HEADER    VIRAL PROTEIN                           11-AUG-23   7GCI              
TITLE     GROUP DEPOSITION SARS-COV-2 MAIN PROTEASE IN COMPLEX WITH INHIBITORS  
TITLE    2 FROM THE COVID MOONSHOT -- CRYSTAL STRUCTURE OF SARS-COV-2 MAIN      
TITLE    3 PROTEASE IN COMPLEX WITH MAT-POS-590AC91E-27 (MPRO-X10610)           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3C-LIKE PROTEINASE;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 3CL-PRO, 3CLP, MAIN PROTEASE, MPRO, NON-STRUCTURAL PROTEIN  
COMPND   5 5, NSP5, SARS CORONAVIRUS MAIN PROTEINASE;                           
COMPND   6 EC: 3.4.22.69;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_TAXID: 2697049;                                             
SOURCE   5 GENE: REP, 1A-1B;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DIAMOND LIGHT SOURCE, I04-1, COVID MOONSHOT, CMD, MPRO, FRAGMENT      
KEYWDS   2 SCREENING, PANDDA, XCHEMEXPLORER, VIRAL PROTEIN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.FEARON,A.AIMON,J.C.ASCHENBRENNER,B.H.BALCOMB,F.K.R.BERTRAM,         
AUTHOR   2 J.BRANDAO-NETO,A.DIAS,A.DOUANGAMATH,L.DUNNETT,A.S.GODOY,T.J.GORRIE-  
AUTHOR   3 STONE,L.KOEKEMOER,T.KROJER,R.M.LITHGO,P.LUKACIK,P.G.MARPLES,         
AUTHOR   4 H.MIKOLAJEK,E.NELSON,C.D.OWEN,A.J.POWELL,V.L.RANGEL,R.SKYNER,        
AUTHOR   5 C.M.STRAIN-DAMERELL,W.THOMPSON,C.W.E.TOMLINSON,C.WILD,M.A.WALSH,     
AUTHOR   6 F.VON DELFT                                                          
REVDAT   2   06-DEC-23 7GCI    1       JRNL   REMARK                            
REVDAT   1   08-NOV-23 7GCI    0                                                
JRNL        AUTH   M.L.BOBY,D.FEARON,M.FERLA,M.FILEP,L.KOEKEMOER,M.C.ROBINSON,  
JRNL        AUTH 2 J.D.CHODERA,A.A.LEE,N.LONDON,A.VON DELFT,F.VON DELFT,        
JRNL        AUTH 3 H.ACHDOUT,A.AIMON,D.S.ALONZI,R.ARBON,J.C.ASCHENBRENNER,      
JRNL        AUTH 4 B.H.BALCOMB,E.BAR-DAVID,H.BARR,A.BEN-SHMUEL,J.BENNETT,       
JRNL        AUTH 5 V.A.BILENKO,B.BORDEN,P.BOULET,G.R.BOWMAN,L.BREWITZ,J.BRUN,   
JRNL        AUTH 6 S.BVNBS,M.CALMIANO,A.CARBERY,D.W.CARNEY,E.CATTERMOLE,        
JRNL        AUTH 7 E.CHANG,E.CHERNYSHENKO,A.CLYDE,J.E.COFFLAND,G.COHEN,         
JRNL        AUTH 8 J.C.COLE,A.CONTINI,L.COX,T.I.CROLL,M.CVITKOVIC,S.DE JONGHE,  
JRNL        AUTH 9 A.DIAS,K.DONCKERS,D.L.DOTSON,A.DOUANGAMATH,S.DUBERSTEIN,     
JRNL        AUTH10 T.DUDGEON,L.E.DUNNETT,P.EASTMAN,N.EREZ,C.J.EYERMANN,         
JRNL        AUTH11 M.FAIRHEAD,G.FATE,O.FEDOROV,R.S.FERNANDES,L.FERRINS,         
JRNL        AUTH12 R.FOSTER,H.FOSTER,L.FRAISSE,R.GABIZON,A.GARCIA-SASTRE,       
JRNL        AUTH13 V.O.GAWRILJUK,P.GEHRTZ,C.GILEADI,C.GIROUD,W.G.GLASS,         
JRNL        AUTH14 R.C.GLEN,I.GLINERT,A.S.GODOY,M.GORICHKO,T.GORRIE-STONE,      
JRNL        AUTH15 E.J.GRIFFEN,A.HANEEF,S.HASSELL HART,J.HEER,M.HENRY,M.HILL,   
JRNL        AUTH16 S.HORRELL,Q.Y.J.HUANG,V.D.HULIAK,M.F.D.HURLEY,T.ISRAELY,     
JRNL        AUTH17 A.JAJACK,J.JANSEN,E.JNOFF,D.JOCHMANS,T.JOHN,B.KAMINOW,       
JRNL        AUTH18 L.KANG,A.L.KANTSADI,P.W.KENNY,J.L.KIAPPES,S.O.KINAKH,        
JRNL        AUTH19 B.KOVAR,T.KROJER,V.N.T.LA,S.LAGHNIMI-HAHN,B.A.LEFKER,H.LEVY, 
JRNL        AUTH20 R.M.LITHGO,I.G.LOGVINENKO,P.LUKACIK,H.B.MACDONALD,           
JRNL        AUTH21 E.M.MACLEAN,L.L.MAKOWER,T.R.MALLA,P.G.MARPLES,T.MATVIIUK,    
JRNL        AUTH22 W.MCCORKINDALE,B.L.MCGOVERN,S.MELAMED,K.P.MELNYKOV,          
JRNL        AUTH23 O.MICHURIN,P.MIESEN,H.MIKOLAJEK,B.F.MILNE,D.MINH,A.MORRIS,   
JRNL        AUTH24 G.M.MORRIS,M.J.MORWITZER,D.MOUSTAKAS,C.E.MOWBRAY,            
JRNL        AUTH25 A.M.NAKAMURA,J.B.NETO,J.NEYTS,L.NGUYEN,G.D.NOSKE,            
JRNL        AUTH26 V.OLEINIKOVAS,G.OLIVA,G.J.OVERHEUL,C.D.OWEN,R.PAI,J.PAN,     
JRNL        AUTH27 N.PARAN,A.M.PAYNE,B.PERRY,M.PINGLE,J.PINJARI,B.POLITI,       
JRNL        AUTH28 A.POWELL,V.PSENAK,I.PULIDO,R.PUNI,V.L.RANGEL,R.N.REDDI,      
JRNL        AUTH29 P.REES,S.P.REID,L.REID,E.RESNICK,E.G.RIPKA,R.P.ROBINSON,     
JRNL        AUTH30 J.RODRIGUEZ-GUERRA,R.ROSALES,D.A.RUFA,K.SAAR,K.S.SAIKATENDU, 
JRNL        AUTH31 E.SALAH,D.SCHALLER,J.SCHEEN,C.A.SCHIFFER,C.J.SCHOFIELD,      
JRNL        AUTH32 M.SHAFEEV,A.SHAIKH,A.M.SHAQRA,J.SHI,K.SHURRUSH,S.SINGH,      
JRNL        AUTH33 A.SITTNER,P.SJO,R.SKYNER,A.SMALLEY,B.SMEETS,M.D.SMILOVA,     
JRNL        AUTH34 L.J.SOLMESKY,J.SPENCER,C.STRAIN-DAMERELL,V.SWAMY,H.TAMIR,    
JRNL        AUTH35 J.C.TAYLOR,R.E.TENNANT,W.THOMPSON,A.THOMPSON,S.TOMASIO,      
JRNL        AUTH36 C.W.E.TOMLINSON,I.S.TSURUPA,A.TUMBER,I.VAKONAKIS,            
JRNL        AUTH37 R.P.VAN RIJ,L.VANGEEL,F.S.VARGHESE,M.VASCHETTO,E.B.VITNER,   
JRNL        AUTH38 V.VOELZ,A.VOLKAMER,M.A.WALSH,W.WARD,C.WEATHERALL,S.WEISS,    
JRNL        AUTH39 K.M.WHITE,C.F.WILD,K.D.WITT,M.WITTMANN,N.WRIGHT,             
JRNL        AUTH40 Y.YAHALOM-RONEN,N.K.YILMAZ,D.ZAIDMANN,I.ZHANG,H.ZIDANE,      
JRNL        AUTH41 N.ZITZMANN,S.N.ZVORNICANIN                                   
JRNL        TITL   OPEN SCIENCE DISCOVERY OF POTENT NONCOVALENT SARS-COV-2 MAIN 
JRNL        TITL 2 PROTEASE INHIBITORS.                                         
JRNL        REF    SCIENCE                       V. 382 O7201 2023              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   37943932                                                     
JRNL        DOI    10.1126/SCIENCE.ABO7201                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3 (20-MAY-2020)                          
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 32774                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.181                          
REMARK   3   R VALUE            (WORKING SET)  : 0.179                          
REMARK   3   FREE R VALUE                      : 0.216                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.990                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1635                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 51                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.54                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.57                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 34.80                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 656                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1859                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 616                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1864                   
REMARK   3   BIN FREE R VALUE                        : 0.1771                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 6.10                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 40                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2347                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 268                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.74830                                             
REMARK   3    B22 (A**2) : 4.93570                                              
REMARK   3    B33 (A**2) : 4.81260                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -3.75620                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.270               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.105               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.102               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.100               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.099               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2444   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3321   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 827    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 426    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2444   ; 10.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 315    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2575   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.99                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.83                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.87                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   11.8811    0.6353    4.8517           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0937 T22:    0.0549                                    
REMARK   3     T33:   -0.0176 T12:   -0.0103                                    
REMARK   3     T13:   -0.0350 T23:   -0.0114                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1351 L22:    0.9568                                    
REMARK   3     L33:    0.6228 L12:    0.0306                                    
REMARK   3     L13:   -0.0221 L23:   -0.7501                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0192 S12:    0.0095 S13:   -0.0189                     
REMARK   3     S21:   -0.0276 S22:    0.0249 S23:   -0.0349                     
REMARK   3     S31:    0.0104 S32:   -0.0057 S33:   -0.0056                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7GCI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-23.                  
REMARK 100 THE DEPOSITION ID IS D_1001406009.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-20                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91257                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37331                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.13300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.16900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4K, 5% DMSO, 0.1M MES PH 6.5,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       56.59550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.53000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       56.59550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       26.53000            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 665  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     PHE A   305                                                      
REMARK 465     GLN A   306                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  33     -133.06     57.95                                   
REMARK 500    ASN A  51       70.80   -152.11                                   
REMARK 500    ASN A  84     -117.68     55.10                                   
REMARK 500    TYR A 154      -87.18     56.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 768        DISTANCE =  6.51 ANGSTROMS                       
DBREF  7GCI A    1   306  UNP    P0DTD1   R1AB_SARS2    3264   3569             
SEQRES   1 A  306  SER GLY PHE ARG LYS MET ALA PHE PRO SER GLY LYS VAL          
SEQRES   2 A  306  GLU GLY CYS MET VAL GLN VAL THR CYS GLY THR THR THR          
SEQRES   3 A  306  LEU ASN GLY LEU TRP LEU ASP ASP VAL VAL TYR CYS PRO          
SEQRES   4 A  306  ARG HIS VAL ILE CYS THR SER GLU ASP MET LEU ASN PRO          
SEQRES   5 A  306  ASN TYR GLU ASP LEU LEU ILE ARG LYS SER ASN HIS ASN          
SEQRES   6 A  306  PHE LEU VAL GLN ALA GLY ASN VAL GLN LEU ARG VAL ILE          
SEQRES   7 A  306  GLY HIS SER MET GLN ASN CYS VAL LEU LYS LEU LYS VAL          
SEQRES   8 A  306  ASP THR ALA ASN PRO LYS THR PRO LYS TYR LYS PHE VAL          
SEQRES   9 A  306  ARG ILE GLN PRO GLY GLN THR PHE SER VAL LEU ALA CYS          
SEQRES  10 A  306  TYR ASN GLY SER PRO SER GLY VAL TYR GLN CYS ALA MET          
SEQRES  11 A  306  ARG PRO ASN PHE THR ILE LYS GLY SER PHE LEU ASN GLY          
SEQRES  12 A  306  SER CYS GLY SER VAL GLY PHE ASN ILE ASP TYR ASP CYS          
SEQRES  13 A  306  VAL SER PHE CYS TYR MET HIS HIS MET GLU LEU PRO THR          
SEQRES  14 A  306  GLY VAL HIS ALA GLY THR ASP LEU GLU GLY ASN PHE TYR          
SEQRES  15 A  306  GLY PRO PHE VAL ASP ARG GLN THR ALA GLN ALA ALA GLY          
SEQRES  16 A  306  THR ASP THR THR ILE THR VAL ASN VAL LEU ALA TRP LEU          
SEQRES  17 A  306  TYR ALA ALA VAL ILE ASN GLY ASP ARG TRP PHE LEU ASN          
SEQRES  18 A  306  ARG PHE THR THR THR LEU ASN ASP PHE ASN LEU VAL ALA          
SEQRES  19 A  306  MET LYS TYR ASN TYR GLU PRO LEU THR GLN ASP HIS VAL          
SEQRES  20 A  306  ASP ILE LEU GLY PRO LEU SER ALA GLN THR GLY ILE ALA          
SEQRES  21 A  306  VAL LEU ASP MET CYS ALA SER LEU LYS GLU LEU LEU GLN          
SEQRES  22 A  306  ASN GLY MET ASN GLY ARG THR ILE LEU GLY SER ALA LEU          
SEQRES  23 A  306  LEU GLU ASP GLU PHE THR PRO PHE ASP VAL VAL ARG GLN          
SEQRES  24 A  306  CYS SER GLY VAL THR PHE GLN                                  
HET    DMS  A 401       4                                                       
HET    DMS  A 402       4                                                       
HET    DMS  A 403       4                                                       
HET    DMS  A 404       4                                                       
HET    LJO  A 405      17                                                       
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     LJO (3R)-3-CYANO-N-(4-METHYLPYRIDIN-3-YL)OXOLANE-3-                  
HETNAM   2 LJO  CARBOXAMIDE                                                     
FORMUL   2  DMS    4(C2 H6 O S)                                                 
FORMUL   6  LJO    C12 H13 N3 O2                                                
FORMUL   7  HOH   *268(H2 O)                                                    
HELIX    1 AA1 SER A   10  GLY A   15  1                                   6    
HELIX    2 AA2 HIS A   41  CYS A   44  5                                   4    
HELIX    3 AA3 GLU A   47  ASN A   51  5                                   5    
HELIX    4 AA4 ASN A   53  ARG A   60  1                                   8    
HELIX    5 AA5 LYS A   61  HIS A   64  5                                   4    
HELIX    6 AA6 ILE A  200  ASN A  214  1                                  15    
HELIX    7 AA7 THR A  226  TYR A  237  1                                  12    
HELIX    8 AA8 THR A  243  GLY A  258  1                                  16    
HELIX    9 AA9 ALA A  260  GLY A  275  1                                  16    
HELIX   10 AB1 THR A  292  GLY A  302  1                                  11    
SHEET    1 AA1 7 VAL A  73  LEU A  75  0                                        
SHEET    2 AA1 7 PHE A  66  ALA A  70 -1  N  VAL A  68   O  LEU A  75           
SHEET    3 AA1 7 MET A  17  CYS A  22 -1  N  THR A  21   O  LEU A  67           
SHEET    4 AA1 7 THR A  25  LEU A  32 -1  O  GLY A  29   N  VAL A  18           
SHEET    5 AA1 7 VAL A  35  PRO A  39 -1  O  TYR A  37   N  LEU A  30           
SHEET    6 AA1 7 VAL A  86  VAL A  91 -1  O  LEU A  87   N  CYS A  38           
SHEET    7 AA1 7 VAL A  77  GLN A  83 -1  N  GLN A  83   O  VAL A  86           
SHEET    1 AA2 5 LYS A 100  PHE A 103  0                                        
SHEET    2 AA2 5 CYS A 156  GLU A 166  1  O  VAL A 157   N  LYS A 100           
SHEET    3 AA2 5 VAL A 148  ASP A 153 -1  N  ASN A 151   O  SER A 158           
SHEET    4 AA2 5 THR A 111  TYR A 118 -1  N  SER A 113   O  PHE A 150           
SHEET    5 AA2 5 SER A 121  ALA A 129 -1  O  SER A 123   N  ALA A 116           
SHEET    1 AA3 3 LYS A 100  PHE A 103  0                                        
SHEET    2 AA3 3 CYS A 156  GLU A 166  1  O  VAL A 157   N  LYS A 100           
SHEET    3 AA3 3 HIS A 172  THR A 175 -1  O  ALA A 173   N  MET A 165           
CRYST1  113.191   53.060   44.309  90.00 103.01  90.00 C 1 2 1       4          
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      0.008835  0.000000  0.002041        0.00000                         
SCALE2      0.000000  0.018847  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023163        0.00000                         
ATOM      1  N   SER A   1      -2.092   4.622 -16.902  1.00 23.89           N  
ANISOU    1  N   SER A   1     2719   3701   2659   -919  -1060    409       N  
ATOM      2  CA  SER A   1      -2.486   5.906 -16.342  1.00 24.82           C  
ANISOU    2  CA  SER A   1     2708   3873   2849   -874  -1026    453       C  
ATOM      3  C   SER A   1      -2.581   5.867 -14.821  1.00 25.24           C  
ANISOU    3  C   SER A   1     2664   3957   2967   -812   -977    459       C  
ATOM      4  O   SER A   1      -3.012   4.866 -14.244  1.00 26.02           O  
ANISOU    4  O   SER A   1     2758   4049   3078   -833  -1008    481       O  
ATOM      5  CB  SER A   1      -3.827   6.341 -16.912  1.00 26.91           C  
ANISOU    5  CB  SER A   1     2926   4159   3141   -941  -1108    560       C  
ATOM      6  OG  SER A   1      -4.784   5.296 -16.814  1.00 28.94           O  
ANISOU    6  OG  SER A   1     3186   4405   3404  -1011  -1192    626       O  
ATOM      7  N   GLY A   2      -2.214   6.966 -14.186  1.00 24.39           N  
ANISOU    7  N   GLY A   2     2486   3881   2901   -739   -904    443       N  
ATOM      8  CA  GLY A   2      -2.275   7.057 -12.740  1.00 24.98           C  
ANISOU    8  CA  GLY A   2     2479   3981   3031   -676   -853    448       C  
ATOM      9  C   GLY A   2      -1.008   6.540 -12.092  1.00 25.53           C  
ANISOU    9  C   GLY A   2     2589   4031   3078   -626   -793    355       C  
ATOM     10  O   GLY A   2      -0.381   5.578 -12.565  1.00 26.41           O  
ANISOU   10  O   GLY A   2     2789   4108   3139   -651   -805    305       O  
ATOM     11  N   PHE A   3      -0.649   7.160 -10.992  1.00 24.47           N  
ANISOU   11  N   PHE A   3     2397   3919   2982   -557   -728    336       N  
ATOM     12  CA  PHE A   3       0.551   6.803 -10.266  1.00 24.25           C  
ANISOU   12  CA  PHE A   3     2394   3877   2942   -508   -673    259       C  
ATOM     13  C   PHE A   3       0.221   6.718  -8.772  1.00 23.46           C  
ANISOU   13  C   PHE A   3     2229   3796   2889   -464   -644    278       C  
ATOM     14  O   PHE A   3      -0.242   7.686  -8.174  1.00 24.47           O  
ANISOU   14  O   PHE A   3     2294   3947   3055   -427   -616    314       O  
ATOM     15  CB  PHE A   3       1.660   7.817 -10.575  1.00 23.80           C  
ANISOU   15  CB  PHE A   3     2352   3819   2872   -469   -621    206       C  
ATOM     16  CG  PHE A   3       3.031   7.260 -10.305  1.00 24.00           C  
ANISOU   16  CG  PHE A   3     2423   3822   2873   -439   -579    131       C  
ATOM     17  CD1 PHE A   3       3.599   6.338 -11.160  1.00 24.79           C  
ANISOU   17  CD1 PHE A   3     2606   3889   2924   -467   -591     97       C  
ATOM     18  CD2 PHE A   3       3.713   7.592  -9.154  1.00 24.51           C  
ANISOU   18  CD2 PHE A   3     2453   3896   2965   -385   -530    102       C  
ATOM     19  CE1 PHE A   3       4.851   5.811 -10.901  1.00 25.56           C  
ANISOU   19  CE1 PHE A   3     2738   3966   3006   -434   -546     39       C  
ATOM     20  CE2 PHE A   3       4.966   7.068  -8.901  1.00 25.60           C  
ANISOU   20  CE2 PHE A   3     2624   4016   3088   -360   -496     46       C  
ATOM     21  CZ  PHE A   3       5.524   6.169  -9.770  1.00 25.47           C  
ANISOU   21  CZ  PHE A   3     2678   3970   3029   -382   -501     18       C  
ATOM     22  N   ARG A   4       0.422   5.555  -8.191  1.00 21.78           N  
ANISOU   22  N   ARG A   4     2036   3570   2670   -466   -648    256       N  
ATOM     23  CA  ARG A   4       0.078   5.298  -6.798  1.00 21.91           C  
ANISOU   23  CA  ARG A   4     1999   3601   2726   -429   -625    275       C  
ATOM     24  C   ARG A   4       1.246   4.870  -5.952  1.00 22.57           C  
ANISOU   24  C   ARG A   4     2104   3671   2799   -387   -580    205       C  
ATOM     25  O   ARG A   4       2.142   4.203  -6.445  1.00 22.15           O  
ANISOU   25  O   ARG A   4     2112   3594   2710   -399   -581    153       O  
ATOM     26  CB  ARG A   4      -0.977   4.183  -6.741  1.00 21.80           C  
ANISOU   26  CB  ARG A   4     1974   3586   2723   -476   -683    334       C  
ATOM     27  CG  ARG A   4      -2.396   4.678  -6.958  1.00 22.19           C  
ANISOU   27  CG  ARG A   4     1960   3661   2812   -502   -719    435       C  
ATOM     28  CD  ARG A   4      -2.913   5.317  -5.684  1.00 25.36           C  
ANISOU   28  CD  ARG A   4     2281   4088   3265   -438   -667    477       C  
ATOM     29  NE  ARG A   4      -4.309   5.734  -5.830  1.00 28.78           N  
ANISOU   29  NE  ARG A   4     2644   4547   3746   -455   -694    588       N  
ATOM     30  CZ  ARG A   4      -5.069   6.193  -4.842  1.00 28.33           C  
ANISOU   30  CZ  ARG A   4     2514   4512   3739   -405   -652    654       C  
ATOM     31  NH1 ARG A   4      -4.582   6.292  -3.613  1.00 28.32           N  
ANISOU   31  NH1 ARG A   4     2511   4509   3742   -338   -587    613       N  
ATOM     32  NH2 ARG A   4      -6.320   6.558  -5.077  1.00 25.31           N  
ANISOU   32  NH2 ARG A   4     2062   4151   3402   -421   -675    765       N  
ATOM     33  N   LYS A   5       1.192   5.167  -4.644  1.00 23.44           N  
ANISOU   33  N   LYS A   5     2170   3796   2940   -337   -542    211       N  
ATOM     34  CA  LYS A   5       2.188   4.690  -3.700  1.00 24.30           C  
ANISOU   34  CA  LYS A   5     2295   3894   3045   -302   -508    155       C  
ATOM     35  C   LYS A   5       1.868   3.201  -3.519  1.00 25.80           C  
ANISOU   35  C   LYS A   5     2499   4073   3230   -331   -540    163       C  
ATOM     36  O   LYS A   5       0.891   2.826  -2.854  1.00 27.67           O  
ANISOU   36  O   LYS A   5     2696   4323   3495   -333   -554    215       O  
ATOM     37  CB  LYS A   5       2.093   5.457  -2.379  1.00 24.98           C  
ANISOU   37  CB  LYS A   5     2341   3994   3158   -247   -465    165       C  
ATOM     38  CG  LYS A   5       3.100   4.979  -1.336  1.00 28.07           C  
ANISOU   38  CG  LYS A   5     2749   4374   3545   -216   -437    114       C  
ATOM     39  CD  LYS A   5       4.537   5.353  -1.663  1.00 31.28           C  
ANISOU   39  CD  LYS A   5     3189   4766   3930   -208   -418     54       C  
ATOM     40  CE  LYS A   5       4.767   6.848  -1.705  1.00 34.67           C  
ANISOU   40  CE  LYS A   5     3610   5199   4362   -185   -395     53       C  
ATOM     41  NZ  LYS A   5       4.294   7.554  -0.486  1.00 35.22           N  
ANISOU   41  NZ  LYS A   5     3660   5274   4448   -145   -369     75       N  
ATOM     42  N   MET A   6       2.598   2.366  -4.247  1.00 25.01           N  
ANISOU   42  N   MET A   6     2460   3947   3095   -357   -554    120       N  
ATOM     43  CA  MET A   6       2.326   0.941  -4.278  1.00 24.56           C  
ANISOU   43  CA  MET A   6     2434   3871   3025   -392   -588    125       C  
ATOM     44  C   MET A   6       3.280   0.184  -3.430  1.00 22.87           C  
ANISOU   44  C   MET A   6     2236   3645   2810   -360   -556     77       C  
ATOM     45  O   MET A   6       4.479   0.435  -3.482  1.00 21.96           O  
ANISOU   45  O   MET A   6     2143   3520   2682   -331   -517     27       O  
ATOM     46  CB  MET A   6       2.546   0.431  -5.694  1.00 26.40           C  
ANISOU   46  CB  MET A   6     2747   4074   3212   -441   -621    108       C  
ATOM     47  CG  MET A   6       1.333   0.370  -6.489  1.00 31.94           C  
ANISOU   47  CG  MET A   6     3450   4777   3909   -500   -685    168       C  
ATOM     48  SD  MET A   6       1.728  -0.631  -7.923  1.00 42.08           S  
ANISOU   48  SD  MET A   6     4857   6007   5122   -559   -724    137       S  
ATOM     49  CE  MET A   6       0.362  -0.210  -8.948  1.00 41.85           C  
ANISOU   49  CE  MET A   6     4823   5986   5090   -631   -803    213       C  
ATOM     50  N   ALA A   7       2.774  -0.831  -2.762  1.00 22.41           N  
ANISOU   50  N   ALA A   7     2167   3584   2763   -370   -575     97       N  
ATOM     51  CA  ALA A   7       3.601  -1.755  -2.018  1.00 22.86           C  
ANISOU   51  CA  ALA A   7     2242   3625   2817   -347   -551     57       C  
ATOM     52  C   ALA A   7       3.749  -3.033  -2.843  1.00 23.63           C  
ANISOU   52  C   ALA A   7     2415   3686   2878   -388   -580     41       C  
ATOM     53  O   ALA A   7       2.936  -3.292  -3.734  1.00 23.40           O  
ANISOU   53  O   ALA A   7     2416   3645   2831   -441   -631     72       O  
ATOM     54  CB  ALA A   7       2.957  -2.076  -0.685  1.00 22.87           C  
ANISOU   54  CB  ALA A   7     2189   3646   2853   -327   -550     89       C  
ATOM     55  N   PHE A   8       4.780  -3.845  -2.565  1.00 23.86           N  
ANISOU   55  N   PHE A   8     2480   3691   2894   -366   -550     -4       N  
ATOM     56  CA  PHE A   8       4.908  -5.137  -3.225  1.00 24.87           C  
ANISOU   56  CA  PHE A   8     2688   3776   2984   -398   -570    -19       C  
ATOM     57  C   PHE A   8       3.750  -6.041  -2.738  1.00 24.23           C  
ANISOU   57  C   PHE A   8     2594   3696   2918   -436   -623     25       C  
ATOM     58  O   PHE A   8       3.238  -5.863  -1.622  1.00 23.24           O  
ANISOU   58  O   PHE A   8     2392   3602   2834   -417   -621     55       O  
ATOM     59  CB  PHE A   8       6.254  -5.777  -2.874  1.00 25.48           C  
ANISOU   59  CB  PHE A   8     2794   3831   3054   -356   -517    -67       C  
ATOM     60  CG  PHE A   8       7.418  -5.083  -3.527  1.00 27.17           C  
ANISOU   60  CG  PHE A   8     3031   4038   3254   -326   -467   -100       C  
ATOM     61  CD1 PHE A   8       7.797  -5.399  -4.821  1.00 28.16           C  
ANISOU   61  CD1 PHE A   8     3246   4123   3331   -341   -460   -118       C  
ATOM     62  CD2 PHE A   8       8.132  -4.110  -2.854  1.00 28.61           C  
ANISOU   62  CD2 PHE A   8     3152   4251   3470   -282   -430   -109       C  
ATOM     63  CE1 PHE A   8       8.853  -4.741  -5.431  1.00 29.06           C  
ANISOU   63  CE1 PHE A   8     3376   4232   3435   -309   -410   -141       C  
ATOM     64  CE2 PHE A   8       9.193  -3.456  -3.470  1.00 29.67           C  
ANISOU   64  CE2 PHE A   8     3299   4378   3595   -257   -389   -130       C  
ATOM     65  CZ  PHE A   8       9.568  -3.800  -4.741  1.00 29.24           C  
ANISOU   65  CZ  PHE A   8     3323   4288   3497   -268   -375   -145       C  
ATOM     66  N   PRO A   9       3.290  -7.015  -3.559  1.00 24.45           N  
ANISOU   66  N   PRO A   9     2696   3686   2909   -492   -673     36       N  
ATOM     67  CA  PRO A   9       2.280  -7.974  -3.053  1.00 24.18           C  
ANISOU   67  CA  PRO A   9     2648   3649   2891   -531   -726     81       C  
ATOM     68  C   PRO A   9       2.891  -8.668  -1.815  1.00 24.09           C  
ANISOU   68  C   PRO A   9     2610   3640   2903   -484   -685     56       C  
ATOM     69  O   PRO A   9       4.097  -8.944  -1.818  1.00 24.68           O  
ANISOU   69  O   PRO A   9     2725   3694   2959   -447   -634      2       O  
ATOM     70  CB  PRO A   9       2.068  -8.934  -4.241  1.00 24.71           C  
ANISOU   70  CB  PRO A   9     2829   3659   2900   -597   -780     79       C  
ATOM     71  CG  PRO A   9       2.604  -8.181  -5.446  1.00 25.48           C  
ANISOU   71  CG  PRO A   9     2985   3741   2955   -598   -763     50       C  
ATOM     72  CD  PRO A   9       3.776  -7.403  -4.895  1.00 24.14           C  
ANISOU   72  CD  PRO A   9     2768   3596   2808   -520   -678      5       C  
ATOM     73  N   SER A  10       2.137  -8.789  -0.730  1.00 23.52           N  
ANISOU   73  N   SER A  10     2463   3599   2875   -479   -698     98       N  
ATOM     74  CA  SER A  10       2.703  -9.267   0.540  1.00 23.46           C  
ANISOU   74  CA  SER A  10     2422   3600   2891   -431   -657     77       C  
ATOM     75  C   SER A  10       2.644 -10.768   0.799  1.00 22.42           C  
ANISOU   75  C   SER A  10     2331   3436   2750   -453   -679     75       C  
ATOM     76  O   SER A  10       3.178 -11.220   1.798  1.00 22.19           O  
ANISOU   76  O   SER A  10     2279   3412   2739   -414   -646     56       O  
ATOM     77  CB  SER A  10       2.061  -8.537   1.716  1.00 24.28           C  
ANISOU   77  CB  SER A  10     2428   3752   3045   -399   -643    118       C  
ATOM     78  OG  SER A  10       0.660  -8.724   1.777  1.00 26.09           O  
ANISOU   78  OG  SER A  10     2619   3996   3299   -438   -695    192       O  
ATOM     79  N   GLY A  11       1.959 -11.520  -0.042  1.00 21.91           N  
ANISOU   79  N   GLY A  11     2327   3338   2658   -517   -741     99       N  
ATOM     80  CA  GLY A  11       1.782 -12.961   0.147  1.00 21.89           C  
ANISOU   80  CA  GLY A  11     2373   3301   2645   -547   -771    103       C  
ATOM     81  C   GLY A  11       3.002 -13.753   0.576  1.00 21.11           C  
ANISOU   81  C   GLY A  11     2315   3174   2532   -502   -715     45       C  
ATOM     82  O   GLY A  11       2.949 -14.513   1.550  1.00 21.87           O  
ANISOU   82  O   GLY A  11     2382   3274   2653   -488   -712     53       O  
ATOM     83  N   LYS A  12       4.114 -13.547  -0.122  1.00 20.20           N  
ANISOU   83  N   LYS A  12     2260   3032   2381   -474   -668     -8       N  
ATOM     84  CA  LYS A  12       5.341 -14.274   0.165  1.00 19.94           C  
ANISOU   84  CA  LYS A  12     2266   2970   2338   -428   -608    -54       C  
ATOM     85  C   LYS A  12       5.858 -14.027   1.583  1.00 19.66           C  
ANISOU   85  C   LYS A  12     2137   2979   2355   -371   -564    -58       C  
ATOM     86  O   LYS A  12       6.449 -14.921   2.179  1.00 20.34           O  
ANISOU   86  O   LYS A  12     2234   3048   2448   -347   -538    -74       O  
ATOM     87  CB  LYS A  12       6.407 -13.950  -0.888  1.00 20.93           C  
ANISOU   87  CB  LYS A  12     2464   3064   2423   -404   -559    -96       C  
ATOM     88  CG  LYS A  12       6.220 -14.741  -2.169  1.00 25.31           C  
ANISOU   88  CG  LYS A  12     3154   3552   2912   -451   -587   -106       C  
ATOM     89  CD  LYS A  12       6.903 -14.067  -3.360  1.00 31.43           C  
ANISOU   89  CD  LYS A  12     3992   4306   3646   -438   -551   -132       C  
ATOM     90  CE  LYS A  12       6.466 -14.694  -4.670  1.00 35.33           C  
ANISOU   90  CE  LYS A  12     4628   4730   4064   -495   -592   -136       C  
ATOM     91  NZ  LYS A  12       7.383 -15.789  -5.079  1.00 37.35           N  
ANISOU   91  NZ  LYS A  12     5000   4916   4273   -464   -535   -173       N  
ATOM     92  N   VAL A  13       5.583 -12.838   2.144  1.00 18.84           N  
ANISOU   92  N   VAL A  13     1946   2926   2285   -352   -560    -40       N  
ATOM     93  CA  VAL A  13       6.012 -12.464   3.484  1.00 18.10           C  
ANISOU   93  CA  VAL A  13     1774   2869   2232   -303   -525    -42       C  
ATOM     94  C   VAL A  13       5.000 -12.907   4.532  1.00 18.20           C  
ANISOU   94  C   VAL A  13     1734   2905   2276   -314   -555     -1       C  
ATOM     95  O   VAL A  13       5.397 -13.362   5.606  1.00 18.67           O  
ANISOU   95  O   VAL A  13     1765   2972   2356   -284   -533     -7       O  
ATOM     96  CB  VAL A  13       6.375 -10.960   3.565  1.00 17.93           C  
ANISOU   96  CB  VAL A  13     1705   2883   2224   -273   -497    -49       C  
ATOM     97  CG1 VAL A  13       6.923 -10.609   4.936  1.00 18.15           C  
ANISOU   97  CG1 VAL A  13     1672   2939   2284   -228   -465    -53       C  
ATOM     98  CG2 VAL A  13       7.391 -10.596   2.480  1.00 17.72           C  
ANISOU   98  CG2 VAL A  13     1731   2834   2170   -263   -466    -84       C  
ATOM     99  N   GLU A  14       3.692 -12.874   4.201  1.00 17.70           N  
ANISOU   99  N   GLU A  14     1660   2849   2216   -359   -608     48       N  
ATOM    100  CA  GLU A  14       2.633 -13.373   5.063  1.00 17.53           C  
ANISOU  100  CA  GLU A  14     1588   2846   2227   -374   -640    100       C  
ATOM    101  C   GLU A  14       2.875 -14.815   5.490  1.00 19.23           C  
ANISOU  101  C   GLU A  14     1836   3032   2438   -380   -646     90       C  
ATOM    102  O   GLU A  14       2.682 -15.129   6.653  1.00 20.60           O  
ANISOU  102  O   GLU A  14     1959   3226   2642   -357   -636    108       O  
ATOM    103  CB  GLU A  14       1.269 -13.294   4.372  1.00 16.96           C  
ANISOU  103  CB  GLU A  14     1509   2778   2158   -433   -704    163       C  
ATOM    104  CG  GLU A  14       0.825 -11.881   4.102  1.00 18.71           C  
ANISOU  104  CG  GLU A  14     1683   3033   2393   -424   -698    189       C  
ATOM    105  CD  GLU A  14      -0.473 -11.848   3.337  1.00 22.27           C  
ANISOU  105  CD  GLU A  14     2126   3486   2850   -487   -765    259       C  
ATOM    106  OE1 GLU A  14      -1.408 -12.602   3.684  1.00 24.53           O  
ANISOU  106  OE1 GLU A  14     2386   3774   3160   -520   -810    318       O  
ATOM    107  OE2 GLU A  14      -0.545 -11.071   2.367  1.00 22.45           O  
ANISOU  107  OE2 GLU A  14     2167   3508   2855   -506   -778    259       O  
ATOM    108  N   GLY A  15       3.323 -15.663   4.559  1.00 19.34           N  
ANISOU  108  N   GLY A  15     1940   2996   2413   -408   -658     60       N  
ATOM    109  CA  GLY A  15       3.600 -17.066   4.857  1.00 20.18           C  
ANISOU  109  CA  GLY A  15     2091   3065   2510   -414   -661     47       C  
ATOM    110  C   GLY A  15       4.801 -17.295   5.760  1.00 19.95           C  
ANISOU  110  C   GLY A  15     2044   3041   2496   -352   -598      9       C  
ATOM    111  O   GLY A  15       5.104 -18.432   6.103  1.00 20.59           O  
ANISOU  111  O   GLY A  15     2154   3094   2575   -349   -593      0       O  
ATOM    112  N   CYS A  16       5.512 -16.226   6.120  1.00 19.22           N  
ANISOU  112  N   CYS A  16     1904   2980   2418   -306   -553    -11       N  
ATOM    113  CA  CYS A  16       6.676 -16.275   6.997  1.00 18.72           C  
ANISOU  113  CA  CYS A  16     1815   2925   2373   -253   -501    -38       C  
ATOM    114  C   CYS A  16       6.403 -15.684   8.377  1.00 18.31           C  
ANISOU  114  C   CYS A  16     1679   2920   2357   -225   -494    -16       C  
ATOM    115  O   CYS A  16       7.278 -15.761   9.227  1.00 18.16           O  
ANISOU  115  O   CYS A  16     1639   2909   2354   -189   -462    -31       O  
ATOM    116  CB  CYS A  16       7.867 -15.579   6.346  1.00 19.49           C  
ANISOU  116  CB  CYS A  16     1934   3014   2456   -224   -456    -73       C  
ATOM    117  SG  CYS A  16       8.306 -16.245   4.727  1.00 22.30           S  
ANISOU  117  SG  CYS A  16     2403   3308   2762   -243   -446    -99       S  
ATOM    118  N   MET A  17       5.255 -15.027   8.587  1.00 17.80           N  
ANISOU  118  N   MET A  17     1572   2885   2305   -240   -521     23       N  
ATOM    119  CA  MET A  17       4.991 -14.395   9.871  1.00 18.11           C  
ANISOU  119  CA  MET A  17     1547   2963   2371   -207   -506     44       C  
ATOM    120  C   MET A  17       4.558 -15.380  10.947  1.00 18.58           C  
ANISOU  120  C   MET A  17     1583   3026   2451   -203   -514     69       C  
ATOM    121  O   MET A  17       3.656 -16.195  10.745  1.00 18.97           O  
ANISOU  121  O   MET A  17     1637   3066   2506   -238   -551    103       O  
ATOM    122  CB  MET A  17       3.998 -13.223   9.725  1.00 18.31           C  
ANISOU  122  CB  MET A  17     1537   3017   2405   -211   -516     80       C  
ATOM    123  CG  MET A  17       4.489 -12.124   8.771  1.00 18.77           C  
ANISOU  123  CG  MET A  17     1614   3074   2444   -210   -504     53       C  
ATOM    124  SD  MET A  17       6.224 -11.628   8.946  1.00 20.32           S  
ANISOU  124  SD  MET A  17     1826   3264   2631   -171   -458     -4       S  
ATOM    125  CE  MET A  17       6.239 -11.035  10.679  1.00 24.22           C  
ANISOU  125  CE  MET A  17     2272   3787   3145   -129   -436      9       C  
ATOM    126  N   VAL A  18       5.264 -15.355  12.058  1.00 18.11           N  
ANISOU  126  N   VAL A  18     1502   2976   2402   -165   -484     54       N  
ATOM    127  CA  VAL A  18       4.928 -16.197  13.210  1.00 17.44           C  
ANISOU  127  CA  VAL A  18     1392   2898   2336   -155   -486     78       C  
ATOM    128  C   VAL A  18       4.876 -15.301  14.468  1.00 17.28           C  
ANISOU  128  C   VAL A  18     1334   2907   2324   -114   -460     90       C  
ATOM    129  O   VAL A  18       5.313 -14.142  14.438  1.00 16.29           O  
ANISOU  129  O   VAL A  18     1210   2792   2189    -96   -442     72       O  
ATOM    130  CB  VAL A  18       5.923 -17.364  13.393  1.00 17.40           C  
ANISOU  130  CB  VAL A  18     1414   2866   2330   -150   -477     48       C  
ATOM    131  CG1 VAL A  18       5.904 -18.304  12.191  1.00 17.90           C  
ANISOU  131  CG1 VAL A  18     1533   2890   2376   -187   -498     37       C  
ATOM    132  CG2 VAL A  18       7.318 -16.835  13.674  1.00 17.04           C  
ANISOU  132  CG2 VAL A  18     1370   2822   2282   -117   -443     12       C  
ATOM    133  N   GLN A  19       4.305 -15.829  15.545  1.00 17.53           N  
ANISOU  133  N   GLN A  19     1340   2950   2372   -102   -459    122       N  
ATOM    134  CA  GLN A  19       4.259 -15.132  16.804  1.00 18.98           C  
ANISOU  134  CA  GLN A  19     1504   3153   2556    -61   -432    133       C  
ATOM    135  C   GLN A  19       5.316 -15.748  17.721  1.00 19.04           C  
ANISOU  135  C   GLN A  19     1521   3152   2562    -45   -422    106       C  
ATOM    136  O   GLN A  19       5.430 -16.978  17.817  1.00 19.46           O  
ANISOU  136  O   GLN A  19     1574   3193   2626    -57   -434    108       O  
ATOM    137  CB  GLN A  19       2.856 -15.251  17.405  1.00 21.57           C  
ANISOU  137  CB  GLN A  19     1795   3498   2901    -53   -431    197       C  
ATOM    138  CG  GLN A  19       2.770 -14.822  18.854  1.00 25.18           C  
ANISOU  138  CG  GLN A  19     2246   3968   3354     -7   -396    212       C  
ATOM    139  CD  GLN A  19       1.474 -15.310  19.421  1.00 29.97           C  
ANISOU  139  CD  GLN A  19     2814   4588   3986      1   -393    281       C  
ATOM    140  OE1 GLN A  19       1.412 -16.317  20.131  1.00 31.79           O  
ANISOU  140  OE1 GLN A  19     3034   4817   4228      3   -397    294       O  
ATOM    141  NE2 GLN A  19       0.405 -14.627  19.084  1.00 30.80           N  
ANISOU  141  NE2 GLN A  19     2893   4708   4104      7   -384    332       N  
ATOM    142  N   VAL A  20       6.087 -14.900  18.393  1.00 18.50           N  
ANISOU  142  N   VAL A  20     1463   3087   2479    -20   -404     85       N  
ATOM    143  CA  VAL A  20       7.106 -15.358  19.316  1.00 18.11           C  
ANISOU  143  CA  VAL A  20     1420   3031   2429     -8   -401     68       C  
ATOM    144  C   VAL A  20       6.780 -14.775  20.686  1.00 18.61           C  
ANISOU  144  C   VAL A  20     1489   3105   2478     22   -385     87       C  
ATOM    145  O   VAL A  20       6.633 -13.561  20.830  1.00 18.53           O  
ANISOU  145  O   VAL A  20     1495   3097   2447     38   -372     86       O  
ATOM    146  CB  VAL A  20       8.542 -14.930  18.902  1.00 18.41           C  
ANISOU  146  CB  VAL A  20     1474   3059   2462    -12   -401     32       C  
ATOM    147  CG1 VAL A  20       9.583 -15.475  19.874  1.00 17.85           C  
ANISOU  147  CG1 VAL A  20     1402   2983   2398     -4   -403     27       C  
ATOM    148  CG2 VAL A  20       8.865 -15.306  17.454  1.00 18.96           C  
ANISOU  148  CG2 VAL A  20     1551   3115   2539    -33   -404     14       C  
ATOM    149  N   THR A  21       6.728 -15.626  21.695  1.00 19.25           N  
ANISOU  149  N   THR A  21     1564   3186   2566     32   -385    102       N  
ATOM    150  CA  THR A  21       6.459 -15.197  23.056  1.00 21.05           C  
ANISOU  150  CA  THR A  21     1808   3417   2774     62   -368    119       C  
ATOM    151  C   THR A  21       7.595 -15.635  23.929  1.00 22.87           C  
ANISOU  151  C   THR A  21     2054   3638   2999     61   -380    102       C  
ATOM    152  O   THR A  21       8.052 -16.768  23.821  1.00 22.89           O  
ANISOU  152  O   THR A  21     2035   3637   3024     47   -393     98       O  
ATOM    153  CB  THR A  21       5.123 -15.786  23.561  1.00 22.81           C  
ANISOU  153  CB  THR A  21     2007   3651   3010     78   -353    168       C  
ATOM    154  OG1 THR A  21       4.048 -15.348  22.716  1.00 23.46           O  
ANISOU  154  OG1 THR A  21     2067   3743   3103     76   -346    196       O  
ATOM    155  CG2 THR A  21       4.832 -15.430  25.038  1.00 23.42           C  
ANISOU  155  CG2 THR A  21     2110   3727   3062    117   -326    190       C  
ATOM    156  N   CYS A  22       8.075 -14.741  24.783  1.00 24.29           N  
ANISOU  156  N   CYS A  22     2272   3811   3147     74   -378     95       N  
ATOM    157  CA  CYS A  22       9.078 -15.098  25.767  1.00 26.60           C  
ANISOU  157  CA  CYS A  22     2581   4094   3431     69   -397     89       C  
ATOM    158  C   CYS A  22       8.597 -14.460  27.059  1.00 28.66           C  
ANISOU  158  C   CYS A  22     2893   4346   3650     96   -382    104       C  
ATOM    159  O   CYS A  22       8.361 -13.252  27.109  1.00 28.38           O  
ANISOU  159  O   CYS A  22     2900   4302   3582    109   -368    100       O  
ATOM    160  CB  CYS A  22      10.473 -14.623  25.372  1.00 27.77           C  
ANISOU  160  CB  CYS A  22     2735   4233   3581     44   -424     65       C  
ATOM    161  SG  CYS A  22      11.789 -15.251  26.450  1.00 34.39           S  
ANISOU  161  SG  CYS A  22     3578   5064   4426     28   -457     72       S  
ATOM    162  N   GLY A  23       8.305 -15.286  28.052  1.00 30.31           N  
ANISOU  162  N   GLY A  23     3102   4556   3859    109   -376    125       N  
ATOM    163  CA  GLY A  23       7.752 -14.808  29.315  1.00 31.56           C  
ANISOU  163  CA  GLY A  23     3316   4703   3973    142   -353    143       C  
ATOM    164  C   GLY A  23       6.382 -14.206  29.083  1.00 32.59           C  
ANISOU  164  C   GLY A  23     3448   4839   4097    178   -305    169       C  
ATOM    165  O   GLY A  23       5.491 -14.885  28.576  1.00 33.46           O  
ANISOU  165  O   GLY A  23     3502   4968   4244    183   -291    196       O  
ATOM    166  N   THR A  24       6.237 -12.910  29.347  1.00 32.58           N  
ANISOU  166  N   THR A  24     3509   4819   4050    199   -284    165       N  
ATOM    167  CA  THR A  24       4.972 -12.216  29.097  1.00 33.33           C  
ANISOU  167  CA  THR A  24     3606   4918   4141    239   -233    197       C  
ATOM    168  C   THR A  24       5.054 -11.243  27.907  1.00 33.26           C  
ANISOU  168  C   THR A  24     3590   4912   4137    225   -238    177       C  
ATOM    169  O   THR A  24       4.150 -10.430  27.728  1.00 34.29           O  
ANISOU  169  O   THR A  24     3733   5040   4257    258   -196    202       O  
ATOM    170  CB  THR A  24       4.458 -11.537  30.377  1.00 35.74           C  
ANISOU  170  CB  THR A  24     3993   5197   4389    290   -185    220       C  
ATOM    171  OG1 THR A  24       5.267 -10.395  30.679  1.00 37.30           O  
ANISOU  171  OG1 THR A  24     4280   5362   4531    282   -199    185       O  
ATOM    172  CG2 THR A  24       4.430 -12.494  31.567  1.00 36.45           C  
ANISOU  172  CG2 THR A  24     4095   5285   4472    302   -182    238       C  
ATOM    173  N   THR A  25       6.122 -11.317  27.094  1.00 31.94           N  
ANISOU  173  N   THR A  25     3401   4747   3987    179   -284    139       N  
ATOM    174  CA  THR A  25       6.262 -10.433  25.936  1.00 31.19           C  
ANISOU  174  CA  THR A  25     3300   4655   3897    165   -290    120       C  
ATOM    175  C   THR A  25       5.988 -11.206  24.659  1.00 29.11           C  
ANISOU  175  C   THR A  25     2961   4415   3684    140   -303    123       C  
ATOM    176  O   THR A  25       6.587 -12.246  24.442  1.00 29.27           O  
ANISOU  176  O   THR A  25     2950   4441   3731    114   -330    111       O  
ATOM    177  CB  THR A  25       7.660  -9.814  25.911  1.00 33.36           C  
ANISOU  177  CB  THR A  25     3612   4912   4150    134   -329     80       C  
ATOM    178  OG1 THR A  25       7.841  -9.021  27.088  1.00 35.24           O  
ANISOU  178  OG1 THR A  25     3936   5121   4333    150   -323     79       O  
ATOM    179  CG2 THR A  25       7.900  -8.971  24.668  1.00 33.70           C  
ANISOU  179  CG2 THR A  25     3643   4959   4202    116   -336     61       C  
ATOM    180  N   THR A  26       5.093 -10.710  23.828  1.00 27.65           N  
ANISOU  180  N   THR A  26     2754   4240   3511    148   -283    142       N  
ATOM    181  CA  THR A  26       4.758 -11.335  22.554  1.00 26.80           C  
ANISOU  181  CA  THR A  26     2589   4149   3443    119   -301    148       C  
ATOM    182  C   THR A  26       5.045 -10.347  21.429  1.00 25.13           C  
ANISOU  182  C   THR A  26     2384   3937   3228    104   -308    125       C  
ATOM    183  O   THR A  26       4.609  -9.195  21.494  1.00 25.54           O  
ANISOU  183  O   THR A  26     2460   3985   3259    128   -282    135       O  
ATOM    184  CB  THR A  26       3.273 -11.745  22.532  1.00 28.28           C  
ANISOU  184  CB  THR A  26     2736   4352   3656    136   -280    207       C  
ATOM    185  OG1 THR A  26       3.103 -12.870  23.395  1.00 30.06           O  
ANISOU  185  OG1 THR A  26     2948   4581   3893    142   -280    227       O  
ATOM    186  CG2 THR A  26       2.783 -12.120  21.143  1.00 28.25           C  
ANISOU  186  CG2 THR A  26     2688   4362   3686    100   -304    220       C  
ATOM    187  N   LEU A  27       5.764 -10.787  20.406  1.00 22.93           N  
ANISOU  187  N   LEU A  27     2087   3659   2965     68   -337     96       N  
ATOM    188  CA  LEU A  27       5.995  -9.952  19.227  1.00 21.56           C  
ANISOU  188  CA  LEU A  27     1916   3486   2791     52   -343     77       C  
ATOM    189  C   LEU A  27       6.006 -10.833  17.953  1.00 19.16           C  
ANISOU  189  C   LEU A  27     1584   3185   2512     18   -366     70       C  
ATOM    190  O   LEU A  27       5.624 -12.000  18.021  1.00 19.28           O  
ANISOU  190  O   LEU A  27     1579   3201   2544      7   -375     87       O  
ATOM    191  CB  LEU A  27       7.223  -9.009  19.370  1.00 21.18           C  
ANISOU  191  CB  LEU A  27     1904   3424   2718     49   -350     40       C  
ATOM    192  CG  LEU A  27       8.474  -9.574  19.981  1.00 22.06           C  
ANISOU  192  CG  LEU A  27     2025   3526   2831     38   -371     20       C  
ATOM    193  CD1 LEU A  27       9.004 -10.720  19.150  1.00 22.84           C  
ANISOU  193  CD1 LEU A  27     2091   3627   2960     14   -385      9       C  
ATOM    194  CD2 LEU A  27       9.546  -8.502  20.063  1.00 22.52           C  
ANISOU  194  CD2 LEU A  27     2115   3571   2869     29   -385     -2       C  
ATOM    195  N   ASN A  28       6.402 -10.279  16.807  1.00 17.52           N  
ANISOU  195  N   ASN A  28     1381   2974   2302     -1   -373     49       N  
ATOM    196  CA  ASN A  28       6.425 -11.024  15.552  1.00 16.56           C  
ANISOU  196  CA  ASN A  28     1252   2848   2193    -32   -391     41       C  
ATOM    197  C   ASN A  28       7.788 -11.618  15.264  1.00 15.53           C  
ANISOU  197  C   ASN A  28     1134   2702   2065    -42   -396      5       C  
ATOM    198  O   ASN A  28       8.819 -11.076  15.652  1.00 14.75           O  
ANISOU  198  O   ASN A  28     1043   2600   1960    -32   -391    -14       O  
ATOM    199  CB  ASN A  28       5.954 -10.141  14.392  1.00 19.01           C  
ANISOU  199  CB  ASN A  28     1563   3163   2498    -45   -394     44       C  
ATOM    200  CG  ASN A  28       4.642  -9.483  14.716  1.00 23.16           C  
ANISOU  200  CG  ASN A  28     2069   3703   3026    -29   -383     89       C  
ATOM    201  OD1 ASN A  28       3.598 -10.144  14.771  1.00 24.69           O  
ANISOU  201  OD1 ASN A  28     2239   3905   3238    -37   -391    132       O  
ATOM    202  ND2 ASN A  28       4.679  -8.198  15.021  1.00 24.14           N  
ANISOU  202  ND2 ASN A  28     2206   3831   3136     -4   -361     88       N  
ATOM    203  N   GLY A  29       7.766 -12.721  14.550  1.00 15.61           N  
ANISOU  203  N   GLY A  29     1148   2699   2083    -63   -406      2       N  
ATOM    204  CA  GLY A  29       8.944 -13.440  14.110  1.00 15.64           C  
ANISOU  204  CA  GLY A  29     1167   2684   2091    -67   -401    -23       C  
ATOM    205  C   GLY A  29       8.856 -13.676  12.617  1.00 16.20           C  
ANISOU  205  C   GLY A  29     1266   2737   2153    -90   -405    -35       C  
ATOM    206  O   GLY A  29       7.755 -13.747  12.040  1.00 16.39           O  
ANISOU  206  O   GLY A  29     1295   2762   2171   -112   -424    -18       O  
ATOM    207  N   LEU A  30       9.999 -13.837  11.989  1.00 16.56           N  
ANISOU  207  N   LEU A  30     1331   2765   2198    -85   -387    -57       N  
ATOM    208  CA  LEU A  30      10.066 -14.114  10.557  1.00 17.45           C  
ANISOU  208  CA  LEU A  30     1485   2852   2293   -102   -383    -71       C  
ATOM    209  C   LEU A  30      10.631 -15.514  10.421  1.00 17.78           C  
ANISOU  209  C   LEU A  30     1557   2862   2337    -98   -368    -77       C  
ATOM    210  O   LEU A  30      11.770 -15.738  10.795  1.00 17.82           O  
ANISOU  210  O   LEU A  30     1551   2862   2359    -73   -341    -81       O  
ATOM    211  CB  LEU A  30      10.978 -13.105   9.860  1.00 17.68           C  
ANISOU  211  CB  LEU A  30     1519   2883   2318    -91   -361    -87       C  
ATOM    212  CG  LEU A  30      11.037 -13.246   8.343  1.00 18.93           C  
ANISOU  212  CG  LEU A  30     1728   3013   2452   -105   -352   -101       C  
ATOM    213  CD1 LEU A  30       9.761 -12.721   7.708  1.00 17.90           C  
ANISOU  213  CD1 LEU A  30     1608   2891   2303   -137   -385    -92       C  
ATOM    214  CD2 LEU A  30      12.240 -12.543   7.792  1.00 20.06           C  
ANISOU  214  CD2 LEU A  30     1871   3153   2598    -85   -319   -112       C  
ATOM    215  N   TRP A  31       9.846 -16.454   9.911  1.00 17.50           N  
ANISOU  215  N   TRP A  31     1559   2802   2287   -124   -388    -73       N  
ATOM    216  CA  TRP A  31      10.240 -17.854   9.793  1.00 17.36           C  
ANISOU  216  CA  TRP A  31     1583   2748   2266   -122   -375    -79       C  
ATOM    217  C   TRP A  31      10.675 -18.183   8.365  1.00 17.53           C  
ANISOU  217  C   TRP A  31     1681   2724   2256   -127   -354    -99       C  
ATOM    218  O   TRP A  31       9.854 -18.191   7.448  1.00 17.16           O  
ANISOU  218  O   TRP A  31     1681   2661   2180   -164   -383   -100       O  
ATOM    219  CB  TRP A  31       9.057 -18.726  10.257  1.00 17.00           C  
ANISOU  219  CB  TRP A  31     1537   2699   2222   -151   -415    -57       C  
ATOM    220  CG  TRP A  31       9.232 -20.220  10.236  1.00 17.93           C  
ANISOU  220  CG  TRP A  31     1701   2777   2335   -155   -412    -60       C  
ATOM    221  CD1 TRP A  31      10.393 -20.930  10.359  1.00 18.61           C  
ANISOU  221  CD1 TRP A  31     1805   2838   2428   -122   -369    -73       C  
ATOM    222  CD2 TRP A  31       8.170 -21.190  10.199  1.00 18.21           C  
ANISOU  222  CD2 TRP A  31     1764   2793   2363   -194   -455    -41       C  
ATOM    223  NE1 TRP A  31      10.125 -22.281  10.347  1.00 18.85           N  
ANISOU  223  NE1 TRP A  31     1881   2831   2450   -136   -378    -69       N  
ATOM    224  CE2 TRP A  31       8.764 -22.468  10.276  1.00 18.50           C  
ANISOU  224  CE2 TRP A  31     1844   2789   2396   -183   -434    -51       C  
ATOM    225  CE3 TRP A  31       6.784 -21.099  10.043  1.00 19.28           C  
ANISOU  225  CE3 TRP A  31     1892   2939   2495   -239   -509    -10       C  
ATOM    226  CZ2 TRP A  31       8.014 -23.643  10.212  1.00 18.93           C  
ANISOU  226  CZ2 TRP A  31     1942   2811   2440   -218   -470    -37       C  
ATOM    227  CZ3 TRP A  31       6.046 -22.265   9.968  1.00 19.95           C  
ANISOU  227  CZ3 TRP A  31     2012   2994   2573   -277   -549     10       C  
ATOM    228  CH2 TRP A  31       6.662 -23.518  10.064  1.00 19.65           C  
ANISOU  228  CH2 TRP A  31     2025   2914   2528   -268   -531     -6       C  
ATOM    229  N   LEU A  32      11.984 -18.392   8.173  1.00 17.91           N  
ANISOU  229  N   LEU A  32     1742   2753   2311    -91   -302   -109       N  
ATOM    230  CA  LEU A  32      12.584 -18.696   6.862  1.00 18.64           C  
ANISOU  230  CA  LEU A  32     1912   2798   2372    -81   -265   -125       C  
ATOM    231  C   LEU A  32      13.425 -19.928   7.060  1.00 19.15           C  
ANISOU  231  C   LEU A  32     2006   2825   2445    -49   -220   -123       C  
ATOM    232  O   LEU A  32      14.282 -19.955   7.952  1.00 18.99           O  
ANISOU  232  O   LEU A  32     1925   2826   2465    -16   -195   -107       O  
ATOM    233  CB  LEU A  32      13.503 -17.555   6.405  1.00 18.68           C  
