HEADER    TRANSFERASE                             22-SEP-10   2XRU              
TITLE     AURORA-A T288E COMPLEXED WITH PHA-828300                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 6;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 126-403;                        
COMPND   5 SYNONYM: AURORA KINASE A, SERINE/THREONINE KINASE 15, AURORA/IPL1-   
COMPND   6 RELATED KINASE 1, BREAST TUMOR-AMPLIFIED KINASE, AURORA-A, AURORA-   
COMPND   7 RELATED KINASE 1, HARK1;                                             
COMPND   8 EC: 2.7.11.1;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    NUCLEOTIDE-BINDING, KINASE, CELL CYCLE, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BINDI,D.FANCELLI,C.ALLI,D.BERTA,J.A.BERTRAND,A.D.CAMERON,           
AUTHOR   2 P.CAPPELLA,P.CARPINELLI,G.CERVI,W.CROCI,M.D'ANELLO,B.FORTE,          
AUTHOR   3 M.LAURAGIORGINI,A.MARSIGLIO,J.MOLL,E.PESENTI,V.PITTALA,M.PULICI,     
AUTHOR   4 F.RICCARDI-SIRTORI,F.ROLETTO,C.SONCINI,P.STORICI,M.VARASI,D.VOLPI,   
AUTHOR   5 P.ZUGNONI,P.VIANELLO                                                 
REVDAT   2   03-APR-19 2XRU    1       SOURCE                                   
REVDAT   1   29-SEP-10 2XRU    0                                                
JRNL        AUTH   S.BINDI,D.FANCELLI,C.ALLI,D.BERTA,J.A.BERTRAND,A.D.CAMERON,  
JRNL        AUTH 2 P.CAPPELLA,P.CARPINELLI,G.CERVI,V.CROCI,M.D'ANELLO,B.FORTE,  
JRNL        AUTH 3 M.LAURA GIORGINI,A.MARSIGLIO,J.MOLL,E.PESENTI,V.PITTALA,     
JRNL        AUTH 4 M.PULICI,F.RICCARDI-SIRTORI,F.ROLETTO,C.SONCINI,P.STORICI,   
JRNL        AUTH 5 M.VARASI,D.VOLPI,P.ZUGNONI,P.VIANELLO                        
JRNL        TITL   THIENO[3,2-C]PYRAZOLES: A NOVEL CLASS OF AURORA INHIBITORS   
JRNL        TITL 2 WITH FAVORABLE ANTITUMOR ACTIVITY.                           
JRNL        REF    BIOORG.MED.CHEM.              V.  18  7113 2010              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   20817473                                                     
JRNL        DOI    10.1016/J.BMC.2010.07.048                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1264925.360                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 7878                           
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 SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.344                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 405                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.017                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1206                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4760                       
REMARK   3   BIN FREE R VALUE                    : 0.6280                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 59                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.082                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2082                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 95.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 97.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -14.09000                                            
REMARK   3    B22 (A**2) : -14.09000                                            
REMARK   3    B33 (A**2) : 28.18000                                             
REMARK   3    B12 (A**2) : 10.41000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.49                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.64                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.53                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.89                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.690                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 13.510; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 20.960; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 17.540; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 24.850; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 73.16                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2XRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290045449.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-SEP-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9330                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7931                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 10.20                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 5000 MME, 0.2 M LITHIUM          
REMARK 280  SULFATE, 0.1 M SODIUM CITRATE PH 5.6 & 2 MM DTT                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.15100            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      110.30200            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       82.72650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      137.87750            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.57550            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       55.15100            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      110.30200            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      137.87750            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       82.72650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       27.57550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR 288 TO GLU                        
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     GLY A   124                                                      
REMARK 465     PRO A   125                                                      
REMARK 465     HIS A   280                                                      
REMARK 465     ALA A   281                                                      
REMARK 465     PRO A   282                                                      
REMARK 465     SER A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     ARG A   285                                                      
REMARK 465     ARG A   286                                                      
REMARK 465     THR A   287                                                      
REMARK 465     GLU A   288                                                      
REMARK 465     LEU A   289                                                      
REMARK 465     PRO A   390                                                      
REMARK 465     SER A   391                                                      
REMARK 465     ASN A   392                                                      
REMARK 465     CYS A   393                                                      
REMARK 465     GLN A   394                                                      
REMARK 465     ASN A   395                                                      
REMARK 465     LYS A   396                                                      
REMARK 465     GLU A   397                                                      
REMARK 465     SER A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     SER A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     GLN A   402                                                      
REMARK 465     SER A   403                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 389    CA   C    O    CB   CG   CD   CE                    
REMARK 470     LYS A 389    NZ                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A   339     NZ   LYS A   339    10664     1.85            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 214   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A 127       91.41     40.80                                   
REMARK 500    LEU A 130        7.02    -49.93                                   
REMARK 500    LYS A 171       -9.86    -49.99                                   
REMARK 500    GLN A 185      -70.55    -58.03                                   
REMARK 500    ASP A 202     -135.86    -89.45                                   
REMARK 500    ILE A 209       89.23    -48.36                                   
REMARK 500    SER A 226      -73.25     75.03                                   
REMARK 500    ARG A 251      -20.03     84.56                                   
REMARK 500    ARG A 255      -79.27     72.75                                   
REMARK 500    ASP A 256       32.69    -65.45                                   
REMARK 500    ASP A 274      129.42     69.40                                   
REMARK 500    PHE A 275      -55.47   -125.84                                   
REMARK 500    TRP A 277       21.10    149.51                                   
REMARK 500    ASP A 294      -36.85    -30.79                                   
REMARK 500    GLU A 299      -78.93    -41.82                                   
REMARK 500    MET A 300      -73.51    -29.38                                   
REMARK 500    ARG A 304      150.80    -46.63                                   
REMARK 500    ASP A 307     -115.31   -132.22                                   
REMARK 500    GLU A 330      128.13    -24.40                                   
REMARK 500    VAL A 344       39.95     71.35                                   
REMARK 500    HIS A 380      131.74    -30.01                                   
REMARK 500    ASN A 386      -18.43   -141.99                                   
REMARK 500    SER A 387     -133.11    -74.58                                   
REMARK 500    SER A 388      -45.73   -175.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 400 A 1389                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MUO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AURORA-2, AN ONCOGENIC SERINE-THREONINE KINASE  
REMARK 900 RELATED ID: 2X6D   RELATED DB: PDB                                   
REMARK 900 AURORA-A BOUND TO AN INHIBITOR                                       
REMARK 900 RELATED ID: 2J50   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA-2 IN COMPLEX WITH PHA -739358                    
REMARK 900 RELATED ID: 2W1D   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 1OL6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF UNPHOSPHORYLATED D274N MUTANT OF AURORA-A               
REMARK 900 RELATED ID: 2XNE   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA-A BOUND TO AN IMIDAZOPYRAZINE INHIBITOR          
REMARK 900 RELATED ID: 2BMC   RELATED DB: PDB                                   
REMARK 900 AURORA-2 T287D T288D COMPLEXED WITH PHA- 680632                      
REMARK 900 RELATED ID: 2C6E   RELATED DB: PDB                                   
REMARK 900 AURORA A KINASE ACTIVATED MUTANT (T287D) IN COMPLEX WITH A 5-        
REMARK 900 AMINOPYRIMIDINYL QUINAZOLINE INHIBITOR                               
REMARK 900 RELATED ID: 2J4Z   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA-2 IN COMPLEX WITH PHA -680626                    
REMARK 900 RELATED ID: 1OL5   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA-A 122-403, PHOSPHORYLATED ON THR287, THR288 AND  
REMARK 900 BOUND TO TPX2 1-43                                                   
REMARK 900 RELATED ID: 2X81   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA A IN COMPLEX WITH MLN8054                        
REMARK 900 RELATED ID: 2XNG   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF AURORA-A BOUND TO A SELECTIVE IMIDAZOPYRAZINE INHIBITOR 
REMARK 900 RELATED ID: 2C6D   RELATED DB: PDB                                   
REMARK 900 AURORA A KINASE ACTIVATED MUTANT (T287D) IN COMPLEX WITH ADPNP       
REMARK 900 RELATED ID: 2WTW   RELATED DB: PDB                                   
REMARK 900 AURORA-A INHIBITOR STRUCTURE (2ND CRYSTAL FORM)                      
REMARK 900 RELATED ID: 2WQE   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF S155R AURORA-A SOMATIC MUTANT                           
REMARK 900 RELATED ID: 2W1C   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 2W1G   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 2WTV   RELATED DB: PDB                                   
REMARK 900 AURORA-A INHIBITOR STRUCTURE                                         
REMARK 900 RELATED ID: 1OL7   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN AURORA-A 122-403 PHOSPHORYLATED ON THR287, THR288 
REMARK 900 RELATED ID: 2W1E   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 2W1F   RELATED DB: PDB                                   
REMARK 900 STRUCTURE DETERMINATION OF AURORA KINASE IN COMPLEX WITH INHIBITOR   
REMARK 900 RELATED ID: 2X6E   RELATED DB: PDB                                   
REMARK 900 AURORA-A BOUND TO AN INHIBITOR                                       
REMARK 900 RELATED ID: 1MQ4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF AURORA-A PROTEIN KINASE                         
DBREF  2XRU A  126   403  UNP    O14965   STK6_HUMAN     126    403             
SEQADV 2XRU GLY A  124  UNP  O14965              EXPRESSION TAG                 
SEQADV 2XRU PRO A  125  UNP  O14965              EXPRESSION TAG                 
SEQADV 2XRU GLU A  288  UNP  O14965    THR   288 ENGINEERED MUTATION            
SEQRES   1 A  280  GLY PRO ARG GLN TRP ALA LEU GLU ASP PHE GLU ILE GLY          
SEQRES   2 A  280  ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN VAL TYR LEU          
SEQRES   3 A  280  ALA ARG GLU LYS GLN SER LYS PHE ILE LEU ALA LEU LYS          
SEQRES   4 A  280  VAL LEU PHE LYS ALA GLN LEU GLU LYS ALA GLY VAL GLU          
SEQRES   5 A  280  HIS GLN LEU ARG ARG GLU VAL GLU ILE GLN SER HIS LEU          
SEQRES   6 A  280  ARG HIS PRO ASN ILE LEU ARG LEU TYR GLY TYR PHE HIS          
SEQRES   7 A  280  ASP ALA THR ARG VAL TYR LEU ILE LEU GLU TYR ALA PRO          
SEQRES   8 A  280  LEU GLY THR VAL TYR ARG GLU LEU GLN LYS LEU SER LYS          
SEQRES   9 A  280  PHE ASP GLU GLN ARG THR ALA THR TYR ILE THR GLU LEU          
SEQRES  10 A  280  ALA ASN ALA LEU SER TYR CYS HIS SER LYS ARG VAL ILE          
SEQRES  11 A  280  HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU LEU GLY SER          
SEQRES  12 A  280  ALA GLY GLU LEU LYS ILE ALA ASP PHE GLY TRP SER VAL          
SEQRES  13 A  280  HIS ALA PRO SER SER ARG ARG THR GLU LEU CYS GLY THR          
SEQRES  14 A  280  LEU ASP TYR LEU PRO PRO GLU MET ILE GLU GLY ARG MET          
SEQRES  15 A  280  HIS ASP GLU LYS VAL ASP LEU TRP SER LEU GLY VAL LEU          
SEQRES  16 A  280  CYS TYR GLU PHE LEU VAL GLY LYS PRO PRO PHE GLU ALA          
SEQRES  17 A  280  ASN THR TYR GLN GLU THR TYR LYS ARG ILE SER ARG VAL          
SEQRES  18 A  280  GLU PHE THR PHE PRO ASP PHE VAL THR GLU GLY ALA ARG          
SEQRES  19 A  280  ASP LEU ILE SER ARG LEU LEU LYS HIS ASN PRO SER GLN          
SEQRES  20 A  280  ARG PRO MET LEU ARG GLU VAL LEU GLU HIS PRO TRP ILE          
SEQRES  21 A  280  THR ALA ASN SER SER LYS PRO SER ASN CYS GLN ASN LYS          
SEQRES  22 A  280  GLU SER ALA SER LYS GLN SER                                  
HET    400  A1389      36                                                       
HETNAM     400 3-({[4-(4-METHYLPIPERAZIN-1-YL)PHENYL]CARBONYL}AMINO)-           
HETNAM   2 400  N-[(1R)-1-PHENYLPROPYL]-1H-THIENO[3,2-C]PYRAZOLE-5-             
HETNAM   3 400  CARBOXAMIDE                                                     
HETSYN     400 PHA-828300                                                       
FORMUL   2  400    C27 H30 N6 O2 S                                              
HELIX    1   1 LYS A  166  GLY A  173  1                                   8    
HELIX    2   2 VAL A  174  HIS A  187  1                                  14    
HELIX    3   3 THR A  217  SER A  226  1                                  10    
HELIX    4   4 ASP A  229  LYS A  250  1                                  22    
HELIX    5   5 LYS A  258  GLU A  260  5                                   3    
HELIX    6   6 THR A  292  LEU A  296  5                                   5    
HELIX    7   7 PRO A  297  GLU A  302  1                                   6    
HELIX    8   8 LYS A  309  GLY A  325  1                                  17    
HELIX    9   9 THR A  333  ARG A  343  1                                  11    
HELIX   10  10 THR A  353  LEU A  364  1                                  12    
HELIX   11  11 ASN A  367  ARG A  371  5                                   5    
HELIX   12  12 MET A  373  HIS A  380  1                                   8    
SHEET    1  AA 5 PHE A 133  LYS A 141  0                                        
SHEET    2  AA 5 ASN A 146  GLU A 152 -1  O  VAL A 147   N  LEU A 139           
SHEET    3  AA 5 PHE A 157  PHE A 165 -1  O  PHE A 157   N  GLU A 152           
SHEET    4  AA 5 ARG A 205  LEU A 210 -1  O  VAL A 206   N  LEU A 164           
SHEET    5  AA 5 PHE A 200  HIS A 201 -1  O  PHE A 200   N  TYR A 207           
SHEET    1  AB 2 LEU A 262  LEU A 264  0                                        
SHEET    2  AB 2 LEU A 270  ILE A 272 -1  O  LYS A 271   N  LEU A 263           
SITE     1 AC1 18 ARG A 137  LEU A 139  ALA A 160  LYS A 162                    
SITE     2 AC1 18 LEU A 194  LEU A 210  GLU A 211  TYR A 212                    
SITE     3 AC1 18 ALA A 213  PRO A 214  LEU A 215  GLY A 216                    
SITE     4 AC1 18 LYS A 224  GLU A 260  ASN A 261  LEU A 263                    
SITE     5 AC1 18 ASP A 274  HIS A 366                                          
CRYST1   82.467   82.467  165.453  90.00  90.00 120.00 P 61 2 2     12          
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      0.012126  0.007001  0.000000        0.00000                         
SCALE2      0.000000  0.014002  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006044        0.00000                         
ATOM      1  N   ARG A 126       0.551  22.381  25.661  1.00112.85           N  
ATOM      2  CA  ARG A 126       1.017  20.981  25.853  1.00112.89           C  
ATOM      3  C   ARG A 126       0.046  19.981  25.213  1.00112.77           C  
ATOM      4  O   ARG A 126      -1.158  19.985  25.494  1.00112.95           O  
ATOM      5  CB  ARG A 126       1.169  20.683  27.352  1.00119.13           C  
ATOM      6  CG  ARG A 126       1.333  21.922  28.236  1.00118.83           C  
ATOM      7  CD  ARG A 126      -0.016  22.593  28.502  1.00118.79           C  
ATOM      8  NE  ARG A 126      -1.117  21.627  28.495  1.00119.21           N  
ATOM      9  CZ  ARG A 126      -2.114  21.618  27.610  1.00119.78           C  
ATOM     10  NH1 ARG A 126      -2.166  22.531  26.646  1.00120.63           N  
ATOM     11  NH2 ARG A 126      -3.052  20.682  27.677  1.00120.26           N  
ATOM     12  N   GLN A 127       0.586  19.127  24.348  1.00179.46           N  
ATOM     13  CA  GLN A 127      -0.198  18.107  23.661  1.00179.87           C  
ATOM     14  C   GLN A 127      -1.564  18.590  23.187  1.00179.86           C  
ATOM     15  O   GLN A 127      -2.552  18.523  23.921  1.00180.56           O  
ATOM     16  CB  GLN A 127      -0.371  16.879  24.560  1.00145.85           C  
ATOM     17  CG  GLN A 127       0.887  16.036  24.704  1.00146.29           C  
ATOM     18  CD  GLN A 127       1.336  15.418  23.389  1.00146.10           C  
ATOM     19  OE1 GLN A 127       1.117  14.231  23.142  1.00148.03           O  
ATOM     20  NE2 GLN A 127       1.971  16.222  22.540  1.00146.31           N  
ATOM     21  N   TRP A 128      -1.609  19.080  21.954  1.00146.77           N  
ATOM     22  CA  TRP A 128      -2.867  19.235  21.241  1.00146.77           C  
ATOM     23  C   TRP A 128      -3.026  18.054  20.300  1.00146.77           C  
ATOM     24  O   TRP A 128      -2.078  17.297  20.085  1.00146.77           O  
ATOM     25  CB  TRP A 128      -2.879  20.535  20.436  1.00119.39           C  
ATOM     26  CG  TRP A 128      -3.085  21.736  21.279  1.00119.39           C  
ATOM     27  CD1 TRP A 128      -4.261  22.388  21.502  1.00119.39           C  
ATOM     28  CD2 TRP A 128      -2.090  22.419  22.051  1.00119.39           C  
ATOM     29  NE1 TRP A 128      -4.063  23.434  22.369  1.00119.39           N  
ATOM     30  CE2 TRP A 128      -2.738  23.476  22.723  1.00119.39           C  
ATOM     31  CE3 TRP A 128      -0.714  22.240  22.241  1.00119.39           C  
ATOM     32  CZ2 TRP A 128      -2.056  24.353  23.574  1.00119.39           C  
ATOM     33  CZ3 TRP A 128      -0.039  23.111  23.083  1.00119.39           C  
ATOM     34  CH2 TRP A 128      -0.711  24.154  23.739  1.00119.39           C  
ATOM     35  N   ALA A 129      -4.226  17.897  19.747  1.00117.11           N  
ATOM     36  CA  ALA A 129      -4.485  16.871  18.741  1.00117.11           C  
ATOM     37  C   ALA A 129      -4.867  17.506  17.410  1.00117.11           C  
ATOM     38  O   ALA A 129      -5.431  18.602  17.372  1.00117.11           O  
ATOM     39  CB  ALA A 129      -5.598  15.939  19.213  1.00148.36           C  
ATOM     40  N   LEU A 130      -4.561  16.805  16.323  1.00 82.25           N  
ATOM     41  CA  LEU A 130      -4.945  17.229  14.976  1.00 82.25           C  
ATOM     42  C   LEU A 130      -6.430  17.606  14.812  1.00 82.25           C  
ATOM     43  O   LEU A 130      -6.892  17.848  13.695  1.00 82.25           O  
ATOM     44  CB  LEU A 130      -4.595  16.127  13.970  1.00125.93           C  
ATOM     45  CG  LEU A 130      -4.909  16.427  12.502  1.00125.93           C  
ATOM     46  CD1 LEU A 130      -4.252  17.727  12.104  1.00125.93           C  
ATOM     47  CD2 LEU A 130      -4.415  15.298  11.622  1.00125.93           C  
ATOM     48  N   GLU A 131      -7.169  17.649  15.920  1.00101.39           N  
ATOM     49  CA  GLU A 131      -8.602  17.904  15.878  1.00101.39           C  
ATOM     50  C   GLU A 131      -8.942  19.170  16.637  1.00101.39           C  
ATOM     51  O   GLU A 131     -10.100  19.582  16.658  1.00101.39           O  
ATOM     52  CB  GLU A 131      -9.380  16.744  16.496  1.00152.55           C  
ATOM     53  CG  GLU A 131      -8.967  15.376  16.010  1.00152.55           C  
