.244 -46.659  1.00  0.00           H
ATOM   6603  HA  ASP B  90      15.028 -22.396 -46.959  1.00  0.00           H
ATOM   6604  HB2 ASP B  90      12.547 -22.513 -47.610  1.00  0.00           H
ATOM   6605  HB3 ASP B  90      12.722 -24.268 -47.426  1.00  0.00           H
ATOM   6606  N   LEU B  91      13.135 -23.410 -44.439  1.00 10.68           N
ANISOU 6606  N   LEU B  91     1176   1558   1323     89   -138     38       N
ATOM   6607  CA  LEU B  91      12.626 -22.952 -43.147  1.00  9.27           C
ANISOU 6607  CA  LEU B  91      946   1387   1191     86   -125     27       C
ATOM   6608  C   LEU B  91      13.702 -22.364 -42.226  1.00 10.17           C
ANISOU 6608  C   LEU B  91     1051   1525   1289     81    -87     42       C
ATOM   6609  O   LEU B  91      13.471 -21.276 -41.654  1.00 10.58           O
ANISOU 6609  O   LEU B  91     1085   1576   1361     78    -90     41       O
ATOM   6610  CB  LEU B  91      11.825 -24.046 -42.457  1.00  7.77           C
ANISOU 6610  CB  LEU B  91      725   1192   1036     77   -105      4       C
ATOM   6611  CG  LEU B  91      10.462 -24.266 -43.123  1.00  9.05           C
ANISOU 6611  CG  LEU B  91      862   1326   1249     80   -149    -36       C
ATOM   6612  CD1 LEU B  91       9.855 -25.611 -42.801  1.00 10.04           C
ANISOU 6612  CD1 LEU B  91      972   1444   1401     59   -115    -63       C
ATOM   6613  CD2 LEU B  91       9.423 -23.162 -42.742  1.00 10.98           C
ANISOU 6613  CD2 LEU B  91     1054   1555   1564     84   -177    -77       C
ATOM   6614  H   LEU B  91      13.080 -24.389 -44.683  1.00  0.00           H
ATOM   6615  HA  LEU B  91      11.926 -22.144 -43.360  1.00  0.00           H
ATOM   6616  HB2 LEU B  91      11.667 -23.763 -41.416  1.00  0.00           H
ATOM   6617  HB3 LEU B  91      12.392 -24.977 -42.490  1.00  0.00           H
ATOM   6618  HG  LEU B  91      10.611 -24.221 -44.202  1.00  0.00           H
ATOM   6619 HD11 LEU B  91      10.562 -26.400 -43.058  1.00  0.00           H
ATOM   6620 HD12 LEU B  91       8.938 -25.743 -43.376  1.00  0.00           H
ATOM   6621 HD13 LEU B  91       9.626 -25.661 -41.736  1.00  0.00           H
ATOM   6622 HD21 LEU B  91       9.838 -22.179 -42.965  1.00  0.00           H
ATOM   6623 HD22 LEU B  91       8.509 -23.309 -43.317  1.00  0.00           H
ATOM   6624 HD23 LEU B  91       9.197 -23.228 -41.678  1.00  0.00           H
ATOM   6625  N   TRP B  92      14.862 -23.026 -42.087  1.00 10.36           N
ANISOU 6625  N   TRP B  92     1083   1568   1287     84    -60     47       N
ATOM   6626  CA  TRP B  92      15.950 -22.485 -41.262  1.00 10.81           C
ANISOU 6626  CA  TRP B  92     1123   1643   1342     86    -40     45       C
ATOM   6627  C   TRP B  92      16.516 -21.190 -41.859  1.00 10.95           C
ANISOU 6627  C   TRP B  92     1146   1662   1351     70    -29     47       C
ATOM   6628  O   TRP B  92      16.893 -20.304 -41.127  1.00 10.82           O
ANISOU 6628  O   TRP B  92     1111   1654   1347     66    -21     44       O
ATOM   6629  CB  TRP B  92      17.056 -23.525 -41.039  1.00 10.38           C
ANISOU 6629  CB  TRP B  92     1066   1599   1280    105    -34     30       C
ATOM   6630  CG  TRP B  92      16.658 -24.421 -39.909  1.00 10.47           C
ANISOU 6630  CG  TRP B  92     1097   1594   1286    118    -45     32       C
ATOM   6631  CD1 TRP B  92      16.300 -25.753 -39.957  1.00 10.84           C
ANISOU 6631  CD1 TRP B  92     1176   1622   1319    124    -50     32       C
ATOM   6632  CD2 TRP B  92      16.506 -24.007 -38.541  1.00 11.29           C
ANISOU 6632  CD2 TRP B  92     1213   1688   1388    118    -46     34       C
ATOM   6633  NE1 TRP B  92      15.928 -26.167 -38.693  1.00 11.48           N
ANISOU 6633  NE1 TRP B  92     1300   1676   1384    123    -47     35       N
ATOM   6634  CE2 TRP B  92      16.046 -25.116 -37.814  1.00 12.24           C
ANISOU 6634  CE2 TRP B  92     1388   1777   1485    119    -44     36       C
ATOM   6635  CE3 TRP B  92      16.721 -22.782 -37.867  1.00 11.60           C
ANISOU 6635  CE3 TRP B  92     1233   1737   1438    114    -44     33       C
ATOM   6636  CZ2 TRP B  92      15.813 -25.062 -36.423  1.00 13.28           C
ANISOU 6636  CZ2 TRP B  92     1574   1880   1593    111    -35     37       C
ATOM   6637  CZ3 TRP B  92      16.466 -22.718 -36.475  1.00 11.92           C
ANISOU 6637  CZ3 TRP B  92     1311   1756   1463    112    -42     34       C
ATOM   6638  CH2 TRP B  92      16.034 -23.862 -35.777  1.00 12.67           C
ANISOU 6638  CH2 TRP B  92     1477   1814   1524    109    -36     36       C
ATOM   6639  H   TRP B  92      14.988 -23.911 -42.558  1.00  0.00           H
ATOM   6640  HA  TRP B  92      15.530 -22.240 -40.287  1.00  0.00           H
ATOM   6641  HB2 TRP B  92      17.990 -23.019 -40.793  1.00  0.00           H
ATOM   6642  HB3 TRP B  92      17.189 -24.117 -41.945  1.00  0.00           H
ATOM   6643  HD1 TRP B  92      16.309 -26.373 -40.842  1.00  0.00           H
ATOM   6644  HE3 TRP B  92      17.073 -21.913 -38.403  1.00  0.00           H
ATOM   6645  HZ2 TRP B  92      15.473 -25.932 -35.881  1.00  0.00           H
ATOM   6646  HZ3 TRP B  92      16.604 -21.786 -35.946  1.00  0.00           H
ATOM   6647  HH2 TRP B  92      15.872 -23.799 -34.711  1.00  0.00           H
ATOM   6648  HE1 TRP B  92      15.617 -27.097 -38.452  1.00  0.00           H
ATOM   6649  N   SER B  93      16.582 -21.101 -43.182  1.00 10.71           N
ANISOU 6649  N   SER B  93     1160   1617   1293     56    -26     49       N
ATOM   6650  CA  SER B  93      17.129 -19.898 -43.841  1.00 11.78           C
ANISOU 6650  CA  SER B  93     1337   1737   1403     27     -2     50       C
ATOM   6651  C   SER B  93      16.182 -18.721 -43.549  1.00 11.35           C
ANISOU 6651  C   SER B  93     1297   1660   1357     33    -43     66       C
ATOM   6652  O   SER B  93      16.640 -17.571 -43.310  1.00 11.26           O
ANISOU 6652  O   SER B  93     1294   1643   1342     15    -24     67       O
ATOM   6653  CB  SER B  93      17.276 -20.119 -45.359  1.00 12.84           C
ANISOU 6653  CB  SER B  93     1552   1841   1484      5     13     50       C
ATOM   6654  OG  SER B  93      18.172 -21.204 -45.630  1.00 12.20           O
ANISOU 6654  OG  SER B  93     1447   1781   1406      0     57     24       O
ATOM   6655  H   SER B  93      16.252 -21.870 -43.748  1.00  0.00           H
ATOM   6656  HA  SER B  93      18.109 -19.677 -43.418  1.00  0.00           H
ATOM   6657  HB2 SER B  93      17.667 -19.210 -45.816  1.00  0.00           H
ATOM   6658  HB3 SER B  93      16.299 -20.345 -45.786  1.00  0.00           H
ATOM   6659  HG  SER B  93      17.685 -22.031 -45.623  1.00  0.00           H
ATOM   6660  N   TYR B  94      14.888 -19.006 -43.585  1.00 10.27           N
ANISOU 6660  N   TYR B  94     1157   1506   1241     57    -98     69       N
ATOM   6661  CA  TYR B  94      13.870 -17.985 -43.226  1.00 10.60           C
ANISOU 6661  CA  TYR B  94     1190   1524   1314     71   -147     65       C
ATOM   6662  C   TYR B  94      14.039 -17.591 -41.736  1.00 12.06           C
ANISOU 6662  C   TYR B  94     1308   1739   1537     69   -115     58       C
ATOM   6663  O   TYR B  94      14.019 -16.405 -41.383  1.00 11.82           O
ANISOU 6663  O   TYR B  94     1279   1697   1514     66   -122     59       O
ATOM   6664  CB  TYR B  94      12.440 -18.526 -43.445  1.00 10.27           C
ANISOU 6664  CB  TYR B  94     1125   1461   1317     98   -208     40       C
ATOM   6665  CG  TYR B  94      11.421 -17.515 -42.960  1.00 11.18           C
ANISOU 6665  CG  TYR B  94     1206   1552   1489    117   -256     13       C
ATOM   6666  CD1 TYR B  94      10.998 -16.491 -43.783  1.00 14.99           C
ANISOU 6666  CD1 TYR B  94     1752   1981   1961    140   -334     10       C
ATOM   6667  CD2 TYR B  94      10.932 -17.573 -41.673  1.00  9.80           C
ANISOU 6667  CD2 TYR B  94      949   1399   1376    111   -221    -13       C
ATOM   6668  CE1 TYR B  94      10.052 -15.547 -43.342  1.00 16.80           C
ANISOU 6668  CE1 TYR B  94     1943   2184   2257    167   -391    -27       C
ATOM   6669  CE2 TYR B  94      10.022 -16.659 -41.211  1.00 10.91           C
ANISOU 6669  CE2 TYR B  94     1047   1518   1579    125   -254    -51       C
ATOM   6670  CZ  TYR B  94       9.600 -15.619 -42.046  1.00 15.17           C
ANISOU 6670  CZ  TYR B  94     1631   2010   2124    158   -344    -61       C
ATOM   6671  OH  TYR B  94       8.675 -14.698 -41.581  1.00 17.82           O
ANISOU 6671  OH  TYR B  94     1916   2320   2537    182   -388   -111       O
ATOM   6672  H   TYR B  94      14.590 -19.931 -43.861  1.00  0.00           H
ATOM   6673  HA  TYR B  94      14.016 -17.102 -43.847  1.00  0.00           H
ATOM   6674  HB2 TYR B  94      12.318 -19.456 -42.890  1.00  0.00           H
ATOM   6675  HB3 TYR B  94      12.284 -18.716 -44.507  1.00  0.00           H
ATOM   6676  HD1 TYR B  94      11.400 -16.413 -44.782  1.00  0.00           H
ATOM   6677  HD2 TYR B  94      11.274 -18.357 -41.013  1.00  0.00           H
ATOM   6678  HE1 TYR B  94       9.688 -14.780 -44.010  1.00  0.00           H
ATOM   6679  HE2 TYR B  94       9.632 -16.741 -40.207  1.00  0.00           H
ATOM   6680  HH  TYR B  94       8.373 -14.960 -40.708  1.00  0.00           H
ATOM   6681  N   ASN B  95      14.218 -18.571 -40.851  1.00 10.42           N
ANISOU 6681  N   ASN B  95     1059   1559   1342     69    -83     52       N
ATOM   6682  CA  ASN B  95      14.378 -18.250 -39.415  1.00 10.79           C
ANISOU 6682  CA  ASN B  95     1072   1620   1407     66    -58     46       C
ATOM   6683  C   ASN B  95      15.625 -17.353 -39.219  1.00 11.96           C
ANISOU 6683  C   ASN B  95     1223   1783   1538     58    -40     52       C
ATOM   6684  O   ASN B  95      15.593 -16.388 -38.464  1.00 12.17           O
ANISOU 6684  O   ASN B  95     1236   1808   1578     54    -38     49       O
ATOM   6685  CB  ASN B  95      14.548 -19.515 -38.577  1.00  9.73           C
ANISOU 6685  CB  ASN B  95      935   1496   1265     68    -35     42       C
ATOM   6686  CG  ASN B  95      13.263 -20.302 -38.456  1.00 10.07           C
ANISOU 6686  CG  ASN B  95      972   1521   1334     60    -29     25       C
ATOM   6687  OD1 ASN B  95      12.160 -19.745 -38.596  1.00 10.18           O
ANISOU 6687  OD1 ASN B  95      956   1519   1393     56    -42      1       O
ATOM   6688  ND2 ASN B  95      13.387 -21.572 -38.078  1.00  9.79           N
ANISOU 6688  ND2 ASN B  95      962   1481   1277     57    -10     25       N
ATOM   6689  H   ASN B  95      14.244 -19.532 -41.160  1.00  0.00           H
ATOM   6690  HA  ASN B  95      13.495 -17.711 -39.071  1.00  0.00           H
ATOM   6691  HB2 ASN B  95      14.880 -19.231 -37.578  1.00  0.00           H
ATOM   6692  HB3 ASN B  95      15.308 -20.146 -39.038  1.00  0.00           H
ATOM   6693 HD21 ASN B  95      12.564 -22.139 -37.935  1.00  0.00           H
ATOM   6694 HD22 ASN B  95      14.305 -21.969 -37.934  1.00  0.00           H
ATOM   6695  N   ALA B  96      16.685 -17.650 -39.939  1.00 10.73           N
ANISOU 6695  N   ALA B  96     1080   1636   1359     50    -22     50       N
ATOM   6696  CA  ALA B  96      17.947 -16.928 -39.788  1.00 10.94           C
ANISOU 6696  CA  ALA B  96     1094   1675   1388     34      7     33       C
ATOM   6697  C   ALA B  96      17.755 -15.473 -40.279  1.00 11.23           C
ANISOU 6697  C   ALA B  96     1168   1687   1413      9     12     44       C
ATOM   6698  O   ALA B  96      18.195 -14.521 -39.622  1.00 11.33           O
ANISOU 6698  O   ALA B  96     1162   1703   1439     -1     25     35       O
ATOM   6699  CB  ALA B  96      19.101 -17.633 -40.547  1.00 11.33           C
ANISOU 6699  CB  ALA B  96     1137   1736   1432     23     40      6       C
ATOM   6700  H   ALA B  96      16.625 -18.398 -40.615  1.00  0.00           H
ATOM   6701  HA  ALA B  96      18.201 -16.901 -38.728  1.00  0.00           H
ATOM   6702  HB1 ALA B  96      18.924 -18.708 -40.561  1.00  0.00           H
ATOM   6703  HB2 ALA B  96      19.145 -17.259 -41.570  1.00  0.00           H
ATOM   6704  HB3 ALA B  96      20.046 -17.427 -40.044  1.00  0.00           H
ATOM   6705  N   GLU B  97      17.118 -15.302 -41.425  1.00 12.50           N
ANISOU 6705  N   GLU B  97     1393   1813   1543      2     -6     61       N
ATOM   6706  CA  GLU B  97      16.871 -13.983 -41.994  1.00 13.97           C
ANISOU 6706  CA  GLU B  97     1650   1955   1704    -15    -19     73       C
ATOM   6707  C   GLU B  97      16.035 -13.106 -41.047  1.00 12.96           C
ANISOU 6707  C   GLU B  97     1490   1820   1613      9    -60     75       C
ATOM   6708  O   GLU B  97      16.384 -11.940 -40.770  1.00 12.88           O
ANISOU 6708  O   GLU B  97     1497   1796   1600     -9    -47     74       O
ATOM   6709  CB  GLU B  97      16.148 -14.102 -43.327  1.00 13.69           C
ANISOU 6709  CB  GLU B  97     1709   1869   1624     -9    -63     88       C
ATOM   6710  CG  GLU B  97      16.201 -12.823 -44.190  1.00 15.03           C
ANISOU 6710  CG  GLU B  97     2005   1970   1735    -34    -73    101       C
ATOM   6711  CD  GLU B  97      17.595 -12.486 -44.783  1.00 18.19           C
ANISOU 6711  CD  GLU B  97     2468   2359   2085   -105     30     92       C
ATOM   6712  OE1 GLU B  97      18.355 -13.406 -45.169  1.00 18.54           O
ANISOU 6712  OE1 GLU B  97     2493   2430   2123   -129     92     73       O
ATOM   6713  OE2 GLU B  97      17.931 -11.261 -44.924  1.00 18.81           O
ANISOU 6713  OE2 GLU B  97     2622   2394   2130   -141     55     95       O
ATOM   6714  H   GLU B  97      16.790 -16.116 -41.925  1.00  0.00           H
ATOM   6715  HA  GLU B  97      17.830 -13.494 -42.163  1.00  0.00           H
ATOM   6716  HB2 GLU B  97      16.604 -14.915 -43.892  1.00  0.00           H
ATOM   6717  HB3 GLU B  97      15.104 -14.352 -43.137  1.00  0.00           H
ATOM   6718  HG2 GLU B  97      15.503 -12.945 -45.018  1.00  0.00           H
ATOM   6719  HG3 GLU B  97      15.871 -11.981 -43.581  1.00  0.00           H
ATOM   6720  N   LEU B  98      14.965 -13.693 -40.534  1.00 10.19           N
ANISOU 6720  N   LEU B  98     1092   1478   1302     41    -97     67       N
ATOM   6721  CA  LEU B  98      14.047 -12.977 -39.672  1.00 11.46           C
ANISOU 6721  CA  LEU B  98     1215   1629   1510     59   -126     52       C
ATOM   6722  C   LEU B  98      14.695 -12.643 -38.338  1.00 12.07           C
ANISOU 6722  C   LEU B  98     1247   1739   1600     46    -81     47       C
ATOM   6723  O   LEU B  98      14.488 -11.561 -37.793  1.00 11.93           O
ANISOU 6723  O   LEU B  98     1223   1710   1602     47    -88     41       O
ATOM   6724  CB  LEU B  98      12.776 -13.791 -39.457  1.00 12.47           C
ANISOU 6724  CB  LEU B  98     1295   1756   1688     81   -153     26       C
ATOM   6725  CG  LEU B  98      11.747 -13.119 -38.538  1.00 13.47           C
ANISOU 6725  CG  LEU B  98     1366   1870   1881     93   -165    -12       C
ATOM   6726  CD1 LEU B  98      11.154 -11.851 -39.170  1.00 14.51           C
ANISOU 6726  CD1 LEU B  98     1529   1952   2033    120   -241    -25       C
ATOM   6727  CD2 LEU B  98      10.614 -14.087 -38.108  1.00 16.83           C
ANISOU 6727  CD2 LEU B  98     1729   2298   2367     94   -153    -57       C
ATOM   6728  H   LEU B  98      14.784 -14.663 -40.749  1.00  0.00           H
ATOM   6729  HA  LEU B  98      13.775 -12.043 -40.163  1.00  0.00           H
ATOM   6730  HB2 LEU B  98      13.054 -14.749 -39.016  1.00  0.00           H
ATOM   6731  HB3 LEU B  98      12.311 -13.974 -40.426  1.00  0.00           H
ATOM   6732  HG  LEU B  98      12.272 -12.814 -37.633  1.00  0.00           H
ATOM   6733 HD11 LEU B  98      11.961 -11.181 -39.467  1.00  0.00           H
ATOM   6734 HD12 LEU B  98      10.514 -11.349 -38.445  1.00  0.00           H
ATOM   6735 HD13 LEU B  98      10.566 -12.123 -40.047  1.00  0.00           H
ATOM   6736 HD21 LEU B  98      11.049 -14.981 -37.662  1.00  0.00           H
ATOM   6737 HD22 LEU B  98      10.025 -14.367 -38.981  1.00  0.00           H
ATOM   6738 HD23 LEU B  98       9.971 -13.593 -37.379  1.00  0.00           H
ATOM   6739  N   LEU B  99      15.467 -13.579 -37.803  1.00 11.44           N
ANISOU 6739  N   LEU B  99     1144   1694   1510     41    -47     47       N
ATOM   6740  CA  LEU B  99      16.095 -13.410 -36.500  1.00 12.20           C
ANISOU 6740  CA  LEU B  99     1212   1811   1612     39    -25     37       C
ATOM   6741  C   LEU B  99      17.048 -12.189 -36.562  1.00 11.83           C
ANISOU 6741  C   LEU B  99     1170   1763   1561     20    -12     33       C
ATOM   6742  O   LEU B  99      16.991 -11.320 -35.672  1.00 11.77           O
ANISOU 6742  O   LEU B  99     1151   1754   1569     19    -12     26       O
ATOM   6743  CB  LEU B  99      16.949 -14.618 -36.133  1.00 13.19           C
ANISOU 6743  CB  LEU B  99     1331   1959   1723     47    -16     30       C
ATOM   6744  CG  LEU B  99      17.720 -14.510 -34.825  1.00 14.78           C
ANISOU 6744  CG  LEU B  99     1524   2170   1923     56    -20     13       C
ATOM   6745  CD1 LEU B  99      16.832 -14.301 -33.650  1.00 14.40           C
ANISOU 6745  CD1 LEU B  99     1493   2106   1873     55    -15     13       C
ATOM   6746  CD2 LEU B  99      18.583 -15.755 -34.613  1.00 17.40           C
ANISOU 6746  CD2 LEU B  99     1860   2509   2243     80    -38     -2       C
ATOM   6747  H   LEU B  99      15.624 -14.435 -38.315  1.00  0.00           H
ATOM   6748  HA  LEU B  99      15.333 -13.248 -35.738  1.00  0.00           H
ATOM   6749  HB2 LEU B  99      16.291 -15.484 -36.063  1.00  0.00           H
ATOM   6750  HB3 LEU B  99      17.662 -14.792 -36.939  1.00  0.00           H
ATOM   6751  HG  LEU B  99      18.386 -13.650 -34.899  1.00  0.00           H
ATOM   6752 HD11 LEU B  99      16.221 -13.413 -33.809  1.00  0.00           H
ATOM   6753 HD12 LEU B  99      16.185 -15.169 -33.525  1.00  0.00           H
ATOM   6754 HD13 LEU B  99      17.439 -14.169 -32.755  1.00  0.00           H
ATOM   6755 HD21 LEU B  99      19.230 -15.901 -35.478  1.00  0.00           H
ATOM   6756 HD22 LEU B  99      17.940 -16.626 -34.490  1.00  0.00           H
ATOM   6757 HD23 LEU B  99      19.194 -15.626 -33.720  1.00  0.00           H
ATOM   6758  N   VAL B 100      17.898 -12.115 -37.574  1.00 11.64           N