ANISOU  233  CB  LEU A  32     1893   2819   2385    -55   -229   -128       C  
ATOM    234  CG  LEU A  32      12.855 -16.187   6.280  1.00 19.00           C  
ANISOU  234  CG  LEU A  32     1898   2899   2422    -78   -264   -129       C  
ATOM    235  CD1 LEU A  32      13.871 -15.155   5.910  1.00 19.50           C  
ANISOU  235  CD1 LEU A  32     1936   2975   2497    -52   -228   -129       C  
ATOM    236  CD2 LEU A  32      11.759 -16.202   5.238  1.00 18.72           C  
ANISOU  236  CD2 LEU A  32     1925   2844   2345   -121   -299   -138       C  
ATOM    237  N   ASP A  33      13.156 -20.976   6.267  1.00 19.36           N  
ANISOU  237  N   ASP A  33     2129   2794   2432    -62   -215   -134       N  
ATOM    238  CA  ASP A  33      13.817 -22.281   6.418  1.00 19.47           C  
ANISOU  238  CA  ASP A  33     2185   2763   2448    -31   -171   -131       C  
ATOM    239  C   ASP A  33      13.542 -22.790   7.866  1.00 19.32           C  
ANISOU  239  C   ASP A  33     2095   2776   2470    -34   -200   -114       C  
ATOM    240  O   ASP A  33      12.403 -22.643   8.308  1.00 19.22           O  
ANISOU  240  O   ASP A  33     2057   2789   2457    -76   -262   -109       O  
ATOM    241  CB  ASP A  33      15.313 -22.203   6.044  1.00 21.25           C  
ANISOU  241  CB  ASP A  33     2413   2972   2690     30    -87   -123       C  
ATOM    242  CG  ASP A  33      15.536 -21.750   4.620  1.00 25.16           C  
ANISOU  242  CG  ASP A  33     2986   3433   3141     36    -54   -138       C  
ATOM    243  OD1 ASP A  33      14.753 -22.161   3.739  1.00 24.36           O  
ANISOU  243  OD1 ASP A  33     2986   3287   2984      0    -79   -158       O  
ATOM    244  OD2 ASP A  33      16.490 -20.976   4.388  1.00 28.86           O  
ANISOU  244  OD2 ASP A  33     3415   3918   3631     73     -7   -125       O  
ATOM    245  N   ASP A  34      14.540 -23.278   8.615  1.00 18.87           N  
ANISOU  245  N   ASP A  34     1998   2721   2450      9   -157    -97       N  
ATOM    246  CA  ASP A  34      14.302 -23.723   9.973  1.00 19.00           C  
ANISOU  246  CA  ASP A  34     1951   2767   2502      6   -185    -81       C  
ATOM    247  C   ASP A  34      14.732 -22.674  11.000  1.00 18.73           C  
ANISOU  247  C   ASP A  34     1813   2795   2510     18   -194    -64       C  
ATOM    248  O   ASP A  34      15.148 -23.048  12.082  1.00 19.09           O  
ANISOU  248  O   ASP A  34     1807   2856   2589     34   -192    -45       O  
ATOM    249  CB  ASP A  34      14.988 -25.071  10.229  1.00 20.76           C  
ANISOU  249  CB  ASP A  34     2202   2948   2737     38   -141    -70       C  
ATOM    250  CG  ASP A  34      16.499 -25.058  10.063  1.00 24.91           C  
ANISOU  250  CG  ASP A  34     2712   3463   3291     96    -65    -50       C  
ATOM    251  OD1 ASP A  34      17.037 -24.057   9.512  1.00 23.95           O  
ANISOU  251  OD1 ASP A  34     2572   3356   3171    110    -43    -48       O  
ATOM    252  OD2 ASP A  34      17.143 -26.056  10.458  1.00 26.58           O  
ANISOU  252  OD2 ASP A  34     2926   3650   3524    129    -26    -31       O  
ATOM    253  N   VAL A  35      14.696 -21.377  10.645  1.00 18.10           N  
ANISOU  253  N   VAL A  35     1710   2743   2425     10   -205    -70       N  
ATOM    254  CA  VAL A  35      15.108 -20.327  11.566  1.00 18.91           C  
ANISOU  254  CA  VAL A  35     1731   2896   2559     17   -218    -56       C  
ATOM    255  C   VAL A  35      14.023 -19.268  11.680  1.00 18.24           C  
ANISOU  255  C   VAL A  35     1629   2844   2458    -15   -265    -65       C  
ATOM    256  O   VAL A  35      13.417 -18.872  10.676  1.00 19.04           O  
ANISOU  256  O   VAL A  35     1769   2936   2529    -35   -274    -81       O  
ATOM    257  CB  VAL A  35      16.477 -19.694  11.172  1.00 19.78           C  
ANISOU  257  CB  VAL A  35     1818   3007   2690     49   -173    -42       C  
ATOM    258  CG1 VAL A  35      16.918 -18.658  12.196  1.00 20.64           C  
ANISOU  258  CG1 VAL A  35     1851   3162   2829     47   -198    -23       C  
ATOM    259  CG2 VAL A  35      17.558 -20.766  10.993  1.00 20.07           C  
ANISOU  259  CG2 VAL A  35     1870   3008   2748     89   -115    -21       C  
ATOM    260  N   VAL A  36      13.765 -18.825  12.902  1.00 17.48           N  
ANISOU  260  N   VAL A  36     1479   2785   2379    -18   -293    -54       N  
ATOM    261  CA  VAL A  36      12.826 -17.737  13.191  1.00 16.73           C  
ANISOU  261  CA  VAL A  36     1364   2722   2272    -37   -327    -55       C  
ATOM    262  C   VAL A  36      13.616 -16.534  13.687  1.00 17.04           C  
ANISOU  262  C   VAL A  36     1364   2786   2324    -25   -325    -50       C  
ATOM    263  O   VAL A  36      14.350 -16.645  14.667  1.00 17.04           O  
ANISOU  263  O   VAL A  36     1333   2795   2345    -13   -325    -35       O  
ATOM    264  CB  VAL A  36      11.789 -18.184  14.232  1.00 16.55           C  
ANISOU  264  CB  VAL A  36     1323   2714   2252    -48   -357    -42       C  
ATOM    265  CG1 VAL A  36      10.861 -17.032  14.616  1.00 15.81           C  
ANISOU  265  CG1 VAL A  36     1208   2652   2149    -56   -379    -35       C  
ATOM    266  CG2 VAL A  36      10.997 -19.395  13.714  1.00 17.29           C  
ANISOU  266  CG2 VAL A  36     1455   2779   2334    -68   -368    -41       C  
ATOM    267  N   TYR A  37      13.492 -15.397  12.999  1.00 16.56           N  
ANISOU  267  N   TYR A  37     1309   2734   2249    -32   -328    -60       N  
ATOM    268  CA  TYR A  37      14.179 -14.153  13.340  1.00 16.72           C  
ANISOU  268  CA  TYR A  37     1302   2774   2276    -27   -332    -55       C  
ATOM    269  C   TYR A  37      13.222 -13.273  14.077  1.00 17.00           C  
ANISOU  269  C   TYR A  37     1330   2832   2296    -36   -359    -55       C  
ATOM    270  O   TYR A  37      12.103 -13.103  13.624  1.00 17.66           O  
ANISOU  270  O   TYR A  37     1428   2919   2363    -47   -367    -59       O  
ATOM    271  CB  TYR A  37      14.651 -13.416  12.060  1.00 16.43           C  
ANISOU  271  CB  TYR A  37     1280   2730   2233    -27   -312    -65       C  
ATOM    272  CG  TYR A  37      15.561 -14.281  11.224  1.00 17.15           C  
ANISOU  272  CG  TYR A  37     1389   2793   2335     -9   -272    -62       C  
ATOM    273  CD1 TYR A  37      15.043 -15.211  10.331  1.00 17.79           C  
ANISOU  273  CD1 TYR A  37     1521   2844   2394    -13   -257    -76       C  
ATOM    274  CD2 TYR A  37      16.944 -14.223  11.377  1.00 18.78           C  
ANISOU  274  CD2 TYR A  37     1564   2998   2573     11   -248    -38       C  
ATOM    275  CE1 TYR A  37      15.875 -16.041   9.595  1.00 19.29           C  
ANISOU  275  CE1 TYR A  37     1742   3000   2588     10   -211    -72       C  
ATOM    276  CE2 TYR A  37      17.786 -15.037  10.630  1.00 19.95           C  
ANISOU  276  CE2 TYR A  37     1729   3118   2734     37   -199    -26       C  
ATOM    277  CZ  TYR A  37      17.246 -15.956   9.750  1.00 20.77           C  
ANISOU  277  CZ  TYR A  37     1894   3187   2809     40   -177    -46       C  
ATOM    278  OH  TYR A  37      18.068 -16.794   9.034  1.00 23.04           O  
ANISOU  278  OH  TYR A  37     2213   3439   3104     72   -119    -35       O  
ATOM    279  N   CYS A  38      13.649 -12.680  15.185  1.00 16.70           N  
ANISOU  279  N   CYS A  38     1274   2807   2263    -32   -373    -45       N  
ATOM    280  CA  CYS A  38      12.800 -11.751  15.932  1.00 16.59           C  
ANISOU  280  CA  CYS A  38     1268   2808   2229    -33   -390    -43       C  
ATOM    281  C   CYS A  38      13.684 -10.741  16.695  1.00 17.05           C  
ANISOU  281  C   CYS A  38     1326   2869   2284    -34   -405    -37       C  
ATOM    282  O   CYS A  38      14.852 -11.028  16.954  1.00 17.03           O  
ANISOU  282  O   CYS A  38     1306   2862   2302    -37   -411    -26       O  
ATOM    283  CB  CYS A  38      11.854 -12.512  16.867  1.00 17.08           C  
ANISOU  283  CB  CYS A  38     1328   2874   2287    -27   -395    -31       C  
ATOM    284  SG  CYS A  38      12.616 -13.087  18.419  1.00 18.24           S  
ANISOU  284  SG  CYS A  38     1466   3021   2445    -20   -407    -17       S  
ATOM    285  N   PRO A  39      13.148  -9.572  17.090  1.00 17.14           N  
ANISOU  285  N   PRO A  39     1359   2886   2269    -34   -414    -40       N  
ATOM    286  CA  PRO A  39      13.958  -8.629  17.888  1.00 17.01           C  
ANISOU  286  CA  PRO A  39     1358   2864   2242    -42   -438    -34       C  
ATOM    287  C   PRO A  39      14.366  -9.259  19.221  1.00 16.51           C  
ANISOU  287  C   PRO A  39     1296   2796   2180    -43   -457    -19       C  
ATOM    288  O   PRO A  39      13.565  -9.943  19.864  1.00 15.25           O  
ANISOU  288  O   PRO A  39     1142   2639   2013    -30   -448    -16       O  
ATOM    289  CB  PRO A  39      13.004  -7.448  18.136  1.00 18.22           C  
ANISOU  289  CB  PRO A  39     1548   3015   2359    -33   -435    -41       C  
ATOM    290  CG  PRO A  39      11.909  -7.609  17.136  1.00 18.88           C  
ANISOU  290  CG  PRO A  39     1620   3109   2445    -25   -410    -46       C  
ATOM    291  CD  PRO A  39      11.777  -9.065  16.862  1.00 16.72           C  
ANISOU  291  CD  PRO A  39     1319   2838   2195    -26   -404    -42       C  
ATOM    292  N   ARG A  40      15.625  -9.061  19.614  1.00 16.97           N  
ANISOU  292  N   ARG A  40     1347   2848   2251    -61   -484     -3       N  
ATOM    293  CA  ARG A  40      16.145  -9.600  20.857  1.00 17.23           C  
ANISOU  293  CA  ARG A  40     1383   2877   2288    -69   -510     17       C  
ATOM    294  C   ARG A  40      15.426  -9.030  22.090  1.00 18.23           C  
ANISOU  294  C   ARG A  40     1568   2993   2366    -65   -524     13       C  
ATOM    295  O   ARG A  40      15.370  -9.713  23.099  1.00 18.98           O  
ANISOU  295  O   ARG A  40     1671   3085   2456    -62   -533     24       O  
ATOM    296  CB  ARG A  40      17.664  -9.414  20.950  1.00 17.09           C  
ANISOU  296  CB  ARG A  40     1340   2854   2298    -95   -543     47       C  
ATOM    297  CG  ARG A  40      18.105  -7.984  21.165  1.00 17.08           C  
ANISOU  297  CG  ARG A  40     1374   2842   2273   -121   -580     52       C  
ATOM    298  CD  ARG A  40      19.607  -7.936  21.296  1.00 18.48           C  
ANISOU  298  CD  ARG A  40     1516   3018   2488   -152   -619     95       C  
ATOM    299  NE  ARG A  40      20.097  -6.561  21.417  1.00 20.22           N  
ANISOU  299  NE  ARG A  40     1771   3225   2689   -184   -663    105       N  
ATOM    300  CZ  ARG A  40      21.341  -6.230  21.743  1.00 21.75           C  
ANISOU  300  CZ  ARG A  40     1946   3412   2906   -224   -716    151       C  
ATOM    301  NH1 ARG A  40      22.238  -7.172  22.010  1.00 19.13           N  
ANISOU  301  NH1 ARG A  40     1557   3089   2624   -231   -727    197       N  
ATOM    302  NH2 ARG A  40      21.690  -4.951  21.840  1.00 21.17           N  
ANISOU  302  NH2 ARG A  40     1912   3322   2809   -258   -760    158       N  
ATOM    303  N   HIS A  41      14.787  -7.839  21.981  1.00 18.60           N  
ANISOU  303  N   HIS A  41     1659   3032   2376    -59   -518     -2       N  
ATOM    304  CA  HIS A  41      14.072  -7.285  23.139  1.00 19.16           C  
ANISOU  304  CA  HIS A  41     1798   3087   2397    -47   -518     -3       C  
ATOM    305  C   HIS A  41      12.812  -8.114  23.517  1.00 19.53           C  
ANISOU  305  C   HIS A  41     1840   3143   2439    -12   -480     -1       C  
ATOM    306  O   HIS A  41      12.187  -7.809  24.530  1.00 20.40           O  
ANISOU  306  O   HIS A  41     2004   3239   2508      6   -471      4       O  
ATOM    307  CB  HIS A  41      13.777  -5.788  22.993  1.00 19.61           C  
ANISOU  307  CB  HIS A  41     1911   3126   2413    -45   -517    -15       C  
ATOM    308  CG  HIS A  41      12.724  -5.453  21.991  1.00 22.76           C  
ANISOU  308  CG  HIS A  41     2293   3538   2816    -20   -473    -26       C  
ATOM    309  ND1 HIS A  41      13.037  -4.798  20.815  1.00 24.67           N  
ANISOU  309  ND1 HIS A  41     2514   3786   3073    -32   -474    -36       N  
ATOM    310  CD2 HIS A  41      11.387  -5.655  22.038  1.00 24.12           C  
ANISOU  310  CD2 HIS A  41     2467   3717   2979     15   -432    -21       C  
ATOM    311  CE1 HIS A  41      11.890  -4.646  20.176  1.00 25.11           C  
ANISOU  311  CE1 HIS A  41     2560   3853   3128     -7   -437    -39       C  
ATOM    312  NE2 HIS A  41      10.870  -5.142  20.875  1.00 25.48           N  
ANISOU  312  NE2 HIS A  41     2617   3902   3163     21   -411    -27       N  
ATOM    313  N   VAL A  42      12.509  -9.208  22.783  1.00 18.80           N  
ANISOU  313  N   VAL A  42     1688   3070   2385     -6   -461      0       N  
ATOM    314  CA  VAL A  42      11.446 -10.125  23.181  1.00 18.53           C  
ANISOU  314  CA  VAL A  42     1641   3045   2355     17   -436     11       C  
ATOM    315  C   VAL A  42      11.750 -10.751  24.562  1.00 18.57           C  
ANISOU  315  C   VAL A  42     1666   3042   2349     19   -452     25       C  
ATOM    316  O   VAL A  42      10.825 -11.182  25.251  1.00 19.35           O  
ANISOU  316  O   VAL A  42     1774   3142   2435     43   -430     38       O  
ATOM    317  CB  VAL A  42      11.217 -11.251  22.150  1.00 18.78           C  
ANISOU  317  CB  VAL A  42     1616   3091   2427     14   -424     11       C  
ATOM    318  CG1 VAL A  42      12.372 -12.249  22.156  1.00 19.40           C  
ANISOU  318  CG1 VAL A  42     1665   3169   2538     -2   -442     13       C  
ATOM    319  CG2 VAL A  42       9.895 -11.959  22.423  1.00 18.45           C  
ANISOU  319  CG2 VAL A  42     1563   3058   2388     34   -402     29       C  
ATOM    320  N   ILE A  43      13.036 -10.843  24.956  1.00 18.16           N  
ANISOU  320  N   ILE A  43     1615   2982   2304     -8   -490     28       N  
ATOM    321  CA  ILE A  43      13.399 -11.403  26.261  1.00 19.29           C  
ANISOU  321  CA  ILE A  43     1778   3116   2435    -13   -512     44       C  
ATOM    322  C   ILE A  43      13.237 -10.377  27.411  1.00 21.54           C  
ANISOU  322  C   ILE A  43     2151   3375   2658    -11   -525     45       C  
ATOM    323  O   ILE A  43      13.439 -10.725  28.576  1.00 22.15           O  
ANISOU  323  O   ILE A  43     2262   3441   2714    -14   -544     58       O  
ATOM    324  CB  ILE A  43      14.849 -11.981  26.250  1.00 19.03           C  
ANISOU  324  CB  ILE A  43     1704   3085   2440    -44   -550     59       C  
ATOM    325  CG1 ILE A  43      15.878 -10.861  26.093  1.00 19.75           C  
ANISOU  325  CG1 ILE A  43     1816   3164   2524    -77   -589     64       C  
ATOM    326  CG2 ILE A  43      15.039 -13.034  25.165  1.00 18.86           C  
ANISOU  326  CG2 ILE A  43     1613   3080   2474    -39   -528     59       C  
ATOM    327  CD1 ILE A  43      17.391 -11.308  26.213  1.00 20.64           C  
ANISOU  327  CD1 ILE A  43     1885   3279   2680   -110   -632     97       C  
ATOM    328  N   CYS A  44      12.914  -9.120  27.088  1.00 22.49           N  
ANISOU  328  N   CYS A  44     2317   3483   2747     -5   -515     32       N  
ATOM    329  CA  CYS A  44      12.816  -8.071  28.069  1.00 23.87           C  
ANISOU  329  CA  CYS A  44     2590   3624   2855     -3   -525     31       C  
ATOM    330  C   CYS A  44      11.421  -7.832  28.596  1.00 26.86           C  
ANISOU  330  C   CYS A  44     3017   3993   3195     49   -468     35       C  
ATOM    331  O   CYS A  44      10.427  -7.885  27.866  1.00 26.95           O  
ANISOU  331  O   CYS A  44     2989   4025   3228     79   -421     37       O  
ATOM    332  CB  CYS A  44      13.407  -6.781  27.508  1.00 22.83           C  
ANISOU  332  CB  CYS A  44     2490   3477   2708    -28   -550     19       C  
ATOM    333  SG  CYS A  44      15.167  -6.875  27.083  1.00 23.00           S  
ANISOU  333  SG  CYS A  44     2462   3503   2774    -89   -620     31       S  
ATOM    334  N   THR A  45      11.373  -7.496  29.874  1.00 29.19           N  
ANISOU  334  N   THR A  45     3404   4255   3430     57   -473     40       N  
ATOM    335  CA  THR A  45      10.186  -6.999  30.558  1.00 31.45           C  
ANISOU  335  CA  THR A  45     3765   4520   3665    110   -414     49       C  
ATOM    336  C   THR A  45      10.237  -5.473  30.331  1.00 33.17           C  
ANISOU  336  C   THR A  45     4062   4704   3835    110   -412     34       C  
ATOM    337  O   THR A  45      11.303  -4.947  29.995  1.00 32.78           O  
ANISOU  337  O   THR A  45     4021   4645   3787     61   -469     20       O  
ATOM    338  CB  THR A  45      10.278  -7.327  32.068  1.00 33.14           C  
ANISOU  338  CB  THR A  45     4059   4706   3828    116   -423     61       C  
ATOM    339  OG1 THR A  45      11.276  -6.514  32.699  1.00 34.07           O  
ANISOU  339  OG1 THR A  45     4273   4781   3890     74   -482     50       O  
ATOM    340  CG2 THR A  45      10.606  -8.798  32.326  1.00 33.77           C  
ANISOU  340  CG2 THR A  45     4062   4814   3954    101   -444     74       C  
ATOM    341  N   SER A  46       9.142  -4.739  30.595  1.00 34.80           N  
ANISOU  341  N   SER A  46     4333   4890   4001    165   -346     43       N  
ATOM    342  CA  SER A  46       9.169  -3.270  30.473  1.00 36.35           C  
ANISOU  342  CA  SER A  46     4619   5048   4146    169   -340     29       C  
ATOM    343  C   SER A  46      10.275  -2.651  31.364  1.00 37.72           C  
ANISOU  343  C   SER A  46     4908   5170   4255    122   -407     14       C  
ATOM    344  O   SER A  46      10.953  -1.716  30.924  1.00 38.45           O  
ANISOU  344  O   SER A  46     5033   5243   4334     85   -448     -2       O  
ATOM    345  CB  SER A  46       7.806  -2.664  30.790  1.00 37.38           C  
ANISOU  345  CB  SER A  46     4808   5157   4239    245   -250     50       C  
ATOM    346  OG  SER A  46       6.995  -2.656  29.626  1.00 39.99           O  
ANISOU  346  OG  SER A  46     5041   5527   4626    270   -207     64       O  
ATOM    347  N   GLU A  47      10.521  -3.237  32.557  1.00 37.69           N  
ANISOU  347  N   GLU A  47     4958   5146   4216    115   -427     22       N  
ATOM    348  CA  GLU A  47      11.583  -2.752  33.437  1.00 38.29           C  
ANISOU  348  CA  GLU A  47     5145   5174   4231     61   -503     15       C  
ATOM    349  C   GLU A  47      12.951  -2.986  32.782  1.00 37.53           C  
ANISOU  349  C   GLU A  47     4965   5102   4191    -17   -593     13       C  
ATOM    350  O   GLU A  47      13.772  -2.073  32.751  1.00 38.00           O  
ANISOU  350  O   GLU A  47     5086   5130   4222    -66   -653      8       O  
ATOM    351  CB  GLU A  47      11.551  -3.436  34.820  1.00 42.59           C  
ANISOU  351  CB  GLU A  47     5757   5695   4730     67   -509     29       C  
ATOM    352  CG  GLU A  47      10.163  -3.652  35.408  1.00 50.99           C  
ANISOU  352  CG  GLU A  47     6858   6752   5764    152   -409     44       C  
ATOM    353  CD  GLU A  47       9.663  -5.087  35.367  1.00 59.94           C  
ANISOU  353  CD  GLU A  47     7870   7939   6964    177   -379     65       C  
ATOM    354  OE1 GLU A  47       8.433  -5.284  35.223  1.00 62.37           O  
ANISOU  354  OE1 GLU A  47     8145   8266   7289    245   -293     84       O  
ATOM    355  OE2 GLU A  47      10.501  -6.014  35.467  1.00 62.11           O  
ANISOU  355  OE2 GLU A  47     8082   8239   7279    129   -441     67       O  
ATOM    356  N   ASP A  48      13.182  -4.195  32.223  1.00 35.91           N  
ANISOU  356  N   ASP A  48     4622   4952   4068    -26   -599     23       N  
ATOM    357  CA  ASP A  48      14.448  -4.552  31.568  1.00 34.25           C  
ANISOU  357  CA  ASP A  48     4322   4769   3920    -87   -669     31       C  
ATOM    358  C   ASP A  48      14.823  -3.553  30.481  1.00 32.73           C  
ANISOU  358  C   ASP A  48     4113   4579   3746   -108   -682     20       C  
ATOM    359  O   ASP A  48      15.992  -3.207  30.361  1.00 32.49           O  
ANISOU  359  O   ASP A  48     4078   4540   3728   -167   -754     31       O  
ATOM    360  CB  ASP A  48      14.395  -5.960  30.944  1.00 34.66           C  
ANISOU  360  CB  ASP A  48     4236   4877   4056    -75   -648     40       C  
ATOM    361  CG  ASP A  48      14.435  -7.132  31.912  1.00 37.40           C  
ANISOU  361  CG  ASP A  48     4573   5230   4406    -73   -656     58       C  
ATOM    362  OD1 ASP A  48      15.021  -6.982  33.013  1.00 37.61           O  
ANISOU  362  OD1 ASP A  48     4680   5224   4387   -104   -707     70       O  
ATOM    363  OD2 ASP A  48      13.896  -8.205  31.562  1.00 38.33           O  
ANISOU  363  OD2 ASP A  48     4606   5384   4572    -43   -615     61       O  
ATOM    364  N   MET A  49      13.838  -3.070  29.713  1.00 31.91           N  
ANISOU  364  N   MET A  49     3998   4484   3643    -61   -616      3       N  
ATOM    365  CA  MET A  49      14.067  -2.131  28.610  1.00 31.76           C  
ANISOU  365  CA  MET A  49     3958   4468   3641    -75   -621     -9       C  
ATOM    366  C   MET A  49      14.774  -0.847  28.987  1.00 32.25           C  
ANISOU  366  C   MET A  49     4127   4480   3647   -117   -676    -12       C  
ATOM    367  O   MET A  49      15.368  -0.238  28.112  1.00 32.53           O  
ANISOU  367  O   MET A  49     4129   4522   3709   -147   -704    -14       O  
ATOM    368  CB  MET A  49      12.765  -1.789  27.862  1.00 31.54           C  
ANISOU  368  CB  MET A  49     3912   4455   3618    -15   -539    -20       C  
ATOM    369  CG  MET A  49      12.278  -2.875  26.928  1.00 33.12           C  
ANISOU  369  CG  MET A  49     3986   4710   3890      6   -503    -16       C  
ATOM    370  SD  MET A  49      13.540  -3.626  25.867  1.00 34.01           S  
ANISOU  370  SD  MET A  49     3981   4860   4082    -44   -553    -14       S  
ATOM    371  CE  MET A  49      13.945  -2.282  24.792  1.00 27.13           C  
ANISOU  371  CE  MET A  49     3116   3981   3210    -65   -566    -26       C  
ATOM    372  N   LEU A  50      14.711  -0.425  30.264  1.00 32.25           N  
ANISOU  372  N   LEU A  50     4261   4427   3567   -121   -694    -11       N  
ATOM    373  CA  LEU A  50      15.354   0.803  30.709  1.00 32.97           C  
ANISOU  373  CA  LEU A  50     4475   4459   3593   -167   -754    -13       C  
ATOM    374  C   LEU A  50      16.853   0.744  30.520  1.00 32.62           C  
ANISOU  374  C   LEU A  50     4383   4423   3589   -251   -856     12       C  
ATOM    375  O   LEU A  50      17.431   1.676  29.973  1.00 32.75           O  
ANISOU  375  O   LEU A  50     4412   4425   3607   -289   -896     13       O  
ATOM    376  CB  LEU A  50      15.012   1.100  32.177  1.00 33.96           C  
ANISOU  376  CB  LEU A  50     4764   4520   3618   -156   -754    -15       C  
ATOM    377  CG  LEU A  50      13.529   1.283  32.509  1.00 36.29           C  
ANISOU  377  CG  LEU A  50     5125   4799   3866    -66   -646    -28       C  
ATOM    378  CD1 LEU A  50      13.354   1.639  33.976  1.00 36.73           C  
ANISOU  378  CD1 LEU A  50     5360   4782   3816    -58   -649    -27       C  
ATOM    379  CD2 LEU A  50      12.880   2.348  31.623  1.00 37.50           C  
ANISOU  379  CD2 LEU A  50     5289   4944   4014    -29   -590    -43       C  
ATOM    380  N   ASN A  51      17.480  -0.366  30.921  1.00 32.15           N  
ANISOU  380  N   ASN A  51     4258   4389   3570   -278   -895     37       N  
ATOM    381  CA  ASN A  51      18.919  -0.535  30.782  1.00 32.26           C  
ANISOU  381  CA  ASN A  51     4211   4414   3633   -355   -988     75       C  
ATOM    382  C   ASN A  51      19.238  -2.031  30.651  1.00 31.50           C  
ANISOU  382  C   ASN A  51     3982   4370   3615   -348   -980     99       C  
ATOM    383  O   ASN A  51      19.801  -2.642  31.566  1.00 32.07           O  
ANISOU  383  O   ASN A  51     4066   4435   3684   -382  -1032    128       O  
ATOM    384  CB  ASN A  51      19.621   0.057  31.999  1.00 34.39           C  
ANISOU  384  CB  ASN A  51     4614   4622   3831   -421  -1081     97       C  
ATOM    385  CG  ASN A  51      21.107   0.236  31.809  1.00 38.71           C  
ANISOU  385  CG  ASN A  51     5111   5172   4425   -508  -1187    148       C  
ATOM    386  OD1 ASN A  51      21.659   0.032  30.713  1.00 39.85           O  
ANISOU  386  OD1 ASN A  51     5123   5363   4656   -516  -1185    168       O  
ATOM    387  ND2 ASN A  51      21.781   0.638  32.869  1.00 39.32           N  
ANISOU  387  ND2 ASN A  51     5295   5198   4445   -577  -1282    176       N  
ATOM    388  N   PRO A  52      18.887  -2.642  29.510  1.00 29.58           N  
ANISOU  388  N   PRO A  52     3619   4178   3441   -307   -917     87       N  
ATOM    389  CA  PRO A  52      19.106  -4.090  29.372  1.00 28.24           C  
ANISOU  389  CA  PRO A  52     3337   4052   3339   -295   -901    106       C  
ATOM    390  C   PRO A  52      20.532  -4.525  29.067  1.00 26.52           C  
ANISOU  390  C   PRO A  52     3029   3855   3193   -347   -962    156       C  
ATOM    391  O   PRO A  52      21.240  -3.866  28.314  1.00 26.88           O  
ANISOU  391  O   PRO A  52     3042   3903   3268   -377   -989    173       O  
ATOM    392  CB  PRO A  52      18.177  -4.472  28.220  1.00 29.11           C  
ANISOU  392  CB  PRO A  52     3373   4200   3488   -236   -815     76       C  
ATOM    393  CG  PRO A  52      18.092  -3.240  27.382  1.00 29.67           C  
ANISOU  393  CG  PRO A  52     3467   4261   3546   -239   -809     59       C  
ATOM    394  CD  PRO A  52      18.226  -2.068  28.321  1.00 28.60           C  
ANISOU  394  CD  PRO A  52     3466   4071   3332   -269   -856     58       C  
ATOM    395  N   ASN A  53      20.944  -5.643  29.658  1.00 24.94           N  
ANISOU  395  N   ASN A  53     2784   3669   3023   -355   -979    186       N  
ATOM    396  CA  ASN A  53      22.201  -6.300  29.334  1.00 24.29           C  
ANISOU  396  CA  ASN A  53     2597   3612   3021   -389  -1018    242       C  
ATOM    397  C   ASN A  53      21.717  -7.586  28.702  1.00 23.61           C  
ANISOU  397  C   ASN A  53     2418   3564   2988   -332   -941    228       C  
ATOM    398  O   ASN A  53      21.350  -8.530  29.402  1.00 23.26           O  
ANISOU  398  O   ASN A  53     2374   3525   2938   -314   -927    226       O  
ATOM    399  CB  ASN A  53      23.067  -6.587  30.554  1.00 25.34           C  
ANISOU  399  CB  ASN A  53     2754   3727   3147   -445  -1102    294       C  
ATOM    400  CG  ASN A  53      24.418  -7.107  30.123  1.00 27.75           C  
ANISOU  400  CG  ASN A  53     2942   4058   3543   -480  -1141    365       C  
ATOM    401  OD1 ASN A  53      24.512  -8.048  29.328  1.00 30.13           O  
ANISOU  401  OD1 ASN A  53     3137   4395   3914   -441  -1082    373       O  
ATOM    402  ND2 ASN A  53      25.489  -6.507  30.603  1.00 26.67           N  
ANISOU  402  ND2 ASN A  53     2823   3902   3410   -553  -1237    425       N  
ATOM    403  N   TYR A  54      21.585  -7.572  27.385  1.00 23.30           N  
ANISOU  403  N   TYR A  54     2315   3549   2990   -304   -889    212       N  
ATOM    404  CA  TYR A  54      21.014  -8.689  26.652  1.00 23.34           C  
ANISOU  404  CA  TYR A  54     2252   3583   3035   -252   -815    192       C  
ATOM    405  C   TYR A  54      21.745 -10.000  26.846  1.00 23.36           C  
ANISOU  405  C   TYR A  54     2178   3602   3096   -253   -818    234       C  
ATOM    406  O   TYR A  54      21.076 -11.022  26.995  1.00 24.14           O  
ANISOU  406  O   TYR A  54     2263   3710   3199   -218   -776    216       O  
ATOM    407  CB  TYR A  54      20.875  -8.351  25.172  1.00 23.17           C  
ANISOU  407  CB  TYR A  54     2186   3576   3041   -230   -768    172       C  
ATOM    408  CG  TYR A  54      19.779  -7.344  24.907  1.00 22.70           C  
ANISOU  408  CG  TYR A  54     2194   3505   2926   -212   -743    124       C  
ATOM    409  CD1 TYR A  54      18.447  -7.737  24.839  1.00 22.73           C  
ANISOU  409  CD1 TYR A  54     2216   3516   2906   -167   -688     86       C  
ATOM    410  CD2 TYR A  54      20.070  -5.998  24.751  1.00 23.18           C  
ANISOU  410  CD2 TYR A  54     2299   3548   2960   -239   -776    123       C  
ATOM    411  CE1 TYR A  54      17.437  -6.821  24.588  1.00 22.47           C  
ANISOU  411  CE1 TYR A  54     2236   3474   2829   -147   -660     53       C  
ATOM    412  CE2 TYR A  54      19.070  -5.074  24.465  1.00 23.44           C  
ANISOU  412  CE2 TYR A  54     2391   3570   2945   -218   -747     83       C  
ATOM    413  CZ  TYR A  54      17.753  -5.494  24.388  1.00 23.61           C  
ANISOU  413  CZ  TYR A  54     2423   3600   2948   -170   -687     50       C  
ATOM    414  OH  TYR A  54      16.762  -4.584  24.142  1.00 24.10           O  
ANISOU  414  OH  TYR A  54     2538   3652   2968   -146   -655     21       O  
ATOM    415  N   GLU A  55      23.090 -10.000  26.900  1.00 22.61           N  
ANISOU  415  N   GLU A  55     2034   3509   3049   -292   -867    296       N  
ATOM    416  CA  GLU A  55      23.813 -11.262  27.130  1.00 23.12           C  
ANISOU  416  CA  GLU A  55     2022   3588   3173   -289   -865    345       C  
ATOM    417  C   GLU A  55      23.435 -11.880  28.482  1.00 22.93           C  
ANISOU  417  C   GLU A  55     2042   3555   3115   -294   -891    343       C  
ATOM    418  O   GLU A  55      23.203 -13.090  28.568  1.00 22.79           O  
ANISOU  418  O   GLU A  55     1986   3551   3124   -263   -852    343       O  
ATOM    419  CB  GLU A  55      25.333 -11.085  27.045  1.00 26.00           C  
ANISOU  419  CB  GLU A  55     2322   3957   3601   -331   -917    427       C  
ATOM    420  CG  GLU A  55      25.850 -10.958  25.632  1.00 31.26           C  
ANISOU  420  CG  GLU A  55     2917   4638   4324   -310   -871    444       C  
ATOM    421  CD  GLU A  55      25.927 -12.224  24.794  1.00 36.63           C  
ANISOU  421  CD  GLU A  55     3523   5335   5061   -255   -790    450       C  
ATOM    422  OE1 GLU A  55      25.398 -13.279  25.213  1.00 34.67           O  
ANISOU  422  OE1 GLU A  55     3278   5089   4807   -228   -761    430       O  
ATOM    423  OE2 GLU A  55      26.493 -12.140  23.681  1.00 41.31           O  
ANISOU  423  OE2 GLU A  55     4061   5935   5700   -236   -751    474       O  
ATOM    424  N   ASP A  56      23.326 -11.032  29.514  1.00 22.65           N  
ANISOU  424  N   ASP A  56     2096   3493   3015   -333   -952    340       N  
ATOM    425  CA  ASP A  56      22.966 -11.468  30.861  1.00 23.43           C  
ANISOU  425  CA  ASP A  56     2255   3578   3069   -341   -979    339       C  
ATOM    426  C   ASP A  56      21.528 -11.926  30.932  1.00 23.64           C  
ANISOU  426  C   ASP A  56     2317   3608   3058   -284   -909    279       C  
ATOM    427  O   ASP A  56      21.236 -12.910  31.607  1.00 23.47           O  
ANISOU  427  O   ASP A  56     2288   3591   3037   -268   -897    282       O  
ATOM    428  CB  ASP A  56      23.202 -10.346  31.876  1.00 25.42           C  
ANISOU  428  CB  ASP A  56     2614   3792   3251   -397  -1061    348       C  
ATOM    429  CG  ASP A  56      24.652 -10.021  32.121  1.00 29.00           C  
ANISOU  429  CG  ASP A  56     3038   4240   3742   -468  -1152    424       C  
ATOM    430  OD1 ASP A  56      25.514 -10.815  31.709  1.00 28.61           O  
ANISOU  430  OD1 ASP A  56     2877   4217   3776   -470  -1151    479       O  
ATOM    431  OD2 ASP A  56      24.926  -8.978  32.731  1.00 32.18           O  
ANISOU  431  OD2 ASP A  56     3530   4608   4089   -522  -1226    434       O  
ATOM    432  N   LEU A  57      20.631 -11.221  30.243  1.00 23.92           N  
ANISOU  432  N   LEU A  57     2385   3641   3063   -254   -863    230       N  
ATOM    433  CA  LEU A  57      19.222 -11.608  30.230  1.00 25.25           C  
ANISOU  433  CA  LEU A  57     2576   3815   3202   -201   -796    184       C  
ATOM    434  C   LEU A  57      19.018 -12.924  29.457  1.00 26.04           C  
ANISOU  434  C   LEU A  57     2586   3945   3365   -166   -742    183       C  
ATOM    435  O   LEU A  57      18.152 -13.720  29.816  1.00 26.61           O  
ANISOU  435  O   LEU A  57     2660   4022   3427   -135   -708    169       O  
ATOM    436  CB  LEU A  57      18.365 -10.499  29.609  1.00 25.69           C  
ANISOU  436  CB  LEU A  57     2680   3862   3218   -181   -763    144       C  
ATOM    437  CG  LEU A  57      18.274  -9.211  30.398  1.00 27.68           C  
ANISOU  437  CG  LEU A  57     3044   4076   3395   -202   -800    136       C  
ATOM    438  CD1 LEU A  57      17.610  -8.132  29.571  1.00 28.73           C  
ANISOU  438  CD1 LEU A  57     3208   4205   3504   -181   -764    103       C  
ATOM    439  CD2 LEU A  57      17.523  -9.431  31.710  1.00 28.66           C  
ANISOU  439  CD2 LEU A  57     3251   4179   3458   -184   -793    130       C  
ATOM    440  N   LEU A  58      19.823 -13.162  28.413  1.00 26.08           N  
ANISOU  440  N   LEU A  58     2515   3964   3430   -171   -735    201       N  
ATOM    441  CA  LEU A  58      19.711 -14.375  27.606  1.00 27.04           C  
ANISOU  441  CA  LEU A  58     2566   4103   3604   -138   -682    199       C  
ATOM    442  C   LEU A  58      20.152 -15.623  28.357  1.00 27.48           C  
ANISOU  442  C   LEU A  58     2587   4163   3690   -138   -692    233       C  
ATOM    443  O   LEU A  58      19.623 -16.705  28.083  1.00 27.78           O  
ANISOU  443  O   LEU A  58     2597   4209   3748   -107   -648    221       O  
ATOM    444  CB  LEU A  58      20.501 -14.210  26.296  1.00 27.85           C  
ANISOU  444  CB  LEU A  58     2612   4214   3756   -138   -665    213       C  
ATOM    445  CG  LEU A  58      20.050 -15.004  25.063  1.00 29.98           C  
ANISOU  445  CG  LEU A  58     2844   4492   4055   -100   -599    190       C  
ATOM    446  CD1 LEU A  58      18.513 -15.012  24.884  1.00 30.01           C  
ANISOU  446  CD1 LEU A  58     2889   4497   4018    -75   -565    140       C  
ATOM    447  CD2 LEU A  58      20.765 -14.484  23.817  1.00 30.78           C  
ANISOU  447  CD2 LEU A  58     2913   4595   4188   -100   -582    199       C  
ATOM    448  N   ILE A  59      21.077 -15.490  29.334  1.00 26.90           N  
ANISOU  448  N   ILE A  59     2518   4083   3619   -177   -753    277       N  
ATOM    449  CA  ILE A  59      21.528 -16.632  30.135  1.00 27.97           C  
ANISOU  449  CA  ILE A  59     2621   4223   3784   -180   -767    315       C  
ATOM    450  C   ILE A  59      20.349 -17.296  30.862  1.00 29.00           C  
ANISOU  450  C   ILE A  59     2790   4352   3876   -153   -742    283       C  
ATOM    451  O   ILE A  59      20.291 -18.518  30.957  1.00 29.45           O  
ANISOU  451  O   ILE A  59     2806   4417   3966   -132   -717    294       O  
ATOM    452  CB  ILE A  59      22.628 -16.215  31.134  1.00 28.46           C  
ANISOU  452  CB  ILE A  59     2693   4275   3846   -235   -850    372       C  
ATOM    453  CG1 ILE A  59      23.897 -15.817  30.400  1.00 29.69           C  
ANISOU  453  CG1 ILE A  59     2784   4436   4060   -260   -873    424       C  
ATOM    454  CG2 ILE A  59      22.912 -17.313  32.186  1.00 29.26           C  
ANISOU  454  CG2 ILE A  59     2775   4378   3963   -241   -871    409       C  
ATOM    455  CD1 ILE A  59      24.915 -15.126  31.335  1.00 31.50           C  
ANISOU  455  CD1 ILE A  59     3033   4653   4284   -328   -970    484       C  
ATOM    456  N   ARG A  60      19.384 -16.490  31.316  1.00 29.12           N  
ANISOU  456  N   ARG A  60     2885   4356   3824   -148   -742    247       N  
ATOM    457  CA  ARG A  60      18.214 -16.999  32.026  1.00 29.69           C  
ANISOU  457  CA  ARG A  60     2995   4427   3860   -118   -713    225       C  
ATOM    458  C   ARG A  60      17.126 -17.540  31.084  1.00 29.57           C  
ANISOU  458  C   ARG A  60     2949   4424   3860    -76   -647    193       C  
ATOM    459  O   ARG A  60      15.992 -17.735  31.525  1.00 30.43           O  
ANISOU  459  O   ARG A  60     3090   4534   3939    -49   -619    177       O  
ATOM    460  CB  ARG A  60      17.626 -15.890  32.920  1.00 31.24           C  
ANISOU  460  CB  ARG A  60     3295   4600   3976   -124   -732    208       C  
ATOM    461  CG  ARG A  60      18.669 -15.154  33.770  1.00 34.08           C  
ANISOU  461  CG  ARG A  60     3706   4937   4307   -177   -809    237       C  
ATOM    462  CD  ARG A  60      19.309 -16.073  34.785  1.00 36.90           C  
ANISOU  462  CD  ARG A  60     4048   5293   4678   -199   -849    278       C  
ATOM    463  NE  ARG A  60      20.706 -15.712  35.045  1.00 38.38           N  
ANISOU  463  NE  ARG A  60     4224   5473   4886   -258   -928    327       N  
ATOM    464  CZ  ARG A  60      21.564 -16.473  35.713  1.00 38.87           C  
ANISOU  464  CZ  ARG A  60     4248   5539   4981   -287   -973    378       C  
ATOM    465  NH1 ARG A  60      22.814 -16.071  35.891  1.00 38.83           N  
ANISOU  465  NH1 ARG A  60     4226   5528   5000   -345  -1047    433       N  
ATOM    466  NH2 ARG A  60      21.185 -17.652  36.194  1.00 37.18           N  
ANISOU  466  NH2 ARG A  60     4009   5336   4781   -260   -945    381       N  
ATOM    467  N   LYS A  61      17.446 -17.755  29.799  1.00 28.12           N  
ANISOU  467  N   LYS A  61     2711   4251   3724    -70   -622    187       N  
ATOM    468  CA  LYS A  61      16.478 -18.226  28.818  1.00 27.37           C  
ANISOU  468  CA  LYS A  61     2595   4163   3640    -40   -570    160       C  
ATOM    469  C   LYS A  61      16.933 -19.521  28.183  1.00 26.72           C  
ANISOU  469  C   LYS A  61     2455   4085   3614    -30   -547    172       C  
ATOM    470  O   LYS A  61      18.089 -19.659  27.792  1.00 27.49           O  
ANISOU  470  O   LYS A  61     2514   4180   3750    -40   -555    196       O  
ATOM    471  CB  LYS A  61      16.243 -17.168  27.715  1.00 28.16           C  
ANISOU  471  CB  LYS A  61     2707   4264   3730    -39   -556    134       C  
ATOM    472  CG  LYS A  61      15.721 -15.829  28.224  1.00 31.09           C  
ANISOU  472  CG  LYS A  61     3143   4627   4044    -43   -569    120       C  
ATOM    473  CD  LYS A  61      14.385 -15.936  28.982  1.00 34.32           C  
ANISOU  473  CD  LYS A  61     3592   5034   4414    -16   -545    112       C  
ATOM    474  CE  LYS A  61      13.938 -14.571  29.449  1.00 39.05           C  
ANISOU  474  CE  LYS A  61     4264   5618   4953    -13   -549    101       C  
ATOM    475  NZ  LYS A  61      12.670 -14.621  30.229  1.00 42.86           N  
ANISOU  475  NZ  LYS A  61     4788   6097   5399     21   -516    103       N  
ATOM    476  N   SER A  62      16.016 -20.473  28.061  1.00 25.33           N  
ANISOU  476  N   SER A  62     2272   3910   3442     -9   -517    161       N  
ATOM    477  CA  SER A  62      16.306 -21.742  27.410  1.00 24.28           C  
ANISOU  477  CA  SER A  62     2100   3772   3354      2   -491    168       C  
ATOM    478  C   SER A  62      15.465 -21.853  26.131  1.00 22.78           C  
ANISOU  478  C   SER A  62     1916   3576   3161     13   -457    138       C  
ATOM    479  O   SER A  62      14.531 -21.073  25.934  1.00 22.20           O  
ANISOU  479  O   SER A  62     1869   3510   3057     13   -456    119       O  
ATOM    480  CB  SER A  62      16.022 -22.907  28.359  1.00 25.99           C  
ANISOU  480  CB  SER A  62     2307   3988   3578     10   -492    185       C  
ATOM    481  OG  SER A  62      16.775 -22.800  29.558  1.00 29.36           O  
ANISOU  481  OG  SER A  62     2733   4418   4003     -4   -529    214       O  
ATOM    482  N   ASN A  63      15.739 -22.862  25.276  1.00 22.09           N  
ANISOU  482  N   ASN A  63     1813   3476   3105     23   -430    139       N  
ATOM    483  CA  ASN A  63      14.953 -23.067  24.048  1.00 21.27           C  
ANISOU  483  CA  ASN A  63     1728   3360   2993     26   -406    113       C  
ATOM    484  C   ASN A  63      13.469 -23.175  24.334  1.00 20.82           C  
ANISOU  484  C   ASN A  63     1688   3311   2912     23   -413    104       C  
ATOM    485  O   ASN A  63      12.672 -22.648  23.562  1.00 20.70           O  
ANISOU  485  O   ASN A  63     1690   3296   2879     17   -410     88       O  
ATOM    486  CB  ASN A  63      15.388 -24.337  23.340  1.00 21.15           C  
ANISOU  486  CB  ASN A  63     1711   3319   3006     38   -376    117       C  
ATOM    487  CG  ASN A  63      16.769 -24.313  22.761  1.00 23.10           C  
ANISOU  487  CG  ASN A  63     1941   3555   3282     50   -352    132       C  
ATOM    488  OD1 ASN A  63      17.281 -23.275  22.335  1.00 21.88           O  
ANISOU  488  OD1 ASN A  63     1781   3408   3126     46   -354    131       O  
ATOM    489  ND2 ASN A  63      17.375 -25.482  22.663  1.00 25.06           N  
ANISOU  489  ND2 ASN A  63     2181   3782   3560     68   -325    151       N  
ATOM    490  N   HIS A  64      13.091 -23.835  25.462  1.00 20.77           N  
ANISOU  490  N   HIS A  64     1675   3311   2908     27   -423    122       N  
ATOM    491  CA  HIS A  64      11.670 -23.994  25.807  1.00 21.15           C  
ANISOU  491  CA  HIS A  64     1730   3367   2939     27   -426    127       C  
ATOM    492  C   HIS A  64      10.985 -22.714  26.271  1.00 21.87           C  
ANISOU  492  C   HIS A  64     1835   3475   2997     32   -431    127       C  
ATOM    493  O   HIS A  64       9.761 -22.693  26.351  1.00 22.96           O  
ANISOU  493  O   HIS A  64     1976   3622   3127     36   -426    138       O  
ATOM    494  CB  HIS A  64      11.440 -25.113  26.840  1.00 21.66           C  
ANISOU  494  CB  HIS A  64     1781   3432   3016     33   -431    150       C  
ATOM    495  CG  HIS A  64      11.973 -24.809  28.208  1.00 21.49           C  
ANISOU  495  CG  HIS A  64     1758   3421   2985     40   -444    165       C  
ATOM    496  ND1 HIS A  64      13.222 -25.253  28.607  1.00 22.62           N  
ANISOU  496  ND1 HIS A  64     1885   3559   3150     38   -452    176       N  
ATOM    497  CD2 HIS A  64      11.396 -24.154  29.245  1.00 22.17           C  
ANISOU  497  CD2 HIS A  64     1862   3520   3040     48   -450    175       C  
ATOM    498  CE1 HIS A  64      13.361 -24.860  29.861  1.00 22.87           C  
ANISOU  498  CE1 HIS A  64     1927   3600   3162     38   -472    191       C  
ATOM    499  NE2 HIS A  64      12.302 -24.174  30.279  1.00 22.82           N  
ANISOU  499  NE2 HIS A  64     1948   3602   3120     46   -469    188       N  
ATOM    500  N   ASN A  65      11.745 -21.662  26.594  1.00 21.23           N  
ANISOU  500  N   ASN A  65     1767   3398   2900     31   -440    120       N  
ATOM    501  CA  ASN A  65      11.130 -20.388  27.002  1.00 21.84           C  
ANISOU  501  CA  ASN A  65     1873   3485   2940     39   -440    118       C  
ATOM    502  C   ASN A  65      10.619 -19.574  25.790  1.00 21.67           C  
ANISOU  502  C   ASN A  65     1857   3465   2912     35   -429    102       C  
ATOM    503  O   ASN A  65       9.829 -18.644  25.969  1.00 21.97           O  
ANISOU  503  O   ASN A  65     1914   3509   2924     46   -420    105       O  
ATOM    504  CB  ASN A  65      12.113 -19.541  27.810  1.00 23.54           C  
ANISOU  504  CB  ASN A  65     2113   3696   3134     32   -461    118       C  
ATOM    505  CG  ASN A  65      12.431 -20.122  29.164  1.00 26.63           C  
ANISOU  505  CG  ASN A  65     2511   4086   3520     34   -477    139       C  
ATOM    506  OD1 ASN A  65      13.595 -20.235  29.546  1.00 27.65           O  
ANISOU  506  OD1 ASN A  65     2634   4210   3661     18   -503    149       O  
ATOM    507  ND2 ASN A  65      11.396 -20.496  29.922  1.00 26.06           N  
ANISOU  507  ND2 ASN A  65     2451   4018   3434     53   -462    153       N  
ATOM    508  N   PHE A  66      11.069 -19.908  24.570  1.00 20.64           N  
ANISOU  508  N   PHE A  66     1713   3326   2804     22   -426     87       N  
ATOM    509  CA  PHE A  66      10.644 -19.177  23.389  1.00 21.54           C  
ANISOU  509  CA  PHE A  66     1834   3440   2910     16   -419     71       C  
ATOM    510  C   PHE A  66       9.526 -19.949  22.744  1.00 22.40           C  
ANISOU  510  C   PHE A  66     1935   3547   3028      9   -415     80       C  
ATOM    511  O   PHE A  66       9.747 -21.041  22.243  1.00 23.62           O  
ANISOU  511  O   PHE A  66     2087   3686   3201     -1   -416     78       O  
ATOM    512  CB  PHE A  66      11.809 -18.964  22.422  1.00 21.24           C  
ANISOU  512  CB  PHE A  66     1794   3391   2884      7   -416     53       C  
ATOM    513  CG  PHE A  66      12.922 -18.098  22.967  1.00 21.80           C  
ANISOU  513  CG  PHE A  66     1868   3466   2951      5   -429     54       C  
ATOM    514  CD1 PHE A  66      12.858 -16.722  22.870  1.00 22.79           C  
ANISOU  514  CD1 PHE A  66     2013   3597   3051      3   -435     45       C  
ATOM    515  CD2 PHE A  66      14.046 -18.665  23.540  1.00 22.98           C  
ANISOU  515  CD2 PHE A  66     1999   3611   3122      4   -438     70       C  
ATOM    516  CE1 PHE A  66      13.890 -15.925  23.342  1.00 23.91           C  
ANISOU  516  CE1 PHE A  66     2161   3735   3187     -7   -456     50       C  
ATOM    517  CE2 PHE A  66      15.074 -17.863  24.035  1.00 24.05           C  
ANISOU  517  CE2 PHE A  66     2135   3747   3255     -7   -461     80       C  
ATOM    518  CZ  PHE A  66      14.991 -16.497  23.925  1.00 24.01           C  
ANISOU  518  CZ  PHE A  66     2155   3745   3223    -14   -472     69       C  
ATOM    519  N   LEU A  67       8.327 -19.420  22.797  1.00 22.20           N  
ANISOU  519  N   LEU A  67     1909   3533   2991     13   -412     97       N  
ATOM    520  CA  LEU A  67       7.154 -20.065  22.232  1.00 23.12           C  
ANISOU  520  CA  LEU A  67     2015   3651   3120     -1   -418    119       C  
ATOM    521  C   LEU A  67       6.908 -19.497  20.841  1.00 23.12           C  
ANISOU  521  C   LEU A  67     2025   3646   3115    -20   -423    106       C  
ATOM    522  O   LEU A  67       6.661 -18.297  20.707  1.00 22.57           O  
ANISOU  522  O   LEU A  67     1957   3587   3030    -11   -415    106       O  
ATOM    523  CB  LEU A  67       5.937 -19.820  23.126  1.00 24.30           C  
ANISOU  523  CB  LEU A  67     2148   3818   3266     18   -409    160       C  
ATOM    524  CG  LEU A  67       6.131 -20.210  24.585  1.00 27.07           C  
ANISOU  524  CG  LEU A  67     2499   4173   3615     41   -401    173       C  
ATOM    525  CD1 LEU A  67       4.978 -19.746  25.428  1.00 28.56           C  
ANISOU  525  CD1 LEU A  67     2681   4376   3794     69   -379    215       C  
ATOM    526  CD2 LEU A  67       6.383 -21.696  24.720  1.00 28.09           C  
ANISOU  526  CD2 LEU A  67     2614   4292   3767     27   -414    177       C  
ATOM    527  N   VAL A  68       6.992 -20.352  19.807  1.00 22.01           N  
ANISOU  527  N   VAL A  68     1896   3485   2982    -45   -436     96       N  
ATOM    528  CA  VAL A  68       6.814 -19.917  18.424  1.00 21.44           C  
ANISOU  528  CA  VAL A  68     1844   3403   2900    -67   -443     83       C  
ATOM    529  C   VAL A  68       5.570 -20.563  17.890  1.00 21.74           C  
ANISOU  529  C   VAL A  68     1881   3435   2944    -99   -471    115       C  
ATOM    530  O   VAL A  68       5.443 -21.783  17.958  1.00 21.78           O  
ANISOU  530  O   VAL A  68     1895   3421   2958   -114   -485    124       O  
ATOM    531  CB  VAL A  68       8.027 -20.270  17.556  1.00 21.92           C  
ANISOU  531  CB  VAL A  68     1937   3437   2957    -72   -433     47       C  
ATOM    532  CG1 VAL A  68       7.865 -19.706  16.141  1.00 22.56           C  
ANISOU  532  CG1 VAL A  68     2045   3506   3021    -92   -438     32       C  
ATOM    533  CG2 VAL A  68       9.318 -19.760  18.198  1.00 22.21           C  
ANISOU  533  CG2 VAL A  68     1962   3480   2996    -45   -412     30       C  
ATOM    534  N   GLN A  69       4.620 -19.756  17.426  1.00 21.88           N  
ANISOU  534  N   GLN A  69     1887   3468   2960   -110   -481    140       N  
ATOM    535  CA  GLN A  69       3.367 -20.265  16.913  1.00 23.68           C  
ANISOU  535  CA  GLN A  69     2106   3692   3198   -146   -516    184       C  
ATOM    536  C   GLN A  69       3.104 -19.684  15.534  1.00 25.41           C  
ANISOU  536  C   GLN A  69     2349   3903   3403   -177   -536    179       C  
ATOM    537  O   GLN A  69       3.150 -18.462  15.354  1.00 25.06           O  
ANISOU  537  O   GLN A  69     2295   3876   3351   -161   -519    172       O  
ATOM    538  CB  GLN A  69       2.228 -19.930  17.871  1.00 25.95           C  
ANISOU  538  CB  GLN A  69     2341   4011   3507   -128   -511    244       C  
ATOM    539  CG  GLN A  69       0.963 -20.710  17.598  1.00 30.41           C  
ANISOU  539  CG  GLN A  69     2884   4575   4095   -167   -551    307       C  
ATOM    540  CD  GLN A  69      -0.141 -20.267  18.522  1.00 34.33           C  
ANISOU  540  CD  GLN A  69     3322   5104   4617   -140   -534    376       C  
ATOM    541  OE1 GLN A  69       0.081 -19.994  19.700  1.00 36.31           O  
ANISOU  541  OE1 GLN A  69     3560   5370   4867    -92   -494    376       O  
ATOM    542  NE2 GLN A  69      -1.351 -20.169  17.998  1.00 34.57           N  
ANISOU  542  NE2 GLN A  69     3321   5146   4670   -169   -563    443       N  
ATOM    543  N   ALA A  70       2.927 -20.575  14.551  1.00 27.27           N  
ANISOU  543  N   ALA A  70     2626   4105   3630   -223   -571    177       N  
ATOM    544  CA  ALA A  70       2.661 -20.240  13.153  1.00 29.88           C  
ANISOU  544  CA  ALA A  70     2994   4418   3939   -262   -599    173       C  
ATOM    545  C   ALA A  70       1.198 -20.600  12.927  1.00 32.71           C  
ANISOU  545  C   ALA A  70     3330   4781   4315   -310   -653    242       C  
ATOM    546  O   ALA A  70       0.849 -21.779  12.918  1.00 32.86           O  
ANISOU  546  O   ALA A  70     3370   4776   4339   -343   -688    262       O  
ATOM    547  CB  ALA A  70       3.541 -21.084  12.249  1.00 29.89           C  
ANISOU  547  CB  ALA A  70     3074   4370   3912   -280   -601    126       C  
ATOM    548  N   GLY A  71       0.340 -19.595  12.853  1.00 34.64           N  
ANISOU  548  N   GLY A  71     3528   5057   4575   -310   -658    286       N  
ATOM    549  CA  GLY A  71      -1.095 -19.825  12.758  1.00 36.76           C  
ANISOU  549  CA  GLY A  71     3757   5338   4872   -350   -706    371       C  
ATOM    550  C   GLY A  71      -1.563 -20.340  14.104  1.00 38.96           C  
ANISOU  550  C   GLY A  71     3980   5639   5185   -323   -691    415       C  
ATOM    551  O   GLY A  71      -1.358 -19.671  15.125  1.00 39.93           O  
ANISOU  551  O   GLY A  71     4065   5789   5317   -263   -637    412       O  
ATOM    552  N   ASN A  72      -2.075 -21.572  14.141  1.00 39.61           N  
ANISOU  552  N   ASN A  72     4067   5702   5281   -365   -737    451       N  
ATOM    553  CA  ASN A  72      -2.462 -22.159  15.420  1.00 40.44           C  
ANISOU  553  CA  ASN A  72     4122   5825   5418   -339   -722    492       C  
ATOM    554  C   ASN A  72      -1.582 -23.343  15.828  1.00 39.82           C  
ANISOU  554  C   ASN A  72     4088   5716   5326   -336   -718    441       C  
ATOM    555  O   ASN A  72      -1.943 -24.059  16.765  1.00 40.43           O  
ANISOU  555  O   ASN A  72     4132   5802   5429   -327   -717    477       O  
ATOM    556  CB  ASN A  72      -3.943 -22.503  15.459  1.00 43.24           C  
ANISOU  556  CB  ASN A  72     4418   6195   5816   -378   -770    599       C  
ATOM    557  CG  ASN A  72      -4.757 -21.339  15.973  1.00 48.60           C  
ANISOU  557  CG  ASN A  72     5019   6920   6526   -336   -732    665       C  
ATOM    558  OD1 ASN A  72      -4.288 -20.559  16.822  1.00 50.39           O  
ANISOU  558  OD1 ASN A  72     5233   7167   6746   -266   -662    636       O  
ATOM    559  ND2 ASN A  72      -5.983 -21.187  15.469  1.00 49.49           N  
ANISOU  559  ND2 ASN A  72     5085   7046   6673   -377   -776    759       N  
ATOM    560  N   VAL A  73      -0.422 -23.545  15.151  1.00 38.00           N  
ANISOU  560  N   VAL A  73     3931   5451   5057   -339   -709    361       N  
ATOM    561  CA  VAL A  73       0.448 -24.657  15.494  1.00 36.58           C  
ANISOU  561  CA  VAL A  73     3792   5240   4867   -331   -698    318       C  
ATOM    562  C   VAL A  73       1.796 -24.195  16.046  1.00 33.80           C  
ANISOU  562  C   VAL A  73     3445   4895   4502   -271   -635    254       C  
ATOM    563  O   VAL A  73       2.404 -23.234  15.588  1.00 32.96           O  
ANISOU  563  O   VAL A  73     3352   4794   4378   -252   -610    217       O  