ATOM     54  CD  GLU A 131      -8.750  14.408  17.157  1.00152.55           C  
ATOM     55  OE1 GLU A 131      -9.595  14.373  18.078  1.00152.55           O  
ATOM     56  OE2 GLU A 131      -7.733  13.686  17.139  1.00152.55           O  
ATOM     57  N   ASP A 132      -7.947  19.774  17.279  1.00102.27           N  
ATOM     58  CA  ASP A 132      -8.137  21.093  17.884  1.00102.27           C  
ATOM     59  C   ASP A 132      -8.034  22.148  16.796  1.00102.27           C  
ATOM     60  O   ASP A 132      -8.124  23.343  17.061  1.00102.27           O  
ATOM     61  CB  ASP A 132      -7.065  21.378  18.932  1.00141.98           C  
ATOM     62  CG  ASP A 132      -7.033  20.347  20.023  1.00141.98           C  
ATOM     63  OD1 ASP A 132      -8.115  19.985  20.531  1.00141.98           O  
ATOM     64  OD2 ASP A 132      -5.921  19.902  20.370  1.00141.98           O  
ATOM     65  N   PHE A 133      -7.824  21.695  15.570  1.00 87.80           N  
ATOM     66  CA  PHE A 133      -7.466  22.600  14.503  1.00 87.80           C  
ATOM     67  C   PHE A 133      -8.416  22.537  13.329  1.00 87.80           C  
ATOM     68  O   PHE A 133      -8.600  21.486  12.704  1.00 87.80           O  
ATOM     69  CB  PHE A 133      -6.041  22.314  14.041  1.00 83.71           C  
ATOM     70  CG  PHE A 133      -5.055  22.317  15.155  1.00 83.71           C  
ATOM     71  CD1 PHE A 133      -4.954  23.414  15.994  1.00 83.71           C  
ATOM     72  CD2 PHE A 133      -4.286  21.203  15.419  1.00 83.71           C  
ATOM     73  CE1 PHE A 133      -4.112  23.396  17.081  1.00 83.71           C  
ATOM     74  CE2 PHE A 133      -3.438  21.179  16.509  1.00 83.71           C  
ATOM     75  CZ  PHE A 133      -3.352  22.277  17.344  1.00 83.71           C  
ATOM     76  N   GLU A 134      -9.023  23.689  13.060  1.00 83.33           N  
ATOM     77  CA  GLU A 134      -9.712  23.966  11.818  1.00 83.33           C  
ATOM     78  C   GLU A 134      -8.643  24.434  10.833  1.00 83.33           C  
ATOM     79  O   GLU A 134      -7.997  25.461  11.043  1.00 83.33           O  
ATOM     80  CB  GLU A 134     -10.734  25.066  12.062  1.00108.95           C  
ATOM     81  CG  GLU A 134     -11.846  25.126  11.055  1.00108.95           C  
ATOM     82  CD  GLU A 134     -12.859  26.194  11.399  1.00108.95           C  
ATOM     83  OE1 GLU A 134     -13.045  27.132  10.587  1.00108.95           O  
ATOM     84  OE2 GLU A 134     -13.463  26.091  12.491  1.00108.95           O  
ATOM     85  N   ILE A 135      -8.440  23.670   9.766  1.00 96.99           N  
ATOM     86  CA  ILE A 135      -7.336  23.939   8.853  1.00 96.99           C  
ATOM     87  C   ILE A 135      -7.794  24.754   7.659  1.00 96.99           C  
ATOM     88  O   ILE A 135      -8.954  24.687   7.265  1.00 96.99           O  
ATOM     89  CB  ILE A 135      -6.680  22.630   8.355  1.00 60.53           C  
ATOM     90  CG1 ILE A 135      -5.828  22.008   9.470  1.00 60.53           C  
ATOM     91  CG2 ILE A 135      -5.806  22.912   7.137  1.00 60.53           C  
ATOM     92  CD1 ILE A 135      -6.529  21.891  10.818  1.00 60.53           C  
ATOM     93  N   GLY A 136      -6.878  25.527   7.090  1.00 71.72           N  
ATOM     94  CA  GLY A 136      -7.268  26.533   6.127  1.00 71.72           C  
ATOM     95  C   GLY A 136      -6.290  26.641   4.988  1.00 71.72           C  
ATOM     96  O   GLY A 136      -5.749  25.626   4.544  1.00 71.72           O  
ATOM     97  N   ARG A 137      -6.065  27.863   4.511  1.00 80.01           N  
ATOM     98  CA  ARG A 137      -5.192  28.081   3.367  1.00 80.01           C  
ATOM     99  C   ARG A 137      -3.811  27.499   3.625  1.00 80.01           C  
ATOM    100  O   ARG A 137      -3.242  27.678   4.706  1.00 80.01           O  
ATOM    101  CB  ARG A 137      -5.055  29.577   3.066  1.00 76.80           C  
ATOM    102  CG  ARG A 137      -4.161  29.882   1.868  1.00 76.80           C  
ATOM    103  CD  ARG A 137      -4.398  31.271   1.318  1.00 76.80           C  
ATOM    104  NE  ARG A 137      -3.619  32.246   2.056  1.00 76.80           N  
ATOM    105  CZ  ARG A 137      -2.354  32.554   1.783  1.00 76.80           C  
ATOM    106  NH1 ARG A 137      -1.731  31.956   0.772  1.00 76.80           N  
ATOM    107  NH2 ARG A 137      -1.701  33.444   2.539  1.00 76.80           N  
ATOM    108  N   PRO A 138      -3.254  26.793   2.627  1.00 89.02           N  
ATOM    109  CA  PRO A 138      -1.849  26.371   2.635  1.00 89.02           C  
ATOM    110  C   PRO A 138      -0.952  27.597   2.474  1.00 89.02           C  
ATOM    111  O   PRO A 138      -1.237  28.497   1.677  1.00 89.02           O  
ATOM    112  CB  PRO A 138      -1.750  25.436   1.438  1.00 79.57           C  
ATOM    113  CG  PRO A 138      -2.783  25.972   0.481  1.00 79.57           C  
ATOM    114  CD  PRO A 138      -3.919  26.472   1.351  1.00 79.57           C  
ATOM    115  N   LEU A 139       0.125  27.639   3.241  1.00 71.48           N  
ATOM    116  CA  LEU A 139       0.998  28.799   3.232  1.00 71.48           C  
ATOM    117  C   LEU A 139       2.289  28.456   2.519  1.00 71.48           C  
ATOM    118  O   LEU A 139       3.016  29.342   2.075  1.00 71.48           O  
ATOM    119  CB  LEU A 139       1.297  29.225   4.661  1.00 65.70           C  
ATOM    120  CG  LEU A 139       0.079  29.759   5.385  1.00 65.70           C  
ATOM    121  CD1 LEU A 139       0.305  29.795   6.868  1.00 65.70           C  
ATOM    122  CD2 LEU A 139      -0.193  31.131   4.852  1.00 65.70           C  
ATOM    123  N   GLY A 140       2.566  27.158   2.426  1.00 85.75           N  
ATOM    124  CA  GLY A 140       3.809  26.699   1.839  1.00 85.75           C  
ATOM    125  C   GLY A 140       3.839  25.194   1.674  1.00 85.75           C  
ATOM    126  O   GLY A 140       3.410  24.450   2.564  1.00 85.75           O  
ATOM    127  N   LYS A 141       4.350  24.756   0.522  1.00 93.13           N  
ATOM    128  CA  LYS A 141       4.401  23.340   0.150  1.00 93.13           C  
ATOM    129  C   LYS A 141       5.857  22.881   0.083  1.00 93.13           C  
ATOM    130  O   LYS A 141       6.587  23.242  -0.838  1.00 93.13           O  
ATOM    131  CB  LYS A 141       3.744  23.132  -1.220  1.00112.30           C  
ATOM    132  CG  LYS A 141       2.465  23.934  -1.445  1.00112.30           C  
ATOM    133  CD  LYS A 141       1.303  23.359  -0.657  1.00112.30           C  
ATOM    134  CE  LYS A 141       0.958  21.961  -1.144  1.00112.30           C  
ATOM    135  NZ  LYS A 141      -0.161  21.351  -0.371  1.00112.30           N  
ATOM    136  N   GLY A 142       6.276  22.089   1.062  1.00155.45           N  
ATOM    137  CA  GLY A 142       7.662  21.662   1.115  1.00155.45           C  
ATOM    138  C   GLY A 142       7.830  20.220   0.689  1.00155.45           C  
ATOM    139  O   GLY A 142       6.845  19.520   0.449  1.00155.45           O  
ATOM    140  N   LYS A 143       9.078  19.772   0.597  1.00107.63           N  
ATOM    141  CA  LYS A 143       9.359  18.391   0.223  1.00107.63           C  
ATOM    142  C   LYS A 143       8.837  17.444   1.301  1.00107.63           C  
ATOM    143  O   LYS A 143       7.965  16.616   1.046  1.00107.63           O  
ATOM    144  CB  LYS A 143      10.868  18.185   0.039  1.00104.82           C  
ATOM    145  CG  LYS A 143      11.239  16.884  -0.665  1.00104.82           C  
ATOM    146  CD  LYS A 143      12.727  16.563  -0.517  1.00104.82           C  
ATOM    147  CE  LYS A 143      13.077  15.197  -1.115  1.00104.82           C  
ATOM    148  NZ  LYS A 143      14.482  14.774  -0.833  1.00104.82           N  
ATOM    149  N   PHE A 144       9.363  17.583   2.511  1.00 88.42           N  
ATOM    150  CA  PHE A 144       8.970  16.728   3.621  1.00 88.42           C  
ATOM    151  C   PHE A 144       7.501  16.926   3.986  1.00 88.42           C  
ATOM    152  O   PHE A 144       6.744  15.961   4.137  1.00 88.42           O  
ATOM    153  CB  PHE A 144       9.836  17.029   4.841  1.00150.23           C  
ATOM    154  CG  PHE A 144      11.304  16.831   4.606  1.00150.23           C  
ATOM    155  CD1 PHE A 144      11.933  17.417   3.520  1.00150.23           C  
ATOM    156  CD2 PHE A 144      12.060  16.072   5.481  1.00150.23           C  
ATOM    157  CE1 PHE A 144      13.287  17.250   3.313  1.00150.23           C  
ATOM    158  CE2 PHE A 144      13.414  15.902   5.280  1.00150.23           C  
ATOM    159  CZ  PHE A 144      14.028  16.492   4.194  1.00150.23           C  
ATOM    160  N   GLY A 145       7.101  18.183   4.133  1.00 91.27           N  
ATOM    161  CA  GLY A 145       5.712  18.465   4.424  1.00 91.27           C  
ATOM    162  C   GLY A 145       5.169  19.692   3.724  1.00 91.27           C  
ATOM    163  O   GLY A 145       5.692  20.123   2.700  1.00 91.27           O  
ATOM    164  N   ASN A 146       4.093  20.236   4.286  1.00118.83           N  
ATOM    165  CA  ASN A 146       3.569  21.538   3.901  1.00118.83           C  
ATOM    166  C   ASN A 146       3.240  22.303   5.172  1.00118.83           C  
ATOM    167  O   ASN A 146       3.481  21.821   6.281  1.00118.83           O  
ATOM    168  CB  ASN A 146       2.308  21.372   3.063  1.00125.16           C  
ATOM    169  CG  ASN A 146       2.413  20.224   2.090  1.00125.16           C  
ATOM    170  OD1 ASN A 146       2.738  20.414   0.918  1.00125.16           O  
ATOM    171  ND2 ASN A 146       2.144  19.018   2.573  1.00125.16           N  
ATOM    172  N   VAL A 147       2.685  23.495   5.011  1.00 65.97           N  
ATOM    173  CA  VAL A 147       2.361  24.339   6.156  1.00 65.97           C  
ATOM    174  C   VAL A 147       1.095  25.120   5.881  1.00 65.97           C  
ATOM    175  O   VAL A 147       0.912  25.686   4.808  1.00 65.97           O  
ATOM    176  CB  VAL A 147       3.526  25.314   6.483  1.00 68.80           C  
ATOM    177  CG1 VAL A 147       3.826  26.226   5.294  1.00 68.80           C  
ATOM    178  CG2 VAL A 147       3.192  26.106   7.717  1.00 68.80           C  
ATOM    179  N   TYR A 148       0.205  25.132   6.855  1.00 66.13           N  
ATOM    180  CA  TYR A 148      -1.128  25.660   6.638  1.00 66.13           C  
ATOM    181  C   TYR A 148      -1.417  26.839   7.515  1.00 66.13           C  
ATOM    182  O   TYR A 148      -0.803  27.016   8.571  1.00 66.13           O  
ATOM    183  CB  TYR A 148      -2.173  24.572   6.880  1.00 81.13           C  
ATOM    184  CG  TYR A 148      -2.026  23.496   5.864  1.00 81.13           C  
ATOM    185  CD1 TYR A 148      -1.385  22.305   6.175  1.00 81.13           C  
ATOM    186  CD2 TYR A 148      -2.399  23.722   4.549  1.00 81.13           C  
ATOM    187  CE1 TYR A 148      -1.107  21.370   5.198  1.00 81.13           C  
ATOM    188  CE2 TYR A 148      -2.131  22.805   3.568  1.00 81.13           C  
ATOM    189  CZ  TYR A 148      -1.479  21.628   3.890  1.00 81.13           C  
ATOM    190  OH  TYR A 148      -1.167  20.730   2.888  1.00 81.13           O  
ATOM    191  N   LEU A 149      -2.358  27.649   7.055  1.00 74.27           N  
ATOM    192  CA  LEU A 149      -3.098  28.520   7.939  1.00 74.27           C  
ATOM    193  C   LEU A 149      -4.004  27.602   8.751  1.00 74.27           C  
ATOM    194  O   LEU A 149      -4.591  26.673   8.196  1.00 74.27           O  
ATOM    195  CB  LEU A 149      -3.926  29.487   7.107  1.00 86.73           C  
ATOM    196  CG  LEU A 149      -4.424  30.709   7.859  1.00 86.73           C  
ATOM    197  CD1 LEU A 149      -3.276  31.307   8.642  1.00 86.73           C  
ATOM    198  CD2 LEU A 149      -5.004  31.707   6.876  1.00 86.73           C  
ATOM    199  N   ALA A 150      -4.106  27.837  10.057  1.00 58.60           N  
ATOM    200  CA  ALA A 150      -4.979  27.025  10.902  1.00 58.60           C  
ATOM    201  C   ALA A 150      -5.465  27.786  12.137  1.00 58.60           C  
ATOM    202  O   ALA A 150      -4.814  28.723  12.611  1.00 58.60           O  
ATOM    203  CB  ALA A 150      -4.255  25.762  11.327  1.00105.01           C  
ATOM    204  N   ARG A 151      -6.612  27.375  12.661  1.00 70.43           N  
ATOM    205  CA  ARG A 151      -7.145  28.001  13.854  1.00 70.43           C  
ATOM    206  C   ARG A 151      -7.564  26.958  14.894  1.00 70.43           C  
ATOM    207  O   ARG A 151      -8.325  26.030  14.613  1.00 70.43           O  
ATOM    208  CB  ARG A 151      -8.335  28.886  13.486  1.00 91.22           C  
ATOM    209  CG  ARG A 151      -8.745  29.878  14.565  1.00 91.22           C  
ATOM    210  CD  ARG A 151      -9.985  30.637  14.128  1.00 91.22           C  
ATOM    211  NE  ARG A 151     -10.979  29.743  13.529  1.00 91.22           N  
ATOM    212  CZ  ARG A 151     -12.290  29.979  13.491  1.00 91.22           C  
ATOM    213  NH1 ARG A 151     -12.790  31.092  14.016  1.00 91.22           N  
ATOM    214  NH2 ARG A 151     -13.103  29.095  12.931  1.00 91.22           N  
ATOM    215  N   GLU A 152      -7.055  27.127  16.106  1.00 75.19           N  
ATOM    216  CA  GLU A 152      -7.383  26.247  17.209  1.00 75.19           C  
ATOM    217  C   GLU A 152      -8.825  26.520  17.590  1.00 75.19           C  
ATOM    218  O   GLU A 152      -9.168  27.642  17.932  1.00 75.19           O  
ATOM    219  CB  GLU A 152      -6.451  26.540  18.387  1.00 92.89           C  
ATOM    220  CG  GLU A 152      -6.433  25.471  19.445  1.00 92.89           C  
ATOM    221  CD  GLU A 152      -7.767  25.332  20.128  1.00 92.89           C  
ATOM    222  OE1 GLU A 152      -8.293  26.365  20.587  1.00 92.89           O  
ATOM    223  OE2 GLU A 152      -8.290  24.196  20.197  1.00 92.89           O  
ATOM    224  N   LYS A 153      -9.659  25.487  17.539  1.00 72.48           N  
ATOM    225  CA  LYS A 153     -11.106  25.624  17.714  1.00 72.48           C  
ATOM    226  C   LYS A 153     -11.608  26.207  19.046  1.00 72.48           C  
ATOM    227  O   LYS A 153     -12.630  26.887  19.074  1.00 72.48           O  
ATOM    228  CB  LYS A 153     -11.782  24.276  17.464  1.00103.80           C  
ATOM    229  CG  LYS A 153     -11.617  23.778  16.040  1.00103.80           C  
ATOM    230  CD  LYS A 153     -11.533  22.258  15.979  1.00103.80           C  
ATOM    231  CE  LYS A 153     -11.294  21.766  14.558  1.00103.80           C  
ATOM    232  NZ  LYS A 153     -11.213  20.277  14.472  1.00103.80           N  
ATOM    233  N   GLN A 154     -10.912  25.957  20.145  1.00 99.84           N  
ATOM    234  CA  GLN A 154     -11.390  26.466  21.425  1.00 99.84           C  
ATOM    235  C   GLN A 154     -11.036  27.941  21.625  1.00 99.84           C  
ATOM    236  O   GLN A 154     -11.839  28.726  22.146  1.00 99.84           O  
ATOM    237  CB  GLN A 154     -10.817  25.628  22.574  1.00189.46           C  
ATOM    238  CG  GLN A 154     -11.086  26.195  23.965  1.00189.46           C  
ATOM    239  CD  GLN A 154     -12.551  26.512  24.205  1.00189.46           C  
ATOM    240  OE1 GLN A 154     -13.431  26.041  23.483  1.00189.46           O  
ATOM    241  NE2 GLN A 154     -12.819  27.318  25.226  1.00189.46           N  
ATOM    242  N   SER A 155      -9.833  28.312  21.196  1.00 82.39           N  
ATOM    243  CA  SER A 155      -9.262  29.621  21.506  1.00 82.39           C  
ATOM    244  C   SER A 155      -9.434  30.565  20.323  1.00 82.39           C  
ATOM    245  O   SER A 155      -9.287  31.781  20.453  1.00 82.39           O  
ATOM    246  CB  SER A 155      -7.775  29.468  21.828  1.00 88.58           C  
ATOM    247  OG  SER A 155      -7.536  28.287  22.575  1.00 88.58           O  
ATOM    248  N   LYS A 156      -9.749  29.979  19.173  1.00 88.85           N  
ATOM    249  CA  LYS A 156      -9.844  30.707  17.919  1.00 88.85           C  
ATOM    250  C   LYS A 156      -8.505  31.321  17.586  1.00 88.85           C  
ATOM    251  O   LYS A 156      -8.444  32.352  16.937  1.00 88.85           O  
ATOM    252  CB  LYS A 156     -10.908  31.805  18.003  1.00101.85           C  
ATOM    253  CG  LYS A 156     -12.328  31.277  18.126  1.00101.85           C  
ATOM    254  CD  LYS A 156     -12.565  30.077  17.202  1.00101.85           C  
ATOM    255  CE  LYS A 156     -13.988  29.526  17.325  1.00101.85           C  
ATOM    256  NZ  LYS A 156     -15.028  30.508  16.879  1.00101.85           N  
ATOM    257  N   PHE A 157      -7.431  30.686  18.039  1.00 67.50           N  
ATOM    258  CA  PHE A 157      -6.090  31.215  17.827  1.00 67.50           C  
ATOM    259  C   PHE A 157      -5.591  30.885  16.433  1.00 67.50           C  
ATOM    260  O   PHE A 157      -5.878  29.812  15.898  1.00 67.50           O  
ATOM    261  CB  PHE A 157      -5.130  30.642  18.854  1.00 89.97           C  
ATOM    262  CG  PHE A 157      -3.772  31.263  18.817  1.00 89.97           C  
ATOM    263  CD1 PHE A 157      -2.869  30.932  17.818  1.00 89.97           C  
ATOM    264  CD2 PHE A 157      -3.396  32.184  19.778  1.00 89.97           C  
ATOM    265  CE1 PHE A 157      -1.617  31.512  17.780  1.00 89.97           C  
ATOM    266  CE2 PHE A 157      -2.147  32.765  19.742  1.00 89.97           C  
ATOM    267  CZ  PHE A 157      -1.257  32.431  18.744  1.00 89.97           C  
ATOM    268  N   ILE A 158      -4.854  31.813  15.836  1.00 79.58           N  
ATOM    269  CA  ILE A 158      -4.343  31.597  14.493  1.00 79.58           C  
ATOM    270  C   ILE A 158      -2.857  31.247  14.474  1.00 79.58           C  
ATOM    271  O   ILE A 158      -2.017  31.982  14.982  1.00 79.58           O  
ATOM    272  CB  ILE A 158      -4.589  32.821  13.594  1.00 60.29           C  
ATOM    273  CG1 ILE A 158      -6.079  32.993  13.353  1.00 60.29           C  
ATOM    274  CG2 ILE A 158      -3.954  32.586  12.216  1.00 60.29           C  
ATOM    275  CD1 ILE A 158      -6.567  32.179  12.163  1.00 60.29           C  
ATOM    276  N   LEU A 159      -2.540  30.110  13.877  1.00 74.44           N  
ATOM    277  CA  LEU A 159      -1.183  29.625  13.888  1.00 74.44           C  
ATOM    278  C   LEU A 159      -0.876  29.143  12.490  1.00 74.44           C  
ATOM    279  O   LEU A 159      -1.793  28.907  11.703  1.00 74.44           O  
ATOM    280  CB  LEU A 159      -1.063  28.474  14.874  1.00 82.50           C  
ATOM    281  CG  LEU A 159      -2.091  27.379  14.596  1.00 82.50           C  
ATOM    282  CD1 LEU A 159      -1.383  26.115  14.128  1.00 82.50           C  
ATOM    283  CD2 LEU A 159      -2.904  27.113  15.846  1.00 82.50           C  
ATOM    284  N   ALA A 160       0.411  29.016  12.178  1.00 61.71           N  
ATOM    285  CA  ALA A 160       0.841  28.228  11.034  1.00 61.71           C  
ATOM    286  C   ALA A 160       0.999  26.762  11.461  1.00 61.71           C  
ATOM    287  O   ALA A 160       1.830  26.433  12.313  1.00 61.71           O  
ATOM    288  CB  ALA A 160       2.150  28.765  10.508  1.00 52.28           C  
ATOM    289  N   LEU A 161       0.185  25.878  10.893  1.00106.39           N  
ATOM    290  CA  LEU A 161       0.323  24.467  11.214  1.00106.39           C  
ATOM    291  C   LEU A 161       1.213  23.814  10.191  1.00106.39           C  
ATOM    292  O   LEU A 161       0.805  23.585   9.055  1.00106.39           O  
ATOM    293  CB  LEU A 161      -1.025  23.754  11.226  1.00 82.06           C  
ATOM    294  CG  LEU A 161      -0.989  22.373  11.894  1.00 82.06           C  
ATOM    295  CD1 LEU A 161      -0.407  22.515  13.287  1.00 82.06           C  
ATOM    296  CD2 LEU A 161      -2.384  21.780  11.980  1.00 82.06           C  
ATOM    297  N   LYS A 162       2.439  23.523  10.601  1.00 85.30           N  
ATOM    298  CA  LYS A 162       3.376  22.807   9.753  1.00 85.30           C  
ATOM    299  C   LYS A 162       3.187  21.301   9.887  1.00 85.30           C  
ATOM    300  O   LYS A 162       3.219  20.731  10.987  1.00 85.30           O  
ATOM    301  CB  LYS A 162       4.803  23.191  10.113  1.00 67.93           C  
ATOM    302  CG  LYS A 162       5.777  22.050  10.007  1.00 67.93           C  
ATOM    303  CD  LYS A 162       7.170  22.572   9.991  1.00 67.93           C  
ATOM    304  CE  LYS A 162       7.371  23.329   8.710  1.00 67.93           C  
ATOM    305  NZ  LYS A 162       8.482  24.275   8.899  1.00 67.93           N  
ATOM    306  N   VAL A 163       2.972  20.668   8.744  1.00 77.98           N  
ATOM    307  CA  VAL A 163       2.670  19.257   8.715  1.00 77.98           C  
ATOM    308  C   VAL A 163       3.749  18.496   7.963  1.00 77.98           C  
ATOM    309  O   VAL A 163       3.736  18.416   6.736  1.00 77.98           O  
ATOM    310  CB  VAL A 163       1.311  19.023   8.071  1.00 66.38           C  
ATOM    311  CG1 VAL A 163       1.133  17.557   7.737  1.00 66.38           C  
ATOM    312  CG2 VAL A 163       0.237  19.480   9.020  1.00 66.38           C  
ATOM    313  N   LEU A 164       4.691  17.950   8.726  1.00118.09           N  
ATOM    314  CA  LEU A 164       5.801  17.188   8.174  1.00118.09           C  
ATOM    315  C   LEU A 164       5.410  15.722   8.073  1.00118.09           C  
ATOM    316  O   LEU A 164       4.500  15.271   8.765  1.00118.09           O  
ATOM    317  CB  LEU A 164       7.024  17.310   9.079  1.00 88.01           C  
ATOM    318  CG  LEU A 164       7.651  18.680   9.304  1.00 88.01           C  
ATOM    319  CD1 LEU A 164       8.790  18.515  10.303  1.00 88.01           C  
ATOM    320  CD2 LEU A 164       8.144  19.268   7.976  1.00 88.01           C  
ATOM    321  N   PHE A 165       6.112  14.981   7.220  1.00144.09           N  
ATOM    322  CA  PHE A 165       5.832  13.563   7.041  1.00144.09           C  
ATOM    323  C   PHE A 165       6.939  12.642   7.537  1.00144.09           C  
ATOM    324  O   PHE A 165       8.072  12.681   7.048  1.00144.09           O  
ATOM    325  CB  PHE A 165       5.535  13.279   5.575  1.00140.94           C  