ANISOU 6758  N   VAL B 100     1167   1736   1519     -2      9     31       N
ATOM   6759  CA  VAL B 100      18.816 -10.964 -37.591  1.00 14.70           C
ANISOU 6759  CA  VAL B 100     1561   2117   1909    -34     40     16       C
ATOM   6760  C   VAL B 100      18.088  -9.653 -37.887  1.00 13.59           C
ANISOU 6760  C   VAL B 100     1474   1934   1756    -43     23     35       C
ATOM   6761  O   VAL B 100      18.472  -8.606 -37.323  1.00 14.80           O
ANISOU 6761  O   VAL B 100     1620   2081   1920    -59     36     24       O
ATOM   6762  CB  VAL B 100      20.021 -11.110 -38.513  1.00 21.00           C
ANISOU 6762  CB  VAL B 100     2367   2915   2697    -74     95    -10       C
ATOM   6763  CG1 VAL B 100      20.743 -12.426 -38.236  1.00 23.13           C
ANISOU 6763  CG1 VAL B 100     2576   3221   2991    -53     96    -42       C
ATOM   6764  CG2 VAL B 100      19.648 -10.994 -39.945  1.00 23.75           C
ANISOU 6764  CG2 VAL B 100     2806   3223   2997    -99    109     13       C
ATOM   6765  H   VAL B 100      17.916 -12.816 -38.301  1.00  0.00           H
ATOM   6766  HA  VAL B 100      19.213 -10.873 -36.580  1.00  0.00           H
ATOM   6767  HB  VAL B 100      20.712 -10.299 -38.285  1.00  0.00           H
ATOM   6768 HG11 VAL B 100      21.601 -12.517 -38.902  1.00  0.00           H
ATOM   6769 HG12 VAL B 100      21.083 -12.443 -37.201  1.00  0.00           H
ATOM   6770 HG13 VAL B 100      20.060 -13.258 -38.408  1.00  0.00           H
ATOM   6771 HG21 VAL B 100      19.135 -10.047 -40.112  1.00  0.00           H
ATOM   6772 HG22 VAL B 100      20.548 -11.033 -40.559  1.00  0.00           H
ATOM   6773 HG23 VAL B 100      18.987 -11.817 -40.216  1.00  0.00           H
ATOM   6774  N   ALA B 101      17.068  -9.682 -38.738  1.00 12.05           N
ANISOU 6774  N   ALA B 101     1333   1703   1542    -28    -17     56       N
ATOM   6775  CA  ALA B 101      16.282  -8.448 -38.954  1.00 11.56           C
ANISOU 6775  CA  ALA B 101     1327   1589   1477    -19    -61     65       C
ATOM   6776  C   ALA B 101      15.652  -7.904 -37.668  1.00 11.14           C
ANISOU 6776  C   ALA B 101     1210   1548   1475      5    -81     50       C
ATOM   6777  O   ALA B 101      15.709  -6.691 -37.400  1.00 10.59           O
ANISOU 6777  O   ALA B 101     1163   1453   1408     -2    -86     48       O
ATOM   6778  CB  ALA B 101      15.208  -8.666 -40.021  1.00 12.25           C
ANISOU 6778  CB  ALA B 101     1477   1629   1548     10   -130     75       C
ATOM   6779  H   ALA B 101      16.833 -10.533 -39.229  1.00  0.00           H
ATOM   6780  HA  ALA B 101      16.966  -7.687 -39.330  1.00  0.00           H
ATOM   6781  HB1 ALA B 101      15.632  -9.226 -40.854  1.00  0.00           H
ATOM   6782  HB2 ALA B 101      14.849  -7.700 -40.378  1.00  0.00           H
ATOM   6783  HB3 ALA B 101      14.377  -9.226 -39.591  1.00  0.00           H
ATOM   6784  N   LEU B 102      15.032  -8.780 -36.871  1.00 11.98           N
ANISOU 6784  N   LEU B 102     1249   1686   1617     28    -84     36       N
ATOM   6785  CA  LEU B 102      14.345  -8.401 -35.643  1.00 13.04           C
ANISOU 6785  CA  LEU B 102     1333   1826   1796     41    -85     13       C
ATOM   6786  C   LEU B 102      15.339  -7.949 -34.591  1.00 13.60           C
ANISOU 6786  C   LEU B 102     1388   1922   1857     22    -46     10       C
ATOM   6787  O   LEU B 102      15.110  -6.953 -33.860  1.00 13.95           O
ANISOU 6787  O   LEU B 102     1425   1955   1921     22    -48     -3       O
ATOM   6788  CB  LEU B 102      13.540  -9.590 -35.058  1.00 12.97           C
ANISOU 6788  CB  LEU B 102     1278   1835   1813     51    -71     -7       C
ATOM   6789  CG  LEU B 102      12.334 -10.068 -35.869  1.00 13.70           C
ANISOU 6789  CG  LEU B 102     1358   1904   1942     72   -112    -28       C
ATOM   6790  CD1 LEU B 102      11.781 -11.349 -35.249  1.00 13.53           C
ANISOU 6790  CD1 LEU B 102     1298   1901   1941     63    -71    -50       C
ATOM   6791  CD2 LEU B 102      11.217  -8.990 -35.919  1.00 20.45           C
ANISOU 6791  CD2 LEU B 102     2194   2717   2861     99   -164    -68       C
ATOM   6792  H   LEU B 102      15.040  -9.755 -37.134  1.00  0.00           H
ATOM   6793  HA  LEU B 102      13.660  -7.581 -35.859  1.00  0.00           H
ATOM   6794  HB2 LEU B 102      14.224 -10.433 -34.955  1.00  0.00           H
ATOM   6795  HB3 LEU B 102      13.192  -9.310 -34.064  1.00  0.00           H
ATOM   6796  HG  LEU B 102      12.659 -10.283 -36.887  1.00  0.00           H
ATOM   6797 HD11 LEU B 102      10.922 -11.691 -35.826  1.00  0.00           H
ATOM   6798 HD12 LEU B 102      12.553 -12.119 -35.257  1.00  0.00           H
ATOM   6799 HD13 LEU B 102      11.474 -11.152 -34.222  1.00  0.00           H
ATOM   6800 HD21 LEU B 102      11.613  -8.076 -36.362  1.00  0.00           H
ATOM   6801 HD22 LEU B 102      10.868  -8.782 -34.908  1.00  0.00           H
ATOM   6802 HD23 LEU B 102      10.386  -9.356 -36.522  1.00  0.00           H
ATOM   6803  N   GLU B 103      16.423  -8.714 -34.447  1.00 12.02           N
ANISOU 6803  N   GLU B 103     1180   1753   1633     10    -21     14       N
ATOM   6804  CA  GLU B 103      17.455  -8.408 -33.466  1.00 11.44           C
ANISOU 6804  CA  GLU B 103     1088   1699   1559      1     -5     -2       C
ATOM   6805  C   GLU B 103      18.080  -7.043 -33.790  1.00 11.31           C
ANISOU 6805  C   GLU B 103     1086   1666   1546    -25      6     -7       C
ATOM   6806  O   GLU B 103      18.317  -6.244 -32.889  1.00 12.24           O
ANISOU 6806  O   GLU B 103     1191   1784   1677    -29      8    -22       O
ATOM   6807  CB  GLU B 103      18.582  -9.473 -33.509  1.00 10.84           C
ANISOU 6807  CB  GLU B 103      995   1651   1473      4      0    -15       C
ATOM   6808  CG  GLU B 103      18.162 -10.851 -32.992  1.00 14.72           C
ANISOU 6808  CG  GLU B 103     1492   2150   1950     29    -13    -11       C
ATOM   6809  CD  GLU B 103      18.269 -11.000 -31.491  1.00 20.64           C
ANISOU 6809  CD  GLU B 103     2259   2897   2687     43    -26    -25       C
ATOM   6810  OE1 GLU B 103      18.483  -9.953 -30.847  1.00 23.12           O
ANISOU 6810  OE1 GLU B 103     2568   3207   3010     36    -27    -37       O
ATOM   6811  OE2 GLU B 103      18.149 -12.160 -30.948  1.00 21.63           O
ANISOU 6811  OE2 GLU B 103     2418   3015   2784     59    -37    -24       O
ATOM   6812  H   GLU B 103      16.531  -9.528 -35.035  1.00  0.00           H
ATOM   6813  HA  GLU B 103      17.015  -8.381 -32.469  1.00  0.00           H
ATOM   6814  HB2 GLU B 103      19.412  -9.117 -32.899  1.00  0.00           H
ATOM   6815  HB3 GLU B 103      18.925  -9.576 -34.538  1.00  0.00           H
ATOM   6816  HG2 GLU B 103      17.126 -11.025 -33.281  1.00  0.00           H
ATOM   6817  HG3 GLU B 103      18.789 -11.608 -33.464  1.00  0.00           H
ATOM   6818  N   ASN B 104      18.380  -6.816 -35.068  1.00 10.26           N
ANISOU 6818  N   ASN B 104      991   1512   1394    -49     21      3       N
ATOM   6819  CA  ASN B 104      19.083  -5.604 -35.475  1.00 10.18           C
ANISOU 6819  CA  ASN B 104     1018   1475   1376    -90     51     -5       C
ATOM   6820  C   ASN B 104      18.177  -4.355 -35.324  1.00 12.11           C
ANISOU 6820  C   ASN B 104     1305   1675   1621    -80     18      9       C
ATOM   6821  O   ASN B 104      18.632  -3.292 -34.848  1.00 13.38           O
ANISOU 6821  O   ASN B 104     1469   1823   1790   -102     34     -4       O
ATOM   6822  CB  ASN B 104      19.597  -5.745 -36.876  1.00  9.94           C
ANISOU 6822  CB  ASN B 104     1048   1419   1310   -130     89     -1       C
ATOM   6823  CG  ASN B 104      20.750  -6.765 -36.964  1.00 10.99           C
ANISOU 6823  CG  ASN B 104     1120   1593   1461   -147    133    -38       C
ATOM   6824  OD1 ASN B 104      21.308  -7.172 -35.937  1.00 12.48           O
ANISOU 6824  OD1 ASN B 104     1229   1822   1690   -126    122    -70       O
ATOM   6825  ND2 ASN B 104      21.127  -7.118 -38.166  1.00 10.57           N
ANISOU 6825  ND2 ASN B 104     1116   1523   1380   -182    178    -41       N
ATOM   6826  H   ASN B 104      18.116  -7.495 -35.768  1.00  0.00           H
ATOM   6827  HA  ASN B 104      19.941  -5.477 -34.815  1.00  0.00           H
ATOM   6828  HB2 ASN B 104      19.957  -4.775 -37.219  1.00  0.00           H
ATOM   6829  HB3 ASN B 104      18.783  -6.071 -37.523  1.00  0.00           H
ATOM   6830 HD21 ASN B 104      21.892  -7.767 -38.285  1.00  0.00           H
ATOM   6831 HD22 ASN B 104      20.653  -6.742 -38.975  1.00  0.00           H
ATOM   6832  N   GLN B 105      16.902  -4.508 -35.664  1.00 12.29           N
ANISOU 6832  N   GLN B 105     1350   1674   1647    -43    -34     25       N
ATOM   6833  CA  GLN B 105      15.944  -3.409 -35.466  1.00 14.00           C
ANISOU 6833  CA  GLN B 105     1591   1845   1884    -19    -82     21       C
ATOM   6834  C   GLN B 105      15.937  -3.040 -33.975  1.00 14.69           C
ANISOU 6834  C   GLN B 105     1610   1963   2009    -14    -65     -2       C
ATOM   6835  O   GLN B 105      15.940  -1.856 -33.587  1.00 15.46           O
ANISOU 6835  O   GLN B 105     1724   2034   2117    -19    -71    -11       O
ATOM   6836  CB  GLN B 105      14.527  -3.763 -35.906  1.00 15.23           C
ANISOU 6836  CB  GLN B 105     1747   1974   2066     30   -150     14       C
ATOM   6837  CG  GLN B 105      13.607  -2.533 -36.018  1.00 17.45           C
ANISOU 6837  CG  GLN B 105     2065   2189   2374     63   -220     -3       C
ATOM   6838  CD  GLN B 105      13.719  -1.796 -37.360  1.00 22.37           C
ANISOU 6838  CD  GLN B 105     2830   2732   2938     61   -271     23       C
ATOM   6839  OE1 GLN B 105      14.025  -2.380 -38.401  1.00 21.53           O
ANISOU 6839  OE1 GLN B 105     2792   2610   2777     46   -269     47       O
ATOM   6840  NE2 GLN B 105      13.421  -0.500 -37.338  1.00 27.29           N
ANISOU 6840  NE2 GLN B 105     3512   3292   3564     76   -319     15       N
ATOM   6841  H   GLN B 105      16.589  -5.383 -36.060  1.00  0.00           H
ATOM   6842  HA  GLN B 105      16.281  -2.545 -36.038  1.00  0.00           H
ATOM   6843  HB2 GLN B 105      14.099  -4.452 -35.177  1.00  0.00           H
ATOM   6844  HB3 GLN B 105      14.572  -4.259 -36.876  1.00  0.00           H
ATOM   6845  HG2 GLN B 105      13.866  -1.836 -35.221  1.00  0.00           H
ATOM   6846  HG3 GLN B 105      12.575  -2.854 -35.880  1.00  0.00           H
ATOM   6847 HE21 GLN B 105      13.158  -0.057 -36.469  1.00  0.00           H
ATOM   6848 HE22 GLN B 105      13.458   0.041 -38.190  1.00  0.00           H
ATOM   6849  N   HIS B 106      15.895  -4.063 -33.150  1.00 14.67           N
ANISOU 6849  N   HIS B 106     1548   2006   2019     -4    -46    -13       N
ATOM   6850  CA  HIS B 106      15.839  -3.872 -31.717  1.00 14.29           C
ANISOU 6850  CA  HIS B 106     1463   1977   1990     -2    -29    -35       C
ATOM   6851  C   HIS B 106      17.141  -3.317 -31.110  1.00 12.98           C
ANISOU 6851  C   HIS B 106     1295   1826   1811    -26     -8    -43       C
ATOM   6852  O   HIS B 106      17.085  -2.539 -30.183  1.00 12.56           O
ANISOU 6852  O   HIS B 106     1236   1767   1769    -27     -6    -60       O
ATOM   6853  CB  HIS B 106      15.456  -5.189 -31.056  1.00 14.19           C
ANISOU 6853  CB  HIS B 106     1426   1991   1975      8    -12    -43       C
ATOM   6854  CG  HIS B 106      15.408  -5.104 -29.583  1.00 14.62           C
ANISOU 6854  CG  HIS B 106     1476   2052   2026      3     12    -65       C
ATOM   6855  ND1 HIS B 106      16.406  -5.627 -28.784  1.00 15.03           N
ANISOU 6855  ND1 HIS B 106     1546   2123   2043      0     14    -66       N
ATOM   6856  CD2 HIS B 106      14.504  -4.534 -28.747  1.00 16.00           C
ANISOU 6856  CD2 HIS B 106     1643   2208   2228      2     31    -95       C
ATOM   6857  CE1 HIS B 106      16.115  -5.383 -27.516  1.00 16.80           C
ANISOU 6857  CE1 HIS B 106     1792   2336   2256     -4     32    -86       C
ATOM   6858  NE2 HIS B 106      14.971  -4.726 -27.466  1.00 17.18           N
ANISOU 6858  NE2 HIS B 106     1823   2364   2342     -9     54   -104       N
ATOM   6859  H   HIS B 106      15.902  -5.001 -33.524  1.00  0.00           H
ATOM   6860  HA  HIS B 106      15.045  -3.155 -31.510  1.00  0.00           H
ATOM   6861  HB2 HIS B 106      16.190  -5.944 -31.336  1.00  0.00           H
ATOM   6862  HB3 HIS B 106      14.477  -5.496 -31.423  1.00  0.00           H
ATOM   6863  HD2 HIS B 106      13.594  -4.027 -29.031  1.00  0.00           H
ATOM   6864  HE1 HIS B 106      16.713  -5.673 -26.665  1.00  0.00           H
ATOM   6865  HE2 HIS B 106      14.512  -4.414 -26.622  1.00  0.00           H
ATOM   6866  N   THR B 107      18.296  -3.702 -31.646  1.00 12.21           N
ANISOU 6866  N   THR B 107     1196   1746   1698    -47      7    -43       N
ATOM   6867  CA  THR B 107      19.584  -3.179 -31.179  1.00 13.47           C
ANISOU 6867  CA  THR B 107     1333   1917   1867    -71     24    -72       C
ATOM   6868  C   THR B 107      19.697  -1.705 -31.487  1.00 12.61           C
ANISOU 6868  C   THR B 107     1257   1771   1763   -102     39    -74       C
ATOM   6869  O   THR B 107      20.190  -0.910 -30.643  1.00 12.56           O
ANISOU 6869  O   THR B 107     1233   1765   1773   -113     42   -100       O
ATOM   6870  CB  THR B 107      20.761  -3.936 -31.800  1.00 14.04           C
ANISOU 6870  CB  THR B 107     1378   2011   1944    -89     44    -95       C
ATOM   6871  OG1 THR B 107      20.710  -5.264 -31.264  1.00 12.79           O
ANISOU 6871  OG1 THR B 107     1197   1880   1781    -51     16    -97       O
ATOM   6872  CG2 THR B 107      22.119  -3.269 -31.458  1.00 10.90           C
ANISOU 6872  CG2 THR B 107      940   1620   1583   -121     65   -150       C
ATOM   6873  H   THR B 107      18.286  -4.376 -32.398  1.00  0.00           H
ATOM   6874  HA  THR B 107      19.631  -3.305 -30.097  1.00  0.00           H
ATOM   6875  HB  THR B 107      20.638  -3.976 -32.882  1.00  0.00           H
ATOM   6876  HG1 THR B 107      20.987  -5.891 -31.936  1.00  0.00           H
ATOM   6877 HG21 THR B 107      22.443  -2.652 -32.296  1.00  0.00           H
ATOM   6878 HG22 THR B 107      22.864  -4.041 -31.266  1.00  0.00           H
ATOM   6879 HG23 THR B 107      22.004  -2.645 -30.571  1.00  0.00           H
ATOM   6880  N   ILE B 108      19.231  -1.315 -32.655  1.00 11.33           N
ANISOU 6880  N   ILE B 108     1156   1569   1580   -115     42    -48       N
ATOM   6881  CA  ILE B 108      19.226   0.105 -33.003  1.00 12.93           C
ANISOU 6881  CA  ILE B 108     1423   1718   1773   -143     48    -45       C
ATOM   6882  C   ILE B 108      18.290   0.883 -32.073  1.00 12.84           C
ANISOU 6882  C   ILE B 108     1402   1691   1785   -107      8    -47       C
ATOM   6883  O   ILE B 108      18.654   1.962 -31.545  1.00 12.53           O
ANISOU 6883  O   ILE B 108     1371   1635   1756   -127     19    -63       O
ATOM   6884  CB  ILE B 108      18.873   0.278 -34.491  1.00 14.39           C
ANISOU 6884  CB  ILE B 108     1712   1844   1912   -157     43    -15       C
ATOM   6885  CG1 ILE B 108      20.059  -0.171 -35.321  1.00 15.40           C
ANISOU 6885  CG1 ILE B 108     1857   1978   2017   -217    115    -28       C
ATOM   6886  CG2 ILE B 108      18.498   1.736 -34.821  1.00 14.86           C
ANISOU 6886  CG2 ILE B 108     1871   1825   1950   -167     21     -4       C
ATOM   6887  CD1 ILE B 108      19.718  -0.394 -36.765  1.00 17.34           C
ANISOU 6887  CD1 ILE B 108     2215   2171   2203   -230    114      3       C
ATOM   6888  H   ILE B 108      18.877  -1.997 -33.311  1.00  0.00           H
ATOM   6889  HA  ILE B 108      20.236   0.487 -32.854  1.00  0.00           H
ATOM   6890  HB  ILE B 108      18.022  -0.362 -34.724  1.00  0.00           H
ATOM   6891 HG12 ILE B 108      20.833   0.594 -35.262  1.00  0.00           H
ATOM   6892 HG13 ILE B 108      20.449  -1.099 -34.904  1.00  0.00           H
ATOM   6893 HG21 ILE B 108      17.644   2.038 -34.214  1.00  0.00           H
ATOM   6894 HG22 ILE B 108      19.345   2.387 -34.605  1.00  0.00           H
ATOM   6895 HG23 ILE B 108      18.239   1.815 -35.877  1.00  0.00           H
ATOM   6896 HD11 ILE B 108      20.610  -0.714 -37.304  1.00  0.00           H
ATOM   6897 HD12 ILE B 108      18.951  -1.165 -36.842  1.00  0.00           H
ATOM   6898 HD13 ILE B 108      19.345   0.534 -37.198  1.00  0.00           H
ATOM   6899  N   ASP B 109      17.109   0.338 -31.818  1.00 13.08           N
ANISOU 6899  N   ASP B 109     1409   1727   1833    -60    -29    -43       N
ATOM   6900  CA  ASP B 109      16.176   1.008 -30.933  1.00 15.32           C
ANISOU 6900  CA  ASP B 109     1672   1996   2152    -32    -53    -64       C
ATOM   6901  C   ASP B 109      16.623   1.026 -29.472  1.00 12.62           C
ANISOU 6901  C   ASP B 109     1284   1691   1819    -40    -24    -88       C
ATOM   6902  O   ASP B 109      16.411   2.028 -28.787  1.00 11.35           O
ANISOU 6902  O   ASP B 109     1126   1511   1677    -39    -27   -106       O
ATOM   6903  CB  ASP B 109      14.795   0.411 -31.064  1.00 19.51           C
ANISOU 6903  CB  ASP B 109     2177   2520   2717     10    -86    -75       C
ATOM   6904  CG  ASP B 109      14.120   0.790 -32.410  1.00 22.35           C
ANISOU 6904  CG  ASP B 109     2597   2818   3076     36   -151    -65       C
ATOM   6905  OD1 ASP B 109      14.431   1.894 -32.984  1.00 21.20           O
ANISOU 6905  OD1 ASP B 109     2533   2616   2904     26   -175    -51       O
ATOM   6906  OD2 ASP B 109      13.275  -0.025 -32.879  1.00 23.86           O
ANISOU 6906  OD2 ASP B 109     2767   3008   3290     66   -182    -74       O
ATOM   6907  H   ASP B 109      16.859  -0.545 -32.240  1.00  0.00           H
ATOM   6908  HA  ASP B 109      16.110   2.045 -31.262  1.00  0.00           H
ATOM   6909  HB2 ASP B 109      14.175   0.776 -30.245  1.00  0.00           H
ATOM   6910  HB3 ASP B 109      14.869  -0.674 -30.997  1.00  0.00           H
ATOM   6911  N   LEU B 110      17.305  -0.011 -28.997  1.00 11.33           N
ANISOU 6911  N   LEU B 110     1094   1573   1639    -46     -6    -90       N
ATOM   6912  CA  LEU B 110      17.683  -0.024 -27.587  1.00 11.88           C
ANISOU 6912  CA  LEU B 110     1149   1661   1703    -45      2   -114       C