ATOM    564  CB  VAL A  73       0.613 -25.704  14.376  1.00 37.82           C  
ANISOU  564  CB  VAL A  73     4036   5338   4995   -387   -742    297       C  
ATOM    565  CG1 VAL A  73      -0.744 -26.146  13.837  1.00 38.09           C  
ANISOU  565  CG1 VAL A  73     4069   5363   5041   -458   -818    368       C  
ATOM    566  CG2 VAL A  73       1.516 -25.182  13.264  1.00 38.68           C  
ANISOU  566  CG2 VAL A  73     4213   5420   5062   -384   -723    235       C  
ATOM    567  N   GLN A  74       2.229 -24.907  17.070  1.00 32.11           N  
ANISOU  567  N   GLN A  74     3217   4682   4301   -244   -615    249       N  
ATOM    568  CA  GLN A  74       3.426 -24.649  17.821  1.00 30.46           C  
ANISOU  568  CA  GLN A  74     3004   4482   4088   -193   -566    205       C  
ATOM    569  C   GLN A  74       4.675 -25.262  17.200  1.00 28.76           C  
ANISOU  569  C   GLN A  74     2849   4226   3854   -191   -550    151       C  
ATOM    570  O   GLN A  74       4.723 -26.467  16.926  1.00 28.39           O  
ANISOU  570  O   GLN A  74     2842   4142   3803   -213   -566    149       O  
ATOM    571  CB  GLN A  74       3.216 -25.167  19.247  1.00 31.63           C  
ANISOU  571  CB  GLN A  74     3109   4650   4260   -168   -555    234       C  
ATOM    572  CG  GLN A  74       3.891 -24.320  20.301  1.00 34.26           C  
ANISOU  572  CG  GLN A  74     3415   5010   4590   -117   -513    217       C  
ATOM    573  CD  GLN A  74       3.287 -22.943  20.407  1.00 38.74           C  
ANISOU  573  CD  GLN A  74     3956   5609   5154   -100   -500    238       C  
ATOM    574  OE1 GLN A  74       2.118 -22.715  20.093  1.00 39.20           O  
ANISOU  574  OE1 GLN A  74     3991   5680   5224   -117   -518    285       O  
ATOM    575  NE2 GLN A  74       4.076 -21.987  20.863  1.00 40.19           N  
ANISOU  575  NE2 GLN A  74     4142   5804   5322    -66   -470    208       N  
ATOM    576  N   LEU A  75       5.709 -24.431  17.012  1.00 26.94           N  
ANISOU  576  N   LEU A  75     2624   4001   3611   -161   -515    112       N  
ATOM    577  CA  LEU A  75       6.981 -24.901  16.475  1.00 26.13           C  
ANISOU  577  CA  LEU A  75     2569   3864   3497   -148   -487     71       C  
ATOM    578  C   LEU A  75       7.916 -25.231  17.618  1.00 24.69           C  
ANISOU  578  C   LEU A  75     2356   3691   3334   -110   -458     66       C  
ATOM    579  O   LEU A  75       7.940 -24.526  18.629  1.00 24.66           O  
ANISOU  579  O   LEU A  75     2304   3723   3341    -88   -451     77       O  
ATOM    580  CB  LEU A  75       7.630 -23.844  15.579  1.00 26.39           C  
ANISOU  580  CB  LEU A  75     2620   3896   3512   -139   -467     41       C  
ATOM    581  CG  LEU A  75       6.821 -23.369  14.392  1.00 27.97           C  
ANISOU  581  CG  LEU A  75     2851   4087   3689   -176   -495     44       C  
ATOM    582  CD1 LEU A  75       7.589 -22.320  13.635  1.00 28.51           C  
ANISOU  582  CD1 LEU A  75     2932   4158   3742   -161   -468     15       C  
ATOM    583  CD2 LEU A  75       6.460 -24.528  13.469  1.00 28.45           C  
ANISOU  583  CD2 LEU A  75     2985   4096   3730   -216   -521     44       C  
ATOM    584  N   ARG A  76       8.692 -26.287  17.453  1.00 23.73           N  
ANISOU  584  N   ARG A  76     2269   3534   3215   -102   -440     53       N  
ATOM    585  CA  ARG A  76       9.607 -26.764  18.480  1.00 23.15           C  
ANISOU  585  CA  ARG A  76     2166   3465   3164    -70   -415     56       C  
ATOM    586  C   ARG A  76      10.915 -26.040  18.316  1.00 23.09           C  
ANISOU  586  C   ARG A  76     2149   3463   3160    -40   -380     38       C  
ATOM    587  O   ARG A  76      11.467 -26.059  17.236  1.00 23.10           O  
ANISOU  587  O   ARG A  76     2193   3435   3150    -37   -357     20       O  
ATOM    588  CB  ARG A  76       9.785 -28.277  18.333  1.00 23.10           C  
ANISOU  588  CB  ARG A  76     2200   3415   3161    -73   -410     57       C  
ATOM    589  CG  ARG A  76      10.657 -28.935  19.394  1.00 24.49           C  
ANISOU  589  CG  ARG A  76     2345   3594   3365    -42   -386     67       C  
ATOM    590  CD  ARG A  76      10.658 -30.461  19.242  1.00 25.45           C  
ANISOU  590  CD  ARG A  76     2511   3669   3489    -47   -382     71       C  
ATOM    591  NE  ARG A  76       9.302 -31.015  19.337  1.00 26.85           N  
ANISOU  591  NE  ARG A  76     2699   3843   3660    -86   -428     90       N  
ATOM    592  CZ  ARG A  76       8.690 -31.308  20.483  1.00 27.90           C  
ANISOU  592  CZ  ARG A  76     2782   4004   3813    -89   -450    119       C  
ATOM    593  NH1 ARG A  76       9.323 -31.154  21.641  1.00 27.18           N  
ANISOU  593  NH1 ARG A  76     2639   3944   3744    -57   -431    127       N  
ATOM    594  NH2 ARG A  76       7.448 -31.777  20.478  1.00 26.86           N  
ANISOU  594  NH2 ARG A  76     2656   3870   3681   -126   -492    144       N  
ATOM    595  N   VAL A  77      11.385 -25.352  19.363  1.00 22.92           N  
ANISOU  595  N   VAL A  77     2078   3477   3154    -21   -377     47       N  
ATOM    596  CA  VAL A  77      12.645 -24.614  19.342  1.00 22.50           C  
ANISOU  596  CA  VAL A  77     2008   3431   3110      1   -354     42       C  
ATOM    597  C   VAL A  77      13.789 -25.514  19.818  1.00 22.65           C  
ANISOU  597  C   VAL A  77     2013   3436   3158     24   -329     57       C  
ATOM    598  O   VAL A  77      13.784 -25.968  20.966  1.00 23.17           O  
ANISOU  598  O   VAL A  77     2050   3514   3238     28   -342     76       O  
ATOM    599  CB  VAL A  77      12.518 -23.324  20.172  1.00 22.65           C  
ANISOU  599  CB  VAL A  77     1992   3490   3124      1   -372     47       C  
ATOM    600  CG1 VAL A  77      13.834 -22.544  20.213  1.00 22.55           C  
ANISOU  600  CG1 VAL A  77     1961   3484   3122     15   -360     49       C  
ATOM    601  CG2 VAL A  77      11.383 -22.467  19.631  1.00 22.78           C  
ANISOU  601  CG2 VAL A  77     2021   3518   3115    -16   -388     38       C  
ATOM    602  N   ILE A  78      14.761 -25.779  18.923  1.00 21.51           N  
ANISOU  602  N   ILE A  78     1889   3262   3021     42   -291     54       N  
ATOM    603  CA  ILE A  78      15.908 -26.662  19.177  1.00 21.01           C  
ANISOU  603  CA  ILE A  78     1813   3180   2991     71   -256     77       C  
ATOM    604  C   ILE A  78      17.272 -25.944  19.263  1.00 21.20           C  
ANISOU  604  C   ILE A  78     1793   3219   3044     92   -236    101       C  
ATOM    605  O   ILE A  78      18.320 -26.588  19.397  1.00 21.04           O  
ANISOU  605  O   ILE A  78     1753   3184   3058    119   -202    132       O  
ATOM    606  CB  ILE A  78      15.936 -27.810  18.131  1.00 21.34           C  
ANISOU  606  CB  ILE A  78     1920   3166   3021     83   -218     66       C  
ATOM    607  CG1 ILE A  78      16.196 -27.270  16.715  1.00 22.92           C  
ANISOU  607  CG1 ILE A  78     2167   3343   3199     89   -188     47       C  
ATOM    608  CG2 ILE A  78      14.626 -28.598  18.175  1.00 21.21           C  
ANISOU  608  CG2 ILE A  78     1943   3134   2981     53   -250     53       C  
ATOM    609  CD1 ILE A  78      16.385 -28.331  15.641  1.00 23.77           C  
ANISOU  609  CD1 ILE A  78     2357   3387   3288    106   -141     37       C  
ATOM    610  N   GLY A  79      17.251 -24.626  19.197  1.00 21.03           N  
ANISOU  610  N   GLY A  79     1755   3224   3011     78   -257     94       N  
ATOM    611  CA  GLY A  79      18.447 -23.805  19.260  1.00 20.86           C  
ANISOU  611  CA  GLY A  79     1692   3218   3016     88   -250    121       C  
ATOM    612  C   GLY A  79      18.087 -22.338  19.319  1.00 20.44           C  
ANISOU  612  C   GLY A  79     1633   3193   2940     64   -285    105       C  
ATOM    613  O   GLY A  79      17.012 -21.936  18.862  1.00 20.17           O  
ANISOU  613  O   GLY A  79     1631   3160   2870     50   -297     72       O  
ATOM    614  N   HIS A  80      18.954 -21.537  19.910  1.00 19.80           N  
ANISOU  614  N   HIS A  80     1511   3132   2878     59   -305    133       N  
ATOM    615  CA  HIS A  80      18.748 -20.097  19.958  1.00 19.91           C  
ANISOU  615  CA  HIS A  80     1528   3168   2870     38   -337    120       C  
ATOM    616  C   HIS A  80      20.077 -19.400  20.088  1.00 20.47           C  
ANISOU  616  C   HIS A  80     1558   3248   2973     34   -346    161       C  
ATOM    617  O   HIS A  80      20.991 -19.860  20.806  1.00 20.59           O  
ANISOU  617  O   HIS A  80     1534   3265   3025     36   -353    206       O  
ATOM    618  CB  HIS A  80      17.752 -19.653  21.039  1.00 20.55           C  
ANISOU  618  CB  HIS A  80     1623   3268   2919     18   -380    105       C  
ATOM    619  CG  HIS A  80      18.275 -19.764  22.435  1.00 23.19           C  
ANISOU  619  CG  HIS A  80     1934   3613   3265      9   -413    136       C  
ATOM    620  ND1 HIS A  80      18.156 -20.933  23.159  1.00 24.82           N  
ANISOU  620  ND1 HIS A  80     2132   3815   3485     17   -411    149       N  
ATOM    621  CD2 HIS A  80      18.873 -18.829  23.211  1.00 24.34           C  
ANISOU  621  CD2 HIS A  80     2071   3769   3407    -11   -453    157       C  
ATOM    622  CE1 HIS A  80      18.701 -20.686  24.340  1.00 25.58           C  
ANISOU  622  CE1 HIS A  80     2212   3922   3585      3   -448    177       C  
ATOM    623  NE2 HIS A  80      19.126 -19.426  24.421  1.00 25.25           N  
ANISOU  623  NE2 HIS A  80     2175   3888   3532    -17   -477    183       N  
ATOM    624  N   SER A  81      20.204 -18.305  19.359  1.00 19.50           N  
ANISOU  624  N   SER A  81     1441   3129   2839     27   -346    151       N  
ATOM    625  CA  SER A  81      21.436 -17.524  19.403  1.00 19.33           C  
ANISOU  625  CA  SER A  81     1379   3116   2849     18   -360    195       C  
ATOM    626  C   SER A  81      21.097 -16.074  19.186  1.00 19.10           C  
ANISOU  626  C   SER A  81     1370   3097   2788     -6   -390    172       C  
ATOM    627  O   SER A  81      20.019 -15.739  18.652  1.00 19.38           O  
ANISOU  627  O   SER A  81     1447   3132   2785     -5   -382    125       O  
ATOM    628  CB  SER A  81      22.415 -18.012  18.344  1.00 20.56           C  
ANISOU  628  CB  SER A  81     1510   3256   3047     49   -302    227       C  
ATOM    629  OG  SER A  81      21.836 -17.898  17.055  1.00 22.99           O  
ANISOU  629  OG  SER A  81     1860   3550   3327     64   -263    185       O  
ATOM    630  N   MET A  82      21.993 -15.200  19.632  1.00 18.24           N  
ANISOU  630  N   MET A  82     1236   2999   2697    -29   -428    209       N  
ATOM    631  CA  MET A  82      21.802 -13.788  19.461  1.00 18.29           C  
ANISOU  631  CA  MET A  82     1264   3010   2674    -53   -458    192       C  
ATOM    632  C   MET A  82      22.790 -13.258  18.436  1.00 18.18           C  
ANISOU  632  C   MET A  82     1217   2997   2695    -48   -437    223       C  
ATOM    633  O   MET A  82      23.987 -13.448  18.601  1.00 18.82           O  
ANISOU  633  O   MET A  82     1246   3080   2827    -51   -442    285       O  
ATOM    634  CB  MET A  82      21.960 -13.052  20.792  1.00 18.31           C  
ANISOU  634  CB  MET A  82     1281   3018   2659    -90   -527    208       C  
ATOM    635  CG  MET A  82      21.746 -11.572  20.649  1.00 20.05           C  
ANISOU  635  CG  MET A  82     1536   3237   2844   -114   -556    189       C  
ATOM    636  SD  MET A  82      21.709 -10.690  22.225  1.00 22.85           S  
ANISOU  636  SD  MET A  82     1943   3584   3155   -157   -634    197       S  
ATOM    637  CE  MET A  82      23.215 -11.183  22.938  1.00 20.12           C  
ANISOU  637  CE  MET A  82     1541   3240   2865   -186   -679    275       C  
ATOM    638  N   GLN A  83      22.303 -12.620  17.379  1.00 18.38           N  
ANISOU  638  N   GLN A  83     1267   3019   2697    -41   -413    188       N  
ATOM    639  CA  GLN A  83      23.179 -12.014  16.377  1.00 18.79           C  
ANISOU  639  CA  GLN A  83     1291   3071   2777    -36   -391    216       C  
ATOM    640  C   GLN A  83      22.858 -10.537  16.383  1.00 18.57           C  
ANISOU  640  C   GLN A  83     1289   3050   2717    -66   -433    195       C  
ATOM    641  O   GLN A  83      21.757 -10.149  16.003  1.00 18.34           O  
ANISOU  641  O   GLN A  83     1305   3020   2644    -63   -426    142       O  
ATOM    642  CB  GLN A  83      22.976 -12.626  14.979  1.00 20.82           C  
ANISOU  642  CB  GLN A  83     1562   3314   3034      3   -319    195       C  
ATOM    643  CG  GLN A  83      23.781 -11.912  13.894  1.00 24.03           C  
ANISOU  643  CG  GLN A  83     1947   3719   3464     13   -290    222       C  
ATOM    644  CD  GLN A  83      23.587 -12.519  12.518  1.00 29.06           C  
ANISOU  644  CD  GLN A  83     2615   4336   4092     52   -217    201       C  
ATOM    645  OE1 GLN A  83      22.615 -13.240  12.253  1.00 30.00           O  
ANISOU  645  OE1 GLN A  83     2784   4441   4175     62   -198    153       O  
ATOM    646  NE2 GLN A  83      24.512 -12.234  11.609  1.00 29.35           N  
ANISOU  646  NE2 GLN A  83     2627   4367   4158     73   -174    239       N  
ATOM    647  N   ASN A  84      23.771  -9.722  16.903  1.00 18.23           N  
ANISOU  647  N   ASN A  84     1220   3012   2695    -98   -482    241       N  
ATOM    648  CA  ASN A  84      23.563  -8.283  17.042  1.00 18.07           C  
ANISOU  648  CA  ASN A  84     1232   2992   2642   -131   -528    226       C  
ATOM    649  C   ASN A  84      22.240  -7.996  17.857  1.00 17.96           C  
ANISOU  649  C   ASN A  84     1288   2974   2564   -139   -552    169       C  
ATOM    650  O   ASN A  84      22.128  -8.475  18.991  1.00 18.15           O  
ANISOU  650  O   ASN A  84     1323   2994   2578   -149   -580    175       O  
ATOM    651  CB  ASN A  84      23.671  -7.605  15.653  1.00 17.56           C  
ANISOU  651  CB  ASN A  84     1161   2928   2583   -119   -492    218       C  
ATOM    652  CG  ASN A  84      25.024  -7.859  15.040  1.00 19.14           C  
ANISOU  652  CG  ASN A  84     1294   3131   2848   -108   -467    286       C  
ATOM    653  OD1 ASN A  84      26.071  -7.602  15.648  1.00 18.59           O  
ANISOU  653  OD1 ASN A  84     1181   3065   2817   -136   -511    351       O  
ATOM    654  ND2 ASN A  84      25.028  -8.376  13.828  1.00 19.63           N  
ANISOU  654  ND2 ASN A  84     1347   3189   2921    -66   -395    278       N  
ATOM    655  N   CYS A  85      21.233  -7.339  17.275  1.00 17.17           N  
ANISOU  655  N   CYS A  85     1228   2872   2423   -130   -535    120       N  
ATOM    656  CA  CYS A  85      19.976  -7.080  17.980  1.00 17.73           C  
ANISOU  656  CA  CYS A  85     1357   2939   2440   -129   -545     79       C  
ATOM    657  C   CYS A  85      18.831  -8.000  17.587  1.00 18.12           C  
ANISOU  657  C   CYS A  85     1413   2993   2478    -97   -499     44       C  
ATOM    658  O   CYS A  85      17.695  -7.722  17.958  1.00 17.89           O  
ANISOU  658  O   CYS A  85     1423   2963   2410    -91   -498     17       O  
ATOM    659  CB  CYS A  85      19.589  -5.615  17.856  1.00 18.43           C  
ANISOU  659  CB  CYS A  85     1490   3020   2491   -143   -564     59       C  
ATOM    660  SG  CYS A  85      20.884  -4.508  18.447  1.00 19.05           S  
ANISOU  660  SG  CYS A  85     1574   3086   2577   -192   -633    103       S  
ATOM    661  N   VAL A  86      19.126  -9.134  16.922  1.00 18.18           N  
ANISOU  661  N   VAL A  86     1386   3002   2518    -78   -463     52       N  
ATOM    662  CA  VAL A  86      18.088 -10.112  16.619  1.00 19.01           C  
ANISOU  662  CA  VAL A  86     1504   3108   2613    -57   -430     25       C  
ATOM    663  C   VAL A  86      18.373 -11.455  17.277  1.00 19.11           C  
ANISOU  663  C   VAL A  86     1497   3118   2649    -48   -425     43       C  
ATOM    664  O   VAL A  86      19.538 -11.831  17.485  1.00 19.70           O  
ANISOU  664  O   VAL A  86     1535   3190   2760    -49   -428     80       O  
ATOM    665  CB  VAL A  86      17.777 -10.319  15.108  1.00 20.17           C  
ANISOU  665  CB  VAL A  86     1654   3250   2760    -42   -389      6       C  
ATOM    666  CG1 VAL A  86      17.204  -9.062  14.465  1.00 21.17           C  
ANISOU  666  CG1 VAL A  86     1804   3381   2860    -51   -393    -16       C  
ATOM    667  CG2 VAL A  86      18.977 -10.854  14.353  1.00 20.54           C  
ANISOU  667  CG2 VAL A  86     1670   3288   2845    -29   -358     32       C  
ATOM    668  N   LEU A  87      17.309 -12.209  17.554  1.00 18.01           N  
ANISOU  668  N   LEU A  87     1375   2977   2491    -38   -416     23       N  
ATOM    669  CA  LEU A  87      17.442 -13.565  18.019  1.00 18.97           C  
ANISOU  669  CA  LEU A  87     1481   3094   2632    -27   -406     36       C  
ATOM    670  C   LEU A  87      17.097 -14.482  16.852  1.00 18.78           C  
ANISOU  670  C   LEU A  87     1465   3057   2614    -11   -366     21       C  
ATOM    671  O   LEU A  87      16.153 -14.236  16.100  1.00 18.68           O  
ANISOU  671  O   LEU A  87     1479   3043   2577    -14   -358     -5       O  
ATOM    672  CB  LEU A  87      16.526 -13.878  19.208  1.00 20.34           C  
ANISOU  672  CB  LEU A  87     1671   3272   2784    -29   -426     30       C  
ATOM    673  CG  LEU A  87      16.824 -13.113  20.511  1.00 22.81           C  
ANISOU  673  CG  LEU A  87     1996   3589   3081    -44   -466     45       C  
ATOM    674  CD1 LEU A  87      15.831 -13.482  21.583  1.00 23.95           C  
ANISOU  674  CD1 LEU A  87     2164   3736   3200    -37   -473     39       C  
ATOM    675  CD2 LEU A  87      18.224 -13.388  20.995  1.00 24.07           C  
ANISOU  675  CD2 LEU A  87     2123   3746   3275    -56   -487     83       C  
ATOM    676  N   LYS A  88      17.892 -15.524  16.683  1.00 18.62           N  
ANISOU  676  N   LYS A  88     1427   3023   2624      4   -340     40       N  
ATOM    677  CA  LYS A  88      17.652 -16.530  15.678  1.00 18.31           C  
ANISOU  677  CA  LYS A  88     1412   2961   2584     20   -300     27       C  
ATOM    678  C   LYS A  88      17.243 -17.781  16.441  1.00 17.96           C  
ANISOU  678  C   LYS A  88     1370   2909   2544     24   -303     31       C  
ATOM    679  O   LYS A  88      18.005 -18.296  17.247  1.00 17.76           O  
ANISOU  679  O   LYS A  88     1314   2886   2548     32   -305     60       O  
ATOM    680  CB  LYS A  88      18.901 -16.777  14.829  1.00 20.10           C  
ANISOU  680  CB  LYS A  88     1627   3171   2840     43   -256     51       C  
ATOM    681  CG  LYS A  88      19.222 -15.584  13.922  1.00 23.77           C  
ANISOU  681  CG  LYS A  88     2093   3641   3299     39   -249     47       C  
ATOM    682  CD  LYS A  88      20.423 -15.863  13.008  1.00 27.36           C  
ANISOU  682  CD  LYS A  88     2536   4076   3783     69   -195     78       C  
ATOM    683  CE  LYS A  88      21.673 -16.139  13.782  1.00 31.02           C  
ANISOU  683  CE  LYS A  88     2941   4547   4300     81   -192    135       C  
ATOM    684  NZ  LYS A  88      22.868 -16.059  12.917  1.00 32.45           N  
ANISOU  684  NZ  LYS A  88     3098   4716   4516    110   -139    177       N  
ATOM    685  N   LEU A  89      16.004 -18.213  16.251  1.00 17.80           N  
ANISOU  685  N   LEU A  89     1381   2884   2497     16   -310      7       N  
ATOM    686  CA  LEU A  89      15.476 -19.388  16.923  1.00 18.30           C  
ANISOU  686  CA  LEU A  89     1449   2941   2565     16   -316     11       C  
ATOM    687  C   LEU A  89      15.443 -20.539  15.951  1.00 18.33           C  
ANISOU  687  C   LEU A  89     1492   2908   2565     25   -285      3       C  
ATOM    688  O   LEU A  89      14.677 -20.495  14.993  1.00 18.66           O  
ANISOU  688  O   LEU A  89     1575   2936   2580     11   -285    -18       O  
ATOM    689  CB  LEU A  89      14.057 -19.104  17.428  1.00 18.51           C  
ANISOU  689  CB  LEU A  89     1483   2984   2566     -1   -348      1       C  
ATOM    690  CG  LEU A  89      13.892 -17.850  18.284  1.00 19.95           C  
ANISOU  690  CG  LEU A  89     1649   3194   2738     -6   -372      5       C  
ATOM    691  CD1 LEU A  89      12.411 -17.621  18.623  1.00 20.77           C  
ANISOU  691  CD1 LEU A  89     1762   3311   2819    -14   -388      4       C  
ATOM    692  CD2 LEU A  89      14.771 -17.902  19.513  1.00 20.03           C  
ANISOU  692  CD2 LEU A  89     1633   3212   2764     -1   -384     27       C  
ATOM    693  N   LYS A  90      16.313 -21.525  16.145  1.00 17.96           N  
ANISOU  693  N   LYS A  90     1437   2842   2544     46   -256     22       N  
ATOM    694  CA  LYS A  90      16.322 -22.681  15.281  1.00 18.52           C  
ANISOU  694  CA  LYS A  90     1560   2869   2607     59   -221     14       C  
ATOM    695  C   LYS A  90      15.149 -23.561  15.639  1.00 18.56           C  
ANISOU  695  C   LYS A  90     1590   2866   2596     38   -249      4       C  
ATOM    696  O   LYS A  90      15.017 -23.977  16.789  1.00 18.81           O  
ANISOU  696  O   LYS A  90     1588   2914   2645     37   -268     20       O  
ATOM    697  CB  LYS A  90      17.626 -23.469  15.389  1.00 20.84           C  
ANISOU  697  CB  LYS A  90     1838   3143   2938     95   -174     45       C  
ATOM    698  CG  LYS A  90      17.893 -24.217  14.101  1.00 26.15           C  
ANISOU  698  CG  LYS A  90     2580   3763   3593    118   -119     36       C  
ATOM    699  CD  LYS A  90      18.601 -25.501  14.405  1.00 34.03           C  
ANISOU  699  CD  LYS A  90     3582   4730   4617    151    -77     62       C  
ATOM    700  CE  LYS A  90      19.164 -26.187  13.182  1.00 38.96           C  
ANISOU  700  CE  LYS A  90     4277   5297   5229    188     -4     62       C  
ATOM    701  NZ  LYS A  90      20.015 -27.342  13.569  1.00 42.70           N  
ANISOU  701  NZ  LYS A  90     4745   5742   5736    229     46     98       N  
ATOM    702  N   VAL A  91      14.273 -23.807  14.671  1.00 18.55           N  
ANISOU  702  N   VAL A  91     1648   2838   2560     17   -257    -17       N  
ATOM    703  CA  VAL A  91      13.125 -24.666  14.889  1.00 18.70           C  
ANISOU  703  CA  VAL A  91     1693   2846   2566    -10   -290    -18       C  
ATOM    704  C   VAL A  91      13.346 -26.023  14.227  1.00 19.26           C  
ANISOU  704  C   VAL A  91     1835   2859   2625     -4   -263    -24       C  
ATOM    705  O   VAL A  91      14.218 -26.136  13.352  1.00 20.16           O  
ANISOU  705  O   VAL A  91     1990   2939   2731     22   -214    -31       O  
ATOM    706  CB  VAL A  91      11.786 -23.995  14.523  1.00 18.89           C  
ANISOU  706  CB  VAL A  91     1726   2887   2566    -49   -335    -25       C  
ATOM    707  CG1 VAL A  91      11.449 -22.923  15.551  1.00 20.00           C  
ANISOU  707  CG1 VAL A  91     1799   3080   2719    -48   -357    -13       C  
ATOM    708  CG2 VAL A  91      11.807 -23.401  13.109  1.00 19.00           C  
ANISOU  708  CG2 VAL A  91     1790   2881   2549    -59   -325    -45       C  
ATOM    709  N   ASP A  92      12.579 -27.063  14.631  1.00 18.85           N  
ANISOU  709  N   ASP A  92     1801   2791   2570    -24   -289    -17       N  
ATOM    710  CA  ASP A  92      12.790 -28.397  14.041  1.00 20.11           C  
ANISOU  710  CA  ASP A  92     2040   2887   2713    -19   -265    -23       C  
ATOM    711  C   ASP A  92      12.101 -28.597  12.658  1.00 21.07           C  
ANISOU  711  C   ASP A  92     2263   2960   2784    -54   -281    -44       C  
ATOM    712  O   ASP A  92      12.217 -29.668  12.055  1.00 21.77           O  
ANISOU  712  O   ASP A  92     2440   2985   2846    -54   -262    -52       O  
ATOM    713  CB  ASP A  92      12.416 -29.521  15.024  1.00 20.96           C  
ANISOU  713  CB  ASP A  92     2133   2991   2840    -25   -284     -5       C  
ATOM    714  CG  ASP A  92      10.937 -29.812  15.150  1.00 25.21           C  
ANISOU  714  CG  ASP A  92     2682   3534   3364    -77   -349      2       C  
ATOM    715  OD1 ASP A  92      10.128 -29.001  14.656  1.00 24.39           O  
ANISOU  715  OD1 ASP A  92     2579   3448   3243   -109   -384      0       O  
ATOM    716  OD2 ASP A  92      10.587 -30.854  15.747  1.00 28.54           O  
ANISOU  716  OD2 ASP A  92     3107   3942   3797    -86   -365     17       O  
ATOM    717  N   THR A  93      11.371 -27.588  12.180  1.00 21.17           N  
ANISOU  717  N   THR A  93     2267   2997   2779    -86   -318    -50       N  
ATOM    718  CA  THR A  93      10.652 -27.666  10.915  1.00 21.38           C  
ANISOU  718  CA  THR A  93     2384   2982   2757   -128   -346    -64       C  
ATOM    719  C   THR A  93      10.992 -26.502  10.008  1.00 21.04           C  
ANISOU  719  C   THR A  93     2350   2949   2696   -121   -327    -80       C  
ATOM    720  O   THR A  93      10.915 -25.345  10.422  1.00 20.25           O  
ANISOU  720  O   THR A  93     2172   2905   2617   -117   -337    -74       O  
ATOM    721  CB  THR A  93       9.141 -27.653  11.178  1.00 22.69           C  
ANISOU  721  CB  THR A  93     2530   3170   2921   -187   -424    -42       C  
ATOM    722  OG1 THR A  93       8.834 -28.694  12.095  1.00 24.25           O  
ANISOU  722  OG1 THR A  93     2710   3363   3140   -192   -441    -22       O  
ATOM    723  CG2 THR A  93       8.314 -27.839   9.903  1.00 22.15           C  
ANISOU  723  CG2 THR A  93     2558   3056   2804   -244   -469    -46       C  
ATOM    724  N   ALA A  94      11.358 -26.808   8.765  1.00 20.75           N  
ANISOU  724  N   ALA A  94     2417   2853   2615   -118   -297   -100       N  
ATOM    725  CA  ALA A  94      11.602 -25.786   7.766  1.00 21.05           C  
ANISOU  725  CA  ALA A  94     2478   2893   2630   -115   -281   -116       C  
ATOM    726  C   ALA A  94      10.231 -25.248   7.370  1.00 21.25           C  
ANISOU  726  C   ALA A  94     2508   2934   2633   -181   -358   -110       C  
ATOM    727  O   ALA A  94       9.296 -26.032   7.182  1.00 20.91           O  
ANISOU  727  O   ALA A  94     2518   2860   2567   -230   -411   -101       O  
ATOM    728  CB  ALA A  94      12.274 -26.398   6.554  1.00 21.92           C  
ANISOU  728  CB  ALA A  94     2712   2926   2692    -95   -227   -135       C  
ATOM    729  N   ASN A  95      10.090 -23.917   7.259  1.00 21.44           N  
ANISOU  729  N   ASN A  95     2474   3006   2667   -183   -368   -109       N  
ATOM    730  CA  ASN A  95       8.830 -23.311   6.835  1.00 21.42           C  
ANISOU  730  CA  ASN A  95     2469   3022   2648   -240   -435    -96       C  
ATOM    731  C   ASN A  95       8.525 -23.769   5.412  1.00 22.08           C  
ANISOU  731  C   ASN A  95     2680   3040   2671   -280   -454   -109       C  
ATOM    732  O   ASN A  95       9.295 -23.494   4.506  1.00 22.27           O  
ANISOU  732  O   ASN A  95     2764   3034   2664   -256   -408   -134       O  
ATOM    733  CB  ASN A  95       8.915 -21.783   6.895  1.00 21.43           C  
ANISOU  733  CB  ASN A  95     2395   3079   2668   -225   -428    -95       C  
ATOM    734  CG  ASN A  95       7.614 -21.079   6.534  1.00 23.71           C  
ANISOU  734  CG  ASN A  95     2667   3392   2950   -277   -492    -72       C  
ATOM    735  OD1 ASN A  95       6.583 -21.690   6.195  1.00 22.69           O  
ANISOU  735  OD1 ASN A  95     2578   3240   2803   -331   -549    -51       O  
ATOM    736  ND2 ASN A  95       7.631 -19.766   6.595  1.00 24.65           N  
ANISOU  736  ND2 ASN A  95     2726   3556   3084   -264   -485    -70       N  
ATOM    737  N   PRO A  96       7.432 -24.511   5.219  1.00 22.39           N  
ANISOU  737  N   PRO A  96     2767   3052   2690   -342   -523    -90       N  
ATOM    738  CA  PRO A  96       7.101 -24.988   3.864  1.00 22.99           C  
ANISOU  738  CA  PRO A  96     2980   3056   2698   -390   -553   -101       C  
ATOM    739  C   PRO A  96       6.825 -23.860   2.874  1.00 23.38           C  
ANISOU  739  C   PRO A  96     3043   3117   2722   -414   -571   -103       C  
ATOM    740  O   PRO A  96       6.936 -24.061   1.668  1.00 24.18           O  
ANISOU  740  O   PRO A  96     3267   3159   2762   -436   -572   -122       O  
ATOM    741  CB  PRO A  96       5.853 -25.840   4.093  1.00 23.64           C  
ANISOU  741  CB  PRO A  96     3081   3124   2780   -461   -641    -64       C  
ATOM    742  CG  PRO A  96       5.270 -25.310   5.353  1.00 24.32           C  
ANISOU  742  CG  PRO A  96     3018   3290   2933   -455   -662    -27       C  
ATOM    743  CD  PRO A  96       6.423 -24.925   6.206  1.00 22.34           C  
ANISOU  743  CD  PRO A  96     2693   3075   2719   -374   -580    -51       C  
ATOM    744  N   LYS A  97       6.444 -22.678   3.389  1.00 22.87           N  
ANISOU  744  N   LYS A  97     2860   3128   2702   -409   -585    -83       N  
ATOM    745  CA  LYS A  97       6.144 -21.485   2.596  1.00 22.47           C  
ANISOU  745  CA  LYS A  97     2801   3099   2638   -428   -602    -80       C  
ATOM    746  C   LYS A  97       7.342 -20.572   2.425  1.00 22.10           C  
ANISOU  746  C   LYS A  97     2730   3070   2596   -363   -524   -113       C  
ATOM    747  O   LYS A  97       7.147 -19.438   2.011  1.00 21.59           O  
ANISOU  747  O   LYS A  97     2634   3036   2532   -370   -532   -109       O  
ATOM    748  CB  LYS A  97       4.987 -20.690   3.222  1.00 24.62           C  
ANISOU  748  CB  LYS A  97     2962   3437   2955   -457   -658    -33       C  
ATOM    749  CG  LYS A  97       3.743 -21.544   3.498  1.00 28.99           C  
ANISOU  749  CG  LYS A  97     3516   3981   3516   -520   -737     16       C  
ATOM    750  CD  LYS A  97       2.570 -20.704   3.980  1.00 32.27           C  
ANISOU  750  CD  LYS A  97     3825   4460   3978   -546   -785     75       C  
ATOM    751  CE  LYS A  97       1.397 -21.573   4.361  1.00 36.67           C  
ANISOU  751  CE  LYS A  97     4366   5013   4554   -602   -857    135       C  
ATOM    752  NZ  LYS A  97       0.317 -20.788   5.019  1.00 38.35           N  
ANISOU  752  NZ  LYS A  97     4461   5290   4822   -611   -887    203       N  
ATOM    753  N   THR A  98       8.577 -21.025   2.750  1.00 22.41           N  
ANISOU  753  N   THR A  98     2779   3092   2643   -303   -450   -137       N  
ATOM    754  CA  THR A  98       9.751 -20.166   2.597  1.00 23.01           C  
ANISOU  754  CA  THR A  98     2826   3186   2732   -244   -379   -156       C  
ATOM    755  C   THR A  98       9.943 -19.795   1.129  1.00 24.19           C  
ANISOU  755  C   THR A  98     3070   3295   2826   -254   -364   -175       C  
ATOM    756  O   THR A  98      10.067 -20.673   0.269  1.00 23.78           O  
ANISOU  756  O   THR A  98     3143   3172   2720   -264   -353   -190       O  
ATOM    757  CB  THR A  98      11.018 -20.855   3.071  1.00 23.67           C  
ANISOU  757  CB  THR A  98     2910   3250   2834   -182   -304   -166       C  
ATOM    758  OG1 THR A  98      10.818 -21.393   4.366  1.00 24.64           O  
ANISOU  758  OG1 THR A  98     2963   3400   2999   -177   -321   -150       O  
ATOM    759  CG2 THR A  98      12.211 -19.920   3.051  1.00 24.10           C  
ANISOU  759  CG2 THR A  98     2912   3331   2913   -126   -239   -171       C  
ATOM    760  N   PRO A  99       9.910 -18.491   0.826  1.00 24.88           N  
ANISOU  760  N   PRO A  99     3107   3423   2922   -254   -367   -173       N  
ATOM    761  CA  PRO A  99      10.124 -18.074  -0.567  1.00 25.41           C  
ANISOU  761  CA  PRO A  99     3262   3454   2937   -261   -351   -190       C  
ATOM    762  C   PRO A  99      11.617 -18.002  -0.865  1.00 25.84           C  
ANISOU  762  C   PRO A  99     3335   3489   2992   -190   -254   -206       C  
ATOM    763  O   PRO A  99      12.442 -18.114   0.044  1.00 26.41           O  
ANISOU  763  O   PRO A  99     3336   3585   3113   -140   -209   -200       O  
ATOM    764  CB  PRO A  99       9.517 -16.665  -0.583  1.00 26.01           C  
ANISOU  764  CB  PRO A  99     3257   3590   3034   -283   -389   -176       C  
ATOM    765  CG  PRO A  99       9.850 -16.125   0.792  1.00 26.34           C  
ANISOU  765  CG  PRO A  99     3169   3695   3143   -245   -372   -165       C  
ATOM    766  CD  PRO A  99       9.776 -17.327   1.730  1.00 24.28           C  
ANISOU  766  CD  PRO A  99     2902   3423   2901   -241   -377   -158       C  
ATOM    767  N   LYS A 100      11.999 -17.719  -2.140  1.00 25.88           N  
ANISOU  767  N   LYS A 100     3429   3455   2948   -182   -221   -221       N  
ATOM    768  CA  LYS A 100      13.416 -17.428  -2.452  1.00 25.90           C  
ANISOU  768  CA  LYS A 100     3430   3449   2962   -110   -125   -224       C  
ATOM    769  C   LYS A 100      13.697 -16.088  -1.740  1.00 24.41           C  
ANISOU  769  C   LYS A 100     3098   3340   2836    -94   -128   -210       C  
ATOM    770  O   LYS A 100      12.819 -15.224  -1.739  1.00 23.59           O  
ANISOU  770  O   LYS A 100     2952   3275   2735   -137   -189   -208       O  
ATOM    771  CB  LYS A 100      13.634 -17.255  -3.957  1.00 29.17           C  
ANISOU  771  CB  LYS A 100     3965   3810   3308   -109    -93   -239       C  
ATOM    772  CG  LYS A 100      14.493 -18.351  -4.560  1.00 35.48           C  
ANISOU  772  CG  LYS A 100     4885   4529   4066    -58     -7   -247       C  
ATOM    773  CD  LYS A 100      14.191 -18.551  -6.033  1.00 40.97           C  
ANISOU  773  CD  LYS A 100     5747   5151   4669    -84     -6   -267       C  
ATOM    774  CE  LYS A 100      12.966 -19.400  -6.239  1.00 45.44           C  
ANISOU  774  CE  LYS A 100     6411   5675   5181   -164    -96   -278       C  
ATOM    775  NZ  LYS A 100      12.805 -19.769  -7.667  1.00 47.76           N  
ANISOU  775  NZ  LYS A 100     6894   5880   5374   -187    -91   -297       N  
ATOM    776  N   TYR A 101      14.803 -15.996  -1.013  1.00 23.80           N  
ANISOU  776  N   TYR A 101     2946   3286   2812    -38    -72   -196       N  
ATOM    777  CA  TYR A 101      15.063 -14.798  -0.239  1.00 23.92           C  
ANISOU  777  CA  TYR A 101     2836   3369   2882    -30    -84   -181       C  
ATOM    778  C   TYR A 101      16.529 -14.472  -0.094  1.00 23.67           C  
ANISOU  778  C   TYR A 101     2753   3346   2892     30    -12   -159       C  
ATOM    779  O   TYR A 101      17.386 -15.340  -0.229  1.00 23.78           O  
ANISOU  779  O   TYR A 101     2804   3322   2908     74     53   -148       O  
ATOM    780  CB  TYR A 101      14.367 -14.889   1.154  1.00 23.90           C  
ANISOU  780  CB  TYR A 101     2752   3410   2918    -54   -142   -173       C  
ATOM    781  CG  TYR A 101      15.083 -15.803   2.119  1.00 24.81           C  
ANISOU  781  CG  TYR A 101     2837   3521   3070    -19   -111   -160       C  
ATOM    782  CD1 TYR A 101      14.812 -17.162   2.148  1.00 25.34           C  
ANISOU  782  CD1 TYR A 101     2969   3543   3115    -23   -109   -166       C  
ATOM    783  CD2 TYR A 101      16.049 -15.312   2.993  1.00 25.94           C  
ANISOU  783  CD2 TYR A 101     2888   3701   3268     15    -86   -138       C  
ATOM    784  CE1 TYR A 101      15.475 -18.010   3.019  1.00 26.48           C  
ANISOU  784  CE1 TYR A 101     3084   3683   3293     10    -78   -151       C  
ATOM    785  CE2 TYR A 101      16.721 -16.155   3.871  1.00 26.72           C  
ANISOU  785  CE2 TYR A 101     2955   3795   3401     45    -60   -119       C  
ATOM    786  CZ  TYR A 101      16.409 -17.501   3.897  1.00 27.61           C  
ANISOU  786  CZ  TYR A 101     3130   3867   3494     44    -55   -127       C  
ATOM    787  OH  TYR A 101      17.039 -18.364   4.757  1.00 29.37           O  
ANISOU  787  OH  TYR A 101     3322   4085   3752     73    -29   -107       O  
ATOM    788  N   LYS A 102      16.797 -13.212   0.242  1.00 22.82           N  
ANISOU  788  N   LYS A 102     2559   3290   2820     31    -25   -147       N  
ATOM    789  CA  LYS A 102      18.109 -12.657   0.546  1.00 22.75           C  
ANISOU  789  CA  LYS A 102     2478   3303   2863     74     22   -115       C  
ATOM    790  C   LYS A 102      17.922 -11.690   1.726  1.00 21.84           C  
ANISOU  790  C   LYS A 102     2260   3247   2790     52    -33   -106       C  
ATOM    791  O   LYS A 102      16.817 -11.192   1.945  1.00 21.39           O  
ANISOU  791  O   LYS A 102     2197   3213   2717     12    -92   -125       O  
ATOM    792  CB  LYS A 102      18.647 -11.840  -0.650  1.00 25.11           C  
ANISOU  792  CB  LYS A 102     2803   3592   3145     92     64   -110       C  
ATOM    793  CG  LYS A 102      19.084 -12.655  -1.838  1.00 30.65           C  
ANISOU  793  CG  LYS A 102     3611   4231   3804    126    136   -113       C  
ATOM    794  CD  LYS A 102      19.693 -11.742  -2.921  1.00 35.60           C  
ANISOU  794  CD  LYS A 102     4252   4854   4421    148    181   -102       C  
ATOM    795  CE  LYS A 102      20.261 -12.528  -4.081  1.00 39.28           C  
ANISOU  795  CE  LYS A 102     4829   5253   4844    195    269    -97       C  
ATOM    796  NZ  LYS A 102      20.531 -11.653  -5.256  1.00 41.53           N  
ANISOU  796  NZ  LYS A 102     5149   5529   5101    205    302    -95       N  
ATOM    797  N   PHE A 103      19.001 -11.378   2.444  1.00 21.37           N  
ANISOU  797  N   PHE A 103     2125   3211   2784     78    -15    -72       N  
ATOM    798  CA  PHE A 103      18.946 -10.361   3.488  1.00 21.84           C  
ANISOU  798  CA  PHE A 103     2104   3318   2876     56    -66    -62       C  
ATOM    799  C   PHE A 103      19.785  -9.214   2.939  1.00 23.48           C  
ANISOU  799  C   PHE A 103     2279   3539   3102     67    -46    -40       C  
ATOM    800  O   PHE A 103      20.949  -9.438   2.589  1.00 23.92           O  
ANISOU  800  O   PHE A 103     2321   3581   3186    104      9     -4       O  
ATOM    801  CB  PHE A 103      19.548 -10.856   4.814  1.00 20.50           C  
ANISOU  801  CB  PHE A 103     1875   3163   2752     67    -74    -34       C  
ATOM    802  CG  PHE A 103      18.730 -11.860   5.595  1.00 20.35           C  
ANISOU  802  CG  PHE A 103     1872   3138   2722     54   -101    -52       C  
ATOM    803  CD1 PHE A 103      17.389 -12.061   5.313  1.00 20.54           C  
ANISOU  803  CD1 PHE A 103     1946   3155   2703     25   -133    -86       C  
ATOM    804  CD2 PHE A 103      19.291 -12.563   6.649  1.00 20.51           C  
ANISOU  804  CD2 PHE A 103     1853   3163   2778     67    -99    -27       C  
ATOM    805  CE1 PHE A 103      16.632 -12.953   6.064  1.00 21.26           C  
ANISOU  805  CE1 PHE A 103     2046   3244   2789     11   -160    -95       C  
ATOM    806  CE2 PHE A 103      18.527 -13.455   7.399  1.00 21.33           C  
ANISOU  806  CE2 PHE A 103     1969   3263   2873     55   -125    -41       C  
ATOM    807  CZ  PHE A 103      17.201 -13.644   7.102  1.00 21.09           C  
ANISOU  807  CZ  PHE A 103     1987   3226   2801     28   -154    -75       C  
ATOM    808  N   VAL A 104      19.196  -8.016   2.787  1.00 23.67           N  
ANISOU  808  N   VAL A 104     2295   3586   3112     38    -86    -57       N  
ATOM    809  CA  VAL A 104      19.967  -6.891   2.265  1.00 24.58           C  
ANISOU  809  CA  VAL A 104     2380   3714   3245     45    -71    -35       C  
ATOM    810  C   VAL A 104      19.943  -5.716   3.221  1.00 24.90           C  
ANISOU  810  C   VAL A 104     2363   3790   3309     19   -127    -27       C  
ATOM    811  O   VAL A 104      18.914  -5.445   3.834  1.00 25.53           O  
ANISOU  811  O   VAL A 104     2448   3883   3368     -8   -174    -52       O  
ATOM    812  CB  VAL A 104      19.517  -6.480   0.846  1.00 25.78           C  
ANISOU  812  CB  VAL A 104     2592   3851   3355     42    -52    -58       C  
ATOM    813  CG1 VAL A 104      19.763  -7.611  -0.148  1.00 26.48           C  
ANISOU  813  CG1 VAL A 104     2752   3893   3415     72     10    -61       C  
ATOM    814  CG2 VAL A 104      18.053  -6.074   0.838  1.00 26.97           C  
ANISOU  814  CG2 VAL A 104     2768   4012   3467      2   -107    -95       C  
ATOM    815  N   ARG A 105      21.071  -5.030   3.361  1.00 24.17           N  
ANISOU  815  N   ARG A 105     2219   3709   3256     25   -121     14       N  
ATOM    816  CA  ARG A 105      21.115  -3.833   4.168  1.00 23.85           C  
ANISOU  816  CA  ARG A 105     2139   3694   3229     -4   -176     23       C  
ATOM    817  C   ARG A 105      20.980  -2.712   3.164  1.00 24.00           C  
ANISOU  817  C   ARG A 105     2172   3717   3232    -11   -172     14       C  
ATOM    818  O   ARG A 105      21.841  -2.574   2.309  1.00 23.59           O  
ANISOU  818  O   ARG A 105     2107   3657   3197      9   -130     42       O  
ATOM    819  CB  ARG A 105      22.423  -3.705   4.935  1.00 23.75           C  
ANISOU  819  CB  ARG A 105     2063   3689   3271     -3   -186     80       C  
ATOM    820  CG  ARG A 105      22.392  -2.485   5.840  1.00 22.81           C  
ANISOU  820  CG  ARG A 105     1923   3587   3155    -41   -253     85       C  
ATOM    821  CD  ARG A 105      23.699  -2.315   6.609  1.00 23.25           C  
ANISOU  821  CD  ARG A 105     1920   3650   3265    -53   -277    149       C  
ATOM    822  NE  ARG A 105      23.667  -1.132   7.479  1.00 24.00           N  
ANISOU  822  NE  ARG A 105     2014   3752   3354    -95   -348    152       N  
ATOM    823  CZ  ARG A 105      23.034  -1.076   8.648  1.00 23.50           C  
ANISOU  823  CZ  ARG A 105     1977   3688   3264   -117   -395    128       C  
ATOM    824  NH1 ARG A 105      22.339  -2.121   9.087  1.00 20.79           N  
ANISOU  824  NH1 ARG A 105     1653   3343   2904   -102   -382    100       N  
ATOM    825  NH2 ARG A 105      23.029   0.046   9.349  1.00 22.53           N  
ANISOU  825  NH2 ARG A 105     1870   3563   3127   -153   -453    131       N  
ATOM    826  N   ILE A 106      19.871  -1.958   3.227  1.00 24.25           N  
ANISOU  826  N   ILE A 106     2227   3758   3229    -36   -209    -22       N  
ATOM    827  CA  ILE A 106      19.604  -0.875   2.300  1.00 25.01           C  
ANISOU  827  CA  ILE A 106     2338   3859   3308    -44   -209    -33       C  
ATOM    828  C   ILE A 106      20.308   0.423   2.687  1.00 25.96           C  
ANISOU  828  C   ILE A 106     2419   3991   3453    -60   -238     -6       C  
ATOM    829  O   ILE A 106      20.756   0.603   3.825  1.00 26.26           O  
ANISOU  829  O   ILE A 106     2429   4035   3513    -74   -273     14       O  
ATOM    830  CB  ILE A 106      18.071  -0.657   2.142  1.00 25.13           C  
ANISOU  830  CB  ILE A 106     2392   3876   3278    -62   -232    -73       C  
ATOM    831  CG1 ILE A 106      17.442  -0.213   3.468  1.00 25.47           C  
ANISOU  831  CG1 ILE A 106     2424   3933   3320    -79   -279    -80       C  
ATOM    832  CG2 ILE A 106      17.388  -1.870   1.525  1.00 25.46           C  
ANISOU  832  CG2 ILE A 106     2479   3901   3292    -55   -211    -94       C  
ATOM    833  CD1 ILE A 106      16.051   0.272   3.301  1.00 26.50           C  
ANISOU  833  CD1 ILE A 106     2581   4070   3419    -91   -297   -103       C  
ATOM    834  N   GLN A 107      20.378   1.339   1.735  1.00 26.16           N  
ANISOU  834  N   GLN A 107     2449   4019   3471    -63   -228     -5       N  
ATOM    835  CA  GLN A 107      20.946   2.650   1.935  1.00 26.73           C  
ANISOU  835  CA  GLN A 107     2494   4101   3563    -82   -258     18       C  
ATOM    836  C   GLN A 107      19.809   3.640   2.203  1.00 26.20           C  
ANISOU  836  C   GLN A 107     2456   4038   3460   -104   -296    -17       C  
ATOM    837  O   GLN A 107      18.679   3.436   1.747  1.00 25.72           O  
ANISOU  837  O   GLN A 107     2430   3978   3366   -100   -287    -50       O  
ATOM    838  CB  GLN A 107      21.725   3.038   0.670  1.00 29.71           C  
ANISOU  838  CB  GLN A 107     2857   4475   3955    -67   -217     44       C  
ATOM    839  CG  GLN A 107      23.068   2.307   0.545  1.00 36.01           C  
ANISOU  839  CG  GLN A 107     3613   5268   4800    -41   -177     99       C  
ATOM    840  CD  GLN A 107      24.000   2.626   1.700  1.00 43.64           C  
ANISOU  840  CD  GLN A 107     4524   6244   5814    -63   -222    148       C  
ATOM    841  OE1 GLN A 107      24.514   3.752   1.834  1.00 45.92           O  
ANISOU  841  OE1 GLN A 107     4787   6539   6122    -89   -258    176       O  
ATOM    842  NE2 GLN A 107      24.243   1.641   2.565  1.00 44.73           N  
ANISOU  842  NE2 GLN A 107     4646   6379   5970    -57   -225    162       N  
ATOM    843  N   PRO A 108      20.089   4.748   2.920  1.00 25.67           N  
ANISOU  843  N   PRO A 108     2380   3973   3400   -127   -339     -4       N  
ATOM    844  CA  PRO A 108      19.061   5.786   3.090  1.00 25.23           C  
ANISOU  844  CA  PRO A 108     2358   3917   3311   -140   -363    -31       C  
ATOM    845  C   PRO A 108      18.589   6.296   1.719  1.00 24.31           C  
ANISOU  845  C   PRO A 108     2254   3805   3178   -134   -337    -45       C  
ATOM    846  O   PRO A 108      19.369   6.340   0.765  1.00 24.09           O  
ANISOU  846  O   PRO A 108     2208   3779   3168   -127   -311    -26       O  
ATOM    847  CB  PRO A 108      19.791   6.893   3.872  1.00 26.53           C  
ANISOU  847  CB  PRO A 108     2519   4075   3488   -166   -409     -7       C  
ATOM    848  CG  PRO A 108      21.240   6.640   3.623  1.00 27.44           C  
ANISOU  848  CG  PRO A 108     2585   4192   3651   -170   -405     41       C  
ATOM    849  CD  PRO A 108      21.382   5.155   3.505  1.00 25.56           C  
ANISOU  849  CD  PRO A 108     2328   3957   3425   -144   -366     43       C  
ATOM    850  N   GLY A 109      17.303   6.571   1.616  1.00 23.77           N  
ANISOU  850  N   GLY A 109     2215   3739   3077   -133   -340    -72       N  
ATOM    851  CA  GLY A 109      16.658   6.984   0.378  1.00 24.26           C  
ANISOU  851  CA  GLY A 109     2291   3806   3120   -132   -322    -84       C  
ATOM    852  C   GLY A 109      15.982   5.831  -0.349  1.00 24.51           C  
ANISOU  852  C   GLY A 109     2341   3838   3135   -123   -298    -98       C  
ATOM    853  O   GLY A 109      15.145   6.047  -1.231  1.00 25.07           O  
ANISOU  853  O   GLY A 109     2431   3912   3184   -128   -293   -108       O  
ATOM    854  N   GLN A 110      16.341   4.587   0.009  1.00 23.89           N  
ANISOU  854  N   GLN A 110     2258   3753   3065   -114   -286    -97       N  
ATOM    855  CA  GLN A 110      15.737   3.422  -0.607  1.00 23.86           C  
ANISOU  855  CA  GLN A 110     2283   3742   3042   -110   -269   -110       C  
ATOM    856  C   GLN A 110      14.390   3.139  -0.010  1.00 22.98           C  
ANISOU  856  C   GLN A 110     2182   3636   2913   -119   -293   -121       C  
ATOM    857  O   GLN A 110      14.142   3.404   1.169  1.00 23.46           O  
ANISOU  857  O   GLN A 110     2228   3703   2982   -118   -313   -119       O  
ATOM    858  CB  GLN A 110      16.658   2.207  -0.567  1.00 25.71           C  
ANISOU  858  CB  GLN A 110     2515   3963   3291    -92   -240   -102       C  
ATOM    859  CG  GLN A 110      17.939   2.413  -1.367  1.00 32.25           C  
ANISOU  859  CG  GLN A 110     3331   4784   4138    -76   -203    -80       C  
ATOM    860  CD  GLN A 110      17.688   2.775  -2.810  1.00 41.14           C  
ANISOU  860  CD  GLN A 110     4493   5904   5237    -76   -180    -88       C  
ATOM    861  OE1 GLN A 110      17.973   3.904  -3.238  1.00 44.29           O  
ANISOU  861  OE1 GLN A 110     4876   6311   5642    -81   -182    -78       O  
ATOM    862  NE2 GLN A 110      17.115   1.843  -3.581  1.00 41.83           N  
ANISOU  862  NE2 GLN A 110     4634   5972   5289    -74   -162   -105       N  
ATOM    863  N   THR A 111      13.495   2.661  -0.853  1.00 21.75           N  
ANISOU  863  N   THR A 111     2055   3476   2733   -130   -293   -128       N  
ATOM    864  CA  THR A 111      12.137   2.370  -0.450  1.00 21.23           C  
ANISOU  864  CA  THR A 111     1993   3417   2656   -142   -318   -126       C  
ATOM    865  C   THR A 111      11.929   0.878  -0.247  1.00 21.50           C  
ANISOU  865  C   THR A 111     2045   3440   2686   -144   -318   -130       C  
ATOM    866  O   THR A 111      12.662   0.051  -0.790  1.00 21.89           O  
ANISOU  866  O   THR A 111     2118   3470   2729   -138   -296   -138       O  
ATOM    867  CB  THR A 111      11.187   2.912  -1.525  1.00 21.29           C  
ANISOU  867  CB  THR A 111     2017   3429   2643   -161   -330   -120       C  
ATOM    868  OG1 THR A 111      11.517   2.261  -2.746  1.00 20.90           O  
ANISOU  868  OG1 THR A 111     2009   3361   2572   -171   -317   -129       O  
ATOM    869  CG2 THR A 111      11.304   4.421  -1.689  1.00 21.34           C  
ANISOU  869  CG2 THR A 111     2007   3446   2655   -158   -329   -115       C  
ATOM    870  N   PHE A 112      10.902   0.533   0.496  1.00 21.03           N  
ANISOU  870  N   PHE A 112     1975   3388   2627   -151   -340   -121       N  
ATOM    871  CA  PHE A 112      10.541  -0.862   0.739  1.00 20.14           C  
ANISOU  871  CA  PHE A 112     1877   3264   2510   -157   -348   -121       C  
ATOM    872  C   PHE A 112       9.133  -0.958   1.247  1.00 18.77           C  
ANISOU  872  C   PHE A 112     1689   3104   2339   -170   -375    -98       C  
ATOM    873  O   PHE A 112       8.573   0.045   1.677  1.00 18.70           O  
ANISOU  873  O   PHE A 112     1654   3112   2338   -163   -380    -83       O  
ATOM    874  CB  PHE A 112      11.506  -1.510   1.734  1.00 20.37           C  
ANISOU  874  CB  PHE A 112     1893   3289   2559   -136   -332   -128       C  
ATOM    875  CG  PHE A 112      11.641  -0.821   3.070  1.00 21.62           C  
ANISOU  875  CG  PHE A 112     2016   3462   2736   -121   -338   -122       C  
ATOM    876  CD1 PHE A 112      10.873  -1.215   4.152  1.00 22.58           C  
ANISOU  876  CD1 PHE A 112     2125   3590   2862   -118   -352   -112       C  
ATOM    877  CD2 PHE A 112      12.575   0.176   3.260  1.00 22.59           C  
ANISOU  877  CD2 PHE A 112     2125   3588   2870   -112   -332   -123       C  
ATOM    878  CE1 PHE A 112      11.028  -0.611   5.393  1.00 23.63           C  
ANISOU  878  CE1 PHE A 112     2244   3731   3004   -103   -355   -108       C  
ATOM    879  CE2 PHE A 112      12.730   0.776   4.502  1.00 23.38           C  
ANISOU  879  CE2 PHE A 112     2211   3694   2980   -104   -343   -118       C  
ATOM    880  CZ  PHE A 112      11.946   0.392   5.557  1.00 23.47           C  
ANISOU  880  CZ  PHE A 112     2221   3709   2988    -98   -353   -112       C  
ATOM    881  N   SER A 113       8.546  -2.160   1.224  1.00 17.96           N  
ANISOU  881  N   SER A 113     1603   2991   2231   -187   -392    -91       N  
ATOM    882  CA  SER A 113       7.197  -2.335   1.756  1.00 17.73           C  
ANISOU  882  CA  SER A 113     1550   2976   2211   -200   -419    -57       C  
ATOM    883  C   SER A 113       7.299  -2.916   3.161  1.00 17.77           C  
ANISOU  883  C   SER A 113     1532   2985   2234   -178   -412    -56       C  
ATOM    884  O   SER A 113       8.227  -3.669   3.436  1.00 16.95           O  
ANISOU  884  O   SER A 113     1442   2868   2131   -168   -398    -79       O  
ATOM    885  CB  SER A 113       6.386  -3.260   0.863  1.00 19.20           C  
ANISOU  885  CB  SER A 113     1769   3147   2379   -241   -453    -41       C  
ATOM    886  OG  SER A 113       6.416  -2.789  -0.473  1.00 21.89           O  
ANISOU  886  OG  SER A 113     2143   3478   2696   -264   -461    -46       O  
ATOM    887  N   VAL A 114       6.340  -2.594   4.029  1.00 17.73           N  
ANISOU  887  N   VAL A 114     1493   2998   2244   -168   -417    -24       N  
ATOM    888  CA  VAL A 114       6.285  -3.103   5.394  1.00 17.56           C  
ANISOU  888  CA  VAL A 114     1454   2982   2238   -146   -410    -18       C  
ATOM    889  C   VAL A 114       5.001  -3.880   5.532  1.00 18.17           C  
ANISOU  889  C   VAL A 114     1514   3065   2325   -163   -433     24       C  
ATOM    890  O   VAL A 114       3.935  -3.357   5.203  1.00 18.27           O  
ANISOU  890  O   VAL A 114     1506   3091   2345   -173   -444     65       O  
ATOM    891  CB  VAL A 114       6.320  -1.948   6.448  1.00 17.64           C  
ANISOU  891  CB  VAL A 114     1448   3003   2252   -111   -387    -13       C  
ATOM    892  CG1 VAL A 114       6.063  -2.475   7.856  1.00 17.91           C  
ANISOU  892  CG1 VAL A 114     1471   3039   2296    -89   -379      0       C  
ATOM    893  CG2 VAL A 114       7.645  -1.190   6.394  1.00 17.90           C  
ANISOU  893  CG2 VAL A 114     1496   3027   2277   -101   -374    -48       C  