ATOM    326  CG  PHE A 165       4.181  13.739   5.149  1.00140.94           C  
ATOM    327  CD1 PHE A 165       3.047  13.226   5.756  1.00140.94           C  
ATOM    328  CD2 PHE A 165       4.036  14.690   4.157  1.00140.94           C  
ATOM    329  CE1 PHE A 165       1.791  13.655   5.382  1.00140.94           C  
ATOM    330  CE2 PHE A 165       2.781  15.125   3.777  1.00140.94           C  
ATOM    331  CZ  PHE A 165       1.656  14.607   4.391  1.00140.94           C  
ATOM    332  N   LYS A 166       6.582  11.802   8.506  1.00157.98           N  
ATOM    333  CA  LYS A 166       7.525  10.919   9.185  1.00157.98           C  
ATOM    334  C   LYS A 166       8.309  10.105   8.157  1.00157.98           C  
ATOM    335  O   LYS A 166       9.538  10.044   8.189  1.00157.98           O  
ATOM    336  CB  LYS A 166       6.756   9.985  10.132  1.00 79.07           C  
ATOM    337  CG  LYS A 166       7.354   9.851  11.532  1.00 79.07           C  
ATOM    338  CD  LYS A 166       6.268   9.852  12.612  1.00 79.07           C  
ATOM    339  CE  LYS A 166       4.979   9.196  12.103  1.00 79.07           C  
ATOM    340  NZ  LYS A 166       3.875   9.208  13.113  1.00 79.07           N  
ATOM    341  N   ALA A 167       7.574   9.500   7.235  1.00126.87           N  
ATOM    342  CA  ALA A 167       8.143   8.666   6.191  1.00126.87           C  
ATOM    343  C   ALA A 167       9.439   9.213   5.582  1.00126.87           C  
ATOM    344  O   ALA A 167      10.463   8.528   5.572  1.00126.87           O  
ATOM    345  CB  ALA A 167       7.101   8.462   5.108  1.00 62.17           C  
ATOM    346  N   GLN A 168       9.397  10.443   5.076  1.00108.69           N  
ATOM    347  CA  GLN A 168      10.521  11.000   4.322  1.00108.69           C  
ATOM    348  C   GLN A 168      11.648  11.489   5.214  1.00108.69           C  
ATOM    349  O   GLN A 168      12.808  11.466   4.813  1.00108.69           O  
ATOM    350  CB  GLN A 168      10.065  12.163   3.433  1.00127.43           C  
ATOM    351  CG  GLN A 168       9.189  11.758   2.269  1.00127.43           C  
ATOM    352  CD  GLN A 168       7.866  11.185   2.721  1.00127.43           C  
ATOM    353  OE1 GLN A 168       7.638   9.978   2.651  1.00127.43           O  
ATOM    354  NE2 GLN A 168       6.983  12.052   3.196  1.00127.43           N  
ATOM    355  N   LEU A 169      11.307  11.941   6.416  1.00134.14           N  
ATOM    356  CA  LEU A 169      12.296  12.533   7.313  1.00134.14           C  
ATOM    357  C   LEU A 169      13.480  11.600   7.535  1.00134.14           C  
ATOM    358  O   LEU A 169      14.616  12.051   7.692  1.00134.14           O  
ATOM    359  CB  LEU A 169      11.650  12.877   8.659  1.00 93.11           C  
ATOM    360  CG  LEU A 169      10.989  14.252   8.781  1.00 93.11           C  
ATOM    361  CD1 LEU A 169      10.267  14.381  10.119  1.00 93.11           C  
ATOM    362  CD2 LEU A 169      12.059  15.314   8.656  1.00 93.11           C  
ATOM    363  N   GLU A 170      13.203  10.298   7.546  1.00130.04           N  
ATOM    364  CA  GLU A 170      14.242   9.286   7.682  1.00130.04           C  
ATOM    365  C   GLU A 170      14.785   8.878   6.315  1.00130.04           C  
ATOM    366  O   GLU A 170      15.996   8.780   6.130  1.00130.04           O  
ATOM    367  CB  GLU A 170      13.696   8.057   8.411  1.00188.35           C  
ATOM    368  CG  GLU A 170      13.172   8.347   9.806  1.00188.35           C  
ATOM    369  CD  GLU A 170      11.662   8.461   9.845  1.00188.35           C  
ATOM    370  OE1 GLU A 170      11.012   8.058   8.857  1.00188.35           O  
ATOM    371  OE2 GLU A 170      11.125   8.952  10.861  1.00188.35           O  
ATOM    372  N   LYS A 171      13.892   8.646   5.356  1.00 96.47           N  
ATOM    373  CA  LYS A 171      14.311   8.434   3.976  1.00 96.47           C  
ATOM    374  C   LYS A 171      15.265   9.547   3.547  1.00 96.47           C  
ATOM    375  O   LYS A 171      15.871   9.478   2.478  1.00 96.47           O  
ATOM    376  CB  LYS A 171      13.096   8.404   3.046  1.00113.17           C  
ATOM    377  CG  LYS A 171      12.441   7.042   2.922  1.00113.17           C  
ATOM    378  CD  LYS A 171      11.672   6.927   1.611  1.00113.17           C  
ATOM    379  CE  LYS A 171      11.527   5.471   1.162  1.00113.17           C  
ATOM    380  NZ  LYS A 171      12.824   4.847   0.745  1.00113.17           N  
ATOM    381  N   ALA A 172      15.374  10.576   4.388  1.00140.65           N  
ATOM    382  CA  ALA A 172      16.350  11.656   4.222  1.00140.65           C  
ATOM    383  C   ALA A 172      17.397  11.574   5.323  1.00140.65           C  
ATOM    384  O   ALA A 172      18.584  11.798   5.088  1.00140.65           O  
ATOM    385  CB  ALA A 172      15.654  13.012   4.286  1.00 53.09           C  
ATOM    386  N   GLY A 173      16.940  11.265   6.532  1.00126.14           N  
ATOM    387  CA  GLY A 173      17.850  11.090   7.647  1.00126.14           C  
ATOM    388  C   GLY A 173      17.817  12.221   8.655  1.00126.14           C  
ATOM    389  O   GLY A 173      18.484  12.150   9.685  1.00126.14           O  
ATOM    390  N   VAL A 174      17.042  13.264   8.375  1.00112.95           N  
ATOM    391  CA  VAL A 174      17.054  14.447   9.231  1.00112.95           C  
ATOM    392  C   VAL A 174      16.071  14.336  10.392  1.00112.95           C  
ATOM    393  O   VAL A 174      15.847  15.308  11.108  1.00112.95           O  
ATOM    394  CB  VAL A 174      16.729  15.737   8.435  1.00 82.43           C  
ATOM    395  CG1 VAL A 174      17.454  15.718   7.111  1.00 82.43           C  
ATOM    396  CG2 VAL A 174      15.230  15.882   8.238  1.00 82.43           C  
ATOM    397  N   GLU A 175      15.490  13.151  10.574  1.00123.32           N  
ATOM    398  CA  GLU A 175      14.575  12.897  11.688  1.00123.32           C  
ATOM    399  C   GLU A 175      15.139  13.482  12.976  1.00123.32           C  
ATOM    400  O   GLU A 175      14.395  13.831  13.897  1.00123.32           O  
ATOM    401  CB  GLU A 175      14.362  11.391  11.874  1.00155.84           C  
ATOM    402  CG  GLU A 175      15.506  10.676  12.588  1.00155.84           C  
ATOM    403  CD  GLU A 175      16.677  10.370  11.672  1.00155.84           C  
ATOM    404  OE1 GLU A 175      16.491   9.604  10.703  1.00155.84           O  
ATOM    405  OE2 GLU A 175      17.785  10.893  11.921  1.00155.84           O  
ATOM    406  N   HIS A 176      16.462  13.586  13.028  1.00106.76           N  
ATOM    407  CA  HIS A 176      17.149  14.093  14.201  1.00106.76           C  
ATOM    408  C   HIS A 176      17.463  15.580  14.064  1.00106.76           C  
ATOM    409  O   HIS A 176      17.533  16.294  15.061  1.00106.76           O  
ATOM    410  CB  HIS A 176      18.444  13.309  14.429  1.00202.19           C  
ATOM    411  CG  HIS A 176      18.886  13.281  15.858  1.00202.19           C  
ATOM    412  ND1 HIS A 176      19.834  12.398  16.329  1.00202.19           N  
ATOM    413  CD2 HIS A 176      18.495  14.017  16.924  1.00202.19           C  
ATOM    414  CE1 HIS A 176      20.007  12.593  17.624  1.00202.19           C  
ATOM    415  NE2 HIS A 176      19.206  13.569  18.010  1.00202.19           N  
ATOM    416  N   GLN A 177      17.654  16.044  12.831  1.00185.08           N  
ATOM    417  CA  GLN A 177      17.861  17.469  12.567  1.00185.08           C  
ATOM    418  C   GLN A 177      16.553  18.215  12.806  1.00185.08           C  
ATOM    419  O   GLN A 177      16.472  19.435  12.658  1.00185.08           O  
ATOM    420  CB  GLN A 177      18.317  17.671  11.123  1.00127.78           C  
ATOM    421  CG  GLN A 177      19.439  16.731  10.708  1.00127.78           C  
ATOM    422  CD  GLN A 177      20.753  17.046  11.394  1.00127.78           C  
ATOM    423  OE1 GLN A 177      21.189  18.197  11.421  1.00127.78           O  
ATOM    424  NE2 GLN A 177      21.392  16.023  11.952  1.00127.78           N  
ATOM    425  N   LEU A 178      15.532  17.446  13.169  1.00113.80           N  
ATOM    426  CA  LEU A 178      14.224  17.959  13.542  1.00113.80           C  
ATOM    427  C   LEU A 178      14.092  17.961  15.059  1.00113.80           C  
ATOM    428  O   LEU A 178      13.621  18.930  15.660  1.00113.80           O  
ATOM    429  CB  LEU A 178      13.144  17.068  12.951  1.00 72.44           C  
ATOM    430  CG  LEU A 178      11.829  17.116  13.720  1.00 72.44           C  
ATOM    431  CD1 LEU A 178      11.271  18.540  13.747  1.00 72.44           C  
ATOM    432  CD2 LEU A 178      10.856  16.155  13.068  1.00 72.44           C  
ATOM    433  N   ARG A 179      14.506  16.855  15.669  1.00115.87           N  
ATOM    434  CA  ARG A 179      14.581  16.756  17.120  1.00115.87           C  
ATOM    435  C   ARG A 179      15.270  18.010  17.636  1.00115.87           C  
ATOM    436  O   ARG A 179      15.029  18.442  18.756  1.00115.87           O  
ATOM    437  CB  ARG A 179      15.377  15.507  17.513  1.00187.39           C  
ATOM    438  CG  ARG A 179      15.387  15.182  18.999  1.00187.39           C  
ATOM    439  CD  ARG A 179      16.141  13.880  19.264  1.00187.39           C  
ATOM    440  NE  ARG A 179      16.340  13.630  20.690  1.00187.39           N  
ATOM    441  CZ  ARG A 179      17.459  13.142  21.220  1.00187.39           C  
ATOM    442  NH1 ARG A 179      18.493  12.846  20.444  1.00187.39           N  
ATOM    443  NH2 ARG A 179      17.546  12.952  22.530  1.00187.39           N  
ATOM    444  N   ARG A 180      16.118  18.595  16.795  1.00128.47           N  
ATOM    445  CA  ARG A 180      16.847  19.810  17.141  1.00128.47           C  
ATOM    446  C   ARG A 180      15.964  21.044  16.980  1.00128.47           C  
ATOM    447  O   ARG A 180      15.852  21.857  17.896  1.00128.47           O  
ATOM    448  CB  ARG A 180      18.093  19.959  16.259  1.00193.62           C  
ATOM    449  CG  ARG A 180      18.997  18.736  16.230  1.00193.62           C  
ATOM    450  CD  ARG A 180      19.103  18.085  17.604  1.00193.62           C  
ATOM    451  NE  ARG A 180      20.016  16.943  17.609  1.00193.62           N  
ATOM    452  CZ  ARG A 180      20.278  16.197  18.679  1.00193.62           C  
ATOM    453  NH1 ARG A 180      19.697  16.467  19.839  1.00193.62           N  
ATOM    454  NH2 ARG A 180      21.133  15.187  18.593  1.00193.62           N  
ATOM    455  N   GLU A 181      15.336  21.184  15.817  1.00168.76           N  
ATOM    456  CA  GLU A 181      14.500  22.350  15.562  1.00168.76           C  
ATOM    457  C   GLU A 181      13.405  22.478  16.616  1.00168.76           C  
ATOM    458  O   GLU A 181      13.173  23.567  17.137  1.00168.76           O  
ATOM    459  CB  GLU A 181      13.864  22.274  14.170  1.00114.22           C  
ATOM    460  CG  GLU A 181      12.901  23.424  13.874  1.00114.22           C  
ATOM    461  CD  GLU A 181      12.085  23.218  12.595  1.00114.22           C  
ATOM    462  OE1 GLU A 181      12.244  22.160  11.945  1.00114.22           O  
ATOM    463  OE2 GLU A 181      11.286  24.117  12.239  1.00114.22           O  
ATOM    464  N   VAL A 182      12.737  21.371  16.937  1.00 68.45           N  
ATOM    465  CA  VAL A 182      11.634  21.425  17.886  1.00 68.45           C  
ATOM    466  C   VAL A 182      12.128  21.837  19.265  1.00 68.45           C  
ATOM    467  O   VAL A 182      11.571  22.745  19.894  1.00 68.45           O  
ATOM    468  CB  VAL A 182      10.895  20.069  17.981  1.00 54.59           C  
ATOM    469  CG1 VAL A 182      10.078  20.012  19.246  1.00 54.59           C  
ATOM    470  CG2 VAL A 182       9.950  19.912  16.808  1.00 54.59           C  
ATOM    471  N   GLU A 183      13.191  21.188  19.729  1.00102.79           N  
ATOM    472  CA  GLU A 183      13.767  21.520  21.027  1.00102.79           C  
ATOM    473  C   GLU A 183      14.358  22.931  21.032  1.00102.79           C  
ATOM    474  O   GLU A 183      14.065  23.718  21.925  1.00102.79           O  
ATOM    475  CB  GLU A 183      14.830  20.485  21.412  1.00201.54           C  
ATOM    476  CG  GLU A 183      14.293  19.290  22.216  1.00201.54           C  
ATOM    477  CD  GLU A 183      13.510  18.281  21.379  1.00201.54           C  
ATOM    478  OE1 GLU A 183      13.115  18.612  20.242  1.00201.54           O  
ATOM    479  OE2 GLU A 183      13.287  17.150  21.866  1.00201.54           O  
ATOM    480  N   ILE A 184      15.164  23.256  20.025  1.00127.90           N  
ATOM    481  CA  ILE A 184      15.777  24.583  19.931  1.00127.90           C  
ATOM    482  C   ILE A 184      14.717  25.677  19.799  1.00127.90           C  
ATOM    483  O   ILE A 184      14.788  26.715  20.464  1.00127.90           O  
ATOM    484  CB  ILE A 184      16.733  24.690  18.710  1.00131.52           C  
ATOM    485  CG1 ILE A 184      17.831  23.630  18.805  1.00131.52           C  
ATOM    486  CG2 ILE A 184      17.375  26.080  18.659  1.00131.52           C  
ATOM    487  CD1 ILE A 184      18.813  23.663  17.654  1.00131.52           C  
ATOM    488  N   GLN A 185      13.735  25.440  18.938  1.00 95.35           N  
ATOM    489  CA  GLN A 185      12.713  26.438  18.665  1.00 95.35           C  
ATOM    490  C   GLN A 185      12.002  26.818  19.951  1.00 95.35           C  
ATOM    491  O   GLN A 185      12.174  27.915  20.472  1.00 95.35           O  
ATOM    492  CB  GLN A 185      11.691  25.885  17.681  1.00108.38           C  
ATOM    493  CG  GLN A 185      11.007  26.949  16.871  1.00108.38           C  
ATOM    494  CD  GLN A 185      11.905  27.503  15.802  1.00108.38           C  
ATOM    495  OE1 GLN A 185      12.337  26.782  14.905  1.00108.38           O  
ATOM    496  NE2 GLN A 185      12.197  28.790  15.888  1.00108.38           N  
ATOM    497  N   SER A 186      11.209  25.889  20.466  1.00 94.16           N  
ATOM    498  CA  SER A 186      10.329  26.176  21.578  1.00 94.16           C  
ATOM    499  C   SER A 186      11.025  26.880  22.729  1.00 94.16           C  
ATOM    500  O   SER A 186      10.397  27.644  23.447  1.00 94.16           O  
ATOM    501  CB  SER A 186       9.702  24.888  22.081  1.00 97.52           C  
ATOM    502  OG  SER A 186      10.710  23.929  22.306  1.00 97.52           O  
ATOM    503  N   HIS A 187      12.315  26.632  22.916  1.00127.59           N  
ATOM    504  CA  HIS A 187      13.011  27.187  24.076  1.00127.59           C  
ATOM    505  C   HIS A 187      13.505  28.617  23.865  1.00127.59           C  
ATOM    506  O   HIS A 187      14.226  29.163  24.707  1.00127.59           O  
ATOM    507  CB  HIS A 187      14.192  26.294  24.465  1.00135.32           C  
ATOM    508  CG  HIS A 187      13.789  25.008  25.118  1.00135.32           C  
ATOM    509  ND1 HIS A 187      14.076  23.774  24.573  1.00135.32           N  
ATOM    510  CD2 HIS A 187      13.125  24.765  26.272  1.00135.32           C  
ATOM    511  CE1 HIS A 187      13.607  22.826  25.363  1.00135.32           C  
ATOM    512  NE2 HIS A 187      13.025  23.400  26.401  1.00135.32           N  
ATOM    513  N   LEU A 188      13.112  29.225  22.747  1.00 99.99           N  
ATOM    514  CA  LEU A 188      13.601  30.557  22.395  1.00 99.99           C  
ATOM    515  C   LEU A 188      12.521  31.643  22.384  1.00 99.99           C  
ATOM    516  O   LEU A 188      11.423  31.441  21.872  1.00 99.99           O  
ATOM    517  CB  LEU A 188      14.305  30.506  21.038  1.00 95.55           C  
ATOM    518  CG  LEU A 188      15.583  29.664  21.031  1.00 95.55           C  
ATOM    519  CD1 LEU A 188      16.142  29.569  19.623  1.00 95.55           C  
ATOM    520  CD2 LEU A 188      16.599  30.294  21.976  1.00 95.55           C  
ATOM    521  N   ARG A 189      12.851  32.797  22.960  1.00 98.73           N  
ATOM    522  CA  ARG A 189      11.900  33.891  23.106  1.00 98.73           C  
ATOM    523  C   ARG A 189      12.539  35.182  22.626  1.00 98.73           C  
ATOM    524  O   ARG A 189      13.396  35.745  23.302  1.00 98.73           O  
ATOM    525  CB  ARG A 189      11.485  34.049  24.571  1.00138.57           C  
ATOM    526  CG  ARG A 189      11.050  32.760  25.243  1.00138.57           C  
ATOM    527  CD  ARG A 189       9.836  32.162  24.560  1.00138.57           C  
ATOM    528  NE  ARG A 189       9.747  30.724  24.792  1.00138.57           N  
ATOM    529  CZ  ARG A 189       9.052  30.166  25.776  1.00138.57           C  
ATOM    530  NH1 ARG A 189       8.377  30.926  26.626  1.00138.57           N  
ATOM    531  NH2 ARG A 189       9.036  28.847  25.913  1.00138.57           N  
ATOM    532  N   HIS A 190      12.108  35.644  21.457  1.00 82.70           N  
ATOM    533  CA  HIS A 190      12.658  36.841  20.838  1.00 82.70           C  
ATOM    534  C   HIS A 190      11.682  37.298  19.760  1.00 82.70           C  
ATOM    535  O   HIS A 190      11.079  36.475  19.073  1.00 82.70           O  
ATOM    536  CB  HIS A 190      14.019  36.529  20.209  1.00 77.98           C  
ATOM    537  CG  HIS A 190      14.833  37.743  19.893  1.00 77.98           C  
ATOM    538  ND1 HIS A 190      14.396  38.732  19.042  1.00 77.98           N  
ATOM    539  CD2 HIS A 190      16.055  38.130  20.322  1.00 77.98           C  
ATOM    540  CE1 HIS A 190      15.313  39.680  18.962  1.00 77.98           C  
ATOM    541  NE2 HIS A 190      16.331  39.338  19.730  1.00 77.98           N  
ATOM    542  N   PRO A 191      11.509  38.622  19.606  1.00 82.13           N  
ATOM    543  CA  PRO A 191      10.531  39.212  18.682  1.00 82.13           C  
ATOM    544  C   PRO A 191      10.824  39.045  17.197  1.00 82.13           C  
ATOM    545  O   PRO A 191      10.021  39.435  16.358  1.00 82.13           O  
ATOM    546  CB  PRO A 191      10.489  40.685  19.089  1.00 62.04           C  
ATOM    547  CG  PRO A 191      11.784  40.934  19.772  1.00 62.04           C  
ATOM    548  CD  PRO A 191      12.151  39.644  20.452  1.00 62.04           C  
ATOM    549  N   ASN A 192      11.977  38.481  16.868  1.00 91.04           N  
ATOM    550  CA  ASN A 192      12.331  38.303  15.474  1.00 91.04           C  
ATOM    551  C   ASN A 192      12.672  36.860  15.168  1.00 91.04           C  
ATOM    552  O   ASN A 192      13.194  36.549  14.100  1.00 91.04           O  
ATOM    553  CB  ASN A 192      13.497  39.204  15.127  1.00 73.95           C  
ATOM    554  CG  ASN A 192      13.271  40.616  15.577  1.00 73.95           C  
ATOM    555  OD1 ASN A 192      13.553  40.952  16.713  1.00 73.95           O  
ATOM    556  ND2 ASN A 192      12.755  41.454  14.689  1.00 73.95           N  
ATOM    557  N   ILE A 193      12.376  35.988  16.122  1.00 74.44           N  
ATOM    558  CA  ILE A 193      12.457  34.551  15.922  1.00 74.44           C  
ATOM    559  C   ILE A 193      11.064  33.980  16.019  1.00 74.44           C  
ATOM    560  O   ILE A 193      10.361  34.237  16.999  1.00 74.44           O  
ATOM    561  CB  ILE A 193      13.272  33.865  17.011  1.00 66.20           C  
ATOM    562  CG1 ILE A 193      14.748  34.277  16.922  1.00 66.20           C  
ATOM    563  CG2 ILE A 193      13.095  32.349  16.880  1.00 66.20           C  
ATOM    564  CD1 ILE A 193      15.016  35.759  17.001  1.00 66.20           C  
ATOM    565  N   LEU A 194      10.663  33.189  15.028  1.00 75.46           N  
ATOM    566  CA  LEU A 194       9.309  32.630  15.014  1.00 75.46           C  
ATOM    567  C   LEU A 194       9.132  31.617  16.129  1.00 75.46           C  
ATOM    568  O   LEU A 194       9.955  30.732  16.302  1.00 75.46           O  
ATOM    569  CB  LEU A 194       9.036  31.948  13.679  1.00 71.82           C  
ATOM    570  CG  LEU A 194       7.595  31.986  13.195  1.00 71.82           C  
ATOM    571  CD1 LEU A 194       7.310  33.372  12.670  1.00 71.82           C  
ATOM    572  CD2 LEU A 194       7.376  30.961  12.114  1.00 71.82           C  
ATOM    573  N   ARG A 195       8.058  31.737  16.889  1.00 83.98           N  
ATOM    574  CA  ARG A 195       7.874  30.852  18.025  1.00 83.98           C  
ATOM    575  C   ARG A 195       7.332  29.505  17.592  1.00 83.98           C  
ATOM    576  O   ARG A 195       6.368  29.439  16.829  1.00 83.98           O  
ATOM    577  CB  ARG A 195       6.917  31.478  19.038  1.00109.51           C  
ATOM    578  CG  ARG A 195       7.536  32.572  19.875  1.00109.51           C  
ATOM    579  CD  ARG A 195       7.262  32.327  21.339  1.00109.51           C  
ATOM    580  NE  ARG A 195       7.589  30.957  21.723  1.00109.51           N  
ATOM    581  CZ  ARG A 195       7.069  30.334  22.777  1.00109.51           C  
ATOM    582  NH1 ARG A 195       6.190  30.961  23.552  1.00109.51           N  
ATOM    583  NH2 ARG A 195       7.428  29.086  23.054  1.00109.51           N  
ATOM    584  N   LEU A 196       7.948  28.426  18.071  1.00 76.19           N  
ATOM    585  CA  LEU A 196       7.242  27.158  18.105  1.00 76.19           C  
ATOM    586  C   LEU A 196       6.453  27.167  19.394  1.00 76.19           C  
ATOM    587  O   LEU A 196       6.970  27.555  20.440  1.00 76.19           O  
ATOM    588  CB  LEU A 196       8.201  25.973  18.104  1.00 69.72           C  
ATOM    589  CG  LEU A 196       7.473  24.625  18.123  1.00 69.72           C  
ATOM    590  CD1 LEU A 196       6.625  24.483  16.880  1.00 69.72           C  
ATOM    591  CD2 LEU A 196       8.470  23.506  18.183  1.00 69.72           C  
ATOM    592  N   TYR A 197       5.196  26.753  19.307  1.00105.23           N  
ATOM    593  CA  TYR A 197       4.272  26.838  20.431  1.00105.23           C  
ATOM    594  C   TYR A 197       4.120  25.490  21.123  1.00105.23           C  
ATOM    595  O   TYR A 197       3.872  25.408  22.327  1.00105.23           O  
ATOM    596  CB  TYR A 197       2.902  27.322  19.941  1.00 77.25           C  
ATOM    597  CG  TYR A 197       2.820  28.818  19.749  1.00 77.25           C  