ATOM   6913  C   LEU B 110      18.870   0.933 -27.366  1.00 11.67           C
ANISOU 6913  C   LEU B 110     1120   1632   1682    -71      2   -133       C
ATOM   6914  O   LEU B 110      18.991   1.568 -26.328  1.00 11.15           O
ANISOU 6914  O   LEU B 110     1056   1561   1619    -71     -2   -155       O
ATOM   6915  CB  LEU B 110      18.015  -1.427 -27.058  1.00 12.95           C
ANISOU 6915  CB  LEU B 110     1280   1827   1811    -33      0   -116       C
ATOM   6916  CG  LEU B 110      19.409  -2.062 -27.282  1.00 15.61           C
ANISOU 6916  CG  LEU B 110     1599   2190   2141    -36    -17   -126       C
ATOM   6917  CD1 LEU B 110      20.431  -1.646 -26.202  1.00 17.51           C
ANISOU 6917  CD1 LEU B 110     1835   2434   2385    -34    -44   -166       C
ATOM   6918  CD2 LEU B 110      19.296  -3.607 -27.362  1.00 19.93           C
ANISOU 6918  CD2 LEU B 110     2154   2753   2665    -15    -27   -115       C
ATOM   6919  H   LEU B 110      17.558  -0.779 -29.603  1.00  0.00           H
ATOM   6920  HA  LEU B 110      16.838   0.356 -27.013  1.00  0.00           H
ATOM   6921  HB2 LEU B 110      17.291  -2.106 -27.509  1.00  0.00           H
ATOM   6922  HB3 LEU B 110      17.830  -1.421 -25.984  1.00  0.00           H
ATOM   6923  HG  LEU B 110      19.782  -1.708 -28.243  1.00  0.00           H
ATOM   6924 HD11 LEU B 110      20.496  -0.559 -26.162  1.00  0.00           H
ATOM   6925 HD12 LEU B 110      20.110  -2.027 -25.232  1.00  0.00           H
ATOM   6926 HD13 LEU B 110      21.409  -2.059 -26.449  1.00  0.00           H
ATOM   6927 HD21 LEU B 110      20.285  -4.037 -27.520  1.00  0.00           H
ATOM   6928 HD22 LEU B 110      18.645  -3.881 -28.192  1.00  0.00           H
ATOM   6929 HD23 LEU B 110      18.878  -3.989 -26.431  1.00  0.00           H
ATOM   6930  N   THR B 111      19.738   1.029 -28.345  1.00 11.36           N
ANISOU 6930  N   THR B 111     1079   1592   1646    -99     16   -131       N
ATOM   6931  CA  THR B 111      20.844   1.997 -28.209  1.00 12.25           C
ANISOU 6931  CA  THR B 111     1181   1696   1777   -137     33   -164       C
ATOM   6932  C   THR B 111      20.365   3.467 -28.281  1.00 12.52           C
ANISOU 6932  C   THR B 111     1260   1682   1813   -153     39   -156       C
ATOM   6933  O   THR B 111      20.914   4.367 -27.560  1.00 13.05           O
ANISOU 6933  O   THR B 111     1318   1742   1897   -171     43   -187       O
ATOM   6934  CB  THR B 111      21.958   1.721 -29.198  1.00 12.81           C
ANISOU 6934  CB  THR B 111     1235   1773   1859   -179     70   -184       C
ATOM   6935  OG1 THR B 111      21.456   1.610 -30.530  1.00 11.43           O
ANISOU 6935  OG1 THR B 111     1116   1570   1655   -194     92   -145       O
ATOM   6936  CG2 THR B 111      22.698   0.420 -28.824  1.00 14.00           C
ANISOU 6936  CG2 THR B 111     1324   1969   2026   -155     48   -216       C
ATOM   6937  H   THR B 111      19.652   0.455 -29.171  1.00  0.00           H
ATOM   6938  HA  THR B 111      21.266   1.853 -27.214  1.00  0.00           H
ATOM   6939  HB  THR B 111      22.668   2.547 -29.162  1.00  0.00           H
ATOM   6940  HG1 THR B 111      20.796   0.914 -30.567  1.00  0.00           H
ATOM   6941 HG21 THR B 111      23.495   0.235 -29.544  1.00  0.00           H
ATOM   6942 HG22 THR B 111      23.125   0.519 -27.826  1.00  0.00           H
ATOM   6943 HG23 THR B 111      21.996  -0.414 -28.837  1.00  0.00           H
ATOM   6944  N   ASP B 112      19.418   3.724 -29.172  1.00 11.50           N
ANISOU 6944  N   ASP B 112     1184   1514   1670   -143     30   -122       N
ATOM   6945  CA  ASP B 112      18.710   5.046 -29.251  1.00 11.65           C
ANISOU 6945  CA  ASP B 112     1259   1475   1693   -139     10   -116       C
ATOM   6946  C   ASP B 112      18.036   5.362 -27.920  1.00 11.76           C
ANISOU 6946  C   ASP B 112     1235   1499   1734   -105     -8   -139       C
ATOM   6947  O   ASP B 112      18.205   6.456 -27.348  1.00 12.85           O
ANISOU 6947  O   ASP B 112     1385   1614   1883   -117     -7   -158       O
ATOM   6948  CB  ASP B 112      17.697   4.946 -30.374  1.00 12.89           C
ANISOU 6948  CB  ASP B 112     1474   1586   1836   -111    -27    -86       C
ATOM   6949  CG  ASP B 112      17.053   6.306 -30.772  1.00 17.33           C
ANISOU 6949  CG  ASP B 112     2121   2067   2397    -99    -70    -83       C
ATOM   6950  OD1 ASP B 112      17.575   7.406 -30.454  1.00 15.56           O
ANISOU 6950  OD1 ASP B 112     1928   1813   2170   -130    -52    -94       O
ATOM   6951  OD2 ASP B 112      16.022   6.225 -31.464  1.00 17.82           O
ANISOU 6951  OD2 ASP B 112     2221   2087   2463    -54   -131    -73       O
ATOM   6952  H   ASP B 112      19.161   2.999 -29.827  1.00  0.00           H
ATOM   6953  HA  ASP B 112      19.432   5.829 -29.485  1.00  0.00           H
ATOM   6954  HB2 ASP B 112      18.197   4.535 -31.251  1.00  0.00           H
ATOM   6955  HB3 ASP B 112      16.906   4.261 -30.070  1.00  0.00           H
ATOM   6956  N   SER B 113      17.345   4.376 -27.361  1.00 11.84           N
ANISOU 6956  N   SER B 113     1205   1542   1750    -73    -14   -143       N
ATOM   6957  CA  SER B 113      16.703   4.502 -26.066  1.00 12.44           C
ANISOU 6957  CA  SER B 113     1259   1625   1843    -55     -8   -173       C
ATOM   6958  C   SER B 113      17.715   4.864 -24.969  1.00 12.54           C
ANISOU 6958  C   SER B 113     1270   1655   1841    -76      2   -194       C
ATOM   6959  O   SER B 113      17.427   5.741 -24.147  1.00 13.00           O
ANISOU 6959  O   SER B 113     1336   1694   1910    -75      5   -218       O
ATOM   6960  CB  SER B 113      15.966   3.180 -25.710  1.00 14.60           C
ANISOU 6960  CB  SER B 113     1508   1925   2112    -37      7   -177       C
ATOM   6961  OG  SER B 113      15.727   3.043 -24.318  1.00 15.52           O
ANISOU 6961  OG  SER B 113     1629   2050   2218    -40     35   -207       O
ATOM   6962  H   SER B 113      17.263   3.501 -27.858  1.00  0.00           H
ATOM   6963  HA  SER B 113      15.964   5.301 -26.127  1.00  0.00           H
ATOM   6964  HB2 SER B 113      16.576   2.340 -26.043  1.00  0.00           H
ATOM   6965  HB3 SER B 113      15.012   3.154 -26.237  1.00  0.00           H
ATOM   6966  HG  SER B 113      14.793   3.171 -24.139  1.00  0.00           H
ATOM   6967  N   GLU B 114      18.861   4.177 -24.899  1.00 11.39           N
ANISOU 6967  N   GLU B 114     1110   1542   1676    -88     -1   -197       N
ATOM   6968  CA  GLU B 114      19.854   4.456 -23.854  1.00 12.38           C
ANISOU 6968  CA  GLU B 114     1230   1678   1796    -97    -15   -231       C
ATOM   6969  C   GLU B 114      20.368   5.921 -23.990  1.00 12.82           C
ANISOU 6969  C   GLU B 114     1287   1706   1879   -129     -7   -249       C
ATOM   6970  O   GLU B 114      20.571   6.598 -22.973  1.00 12.94           O
ANISOU 6970  O   GLU B 114     1309   1713   1896   -130    -18   -278       O
ATOM   6971  CB  GLU B 114      21.055   3.491 -23.921  1.00 13.17           C
ANISOU 6971  CB  GLU B 114     1300   1810   1894    -96    -38   -249       C
ATOM   6972  CG  GLU B 114      20.670   2.039 -23.495  1.00 19.75           C
ANISOU 6972  CG  GLU B 114     2155   2662   2689    -62    -56   -236       C
ATOM   6973  CD  GLU B 114      20.087   1.941 -22.076  1.00 19.47           C
ANISOU 6973  CD  GLU B 114     2179   2609   2610    -46    -63   -246       C
ATOM   6974  OE1 GLU B 114      20.510   2.721 -21.171  1.00 17.50           O
ANISOU 6974  OE1 GLU B 114     1948   2345   2357    -48    -84   -277       O
ATOM   6975  OE2 GLU B 114      19.213   1.068 -21.875  1.00 21.51           O
ANISOU 6975  OE2 GLU B 114     2474   2863   2835    -37    -41   -229       O
ATOM   6976  H   GLU B 114      19.047   3.453 -25.578  1.00  0.00           H
ATOM   6977  HA  GLU B 114      19.374   4.346 -22.881  1.00  0.00           H
ATOM   6978  HB2 GLU B 114      21.430   3.469 -24.944  1.00  0.00           H
ATOM   6979  HB3 GLU B 114      21.842   3.857 -23.262  1.00  0.00           H
ATOM   6980  HG2 GLU B 114      21.565   1.419 -23.542  1.00  0.00           H
ATOM   6981  HG3 GLU B 114      19.937   1.650 -24.202  1.00  0.00           H
ATOM   6982  N   MET B 115      20.550   6.389 -25.221  1.00 11.95           N
ANISOU 6982  N   MET B 115     1188   1573   1779   -158     15   -232       N
ATOM   6983  CA  MET B 115      20.929   7.813 -25.413  1.00 12.42           C
ANISOU 6983  CA  MET B 115     1275   1590   1854   -196     32   -246       C
ATOM   6984  C   MET B 115      19.860   8.742 -24.829  1.00 13.63           C
ANISOU 6984  C   MET B 115     1460   1707   2011   -170     15   -242       C
ATOM   6985  O   MET B 115      20.154   9.690 -24.079  1.00 13.78           O
ANISOU 6985  O   MET B 115     1484   1712   2042   -183     14   -270       O
ATOM   6986  CB  MET B 115      21.120   8.099 -26.897  1.00 12.31           C
ANISOU 6986  CB  MET B 115     1310   1538   1829   -236     64   -223       C
ATOM   6987  CG  MET B 115      21.558   9.528 -27.205  1.00 12.82           C
ANISOU 6987  CG  MET B 115     1432   1543   1896   -289     93   -236       C
ATOM   6988  SD  MET B 115      23.290   9.912 -26.888  1.00 14.40           S
ANISOU 6988  SD  MET B 115     1575   1760   2138   -362    147   -308       S
ATOM   6989  CE  MET B 115      23.273  10.447 -25.171  1.00 16.65           C
ANISOU 6989  CE  MET B 115     1812   2066   2449   -326     98   -345       C
ATOM   6990  H   MET B 115      20.432   5.782 -26.019  1.00  0.00           H
ATOM   6991  HA  MET B 115      21.872   7.997 -24.897  1.00  0.00           H
ATOM   6992  HB2 MET B 115      21.879   7.418 -27.282  1.00  0.00           H
ATOM   6993  HB3 MET B 115      20.181   7.903 -27.414  1.00  0.00           H
ATOM   6994  HG2 MET B 115      20.951  10.200 -26.598  1.00  0.00           H
ATOM   6995  HG3 MET B 115      21.349   9.732 -28.255  1.00  0.00           H
ATOM   6996  HE1 MET B 115      24.285  10.710 -24.862  1.00  0.00           H
ATOM   6997  HE2 MET B 115      22.624  11.317 -25.068  1.00  0.00           H
ATOM   6998  HE3 MET B 115      22.900   9.639 -24.542  1.00  0.00           H
ATOM   6999  N   ASN B 116      18.615   8.445 -25.168  1.00 14.08           N
ANISOU 6999  N   ASN B 116     1531   1752   2068   -132     -1   -219       N
ATOM   7000  CA  ASN B 116      17.485   9.271 -24.734  1.00 15.21           C
ANISOU 7000  CA  ASN B 116     1689   1856   2236   -102    -19   -233       C
ATOM   7001  C   ASN B 116      17.315   9.224 -23.221  1.00 15.17           C
ANISOU 7001  C   ASN B 116     1656   1876   2234    -93     -5   -269       C
ATOM   7002  O   ASN B 116      17.006  10.235 -22.590  1.00 16.39           O
ANISOU 7002  O   ASN B 116     1820   2000   2405    -90     -6   -295       O
ATOM   7003  CB  ASN B 116      16.213   8.805 -25.427  1.00 15.62           C
ANISOU 7003  CB  ASN B 116     1739   1890   2307    -59    -46   -223       C
ATOM   7004  CG  ASN B 116      15.087   9.789 -25.265  1.00 18.55           C
ANISOU 7004  CG  ASN B 116     2117   2207   2725    -23    -78   -255       C
ATOM   7005  OD1 ASN B 116      15.214  10.928 -25.654  1.00 18.04           O
ANISOU 7005  OD1 ASN B 116     2108   2086   2661    -26   -105   -251       O
ATOM   7006  ND2 ASN B 116      14.005   9.366 -24.641  1.00 22.05           N
ANISOU 7006  ND2 ASN B 116     2506   2662   3211      8    -69   -295       N
ATOM   7007  H   ASN B 116      18.440   7.630 -25.739  1.00  0.00           H
ATOM   7008  HA  ASN B 116      17.679  10.303 -25.027  1.00  0.00           H
ATOM   7009  HB2 ASN B 116      15.909   7.850 -24.999  1.00  0.00           H
ATOM   7010  HB3 ASN B 116      16.416   8.669 -26.489  1.00  0.00           H
ATOM   7011 HD21 ASN B 116      13.951   8.412 -24.315  1.00  0.00           H
ATOM   7012 HD22 ASN B 116      13.231   9.996 -24.489  1.00  0.00           H
ATOM   7013  N   LYS B 117      17.550   8.068 -22.606  1.00 12.76           N
ANISOU 7013  N   LYS B 117     1332   1616   1902    -90      7   -271       N
ATOM   7014  CA  LYS B 117      17.387   7.932 -21.154  1.00 12.99           C
ANISOU 7014  CA  LYS B 117     1373   1654   1910    -86     22   -303       C
ATOM   7015  C   LYS B 117      18.451   8.773 -20.412  1.00 13.29           C
ANISOU 7015  C   LYS B 117     1425   1687   1939   -106      5   -327       C
ATOM   7016  O   LYS B 117      18.152   9.378 -19.370  1.00 14.08           O
ANISOU 7016  O   LYS B 117     1549   1768   2031   -106     15   -357       O
ATOM   7017  CB  LYS B 117      17.514   6.478 -20.666  1.00 14.48           C
ANISOU 7017  CB  LYS B 117     1574   1874   2053    -81     29   -298       C
ATOM   7018  CG  LYS B 117      16.358   5.576 -21.120  1.00 17.39           C
ANISOU 7018  CG  LYS B 117     1929   2245   2432    -68     58   -289       C
ATOM   7019  CD  LYS B 117      16.398   4.217 -20.429  1.00 22.12           C
ANISOU 7019  CD  LYS B 117     2569   2862   2976    -70     76   -288       C
ATOM   7020  CE  LYS B 117      17.014   3.170 -21.192  1.00 24.22           C
ANISOU 7020  CE  LYS B 117     2822   3155   3225    -61     47   -255       C
ATOM   7021  NZ  LYS B 117      16.810   1.822 -20.501  1.00 22.29           N
ANISOU 7021  NZ  LYS B 117     2636   2911   2921    -61     65   -256       N
ATOM   7022  H   LYS B 117      17.846   7.269 -23.149  1.00  0.00           H
ATOM   7023  HA  LYS B 117      16.400   8.304 -20.880  1.00  0.00           H
ATOM   7024  HB2 LYS B 117      17.541   6.481 -19.576  1.00  0.00           H
ATOM   7025  HB3 LYS B 117      18.450   6.063 -21.039  1.00  0.00           H
ATOM   7026  HG2 LYS B 117      15.414   6.066 -20.882  1.00  0.00           H
ATOM   7027  HG3 LYS B 117      16.422   5.430 -22.198  1.00  0.00           H
ATOM   7028  HD2 LYS B 117      16.952   4.327 -19.497  1.00  0.00           H
ATOM   7029  HD3 LYS B 117      15.377   3.918 -20.192  1.00  0.00           H
ATOM   7030  HE2 LYS B 117      16.566   3.137 -22.185  1.00  0.00           H
ATOM   7031  HE3 LYS B 117      18.081   3.371 -21.284  1.00  0.00           H
ATOM   7032  HZ1 LYS B 117      16.002   1.361 -20.895  1.00  0.00           H
ATOM   7033  HZ2 LYS B 117      17.627   1.245 -20.640  1.00  0.00           H
ATOM   7034  HZ3 LYS B 117      16.665   1.968 -19.512  1.00  0.00           H
ATOM   7035  N   LEU B 118      19.672   8.771 -20.915  1.00 13.89           N
ANISOU 7035  N   LEU B 118     1482   1777   2019   -125    -15   -324       N
ATOM   7036  CA  LEU B 118      20.723   9.587 -20.324  1.00 15.27           C
ANISOU 7036  CA  LEU B 118     1653   1945   2204   -147    -34   -362       C
ATOM   7037  C   LEU B 118      20.409  11.086 -20.425  1.00 15.55           C
ANISOU 7037  C   LEU B 118     1706   1936   2266   -165    -18   -368       C
ATOM   7038  O   LEU B 118      20.621  11.814 -19.466  1.00 15.13           O
ANISOU 7038  O   LEU B 118     1666   1870   2212   -169    -27   -401       O
ATOM   7039  CB  LEU B 118      22.065   9.309 -20.982  1.00 15.33           C
ANISOU 7039  CB  LEU B 118     1616   1973   2237   -173    -44   -379       C
ATOM   7040  CG  LEU B 118      23.293  10.049 -20.447  1.00 15.77           C
ANISOU 7040  CG  LEU B 118     1644   2024   2326   -199    -65   -440       C
ATOM   7041  CD1 LEU B 118      23.532   9.836 -18.932  1.00 18.06           C
ANISOU 7041  CD1 LEU B 118     1954   2318   2589   -165   -126   -479       C
ATOM   7042  CD2 LEU B 118      24.504   9.606 -21.217  1.00 17.76           C
ANISOU 7042  CD2 LEU B 118     1830   2295   2621   -229    -60   -476       C
ATOM   7043  H   LEU B 118      19.879   8.196 -21.719  1.00  0.00           H
ATOM   7044  HA  LEU B 118      20.802   9.327 -19.268  1.00  0.00           H
ATOM   7045  HB2 LEU B 118      22.260   8.241 -20.881  1.00  0.00           H
ATOM   7046  HB3 LEU B 118      21.972   9.535 -22.044  1.00  0.00           H
ATOM   7047  HG  LEU B 118      23.150  11.115 -20.622  1.00  0.00           H
ATOM   7048 HD11 LEU B 118      22.652  10.158 -18.376  1.00  0.00           H
ATOM   7049 HD12 LEU B 118      23.717   8.779 -18.739  1.00  0.00           H
ATOM   7050 HD13 LEU B 118      24.396  10.420 -18.615  1.00  0.00           H
ATOM   7051 HD21 LEU B 118      25.384  10.128 -20.843  1.00  0.00           H
ATOM   7052 HD22 LEU B 118      24.640   8.531 -21.094  1.00  0.00           H
ATOM   7053 HD23 LEU B 118      24.367   9.836 -22.274  1.00  0.00           H
ATOM   7054  N   PHE B 119      19.952  11.519 -21.597  1.00 15.87           N
ANISOU 7054  N   PHE B 119     1760   1947   2323   -173     -3   -338       N
ATOM   7055  CA  PHE B 119      19.552  12.893 -21.811  1.00 17.62           C
ANISOU 7055  CA  PHE B 119     2020   2112   2563   -182     -1   -341       C
ATOM   7056  C   PHE B 119      18.445  13.284 -20.832  1.00 16.04           C
ANISOU 7056  C   PHE B 119     1825   1897   2374   -146     -6   -363       C
ATOM   7057  O   PHE B 119      18.551  14.296 -20.140  1.00 15.83           O
ANISOU 7057  O   PHE B 119     1814   1845   2357   -154     -6   -391       O
ATOM   7058  CB  PHE B 119      19.096  13.111 -23.252  1.00 18.84           C
ANISOU 7058  CB  PHE B 119     2219   2222   2718   -183     -4   -303       C
ATOM   7059  CG  PHE B 119      18.748  14.535 -23.540  1.00 18.84           C
ANISOU 7059  CG  PHE B 119     2284   2146   2729   -188    -18   -305       C
ATOM   7060  CD1 PHE B 119      17.441  14.944 -23.533  1.00 21.04           C
ANISOU 7060  CD1 PHE B 119     2579   2384   3031   -133    -57   -310       C
ATOM   7061  CD2 PHE B 119      19.745  15.468 -23.774  1.00 17.93           C
ANISOU 7061  CD2 PHE B 119     2211   1996   2607   -247      8   -314       C
ATOM   7062  CE1 PHE B 119      17.094  16.277 -23.770  1.00 22.06           C
ANISOU 7062  CE1 PHE B 119     2777   2432   3173   -126    -87   -317       C
ATOM   7063  CE2 PHE B 119      19.401  16.818 -24.022  1.00 20.68           C
ANISOU 7063  CE2 PHE B 119     2642   2261   2956   -251     -8   -314       C
ATOM   7064  CZ  PHE B 119      18.063  17.205 -24.002  1.00 21.81           C
ANISOU 7064  CZ  PHE B 119     2809   2360   3118   -184    -64   -313       C
ATOM   7065  H   PHE B 119      19.882  10.866 -22.364  1.00  0.00           H
ATOM   7066  HA  PHE B 119      20.415  13.533 -21.625  1.00  0.00           H
ATOM   7067  HB2 PHE B 119      19.901  12.807 -23.922  1.00  0.00           H