ATOM    894  N   LEU A 115       5.081  -5.119   6.042  1.00 17.98           N  
ANISOU  894  N   LEU A 115     1494   3031   2305   -168   -440     22       N  
ATOM    895  CA  LEU A 115       3.881  -5.879   6.338  1.00 18.29           C  
ANISOU  895  CA  LEU A 115     1512   3078   2360   -184   -465     68       C  
ATOM    896  C   LEU A 115       3.684  -5.740   7.852  1.00 18.86           C  
ANISOU  896  C   LEU A 115     1554   3163   2449   -144   -439     84       C  
ATOM    897  O   LEU A 115       4.386  -6.393   8.627  1.00 18.85           O  
ANISOU  897  O   LEU A 115     1561   3155   2447   -130   -429     60       O  
ATOM    898  CB  LEU A 115       4.057  -7.347   5.952  1.00 18.37           C  
ANISOU  898  CB  LEU A 115     1554   3064   2362   -216   -489     56       C  
ATOM    899  CG  LEU A 115       2.844  -8.248   6.220  1.00 19.95           C  
ANISOU  899  CG  LEU A 115     1733   3267   2579   -242   -524    109       C  
ATOM    900  CD1 LEU A 115       1.649  -7.784   5.419  1.00 20.52           C  
ANISOU  900  CD1 LEU A 115     1788   3351   2658   -276   -558    163       C  
ATOM    901  CD2 LEU A 115       3.174  -9.701   5.909  1.00 20.43           C  
ANISOU  901  CD2 LEU A 115     1840   3298   2626   -271   -546     89       C  
ATOM    902  N   ALA A 116       2.809  -4.829   8.276  1.00 19.11           N  
ANISOU  902  N   ALA A 116     1556   3213   2492   -122   -424    126       N  
ATOM    903  CA  ALA A 116       2.573  -4.604   9.695  1.00 19.44           C  
ANISOU  903  CA  ALA A 116     1582   3261   2541    -78   -392    144       C  
ATOM    904  C   ALA A 116       1.821  -5.798  10.238  1.00 20.47           C  
ANISOU  904  C   ALA A 116     1688   3397   2692    -86   -406    182       C  
ATOM    905  O   ALA A 116       0.796  -6.181   9.665  1.00 20.58           O  
ANISOU  905  O   ALA A 116     1676   3419   2725   -115   -434    233       O  
ATOM    906  CB  ALA A 116       1.773  -3.325   9.922  1.00 19.46           C  
ANISOU  906  CB  ALA A 116     1569   3277   2550    -47   -363    184       C  
ATOM    907  N   CYS A 117       2.343  -6.389  11.319  1.00 20.93           N  
ANISOU  907  N   CYS A 117     1755   3449   2748    -65   -393    162       N  
ATOM    908  CA  CYS A 117       1.796  -7.555  12.003  1.00 22.02           C  
ANISOU  908  CA  CYS A 117     1872   3589   2903    -68   -402    194       C  
ATOM    909  C   CYS A 117       1.604  -7.348  13.485  1.00 23.49           C  
ANISOU  909  C   CYS A 117     2053   3780   3090    -19   -364    212       C  
ATOM    910  O   CYS A 117       2.364  -6.632  14.115  1.00 23.25           O  
ANISOU  910  O   CYS A 117     2053   3742   3038     10   -339    177       O  
ATOM    911  CB  CYS A 117       2.674  -8.777  11.766  1.00 22.91           C  
ANISOU  911  CB  CYS A 117     2009   3685   3009    -95   -427    151       C  
ATOM    912  SG  CYS A 117       2.810  -9.270  10.041  1.00 24.70           S  
ANISOU  912  SG  CYS A 117     2263   3895   3226   -152   -468    134       S  
ATOM    913  N   TYR A 118       0.654  -8.093  14.065  1.00 24.69           N  
ANISOU  913  N   TYR A 118     2172   3943   3267    -14   -364    267       N  
ATOM    914  CA  TYR A 118       0.362  -8.131  15.497  1.00 25.92           C  
ANISOU  914  CA  TYR A 118     2324   4101   3424     33   -326    292       C  
ATOM    915  C   TYR A 118       0.082  -9.576  15.838  1.00 26.68           C  
ANISOU  915  C   TYR A 118     2397   4199   3540     13   -350    313       C  
ATOM    916  O   TYR A 118      -0.718 -10.201  15.143  1.00 26.04           O  
ANISOU  916  O   TYR A 118     2283   4125   3485    -23   -384    356       O  
ATOM    917  CB  TYR A 118      -0.851  -7.228  15.864  1.00 26.00           C  
ANISOU  917  CB  TYR A 118     2308   4124   3448     75   -284    364       C  
ATOM    918  CG  TYR A 118      -0.526  -5.777  15.611  1.00 26.81           C  
ANISOU  918  CG  TYR A 118     2443   4220   3526     98   -256    339       C  
ATOM    919  CD1 TYR A 118       0.233  -5.048  16.519  1.00 27.77           C  
ANISOU  919  CD1 TYR A 118     2620   4322   3609    136   -223    297       C  
ATOM    920  CD2 TYR A 118      -0.802  -5.189  14.383  1.00 27.72           C  
ANISOU  920  CD2 TYR A 118     2541   4342   3650     72   -275    349       C  
ATOM    921  CE1 TYR A 118       0.619  -3.741  16.253  1.00 28.35           C  
ANISOU  921  CE1 TYR A 118     2730   4384   3657    150   -205    271       C  
ATOM    922  CE2 TYR A 118      -0.381  -3.899  14.088  1.00 28.51           C  
ANISOU  922  CE2 TYR A 118     2672   4433   3726     89   -254    321       C  
ATOM    923  CZ  TYR A 118       0.337  -3.181  15.023  1.00 29.16           C  
ANISOU  923  CZ  TYR A 118     2810   4497   3773    128   -220    281       C  
ATOM    924  OH  TYR A 118       0.748  -1.906  14.734  1.00 30.10           O  
ANISOU  924  OH  TYR A 118     2965   4604   3868    140   -204    254       O  
ATOM    925  N   ASN A 119       0.799 -10.134  16.852  1.00 27.27           N  
ANISOU  925  N   ASN A 119     2494   4265   3602     31   -340    281       N  
ATOM    926  CA  ASN A 119       0.627 -11.524  17.294  1.00 28.02           C  
ANISOU  926  CA  ASN A 119     2572   4360   3716     16   -360    297       C  
ATOM    927  C   ASN A 119       0.818 -12.528  16.128  1.00 27.55           C  
ANISOU  927  C   ASN A 119     2512   4290   3665    -43   -412    280       C  
ATOM    928  O   ASN A 119       0.060 -13.480  16.012  1.00 27.55           O  
ANISOU  928  O   ASN A 119     2487   4293   3689    -69   -440    323       O  
ATOM    929  CB  ASN A 119      -0.756 -11.709  17.954  1.00 30.18           C  
ANISOU  929  CB  ASN A 119     2800   4650   4018     39   -340    382       C  
ATOM    930  CG  ASN A 119      -1.080 -10.682  19.007  1.00 35.12           C  
ANISOU  930  CG  ASN A 119     3436   5278   4629    104   -279    406       C  
ATOM    931  OD1 ASN A 119      -1.890  -9.772  18.792  1.00 36.72           O  
ANISOU  931  OD1 ASN A 119     3621   5490   4841    127   -251    453       O  
ATOM    932  ND2 ASN A 119      -0.452 -10.798  20.173  1.00 36.57           N  
ANISOU  932  ND2 ASN A 119     3655   5450   4788    134   -255    377       N  
ATOM    933  N   GLY A 120       1.788 -12.261  15.256  1.00 26.71           N  
ANISOU  933  N   GLY A 120     2439   4170   3539    -63   -424    222       N  
ATOM    934  CA  GLY A 120       2.093 -13.101  14.106  1.00 26.39           C  
ANISOU  934  CA  GLY A 120     2420   4112   3496   -111   -463    199       C  
ATOM    935  C   GLY A 120       1.130 -13.002  12.938  1.00 26.34           C  
ANISOU  935  C   GLY A 120     2404   4108   3498   -152   -498    239       C  
ATOM    936  O   GLY A 120       1.312 -13.697  11.934  1.00 25.98           O  
ANISOU  936  O   GLY A 120     2390   4040   3442   -197   -534    222       O  
ATOM    937  N   SER A 121       0.093 -12.138  13.062  1.00 26.86           N  
ANISOU  937  N   SER A 121     2429   4196   3580   -138   -487    296       N  
ATOM    938  CA  SER A 121      -0.947 -11.943  12.044  1.00 27.45           C  
ANISOU  938  CA  SER A 121     2483   4277   3671   -178   -523    351       C  
ATOM    939  C   SER A 121      -0.830 -10.592  11.362  1.00 27.02           C  
ANISOU  939  C   SER A 121     2434   4230   3603   -168   -507    338       C  
ATOM    940  O   SER A 121      -0.732  -9.569  12.027  1.00 25.60           O  
ANISOU  940  O   SER A 121     2245   4062   3420   -119   -460    336       O  
ATOM    941  CB  SER A 121      -2.329 -12.028  12.683  1.00 29.67           C  
ANISOU  941  CB  SER A 121     2701   4582   3992   -167   -521    446       C  
ATOM    942  OG  SER A 121      -2.581 -13.347  13.131  1.00 33.76           O  
ANISOU  942  OG  SER A 121     3209   5093   4525   -186   -546    467       O  
ATOM    943  N   PRO A 122      -0.911 -10.560  10.026  1.00 28.26           N  
ANISOU  943  N   PRO A 122     2612   4376   3750   -217   -548    334       N  
ATOM    944  CA  PRO A 122      -0.778  -9.275   9.321  1.00 28.30           C  
ANISOU  944  CA  PRO A 122     2622   4388   3743   -210   -534    322       C  
ATOM    945  C   PRO A 122      -2.009  -8.377   9.399  1.00 28.25           C  
ANISOU  945  C   PRO A 122     2560   4408   3767   -195   -523    403       C  
ATOM    946  O   PRO A 122      -3.149  -8.835   9.311  1.00 29.20           O  
ANISOU  946  O   PRO A 122     2637   4539   3919   -222   -555    483       O  
ATOM    947  CB  PRO A 122      -0.460  -9.682   7.873  1.00 29.64           C  
ANISOU  947  CB  PRO A 122     2841   4534   3888   -268   -581    293       C  
ATOM    948  CG  PRO A 122      -0.219 -11.179   7.894  1.00 30.52           C  
ANISOU  948  CG  PRO A 122     2984   4619   3991   -300   -612    277       C  
ATOM    949  CD  PRO A 122      -1.007 -11.687   9.082  1.00 28.47           C  
ANISOU  949  CD  PRO A 122     2671   4378   3767   -282   -607    333       C  
ATOM    950  N   SER A 123      -1.777  -7.093   9.602  1.00 26.80           N  
ANISOU  950  N   SER A 123     2375   4233   3575   -151   -478    390       N  
ATOM    951  CA  SER A 123      -2.835  -6.097   9.631  1.00 26.19           C  
ANISOU  951  CA  SER A 123     2250   4176   3523   -127   -455    463       C  
ATOM    952  C   SER A 123      -2.873  -5.295   8.327  1.00 24.40           C  
ANISOU  952  C   SER A 123     2032   3951   3289   -158   -478    461       C  
ATOM    953  O   SER A 123      -3.941  -4.853   7.941  1.00 24.53           O  
ANISOU  953  O   SER A 123     2002   3984   3334   -167   -488    540       O  
ATOM    954  CB  SER A 123      -2.701  -5.166  10.829  1.00 28.19           C  
ANISOU  954  CB  SER A 123     2506   4434   3771    -52   -383    460       C  
ATOM    955  OG  SER A 123      -1.388  -4.658  10.972  1.00 33.43           O  
ANISOU  955  OG  SER A 123     3226   5081   4396    -35   -363    371       O  
ATOM    956  N   GLY A 124      -1.734  -5.117   7.665  1.00 22.48           N  
ANISOU  956  N   GLY A 124     1843   3691   3009   -173   -486    379       N  
ATOM    957  CA  GLY A 124      -1.697  -4.380   6.415  1.00 21.20           C  
ANISOU  957  CA  GLY A 124     1694   3527   2835   -201   -506    373       C  
ATOM    958  C   GLY A 124      -0.325  -4.219   5.819  1.00 19.93           C  
ANISOU  958  C   GLY A 124     1593   3346   2635   -208   -503    283       C  
ATOM    959  O   GLY A 124       0.671  -4.601   6.426  1.00 18.85           O  
ANISOU  959  O   GLY A 124     1483   3197   2482   -188   -483    227       O  
ATOM    960  N   VAL A 125      -0.269  -3.630   4.620  1.00 19.68           N  
ANISOU  960  N   VAL A 125     1577   3311   2589   -236   -522    276       N  
ATOM    961  CA  VAL A 125       0.977  -3.410   3.938  1.00 20.37           C  
ANISOU  961  CA  VAL A 125     1717   3381   2643   -241   -516    202       C  
ATOM    962  C   VAL A 125       1.056  -1.984   3.414  1.00 21.25           C  
ANISOU  962  C   VAL A 125     1824   3501   2749   -227   -496    200       C  
ATOM    963  O   VAL A 125       0.062  -1.443   2.912  1.00 21.82           O  
ANISOU  963  O   VAL A 125     1866   3588   2837   -242   -512    257       O  
ATOM    964  CB  VAL A 125       1.238  -4.496   2.851  1.00 21.19           C  
ANISOU  964  CB  VAL A 125     1872   3459   2721   -297   -561    181       C  
ATOM    965  CG1 VAL A 125       0.109  -4.544   1.831  1.00 22.09           C  
ANISOU  965  CG1 VAL A 125     1980   3574   2838   -352   -616    240       C  
ATOM    966  CG2 VAL A 125       2.586  -4.301   2.168  1.00 21.52           C  
ANISOU  966  CG2 VAL A 125     1968   3480   2729   -292   -541    110       C  
ATOM    967  N   TYR A 126       2.214  -1.344   3.583  1.00 21.24           N  
ANISOU  967  N   TYR A 126     1847   3493   2730   -197   -463    142       N  
ATOM    968  CA  TYR A 126       2.401   0.015   3.095  1.00 21.43           C  
ANISOU  968  CA  TYR A 126     1872   3523   2748   -184   -445    136       C  
ATOM    969  C   TYR A 126       3.820   0.219   2.591  1.00 22.66           C  
ANISOU  969  C   TYR A 126     2069   3663   2880   -184   -435     70       C  
ATOM    970  O   TYR A 126       4.732  -0.493   2.997  1.00 22.71           O  
ANISOU  970  O   TYR A 126     2094   3656   2879   -178   -427     33       O  
ATOM    971  CB  TYR A 126       2.015   1.064   4.164  1.00 21.61           C  
ANISOU  971  CB  TYR A 126     1869   3557   2785   -134   -404    160       C  
ATOM    972  CG  TYR A 126       2.795   0.956   5.456  1.00 22.33           C  
ANISOU  972  CG  TYR A 126     1976   3639   2870    -97   -375    125       C  
ATOM    973  CD1 TYR A 126       3.996   1.627   5.622  1.00 23.15           C  
ANISOU  973  CD1 TYR A 126     2111   3731   2956    -82   -359     74       C  
ATOM    974  CD2 TYR A 126       2.337   0.170   6.505  1.00 23.38           C  
ANISOU  974  CD2 TYR A 126     2094   3775   3015    -81   -369    148       C  
ATOM    975  CE1 TYR A 126       4.722   1.523   6.797  1.00 23.95           C  
ANISOU  975  CE1 TYR A 126     2230   3822   3050    -57   -343     48       C  
ATOM    976  CE2 TYR A 126       3.066   0.044   7.680  1.00 24.27           C  
ANISOU  976  CE2 TYR A 126     2227   3877   3118    -52   -348    117       C  
ATOM    977  CZ  TYR A 126       4.247   0.739   7.828  1.00 25.20           C  
ANISOU  977  CZ  TYR A 126     2378   3982   3216    -42   -337     68       C  
ATOM    978  OH  TYR A 126       4.960   0.648   8.991  1.00 27.71           O  
ANISOU  978  OH  TYR A 126     2717   4287   3523    -20   -325     43       O  
ATOM    979  N   GLN A 127       4.012   1.205   1.722  1.00 23.35           N  
ANISOU  979  N   GLN A 127     2164   3751   2957   -190   -432     64       N  
ATOM    980  CA  GLN A 127       5.317   1.510   1.176  1.00 24.07           C  
ANISOU  980  CA  GLN A 127     2286   3829   3029   -188   -419     13       C  
ATOM    981  C   GLN A 127       5.977   2.592   2.031  1.00 25.21           C  
ANISOU  981  C   GLN A 127     2423   3976   3178   -151   -388     -4       C  
ATOM    982  O   GLN A 127       5.316   3.542   2.450  1.00 26.07           O  
ANISOU  982  O   GLN A 127     2515   4095   3296   -131   -376     22       O  
ATOM    983  CB  GLN A 127       5.181   1.873  -0.315  1.00 24.72           C  
ANISOU  983  CB  GLN A 127     2388   3908   3095   -220   -436     16       C  
ATOM    984  CG  GLN A 127       6.484   2.031  -1.041  1.00 25.75           C  
ANISOU  984  CG  GLN A 127     2554   4024   3207   -219   -420    -29       C  
ATOM    985  CD  GLN A 127       7.122   0.744  -1.488  1.00 28.00           C  
ANISOU  985  CD  GLN A 127     2881   4286   3474   -233   -421    -54       C  
ATOM    986  OE1 GLN A 127       6.719  -0.367  -1.128  1.00 27.59           O  
ANISOU  986  OE1 GLN A 127     2836   4227   3422   -244   -437    -47       O  
ATOM    987  NE2 GLN A 127       8.163   0.880  -2.279  1.00 28.91           N  
ANISOU  987  NE2 GLN A 127     3027   4386   3572   -229   -400    -82       N  
ATOM    988  N   CYS A 128       7.244   2.369   2.377  1.00 25.19           N  
ANISOU  988  N   CYS A 128     2436   3963   3172   -141   -377    -42       N  
ATOM    989  CA  CYS A 128       8.121   3.163   3.258  1.00 25.83           C  
ANISOU  989  CA  CYS A 128     2520   4040   3256   -116   -360    -60       C  
ATOM    990  C   CYS A 128       9.370   3.622   2.506  1.00 24.49           C  
ANISOU  990  C   CYS A 128     2361   3862   3082   -123   -355    -85       C  
ATOM    991  O   CYS A 128       9.685   3.091   1.454  1.00 24.43           O  
ANISOU  991  O   CYS A 128     2364   3850   3068   -139   -355    -94       O  
ATOM    992  CB  CYS A 128       8.563   2.274   4.430  1.00 27.93           C  
ANISOU  992  CB  CYS A 128     2785   4299   3528   -105   -359    -69       C  
ATOM    993  SG  CYS A 128       7.760   2.645   5.982  1.00 40.83           S  
ANISOU  993  SG  CYS A 128     4416   5934   5162    -75   -349    -48       S  
ATOM    994  N   ALA A 129      10.195   4.436   3.172  1.00 23.17           N  
ANISOU  994  N   ALA A 129     2197   3690   2918   -110   -350    -94       N  
ATOM    995  CA  ALA A 129      11.533   4.736   2.699  1.00 22.33           C  
ANISOU  995  CA  ALA A 129     2092   3577   2818   -115   -347   -108       C  
ATOM    996  C   ALA A 129      12.424   4.894   3.915  1.00 21.38           C  
ANISOU  996  C   ALA A 129     1971   3448   2706   -109   -355   -111       C  
ATOM    997  O   ALA A 129      12.029   5.512   4.901  1.00 21.87           O  
ANISOU  997  O   ALA A 129     2047   3504   2759    -99   -361   -107       O  
ATOM    998  CB  ALA A 129      11.569   5.995   1.850  1.00 21.47           C  
ANISOU  998  CB  ALA A 129     1986   3469   2703   -121   -344   -106       C  
ATOM    999  N   MET A 130      13.655   4.402   3.826  1.00 20.63           N  
ANISOU  999  N   MET A 130     1864   3347   2626   -113   -353   -112       N  
ATOM   1000  CA  MET A 130      14.657   4.613   4.862  1.00 20.36           C  
ANISOU 1000  CA  MET A 130     1826   3305   2605   -115   -370   -105       C  
ATOM   1001  C   MET A 130      15.035   6.094   4.759  1.00 19.98           C  
ANISOU 1001  C   MET A 130     1788   3251   2554   -125   -383   -100       C  
ATOM   1002  O   MET A 130      15.514   6.517   3.716  1.00 19.31           O  
ANISOU 1002  O   MET A 130     1691   3170   2477   -131   -374    -96       O  
ATOM   1003  CB  MET A 130      15.902   3.768   4.572  1.00 20.58           C  
ANISOU 1003  CB  MET A 130     1828   3331   2660   -116   -361    -95       C  
ATOM   1004  CG  MET A 130      17.020   3.934   5.592  1.00 22.82           C  
ANISOU 1004  CG  MET A 130     2099   3609   2964   -126   -386    -75       C  
ATOM   1005  SD  MET A 130      16.514   3.597   7.305  1.00 25.57           S  
ANISOU 1005  SD  MET A 130     2469   3949   3297   -126   -413    -79       S  
ATOM   1006  CE  MET A 130      15.823   1.924   7.127  1.00 23.92           C  
ANISOU 1006  CE  MET A 130     2250   3748   3090   -108   -385    -91       C  
ATOM   1007  N   ARG A 131      14.688   6.895   5.764  1.00 19.16           N  
ANISOU 1007  N   ARG A 131     1713   3135   2431   -125   -401   -101       N  
ATOM   1008  CA  ARG A 131      14.974   8.323   5.728  1.00 18.78           C  
ANISOU 1008  CA  ARG A 131     1688   3074   2374   -135   -416    -97       C  
ATOM   1009  C   ARG A 131      16.485   8.566   5.744  1.00 20.18           C  
ANISOU 1009  C   ARG A 131     1847   3246   2576   -160   -442    -79       C  
ATOM   1010  O   ARG A 131      17.232   7.730   6.255  1.00 20.18           O  
ANISOU 1010  O   ARG A 131     1826   3245   2595   -166   -454    -67       O  
ATOM   1011  CB  ARG A 131      14.306   9.027   6.921  1.00 18.59           C  
ANISOU 1011  CB  ARG A 131     1717   3029   2319   -126   -425   -101       C  
ATOM   1012  CG  ARG A 131      12.775   8.898   6.995  1.00 19.96           C  
ANISOU 1012  CG  ARG A 131     1901   3209   2474    -97   -394   -104       C  
ATOM   1013  CD  ARG A 131      12.071   9.264   5.689  1.00 20.28           C  
ANISOU 1013  CD  ARG A 131     1920   3266   2519    -92   -373   -101       C  
ATOM   1014  NE  ARG A 131      12.538  10.549   5.163  1.00 20.53           N  
ANISOU 1014  NE  ARG A 131     1966   3288   2547   -103   -381   -101       N  
ATOM   1015  CZ  ARG A 131      12.177  11.066   3.994  1.00 20.91           C  
ANISOU 1015  CZ  ARG A 131     1998   3349   2600   -104   -368    -97       C  
ATOM   1016  NH1 ARG A 131      11.305  10.430   3.219  1.00 18.68           N  
ANISOU 1016  NH1 ARG A 131     1689   3086   2322    -98   -351    -92       N  
ATOM   1017  NH2 ARG A 131      12.663  12.237   3.603  1.00 20.56           N  
ANISOU 1017  NH2 ARG A 131     1966   3293   2551   -114   -376    -96       N  
ATOM   1018  N   PRO A 132      16.959   9.747   5.285  1.00 20.22           N  
ANISOU 1018  N   PRO A 132     1858   3242   2581   -175   -456    -70       N  
ATOM   1019  CA  PRO A 132      18.395  10.038   5.363  1.00 20.33           C  
ANISOU 1019  CA  PRO A 132     1850   3250   2625   -203   -487    -40       C  
ATOM   1020  C   PRO A 132      18.942  10.103   6.802  1.00 20.63           C  
ANISOU 1020  C   PRO A 132     1916   3266   2656   -226   -535    -26       C  
ATOM   1021  O   PRO A 132      20.157  10.002   6.993  1.00 20.58           O  
ANISOU 1021  O   PRO A 132     1879   3258   2682   -252   -567      9       O  
ATOM   1022  CB  PRO A 132      18.499  11.376   4.637  1.00 20.71           C  
ANISOU 1022  CB  PRO A 132     1909   3293   2669   -214   -493    -36       C  
ATOM   1023  CG  PRO A 132      17.329  11.359   3.679  1.00 21.19           C  
ANISOU 1023  CG  PRO A 132     1971   3368   2712   -187   -450    -61       C  
ATOM   1024  CD  PRO A 132      16.250  10.846   4.606  1.00 19.51           C  
ANISOU 1024  CD  PRO A 132     1789   3151   2473   -169   -444    -80       C  
ATOM   1025  N   ASN A 133      18.062  10.222   7.823  1.00 20.57           N  
ANISOU 1025  N   ASN A 133     1965   3240   2609   -217   -541    -48       N  
ATOM   1026  CA  ASN A 133      18.520  10.177   9.224  1.00 21.03           C  
ANISOU 1026  CA  ASN A 133     2064   3275   2654   -239   -586    -37       C  
ATOM   1027  C   ASN A 133      18.392   8.725   9.816  1.00 20.94           C  
ANISOU 1027  C   ASN A 133     2028   3277   2652   -224   -574    -39       C  
ATOM   1028  O   ASN A 133      18.436   8.557  11.031  1.00 20.73           O  
ANISOU 1028  O   ASN A 133     2041   3230   2604   -234   -602    -37       O  
ATOM   1029  CB  ASN A 133      17.737  11.183  10.085  1.00 21.75           C  
ANISOU 1029  CB  ASN A 133     2247   3330   2689   -235   -596    -56       C  
ATOM   1030  CG  ASN A 133      16.254  10.917  10.130  1.00 24.11           C  
ANISOU 1030  CG  ASN A 133     2566   3635   2961   -189   -543    -82       C  
ATOM   1031  OD1 ASN A 133      15.764   9.909   9.612  1.00 23.74           O  
ANISOU 1031  OD1 ASN A 133     2466   3618   2935   -166   -508    -88       O  
ATOM   1032  ND2 ASN A 133      15.496  11.815  10.765  1.00 25.21           N  
ANISOU 1032  ND2 ASN A 133     2784   3742   3053   -173   -535    -93       N  
ATOM   1033  N   PHE A 134      18.125   7.712   8.952  1.00 21.08           N  
ANISOU 1033  N   PHE A 134     1990   3323   2695   -199   -531    -45       N  
ATOM   1034  CA  PHE A 134      17.997   6.293   9.284  1.00 21.54           C  
ANISOU 1034  CA  PHE A 134     2022   3395   2767   -184   -514    -47       C  
ATOM   1035  C   PHE A 134      16.766   5.905  10.133  1.00 22.03           C  
ANISOU 1035  C   PHE A 134     2124   3452   2795   -161   -500    -70       C  
ATOM   1036  O   PHE A 134      16.776   4.882  10.836  1.00 23.45           O  
ANISOU 1036  O   PHE A 134     2296   3634   2979   -156   -502    -68       O  
ATOM   1037  CB  PHE A 134      19.268   5.773   9.929  1.00 20.98           C  
ANISOU 1037  CB  PHE A 134     1924   3320   2726   -208   -549    -13       C  
ATOM   1038  CG  PHE A 134      20.439   5.798   8.980  1.00 21.53           C  
ANISOU 1038  CG  PHE A 134     1935   3402   2843   -219   -546     21       C  
ATOM   1039  CD1 PHE A 134      20.588   4.818   8.012  1.00 22.73           C  
ANISOU 1039  CD1 PHE A 134     2040   3573   3023   -193   -498     25       C  
ATOM   1040  CD2 PHE A 134      21.373   6.816   9.035  1.00 22.16           C  
ANISOU 1040  CD2 PHE A 134     2012   3470   2936   -253   -589     54       C  
ATOM   1041  CE1 PHE A 134      21.684   4.832   7.149  1.00 23.65           C  
ANISOU 1041  CE1 PHE A 134     2107   3697   3183   -194   -484     63       C  
ATOM   1042  CE2 PHE A 134      22.465   6.825   8.178  1.00 22.79           C  
ANISOU 1042  CE2 PHE A 134     2032   3562   3065   -260   -581     97       C  
ATOM   1043  CZ  PHE A 134      22.616   5.835   7.242  1.00 22.87           C  
ANISOU 1043  CZ  PHE A 134     1994   3592   3104   -226   -524    102       C  
ATOM   1044  N   THR A 135      15.730   6.711  10.078  1.00 20.99           N  
ANISOU 1044  N   THR A 135     2031   3312   2631   -145   -484    -86       N  
ATOM   1045  CA  THR A 135      14.470   6.374  10.724  1.00 20.61           C  
ANISOU 1045  CA  THR A 135     2011   3262   2556   -116   -460    -97       C  
ATOM   1046  C   THR A 135      13.513   6.016   9.573  1.00 20.42           C  
ANISOU 1046  C   THR A 135     1952   3263   2544    -97   -422   -102       C  
ATOM   1047  O   THR A 135      13.857   6.158   8.401  1.00 19.92           O  
ANISOU 1047  O   THR A 135     1858   3212   2499   -106   -416   -103       O  
ATOM   1048  CB  THR A 135      13.931   7.575  11.563  1.00 20.97           C  
ANISOU 1048  CB  THR A 135     2133   3276   2557   -107   -462   -101       C  
ATOM   1049  OG1 THR A 135      13.498   8.604  10.679  1.00 20.97           O  
ANISOU 1049  OG1 THR A 135     2139   3276   2552   -100   -445   -103       O  
ATOM   1050  CG2 THR A 135      14.931   8.092  12.560  1.00 20.61           C  
ANISOU 1050  CG2 THR A 135     2139   3198   2493   -137   -511    -94       C  
ATOM   1051  N   ILE A 136      12.345   5.496   9.907  1.00 20.62           N  
ANISOU 1051  N   ILE A 136     1980   3294   2559    -73   -398   -101       N  
ATOM   1052  CA  ILE A 136      11.300   5.259   8.937  1.00 21.48           C  
ANISOU 1052  CA  ILE A 136     2063   3424   2676    -61   -372    -97       C  
ATOM   1053  C   ILE A 136      10.053   5.875   9.552  1.00 21.35           C  
ANISOU 1053  C   ILE A 136     2076   3399   2637    -31   -349    -83       C  
ATOM   1054  O   ILE A 136       9.892   5.881  10.779  1.00 20.97           O  
ANISOU 1054  O   ILE A 136     2064   3334   2570    -15   -345    -79       O  
ATOM   1055  CB  ILE A 136      11.113   3.767   8.470  1.00 22.73           C  
ANISOU 1055  CB  ILE A 136     2181   3601   2856    -65   -368    -96       C  
ATOM   1056  CG1 ILE A 136      10.326   2.917   9.460  1.00 23.82           C  
ANISOU 1056  CG1 ILE A 136     2321   3740   2990    -48   -361    -86       C  
ATOM   1057  CG2 ILE A 136      12.459   3.058   8.108  1.00 23.16           C  
ANISOU 1057  CG2 ILE A 136     2214   3656   2931    -83   -380   -105       C  
ATOM   1058  CD1 ILE A 136       9.816   1.574   8.828  1.00 25.44           C  
ANISOU 1058  CD1 ILE A 136     2493   3960   3212    -55   -358    -81       C  
ATOM   1059  N   LYS A 137       9.188   6.418   8.715  1.00 21.62           N  
ANISOU 1059  N   LYS A 137     2098   3444   2674    -22   -330    -70       N  
ATOM   1060  CA  LYS A 137       7.932   6.992   9.184  1.00 22.69           C  
ANISOU 1060  CA  LYS A 137     2252   3573   2796     12   -298    -44       C  
ATOM   1061  C   LYS A 137       6.915   5.920   8.875  1.00 22.65           C  
ANISOU 1061  C   LYS A 137     2200   3594   2814     16   -289    -18       C  
ATOM   1062  O   LYS A 137       6.355   5.891   7.787  1.00 22.46           O  
ANISOU 1062  O   LYS A 137     2142   3588   2805      5   -290     -2       O  
ATOM   1063  CB  LYS A 137       7.613   8.301   8.436  1.00 25.85           C  
ANISOU 1063  CB  LYS A 137     2662   3969   3190     18   -285    -36       C  
ATOM   1064  CG  LYS A 137       8.537   9.457   8.790  1.00 30.85           C  
ANISOU 1064  CG  LYS A 137     3349   4573   3799     12   -297    -57       C  
ATOM   1065  CD  LYS A 137       8.162  10.698   7.981  1.00 36.86           C  
ANISOU 1065  CD  LYS A 137     4116   5331   4557     18   -282    -47       C  
ATOM   1066  CE  LYS A 137       8.872  11.952   8.413  1.00 42.12           C  
ANISOU 1066  CE  LYS A 137     4847   5962   5195     14   -292    -62       C  
ATOM   1067  NZ  LYS A 137       9.352  12.744   7.232  1.00 45.12           N  
ANISOU 1067  NZ  LYS A 137     5210   6349   5586     -7   -303    -67       N  
ATOM   1068  N   GLY A 138       6.758   4.982   9.798  1.00 22.28           N  
ANISOU 1068  N   GLY A 138     2152   3546   2767     26   -287    -13       N  
ATOM   1069  CA  GLY A 138       5.851   3.863   9.601  1.00 21.99           C  
ANISOU 1069  CA  GLY A 138     2072   3530   2753     25   -285     14       C  
ATOM   1070  C   GLY A 138       4.536   4.048  10.313  1.00 22.04           C  
ANISOU 1070  C   GLY A 138     2076   3538   2762     64   -250     62       C  
ATOM   1071  O   GLY A 138       4.114   5.172  10.606  1.00 22.71           O  
ANISOU 1071  O   GLY A 138     2188   3610   2832     96   -218     79       O  
ATOM   1072  N   SER A 139       3.865   2.940  10.577  1.00 20.83           N  
ANISOU 1072  N   SER A 139     1890   3399   2627     64   -251     90       N  
ATOM   1073  CA  SER A 139       2.626   2.952  11.313  1.00 20.79           C  
ANISOU 1073  CA  SER A 139     1872   3396   2630    104   -214    146       C  
ATOM   1074  C   SER A 139       2.730   1.701  12.152  1.00 21.35           C  
ANISOU 1074  C   SER A 139     1937   3470   2706    103   -223    143       C  
ATOM   1075  O   SER A 139       2.511   0.601  11.652  1.00 21.57           O  
ANISOU 1075  O   SER A 139     1924   3514   2758     72   -252    153       O  
ATOM   1076  CB  SER A 139       1.438   2.909  10.361  1.00 21.73           C  
ANISOU 1076  CB  SER A 139     1935   3540   2783     95   -216    204       C  
ATOM   1077  OG  SER A 139       0.222   2.744  11.071  1.00 24.57           O  
ANISOU 1077  OG  SER A 139     2268   3907   3161    133   -180    272       O  
ATOM   1078  N   PHE A 140       3.179   1.859  13.396  1.00 21.67           N  
ANISOU 1078  N   PHE A 140     2026   3488   2719    130   -205    125       N  
ATOM   1079  CA  PHE A 140       3.395   0.719  14.271  1.00 23.11           C  
ANISOU 1079  CA  PHE A 140     2207   3670   2903    129   -214    119       C  
ATOM   1080  C   PHE A 140       2.918   1.036  15.656  1.00 23.85           C  
ANISOU 1080  C   PHE A 140     2344   3744   2972    181   -169    143       C  
ATOM   1081  O   PHE A 140       3.279   2.060  16.209  1.00 23.78           O  
ANISOU 1081  O   PHE A 140     2401   3708   2927    203   -150    126       O  
ATOM   1082  CB  PHE A 140       4.895   0.366  14.361  1.00 23.36           C  
ANISOU 1082  CB  PHE A 140     2263   3691   2921     97   -252     60       C  
ATOM   1083  CG  PHE A 140       5.654  -0.037  13.119  1.00 24.27           C  
ANISOU 1083  CG  PHE A 140     2349   3818   3053     52   -289     31       C  
ATOM   1084  CD1 PHE A 140       5.643  -1.348  12.671  1.00 24.97           C  
ANISOU 1084  CD1 PHE A 140     2402   3920   3166     27   -310     32       C  
ATOM   1085  CD2 PHE A 140       6.464   0.872  12.459  1.00 25.12           C  
ANISOU 1085  CD2 PHE A 140     2475   3918   3151     37   -300      3       C  
ATOM   1086  CE1 PHE A 140       6.391  -1.729  11.558  1.00 25.27           C  
ANISOU 1086  CE1 PHE A 140     2428   3960   3212     -8   -335      4       C  
ATOM   1087  CE2 PHE A 140       7.216   0.486  11.354  1.00 25.38           C  
ANISOU 1087  CE2 PHE A 140     2487   3958   3198      2   -325    -21       C  
ATOM   1088  CZ  PHE A 140       7.188  -0.813  10.920  1.00 25.03           C  
ANISOU 1088  CZ  PHE A 140     2414   3924   3173    -17   -339    -21       C  
ATOM   1089  N   LEU A 141       2.145   0.128  16.236  1.00 24.31           N  
ANISOU 1089  N   LEU A 141     2372   3814   3049    198   -154    183       N  
ATOM   1090  CA  LEU A 141       1.660   0.218  17.606  1.00 25.13           C  
ANISOU 1090  CA  LEU A 141     2517   3900   3131    251   -106    210       C  
ATOM   1091  C   LEU A 141       2.400  -0.859  18.422  1.00 25.84           C  
ANISOU 1091  C   LEU A 141     2620   3986   3212    234   -134    179       C  
ATOM   1092  O   LEU A 141       3.176  -1.629  17.848  1.00 26.23           O  
ANISOU 1092  O   LEU A 141     2640   4048   3279    186   -183    145       O  
ATOM   1093  CB  LEU A 141       0.162  -0.090  17.629  1.00 25.06           C  
ANISOU 1093  CB  LEU A 141     2451   3911   3158    284    -66    292       C  
ATOM   1094  CG  LEU A 141      -0.757   0.873  16.908  1.00 26.36           C  
ANISOU 1094  CG  LEU A 141     2591   4083   3341    307    -33    343       C  
ATOM   1095  CD1 LEU A 141      -2.139   0.284  16.814  1.00 26.93           C  
ANISOU 1095  CD1 LEU A 141     2584   4183   3464    324    -12    434       C  
ATOM   1096  CD2 LEU A 141      -0.806   2.228  17.619  1.00 26.87           C  
ANISOU 1096  CD2 LEU A 141     2737   4111   3360    366     28    344       C  
ATOM   1097  N   ASN A 142       2.174  -0.944  19.754  1.00 26.04           N  
ANISOU 1097  N   ASN A 142     2692   3992   3211    274    -99    195       N  
ATOM   1098  CA  ASN A 142       2.810  -1.987  20.572  1.00 26.71           C  
ANISOU 1098  CA  ASN A 142     2786   4074   3289    259   -125    172       C  
ATOM   1099  C   ASN A 142       2.366  -3.376  20.056  1.00 25.89           C  
ANISOU 1099  C   ASN A 142     2596   4005   3237    233   -149    196       C  
ATOM   1100  O   ASN A 142       1.212  -3.542  19.638  1.00 25.91           O  
ANISOU 1100  O   ASN A 142     2544   4026   3272    247   -128    252       O  
ATOM   1101  CB  ASN A 142       2.466  -1.807  22.051  1.00 29.49           C  
ANISOU 1101  CB  ASN A 142     3207   4398   3601    311    -79    192       C  
ATOM   1102  CG  ASN A 142       3.156  -2.809  22.931  1.00 36.31           C  
ANISOU 1102  CG  ASN A 142     4085   5257   4455    293   -108    169       C  
ATOM   1103  OD1 ASN A 142       4.397  -2.837  23.044  1.00 38.49           O  
ANISOU 1103  OD1 ASN A 142     4393   5520   4711    255   -156    119       O  
ATOM   1104  ND2 ASN A 142       2.370  -3.669  23.565  1.00 38.27           N  
ANISOU 1104  ND2 ASN A 142     4304   5517   4719    320    -82    211       N  
ATOM   1105  N   GLY A 143       3.305  -4.312  19.974  1.00 25.08           N  
ANISOU 1105  N   GLY A 143     2480   3906   3142    192   -196    157       N  
ATOM   1106  CA  GLY A 143       3.016  -5.626  19.414  1.00 24.13           C  
ANISOU 1106  CA  GLY A 143     2293   3810   3064    162   -223    172       C  
ATOM   1107  C   GLY A 143       3.488  -5.786  17.975  1.00 22.85           C  
ANISOU 1107  C   GLY A 143     2101   3658   2922    115   -262    145       C  
ATOM   1108  O   GLY A 143       3.608  -6.918  17.490  1.00 22.04           O  
ANISOU 1108  O   GLY A 143     1966   3564   2843     83   -292    141       O  
ATOM   1109  N   SER A 144       3.773  -4.651  17.280  1.00 21.98           N  
ANISOU 1109  N   SER A 144     2010   3543   2799    111   -261    126       N  
ATOM   1110  CA  SER A 144       4.213  -4.648  15.878  1.00 21.08           C  
ANISOU 1110  CA  SER A 144     1875   3436   2698     71   -291    102       C  
ATOM   1111  C   SER A 144       5.686  -4.961  15.696  1.00 20.40           C  
ANISOU 1111  C   SER A 144     1806   3339   2605     44   -319     49       C  
ATOM   1112  O   SER A 144       6.101  -5.222  14.570  1.00 20.12           O  
ANISOU 1112  O   SER A 144     1756   3308   2582     14   -340     31       O  
ATOM   1113  CB  SER A 144       3.911  -3.314  15.205  1.00 22.28           C  
ANISOU 1113  CB  SER A 144     2037   3587   2842     79   -276    108       C  
ATOM   1114  OG  SER A 144       4.665  -2.270  15.801  1.00 22.20           O  
ANISOU 1114  OG  SER A 144     2081   3557   2799     97   -264     79       O  
ATOM   1115  N   CYS A 145       6.486  -4.979  16.779  1.00 19.68           N  
ANISOU 1115  N   CYS A 145     1747   3235   2497     54   -321     31       N  
ATOM   1116  CA  CYS A 145       7.895  -5.332  16.667  1.00 19.64           C  
ANISOU 1116  CA  CYS A 145     1746   3222   2494     29   -348     -4       C  
ATOM   1117  C   CYS A 145       8.083  -6.712  16.031  1.00 17.86           C  
ANISOU 1117  C   CYS A 145     1485   3004   2296      6   -363     -8       C  
ATOM   1118  O   CYS A 145       7.265  -7.601  16.222  1.00 17.94           O  
ANISOU 1118  O   CYS A 145     1476   3022   2319     10   -360     14       O  
ATOM   1119  CB  CYS A 145       8.598  -5.223  18.010  1.00 21.63           C  
ANISOU 1119  CB  CYS A 145     2035   3458   2724     37   -355    -12       C  
ATOM   1120  SG  CYS A 145       8.487  -3.582  18.738  1.00 26.70           S  
ANISOU 1120  SG  CYS A 145     2746   4078   3322     60   -340    -12       S  
ATOM   1121  N   GLY A 146       9.080  -6.823  15.195  1.00 17.57           N  
ANISOU 1121  N   GLY A 146     1443   2963   2268    -14   -375    -32       N  
ATOM   1122  CA  GLY A 146       9.324  -8.049  14.458  1.00 18.06           C  
ANISOU 1122  CA  GLY A 146     1487   3024   2350    -32   -382    -38       C  
ATOM   1123  C   GLY A 146       8.708  -8.007  13.078  1.00 18.39           C  
ANISOU 1123  C   GLY A 146     1526   3068   2393    -48   -383    -36       C  
ATOM   1124  O   GLY A 146       9.068  -8.835  12.238  1.00 18.29           O  
ANISOU 1124  O   GLY A 146     1517   3045   2387    -65   -387    -47       O  
ATOM   1125  N   SER A 147       7.781  -7.028  12.802  1.00 18.59           N  
ANISOU 1125  N   SER A 147     1550   3103   2410    -44   -378    -20       N  
ATOM   1126  CA  SER A 147       7.233  -6.826  11.444  1.00 18.77           C  
ANISOU 1126  CA  SER A 147     1571   3127   2432    -65   -385    -16       C  
ATOM   1127  C   SER A 147       8.429  -6.460  10.530  1.00 18.62           C  
ANISOU 1127  C   SER A 147     1568   3099   2408    -75   -383    -48       C  
ATOM   1128  O   SER A 147       9.408  -5.874  11.013  1.00 18.44           O  
ANISOU 1128  O   SER A 147     1550   3073   2383    -64   -377    -63       O  
ATOM   1129  CB  SER A 147       6.190  -5.709  11.410  1.00 19.68           C  
ANISOU 1129  CB  SER A 147     1678   3256   2544    -54   -377     12       C  
ATOM   1130  OG  SER A 147       5.089  -5.983  12.264  1.00 21.65           O  
ANISOU 1130  OG  SER A 147     1909   3515   2803    -37   -370     53       O  
ATOM   1131  N   VAL A 148       8.398  -6.890   9.256  1.00 17.94           N  
ANISOU 1131  N   VAL A 148     1494   3004   2318    -98   -390    -55       N  
ATOM   1132  CA  VAL A 148       9.547  -6.709   8.392  1.00 17.98           C  
ANISOU 1132  CA  VAL A 148     1516   2997   2319   -101   -379    -81       C  
ATOM   1133  C   VAL A 148       9.288  -5.823   7.170  1.00 17.42           C  
ANISOU 1133  C   VAL A 148     1457   2927   2235   -114   -380    -83       C  
ATOM   1134  O   VAL A 148       8.150  -5.616   6.764  1.00 16.91           O  
ANISOU 1134  O   VAL A 148     1391   2870   2164   -129   -396    -64       O  
ATOM   1135  CB  VAL A 148      10.123  -8.094   7.976  1.00 18.81           C  
ANISOU 1135  CB  VAL A 148     1642   3080   2426   -107   -373    -92       C  
ATOM   1136  CG1 VAL A 148      10.590  -8.901   9.199  1.00 19.79           C  
ANISOU 1136  CG1 VAL A 148     1750   3203   2566    -91   -369    -89       C  
ATOM   1137  CG2 VAL A 148       9.108  -8.875   7.162  1.00 17.97           C  
ANISOU 1137  CG2 VAL A 148     1561   2961   2305   -135   -392    -83       C  
ATOM   1138  N   GLY A 149      10.373  -5.275   6.650  1.00 17.06           N  
ANISOU 1138  N   GLY A 149     1419   2876   2188   -109   -365   -101       N  
ATOM   1139  CA  GLY A 149      10.439  -4.477   5.440  1.00 17.27           C  
ANISOU 1139  CA  GLY A 149     1459   2900   2201   -118   -361   -108       C  
ATOM   1140  C   GLY A 149      11.128  -5.300   4.372  1.00 17.94           C  
ANISOU 1140  C   GLY A 149     1578   2961   2277   -124   -345   -122       C  
ATOM   1141  O   GLY A 149      12.048  -6.075   4.669  1.00 18.29           O  
ANISOU 1141  O   GLY A 149     1624   2993   2332   -109   -326   -127       O  
ATOM   1142  N   PHE A 150      10.718  -5.120   3.122  1.00 18.12           N  
ANISOU 1142  N   PHE A 150     1632   2975   2278   -143   -349   -124       N  
ATOM   1143  CA  PHE A 150      11.242  -5.957   2.056  1.00 19.26           C  
ANISOU 1143  CA  PHE A 150     1828   3089   2402   -147   -330   -138       C  
ATOM   1144  C   PHE A 150      11.013  -5.376   0.680  1.00 20.62           C  
ANISOU 1144  C   PHE A 150     2037   3251   2546   -164   -332   -142       C  
ATOM   1145  O   PHE A 150      10.129  -4.556   0.502  1.00 20.69           O  
ANISOU 1145  O   PHE A 150     2030   3278   2552   -183   -358   -130       O  
ATOM   1146  CB  PHE A 150      10.519  -7.327   2.130  1.00 18.58           C  
ANISOU 1146  CB  PHE A 150     1774   2982   2303   -166   -350   -134       C  
ATOM   1147  CG  PHE A 150       9.016  -7.247   1.964  1.00 18.59           C  
ANISOU 1147  CG  PHE A 150     1775   2994   2295   -203   -397   -113       C  
ATOM   1148  CD1 PHE A 150       8.194  -7.033   3.051  1.00 19.73           C  
ANISOU 1148  CD1 PHE A 150     1867   3165   2462   -202   -417    -89       C  
ATOM   1149  CD2 PHE A 150       8.426  -7.425   0.722  1.00 19.11           C  
ANISOU 1149  CD2 PHE A 150     1894   3038   2328   -239   -420   -110       C  
ATOM   1150  CE1 PHE A 150       6.812  -6.968   2.897  1.00 20.91           C  
ANISOU 1150  CE1 PHE A 150     2007   3325   2612   -232   -456    -55       C  
ATOM   1151  CE2 PHE A 150       7.052  -7.341   0.567  1.00 19.64           C  
ANISOU 1151  CE2 PHE A 150     1952   3116   2393   -277   -469    -77       C  
ATOM   1152  CZ  PHE A 150       6.251  -7.113   1.654  1.00 20.20           C  
ANISOU 1152  CZ  PHE A 150     1960   3219   2496   -272   -485    -47       C  
ATOM   1153  N   ASN A 151      11.745  -5.892  -0.300  1.00 22.30           N  
ANISOU 1153  N   ASN A 151     2304   3433   2738   -158   -302   -155       N  
ATOM   1154  CA  ASN A 151      11.555  -5.609  -1.721  1.00 24.76           C  
ANISOU 1154  CA  ASN A 151     2672   3725   3012   -176   -301   -161       C  
ATOM   1155  C   ASN A 151      11.450  -6.977  -2.431  1.00 27.37           C  
ANISOU 1155  C   ASN A 151     3089   4007   3303   -190   -297   -171       C  
ATOM   1156  O   ASN A 151      11.925  -7.984  -1.898  1.00 27.20           O  
ANISOU 1156  O   ASN A 151     3077   3968   3290   -171   -276   -175       O  
ATOM   1157  CB  ASN A 151      12.716  -4.794  -2.303  1.00 25.09           C  
ANISOU 1157  CB  ASN A 151     2709   3767   3059   -147   -256   -166       C  
ATOM   1158  CG  ASN A 151      12.683  -3.325  -1.935  1.00 26.99           C  
ANISOU 1158  CG  ASN A 151     2886   4045   3324   -146   -268   -157       C  
ATOM   1159  OD1 ASN A 151      12.146  -2.488  -2.659  1.00 27.51           O  
ANISOU 1159  OD1 ASN A 151     2960   4119   3374   -165   -285   -155       O  
ATOM   1160  ND2 ASN A 151      13.271  -2.972  -0.812  1.00 26.97           N  
ANISOU 1160  ND2 ASN A 151     2825   4063   3358   -125   -263   -151       N  
ATOM   1161  N   ILE A 152      10.812  -7.030  -3.615  1.00 29.64           N  
ANISOU 1161  N   ILE A 152     3447   4269   3544   -225   -320   -173       N  
ATOM   1162  CA  ILE A 152      10.732  -8.288  -4.369  1.00 32.01           C  
ANISOU 1162  CA  ILE A 152     3852   4514   3796   -242   -319   -184       C  
ATOM   1163  C   ILE A 152      11.223  -8.122  -5.787  1.00 34.65           C  
ANISOU 1163  C   ILE A 152     4275   4810   4081   -239   -287   -197       C  
ATOM   1164  O   ILE A 152      10.767  -7.217  -6.473  1.00 34.82           O  
ANISOU 1164  O   ILE A 152     4296   4845   4088   -263   -311   -192       O  
ATOM   1165  CB  ILE A 152       9.323  -8.920  -4.384  1.00 32.50           C  
ANISOU 1165  CB  ILE A 152     3943   4566   3838   -303   -394   -168       C  
ATOM   1166  CG1 ILE A 152       8.698  -9.007  -2.984  1.00 33.08           C  
ANISOU 1166  CG1 ILE A 152     3926   4682   3963   -305   -424   -146       C  
ATOM   1167  CG2 ILE A 152       9.357 -10.302  -5.076  1.00 33.01           C  
ANISOU 1167  CG2 ILE A 152     4130   4564   3849   -321   -394   -181       C  
ATOM   1168  CD1 ILE A 152       7.251  -9.472  -3.027  1.00 33.80           C  
ANISOU 1168  CD1 ILE A 152     4029   4771   4044   -366   -499   -116       C  
ATOM   1169  N   ASP A 153      12.129  -9.005  -6.245  1.00 36.33           N  
ANISOU 1169  N   ASP A 153     4566   4972   4265   -206   -229   -212       N  
ATOM   1170  CA  ASP A 153      12.572  -9.042  -7.639  1.00 37.71           C  
ANISOU 1170  CA  ASP A 153     4849   5098   4382   -198   -189   -224       C  
ATOM   1171  C   ASP A 153      12.065 -10.378  -8.179  1.00 38.47           C  
ANISOU 1171  C   ASP A 153     5076   5127   4415   -230   -210   -235       C  
ATOM   1172  O   ASP A 153      12.666 -11.414  -7.901  1.00 38.57           O  
ANISOU 1172  O   ASP A 153     5130   5103   4422   -196   -164   -243       O  
ATOM   1173  CB  ASP A 153      14.101  -8.952  -7.772  1.00 40.57           C  
ANISOU 1173  CB  ASP A 153     5203   5449   4762   -125    -92   -223       C  
ATOM   1174  CG  ASP A 153      14.581  -8.676  -9.204  1.00 47.90           C  
ANISOU 1174  CG  ASP A 153     6227   6337   5636   -109    -43   -229       C  
ATOM   1175  OD1 ASP A 153      13.725  -8.343 -10.074  1.00 48.42           O  
ANISOU 1175  OD1 ASP A 153     6356   6389   5651   -160    -93   -237       O  
ATOM   1176  OD2 ASP A 153      15.817  -8.774  -9.454  1.00 50.69           O  
ANISOU 1176  OD2 ASP A 153     6590   6672   5999    -45     45   -220       O  
ATOM   1177  N   TYR A 154      10.933 -10.342  -8.905  1.00 38.55           N  
ANISOU 1177  N   TYR A 154     5150   5121   4377   -299   -284   -232       N  
ATOM   1178  CA  TYR A 154      10.188 -11.470  -9.463  1.00 39.44           C  
ANISOU 1178  CA  TYR A 154     5390   5170   4425   -354   -333   -236       C  
ATOM   1179  C   TYR A 154       9.777 -12.475  -8.373  1.00 38.36           C  
ANISOU 1179  C   TYR A 154     5222   5036   4317   -366   -365   -229       C  
ATOM   1180  O   TYR A 154       8.669 -12.360  -7.850  1.00 38.69           O  
ANISOU 1180  O   TYR A 154     5202   5113   4385   -418   -444   -204       O  
ATOM   1181  CB  TYR A 154      10.873 -12.143 -10.678  1.00 40.77           C  
ANISOU 1181  CB  TYR A 154     5727   5253   4511   -333   -275   -260       C  
ATOM   1182  CG  TYR A 154      10.164 -13.401 -11.153  1.00 43.42           C  
ANISOU 1182  CG  TYR A 154     6210   5514   4773   -391   -328   -266       C  
ATOM   1183  CD1 TYR A 154       8.805 -13.391 -11.446  1.00 45.20           C  
ANISOU 1183  CD1 TYR A 154     6461   5740   4975   -485   -442   -245       C  
ATOM   1184  CD2 TYR A 154      10.849 -14.604 -11.286  1.00 45.22           C  
ANISOU 1184  CD2 TYR A 154     6552   5670   4961   -354   -266   -285       C  
ATOM   1185  CE1 TYR A 154       8.144 -14.546 -11.858  1.00 46.71           C  
ANISOU 1185  CE1 TYR A 154     6788   5859   5100   -547   -502   -245       C  
ATOM   1186  CE2 TYR A 154      10.196 -15.769 -11.681  1.00 46.67           C  
ANISOU 1186  CE2 TYR A 154     6879   5779   5075   -410   -320   -291       C  
ATOM   1187  CZ  TYR A 154       8.846 -15.732 -11.985  1.00 48.07           C  
ANISOU 1187  CZ  TYR A 154     7083   5956   5226   -511   -442   -271       C  
ATOM   1188  OH  TYR A 154       8.202 -16.872 -12.410  1.00 50.58           O  
ANISOU 1188  OH  TYR A 154     7550   6195   5472   -576   -505   -272       O  
ATOM   1189  N   ASP A 155      10.638 -13.451  -8.035  1.00 37.12           N  
ANISOU 1189  N   ASP A 155     5104   4842   4158   -316   -300   -244       N  
ATOM   1190  CA  ASP A 155      10.315 -14.475  -7.041  1.00 36.13           C  
ANISOU 1190  CA  ASP A 155     4957   4713   4057   -326   -325   -238       C  
ATOM   1191  C   ASP A 155      11.182 -14.448  -5.790  1.00 34.21           C  
ANISOU 1191  C   ASP A 155     4596   4514   3887   -260   -268   -235       C  
ATOM   1192  O   ASP A 155      11.007 -15.302  -4.915  1.00 34.78           O  
ANISOU 1192  O   ASP A 155     4647   4585   3982   -262   -282   -230       O  
ATOM   1193  CB  ASP A 155      10.352 -15.881  -7.671  1.00 38.27           C  
ANISOU 1193  CB  ASP A 155     5392   4893   4256   -339   -317   -254       C  
ATOM   1194  CG  ASP A 155      11.677 -16.284  -8.304  1.00 43.47           C  
ANISOU 1194  CG  ASP A 155     6146   5494   4878   -266   -206   -276       C  
ATOM   1195  OD1 ASP A 155      12.574 -15.414  -8.423  1.00 43.98           O  
ANISOU 1195  OD1 ASP A 155     6150   5589   4972   -209   -138   -275       O  
ATOM   1196  OD2 ASP A 155      11.804 -17.462  -8.714  1.00 45.95           O  
ANISOU 1196  OD2 ASP A 155     6598   5728   5134   -265   -185   -290       O  
ATOM   1197  N   CYS A 156      12.134 -13.513  -5.715  1.00 31.90           N  
ANISOU 1197  N   CYS A 156     4234   4257   3631   -206   -207   -235       N  
ATOM   1198  CA  CYS A 156      13.043 -13.416  -4.591  1.00 30.26           C  
ANISOU 1198  CA  CYS A 156     3919   4088   3490   -149   -158   -226       C  
ATOM   1199  C   CYS A 156      12.713 -12.226  -3.691  1.00 28.53           C  
ANISOU 1199  C   CYS A 156     3562   3946   3331   -158   -197   -212       C  
ATOM   1200  O   CYS A 156      12.624 -11.092  -4.163  1.00 28.19           O  
ANISOU 1200  O   CYS A 156     3493   3930   3288   -166   -205   -210       O  
ATOM   1201  CB  CYS A 156      14.485 -13.367  -5.079  1.00 31.02           C  
ANISOU 1201  CB  CYS A 156     4039   4160   3588    -79    -59   -226       C  
ATOM   1202  SG  CYS A 156      15.704 -13.257  -3.750  1.00 36.78           S  
ANISOU 1202  SG  CYS A 156     4637   4935   4405    -16     -5   -201       S  
ATOM   1203  N   VAL A 157      12.503 -12.500  -2.400  1.00 26.70           N  
ANISOU 1203  N   VAL A 157     3252   3748   3146   -157   -219   -201       N  
ATOM   1204  CA  VAL A 157      12.195 -11.478  -1.409  1.00 25.12           C  
ANISOU 1204  CA  VAL A 157     2935   3613   2997   -160   -250   -187       C  
ATOM   1205  C   VAL A 157      13.492 -11.043  -0.748  1.00 23.90           C  
ANISOU 1205  C   VAL A 157     2710   3482   2888   -106   -195   -181       C  
ATOM   1206  O   VAL A 157      14.151 -11.858  -0.112  1.00 24.62           O  
ANISOU 1206  O   VAL A 157     2791   3563   3001    -77   -165   -176       O  
ATOM   1207  CB  VAL A 157      11.190 -11.984  -0.342  1.00 25.24           C  
ANISOU 1207  CB  VAL A 157     2909   3649   3033   -189   -305   -175       C  
ATOM   1208  CG1 VAL A 157      10.879 -10.891   0.686  1.00 25.75           C  
ANISOU 1208  CG1 VAL A 157     2867   3774   3142   -185   -327   -160       C  
ATOM   1209  CG2 VAL A 157       9.904 -12.483  -0.988  1.00 25.87           C  
ANISOU 1209  CG2 VAL A 157     3053   3703   3072   -248   -366   -168       C  
ATOM   1210  N   SER A 158      13.849  -9.769  -0.873  1.00 22.12           N  
ANISOU 1210  N   SER A 158     2434   3288   2681    -97   -188   -176       N  
ATOM   1211  CA  SER A 158      15.028  -9.228  -0.216  1.00 21.10           C  
ANISOU 1211  CA  SER A 158     2233   3184   2599    -57   -152   -161       C  
ATOM   1212  C   SER A 158      14.548  -8.555   1.051  1.00 19.75           C  
ANISOU 1212  C   SER A 158     1981   3060   2463    -71   -197   -153       C  
ATOM   1213  O   SER A 158      13.951  -7.477   0.986  1.00 18.92           O  
ANISOU 1213  O   SER A 158     1852   2981   2355    -91   -228   -154       O  
ATOM   1214  CB  SER A 158      15.728  -8.200  -1.105  1.00 23.13           C  
ANISOU 1214  CB  SER A 158     2489   3444   2854    -41   -119   -157       C  
ATOM   1215  OG  SER A 158      16.433  -8.846  -2.154  1.00 26.44           O  
ANISOU 1215  OG  SER A 158     2983   3818   3246    -13    -59   -157       O  
ATOM   1216  N   PHE A 159      14.775  -9.188   2.207  1.00 18.81           N  
ANISOU 1216  N   PHE A 159     1826   2949   2372    -59   -200   -145       N  
ATOM   1217  CA  PHE A 159      14.361  -8.604   3.481  1.00 17.77           C  
ANISOU 1217  CA  PHE A 159     1629   2855   2266    -69   -238   -137       C  
ATOM   1218  C   PHE A 159      15.366  -7.563   3.877  1.00 17.49           C  
ANISOU 1218  C   PHE A 159     1542   2841   2261    -51   -227   -123       C  
ATOM   1219  O   PHE A 159      16.558  -7.854   3.903  1.00 17.72           O  
ANISOU 1219  O   PHE A 159     1556   2861   2314    -26   -192   -107       O  
ATOM   1220  CB  PHE A 159      14.255  -9.676   4.573  1.00 17.10           C  
ANISOU 1220  CB  PHE A 159     1531   2768   2197    -64   -247   -131       C  
ATOM   1221  CG  PHE A 159      13.089 -10.605   4.331  1.00 17.56           C  
ANISOU 1221  CG  PHE A 159     1634   2809   2229    -90   -272   -139       C  
ATOM   1222  CD1 PHE A 159      11.800 -10.224   4.665  1.00 18.11           C  
ANISOU 1222  CD1 PHE A 159     1688   2900   2293   -118   -317   -133       C  
ATOM   1223  CD2 PHE A 159      13.282 -11.847   3.752  1.00 18.21           C  
ANISOU 1223  CD2 PHE A 159     1777   2850   2292    -86   -250   -146       C  
ATOM   1224  CE1 PHE A 159      10.729 -11.072   4.429  1.00 18.40           C  