ATOM    598  CD1 TYR A 197       3.148  29.684  20.789  1.00 77.25           C  
ATOM    599  CD2 TYR A 197       2.426  29.364  18.533  1.00 77.25           C  
ATOM    600  CE1 TYR A 197       3.091  31.043  20.630  1.00 77.25           C  
ATOM    601  CE2 TYR A 197       2.363  30.731  18.358  1.00 77.25           C  
ATOM    602  CZ  TYR A 197       2.698  31.572  19.412  1.00 77.25           C  
ATOM    603  OH  TYR A 197       2.646  32.949  19.253  1.00 77.25           O  
ATOM    604  N   GLY A 198       4.273  24.433  20.341  1.00 77.41           N  
ATOM    605  CA  GLY A 198       3.965  23.104  20.821  1.00 77.41           C  
ATOM    606  C   GLY A 198       4.143  22.158  19.662  1.00 77.41           C  
ATOM    607  O   GLY A 198       4.403  22.590  18.542  1.00 77.41           O  
ATOM    608  N   TYR A 199       4.028  20.866  19.927  1.00103.47           N  
ATOM    609  CA  TYR A 199       4.093  19.897  18.856  1.00103.47           C  
ATOM    610  C   TYR A 199       3.440  18.606  19.277  1.00103.47           C  
ATOM    611  O   TYR A 199       3.326  18.300  20.472  1.00103.47           O  
ATOM    612  CB  TYR A 199       5.543  19.638  18.443  1.00142.55           C  
ATOM    613  CG  TYR A 199       6.391  18.976  19.502  1.00142.55           C  
ATOM    614  CD1 TYR A 199       6.898  19.707  20.569  1.00142.55           C  
ATOM    615  CD2 TYR A 199       6.699  17.625  19.427  1.00142.55           C  
ATOM    616  CE1 TYR A 199       7.691  19.112  21.534  1.00142.55           C  
ATOM    617  CE2 TYR A 199       7.492  17.019  20.387  1.00142.55           C  
ATOM    618  CZ  TYR A 199       7.986  17.768  21.440  1.00142.55           C  
ATOM    619  OH  TYR A 199       8.774  17.172  22.402  1.00142.55           O  
ATOM    620  N   PHE A 200       2.997  17.861  18.275  1.00 94.49           N  
ATOM    621  CA  PHE A 200       2.411  16.558  18.490  1.00 94.49           C  
ATOM    622  C   PHE A 200       2.485  15.877  17.148  1.00 94.49           C  
ATOM    623  O   PHE A 200       2.202  16.492  16.124  1.00 94.49           O  
ATOM    624  CB  PHE A 200       0.951  16.693  18.912  1.00120.04           C  
ATOM    625  CG  PHE A 200       0.068  17.252  17.836  1.00120.04           C  
ATOM    626  CD1 PHE A 200       0.024  18.611  17.595  1.00120.04           C  
ATOM    627  CD2 PHE A 200      -0.699  16.415  17.048  1.00120.04           C  
ATOM    628  CE1 PHE A 200      -0.767  19.122  16.586  1.00120.04           C  
ATOM    629  CE2 PHE A 200      -1.491  16.924  16.038  1.00120.04           C  
ATOM    630  CZ  PHE A 200      -1.525  18.277  15.806  1.00120.04           C  
ATOM    631  N   HIS A 201       2.870  14.611  17.145  1.00125.71           N  
ATOM    632  CA  HIS A 201       2.789  13.824  15.929  1.00125.71           C  
ATOM    633  C   HIS A 201       1.666  12.807  16.067  1.00125.71           C  
ATOM    634  O   HIS A 201       1.379  12.328  17.161  1.00125.71           O  
ATOM    635  CB  HIS A 201       4.114  13.107  15.670  1.00142.81           C  
ATOM    636  CG  HIS A 201       4.425  12.036  16.668  1.00142.81           C  
ATOM    637  ND1 HIS A 201       4.231  10.696  16.406  1.00142.81           N  
ATOM    638  CD2 HIS A 201       4.915  12.108  17.928  1.00142.81           C  
ATOM    639  CE1 HIS A 201       4.589   9.989  17.462  1.00142.81           C  
ATOM    640  NE2 HIS A 201       5.007  10.821  18.399  1.00142.81           N  
ATOM    641  N   ASP A 202       1.020  12.489  14.956  1.00136.23           N  
ATOM    642  CA  ASP A 202       0.089  11.378  14.947  1.00136.23           C  
ATOM    643  C   ASP A 202       0.860  10.116  14.590  1.00136.23           C  
ATOM    644  O   ASP A 202       1.961   9.877  15.096  1.00136.23           O  
ATOM    645  CB  ASP A 202      -1.033  11.617  13.928  1.00137.81           C  
ATOM    646  CG  ASP A 202      -0.518  11.749  12.507  1.00137.81           C  
ATOM    647  OD1 ASP A 202       0.710  11.872  12.332  1.00137.81           O  
ATOM    648  OD2 ASP A 202      -1.338  11.729  11.565  1.00137.81           O  
ATOM    649  N   ALA A 203       0.276   9.316  13.709  1.00161.65           N  
ATOM    650  CA  ALA A 203       0.873   8.059  13.295  1.00161.65           C  
ATOM    651  C   ALA A 203       1.561   8.214  11.939  1.00161.65           C  
ATOM    652  O   ALA A 203       2.562   7.554  11.656  1.00161.65           O  
ATOM    653  CB  ALA A 203      -0.206   6.986  13.223  1.00 69.97           C  
ATOM    654  N   THR A 204       1.021   9.101  11.111  1.00197.95           N  
ATOM    655  CA  THR A 204       1.488   9.259   9.738  1.00197.95           C  
ATOM    656  C   THR A 204       2.569  10.335   9.644  1.00197.95           C  
ATOM    657  O   THR A 204       3.510  10.219   8.854  1.00197.95           O  
ATOM    658  CB  THR A 204       0.319   9.654   8.806  1.00135.20           C  
ATOM    659  OG1 THR A 204      -0.779   8.752   9.006  1.00135.20           O  
ATOM    660  CG2 THR A 204       0.761   9.607   7.340  1.00135.20           C  
ATOM    661  N   ARG A 205       2.428  11.375  10.463  1.00155.92           N  
ATOM    662  CA  ARG A 205       3.207  12.599  10.307  1.00155.92           C  
ATOM    663  C   ARG A 205       3.424  13.338  11.632  1.00155.92           C  
ATOM    664  O   ARG A 205       2.783  13.038  12.639  1.00155.92           O  
ATOM    665  CB  ARG A 205       2.505  13.522   9.305  1.00115.67           C  
ATOM    666  CG  ARG A 205       1.057  13.813   9.639  1.00115.67           C  
ATOM    667  CD  ARG A 205       0.243  14.041   8.379  1.00115.67           C  
ATOM    668  NE  ARG A 205      -0.802  13.031   8.216  1.00115.67           N  
ATOM    669  CZ  ARG A 205      -1.662  12.986   7.199  1.00115.67           C  
ATOM    670  NH1 ARG A 205      -1.615  13.898   6.234  1.00115.67           N  
ATOM    671  NH2 ARG A 205      -2.577  12.024   7.151  1.00115.67           N  
ATOM    672  N   VAL A 206       4.343  14.299  11.625  1.00 97.47           N  
ATOM    673  CA  VAL A 206       4.497  15.216  12.753  1.00 97.47           C  
ATOM    674  C   VAL A 206       3.778  16.527  12.457  1.00 97.47           C  
ATOM    675  O   VAL A 206       3.663  16.956  11.305  1.00 97.47           O  
ATOM    676  CB  VAL A 206       5.983  15.558  13.042  1.00 75.61           C  
ATOM    677  CG1 VAL A 206       6.095  16.327  14.344  1.00 75.61           C  
ATOM    678  CG2 VAL A 206       6.815  14.297  13.094  1.00 75.61           C  
ATOM    679  N   TYR A 207       3.298  17.156  13.517  1.00 83.10           N  
ATOM    680  CA  TYR A 207       2.691  18.467  13.418  1.00 83.10           C  
ATOM    681  C   TYR A 207       3.458  19.459  14.281  1.00 83.10           C  
ATOM    682  O   TYR A 207       3.831  19.145  15.414  1.00 83.10           O  
ATOM    683  CB  TYR A 207       1.243  18.383  13.876  1.00111.84           C  
ATOM    684  CG  TYR A 207       0.432  17.446  13.035  1.00111.84           C  
ATOM    685  CD1 TYR A 207       0.181  16.151  13.448  1.00111.84           C  
ATOM    686  CD2 TYR A 207      -0.076  17.855  11.815  1.00111.84           C  
ATOM    687  CE1 TYR A 207      -0.563  15.283  12.662  1.00111.84           C  
ATOM    688  CE2 TYR A 207      -0.817  17.000  11.022  1.00111.84           C  
ATOM    689  CZ  TYR A 207      -1.059  15.716  11.448  1.00111.84           C  
ATOM    690  OH  TYR A 207      -1.803  14.874  10.655  1.00111.84           O  
ATOM    691  N   LEU A 208       3.692  20.655  13.754  1.00104.23           N  
ATOM    692  CA  LEU A 208       4.357  21.684  14.541  1.00104.23           C  
ATOM    693  C   LEU A 208       3.576  22.987  14.579  1.00104.23           C  
ATOM    694  O   LEU A 208       3.720  23.829  13.700  1.00104.23           O  
ATOM    695  CB  LEU A 208       5.765  21.948  14.004  1.00 71.23           C  
ATOM    696  CG  LEU A 208       6.651  20.707  13.822  1.00 71.23           C  
ATOM    697  CD1 LEU A 208       6.116  19.865  12.660  1.00 71.23           C  
ATOM    698  CD2 LEU A 208       8.094  21.125  13.580  1.00 71.23           C  
ATOM    699  N   ILE A 209       2.750  23.138  15.611  1.00 67.32           N  
ATOM    700  CA  ILE A 209       2.068  24.390  15.921  1.00 67.32           C  
ATOM    701  C   ILE A 209       3.018  25.590  15.911  1.00 67.32           C  
ATOM    702  O   ILE A 209       3.587  25.955  16.939  1.00 67.32           O  
ATOM    703  CB  ILE A 209       1.429  24.299  17.306  1.00 71.49           C  
ATOM    704  CG1 ILE A 209       0.529  23.065  17.373  1.00 71.49           C  
ATOM    705  CG2 ILE A 209       0.662  25.573  17.611  1.00 71.49           C  
ATOM    706  CD1 ILE A 209      -0.043  22.797  18.764  1.00 71.49           C  
ATOM    707  N   LEU A 210       3.181  26.215  14.751  1.00 71.96           N  
ATOM    708  CA  LEU A 210       4.092  27.348  14.632  1.00 71.96           C  
ATOM    709  C   LEU A 210       3.372  28.675  14.777  1.00 71.96           C  
ATOM    710  O   LEU A 210       2.145  28.741  14.647  1.00 71.96           O  
ATOM    711  CB  LEU A 210       4.808  27.305  13.286  1.00 71.11           C  
ATOM    712  CG  LEU A 210       5.970  26.316  13.253  1.00 71.11           C  
ATOM    713  CD1 LEU A 210       6.656  26.333  11.890  1.00 71.11           C  
ATOM    714  CD2 LEU A 210       6.950  26.687  14.362  1.00 71.11           C  
ATOM    715  N   GLU A 211       4.131  29.733  15.049  1.00 52.70           N  
ATOM    716  CA  GLU A 211       3.573  31.087  14.998  1.00 52.70           C  
ATOM    717  C   GLU A 211       3.182  31.484  13.569  1.00 52.70           C  
ATOM    718  O   GLU A 211       3.658  30.911  12.581  1.00 52.70           O  
ATOM    719  CB  GLU A 211       4.550  32.116  15.556  1.00 81.72           C  
ATOM    720  CG  GLU A 211       3.923  33.484  15.684  1.00 81.72           C  
ATOM    721  CD  GLU A 211       4.918  34.639  15.559  1.00 81.72           C  
ATOM    722  OE1 GLU A 211       5.803  34.775  16.441  1.00 81.72           O  
ATOM    723  OE2 GLU A 211       4.803  35.419  14.581  1.00 81.72           O  
ATOM    724  N   TYR A 212       2.284  32.453  13.462  1.00 77.35           N  
ATOM    725  CA  TYR A 212       1.823  32.877  12.153  1.00 77.35           C  
ATOM    726  C   TYR A 212       2.408  34.240  11.793  1.00 77.35           C  
ATOM    727  O   TYR A 212       2.460  35.159  12.607  1.00 77.35           O  
ATOM    728  CB  TYR A 212       0.287  32.891  12.109  1.00 87.84           C  
ATOM    729  CG  TYR A 212      -0.288  33.507  10.854  1.00 87.84           C  
ATOM    730  CD1 TYR A 212       0.076  33.050   9.589  1.00 87.84           C  
ATOM    731  CD2 TYR A 212      -1.173  34.574  10.932  1.00 87.84           C  
ATOM    732  CE1 TYR A 212      -0.427  33.651   8.439  1.00 87.84           C  
ATOM    733  CE2 TYR A 212      -1.676  35.174   9.798  1.00 87.84           C  
ATOM    734  CZ  TYR A 212      -1.301  34.717   8.561  1.00 87.84           C  
ATOM    735  OH  TYR A 212      -1.787  35.362   7.450  1.00 87.84           O  
ATOM    736  N   ALA A 213       2.883  34.344  10.562  1.00 54.42           N  
ATOM    737  CA  ALA A 213       3.564  35.536  10.108  1.00 54.42           C  
ATOM    738  C   ALA A 213       2.803  36.033   8.899  1.00 54.42           C  
ATOM    739  O   ALA A 213       2.934  35.489   7.806  1.00 54.42           O  
ATOM    740  CB  ALA A 213       5.005  35.199   9.749  1.00 61.68           C  
ATOM    741  N   PRO A 214       1.965  37.061   9.102  1.00 93.30           N  
ATOM    742  CA  PRO A 214       0.940  37.601   8.203  1.00 93.30           C  
ATOM    743  C   PRO A 214       1.430  38.175   6.893  1.00 93.30           C  
ATOM    744  O   PRO A 214       0.693  38.193   5.917  1.00 93.30           O  
ATOM    745  CB  PRO A 214       0.250  38.662   9.045  1.00 87.86           C  
ATOM    746  CG  PRO A 214       0.453  38.206  10.427  1.00 87.86           C  
ATOM    747  CD  PRO A 214       1.823  37.616  10.455  1.00 87.86           C  
ATOM    748  N   LEU A 215       2.668  38.648   6.866  1.00 63.91           N  
ATOM    749  CA  LEU A 215       3.157  39.369   5.698  1.00 63.91           C  
ATOM    750  C   LEU A 215       4.016  38.498   4.801  1.00 63.91           C  
ATOM    751  O   LEU A 215       4.591  38.973   3.817  1.00 63.91           O  
ATOM    752  CB  LEU A 215       3.953  40.607   6.129  1.00 65.04           C  
ATOM    753  CG  LEU A 215       3.138  41.724   6.777  1.00 65.04           C  
ATOM    754  CD1 LEU A 215       4.047  42.739   7.407  1.00 65.04           C  
ATOM    755  CD2 LEU A 215       2.270  42.348   5.729  1.00 65.04           C  
ATOM    756  N   GLY A 216       4.104  37.218   5.139  1.00 61.83           N  
ATOM    757  CA  GLY A 216       4.850  36.299   4.301  1.00 61.83           C  
ATOM    758  C   GLY A 216       6.350  36.483   4.412  1.00 61.83           C  
ATOM    759  O   GLY A 216       6.853  36.999   5.420  1.00 61.83           O  
ATOM    760  N   THR A 217       7.058  36.070   3.363  1.00 54.35           N  
ATOM    761  CA  THR A 217       8.501  35.831   3.436  1.00 54.35           C  
ATOM    762  C   THR A 217       9.284  37.030   2.935  1.00 54.35           C  
ATOM    763  O   THR A 217       8.813  37.756   2.074  1.00 54.35           O  
ATOM    764  CB  THR A 217       8.922  34.618   2.576  1.00 45.70           C  
ATOM    765  OG1 THR A 217       8.649  34.908   1.203  1.00 45.70           O  
ATOM    766  CG2 THR A 217       8.176  33.373   2.981  1.00 45.70           C  
ATOM    767  N   VAL A 218      10.475  37.238   3.471  1.00 65.31           N  
ATOM    768  CA  VAL A 218      11.352  38.224   2.881  1.00 65.31           C  
ATOM    769  C   VAL A 218      11.551  37.875   1.406  1.00 65.31           C  
ATOM    770  O   VAL A 218      11.899  38.732   0.578  1.00 65.31           O  
ATOM    771  CB  VAL A 218      12.712  38.248   3.578  1.00 61.60           C  
ATOM    772  CG1 VAL A 218      13.734  38.907   2.671  1.00 61.60           C  
ATOM    773  CG2 VAL A 218      12.603  39.002   4.895  1.00 61.60           C  
ATOM    774  N   TYR A 219      11.312  36.610   1.080  1.00 53.53           N  
ATOM    775  CA  TYR A 219      11.519  36.145  -0.271  1.00 53.53           C  
ATOM    776  C   TYR A 219      10.507  36.765  -1.263  1.00 53.53           C  
ATOM    777  O   TYR A 219      10.898  37.400  -2.253  1.00 53.53           O  
ATOM    778  CB  TYR A 219      11.433  34.622  -0.306  1.00 75.73           C  
ATOM    779  CG  TYR A 219      11.715  34.064  -1.669  1.00 75.73           C  
ATOM    780  CD1 TYR A 219      12.950  33.512  -1.969  1.00 75.73           C  
ATOM    781  CD2 TYR A 219      10.771  34.142  -2.676  1.00 75.73           C  
ATOM    782  CE1 TYR A 219      13.237  33.057  -3.236  1.00 75.73           C  
ATOM    783  CE2 TYR A 219      11.048  33.696  -3.941  1.00 75.73           C  
ATOM    784  CZ  TYR A 219      12.284  33.152  -4.221  1.00 75.73           C  
ATOM    785  OH  TYR A 219      12.565  32.709  -5.497  1.00 75.73           O  
ATOM    786  N   ARG A 220       9.212  36.570  -1.013  1.00 62.10           N  
ATOM    787  CA  ARG A 220       8.184  37.138  -1.885  1.00 62.10           C  
ATOM    788  C   ARG A 220       8.313  38.654  -1.891  1.00 62.10           C  
ATOM    789  O   ARG A 220       8.217  39.296  -2.939  1.00 62.10           O  
ATOM    790  CB  ARG A 220       6.776  36.737  -1.411  1.00138.48           C  
ATOM    791  CG  ARG A 220       6.208  35.487  -2.093  1.00138.48           C  
ATOM    792  CD  ARG A 220       5.097  35.810  -3.107  1.00138.48           C  
ATOM    793  NE  ARG A 220       3.771  35.398  -2.633  1.00138.48           N  
ATOM    794  CZ  ARG A 220       2.659  35.423  -3.367  1.00138.48           C  
ATOM    795  NH1 ARG A 220       2.694  35.839  -4.627  1.00138.48           N  
ATOM    796  NH2 ARG A 220       1.504  35.038  -2.836  1.00138.48           N  
ATOM    797  N   GLU A 221       8.537  39.206  -0.699  1.00 74.85           N  
ATOM    798  CA  GLU A 221       8.679  40.641  -0.495  1.00 74.85           C  
ATOM    799  C   GLU A 221       9.706  41.183  -1.473  1.00 74.85           C  
ATOM    800  O   GLU A 221       9.580  42.294  -1.979  1.00 74.85           O  
ATOM    801  CB  GLU A 221       9.121  40.905   0.942  1.00145.21           C  
ATOM    802  CG  GLU A 221       9.572  42.318   1.213  1.00145.21           C  
ATOM    803  CD  GLU A 221       8.494  43.338   0.945  1.00145.21           C  
ATOM    804  OE1 GLU A 221       7.458  42.968   0.353  1.00145.21           O  
ATOM    805  OE2 GLU A 221       8.683  44.513   1.329  1.00145.21           O  
ATOM    806  N   LEU A 222      10.714  40.367  -1.752  1.00 68.30           N  
ATOM    807  CA  LEU A 222      11.849  40.784  -2.554  1.00 68.30           C  
ATOM    808  C   LEU A 222      11.538  40.646  -4.036  1.00 68.30           C  
ATOM    809  O   LEU A 222      11.706  41.594  -4.797  1.00 68.30           O  
ATOM    810  CB  LEU A 222      13.059  39.931  -2.186  1.00 73.46           C  
ATOM    811  CG  LEU A 222      14.438  40.341  -2.686  1.00 73.46           C  
ATOM    812  CD1 LEU A 222      14.868  41.664  -2.046  1.00 73.46           C  
ATOM    813  CD2 LEU A 222      15.416  39.228  -2.342  1.00 73.46           C  
ATOM    814  N   GLN A 223      11.089  39.461  -4.444  1.00 76.14           N  
ATOM    815  CA  GLN A 223      10.571  39.254  -5.797  1.00 76.14           C  
ATOM    816  C   GLN A 223       9.547  40.329  -6.127  1.00 76.14           C  
ATOM    817  O   GLN A 223       9.443  40.797  -7.258  1.00 76.14           O  
ATOM    818  CB  GLN A 223       9.887  37.901  -5.905  1.00 90.61           C  
ATOM    819  CG  GLN A 223      10.809  36.727  -6.093  1.00 90.61           C  
ATOM    820  CD  GLN A 223      10.016  35.480  -6.442  1.00 90.61           C  
ATOM    821  OE1 GLN A 223       8.796  35.453  -6.271  1.00 90.61           O  
ATOM    822  NE2 GLN A 223      10.699  34.444  -6.933  1.00 90.61           N  
ATOM    823  N   LYS A 224       8.778  40.709  -5.118  1.00 98.45           N  
ATOM    824  CA  LYS A 224       7.750  41.713  -5.296  1.00 98.45           C  
ATOM    825  C   LYS A 224       8.417  43.045  -5.665  1.00 98.45           C  
ATOM    826  O   LYS A 224       8.042  43.674  -6.650  1.00 98.45           O  
ATOM    827  CB  LYS A 224       6.928  41.837  -4.002  1.00129.98           C  
ATOM    828  CG  LYS A 224       5.481  42.294  -4.191  1.00129.98           C  
ATOM    829  CD  LYS A 224       4.583  41.849  -3.034  1.00129.98           C  
ATOM    830  CE  LYS A 224       3.158  42.394  -3.182  1.00129.98           C  
ATOM    831  NZ  LYS A 224       2.178  41.769  -2.238  1.00129.98           N  
ATOM    832  N   LEU A 225       9.426  43.450  -4.894  1.00 84.11           N  
ATOM    833  CA  LEU A 225       9.976  44.804  -4.985  1.00 84.11           C  
ATOM    834  C   LEU A 225      11.259  44.899  -5.788  1.00 84.11           C  
ATOM    835  O   LEU A 225      11.719  45.995  -6.064  1.00 84.11           O  
ATOM    836  CB  LEU A 225      10.237  45.362  -3.589  1.00 62.18           C  
ATOM    837  CG  LEU A 225       9.116  45.105  -2.583  1.00 62.18           C  
ATOM    838  CD1 LEU A 225       9.388  45.808  -1.260  1.00 62.18           C  
ATOM    839  CD2 LEU A 225       7.818  45.583  -3.194  1.00 62.18           C  
ATOM    840  N   SER A 226      11.833  43.753  -6.148  1.00 99.20           N  
ATOM    841  CA  SER A 226      13.127  43.684  -6.835  1.00 99.20           C  
ATOM    842  C   SER A 226      14.300  43.959  -5.905  1.00 99.20           C  
ATOM    843  O   SER A 226      15.052  43.045  -5.543  1.00 99.20           O  
ATOM    844  CB  SER A 226      13.184  44.666  -8.005  1.00 70.41           C  
ATOM    845  OG  SER A 226      12.444  44.195  -9.114  1.00 70.41           O  
ATOM    846  N   LYS A 227      14.463  45.222  -5.528  1.00 74.20           N  
ATOM    847  CA  LYS A 227      15.513  45.599  -4.587  1.00 74.20           C  
ATOM    848  C   LYS A 227      14.898  46.234  -3.349  1.00 74.20           C  
ATOM    849  O   LYS A 227      13.804  46.779  -3.404  1.00 74.20           O  
ATOM    850  CB  LYS A 227      16.487  46.581  -5.241  1.00102.06           C  
ATOM    851  CG  LYS A 227      16.875  46.214  -6.654  1.00102.06           C  
ATOM    852  CD  LYS A 227      17.878  47.188  -7.221  1.00102.06           C  
ATOM    853  CE  LYS A 227      17.494  48.625  -6.907  1.00102.06           C  
ATOM    854  NZ  LYS A 227      18.077  49.105  -5.613  1.00102.06           N  
ATOM    855  N   PHE A 228      15.604  46.152  -2.231  1.00 70.10           N  
ATOM    856  CA  PHE A 228      15.236  46.908  -1.051  1.00 70.10           C  
ATOM    857  C   PHE A 228      16.058  48.167  -1.016  1.00 70.10           C  
ATOM    858  O   PHE A 228      17.112  48.244  -1.662  1.00 70.10           O  
ATOM    859  CB  PHE A 228      15.507  46.103   0.204  1.00 47.42           C  
ATOM    860  CG  PHE A 228      14.559  44.988   0.401  1.00 47.42           C  
ATOM    861  CD1 PHE A 228      13.356  44.965  -0.285  1.00 47.42           C  
ATOM    862  CD2 PHE A 228      14.838  43.975   1.297  1.00 47.42           C  
ATOM    863  CE1 PHE A 228      12.439  43.958  -0.077  1.00 47.42           C  
ATOM    864  CE2 PHE A 228      13.916  42.945   1.516  1.00 47.42           C  
ATOM    865  CZ  PHE A 228      12.717  42.941   0.829  1.00 47.42           C  
ATOM    866  N   ASP A 229      15.582  49.156  -0.261  1.00 80.39           N  
ATOM    867  CA  ASP A 229      16.322  50.402  -0.087  1.00 80.39           C  
ATOM    868  C   ASP A 229      17.231  50.290   1.125  1.00 80.39           C  
ATOM    869  O   ASP A 229      17.184  49.303   1.869  1.00 80.39           O  