ATOM   7068  HB3 PHE B 119      18.222  12.488 -23.444  1.00  0.00           H
ATOM   7069  HD1 PHE B 119      16.662  14.221 -23.340  1.00  0.00           H
ATOM   7070  HD2 PHE B 119      20.782  15.166 -23.767  1.00  0.00           H
ATOM   7071  HE1 PHE B 119      16.055  16.572 -23.769  1.00  0.00           H
ATOM   7072  HE2 PHE B 119      20.173  17.545 -24.226  1.00  0.00           H
ATOM   7073  HZ  PHE B 119      17.795  18.238 -24.170  1.00  0.00           H
ATOM   7074  N   GLU B 120      17.432  12.449 -20.681  1.00 13.27           N
ANISOU 7074  N   GLU B 120     1456   1562   2024   -112      1   -361       N
ATOM   7075  CA  GLU B 120      16.309  12.757 -19.797  1.00 14.91           C
ANISOU 7075  CA  GLU B 120     1659   1752   2254    -88     19   -401       C
ATOM   7076  C   GLU B 120      16.757  12.797 -18.341  1.00 15.02           C
ANISOU 7076  C   GLU B 120     1693   1781   2231   -105     39   -433       C
ATOM   7077  O   GLU B 120      16.304  13.632 -17.551  1.00 13.91           O
ANISOU 7077  O   GLU B 120     1567   1613   2106   -103     55   -472       O
ATOM   7078  CB  GLU B 120      15.199  11.691 -19.941  1.00 16.12           C
ANISOU 7078  CB  GLU B 120     1781   1920   2422    -63     40   -408       C
ATOM   7079  CG  GLU B 120      14.491  11.749 -21.337  1.00 23.26           C
ANISOU 7079  CG  GLU B 120     2670   2796   3373    -32      1   -391       C
ATOM   7080  CD  GLU B 120      13.146  10.962 -21.385  1.00 48.37           C
ANISOU 7080  CD  GLU B 120     5799   5979   6602     -2     19   -427       C
ATOM   7081  OE1 GLU B 120      12.735  10.303 -20.375  1.00 47.10           O
ANISOU 7081  OE1 GLU B 120     5620   5841   6433    -18     83   -464       O
ATOM   7082  OE2 GLU B 120      12.487  11.026 -22.453  1.00 49.04           O
ANISOU 7082  OE2 GLU B 120     5870   6033   6732     34    -31   -427       O
ATOM   7083  H   GLU B 120      17.434  11.576 -21.189  1.00  0.00           H
ATOM   7084  HA  GLU B 120      15.902  13.731 -20.069  1.00  0.00           H
ATOM   7085  HB2 GLU B 120      15.644  10.704 -19.815  1.00  0.00           H
ATOM   7086  HB3 GLU B 120      14.455  11.846 -19.160  1.00  0.00           H
ATOM   7087  HG2 GLU B 120      14.289  12.793 -21.578  1.00  0.00           H
ATOM   7088  HG3 GLU B 120      15.165  11.339 -22.090  1.00  0.00           H
ATOM   7089  N   LYS B 121      17.667  11.905 -17.989  1.00 16.69           N
ANISOU 7089  N   LYS B 121     1915   2030   2395   -117     30   -421       N
ATOM   7090  CA  LYS B 121      18.123  11.825 -16.611  1.00 17.64           C
ANISOU 7090  CA  LYS B 121     2081   2155   2468   -124     27   -452       C
ATOM   7091  C   LYS B 121      18.906  13.106 -16.257  1.00 16.35           C
ANISOU 7091  C   LYS B 121     1923   1969   2320   -140      1   -477       C
ATOM   7092  O   LYS B 121      18.760  13.687 -15.164  1.00 16.76           O
ANISOU 7092  O   LYS B 121     2015   1999   2352   -144      8   -513       O
ATOM   7093  CB  LYS B 121      19.045  10.616 -16.449  1.00 19.91           C
ANISOU 7093  CB  LYS B 121     2383   2474   2707   -120     -9   -440       C
ATOM   7094  CG  LYS B 121      19.654  10.534 -15.101  1.00 26.78           C
ANISOU 7094  CG  LYS B 121     3321   3333   3519   -118    -43   -474       C
ATOM   7095  CD  LYS B 121      20.308   9.183 -14.849  1.00 37.12           C
ANISOU 7095  CD  LYS B 121     4669   4661   4776    -98    -93   -468       C
ATOM   7096  CE  LYS B 121      21.506   8.962 -15.717  1.00 45.69           C
ANISOU 7096  CE  LYS B 121     5677   5776   5909    -93   -150   -469       C
ATOM   7097  NZ  LYS B 121      22.406   7.930 -15.084  1.00 51.97           N
ANISOU 7097  NZ  LYS B 121     6515   6572   6660    -61   -235   -493       N
ATOM   7098  H   LYS B 121      18.047  11.276 -18.681  1.00  0.00           H
ATOM   7099  HA  LYS B 121      17.265  11.724 -15.946  1.00  0.00           H
ATOM   7100  HB2 LYS B 121      19.843  10.686 -17.188  1.00  0.00           H
ATOM   7101  HB3 LYS B 121      18.472   9.707 -16.633  1.00  0.00           H
ATOM   7102  HG2 LYS B 121      20.411  11.313 -15.009  1.00  0.00           H
ATOM   7103  HG3 LYS B 121      18.881  10.700 -14.351  1.00  0.00           H
ATOM   7104  HD2 LYS B 121      19.579   8.398 -15.051  1.00  0.00           H
ATOM   7105  HD3 LYS B 121      20.612   9.125 -13.804  1.00  0.00           H
ATOM   7106  HE2 LYS B 121      22.051   9.899 -15.828  1.00  0.00           H
ATOM   7107  HE3 LYS B 121      21.184   8.611 -16.697  1.00  0.00           H
ATOM   7108  HZ1 LYS B 121      21.846   7.267 -14.567  1.00  0.00           H
ATOM   7109  HZ2 LYS B 121      22.922   7.445 -15.804  1.00  0.00           H
ATOM   7110  HZ3 LYS B 121      23.052   8.387 -14.456  1.00  0.00           H
ATOM   7111  N   THR B 122      19.719  13.539 -17.208  1.00 13.98           N
ANISOU 7111  N   THR B 122     1588   1671   2054   -158    -20   -463       N
ATOM   7112  CA  THR B 122      20.526  14.746 -17.027  1.00 14.52           C
ANISOU 7112  CA  THR B 122     1656   1715   2145   -186    -35   -491       C
ATOM   7113  C   THR B 122      19.620  15.984 -16.843  1.00 15.84           C
ANISOU 7113  C   THR B 122     1849   1833   2335   -181    -15   -502       C
ATOM   7114  O   THR B 122      19.824  16.839 -15.929  1.00 15.12           O
ANISOU 7114  O   THR B 122     1781   1721   2242   -190    -20   -539       O
ATOM   7115  CB  THR B 122      21.446  14.949 -18.213  1.00 13.87           C
ANISOU 7115  CB  THR B 122     1542   1632   2097   -222    -33   -481       C
ATOM   7116  OG1 THR B 122      22.278  13.790 -18.356  1.00 14.85           O
ANISOU 7116  OG1 THR B 122     1628   1801   2215   -221    -53   -487       O
ATOM   7117  CG2 THR B 122      22.368  16.155 -17.950  1.00 13.73           C
ANISOU 7117  CG2 THR B 122     1522   1586   2107   -263    -36   -524       C
ATOM   7118  H   THR B 122      19.783  13.026 -18.076  1.00  0.00           H
ATOM   7119  HA  THR B 122      21.135  14.625 -16.131  1.00  0.00           H
ATOM   7120  HB  THR B 122      20.863  15.110 -19.120  1.00  0.00           H
ATOM   7121  HG1 THR B 122      21.822  13.132 -18.886  1.00  0.00           H
ATOM   7122 HG21 THR B 122      23.030  16.300 -18.804  1.00  0.00           H
ATOM   7123 HG22 THR B 122      22.964  15.968 -17.057  1.00  0.00           H
ATOM   7124 HG23 THR B 122      21.763  17.050 -17.803  1.00  0.00           H
ATOM   7125  N   GLY B 123      18.632  16.089 -17.733  1.00 17.33           N
ANISOU 7125  N   GLY B 123     2035   1999   2549   -163     -2   -476       N
ATOM   7126  CA  GLY B 123      17.619  17.137 -17.649  1.00 18.19           C
ANISOU 7126  CA  GLY B 123     2161   2056   2695   -142      2   -496       C
ATOM   7127  C   GLY B 123      16.946  17.187 -16.295  1.00 19.05           C
ANISOU 7127  C   GLY B 123     2275   2165   2797   -129     31   -544       C
ATOM   7128  O   GLY B 123      16.788  18.254 -15.677  1.00 20.54           O
ANISOU 7128  O   GLY B 123     2484   2319   3003   -131     34   -580       O
ATOM   7129  H   GLY B 123      18.583  15.422 -18.490  1.00  0.00           H
ATOM   7130  HA2 GLY B 123      18.095  18.099 -17.838  1.00  0.00           H
ATOM   7131  HA3 GLY B 123      16.863  16.960 -18.414  1.00  0.00           H
ATOM   7132  N   ARG B 124      16.588  16.015 -15.795  1.00 17.27           N
ANISOU 7132  N   ARG B 124     2046   1976   2541   -123     60   -548       N
ATOM   7133  CA  ARG B 124      15.898  15.928 -14.514  1.00 16.45           C
ANISOU 7133  CA  ARG B 124     1970   1863   2416   -125    111   -598       C
ATOM   7134  C   ARG B 124      16.784  16.379 -13.359  1.00 17.06           C
ANISOU 7134  C   ARG B 124     2106   1936   2440   -147     97   -620       C
ATOM   7135  O   ARG B 124      16.296  17.015 -12.418  1.00 19.44           O
ANISOU 7135  O   ARG B 124     2440   2208   2738   -153    133   -668       O
ATOM   7136  CB  ARG B 124      15.315  14.508 -14.291  1.00 16.96           C
ANISOU 7136  CB  ARG B 124     2041   1955   2447   -127    158   -598       C
ATOM   7137  CG  ARG B 124      13.999  14.350 -15.053  1.00 18.17           C
ANISOU 7137  CG  ARG B 124     2129   2097   2678   -104    187   -617       C
ATOM   7138  CD  ARG B 124      13.524  12.906 -15.135  1.00 18.21           C
ANISOU 7138  CD  ARG B 124     2129   2130   2661   -111    231   -611       C
ATOM   7139  NE  ARG B 124      12.214  12.879 -15.743  1.00 19.67           N
ANISOU 7139  NE  ARG B 124     2237   2297   2938    -88    256   -654       N
ATOM   7140  CZ  ARG B 124      11.827  11.986 -16.646  1.00 20.46           C
ANISOU 7140  CZ  ARG B 124     2294   2416   3064    -73    247   -634       C
ATOM   7141  NH1 ARG B 124      12.644  11.011 -17.012  1.00 18.72           N
ANISOU 7141  NH1 ARG B 124     2103   2234   2778    -82    224   -568       N
ATOM   7142  NH2 ARG B 124      10.613  12.062 -17.157  1.00 21.62           N
ANISOU 7142  NH2 ARG B 124     2363   2540   3311    -46    255   -692       N
ATOM   7143  H   ARG B 124      16.796  15.170 -16.308  1.00  0.00           H
ATOM   7144  HA  ARG B 124      15.054  16.617 -14.558  1.00  0.00           H
ATOM   7145  HB2 ARG B 124      16.029  13.766 -14.649  1.00  0.00           H
ATOM   7146  HB3 ARG B 124      15.137  14.354 -13.227  1.00  0.00           H
ATOM   7147  HG2 ARG B 124      13.233  14.938 -14.548  1.00  0.00           H
ATOM   7148  HG3 ARG B 124      14.129  14.736 -16.064  1.00  0.00           H
ATOM   7149  HD2 ARG B 124      14.220  12.326 -15.740  1.00  0.00           H
ATOM   7150  HD3 ARG B 124      13.470  12.482 -14.132  1.00  0.00           H
ATOM   7151  HE  ARG B 124      11.549  13.586 -15.463  1.00  0.00           H
ATOM   7152 HH11 ARG B 124      13.569  10.950 -16.611  1.00  0.00           H
ATOM   7153 HH12 ARG B 124      12.342  10.328 -17.692  1.00  0.00           H
ATOM   7154 HH21 ARG B 124       9.989  12.802 -16.868  1.00  0.00           H
ATOM   7155 HH22 ARG B 124      10.308  11.381 -17.837  1.00  0.00           H
ATOM   7156  N   GLN B 125      18.082  16.098 -13.415  1.00 15.06           N
ANISOU 7156  N   GLN B 125     1862   1707   2153   -157     43   -597       N
ATOM   7157  CA  GLN B 125      18.962  16.580 -12.357  1.00 16.52           C
ANISOU 7157  CA  GLN B 125     2096   1880   2299   -170      9   -630       C
ATOM   7158  C   GLN B 125      19.008  18.116 -12.345  1.00 17.47           C
ANISOU 7158  C   GLN B 125     2205   1965   2469   -181      7   -655       C
ATOM   7159  O   GLN B 125      19.056  18.721 -11.285  1.00 18.22           O
ANISOU 7159  O   GLN B 125     2348   2035   2538   -188      8   -695       O
ATOM   7160  CB  GLN B 125      20.421  16.136 -12.556  1.00 17.99           C
ANISOU 7160  CB  GLN B 125     2264   2094   2476   -174    -64   -625       C
ATOM   7161  CG  GLN B 125      20.731  14.670 -12.374  1.00 21.44           C
ANISOU 7161  CG  GLN B 125     2728   2560   2859   -156    -93   -611       C
ATOM   7162  CD  GLN B 125      22.237  14.469 -12.321  1.00 23.71           C
ANISOU 7162  CD  GLN B 125     2990   2862   3156   -151   -182   -638       C
ATOM   7163  OE1 GLN B 125      22.856  14.017 -13.298  1.00 26.05           O
ANISOU 7163  OE1 GLN B 125     3213   3188   3496   -155   -199   -626       O
ATOM   7164  NE2 GLN B 125      22.838  14.836 -11.194  1.00 22.57           N
ANISOU 7164  NE2 GLN B 125     2901   2694   2980   -144   -241   -687       N
ATOM   7165  H   GLN B 125      18.455  15.557 -14.182  1.00  0.00           H
ATOM   7166  HA  GLN B 125      18.602  16.220 -11.393  1.00  0.00           H
ATOM   7167  HB2 GLN B 125      21.032  16.690 -11.843  1.00  0.00           H
ATOM   7168  HB3 GLN B 125      20.728  16.425 -13.561  1.00  0.00           H
ATOM   7169  HG2 GLN B 125      20.285  14.318 -11.444  1.00  0.00           H
ATOM   7170  HG3 GLN B 125      20.319  14.105 -13.210  1.00  0.00           H
ATOM   7171 HE21 GLN B 125      22.294  15.211 -10.430  1.00  0.00           H
ATOM   7172 HE22 GLN B 125      23.839  14.740 -11.101  1.00  0.00           H
ATOM   7173  N   LEU B 126      19.066  18.714 -13.532  1.00 16.54           N
ANISOU 7173  N   LEU B 126     2040   1835   2409   -186      0   -630       N
ATOM   7174  CA  LEU B 126      19.262  20.153 -13.644  1.00 16.99           C
ANISOU 7174  CA  LEU B 126     2103   1848   2505   -202     -7   -648       C
ATOM   7175  C   LEU B 126      18.056  21.008 -13.208  1.00 17.40           C
ANISOU 7175  C   LEU B 126     2173   1855   2585   -180     22   -680       C
ATOM   7176  O   LEU B 126      18.229  22.167 -12.901  1.00 15.93           O
ANISOU 7176  O   LEU B 126     2007   1630   2417   -191     14   -706       O
ATOM   7177  CB  LEU B 126      19.695  20.505 -15.079  1.00 18.17           C
ANISOU 7177  CB  LEU B 126     2232   1981   2691   -222    -18   -611       C
ATOM   7178  CG  LEU B 126      21.073  19.952 -15.484  1.00 18.99           C
ANISOU 7178  CG  LEU B 126     2305   2120   2789   -258    -34   -606       C
ATOM   7179  CD1 LEU B 126      21.333  20.079 -16.985  1.00 16.84           C
ANISOU 7179  CD1 LEU B 126     2032   1829   2540   -287    -17   -569       C
ATOM   7180  CD2 LEU B 126      22.138  20.716 -14.689  1.00 21.22           C
ANISOU 7180  CD2 LEU B 126     2587   2393   3082   -290    -55   -660       C
ATOM   7181  H   LEU B 126      18.972  18.160 -14.371  1.00  0.00           H
ATOM   7182  HA  LEU B 126      20.092  20.414 -12.987  1.00  0.00           H
ATOM   7183  HB2 LEU B 126      19.724  21.591 -15.169  1.00  0.00           H
ATOM   7184  HB3 LEU B 126      18.948  20.119 -15.772  1.00  0.00           H
ATOM   7185  HG  LEU B 126      21.121  18.898 -15.209  1.00  0.00           H
ATOM   7186 HD21 LEU B 126      23.127  20.345 -14.956  1.00  0.00           H
ATOM   7187 HD22 LEU B 126      22.074  21.778 -14.924  1.00  0.00           H
ATOM   7188 HD23 LEU B 126      21.970  20.569 -13.622  1.00  0.00           H
ATOM   7189 HD11 LEU B 126      20.568  19.531 -17.534  1.00  0.00           H
ATOM   7190 HD12 LEU B 126      22.314  19.666 -17.220  1.00  0.00           H
ATOM   7191 HD13 LEU B 126      21.303  21.130 -17.271  1.00  0.00           H
ATOM   7192  N   ARG B 127      16.859  20.422 -13.184  1.00 19.23           N
ANISOU 7192  N   ARG B 127     2389   2090   2828   -152     59   -689       N
ATOM   7193  CA  ARG B 127      15.641  21.095 -12.715  1.00 21.10           C
ANISOU 7193  CA  ARG B 127     2621   2286   3111   -131     96   -744       C
ATOM   7194  C   ARG B 127      15.453  22.424 -13.429  1.00 19.83           C
ANISOU 7194  C   ARG B 127     2457   2066   3013   -112     55   -748       C
ATOM   7195  O   ARG B 127      15.437  22.453 -14.668  1.00 19.63           O
ANISOU 7195  O   ARG B 127     2423   2023   3012    -97     15   -707       O
ATOM   7196  CB  ARG B 127      15.660  21.294 -11.190  1.00 23.64           C
ANISOU 7196  CB  ARG B 127     2994   2602   3386   -151    138   -797       C
ATOM   7197  CG  ARG B 127      15.397  20.037 -10.396  1.00 23.61           C
ANISOU 7197  CG  ARG B 127     3027   2628   3315   -166    193   -808       C
ATOM   7198  CD  ARG B 127      13.931  19.660 -10.401  1.00 23.44           C
ANISOU 7198  CD  ARG B 127     2967   2596   3345   -157    274   -856       C
ATOM   7199  NE  ARG B 127      13.091  20.538  -9.577  1.00 24.37           N
ANISOU 7199  NE  ARG B 127     3089   2668   3502   -161    336   -940       N
ATOM   7200  CZ  ARG B 127      12.855  20.357  -8.279  1.00 24.86           C
ANISOU 7200  CZ  ARG B 127     3229   2717   3502   -200    419   -992       C
ATOM   7201  NH1 ARG B 127      13.437  19.363  -7.618  1.00 25.09           N
ANISOU 7201  NH1 ARG B 127     3356   2763   3413   -231    432   -964       N
ATOM   7202  NH2 ARG B 127      12.067  21.181  -7.622  1.00 24.94           N
ANISOU 7202  NH2 ARG B 127     3233   2684   3559   -206    484  -1078       N
ATOM   7203  H   ARG B 127      16.786  19.467 -13.505  1.00  0.00           H
ATOM   7204  HA  ARG B 127      14.790  20.459 -12.960  1.00  0.00           H
ATOM   7205  HB2 ARG B 127      16.641  21.677 -10.908  1.00  0.00           H
ATOM   7206  HB3 ARG B 127      14.907  22.037 -10.926  1.00  0.00           H
ATOM   7207  HG2 ARG B 127      15.715  20.198  -9.366  1.00  0.00           H
ATOM   7208  HG3 ARG B 127      15.976  19.219 -10.823  1.00  0.00           H
ATOM   7209  HD2 ARG B 127      13.837  18.642 -10.024  1.00  0.00           H
ATOM   7210  HD3 ARG B 127      13.566  19.689 -11.428  1.00  0.00           H
ATOM   7211  HE  ARG B 127      12.662  21.335 -10.026  1.00  0.00           H
ATOM   7212 HH11 ARG B 127      14.055  18.728  -8.102  1.00  0.00           H
ATOM   7213 HH12 ARG B 127      13.261  19.242  -6.631  1.00  0.00           H
ATOM   7214 HH21 ARG B 127      11.626  21.951  -8.105  1.00  0.00           H
ATOM   7215 HH22 ARG B 127      11.904  21.044  -6.635  1.00  0.00           H
ATOM   7216  N   GLU B 128      15.334  23.526 -12.681  1.00 18.79           N
ANISOU 7216  N   GLU B 128     2348   1892   2897   -114     62   -796       N
ATOM   7217  CA  GLU B 128      15.083  24.826 -13.298  1.00 19.61           C
ANISOU 7217  CA  GLU B 128     2467   1926   3058    -92     17   -804       C
ATOM   7218  C   GLU B 128      16.379  25.598 -13.575  1.00 19.51           C
ANISOU 7218  C   GLU B 128     2505   1894   3013   -135    -15   -769       C
ATOM   7219  O   GLU B 128      16.330  26.791 -13.813  1.00 19.66           O
ANISOU 7219  O   GLU B 128     2564   1846   3061   -131    -42   -781       O
ATOM   7220  CB  GLU B 128      14.206  25.720 -12.393  1.00 23.40           C
ANISOU 7220  CB  GLU B 128     2943   2361   3585    -69     42   -886       C
ATOM   7221  CG  GLU B 128      12.841  25.123 -12.090  1.00 28.38           C
ANISOU 7221  CG  GLU B 128     3511   3000   4273    -36     93   -952       C
ATOM   7222  CD  GLU B 128      12.074  24.841 -13.365  1.00 33.04           C
ANISOU 7222  CD  GLU B 128     4053   3568   4932     17     40   -942       C
ATOM   7223  OE1 GLU B 128      12.179  25.663 -14.306  1.00 35.60           O
ANISOU 7223  OE1 GLU B 128     4412   3832   5282     47    -43   -915       O
ATOM   7224  OE2 GLU B 128      11.370  23.811 -13.427  1.00 33.69           O
ANISOU 7224  OE2 GLU B 128     4078   3684   5039     27     79   -965       O
ATOM   7225  H   GLU B 128      15.419  23.459 -11.677  1.00  0.00           H