ANISOU 1224  CE1 PHE A 159     1760   2922   2311   -147   -348   -129       C  
ATOM   1225  CE2 PHE A 159      12.210 -12.691   3.516  1.00 18.65           C  
ANISOU 1225  CE2 PHE A 159     1880   2886   2322   -118   -284   -149       C  
ATOM   1226  CZ  PHE A 159      10.945 -12.304   3.875  1.00 18.39           C  
ANISOU 1226  CZ  PHE A 159     1820   2878   2288   -152   -336   -138       C  
ATOM   1227  N   CYS A 160      14.903  -6.353   4.175  1.00 17.27           N  
ANISOU 1227  N   CYS A 160     1488   2840   2234    -66   -257   -124       N  
ATOM   1228  CA  CYS A 160      15.822  -5.277   4.523  1.00 17.70           C  
ANISOU 1228  CA  CYS A 160     1502   2910   2313    -58   -255   -110       C  
ATOM   1229  C   CYS A 160      15.610  -4.681   5.885  1.00 17.62           C  
ANISOU 1229  C   CYS A 160     1460   2921   2316    -65   -290   -104       C  
ATOM   1230  O   CYS A 160      16.529  -4.045   6.381  1.00 19.09           O  
ANISOU 1230  O   CYS A 160     1617   3113   2523    -63   -296    -87       O  
ATOM   1231  CB  CYS A 160      15.801  -4.191   3.451  1.00 18.43           C  
ANISOU 1231  CB  CYS A 160     1605   3005   2391    -64   -249   -114       C  
ATOM   1232  SG  CYS A 160      14.178  -3.443   3.193  1.00 22.76           S  
ANISOU 1232  SG  CYS A 160     2171   3567   2909    -90   -285   -129       S  
ATOM   1233  N   TYR A 161      14.423  -4.799   6.457  1.00 16.73           N  
ANISOU 1233  N   TYR A 161     1354   2815   2187    -75   -314   -112       N  
ATOM   1234  CA  TYR A 161      14.132  -4.140   7.722  1.00 17.36           C  
ANISOU 1234  CA  TYR A 161     1418   2910   2270    -76   -339   -106       C  
ATOM   1235  C   TYR A 161      13.396  -5.047   8.681  1.00 17.75           C  
ANISOU 1235  C   TYR A 161     1467   2960   2317    -74   -349   -104       C  
ATOM   1236  O   TYR A 161      12.602  -5.888   8.254  1.00 18.20           O  
ANISOU 1236  O   TYR A 161     1538   3013   2366    -79   -347   -107       O  
ATOM   1237  CB  TYR A 161      13.290  -2.869   7.422  1.00 16.71           C  
ANISOU 1237  CB  TYR A 161     1344   2836   2167    -84   -350   -110       C  
ATOM   1238  CG  TYR A 161      12.897  -2.051   8.632  1.00 17.56           C  
ANISOU 1238  CG  TYR A 161     1453   2951   2268    -79   -367   -104       C  
ATOM   1239  CD1 TYR A 161      13.795  -1.167   9.221  1.00 18.29           C  
ANISOU 1239  CD1 TYR A 161     1546   3039   2364    -82   -380   -100       C  
ATOM   1240  CD2 TYR A 161      11.615  -2.120   9.154  1.00 17.88           C  
ANISOU 1240  CD2 TYR A 161     1501   2997   2296    -73   -370    -98       C  
ATOM   1241  CE1 TYR A 161      13.422  -0.376  10.304  1.00 18.68           C  
ANISOU 1241  CE1 TYR A 161     1617   3085   2396    -78   -395    -97       C  
ATOM   1242  CE2 TYR A 161      11.243  -1.362  10.257  1.00 18.85           C  
ANISOU 1242  CE2 TYR A 161     1636   3119   2406    -62   -375    -91       C  
ATOM   1243  CZ  TYR A 161      12.155  -0.505  10.845  1.00 19.47           C  
ANISOU 1243  CZ  TYR A 161     1729   3187   2479    -64   -387    -94       C  
ATOM   1244  OH  TYR A 161      11.770   0.252  11.931  1.00 20.56           O  
ANISOU 1244  OH  TYR A 161     1901   3317   2595    -52   -391    -90       O  
ATOM   1245  N   MET A 162      13.619  -4.851   9.975  1.00 16.89           N  
ANISOU 1245  N   MET A 162     1349   2856   2214    -69   -364    -96       N  
ATOM   1246  CA  MET A 162      12.850  -5.529  11.020  1.00 16.52           C  
ANISOU 1246  CA  MET A 162     1303   2812   2163    -64   -373    -90       C  
ATOM   1247  C   MET A 162      12.564  -4.445  12.045  1.00 16.99           C  
ANISOU 1247  C   MET A 162     1374   2875   2207    -59   -386    -86       C  
ATOM   1248  O   MET A 162      13.493  -3.746  12.471  1.00 17.24           O  
ANISOU 1248  O   MET A 162     1410   2902   2240    -64   -400    -84       O  
ATOM   1249  CB  MET A 162      13.549  -6.740  11.663  1.00 16.24           C  
ANISOU 1249  CB  MET A 162     1254   2769   2146    -59   -372    -84       C  
ATOM   1250  CG  MET A 162      12.732  -7.303  12.824  1.00 18.77           C  
ANISOU 1250  CG  MET A 162     1576   3094   2461    -53   -381    -77       C  
ATOM   1251  SD  MET A 162      13.231  -8.937  13.432  1.00 21.60           S  
ANISOU 1251  SD  MET A 162     1920   3445   2840    -48   -379    -69       S  
ATOM   1252  CE  MET A 162      12.375  -9.963  12.291  1.00 19.24           C  
ANISOU 1252  CE  MET A 162     1635   3138   2538    -54   -366    -76       C  
ATOM   1253  N   HIS A 163      11.282  -4.235  12.359  1.00 15.92           N  
ANISOU 1253  N   HIS A 163     1248   2746   2056    -50   -382    -79       N  
ATOM   1254  CA  HIS A 163      10.911  -3.186  13.285  1.00 16.28           C  
ANISOU 1254  CA  HIS A 163     1318   2787   2079    -37   -383    -73       C  
ATOM   1255  C   HIS A 163      11.295  -3.501  14.735  1.00 16.59           C  
ANISOU 1255  C   HIS A 163     1374   2818   2112    -30   -394    -68       C  
ATOM   1256  O   HIS A 163      11.000  -4.599  15.210  1.00 16.58           O  
ANISOU 1256  O   HIS A 163     1360   2821   2121    -25   -392    -61       O  
ATOM   1257  CB  HIS A 163       9.411  -2.923  13.188  1.00 16.99           C  
ANISOU 1257  CB  HIS A 163     1409   2886   2161    -21   -366    -56       C  
ATOM   1258  CG  HIS A 163       9.031  -1.744  14.002  1.00 18.81           C  
ANISOU 1258  CG  HIS A 163     1675   3106   2365      0   -355    -48       C  
ATOM   1259  ND1 HIS A 163       9.636  -0.526  13.808  1.00 19.88           N  
ANISOU 1259  ND1 HIS A 163     1837   3231   2486     -6   -361    -61       N  
ATOM   1260  CD2 HIS A 163       8.187  -1.654  15.053  1.00 19.60           C  
ANISOU 1260  CD2 HIS A 163     1795   3202   2450     28   -336    -28       C  
ATOM   1261  CE1 HIS A 163       9.097   0.282  14.702  1.00 20.36           C  
ANISOU 1261  CE1 HIS A 163     1941   3277   2519     19   -345    -51       C  
ATOM   1262  NE2 HIS A 163       8.228  -0.358  15.477  1.00 20.13           N  
ANISOU 1262  NE2 HIS A 163     1910   3251   2488     43   -326    -30       N  
ATOM   1263  N   HIS A 164      11.928  -2.532  15.441  1.00 16.30           N  
ANISOU 1263  N   HIS A 164     1372   2767   2056    -34   -410    -71       N  
ATOM   1264  CA  HIS A 164      12.298  -2.711  16.846  1.00 16.68           C  
ANISOU 1264  CA  HIS A 164     1448   2800   2088    -33   -427    -65       C  
ATOM   1265  C   HIS A 164      11.776  -1.626  17.775  1.00 18.49           C  
ANISOU 1265  C   HIS A 164     1744   3009   2274    -17   -423    -63       C  
ATOM   1266  O   HIS A 164      11.422  -1.919  18.920  1.00 19.49           O  
ANISOU 1266  O   HIS A 164     1902   3124   2378     -2   -419    -55       O  
ATOM   1267  CB  HIS A 164      13.840  -2.739  17.029  1.00 15.28           C  
ANISOU 1267  CB  HIS A 164     1264   2616   1926    -63   -464    -62       C  
ATOM   1268  CG  HIS A 164      14.518  -3.968  16.504  1.00 16.12           C  
ANISOU 1268  CG  HIS A 164     1316   2736   2075    -70   -463    -56       C  
ATOM   1269  ND1 HIS A 164      15.259  -4.791  17.329  1.00 17.10           N  
ANISOU 1269  ND1 HIS A 164     1427   2857   2214    -78   -482    -41       N  
ATOM   1270  CD2 HIS A 164      14.623  -4.415  15.233  1.00 16.87           C  
ANISOU 1270  CD2 HIS A 164     1374   2841   2195    -69   -442    -60       C  
ATOM   1271  CE1 HIS A 164      15.741  -5.740  16.547  1.00 18.34           C  
ANISOU 1271  CE1 HIS A 164     1538   3023   2407    -77   -467    -36       C  
ATOM   1272  NE2 HIS A 164      15.374  -5.567  15.279  1.00 18.42           N  
ANISOU 1272  NE2 HIS A 164     1538   3039   2421    -71   -442    -49       N  
ATOM   1273  N   MET A 165      11.851  -0.361  17.343  1.00 18.54           N  
ANISOU 1273  N   MET A 165     1778   3003   2262    -21   -424    -69       N  
ATOM   1274  CA  MET A 165      11.620   0.750  18.237  1.00 19.88           C  
ANISOU 1274  CA  MET A 165     2027   3142   2383     -9   -422    -69       C  
ATOM   1275  C   MET A 165      10.770   1.890  17.719  1.00 19.98           C  
ANISOU 1275  C   MET A 165     2065   3148   2378     14   -390    -69       C  
ATOM   1276  O   MET A 165      10.819   2.225  16.542  1.00 20.02           O  
ANISOU 1276  O   MET A 165     2032   3168   2404      4   -388    -73       O  
ATOM   1277  CB  MET A 165      12.981   1.369  18.595  1.00 21.60           C  
ANISOU 1277  CB  MET A 165     2280   3338   2591    -49   -475    -73       C  
ATOM   1278  CG  MET A 165      13.804   0.589  19.570  1.00 28.05           C  
ANISOU 1278  CG  MET A 165     3101   4148   3410    -71   -512    -65       C  
ATOM   1279  SD  MET A 165      14.729   1.746  20.599  1.00 39.15           S  
ANISOU 1279  SD  MET A 165     4604   5506   4766   -109   -571    -60       S  
ATOM   1280  CE  MET A 165      15.490   2.820  19.293  1.00 36.74           C  
ANISOU 1280  CE  MET A 165     4269   5205   4486   -139   -592    -61       C  
ATOM   1281  N   GLU A 166      10.136   2.584  18.657  1.00 19.94           N  
ANISOU 1281  N   GLU A 166     2135   3114   2327     44   -366    -62       N  
ATOM   1282  CA  GLU A 166       9.398   3.800  18.408  1.00 20.36           C  
ANISOU 1282  CA  GLU A 166     2230   3150   2354     71   -331    -57       C  
ATOM   1283  C   GLU A 166      10.138   4.845  19.247  1.00 21.41           C  
ANISOU 1283  C   GLU A 166     2466   3235   2435     56   -359    -70       C  
ATOM   1284  O   GLU A 166      10.221   4.701  20.471  1.00 21.02           O  
ANISOU 1284  O   GLU A 166     2484   3156   2347     63   -365    -69       O  
ATOM   1285  CB  GLU A 166       7.967   3.626  18.910  1.00 22.35           C  
ANISOU 1285  CB  GLU A 166     2492   3403   2597    127   -270    -29       C  
ATOM   1286  CG  GLU A 166       7.192   4.898  19.165  1.00 28.33           C  
ANISOU 1286  CG  GLU A 166     3321   4129   3315    171   -222    -15       C  
ATOM   1287  CD  GLU A 166       5.933   4.617  19.962  1.00 32.92           C  
ANISOU 1287  CD  GLU A 166     3918   4705   3884    231   -157     23       C  
ATOM   1288  OE1 GLU A 166       6.042   4.320  21.178  1.00 32.40           O  
ANISOU 1288  OE1 GLU A 166     3915   4612   3781    245   -153     23       O  
ATOM   1289  OE2 GLU A 166       4.834   4.694  19.366  1.00 34.09           O  
ANISOU 1289  OE2 GLU A 166     4015   4875   4061    264   -112     60       O  
ATOM   1290  N   LEU A 167      10.703   5.864  18.598  1.00 22.19           N  
ANISOU 1290  N   LEU A 167     2581   3322   2530     32   -382    -81       N  
ATOM   1291  CA  LEU A 167      11.374   6.945  19.301  1.00 23.64           C  
ANISOU 1291  CA  LEU A 167     2868   3454   2660     10   -415    -91       C  
ATOM   1292  C   LEU A 167      10.322   7.843  19.951  1.00 25.11           C  
ANISOU 1292  C   LEU A 167     3153   3599   2789     64   -359    -85       C  
ATOM   1293  O   LEU A 167       9.169   7.867  19.500  1.00 25.69           O  
ANISOU 1293  O   LEU A 167     3192   3690   2877    112   -295    -68       O  
ATOM   1294  CB  LEU A 167      12.264   7.751  18.331  1.00 23.94           C  
ANISOU 1294  CB  LEU A 167     2886   3493   2716    -32   -456    -99       C  
ATOM   1295  CG  LEU A 167      13.355   6.979  17.568  1.00 26.15           C  
ANISOU 1295  CG  LEU A 167     3068   3812   3055    -77   -501    -97       C  
ATOM   1296  CD1 LEU A 167      14.285   7.941  16.830  1.00 26.80           C  
ANISOU 1296  CD1 LEU A 167     3148   3887   3149   -118   -541    -97       C  
ATOM   1297  CD2 LEU A 167      14.165   6.060  18.495  1.00 26.58           C  
ANISOU 1297  CD2 LEU A 167     3121   3864   3115   -106   -545    -89       C  
ATOM   1298  N   PRO A 168      10.683   8.607  20.999  1.00 26.07           N  
ANISOU 1298  N   PRO A 168     3402   3660   2844     56   -378    -92       N  
ATOM   1299  CA  PRO A 168       9.690   9.487  21.641  1.00 27.02           C  
ANISOU 1299  CA  PRO A 168     3632   3732   2903    115   -313    -85       C  
ATOM   1300  C   PRO A 168       9.015  10.495  20.707  1.00 28.31           C  
ANISOU 1300  C   PRO A 168     3786   3896   3074    147   -266    -78       C  
ATOM   1301  O   PRO A 168       7.998  11.065  21.080  1.00 29.34           O  
ANISOU 1301  O   PRO A 168     3981   3997   3170    210   -193    -61       O  
ATOM   1302  CB  PRO A 168      10.488  10.177  22.762  1.00 27.88           C  
ANISOU 1302  CB  PRO A 168     3890   3770   2935     82   -363    -99       C  
ATOM   1303  CG  PRO A 168      11.669   9.312  22.986  1.00 27.58           C  
ANISOU 1303  CG  PRO A 168     3804   3751   2923     16   -447   -104       C  
ATOM   1304  CD  PRO A 168      11.993   8.681  21.671  1.00 25.89           C  
ANISOU 1304  CD  PRO A 168     3434   3607   2796     -7   -461   -101       C  
ATOM   1305  N   THR A 169       9.548  10.709  19.491  1.00 28.17           N  
ANISOU 1305  N   THR A 169     3689   3912   3104    108   -301    -87       N  
ATOM   1306  CA  THR A 169       8.941  11.598  18.495  1.00 28.42           C  
ANISOU 1306  CA  THR A 169     3699   3950   3149    132   -261    -79       C  
ATOM   1307  C   THR A 169       7.987  10.871  17.508  1.00 28.56           C  
ANISOU 1307  C   THR A 169     3590   4030   3231    162   -216    -55       C  
ATOM   1308  O   THR A 169       7.634  11.440  16.473  1.00 29.07           O  
ANISOU 1308  O   THR A 169     3614   4113   3320    169   -198    -47       O  
ATOM   1309  CB  THR A 169      10.017  12.308  17.677  1.00 29.63           C  
ANISOU 1309  CB  THR A 169     3842   4102   3315     74   -323    -97       C  
ATOM   1310  OG1 THR A 169      10.701  11.350  16.859  1.00 30.18           O  
ANISOU 1310  OG1 THR A 169     3791   4227   3448     32   -365   -101       O  
ATOM   1311  CG2 THR A 169      10.984  13.096  18.550  1.00 29.79           C  
ANISOU 1311  CG2 THR A 169     3984   4059   3275     32   -381   -112       C  
ATOM   1312  N   GLY A 170       7.648   9.617  17.790  1.00 27.44           N  
ANISOU 1312  N   GLY A 170     3388   3921   3116    171   -208    -44       N  
ATOM   1313  CA  GLY A 170       6.738   8.853  16.947  1.00 27.40           C  
ANISOU 1313  CA  GLY A 170     3273   3969   3167    190   -176    -17       C  
ATOM   1314  C   GLY A 170       7.306   8.325  15.640  1.00 26.29           C  
ANISOU 1314  C   GLY A 170     3034   3875   3081    142   -220    -30       C  
ATOM   1315  O   GLY A 170       6.550   7.850  14.796  1.00 27.05           O  
ANISOU 1315  O   GLY A 170     3051   4009   3217    151   -201     -8       O  
ATOM   1316  N   VAL A 171       8.622   8.463  15.426  1.00 24.67           N  
ANISOU 1316  N   VAL A 171     2835   3664   2875     91   -278    -60       N  
ATOM   1317  CA  VAL A 171       9.279   7.907  14.252  1.00 23.34           C  
ANISOU 1317  CA  VAL A 171     2580   3533   2753     50   -313    -71       C  
ATOM   1318  C   VAL A 171       9.830   6.530  14.641  1.00 20.80           C  
ANISOU 1318  C   VAL A 171     2220   3229   2452     30   -340    -76       C  
ATOM   1319  O   VAL A 171       9.894   6.180  15.840  1.00 20.43           O  
ANISOU 1319  O   VAL A 171     2218   3163   2381     38   -343    -75       O  
ATOM   1320  CB  VAL A 171      10.327   8.828  13.572  1.00 25.10           C  
ANISOU 1320  CB  VAL A 171     2813   3746   2977     12   -350    -88       C  
ATOM   1321  CG1 VAL A 171       9.704  10.162  13.170  1.00 26.19           C  
ANISOU 1321  CG1 VAL A 171     2989   3867   3096     35   -320    -81       C  
ATOM   1322  CG2 VAL A 171      11.541   9.025  14.465  1.00 25.56           C  
ANISOU 1322  CG2 VAL A 171     2928   3772   3010    -23   -402   -100       C  
ATOM   1323  N   HIS A 172      10.170   5.729  13.642  1.00 19.30           N  
ANISOU 1323  N   HIS A 172     1955   3074   2306      7   -354    -80       N  
ATOM   1324  CA  HIS A 172      10.516   4.345  13.895  1.00 18.55           C  
ANISOU 1324  CA  HIS A 172     1819   2996   2234     -5   -369    -81       C  
ATOM   1325  C   HIS A 172      11.985   3.991  13.581  1.00 17.63           C  
ANISOU 1325  C   HIS A 172     1677   2884   2140    -45   -410    -92       C  
ATOM   1326  O   HIS A 172      12.607   4.530  12.671  1.00 16.54           O  
ANISOU 1326  O   HIS A 172     1520   2749   2014    -64   -422    -97       O  
ATOM   1327  CB  HIS A 172       9.496   3.462  13.160  1.00 18.73           C  
ANISOU 1327  CB  HIS A 172     1784   3050   2284      9   -343    -67       C  
ATOM   1328  CG  HIS A 172       8.082   3.816  13.546  1.00 19.32           C  
ANISOU 1328  CG  HIS A 172     1874   3122   2345     49   -301    -40       C  
ATOM   1329  ND1 HIS A 172       7.194   4.366  12.630  1.00 21.11           N  
ANISOU 1329  ND1 HIS A 172     2077   3362   2582     61   -279    -21       N  
ATOM   1330  CD2 HIS A 172       7.481   3.789  14.765  1.00 20.19           C  
ANISOU 1330  CD2 HIS A 172     2024   3216   2432     83   -276    -24       C  
ATOM   1331  CE1 HIS A 172       6.067   4.594  13.294  1.00 21.37           C  
ANISOU 1331  CE1 HIS A 172     2127   3389   2605    102   -239     12       C  
ATOM   1332  NE2 HIS A 172       6.186   4.266  14.585  1.00 20.96           N  
ANISOU 1332  NE2 HIS A 172     2116   3318   2531    120   -232     10       N  
ATOM   1333  N   ALA A 173      12.522   3.092  14.382  1.00 17.06           N  
ANISOU 1333  N   ALA A 173     1600   2809   2073    -53   -430    -90       N  
ATOM   1334  CA  ALA A 173      13.882   2.604  14.231  1.00 17.14           C  
ANISOU 1334  CA  ALA A 173     1578   2824   2111    -85   -464    -87       C  
ATOM   1335  C   ALA A 173      13.895   1.087  14.257  1.00 16.55           C  
ANISOU 1335  C   ALA A 173     1456   2768   2065    -80   -455    -84       C  
ATOM   1336  O   ALA A 173      13.069   0.433  14.918  1.00 16.32           O  
ANISOU 1336  O   ALA A 173     1435   2741   2026    -60   -439    -82       O  
ATOM   1337  CB  ALA A 173      14.803   3.171  15.310  1.00 17.26           C  
ANISOU 1337  CB  ALA A 173     1642   2811   2106   -111   -509    -80       C  
ATOM   1338  N   GLY A 174      14.800   0.534  13.472  1.00 16.27           N  
ANISOU 1338  N   GLY A 174     1373   2745   2065    -96   -461    -79       N  
ATOM   1339  CA  GLY A 174      14.900  -0.899  13.338  1.00 15.97           C  
ANISOU 1339  CA  GLY A 174     1296   2719   2053    -90   -448    -76       C  
ATOM   1340  C   GLY A 174      16.220  -1.343  12.784  1.00 16.82           C  
ANISOU 1340  C   GLY A 174     1363   2830   2198   -104   -454    -61       C  
ATOM   1341  O   GLY A 174      17.128  -0.535  12.568  1.00 17.13           O  
ANISOU 1341  O   GLY A 174     1397   2865   2247   -121   -473    -48       O  
ATOM   1342  N   THR A 175      16.305  -2.626  12.514  1.00 16.45           N  
ANISOU 1342  N   THR A 175     1288   2791   2173    -94   -435    -59       N  
ATOM   1343  CA  THR A 175      17.540  -3.247  12.072  1.00 16.57           C  
ANISOU 1343  CA  THR A 175     1264   2805   2226    -96   -428    -37       C  
ATOM   1344  C   THR A 175      17.411  -3.895  10.678  1.00 16.70           C  
ANISOU 1344  C   THR A 175     1270   2824   2252    -81   -386    -46       C  
ATOM   1345  O   THR A 175      16.309  -4.061  10.168  1.00 16.67           O  
ANISOU 1345  O   THR A 175     1286   2821   2225    -74   -372    -69       O  
ATOM   1346  CB  THR A 175      17.900  -4.366  13.100  1.00 16.92           C  
ANISOU 1346  CB  THR A 175     1294   2848   2286    -94   -437    -21       C  
ATOM   1347  OG1 THR A 175      16.991  -5.471  12.975  1.00 17.58           O  
ANISOU 1347  OG1 THR A 175     1382   2933   2362    -76   -412    -39       O  
ATOM   1348  CG2 THR A 175      17.988  -3.872  14.535  1.00 17.12           C  
ANISOU 1348  CG2 THR A 175     1344   2867   2295   -111   -481    -12       C  
ATOM   1349  N   ASP A 176      18.538  -4.327  10.101  1.00 16.69           N  
ANISOU 1349  N   ASP A 176     1240   2820   2284    -74   -365    -23       N  
ATOM   1350  CA  ASP A 176      18.508  -5.186   8.928  1.00 17.68           C  
ANISOU 1350  CA  ASP A 176     1369   2936   2412    -54   -319    -30       C  
ATOM   1351  C   ASP A 176      18.308  -6.643   9.497  1.00 18.17           C  
ANISOU 1351  C   ASP A 176     1432   2991   2479    -42   -309    -31       C  
ATOM   1352  O   ASP A 176      18.248  -6.825  10.732  1.00 17.74           O  
ANISOU 1352  O   ASP A 176     1368   2942   2429    -50   -338    -23       O  
ATOM   1353  CB  ASP A 176      19.783  -5.025   8.085  1.00 18.08           C  
ANISOU 1353  CB  ASP A 176     1394   2982   2494    -43   -290      1       C  
ATOM   1354  CG  ASP A 176      21.083  -5.361   8.779  1.00 20.64           C  
ANISOU 1354  CG  ASP A 176     1671   3308   2865    -40   -294     50       C  
ATOM   1355  OD1 ASP A 176      21.056  -6.115   9.782  1.00 20.35           O  
ANISOU 1355  OD1 ASP A 176     1626   3271   2836    -42   -310     57       O  
ATOM   1356  OD2 ASP A 176      22.123  -4.859   8.339  1.00 20.62           O  
ANISOU 1356  OD2 ASP A 176     1634   3306   2893    -38   -284     88       O  
ATOM   1357  N   LEU A 177      18.223  -7.669   8.632  1.00 18.43           N  
ANISOU 1357  N   LEU A 177     1484   3007   2509    -25   -270    -39       N  
ATOM   1358  CA  LEU A 177      17.969  -9.033   9.131  1.00 18.43           C  
ANISOU 1358  CA  LEU A 177     1492   2997   2512    -16   -263    -40       C  
ATOM   1359  C   LEU A 177      19.212  -9.698   9.755  1.00 18.22           C  
ANISOU 1359  C   LEU A 177     1427   2967   2528      0   -249     -2       C  
ATOM   1360  O   LEU A 177      19.105 -10.811  10.258  1.00 18.97           O  
ANISOU 1360  O   LEU A 177     1525   3054   2630      9   -242      0       O  
ATOM   1361  CB  LEU A 177      17.273  -9.944   8.112  1.00 18.43           C  
ANISOU 1361  CB  LEU A 177     1542   2975   2486    -10   -235    -64       C  
ATOM   1362  CG  LEU A 177      15.736  -9.890   8.148  1.00 19.95           C  
ANISOU 1362  CG  LEU A 177     1762   3174   2645    -32   -267    -89       C  
ATOM   1363  CD1 LEU A 177      15.207 -10.395   9.469  1.00 21.03           C  
ANISOU 1363  CD1 LEU A 177     1881   3321   2788    -37   -293    -85       C  
ATOM   1364  CD2 LEU A 177      15.201  -8.494   7.851  1.00 20.55           C  
ANISOU 1364  CD2 LEU A 177     1836   3268   2705    -48   -287    -98       C  
ATOM   1365  N   GLU A 178      20.350  -9.007   9.792  1.00 16.69           N  
ANISOU 1365  N   GLU A 178     1193   2780   2366      1   -250     34       N  
ATOM   1366  CA  GLU A 178      21.516  -9.437  10.560  1.00 17.14           C  
ANISOU 1366  CA  GLU A 178     1202   2841   2471      7   -251     84       C  
ATOM   1367  C   GLU A 178      21.500  -8.831  12.004  1.00 17.68           C  
ANISOU 1367  C   GLU A 178     1252   2925   2540    -25   -317     94       C  
ATOM   1368  O   GLU A 178      22.427  -9.046  12.778  1.00 18.20           O  
ANISOU 1368  O   GLU A 178     1278   2995   2643    -31   -335    140       O  
ATOM   1369  CB  GLU A 178      22.815  -9.072   9.834  1.00 19.19           C  
ANISOU 1369  CB  GLU A 178     1424   3098   2771     23   -219    133       C  
ATOM   1370  CG  GLU A 178      22.871  -9.669   8.442  1.00 23.81           C  
ANISOU 1370  CG  GLU A 178     2040   3659   3346     60   -147    125       C  
ATOM   1371  CD  GLU A 178      24.219  -9.599   7.770  1.00 32.47           C  
ANISOU 1371  CD  GLU A 178     3097   4750   4489     90    -96    185       C  
ATOM   1372  OE1 GLU A 178      24.949  -8.606   8.008  1.00 32.57           O  
ANISOU 1372  OE1 GLU A 178     3059   4781   4534     71   -126    226       O  
ATOM   1373  OE2 GLU A 178      24.548 -10.536   7.001  1.00 36.25           O  
ANISOU 1373  OE2 GLU A 178     3599   5202   4972    132    -25    195       O  
ATOM   1374  N   GLY A 179      20.478  -8.045  12.332  1.00 17.81           N  
ANISOU 1374  N   GLY A 179     1302   2949   2516    -45   -351     57       N  
ATOM   1375  CA  GLY A 179      20.337  -7.451  13.646  1.00 18.00           C  
ANISOU 1375  CA  GLY A 179     1332   2980   2528    -71   -406     61       C  
ATOM   1376  C   GLY A 179      21.041  -6.134  13.842  1.00 18.33           C  
ANISOU 1376  C   GLY A 179     1365   3024   2574    -98   -445     84       C  
ATOM   1377  O   GLY A 179      21.034  -5.624  14.965  1.00 19.69           O  
ANISOU 1377  O   GLY A 179     1555   3194   2731   -123   -494     90       O  
ATOM   1378  N   ASN A 180      21.645  -5.564  12.788  1.00 17.14           N  
ANISOU 1378  N   ASN A 180     1196   2875   2443    -95   -426     99       N  
ATOM   1379  CA  ASN A 180      22.318  -4.276  12.916  1.00 17.70           C  
ANISOU 1379  CA  ASN A 180     1258   2947   2521   -126   -467    125       C  
ATOM   1380  C   ASN A 180      21.353  -3.134  12.676  1.00 17.50           C  
ANISOU 1380  C   ASN A 180     1282   2920   2448   -135   -479     81       C  
ATOM   1381  O   ASN A 180      20.754  -3.058  11.612  1.00 17.42           O  
ANISOU 1381  O   ASN A 180     1283   2912   2424   -116   -441     53       O  
ATOM   1382  CB  ASN A 180      23.465  -4.160  11.928  1.00 18.57           C  
ANISOU 1382  CB  ASN A 180     1318   3059   2678   -117   -439    171       C  
ATOM   1383  CG  ASN A 180      24.591  -5.083  12.271  1.00 20.04           C  
ANISOU 1383  CG  ASN A 180     1448   3247   2921   -109   -431    233       C  
ATOM   1384  OD1 ASN A 180      24.992  -5.910  11.472  1.00 21.94           O  
ANISOU 1384  OD1 ASN A 180     1663   3485   3190    -72   -369    252       O  
ATOM   1385  ND2 ASN A 180      25.108  -4.977  13.471  1.00 19.91           N  
ANISOU 1385  ND2 ASN A 180     1415   3231   2917   -142   -490    270       N  
ATOM   1386  N   PHE A 181      21.236  -2.235  13.641  1.00 17.32           N  
ANISOU 1386  N   PHE A 181     1294   2889   2399   -164   -531     80       N  
ATOM   1387  CA  PHE A 181      20.344  -1.085  13.507  1.00 17.42           C  
ANISOU 1387  CA  PHE A 181     1358   2896   2366   -169   -539     44       C  
ATOM   1388  C   PHE A 181      20.738  -0.189  12.333  1.00 17.18           C  
ANISOU 1388  C   PHE A 181     1311   2868   2348   -173   -528     50       C  
ATOM   1389  O   PHE A 181      21.925  -0.015  12.044  1.00 16.76           O  
ANISOU 1389  O   PHE A 181     1216   2817   2335   -188   -540     95       O  
ATOM   1390  CB  PHE A 181      20.346  -0.246  14.809  1.00 17.37           C  
ANISOU 1390  CB  PHE A 181     1403   2870   2326   -199   -597     48       C  
ATOM   1391  CG  PHE A 181      19.180  -0.534  15.732  1.00 17.57           C  
ANISOU 1391  CG  PHE A 181     1481   2888   2307   -183   -591     16       C  
ATOM   1392  CD1 PHE A 181      19.303  -1.449  16.766  1.00 18.46           C  
ANISOU 1392  CD1 PHE A 181     1593   2999   2422   -185   -606     28       C  
ATOM   1393  CD2 PHE A 181      17.959   0.089  15.546  1.00 17.90           C  
ANISOU 1393  CD2 PHE A 181     1568   2926   2308   -163   -567    -19       C  
ATOM   1394  CE1 PHE A 181      18.226  -1.736  17.594  1.00 18.75           C  
ANISOU 1394  CE1 PHE A 181     1676   3029   2420   -165   -595      3       C  
ATOM   1395  CE2 PHE A 181      16.875  -0.203  16.368  1.00 18.84           C  
ANISOU 1395  CE2 PHE A 181     1727   3038   2392   -142   -553    -37       C  
ATOM   1396  CZ  PHE A 181      17.018  -1.101  17.399  1.00 18.75           C  
ANISOU 1396  CZ  PHE A 181     1718   3025   2382   -143   -567    -27       C  
ATOM   1397  N   TYR A 182      19.738   0.395  11.683  1.00 16.59           N  
ANISOU 1397  N   TYR A 182     1268   2795   2242   -160   -505     13       N  
ATOM   1398  CA  TYR A 182      19.990   1.453  10.737  1.00 17.38           C  
ANISOU 1398  CA  TYR A 182     1364   2895   2344   -168   -502     16       C  
ATOM   1399  C   TYR A 182      20.167   2.695  11.618  1.00 19.31           C  
ANISOU 1399  C   TYR A 182     1651   3122   2565   -200   -557     23       C  
ATOM   1400  O   TYR A 182      19.361   2.949  12.531  1.00 19.90           O  
ANISOU 1400  O   TYR A 182     1781   3183   2598   -199   -571      0       O  
ATOM   1401  CB  TYR A 182      18.794   1.625   9.804  1.00 16.89           C  
ANISOU 1401  CB  TYR A 182     1322   2839   2254   -146   -464    -23       C  
ATOM   1402  CG  TYR A 182      18.754   0.531   8.765  1.00 15.68           C  
ANISOU 1402  CG  TYR A 182     1142   2695   2119   -122   -417    -27       C  
ATOM   1403  CD1 TYR A 182      19.564   0.585   7.640  1.00 15.98           C  
ANISOU 1403  CD1 TYR A 182     1152   2736   2183   -117   -391     -9       C  
ATOM   1404  CD2 TYR A 182      17.911  -0.560   8.910  1.00 15.45           C  
ANISOU 1404  CD2 TYR A 182     1123   2668   2078   -106   -398    -47       C  
ATOM   1405  CE1 TYR A 182      19.506  -0.401   6.660  1.00 15.45           C  
ANISOU 1405  CE1 TYR A 182     1080   2669   2122    -93   -344    -15       C  
ATOM   1406  CE2 TYR A 182      17.845  -1.555   7.941  1.00 15.98           C  
ANISOU 1406  CE2 TYR A 182     1182   2735   2153    -89   -359    -53       C  
ATOM   1407  CZ  TYR A 182      18.635  -1.465   6.809  1.00 15.88           C  
ANISOU 1407  CZ  TYR A 182     1154   2720   2158    -82   -330    -39       C  
ATOM   1408  OH  TYR A 182      18.576  -2.459   5.860  1.00 15.81           O  
ANISOU 1408  OH  TYR A 182     1156   2703   2148    -63   -288    -46       O  
ATOM   1409  N   GLY A 183      21.226   3.442  11.361  1.00 19.72           N  
ANISOU 1409  N   GLY A 183     1682   3170   2642   -227   -586     58       N  
ATOM   1410  CA  GLY A 183      21.506   4.639  12.139  1.00 20.44           C  
ANISOU 1410  CA  GLY A 183     1821   3237   2708   -266   -646     69       C  
ATOM   1411  C   GLY A 183      22.124   4.317  13.480  1.00 21.12           C  
ANISOU 1411  C   GLY A 183     1921   3308   2795   -297   -702     98       C  
ATOM   1412  O   GLY A 183      22.635   3.218  13.707  1.00 21.48           O  
ANISOU 1412  O   GLY A 183     1918   3367   2876   -292   -697    124       O  
ATOM   1413  N   PRO A 184      22.106   5.296  14.381  1.00 21.39           N  
ANISOU 1413  N   PRO A 184     2029   3312   2788   -331   -757     97       N  
ATOM   1414  CA  PRO A 184      22.785   5.114  15.662  1.00 21.43           C  
ANISOU 1414  CA  PRO A 184     2059   3296   2788   -372   -823    130       C  
ATOM   1415  C   PRO A 184      21.916   4.630  16.808  1.00 21.99           C  
ANISOU 1415  C   PRO A 184     2195   3351   2808   -356   -819     97       C  
ATOM   1416  O   PRO A 184      22.330   4.693  17.959  1.00 22.48           O  
ANISOU 1416  O   PRO A 184     2305   3388   2849   -392   -879    118       O  
ATOM   1417  CB  PRO A 184      23.307   6.516  15.949  1.00 22.01           C  
ANISOU 1417  CB  PRO A 184     2190   3336   2837   -424   -891    150       C  
ATOM   1418  CG  PRO A 184      22.296   7.435  15.298  1.00 22.59           C  
ANISOU 1418  CG  PRO A 184     2312   3402   2871   -395   -848    100       C  
ATOM   1419  CD  PRO A 184      21.557   6.658  14.238  1.00 20.71           C  
ANISOU 1419  CD  PRO A 184     2012   3201   2655   -338   -765     70       C  
ATOM   1420  N   PHE A 185      20.723   4.154  16.502  1.00 21.73           N  
ANISOU 1420  N   PHE A 185     2167   3333   2757   -304   -753     52       N  
ATOM   1421  CA  PHE A 185      19.765   3.756  17.502  1.00 21.74           C  
ANISOU 1421  CA  PHE A 185     2228   3321   2712   -281   -739     24       C  
ATOM   1422  C   PHE A 185      20.146   2.464  18.197  1.00 21.84           C  
ANISOU 1422  C   PHE A 185     2204   3345   2749   -283   -749     44       C  
ATOM   1423  O   PHE A 185      20.833   1.612  17.629  1.00 21.00           O  
ANISOU 1423  O   PHE A 185     2013   3265   2701   -282   -739     70       O  
ATOM   1424  CB  PHE A 185      18.356   3.708  16.873  1.00 21.60           C  
ANISOU 1424  CB  PHE A 185     2215   3317   2676   -227   -667    -17       C  
ATOM   1425  CG  PHE A 185      18.033   5.016  16.181  1.00 21.66           C  
ANISOU 1425  CG  PHE A 185     2255   3313   2663   -226   -658    -32       C  
ATOM   1426  CD1 PHE A 185      17.977   6.200  16.899  1.00 21.96           C  
ANISOU 1426  CD1 PHE A 185     2387   3309   2648   -244   -690    -36       C  
ATOM   1427  CD2 PHE A 185      17.933   5.082  14.801  1.00 22.13           C  
ANISOU 1427  CD2 PHE A 185     2255   3398   2754   -212   -623    -37       C  
ATOM   1428  CE1 PHE A 185      17.770   7.412  16.254  1.00 22.65           C  
ANISOU 1428  CE1 PHE A 185     2503   3383   2719   -245   -683    -46       C  
ATOM   1429  CE2 PHE A 185      17.701   6.292  14.159  1.00 22.67           C  
ANISOU 1429  CE2 PHE A 185     2350   3457   2807   -214   -618    -46       C  
ATOM   1430  CZ  PHE A 185      17.608   7.447  14.886  1.00 22.57           C  
ANISOU 1430  CZ  PHE A 185     2424   3405   2746   -228   -647    -50       C  
ATOM   1431  N   VAL A 186      19.762   2.368  19.476  1.00 22.53           N  
ANISOU 1431  N   VAL A 186     2363   3408   2790   -285   -769     36       N  
ATOM   1432  CA  VAL A 186      19.978   1.194  20.309  1.00 22.86           C  
ANISOU 1432  CA  VAL A 186     2384   3457   2845   -287   -780     52       C  
ATOM   1433  C   VAL A 186      18.633   0.684  20.831  1.00 22.63           C  
ANISOU 1433  C   VAL A 186     2395   3427   2777   -239   -730     17       C  
ATOM   1434  O   VAL A 186      17.721   1.482  21.061  1.00 23.04           O  
ANISOU 1434  O   VAL A 186     2522   3457   2776   -218   -708     -9       O  
ATOM   1435  CB  VAL A 186      20.984   1.429  21.462  1.00 24.42           C  
ANISOU 1435  CB  VAL A 186     2625   3625   3028   -344   -865     91       C  
ATOM   1436  CG1 VAL A 186      22.386   1.653  20.918  1.00 25.61           C  
ANISOU 1436  CG1 VAL A 186     2706   3786   3238   -391   -914    145       C  
ATOM   1437  CG2 VAL A 186      20.560   2.598  22.344  1.00 25.15           C  
ANISOU 1437  CG2 VAL A 186     2848   3667   3039   -361   -897     71       C  
ATOM   1438  N   ASP A 187      18.511  -0.625  21.048  1.00 21.20           N  
ANISOU 1438  N   ASP A 187     2165   3267   2623   -221   -709     21       N  
ATOM   1439  CA  ASP A 187      17.285  -1.205  21.585  1.00 20.56           C  
ANISOU 1439  CA  ASP A 187     2112   3187   2512   -178   -665     -2       C  
ATOM   1440  C   ASP A 187      17.221  -1.051  23.101  1.00 21.43           C  
ANISOU 1440  C   ASP A 187     2311   3265   2568   -189   -697      2       C  
ATOM   1441  O   ASP A 187      17.381  -2.014  23.860  1.00 20.69           O  
ANISOU 1441  O   ASP A 187     2204   3174   2481   -191   -708     15       O  
ATOM   1442  CB  ASP A 187      17.073  -2.660  21.144  1.00 19.66           C  
ANISOU 1442  CB  ASP A 187     1917   3107   2445   -154   -628     -1       C  
ATOM   1443  CG  ASP A 187      18.245  -3.610  21.309  1.00 20.41           C  
ANISOU 1443  CG  ASP A 187     1953   3213   2588   -178   -658     32       C  
ATOM   1444  OD1 ASP A 187      19.332  -3.154  21.721  1.00 21.14           O  
ANISOU 1444  OD1 ASP A 187     2054   3292   2687   -220   -714     62       O  
ATOM   1445  OD2 ASP A 187      18.081  -4.798  21.007  1.00 20.44           O  
ANISOU 1445  OD2 ASP A 187     1903   3238   2627   -157   -626     33       O  
ATOM   1446  N   ARG A 188      16.991   0.191  23.529  1.00 22.10           N  
ANISOU 1446  N   ARG A 188     2492   3311   2594   -197   -712     -8       N  
ATOM   1447  CA  ARG A 188      16.904   0.589  24.918  1.00 23.54           C  
ANISOU 1447  CA  ARG A 188     2788   3449   2708   -207   -741     -7       C  
ATOM   1448  C   ARG A 188      15.846   1.704  25.042  1.00 24.68           C  
ANISOU 1448  C   ARG A 188     3031   3560   2788   -170   -697    -33       C  
ATOM   1449  O   ARG A 188      15.728   2.551  24.150  1.00 24.55           O  
ANISOU 1449  O   ARG A 188     3007   3545   2777   -167   -683    -43       O  
ATOM   1450  CB  ARG A 188      18.286   1.088  25.386  1.00 25.09           C  
ANISOU 1450  CB  ARG A 188     3016   3619   2899   -279   -834     22       C  
ATOM   1451  CG  ARG A 188      18.285   1.688  26.767  1.00 29.82           C  
ANISOU 1451  CG  ARG A 188     3756   4159   3415   -302   -877     23       C  
ATOM   1452  CD  ARG A 188      19.673   2.022  27.265  1.00 34.88           C  
ANISOU 1452  CD  ARG A 188     4422   4775   4056   -384   -983     62       C  
ATOM   1453  NE  ARG A 188      19.595   2.676  28.567  1.00 40.23           N  
ANISOU 1453  NE  ARG A 188     5258   5386   4639   -408  -1026     58       N  
ATOM   1454  CZ  ARG A 188      20.644   3.044  29.296  1.00 43.73           C  
ANISOU 1454  CZ  ARG A 188     5762   5793   5059   -486  -1129     94       C  
ATOM   1455  NH1 ARG A 188      21.877   2.815  28.860  1.00 44.39           N  
ANISOU 1455  NH1 ARG A 188     5747   5903   5215   -545  -1197    143       N  
ATOM   1456  NH2 ARG A 188      20.467   3.634  30.471  1.00 43.85           N  
ANISOU 1456  NH2 ARG A 188     5941   5742   4978   -505  -1164     85       N  
ATOM   1457  N   GLN A 189      15.081   1.689  26.144  1.00 25.78           N  
ANISOU 1457  N   GLN A 189     3260   3668   2866   -139   -671    -39       N  
ATOM   1458  CA  GLN A 189      14.040   2.662  26.489  1.00 27.16           C  
ANISOU 1458  CA  GLN A 189     3541   3803   2974    -93   -618    -54       C  
ATOM   1459  C   GLN A 189      14.735   3.883  27.066  1.00 28.28           C  
ANISOU 1459  C   GLN A 189     3811   3883   3050   -138   -678    -56       C  
ATOM   1460  O   GLN A 189      14.727   4.137  28.268  1.00 28.99           O  
ANISOU 1460  O   GLN A 189     4025   3922   3069   -143   -697    -56       O  
ATOM   1461  CB  GLN A 189      13.057   2.044  27.508  1.00 28.80           C  
ANISOU 1461  CB  GLN A 189     3796   4001   3146    -40   -564    -51       C  
ATOM   1462  CG  GLN A 189      11.887   2.937  27.940  1.00 32.91           C  
ANISOU 1462  CG  GLN A 189     4427   4479   3599     23   -492    -56       C  
ATOM   1463  CD  GLN A 189      11.096   3.414  26.760  1.00 38.75           C  
ANISOU 1463  CD  GLN A 189     5105   5245   4372     61   -433    -58       C  
ATOM   1464  OE1 GLN A 189      10.643   2.622  25.918  1.00 40.33           O  
ANISOU 1464  OE1 GLN A 189     5183   5500   4639     78   -404    -51       O  
ATOM   1465  NE2 GLN A 189      10.936   4.723  26.666  1.00 40.20           N  
ANISOU 1465  NE2 GLN A 189     5379   5386   4508     72   -418    -66       N  
ATOM   1466  N   THR A 190      15.427   4.578  26.209  1.00 29.21           N  
ANISOU 1466  N   THR A 190     3899   4006   3194   -176   -716    -56       N  
ATOM   1467  CA  THR A 190      16.142   5.789  26.549  1.00 31.26           C  
ANISOU 1467  CA  THR A 190     4268   4208   3401   -228   -781    -54       C  
ATOM   1468  C   THR A 190      15.891   6.770  25.415  1.00 33.05           C  
ANISOU 1468  C   THR A 190     4475   4440   3642   -215   -753    -67       C  
ATOM   1469  O   THR A 190      15.785   6.365  24.250  1.00 33.74           O  
ANISOU 1469  O   THR A 190     4436   4584   3801   -200   -722    -67       O  
ATOM   1470  CB  THR A 190      17.632   5.492  26.850  1.00 32.57           C  
ANISOU 1470  CB  THR A 190     4407   4374   3593   -313   -889    -23       C  
ATOM   1471  OG1 THR A 190      18.174   6.559  27.632  1.00 33.36           O  
ANISOU 1471  OG1 THR A 190     4653   4404   3620   -366   -960    -17       O  
ATOM   1472  CG2 THR A 190      18.462   5.237  25.594  1.00 32.52           C  
ANISOU 1472  CG2 THR A 190     4253   4422   3680   -343   -912     -3       C  
ATOM   1473  N   ALA A 191      15.736   8.057  25.743  1.00 33.42           N  
ANISOU 1473  N   ALA A 191     4656   4426   3618   -218   -758    -78       N  
ATOM   1474  CA  ALA A 191      15.458   9.065  24.730  1.00 33.92           C  
ANISOU 1474  CA  ALA A 191     4710   4488   3689   -203   -730    -89       C  
ATOM   1475  C   ALA A 191      16.599   9.158  23.730  1.00 32.96           C  
ANISOU 1475  C   ALA A 191     4486   4401   3636   -265   -794    -72       C  
ATOM   1476  O   ALA A 191      17.754   9.321  24.108  1.00 33.56           O  
ANISOU 1476  O   ALA A 191     4585   4456   3709   -337   -885    -50       O  
ATOM   1477  CB  ALA A 191      15.197  10.411  25.375  1.00 34.52           C  
ANISOU 1477  CB  ALA A 191     4962   4484   3671   -199   -730   -101       C  
ATOM   1478  N   GLN A 192      16.270   8.896  22.477  1.00 31.30           N  
ANISOU 1478  N   GLN A 192     4155   4247   3491   -236   -746    -77       N  
ATOM   1479  CA  GLN A 192      17.195   8.911  21.360  1.00 30.71           C  
ANISOU 1479  CA  GLN A 192     3972   4210   3486   -277   -784    -61       C  
ATOM   1480  C   GLN A 192      16.567   9.825  20.334  1.00 30.49           C  
ANISOU 1480  C   GLN A 192     3939   4187   3460   -247   -735    -77       C  
ATOM   1481  O   GLN A 192      15.424   9.588  19.927  1.00 31.08           O  
ANISOU 1481  O   GLN A 192     3985   4284   3539   -185   -657    -92       O  
ATOM   1482  CB  GLN A 192      17.320   7.497  20.777  1.00 31.07           C  
ANISOU 1482  CB  GLN A 192     3877   4321   3607   -264   -762    -51       C  
ATOM   1483  CG  GLN A 192      17.825   6.497  21.786  1.00 32.03           C  
ANISOU 1483  CG  GLN A 192     3997   4442   3731   -286   -800    -33       C  
ATOM   1484  CD  GLN A 192      17.798   5.119  21.213  1.00 32.78           C  
ANISOU 1484  CD  GLN A 192     3965   4595   3894   -264   -766    -27       C  
ATOM   1485  OE1 GLN A 192      18.336   4.879  20.150  1.00 32.46           O  
ANISOU 1485  OE1 GLN A 192     3829   4589   3914   -273   -765    -15       O  
ATOM   1486  NE2 GLN A 192      17.182   4.182  21.920  1.00 33.35           N  
ANISOU 1486  NE2 GLN A 192     4043   4674   3955   -233   -737    -34       N  
ATOM   1487  N   ALA A 193      17.259  10.900  19.966  1.00 29.99           N  
ANISOU 1487  N   ALA A 193     3906   4099   3390   -290   -783    -69       N  
ATOM   1488  CA  ALA A 193      16.682  11.848  19.015  1.00 29.65           C  
ANISOU 1488  CA  ALA A 193     3863   4056   3346   -262   -739    -84       C  
ATOM   1489  C   ALA A 193      17.173  11.598  17.613  1.00 29.40           C  
ANISOU 1489  C   ALA A 193     3697   4081   3392   -274   -737    -73       C  
ATOM   1490  O   ALA A 193      18.288  11.101  17.411  1.00 29.91           O  
ANISOU 1490  O   ALA A 193     3691   4168   3505   -319   -789    -46       O  
ATOM   1491  CB  ALA A 193      16.973  13.269  19.443  1.00 29.43           C  
ANISOU 1491  CB  ALA A 193     3966   3961   3256   -295   -781    -86       C  
ATOM   1492  N   ALA A 194      16.330  11.911  16.640  1.00 28.17           N  
ANISOU 1492  N   ALA A 194     3506   3947   3248   -231   -674    -88       N  
ATOM   1493  CA  ALA A 194      16.706  11.728  15.251  1.00 27.09           C  
ANISOU 1493  CA  ALA A 194     3257   3860   3177   -238   -666    -80       C  
ATOM   1494  C   ALA A 194      17.406  12.972  14.707  1.00 24.69           C  
ANISOU 1494  C   ALA A 194     2974   3534   2872   -276   -706    -70       C  
ATOM   1495  O   ALA A 194      17.212  14.083  15.197  1.00 24.35           O  
ANISOU 1495  O   ALA A 194     3036   3441   2776   -282   -718    -78       O  
ATOM   1496  CB  ALA A 194      15.481  11.387  14.410  1.00 27.77           C  
ANISOU 1496  CB  ALA A 194     3292   3982   3280   -180   -588    -96       C  
ATOM   1497  N   GLY A 195      18.236  12.768  13.711  1.00 23.19           N  
ANISOU 1497  N   GLY A 195     2689   3380   2742   -301   -722    -50       N  
ATOM   1498  CA  GLY A 195      18.876  13.865  13.011  1.00 22.56           C  
ANISOU 1498  CA  GLY A 195     2609   3290   2673   -334   -753    -36       C  
ATOM   1499  C   GLY A 195      17.905  14.509  12.037  1.00 21.56           C  
ANISOU 1499  C   GLY A 195     2478   3173   2539   -292   -692    -59       C  
ATOM   1500  O   GLY A 195      16.708  14.184  12.011  1.00 20.99           O  
ANISOU 1500  O   GLY A 195     2412   3113   2452   -241   -631    -81       O  
ATOM   1501  N   THR A 196      18.412  15.444  11.227  1.00 21.70           N  
ANISOU 1501  N   THR A 196     2484   3188   2572   -317   -711    -47       N  
ATOM   1502  CA  THR A 196      17.623  16.174  10.249  1.00 22.37           C  
ANISOU 1502  CA  THR A 196     2564   3281   2653   -285   -662    -63       C  
ATOM   1503  C   THR A 196      17.001  15.237   9.255  1.00 22.28           C  
ANISOU 1503  C   THR A 196     2462   3324   2679   -245   -603    -72       C  
ATOM   1504  O   THR A 196      17.686  14.375   8.706  1.00 21.07           O  
ANISOU 1504  O   THR A 196     2228   3205   2572   -257   -608    -57       O  
ATOM   1505  CB  THR A 196      18.467  17.208   9.503  1.00 24.42           C  
ANISOU 1505  CB  THR A 196     2813   3533   2932   -324   -699    -43       C  
ATOM   1506  OG1 THR A 196      19.082  18.077  10.444  1.00 25.34           O  
ANISOU 1506  OG1 THR A 196     3023   3595   3012   -370   -766    -31       O  
ATOM   1507  CG2 THR A 196      17.642  18.037   8.532  1.00 25.51           C  
ANISOU 1507  CG2 THR A 196     2952   3678   3063   -292   -651    -59       C  
ATOM   1508  N   ASP A 197      15.683  15.363   9.074  1.00 22.98           N  
ANISOU 1508  N   ASP A 197     2569   3416   2746   -198   -547    -91       N  
ATOM   1509  CA  ASP A 197      15.009  14.556   8.090  1.00 23.43           C  
ANISOU 1509  CA  ASP A 197     2550   3520   2834   -169   -499    -95       C  
ATOM   1510  C   ASP A 197      15.043  15.298   6.768  1.00 23.57           C  
ANISOU 1510  C   ASP A 197     2533   3552   2869   -173   -488    -91       C  
ATOM   1511  O   ASP A 197      14.098  16.003   6.432  1.00 24.54           O  
ANISOU 1511  O   ASP A 197     2678   3671   2975   -147   -455    -96       O  
ATOM   1512  CB  ASP A 197      13.581  14.194   8.493  1.00 24.99           C  
ANISOU 1512  CB  ASP A 197     2767   3720   3010   -121   -450   -103       C  
ATOM   1513  CG  ASP A 197      13.022  13.011   7.700  1.00 29.17           C  
ANISOU 1513  CG  ASP A 197     3217   4294   3571   -105   -419   -102       C  
ATOM   1514  OD1 ASP A 197      13.644  12.622   6.668  1.00 28.74           O  
ANISOU 1514  OD1 ASP A 197     3104   4267   3550   -124   -427   -100       O  
ATOM   1515  OD2 ASP A 197      11.982  12.463   8.112  1.00 31.14           O  
ANISOU 1515  OD2 ASP A 197     3470   4550   3812    -73   -388   -100       O  
ATOM   1516  N   THR A 198      16.134  15.151   6.024  1.00 23.11           N  
ANISOU 1516  N   THR A 198     2421   3512   2848   -202   -511    -78       N  
ATOM   1517  CA  THR A 198      16.259  15.810   4.724  1.00 22.96           C  
ANISOU 1517  CA  THR A 198     2368   3508   2846   -206   -499    -72       C  
ATOM   1518  C   THR A 198      15.406  15.110   3.662  1.00 21.49           C  
ANISOU 1518  C   THR A 198     2134   3359   2673   -178   -452    -81       C  
ATOM   1519  O   THR A 198      15.013  13.961   3.839  1.00 21.70           O  
ANISOU 1519  O   THR A 198     2140   3401   2704   -163   -436    -87       O  
ATOM   1520  CB  THR A 198      17.726  15.913   4.306  1.00 25.45           C  
ANISOU 1520  CB  THR A 198     2643   3828   3198   -244   -534    -46       C  
ATOM   1521  OG1 THR A 198      18.294  14.612   4.350  1.00 26.63           O  
ANISOU 1521  OG1 THR A 198     2740   4000   3377   -244   -532    -36       O  
ATOM   1522  CG2 THR A 198      18.527  16.869   5.203  1.00 26.37           C  
ANISOU 1522  CG2 THR A 198     2812   3905   3301   -283   -594    -29       C  
ATOM   1523  N   THR A 199      15.083  15.824   2.583  1.00 20.12           N  
ANISOU 1523  N   THR A 199     1949   3195   2502   -174   -434    -80       N  
ATOM   1524  CA  THR A 199      14.299  15.261   1.494  1.00 19.34           C  
ANISOU 1524  CA  THR A 199     1812   3125   2410   -157   -400    -83       C  
ATOM   1525  C   THR A 199      15.200  14.521   0.505  1.00 18.80           C  
ANISOU 1525  C   THR A 199     1695   3078   2370   -169   -396    -77       C  
ATOM   1526  O   THR A 199      16.279  15.024   0.155  1.00 19.52           O  
ANISOU 1526  O   THR A 199     1772   3166   2480   -188   -411    -63       O  
ATOM   1527  CB  THR A 199      13.437  16.351   0.845  1.00 20.25           C  
ANISOU 1527  CB  THR A 199     1941   3239   2512   -145   -382    -80       C  
ATOM   1528  OG1 THR A 199      12.707  17.029   1.873  1.00 20.58           O  
ANISOU 1528  OG1 THR A 199     2038   3255   2528   -126   -377    -80       O  
ATOM   1529  CG2 THR A 199      12.439  15.796  -0.147  1.00 19.95           C  
ANISOU 1529  CG2 THR A 199     1872   3228   2478   -133   -355    -77       C  
ATOM   1530  N   ILE A 200      14.771  13.311   0.055  1.00 17.28           N  
ANISOU 1530  N   ILE A 200     1480   2905   2181   -158   -375    -84       N  
ATOM   1531  CA  ILE A 200      15.546  12.503  -0.883  1.00 16.21           C  
ANISOU 1531  CA  ILE A 200     1313   2782   2064   -162   -360    -79       C  
ATOM   1532  C   ILE A 200      15.388  13.077  -2.312  1.00 15.47           C  
ANISOU 1532  C   ILE A 200     1213   2697   1966   -164   -343    -76       C  
ATOM   1533  O   ILE A 200      14.463  12.710  -3.054  1.00 15.46           O  
ANISOU 1533  O   ILE A 200     1219   2707   1950   -160   -329    -83       O  
ATOM   1534  CB  ILE A 200      15.140  11.015  -0.799  1.00 16.25           C  
ANISOU 1534  CB  ILE A 200     1312   2795   2066   -152   -346    -88       C  
ATOM   1535  CG1 ILE A 200      15.126  10.514   0.689  1.00 17.14           C  
ANISOU 1535  CG1 ILE A 200     1433   2899   2180   -149   -363    -91       C  
ATOM   1536  CG2 ILE A 200      16.050  10.153  -1.665  1.00 16.30           C  
ANISOU 1536  CG2 ILE A 200     1301   2806   2089   -150   -324    -82       C  
ATOM   1537  CD1 ILE A 200      13.992   9.509   1.020  1.00 17.58           C  
ANISOU 1537  CD1 ILE A 200     1495   2961   2223   -136   -354   -101       C  
ATOM   1538  N   THR A 201      16.257  14.023  -2.658  1.00 14.44           N  
ANISOU 1538  N   THR A 201     1074   2562   1849   -175   -350    -62       N  
ATOM   1539  CA  THR A 201      16.222  14.733  -3.942  1.00 14.62           C  
ANISOU 1539  CA  THR A 201     1094   2593   1869   -177   -336    -56       C  
ATOM   1540  C   THR A 201      16.019  13.857  -5.175  1.00 15.07           C  
ANISOU 1540  C   THR A 201     1150   2661   1917   -169   -305    -61       C  
ATOM   1541  O   THR A 201      15.162  14.185  -6.019  1.00 15.99           O  
ANISOU 1541  O   THR A 201     1279   2783   2013   -172   -299    -66       O  
ATOM   1542  CB  THR A 201      17.511  15.571  -4.094  1.00 15.33           C  
ANISOU 1542  CB  THR A 201     1164   2677   1985   -190   -346    -32       C  
ATOM   1543  OG1 THR A 201      17.694  16.315  -2.891  1.00 16.17           O  
ANISOU 1543  OG1 THR A 201     1286   2765   2093   -204   -384    -28       O  
ATOM   1544  CG2 THR A 201      17.448  16.511  -5.280  1.00 15.84           C  
ANISOU 1544  CG2 THR A 201     1227   2746   2046   -193   -334    -25       C  
ATOM   1545  N   VAL A 202      16.823  12.779  -5.326  1.00 14.26           N  
ANISOU 1545  N   VAL A 202     1035   2556   1825   -161   -285    -56       N  
ATOM   1546  CA  VAL A 202      16.742  11.890  -6.491  1.00 14.91           C  
ANISOU 1546  CA  VAL A 202     1135   2639   1891   -152   -252    -61       C  
ATOM   1547  C   VAL A 202      15.332  11.267  -6.600  1.00 15.06           C  
ANISOU 1547  C   VAL A 202     1184   2660   1878   -158   -261    -81       C  
ATOM   1548  O   VAL A 202      14.819  11.105  -7.704  1.00 15.18           O  
ANISOU 1548  O   VAL A 202     1226   2674   1868   -164   -252    -85       O  
ATOM   1549  CB  VAL A 202      17.881  10.826  -6.519  1.00 15.65           C  
ANISOU 1549  CB  VAL A 202     1217   2724   2003   -134   -221    -47       C  
ATOM   1550  CG1 VAL A 202      17.737   9.825  -5.379  1.00 16.87           C  
ANISOU 1550  CG1 VAL A 202     1370   2877   2165   -131   -233    -56       C  
ATOM   1551  CG2 VAL A 202      17.943  10.106  -7.859  1.00 16.64           C  
ANISOU 1551  CG2 VAL A 202     1378   2840   2104   -121   -177    -50       C  
ATOM   1552  N   ASN A 203      14.696  10.969  -5.444  1.00 14.63           N  
ANISOU 1552  N   ASN A 203     1125   2607   1826   -159   -283    -89       N  
ATOM   1553  CA  ASN A 203      13.344  10.416  -5.432  1.00 14.72           C  
ANISOU 1553  CA  ASN A 203     1154   2622   1816   -166   -295    -96       C  
ATOM   1554  C   ASN A 203      12.320  11.443  -5.854  1.00 15.28           C  