ATOM    870  CB  ASP A 229      15.368  51.595   0.083  1.00104.94           C  
ATOM    871  CG  ASP A 229      14.606  51.560   1.400  1.00104.94           C  
ATOM    872  OD1 ASP A 229      14.941  50.727   2.265  1.00104.94           O  
ATOM    873  OD2 ASP A 229      13.666  52.366   1.574  1.00104.94           O  
ATOM    874  N   GLU A 230      18.055  51.315   1.303  1.00 80.44           N  
ATOM    875  CA  GLU A 230      18.985  51.405   2.420  1.00 80.44           C  
ATOM    876  C   GLU A 230      18.299  51.236   3.778  1.00 80.44           C  
ATOM    877  O   GLU A 230      18.700  50.396   4.585  1.00 80.44           O  
ATOM    878  CB  GLU A 230      19.686  52.756   2.374  1.00 96.22           C  
ATOM    879  CG  GLU A 230      20.407  53.038   1.080  1.00 96.22           C  
ATOM    880  CD  GLU A 230      21.898  52.880   1.232  1.00 96.22           C  
ATOM    881  OE1 GLU A 230      22.338  51.741   1.472  1.00 96.22           O  
ATOM    882  OE2 GLU A 230      22.630  53.887   1.121  1.00 96.22           O  
ATOM    883  N   GLN A 231      17.270  52.037   4.031  1.00 82.20           N  
ATOM    884  CA  GLN A 231      16.590  51.981   5.311  1.00 82.20           C  
ATOM    885  C   GLN A 231      16.036  50.567   5.556  1.00 82.20           C  
ATOM    886  O   GLN A 231      16.268  49.962   6.615  1.00 82.20           O  
ATOM    887  CB  GLN A 231      15.452  53.008   5.342  1.00173.33           C  
ATOM    888  CG  GLN A 231      14.867  53.267   6.729  1.00173.33           C  
ATOM    889  CD  GLN A 231      13.758  52.295   7.107  1.00173.33           C  
ATOM    890  OE1 GLN A 231      12.940  51.909   6.271  1.00173.33           O  
ATOM    891  NE2 GLN A 231      13.725  51.900   8.375  1.00173.33           N  
ATOM    892  N   ARG A 232      15.308  50.044   4.572  1.00 73.26           N  
ATOM    893  CA  ARG A 232      14.703  48.726   4.688  1.00 73.26           C  
ATOM    894  C   ARG A 232      15.782  47.684   4.909  1.00 73.26           C  
ATOM    895  O   ARG A 232      15.719  46.900   5.861  1.00 73.26           O  
ATOM    896  CB  ARG A 232      13.917  48.383   3.420  1.00116.82           C  
ATOM    897  CG  ARG A 232      13.128  47.095   3.524  1.00116.82           C  
ATOM    898  CD  ARG A 232      12.178  46.938   2.363  1.00116.82           C  
ATOM    899  NE  ARG A 232      10.899  46.385   2.794  1.00116.82           N  
ATOM    900  CZ  ARG A 232       9.920  47.104   3.337  1.00116.82           C  
ATOM    901  NH1 ARG A 232      10.070  48.407   3.520  1.00116.82           N  
ATOM    902  NH2 ARG A 232       8.788  46.518   3.694  1.00116.82           N  
ATOM    903  N   THR A 233      16.774  47.674   4.027  1.00 62.66           N  
ATOM    904  CA  THR A 233      17.828  46.681   4.133  1.00 62.66           C  
ATOM    905  C   THR A 233      18.448  46.872   5.513  1.00 62.66           C  
ATOM    906  O   THR A 233      18.542  45.925   6.306  1.00 62.66           O  
ATOM    907  CB  THR A 233      18.918  46.865   3.018  1.00 67.66           C  
ATOM    908  OG1 THR A 233      18.322  46.732   1.716  1.00 67.66           O  
ATOM    909  CG2 THR A 233      20.030  45.817   3.182  1.00 67.66           C  
ATOM    910  N   ALA A 234      18.824  48.116   5.806  1.00 63.93           N  
ATOM    911  CA  ALA A 234      19.455  48.457   7.077  1.00 63.93           C  
ATOM    912  C   ALA A 234      18.653  47.956   8.273  1.00 63.93           C  
ATOM    913  O   ALA A 234      19.167  47.227   9.119  1.00 63.93           O  
ATOM    914  CB  ALA A 234      19.637  49.940   7.168  1.00 56.37           C  
ATOM    915  N   THR A 235      17.384  48.335   8.332  1.00 73.22           N  
ATOM    916  CA  THR A 235      16.501  47.820   9.367  1.00 73.22           C  
ATOM    917  C   THR A 235      16.515  46.292   9.471  1.00 73.22           C  
ATOM    918  O   THR A 235      16.727  45.758  10.556  1.00 73.22           O  
ATOM    919  CB  THR A 235      15.058  48.271   9.133  1.00 98.09           C  
ATOM    920  OG1 THR A 235      15.015  49.698   9.003  1.00 98.09           O  
ATOM    921  CG2 THR A 235      14.184  47.844  10.299  1.00 98.09           C  
ATOM    922  N   TYR A 236      16.293  45.588   8.362  1.00 76.49           N  
ATOM    923  CA  TYR A 236      16.274  44.120   8.408  1.00 76.49           C  
ATOM    924  C   TYR A 236      17.561  43.545   8.973  1.00 76.49           C  
ATOM    925  O   TYR A 236      17.526  42.659   9.828  1.00 76.49           O  
ATOM    926  CB  TYR A 236      16.052  43.515   7.021  1.00 65.03           C  
ATOM    927  CG  TYR A 236      14.629  43.582   6.528  1.00 65.03           C  
ATOM    928  CD1 TYR A 236      13.590  43.068   7.278  1.00 65.03           C  
ATOM    929  CD2 TYR A 236      14.335  44.148   5.298  1.00 65.03           C  
ATOM    930  CE1 TYR A 236      12.309  43.118   6.813  1.00 65.03           C  
ATOM    931  CE2 TYR A 236      13.058  44.203   4.831  1.00 65.03           C  
ATOM    932  CZ  TYR A 236      12.046  43.690   5.584  1.00 65.03           C  
ATOM    933  OH  TYR A 236      10.755  43.766   5.106  1.00 65.03           O  
ATOM    934  N   ILE A 237      18.698  44.040   8.494  1.00 72.71           N  
ATOM    935  CA  ILE A 237      19.980  43.547   8.988  1.00 72.71           C  
ATOM    936  C   ILE A 237      20.048  43.692  10.514  1.00 72.71           C  
ATOM    937  O   ILE A 237      20.458  42.784  11.244  1.00 72.71           O  
ATOM    938  CB  ILE A 237      21.148  44.322   8.377  1.00 71.86           C  
ATOM    939  CG1 ILE A 237      21.221  44.081   6.859  1.00 71.86           C  
ATOM    940  CG2 ILE A 237      22.424  43.914   9.065  1.00 71.86           C  
ATOM    941  CD1 ILE A 237      21.570  42.665   6.438  1.00 71.86           C  
ATOM    942  N   THR A 238      19.625  44.856  10.984  1.00 78.27           N  
ATOM    943  CA  THR A 238      19.427  45.104  12.402  1.00 78.27           C  
ATOM    944  C   THR A 238      18.595  43.987  13.035  1.00 78.27           C  
ATOM    945  O   THR A 238      19.098  43.220  13.855  1.00 78.27           O  
ATOM    946  CB  THR A 238      18.689  46.424  12.582  1.00 74.82           C  
ATOM    947  OG1 THR A 238      19.150  47.351  11.592  1.00 74.82           O  
ATOM    948  CG2 THR A 238      18.929  46.993  13.976  1.00 74.82           C  
ATOM    949  N   GLU A 239      17.323  43.905  12.629  1.00 73.75           N  
ATOM    950  CA  GLU A 239      16.361  43.002  13.257  1.00 73.75           C  
ATOM    951  C   GLU A 239      16.978  41.616  13.304  1.00 73.75           C  
ATOM    952  O   GLU A 239      16.819  40.866  14.275  1.00 73.75           O  
ATOM    953  CB  GLU A 239      15.057  42.956  12.451  1.00106.53           C  
ATOM    954  CG  GLU A 239      14.818  44.168  11.569  1.00106.53           C  
ATOM    955  CD  GLU A 239      13.347  44.373  11.219  1.00106.53           C  
ATOM    956  OE1 GLU A 239      13.046  44.949  10.144  1.00106.53           O  
ATOM    957  OE2 GLU A 239      12.488  43.962  12.026  1.00106.53           O  
ATOM    958  N   LEU A 240      17.705  41.307  12.237  1.00 58.55           N  
ATOM    959  CA  LEU A 240      18.283  40.000  12.021  1.00 58.55           C  
ATOM    960  C   LEU A 240      19.557  39.886  12.857  1.00 58.55           C  
ATOM    961  O   LEU A 240      19.831  38.849  13.476  1.00 58.55           O  
ATOM    962  CB  LEU A 240      18.568  39.869  10.530  1.00 58.80           C  
ATOM    963  CG  LEU A 240      19.245  38.637   9.940  1.00 58.80           C  
ATOM    964  CD1 LEU A 240      18.698  37.312  10.528  1.00 58.80           C  
ATOM    965  CD2 LEU A 240      19.041  38.740   8.440  1.00 58.80           C  
ATOM    966  N   ALA A 241      20.312  40.979  12.896  1.00 84.88           N  
ATOM    967  CA  ALA A 241      21.479  41.067  13.754  1.00 84.88           C  
ATOM    968  C   ALA A 241      21.068  40.842  15.200  1.00 84.88           C  
ATOM    969  O   ALA A 241      21.581  39.952  15.875  1.00 84.88           O  
ATOM    970  CB  ALA A 241      22.134  42.428  13.610  1.00 75.99           C  
ATOM    971  N   ASN A 242      20.128  41.643  15.677  1.00 76.61           N  
ATOM    972  CA  ASN A 242      19.757  41.545  17.070  1.00 76.61           C  
ATOM    973  C   ASN A 242      19.193  40.160  17.311  1.00 76.61           C  
ATOM    974  O   ASN A 242      19.601  39.456  18.231  1.00 76.61           O  
ATOM    975  CB  ASN A 242      18.733  42.617  17.437  1.00142.23           C  
ATOM    976  CG  ASN A 242      18.859  43.061  18.883  1.00142.23           C  
ATOM    977  OD1 ASN A 242      19.202  44.211  19.166  1.00142.23           O  
ATOM    978  ND2 ASN A 242      18.589  42.145  19.810  1.00142.23           N  
ATOM    979  N   ALA A 243      18.269  39.750  16.464  1.00 92.13           N  
ATOM    980  CA  ALA A 243      17.728  38.416  16.603  1.00 92.13           C  
ATOM    981  C   ALA A 243      18.873  37.401  16.597  1.00 92.13           C  
ATOM    982  O   ALA A 243      18.878  36.447  17.381  1.00 92.13           O  
ATOM    983  CB  ALA A 243      16.760  38.138  15.481  1.00 41.85           C  
ATOM    984  N   LEU A 244      19.855  37.617  15.726  1.00 89.01           N  
ATOM    985  CA  LEU A 244      20.954  36.671  15.597  1.00 89.01           C  
ATOM    986  C   LEU A 244      21.918  36.721  16.779  1.00 89.01           C  
ATOM    987  O   LEU A 244      22.316  35.680  17.315  1.00 89.01           O  
ATOM    988  CB  LEU A 244      21.717  36.920  14.297  1.00100.10           C  
ATOM    989  CG  LEU A 244      21.416  35.859  13.240  1.00100.10           C  
ATOM    990  CD1 LEU A 244      22.498  35.840  12.172  1.00100.10           C  
ATOM    991  CD2 LEU A 244      21.331  34.508  13.930  1.00100.10           C  
ATOM    992  N   SER A 245      22.296  37.934  17.171  1.00 91.86           N  
ATOM    993  CA  SER A 245      23.054  38.132  18.392  1.00 91.86           C  
ATOM    994  C   SER A 245      22.451  37.243  19.462  1.00 91.86           C  
ATOM    995  O   SER A 245      23.085  36.292  19.901  1.00 91.86           O  
ATOM    996  CB  SER A 245      22.979  39.592  18.839  1.00115.92           C  
ATOM    997  OG  SER A 245      23.251  39.710  20.225  1.00115.92           O  
ATOM    998  N   TYR A 246      21.215  37.542  19.855  1.00 80.48           N  
ATOM    999  CA  TYR A 246      20.509  36.753  20.861  1.00 80.48           C  
ATOM   1000  C   TYR A 246      20.760  35.255  20.704  1.00 80.48           C  
ATOM   1001  O   TYR A 246      21.210  34.596  21.628  1.00 80.48           O  
ATOM   1002  CB  TYR A 246      19.002  37.029  20.793  1.00109.46           C  
ATOM   1003  CG  TYR A 246      18.143  36.133  21.680  1.00109.46           C  
ATOM   1004  CD1 TYR A 246      17.485  36.643  22.796  1.00109.46           C  
ATOM   1005  CD2 TYR A 246      17.953  34.784  21.377  1.00109.46           C  
ATOM   1006  CE1 TYR A 246      16.655  35.835  23.582  1.00109.46           C  
ATOM   1007  CE2 TYR A 246      17.129  33.969  22.159  1.00109.46           C  
ATOM   1008  CZ  TYR A 246      16.480  34.500  23.256  1.00109.46           C  
ATOM   1009  OH  TYR A 246      15.643  33.700  24.008  1.00109.46           O  
ATOM   1010  N   CYS A 247      20.462  34.701  19.540  1.00 91.07           N  
ATOM   1011  CA  CYS A 247      20.639  33.268  19.377  1.00 91.07           C  
ATOM   1012  C   CYS A 247      22.042  32.924  19.840  1.00 91.07           C  
ATOM   1013  O   CYS A 247      22.293  31.842  20.362  1.00 91.07           O  
ATOM   1014  CB  CYS A 247      20.468  32.871  17.912  1.00115.70           C  
ATOM   1015  SG  CYS A 247      19.006  33.555  17.150  1.00115.70           S  
ATOM   1016  N   HIS A 248      22.955  33.865  19.645  1.00102.74           N  
ATOM   1017  CA  HIS A 248      24.336  33.660  20.028  1.00102.74           C  
ATOM   1018  C   HIS A 248      24.548  33.939  21.511  1.00102.74           C  
ATOM   1019  O   HIS A 248      25.291  33.218  22.171  1.00102.74           O  
ATOM   1020  CB  HIS A 248      25.247  34.541  19.174  1.00132.18           C  
ATOM   1021  CG  HIS A 248      25.306  34.121  17.739  1.00132.18           C  
ATOM   1022  ND1 HIS A 248      25.792  34.937  16.741  1.00132.18           N  
ATOM   1023  CD2 HIS A 248      24.942  32.964  17.136  1.00132.18           C  
ATOM   1024  CE1 HIS A 248      25.726  34.301  15.585  1.00132.18           C  
ATOM   1025  NE2 HIS A 248      25.214  33.102  15.797  1.00132.18           N  
ATOM   1026  N   SER A 249      23.894  34.974  22.037  1.00 87.83           N  
ATOM   1027  CA  SER A 249      23.854  35.197  23.486  1.00 87.83           C  
ATOM   1028  C   SER A 249      23.522  33.853  24.132  1.00 87.83           C  
ATOM   1029  O   SER A 249      24.188  33.400  25.063  1.00 87.83           O  
ATOM   1030  CB  SER A 249      22.759  36.220  23.848  1.00126.67           C  
ATOM   1031  OG  SER A 249      22.906  37.448  23.147  1.00126.67           O  
ATOM   1032  N   LYS A 250      22.482  33.221  23.600  1.00 96.48           N  
ATOM   1033  CA  LYS A 250      22.007  31.935  24.081  1.00 96.48           C  
ATOM   1034  C   LYS A 250      22.650  30.790  23.312  1.00 96.48           C  
ATOM   1035  O   LYS A 250      22.038  29.736  23.144  1.00 96.48           O  
ATOM   1036  CB  LYS A 250      20.481  31.851  23.945  1.00111.71           C  
ATOM   1037  CG  LYS A 250      19.712  32.876  24.775  1.00111.71           C  
ATOM   1038  CD  LYS A 250      19.650  32.481  26.245  1.00111.71           C  
ATOM   1039  CE  LYS A 250      19.112  31.066  26.414  1.00111.71           C  
ATOM   1040  NZ  LYS A 250      17.750  30.903  25.822  1.00111.71           N  
ATOM   1041  N   ARG A 251      23.868  31.009  22.826  1.00 79.16           N  
ATOM   1042  CA  ARG A 251      24.763  29.902  22.500  1.00 79.16           C  
ATOM   1043  C   ARG A 251      24.556  29.293  21.099  1.00 79.16           C  
ATOM   1044  O   ARG A 251      25.461  28.625  20.560  1.00 79.16           O  
ATOM   1045  CB  ARG A 251      24.609  28.810  23.573  1.00202.90           C  
ATOM   1046  CG  ARG A 251      25.806  27.884  23.767  1.00202.90           C  
ATOM   1047  CD  ARG A 251      25.699  27.120  25.096  1.00202.90           C  
ATOM   1048  NE  ARG A 251      25.319  25.715  24.925  1.00202.90           N  
ATOM   1049  CZ  ARG A 251      24.884  24.928  25.907  1.00202.90           C  
ATOM   1050  NH1 ARG A 251      24.766  25.401  27.140  1.00202.90           N  
ATOM   1051  NH2 ARG A 251      24.569  23.663  25.658  1.00202.90           N  
ATOM   1052  N   VAL A 252      23.374  29.528  20.519  1.00139.89           N  
ATOM   1053  CA  VAL A 252      22.906  28.801  19.331  1.00139.89           C  
ATOM   1054  C   VAL A 252      23.245  29.507  18.017  1.00139.89           C  
ATOM   1055  O   VAL A 252      23.260  30.735  17.950  1.00139.89           O  
ATOM   1056  CB  VAL A 252      21.369  28.578  19.388  1.00 92.84           C  
ATOM   1057  CG1 VAL A 252      20.640  29.902  19.247  1.00 92.84           C  
ATOM   1058  CG2 VAL A 252      20.930  27.614  18.300  1.00 92.84           C  
ATOM   1059  N   ILE A 253      23.521  28.721  16.977  1.00 74.06           N  
ATOM   1060  CA  ILE A 253      23.831  29.267  15.651  1.00 74.06           C  
ATOM   1061  C   ILE A 253      22.880  28.725  14.580  1.00 74.06           C  
ATOM   1062  O   ILE A 253      22.585  27.518  14.543  1.00 74.06           O  
ATOM   1063  CB  ILE A 253      25.264  28.918  15.196  1.00 98.57           C  
ATOM   1064  CG1 ILE A 253      25.415  27.396  15.100  1.00 98.57           C  
ATOM   1065  CG2 ILE A 253      26.273  29.516  16.149  1.00 98.57           C  
ATOM   1066  CD1 ILE A 253      26.369  26.927  14.023  1.00 98.57           C  
ATOM   1067  N   HIS A 254      22.430  29.611  13.690  1.00 59.65           N  
ATOM   1068  CA  HIS A 254      21.359  29.260  12.770  1.00 59.65           C  
ATOM   1069  C   HIS A 254      21.854  28.640  11.479  1.00 59.65           C  
ATOM   1070  O   HIS A 254      21.299  27.641  11.011  1.00 59.65           O  
ATOM   1071  CB  HIS A 254      20.503  30.485  12.442  1.00 86.59           C  
ATOM   1072  CG  HIS A 254      19.304  30.166  11.600  1.00 86.59           C  
ATOM   1073  ND1 HIS A 254      19.404  29.622  10.338  1.00 86.59           N  
ATOM   1074  CD2 HIS A 254      17.980  30.275  11.858  1.00 86.59           C  
ATOM   1075  CE1 HIS A 254      18.194  29.406   9.856  1.00 86.59           C  
ATOM   1076  NE2 HIS A 254      17.312  29.793  10.759  1.00 86.59           N  
ATOM   1077  N   ARG A 255      22.882  29.251  10.900  1.00118.14           N  
ATOM   1078  CA  ARG A 255      23.414  28.823   9.614  1.00118.14           C  
ATOM   1079  C   ARG A 255      22.505  29.173   8.449  1.00118.14           C  
ATOM   1080  O   ARG A 255      22.738  30.153   7.742  1.00118.14           O  
ATOM   1081  CB  ARG A 255      23.653  27.324   9.624  1.00106.55           C  
ATOM   1082  CG  ARG A 255      24.532  26.897  10.754  1.00106.55           C  
ATOM   1083  CD  ARG A 255      24.963  25.486  10.557  1.00106.55           C  
ATOM   1084  NE  ARG A 255      24.395  24.608  11.565  1.00106.55           N  
ATOM   1085  CZ  ARG A 255      24.819  23.371  11.777  1.00106.55           C  
ATOM   1086  NH1 ARG A 255      25.811  22.886  11.042  1.00106.55           N  
ATOM   1087  NH2 ARG A 255      24.256  22.620  12.717  1.00106.55           N  
ATOM   1088  N   ASP A 256      21.466  28.366   8.264  1.00 70.04           N  
ATOM   1089  CA  ASP A 256      20.627  28.434   7.078  1.00 70.04           C  
ATOM   1090  C   ASP A 256      19.816  29.732   6.912  1.00 70.04           C  
ATOM   1091  O   ASP A 256      18.707  29.723   6.365  1.00 70.04           O  
ATOM   1092  CB  ASP A 256      19.685  27.234   7.060  1.00 85.97           C  
ATOM   1093  CG  ASP A 256      19.149  26.936   5.674  1.00 85.97           C  
ATOM   1094  OD1 ASP A 256      19.951  26.588   4.778  1.00 85.97           O  
ATOM   1095  OD2 ASP A 256      17.923  27.049   5.478  1.00 85.97           O  
ATOM   1096  N   ILE A 257      20.371  30.849   7.370  1.00 60.06           N  
ATOM   1097  CA  ILE A 257      19.788  32.153   7.087  1.00 60.06           C  
ATOM   1098  C   ILE A 257      19.741  32.540   5.612  1.00 60.06           C  
ATOM   1099  O   ILE A 257      20.735  32.982   5.056  1.00 60.06           O  
ATOM   1100  CB  ILE A 257      20.544  33.248   7.841  1.00 67.74           C  
ATOM   1101  CG1 ILE A 257      20.191  33.147   9.314  1.00 67.74           C  
ATOM   1102  CG2 ILE A 257      20.193  34.628   7.291  1.00 67.74           C  
ATOM   1103  CD1 ILE A 257      18.715  33.400   9.570  1.00 67.74           C  
ATOM   1104  N   LYS A 258      18.576  32.386   4.994  1.00 57.26           N  
ATOM   1105  CA  LYS A 258      18.315  32.918   3.658  1.00 57.26           C  
ATOM   1106  C   LYS A 258      16.946  33.573   3.606  1.00 57.26           C  
ATOM   1107  O   LYS A 258      16.157  33.450   4.536  1.00 57.26           O  
ATOM   1108  CB  LYS A 258      18.385  31.808   2.613  1.00 67.72           C  
ATOM   1109  CG  LYS A 258      18.100  30.434   3.160  1.00 67.72           C  
ATOM   1110  CD  LYS A 258      17.463  29.538   2.111  1.00 67.72           C  
ATOM   1111  CE  LYS A 258      17.696  28.078   2.446  1.00 67.72           C  
ATOM   1112  NZ  LYS A 258      19.144  27.804   2.716  1.00 67.72           N  
ATOM   1113  N   PRO A 259      16.646  34.282   2.508  1.00 79.65           N  
ATOM   1114  CA  PRO A 259      15.397  35.040   2.455  1.00 79.65           C  
ATOM   1115  C   PRO A 259      14.179  34.146   2.572  1.00 79.65           C  
ATOM   1116  O   PRO A 259      13.159  34.564   3.108  1.00 79.65           O  
ATOM   1117  CB  PRO A 259      15.467  35.757   1.106  1.00 61.69           C  
ATOM   1118  CG  PRO A 259      16.906  35.826   0.789  1.00 61.69           C  
ATOM   1119  CD  PRO A 259      17.482  34.549   1.327  1.00 61.69           C  
ATOM   1120  N   GLU A 260      14.289  32.914   2.083  1.00 61.28           N  
ATOM   1121  CA  GLU A 260      13.188  31.955   2.189  1.00 61.28           C  
ATOM   1122  C   GLU A 260      12.790  31.637   3.639  1.00 61.28           C  
ATOM   1123  O   GLU A 260      11.651  31.249   3.900  1.00 61.28           O  
ATOM   1124  CB  GLU A 260      13.561  30.669   1.476  1.00131.28           C  
ATOM   1125  CG  GLU A 260      13.728  30.854  -0.001  1.00131.28           C  
ATOM   1126  CD  GLU A 260      14.176  29.588  -0.681  1.00131.28           C  
ATOM   1127  OE1 GLU A 260      15.193  29.019  -0.232  1.00131.28           O  
ATOM   1128  OE2 GLU A 260      13.516  29.161  -1.656  1.00131.28           O  
ATOM   1129  N   ASN A 261      13.731  31.815   4.572  1.00 61.98           N  
ATOM   1130  CA  ASN A 261      13.525  31.494   5.983  1.00 61.98           C  
ATOM   1131  C   ASN A 261      13.191  32.686   6.855  1.00 61.98           C  
ATOM   1132  O   ASN A 261      12.977  32.541   8.055  1.00 61.98           O  
ATOM   1133  CB  ASN A 261      14.759  30.819   6.551  1.00110.89           C  
ATOM   1134  CG  ASN A 261      15.041  29.518   5.888  1.00110.89           C  
ATOM   1135  OD1 ASN A 261      14.185  28.635   5.846  1.00110.89           O  
ATOM   1136  ND2 ASN A 261      16.244  29.381   5.350  1.00110.89           N  
ATOM   1137  N   LEU A 262      13.158  33.871   6.272  1.00 69.25           N  
ATOM   1138  CA  LEU A 262      12.668  35.012   7.028  1.00 69.25           C  
ATOM   1139  C   LEU A 262      11.176  35.292   6.767  1.00 69.25           C  
ATOM   1140  O   LEU A 262      10.664  35.152   5.653  1.00 69.25           O  
ATOM   1141  CB  LEU A 262      13.530  36.248   6.736  1.00 56.69           C  