ATOM   7226  HA  GLU B 128      14.562  24.669 -14.243  1.00  0.00           H
ATOM   7227  HB2 GLU B 128      14.731  25.877 -11.451  1.00  0.00           H
ATOM   7228  HB3 GLU B 128      14.067  26.684 -12.882  1.00  0.00           H
ATOM   7229  HG2 GLU B 128      12.273  25.826 -11.481  1.00  0.00           H
ATOM   7230  HG3 GLU B 128      12.971  24.193 -11.537  1.00  0.00           H
ATOM   7231  N   ASN B 129      17.528  24.942 -13.506  1.00 21.01           N
ANISOU 7231  N   ASN B 129     2694   2137   3153   -178    -10   -738       N
ATOM   7232  CA  ASN B 129      18.787  25.670 -13.626  1.00 21.61           C
ANISOU 7232  CA  ASN B 129     2798   2195   3217   -230    -25   -732       C
ATOM   7233  C   ASN B 129      19.353  25.656 -15.033  1.00 20.33           C
ANISOU 7233  C   ASN B 129     2652   2014   3058   -260    -34   -683       C
ATOM   7234  O   ASN B 129      20.424  26.207 -15.267  1.00 20.53           O
ANISOU 7234  O   ASN B 129     2697   2021   3082   -318    -27   -687       O
ATOM   7235  CB  ASN B 129      19.836  25.106 -12.656  1.00 21.38           C
ANISOU 7235  CB  ASN B 129     2753   2223   3149   -261    -26   -755       C
ATOM   7236  CG  ASN B 129      19.389  25.174 -11.213  1.00 22.12           C
ANISOU 7236  CG  ASN B 129     2868   2320   3215   -243    -14   -804       C
ATOM   7237  OD1 ASN B 129      18.406  25.832 -10.898  1.00 21.20           O
ANISOU 7237  OD1 ASN B 129     2768   2165   3123   -219      8   -831       O
ATOM   7238  ND2 ASN B 129      20.091  24.466 -10.329  1.00 23.80           N
ANISOU 7238  ND2 ASN B 129     3092   2574   3377   -252    -31   -821       N
ATOM   7239  H   ASN B 129      17.533  23.941 -13.371  1.00  0.00           H
ATOM   7240  HA  ASN B 129      18.601  26.708 -13.351  1.00  0.00           H
ATOM   7241  HB2 ASN B 129      20.026  24.064 -12.914  1.00  0.00           H
ATOM   7242  HB3 ASN B 129      20.761  25.672 -12.767  1.00  0.00           H
ATOM   7243 HD21 ASN B 129      19.825  24.469  -9.355  1.00  0.00           H
ATOM   7244 HD22 ASN B 129      20.889  23.927 -10.633  1.00  0.00           H
ATOM   7245  N   ALA B 130      18.673  24.953 -15.952  1.00 18.09           N
ANISOU 7245  N   ALA B 130     2361   1733   2777   -227    -42   -644       N
ATOM   7246  CA  ALA B 130      19.143  24.797 -17.310  1.00 18.07           C
ANISOU 7246  CA  ALA B 130     2393   1711   2764   -257    -45   -596       C
ATOM   7247  C   ALA B 130      17.958  24.721 -18.269  1.00 18.72           C
ANISOU 7247  C   ALA B 130     2508   1745   2860   -199    -83   -568       C
ATOM   7248  O   ALA B 130      16.822  24.444 -17.840  1.00 19.57           O
ANISOU 7248  O   ALA B 130     2573   1863   3001   -136    -99   -594       O
ATOM   7249  CB  ALA B 130      19.954  23.450 -17.430  1.00 16.32           C
ANISOU 7249  CB  ALA B 130     2111   1572   2518   -283    -22   -578       C
ATOM   7250  H   ALA B 130      17.802  24.517 -15.685  1.00  0.00           H
ATOM   7251  HA  ALA B 130      19.782  25.638 -17.579  1.00  0.00           H
ATOM   7252  HB1 ALA B 130      20.310  23.329 -18.453  1.00  0.00           H
ATOM   7253  HB2 ALA B 130      19.307  22.612 -17.170  1.00  0.00           H
ATOM   7254  HB3 ALA B 130      20.805  23.477 -16.750  1.00  0.00           H
ATOM   7255  N   GLU B 131      18.229  24.903 -19.562  1.00 18.72           N
ANISOU 7255  N   GLU B 131     2585   1690   2836   -222    -94   -524       N
ATOM   7256  CA  GLU B 131      17.241  24.663 -20.599  1.00 19.56           C
ANISOU 7256  CA  GLU B 131     2735   1749   2947   -165   -149   -496       C
ATOM   7257  C   GLU B 131      17.827  23.770 -21.715  1.00 19.48           C
ANISOU 7257  C   GLU B 131     2750   1760   2892   -203   -127   -443       C
ATOM   7258  O   GLU B 131      19.019  23.855 -22.063  1.00 18.81           O
ANISOU 7258  O   GLU B 131     2699   1676   2773   -287    -71   -429       O
ATOM   7259  CB  GLU B 131      16.736  25.985 -21.211  1.00 21.01           C
ANISOU 7259  CB  GLU B 131     3045   1804   3133   -138   -212   -496       C
ATOM   7260  CG  GLU B 131      16.066  26.902 -20.197  1.00 22.16           C
ANISOU 7260  CG  GLU B 131     3165   1921   3334    -92   -239   -556       C
ATOM   7261  CD  GLU B 131      15.683  28.277 -20.731  1.00 23.25           C
ANISOU 7261  CD  GLU B 131     3437   1922   3474    -64   -311   -562       C
ATOM   7262  OE1 GLU B 131      15.701  28.508 -21.959  1.00 25.36           O
ANISOU 7262  OE1 GLU B 131     3839   2101   3696    -65   -358   -518       O
ATOM   7263  OE2 GLU B 131      15.333  29.139 -19.896  1.00 21.44           O
ANISOU 7263  OE2 GLU B 131     3193   1665   3288    -38   -325   -614       O
ATOM   7264  H   GLU B 131      19.151  25.218 -19.829  1.00  0.00           H
ATOM   7265  HA  GLU B 131      16.393  24.144 -20.153  1.00  0.00           H
ATOM   7266  HB2 GLU B 131      16.015  25.750 -21.994  1.00  0.00           H
ATOM   7267  HB3 GLU B 131      17.580  26.511 -21.657  1.00  0.00           H
ATOM   7268  HG2 GLU B 131      15.159  26.411 -19.844  1.00  0.00           H
ATOM   7269  HG3 GLU B 131      16.740  27.034 -19.351  1.00  0.00           H
ATOM   7270  N   ASP B 132      16.958  22.923 -22.247  1.00 19.88           N
ANISOU 7270  N   ASP B 132     2777   1824   2952   -145   -167   -426       N
ATOM   7271  CA  ASP B 132      17.225  22.036 -23.380  1.00 21.21           C
ANISOU 7271  CA  ASP B 132     2976   2002   3080   -163   -160   -378       C
ATOM   7272  C   ASP B 132      17.324  22.899 -24.626  1.00 22.79           C
ANISOU 7272  C   ASP B 132     3349   2081   3230   -184   -192   -343       C
ATOM   7273  O   ASP B 132      16.363  23.564 -24.983  1.00 22.79           O
ANISOU 7273  O   ASP B 132     3426   1991   3244   -117   -281   -350       O
ATOM   7274  CB  ASP B 132      16.042  21.081 -23.473  1.00 21.33           C
ANISOU 7274  CB  ASP B 132     2921   2051   3132    -83   -208   -384       C
ATOM   7275  CG  ASP B 132      16.127  20.096 -24.629  1.00 21.16           C
ANISOU 7275  CG  ASP B 132     2928   2040   3073    -88   -214   -337       C
ATOM   7276  OD1 ASP B 132      16.995  20.212 -25.506  1.00 21.44           O
ANISOU 7276  OD1 ASP B 132     3056   2041   3049   -151   -184   -298       O
ATOM   7277  OD2 ASP B 132      15.254  19.225 -24.667  1.00 20.58           O
ANISOU 7277  OD2 ASP B 132     2784   2002   3034    -31   -244   -347       O
ATOM   7278  H   ASP B 132      16.036  22.887 -21.837  1.00  0.00           H
ATOM   7279  HA  ASP B 132      18.151  21.483 -23.223  1.00  0.00           H
ATOM   7280  HB2 ASP B 132      15.134  21.672 -23.593  1.00  0.00           H
ATOM   7281  HB3 ASP B 132      15.972  20.520 -22.541  1.00  0.00           H
ATOM   7282  N   MET B 133      18.489  22.919 -25.270  1.00 23.20           N
ANISOU 7282  N   MET B 133     3470   2119   3226   -280   -120   -317       N
ATOM   7283  CA  MET B 133      18.688  23.732 -26.460  1.00 23.49           C
ANISOU 7283  CA  MET B 133     3707   2026   3193   -322   -127   -284       C
ATOM   7284  C   MET B 133      18.155  23.071 -27.705  1.00 23.39           C
ANISOU 7284  C   MET B 133     3784   1971   3133   -289   -177   -239       C
ATOM   7285  O   MET B 133      18.152  23.677 -28.766  1.00 24.30           O
ANISOU 7285  O   MET B 133     4099   1961   3173   -311   -201   -208       O
ATOM   7286  CB  MET B 133      20.170  24.037 -26.637  1.00 23.34           C
ANISOU 7286  CB  MET B 133     3726   2002   3140   -456     -4   -292       C
ATOM   7287  CG  MET B 133      20.737  24.806 -25.422  1.00 24.77           C
ANISOU 7287  CG  MET B 133     3829   2212   3370   -489     34   -344       C
ATOM   7288  SD  MET B 133      22.534  24.967 -25.426  1.00 34.72           S
ANISOU 7288  SD  MET B 133     5065   3494   4633   -643    180   -388       S
ATOM   7289  CE  MET B 133      22.761  25.757 -27.012  1.00 54.38           C
ANISOU 7289  CE  MET B 133     7819   5820   7022   -733    232   -350       C
ATOM   7290  H   MET B 133      19.253  22.356 -24.924  1.00  0.00           H
ATOM   7291  HA  MET B 133      18.160  24.675 -26.321  1.00  0.00           H
ATOM   7292  HB2 MET B 133      20.714  23.099 -26.748  1.00  0.00           H
ATOM   7293  HB3 MET B 133      20.306  24.638 -27.536  1.00  0.00           H
ATOM   7294  HG2 MET B 133      20.304  25.806 -25.417  1.00  0.00           H
ATOM   7295  HG3 MET B 133      20.435  24.290 -24.510  1.00  0.00           H
ATOM   7296  HE1 MET B 133      23.695  26.320 -27.008  1.00  0.00           H
ATOM   7297  HE2 MET B 133      21.929  26.435 -27.202  1.00  0.00           H
ATOM   7298  HE3 MET B 133      22.797  24.998 -27.794  1.00  0.00           H
ATOM   7299  N   GLY B 134      17.704  21.827 -27.571  1.00 20.40           N
ANISOU 7299  N   GLY B 134     3274   1689   2790   -237   -195   -238       N
ATOM   7300  CA  GLY B 134      17.028  21.139 -28.648  1.00 21.17           C
ANISOU 7300  CA  GLY B 134     3435   1753   2856   -187   -260   -204       C
ATOM   7301  C   GLY B 134      17.949  20.287 -29.530  1.00 21.73           C
ANISOU 7301  C   GLY B 134     3542   1850   2863   -270   -174   -168       C
ATOM   7302  O   GLY B 134      17.476  19.648 -30.479  1.00 19.99           O
ANISOU 7302  O   GLY B 134     3385   1604   2607   -237   -222   -138       O
ATOM   7303  H   GLY B 134      17.838  21.349 -26.691  1.00  0.00           H
ATOM   7304  HA2 GLY B 134      16.271  20.486 -28.214  1.00  0.00           H
ATOM   7305  HA3 GLY B 134      16.531  21.878 -29.276  1.00  0.00           H
ATOM   7306  N   ASN B 135      19.253  20.282 -29.221  1.00 23.19           N
ANISOU 7306  N   ASN B 135     3684   2085   3042   -375    -51   -183       N
ATOM   7307  CA  ASN B 135      20.252  19.530 -30.010  1.00 22.83           C
ANISOU 7307  CA  ASN B 135     3657   2064   2953   -466     50   -171       C
ATOM   7308  C   ASN B 135      21.086  18.572 -29.139  1.00 21.03           C
ANISOU 7308  C   ASN B 135     3222   1979   2791   -493    121   -211       C
ATOM   7309  O   ASN B 135      22.236  18.229 -29.481  1.00 23.47           O
ANISOU 7309  O   ASN B 135     3511   2313   3095   -586    224   -234       O
ATOM   7310  CB  ASN B 135      21.195  20.528 -30.674  1.00 24.79           C
ANISOU 7310  CB  ASN B 135     4075   2208   3138   -586    143   -175       C
ATOM   7311  CG  ASN B 135      21.958  21.345 -29.654  1.00 26.20           C
ANISOU 7311  CG  ASN B 135     4177   2408   3368   -641    204   -228       C
ATOM   7312  OD1 ASN B 135      21.633  21.330 -28.459  1.00 23.80           O
ANISOU 7312  OD1 ASN B 135     3727   2180   3136   -576    155   -254       O
ATOM   7313  ND2 ASN B 135      22.982  22.054 -30.108  1.00 30.19           N
ANISOU 7313  ND2 ASN B 135     4787   2845   3839   -768    318   -252       N
ATOM   7314  H   ASN B 135      19.565  20.812 -28.419  1.00  0.00           H
ATOM   7315  HA  ASN B 135      19.739  18.956 -30.782  1.00  0.00           H
ATOM   7316  HB2 ASN B 135      20.611  21.202 -31.300  1.00  0.00           H
ATOM   7317  HB3 ASN B 135      21.905  19.986 -31.299  1.00  0.00           H
ATOM   7318 HD21 ASN B 135      23.214  22.033 -31.091  1.00  0.00           H
ATOM   7319 HD22 ASN B 135      23.530  22.615 -29.471  1.00  0.00           H
ATOM   7320  N   GLY B 136      20.500  18.185 -28.018  1.00 17.18           N
ANISOU 7320  N   GLY B 136     2591   1571   2364   -414     65   -227       N
ATOM   7321  CA  GLY B 136      21.096  17.299 -27.031  1.00 17.22           C
ANISOU 7321  CA  GLY B 136     2426   1696   2422   -416     97   -263       C
ATOM   7322  C   GLY B 136      22.004  18.064 -26.067  1.00 18.90           C
ANISOU 7322  C   GLY B 136     2587   1922   2671   -467    139   -317       C
ATOM   7323  O   GLY B 136      22.738  17.454 -25.287  1.00 21.21           O
ANISOU 7323  O   GLY B 136     2757   2296   3003   -477    159   -359       O
ATOM   7324  H   GLY B 136      19.569  18.531 -27.834  1.00  0.00           H
ATOM   7325  HA2 GLY B 136      21.686  16.541 -27.546  1.00  0.00           H
ATOM   7326  HA3 GLY B 136      20.303  16.811 -26.464  1.00  0.00           H
ATOM   7327  N   CYS B 137      21.944  19.395 -26.093  1.00 17.25           N
ANISOU 7327  N   CYS B 137     2477   1628   2450   -492    140   -322       N
ATOM   7328  CA  CYS B 137      22.762  20.210 -25.200  1.00 18.44           C
ANISOU 7328  CA  CYS B 137     2585   1783   2638   -542    176   -377       C
ATOM   7329  C   CYS B 137      21.862  20.958 -24.214  1.00 18.42           C
ANISOU 7329  C   CYS B 137     2580   1766   2655   -471    106   -382       C
ATOM   7330  O   CYS B 137      20.723  21.339 -24.549  1.00 19.61           O
ANISOU 7330  O   CYS B 137     2809   1856   2788   -409     43   -349       O
ATOM   7331  CB  CYS B 137      23.605  21.228 -25.969  1.00 22.20           C
ANISOU 7331  CB  CYS B 137     3180   2167   3087   -652    259   -393       C
ATOM   7332  SG  CYS B 137      24.913  20.536 -27.015  1.00 31.23           S
ANISOU 7332  SG  CYS B 137     4317   3322   4226   -769    384   -423       S
ATOM   7333  H   CYS B 137      21.320  19.849 -26.744  1.00  0.00           H
ATOM   7334  HA  CYS B 137      23.428  19.555 -24.639  1.00  0.00           H
ATOM   7335  HB2 CYS B 137      24.074  21.892 -25.242  1.00  0.00           H
ATOM   7336  HB3 CYS B 137      22.940  21.821 -26.597  1.00  0.00           H
ATOM   7337  N   PHE B 138      22.350  21.112 -22.994  1.00 17.40           N
ANISOU 7337  N   PHE B 138     2357   1689   2567   -475    111   -432       N
ATOM   7338  CA  PHE B 138      21.705  21.964 -22.004  1.00 16.94           C
ANISOU 7338  CA  PHE B 138     2301   1608   2526   -429     66   -450       C
ATOM   7339  C   PHE B 138      22.490  23.251 -21.832  1.00 17.88           C
ANISOU 7339  C   PHE B 138     2471   1669   2655   -501    104   -486       C
ATOM   7340  O   PHE B 138      23.703  23.207 -21.666  1.00 18.64           O
ANISOU 7340  O   PHE B 138     2514   1793   2775   -573    157   -533       O
ATOM   7341  CB  PHE B 138      21.661  21.267 -20.666  1.00 16.50           C
ANISOU 7341  CB  PHE B 138     2131   1642   2496   -385     43   -482       C
ATOM   7342  CG  PHE B 138      20.761  20.084 -20.651  1.00 16.78           C
ANISOU 7342  CG  PHE B 138     2125   1728   2523   -318     15   -454       C
ATOM   7343  CD1 PHE B 138      19.389  20.267 -20.543  1.00 17.35           C
ANISOU 7343  CD1 PHE B 138     2217   1772   2604   -251    -23   -444       C
ATOM   7344  CD2 PHE B 138      21.274  18.800 -20.800  1.00 17.69           C
ANISOU 7344  CD2 PHE B 138     2179   1912   2631   -324     27   -447       C
ATOM   7345  CE1 PHE B 138      18.530  19.192 -20.529  1.00 16.71           C
ANISOU 7345  CE1 PHE B 138     2090   1732   2526   -198    -37   -432       C
ATOM   7346  CE2 PHE B 138      20.424  17.704 -20.785  1.00 18.33           C
ANISOU 7346  CE2 PHE B 138     2230   2034   2702   -268      7   -423       C
ATOM   7347  CZ  PHE B 138      19.052  17.892 -20.676  1.00 16.75           C
ANISOU 7347  CZ  PHE B 138     2046   1806   2511   -210    -19   -415       C
ATOM   7348  H   PHE B 138      23.197  20.623 -22.741  1.00  0.00           H
ATOM   7349  HA  PHE B 138      20.690  22.196 -22.328  1.00  0.00           H
ATOM   7350  HB2 PHE B 138      22.669  20.938 -20.413  1.00  0.00           H
ATOM   7351  HB3 PHE B 138      21.323  21.976 -19.911  1.00  0.00           H
ATOM   7352  HD1 PHE B 138      18.990  21.268 -20.469  1.00  0.00           H
ATOM   7353  HD2 PHE B 138      22.337  18.656 -20.928  1.00  0.00           H
ATOM   7354  HE1 PHE B 138      17.468  19.343 -20.407  1.00  0.00           H
ATOM   7355  HE2 PHE B 138      20.829  16.705 -20.858  1.00  0.00           H
ATOM   7356  HZ  PHE B 138      18.386  17.042 -20.704  1.00  0.00           H
ATOM   7357  N   LYS B 139      21.797  24.383 -21.882  1.00 18.07           N
ANISOU 7357  N   LYS B 139     2593   1606   2668   -480     72   -475       N
ATOM   7358  CA  LYS B 139      22.339  25.649 -21.433  1.00 19.24           C
ANISOU 7358  CA  LYS B 139     2783   1698   2828   -532     96   -514       C
ATOM   7359  C   LYS B 139      22.117  25.762 -19.923  1.00 20.38           C
ANISOU 7359  C   LYS B 139     2833   1899   3012   -483     61   -557       C
ATOM   7360  O   LYS B 139      20.978  25.778 -19.446  1.00 21.76           O
ANISOU 7360  O   LYS B 139     3001   2074   3194   -401      7   -550       O
ATOM   7361  CB  LYS B 139      21.653  26.807 -22.155  1.00 19.56           C
ANISOU 7361  CB  LYS B 139     2990   1609   2834   -523     65   -483       C
ATOM   7362  CG  LYS B 139      22.255  28.200 -21.816  1.00 24.26           C
ANISOU 7362  CG  LYS B 139     3654   2129   3433   -590     99   -520       C
ATOM   7363  CD  LYS B 139      21.627  29.261 -22.702  1.00 30.16           C
ANISOU 7363  CD  LYS B 139     4600   2729   4130   -581     62   -483       C
ATOM   7364  CE  LYS B 139      22.086  30.695 -22.345  1.00 37.57           C
ANISOU 7364  CE  LYS B 139     5624   3580   5069   -641     89   -517       C
ATOM   7365  NZ  LYS B 139      21.633  31.662 -23.391  1.00 41.22           N
ANISOU 7365  NZ  LYS B 139     6321   3879   5461   -647     56   -476       N
ATOM   7366  H   LYS B 139      20.856  24.360 -22.247  1.00  0.00           H
ATOM   7367  HA  LYS B 139      23.408  25.677 -21.643  1.00  0.00           H
ATOM   7368  HB2 LYS B 139      21.744  26.645 -23.229  1.00  0.00           H
ATOM   7369  HB3 LYS B 139      20.596  26.808 -21.890  1.00  0.00           H
ATOM   7370  HG2 LYS B 139      23.332  28.179 -21.984  1.00  0.00           H
ATOM   7371  HG3 LYS B 139      22.056  28.436 -20.771  1.00  0.00           H
ATOM   7372  HD2 LYS B 139      20.544  29.206 -22.595  1.00  0.00           H
ATOM   7373  HD3 LYS B 139      21.890  29.055 -23.740  1.00  0.00           H
ATOM   7374  HE2 LYS B 139      21.659  30.980 -21.383  1.00  0.00           H
ATOM   7375  HE3 LYS B 139      23.174  30.719 -22.278  1.00  0.00           H
ATOM   7376  HZ1 LYS B 139      21.939  32.593 -23.145  1.00  0.00           H
ATOM   7377  HZ2 LYS B 139      20.625  31.645 -23.451  1.00  0.00           H
ATOM   7378  HZ3 LYS B 139      22.028  31.402 -24.283  1.00  0.00           H
ATOM   7379  N   ILE B 140      23.212  25.821 -19.181  1.00 20.08           N
ANISOU 7379  N   ILE B 140     2722   1904   3002   -536     92   -613       N