ANISOU 1554  C   ASN A 203     1226   2702   1877   -175   -308    -86       C  
ATOM   1555  O   ASN A 203      11.365  11.109  -6.569  1.00 15.45           O  
ANISOU 1555  O   ASN A 203     1262   2728   1880   -189   -316    -81       O  
ATOM   1556  CB  ASN A 203      13.000   9.827  -4.070  1.00 15.80           C  
ANISOU 1556  CB  ASN A 203     1282   2759   1962   -160   -308    -99       C  
ATOM   1557  CG  ASN A 203      13.789   8.575  -3.747  1.00 19.67           C  
ANISOU 1557  CG  ASN A 203     1772   3240   2460   -152   -296   -105       C  
ATOM   1558  OD1 ASN A 203      14.699   8.166  -4.482  1.00 18.89           O  
ANISOU 1558  OD1 ASN A 203     1679   3134   2363   -146   -272   -104       O  
ATOM   1559  ND2 ASN A 203      13.449   7.937  -2.623  1.00 21.64           N  
ANISOU 1559  ND2 ASN A 203     2018   3491   2716   -147   -308   -109       N  
ATOM   1560  N   VAL A 204      12.498  12.700  -5.429  1.00 14.92           N  
ANISOU 1560  N   VAL A 204     1169   2658   1844   -171   -313    -80       N  
ATOM   1561  CA  VAL A 204      11.575  13.769  -5.845  1.00 15.36           C  
ANISOU 1561  CA  VAL A 204     1224   2719   1892   -174   -319    -67       C  
ATOM   1562  C   VAL A 204      11.631  13.931  -7.391  1.00 15.02           C  
ANISOU 1562  C   VAL A 204     1190   2681   1835   -189   -313    -63       C  
ATOM   1563  O   VAL A 204      10.595  13.992  -8.051  1.00 14.61           O  
ANISOU 1563  O   VAL A 204     1144   2637   1770   -201   -322    -50       O  
ATOM   1564  CB  VAL A 204      11.912  15.092  -5.135  1.00 17.15           C  
ANISOU 1564  CB  VAL A 204     1450   2938   2130   -166   -323    -64       C  
ATOM   1565  CG1 VAL A 204      11.027  16.222  -5.661  1.00 18.38           C  
ANISOU 1565  CG1 VAL A 204     1607   3098   2280   -165   -322    -47       C  
ATOM   1566  CG2 VAL A 204      11.780  14.942  -3.612  1.00 17.88           C  
ANISOU 1566  CG2 VAL A 204     1550   3020   2225   -152   -329    -68       C  
ATOM   1567  N   LEU A 205      12.835  13.932  -7.956  1.00 14.89           N  
ANISOU 1567  N   LEU A 205     1176   2659   1822   -187   -296    -69       N  
ATOM   1568  CA  LEU A 205      13.035  14.065  -9.404  1.00 15.74           C  
ANISOU 1568  CA  LEU A 205     1300   2767   1913   -196   -282    -66       C  
ATOM   1569  C   LEU A 205      12.401  12.902 -10.145  1.00 15.95           C  
ANISOU 1569  C   LEU A 205     1363   2789   1910   -209   -284    -71       C  
ATOM   1570  O   LEU A 205      11.745  13.099 -11.174  1.00 15.67           O  
ANISOU 1570  O   LEU A 205     1349   2754   1850   -227   -293    -63       O  
ATOM   1571  CB  LEU A 205      14.535  14.154  -9.728  1.00 15.73           C  
ANISOU 1571  CB  LEU A 205     1292   2759   1927   -184   -256    -62       C  
ATOM   1572  CG  LEU A 205      15.179  15.442  -9.256  1.00 16.89           C  
ANISOU 1572  CG  LEU A 205     1410   2908   2101   -182   -264    -50       C  
ATOM   1573  CD1 LEU A 205      16.693  15.350  -9.331  1.00 18.14           C  
ANISOU 1573  CD1 LEU A 205     1547   3061   2285   -172   -243    -34       C  
ATOM   1574  CD2 LEU A 205      14.628  16.625 -10.059  1.00 17.98           C  
ANISOU 1574  CD2 LEU A 205     1551   3052   2229   -192   -270    -43       C  
ATOM   1575  N   ALA A 206      12.578  11.681  -9.614  1.00 16.01           N  
ANISOU 1575  N   ALA A 206     1380   2787   1915   -203   -279    -82       N  
ATOM   1576  CA  ALA A 206      11.994  10.473 -10.195  1.00 17.08           C  
ANISOU 1576  CA  ALA A 206     1559   2911   2019   -219   -286    -87       C  
ATOM   1577  C   ALA A 206      10.453  10.605 -10.209  1.00 16.72           C  
ANISOU 1577  C   ALA A 206     1510   2877   1964   -245   -326    -70       C  
ATOM   1578  O   ALA A 206       9.818  10.384 -11.248  1.00 16.05           O  
ANISOU 1578  O   ALA A 206     1462   2786   1850   -273   -344    -61       O  
ATOM   1579  CB  ALA A 206      12.420   9.252  -9.387  1.00 17.20           C  
ANISOU 1579  CB  ALA A 206     1579   2916   2042   -205   -275    -99       C  
ATOM   1580  N   TRP A 207       9.884  11.103  -9.105  1.00 16.26           N  
ANISOU 1580  N   TRP A 207     1410   2833   1933   -236   -339    -59       N  
ATOM   1581  CA  TRP A 207       8.442  11.332  -9.002  1.00 17.29           C  
ANISOU 1581  CA  TRP A 207     1525   2978   2067   -253   -368    -29       C  
ATOM   1582  C   TRP A 207       7.965  12.471  -9.959  1.00 16.89           C  
ANISOU 1582  C   TRP A 207     1470   2936   2012   -266   -377     -7       C  
ATOM   1583  O   TRP A 207       6.901  12.356 -10.556  1.00 16.59           O  
ANISOU 1583  O   TRP A 207     1435   2903   1963   -294   -406     23       O  
ATOM   1584  CB  TRP A 207       8.082  11.599  -7.544  1.00 18.12           C  
ANISOU 1584  CB  TRP A 207     1593   3090   2200   -229   -365    -20       C  
ATOM   1585  CG  TRP A 207       6.706  12.131  -7.305  1.00 19.65           C  
ANISOU 1585  CG  TRP A 207     1761   3299   2407   -230   -380     21       C  
ATOM   1586  CD1 TRP A 207       5.556  11.413  -7.173  1.00 21.16           C  
ANISOU 1586  CD1 TRP A 207     1940   3497   2602   -246   -403     54       C  
ATOM   1587  CD2 TRP A 207       6.377  13.483  -6.986  1.00 20.12           C  
ANISOU 1587  CD2 TRP A 207     1799   3365   2482   -209   -366     40       C  
ATOM   1588  NE1 TRP A 207       4.528  12.244  -6.792  1.00 21.74           N  
ANISOU 1588  NE1 TRP A 207     1979   3584   2698   -232   -400     99       N  
ATOM   1589  CE2 TRP A 207       5.004  13.524  -6.687  1.00 20.99           C  
ANISOU 1589  CE2 TRP A 207     1882   3486   2608   -208   -375     89       C  
ATOM   1590  CE3 TRP A 207       7.128  14.657  -6.854  1.00 21.27           C  
ANISOU 1590  CE3 TRP A 207     1946   3503   2631   -191   -347     25       C  
ATOM   1591  CZ2 TRP A 207       4.360  14.704  -6.309  1.00 21.78           C  
ANISOU 1591  CZ2 TRP A 207     1961   3591   2725   -181   -356    121       C  
ATOM   1592  CZ3 TRP A 207       6.474  15.836  -6.548  1.00 21.89           C  
ANISOU 1592  CZ3 TRP A 207     2013   3584   2722   -171   -335     52       C  
ATOM   1593  CH2 TRP A 207       5.105  15.853  -6.287  1.00 21.67           C  
ANISOU 1593  CH2 TRP A 207     1960   3566   2707   -163   -335     99       C  
ATOM   1594  N   LEU A 208       8.777  13.512 -10.168  1.00 16.12           N  
ANISOU 1594  N   LEU A 208     1366   2839   1921   -251   -355    -17       N  
ATOM   1595  CA  LEU A 208       8.472  14.557 -11.142  1.00 16.44           C  
ANISOU 1595  CA  LEU A 208     1406   2887   1956   -262   -360      1       C  
ATOM   1596  C   LEU A 208       8.438  13.940 -12.573  1.00 16.25           C  
ANISOU 1596  C   LEU A 208     1427   2852   1893   -293   -372      0       C  
ATOM   1597  O   LEU A 208       7.561  14.270 -13.373  1.00 15.89           O  
ANISOU 1597  O   LEU A 208     1388   2814   1836   -320   -398     28       O  
ATOM   1598  CB  LEU A 208       9.524  15.678 -11.039  1.00 16.32           C  
ANISOU 1598  CB  LEU A 208     1378   2869   1955   -241   -335    -12       C  
ATOM   1599  CG  LEU A 208       9.362  16.562  -9.776  1.00 17.14           C  
ANISOU 1599  CG  LEU A 208     1454   2974   2085   -217   -331     -6       C  
ATOM   1600  CD1 LEU A 208      10.489  17.572  -9.673  1.00 17.09           C  
ANISOU 1600  CD1 LEU A 208     1444   2960   2090   -206   -317    -17       C  
ATOM   1601  CD2 LEU A 208       7.998  17.303  -9.790  1.00 17.94           C  
ANISOU 1601  CD2 LEU A 208     1537   3086   2193   -217   -341     31       C  
ATOM   1602  N   TYR A 209       9.357  13.007 -12.877  1.00 16.41           N  
ANISOU 1602  N   TYR A 209     1488   2854   1893   -290   -353    -27       N  
ATOM   1603  CA  TYR A 209       9.334  12.308 -14.172  1.00 16.97           C  
ANISOU 1603  CA  TYR A 209     1624   2907   1918   -316   -359    -31       C  
ATOM   1604  C   TYR A 209       8.050  11.477 -14.276  1.00 17.63           C  
ANISOU 1604  C   TYR A 209     1729   2987   1983   -356   -408    -10       C  
ATOM   1605  O   TYR A 209       7.384  11.540 -15.301  1.00 17.95           O  
ANISOU 1605  O   TYR A 209     1804   3023   1994   -393   -439     10       O  
ATOM   1606  CB  TYR A 209      10.560  11.416 -14.348  1.00 16.54           C  
ANISOU 1606  CB  TYR A 209     1612   2827   1845   -294   -318    -60       C  
ATOM   1607  CG  TYR A 209      11.761  12.195 -14.828  1.00 16.91           C  
ANISOU 1607  CG  TYR A 209     1652   2872   1899   -267   -274    -65       C  
ATOM   1608  CD1 TYR A 209      11.823  12.682 -16.127  1.00 18.23           C  
ANISOU 1608  CD1 TYR A 209     1857   3032   2035   -279   -267    -59       C  
ATOM   1609  CD2 TYR A 209      12.877  12.347 -14.028  1.00 17.30           C  
ANISOU 1609  CD2 TYR A 209     1662   2926   1986   -233   -241    -71       C  
ATOM   1610  CE1 TYR A 209      12.930  13.378 -16.583  1.00 18.50           C  
ANISOU 1610  CE1 TYR A 209     1883   3066   2080   -252   -224    -57       C  
ATOM   1611  CE2 TYR A 209      13.992  13.043 -14.472  1.00 18.30           C  
ANISOU 1611  CE2 TYR A 209     1776   3052   2125   -211   -204    -65       C  
ATOM   1612  CZ  TYR A 209      14.011  13.564 -15.750  1.00 18.87           C  
ANISOU 1612  CZ  TYR A 209     1880   3119   2169   -219   -193    -58       C  
ATOM   1613  OH  TYR A 209      15.101  14.243 -16.218  1.00 20.85           O  
ANISOU 1613  OH  TYR A 209     2116   3370   2435   -196   -155    -46       O  
ATOM   1614  N   ALA A 210       7.653  10.771 -13.182  1.00 17.47           N  
ANISOU 1614  N   ALA A 210     1683   2971   1983   -351   -419     -8       N  
ATOM   1615  CA  ALA A 210       6.394  10.006 -13.156  1.00 17.87           C  
ANISOU 1615  CA  ALA A 210     1742   3022   2026   -390   -469     22       C  
ATOM   1616  C   ALA A 210       5.202  10.918 -13.420  1.00 18.73           C  
ANISOU 1616  C   ALA A 210     1810   3154   2153   -413   -504     74       C  
ATOM   1617  O   ALA A 210       4.254  10.511 -14.106  1.00 20.34           O  
ANISOU 1617  O   ALA A 210     2036   3353   2338   -462   -555    109       O  
ATOM   1618  CB  ALA A 210       6.215   9.317 -11.806  1.00 17.36           C  
ANISOU 1618  CB  ALA A 210     1643   2963   1991   -372   -467     21       C  
ATOM   1619  N   ALA A 211       5.232  12.131 -12.870  1.00 18.12           N  
ANISOU 1619  N   ALA A 211     1675   3098   2112   -380   -480     83       N  
ATOM   1620  CA  ALA A 211       4.152  13.088 -13.049  1.00 18.70           C  
ANISOU 1620  CA  ALA A 211     1704   3192   2208   -391   -501    137       C  
ATOM   1621  C   ALA A 211       4.082  13.519 -14.523  1.00 18.92           C  
ANISOU 1621  C   ALA A 211     1768   3215   2204   -427   -523    148       C  
ATOM   1622  O   ALA A 211       3.002  13.520 -15.097  1.00 19.19           O  
ANISOU 1622  O   ALA A 211     1796   3257   2237   -468   -569    199       O  
ATOM   1623  CB  ALA A 211       4.359  14.292 -12.143  1.00 18.96           C  
ANISOU 1623  CB  ALA A 211     1688   3239   2278   -343   -462    136       C  
ATOM   1624  N   VAL A 212       5.217  13.804 -15.150  1.00 19.08           N  
ANISOU 1624  N   VAL A 212     1826   3223   2200   -414   -492    106       N  
ATOM   1625  CA  VAL A 212       5.239  14.198 -16.572  1.00 20.74           C  
ANISOU 1625  CA  VAL A 212     2079   3426   2375   -444   -507    113       C  
ATOM   1626  C   VAL A 212       4.660  13.090 -17.446  1.00 23.15           C  
ANISOU 1626  C   VAL A 212     2454   3710   2633   -501   -558    126       C  
ATOM   1627  O   VAL A 212       3.743  13.343 -18.212  1.00 24.10           O  
ANISOU 1627  O   VAL A 212     2579   3835   2742   -545   -606    171       O  
ATOM   1628  CB  VAL A 212       6.648  14.616 -17.044  1.00 20.87           C  
ANISOU 1628  CB  VAL A 212     2126   3430   2375   -415   -457     69       C  
ATOM   1629  CG1 VAL A 212       6.673  14.873 -18.551  1.00 20.85           C  
ANISOU 1629  CG1 VAL A 212     2180   3415   2327   -445   -469     76       C  
ATOM   1630  CG2 VAL A 212       7.116  15.847 -16.305  1.00 20.75           C  
ANISOU 1630  CG2 VAL A 212     2048   3433   2404   -373   -423     66       C  
ATOM   1631  N   ILE A 213       5.107  11.837 -17.225  1.00 24.26           N  
ANISOU 1631  N   ILE A 213     2645   3825   2748   -501   -552     94       N  
ATOM   1632  CA  ILE A 213       4.648  10.620 -17.918  1.00 25.71           C  
ANISOU 1632  CA  ILE A 213     2911   3978   2880   -554   -599     99       C  
ATOM   1633  C   ILE A 213       3.128  10.446 -17.789  1.00 27.38           C  
ANISOU 1633  C   ILE A 213     3086   4204   3111   -606   -673    165       C  
ATOM   1634  O   ILE A 213       2.483   9.919 -18.700  1.00 28.18           O  
ANISOU 1634  O   ILE A 213     3250   4285   3171   -670   -734    192       O  
ATOM   1635  CB  ILE A 213       5.395   9.414 -17.264  1.00 26.26           C  
ANISOU 1635  CB  ILE A 213     3016   4023   2939   -529   -568     56       C  
ATOM   1636  CG1 ILE A 213       6.881   9.396 -17.668  1.00 26.31           C  
ANISOU 1636  CG1 ILE A 213     3072   4006   2918   -486   -499      5       C  
ATOM   1637  CG2 ILE A 213       4.714   8.051 -17.543  1.00 26.88           C  
ANISOU 1637  CG2 ILE A 213     3167   4071   2977   -583   -624     67       C  
ATOM   1638  CD1 ILE A 213       7.720   8.459 -16.914  1.00 26.39           C  
ANISOU 1638  CD1 ILE A 213     3094   4000   2933   -449   -457    -30       C  
ATOM   1639  N   ASN A 214       2.560  10.871 -16.651  1.00 27.56           N  
ANISOU 1639  N   ASN A 214     3014   4262   3197   -581   -667    196       N  
ATOM   1640  CA  ASN A 214       1.148  10.696 -16.380  1.00 28.45           C  
ANISOU 1640  CA  ASN A 214     3078   4392   3341   -620   -726    269       C  
ATOM   1641  C   ASN A 214       0.267  11.916 -16.608  1.00 29.23           C  
ANISOU 1641  C   ASN A 214     3106   4522   3477   -626   -743    336       C  
ATOM   1642  O   ASN A 214      -0.898  11.865 -16.248  1.00 30.34           O  
ANISOU 1642  O   ASN A 214     3188   4682   3656   -647   -781    409       O  
ATOM   1643  CB  ASN A 214       0.948  10.149 -14.980  1.00 29.24           C  
ANISOU 1643  CB  ASN A 214     3126   4504   3482   -588   -710    272       C  
ATOM   1644  CG  ASN A 214       1.290   8.685 -14.974  1.00 31.00           C  
ANISOU 1644  CG  ASN A 214     3420   4694   3666   -611   -727    238       C  
ATOM   1645  OD1 ASN A 214       0.511   7.856 -15.444  1.00 32.16           O  
ANISOU 1645  OD1 ASN A 214     3603   4825   3791   -673   -793    274       O  
ATOM   1646  ND2 ASN A 214       2.491   8.335 -14.530  1.00 30.29           N  
ANISOU 1646  ND2 ASN A 214     3358   4588   3562   -566   -671    169       N  
ATOM   1647  N   GLY A 215       0.788  12.971 -17.225  1.00 28.99           N  
ANISOU 1647  N   GLY A 215     3080   4496   3438   -608   -714    318       N  
ATOM   1648  CA  GLY A 215      -0.038  14.120 -17.571  1.00 28.65           C  
ANISOU 1648  CA  GLY A 215     2979   4480   3428   -616   -730    383       C  
ATOM   1649  C   GLY A 215       0.132  15.408 -16.811  1.00 28.34           C  
ANISOU 1649  C   GLY A 215     2868   4463   3437   -551   -670    384       C  
ATOM   1650  O   GLY A 215      -0.295  16.454 -17.303  1.00 28.51           O  
ANISOU 1650  O   GLY A 215     2857   4501   3476   -554   -673    425       O  
ATOM   1651  N   ASP A 216       0.717  15.359 -15.601  1.00 27.76           N  
ANISOU 1651  N   ASP A 216     2772   4390   3385   -495   -617    344       N  
ATOM   1652  CA AASP A 216       0.925  16.569 -14.801  0.50 27.85           C  
ANISOU 1652  CA AASP A 216     2734   4415   3435   -435   -562    341       C  
ATOM   1653  CA BASP A 216       0.912  16.580 -14.828  0.50 27.80           C  
ANISOU 1653  CA BASP A 216     2727   4408   3427   -435   -562    342       C  
ATOM   1654  C   ASP A 216       2.211  17.213 -15.268  1.00 27.90           C  
ANISOU 1654  C   ASP A 216     2777   4408   3415   -415   -527    279       C  
ATOM   1655  O   ASP A 216       3.284  16.670 -15.012  1.00 28.61           O  
ANISOU 1655  O   ASP A 216     2904   4483   3485   -400   -504    218       O  
ATOM   1656  CB AASP A 216       1.007  16.223 -13.308  0.50 29.39           C  
ANISOU 1656  CB AASP A 216     2901   4609   3656   -389   -527    327       C  
ATOM   1657  CB BASP A 216       0.864  16.297 -13.322  0.50 29.18           C  
ANISOU 1657  CB BASP A 216     2869   4585   3633   -390   -529    336       C  
ATOM   1658  CG AASP A 216      -0.257  16.547 -12.548  0.50 34.00           C  
ANISOU 1658  CG AASP A 216     3419   5212   4289   -370   -524    404       C  
ATOM   1659  CG BASP A 216      -0.454  15.707 -12.854  0.50 33.78           C  
ANISOU 1659  CG BASP A 216     3407   5182   4248   -405   -559    409       C  
ATOM   1660  OD1AASP A 216      -0.929  17.535 -12.910  0.50 35.12           O  
ANISOU 1660  OD1AASP A 216     3524   5367   4454   -366   -522    460       O  
ATOM   1661  OD1BASP A 216      -1.461  15.819 -13.595  0.50 34.54           O  
ANISOU 1661  OD1BASP A 216     3477   5290   4355   -445   -603    481       O  
ATOM   1662  OD2AASP A 216      -0.575  15.813 -11.591  0.50 36.00           O  
ANISOU 1662  OD2AASP A 216     3655   5466   4558   -356   -519    413       O  
ATOM   1663  OD2BASP A 216      -0.484  15.131 -11.755  0.50 35.62           O  
ANISOU 1663  OD2BASP A 216     3625   5412   4495   -378   -540    401       O  
ATOM   1664  N   ARG A 217       2.111  18.323 -16.017  1.00 26.79           N  
ANISOU 1664  N   ARG A 217     2626   4275   3277   -418   -525    299       N  
ATOM   1665  CA AARG A 217       3.259  18.985 -16.630  0.50 26.66           C  
ANISOU 1665  CA AARG A 217     2643   4250   3238   -406   -496    251       C  
ATOM   1666  CA BARG A 217       3.306  18.971 -16.551  0.50 26.93           C  
ANISOU 1666  CA BARG A 217     2677   4283   3274   -403   -494    249       C  
ATOM   1667  C   ARG A 217       3.374  20.479 -16.301  1.00 26.08           C  
ANISOU 1667  C   ARG A 217     2530   4183   3195   -366   -460    261       C  
ATOM   1668  O   ARG A 217       4.309  21.121 -16.766  1.00 25.94           O  
ANISOU 1668  O   ARG A 217     2533   4160   3165   -357   -439    228       O  
ATOM   1669  CB AARG A 217       3.156  18.860 -18.166  0.50 27.80           C  
ANISOU 1669  CB AARG A 217     2833   4388   3341   -457   -533    262       C  
ATOM   1670  CB BARG A 217       3.458  18.671 -18.056  0.50 28.84           C  
ANISOU 1670  CB BARG A 217     2975   4516   3468   -451   -526    246       C  
ATOM   1671  CG AARG A 217       2.491  17.582 -18.675  0.50 29.95           C  
ANISOU 1671  CG AARG A 217     3146   4651   3583   -512   -590    283       C  
ATOM   1672  CG BARG A 217       3.699  17.195 -18.366  0.50 32.07           C  
ANISOU 1672  CG BARG A 217     3448   4903   3834   -482   -549    219       C  
ATOM   1673  CD AARG A 217       2.168  17.681 -20.159  0.50 31.77           C  
ANISOU 1673  CD AARG A 217     3424   4875   3773   -567   -635    308       C  
ATOM   1674  CD BARG A 217       3.761  16.909 -19.855  0.50 34.95           C  
ANISOU 1674  CD BARG A 217     3886   5250   4143   -530   -580    219       C  
ATOM   1675  NE AARG A 217       3.307  18.172 -20.927  0.50 33.25           N  
ANISOU 1675  NE AARG A 217     3657   5049   3926   -551   -598    261       N  
ATOM   1676  NE BARG A 217       3.694  15.474 -20.125  0.50 36.93           N  
ANISOU 1676  NE BARG A 217     4207   5474   4349   -566   -610    205       N  
ATOM   1677  CZ AARG A 217       4.215  17.380 -21.479  0.50 34.81           C  
ANISOU 1677  CZ AARG A 217     3936   5218   4072   -556   -583    211       C  
ATOM   1678  CZ BARG A 217       2.679  14.891 -20.749  0.50 38.71           C  
ANISOU 1678  CZ BARG A 217     4464   5692   4550   -629   -679    249       C  
ATOM   1679  NH1AARG A 217       4.114  16.064 -21.363  0.50 34.39           N  
ANISOU 1679  NH1AARG A 217     3933   5143   3990   -578   -605    198       N  
ATOM   1680  NH1BARG A 217       1.650  15.611 -21.167  0.50 38.43           N  
ANISOU 1680  NH1BARG A 217     4387   5678   4535   -662   -723    314       N  
ATOM   1681  NH2AARG A 217       5.231  17.898 -22.157  0.50 34.77           N  
ANISOU 1681  NH2AARG A 217     3965   5203   4044   -535   -543    178       N  
ATOM   1682  NH2BARG A 217       2.683  13.580 -20.953  0.50 38.15           N  
ANISOU 1682  NH2BARG A 217     4470   5592   4436   -662   -707    232       N  
ATOM   1683  N   TRP A 218       2.418  21.051 -15.558  1.00 24.80           N  
ANISOU 1683  N   TRP A 218     2317   4033   3072   -343   -452    310       N  
ATOM   1684  CA  TRP A 218       2.423  22.488 -15.275  1.00 24.24           C  
ANISOU 1684  CA  TRP A 218     2221   3963   3026   -305   -416    323       C  
ATOM   1685  C   TRP A 218       3.731  23.024 -14.684  1.00 23.25           C  
ANISOU 1685  C   TRP A 218     2120   3820   2895   -270   -377    261       C  
ATOM   1686  O   TRP A 218       4.051  24.189 -14.869  1.00 23.40           O  
ANISOU 1686  O   TRP A 218     2137   3833   2920   -254   -358    260       O  
ATOM   1687  CB  TRP A 218       1.239  22.880 -14.382  1.00 24.27           C  
ANISOU 1687  CB  TRP A 218     2176   3975   3071   -273   -399    386       C  
ATOM   1688  CG  TRP A 218       1.295  22.309 -12.991  1.00 24.31           C  
ANISOU 1688  CG  TRP A 218     2181   3970   3086   -238   -374    368       C  
ATOM   1689  CD1 TRP A 218       0.672  21.185 -12.547  1.00 25.07           C  
ANISOU 1689  CD1 TRP A 218     2261   4073   3189   -250   -394    390       C  
ATOM   1690  CD2 TRP A 218       1.995  22.857 -11.858  1.00 24.11           C  
ANISOU 1690  CD2 TRP A 218     2174   3923   3062   -190   -329    327       C  
ATOM   1691  NE1 TRP A 218       0.921  21.005 -11.206  1.00 25.33           N  
ANISOU 1691  NE1 TRP A 218     2300   4093   3230   -207   -359    366       N  
ATOM   1692  CE2 TRP A 218       1.758  22.000 -10.767  1.00 24.83           C  
ANISOU 1692  CE2 TRP A 218     2263   4012   3161   -172   -321    325       C  
ATOM   1693  CE3 TRP A 218       2.795  23.992 -11.660  1.00 24.40           C  
ANISOU 1693  CE3 TRP A 218     2236   3942   3094   -163   -300    294       C  
ATOM   1694  CZ2 TRP A 218       2.307  22.229  -9.506  1.00 25.19           C  
ANISOU 1694  CZ2 TRP A 218     2333   4034   3203   -130   -286    289       C  
ATOM   1695  CZ3 TRP A 218       3.354  24.205 -10.414  1.00 25.01           C  
ANISOU 1695  CZ3 TRP A 218     2340   3994   3169   -127   -270    260       C  
ATOM   1696  CH2 TRP A 218       3.094  23.341  -9.352  1.00 25.04           C  
ANISOU 1696  CH2 TRP A 218     2344   3994   3175   -110   -263    258       C  
ATOM   1697  N   PHE A 219       4.452  22.197 -13.945  1.00 22.71           N  
ANISOU 1697  N   PHE A 219     2071   3740   2817   -261   -370    216       N  
ATOM   1698  CA  PHE A 219       5.682  22.611 -13.274  1.00 23.09           C  
ANISOU 1698  CA  PHE A 219     2138   3770   2865   -235   -342    167       C  
ATOM   1699  C   PHE A 219       6.901  22.679 -14.188  1.00 23.98           C  
ANISOU 1699  C   PHE A 219     2275   3879   2958   -251   -342    132       C  
ATOM   1700  O   PHE A 219       7.960  23.116 -13.742  1.00 24.57           O  
ANISOU 1700  O   PHE A 219     2358   3940   3037   -235   -325    103       O  
ATOM   1701  CB  PHE A 219       5.963  21.702 -12.076  1.00 22.48           C  
ANISOU 1701  CB  PHE A 219     2067   3684   2790   -219   -336    141       C  
ATOM   1702  CG  PHE A 219       6.094  20.259 -12.476  1.00 22.16           C  
ANISOU 1702  CG  PHE A 219     2041   3649   2731   -247   -357    126       C  
ATOM   1703  CD1 PHE A 219       7.317  19.734 -12.853  1.00 22.46           C  
ANISOU 1703  CD1 PHE A 219     2106   3677   2750   -255   -353     84       C  
ATOM   1704  CD2 PHE A 219       4.996  19.416 -12.460  1.00 22.30           C  
ANISOU 1704  CD2 PHE A 219     2047   3677   2751   -264   -381    159       C  
ATOM   1705  CE1 PHE A 219       7.424  18.413 -13.257  1.00 22.95           C  
ANISOU 1705  CE1 PHE A 219     2193   3737   2790   -276   -366     70       C  
ATOM   1706  CE2 PHE A 219       5.117  18.101 -12.849  1.00 22.53           C  
ANISOU 1706  CE2 PHE A 219     2100   3704   2757   -292   -403    144       C  
ATOM   1707  CZ  PHE A 219       6.328  17.606 -13.242  1.00 22.16           C  
ANISOU 1707  CZ  PHE A 219     2091   3644   2687   -297   -393     97       C  
ATOM   1708  N   LEU A 220       6.784  22.197 -15.433  1.00 23.80           N  
ANISOU 1708  N   LEU A 220     2268   3864   2911   -284   -362    139       N  
ATOM   1709  CA  LEU A 220       7.885  22.269 -16.374  1.00 24.27           C  
ANISOU 1709  CA  LEU A 220     2354   3917   2949   -293   -352    113       C  
ATOM   1710  C   LEU A 220       8.104  23.721 -16.758  1.00 25.44           C  
ANISOU 1710  C   LEU A 220     2489   4067   3111   -285   -340    125       C  
ATOM   1711  O   LEU A 220       7.150  24.434 -17.092  1.00 25.60           O  
ANISOU 1711  O   LEU A 220     2491   4097   3139   -291   -351    162       O  
ATOM   1712  CB  LEU A 220       7.599  21.410 -17.610  1.00 23.99           C  
ANISOU 1712  CB  LEU A 220     2356   3882   2876   -330   -374    118       C  
ATOM   1713  CG  LEU A 220       7.469  19.895 -17.364  1.00 24.30           C  
ANISOU 1713  CG  LEU A 220     2423   3913   2896   -343   -388    104       C  
ATOM   1714  CD1 LEU A 220       7.202  19.143 -18.686  1.00 24.14           C  
ANISOU 1714  CD1 LEU A 220     2460   3884   2829   -384   -414    110       C  
ATOM   1715  CD2 LEU A 220       8.686  19.338 -16.592  1.00 24.01           C  
ANISOU 1715  CD2 LEU A 220     2392   3864   2865   -315   -356     62       C  
ATOM   1716  N   ASN A 221       9.343  24.170 -16.648  1.00 26.24           N  
ANISOU 1716  N   ASN A 221     2594   4159   3219   -271   -319    100       N  
ATOM   1717  CA  ASN A 221       9.662  25.545 -16.964  1.00 27.65           C  
ANISOU 1717  CA  ASN A 221     2761   4335   3409   -264   -310    111       C  
ATOM   1718  C   ASN A 221      10.631  25.661 -18.144  1.00 27.59           C  
ANISOU 1718  C   ASN A 221     2770   4328   3387   -275   -299    104       C  
ATOM   1719  O   ASN A 221      11.007  24.662 -18.756  1.00 26.85           O  
ANISOU 1719  O   ASN A 221     2701   4233   3268   -284   -293     91       O  
ATOM   1720  CB  ASN A 221      10.140  26.285 -15.720  1.00 29.49           C  
ANISOU 1720  CB  ASN A 221     2985   4552   3667   -240   -301    101       C  
ATOM   1721  CG  ASN A 221      11.316  25.622 -15.077  1.00 34.55           C  
ANISOU 1721  CG  ASN A 221     3632   5183   4313   -235   -295     73       C  
ATOM   1722  OD1 ASN A 221      12.191  25.019 -15.734  1.00 36.00           O  
ANISOU 1722  OD1 ASN A 221     3820   5368   4488   -242   -286     63       O  
ATOM   1723  ND2 ASN A 221      11.350  25.717 -13.769  1.00 35.87           N  
ANISOU 1723  ND2 ASN A 221     3800   5335   4492   -221   -298     64       N  
ATOM   1724  N   ARG A 222      10.989  26.903 -18.476  1.00 28.15           N  
ANISOU 1724  N   ARG A 222     2828   4396   3470   -271   -292    115       N  
ATOM   1725  CA  ARG A 222      11.890  27.270 -19.559  1.00 28.53           C  
ANISOU 1725  CA  ARG A 222     2884   4446   3510   -277   -277    117       C  
ATOM   1726  C   ARG A 222      13.368  27.299 -19.125  1.00 27.81           C  
ANISOU 1726  C   ARG A 222     2783   4344   3440   -263   -258    106       C  
ATOM   1727  O   ARG A 222      14.201  27.809 -19.872  1.00 28.04           O  
ANISOU 1727  O   ARG A 222     2807   4373   3473   -263   -242    117       O  
ATOM   1728  CB  ARG A 222      11.504  28.683 -20.042  1.00 30.75           C  
ANISOU 1728  CB  ARG A 222     3151   4731   3802   -280   -282    142       C  
ATOM   1729  CG  ARG A 222      10.011  28.867 -20.294  1.00 35.46           C  
ANISOU 1729  CG  ARG A 222     3743   5338   4391   -291   -302    168       C  
ATOM   1730  CD  ARG A 222       9.680  30.210 -20.921  1.00 39.65           C  
ANISOU 1730  CD  ARG A 222     4261   5873   4931   -293   -302    196       C  
ATOM   1731  NE  ARG A 222       8.450  30.126 -21.710  1.00 44.31           N  
ANISOU 1731  NE  ARG A 222     4849   6479   5508   -314   -324    230       N  
ATOM   1732  CZ  ARG A 222       8.397  29.762 -22.989  1.00 47.04           C  
ANISOU 1732  CZ  ARG A 222     5219   6833   5822   -342   -336    238       C  
ATOM   1733  NH1 ARG A 222       9.512  29.473 -23.652  1.00 46.89           N  
ANISOU 1733  NH1 ARG A 222     5229   6808   5781   -344   -317    214       N  
ATOM   1734  NH2 ARG A 222       7.229  29.696 -23.619  1.00 46.60           N  
ANISOU 1734  NH2 ARG A 222     5162   6790   5755   -368   -365    276       N  
ATOM   1735  N   PHE A 223      13.694  26.791 -17.938  1.00 26.82           N  
ANISOU 1735  N   PHE A 223     2650   4209   3329   -253   -262     90       N  
ATOM   1736  CA  PHE A 223      15.037  26.911 -17.394  1.00 26.68           C  
ANISOU 1736  CA  PHE A 223     2616   4182   3339   -247   -254     91       C  
ATOM   1737  C   PHE A 223      15.810  25.609 -17.280  1.00 25.00           C  
ANISOU 1737  C   PHE A 223     2406   3968   3124   -238   -236     82       C  
ATOM   1738  O   PHE A 223      15.251  24.512 -17.324  1.00 24.52           O  
ANISOU 1738  O   PHE A 223     2366   3910   3040   -236   -232     66       O  
ATOM   1739  CB  PHE A 223      14.990  27.599 -16.003  1.00 28.09           C  
ANISOU 1739  CB  PHE A 223     2788   4345   3540   -245   -278     87       C  
ATOM   1740  CG  PHE A 223      13.940  28.675 -15.805  1.00 30.09           C  
ANISOU 1740  CG  PHE A 223     3050   4592   3789   -244   -290     94       C  
ATOM   1741  CD1 PHE A 223      13.733  29.653 -16.765  1.00 31.87           C  
ANISOU 1741  CD1 PHE A 223     3272   4823   4013   -249   -286    112       C  
ATOM   1742  CD2 PHE A 223      13.192  28.728 -14.649  1.00 31.51           C  
ANISOU 1742  CD2 PHE A 223     3244   4760   3970   -233   -299     86       C  
ATOM   1743  CE1 PHE A 223      12.769  30.635 -16.588  1.00 33.01           C  
ANISOU 1743  CE1 PHE A 223     3423   4960   4158   -244   -291    123       C  
ATOM   1744  CE2 PHE A 223      12.245  29.724 -14.462  1.00 32.90           C  
ANISOU 1744  CE2 PHE A 223     3431   4926   4144   -224   -299     99       C  
ATOM   1745  CZ  PHE A 223      12.048  30.678 -15.430  1.00 33.03           C  
ANISOU 1745  CZ  PHE A 223     3440   4948   4162   -229   -294    118       C  
ATOM   1746  N   THR A 224      17.112  25.747 -17.111  1.00 23.53           N  
ANISOU 1746  N   THR A 224     2196   3777   2967   -233   -225     97       N  
ATOM   1747  CA  THR A 224      17.996  24.646 -16.810  1.00 23.24           C  
ANISOU 1747  CA  THR A 224     2152   3737   2941   -220   -204     99       C  
ATOM   1748  C   THR A 224      18.926  25.100 -15.659  1.00 23.06           C  
ANISOU 1748  C   THR A 224     2096   3706   2962   -227   -228    116       C  
ATOM   1749  O   THR A 224      18.833  26.241 -15.193  1.00 23.39           O  
ANISOU 1749  O   THR A 224     2132   3739   3016   -242   -259    122       O  
ATOM   1750  CB  THR A 224      18.699  24.121 -18.047  1.00 24.19           C  
ANISOU 1750  CB  THR A 224     2281   3860   3049   -204   -157    115       C  
ATOM   1751  OG1 THR A 224      19.188  22.815 -17.719  1.00 24.88           O  
ANISOU 1751  OG1 THR A 224     2374   3942   3138   -186   -133    111       O  
ATOM   1752  CG2 THR A 224      19.847  25.021 -18.474  1.00 24.72           C  
ANISOU 1752  CG2 THR A 224     2312   3928   3151   -201   -142    156       C  
ATOM   1753  N   THR A 225      19.756  24.196 -15.139  1.00 22.41           N  
ANISOU 1753  N   THR A 225     1996   3620   2899   -218   -218    126       N  
ATOM   1754  CA  THR A 225      20.677  24.528 -14.060  1.00 22.49           C  
ANISOU 1754  CA  THR A 225     1975   3621   2950   -231   -248    150       C  
ATOM   1755  C   THR A 225      21.917  23.610 -14.156  1.00 21.91           C  
ANISOU 1755  C   THR A 225     1867   3551   2907   -215   -216    185       C  
ATOM   1756  O   THR A 225      22.086  22.901 -15.140  1.00 21.54           O  
ANISOU 1756  O   THR A 225     1827   3510   2846   -189   -165    190       O  
ATOM   1757  CB  THR A 225      19.930  24.503 -12.689  1.00 24.68           C  
ANISOU 1757  CB  THR A 225     2275   3886   3216   -243   -289    119       C  
ATOM   1758  OG1 THR A 225      20.837  24.957 -11.691  1.00 25.83           O  
ANISOU 1758  OG1 THR A 225     2401   4017   3395   -264   -327    145       O  
ATOM   1759  CG2 THR A 225      19.438  23.125 -12.334  1.00 25.53           C  
ANISOU 1759  CG2 THR A 225     2397   3999   3305   -227   -274     92       C  
ATOM   1760  N   THR A 226      22.828  23.707 -13.195  1.00 21.65           N  
ANISOU 1760  N   THR A 226     1800   3511   2916   -230   -246    216       N  
ATOM   1761  CA  THR A 226      24.004  22.869 -13.107  1.00 21.29           C  
ANISOU 1761  CA  THR A 226     1712   3470   2909   -215   -220    261       C  
ATOM   1762  C   THR A 226      23.893  22.125 -11.789  1.00 21.30           C  
ANISOU 1762  C   THR A 226     1717   3464   2913   -223   -251    244       C  
ATOM   1763  O   THR A 226      23.188  22.585 -10.891  1.00 21.51           O  
ANISOU 1763  O   THR A 226     1772   3479   2920   -246   -299    211       O  
ATOM   1764  CB  THR A 226      25.272  23.744 -13.112  1.00 21.49           C  
ANISOU 1764  CB  THR A 226     1681   3495   2991   -234   -239    331       C  
ATOM   1765  OG1 THR A 226      25.347  24.479 -11.888  1.00 21.51           O  
ANISOU 1765  OG1 THR A 226     1684   3481   3008   -278   -315    335       O  
ATOM   1766  CG2 THR A 226      25.325  24.682 -14.303  1.00 22.42           C  
ANISOU 1766  CG2 THR A 226     1795   3618   3106   -231   -218    348       C  
ATOM   1767  N   LEU A 227      24.651  21.045 -11.611  1.00 21.18           N  
ANISOU 1767  N   LEU A 227     1674   3452   2924   -204   -222    271       N  
ATOM   1768  CA  LEU A 227      24.656  20.305 -10.344  1.00 21.41           C  
ANISOU 1768  CA  LEU A 227     1701   3474   2959   -212   -252    261       C  
ATOM   1769  C   LEU A 227      25.027  21.203  -9.167  1.00 22.24           C  
ANISOU 1769  C   LEU A 227     1795   3567   3089   -258   -329    282       C  
ATOM   1770  O   LEU A 227      24.344  21.176  -8.154  1.00 22.93           O  
ANISOU 1770  O   LEU A 227     1919   3642   3151   -274   -368    243       O  
ATOM   1771  CB  LEU A 227      25.631  19.119 -10.402  1.00 21.79           C  
ANISOU 1771  CB  LEU A 227     1710   3528   3042   -183   -207    304       C  
ATOM   1772  CG  LEU A 227      25.062  17.744 -10.752  1.00 24.48           C  
ANISOU 1772  CG  LEU A 227     2088   3868   3347   -145   -152    265       C  
ATOM   1773  CD1 LEU A 227      26.086  16.660 -10.447  1.00 25.50           C  
ANISOU 1773  CD1 LEU A 227     2177   3996   3516   -120   -118    312       C  
ATOM   1774  CD2 LEU A 227      23.723  17.461 -10.020  1.00 25.10           C  
ANISOU 1774  CD2 LEU A 227     2218   3942   3378   -159   -188    195       C  
ATOM   1775  N   ASN A 228      26.064  22.044  -9.320  1.00 22.05           N  
ANISOU 1775  N   ASN A 228     1727   3541   3110   -281   -351    345       N  
ATOM   1776  CA  ASN A 228      26.476  22.943  -8.248  1.00 22.25           C  
ANISOU 1776  CA  ASN A 228     1753   3548   3155   -333   -433    369       C  
ATOM   1777  C   ASN A 228      25.433  24.031  -7.950  1.00 23.10           C  
ANISOU 1777  C   ASN A 228     1928   3636   3214   -354   -472    316       C  
ATOM   1778  O   ASN A 228      25.187  24.324  -6.771  1.00 23.68           O  
ANISOU 1778  O   ASN A 228     2042   3684   3270   -384   -529    298       O  
ATOM   1779  CB  ASN A 228      27.860  23.544  -8.520  1.00 22.85           C  
ANISOU 1779  CB  ASN A 228     1761   3626   3294   -357   -453    460       C  
ATOM   1780  CG  ASN A 228      29.012  22.549  -8.475  1.00 25.98           C  
ANISOU 1780  CG  ASN A 228     2085   4036   3749   -341   -426    531       C  
ATOM   1781  OD1 ASN A 228      30.045  22.730  -9.137  1.00 29.25           O  
ANISOU 1781  OD1 ASN A 228     2433   4462   4217   -335   -402    610       O  
ATOM   1782  ND2 ASN A 228      28.888  21.485  -7.701  1.00 24.27           N  
ANISOU 1782  ND2 ASN A 228     1875   3819   3527   -331   -424    513       N  
ATOM   1783  N   ASP A 229      24.799  24.598  -8.988  1.00 22.80           N  
ANISOU 1783  N   ASP A 229     1906   3604   3151   -337   -439    291       N  
ATOM   1784  CA  ASP A 229      23.785  25.627  -8.761  1.00 23.90           C  
ANISOU 1784  CA  ASP A 229     2106   3725   3250   -350   -466    248       C  
ATOM   1785  C   ASP A 229      22.560  25.004  -8.094  1.00 23.41           C  
ANISOU 1785  C   ASP A 229     2095   3659   3143   -332   -458    187       C  
ATOM   1786  O   ASP A 229      22.055  25.537  -7.110  1.00 23.96           O  
ANISOU 1786  O   ASP A 229     2214   3701   3187   -348   -497    164       O  
ATOM   1787  CB  ASP A 229      23.376  26.369 -10.049  1.00 26.78           C  
ANISOU 1787  CB  ASP A 229     2472   4101   3603   -336   -433    242       C  
ATOM   1788  CG  ASP A 229      22.298  27.397  -9.770  1.00 32.66           C  
ANISOU 1788  CG  ASP A 229     3277   4826   4308   -345   -455    202       C  
ATOM   1789  OD1 ASP A 229      22.561  28.325  -8.981  1.00 34.35           O  
ANISOU 1789  OD1 ASP A 229     3518   5008   4523   -379   -509    214       O  
ATOM   1790  OD2 ASP A 229      21.171  27.234 -10.286  1.00 34.80           O  
ANISOU 1790  OD2 ASP A 229     3571   5107   4545   -318   -421    163       O  
ATOM   1791  N   PHE A 230      22.141  23.841  -8.576  1.00 22.01           N  
ANISOU 1791  N   PHE A 230     1906   3503   2954   -298   -409    165       N  
ATOM   1792  CA  PHE A 230      21.030  23.120  -8.001  1.00 21.64           C  
ANISOU 1792  CA  PHE A 230     1897   3455   2871   -281   -401    118       C  
ATOM   1793  C   PHE A 230      21.300  22.806  -6.513  1.00 21.78           C  
ANISOU 1793  C   PHE A 230     1929   3454   2893   -298   -443    118       C  
ATOM   1794  O   PHE A 230      20.462  23.104  -5.674  1.00 22.40           O  
ANISOU 1794  O   PHE A 230     2057   3514   2940   -300   -463     87       O  
ATOM   1795  CB  PHE A 230      20.728  21.818  -8.790  1.00 20.45           C  
ANISOU 1795  CB  PHE A 230     1732   3326   2710   -249   -347    103       C  
ATOM   1796  CG  PHE A 230      19.600  21.080  -8.115  1.00 20.23           C  
ANISOU 1796  CG  PHE A 230     1738   3298   2651   -237   -348     61       C  
ATOM   1797  CD1 PHE A 230      18.287  21.475  -8.301  1.00 20.75           C  
ANISOU 1797  CD1 PHE A 230     1837   3364   2684   -231   -344     33       C  
ATOM   1798  CD2 PHE A 230      19.860  20.081  -7.191  1.00 20.00           C  
ANISOU 1798  CD2 PHE A 230     1704   3266   2630   -235   -355     58       C  
ATOM   1799  CE1 PHE A 230      17.261  20.861  -7.612  1.00 20.36           C  
ANISOU 1799  CE1 PHE A 230     1811   3314   2612   -220   -345      6       C  
ATOM   1800  CE2 PHE A 230      18.834  19.491  -6.489  1.00 19.81           C  
ANISOU 1800  CE2 PHE A 230     1709   3239   2578   -226   -358     25       C  
ATOM   1801  CZ  PHE A 230      17.541  19.879  -6.708  1.00 19.58           C  
ANISOU 1801  CZ  PHE A 230     1709   3212   2519   -218   -352      1       C  
ATOM   1802  N   ASN A 231      22.488  22.288  -6.204  1.00 21.69           N  
ANISOU 1802  N   ASN A 231     1875   3445   2920   -311   -456    158       N  
ATOM   1803  CA  ASN A 231      22.847  21.888  -4.853  1.00 22.54           C  
ANISOU 1803  CA  ASN A 231     1994   3537   3035   -331   -499    165       C  
ATOM   1804  C   ASN A 231      22.899  23.044  -3.855  1.00 23.34           C  
ANISOU 1804  C   ASN A 231     2145   3602   3122   -371   -566    168       C  
ATOM   1805  O   ASN A 231      22.641  22.815  -2.678  1.00 23.39           O  
ANISOU 1805  O   ASN A 231     2194   3588   3107   -382   -596    150       O  
ATOM   1806  CB  ASN A 231      24.134  21.056  -4.842  1.00 22.98           C  
ANISOU 1806  CB  ASN A 231     1984   3605   3141   -334   -496    219       C  
ATOM   1807  CG  ASN A 231      23.901  19.643  -5.317  1.00 23.99           C  
ANISOU 1807  CG  ASN A 231     2092   3755   3268   -292   -434    203       C  
ATOM   1808  OD1 ASN A 231      22.778  19.158  -5.359  1.00 23.55           O  
ANISOU 1808  OD1 ASN A 231     2073   3702   3172   -270   -411    150       O  
ATOM   1809  ND2 ASN A 231      24.948  18.929  -5.685  1.00 24.66           N  
ANISOU 1809  ND2 ASN A 231     2120   3853   3396   -279   -406    252       N  
ATOM   1810  N   LEU A 232      23.117  24.284  -4.319  1.00 23.45           N  
ANISOU 1810  N   LEU A 232     2167   3603   3139   -392   -585    186       N  
ATOM   1811  CA  LEU A 232      23.059  25.450  -3.437  1.00 23.96           C  
ANISOU 1811  CA  LEU A 232     2299   3625   3180   -430   -646    184       C  
ATOM   1812  C   LEU A 232      21.614  25.617  -2.956  1.00 24.67           C  
ANISOU 1812  C   LEU A 232     2464   3696   3212   -401   -625    123       C  
ATOM   1813  O   LEU A 232      21.386  25.829  -1.767  1.00 25.56           O  
ANISOU 1813  O   LEU A 232     2645   3773   3294   -416   -660    109       O  
ATOM   1814  CB  LEU A 232      23.480  26.707  -4.199  1.00 24.23           C  
ANISOU 1814  CB  LEU A 232     2326   3651   3229   -452   -662    212       C  
ATOM   1815  CG  LEU A 232      24.941  26.842  -4.584  1.00 25.39           C  
ANISOU 1815  CG  LEU A 232     2402   3809   3437   -486   -691    286       C  
ATOM   1816  CD1 LEU A 232      25.180  28.212  -5.173  1.00 26.16           C  
ANISOU 1816  CD1 LEU A 232     2508   3891   3540   -511   -714    309       C  
ATOM   1817  CD2 LEU A 232      25.862  26.635  -3.379  1.00 26.07           C  
ANISOU 1817  CD2 LEU A 232     2489   3872   3543   -534   -763    328       C  
ATOM   1818  N   VAL A 233      20.647  25.457  -3.870  1.00 24.50           N  
ANISOU 1818  N   VAL A 233     2432   3701   3177   -361   -566     95       N  
ATOM   1819  CA  VAL A 233      19.219  25.495  -3.580  1.00 24.45           C  
ANISOU 1819  CA  VAL A 233     2477   3686   3127   -328   -537     52       C  
ATOM   1820  C   VAL A 233      18.809  24.307  -2.695  1.00 23.80           C  
ANISOU 1820  C   VAL A 233     2403   3608   3033   -310   -528     31       C  
ATOM   1821  O   VAL A 233      18.117  24.496  -1.692  1.00 23.56           O  
ANISOU 1821  O   VAL A 233     2436   3550   2967   -301   -534     10       O  
ATOM   1822  CB  VAL A 233      18.420  25.529  -4.896  1.00 25.63           C  
ANISOU 1822  CB  VAL A 233     2597   3867   3275   -298   -485     41       C  
ATOM   1823  CG1 VAL A 233      16.916  25.458  -4.633  1.00 26.12           C  
ANISOU 1823  CG1 VAL A 233     2697   3926   3303   -263   -454     11       C  
ATOM   1824  CG2 VAL A 233      18.779  26.773  -5.700  1.00 26.36           C  
ANISOU 1824  CG2 VAL A 233     2686   3952   3377   -314   -494     61       C  
ATOM   1825  N   ALA A 234      19.270  23.099  -3.029  1.00 23.45           N  
ANISOU 1825  N   ALA A 234     2300   3595   3015   -304   -512     39       N  
ATOM   1826  CA  ALA A 234      18.960  21.914  -2.229  1.00 24.93           C  
ANISOU 1826  CA  ALA A 234     2491   3788   3194   -290   -505     22       C  
ATOM   1827  C   ALA A 234      19.485  22.051  -0.783  1.00 25.54           C  
ANISOU 1827  C   ALA A 234     2611   3830   3262   -317   -557     29       C  
ATOM   1828  O   ALA A 234      18.857  21.562   0.145  1.00 25.87           O  
ANISOU 1828  O   ALA A 234     2692   3860   3278   -303   -555      7       O  
ATOM   1829  CB  ALA A 234      19.546  20.668  -2.885  1.00 25.24           C  
ANISOU 1829  CB  ALA A 234     2465   3860   3265   -280   -479     36       C  
ATOM   1830  N   MET A 235      20.622  22.716  -0.595  1.00 25.61           N  
ANISOU 1830  N   MET A 235     2617   3821   3292   -359   -607     65       N  
ATOM   1831  CA  MET A 235      21.200  22.901   0.726  1.00 26.74           C  
ANISOU 1831  CA  MET A 235     2808   3927   3425   -397   -670     79       C  
ATOM   1832  C   MET A 235      20.260  23.762   1.581  1.00 25.57           C  
ANISOU 1832  C   MET A 235     2766   3733   3217   -391   -678     45       C  
ATOM   1833  O   MET A 235      19.943  23.390   2.708  1.00 25.10           O  
ANISOU 1833  O   MET A 235     2760   3650   3127   -388   -690     28       O  
ATOM   1834  CB  MET A 235      22.594  23.525   0.624  1.00 29.24           C  
ANISOU 1834  CB  MET A 235     3096   4233   3780   -450   -728    135       C  
ATOM   1835  CG  MET A 235      23.182  23.903   1.983  1.00 35.68           C  
ANISOU 1835  CG  MET A 235     3979   5001   4578   -503   -809    153       C  
ATOM   1836  SD  MET A 235      24.357  22.692   2.596  1.00 50.44           S  
ANISOU 1836  SD  MET A 235     5788   6885   6492   -532   -849    201       S  
ATOM   1837  CE  MET A 235      25.757  23.080   1.571  1.00 49.18           C  
ANISOU 1837  CE  MET A 235     5521   6755   6411   -560   -864    280       C  
ATOM   1838  N   LYS A 236      19.761  24.854   0.988  1.00 24.13           N  
ANISOU 1838  N   LYS A 236     2613   3538   3019   -382   -662     36       N  
ATOM   1839  CA  LYS A 236      18.863  25.809   1.616  1.00 23.87           C  
ANISOU 1839  CA  LYS A 236     2681   3458   2931   -368   -657     11       C  
ATOM   1840  C   LYS A 236      17.552  25.145   2.037  1.00 22.57           C  
ANISOU 1840  C   LYS A 236     2539   3300   2737   -314   -601    -22       C  
ATOM   1841  O   LYS A 236      17.023  25.448   3.106  1.00 22.60           O  
ANISOU 1841  O   LYS A 236     2634   3260   2695   -302   -601    -37       O  
ATOM   1842  CB  LYS A 236      18.601  26.970   0.632  1.00 26.74           C  
ANISOU 1842  CB  LYS A 236     3047   3818   3295   -363   -640     15       C  
ATOM   1843  CG  LYS A 236      17.566  27.993   1.094  1.00 32.52           C  
ANISOU 1843  CG  LYS A 236     3879   4503   3974   -335   -617     -7       C  
ATOM   1844  CD  LYS A 236      17.607  29.251   0.217  1.00 38.82           C  
ANISOU 1844  CD  LYS A 236     4683   5290   4776   -344   -616      4       C  
ATOM   1845  CE  LYS A 236      16.248  29.904   0.049  1.00 42.33           C  
ANISOU 1845  CE  LYS A 236     5174   5720   5189   -291   -556    -13       C  
ATOM   1846  NZ  LYS A 236      15.918  30.816   1.174  1.00 43.70           N  
ANISOU 1846  NZ  LYS A 236     5481   5819   5305   -286   -564    -24       N  
ATOM   1847  N   TYR A 237      17.043  24.223   1.215  1.00 21.19           N  
ANISOU 1847  N   TYR A 237     2287   3177   2587   -282   -553    -28       N  
ATOM   1848  CA  TYR A 237      15.758  23.580   1.504  1.00 20.57           C  
ANISOU 1848  CA  TYR A 237     2218   3110   2489   -234   -502    -49       C  
ATOM   1849  C   TYR A 237      15.857  22.216   2.211  1.00 20.43           C  
ANISOU 1849  C   TYR A 237     2179   3107   2477   -231   -505    -55       C  
ATOM   1850  O   TYR A 237      14.844  21.496   2.307  1.00 19.79           O  
ANISOU 1850  O   TYR A 237     2087   3043   2389   -194   -464    -66       O  
ATOM   1851  CB  TYR A 237      14.928  23.489   0.217  1.00 20.14           C  
ANISOU 1851  CB  TYR A 237     2106   3095   2451   -206   -454    -49       C  
ATOM   1852  CG  TYR A 237      14.428  24.857  -0.199  1.00 21.25           C  
ANISOU 1852  CG  TYR A 237     2284   3214   2576   -195   -440    -44       C  
ATOM   1853  CD1 TYR A 237      13.278  25.397   0.362  1.00 22.19           C  
ANISOU 1853  CD1 TYR A 237     2464   3305   2662   -157   -404    -48       C  
ATOM   1854  CD2 TYR A 237      15.162  25.654  -1.073  1.00 22.03           C  
ANISOU 1854  CD2 TYR A 237     2362   3315   2692   -223   -460    -31       C  
ATOM   1855  CE1 TYR A 237      12.850  26.678   0.040  1.00 23.05           C  
ANISOU 1855  CE1 TYR A 237     2613   3390   2757   -144   -388    -40       C  
ATOM   1856  CE2 TYR A 237      14.751  26.939  -1.393  1.00 23.16           C  
ANISOU 1856  CE2 TYR A 237     2545   3434   2821   -215   -449    -26       C  
ATOM   1857  CZ  TYR A 237      13.590  27.450  -0.834  1.00 24.32           C  
ANISOU 1857  CZ  TYR A 237     2754   3553   2934   -175   -413    -32       C  
ATOM   1858  OH  TYR A 237      13.142  28.712  -1.158  1.00 26.06           O  
ANISOU 1858  OH  TYR A 237     3013   3747   3140   -161   -395    -24       O  
ATOM   1859  N   ASN A 238      17.036  21.897   2.763  1.00 20.02           N  
ANISOU 1859  N   ASN A 238     2123   3046   2439   -270   -555    -42       N  
ATOM   1860  CA  ASN A 238      17.279  20.639   3.459  1.00 21.14           C  
ANISOU 1860  CA  ASN A 238     2244   3200   2590   -271   -563    -44       C  
ATOM   1861  C   ASN A 238      16.982  19.430   2.583  1.00 20.92           C  
ANISOU 1861  C   ASN A 238     2134   3223   2592   -246   -522    -48       C  
ATOM   1862  O   ASN A 238      16.291  18.515   3.002  1.00 22.02           O  
ANISOU 1862  O   ASN A 238     2272   3373   2723   -221   -498    -62       O  
ATOM   1863  CB  ASN A 238      16.559  20.557   4.814  1.00 23.72           C  
ANISOU 1863  CB  ASN A 238     2651   3492   2870   -252   -561    -62       C  
ATOM   1864  CG  ASN A 238      17.145  21.486   5.855  1.00 28.62           C  
ANISOU 1864  CG  ASN A 238     3365   4054   3455   -288   -616    -56       C  
ATOM   1865  OD1 ASN A 238      16.435  22.303   6.448  1.00 32.47           O  
ANISOU 1865  OD1 ASN A 238     3946   4497   3893   -269   -602    -69       O  
ATOM   1866  ND2 ASN A 238      18.434  21.388   6.094  1.00 27.71           N  
ANISOU 1866  ND2 ASN A 238     3233   3934   3363   -340   -679    -31       N  
ATOM   1867  N   TYR A 239      17.417  19.493   1.335  1.00 19.29           N  
ANISOU 1867  N   TYR A 239     1870   3044   2417   -252   -510    -35       N  
ATOM   1868  CA  TYR A 239      17.323  18.416   0.361  1.00 19.05           C  
ANISOU 1868  CA  TYR A 239     1774   3053   2410   -235   -474    -37       C  
ATOM   1869  C   TYR A 239      18.707  17.797   0.289  1.00 19.28           C  
ANISOU 1869  C   TYR A 239     1755   3092   2478   -257   -494     -9       C  
ATOM   1870  O   TYR A 239      19.717  18.502   0.455  1.00 18.55           O  
ANISOU 1870  O   TYR A 239     1661   2985   2403   -289   -533     19       O  
ATOM   1871  CB  TYR A 239      16.983  18.973  -1.031  1.00 18.49           C  
ANISOU 1871  CB  TYR A 239     1681   3000   2344   -226   -447    -35       C  
ATOM   1872  CG  TYR A 239      15.511  18.919  -1.353  1.00 18.27           C  
ANISOU 1872  CG  TYR A 239     1667   2982   2293   -197   -412    -53       C  
ATOM   1873  CD1 TYR A 239      14.583  19.584  -0.564  1.00 18.58           C  
ANISOU 1873  CD1 TYR A 239     1757   2998   2304   -181   -409    -61       C  
ATOM   1874  CD2 TYR A 239      15.048  18.230  -2.465  1.00 18.19           C  
ANISOU 1874  CD2 TYR A 239     1622   3002   2289   -186   -383    -56       C  
ATOM   1875  CE1 TYR A 239      13.225  19.537  -0.857  1.00 19.02           C  
ANISOU 1875  CE1 TYR A 239     1814   3065   2347   -153   -375    -62       C  
ATOM   1876  CE2 TYR A 239      13.692  18.162  -2.758  1.00 18.19           C  
ANISOU 1876  CE2 TYR A 239     1627   3011   2272   -166   -360    -61       C  
ATOM   1877  CZ  TYR A 239      12.785  18.832  -1.962  1.00 19.25           C  
ANISOU 1877  CZ  TYR A 239     1798   3128   2389   -149   -356    -60       C  
ATOM   1878  OH  TYR A 239      11.445  18.785  -2.261  1.00 19.99           O  
ANISOU 1878  OH  TYR A 239     1887   3234   2475   -129   -332    -51       O  
ATOM   1879  N   GLU A 240      18.767  16.503   0.000  1.00 19.78           N  
ANISOU 1879  N   GLU A 240     1779   3179   2557   -240   -467    -11       N  
ATOM   1880  CA  GLU A 240      20.042  15.802  -0.142  1.00 21.28           C  
ANISOU 1880  CA  GLU A 240     1918   3379   2787   -251   -471     22       C  
ATOM   1881  C   GLU A 240      20.779  16.358  -1.369  1.00 22.01           C  
ANISOU 1881  C   GLU A 240     1973   3482   2907   -255   -457     51       C  
ATOM   1882  O   GLU A 240      20.131  16.716  -2.349  1.00 21.71           O  
ANISOU 1882  O   GLU A 240     1942   3454   2853   -241   -428     34       O  
ATOM   1883  CB  GLU A 240      19.786  14.296  -0.331  1.00 24.29           C  
ANISOU 1883  CB  GLU A 240     2277   3780   3174   -224   -434     10       C  
ATOM   1884  CG  GLU A 240      19.392  13.584   0.945  1.00 31.81           C  
ANISOU 1884  CG  GLU A 240     3251   4723   4111   -222   -450     -5       C  