ATOM   1142  CG  LEU A 262      15.015  35.927   6.947  1.00 56.69           C  
ATOM   1143  CD1 LEU A 262      15.880  37.106   6.496  1.00 56.69           C  
ATOM   1144  CD2 LEU A 262      15.265  35.542   8.418  1.00 56.69           C  
ATOM   1145  N   LEU A 263      10.481  35.659   7.831  1.00 78.73           N  
ATOM   1146  CA  LEU A 263       9.081  36.017   7.736  1.00 78.73           C  
ATOM   1147  C   LEU A 263       8.796  37.383   8.362  1.00 78.73           C  
ATOM   1148  O   LEU A 263       9.597  37.899   9.146  1.00 78.73           O  
ATOM   1149  CB  LEU A 263       8.245  34.939   8.405  1.00 84.11           C  
ATOM   1150  CG  LEU A 263       8.288  33.657   7.598  1.00 84.11           C  
ATOM   1151  CD1 LEU A 263       7.528  32.591   8.323  1.00 84.11           C  
ATOM   1152  CD2 LEU A 263       7.691  33.907   6.236  1.00 84.11           C  
ATOM   1153  N   LEU A 264       7.652  37.963   8.006  1.00 83.50           N  
ATOM   1154  CA  LEU A 264       7.303  39.296   8.471  1.00 83.50           C  
ATOM   1155  C   LEU A 264       6.034  39.335   9.330  1.00 83.50           C  
ATOM   1156  O   LEU A 264       4.978  38.825   8.931  1.00 83.50           O  
ATOM   1157  CB  LEU A 264       7.185  40.218   7.261  1.00 63.47           C  
ATOM   1158  CG  LEU A 264       8.570  40.246   6.611  1.00 63.47           C  
ATOM   1159  CD1 LEU A 264       8.460  40.476   5.118  1.00 63.47           C  
ATOM   1160  CD2 LEU A 264       9.426  41.308   7.302  1.00 63.47           C  
ATOM   1161  N   GLY A 265       6.168  39.922  10.524  1.00 66.98           N  
ATOM   1162  CA  GLY A 265       5.023  40.153  11.387  1.00 66.98           C  
ATOM   1163  C   GLY A 265       4.101  41.236  10.850  1.00 66.98           C  
ATOM   1164  O   GLY A 265       4.441  41.923   9.884  1.00 66.98           O  
ATOM   1165  N   SER A 266       2.925  41.370  11.467  1.00 61.86           N  
ATOM   1166  CA  SER A 266       1.969  42.459  11.214  1.00 61.86           C  
ATOM   1167  C   SER A 266       2.657  43.832  11.330  1.00 61.86           C  
ATOM   1168  O   SER A 266       2.379  44.767  10.568  1.00 61.86           O  
ATOM   1169  CB  SER A 266       0.868  42.374  12.251  1.00 61.50           C  
ATOM   1170  OG  SER A 266       1.441  42.492  13.551  1.00 61.50           O  
ATOM   1171  N   ALA A 267       3.559  43.932  12.305  1.00 70.59           N  
ATOM   1172  CA  ALA A 267       4.384  45.114  12.464  1.00 70.59           C  
ATOM   1173  C   ALA A 267       5.234  45.300  11.219  1.00 70.59           C  
ATOM   1174  O   ALA A 267       5.635  46.417  10.894  1.00 70.59           O  
ATOM   1175  CB  ALA A 267       5.269  44.971  13.699  1.00192.79           C  
ATOM   1176  N   GLY A 268       5.512  44.196  10.527  1.00 76.77           N  
ATOM   1177  CA  GLY A 268       6.279  44.256   9.290  1.00 76.77           C  
ATOM   1178  C   GLY A 268       7.754  43.941   9.476  1.00 76.77           C  
ATOM   1179  O   GLY A 268       8.587  44.200   8.598  1.00 76.77           O  
ATOM   1180  N   GLU A 269       8.057  43.364  10.636  1.00 71.78           N  
ATOM   1181  CA  GLU A 269       9.417  43.157  11.096  1.00 71.78           C  
ATOM   1182  C   GLU A 269       9.853  41.734  10.827  1.00 71.78           C  
ATOM   1183  O   GLU A 269       9.063  40.797  10.935  1.00 71.78           O  
ATOM   1184  CB  GLU A 269       9.496  43.388  12.596  1.00 88.35           C  
ATOM   1185  CG  GLU A 269       9.060  42.173  13.403  1.00 88.35           C  
ATOM   1186  CD  GLU A 269       7.576  42.159  13.685  1.00 88.35           C  
ATOM   1187  OE1 GLU A 269       6.796  42.670  12.850  1.00 88.35           O  
ATOM   1188  OE2 GLU A 269       7.191  41.635  14.753  1.00 88.35           O  
ATOM   1189  N   LEU A 270      11.134  41.589  10.511  1.00 62.33           N  
ATOM   1190  CA  LEU A 270      11.767  40.300  10.270  1.00 62.33           C  
ATOM   1191  C   LEU A 270      11.516  39.301  11.412  1.00 62.33           C  
ATOM   1192  O   LEU A 270      11.443  39.679  12.572  1.00 62.33           O  
ATOM   1193  CB  LEU A 270      13.268  40.542  10.053  1.00 79.38           C  
ATOM   1194  CG  LEU A 270      14.239  39.379   9.854  1.00 79.38           C  
ATOM   1195  CD1 LEU A 270      15.423  39.880   9.060  1.00 79.38           C  
ATOM   1196  CD2 LEU A 270      14.688  38.792  11.203  1.00 79.38           C  
ATOM   1197  N   LYS A 271      11.350  38.031  11.057  1.00 56.52           N  
ATOM   1198  CA  LYS A 271      11.296  36.940  12.021  1.00 56.52           C  
ATOM   1199  C   LYS A 271      11.974  35.702  11.443  1.00 56.52           C  
ATOM   1200  O   LYS A 271      11.760  35.362  10.282  1.00 56.52           O  
ATOM   1201  CB  LYS A 271       9.851  36.588  12.354  1.00 94.65           C  
ATOM   1202  CG  LYS A 271       9.027  37.755  12.801  1.00 94.65           C  
ATOM   1203  CD  LYS A 271       7.712  37.289  13.369  1.00 94.65           C  
ATOM   1204  CE  LYS A 271       7.823  37.010  14.858  1.00 94.65           C  
ATOM   1205  NZ  LYS A 271       7.820  38.261  15.660  1.00 94.65           N  
ATOM   1206  N   ILE A 272      12.772  35.012  12.248  1.00 85.87           N  
ATOM   1207  CA  ILE A 272      13.565  33.892  11.752  1.00 85.87           C  
ATOM   1208  C   ILE A 272      12.864  32.546  11.921  1.00 85.87           C  
ATOM   1209  O   ILE A 272      12.436  32.187  13.019  1.00 85.87           O  
ATOM   1210  CB  ILE A 272      14.898  33.831  12.475  1.00 95.77           C  
ATOM   1211  CG1 ILE A 272      15.606  35.170  12.310  1.00 95.77           C  
ATOM   1212  CG2 ILE A 272      15.732  32.700  11.942  1.00 95.77           C  
ATOM   1213  CD1 ILE A 272      16.854  35.287  13.138  1.00 95.77           C  
ATOM   1214  N   ALA A 273      12.762  31.795  10.832  1.00 84.54           N  
ATOM   1215  CA  ALA A 273      12.035  30.533  10.847  1.00 84.54           C  
ATOM   1216  C   ALA A 273      12.881  29.362  10.360  1.00 84.54           C  
ATOM   1217  O   ALA A 273      13.825  29.544   9.597  1.00 84.54           O  
ATOM   1218  CB  ALA A 273      10.792  30.653   9.991  1.00117.62           C  
ATOM   1219  N   ASP A 274      12.520  28.157  10.796  1.00 88.50           N  
ATOM   1220  CA  ASP A 274      13.270  26.957  10.461  1.00 88.50           C  
ATOM   1221  C   ASP A 274      14.595  27.008  11.174  1.00 88.50           C  
ATOM   1222  O   ASP A 274      15.299  28.005  11.111  1.00 88.50           O  
ATOM   1223  CB  ASP A 274      13.504  26.875   8.948  1.00134.19           C  
ATOM   1224  CG  ASP A 274      12.452  26.052   8.236  1.00134.19           C  
ATOM   1225  OD1 ASP A 274      11.781  25.240   8.903  1.00134.19           O  
ATOM   1226  OD2 ASP A 274      12.296  26.209   7.006  1.00134.19           O  
ATOM   1227  N   PHE A 275      14.934  25.938  11.868  1.00118.41           N  
ATOM   1228  CA  PHE A 275      16.256  25.848  12.440  1.00118.17           C  
ATOM   1229  C   PHE A 275      16.937  24.578  12.011  1.00117.62           C  
ATOM   1230  O   PHE A 275      18.022  24.643  11.440  1.00117.16           O  
ATOM   1231  CB  PHE A 275      16.194  25.962  13.965  1.00 90.92           C  
ATOM   1232  CG  PHE A 275      16.153  27.388  14.438  1.00 90.85           C  
ATOM   1233  CD1 PHE A 275      14.997  28.147  14.294  1.00 91.38           C  
ATOM   1234  CD2 PHE A 275      17.295  28.002  14.929  1.00 91.35           C  
ATOM   1235  CE1 PHE A 275      14.987  29.496  14.624  1.00 92.70           C  
ATOM   1236  CE2 PHE A 275      17.292  29.352  15.261  1.00 91.59           C  
ATOM   1237  CZ  PHE A 275      16.139  30.102  15.108  1.00 91.61           C  
ATOM   1238  N   GLY A 276      16.284  23.444  12.268  1.00173.51           N  
ATOM   1239  CA  GLY A 276      16.784  22.144  11.855  1.00173.79           C  
ATOM   1240  C   GLY A 276      17.992  22.235  10.955  1.00173.70           C  
ATOM   1241  O   GLY A 276      17.914  21.920   9.772  1.00175.01           O  
ATOM   1242  N   TRP A 277      19.106  22.661  11.544  1.00 83.33           N  
ATOM   1243  CA  TRP A 277      20.293  23.120  10.832  1.00 83.49           C  
ATOM   1244  C   TRP A 277      20.965  24.162  11.704  1.00 82.93           C  
ATOM   1245  O   TRP A 277      21.739  24.993  11.218  1.00 83.44           O  
ATOM   1246  CB  TRP A 277      19.937  23.763   9.491  1.00160.32           C  
ATOM   1247  CG  TRP A 277      20.124  22.878   8.287  1.00160.92           C  
ATOM   1248  CD1 TRP A 277      19.861  23.210   6.993  1.00162.29           C  
ATOM   1249  CD2 TRP A 277      20.565  21.508   8.267  1.00160.95           C  
ATOM   1250  NE1 TRP A 277      20.101  22.139   6.167  1.00163.51           N  
ATOM   1251  CE2 TRP A 277      20.534  21.080   6.923  1.00162.65           C  
ATOM   1252  CE3 TRP A 277      20.979  20.600   9.253  1.00161.44           C  
ATOM   1253  CZ2 TRP A 277      20.900  19.788   6.538  1.00163.18           C  
ATOM   1254  CZ3 TRP A 277      21.341  19.317   8.868  1.00162.62           C  
ATOM   1255  CH2 TRP A 277      21.299  18.924   7.523  1.00163.07           C  
ATOM   1256  N   SER A 278      20.649  24.111  12.993  1.00126.77           N  
ATOM   1257  CA  SER A 278      21.141  25.082  13.957  1.00126.90           C  
ATOM   1258  C   SER A 278      21.591  24.371  15.230  1.00127.11           C  
ATOM   1259  O   SER A 278      20.996  23.369  15.628  1.00127.08           O  
ATOM   1260  CB  SER A 278      20.031  26.074  14.276  0.50 72.77           C  
ATOM   1261  OG  SER A 278      19.431  26.530  13.076  0.50 75.14           O  
ATOM   1262  N   VAL A 279      22.644  24.886  15.861  1.00141.65           N  
ATOM   1263  CA  VAL A 279      23.169  24.297  17.093  1.00141.55           C  
ATOM   1264  C   VAL A 279      24.042  25.261  17.896  1.00141.37           C  
ATOM   1265  O   VAL A 279      23.547  26.212  18.502  1.00141.96           O  
ATOM   1266  CB  VAL A 279      23.995  23.014  16.802  1.00 82.62           C  
ATOM   1267  CG1 VAL A 279      24.973  23.258  15.626  1.00 83.29           C  
ATOM   1268  CG2 VAL A 279      24.749  22.593  18.076  1.00 83.48           C  
ATOM   1269  N   CYS A 290      23.126  19.571   0.967  1.00158.29           N  
ATOM   1270  CA  CYS A 290      22.342  19.767  -0.248  1.00158.15           C  
ATOM   1271  C   CYS A 290      21.555  21.073  -0.218  1.00158.24           C  
ATOM   1272  O   CYS A 290      21.532  21.772   0.794  1.00158.87           O  
ATOM   1273  CB  CYS A 290      21.385  18.593  -0.453  1.00167.26           C  
ATOM   1274  SG  CYS A 290      22.223  17.033  -0.782  1.00168.61           S  
ATOM   1275  N   GLY A 291      20.911  21.395  -1.335  1.00131.39           N  
ATOM   1276  CA  GLY A 291      20.229  22.669  -1.454  1.00132.26           C  
ATOM   1277  C   GLY A 291      21.100  23.686  -2.162  1.00132.55           C  
ATOM   1278  O   GLY A 291      21.952  23.325  -2.973  1.00133.80           O  
ATOM   1279  N   THR A 292      20.893  24.962  -1.860  1.00 98.78           N  
ATOM   1280  CA  THR A 292      21.670  26.012  -2.492  1.00 98.78           C  
ATOM   1281  C   THR A 292      22.763  26.578  -1.604  1.00 98.78           C  
ATOM   1282  O   THR A 292      22.533  26.903  -0.433  1.00 98.78           O  
ATOM   1283  CB  THR A 292      20.756  27.144  -2.990  1.00 79.53           C  
ATOM   1284  OG1 THR A 292      20.407  26.889  -4.362  1.00 79.53           O  
ATOM   1285  CG2 THR A 292      21.435  28.490  -2.867  1.00 79.53           C  
ATOM   1286  N   LEU A 293      23.955  26.681  -2.192  1.00 65.50           N  
ATOM   1287  CA  LEU A 293      25.171  27.129  -1.513  1.00 65.50           C  
ATOM   1288  C   LEU A 293      25.159  28.615  -1.239  1.00 65.50           C  
ATOM   1289  O   LEU A 293      25.862  29.108  -0.348  1.00 65.50           O  
ATOM   1290  CB  LEU A 293      26.374  26.832  -2.380  1.00 87.77           C  
ATOM   1291  CG  LEU A 293      26.506  25.348  -2.611  1.00 87.77           C  
ATOM   1292  CD1 LEU A 293      27.537  25.056  -3.678  1.00 87.77           C  
ATOM   1293  CD2 LEU A 293      26.873  24.734  -1.282  1.00 87.77           C  
ATOM   1294  N   ASP A 294      24.362  29.320  -2.029  1.00 57.29           N  
ATOM   1295  CA  ASP A 294      24.343  30.768  -2.036  1.00 57.29           C  
ATOM   1296  C   ASP A 294      24.664  31.496  -0.738  1.00 57.29           C  
ATOM   1297  O   ASP A 294      25.314  32.534  -0.784  1.00 57.29           O  
ATOM   1298  CB  ASP A 294      23.008  31.254  -2.588  1.00 76.61           C  
ATOM   1299  CG  ASP A 294      23.077  31.531  -4.064  1.00 76.61           C  
ATOM   1300  OD1 ASP A 294      24.115  32.100  -4.487  1.00 76.61           O  
ATOM   1301  OD2 ASP A 294      22.115  31.187  -4.789  1.00 76.61           O  
ATOM   1302  N   TYR A 295      24.236  30.967   0.406  1.00 58.20           N  
ATOM   1303  CA  TYR A 295      24.375  31.713   1.651  1.00 58.20           C  
ATOM   1304  C   TYR A 295      25.358  31.099   2.619  1.00 58.20           C  
ATOM   1305  O   TYR A 295      25.563  31.641   3.715  1.00 58.20           O  
ATOM   1306  CB  TYR A 295      23.027  31.851   2.358  1.00 79.49           C  
ATOM   1307  CG  TYR A 295      21.964  32.412   1.471  1.00 79.49           C  
ATOM   1308  CD1 TYR A 295      21.256  31.586   0.611  1.00 79.49           C  
ATOM   1309  CD2 TYR A 295      21.719  33.773   1.431  1.00 79.49           C  
ATOM   1310  CE1 TYR A 295      20.338  32.098  -0.276  1.00 79.49           C  
ATOM   1311  CE2 TYR A 295      20.798  34.303   0.543  1.00 79.49           C  
ATOM   1312  CZ  TYR A 295      20.113  33.456  -0.314  1.00 79.49           C  
ATOM   1313  OH  TYR A 295      19.232  33.969  -1.238  1.00 79.49           O  
ATOM   1314  N   LEU A 296      25.964  29.978   2.238  1.00 78.34           N  
ATOM   1315  CA  LEU A 296      26.812  29.240   3.175  1.00 78.34           C  
ATOM   1316  C   LEU A 296      28.278  29.598   2.965  1.00 78.34           C  
ATOM   1317  O   LEU A 296      28.757  29.582   1.841  1.00 78.34           O  
ATOM   1318  CB  LEU A 296      26.596  27.736   2.999  1.00 95.86           C  
ATOM   1319  CG  LEU A 296      25.433  27.348   2.073  1.00 95.86           C  
ATOM   1320  CD1 LEU A 296      25.357  25.838   2.011  1.00 95.86           C  
ATOM   1321  CD2 LEU A 296      24.096  27.935   2.549  1.00 95.86           C  
ATOM   1322  N   PRO A 297      29.000  29.943   4.049  1.00 94.57           N  
ATOM   1323  CA  PRO A 297      30.381  30.440   4.019  1.00 94.57           C  
ATOM   1324  C   PRO A 297      31.389  29.373   3.602  1.00 94.57           C  
ATOM   1325  O   PRO A 297      31.060  28.190   3.544  1.00 94.57           O  
ATOM   1326  CB  PRO A 297      30.618  30.916   5.449  1.00 94.10           C  
ATOM   1327  CG  PRO A 297      29.744  30.059   6.259  1.00 94.10           C  
ATOM   1328  CD  PRO A 297      28.504  29.844   5.429  1.00 94.10           C  
ATOM   1329  N   PRO A 298      32.640  29.778   3.324  1.00101.55           N  
ATOM   1330  CA  PRO A 298      33.670  28.861   2.821  1.00101.55           C  
ATOM   1331  C   PRO A 298      33.848  27.656   3.728  1.00101.55           C  
ATOM   1332  O   PRO A 298      33.734  26.511   3.281  1.00101.55           O  
ATOM   1333  CB  PRO A 298      34.932  29.719   2.779  1.00121.31           C  
ATOM   1334  CG  PRO A 298      34.432  31.115   2.702  1.00121.31           C  
ATOM   1335  CD  PRO A 298      33.173  31.137   3.515  1.00121.31           C  
ATOM   1336  N   GLU A 299      34.122  27.924   5.005  1.00107.94           N  
ATOM   1337  CA  GLU A 299      34.394  26.867   5.972  1.00107.94           C  
ATOM   1338  C   GLU A 299      33.440  25.709   5.777  1.00107.94           C  
ATOM   1339  O   GLU A 299      33.797  24.697   5.179  1.00107.94           O  
ATOM   1340  CB  GLU A 299      34.267  27.389   7.404  1.00 88.89           C  
ATOM   1341  CG  GLU A 299      33.077  28.277   7.654  1.00 88.89           C  
ATOM   1342  CD  GLU A 299      33.438  29.750   7.593  1.00 88.89           C  
ATOM   1343  OE1 GLU A 299      34.111  30.156   6.627  1.00 88.89           O  
ATOM   1344  OE2 GLU A 299      33.049  30.501   8.512  1.00 88.89           O  
ATOM   1345  N   MET A 300      32.225  25.873   6.280  1.00109.24           N  
ATOM   1346  CA  MET A 300      31.160  24.906   6.066  1.00109.24           C  
ATOM   1347  C   MET A 300      31.323  24.176   4.745  1.00109.24           C  
ATOM   1348  O   MET A 300      31.694  23.008   4.706  1.00109.24           O  
ATOM   1349  CB  MET A 300      29.828  25.623   6.054  1.00 87.59           C  
ATOM   1350  CG  MET A 300      28.672  24.766   6.433  1.00 87.59           C  
ATOM   1351  SD  MET A 300      27.702  25.749   7.542  1.00 87.59           S  
ATOM   1352  CE  MET A 300      27.042  26.947   6.411  1.00 87.59           C  
ATOM   1353  N   ILE A 301      31.041  24.881   3.661  1.00 80.61           N  
ATOM   1354  CA  ILE A 301      31.101  24.303   2.331  1.00 80.61           C  
ATOM   1355  C   ILE A 301      32.379  23.512   2.075  1.00 80.61           C  
ATOM   1356  O   ILE A 301      32.341  22.431   1.488  1.00 80.61           O  
ATOM   1357  CB  ILE A 301      30.986  25.401   1.255  1.00109.89           C  
ATOM   1358  CG1 ILE A 301      29.619  26.080   1.354  1.00109.89           C  
ATOM   1359  CG2 ILE A 301      31.200  24.807  -0.122  1.00109.89           C  
ATOM   1360  CD1 ILE A 301      29.390  27.146   0.316  1.00109.89           C  
ATOM   1361  N   GLU A 302      33.511  24.060   2.505  1.00185.15           N  
ATOM   1362  CA  GLU A 302      34.793  23.388   2.336  1.00185.15           C  
ATOM   1363  C   GLU A 302      34.967  22.285   3.379  1.00185.15           C  
ATOM   1364  O   GLU A 302      36.049  21.721   3.534  1.00185.15           O  
ATOM   1365  CB  GLU A 302      35.937  24.403   2.440  1.00116.01           C  
ATOM   1366  CG  GLU A 302      36.066  25.311   1.222  1.00116.01           C  
ATOM   1367  CD  GLU A 302      37.221  26.291   1.338  1.00116.01           C  
ATOM   1368  OE1 GLU A 302      37.984  26.204   2.323  1.00116.01           O  
ATOM   1369  OE2 GLU A 302      37.366  27.153   0.443  1.00116.01           O  
ATOM   1370  N   GLY A 303      33.885  21.988   4.091  1.00117.72           N  
ATOM   1371  CA  GLY A 303      33.900  20.920   5.072  1.00117.72           C  
ATOM   1372  C   GLY A 303      34.328  21.341   6.469  1.00117.72           C  
ATOM   1373  O   GLY A 303      33.739  20.905   7.462  1.00117.72           O  
ATOM   1374  N   ARG A 304      35.350  22.187   6.553  1.00148.84           N  
ATOM   1375  CA  ARG A 304      35.987  22.483   7.832  1.00148.84           C  
ATOM   1376  C   ARG A 304      34.988  22.779   8.952  1.00148.84           C  
ATOM   1377  O   ARG A 304      33.886  23.265   8.707  1.00148.84           O  
ATOM   1378  CB  ARG A 304      36.955  23.659   7.678  1.00166.56           C  
ATOM   1379  CG  ARG A 304      38.144  23.378   6.774  1.00166.56           C  
ATOM   1380  CD  ARG A 304      39.202  24.450   6.943  1.00166.56           C  
ATOM   1381  NE  ARG A 304      38.599  25.774   7.071  1.00166.56           N  
ATOM   1382  CZ  ARG A 304      38.506  26.657   6.081  1.00166.56           C  
ATOM   1383  NH1 ARG A 304      38.983  26.360   4.879  1.00166.56           N  
ATOM   1384  NH2 ARG A 304      37.930  27.836   6.288  1.00166.56           N  
ATOM   1385  N   MET A 305      35.386  22.468  10.182  1.00116.01           N  
ATOM   1386  CA  MET A 305      34.577  22.748  11.365  1.00116.01           C  
ATOM   1387  C   MET A 305      34.269  24.228  11.451  1.00116.01           C  
ATOM   1388  O   MET A 305      35.147  25.066  11.246  1.00116.01           O  
ATOM   1389  CB  MET A 305      35.322  22.309  12.632  1.00113.79           C  
ATOM   1390  CG  MET A 305      34.852  22.980  13.916  1.00113.79           C  
ATOM   1391  SD  MET A 305      35.836  22.486  15.353  1.00113.79           S  
ATOM   1392  CE  MET A 305      37.503  23.096  14.877  1.00113.79           C  
ATOM   1393  N   HIS A 306      33.016  24.543  11.762  1.00184.98           N  
ATOM   1394  CA  HIS A 306      32.554  25.922  11.773  1.00184.98           C  
ATOM   1395  C   HIS A 306      31.925  26.325  13.102  1.00184.98           C  
ATOM   1396  O   HIS A 306      31.742  25.500  13.999  1.00184.98           O  
ATOM   1397  CB  HIS A 306      31.558  26.152  10.632  1.00111.72           C  
ATOM   1398  CG  HIS A 306      30.544  25.058  10.483  1.00111.72           C  
ATOM   1399  ND1 HIS A 306      30.616  24.106   9.487  1.00111.72           N  
ATOM   1400  CD2 HIS A 306      29.438  24.761  11.207  1.00111.72           C  
ATOM   1401  CE1 HIS A 306      29.600  23.270   9.605  1.00111.72           C  
ATOM   1402  NE2 HIS A 306      28.870  23.645  10.641  1.00111.72           N  
ATOM   1403  N   ASP A 307      31.594  27.606  13.208  1.00152.88           N  
ATOM   1404  CA  ASP A 307      31.202  28.214  14.471  1.00152.88           C  
ATOM   1405  C   ASP A 307      29.928  29.041  14.313  1.00152.88           C  
ATOM   1406  O   ASP A 307      28.862  28.507  14.017  1.00152.88           O  
ATOM   1407  CB  ASP A 307      32.327  29.114  14.961  1.00132.05           C  
ATOM   1408  CG  ASP A 307      32.761  30.108  13.908  1.00132.05           C  
ATOM   1409  OD1 ASP A 307      32.408  31.297  14.040  1.00132.05           O  
ATOM   1410  OD2 ASP A 307      33.445  29.700  12.944  1.00132.05           O  
ATOM   1411  N   GLU A 308      30.054  30.351  14.514  1.00107.15           N  
ATOM   1412  CA  GLU A 308      28.920  31.263  14.427  1.00107.15           C  
ATOM   1413  C   GLU A 308      29.240  32.459  13.542  1.00107.15           C  