ATOM   7380  CA  ILE B 140      23.182  25.909 -17.714  1.00 19.83           C
ANISOU 7380  CA  ILE B 140     2622   1920   2993   -499     57   -659       C
ATOM   7381  C   ILE B 140      23.371  27.379 -17.302  1.00 21.85           C
ANISOU 7381  C   ILE B 140     2935   2104   3263   -533     64   -694       C
ATOM   7382  O   ILE B 140      24.387  28.012 -17.645  1.00 21.67           O
ANISOU 7382  O   ILE B 140     2933   2043   3257   -620    113   -727       O
ATOM   7383  CB  ILE B 140      24.313  25.053 -17.141  1.00 19.31           C
ANISOU 7383  CB  ILE B 140     2450   1935   2951   -525     60   -709       C
ATOM   7384  CG1 ILE B 140      24.065  23.563 -17.476  1.00 19.89           C
ANISOU 7384  CG1 ILE B 140     2475   2076   3007   -483     47   -673       C
ATOM   7385  CG2 ILE B 140      24.458  25.211 -15.644  1.00 18.69           C
ANISOU 7385  CG2 ILE B 140     2332   1887   2882   -495     16   -762       C
ATOM   7386  CD1 ILE B 140      25.271  22.701 -17.171  1.00 21.34           C
ANISOU 7386  CD1 ILE B 140     2563   2324   3220   -507     40   -727       C
ATOM   7387  H   ILE B 140      24.109  25.805 -19.644  1.00  0.00           H
ATOM   7388  HA  ILE B 140      22.223  25.545 -17.344  1.00  0.00           H
ATOM   7389  HB  ILE B 140      25.248  25.360 -17.611  1.00  0.00           H
ATOM   7390 HG12 ILE B 140      23.220  23.206 -16.886  1.00  0.00           H
ATOM   7391 HG13 ILE B 140      23.822  23.473 -18.535  1.00  0.00           H
ATOM   7392 HG21 ILE B 140      24.633  26.260 -15.404  1.00  0.00           H
ATOM   7393 HG22 ILE B 140      23.545  24.874 -15.153  1.00  0.00           H
ATOM   7394 HG23 ILE B 140      25.300  24.613 -15.295  1.00  0.00           H
ATOM   7395 HD11 ILE B 140      25.050  21.664 -17.422  1.00  0.00           H
ATOM   7396 HD12 ILE B 140      26.121  23.044 -17.761  1.00  0.00           H
ATOM   7397 HD13 ILE B 140      25.511  22.775 -16.110  1.00  0.00           H
ATOM   7398  N   TYR B 141      22.412  27.902 -16.541  1.00 24.11           N
ANISOU 7398  N   TYR B 141     3242   2369   3549   -470     24   -698       N
ATOM   7399  CA  TYR B 141      22.314  29.350 -16.327  1.00 24.90           C
ANISOU 7399  CA  TYR B 141     3417   2385   3658   -488     22   -720       C
ATOM   7400  C   TYR B 141      22.994  29.799 -15.022  1.00 27.10           C
ANISOU 7400  C   TYR B 141     3647   2691   3960   -510     20   -788       C
ATOM   7401  O   TYR B 141      22.515  30.682 -14.309  1.00 28.36           O
ANISOU 7401  O   TYR B 141     3838   2811   4125   -485      0   -812       O
ATOM   7402  CB  TYR B 141      20.833  29.735 -16.332  1.00 22.90           C
ANISOU 7402  CB  TYR B 141     3213   2082   3406   -402    -26   -700       C
ATOM   7403  CG  TYR B 141      20.227  29.847 -17.710  1.00 24.47           C
ANISOU 7403  CG  TYR B 141     3507   2206   3586   -383    -49   -646       C
ATOM   7404  CD1 TYR B 141      19.709  28.722 -18.359  1.00 24.43           C
ANISOU 7404  CD1 TYR B 141     3472   2240   3570   -343    -64   -607       C
ATOM   7405  CD2 TYR B 141      20.164  31.074 -18.370  1.00 27.77           C
ANISOU 7405  CD2 TYR B 141     4062   2502   3989   -405    -63   -636       C
ATOM   7406  CE1 TYR B 141      19.148  28.820 -19.614  1.00 25.52           C
ANISOU 7406  CE1 TYR B 141     3711   2302   3686   -319   -101   -562       C
ATOM   7407  CE2 TYR B 141      19.585  31.178 -19.641  1.00 28.90           C
ANISOU 7407  CE2 TYR B 141     4324   2557   4099   -379   -103   -587       C
ATOM   7408  CZ  TYR B 141      19.079  30.036 -20.247  1.00 27.97           C
ANISOU 7408  CZ  TYR B 141     4169   2485   3974   -334   -126   -552       C
ATOM   7409  OH  TYR B 141      18.522  30.111 -21.500  1.00 30.18           O
ANISOU 7409  OH  TYR B 141     4576   2673   4217   -305   -180   -508       O
ATOM   7410  H   TYR B 141      21.739  27.290 -16.102  1.00  0.00           H
ATOM   7411  HA  TYR B 141      22.803  29.854 -17.160  1.00  0.00           H
ATOM   7412  HB2 TYR B 141      20.729  30.699 -15.834  1.00  0.00           H
ATOM   7413  HB3 TYR B 141      20.277  28.988 -15.766  1.00  0.00           H
ATOM   7414  HD1 TYR B 141      19.749  27.761 -17.869  1.00  0.00           H
ATOM   7415  HD2 TYR B 141      20.567  31.956 -17.895  1.00  0.00           H
ATOM   7416  HE1 TYR B 141      18.761  27.937 -20.101  1.00  0.00           H
ATOM   7417  HE2 TYR B 141      19.533  32.133 -20.143  1.00  0.00           H
ATOM   7418  HH  TYR B 141      17.574  29.974 -21.438  1.00  0.00           H
ATOM   7419  N   HIS B 142      24.124  29.187 -14.712  1.00 27.36           N
ANISOU 7419  N   HIS B 142     3601   2786   4008   -553     31   -826       N
ATOM   7420  CA  HIS B 142      24.916  29.582 -13.562  1.00 27.45           C
ANISOU 7420  CA  HIS B 142     3569   2816   4045   -575     12   -900       C
ATOM   7421  C   HIS B 142      26.356  29.198 -13.799  1.00 27.22           C
ANISOU 7421  C   HIS B 142     3462   2821   4061   -645     32   -956       C
ATOM   7422  O   HIS B 142      26.667  28.347 -14.643  1.00 27.36           O
ANISOU 7422  O   HIS B 142     3444   2867   4083   -663     58   -937       O
ATOM   7423  CB  HIS B 142      24.411  28.955 -12.258  1.00 25.63           C
ANISOU 7423  CB  HIS B 142     3309   2641   3786   -501    -41   -915       C
ATOM   7424  CG  HIS B 142      24.459  27.450 -12.210  1.00 23.63           C
ANISOU 7424  CG  HIS B 142     3002   2464   3511   -465    -64   -898       C
ATOM   7425  ND1 HIS B 142      25.593  26.750 -11.853  1.00 23.76           N
ANISOU 7425  ND1 HIS B 142     2952   2529   3545   -480    -99   -947       N
ATOM   7426  CD2 HIS B 142      23.488  26.522 -12.393  1.00 22.41           C
ANISOU 7426  CD2 HIS B 142     2854   2340   3322   -410    -63   -845       C
ATOM   7427  CE1 HIS B 142      25.327  25.451 -11.854  1.00 23.77           C
ANISOU 7427  CE1 HIS B 142     2933   2584   3514   -435   -121   -917       C
ATOM   7428  NE2 HIS B 142      24.056  25.285 -12.176  1.00 22.18           N
ANISOU 7428  NE2 HIS B 142     2774   2373   3278   -398    -92   -853       N
ATOM   7429  H   HIS B 142      24.445  28.424 -15.291  1.00  0.00           H
ATOM   7430  HA  HIS B 142      24.862  30.666 -13.465  1.00  0.00           H
ATOM   7431  HB2 HIS B 142      25.022  29.338 -11.441  1.00  0.00           H
ATOM   7432  HB3 HIS B 142      23.381  29.273 -12.098  1.00  0.00           H
ATOM   7433  HD2 HIS B 142      22.460  26.716 -12.660  1.00  0.00           H
ATOM   7434  HE1 HIS B 142      26.030  24.662 -11.630  1.00  0.00           H
ATOM   7435  HD1 HIS B 142      26.487  27.163 -11.626  1.00  0.00           H
ATOM   7436  N   LYS B 143      27.254  29.836 -13.061  1.00 25.57           N
ANISOU 7436  N   LYS B 143     3218   2603   3895   -686     20  -1039       N
ATOM   7437  CA  LYS B 143      28.644  29.418 -13.116  1.00 26.74           C
ANISOU 7437  CA  LYS B 143     3262   2786   4111   -742     24  -1123       C
ATOM   7438  C   LYS B 143      28.757  27.959 -12.703  1.00 24.62           C
ANISOU 7438  C   LYS B 143     2921   2601   3833   -675    -46  -1126       C
ATOM   7439  O   LYS B 143      28.232  27.562 -11.666  1.00 23.24           O
ANISOU 7439  O   LYS B 143     2767   2454   3611   -598   -119  -1115       O
ATOM   7440  CB  LYS B 143      29.488  30.284 -12.183  1.00 33.22           C
ANISOU 7440  CB  LYS B 143     4050   3594   4977   -769     -5  -1210       C
ATOM   7441  CG  LYS B 143      29.515  31.735 -12.601  1.00 41.38           C
ANISOU 7441  CG  LYS B 143     5161   4548   6014   -836     66  -1200       C
ATOM   7442  CD  LYS B 143      30.437  32.557 -11.680  1.00 49.63           C
ANISOU 7442  CD  LYS B 143     6164   5595   7099   -853     37  -1274       C
ATOM   7443  CE  LYS B 143      30.497  34.008 -12.122  1.00 55.43           C
ANISOU 7443  CE  LYS B 143     6981   6246   7833   -924    113  -1264       C
ATOM   7444  NZ  LYS B 143      31.470  34.796 -11.318  1.00 59.45           N
ANISOU 7444  NZ  LYS B 143     7439   6758   8390   -949     94  -1341       N
ATOM   7445  H   LYS B 143      26.975  30.604 -12.467  1.00  0.00           H
ATOM   7446  HA  LYS B 143      29.011  29.530 -14.136  1.00  0.00           H
ATOM   7447  HB2 LYS B 143      29.074  30.219 -11.177  1.00  0.00           H
ATOM   7448  HB3 LYS B 143      30.508  29.900 -12.171  1.00  0.00           H
ATOM   7449  HG2 LYS B 143      28.505  32.140 -12.547  1.00  0.00           H
ATOM   7450  HG3 LYS B 143      29.876  31.806 -13.627  1.00  0.00           H
ATOM   7451  HD2 LYS B 143      30.054  32.511 -10.660  1.00  0.00           H
ATOM   7452  HD3 LYS B 143      31.441  32.132 -11.706  1.00  0.00           H
ATOM   7453  HE2 LYS B 143      30.795  34.044 -13.170  1.00  0.00           H
ATOM   7454  HE3 LYS B 143      29.507  34.453 -12.018  1.00  0.00           H
ATOM   7455  HZ1 LYS B 143      31.479  35.752 -11.643  1.00  0.00           H
ATOM   7456  HZ2 LYS B 143      32.392  34.397 -11.420  1.00  0.00           H
ATOM   7457  HZ3 LYS B 143      31.199  34.773 -10.345  1.00  0.00           H
ATOM   7458  N   CYS B 144      29.443  27.154 -13.500  1.00 26.77           N
ANISOU 7458  N   CYS B 144     3120   2906   4146   -707    -18  -1145       N
ATOM   7459  CA  CYS B 144      29.439  25.695 -13.266  1.00 28.10           C
ANISOU 7459  CA  CYS B 144     3235   3145   4296   -637    -85  -1135       C
ATOM   7460  C   CYS B 144      30.831  25.185 -13.618  1.00 29.89           C
ANISOU 7460  C   CYS B 144     3343   3408   4608   -672    -83  -1216       C
ATOM   7461  O   CYS B 144      31.094  24.833 -14.772  1.00 28.94           O
ANISOU 7461  O   CYS B 144     3196   3294   4507   -717     -4  -1197       O
ATOM   7462  CB  CYS B 144      28.342  24.970 -14.089  1.00 34.21           C
ANISOU 7462  CB  CYS B 144     4064   3932   5002   -601    -50  -1022       C
ATOM   7463  SG  CYS B 144      28.036  23.234 -13.513  1.00 36.03           S
ANISOU 7463  SG  CYS B 144     4266   4239   5185   -504   -136   -996       S
ATOM   7464  H   CYS B 144      29.971  27.539 -14.270  1.00  0.00           H
ATOM   7465  HA  CYS B 144      29.258  25.512 -12.207  1.00  0.00           H
ATOM   7466  HB2 CYS B 144      28.654  24.940 -15.133  1.00  0.00           H
ATOM   7467  HB3 CYS B 144      27.413  25.535 -14.014  1.00  0.00           H
ATOM   7468  N   ASP B 145      31.731  25.214 -12.625  1.00 31.66           N
ANISOU 7468  N   ASP B 145     3506   3655   4868   -635   -165  -1289       N
ATOM   7469  CA  ASP B 145      33.137  24.833 -12.811  1.00 32.75           C
ANISOU 7469  CA  ASP B 145     3523   3828   5091   -639   -170  -1366       C
ATOM   7470  C   ASP B 145      33.335  23.320 -12.940  1.00 31.18           C
ANISOU 7470  C   ASP B 145     3269   3683   4896   -575   -231  -1367       C
ATOM   7471  O   ASP B 145      32.353  22.552 -12.999  1.00 29.66           O
ANISOU 7471  O   ASP B 145     3135   3501   4635   -539   -257  -1301       O
ATOM   7472  CB  ASP B 145      34.034  25.433 -11.694  1.00 36.13           C
ANISOU 7472  CB  ASP B 145     3909   4253   5568   -614   -248  -1452       C
ATOM   7473  CG  ASP B 145      33.748  24.852 -10.305  1.00 35.35           C
ANISOU 7473  CG  ASP B 145     3855   4165   5411   -512   -405  -1458       C
ATOM   7474  OD1 ASP B 145      33.036  23.832 -10.193  1.00 31.38           O
ANISOU 7474  OD1 ASP B 145     3401   3680   4841   -458   -455  -1408       O
ATOM   7475  OD2 ASP B 145      34.252  25.425  -9.318  1.00 37.57           O
ANISOU 7475  OD2 ASP B 145     4136   4431   5708   -488   -477  -1513       O
ATOM   7476  H   ASP B 145      31.429  25.511 -11.708  1.00  0.00           H
ATOM   7477  HA  ASP B 145      33.463  25.276 -13.752  1.00  0.00           H
ATOM   7478  HB2 ASP B 145      33.868  26.510 -11.659  1.00  0.00           H
ATOM   7479  HB3 ASP B 145      35.078  25.247 -11.944  1.00  0.00           H
ATOM   7480  N   ASN B 146      34.590  22.885 -13.024  1.00 31.26           N
ANISOU 7480  N   ASN B 146     3165   3721   4992   -559   -248  -1448       N
ATOM   7481  CA  ASN B 146      34.843  21.489 -13.346  1.00 31.73           C
ANISOU 7481  CA  ASN B 146     3171   3822   5064   -504   -289  -1452       C
ATOM   7482  C   ASN B 146      34.241  20.553 -12.318  1.00 29.07           C
ANISOU 7482  C   ASN B 146     2898   3497   4649   -403   -437  -1419       C
ATOM   7483  O   ASN B 146      33.723  19.515 -12.661  1.00 27.34           O
ANISOU 7483  O   ASN B 146     2700   3300   4386   -372   -452  -1370       O
ATOM   7484  CB  ASN B 146      36.336  21.208 -13.499  1.00 35.90           C
ANISOU 7484  CB  ASN B 146     3561   4367   5710   -490   -292  -1565       C
ATOM   7485  CG  ASN B 146      36.907  21.783 -14.782  1.00 37.47           C
ANISOU 7485  CG  ASN B 146     3706   4557   5973   -596   -117  -1596       C
ATOM   7486  OD1 ASN B 146      36.173  22.248 -15.656  1.00 35.61           O
ANISOU 7486  OD1 ASN B 146     3549   4300   5681   -676     -2  -1519       O
ATOM   7487  ND2 ASN B 146      38.226  21.712 -14.918  1.00 40.54           N
ANISOU 7487  ND2 ASN B 146     3972   4955   6477   -594    -96  -1716       N
ATOM   7488  H   ASN B 146      35.360  23.519 -12.866  1.00  0.00           H
ATOM   7489  HA  ASN B 146      34.367  21.279 -14.304  1.00  0.00           H
ATOM   7490  HB2 ASN B 146      36.490  20.129 -13.501  1.00  0.00           H
ATOM   7491  HB3 ASN B 146      36.866  21.640 -12.650  1.00  0.00           H
ATOM   7492 HD21 ASN B 146      38.789  21.308 -14.183  1.00  0.00           H
ATOM   7493 HD22 ASN B 146      38.667  22.062 -15.757  1.00  0.00           H
ATOM   7494  N   ALA B 147      34.303  20.936 -11.055  1.00 29.18           N
ANISOU 7494  N   ALA B 147     2959   3491   4637   -354   -543  -1447       N
ATOM   7495  CA  ALA B 147      33.729  20.100 -10.021  1.00 29.66           C
ANISOU 7495  CA  ALA B 147     3120   3549   4600   -263   -675  -1415       C
ATOM   7496  C   ALA B 147      32.200  20.073 -10.114  1.00 26.51           C
ANISOU 7496  C   ALA B 147     2840   3140   4094   -282   -630  -1324       C
ATOM   7497  O   ALA B 147      31.600  19.055  -9.835  1.00 24.22           O
ANISOU 7497  O   ALA B 147     2620   2856   3724   -227   -686  -1284       O
ATOM   7498  CB  ALA B 147      34.193  20.559  -8.629  1.00 32.13           C
ANISOU 7498  CB  ALA B 147     3478   3832   4898   -210   -794  -1467       C
ATOM   7499  H   ALA B 147      34.749  21.809 -10.811  1.00  0.00           H
ATOM   7500  HA  ALA B 147      34.091  19.083 -10.175  1.00  0.00           H
ATOM   7501  HB1 ALA B 147      33.750  19.917  -7.868  1.00  0.00           H
ATOM   7502  HB2 ALA B 147      35.280  20.496  -8.569  1.00  0.00           H
ATOM   7503  HB3 ALA B 147      33.879  21.590  -8.463  1.00  0.00           H
ATOM   7504  N   CYS B 148      31.578  21.185 -10.501  1.00 25.85           N
ANISOU 7504  N   CYS B 148     2782   3032   4009   -355   -527  -1297       N
ATOM   7505  CA  CYS B 148      30.126  21.240 -10.720  1.00 24.75           C
ANISOU 7505  CA  CYS B 148     2742   2880   3782   -362   -462  -1203       C
ATOM   7506  C   CYS B 148      29.689  20.342 -11.895  1.00 22.86           C
ANISOU 7506  C   CYS B 148     2480   2673   3531   -367   -392  -1127       C
ATOM   7507  O   CYS B 148      28.740  19.547 -11.779  1.00 23.59           O
ANISOU 7507  O   CYS B 148     2647   2781   3537   -317   -394  -1046       O
ATOM   7508  CB  CYS B 148      29.714  22.695 -10.982  1.00 25.58           C
ANISOU 7508  CB  CYS B 148     2877   2945   3898   -426   -366  -1181       C
ATOM   7509  SG  CYS B 148      27.981  22.970 -11.332  1.00 32.34           S
ANISOU 7509  SG  CYS B 148     3845   3784   4660   -414   -276  -1048       S
ATOM   7510  H   CYS B 148      32.124  22.021 -10.649  1.00  0.00           H
ATOM   7511  HA  CYS B 148      29.625  20.895  -9.815  1.00  0.00           H
ATOM   7512  HB2 CYS B 148      29.972  23.279 -10.098  1.00  0.00           H
ATOM   7513  HB3 CYS B 148      30.297  23.070 -11.823  1.00  0.00           H
ATOM   7514  N   ILE B 149      30.416  20.436 -13.013  1.00 20.71           N
ANISOU 7514  N   ILE B 149     2110   2408   3349   -433   -325  -1164       N
ATOM   7515  CA  ILE B 149      30.169  19.547 -14.149  1.00 19.82           C
ANISOU 7515  CA  ILE B 149     1976   2325   3231   -440   -266  -1106       C
ATOM   7516  C   ILE B 149      30.303  18.093 -13.696  1.00 19.72           C
ANISOU 7516  C   ILE B 149     1951   2351   3191   -359   -368  -1112       C
ATOM   7517  O   ILE B 149      29.465  17.237 -14.003  1.00 18.49           O
ANISOU 7517  O   ILE B 149     1846   2215   2965   -324   -352  -1025       O
ATOM   7518  CB  ILE B 149      31.144  19.833 -15.310  1.00 21.51           C
ANISOU 7518  CB  ILE B 149     2094   2536   3544   -530   -174  -1164       C
ATOM   7519  CG1 ILE B 149      30.912  21.258 -15.853  1.00 20.64           C
ANISOU 7519  CG1 ILE B 149     2036   2369   3438   -618    -65  -1146       C
ATOM   7520  CG2 ILE B 149      30.998  18.750 -16.396  1.00 22.02           C
ANISOU 7520  CG2 ILE B 149     2133   2630   3605   -534   -129  -1123       C
ATOM   7521  CD1 ILE B 149      29.506  21.458 -16.479  1.00 23.87           C
ANISOU 7521  CD1 ILE B 149     2567   2752   3750   -609     -6  -1012       C
ATOM   7522  H   ILE B 149      31.146  21.131 -13.075  1.00  0.00           H
ATOM   7523  HA  ILE B 149      29.151  19.709 -14.502  1.00  0.00           H
ATOM   7524  HB  ILE B 149      32.160  19.783 -14.918  1.00  0.00           H
ATOM   7525 HG12 ILE B 149      31.662  21.463 -16.617  1.00  0.00           H
ATOM   7526 HG13 ILE B 149      31.038  21.970 -15.037  1.00  0.00           H
ATOM   7527 HG21 ILE B 149      31.689  18.958 -17.213  1.00  0.00           H
ATOM   7528 HG22 ILE B 149      29.976  18.752 -16.776  1.00  0.00           H
ATOM   7529 HG23 ILE B 149      31.225  17.773 -15.968  1.00  0.00           H
ATOM   7530 HD11 ILE B 149      29.411  22.482 -16.840  1.00  0.00           H
ATOM   7531 HD12 ILE B 149      28.742  21.267 -15.725  1.00  0.00           H
ATOM   7532 HD13 ILE B 149      29.377  20.766 -17.311  1.00  0.00           H
ATOM   7533  N   GLU B 150      31.331  17.795 -12.919  1.00 22.15           N
ANISOU 7533  N   GLU B 150     2205   2663   3547   -319   -479  -1208       N