ATOM   1885  CD  GLU A 240      20.537  13.489   1.934  1.00 41.80           C  
ANISOU 1885  CD  GLU A 240     4503   5976   5402   -249   -494     29       C  
ATOM   1886  OE1 GLU A 240      21.525  12.776   1.639  1.00 43.83           O  
ANISOU 1886  OE1 GLU A 240     4710   6245   5699   -248   -483     62       O  
ATOM   1887  OE2 GLU A 240      20.456  14.143   2.999  1.00 44.04           O  
ANISOU 1887  OE2 GLU A 240     4832   6236   5666   -271   -537     26       O  
ATOM   1888  N   PRO A 241      22.117  16.516  -1.314  1.00 23.50           N  
ANISOU 1888  N   PRO A 241     2122   3670   3138   -278   -480    100       N  
ATOM   1889  CA  PRO A 241      22.831  17.017  -2.497  1.00 24.16           C  
ANISOU 1889  CA  PRO A 241     2165   3765   3250   -277   -460    135       C  
ATOM   1890  C   PRO A 241      22.774  15.962  -3.593  1.00 24.42           C  
ANISOU 1890  C   PRO A 241     2173   3819   3288   -238   -392    130       C  
ATOM   1891  O   PRO A 241      22.876  14.768  -3.314  1.00 25.21           O  
ANISOU 1891  O   PRO A 241     2261   3923   3394   -220   -371    129       O  
ATOM   1892  CB  PRO A 241      24.269  17.235  -2.004  1.00 25.22           C  
ANISOU 1892  CB  PRO A 241     2255   3893   3434   -310   -502    201       C  
ATOM   1893  CG  PRO A 241      24.229  17.024  -0.509  1.00 25.76           C  
ANISOU 1893  CG  PRO A 241     2355   3942   3491   -335   -556    194       C  
ATOM   1894  CD  PRO A 241      23.048  16.144  -0.236  1.00 23.67           C  
ANISOU 1894  CD  PRO A 241     2125   3681   3185   -303   -523    136       C  
ATOM   1895  N   LEU A 242      22.528  16.400  -4.813  1.00 23.33           N  
ANISOU 1895  N   LEU A 242     2036   3689   3140   -225   -358    124       N  
ATOM   1896  CA  LEU A 242      22.437  15.533  -5.968  1.00 23.53           C  
ANISOU 1896  CA  LEU A 242     2056   3725   3158   -190   -295    118       C  
ATOM   1897  C   LEU A 242      23.836  15.296  -6.531  1.00 23.87           C  
ANISOU 1897  C   LEU A 242     2047   3773   3249   -177   -263    180       C  
ATOM   1898  O   LEU A 242      24.638  16.217  -6.638  1.00 24.51           O  
ANISOU 1898  O   LEU A 242     2094   3855   3363   -196   -283    224       O  
ATOM   1899  CB  LEU A 242      21.547  16.184  -7.026  1.00 23.45           C  
ANISOU 1899  CB  LEU A 242     2077   3719   3112   -185   -278     90       C  
ATOM   1900  CG  LEU A 242      20.940  15.215  -8.022  1.00 24.01           C  
ANISOU 1900  CG  LEU A 242     2176   3795   3153   -159   -227     65       C  
ATOM   1901  CD1 LEU A 242      19.810  14.468  -7.396  1.00 24.36           C  
ANISOU 1901  CD1 LEU A 242     2253   3838   3166   -158   -240     23       C  
ATOM   1902  CD2 LEU A 242      20.456  15.932  -9.243  1.00 23.50           C  
ANISOU 1902  CD2 LEU A 242     2132   3734   3064   -158   -211     56       C  
ATOM   1903  N   THR A 243      24.132  14.058  -6.857  1.00 23.48           N  
ANISOU 1903  N   THR A 243     1991   3725   3205   -144   -211    187       N  
ATOM   1904  CA  THR A 243      25.434  13.687  -7.413  1.00 24.05           C  
ANISOU 1904  CA  THR A 243     2014   3800   3324   -119   -164    253       C  
ATOM   1905  C   THR A 243      25.260  13.170  -8.856  1.00 24.17           C  
ANISOU 1905  C   THR A 243     2062   3812   3310    -77    -86    242       C  
ATOM   1906  O   THR A 243      24.131  12.928  -9.298  1.00 23.63           O  
ANISOU 1906  O   THR A 243     2053   3738   3186    -75    -79    183       O  
ATOM   1907  CB  THR A 243      26.072  12.619  -6.512  1.00 24.70           C  
ANISOU 1907  CB  THR A 243     2065   3881   3441   -110   -162    283       C  
ATOM   1908  OG1 THR A 243      25.312  11.416  -6.626  1.00 25.44           O  
ANISOU 1908  OG1 THR A 243     2205   3967   3494    -83   -126    234       O  
ATOM   1909  CG2 THR A 243      26.167  13.066  -5.054  1.00 24.74           C  
ANISOU 1909  CG2 THR A 243     2053   3885   3464   -156   -245    290       C  
ATOM   1910  N   GLN A 244      26.367  12.966  -9.571  1.00 24.27           N  
ANISOU 1910  N   GLN A 244     2040   3824   3360    -45    -27    303       N  
ATOM   1911  CA  GLN A 244      26.317  12.389 -10.907  1.00 24.62           C  
ANISOU 1911  CA  GLN A 244     2128   3855   3370      0     55    297       C  
ATOM   1912  C   GLN A 244      25.768  10.943 -10.837  1.00 24.57           C  
ANISOU 1912  C   GLN A 244     2177   3832   3324     25     88    255       C  
ATOM   1913  O   GLN A 244      25.064  10.519 -11.758  1.00 24.92           O  
ANISOU 1913  O   GLN A 244     2296   3861   3311     41    123    213       O  
ATOM   1914  CB  GLN A 244      27.695  12.442 -11.586  1.00 25.91           C  
ANISOU 1914  CB  GLN A 244     2239   4019   3586     38    120    382       C  
ATOM   1915  CG  GLN A 244      27.685  12.054 -13.062  1.00 28.53           C  
ANISOU 1915  CG  GLN A 244     2630   4333   3877     87    211    378       C  
ATOM   1916  CD  GLN A 244      26.741  12.906 -13.873  1.00 30.75           C  
ANISOU 1916  CD  GLN A 244     2965   4616   4104     64    190    327       C  
ATOM   1917  OE1 GLN A 244      26.710  14.134 -13.756  1.00 32.12           O  
ANISOU 1917  OE1 GLN A 244     3103   4806   4296     29    139    335       O  
ATOM   1918  NE2 GLN A 244      25.942  12.262 -14.695  1.00 30.85           N  
ANISOU 1918  NE2 GLN A 244     3067   4608   4046     81    225    275       N  
ATOM   1919  N   ASP A 245      25.967  10.230  -9.702  1.00 23.82           N  
ANISOU 1919  N   ASP A 245     2056   3738   3256     21     66    262       N  
ATOM   1920  CA  ASP A 245      25.387   8.901  -9.541  1.00 23.31           C  
ANISOU 1920  CA  ASP A 245     2044   3658   3155     39     88    221       C  
ATOM   1921  C   ASP A 245      23.869   8.961  -9.615  1.00 21.83           C  
ANISOU 1921  C   ASP A 245     1923   3469   2904     11     47    144       C  
ATOM   1922  O   ASP A 245      23.263   8.143 -10.297  1.00 21.74           O  
ANISOU 1922  O   ASP A 245     1982   3438   2842     26     80    109       O  
ATOM   1923  CB  ASP A 245      25.821   8.268  -8.215  1.00 26.14           C  
ANISOU 1923  CB  ASP A 245     2355   4020   3555     34     61    243       C  
ATOM   1924  CG  ASP A 245      27.173   7.588  -8.269  1.00 31.76           C  
ANISOU 1924  CG  ASP A 245     3018   4727   4323     77    124    319       C  
ATOM   1925  OD1 ASP A 245      27.889   7.763  -9.284  1.00 33.03           O  
ANISOU 1925  OD1 ASP A 245     3170   4881   4497    112    189    365       O  
ATOM   1926  OD2 ASP A 245      27.533   6.911  -7.283  1.00 34.10           O  
ANISOU 1926  OD2 ASP A 245     3280   5024   4651     77    109    339       O  
ATOM   1927  N   HIS A 246      23.268   9.978  -8.977  1.00 20.70           N  
ANISOU 1927  N   HIS A 246     1761   3342   2761    -31    -23    123       N  
ATOM   1928  CA  HIS A 246      21.816  10.166  -8.985  1.00 19.69           C  
ANISOU 1928  CA  HIS A 246     1683   3216   2583    -57    -62     64       C  
ATOM   1929  C   HIS A 246      21.350  10.492 -10.404  1.00 18.97           C  
ANISOU 1929  C   HIS A 246     1640   3118   2448    -52    -34     49       C  
ATOM   1930  O   HIS A 246      20.325   9.974 -10.845  1.00 18.31           O  
ANISOU 1930  O   HIS A 246     1616   3024   2315    -59    -37     11       O  
ATOM   1931  CB  HIS A 246      21.419  11.301  -8.026  1.00 19.69           C  
ANISOU 1931  CB  HIS A 246     1654   3231   2596    -93   -130     57       C  
ATOM   1932  CG  HIS A 246      21.674  10.999  -6.585  1.00 21.28           C  
ANISOU 1932  CG  HIS A 246     1825   3434   2825   -104   -167     64       C  
ATOM   1933  ND1 HIS A 246      22.226  11.945  -5.738  1.00 23.27           N  
ANISOU 1933  ND1 HIS A 246     2040   3691   3111   -129   -213     90       N  
ATOM   1934  CD2 HIS A 246      21.457   9.861  -5.888  1.00 22.18           C  
ANISOU 1934  CD2 HIS A 246     1949   3544   2936    -96   -165     50       C  
ATOM   1935  CE1 HIS A 246      22.325  11.355  -4.557  1.00 23.64           C  
ANISOU 1935  CE1 HIS A 246     2077   3736   3170   -135   -238     91       C  
ATOM   1936  NE2 HIS A 246      21.855  10.108  -4.591  1.00 23.45           N  
ANISOU 1936  NE2 HIS A 246     2077   3708   3126   -115   -210     66       N  
ATOM   1937  N   VAL A 247      22.077  11.389 -11.094  1.00 19.23           N  
ANISOU 1937  N   VAL A 247     1649   3155   2501    -46    -14     83       N  
ATOM   1938  CA  VAL A 247      21.801  11.792 -12.485  1.00 19.55           C  
ANISOU 1938  CA  VAL A 247     1734   3190   2504    -40     16     76       C  
ATOM   1939  C   VAL A 247      21.777  10.563 -13.388  1.00 20.35           C  
ANISOU 1939  C   VAL A 247     1907   3264   2562     -9     77     65       C  
ATOM   1940  O   VAL A 247      20.840  10.376 -14.147  1.00 20.79           O  
ANISOU 1940  O   VAL A 247     2032   3307   2560    -22     72     30       O  
ATOM   1941  CB  VAL A 247      22.799  12.851 -13.004  1.00 19.97           C  
ANISOU 1941  CB  VAL A 247     1741   3252   2595    -32     36    124       C  
ATOM   1942  CG1 VAL A 247      22.539  13.162 -14.478  1.00 20.63           C  
ANISOU 1942  CG1 VAL A 247     1877   3327   2635    -21     73    118       C  
ATOM   1943  CG2 VAL A 247      22.708  14.128 -12.178  1.00 20.32           C  
ANISOU 1943  CG2 VAL A 247     1734   3316   2670    -69    -32    130       C  
ATOM   1944  N   ASP A 248      22.757   9.681 -13.217  1.00 20.38           N  
ANISOU 1944  N   ASP A 248     1898   3254   2590     29    129     96       N  
ATOM   1945  CA  ASP A 248      22.886   8.430 -13.971  1.00 20.46           C  
ANISOU 1945  CA  ASP A 248     1985   3229   2560     67    198     90       C  
ATOM   1946  C   ASP A 248      21.676   7.531 -13.788  1.00 20.55           C  
ANISOU 1946  C   ASP A 248     2066   3224   2517     43    164     35       C  
ATOM   1947  O   ASP A 248      21.142   7.019 -14.774  1.00 20.59           O  
ANISOU 1947  O   ASP A 248     2164   3200   2458     44    185      9       O  
ATOM   1948  CB  ASP A 248      24.139   7.661 -13.532  1.00 21.93           C  
ANISOU 1948  CB  ASP A 248     2130   3406   2795    113    256    142       C  
ATOM   1949  CG  ASP A 248      25.468   8.262 -13.901  1.00 26.04           C  
ANISOU 1949  CG  ASP A 248     2589   3935   3372    147    309    215       C  
ATOM   1950  OD1 ASP A 248      25.484   9.231 -14.698  1.00 25.08           O  
ANISOU 1950  OD1 ASP A 248     2468   3820   3241    141    312    223       O  
ATOM   1951  OD2 ASP A 248      26.506   7.745 -13.415  1.00 29.80           O  
ANISOU 1951  OD2 ASP A 248     3011   4409   3901    181    348    270       O  
ATOM   1952  N   ILE A 249      21.216   7.345 -12.532  1.00 20.74           N  
ANISOU 1952  N   ILE A 249     2049   3266   2564     18    107     18       N  
ATOM   1953  CA  ILE A 249      20.051   6.499 -12.270  1.00 22.41           C  
ANISOU 1953  CA  ILE A 249     2315   3466   2732     -6     71    -27       C  
ATOM   1954  C   ILE A 249      18.750   7.092 -12.821  1.00 22.05           C  
ANISOU 1954  C   ILE A 249     2309   3427   2642    -49     20    -58       C  
ATOM   1955  O   ILE A 249      17.819   6.339 -13.112  1.00 23.21           O  
ANISOU 1955  O   ILE A 249     2523   3555   2741    -69      1    -85       O  
ATOM   1956  CB  ILE A 249      19.957   6.141 -10.767  1.00 24.84           C  
ANISOU 1956  CB  ILE A 249     2569   3791   3079    -17     31    -30       C  
ATOM   1957  CG1 ILE A 249      21.259   5.465 -10.321  1.00 26.37           C  
ANISOU 1957  CG1 ILE A 249     2726   3977   3317     24     82      9       C  
ATOM   1958  CG2 ILE A 249      18.771   5.233 -10.501  1.00 26.67           C  
ANISOU 1958  CG2 ILE A 249     2851   4011   3270    -40     -3    -68       C  
ATOM   1959  CD1 ILE A 249      21.321   5.141  -8.808  1.00 28.68           C  
ANISOU 1959  CD1 ILE A 249     2960   4286   3651     13     42     12       C  
ATOM   1960  N   LEU A 250      18.682   8.422 -12.998  1.00 21.17           N  
ANISOU 1960  N   LEU A 250     2158   3340   2547    -64     -3    -48       N  
ATOM   1961  CA  LEU A 250      17.516   9.092 -13.609  1.00 20.77           C  
ANISOU 1961  CA  LEU A 250     2136   3296   2460   -101    -46    -67       C  
ATOM   1962  C   LEU A 250      17.509   9.013 -15.166  1.00 22.15           C  
ANISOU 1962  C   LEU A 250     2391   3445   2580    -97    -11    -68       C  
ATOM   1963  O   LEU A 250      16.485   9.316 -15.795  1.00 22.40           O  
ANISOU 1963  O   LEU A 250     2462   3476   2572   -132    -49    -82       O  
ATOM   1964  CB  LEU A 250      17.430  10.558 -13.170  1.00 19.52           C  
ANISOU 1964  CB  LEU A 250     1910   3169   2339   -116    -81    -55       C  
ATOM   1965  CG  LEU A 250      17.092  10.770 -11.702  1.00 19.20           C  
ANISOU 1965  CG  LEU A 250     1814   3147   2333   -129   -126    -60       C  
ATOM   1966  CD1 LEU A 250      17.426  12.177 -11.275  1.00 19.01           C  
ANISOU 1966  CD1 LEU A 250     1735   3143   2345   -135   -146    -43       C  
ATOM   1967  CD2 LEU A 250      15.631  10.431 -11.420  1.00 19.27           C  
ANISOU 1967  CD2 LEU A 250     1847   3160   2315   -156   -170    -82       C  
ATOM   1968  N   GLY A 251      18.643   8.617 -15.750  1.00 22.02           N  
ANISOU 1968  N   GLY A 251     2399   3406   2562    -55     61    -49       N  
ATOM   1969  CA  GLY A 251      18.840   8.430 -17.189  1.00 22.75           C  
ANISOU 1969  CA  GLY A 251     2579   3465   2598    -39    110    -47       C  
ATOM   1970  C   GLY A 251      17.681   7.803 -17.941  1.00 22.66           C  
ANISOU 1970  C   GLY A 251     2674   3425   2510    -76     78    -79       C  
ATOM   1971  O   GLY A 251      17.204   8.414 -18.894  1.00 23.10           O  
ANISOU 1971  O   GLY A 251     2770   3478   2529    -99     62    -82       O  
ATOM   1972  N   PRO A 252      17.182   6.604 -17.553  1.00 22.68           N  
ANISOU 1972  N   PRO A 252     2726   3405   2488    -87     62   -100       N  
ATOM   1973  CA  PRO A 252      16.047   6.011 -18.293  1.00 22.55           C  
ANISOU 1973  CA  PRO A 252     2813   3357   2396   -133     19   -123       C  
ATOM   1974  C   PRO A 252      14.789   6.902 -18.307  1.00 22.40           C  
ANISOU 1974  C   PRO A 252     2762   3371   2378   -191    -66   -124       C  
ATOM   1975  O   PRO A 252      14.054   6.924 -19.297  1.00 22.38           O  
ANISOU 1975  O   PRO A 252     2836   3348   2317   -229    -97   -127       O  
ATOM   1976  CB  PRO A 252      15.806   4.674 -17.569  1.00 23.11           C  
ANISOU 1976  CB  PRO A 252     2914   3406   2460   -135      9   -139       C  
ATOM   1977  CG  PRO A 252      17.104   4.356 -16.908  1.00 23.27           C  
ANISOU 1977  CG  PRO A 252     2883   3428   2530    -74     79   -124       C  
ATOM   1978  CD  PRO A 252      17.651   5.702 -16.484  1.00 21.80           C  
ANISOU 1978  CD  PRO A 252     2581   3290   2411    -61     80   -100       C  
ATOM   1979  N   LEU A 253      14.566   7.668 -17.234  1.00 22.10           N  
ANISOU 1979  N   LEU A 253     2613   3380   2404   -197   -101   -116       N  
ATOM   1980  CA  LEU A 253      13.412   8.570 -17.153  1.00 22.00           C  
ANISOU 1980  CA  LEU A 253     2560   3398   2400   -242   -169   -108       C  
ATOM   1981  C   LEU A 253      13.626   9.808 -18.010  1.00 22.13           C  
ANISOU 1981  C   LEU A 253     2566   3427   2415   -241   -158    -95       C  
ATOM   1982  O   LEU A 253      12.726  10.242 -18.732  1.00 22.05           O  
ANISOU 1982  O   LEU A 253     2583   3419   2375   -281   -200    -88       O  
ATOM   1983  CB  LEU A 253      13.109   8.927 -15.697  1.00 22.11           C  
ANISOU 1983  CB  LEU A 253     2476   3449   2476   -241   -199   -104       C  
ATOM   1984  CG  LEU A 253      12.596   7.748 -14.852  1.00 24.40           C  
ANISOU 1984  CG  LEU A 253     2775   3731   2765   -251   -223   -114       C  
ATOM   1985  CD1 LEU A 253      12.500   8.132 -13.367  1.00 24.97           C  
ANISOU 1985  CD1 LEU A 253     2756   3836   2897   -240   -240   -109       C  
ATOM   1986  CD2 LEU A 253      11.255   7.258 -15.375  1.00 24.96           C  
ANISOU 1986  CD2 LEU A 253     2900   3789   2793   -304   -282   -109       C  
ATOM   1987  N   SER A 254      14.861  10.318 -18.024  1.00 22.07           N  
ANISOU 1987  N   SER A 254     2523   3425   2438   -198   -101    -86       N  
ATOM   1988  CA  SER A 254      15.232  11.419 -18.882  1.00 23.46           C  
ANISOU 1988  CA  SER A 254     2691   3609   2612   -192    -82    -71       C  
ATOM   1989  C   SER A 254      15.072  10.998 -20.357  1.00 24.77           C  
ANISOU 1989  C   SER A 254     2972   3737   2702   -202    -64    -76       C  
ATOM   1990  O   SER A 254      14.600  11.779 -21.167  1.00 24.95           O  
ANISOU 1990  O   SER A 254     3011   3766   2703   -227    -86    -68       O  
ATOM   1991  CB  SER A 254      16.685  11.793 -18.612  1.00 25.04           C  
ANISOU 1991  CB  SER A 254     2837   3816   2861   -142    -20    -52       C  
ATOM   1992  OG  SER A 254      17.180  12.634 -19.635  1.00 28.90           O  
ANISOU 1992  OG  SER A 254     3337   4305   3341   -130     12    -34       O  
ATOM   1993  N   ALA A 255      15.443   9.756 -20.684  1.00 25.59           N  
ANISOU 1993  N   ALA A 255     3161   3798   2763   -183    -24    -88       N  
ATOM   1994  CA  ALA A 255      15.378   9.231 -22.039  1.00 26.68           C  
ANISOU 1994  CA  ALA A 255     3431   3888   2818   -189      0    -95       C  
ATOM   1995  C   ALA A 255      13.959   8.994 -22.495  1.00 27.69           C  
ANISOU 1995  C   ALA A 255     3624   4004   2892   -259    -83   -104       C  
ATOM   1996  O   ALA A 255      13.629   9.316 -23.626  1.00 28.41           O  
ANISOU 1996  O   ALA A 255     3788   4077   2929   -285    -96   -100       O  
ATOM   1997  CB  ALA A 255      16.185   7.949 -22.127  1.00 26.99           C  
ANISOU 1997  CB  ALA A 255     3548   3879   2828   -145     70   -103       C  
ATOM   1998  N   GLN A 256      13.111   8.455 -21.625  1.00 27.99           N  
ANISOU 1998  N   GLN A 256     3636   4054   2947   -292   -143   -110       N  
ATOM   1999  CA  GLN A 256      11.722   8.173 -21.985  1.00 28.29           C  
ANISOU 1999  CA  GLN A 256     3724   4082   2942   -364   -229   -105       C  
ATOM   2000  C   GLN A 256      10.942   9.459 -22.196  1.00 27.48           C  
ANISOU 2000  C   GLN A 256     3556   4022   2865   -399   -282    -80       C  
ATOM   2001  O   GLN A 256      10.172   9.560 -23.154  1.00 28.46           O  
ANISOU 2001  O   GLN A 256     3746   4130   2938   -450   -331    -67       O  
ATOM   2002  CB  GLN A 256      11.067   7.322 -20.903  1.00 31.19           C  
ANISOU 2002  CB  GLN A 256     4062   4456   3333   -384   -274   -109       C  
ATOM   2003  CG  GLN A 256       9.720   6.763 -21.299  1.00 37.37           C  
ANISOU 2003  CG  GLN A 256     4909   5220   4070   -459   -362    -96       C  
ATOM   2004  CD  GLN A 256       8.982   6.307 -20.069  1.00 44.14           C  
ANISOU 2004  CD  GLN A 256     5694   6103   4976   -477   -409    -86       C  
ATOM   2005  OE1 GLN A 256       9.571   5.750 -19.118  1.00 45.73           O  
ANISOU 2005  OE1 GLN A 256     5860   6306   5208   -437   -372   -103       O  
ATOM   2006  NE2 GLN A 256       7.672   6.547 -20.060  1.00 45.80           N  
ANISOU 2006  NE2 GLN A 256     5874   6334   5194   -537   -492    -51       N  
ATOM   2007  N   THR A 257      11.174  10.467 -21.342  1.00 24.88           N  
ANISOU 2007  N   THR A 257     3104   3741   2610   -372   -273    -71       N  
ATOM   2008  CA  THR A 257      10.424  11.720 -21.447  1.00 23.88           C  
ANISOU 2008  CA  THR A 257     2912   3651   2511   -399   -317    -45       C  
ATOM   2009  C   THR A 257      11.043  12.775 -22.359  1.00 23.76           C  
ANISOU 2009  C   THR A 257     2900   3640   2488   -382   -281    -39       C  
ATOM   2010  O   THR A 257      10.382  13.760 -22.663  1.00 24.62           O  
ANISOU 2010  O   THR A 257     2972   3773   2608   -408   -318    -16       O  
ATOM   2011  CB  THR A 257      10.198  12.325 -20.058  1.00 23.93           C  
ANISOU 2011  CB  THR A 257     2798   3701   2594   -384   -329    -36       C  
ATOM   2012  OG1 THR A 257      11.456  12.774 -19.527  1.00 23.66           O  
ANISOU 2012  OG1 THR A 257     2713   3676   2600   -329   -268    -48       O  
ATOM   2013  CG2 THR A 257       9.564  11.343 -19.105  1.00 24.41           C  
ANISOU 2013  CG2 THR A 257     2848   3762   2667   -398   -362    -38       C  
ATOM   2014  N   GLY A 258      12.324  12.639 -22.665  1.00 22.62           N  
ANISOU 2014  N   GLY A 258     2783   3477   2336   -333   -206    -52       N  
ATOM   2015  CA  GLY A 258      13.035  13.651 -23.434  1.00 22.87           C  
ANISOU 2015  CA  GLY A 258     2807   3515   2369   -310   -165    -41       C  
ATOM   2016  C   GLY A 258      13.358  14.893 -22.614  1.00 23.07           C  
ANISOU 2016  C   GLY A 258     2709   3584   2471   -289   -162    -28       C  
ATOM   2017  O   GLY A 258      13.767  15.908 -23.175  1.00 23.81           O  
ANISOU 2017  O   GLY A 258     2782   3689   2574   -279   -143    -14       O  
ATOM   2018  N   ILE A 259      13.229  14.824 -21.276  1.00 22.13           N  
ANISOU 2018  N   ILE A 259     2515   3487   2405   -282   -180    -32       N  
ATOM   2019  CA  ILE A 259      13.546  15.955 -20.424  1.00 21.52           C  
ANISOU 2019  CA  ILE A 259     2341   3443   2394   -265   -180    -21       C  
ATOM   2020  C   ILE A 259      14.854  15.664 -19.743  1.00 21.24           C  
ANISOU 2020  C   ILE A 259     2272   3404   2394   -222   -129    -23       C  
ATOM   2021  O   ILE A 259      14.930  14.741 -18.927  1.00 21.18           O  
ANISOU 2021  O   ILE A 259     2262   3390   2396   -213   -129    -36       O  
ATOM   2022  CB  ILE A 259      12.441  16.259 -19.392  1.00 21.60           C  
ANISOU 2022  CB  ILE A 259     2295   3478   2436   -288   -236    -16       C  
ATOM   2023  CG1 ILE A 259      11.127  16.626 -20.092  1.00 22.94           C  
ANISOU 2023  CG1 ILE A 259     2483   3654   2579   -332   -287      2       C  
ATOM   2024  CG2 ILE A 259      12.888  17.381 -18.418  1.00 22.27           C  
ANISOU 2024  CG2 ILE A 259     2296   3586   2580   -267   -231     -9       C  
ATOM   2025  CD1 ILE A 259       9.967  16.618 -19.170  1.00 23.96           C  
ANISOU 2025  CD1 ILE A 259     2568   3802   2735   -351   -333     16       C  
ATOM   2026  N   ALA A 260      15.897  16.434 -20.081  1.00 20.34           N  
ANISOU 2026  N   ALA A 260     2129   3294   2304   -195    -89     -6       N  
ATOM   2027  CA  ALA A 260      17.233  16.298 -19.490  1.00 19.83           C  
ANISOU 2027  CA  ALA A 260     2022   3230   2284   -156    -44      8       C  
ATOM   2028  C   ALA A 260      17.156  16.397 -17.960  1.00 19.07           C  
ANISOU 2028  C   ALA A 260     1857   3151   2238   -161    -79      4       C  
ATOM   2029  O   ALA A 260      16.349  17.163 -17.424  1.00 18.83           O  
ANISOU 2029  O   ALA A 260     1795   3137   2220   -184   -126     -1       O  
ATOM   2030  CB  ALA A 260      18.145  17.391 -20.018  1.00 20.11           C  
ANISOU 2030  CB  ALA A 260     2021   3274   2347   -139    -13     38       C  
ATOM   2031  N   VAL A 261      17.970  15.618 -17.256  1.00 18.75           N  
ANISOU 2031  N   VAL A 261     1798   3103   2222   -136    -53      8       N  
ATOM   2032  CA  VAL A 261      17.952  15.606 -15.786  1.00 18.73           C  
ANISOU 2032  CA  VAL A 261     1743   3114   2261   -141    -86      4       C  
ATOM   2033  C   VAL A 261      18.128  17.012 -15.191  1.00 18.84           C  
ANISOU 2033  C   VAL A 261     1697   3145   2316   -153   -118     20       C  
ATOM   2034  O   VAL A 261      17.327  17.406 -14.338  1.00 18.53           O  
ANISOU 2034  O   VAL A 261     1642   3114   2283   -172   -161      6       O  
ATOM   2035  CB  VAL A 261      18.951  14.578 -15.206  1.00 18.67           C  
ANISOU 2035  CB  VAL A 261     1722   3095   2277   -113    -51     15       C  
ATOM   2036  CG1 VAL A 261      19.024  14.681 -13.689  1.00 18.93           C  
ANISOU 2036  CG1 VAL A 261     1700   3140   2352   -121    -90     15       C  
ATOM   2037  CG2 VAL A 261      18.561  13.151 -15.628  1.00 19.33           C  
ANISOU 2037  CG2 VAL A 261     1876   3154   2313   -104    -28     -7       C  
ATOM   2038  N   LEU A 262      19.093  17.796 -15.713  1.00 18.81           N  
ANISOU 2038  N   LEU A 262     1667   3144   2336   -143    -94     50       N  
ATOM   2039  CA  LEU A 262      19.328  19.151 -15.204  1.00 20.19           C  
ANISOU 2039  CA  LEU A 262     1793   3329   2547   -159   -127     67       C  
ATOM   2040  C   LEU A 262      18.166  20.112 -15.479  1.00 20.88           C  
ANISOU 2040  C   LEU A 262     1896   3424   2612   -181   -160     51       C  
ATOM   2041  O   LEU A 262      17.957  21.038 -14.687  1.00 21.68           O  
ANISOU 2041  O   LEU A 262     1974   3529   2734   -195   -196     52       O  
ATOM   2042  CB  LEU A 262      20.662  19.737 -15.675  1.00 20.80           C  
ANISOU 2042  CB  LEU A 262     1833   3408   2660   -146    -97    113       C  
ATOM   2043  CG  LEU A 262      21.915  19.048 -15.119  1.00 22.87           C  
ANISOU 2043  CG  LEU A 262     2058   3667   2966   -126    -73    148       C  
ATOM   2044  CD1 LEU A 262      23.177  19.702 -15.660  1.00 23.31           C  
ANISOU 2044  CD1 LEU A 262     2068   3726   3064   -114    -44    206       C  
ATOM   2045  CD2 LEU A 262      21.919  19.016 -13.595  1.00 23.61           C  
ANISOU 2045  CD2 LEU A 262     2122   3761   3087   -145   -123    143       C  
ATOM   2046  N   ASP A 263      17.374  19.865 -16.534  1.00 19.86           N  
ANISOU 2046  N   ASP A 263     1811   3295   2440   -186   -151     38       N  
ATOM   2047  CA  ASP A 263      16.177  20.668 -16.782  1.00 19.64           C  
ANISOU 2047  CA  ASP A 263     1792   3275   2394   -208   -184     31       C  
ATOM   2048  C   ASP A 263      15.150  20.356 -15.709  1.00 20.09           C  
ANISOU 2048  C   ASP A 263     1847   3336   2452   -217   -219     14       C  
ATOM   2049  O   ASP A 263      14.529  21.281 -15.197  1.00 19.90           O  
ANISOU 2049  O   ASP A 263     1806   3317   2440   -224   -244     18       O  
ATOM   2050  CB  ASP A 263      15.568  20.394 -18.168  1.00 20.10           C  
ANISOU 2050  CB  ASP A 263     1901   3332   2406   -217   -174     29       C  
ATOM   2051  CG  ASP A 263      16.435  20.807 -19.339  1.00 20.68           C  
ANISOU 2051  CG  ASP A 263     1986   3401   2472   -206   -135     47       C  
ATOM   2052  OD1 ASP A 263      17.551  21.313 -19.104  1.00 19.27           O  
ANISOU 2052  OD1 ASP A 263     1767   3224   2331   -189   -115     68       O  
ATOM   2053  OD2 ASP A 263      15.999  20.619 -20.486  1.00 22.38           O  
ANISOU 2053  OD2 ASP A 263     2252   3609   2642   -215   -127     46       O  
ATOM   2054  N   MET A 264      14.966  19.058 -15.365  1.00 19.64           N  
ANISOU 2054  N   MET A 264     1809   3272   2380   -213   -215     -1       N  
ATOM   2055  CA  MET A 264      14.057  18.662 -14.293  1.00 18.66           C  
ANISOU 2055  CA  MET A 264     1679   3151   2260   -219   -244    -12       C  
ATOM   2056  C   MET A 264      14.519  19.252 -12.962  1.00 17.91           C  
ANISOU 2056  C   MET A 264     1549   3055   2201   -210   -256    -11       C  
ATOM   2057  O   MET A 264      13.694  19.740 -12.205  1.00 17.74           O  
ANISOU 2057  O   MET A 264     1521   3035   2184   -213   -277    -12       O  
ATOM   2058  CB  MET A 264      13.908  17.138 -14.184  1.00 18.84           C  
ANISOU 2058  CB  MET A 264     1730   3165   2263   -218   -238    -27       C  
ATOM   2059  CG  MET A 264      12.701  16.742 -13.358  1.00 19.27           C  
ANISOU 2059  CG  MET A 264     1781   3225   2315   -228   -270    -32       C  
ATOM   2060  SD  MET A 264      11.136  17.304 -14.116  1.00 22.01           S  
ANISOU 2060  SD  MET A 264     2136   3584   2642   -255   -301    -11       S  
ATOM   2061  CE  MET A 264      10.695  15.861 -15.101  1.00 23.36           C  
ANISOU 2061  CE  MET A 264     2367   3742   2766   -281   -311    -16       C  
ATOM   2062  N   CYS A 265      15.838  19.291 -12.714  1.00 17.40           N  
ANISOU 2062  N   CYS A 265     1464   2984   2161   -201   -241     -3       N  
ATOM   2063  CA  CYS A 265      16.418  19.961 -11.538  1.00 17.57           C  
ANISOU 2063  CA  CYS A 265     1461   3000   2215   -202   -262      4       C  
ATOM   2064  C   CYS A 265      16.011  21.455 -11.469  1.00 18.00           C  
ANISOU 2064  C   CYS A 265     1515   3052   2272   -212   -282     12       C  
ATOM   2065  O   CYS A 265      15.715  21.973 -10.378  1.00 16.58           O  
ANISOU 2065  O   CYS A 265     1341   2860   2097   -214   -306      7       O  
ATOM   2066  CB  CYS A 265      17.940  19.811 -11.543  1.00 18.31           C  
ANISOU 2066  CB  CYS A 265     1527   3089   2339   -197   -247     28       C  
ATOM   2067  SG  CYS A 265      18.517  18.130 -11.204  1.00 18.86           S  
ANISOU 2067  SG  CYS A 265     1595   3156   2414   -180   -222     25       S  
ATOM   2068  N   ALA A 266      15.966  22.144 -12.628  1.00 18.82           N  
ANISOU 2068  N   ALA A 266     1619   3162   2370   -216   -271     23       N  
ATOM   2069  CA  ALA A 266      15.565  23.549 -12.648  1.00 19.98           C  
ANISOU 2069  CA  ALA A 266     1768   3306   2520   -223   -287     31       C  
ATOM   2070  C   ALA A 266      14.084  23.717 -12.326  1.00 20.90           C  
ANISOU 2070  C   ALA A 266     1900   3423   2618   -220   -296     23       C  
ATOM   2071  O   ALA A 266      13.726  24.668 -11.636  1.00 21.54           O  
ANISOU 2071  O   ALA A 266     1990   3492   2704   -216   -308     27       O  
ATOM   2072  CB  ALA A 266      15.908  24.191 -13.973  1.00 21.11           C  
ANISOU 2072  CB  ALA A 266     1904   3455   2660   -228   -271     48       C  
ATOM   2073  N   SER A 267      13.243  22.762 -12.747  1.00 20.76           N  
ANISOU 2073  N   SER A 267     1889   3417   2580   -220   -291     18       N  
ATOM   2074  CA  SER A 267      11.830  22.733 -12.403  1.00 21.25           C  
ANISOU 2074  CA  SER A 267     1957   3484   2634   -216   -300     23       C  
ATOM   2075  C   SER A 267      11.698  22.531 -10.889  1.00 19.58           C  
ANISOU 2075  C   SER A 267     1748   3260   2431   -202   -306     14       C  
ATOM   2076  O   SER A 267      10.906  23.225 -10.229  1.00 18.69           O  
ANISOU 2076  O   SER A 267     1642   3139   2321   -189   -306     24       O  
ATOM   2077  CB  SER A 267      11.112  21.601 -13.138  1.00 24.44           C  
ANISOU 2077  CB  SER A 267     2369   3901   3016   -228   -303     25       C  
ATOM   2078  OG  SER A 267      10.718  22.012 -14.435  1.00 28.77           O  
ANISOU 2078  OG  SER A 267     2923   4458   3549   -244   -305     41       O  
ATOM   2079  N   LEU A 268      12.503  21.609 -10.337  1.00 18.52           N  
ANISOU 2079  N   LEU A 268     1614   3122   2302   -202   -306     -2       N  
ATOM   2080  CA  LEU A 268      12.482  21.342  -8.909  1.00 19.15           C  
ANISOU 2080  CA  LEU A 268     1702   3189   2387   -191   -314    -12       C  
ATOM   2081  C   LEU A 268      12.945  22.587  -8.131  1.00 19.24           C  
ANISOU 2081  C   LEU A 268     1728   3176   2405   -189   -325     -9       C  
ATOM   2082  O   LEU A 268      12.308  22.972  -7.157  1.00 18.94           O  
ANISOU 2082  O   LEU A 268     1714   3122   2360   -175   -326     -9       O  
ATOM   2083  CB  LEU A 268      13.348  20.131  -8.564  1.00 19.31           C  
ANISOU 2083  CB  LEU A 268     1715   3209   2413   -193   -314    -25       C  
ATOM   2084  CG  LEU A 268      13.431  19.763  -7.060  1.00 19.90           C  
ANISOU 2084  CG  LEU A 268     1799   3270   2492   -185   -326    -34       C  
ATOM   2085  CD1 LEU A 268      12.026  19.699  -6.407  1.00 19.92           C  
ANISOU 2085  CD1 LEU A 268     1815   3272   2483   -170   -323    -32       C  
ATOM   2086  CD2 LEU A 268      14.069  18.420  -6.890  1.00 20.51           C  
ANISOU 2086  CD2 LEU A 268     1866   3352   2576   -186   -322    -43       C  
ATOM   2087  N   LYS A 269      13.985  23.273  -8.630  1.00 19.46           N  
ANISOU 2087  N   LYS A 269     1749   3199   2445   -203   -331     -2       N  
ATOM   2088  CA  LYS A 269      14.512  24.504  -8.057  1.00 20.21           C  
ANISOU 2088  CA  LYS A 269     1865   3268   2546   -211   -350      4       C  
ATOM   2089  C   LYS A 269      13.417  25.554  -7.963  1.00 21.02           C  
ANISOU 2089  C   LYS A 269     1994   3358   2633   -196   -342      9       C  
ATOM   2090  O   LYS A 269      13.196  26.091  -6.880  1.00 21.25           O  
ANISOU 2090  O   LYS A 269     2064   3357   2651   -187   -348      6       O  
ATOM   2091  CB  LYS A 269      15.711  25.015  -8.879  1.00 21.65           C  
ANISOU 2091  CB  LYS A 269     2023   3454   2748   -230   -357     21       C  
ATOM   2092  CG  LYS A 269      16.085  26.477  -8.645  1.00 24.42           C  
ANISOU 2092  CG  LYS A 269     2397   3780   3104   -244   -379     33       C  
ATOM   2093  CD  LYS A 269      17.453  26.777  -9.180  1.00 28.22           C  
ANISOU 2093  CD  LYS A 269     2847   4263   3613   -267   -393     58       C  
ATOM   2094  CE  LYS A 269      17.615  28.251  -9.430  1.00 31.31           C  
ANISOU 2094  CE  LYS A 269     3255   4635   4007   -282   -410     74       C  
ATOM   2095  NZ  LYS A 269      18.728  28.527 -10.386  1.00 31.27           N  
ANISOU 2095  NZ  LYS A 269     3206   4642   4031   -298   -410    105       N  
ATOM   2096  N   GLU A 270      12.696  25.814  -9.078  1.00 21.51           N  
ANISOU 2096  N   GLU A 270     2039   3440   2693   -192   -325     21       N  
ATOM   2097  CA  GLU A 270      11.599  26.773  -9.077  1.00 21.98           C  
ANISOU 2097  CA  GLU A 270     2116   3491   2745   -174   -311     36       C  
ATOM   2098  C   GLU A 270      10.488  26.332  -8.118  1.00 22.38           C  
ANISOU 2098  C   GLU A 270     2180   3535   2786   -147   -296     39       C  
ATOM   2099  O   GLU A 270       9.955  27.175  -7.405  1.00 23.14           O  
ANISOU 2099  O   GLU A 270     2312   3604   2874   -124   -282     48       O  
ATOM   2100  CB  GLU A 270      11.051  26.984 -10.485  1.00 25.05           C  
ANISOU 2100  CB  GLU A 270     2476   3905   3135   -179   -301     54       C  
ATOM   2101  CG  GLU A 270      12.070  27.581 -11.437  1.00 30.17           C  
ANISOU 2101  CG  GLU A 270     3114   4558   3792   -199   -308     56       C  
ATOM   2102  CD  GLU A 270      12.707  28.903 -11.052  1.00 35.37           C  
ANISOU 2102  CD  GLU A 270     3795   5186   4456   -204   -319     60       C  
ATOM   2103  OE1 GLU A 270      11.989  29.930 -11.038  1.00 37.20           O  
ANISOU 2103  OE1 GLU A 270     4047   5405   4684   -191   -310     73       O  
ATOM   2104  OE2 GLU A 270      13.932  28.915 -10.785  1.00 34.22           O  
ANISOU 2104  OE2 GLU A 270     3650   5030   4322   -222   -338     55       O  
ATOM   2105  N   LEU A 271      10.164  25.023  -8.061  1.00 21.77           N  
ANISOU 2105  N   LEU A 271     2082   3480   2711   -147   -296     34       N  
ATOM   2106  CA  LEU A 271       9.135  24.529  -7.126  1.00 21.66           C  
ANISOU 2106  CA  LEU A 271     2076   3462   2692   -122   -281     43       C  
ATOM   2107  C   LEU A 271       9.544  24.764  -5.674  1.00 22.28           C  
ANISOU 2107  C   LEU A 271     2201   3505   2759   -107   -282     27       C  
ATOM   2108  O   LEU A 271       8.707  25.107  -4.843  1.00 23.08           O  
ANISOU 2108  O   LEU A 271     2331   3587   2851    -75   -258     40       O  
ATOM   2109  CB  LEU A 271       8.822  23.049  -7.363  1.00 21.31           C  
ANISOU 2109  CB  LEU A 271     2001   3444   2650   -131   -287     42       C  
ATOM   2110  CG  LEU A 271       7.905  22.763  -8.535  1.00 22.10           C  
ANISOU 2110  CG  LEU A 271     2070   3573   2754   -143   -289     69       C  
ATOM   2111  CD1 LEU A 271       8.005  21.315  -8.953  1.00 22.12           C  
ANISOU 2111  CD1 LEU A 271     2060   3593   2751   -165   -304     58       C  
ATOM   2112  CD2 LEU A 271       6.484  23.159  -8.222  1.00 22.22           C  
ANISOU 2112  CD2 LEU A 271     2074   3590   2777   -118   -271    112       C  
ATOM   2113  N   LEU A 272      10.835  24.625  -5.377  1.00 21.99           N  
ANISOU 2113  N   LEU A 272     2176   3457   2723   -130   -307      4       N  
ATOM   2114  CA  LEU A 272      11.343  24.883  -4.041  1.00 22.73           C  
ANISOU 2114  CA  LEU A 272     2321   3513   2802   -128   -320     -9       C  
ATOM   2115  C   LEU A 272      11.276  26.360  -3.709  1.00 23.98           C  
ANISOU 2115  C   LEU A 272     2536   3632   2944   -119   -317     -3       C  
ATOM   2116  O   LEU A 272      10.829  26.708  -2.621  1.00 24.74           O  
ANISOU 2116  O   LEU A 272     2692   3692   3017    -95   -304     -4       O  
ATOM   2117  CB  LEU A 272      12.768  24.347  -3.883  1.00 21.86           C  
ANISOU 2117  CB  LEU A 272     2200   3404   2704   -161   -356    -23       C  
ATOM   2118  CG  LEU A 272      12.852  22.830  -3.928  1.00 22.46           C  
ANISOU 2118  CG  LEU A 272     2235   3508   2790   -163   -354    -31       C  
ATOM   2119  CD1 LEU A 272      14.307  22.354  -3.972  1.00 22.44           C  
ANISOU 2119  CD1 LEU A 272     2210   3508   2806   -191   -380    -33       C  
ATOM   2120  CD2 LEU A 272      12.069  22.210  -2.761  1.00 22.80           C  
ANISOU 2120  CD2 LEU A 272     2303   3541   2818   -139   -343    -37       C  
ATOM   2121  N   GLN A 273      11.657  27.226  -4.652  1.00 23.54           N  
ANISOU 2121  N   GLN A 273     2467   3578   2897   -136   -325      5       N  
ATOM   2122  CA  GLN A 273      11.685  28.652  -4.406  1.00 24.03           C  
ANISOU 2122  CA  GLN A 273     2586   3599   2943   -132   -325     11       C  
ATOM   2123  C   GLN A 273      10.324  29.330  -4.405  1.00 26.02           C  
ANISOU 2123  C   GLN A 273     2862   3841   3185    -87   -278     31       C  
ATOM   2124  O   GLN A 273      10.155  30.328  -3.709  1.00 26.36           O  
ANISOU 2124  O   GLN A 273     2978   3835   3204    -69   -267     33       O  
ATOM   2125  CB  GLN A 273      12.625  29.344  -5.392  1.00 24.58           C  
ANISOU 2125  CB  GLN A 273     2633   3676   3031   -165   -350     16       C  
ATOM   2126  CG  GLN A 273      14.084  28.958  -5.184  1.00 25.72           C  
ANISOU 2126  CG  GLN A 273     2765   3818   3188   -207   -396     10       C  
ATOM   2127  CD  GLN A 273      14.990  29.450  -6.285  1.00 28.94           C  
ANISOU 2127  CD  GLN A 273     3133   4241   3621   -236   -413     26       C  
ATOM   2128  OE1 GLN A 273      14.560  30.042  -7.294  1.00 30.81           O  
ANISOU 2128  OE1 GLN A 273     3351   4493   3864   -228   -393     36       O  
ATOM   2129  NE2 GLN A 273      16.273  29.209  -6.115  1.00 28.08           N  
ANISOU 2129  NE2 GLN A 273     3007   4131   3532   -270   -450     34       N  
ATOM   2130  N   ASN A 274       9.368  28.823  -5.182  1.00 26.98           N  
ANISOU 2130  N   ASN A 274     2924   4002   3324    -71   -252     51       N  
ATOM   2131  CA  ASN A 274       8.054  29.444  -5.314  1.00 28.77           C  
ANISOU 2131  CA  ASN A 274     3154   4226   3552    -30   -208     86       C  
ATOM   2132  C   ASN A 274       6.903  28.670  -4.714  1.00 29.94           C  
ANISOU 2132  C   ASN A 274     3289   4384   3702      7   -174    109       C  
ATOM   2133  O   ASN A 274       5.802  29.197  -4.692  1.00 30.59           O  
ANISOU 2133  O   ASN A 274     3372   4461   3790     47   -132    148       O  
ATOM   2134  CB  ASN A 274       7.721  29.666  -6.795  1.00 30.52           C  
ANISOU 2134  CB  ASN A 274     3314   4486   3796    -43   -208    110       C  
ATOM   2135  CG  ASN A 274       8.765  30.443  -7.544  1.00 35.18           C  
ANISOU 2135  CG  ASN A 274     3907   5072   4389    -77   -235     95       C  
ATOM   2136  OD1 ASN A 274       9.385  31.363  -7.013  1.00 36.97           O  
ANISOU 2136  OD1 ASN A 274     4189   5257   4601    -81   -245     83       O  
ATOM   2137  ND2 ASN A 274       8.986  30.084  -8.804  1.00 36.52           N  
ANISOU 2137  ND2 ASN A 274     4020   5281   4574   -103   -250    100       N  
ATOM   2138  N   GLY A 275       7.117  27.425  -4.313  1.00 30.34           N  
ANISOU 2138  N   GLY A 275     3320   4454   3755     -5   -191     91       N  
ATOM   2139  CA  GLY A 275       6.034  26.582  -3.817  1.00 31.13           C  
ANISOU 2139  CA  GLY A 275     3398   4569   3863     25   -164    117       C  
ATOM   2140  C   GLY A 275       5.120  26.114  -4.944  1.00 32.18           C  
ANISOU 2140  C   GLY A 275     3454   4748   4024     18   -162    157       C  
ATOM   2141  O   GLY A 275       5.375  26.398  -6.118  1.00 32.26           O  
ANISOU 2141  O   GLY A 275     3435   4779   4043    -11   -182    158       O  
ATOM   2142  N   MET A 276       4.050  25.381  -4.610  1.00 32.71           N  
ANISOU 2142  N   MET A 276     3491   4833   4105     40   -142    194       N  
ATOM   2143  CA  MET A 276       3.118  24.878  -5.621  1.00 33.80           C  
ANISOU 2143  CA  MET A 276     3560   5013   4271     24   -152    241       C  
ATOM   2144  C   MET A 276       2.039  25.910  -6.011  1.00 33.78           C  
ANISOU 2144  C   MET A 276     3537   5010   4288     56   -117    306       C  
ATOM   2145  O   MET A 276       1.407  25.743  -7.053  1.00 33.64           O  
ANISOU 2145  O   MET A 276     3463   5026   4292     32   -135    347       O  
ATOM   2146  CB  MET A 276       2.448  23.563  -5.183  1.00 35.30           C  
ANISOU 2146  CB  MET A 276     3716   5223   4473     25   -157    263       C  
ATOM   2147  CG  MET A 276       3.331  22.636  -4.353  1.00 38.40           C  
ANISOU 2147  CG  MET A 276     4137   5606   4846     15   -173    208       C  
ATOM   2148  SD  MET A 276       3.881  21.129  -5.193  1.00 45.04           S  
ANISOU 2148  SD  MET A 276     4944   6480   5689    -43   -226    179       S  
ATOM   2149  CE  MET A 276       2.396  20.411  -5.593  1.00 40.65           C  
ANISOU 2149  CE  MET A 276     4331   5954   5158    -48   -232    247       C  
ATOM   2150  N   ASN A 277       1.836  26.969  -5.193  1.00 33.42           N  
ANISOU 2150  N   ASN A 277     3542   4925   4232    107    -67    317       N  
ATOM   2151  CA  ASN A 277       0.814  27.998  -5.448  1.00 33.88           C  
ANISOU 2151  CA  ASN A 277     3585   4976   4310    148    -21    384       C  
ATOM   2152  C   ASN A 277      -0.601  27.417  -5.467  1.00 33.61           C  
ANISOU 2152  C   ASN A 277     3482   4973   4314    170      1    468       C  
ATOM   2153  O   ASN A 277      -1.364  27.658  -6.407  1.00 34.03           O  
ANISOU 2153  O   ASN A 277     3477   5055   4400    161     -4    529       O  
ATOM   2154  CB  ASN A 277       1.112  28.823  -6.705  1.00 35.25           C  
ANISOU 2154  CB  ASN A 277     3742   5162   4490    118    -44    384       C  
ATOM   2155  CG  ASN A 277       2.169  29.879  -6.475  1.00 39.70           C  
ANISOU 2155  CG  ASN A 277     4379   5682   5022    119    -42    331       C  
ATOM   2156  OD1 ASN A 277       3.246  29.868  -7.082  1.00 41.85           O  
ANISOU 2156  OD1 ASN A 277     4657   5962   5284     72    -87    282       O  
ATOM   2157  ND2 ASN A 277       1.896  30.805  -5.568  1.00 40.11           N  
ANISOU 2157  ND2 ASN A 277     4496   5686   5059    173     11    342       N  
ATOM   2158  N   GLY A 278      -0.908  26.615  -4.449  1.00 32.47           N  
ANISOU 2158  N   GLY A 278     3344   4824   4170    194     19    473       N  
ATOM   2159  CA  GLY A 278      -2.206  25.969  -4.290  1.00 31.27           C  
ANISOU 2159  CA  GLY A 278     3125   4699   4057    216     39    558       C  
ATOM   2160  C   GLY A 278      -2.493  24.852  -5.276  1.00 30.07           C  
ANISOU 2160  C   GLY A 278     2897   4598   3930    151    -28    579       C  
ATOM   2161  O   GLY A 278      -3.622  24.370  -5.363  1.00 29.83           O  
ANISOU 2161  O   GLY A 278     2800   4594   3939    156    -25    663       O  
ATOM   2162  N   ARG A 279      -1.488  24.440  -6.036  1.00 29.36           N  
ANISOU 2162  N   ARG A 279     2818   4520   3817     90    -88    511       N  
ATOM   2163  CA  ARG A 279      -1.646  23.398  -7.043  1.00 29.31           C  
ANISOU 2163  CA  ARG A 279     2763   4552   3822     24   -153    522       C  
ATOM   2164  C   ARG A 279      -1.174  22.032  -6.538  1.00 27.75           C  
ANISOU 2164  C   ARG A 279     2577   4359   3610      1   -181    476       C  
ATOM   2165  O   ARG A 279      -0.583  21.922  -5.454  1.00 28.12           O  
ANISOU 2165  O   ARG A 279     2668   4380   3636     30   -156    429       O  
ATOM   2166  CB  ARG A 279      -0.919  23.805  -8.332  1.00 31.85           C  
ANISOU 2166  CB  ARG A 279     3094   4882   4127    -24   -193    485       C  
ATOM   2167  CG  ARG A 279      -1.337  25.179  -8.821  1.00 37.96           C  
ANISOU 2167  CG  ARG A 279     3857   5651   4915     -1   -165    528       C  
ATOM   2168  CD  ARG A 279      -0.779  25.486 -10.197  1.00 43.84           C  
ANISOU 2168  CD  ARG A 279     4602   6408   5646    -52   -208    504       C  
ATOM   2169  NE  ARG A 279       0.628  25.892 -10.159  1.00 48.77           N  
ANISOU 2169  NE  ARG A 279     5284   7011   6238    -57   -208    419       N  
ATOM   2170  CZ  ARG A 279       1.048  27.154 -10.162  1.00 52.27           C  
ANISOU 2170  CZ  ARG A 279     5756   7430   6674    -33   -181    405       C  
ATOM   2171  NH1 ARG A 279       2.347  27.429 -10.151  1.00 52.12           N  
ANISOU 2171  NH1 ARG A 279     5782   7392   6629    -46   -190    336       N  
ATOM   2172  NH2 ARG A 279       0.174  28.153 -10.166  1.00 52.82           N  
ANISOU 2172  NH2 ARG A 279     5810   7495   6767      4   -144    466       N  
ATOM   2173  N   THR A 280      -1.469  20.978  -7.302  1.00 25.67           N  
ANISOU 2173  N   THR A 280     2278   4122   3352    -54   -236    493       N  
ATOM   2174  CA  THR A 280      -1.057  19.633  -6.942  1.00 24.28           C  
ANISOU 2174  CA  THR A 280     2115   3949   3163    -79   -265    453       C  
ATOM   2175  C   THR A 280      -0.285  18.960  -8.089  1.00 22.85           C  
ANISOU 2175  C   THR A 280     1952   3776   2954   -143   -322    404       C  
ATOM   2176  O   THR A 280      -0.367  19.376  -9.258  1.00 22.19           O  
ANISOU 2176  O   THR A 280     1861   3702   2867   -176   -348    419       O  
ATOM   2177  CB  THR A 280      -2.285  18.800  -6.544  1.00 24.99           C  
ANISOU 2177  CB  THR A 280     2153   4058   3286    -78   -271    530       C  
ATOM   2178  OG1 THR A 280      -3.107  18.655  -7.698  1.00 25.52           O  
ANISOU 2178  OG1 THR A 280     2174   4150   3374   -126   -318    597       O  
ATOM   2179  CG2 THR A 280      -3.065  19.420  -5.406  1.00 25.24           C  
ANISOU 2179  CG2 THR A 280     2168   4078   3344     -5   -203    585       C  
ATOM   2180  N   ILE A 281       0.448  17.897  -7.738  1.00 21.87           N  
ANISOU 2180  N   ILE A 281     1855   3645   2809   -159   -338    349       N  
ATOM   2181  CA  ILE A 281       1.206  17.061  -8.665  1.00 21.34           C  
ANISOU 2181  CA  ILE A 281     1817   3579   2714   -210   -380    302       C  
ATOM   2182  C   ILE A 281       0.922  15.648  -8.240  1.00 20.70           C  
ANISOU 2182  C   ILE A 281     1732   3500   2633   -228   -404    306       C  
ATOM   2183  O   ILE A 281       1.174  15.298  -7.077  1.00 19.70           O  
ANISOU 2183  O   ILE A 281     1610   3364   2509   -196   -379    285       O  
ATOM   2184  CB  ILE A 281       2.721  17.338  -8.586  1.00 21.64           C  
ANISOU 2184  CB  ILE A 281     1898   3598   2725   -200   -363    224       C  
ATOM   2185  CG1 ILE A 281       3.048  18.766  -9.021  1.00 22.04           C  
ANISOU 2185  CG1 ILE A 281     1954   3644   2776   -185   -343    221       C  
ATOM   2186  CG2 ILE A 281       3.479  16.325  -9.417  1.00 22.43           C  
ANISOU 2186  CG2 ILE A 281     2029   3695   2797   -241   -393    183       C  
ATOM   2187  CD1 ILE A 281       4.525  19.155  -8.818  1.00 22.27           C  
ANISOU 2187  CD1 ILE A 281     2019   3655   2788   -176   -328    157       C  
ATOM   2188  N   LEU A 282       0.347  14.834  -9.141  1.00 20.64           N  
ANISOU 2188  N   LEU A 282     1720   3502   2619   -281   -455    337       N  
ATOM   2189  CA  LEU A 282      -0.032  13.443  -8.845  1.00 20.96           C  
ANISOU 2189  CA  LEU A 282     1762   3543   2660   -307   -487    348       C  
ATOM   2190  C   LEU A 282      -0.848  13.340  -7.557  1.00 22.13           C  
ANISOU 2190  C   LEU A 282     1863   3699   2845   -267   -461    395       C  
ATOM   2191  O   LEU A 282      -0.600  12.470  -6.734  1.00 22.92           O  
ANISOU 2191  O   LEU A 282     1972   3792   2942   -257   -455    370       O  
ATOM   2192  CB  LEU A 282       1.185  12.491  -8.824  1.00 20.78           C  
ANISOU 2192  CB  LEU A 282     1794   3500   2601   -317   -489    268       C  
ATOM   2193  CG  LEU A 282       1.823  12.226 -10.194  1.00 21.43           C  
ANISOU 2193  CG  LEU A 282     1930   3571   2642   -360   -516    234       C  
ATOM   2194  CD1 LEU A 282       3.127  11.455 -10.047  1.00 21.14           C  
ANISOU 2194  CD1 LEU A 282     1943   3513   2578   -351   -498    162       C  
ATOM   2195  CD2 LEU A 282       0.835  11.549 -11.127  1.00 21.45           C  
ANISOU 2195  CD2 LEU A 282     1941   3574   2634   -422   -579    286       C  
ATOM   2196  N   GLY A 283      -1.762  14.288  -7.388  1.00 23.08           N  
ANISOU 2196  N   GLY A 283     1936   3832   3000   -240   -438    464       N  
ATOM   2197  CA  GLY A 283      -2.667  14.342  -6.251  1.00 24.14           C  
ANISOU 2197  CA  GLY A 283     2025   3973   3172   -194   -402    525       C  
ATOM   2198  C   GLY A 283      -2.055  14.776  -4.935  1.00 24.51           C  
ANISOU 2198  C   GLY A 283     2098   4001   3212   -128   -338    478       C  
ATOM   2199  O   GLY A 283      -2.734  14.728  -3.915  1.00 25.14           O  
ANISOU 2199  O   GLY A 283     2154   4082   3316    -84   -302    523       O  
ATOM   2200  N   SER A 284      -0.773  15.170  -4.928  1.00 23.98           N  
ANISOU 2200  N   SER A 284     2084   3916   3111   -121   -325    394       N  
ATOM   2201  CA  SER A 284      -0.106  15.608  -3.706  1.00 24.13           C  
ANISOU 2201  CA  SER A 284     2139   3913   3118    -69   -277    349       C  
ATOM   2202  C   SER A 284       0.140  17.129  -3.727  1.00 24.08           C  
ANISOU 2202  C   SER A 284     2154   3890   3106    -35   -240    343       C  
ATOM   2203  O   SER A 284       0.497  17.665  -4.778  1.00 23.82           O  
ANISOU 2203  O   SER A 284     2124   3861   3064    -62   -259    330       O  
ATOM   2204  CB  SER A 284       1.229  14.878  -3.548  1.00 25.38           C  
ANISOU 2204  CB  SER A 284     2340   4058   3246    -89   -296    266       C  
ATOM   2205  OG  SER A 284       1.954  15.395  -2.441  1.00 27.66           O  
ANISOU 2205  OG  SER A 284     2667   4323   3520    -49   -260    225       O  
ATOM   2206  N   ALA A 285      -0.019  17.817  -2.564  1.00 23.74           N  
ANISOU 2206  N   ALA A 285     2134   3824   3061     24   -185    352       N  
ATOM   2207  CA  ALA A 285       0.302  19.250  -2.497  1.00 24.28           C  
ANISOU 2207  CA  ALA A 285     2239   3868   3117     56   -150    340       C  
ATOM   2208  C   ALA A 285       1.714  19.525  -1.962  1.00 25.07           C  
ANISOU 2208  C   ALA A 285     2406   3938   3181     55   -154    258       C  
ATOM   2209  O   ALA A 285       2.031  20.651  -1.613  1.00 26.64           O  
ANISOU 2209  O   ALA A 285     2650   4107   3363     82   -126    244       O  
ATOM   2210  CB  ALA A 285      -0.730  20.018  -1.694  1.00 24.74           C  
ANISOU 2210  CB  ALA A 285     2298   3911   3191    122    -86    404       C  
ATOM   2211  N   LEU A 286       2.538  18.504  -1.858  1.00 24.57           N  
ANISOU 2211  N   LEU A 286     2350   3881   3107     23   -188    209       N  
ATOM   2212  CA  LEU A 286       3.930  18.643  -1.484  1.00 24.92           C  
ANISOU 2212  CA  LEU A 286     2442   3901   3124     12   -201    143       C  
ATOM   2213  C   LEU A 286       4.778  17.737  -2.389  1.00 23.67           C  
ANISOU 2213  C   LEU A 286     2265   3764   2966    -39   -245    108       C  
ATOM   2214  O   LEU A 286       4.228  16.943  -3.160  1.00 24.15           O  
ANISOU 2214  O   LEU A 286     2288   3849   3038    -64   -265    129       O  