ATOM   1414  O   GLU A 308      28.410  33.348  13.347  1.00107.15           O  
ATOM   1415  CB  GLU A 308      28.526  31.748  15.814  1.00201.79           C  
ATOM   1416  CG  GLU A 308      29.636  32.448  16.551  1.00201.79           C  
ATOM   1417  CD  GLU A 308      29.226  32.817  17.955  1.00201.79           C  
ATOM   1418  OE1 GLU A 308      28.094  32.466  18.347  1.00201.79           O  
ATOM   1419  OE2 GLU A 308      30.031  33.455  18.664  1.00201.79           O  
ATOM   1420  N   LYS A 309      30.454  32.479  13.012  1.00108.68           N  
ATOM   1421  CA  LYS A 309      30.796  33.428  11.973  1.00108.68           C  
ATOM   1422  C   LYS A 309      29.948  33.135  10.739  1.00108.68           C  
ATOM   1423  O   LYS A 309      29.595  34.039   9.984  1.00108.68           O  
ATOM   1424  CB  LYS A 309      32.279  33.312  11.636  1.00136.54           C  
ATOM   1425  CG  LYS A 309      33.196  33.647  12.797  1.00136.54           C  
ATOM   1426  CD  LYS A 309      33.080  35.112  13.197  1.00136.54           C  
ATOM   1427  CE  LYS A 309      32.013  35.338  14.258  1.00136.54           C  
ATOM   1428  NZ  LYS A 309      31.869  36.791  14.573  1.00136.54           N  
ATOM   1429  N   VAL A 310      29.628  31.862  10.545  1.00 95.16           N  
ATOM   1430  CA  VAL A 310      28.710  31.440   9.497  1.00 95.16           C  
ATOM   1431  C   VAL A 310      27.681  32.529   9.231  1.00 95.16           C  
ATOM   1432  O   VAL A 310      27.414  32.886   8.090  1.00 95.16           O  
ATOM   1433  CB  VAL A 310      27.962  30.175   9.926  1.00 65.73           C  
ATOM   1434  CG1 VAL A 310      28.195  29.052   8.933  1.00 65.73           C  
ATOM   1435  CG2 VAL A 310      28.425  29.771  11.313  1.00 65.73           C  
ATOM   1436  N   ASP A 311      27.119  33.072  10.299  1.00 92.14           N  
ATOM   1437  CA  ASP A 311      25.929  33.893  10.186  1.00 92.14           C  
ATOM   1438  C   ASP A 311      26.252  35.355   9.871  1.00 92.14           C  
ATOM   1439  O   ASP A 311      25.396  36.106   9.383  1.00 92.14           O  
ATOM   1440  CB  ASP A 311      25.122  33.755  11.476  1.00 84.01           C  
ATOM   1441  CG  ASP A 311      24.785  32.309  11.783  1.00 84.01           C  
ATOM   1442  OD1 ASP A 311      25.307  31.424  11.086  1.00 84.01           O  
ATOM   1443  OD2 ASP A 311      24.002  32.039  12.706  1.00 84.01           O  
ATOM   1444  N   LEU A 312      27.498  35.746  10.139  1.00 57.56           N  
ATOM   1445  CA  LEU A 312      28.005  37.074   9.780  1.00 57.56           C  
ATOM   1446  C   LEU A 312      28.288  37.093   8.289  1.00 57.56           C  
ATOM   1447  O   LEU A 312      28.247  38.138   7.631  1.00 57.56           O  
ATOM   1448  CB  LEU A 312      29.290  37.369  10.556  1.00 71.60           C  
ATOM   1449  CG  LEU A 312      29.107  37.575  12.059  1.00 71.60           C  
ATOM   1450  CD1 LEU A 312      28.340  38.868  12.273  1.00 71.60           C  
ATOM   1451  CD2 LEU A 312      28.373  36.397  12.691  1.00 71.60           C  
ATOM   1452  N   TRP A 313      28.567  35.903   7.772  1.00 68.45           N  
ATOM   1453  CA  TRP A 313      28.751  35.697   6.351  1.00 68.45           C  
ATOM   1454  C   TRP A 313      27.418  35.744   5.615  1.00 68.45           C  
ATOM   1455  O   TRP A 313      27.274  36.447   4.606  1.00 68.45           O  
ATOM   1456  CB  TRP A 313      29.397  34.348   6.111  1.00 60.29           C  
ATOM   1457  CG  TRP A 313      29.527  34.046   4.679  1.00 60.29           C  
ATOM   1458  CD1 TRP A 313      28.587  33.484   3.864  1.00 60.29           C  
ATOM   1459  CD2 TRP A 313      30.667  34.289   3.872  1.00 60.29           C  
ATOM   1460  NE1 TRP A 313      29.074  33.363   2.588  1.00 60.29           N  
ATOM   1461  CE2 TRP A 313      30.357  33.847   2.568  1.00 60.29           C  
ATOM   1462  CE3 TRP A 313      31.931  34.835   4.122  1.00 60.29           C  
ATOM   1463  CZ2 TRP A 313      31.267  33.932   1.518  1.00 60.29           C  
ATOM   1464  CZ3 TRP A 313      32.830  34.921   3.087  1.00 60.29           C  
ATOM   1465  CH2 TRP A 313      32.496  34.471   1.797  1.00 60.29           C  
ATOM   1466  N   SER A 314      26.454  34.974   6.110  1.00 77.90           N  
ATOM   1467  CA  SER A 314      25.105  35.034   5.575  1.00 77.90           C  
ATOM   1468  C   SER A 314      24.588  36.469   5.687  1.00 77.90           C  
ATOM   1469  O   SER A 314      23.995  37.008   4.751  1.00 77.90           O  
ATOM   1470  CB  SER A 314      24.183  34.102   6.356  1.00 92.47           C  
ATOM   1471  OG  SER A 314      24.601  32.759   6.238  1.00 92.47           O  
ATOM   1472  N   LEU A 315      24.821  37.086   6.843  1.00 60.07           N  
ATOM   1473  CA  LEU A 315      24.310  38.416   7.097  1.00 60.07           C  
ATOM   1474  C   LEU A 315      24.848  39.346   6.023  1.00 60.07           C  
ATOM   1475  O   LEU A 315      24.229  40.353   5.680  1.00 60.07           O  
ATOM   1476  CB  LEU A 315      24.734  38.873   8.495  1.00 67.39           C  
ATOM   1477  CG  LEU A 315      24.102  40.182   8.977  1.00 67.39           C  
ATOM   1478  CD1 LEU A 315      22.657  40.286   8.510  1.00 67.39           C  
ATOM   1479  CD2 LEU A 315      24.175  40.235  10.488  1.00 67.39           C  
ATOM   1480  N   GLY A 316      26.000  38.987   5.474  1.00 63.52           N  
ATOM   1481  CA  GLY A 316      26.593  39.800   4.430  1.00 63.52           C  
ATOM   1482  C   GLY A 316      25.964  39.546   3.076  1.00 63.52           C  
ATOM   1483  O   GLY A 316      25.528  40.480   2.404  1.00 63.52           O  
ATOM   1484  N   VAL A 317      25.922  38.276   2.683  1.00 58.81           N  
ATOM   1485  CA  VAL A 317      25.180  37.834   1.509  1.00 58.81           C  
ATOM   1486  C   VAL A 317      23.753  38.383   1.589  1.00 58.81           C  
ATOM   1487  O   VAL A 317      23.284  39.033   0.656  1.00 58.81           O  
ATOM   1488  CB  VAL A 317      25.101  36.292   1.460  1.00 61.22           C  
ATOM   1489  CG1 VAL A 317      24.791  35.827   0.056  1.00 61.22           C  
ATOM   1490  CG2 VAL A 317      26.381  35.684   1.996  1.00 61.22           C  
ATOM   1491  N   LEU A 318      23.081  38.119   2.711  1.00 65.91           N  
ATOM   1492  CA  LEU A 318      21.744  38.664   2.985  1.00 65.91           C  
ATOM   1493  C   LEU A 318      21.700  40.129   2.641  1.00 65.91           C  
ATOM   1494  O   LEU A 318      20.883  40.593   1.844  1.00 65.91           O  
ATOM   1495  CB  LEU A 318      21.376  38.520   4.462  1.00 90.21           C  
ATOM   1496  CG  LEU A 318      20.219  37.562   4.728  1.00 90.21           C  
ATOM   1497  CD1 LEU A 318      19.090  37.827   3.743  1.00 90.21           C  
ATOM   1498  CD2 LEU A 318      20.708  36.137   4.567  1.00 90.21           C  
ATOM   1499  N   CYS A 319      22.605  40.863   3.246  1.00 61.91           N  
ATOM   1500  CA  CYS A 319      22.622  42.274   3.014  1.00 61.91           C  
ATOM   1501  C   CYS A 319      22.715  42.600   1.525  1.00 61.91           C  
ATOM   1502  O   CYS A 319      21.909  43.359   0.969  1.00 61.91           O  
ATOM   1503  CB  CYS A 319      23.782  42.890   3.755  1.00 75.60           C  
ATOM   1504  SG  CYS A 319      23.501  44.617   3.917  1.00 75.60           S  
ATOM   1505  N   TYR A 320      23.713  42.016   0.887  1.00 59.76           N  
ATOM   1506  CA  TYR A 320      23.954  42.249  -0.520  1.00 59.76           C  
ATOM   1507  C   TYR A 320      22.708  41.927  -1.321  1.00 59.76           C  
ATOM   1508  O   TYR A 320      22.282  42.705  -2.179  1.00 59.76           O  
ATOM   1509  CB  TYR A 320      25.093  41.361  -0.984  1.00 61.02           C  
ATOM   1510  CG  TYR A 320      25.481  41.562  -2.408  1.00 61.02           C  
ATOM   1511  CD1 TYR A 320      24.675  41.116  -3.439  1.00 61.02           C  
ATOM   1512  CD2 TYR A 320      26.687  42.148  -2.725  1.00 61.02           C  
ATOM   1513  CE1 TYR A 320      25.068  41.245  -4.754  1.00 61.02           C  
ATOM   1514  CE2 TYR A 320      27.096  42.279  -4.042  1.00 61.02           C  
ATOM   1515  CZ  TYR A 320      26.285  41.826  -5.050  1.00 61.02           C  
ATOM   1516  OH  TYR A 320      26.708  41.956  -6.349  1.00 61.02           O  
ATOM   1517  N   GLU A 321      22.117  40.770  -1.048  1.00 68.05           N  
ATOM   1518  CA  GLU A 321      20.986  40.355  -1.849  1.00 68.05           C  
ATOM   1519  C   GLU A 321      19.892  41.421  -1.828  1.00 68.05           C  
ATOM   1520  O   GLU A 321      19.388  41.809  -2.876  1.00 68.05           O  
ATOM   1521  CB  GLU A 321      20.441  39.024  -1.359  1.00 76.79           C  
ATOM   1522  CG  GLU A 321      19.525  38.372  -2.373  1.00 76.79           C  
ATOM   1523  CD  GLU A 321      19.211  36.925  -2.040  1.00 76.79           C  
ATOM   1524  OE1 GLU A 321      20.149  36.172  -1.692  1.00 76.79           O  
ATOM   1525  OE2 GLU A 321      18.024  36.536  -2.122  1.00 76.79           O  
ATOM   1526  N   PHE A 322      19.548  41.909  -0.634  1.00 64.87           N  
ATOM   1527  CA  PHE A 322      18.510  42.936  -0.477  1.00 64.87           C  
ATOM   1528  C   PHE A 322      18.786  44.127  -1.373  1.00 64.87           C  
ATOM   1529  O   PHE A 322      17.928  44.587  -2.114  1.00 64.87           O  
ATOM   1530  CB  PHE A 322      18.463  43.438   0.956  1.00 51.15           C  
ATOM   1531  CG  PHE A 322      18.047  42.407   1.953  1.00 51.15           C  
ATOM   1532  CD1 PHE A 322      17.325  41.293   1.566  1.00 51.15           C  
ATOM   1533  CD2 PHE A 322      18.333  42.578   3.305  1.00 51.15           C  
ATOM   1534  CE1 PHE A 322      16.882  40.355   2.523  1.00 51.15           C  
ATOM   1535  CE2 PHE A 322      17.897  41.652   4.258  1.00 51.15           C  
ATOM   1536  CZ  PHE A 322      17.167  40.539   3.863  1.00 51.15           C  
ATOM   1537  N   LEU A 323      19.999  44.631  -1.301  1.00 43.27           N  
ATOM   1538  CA  LEU A 323      20.299  45.877  -1.974  1.00 43.27           C  
ATOM   1539  C   LEU A 323      20.402  45.706  -3.478  1.00 43.27           C  
ATOM   1540  O   LEU A 323      20.159  46.645  -4.253  1.00 43.27           O  
ATOM   1541  CB  LEU A 323      21.605  46.466  -1.441  1.00 54.97           C  
ATOM   1542  CG  LEU A 323      21.559  47.052  -0.034  1.00 54.97           C  
ATOM   1543  CD1 LEU A 323      22.954  47.441   0.403  1.00 54.97           C  
ATOM   1544  CD2 LEU A 323      20.624  48.250  -0.021  1.00 54.97           C  
ATOM   1545  N   VAL A 324      20.785  44.509  -3.907  1.00 59.27           N  
ATOM   1546  CA  VAL A 324      21.067  44.313  -5.316  1.00 59.27           C  
ATOM   1547  C   VAL A 324      20.039  43.384  -5.919  1.00 59.27           C  
ATOM   1548  O   VAL A 324      19.787  43.448  -7.095  1.00 59.27           O  
ATOM   1549  CB  VAL A 324      22.490  43.745  -5.551  1.00 48.17           C  
ATOM   1550  CG1 VAL A 324      22.872  43.961  -6.960  1.00 48.17           C  
ATOM   1551  CG2 VAL A 324      23.497  44.425  -4.694  1.00 48.17           C  
ATOM   1552  N   GLY A 325      19.434  42.527  -5.114  1.00 94.52           N  
ATOM   1553  CA  GLY A 325      18.416  41.641  -5.649  1.00 94.52           C  
ATOM   1554  C   GLY A 325      18.892  40.227  -5.963  1.00 94.52           C  
ATOM   1555  O   GLY A 325      18.149  39.264  -5.782  1.00 94.52           O  
ATOM   1556  N   LYS A 326      20.118  40.081  -6.444  1.00 67.98           N  
ATOM   1557  CA  LYS A 326      20.720  38.758  -6.534  1.00 67.98           C  
ATOM   1558  C   LYS A 326      21.691  38.625  -5.371  1.00 67.98           C  
ATOM   1559  O   LYS A 326      22.163  39.625  -4.836  1.00 67.98           O  
ATOM   1560  CB  LYS A 326      21.477  38.590  -7.859  1.00133.29           C  
ATOM   1561  CG  LYS A 326      22.808  39.334  -7.905  1.00133.29           C  
ATOM   1562  CD  LYS A 326      23.748  38.784  -8.973  1.00133.29           C  
ATOM   1563  CE  LYS A 326      25.159  39.340  -8.796  1.00133.29           C  
ATOM   1564  NZ  LYS A 326      25.197  40.831  -8.869  1.00133.29           N  
ATOM   1565  N   PRO A 327      21.993  37.384  -4.958  1.00 63.81           N  
ATOM   1566  CA  PRO A 327      23.041  37.148  -3.960  1.00 63.81           C  
ATOM   1567  C   PRO A 327      24.389  37.307  -4.604  1.00 63.81           C  
ATOM   1568  O   PRO A 327      24.547  37.095  -5.799  1.00 63.81           O  
ATOM   1569  CB  PRO A 327      22.804  35.721  -3.503  1.00 47.11           C  
ATOM   1570  CG  PRO A 327      22.152  35.085  -4.670  1.00 47.11           C  
ATOM   1571  CD  PRO A 327      21.345  36.134  -5.382  1.00 47.11           C  
ATOM   1572  N   PRO A 328      25.387  37.679  -3.811  1.00 72.37           N  
ATOM   1573  CA  PRO A 328      26.724  37.998  -4.305  1.00 72.37           C  
ATOM   1574  C   PRO A 328      27.449  36.890  -5.082  1.00 72.37           C  
ATOM   1575  O   PRO A 328      28.384  37.173  -5.811  1.00 72.37           O  
ATOM   1576  CB  PRO A 328      27.474  38.414  -3.045  1.00 88.38           C  
ATOM   1577  CG  PRO A 328      26.691  37.822  -1.908  1.00 88.38           C  
ATOM   1578  CD  PRO A 328      25.279  37.811  -2.350  1.00 88.38           C  
ATOM   1579  N   PHE A 329      27.039  35.636  -4.942  1.00 68.58           N  
ATOM   1580  CA  PHE A 329      27.760  34.564  -5.610  1.00 68.58           C  
ATOM   1581  C   PHE A 329      26.922  33.829  -6.626  1.00 68.58           C  
ATOM   1582  O   PHE A 329      27.329  32.778  -7.130  1.00 68.58           O  
ATOM   1583  CB  PHE A 329      28.290  33.585  -4.592  1.00 80.81           C  
ATOM   1584  CG  PHE A 329      29.061  34.236  -3.520  1.00 80.81           C  
ATOM   1585  CD1 PHE A 329      30.296  34.775  -3.784  1.00 80.81           C  
ATOM   1586  CD2 PHE A 329      28.531  34.364  -2.254  1.00 80.81           C  
ATOM   1587  CE1 PHE A 329      30.992  35.438  -2.803  1.00 80.81           C  
ATOM   1588  CE2 PHE A 329      29.222  35.026  -1.269  1.00 80.81           C  
ATOM   1589  CZ  PHE A 329      30.453  35.564  -1.545  1.00 80.81           C  
ATOM   1590  N   GLU A 330      25.746  34.382  -6.912  1.00 87.31           N  
ATOM   1591  CA  GLU A 330      24.927  33.957  -8.047  1.00 87.31           C  
ATOM   1592  C   GLU A 330      25.775  33.308  -9.138  1.00 87.31           C  
ATOM   1593  O   GLU A 330      26.782  33.863  -9.582  1.00 87.31           O  
ATOM   1594  CB  GLU A 330      24.191  35.169  -8.631  1.00 97.76           C  
ATOM   1595  CG  GLU A 330      23.046  34.833  -9.562  1.00 97.76           C  
ATOM   1596  CD  GLU A 330      21.863  34.253  -8.820  1.00 97.76           C  
ATOM   1597  OE1 GLU A 330      22.082  33.612  -7.773  1.00 97.76           O  
ATOM   1598  OE2 GLU A 330      20.716  34.435  -9.277  1.00 97.76           O  
ATOM   1599  N   ALA A 331      25.373  32.119  -9.558  1.00127.81           N  
ATOM   1600  CA  ALA A 331      25.922  31.514 -10.762  1.00127.81           C  
ATOM   1601  C   ALA A 331      24.801  30.716 -11.392  1.00127.81           C  
ATOM   1602  O   ALA A 331      23.686  30.689 -10.872  1.00127.81           O  
ATOM   1603  CB  ALA A 331      27.094  30.603 -10.420  1.00 38.26           C  
ATOM   1604  N   ASN A 332      25.079  30.066 -12.510  1.00 92.06           N  
ATOM   1605  CA  ASN A 332      24.037  29.270 -13.132  1.00 92.06           C  
ATOM   1606  C   ASN A 332      24.137  27.809 -12.718  1.00 92.06           C  
ATOM   1607  O   ASN A 332      23.179  27.044 -12.856  1.00 92.06           O  
ATOM   1608  CB  ASN A 332      24.086  29.410 -14.656  1.00107.16           C  
ATOM   1609  CG  ASN A 332      22.776  29.926 -15.224  1.00107.16           C  
ATOM   1610  OD1 ASN A 332      22.680  30.251 -16.405  1.00107.16           O  
ATOM   1611  ND2 ASN A 332      21.758  30.008 -14.374  1.00107.16           N  
ATOM   1612  N   THR A 333      25.296  27.429 -12.193  1.00 65.43           N  
ATOM   1613  CA  THR A 333      25.485  26.065 -11.727  1.00 65.43           C  
ATOM   1614  C   THR A 333      26.058  25.979 -10.321  1.00 65.43           C  
ATOM   1615  O   THR A 333      26.650  26.930  -9.795  1.00 65.43           O  
ATOM   1616  CB  THR A 333      26.408  25.245 -12.675  1.00 71.91           C  
ATOM   1617  OG1 THR A 333      27.761  25.715 -12.573  1.00 71.91           O  
ATOM   1618  CG2 THR A 333      25.930  25.371 -14.112  1.00 71.91           C  
ATOM   1619  N   TYR A 334      25.866  24.805  -9.731  1.00 77.60           N  
ATOM   1620  CA  TYR A 334      26.353  24.488  -8.403  1.00 77.60           C  
ATOM   1621  C   TYR A 334      27.867  24.621  -8.421  1.00 77.60           C  
ATOM   1622  O   TYR A 334      28.493  25.016  -7.426  1.00 77.60           O  
ATOM   1623  CB  TYR A 334      25.946  23.052  -8.068  1.00 86.06           C  
ATOM   1624  CG  TYR A 334      26.284  22.597  -6.666  1.00 86.06           C  
ATOM   1625  CD1 TYR A 334      25.374  22.752  -5.630  1.00 86.06           C  
ATOM   1626  CD2 TYR A 334      27.507  22.005  -6.381  1.00 86.06           C  
ATOM   1627  CE1 TYR A 334      25.671  22.330  -4.360  1.00 86.06           C  
ATOM   1628  CE2 TYR A 334      27.810  21.584  -5.111  1.00 86.06           C  
ATOM   1629  CZ  TYR A 334      26.889  21.746  -4.104  1.00 86.06           C  
ATOM   1630  OH  TYR A 334      27.176  21.304  -2.832  1.00 86.06           O  
ATOM   1631  N   GLN A 335      28.440  24.305  -9.581  1.00 93.53           N  
ATOM   1632  CA  GLN A 335      29.878  24.124  -9.722  1.00 93.53           C  
ATOM   1633  C   GLN A 335      30.635  25.441  -9.560  1.00 93.53           C  
ATOM   1634  O   GLN A 335      31.472  25.589  -8.655  1.00 93.53           O  
ATOM   1635  CB  GLN A 335      30.185  23.516 -11.091  1.00140.01           C  
ATOM   1636  CG  GLN A 335      29.078  22.623 -11.640  1.00140.01           C  
ATOM   1637  CD  GLN A 335      28.638  21.548 -10.664  1.00140.01           C  
ATOM   1638  OE1 GLN A 335      29.352  21.213  -9.720  1.00140.01           O  
ATOM   1639  NE2 GLN A 335      27.452  21.000 -10.892  1.00140.01           N  
ATOM   1640  N   GLU A 336      30.330  26.392 -10.440  1.00 83.62           N  
ATOM   1641  CA  GLU A 336      30.962  27.703 -10.394  1.00 83.62           C  
ATOM   1642  C   GLU A 336      30.641  28.444  -9.094  1.00 83.62           C  
ATOM   1643  O   GLU A 336      31.497  29.144  -8.535  1.00 83.62           O  
ATOM   1644  CB  GLU A 336      30.515  28.531 -11.589  1.00 99.10           C  
ATOM   1645  CG  GLU A 336      29.067  28.312 -11.967  1.00 99.10           C  
ATOM   1646  CD  GLU A 336      28.563  29.359 -12.945  1.00 99.10           C  
ATOM   1647  OE1 GLU A 336      27.843  29.001 -13.913  1.00 99.10           O  
ATOM   1648  OE2 GLU A 336      28.895  30.547 -12.737  1.00 99.10           O  
ATOM   1649  N   THR A 337      29.412  28.282  -8.608  1.00 57.16           N  
ATOM   1650  CA  THR A 337      29.029  28.895  -7.344  1.00 57.16           C  
ATOM   1651  C   THR A 337      29.938  28.468  -6.200  1.00 57.16           C  
ATOM   1652  O   THR A 337      30.235  29.282  -5.314  1.00 57.16           O  
ATOM   1653  CB  THR A 337      27.581  28.561  -6.965  1.00 51.25           C  
ATOM   1654  OG1 THR A 337      26.694  29.129  -7.938  1.00 51.25           O  
ATOM   1655  CG2 THR A 337      27.250  29.112  -5.580  1.00 51.25           C  
ATOM   1656  N   TYR A 338      30.382  27.204  -6.211  1.00 73.93           N  
ATOM   1657  CA  TYR A 338      31.360  26.763  -5.219  1.00 73.93           C  
ATOM   1658  C   TYR A 338      32.604  27.608  -5.400  1.00 73.93           C  
ATOM   1659  O   TYR A 338      33.130  28.175  -4.440  1.00 73.93           O  
ATOM   1660  CB  TYR A 338      31.747  25.294  -5.389  1.00144.73           C  
ATOM   1661  CG  TYR A 338      32.890  24.912  -4.466  1.00144.73           C  
ATOM   1662  CD1 TYR A 338      32.651  24.549  -3.147  1.00144.73           C  
ATOM   1663  CD2 TYR A 338      34.215  24.996  -4.888  1.00144.73           C  
ATOM   1664  CE1 TYR A 338      33.694  24.289  -2.269  1.00144.73           C  
ATOM   1665  CE2 TYR A 338      35.268  24.738  -4.016  1.00144.73           C  
ATOM   1666  CZ  TYR A 338      34.999  24.388  -2.706  1.00144.73           C  
ATOM   1667  OH  TYR A 338      36.032  24.159  -1.822  1.00144.73           O  
ATOM   1668  N   LYS A 339      33.069  27.683  -6.647  1.00 72.64           N  
ATOM   1669  CA  LYS A 339      34.244  28.474  -6.979  1.00 72.64           C  
ATOM   1670  C   LYS A 339      34.056  29.877  -6.419  1.00 72.64           C  
ATOM   1671  O   LYS A 339      34.792  30.304  -5.529  1.00 72.64           O  
ATOM   1672  CB  LYS A 339      34.421  28.546  -8.496  1.00 86.81           C  
ATOM   1673  CG  LYS A 339      35.094  27.338  -9.145  1.00 86.81           C  
ATOM   1674  CD  LYS A 339      35.185  27.578 -10.655  1.00 86.81           C  
ATOM   1675  CE  LYS A 339      35.905  26.470 -11.403  1.00 86.81           C  
ATOM   1676  NZ  LYS A 339      35.970  26.789 -12.866  1.00 86.81           N  
ATOM   1677  N   ARG A 340      33.046  30.574  -6.933  1.00 63.09           N  
ATOM   1678  CA  ARG A 340      32.787  31.959  -6.552  1.00 63.09           C  
ATOM   1679  C   ARG A 340      32.861  32.195  -5.048  1.00 63.09           C  
ATOM   1680  O   ARG A 340      33.411  33.200  -4.614  1.00 63.09           O  
ATOM   1681  CB  ARG A 340      31.424  32.403  -7.083  1.00 92.18           C  
ATOM   1682  CG  ARG A 340      31.299  32.286  -8.593  1.00 92.18           C  
ATOM   1683  CD  ARG A 340      30.401  33.370  -9.174  1.00 92.18           C  
ATOM   1684  NE  ARG A 340      30.892  34.716  -8.867  1.00 92.18           N  
ATOM   1685  CZ  ARG A 340      30.151  35.824  -8.894  1.00 92.18           C  