ATOM   7534  CA  GLU B 150      31.517  16.415 -12.486  1.00 22.88           C
ANISOU 7534  CA  GLU B 150     2310   2778   3606   -232   -587  -1210       C
ATOM   7535  C   GLU B 150      30.370  15.984 -11.568  1.00 21.91           C
ANISOU 7535  C   GLU B 150     2339   2638   3345   -176   -640  -1139       C
ATOM   7536  O   GLU B 150      29.993  14.833 -11.578  1.00 20.98           O
ANISOU 7536  O   GLU B 150     2270   2536   3167   -128   -671  -1092       O
ATOM   7537  CB  GLU B 150      32.896  16.232 -11.805  1.00 26.29           C
ANISOU 7537  CB  GLU B 150     2680   3207   4102   -173   -689  -1295       C
ATOM   7538  CG  GLU B 150      33.171  14.794 -11.262  1.00 43.98           C
ANISOU 7538  CG  GLU B 150     4955   5451   6304    -70   -820  -1299       C
ATOM   7539  CD  GLU B 150      32.891  13.649 -12.270  1.00 46.17           C
ANISOU 7539  CD  GLU B 150     5202   5761   6579    -68   -779  -1257       C
ATOM   7540  OE1 GLU B 150      33.048  13.846 -13.495  1.00 47.50           O
ANISOU 7540  OE1 GLU B 150     5277   5955   6816   -137   -657  -1256       O
ATOM   7541  OE2 GLU B 150      32.510  12.532 -11.824  1.00 46.09           O
ANISOU 7541  OE2 GLU B 150     5279   5746   6488      1   -866  -1221       O
ATOM   7542  H   GLU B 150      31.979  18.514 -12.629  1.00  0.00           H
ATOM   7543  HA  GLU B 150      31.494  15.780 -13.372  1.00  0.00           H
ATOM   7544  HB2 GLU B 150      32.956  16.928 -10.968  1.00  0.00           H
ATOM   7545  HB3 GLU B 150      33.675  16.486 -12.524  1.00  0.00           H
ATOM   7546  HG2 GLU B 150      32.540  14.636 -10.387  1.00  0.00           H
ATOM   7547  HG3 GLU B 150      34.214  14.735 -10.952  1.00  0.00           H
ATOM   7548  N   SER B 151      29.825  16.897 -10.757  1.00 23.90           N
ANISOU 7548  N   SER B 151     2681   2859   3542   -181   -632  -1121       N
ATOM   7549  CA  SER B 151      28.681  16.552  -9.919  1.00 23.14           C
ANISOU 7549  CA  SER B 151     2739   2744   3310   -139   -636  -1044       C
ATOM   7550  C   SER B 151      27.466  16.178 -10.774  1.00 21.86           C
ANISOU 7550  C   SER B 151     2600   2603   3104   -157   -516   -935       C
ATOM   7551  O   SER B 151      26.686  15.297 -10.434  1.00 22.60           O
ANISOU 7551  O   SER B 151     2785   2696   3107   -122   -516   -882       O
ATOM   7552  CB  SER B 151      28.359  17.683  -8.932  1.00 23.29           C
ANISOU 7552  CB  SER B 151     2838   2722   3289   -150   -636  -1059       C
ATOM   7553  OG  SER B 151      27.667  18.759  -9.544  1.00 23.24           O
ANISOU 7553  OG  SER B 151     2811   2712   3307   -207   -512  -1013       O
ATOM   7554  H   SER B 151      30.207  17.831 -10.724  1.00  0.00           H
ATOM   7555  HA  SER B 151      28.955  15.674  -9.335  1.00  0.00           H
ATOM   7556  HB2 SER B 151      27.740  17.281  -8.130  1.00  0.00           H
ATOM   7557  HB3 SER B 151      29.290  18.057  -8.507  1.00  0.00           H
ATOM   7558  HG  SER B 151      28.183  19.094 -10.281  1.00  0.00           H
ATOM   7559  N   ILE B 152      27.289  16.833 -11.905  1.00 20.45           N
ANISOU 7559  N   ILE B 152     2349   2436   2987   -212   -416   -907       N
ATOM   7560  CA  ILE B 152      26.220  16.398 -12.801  1.00 20.76           C
ANISOU 7560  CA  ILE B 152     2403   2491   2995   -218   -328   -816       C
ATOM   7561  C   ILE B 152      26.513  14.997 -13.382  1.00 21.05           C
ANISOU 7561  C   ILE B 152     2402   2564   3032   -193   -353   -802       C
ATOM   7562  O   ILE B 152      25.663  14.054 -13.368  1.00 20.57           O
ANISOU 7562  O   ILE B 152     2397   2514   2904   -161   -340   -743       O
ATOM   7563  CB  ILE B 152      26.005  17.417 -13.949  1.00 20.37           C
ANISOU 7563  CB  ILE B 152     2312   2428   3000   -278   -233   -790       C
ATOM   7564  CG1 ILE B 152      25.669  18.782 -13.371  1.00 20.92           C
ANISOU 7564  CG1 ILE B 152     2426   2456   3068   -297   -214   -803       C
ATOM   7565  CG2 ILE B 152      24.864  16.947 -14.888  1.00 19.92           C
ANISOU 7565  CG2 ILE B 152     2278   2379   2913   -271   -167   -704       C
ATOM   7566  CD1 ILE B 152      25.922  19.941 -14.322  1.00 20.45           C
ANISOU 7566  CD1 ILE B 152     2340   2364   3068   -363   -147   -807       C
ATOM   7567  H   ILE B 152      27.879  17.617 -12.146  1.00  0.00           H
ATOM   7568  HA  ILE B 152      25.297  16.339 -12.224  1.00  0.00           H
ATOM   7569  HB  ILE B 152      26.926  17.496 -14.526  1.00  0.00           H
ATOM   7570 HG12 ILE B 152      24.614  18.787 -13.099  1.00  0.00           H
ATOM   7571 HG13 ILE B 152      26.262  18.935 -12.470  1.00  0.00           H
ATOM   7572 HG21 ILE B 152      25.111  15.968 -15.299  1.00  0.00           H
ATOM   7573 HG22 ILE B 152      24.745  17.663 -15.701  1.00  0.00           H
ATOM   7574 HG23 ILE B 152      23.934  16.880 -14.324  1.00  0.00           H
ATOM   7575 HD11 ILE B 152      25.657  20.878 -13.832  1.00  0.00           H
ATOM   7576 HD12 ILE B 152      25.314  19.815 -15.218  1.00  0.00           H
ATOM   7577 HD13 ILE B 152      26.976  19.961 -14.598  1.00  0.00           H
ATOM   7578  N   ARG B 153      27.727  14.835 -13.870  1.00 20.94           N
ANISOU 7578  N   ARG B 153     2288   2566   3101   -209   -385   -868       N
ATOM   7579  CA  ARG B 153      28.107  13.586 -14.497  1.00 21.57           C
ANISOU 7579  CA  ARG B 153     2318   2679   3199   -188   -407   -869       C
ATOM   7580  C   ARG B 153      28.014  12.421 -13.497  1.00 23.54           C
ANISOU 7580  C   ARG B 153     2648   2926   3372   -110   -515   -868       C
ATOM   7581  O   ARG B 153      27.670  11.330 -13.905  1.00 22.10           O
ANISOU 7581  O   ARG B 153     2481   2763   3155    -86   -510   -823       O
ATOM   7582  CB  ARG B 153      29.516  13.666 -15.104  1.00 21.33           C
ANISOU 7582  CB  ARG B 153     2152   2661   3291   -223   -420   -969       C
ATOM   7583  CG  ARG B 153      29.620  14.680 -16.299  1.00 22.63           C
ANISOU 7583  CG  ARG B 153     2265   2816   3516   -318   -287   -964       C
ATOM   7584  CD  ARG B 153      30.966  14.600 -17.065  1.00 25.39           C
ANISOU 7584  CD  ARG B 153     2479   3177   3990   -373   -260  -1072       C
ATOM   7585  NE  ARG B 153      32.095  14.612 -16.145  1.00 28.64           N
ANISOU 7585  NE  ARG B 153     2836   3588   4456   -324   -354  -1164       N
ATOM   7586  CZ  ARG B 153      33.230  15.291 -16.308  1.00 32.60           C
ANISOU 7586  CZ  ARG B 153     3260   4081   5046   -357   -310  -1241       C
ATOM   7587  NH1 ARG B 153      33.448  16.011 -17.396  1.00 35.69           N
ANISOU 7587  NH1 ARG B 153     3626   4459   5474   -451   -166  -1243       N
ATOM   7588  NH2 ARG B 153      34.178  15.212 -15.383  1.00 32.78           N
ANISOU 7588  NH2 ARG B 153     3237   4099   5117   -293   -412  -1323       N
ATOM   7589  H   ARG B 153      28.397  15.588 -13.806  1.00  0.00           H
ATOM   7590  HA  ARG B 153      27.404  13.390 -15.307  1.00  0.00           H
ATOM   7591  HB2 ARG B 153      30.211  13.977 -14.325  1.00  0.00           H
ATOM   7592  HB3 ARG B 153      29.804  12.676 -15.457  1.00  0.00           H
ATOM   7593  HG2 ARG B 153      29.507  15.690 -15.905  1.00  0.00           H
ATOM   7594  HG3 ARG B 153      28.807  14.483 -16.998  1.00  0.00           H
ATOM   7595  HD2 ARG B 153      30.990  13.678 -17.646  1.00  0.00           H
ATOM   7596  HD3 ARG B 153      31.045  15.452 -17.741  1.00  0.00           H
ATOM   7597  HE  ARG B 153      32.010  14.055 -15.307  1.00  0.00           H
ATOM   7598 HH11 ARG B 153      34.322  16.506 -17.508  1.00  0.00           H
ATOM   7599 HH12 ARG B 153      32.741  16.066 -18.115  1.00  0.00           H
ATOM   7600 HH21 ARG B 153      35.047  15.711 -15.507  1.00  0.00           H
ATOM   7601 HH22 ARG B 153      34.030  14.653 -14.555  1.00  0.00           H
ATOM   7602  N   ASN B 154      28.294  12.648 -12.210  1.00 26.27           N
ANISOU 7602  N   ASN B 154     3064   3238   3679    -74   -610   -916       N
ATOM   7603  CA  ASN B 154      28.264  11.529 -11.271  1.00 28.42           C
ANISOU 7603  CA  ASN B 154     3450   3489   3861     -3   -719   -917       C
ATOM   7604  C   ASN B 154      26.944  11.437 -10.469  1.00 28.88           C
ANISOU 7604  C   ASN B 154     3676   3515   3781      1   -669   -841       C
ATOM   7605  O   ASN B 154      26.787  10.559  -9.625  1.00 28.56           O
ANISOU 7605  O   ASN B 154     3772   3441   3640     46   -738   -835       O
ATOM   7606  CB  ASN B 154      29.526  11.449 -10.393  1.00 30.17           C
ANISOU 7606  CB  ASN B 154     3666   3680   4118     50   -889  -1031       C
ATOM   7607  CG  ASN B 154      29.643  12.562  -9.376  1.00 35.82           C
ANISOU 7607  CG  ASN B 154     4437   4356   4815     44   -927  -1074       C
ATOM   7608  OD1 ASN B 154      28.662  13.260  -9.048  1.00 35.88           O
ANISOU 7608  OD1 ASN B 154     4528   4350   4754     10   -835  -1013       O
ATOM   7609  ND2 ASN B 154      30.862  12.722  -8.848  1.00 45.72           N
ANISOU 7609  ND2 ASN B 154     5644   5595   6134     85  -1033  -1150       N
ATOM   7610  H   ASN B 154      28.523  13.579 -11.891  1.00  0.00           H
ATOM   7611  HA  ASN B 154      28.287  10.633 -11.891  1.00  0.00           H
ATOM   7612  HB2 ASN B 154      29.512  10.498  -9.860  1.00  0.00           H
ATOM   7613  HB3 ASN B 154      30.403  11.473 -11.040  1.00  0.00           H
ATOM   7614 HD21 ASN B 154      31.022  13.439  -8.155  1.00  0.00           H
ATOM   7615 HD22 ASN B 154      31.622  12.125  -9.142  1.00  0.00           H
ATOM   7616  N   GLY B 155      26.000  12.328 -10.762  1.00 28.04           N
ANISOU 7616  N   GLY B 155     3564   3414   3675    -48   -546   -793       N
ATOM   7617  CA  GLY B 155      24.643  12.180 -10.266  1.00 27.45           C
ANISOU 7617  CA  GLY B 155     3609   3318   3502    -55   -466   -734       C
ATOM   7618  C   GLY B 155      24.402  12.735  -8.868  1.00 27.12           C
ANISOU 7618  C   GLY B 155     3702   3224   3379    -52   -487   -762       C
ATOM   7619  O   GLY B 155      23.434  12.374  -8.229  1.00 30.11           O
ANISOU 7619  O   GLY B 155     4205   3572   3661    -58   -430   -734       O
ATOM   7620  H   GLY B 155      26.232  13.123 -11.341  1.00  0.00           H
ATOM   7621  HA2 GLY B 155      23.974  12.696 -10.954  1.00  0.00           H
ATOM   7622  HA3 GLY B 155      24.388  11.120 -10.266  1.00  0.00           H
ATOM   7623  N   THR B 156      25.245  13.647  -8.425  1.00 24.32           N
ANISOU 7623  N   THR B 156     3320   2854   3066    -50   -556   -824       N
ATOM   7624  CA  THR B 156      25.140  14.216  -7.097  1.00 25.28           C
ANISOU 7624  CA  THR B 156     3573   2921   3110    -45   -589   -858       C
ATOM   7625  C   THR B 156      24.901  15.743  -7.148  1.00 24.98           C
ANISOU 7625  C   THR B 156     3476   2882   3133    -88   -520   -873       C
ATOM   7626  O   THR B 156      24.955  16.422  -6.140  1.00 26.63           O
ANISOU 7626  O   THR B 156     3769   3050   3299    -88   -548   -911       O
ATOM   7627  CB  THR B 156      26.403  13.948  -6.291  1.00 29.23           C
ANISOU 7627  CB  THR B 156     4122   3390   3596      7   -765   -934       C
ATOM   7628  OG1 THR B 156      27.498  14.640  -6.896  1.00 32.14           O
ANISOU 7628  OG1 THR B 156     4319   3788   4105     -1   -814   -998       O
ATOM   7629  CG2 THR B 156      26.710  12.444  -6.253  1.00 29.59           C
ANISOU 7629  CG2 THR B 156     4234   3425   3584     60   -856   -926       C
ATOM   7630  H   THR B 156      25.989  13.959  -9.032  1.00  0.00           H
ATOM   7631  HA  THR B 156      24.297  13.750  -6.586  1.00  0.00           H
ATOM   7632  HB  THR B 156      26.265  14.313  -5.273  1.00  0.00           H
ATOM   7633  HG1 THR B 156      27.961  14.048  -7.493  1.00  0.00           H
ATOM   7634 HG21 THR B 156      27.616  12.272  -5.672  1.00  0.00           H
ATOM   7635 HG22 THR B 156      26.855  12.077  -7.269  1.00  0.00           H
ATOM   7636 HG23 THR B 156      25.877  11.915  -5.791  1.00  0.00           H
ATOM   7637  N   TYR B 157      24.673  16.286  -8.335  1.00 23.74           N
ANISOU 7637  N   TYR B 157     3189   2761   3070   -122   -437   -844       N
ATOM   7638  CA  TYR B 157      24.412  17.726  -8.483  1.00 23.67           C
ANISOU 7638  CA  TYR B 157     3137   2740   3117   -161   -376   -854       C
ATOM   7639  C   TYR B 157      23.243  18.168  -7.596  1.00 23.48           C
ANISOU 7639  C   TYR B 157     3222   2678   3020   -167   -307   -844       C
ATOM   7640  O   TYR B 157      22.183  17.517  -7.574  1.00 22.79           O
ANISOU 7640  O   TYR B 157     3185   2591   2882   -165   -235   -806       O
ATOM   7641  CB  TYR B 157      24.089  18.018  -9.942  1.00 21.94           C
ANISOU 7641  CB  TYR B 157     2810   2548   2978   -191   -295   -809       C
ATOM   7642  CG  TYR B 157      23.637  19.440 -10.276  1.00 20.38           C
ANISOU 7642  CG  TYR B 157     2588   2324   2830   -226   -231   -807       C
ATOM   7643  CD1 TYR B 157      24.558  20.443 -10.543  1.00 20.73           C
ANISOU 7643  CD1 TYR B 157     2578   2356   2944   -261   -248   -849       C
ATOM   7644  CD2 TYR B 157      22.283  19.735 -10.418  1.00 18.91           C
ANISOU 7644  CD2 TYR B 157     2432   2122   2632   -223   -152   -770       C
ATOM   7645  CE1 TYR B 157      24.160  21.702 -10.904  1.00 20.13           C
ANISOU 7645  CE1 TYR B 157     2500   2246   2905   -292   -193   -842       C
ATOM   7646  CE2 TYR B 157      21.873  20.991 -10.793  1.00 18.84           C
ANISOU 7646  CE2 TYR B 157     2407   2080   2671   -243   -112   -770       C
ATOM   7647  CZ  TYR B 157      22.820  21.971 -11.028  1.00 19.39           C
ANISOU 7647  CZ  TYR B 157     2445   2132   2791   -277   -134   -800       C
ATOM   7648  OH  TYR B 157      22.422  23.212 -11.371  1.00 19.59           O
ANISOU 7648  OH  TYR B 157     2478   2112   2853   -296   -100   -799       O
ATOM   7649  H   TYR B 157      24.679  15.698  -9.156  1.00  0.00           H
ATOM   7650  HA  TYR B 157      25.306  18.281  -8.198  1.00  0.00           H
ATOM   7651  HB2 TYR B 157      24.986  17.811 -10.526  1.00  0.00           H
ATOM   7652  HB3 TYR B 157      23.308  17.329 -10.262  1.00  0.00           H
ATOM   7653  HD1 TYR B 157      25.613  20.225 -10.464  1.00  0.00           H
ATOM   7654  HD2 TYR B 157      21.547  18.967 -10.231  1.00  0.00           H
ATOM   7655  HE1 TYR B 157      24.892  22.474 -11.089  1.00  0.00           H
ATOM   7656  HE2 TYR B 157      20.821  21.211 -10.903  1.00  0.00           H
ATOM   7657  HH  TYR B 157      22.261  23.246 -12.317  1.00  0.00           H
ATOM   7658  N   ASP B 158      23.444  19.266  -6.879  1.00 24.02           N
ANISOU 7658  N   ASP B 158     3319   2714   3092   -179   -322   -889       N
ATOM   7659  CA  ASP B 158      22.425  19.794  -5.956  1.00 24.88           C
ANISOU 7659  CA  ASP B 158     3531   2783   3140   -190   -253   -898       C
ATOM   7660  C   ASP B 158      21.812  21.064  -6.530  1.00 21.89           C
ANISOU 7660  C   ASP B 158     3078   2396   2842   -215   -176   -894       C
ATOM   7661  O   ASP B 158      22.382  22.156  -6.465  1.00 23.32           O
ANISOU 7661  O   ASP B 158     3229   2560   3071   -230   -205   -927       O
ATOM   7662  CB  ASP B 158      23.011  20.039  -4.577  1.00 30.69           C
ANISOU 7662  CB  ASP B 158     4388   3474   3799   -179   -333   -954       C
ATOM   7663  CG  ASP B 158      21.953  20.483  -3.557  1.00 36.88           C
ANISOU 7663  CG  ASP B 158     5296   4210   4505   -198   -245   -970       C
ATOM   7664  OD1 ASP B 158      20.830  20.879  -3.957  1.00 38.41           O
ANISOU 7664  OD1 ASP B 158     5448   4408   4740   -220   -127   -954       O
ATOM   7665  OD2 ASP B 158      22.256  20.412  -2.349  1.00 40.03           O
ANISOU 7665  OD2 ASP B 158     5843   4563   4805   -190   -300  -1008       O
ATOM   7666  H   ASP B 158      24.323  19.755  -6.969  1.00  0.00           H
ATOM   7667  HA  ASP B 158      21.635  19.049  -5.861  1.00  0.00           H
ATOM   7668  HB2 ASP B 158      23.770  20.817  -4.654  1.00  0.00           H
ATOM   7669  HB3 ASP B 158      23.480  19.121  -4.224  1.00  0.00           H
ATOM   7670  N   HIS B 159      20.668  20.907  -7.168  1.00 21.43           N
ANISOU 7670  N   HIS B 159     2343   3225   2575   -182   -478  -1360       N
ATOM   7671  CA  HIS B 159      20.094  22.008  -7.928  1.00 21.49           C
ANISOU 7671  CA  HIS B 159     2222   3164   2777   -175   -342  -1410       C
ATOM   7672  C   HIS B 159      19.785  23.207  -7.020  1.00 25.11           C
ANISOU 7672  C   HIS B 159     2711   3594   3237   -263   -254  -1576       C
ATOM   7673  O   HIS B 159      19.844  24.359  -7.464  1.00 28.36           O
ANISOU 7673  O   HIS B 159     3061   3910   3803   -252   -201  -1634       O
ATOM   7674  CB  HIS B 159      18.847  21.558  -8.693  1.00 19.60           C
ANISOU 7674  CB  HIS B 159     1973   2904   2573   -149   -236  -1336       C
ATOM   7675  CG  HIS B 159      17.606  21.532  -7.861  1.00 21.46           C
ANISOU 7675  CG  HIS B 159     2259   3197   2697   -227   -115  -1409       C
ATOM   7676  ND1 HIS B 159      16.669  22.534  -7.901  1.00 22.63           N
ANISOU 7676  ND1 HIS B 159     2292   3334   2974   -196     31  -1498       N
ATOM   7677  CD2 HIS B 159      17.158  20.634  -6.951  1.00 22.81           C
ANISOU 7677  CD2 HIS B 159     2584   3454   2629   -340   -113  -1415       C
ATOM   7678  CE1 HIS B 159      15.712  22.275  -7.031  1.00 25.09           C
ANISOU 7678  CE1 HIS B 159     2636   3758   3138   -276    145  -1576       C
ATOM   7679  NE2 HIS B 159      15.972  21.114  -6.455  1.00 23.92           N
ANISOU 7679  NE2 HIS B 159     2664   3675   2749   -400     60  -1523       N
ATOM   7680  H   HIS B 159      20.188  20.019  -7.129  1.00  0.00           H
ATOM   7681  HA  HIS B 159      20.835  22.328  -8.660  1.00  0.00           H
ATOM   7682  HB2 HIS B 159      18.688  22.244  -9.525  1.00  0.00           H
ATOM   7683  HB3 HIS B 159      19.022  20.559  -9.091  1.00  0.00           H
ATOM   7684  HD2 HIS B 159      17.644  19.712  -6.668  1.00  0.00           H
ATOM   7685  HE1 HIS B 159      14.860  22.905  -6.824  1.00  0.00           H
ATOM   7686  HD1 HIS B 159      16.706  23.344  -8.503  1.00  0.00           H