ATOM   2215  CB  LEU A 286       4.168  18.430   0.015  1.00 25.88           C  
ANISOU 2215  CB  LEU A 286     2609   3996   3230     42   -182    125       C  
ATOM   2216  CG  LEU A 286       3.635  17.191   0.668  1.00 28.93           C  
ANISOU 2216  CG  LEU A 286     2973   4395   3625     49   -180    140       C  
ATOM   2217  CD1 LEU A 286       4.532  16.000   0.376  1.00 30.13           C  
ANISOU 2217  CD1 LEU A 286     3111   4562   3777      6   -222     99       C  
ATOM   2218  CD2 LEU A 286       3.603  17.400   2.173  1.00 30.27           C  
ANISOU 2218  CD2 LEU A 286     3198   4531   3774     93   -146    136       C  
ATOM   2219  N   LEU A 287       6.095  17.890  -2.343  1.00 22.28           N  
ANISOU 2219  N   LEU A 287     2116   3573   2776    -54   -260     60       N  
ATOM   2220  CA  LEU A 287       6.979  17.126  -3.191  1.00 22.00           C  
ANISOU 2220  CA  LEU A 287     2067   3551   2740    -92   -288     32       C  
ATOM   2221  C   LEU A 287       7.260  15.753  -2.577  1.00 21.56           C  
ANISOU 2221  C   LEU A 287     2009   3498   2684    -98   -298     14       C  
ATOM   2222  O   LEU A 287       7.927  15.665  -1.552  1.00 21.72           O  
ANISOU 2222  O   LEU A 287     2052   3501   2699    -87   -297     -7       O  
ATOM   2223  CB  LEU A 287       8.257  17.937  -3.470  1.00 23.09           C  
ANISOU 2223  CB  LEU A 287     2226   3675   2872   -104   -296      3       C  
ATOM   2224  CG  LEU A 287       7.989  19.315  -4.099  1.00 25.90           C  
ANISOU 2224  CG  LEU A 287     2586   4026   3227    -99   -286     20       C  
ATOM   2225  CD1 LEU A 287       9.229  20.178  -4.133  1.00 26.95           C  
ANISOU 2225  CD1 LEU A 287     2743   4141   3357   -110   -296     -3       C  
ATOM   2226  CD2 LEU A 287       7.409  19.180  -5.488  1.00 27.49           C  
ANISOU 2226  CD2 LEU A 287     2756   4253   3434   -118   -292     41       C  
ATOM   2227  N   GLU A 288       6.721  14.688  -3.196  1.00 20.11           N  
ANISOU 2227  N   GLU A 288     1801   3333   2505   -117   -312     26       N  
ATOM   2228  CA  GLU A 288       6.881  13.299  -2.756  1.00 19.18           C  
ANISOU 2228  CA  GLU A 288     1682   3219   2388   -124   -322     13       C  
ATOM   2229  C   GLU A 288       8.301  12.731  -2.960  1.00 17.97           C  
ANISOU 2229  C   GLU A 288     1541   3058   2228   -139   -330    -27       C  
ATOM   2230  O   GLU A 288       8.842  12.802  -4.061  1.00 18.16           O  
ANISOU 2230  O   GLU A 288     1568   3084   2247   -157   -334    -36       O  
ATOM   2231  CB  GLU A 288       5.844  12.410  -3.455  1.00 21.55           C  
ANISOU 2231  CB  GLU A 288     1961   3536   2692   -146   -340     43       C  
ATOM   2232  CG  GLU A 288       4.417  12.805  -3.124  1.00 28.16           C  
ANISOU 2232  CG  GLU A 288     2771   4383   3545   -130   -331     98       C  
ATOM   2233  CD  GLU A 288       4.046  12.549  -1.671  1.00 36.32           C  
ANISOU 2233  CD  GLU A 288     3804   5410   4587    -95   -310    109       C  
ATOM   2234  OE1 GLU A 288       4.521  11.535  -1.104  1.00 36.51           O  
ANISOU 2234  OE1 GLU A 288     3836   5429   4606    -99   -318     84       O  
ATOM   2235  OE2 GLU A 288       3.270  13.352  -1.104  1.00 37.93           O  
ANISOU 2235  OE2 GLU A 288     4001   5611   4800    -60   -281    146       O  
ATOM   2236  N   ASP A 289       8.893  12.151  -1.910  1.00 16.31           N  
ANISOU 2236  N   ASP A 289     1338   2838   2020   -130   -329    -45       N  
ATOM   2237  CA  ASP A 289      10.248  11.594  -1.999  1.00 15.81           C  
ANISOU 2237  CA  ASP A 289     1279   2769   1960   -139   -333    -70       C  
ATOM   2238  C   ASP A 289      10.346  10.119  -1.616  1.00 16.26           C  
ANISOU 2238  C   ASP A 289     1333   2826   2018   -141   -336    -79       C  
ATOM   2239  O   ASP A 289      11.462   9.630  -1.366  1.00 16.39           O  
ANISOU 2239  O   ASP A 289     1349   2835   2042   -142   -334    -93       O  
ATOM   2240  CB  ASP A 289      11.260  12.433  -1.193  1.00 15.69           C  
ANISOU 2240  CB  ASP A 289     1274   2738   1949   -133   -335    -80       C  
ATOM   2241  CG  ASP A 289      11.180  12.286   0.329  1.00 19.15           C  
ANISOU 2241  CG  ASP A 289     1729   3163   2385   -118   -340    -82       C  
ATOM   2242  OD1 ASP A 289      10.158  11.769   0.827  1.00 18.99           O  
ANISOU 2242  OD1 ASP A 289     1707   3147   2361   -105   -332    -72       O  
ATOM   2243  OD2 ASP A 289      12.164  12.644   1.012  1.00 19.56           O  
ANISOU 2243  OD2 ASP A 289     1794   3199   2439   -123   -353    -89       O  
ATOM   2244  N   GLU A 290       9.214   9.392  -1.614  1.00 16.32           N  
ANISOU 2244  N   GLU A 290     1336   2842   2024   -145   -341    -64       N  
ATOM   2245  CA  GLU A 290       9.280   7.968  -1.262  1.00 17.85           C  
ANISOU 2245  CA  GLU A 290     1530   3034   2218   -149   -346    -72       C  
ATOM   2246  C   GLU A 290       8.983   7.068  -2.499  1.00 18.08           C  
ANISOU 2246  C   GLU A 290     1574   3063   2234   -174   -355    -70       C  
ATOM   2247  O   GLU A 290       8.440   5.965  -2.373  1.00 18.90           O  
ANISOU 2247  O   GLU A 290     1682   3165   2334   -184   -367    -64       O  
ATOM   2248  CB  GLU A 290       8.453   7.629   0.007  1.00 19.96           C  
ANISOU 2248  CB  GLU A 290     1788   3303   2492   -132   -347    -56       C  
ATOM   2249  CG  GLU A 290       9.032   8.327   1.239  1.00 23.87           C  
ANISOU 2249  CG  GLU A 290     2292   3788   2989   -110   -338    -66       C  
ATOM   2250  CD  GLU A 290       8.607   7.793   2.600  1.00 30.60           C  
ANISOU 2250  CD  GLU A 290     3147   4636   3843    -91   -335    -59       C  
ATOM   2251  OE1 GLU A 290       7.719   6.913   2.630  1.00 29.10           O  
ANISOU 2251  OE1 GLU A 290     2942   4456   3658    -93   -337    -41       O  
ATOM   2252  OE2 GLU A 290       9.162   8.244   3.635  1.00 34.72           O  
ANISOU 2252  OE2 GLU A 290     3689   5143   4359    -78   -333    -69       O  
ATOM   2253  N   PHE A 291       9.450   7.521  -3.681  1.00 17.02           N  
ANISOU 2253  N   PHE A 291     1453   2925   2087   -185   -350    -77       N  
ATOM   2254  CA  PHE A 291       9.487   6.731  -4.924  1.00 17.61           C  
ANISOU 2254  CA  PHE A 291     1562   2989   2139   -208   -354    -82       C  
ATOM   2255  C   PHE A 291      10.900   6.838  -5.475  1.00 16.57           C  
ANISOU 2255  C   PHE A 291     1446   2847   2005   -196   -325   -103       C  
ATOM   2256  O   PHE A 291      11.290   7.923  -5.871  1.00 15.91           O  
ANISOU 2256  O   PHE A 291     1352   2768   1925   -192   -317   -100       O  
ATOM   2257  CB  PHE A 291       8.553   7.277  -6.013  1.00 18.04           C  
ANISOU 2257  CB  PHE A 291     1626   3051   2178   -233   -374    -61       C  
ATOM   2258  CG  PHE A 291       7.081   7.204  -5.715  1.00 18.84           C  
ANISOU 2258  CG  PHE A 291     1706   3165   2288   -249   -404    -24       C  
ATOM   2259  CD1 PHE A 291       6.370   6.040  -5.946  1.00 19.69           C  
ANISOU 2259  CD1 PHE A 291     1832   3266   2383   -278   -432    -10       C  
ATOM   2260  CD2 PHE A 291       6.396   8.319  -5.265  1.00 19.57           C  
ANISOU 2260  CD2 PHE A 291     1762   3274   2400   -235   -402      4       C  
ATOM   2261  CE1 PHE A 291       5.000   5.991  -5.708  1.00 20.62           C  
ANISOU 2261  CE1 PHE A 291     1921   3398   2516   -295   -462     37       C  
ATOM   2262  CE2 PHE A 291       5.034   8.265  -5.026  1.00 20.39           C  
ANISOU 2262  CE2 PHE A 291     1838   3391   2517   -244   -422     51       C  
ATOM   2263  CZ  PHE A 291       4.341   7.105  -5.261  1.00 20.39           C  
ANISOU 2263  CZ  PHE A 291     1846   3388   2512   -275   -454     71       C  
ATOM   2264  N   THR A 292      11.645   5.734  -5.565  1.00 16.55           N  
ANISOU 2264  N   THR A 292     1465   2827   1995   -189   -307   -116       N  
ATOM   2265  CA  THR A 292      12.982   5.762  -6.174  1.00 17.21           C  
ANISOU 2265  CA  THR A 292     1561   2899   2081   -172   -271   -123       C  
ATOM   2266  C   THR A 292      12.826   5.807  -7.722  1.00 18.10           C  
ANISOU 2266  C   THR A 292     1724   2998   2157   -186   -262   -125       C  
ATOM   2267  O   THR A 292      11.762   5.437  -8.247  1.00 17.04           O  
ANISOU 2267  O   THR A 292     1622   2857   1994   -214   -290   -122       O  
ATOM   2268  CB  THR A 292      13.765   4.468  -5.835  1.00 18.33           C  
ANISOU 2268  CB  THR A 292     1715   3022   2226   -154   -246   -130       C  
ATOM   2269  OG1 THR A 292      13.129   3.341  -6.467  1.00 20.12           O  
ANISOU 2269  OG1 THR A 292     1999   3228   2418   -170   -250   -139       O  
ATOM   2270  CG2 THR A 292      13.960   4.246  -4.311  1.00 18.59           C  
ANISOU 2270  CG2 THR A 292     1706   3065   2291   -143   -257   -128       C  
ATOM   2271  N   PRO A 293      13.897   6.125  -8.472  1.00 18.86           N  
ANISOU 2271  N   PRO A 293     1829   3084   2251   -168   -224   -123       N  
ATOM   2272  CA  PRO A 293      13.816   6.026  -9.936  1.00 19.75           C  
ANISOU 2272  CA  PRO A 293     2005   3178   2323   -178   -209   -126       C  
ATOM   2273  C   PRO A 293      13.434   4.608 -10.383  1.00 21.04           C  
ANISOU 2273  C   PRO A 293     2241   3309   2444   -189   -209   -138       C  
ATOM   2274  O   PRO A 293      12.677   4.454 -11.331  1.00 20.94           O  
ANISOU 2274  O   PRO A 293     2287   3281   2388   -219   -231   -140       O  
ATOM   2275  CB  PRO A 293      15.240   6.375 -10.377  1.00 20.55           C  
ANISOU 2275  CB  PRO A 293     2097   3271   2438   -144   -155   -117       C  
ATOM   2276  CG  PRO A 293      15.750   7.260  -9.276  1.00 20.24           C  
ANISOU 2276  CG  PRO A 293     1980   3258   2451   -135   -166   -104       C  
ATOM   2277  CD  PRO A 293      15.229   6.599  -8.048  1.00 18.83           C  
ANISOU 2277  CD  PRO A 293     1783   3086   2285   -140   -194   -113       C  
ATOM   2278  N   PHE A 294      13.885   3.580  -9.651  1.00 22.47           N  
ANISOU 2278  N   PHE A 294     2422   3478   2638   -170   -191   -144       N  
ATOM   2279  CA  PHE A 294      13.545   2.192  -9.997  1.00 23.76           C  
ANISOU 2279  CA  PHE A 294     2661   3606   2760   -181   -191   -156       C  
ATOM   2280  C   PHE A 294      12.050   1.909  -9.785  1.00 22.53           C  
ANISOU 2280  C   PHE A 294     2514   3457   2590   -228   -258   -154       C  
ATOM   2281  O   PHE A 294      11.443   1.242 -10.612  1.00 23.12           O  
ANISOU 2281  O   PHE A 294     2666   3502   2616   -259   -279   -157       O  
ATOM   2282  CB  PHE A 294      14.438   1.194  -9.253  1.00 25.97           C  
ANISOU 2282  CB  PHE A 294     2934   3872   3062   -145   -152   -159       C  
ATOM   2283  CG  PHE A 294      15.899   1.308  -9.628  1.00 29.71           C  
ANISOU 2283  CG  PHE A 294     3404   4335   3551    -98    -81   -147       C  
ATOM   2284  CD1 PHE A 294      16.385   0.720 -10.787  1.00 31.82           C  
ANISOU 2284  CD1 PHE A 294     3757   4558   3773    -78    -29   -149       C  
ATOM   2285  CD2 PHE A 294      16.788   2.010  -8.825  1.00 32.21           C  
ANISOU 2285  CD2 PHE A 294     3634   4679   3924    -74    -68   -127       C  
ATOM   2286  CE1 PHE A 294      17.735   0.821 -11.130  1.00 33.28           C  
ANISOU 2286  CE1 PHE A 294     3932   4733   3978    -28     45   -127       C  
ATOM   2287  CE2 PHE A 294      18.141   2.105  -9.170  1.00 33.43           C  
ANISOU 2287  CE2 PHE A 294     3774   4826   4102    -33     -5   -102       C  
ATOM   2288  CZ  PHE A 294      18.600   1.519 -10.327  1.00 33.39           C  
ANISOU 2288  CZ  PHE A 294     3845   4781   4059     -6     55    -99       C  
ATOM   2289  N   ASP A 295      11.452   2.457  -8.723  1.00 21.10           N  
ANISOU 2289  N   ASP A 295     2257   3311   2447   -234   -291   -142       N  
ATOM   2290  CA  ASP A 295      10.023   2.310  -8.443  1.00 21.01           C  
ANISOU 2290  CA  ASP A 295     2236   3311   2433   -273   -349   -126       C  
ATOM   2291  C   ASP A 295       9.205   2.956  -9.555  1.00 20.51           C  
ANISOU 2291  C   ASP A 295     2199   3249   2343   -310   -381   -109       C  
ATOM   2292  O   ASP A 295       8.183   2.412  -9.958  1.00 20.23           O  
ANISOU 2292  O   ASP A 295     2199   3203   2283   -354   -428    -93       O  
ATOM   2293  CB  ASP A 295       9.652   3.019  -7.136  1.00 22.73           C  
ANISOU 2293  CB  ASP A 295     2370   3566   2699   -260   -361   -112       C  
ATOM   2294  CG  ASP A 295      10.153   2.366  -5.872  1.00 25.39           C  
ANISOU 2294  CG  ASP A 295     2679   3906   3064   -233   -345   -121       C  
ATOM   2295  OD1 ASP A 295      10.554   1.185  -5.933  1.00 25.59           O  
ANISOU 2295  OD1 ASP A 295     2743   3906   3075   -230   -332   -134       O  
ATOM   2296  OD2 ASP A 295      10.170   3.051  -4.821  1.00 26.20           O  
ANISOU 2296  OD2 ASP A 295     2725   4031   3199   -216   -345   -115       O  
ATOM   2297  N   VAL A 296       9.615   4.156 -10.007  1.00 20.09           N  
ANISOU 2297  N   VAL A 296     2125   3211   2297   -297   -362   -108       N  
ATOM   2298  CA  VAL A 296       8.897   4.876 -11.068  1.00 20.17           C  
ANISOU 2298  CA  VAL A 296     2155   3224   2284   -331   -392    -90       C  
ATOM   2299  C   VAL A 296       8.956   4.056 -12.353  1.00 20.96           C  
ANISOU 2299  C   VAL A 296     2359   3283   2323   -357   -396   -100       C  
ATOM   2300  O   VAL A 296       7.913   3.786 -12.944  1.00 20.84           O  
ANISOU 2300  O   VAL A 296     2381   3258   2279   -408   -450    -80       O  
ATOM   2301  CB  VAL A 296       9.435   6.316 -11.271  1.00 19.79           C  
ANISOU 2301  CB  VAL A 296     2066   3198   2257   -308   -366    -89       C  
ATOM   2302  CG1 VAL A 296       8.849   6.952 -12.534  1.00 19.96           C  
ANISOU 2302  CG1 VAL A 296     2119   3218   2248   -341   -391    -72       C  
ATOM   2303  CG2 VAL A 296       9.149   7.175 -10.046  1.00 19.99           C  
ANISOU 2303  CG2 VAL A 296     2007   3256   2331   -290   -372    -76       C  
ATOM   2304  N   VAL A 297      10.154   3.600 -12.741  1.00 21.52           N  
ANISOU 2304  N   VAL A 297     2479   3324   2372   -324   -339   -126       N  
ATOM   2305  CA  VAL A 297      10.338   2.743 -13.932  1.00 23.20           C  
ANISOU 2305  CA  VAL A 297     2811   3486   2518   -339   -328   -140       C  
ATOM   2306  C   VAL A 297       9.434   1.489 -13.848  1.00 24.34           C  
ANISOU 2306  C   VAL A 297     3013   3602   2631   -383   -380   -137       C  
ATOM   2307  O   VAL A 297       8.667   1.210 -14.779  1.00 24.83           O  
ANISOU 2307  O   VAL A 297     3153   3638   2642   -436   -428   -126       O  
ATOM   2308  CB  VAL A 297      11.837   2.362 -14.112  1.00 24.67           C  
ANISOU 2308  CB  VAL A 297     3029   3645   2698   -281   -244   -160       C  
ATOM   2309  CG1 VAL A 297      12.013   1.225 -15.130  1.00 25.61           C  
ANISOU 2309  CG1 VAL A 297     3286   3701   2743   -287   -222   -175       C  
ATOM   2310  CG2 VAL A 297      12.662   3.581 -14.530  1.00 25.21           C  
ANISOU 2310  CG2 VAL A 297     3058   3733   2786   -249   -201   -154       C  
ATOM   2311  N   ARG A 298       9.507   0.772 -12.711  1.00 24.33           N  
ANISOU 2311  N   ARG A 298     2973   3608   2663   -366   -376   -141       N  
ATOM   2312  CA  ARG A 298       8.723  -0.425 -12.436  1.00 25.32           C  
ANISOU 2312  CA  ARG A 298     3140   3710   2769   -404   -422   -136       C  
ATOM   2313  C   ARG A 298       7.234  -0.168 -12.605  1.00 26.07           C  
ANISOU 2313  C   ARG A 298     3218   3823   2864   -469   -508    -97       C  
ATOM   2314  O   ARG A 298       6.589  -0.826 -13.419  1.00 26.72           O  
ANISOU 2314  O   ARG A 298     3389   3869   2895   -524   -558    -87       O  
ATOM   2315  CB  ARG A 298       9.037  -0.951 -11.020  1.00 27.81           C  
ANISOU 2315  CB  ARG A 298     3388   4044   3134   -369   -403   -142       C  
ATOM   2316  CG  ARG A 298       8.448  -2.337 -10.754  1.00 32.58           C  
ANISOU 2316  CG  ARG A 298     4043   4618   3718   -401   -439   -140       C  
ATOM   2317  CD  ARG A 298       8.692  -2.830  -9.329  1.00 37.03           C  
ANISOU 2317  CD  ARG A 298     4537   5202   4331   -368   -422   -143       C  
ATOM   2318  NE  ARG A 298      10.113  -2.945  -9.004  1.00 41.51           N  
ANISOU 2318  NE  ARG A 298     5096   5762   4914   -306   -346   -168       N  
ATOM   2319  CZ  ARG A 298      10.736  -2.216  -8.080  1.00 45.73           C  
ANISOU 2319  CZ  ARG A 298     5538   6336   5503   -266   -316   -166       C  
ATOM   2320  NH1 ARG A 298      12.034  -2.389  -7.851  1.00 46.57           N  
ANISOU 2320  NH1 ARG A 298     5636   6433   5625   -216   -253   -178       N  
ATOM   2321  NH2 ARG A 298      10.064  -1.313  -7.370  1.00 44.95           N  
ANISOU 2321  NH2 ARG A 298     5356   6281   5441   -276   -350   -148       N  
ATOM   2322  N   GLN A 299       6.698   0.838 -11.907  1.00 26.26           N  
ANISOU 2322  N   GLN A 299     3134   3900   2944   -464   -524    -70       N  
ATOM   2323  CA  GLN A 299       5.279   1.143 -11.988  1.00 26.90           C  
ANISOU 2323  CA  GLN A 299     3181   4002   3037   -518   -597    -20       C  
ATOM   2324  C   GLN A 299       4.829   1.583 -13.355  1.00 29.05           C  
ANISOU 2324  C   GLN A 299     3512   4260   3266   -566   -636     -2       C  
ATOM   2325  O   GLN A 299       3.793   1.121 -13.834  1.00 29.41           O  
ANISOU 2325  O   GLN A 299     3594   4292   3290   -631   -708     36       O  
ATOM   2326  CB  GLN A 299       4.876   2.162 -10.936  1.00 26.77           C  
ANISOU 2326  CB  GLN A 299     3044   4039   3087   -490   -591      7       C  
ATOM   2327  CG  GLN A 299       3.370   2.274 -10.820  1.00 26.95           C  
ANISOU 2327  CG  GLN A 299     3023   4085   3134   -537   -658     72       C  
ATOM   2328  CD  GLN A 299       2.913   3.096  -9.652  1.00 26.28           C  
ANISOU 2328  CD  GLN A 299     2829   4045   3112   -501   -642    102       C  
ATOM   2329  OE1 GLN A 299       1.765   3.524  -9.613  1.00 27.16           O  
ANISOU 2329  OE1 GLN A 299     2890   4180   3251   -526   -680    164       O  
ATOM   2330  NE2 GLN A 299       3.768   3.320  -8.669  1.00 24.11           N  
ANISOU 2330  NE2 GLN A 299     2520   3780   2861   -444   -586     66       N  
ATOM   2331  N   CYS A 300       5.609   2.458 -14.003  1.00 30.13           N  
ANISOU 2331  N   CYS A 300     3661   4398   3390   -537   -591    -24       N  
ATOM   2332  CA  CYS A 300       5.260   2.985 -15.312  1.00 32.30           C  
ANISOU 2332  CA  CYS A 300     3991   4660   3623   -579   -622     -8       C  
ATOM   2333  C   CYS A 300       5.404   1.955 -16.448  1.00 35.18           C  
ANISOU 2333  C   CYS A 300     4505   4960   3903   -617   -639    -27       C  
ATOM   2334  O   CYS A 300       4.909   2.212 -17.542  1.00 35.75           O  
ANISOU 2334  O   CYS A 300     4637   5015   3930   -667   -683     -8       O  
ATOM   2335  CB  CYS A 300       6.033   4.269 -15.612  1.00 32.41           C  
ANISOU 2335  CB  CYS A 300     3967   4695   3651   -535   -568    -23       C  
ATOM   2336  SG  CYS A 300       5.635   5.654 -14.507  1.00 35.43           S  
ANISOU 2336  SG  CYS A 300     4201   5143   4117   -504   -562      6       S  
ATOM   2337  N   SER A 301       6.058   0.805 -16.204  1.00 36.93           N  
ANISOU 2337  N   SER A 301     4790   5142   4098   -595   -606    -62       N  
ATOM   2338  CA  SER A 301       6.228  -0.224 -17.238  1.00 39.68           C  
ANISOU 2338  CA  SER A 301     5297   5419   4360   -626   -614    -82       C  
ATOM   2339  C   SER A 301       5.400  -1.492 -17.013  1.00 42.98           C  
ANISOU 2339  C   SER A 301     5771   5804   4754   -683   -683    -66       C  
ATOM   2340  O   SER A 301       5.213  -2.272 -17.947  1.00 43.13           O  
ANISOU 2340  O   SER A 301     5932   5760   4694   -731   -716    -72       O  
ATOM   2341  CB  SER A 301       7.699  -0.590 -17.402  1.00 40.82           C  
ANISOU 2341  CB  SER A 301     5502   5529   4480   -554   -512   -130       C  
ATOM   2342  OG  SER A 301       8.163  -1.321 -16.280  1.00 43.13           O  
ANISOU 2342  OG  SER A 301     5751   5826   4810   -512   -476   -146       O  
ATOM   2343  N   GLY A 302       4.946  -1.708 -15.779  1.00 45.31           N  
ANISOU 2343  N   GLY A 302     5965   6138   5115   -678   -702    -47       N  
ATOM   2344  CA  GLY A 302       4.134  -2.866 -15.426  1.00 47.57           C  
ANISOU 2344  CA  GLY A 302     6284   6400   5391   -731   -768    -25       C  
ATOM   2345  C   GLY A 302       4.947  -4.078 -15.024  1.00 49.82           C  
ANISOU 2345  C   GLY A 302     6636   6641   5653   -694   -717    -69       C  
ATOM   2346  O   GLY A 302       4.588  -5.203 -15.389  1.00 50.44           O  
ANISOU 2346  O   GLY A 302     6824   6663   5677   -743   -762    -68       O  
ATOM   2347  N   VAL A 303       6.049  -3.869 -14.271  1.00 50.44           N  
ANISOU 2347  N   VAL A 303     6652   6742   5773   -611   -627   -103       N  
ATOM   2348  CA  VAL A 303       6.894  -4.988 -13.837  1.00 51.80           C  
ANISOU 2348  CA  VAL A 303     6875   6876   5931   -568   -570   -138       C  
ATOM   2349  C   VAL A 303       6.189  -5.866 -12.797  1.00 51.65           C  
ANISOU 2349  C   VAL A 303     6813   6865   5945   -593   -618   -119       C  
ATOM   2350  O   VAL A 303       5.715  -5.365 -11.782  1.00 51.57           O  
ANISOU 2350  O   VAL A 303     6675   6914   6004   -586   -636    -93       O  
ATOM   2351  CB  VAL A 303       8.310  -4.548 -13.364  1.00 52.45           C  
ANISOU 2351  CB  VAL A 303     6901   6979   6051   -476   -465   -169       C  
ATOM   2352  CG1 VAL A 303       9.078  -5.710 -12.735  1.00 52.85           C  
ANISOU 2352  CG1 VAL A 303     6979   6997   6103   -433   -412   -192       C  
ATOM   2353  CG2 VAL A 303       9.110  -3.949 -14.513  1.00 52.88           C  
ANISOU 2353  CG2 VAL A 303     7021   7008   6062   -450   -410   -186       C  
ATOM   2354  N   THR A 304       6.112  -7.174 -13.065  1.00 51.27           N  
ANISOU 2354  N   THR A 304     6881   6755   5844   -621   -637   -130       N  
ATOM   2355  CA  THR A 304       5.489  -8.132 -12.161  1.00 51.57           C  
ANISOU 2355  CA  THR A 304     6894   6794   5908   -647   -683   -112       C  
ATOM   2356  C   THR A 304       6.529  -9.159 -11.709  1.00 51.90           C  
ANISOU 2356  C   THR A 304     6981   6797   5940   -589   -609   -152       C  
ATOM   2357  O   THR A 304       6.335  -9.834 -10.699  1.00 52.21           O  
ANISOU 2357  O   THR A 304     6967   6851   6019   -584   -619   -145       O  
ATOM   2358  CB  THR A 304       4.287  -8.788 -12.851  1.00 52.47           C  
ANISOU 2358  CB  THR A 304     7099   6867   5972   -747   -791    -76       C  
ATOM   2359  OG1 THR A 304       4.746  -9.489 -14.007  1.00 53.45           O  
ANISOU 2359  OG1 THR A 304     7404   6906   5999   -763   -779   -109       O  
ATOM   2360  CG2 THR A 304       3.250  -7.776 -13.276  1.00 52.62           C  
ANISOU 2360  CG2 THR A 304     7059   6927   6009   -803   -864    -24       C  
TER    2361      THR A 304                                                      
HETATM 2362  S   DMS A 401       7.094 -28.187  21.313  1.00 31.26           S  
ANISOU 2362  S   DMS A 401     3102   4543   4233    -89   -479    149       S  
HETATM 2363  O   DMS A 401       7.653 -27.120  22.137  1.00 31.35           O  
ANISOU 2363  O   DMS A 401     3079   4589   4244    -57   -458    143       O  
HETATM 2364  C1  DMS A 401       5.811 -28.923  22.289  1.00 30.77           C  
ANISOU 2364  C1  DMS A 401     3004   4497   4191   -102   -506    201       C  
HETATM 2365  C2  DMS A 401       6.101 -27.378  20.085  1.00 30.98           C  
ANISOU 2365  C2  DMS A 401     3084   4507   4178   -124   -504    153       C  
HETATM 2366  S   DMS A 402       6.227  -0.986  -6.433  1.00 38.46           S  
ANISOU 2366  S   DMS A 402     4437   5518   4657   -378   -509    -53       S  
HETATM 2367  O   DMS A 402       7.220  -0.602  -7.434  1.00 38.42           O  
ANISOU 2367  O   DMS A 402     4483   5493   4621   -366   -474    -83       O  
HETATM 2368  C1  DMS A 402       7.142  -0.921  -4.925  1.00 38.75           C  
ANISOU 2368  C1  DMS A 402     4412   5574   4736   -318   -459    -75       C  
HETATM 2369  C2  DMS A 402       6.083  -2.726  -6.573  1.00 38.38           C  
ANISOU 2369  C2  DMS A 402     4503   5466   4615   -408   -533    -61       C  
HETATM 2370  S   DMS A 403       2.376 -19.260   8.173  1.00 57.48           S  
ANISOU 2370  S   DMS A 403     6683   7829   7330   -398   -689    133       S  
HETATM 2371  O   DMS A 403       3.708 -19.044   8.786  1.00 57.32           O  
ANISOU 2371  O   DMS A 403     6655   7815   7311   -336   -622     81       O  
HETATM 2372  C1  DMS A 403       1.324 -18.032   8.903  1.00 57.39           C  
ANISOU 2372  C1  DMS A 403     6565   7880   7361   -382   -690    194       C  
HETATM 2373  C2  DMS A 403       1.726 -20.684   9.019  1.00 57.41           C  
ANISOU 2373  C2  DMS A 403     6662   7808   7343   -421   -723    172       C  
HETATM 2374  S   DMS A 404      21.050  14.556   7.669  1.00 77.44           S  
ANISOU 2374  S   DMS A 404     9234  10367   9824   -356   -706     40       S  
HETATM 2375  O   DMS A 404      22.416  15.080   7.794  1.00 77.51           O  
ANISOU 2375  O   DMS A 404     9223  10363   9864   -411   -771     93       O  
HETATM 2376  C1  DMS A 404      20.942  13.315   8.914  1.00 77.44           C  
ANISOU 2376  C1  DMS A 404     9245  10365   9814   -350   -715     34       C  
HETATM 2377  C2  DMS A 404      21.105  13.476   6.277  1.00 77.31           C  
ANISOU 2377  C2  DMS A 404     9117  10402   9857   -319   -640     43       C  
HETATM 2378  N1  LJO A 405       8.049   0.142  21.490  0.68 24.39           N  
ANISOU 2378  N1  LJO A 405     2719   3679   2868    134   -288     -9       N  
HETATM 2379  C4  LJO A 405       7.740   0.129  19.034  0.68 22.91           C  
ANISOU 2379  C4  LJO A 405     2408   3544   2752    110   -289    -10       C  
HETATM 2380  C5  LJO A 405       7.252   0.312  20.333  0.68 23.66           C  
ANISOU 2380  C5  LJO A 405     2568   3613   2809    146   -261      5       C  
HETATM 2381  C6  LJO A 405       9.383   0.122  21.591  0.68 24.88           C  
ANISOU 2381  C6  LJO A 405     2794   3733   2928     88   -345    -33       C  
HETATM 2382  C7  LJO A 405       9.999  -0.709  22.734  0.68 25.92           C  
ANISOU 2382  C7  LJO A 405     2948   3854   3047     73   -375    -33       C  
HETATM 2383  C8  LJO A 405       9.050  -1.137  23.885  0.68 26.34           C  
ANISOU 2383  C8  LJO A 405     3040   3895   3071    118   -333    -12       C  
HETATM 2384  C10 LJO A 405      10.611  -2.030  22.254  0.68 26.30           C  
ANISOU 2384  C10 LJO A 405     2906   3936   3151     44   -403    -34       C  
HETATM 2385  N2  LJO A 405      11.900   0.810  23.673  0.68 26.65           N  
ANISOU 2385  N2  LJO A 405     3175   3880   3071      7   -466    -53       N  
HETATM 2386  C11 LJO A 405      11.081   0.119  23.294  0.68 26.19           C  
ANISOU 2386  C11 LJO A 405     3058   3852   3043     38   -424    -46       C  
HETATM 2387  O1  LJO A 405      10.585  -2.871  23.402  0.68 26.86           O  
ANISOU 2387  O1  LJO A 405     2994   4002   3211     52   -406    -24       O  
HETATM 2388  C9  LJO A 405       9.329  -2.622  24.035  0.68 26.68           C  
ANISOU 2388  C9  LJO A 405     3015   3967   3156    102   -353     -7       C  
HETATM 2389  O   LJO A 405      10.102   0.862  20.945  0.68 24.73           O  
ANISOU 2389  O   LJO A 405     2779   3708   2911     59   -372    -48       O  
HETATM 2390  C1  LJO A 405       5.899   0.632  20.496  0.68 23.59           C  
ANISOU 2390  C1  LJO A 405     2565   3605   2795    197   -201     42       C  
HETATM 2391  C   LJO A 405       5.296   0.865  21.858  0.68 23.93           C  
ANISOU 2391  C   LJO A 405     2684   3616   2793    247   -156     65       C  
HETATM 2392  N   LJO A 405       7.005   0.312  17.932  0.68 22.32           N  
ANISOU 2392  N   LJO A 405     2286   3490   2704    115   -270      4       N  
HETATM 2393  C3  LJO A 405       5.733   0.683  18.103  0.68 22.86           C  
ANISOU 2393  C3  LJO A 405     2358   3559   2767    158   -222     41       C  
HETATM 2394  C2  LJO A 405       5.145   0.839  19.344  0.68 23.41           C  
ANISOU 2394  C2  LJO A 405     2482   3607   2806    202   -183     63       C  
HETATM 2395  O   HOH A 501       9.566 -23.297  22.968  1.00 26.09           O  
HETATM 2396  O   HOH A 502      24.329  -5.664   8.767  1.00 27.19           O  
HETATM 2397  O   HOH A 503       6.445  10.065  -1.034  1.00 22.02           O  
HETATM 2398  O   HOH A 504      12.401 -27.096  22.642  1.00 22.59           O  
HETATM 2399  O   HOH A 505      21.599 -20.531  30.428  1.00 32.30           O  
HETATM 2400  O   HOH A 506      24.794  29.261  -8.535  1.00 33.98           O  
HETATM 2401  O   HOH A 507      19.541   5.501  -1.553  1.00 43.29           O  
HETATM 2402  O   HOH A 508      -3.114  28.542  -7.922  1.00 23.48           O  
HETATM 2403  O   HOH A 509       5.571 -17.543   1.694  1.00 27.85           O  
HETATM 2404  O   HOH A 510       0.183   4.238 -14.585  1.00 30.63           O  
HETATM 2405  O   HOH A 511      15.358  18.642 -21.860  1.00 22.14           O  
HETATM 2406  O   HOH A 512      10.842 -24.579   2.870  1.00 22.08           O  
HETATM 2407  O   HOH A 513       8.578   4.427  22.340  1.00 27.63           O  
HETATM 2408  O   HOH A 514      12.017 -32.668  16.737  1.00 31.40           O  
HETATM 2409  O   HOH A 515      17.364  -6.229  33.545  1.00 36.53           O  
HETATM 2410  O   HOH A 516       4.863  24.533 -18.176  1.00 36.99           O  
HETATM 2411  O   HOH A 517      13.329  23.191 -18.342  1.00 31.87           O  
HETATM 2412  O   HOH A 518      16.667  28.318 -20.269  1.00 26.99           O  
HETATM 2413  O   HOH A 519      24.748   4.883  18.756  1.00 27.01           O  
HETATM 2414  O   HOH A 520       7.919   3.483  -3.678  1.00 17.87           O  
HETATM 2415  O   HOH A 521      11.833  31.892  -2.564  1.00 32.17           O  
HETATM 2416  O   HOH A 522       8.677  24.569 -11.750  1.00 22.37           O  
HETATM 2417  O   HOH A 523      20.572 -18.349  26.254  1.00 22.96           O  
HETATM 2418  O   HOH A 524       4.841  27.024  -8.555  1.00 40.02           O  
HETATM 2419  O   HOH A 525       3.841   4.393  22.519  1.00 32.27           O  
HETATM 2420  O   HOH A 526      23.618  22.779 -17.211  1.00 17.79           O  
HETATM 2421  O   HOH A 527      16.770   6.714  -3.943  1.00 20.13           O  
HETATM 2422  O   HOH A 528       6.032  -8.390   8.517  1.00 23.55           O  
HETATM 2423  O   HOH A 529      15.983 -27.842  11.939  1.00 31.75           O  
HETATM 2424  O   HOH A 530       8.220  16.336   0.937  1.00 29.55           O  
HETATM 2425  O   HOH A 531      18.842  10.158  13.037  1.00 26.58           O  
HETATM 2426  O   HOH A 532      20.682 -13.063  10.524  1.00 32.70           O  
HETATM 2427  O   HOH A 533       7.010 -23.153  20.646  1.00 28.28           O  
HETATM 2428  O   HOH A 534       0.300  -1.029  12.313  1.00 25.74           O  
HETATM 2429  O   HOH A 535      12.026 -22.182  -8.317  1.00 34.23           O  
HETATM 2430  O   HOH A 536      21.576  -0.813  28.234  1.00 43.77           O  
HETATM 2431  O   HOH A 537      13.378 -24.398   3.642  1.00 24.80           O  
HETATM 2432  O   HOH A 538      22.104  19.597   0.563  1.00 30.02           O  
HETATM 2433  O   HOH A 539       3.135   9.480 -21.223  1.00 40.91           O  
HETATM 2434  O   HOH A 540      13.494   1.002  -5.292  1.00 26.02           O  
HETATM 2435  O   HOH A 541       5.302 -17.491  28.171  1.00 46.23           O  
HETATM 2436  O   HOH A 542       1.527  14.204   0.698  1.00 55.44           O  
HETATM 2437  O   HOH A 543       6.263   8.630  12.281  1.00 34.32           O  
HETATM 2438  O   HOH A 544       8.458 -18.180  28.189  1.00 39.75           O  
HETATM 2439  O   HOH A 545      -1.547 -15.063   2.706  1.00 32.30           O  
HETATM 2440  O   HOH A 546      22.020   9.914   5.107  1.00 46.90           O  
HETATM 2441  O   HOH A 547      22.660   1.952   5.088  1.00 31.25           O  
HETATM 2442  O   HOH A 548      11.694  21.775 -16.891  1.00 32.17           O  
HETATM 2443  O   HOH A 549      13.301  19.178   3.318  1.00 45.79           O  
HETATM 2444  O   HOH A 550      27.319  26.197 -11.366  1.00 31.18           O  
HETATM 2445  O   HOH A 551       3.741   4.488 -18.309  1.00 36.43           O  
HETATM 2446  O   HOH A 552       4.086 -10.263 -16.481  1.00 55.76           O  
HETATM 2447  O   HOH A 553      21.584 -13.136  34.250  1.00 38.32           O  
HETATM 2448  O   HOH A 554      23.228  26.812  -0.093  1.00 46.11           O  
HETATM 2449  O   HOH A 555      27.409  -7.800   8.704  1.00 48.37           O  
HETATM 2450  O   HOH A 556      14.695  26.328   4.110  1.00 25.20           O  
HETATM 2451  O   HOH A 557      20.958  21.398   4.199  1.00 33.05           O  
HETATM 2452  O   HOH A 558       4.019 -22.060   6.914  1.00 18.96           O  
HETATM 2453  O   HOH A 559      24.012 -14.994  26.847  1.00 22.78           O  
HETATM 2454  O   HOH A 560      26.936 -11.089  11.875  1.00 40.66           O  
HETATM 2455  O   HOH A 561      12.209  22.056   2.340  1.00 27.56           O  
HETATM 2456  O   HOH A 562      15.298 -22.047  31.683  1.00 40.24           O  
HETATM 2457  O   HOH A 563       2.595  -9.017  18.847  1.00 33.36           O  
HETATM 2458  O   HOH A 564      26.602  -6.141  17.854  1.00 40.42           O  
HETATM 2459  O   HOH A 565      20.560 -17.514   9.796  1.00 41.73           O  
HETATM 2460  O   HOH A 566       9.678  19.729  -0.441  1.00 26.69           O  
HETATM 2461  O   HOH A 567      -1.274  17.567 -19.569  1.00 33.22           O  
HETATM 2462  O   HOH A 568      28.882   8.244 -11.757  1.00 33.98           O  
HETATM 2463  O   HOH A 569       9.506  10.208  -4.818  1.00 18.07           O  
HETATM 2464  O   HOH A 570      23.176  -7.493  34.170  1.00 32.14           O  
HETATM 2465  O   HOH A 571      14.679  -9.198  -4.191  1.00 39.63           O  
HETATM 2466  O   HOH A 572       4.055 -17.549  20.672  1.00 21.60           O  
HETATM 2467  O   HOH A 573      14.985 -25.855  26.633  1.00 23.71           O  
HETATM 2468  O   HOH A 574       8.184 -24.625  25.272  1.00 20.17           O  
HETATM 2469  O   HOH A 575      15.702  -5.640  19.994  1.00 17.56           O  
HETATM 2470  O   HOH A 576      10.514  -0.205  -3.307  1.00 23.43           O  
HETATM 2471  O   HOH A 577      20.252 -19.932  16.181  1.00 30.52           O  
HETATM 2472  O   HOH A 578      23.760  12.902  -1.534  1.00 31.25           O  
HETATM 2473  O   HOH A 579      12.551  11.152  10.893  1.00 32.05           O  
HETATM 2474  O   HOH A 580      -5.436  14.372  -4.011  1.00 49.36           O  
HETATM 2475  O   HOH A 581      16.757 -18.738   7.449  1.00 25.54           O  
HETATM 2476  O   HOH A 582      20.602  19.023   2.994  1.00 29.46           O  
HETATM 2477  O   HOH A 583      16.663   2.517  12.325  1.00 18.09           O  
HETATM 2478  O   HOH A 584      -2.311  19.237 -11.265  1.00 30.21           O  
HETATM 2479  O   HOH A 585       9.052  28.367  -1.348  1.00 34.75           O  
HETATM 2480  O   HOH A 586      15.023  -4.827   0.215  1.00 27.87           O  
HETATM 2481  O   HOH A 587      -0.231  23.296  -3.096  1.00 46.43           O  
HETATM 2482  O   HOH A 588      16.423 -27.939  23.457  1.00 20.94           O  
HETATM 2483  O   HOH A 589      23.209   1.642  15.891  1.00 30.81           O  
HETATM 2484  O   HOH A 590       9.883 -17.698  -4.154  1.00 42.07           O  
HETATM 2485  O   HOH A 591      14.114  14.800  12.719  1.00 40.20           O  
HETATM 2486  O   HOH A 592      16.164 -12.921  31.555  1.00 28.49           O  
HETATM 2487  O   HOH A 593      15.441  27.026 -12.129  1.00 29.04           O  
HETATM 2488  O   HOH A 594      26.793  23.339  -4.744  1.00 24.31           O  
HETATM 2489  O   HOH A 595      -0.556   1.907  13.593  1.00 30.24           O  
HETATM 2490  O   HOH A 596       5.351   8.480   1.901  1.00 59.05           O  
HETATM 2491  O   HOH A 597      14.742   0.578  -2.901  1.00 35.93           O  
HETATM 2492  O   HOH A 598      20.281  10.352  15.630  1.00 22.81           O  
HETATM 2493  O   HOH A 599      -5.444  24.421  -7.460  1.00 21.16           O  
HETATM 2494  O   HOH A 600       5.292  -6.617  22.291  1.00 42.12           O  
HETATM 2495  O   HOH A 601      22.099   6.469   0.231  1.00 47.92           O  
HETATM 2496  O   HOH A 602       9.563   6.434   5.835  1.00 16.88           O  
HETATM 2497  O   HOH A 603      25.367   9.338  -4.751  1.00 34.94           O  
HETATM 2498  O   HOH A 604      14.939  33.120  -0.089  1.00 41.85           O  
HETATM 2499  O   HOH A 605      18.396 -29.069  20.706  1.00 48.69           O  
HETATM 2500  O   HOH A 606       7.350  11.792   0.905  1.00 34.48           O  
HETATM 2501  O   HOH A 607      30.406  25.229 -10.378  1.00 31.31           O  
HETATM 2502  O   HOH A 608      18.266 -16.068  -2.803  1.00 36.94           O  
HETATM 2503  O   HOH A 609       5.528   2.808  -4.582  1.00 20.62           O  
HETATM 2504  O   HOH A 610      24.492  -9.012  20.428  1.00 24.42           O  
HETATM 2505  O   HOH A 611      17.768  27.505 -12.831  1.00 30.34           O  
HETATM 2506  O   HOH A 612      22.423   7.414 -17.256  1.00 30.11           O  
HETATM 2507  O   HOH A 613      -2.406  13.069 -11.885  1.00 48.40           O  
HETATM 2508  O   HOH A 614      20.554  -1.886  23.946  1.00 26.92           O  
HETATM 2509  O   HOH A 615      10.219 -25.907  21.890  1.00 19.62           O  
HETATM 2510  O   HOH A 616      16.472   4.696  30.437  1.00 43.54           O  
HETATM 2511  O   HOH A 617      27.595  20.578  -5.338  1.00 32.29           O  
HETATM 2512  O   HOH A 618      22.498 -18.138  38.670  1.00 31.59           O  
HETATM 2513  O   HOH A 619       2.454 -19.713  21.467  1.00 25.04           O  
HETATM 2514  O   HOH A 620      22.518  -0.671  18.034  1.00 22.16           O  
HETATM 2515  O   HOH A 621      21.574  21.588 -18.737  1.00 23.18           O  
HETATM 2516  O   HOH A 622      18.871  -7.527   5.840  1.00 24.57           O  
HETATM 2517  O   HOH A 623      10.063   5.785  24.146  1.00 28.28           O  
HETATM 2518  O   HOH A 624       6.256   2.302  -7.647  1.00 23.73           O  
HETATM 2519  O   HOH A 625      13.088  -0.769 -11.847  1.00 49.11           O  
HETATM 2520  O   HOH A 626      -2.530  29.129 -10.351  1.00 53.43           O  
HETATM 2521  O   HOH A 627      23.407   2.899   9.496  1.00 35.49           O  
HETATM 2522  O   HOH A 628      21.329  10.525 -16.983  1.00 22.42           O  
HETATM 2523  O   HOH A 629      24.597  -0.536  13.003  1.00 35.23           O  
HETATM 2524  O   HOH A 630      10.779  29.486   0.311  1.00 28.16           O  
HETATM 2525  O   HOH A 631      12.001 -30.230  22.223  1.00 25.31           O  
HETATM 2526  O   HOH A 632      19.604  -6.274  32.146  1.00 40.29           O  
HETATM 2527  O   HOH A 633       7.189  19.788  -0.449  1.00 26.48           O  
HETATM 2528  O   HOH A 634      17.457  29.203  -3.472  1.00 39.06           O  
HETATM 2529  O   HOH A 635       2.003  11.456  -5.605  1.00 21.14           O  
HETATM 2530  O   HOH A 636      12.020 -29.587   8.270  1.00 30.09           O  
HETATM 2531  O   HOH A 637      24.081 -16.126  21.418  1.00 29.51           O  
HETATM 2532  O   HOH A 638      12.079   9.337 -26.078  1.00 39.30           O  
HETATM 2533  O   HOH A 639      13.953  17.147  10.574  1.00 47.10           O  
HETATM 2534  O   HOH A 640      -2.659  16.175  -9.404  1.00 36.07           O  
HETATM 2535  O   HOH A 641       1.207   1.508  20.976  1.00 40.79           O  
HETATM 2536  O   HOH A 642       1.029  26.046  -2.359  1.00 37.93           O  
HETATM 2537  O   HOH A 643       3.798  21.023 -21.201  1.00 37.62           O  
HETATM 2538  O   HOH A 644      22.839  -2.336  16.063  1.00 25.83           O  
HETATM 2539  O   HOH A 645       3.943  24.917  -1.739  1.00 41.20           O  
HETATM 2540  O   HOH A 646      20.193  14.393 -18.684  1.00 27.38           O  
HETATM 2541  O   HOH A 647       6.087  -5.182  20.160  1.00 36.58           O  
HETATM 2542  O   HOH A 648       9.836  24.868  -0.578  1.00 31.25           O  
HETATM 2543  O   HOH A 649       1.272 -16.876  12.317  1.00 31.51           O  
HETATM 2544  O   HOH A 650      -3.971 -11.818   2.508  1.00 23.05           O  
HETATM 2545  O   HOH A 651      10.996 -17.020  30.022  1.00 39.46           O  
HETATM 2546  O   HOH A 652      -0.446  19.735 -15.749  1.00 32.25           O  
HETATM 2547  O   HOH A 653      27.906  21.758 -11.595  1.00 22.67           O  
HETATM 2548  O   HOH A 654      24.930 -14.002   9.291  1.00 39.25           O  
HETATM 2549  O   HOH A 655       2.616  25.963 -16.733  1.00 31.87           O  
HETATM 2550  O   HOH A 656       2.288   5.575 -16.019  1.00 34.93           O  
HETATM 2551  O   HOH A 657      27.277 -11.546   7.485  1.00 40.27           O  
HETATM 2552  O   HOH A 658      19.244  12.493  -3.660  1.00 26.34           O  
HETATM 2553  O   HOH A 659      18.417 -24.026  25.725  1.00 26.82           O  
HETATM 2554  O   HOH A 660      18.100 -24.334   6.767  1.00 42.04           O  
HETATM 2555  O   HOH A 661      21.503  -1.764  20.267  1.00 21.41           O  
HETATM 2556  O   HOH A 662       0.102 -17.101  15.368  1.00 38.45           O  
HETATM 2557  O   HOH A 663      21.366 -13.106   1.968  1.00 34.64           O  
HETATM 2558  O   HOH A 664      26.346  20.521 -13.990  1.00 31.17           O  
HETATM 2559  O   HOH A 665       0.000  16.315   0.000  0.50 19.93           O  
HETATM 2560  O   HOH A 666      20.254 -21.692  27.923  1.00 38.31           O  
HETATM 2561  O   HOH A 667      21.541  30.693 -10.525  1.00 40.48           O  
HETATM 2562  O   HOH A 668       3.296  28.651  -3.125  1.00 36.03           O  
HETATM 2563  O   HOH A 669       1.603   2.003   0.108  1.00 33.06           O  
HETATM 2564  O   HOH A 670       8.312 -28.730   6.245  1.00 32.34           O  
HETATM 2565  O   HOH A 671      21.690   9.834   2.318  1.00 51.07           O  
HETATM 2566  O   HOH A 672      21.211  16.725 -17.602  1.00 22.98           O  
HETATM 2567  O   HOH A 673      13.111   5.050  23.654  1.00 29.51           O  
HETATM 2568  O   HOH A 674      22.818  -2.863  31.894  1.00 43.38           O  
HETATM 2569  O   HOH A 675       8.687 -11.467  30.479  1.00 44.96           O  
HETATM 2570  O   HOH A 676      27.193  -8.144  11.674  1.00 36.42           O  
HETATM 2571  O   HOH A 677      18.670   3.436 -13.616  1.00 36.23           O  
HETATM 2572  O   HOH A 678       9.277   0.593  27.773  1.00 40.52           O  
HETATM 2573  O   HOH A 679      11.497  14.891   4.631  1.00 50.04           O  
HETATM 2574  O   HOH A 680      19.818  -0.001  -1.004  1.00 37.19           O  
HETATM 2575  O   HOH A 681      22.141  16.612   3.824  1.00 39.59           O  
HETATM 2576  O   HOH A 682      24.663  -7.564  25.790  1.00 41.08           O  
HETATM 2577  O   HOH A 683      21.158   6.094  20.664  1.00 40.48           O  
HETATM 2578  O   HOH A 684      25.218  -7.800  22.682  1.00 29.84           O  
HETATM 2579  O   HOH A 685      18.577 -17.951   0.999  1.00 44.94           O  
HETATM 2580  O   HOH A 686      15.383  24.919   7.820  1.00 48.63           O  
HETATM 2581  O   HOH A 687      24.855  -4.458  16.554  1.00 38.90           O  
HETATM 2582  O   HOH A 688      20.982 -22.864  21.902  1.00 27.73           O  
HETATM 2583  O   HOH A 689      19.829 -23.623  10.883  1.00 39.47           O  
HETATM 2584  O   HOH A 690      28.701  10.491  -7.938  1.00 40.51           O  
HETATM 2585  O   HOH A 691      -3.178  21.432  -9.929  1.00 38.07           O  
HETATM 2586  O   HOH A 692      14.359 -29.311   9.740  1.00 44.78           O  
HETATM 2587  O   HOH A 693      -1.233   6.336  -2.961  1.00 46.17           O  
HETATM 2588  O   HOH A 694      19.486   9.510   0.898  0.50 19.59           O  
HETATM 2589  O   HOH A 695       1.607  -8.092  21.577  1.00 53.57           O  
HETATM 2590  O   HOH A 696      20.431 -27.189  17.061  1.00 46.80           O  
HETATM 2591  O   HOH A 697      26.713 -10.845  17.531  1.00 42.16           O  
HETATM 2592  O   HOH A 698      20.555 -25.516  22.198  1.00 31.37           O  
HETATM 2593  O   HOH A 699      22.092 -18.288  23.402  1.00 34.05           O  
HETATM 2594  O   HOH A 700      -2.025   3.923  -1.992  1.00 41.27           O  
HETATM 2595  O   HOH A 701      24.640  13.665 -17.305  1.00 24.16           O  
HETATM 2596  O   HOH A 702       3.111  30.587 -10.495  1.00 42.67           O  
HETATM 2597  O   HOH A 703       7.514 -34.952  19.700  1.00 36.47           O  
HETATM 2598  O   HOH A 704      25.000   2.502  27.921  1.00 41.81           O  
HETATM 2599  O   HOH A 705      23.507  -4.825  26.137  1.00 32.04           O  
HETATM 2600  O   HOH A 706      25.848  22.812  -1.949  1.00 34.11           O  
HETATM 2601  O   HOH A 707      13.762  19.290   6.886  1.00 41.50           O  
HETATM 2602  O   HOH A 708       2.504  -1.347 -11.967  1.00 32.61           O  
HETATM 2603  O   HOH A 709      -0.163 -27.188  17.666  1.00 36.80           O  
HETATM 2604  O   HOH A 710      -2.794  10.852  -8.718  1.00 47.38           O  
HETATM 2605  O   HOH A 711      16.928 -18.625  -0.882  1.00 32.14           O  
HETATM 2606  O   HOH A 712      -4.460 -11.898   4.981  1.00 33.17           O  
HETATM 2607  O   HOH A 713      23.724  -7.133   3.720  1.00 49.29           O  
HETATM 2608  O   HOH A 714      21.978 -23.072  19.487  1.00 36.99           O  
HETATM 2609  O   HOH A 715      27.781  -9.012  28.964  1.00 37.76           O  
HETATM 2610  O   HOH A 716      19.151  25.121   5.826  1.00 40.45           O  
HETATM 2611  O   HOH A 717      15.787 -25.901   6.670  1.00 33.29           O  
HETATM 2612  O   HOH A 718      20.850 -22.352  17.081  1.00 26.11           O  
HETATM 2613  O   HOH A 719       7.285 -21.909  28.712  1.00 35.33           O  
HETATM 2614  O   HOH A 720      21.806  -7.580   5.730  1.00 28.44           O  
HETATM 2615  O   HOH A 721      12.875  22.581   5.940  1.00 45.58           O  
HETATM 2616  O   HOH A 722       0.689 -17.437   2.848  1.00 48.53           O  
HETATM 2617  O   HOH A 723       3.936  10.337  14.854  1.00 35.09           O  
HETATM 2618  O   HOH A 724      10.540 -34.419  20.599  1.00 39.67           O  
HETATM 2619  O   HOH A 725      19.750  14.525 -21.447  1.00 32.80           O  
HETATM 2620  O   HOH A 726       8.934  -4.676  26.884  1.00 33.84           O  
HETATM 2621  O   HOH A 727      22.303 -14.107   8.692  1.00 39.44           O  
HETATM 2622  O   HOH A 728      10.763 -32.993  12.750  1.00 38.54           O  
HETATM 2623  O   HOH A 729      24.672  -4.730  19.647  1.00 35.74           O  
HETATM 2624  O   HOH A 730      19.634  10.533  -1.643  1.00 27.96           O  
HETATM 2625  O   HOH A 731      28.345   9.819  -5.115  1.00 44.80           O  
HETATM 2626  O   HOH A 732      20.188 -16.429   5.171  1.00 33.01           O  
HETATM 2627  O   HOH A 733      17.676  15.394 -23.199  1.00 51.69           O  
HETATM 2628  O   HOH A 734      22.307  26.879   2.848  1.00 35.38           O  
HETATM 2629  O   HOH A 735      14.457  -2.801 -10.680  1.00 38.30           O  
HETATM 2630  O   HOH A 736      23.021  -1.510  22.589  1.00 38.35           O  
HETATM 2631  O   HOH A 737      16.602  -4.388  -1.995  1.00 32.57           O  
HETATM 2632  O   HOH A 738      12.639  24.226   3.884  1.00 43.38           O  
HETATM 2633  O   HOH A 739      19.231   7.552  -3.171  1.00 39.20           O  
HETATM 2634  O   HOH A 740      11.359  20.804 -19.225  1.00 40.08           O  
HETATM 2635  O   HOH A 741      25.164  10.180  -2.395  1.00 37.77           O  
HETATM 2636  O   HOH A 742      12.156  12.915  12.691  1.00 44.43           O  
HETATM 2637  O   HOH A 743      -3.943   9.525  -7.084  1.00 39.20           O  
HETATM 2638  O   HOH A 744       6.363  21.861  -1.784  1.00 33.67           O  
HETATM 2639  O   HOH A 745       1.234  21.536 -21.696  1.00 47.21           O  
HETATM 2640  O   HOH A 746      13.873 -27.795  25.017  1.00 21.63           O  
HETATM 2641  O   HOH A 747      20.593   6.141  -5.469  1.00 41.09           O  
HETATM 2642  O   HOH A 748      20.518  -8.739  33.528  1.00 39.12           O  
HETATM 2643  O   HOH A 749      22.904 -17.178  25.621  1.00 23.17           O  
HETATM 2644  O   HOH A 750      18.128  -7.757  35.719  1.00 36.52           O  
HETATM 2645  O   HOH A 751      16.809  13.349  23.390  1.00 42.34           O  
HETATM 2646  O   HOH A 752      17.551 -26.228  27.026  1.00 25.09           O  
HETATM 2647  O   HOH A 753      20.918 -19.817  13.030  1.00 37.69           O  
HETATM 2648  O   HOH A 754      11.698 -34.154  23.662  1.00 33.46           O  
HETATM 2649  O   HOH A 755      10.352 -27.268   2.468  1.00 30.54           O  
HETATM 2650  O   HOH A 756       5.920   1.609  28.937  1.00 40.77           O  
HETATM 2651  O   HOH A 757      16.252 -29.800  21.701  1.00 39.14           O  
HETATM 2652  O   HOH A 758      27.285  15.021  -2.161  1.00 30.20           O  
HETATM 2653  O   HOH A 759      -4.882  26.441  -9.253  1.00 35.39           O  
HETATM 2654  O   HOH A 760      23.772  16.221 -16.676  1.00 23.96           O  
HETATM 2655  O   HOH A 761      10.458  22.420   0.476  1.00 24.27           O  
HETATM 2656  O   HOH A 762      -5.578  22.457  -9.186  1.00 36.71           O  
HETATM 2657  O   HOH A 763      13.304   2.304 -18.675  1.00 36.89           O  
HETATM 2658  O   HOH A 764      21.947  12.673 -18.254  1.00 20.18           O  
HETATM 2659  O   HOH A 765      14.247 -31.395  20.940  1.00 33.27           O  
HETATM 2660  O   HOH A 766       5.194   1.188  26.265  1.00 41.26           O  
HETATM 2661  O   HOH A 767      30.870 -10.651  20.697  1.00 41.40           O  
HETATM 2662  O   HOH A 768      25.096  18.171 -18.602  1.00 38.56           O  
CONECT 2362 2363 2364 2365                                                      
CONECT 2363 2362                                                                
CONECT 2364 2362                                                                
CONECT 2365 2362                                                                
CONECT 2366 2367 2368 2369                                                      
CONECT 2367 2366                                                                
CONECT 2368 2366                                                                
CONECT 2369 2366                                                                
CONECT 2370 2371 2372 2373                                                      
CONECT 2371 2370                                                                
CONECT 2372 2370                                                                
CONECT 2373 2370                                                                
CONECT 2374 2375 2376 2377                                                      
CONECT 2375 2374                                                                
CONECT 2376 2374                                                                
CONECT 2377 2374                                                                
CONECT 2378 2380 2381                                                           
CONECT 2379 2380 2392                                                           
CONECT 2380 2378 2379 2390                                                      
CONECT 2381 2378 2382 2389                                                      
CONECT 2382 2381 2383 2384 2386                                                 
CONECT 2383 2382 2388                                                           
CONECT 2384 2382 2387                                                           
CONECT 2385 2386                                                                
CONECT 2386 2382 2385                                                           
CONECT 2387 2384 2388                                                           
CONECT 2388 2383 2387                                                           
CONECT 2389 2381                                                                
CONECT 2390 2380 2391 2394                                                      
CONECT 2391 2390                                                                
CONECT 2392 2379 2393                                                           
CONECT 2393 2392 2394                                                           
CONECT 2394 2390 2393                                                           
MASTER      286    0    5   10   15    0    0    6 2648    1   33   24          
END