ATOM   7687  N   ASP B 160      19.469  22.950  -5.757  1.00 24.98           N
ANISOU 7687  N   ASP B 160     2832   3631   3027   -363   -231  -1644       N
ATOM   7688  CA  ASP B 160      19.063  24.039  -4.866  1.00 27.39           C
ANISOU 7688  CA  ASP B 160     3206   3886   3313   -436    -95  -1782       C
ATOM   7689  C   ASP B 160      20.199  25.034  -4.622  1.00 28.33           C
ANISOU 7689  C   ASP B 160     3360   3948   3457   -508   -171  -1812       C
ATOM   7690  O   ASP B 160      19.965  26.208  -4.369  1.00 31.16           O
ANISOU 7690  O   ASP B 160     3784   4191   3865   -536    -59  -1925       O
ATOM   7691  CB  ASP B 160      18.585  23.491  -3.529  1.00 33.88           C
ANISOU 7691  CB  ASP B 160     4194   4784   3895   -564    -52  -1799       C
ATOM   7692  CG  ASP B 160      17.102  23.156  -3.534  1.00 44.68           C
ANISOU 7692  CG  ASP B 160     5520   6221   5236   -557    130  -1851       C
ATOM   7693  OD1 ASP B 160      16.285  24.025  -3.940  1.00 49.72           O
ANISOU 7693  OD1 ASP B 160     6027   6825   6039   -456    301  -1973       O
ATOM   7694  OD2 ASP B 160      16.753  22.020  -3.132  1.00 49.02           O
ANISOU 7694  OD2 ASP B 160     6170   6862   5595   -653     95  -1761       O
ATOM   7695  H   ASP B 160      19.509  22.002  -5.410  1.00  0.00           H
ATOM   7696  HA  ASP B 160      18.235  24.573  -5.333  1.00  0.00           H
ATOM   7697  HB2 ASP B 160      18.772  24.239  -2.758  1.00  0.00           H
ATOM   7698  HB3 ASP B 160      19.151  22.590  -3.293  1.00  0.00           H
ATOM   7699  N   VAL B 161      21.427  24.554  -4.666  1.00 28.18           N
ANISOU 7699  N   VAL B 161     3306   4017   3383   -544   -363  -1712       N
ATOM   7700  CA  VAL B 161      22.566  25.410  -4.410  1.00 30.40           C
ANISOU 7700  CA  VAL B 161     3596   4309   3646   -666   -452  -1722       C
ATOM   7701  C   VAL B 161      22.631  26.530  -5.424  1.00 29.37           C
ANISOU 7701  C   VAL B 161     3400   4059   3701   -650   -383  -1760       C
ATOM   7702  O   VAL B 161      23.072  27.609  -5.113  1.00 29.41           O
ANISOU 7702  O   VAL B 161     3508   3990   3674   -786   -376  -1815       O
ATOM   7703  CB  VAL B 161      23.881  24.613  -4.534  1.00 31.42           C
ANISOU 7703  CB  VAL B 161     3597   4614   3727   -658   -675  -1594       C
ATOM   7704  CG1 VAL B 161      25.059  25.564  -4.712  1.00 33.51           C
ANISOU 7704  CG1 VAL B 161     3781   4935   4016   -788   -749  -1580       C
ATOM   7705  CG2 VAL B 161      24.051  23.714  -3.312  1.00 32.50           C
ANISOU 7705  CG2 VAL B 161     3864   4839   3646   -717   -808  -1546       C
ATOM   7706  H   VAL B 161      21.574  23.578  -4.881  1.00  0.00           H
ATOM   7707  HA  VAL B 161      22.488  25.830  -3.407  1.00  0.00           H
ATOM   7708  HB  VAL B 161      23.815  23.980  -5.419  1.00  0.00           H
ATOM   7709 HG11 VAL B 161      25.977  25.069  -4.395  1.00  0.00           H
ATOM   7710 HG12 VAL B 161      25.142  25.846  -5.762  1.00  0.00           H
ATOM   7711 HG13 VAL B 161      24.900  26.457  -4.107  1.00  0.00           H
ATOM   7712 HG21 VAL B 161      24.980  23.151  -3.401  1.00  0.00           H
ATOM   7713 HG22 VAL B 161      24.082  24.327  -2.412  1.00  0.00           H
ATOM   7714 HG23 VAL B 161      23.211  23.021  -3.251  1.00  0.00           H
ATOM   7715  N   TYR B 162      22.226  26.244  -6.654  1.00 26.03           N
ANISOU 7715  N   TYR B 162     2842   3601   3448   -508   -352  -1713       N
ATOM   7716  CA  TYR B 162      22.438  27.159  -7.761  1.00 26.12           C
ANISOU 7716  CA  TYR B 162     2802   3502   3621   -515   -334  -1701       C
ATOM   7717  C   TYR B 162      21.133  27.820  -8.240  1.00 27.18           C
ANISOU 7717  C   TYR B 162     2983   3429   3914   -405   -195  -1777       C
ATOM   7718  O   TYR B 162      21.168  28.653  -9.142  1.00 27.32           O
ANISOU 7718  O   TYR B 162     3013   3302   4065   -411   -196  -1759       O
ATOM   7719  CB  TYR B 162      23.026  26.393  -8.952  1.00 24.03           C
ANISOU 7719  CB  TYR B 162     2353   3343   3433   -446   -411  -1565       C
ATOM   7720  CG  TYR B 162      24.310  25.708  -8.628  1.00 23.94           C
ANISOU 7720  CG  TYR B 162     2243   3542   3309   -475   -542  -1491       C
ATOM   7721  CD1 TYR B 162      25.464  26.430  -8.507  1.00 25.65           C
ANISOU 7721  CD1 TYR B 162     2428   3846   3472   -631   -608  -1472       C
ATOM   7722  CD2 TYR B 162      24.368  24.324  -8.444  1.00 24.14           C
ANISOU 7722  CD2 TYR B 162     2216   3681   3276   -341   -615  -1436       C
ATOM   7723  CE1 TYR B 162      26.672  25.815  -8.199  1.00 28.46           C
ANISOU 7723  CE1 TYR B 162     2641   4431   3744   -636   -739  -1396       C
ATOM   7724  CE2 TYR B 162      25.572  23.695  -8.142  1.00 25.61           C
ANISOU 7724  CE2 TYR B 162     2291   4056   3385   -311   -759  -1369       C
ATOM   7725  CZ  TYR B 162      26.713  24.447  -8.032  1.00 28.77           C
ANISOU 7725  CZ  TYR B 162     2601   4573   3759   -448   -814  -1346       C
ATOM   7726  OH  TYR B 162      27.917  23.861  -7.719  1.00 32.49           O
ANISOU 7726  OH  TYR B 162     2915   5262   4169   -403   -959  -1266       O
ATOM   7727  H   TYR B 162      21.757  25.366  -6.825  1.00  0.00           H
ATOM   7728  HA  TYR B 162      23.139  27.935  -7.454  1.00  0.00           H
ATOM   7729  HB2 TYR B 162      23.204  27.098  -9.764  1.00  0.00           H
ATOM   7730  HB3 TYR B 162      22.303  25.648  -9.284  1.00  0.00           H
ATOM   7731  HD1 TYR B 162      25.437  27.500  -8.654  1.00  0.00           H
ATOM   7732  HD2 TYR B 162      23.467  23.735  -8.537  1.00  0.00           H
ATOM   7733  HE1 TYR B 162      27.571  26.404  -8.091  1.00  0.00           H
ATOM   7734  HE2 TYR B 162      25.607  22.626  -7.996  1.00  0.00           H
ATOM   7735  HH  TYR B 162      28.616  24.516  -7.774  1.00  0.00           H
ATOM   7736  N   ARG B 163      19.999  27.435  -7.659  1.00 26.73           N
ANISOU 7736  N   ARG B 163     2948   3372   3834   -308    -83  -1846       N
ATOM   7737  CA  ARG B 163      18.698  27.815  -8.225  1.00 26.33           C
ANISOU 7737  CA  ARG B 163     2852   3201   3950   -139     42  -1854       C
ATOM   7738  C   ARG B 163      18.468  29.325  -8.290  1.00 27.69           C
ANISOU 7738  C   ARG B 163     3156   3119   4247    -92    113  -1964       C
ATOM   7739  O   ARG B 163      17.922  29.810  -9.273  1.00 28.18           O
ANISOU 7739  O   ARG B 163     3170   3043   4493     40    114  -1888       O
ATOM   7740  CB  ARG B 163      17.568  27.170  -7.426  1.00 26.95           C
ANISOU 7740  CB  ARG B 163     2904   3395   3939    -77    174  -1914       C
ATOM   7741  CG  ARG B 163      16.148  27.369  -7.996  1.00 27.01           C
ANISOU 7741  CG  ARG B 163     2771   3382   4107    111    297  -1888       C
ATOM   7742  CD  ARG B 163      15.149  26.610  -7.141  1.00 26.15           C
ANISOU 7742  CD  ARG B 163     2608   3475   3854     98    431  -1953       C
ATOM   7743  NE  ARG B 163      13.752  26.859  -7.473  1.00 26.76           N
ANISOU 7743  NE  ARG B 163     2493   3609   4065    271    568  -1957       N
ATOM   7744  CZ  ARG B 163      12.966  26.031  -8.173  1.00 26.02           C
ANISOU 7744  CZ  ARG B 163     2217   3693   3979    275    549  -1796       C
ATOM   7745  NH1 ARG B 163      13.441  24.887  -8.666  1.00 23.69           N
ANISOU 7745  NH1 ARG B 163     1963   3475   3561    125    414  -1629       N
ATOM   7746  NH2 ARG B 163      11.700  26.357  -8.378  1.00 27.54           N
ANISOU 7746  NH2 ARG B 163     2191   3984   4288    429    664  -1798       N
ATOM   7747  H   ARG B 163      20.034  26.875  -6.819  1.00  0.00           H
ATOM   7748  HA  ARG B 163      18.651  27.427  -9.242  1.00  0.00           H
ATOM   7749  HB2 ARG B 163      17.762  26.099  -7.377  1.00  0.00           H
ATOM   7750  HB3 ARG B 163      17.591  27.571  -6.413  1.00  0.00           H
ATOM   7751  HG2 ARG B 163      16.111  26.993  -9.018  1.00  0.00           H
ATOM   7752  HG3 ARG B 163      15.899  28.430  -7.990  1.00  0.00           H
ATOM   7753  HD2 ARG B 163      15.307  26.895  -6.101  1.00  0.00           H
ATOM   7754  HD3 ARG B 163      15.345  25.543  -7.243  1.00  0.00           H
ATOM   7755  HE  ARG B 163      13.344  27.725  -7.150  1.00  0.00           H
ATOM   7756 HH11 ARG B 163      14.407  24.634  -8.513  1.00  0.00           H
ATOM   7757 HH12 ARG B 163      12.835  24.274  -9.192  1.00  0.00           H
ATOM   7758 HH21 ARG B 163      11.335  27.223  -8.007  1.00  0.00           H
ATOM   7759 HH22 ARG B 163      11.099  25.740  -8.905  1.00  0.00           H
ATOM   7760  N   ASP B 164      18.819  30.049  -7.229  1.00 29.05           N
ANISOU 7760  N   ASP B 164     3527   3228   4284   -194    160  -2062       N
ATOM   7761  CA  ASP B 164      18.619  31.496  -7.204  1.00 32.82           C
ANISOU 7761  CA  ASP B 164     4217   3427   4827   -147    228  -2138       C
ATOM   7762  C   ASP B 164      19.394  32.167  -8.335  1.00 32.15           C
ANISOU 7762  C   ASP B 164     4193   3190   4833   -238     91  -2051       C
ATOM   7763  O   ASP B 164      18.849  33.013  -9.055  1.00 33.14           O
ANISOU 7763  O   ASP B 164     4403   3066   5121   -101    105  -2035       O
ATOM   7764  CB  ASP B 164      19.039  32.075  -5.851  1.00 39.53           C
ANISOU 7764  CB  ASP B 164     5322   4237   5459   -303    282  -2256       C
ATOM   7765  CG  ASP B 164      17.992  31.860  -4.778  1.00 48.43           C
ANISOU 7765  CG  ASP B 164     6461   5426   6516   -195    468  -2369       C
ATOM   7766  OD1 ASP B 164      16.822  31.589  -5.124  1.00 50.40           O
ANISOU 7766  OD1 ASP B 164     6535   5709   6907     33    578  -2368       O
ATOM   7767  OD2 ASP B 164      18.325  31.982  -3.580  1.00 54.48           O
ANISOU 7767  OD2 ASP B 164     7401   6225   7072   -356    500  -2451       O
ATOM   7768  H   ASP B 164      19.230  29.590  -6.429  1.00  0.00           H
ATOM   7769  HA  ASP B 164      17.558  31.698  -7.349  1.00  0.00           H
ATOM   7770  HB2 ASP B 164      19.207  33.146  -5.966  1.00  0.00           H
ATOM   7771  HB3 ASP B 164      19.970  31.603  -5.537  1.00  0.00           H
ATOM   7772  N   GLU B 165      20.667  31.800  -8.461  1.00 31.60           N
ANISOU 7772  N   GLU B 165     4080   3282   4642   -471    -46  -1977       N
ATOM   7773  CA  GLU B 165      21.536  32.333  -9.504  1.00 32.46           C
ANISOU 7773  CA  GLU B 165     4222   3333   4778   -628   -169  -1875       C
ATOM   7774  C   GLU B 165      20.965  32.037 -10.890  1.00 29.57           C
ANISOU 7774  C   GLU B 165     3702   2911   4622   -493   -199  -1768       C
ATOM   7775  O   GLU B 165      20.910  32.928 -11.751  1.00 29.41           O
ANISOU 7775  O   GLU B 165     3819   2666   4691   -523   -245  -1715       O
ATOM   7776  CB  GLU B 165      22.966  31.761  -9.352  1.00 32.00           C
ANISOU 7776  CB  GLU B 165     4041   3567   4548   -853   -290  -1790       C
ATOM   7777  CG  GLU B 165      23.934  32.077 -10.503  1.00 31.36           C
ANISOU 7777  CG  GLU B 165     3914   3536   4464  -1024   -394  -1656       C
ATOM   7778  CD  GLU B 165      25.338  31.480 -10.315  1.00 32.01           C
ANISOU 7778  CD  GLU B 165     3812   3947   4403  -1174   -491  -1570       C
ATOM   7779  OE1 GLU B 165      25.573  30.765  -9.293  1.00 34.05           O
ANISOU 7779  OE1 GLU B 165     3987   4379   4570  -1143   -510  -1600       O
ATOM   7780  OE2 GLU B 165      26.210  31.732 -11.193  1.00 30.55           O
ANISOU 7780  OE2 GLU B 165     3562   3847   4200  -1311   -551  -1466       O
ATOM   7781  H   GLU B 165      21.046  31.127  -7.810  1.00  0.00           H
ATOM   7782  HA  GLU B 165      21.588  33.415  -9.382  1.00  0.00           H
ATOM   7783  HB2 GLU B 165      22.886  30.677  -9.269  1.00  0.00           H
ATOM   7784  HB3 GLU B 165      23.394  32.146  -8.427  1.00  0.00           H
ATOM   7785  HG2 GLU B 165      23.512  31.679 -11.426  1.00  0.00           H
ATOM   7786  HG3 GLU B 165      24.024  33.159 -10.598  1.00  0.00           H
ATOM   7787  N   ALA B 166      20.516  30.790 -11.102  1.00 26.01           N
ANISOU 7787  N   ALA B 166     3011   2647   4226   -367   -189  -1719       N
ATOM   7788  CA  ALA B 166      20.060  30.367 -12.417  1.00 25.31           C
ANISOU 7788  CA  ALA B 166     2787   2564   4265   -282   -227  -1542       C
ATOM   7789  C   ALA B 166      18.769  31.068 -12.828  1.00 26.43           C
ANISOU 7789  C   ALA B 166     2980   2477   4585    -73   -186  -1510       C
ATOM   7790  O   ALA B 166      18.659  31.521 -13.955  1.00 27.09           O
ANISOU 7790  O   ALA B 166     3098   2424   4771    -89   -268  -1382       O
ATOM   7791  CB  ALA B 166      19.872  28.848 -12.474  1.00 23.36           C
ANISOU 7791  CB  ALA B 166     2342   2569   3965   -214   -216  -1456       C
ATOM   7792  H   ALA B 166      20.494  30.134 -10.335  1.00  0.00           H
ATOM   7793  HA  ALA B 166      20.830  30.635 -13.140  1.00  0.00           H
ATOM   7794  HB1 ALA B 166      19.531  28.561 -13.469  1.00  0.00           H
ATOM   7795  HB2 ALA B 166      19.130  28.546 -11.734  1.00  0.00           H
ATOM   7796  HB3 ALA B 166      20.821  28.356 -12.259  1.00  0.00           H
ATOM   7797  N   LEU B 167      17.804  31.140 -11.918  1.00 26.88           N
ANISOU 7797  N   LEU B 167     3030   2514   4669    121    -62  -1623       N
ATOM   7798  CA  LEU B 167      16.532  31.773 -12.196  1.00 30.47           C
ANISOU 7798  CA  LEU B 167     3467   2801   5309    384    -11  -1606       C
ATOM   7799  C   LEU B 167      16.738  33.243 -12.494  1.00 33.35           C
ANISOU 7799  C   LEU B 167     4111   2795   5766    403    -63  -1644       C
ATOM   7800  O   LEU B 167      16.065  33.813 -13.366  1.00 35.44           O
ANISOU 7800  O   LEU B 167     4388   2872   6204    567   -136  -1522       O
ATOM   7801  CB  LEU B 167      15.581  31.653 -11.006  1.00 34.39           C
ANISOU 7801  CB  LEU B 167     3896   3380   5791    572    175  -1775       C
ATOM   7802  CG  LEU B 167      15.042  30.256 -10.724  1.00 33.14           C
ANISOU 7802  CG  LEU B 167     3494   3564   5535    559    232  -1725       C
ATOM   7803  CD1 LEU B 167      14.141  30.303  -9.500  1.00 34.63           C
ANISOU 7803  CD1 LEU B 167     3651   3852   5654    675    428  -1885       C
ATOM   7804  CD2 LEU B 167      14.316  29.674 -11.939  1.00 31.52           C
ANISOU 7804  CD2 LEU B 167     3070   3469   5435    622    149  -1495       C
ATOM   7805  H   LEU B 167      17.963  30.741 -11.004  1.00  0.00           H
ATOM   7806  HA  LEU B 167      16.078  31.294 -13.064  1.00  0.00           H
ATOM   7807  HB2 LEU B 167      16.114  31.991 -10.117  1.00  0.00           H
ATOM   7808  HB3 LEU B 167      14.735  32.320 -11.174  1.00  0.00           H
ATOM   7809  HG  LEU B 167      15.888  29.608 -10.495  1.00  0.00           H
ATOM   7810 HD11 LEU B 167      13.753  29.305  -9.295  1.00  0.00           H
ATOM   7811 HD12 LEU B 167      13.311  30.984  -9.686  1.00  0.00           H
ATOM   7812 HD13 LEU B 167      14.713  30.654  -8.641  1.00  0.00           H
ATOM   7813 HD21 LEU B 167      14.993  29.657 -12.793  1.00  0.00           H
ATOM   7814 HD22 LEU B 167      13.989  28.659 -11.715  1.00  0.00           H
ATOM   7815 HD23 LEU B 167      13.449  30.291 -12.174  1.00  0.00           H
ATOM   7816  N   ASN B 168      17.640  33.879 -11.753  1.00 35.68           N
ANISOU 7816  N   ASN B 168     4659   2978   5920    221    -44  -1793       N
ATOM   7817  CA  ASN B 168      17.923  35.268 -12.042  1.00 39.48           C
ANISOU 7817  CA  ASN B 168     5488   3117   6398    171    -99  -1785       C
ATOM   7818  C   ASN B 168      18.419  35.393 -13.480  1.00 37.39           C
ANISOU 7818  C   ASN B 168     5240   2766   6200      1   -288  -1605       C
ATOM   7819  O   ASN B 168      17.994  36.286 -14.223  1.00 39.48           O
ANISOU 7819  O   ASN B 168     5693   2733   6575     97   -371  -1506       O
ATOM   7820  CB  ASN B 168      18.943  35.850 -11.061  1.00 44.90           C
ANISOU 7820  CB  ASN B 168     6462   3772   6826    -95    -67  -1909       C
ATOM   7821  CG  ASN B 168      19.244  37.280 -11.353  1.00 54.32           C
ANISOU 7821  CG  ASN B 168     8089   4587   7964   -193   -122  -1904       C
ATOM   7822  OD1 ASN B 168      20.374  37.632 -11.717  1.00 58.92           O
ANISOU 7822  OD1 ASN B 168     8836   5166   8384   -548   -246  -1851       O
ATOM   7823  ND2 ASN B 168      18.217  38.134 -11.240  1.00 57.78           N
ANISOU 7823  ND2 ASN B 168     8722   4713   8518    124    -30  -1944       N
ATOM   7824  H   ASN B 168      18.119  33.402 -11.003  1.00  0.00           H
ATOM   7825  HA  ASN B 168      16.996  35.834 -11.949  1.00  0.00           H
ATOM   7826  HB2 ASN B 168      18.542  35.774 -10.050  1.00  0.00           H
ATOM   7827  HB3 ASN B 168      19.865  35.272 -11.122  1.00  0.00           H
ATOM   7828 HD21 ASN B 168      17.309  37.797 -10.955  1.00  0.00           H
ATOM   7829 HD22 ASN B 168      18.351  39.115 -11.440  1.00  0.00           H
ATOM   7830  N   ASN B 169      19.324  34.508 -13.880  1.00 33.61           N
ANISOU 7830  N   ASN B 169     4581   2569   5619   -255   -352  -1537       N
ATOM   7831  CA  ASN B 169      19.799  34.554 -15.253  1.00 34.34           C
ANISOU 7831  CA  ASN B 169     4679   2651   5718   -453   -492  -1354       C
ATOM   7832  C   ASN B 169      18.774  34.153 -16.319  1.00 33.66           C
ANISOU 7832  C   ASN B 169     4435   2559   5797   -264   -551  -1151       C
ATOM   7833  O   ASN B 169      18.803  34.698 -17.411  1.00 36.38           O
ANISOU 7833  O   ASN B 169     4917   2728   6180   -373   -682  -1005       O
ATOM   7834  CB  ASN B 169      21.054  33.701 -15.419  1.00 33.47           C
ANISOU 7834  CB  ASN B 169     4395   2912   5409   -731   -497  -1310       C
ATOM   7835  CG  ASN B 169      22.243  34.300 -14.749  1.00 33.57           C
ANISOU 7835  CG  ASN B 169     4579   2991   5185   -992   -498  -1377       C
ATOM   7836  OD1 ASN B 169      22.444  35.518 -14.788  1.00 33.74           O
ANISOU 7836  OD1 ASN B 169     4933   2754   5133  -1136   -540  -1393       O
ATOM   7837  ND2 ASN B 169      23.027  33.461 -14.085  1.00 32.27           N
ANISOU 7837  ND2 ASN B 169     4216   3155   4892  -1051   -474  -1404       N
ATOM   78