ATOM   1686  NH1 ARG A 340      28.863  35.768  -9.215  1.00 92.18           N  
ATOM   1687  NH2 ARG A 340      30.705  36.995  -8.599  1.00 92.18           N  
ATOM   1688  N   ILE A 341      32.332  31.271  -4.247  1.00 67.70           N  
ATOM   1689  CA  ILE A 341      32.339  31.466  -2.797  1.00 67.70           C  
ATOM   1690  C   ILE A 341      33.701  31.229  -2.182  1.00 67.70           C  
ATOM   1691  O   ILE A 341      34.108  31.947  -1.274  1.00 67.70           O  
ATOM   1692  CB  ILE A 341      31.352  30.545  -2.043  1.00 76.57           C  
ATOM   1693  CG1 ILE A 341      29.921  30.729  -2.554  1.00 76.57           C  
ATOM   1694  CG2 ILE A 341      31.390  30.894  -0.563  1.00 76.57           C  
ATOM   1695  CD1 ILE A 341      28.865  30.169  -1.622  1.00 76.57           C  
ATOM   1696  N   SER A 342      34.406  30.217  -2.672  1.00102.72           N  
ATOM   1697  CA  SER A 342      35.706  29.877  -2.122  1.00102.72           C  
ATOM   1698  C   SER A 342      36.778  30.889  -2.525  1.00102.72           C  
ATOM   1699  O   SER A 342      37.604  31.280  -1.699  1.00102.72           O  
ATOM   1700  CB  SER A 342      36.101  28.471  -2.563  1.00 98.34           C  
ATOM   1701  OG  SER A 342      35.816  28.283  -3.935  1.00 98.34           O  
ATOM   1702  N   ARG A 343      36.771  31.327  -3.780  1.00 99.36           N  
ATOM   1703  CA  ARG A 343      37.703  32.375  -4.186  1.00 99.36           C  
ATOM   1704  C   ARG A 343      37.174  33.722  -3.690  1.00 99.36           C  
ATOM   1705  O   ARG A 343      37.895  34.725  -3.702  1.00 99.36           O  
ATOM   1706  CB  ARG A 343      37.881  32.397  -5.712  1.00 92.14           C  
ATOM   1707  CG  ARG A 343      37.408  31.134  -6.406  1.00 92.14           C  
ATOM   1708  CD  ARG A 343      38.520  30.339  -7.054  1.00 92.14           C  
ATOM   1709  NE  ARG A 343      38.479  30.438  -8.510  1.00 92.14           N  
ATOM   1710  CZ  ARG A 343      38.999  29.539  -9.349  1.00 92.14           C  
ATOM   1711  NH1 ARG A 343      39.604  28.447  -8.877  1.00 92.14           N  
ATOM   1712  NH2 ARG A 343      38.941  29.741 -10.669  1.00 92.14           N  
ATOM   1713  N   VAL A 344      35.910  33.722  -3.255  1.00 75.38           N  
ATOM   1714  CA  VAL A 344      35.278  34.876  -2.608  1.00 75.38           C  
ATOM   1715  C   VAL A 344      35.014  35.995  -3.621  1.00 75.38           C  
ATOM   1716  O   VAL A 344      35.169  37.177  -3.337  1.00 75.38           O  
ATOM   1717  CB  VAL A 344      36.153  35.363  -1.399  1.00 47.45           C  
ATOM   1718  CG1 VAL A 344      35.720  36.731  -0.898  1.00 47.45           C  
ATOM   1719  CG2 VAL A 344      36.023  34.370  -0.259  1.00 47.45           C  
ATOM   1720  N   GLU A 345      34.585  35.606  -4.814  1.00 66.84           N  
ATOM   1721  CA  GLU A 345      34.498  36.542  -5.919  1.00 66.84           C  
ATOM   1722  C   GLU A 345      33.134  37.198  -6.065  1.00 66.84           C  
ATOM   1723  O   GLU A 345      32.163  36.539  -6.433  1.00 66.84           O  
ATOM   1724  CB  GLU A 345      34.861  35.819  -7.201  1.00101.35           C  
ATOM   1725  CG  GLU A 345      36.190  35.136  -7.098  1.00101.35           C  
ATOM   1726  CD  GLU A 345      36.416  34.162  -8.216  1.00101.35           C  
ATOM   1727  OE1 GLU A 345      37.596  33.863  -8.504  1.00101.35           O  
ATOM   1728  OE2 GLU A 345      35.413  33.696  -8.804  1.00101.35           O  
ATOM   1729  N   PHE A 346      33.068  38.502  -5.794  1.00 97.89           N  
ATOM   1730  CA  PHE A 346      31.854  39.279  -6.047  1.00 97.89           C  
ATOM   1731  C   PHE A 346      32.175  40.711  -6.477  1.00 97.89           C  
ATOM   1732  O   PHE A 346      33.264  41.209  -6.205  1.00 97.89           O  
ATOM   1733  CB  PHE A 346      30.981  39.305  -4.793  1.00 78.92           C  
ATOM   1734  CG  PHE A 346      31.597  40.038  -3.645  1.00 78.92           C  
ATOM   1735  CD1 PHE A 346      32.195  39.352  -2.614  1.00 78.92           C  
ATOM   1736  CD2 PHE A 346      31.578  41.417  -3.597  1.00 78.92           C  
ATOM   1737  CE1 PHE A 346      32.764  40.028  -1.552  1.00 78.92           C  
ATOM   1738  CE2 PHE A 346      32.144  42.096  -2.543  1.00 78.92           C  
ATOM   1739  CZ  PHE A 346      32.737  41.400  -1.518  1.00 78.92           C  
ATOM   1740  N   THR A 347      31.226  41.370  -7.140  1.00 88.79           N  
ATOM   1741  CA  THR A 347      31.400  42.765  -7.558  1.00 88.79           C  
ATOM   1742  C   THR A 347      30.153  43.630  -7.378  1.00 88.79           C  
ATOM   1743  O   THR A 347      29.063  43.242  -7.786  1.00 88.79           O  
ATOM   1744  CB  THR A 347      31.813  42.853  -9.031  1.00 88.55           C  
ATOM   1745  OG1 THR A 347      30.905  42.077  -9.831  1.00 88.55           O  
ATOM   1746  CG2 THR A 347      33.246  42.356  -9.210  1.00 88.55           C  
ATOM   1747  N   PHE A 348      30.332  44.814  -6.791  1.00129.84           N  
ATOM   1748  CA  PHE A 348      29.226  45.729  -6.480  1.00129.84           C  
ATOM   1749  C   PHE A 348      28.729  46.521  -7.688  1.00129.84           C  
ATOM   1750  O   PHE A 348      29.519  47.142  -8.400  1.00129.84           O  
ATOM   1751  CB  PHE A 348      29.650  46.747  -5.422  1.00 71.98           C  
ATOM   1752  CG  PHE A 348      29.987  46.151  -4.087  1.00 71.98           C  
ATOM   1753  CD1 PHE A 348      29.003  45.584  -3.292  1.00 71.98           C  
ATOM   1754  CD2 PHE A 348      31.272  46.229  -3.586  1.00 71.98           C  
ATOM   1755  CE1 PHE A 348      29.289  45.110  -2.018  1.00 71.98           C  
ATOM   1756  CE2 PHE A 348      31.567  45.756  -2.308  1.00 71.98           C  
ATOM   1757  CZ  PHE A 348      30.569  45.197  -1.526  1.00 71.98           C  
ATOM   1758  N   PRO A 349      27.403  46.537  -7.908  1.00 88.93           N  
ATOM   1759  CA  PRO A 349      26.744  47.401  -8.895  1.00 88.93           C  
ATOM   1760  C   PRO A 349      26.939  48.878  -8.568  1.00 88.93           C  
ATOM   1761  O   PRO A 349      27.149  49.246  -7.406  1.00 88.93           O  
ATOM   1762  CB  PRO A 349      25.272  47.005  -8.808  1.00 62.18           C  
ATOM   1763  CG  PRO A 349      25.276  45.665  -8.213  1.00 62.18           C  
ATOM   1764  CD  PRO A 349      26.442  45.635  -7.261  1.00 62.18           C  
ATOM   1765  N   ASP A 350      26.852  49.716  -9.598  1.00103.70           N  
ATOM   1766  CA  ASP A 350      27.231  51.123  -9.507  1.00103.70           C  
ATOM   1767  C   ASP A 350      26.476  51.847  -8.401  1.00103.70           C  
ATOM   1768  O   ASP A 350      27.045  52.654  -7.664  1.00103.70           O  
ATOM   1769  CB  ASP A 350      26.970  51.792 -10.850  1.00117.15           C  
ATOM   1770  CG  ASP A 350      27.646  51.060 -11.992  1.00117.15           C  
ATOM   1771  OD1 ASP A 350      28.897  51.078 -12.040  1.00117.15           O  
ATOM   1772  OD2 ASP A 350      26.935  50.463 -12.833  1.00117.15           O  
ATOM   1773  N   PHE A 351      25.193  51.530  -8.283  1.00 86.95           N  
ATOM   1774  CA  PHE A 351      24.325  52.142  -7.295  1.00 86.95           C  
ATOM   1775  C   PHE A 351      24.531  51.611  -5.877  1.00 86.95           C  
ATOM   1776  O   PHE A 351      23.803  51.975  -4.961  1.00 86.95           O  
ATOM   1777  CB  PHE A 351      22.867  51.950  -7.711  1.00 73.26           C  
ATOM   1778  CG  PHE A 351      22.366  50.525  -7.599  1.00 73.26           C  
ATOM   1779  CD1 PHE A 351      22.120  49.947  -6.351  1.00 73.26           C  
ATOM   1780  CD2 PHE A 351      22.075  49.789  -8.736  1.00 73.26           C  
ATOM   1781  CE1 PHE A 351      21.591  48.670  -6.240  1.00 73.26           C  
ATOM   1782  CE2 PHE A 351      21.545  48.515  -8.633  1.00 73.26           C  
ATOM   1783  CZ  PHE A 351      21.301  47.955  -7.380  1.00 73.26           C  
ATOM   1784  N   VAL A 352      25.506  50.741  -5.675  1.00 87.59           N  
ATOM   1785  CA  VAL A 352      25.793  50.334  -4.315  1.00 87.59           C  
ATOM   1786  C   VAL A 352      26.651  51.407  -3.666  1.00 87.59           C  
ATOM   1787  O   VAL A 352      27.679  51.813  -4.213  1.00 87.59           O  
ATOM   1788  CB  VAL A 352      26.524  48.978  -4.272  1.00 81.22           C  
ATOM   1789  CG1 VAL A 352      26.889  48.619  -2.843  1.00 81.22           C  
ATOM   1790  CG2 VAL A 352      25.626  47.909  -4.834  1.00 81.22           C  
ATOM   1791  N   THR A 353      26.222  51.875  -2.502  1.00 87.74           N  
ATOM   1792  CA  THR A 353      26.949  52.923  -1.802  1.00 87.74           C  
ATOM   1793  C   THR A 353      28.142  52.357  -1.040  1.00 87.74           C  
ATOM   1794  O   THR A 353      28.121  51.204  -0.609  1.00 87.74           O  
ATOM   1795  CB  THR A 353      26.039  53.644  -0.804  1.00114.21           C  
ATOM   1796  OG1 THR A 353      25.840  52.817   0.352  1.00114.21           O  
ATOM   1797  CG2 THR A 353      24.695  53.935  -1.455  1.00114.21           C  
ATOM   1798  N   GLU A 354      29.173  53.180  -0.868  1.00 99.80           N  
ATOM   1799  CA  GLU A 354      30.385  52.763  -0.170  1.00 99.80           C  
ATOM   1800  C   GLU A 354      30.116  52.416   1.287  1.00 99.80           C  
ATOM   1801  O   GLU A 354      30.733  51.506   1.835  1.00 99.80           O  
ATOM   1802  CB  GLU A 354      31.454  53.857  -0.249  1.00166.36           C  
ATOM   1803  CG  GLU A 354      32.587  53.562  -1.227  1.00166.36           C  
ATOM   1804  CD  GLU A 354      32.242  53.914  -2.666  1.00166.36           C  
ATOM   1805  OE1 GLU A 354      31.220  53.411  -3.180  1.00166.36           O  
ATOM   1806  OE2 GLU A 354      32.995  54.696  -3.286  1.00166.36           O  
ATOM   1807  N   GLY A 355      29.194  53.139   1.912  1.00 85.75           N  
ATOM   1808  CA  GLY A 355      28.834  52.829   3.284  1.00 85.75           C  
ATOM   1809  C   GLY A 355      28.441  51.369   3.410  1.00 85.75           C  
ATOM   1810  O   GLY A 355      28.912  50.658   4.300  1.00 85.75           O  
ATOM   1811  N   ALA A 356      27.581  50.919   2.501  1.00 90.83           N  
ATOM   1812  CA  ALA A 356      27.169  49.520   2.454  1.00 90.83           C  
ATOM   1813  C   ALA A 356      28.313  48.677   1.903  1.00 90.83           C  
ATOM   1814  O   ALA A 356      28.685  47.658   2.485  1.00 90.83           O  
ATOM   1815  CB  ALA A 356      25.917  49.367   1.575  1.00 39.47           C  
ATOM   1816  N   ARG A 357      28.872  49.123   0.782  1.00 85.96           N  
ATOM   1817  CA  ARG A 357      30.040  48.477   0.199  1.00 85.96           C  
ATOM   1818  C   ARG A 357      31.001  48.045   1.297  1.00 85.96           C  
ATOM   1819  O   ARG A 357      31.406  46.891   1.372  1.00 85.96           O  
ATOM   1820  CB  ARG A 357      30.748  49.433  -0.766  1.00 51.45           C  
ATOM   1821  CG  ARG A 357      30.557  49.086  -2.213  1.00 51.45           C  
ATOM   1822  CD  ARG A 357      30.397  50.327  -3.056  1.00 51.45           C  
ATOM   1823  NE  ARG A 357      29.780  50.060  -4.357  1.00 51.45           N  
ATOM   1824  CZ  ARG A 357      30.440  50.024  -5.509  1.00 51.45           C  
ATOM   1825  NH1 ARG A 357      31.754  50.237  -5.531  1.00 51.45           N  
ATOM   1826  NH2 ARG A 357      29.785  49.789  -6.637  1.00 51.45           N  
ATOM   1827  N   ASP A 358      31.355  48.974   2.168  1.00 78.15           N  
ATOM   1828  CA  ASP A 358      32.331  48.663   3.189  1.00 78.15           C  
ATOM   1829  C   ASP A 358      31.811  47.584   4.124  1.00 78.15           C  
ATOM   1830  O   ASP A 358      32.501  46.607   4.403  1.00 78.15           O  
ATOM   1831  CB  ASP A 358      32.676  49.913   3.991  1.00105.09           C  
ATOM   1832  CG  ASP A 358      33.706  49.639   5.055  1.00105.09           C  
ATOM   1833  OD1 ASP A 358      33.348  49.028   6.087  1.00105.09           O  
ATOM   1834  OD2 ASP A 358      34.874  50.027   4.848  1.00105.09           O  
ATOM   1835  N   LEU A 359      30.585  47.778   4.597  1.00 88.69           N  
ATOM   1836  CA  LEU A 359      29.914  46.839   5.491  1.00 88.69           C  
ATOM   1837  C   LEU A 359      30.004  45.391   5.008  1.00 88.69           C  
ATOM   1838  O   LEU A 359      30.439  44.494   5.739  1.00 88.69           O  
ATOM   1839  CB  LEU A 359      28.442  47.231   5.607  1.00 62.07           C  
ATOM   1840  CG  LEU A 359      27.565  46.263   6.391  1.00 62.07           C  
ATOM   1841  CD1 LEU A 359      28.180  46.040   7.757  1.00 62.07           C  
ATOM   1842  CD2 LEU A 359      26.173  46.820   6.515  1.00 62.07           C  
ATOM   1843  N   ILE A 360      29.574  45.178   3.768  1.00 76.75           N  
ATOM   1844  CA  ILE A 360      29.505  43.853   3.185  1.00 76.75           C  
ATOM   1845  C   ILE A 360      30.873  43.198   3.093  1.00 76.75           C  
ATOM   1846  O   ILE A 360      31.005  41.974   3.188  1.00 76.75           O  
ATOM   1847  CB  ILE A 360      28.882  43.925   1.796  1.00 88.66           C  
ATOM   1848  CG1 ILE A 360      27.382  44.175   1.937  1.00 88.66           C  
ATOM   1849  CG2 ILE A 360      29.173  42.663   1.022  1.00 88.66           C  
ATOM   1850  CD1 ILE A 360      26.649  44.360   0.626  1.00 88.66           C  
ATOM   1851  N   SER A 361      31.892  44.030   2.935  1.00 94.95           N  
ATOM   1852  CA  SER A 361      33.237  43.562   2.645  1.00 94.95           C  
ATOM   1853  C   SER A 361      33.969  43.068   3.884  1.00 94.95           C  
ATOM   1854  O   SER A 361      34.930  42.300   3.787  1.00 94.95           O  
ATOM   1855  CB  SER A 361      34.003  44.689   1.981  1.00 76.19           C  
ATOM   1856  OG  SER A 361      33.296  45.101   0.826  1.00 76.19           O  
ATOM   1857  N   ARG A 362      33.498  43.504   5.047  1.00 58.17           N  
ATOM   1858  CA  ARG A 362      34.009  42.995   6.303  1.00 58.17           C  
ATOM   1859  C   ARG A 362      33.165  41.846   6.847  1.00 58.17           C  
ATOM   1860  O   ARG A 362      33.535  41.214   7.843  1.00 58.17           O  
ATOM   1861  CB  ARG A 362      34.099  44.125   7.335  1.00108.15           C  
ATOM   1862  CG  ARG A 362      33.075  45.227   7.151  1.00108.15           C  
ATOM   1863  CD  ARG A 362      33.403  46.434   8.015  1.00108.15           C  
ATOM   1864  NE  ARG A 362      34.692  47.026   7.670  1.00108.15           N  
ATOM   1865  CZ  ARG A 362      35.165  48.148   8.202  1.00108.15           C  
ATOM   1866  NH1 ARG A 362      34.454  48.806   9.111  1.00108.15           N  
ATOM   1867  NH2 ARG A 362      36.348  48.617   7.825  1.00108.15           N  
ATOM   1868  N   LEU A 363      32.032  41.573   6.199  1.00 87.63           N  
ATOM   1869  CA  LEU A 363      31.245  40.381   6.513  1.00 87.63           C  
ATOM   1870  C   LEU A 363      31.675  39.222   5.621  1.00 87.63           C  
ATOM   1871  O   LEU A 363      31.607  38.055   6.006  1.00 87.63           O  
ATOM   1872  CB  LEU A 363      29.753  40.651   6.309  1.00 94.99           C  
ATOM   1873  CG  LEU A 363      29.070  41.617   7.281  1.00 94.99           C  
ATOM   1874  CD1 LEU A 363      27.629  41.821   6.867  1.00 94.99           C  
ATOM   1875  CD2 LEU A 363      29.129  41.060   8.684  1.00 94.99           C  
ATOM   1876  N   LEU A 364      32.130  39.553   4.423  1.00 86.67           N  
ATOM   1877  CA  LEU A 364      32.424  38.531   3.442  1.00 86.67           C  
ATOM   1878  C   LEU A 364      33.907  38.186   3.291  1.00 86.67           C  
ATOM   1879  O   LEU A 364      34.369  37.929   2.183  1.00 86.67           O  
ATOM   1880  CB  LEU A 364      31.835  38.934   2.085  1.00 85.25           C  
ATOM   1881  CG  LEU A 364      30.316  38.734   1.966  1.00 85.25           C  
ATOM   1882  CD1 LEU A 364      29.767  39.400   0.713  1.00 85.25           C  
ATOM   1883  CD2 LEU A 364      30.011  37.249   1.947  1.00 85.25           C  
ATOM   1884  N   LYS A 365      34.650  38.156   4.395  1.00104.32           N  
ATOM   1885  CA  LYS A 365      36.044  37.728   4.330  1.00104.32           C  
ATOM   1886  C   LYS A 365      36.193  36.229   4.579  1.00104.32           C  
ATOM   1887  O   LYS A 365      35.585  35.689   5.507  1.00104.32           O  
ATOM   1888  CB  LYS A 365      36.888  38.528   5.325  1.00105.38           C  
ATOM   1889  CG  LYS A 365      37.207  39.929   4.822  1.00105.38           C  
ATOM   1890  CD  LYS A 365      37.855  40.795   5.885  1.00105.38           C  
ATOM   1891  CE  LYS A 365      38.380  42.098   5.287  1.00105.38           C  
ATOM   1892  NZ  LYS A 365      39.379  41.862   4.197  1.00105.38           N  
ATOM   1893  N   HIS A 366      37.002  35.574   3.737  1.00 94.38           N  
ATOM   1894  CA  HIS A 366      37.124  34.108   3.685  1.00 94.38           C  
ATOM   1895  C   HIS A 366      37.462  33.538   5.059  1.00 94.38           C  
ATOM   1896  O   HIS A 366      37.016  32.449   5.429  1.00 94.38           O  
ATOM   1897  CB  HIS A 366      38.217  33.705   2.671  1.00 81.38           C  
ATOM   1898  CG  HIS A 366      38.359  32.222   2.470  1.00 81.38           C  
ATOM   1899  ND1 HIS A 366      38.910  31.386   3.420  1.00 81.38           N  
ATOM   1900  CD2 HIS A 366      38.025  31.428   1.424  1.00 81.38           C  
ATOM   1901  CE1 HIS A 366      38.906  30.144   2.971  1.00 81.38           C  
ATOM   1902  NE2 HIS A 366      38.374  30.141   1.762  1.00 81.38           N  
ATOM   1903  N   ASN A 367      38.248  34.298   5.811  1.00 99.27           N  
ATOM   1904  CA  ASN A 367      38.717  33.888   7.128  1.00 99.27           C  
ATOM   1905  C   ASN A 367      37.721  34.256   8.233  1.00 99.27           C  
ATOM   1906  O   ASN A 367      37.502  35.435   8.519  1.00 99.27           O  
ATOM   1907  CB  ASN A 367      40.080  34.543   7.391  1.00145.81           C  
ATOM   1908  CG  ASN A 367      40.375  34.718   8.865  1.00145.81           C  
ATOM   1909  OD1 ASN A 367      40.020  33.876   9.689  1.00145.81           O  
ATOM   1910  ND2 ASN A 367      41.032  35.821   9.206  1.00145.81           N  
ATOM   1911  N   PRO A 368      37.116  33.247   8.880  1.00 86.79           N  
ATOM   1912  CA  PRO A 368      36.161  33.514   9.962  1.00 86.79           C  
ATOM   1913  C   PRO A 368      36.668  34.541  10.965  1.00 86.79           C  
ATOM   1914  O   PRO A 368      35.908  35.381  11.440  1.00 86.79           O  
ATOM   1915  CB  PRO A 368      35.946  32.146  10.596  1.00 70.61           C  
ATOM   1916  CG  PRO A 368      36.162  31.198   9.454  1.00 70.61           C  
ATOM   1917  CD  PRO A 368      37.264  31.806   8.617  1.00 70.61           C  
ATOM   1918  N   SER A 369      37.956  34.487  11.273  1.00106.25           N  
ATOM   1919  CA  SER A 369      38.532  35.391  12.257  1.00106.25           C  
ATOM   1920  C   SER A 369      38.223  36.848  11.922  1.00106.25           C  
ATOM   1921  O   SER A 369      37.836  37.619  12.794  1.00106.25           O  
ATOM   1922  CB  SER A 369      40.044  35.182  12.333  1.00203.22           C  
ATOM   1923  OG  SER A 369      40.351  33.824  12.599  1.00203.22           O  
ATOM   1924  N   GLN A 370      38.389  37.226  10.660  1.00128.56           N  
ATOM   1925  CA  GLN A 370      38.192  38.615  10.267  1.00128.56           C  
ATOM   1926  C   GLN A 370      36.747  38.896   9.868  1.00128.56           C  
ATOM   1927  O   GLN A 370      36.472  39.395   8.775  1.00128.56           O  
ATOM   1928  CB  GLN A 370      39.149  38.988   9.126  1.00141.32           C  
ATOM   1929  CG  GLN A 370      39.228  37.976   7.993  1.00141.32           C  
ATOM   1930  CD  GLN A 370      40.442  38.195   7.112  1.00141.32           C  
ATOM   1931  OE1 GLN A 370      41.150  39.189   7.261  1.00141.32           O  
ATOM   1932  NE2 GLN A 370      40.690  37.267   6.191  1.00141.32           N  
ATOM   1933  N   ARG A 371      35.831  38.563  10.771  1.00120.64           N  
ATOM   1934  CA  ARG A 371      34.415  38.877  10.616  1.00120.64           C  
ATOM   1935  C   ARG A 371      33.896  39.482  11.920  1.00120.64           C  
ATOM   1936  O   ARG A 371      34.038  38.889  12.990  1.00120.64           O  
ATOM   1937  CB  ARG A 371      33.617  37.608  10.298  1.00 75.78           C  
ATOM   1938  CG  ARG A 371      33.756  37.084   8.888  1.00 75.78           C  
ATOM   1939  CD  ARG A 371      32.911  35.836   8.711  1.00 75.78           C  
ATOM   1940  NE  ARG A 371      33.475  34.929   7.716  1.00 75.78           N  
ATOM   1941  CZ  ARG A 371      33.113  33.659   7.582  1.00 75.78           C  
ATOM   1942  NH1 ARG A 371      32.186  33.145   8.381  1.00 75.78           N  
ATOM   1943  NH2 ARG A 371      33.674  32.903   6.651  1.00 75.78           N  
ATOM   1944  N   PRO A 372      33.270  40.664  11.839  1.00 71.93           N  
ATOM   1945  CA  PRO A 372      32.806  41.463  12.978  1.00 71.93           C  
ATOM   1946  C   PRO A 372      31.779  40.756  13.829  1.00 71.93           C  
ATOM   1947  O   PRO A 372      31.143  39.813  13.369  1.00 71.93           O  
ATOM   1948  CB  PRO A 372      32.222  42.722  12.339  1.00 81.48           C  
ATOM   1949  CG  PRO A 372      31.902  42.337  10.961  1.00 81.48           C  
ATOM   1950  CD  PRO A 372      32.902  41.279  10.557  1.00 81.48           C  
ATOM   1951  N   MET A 373      31.633  41.210  15.074  1.00109.25           N  
ATOM   1952  CA  MET A 373      30.563  40.742  15.944  1.00109.25           C  
ATOM   1953  C   MET A 373      29.339  41.623  15.729  1.00109.25           C  
ATOM   1954  O   MET A 373      29.453  42.781  15.318  1.00109.25           O  
ATOM   1955  CB  MET A 373      30.988  40.800  17.414  1.00194.29           C  
ATOM   1956  CG  MET A 373      30.588  39.566  18.233  1.00194.29           C  
ATOM   1957  SD  MET A 373      28.824  39.138  18.177  1.00194.29           S  
ATOM   1958  CE  MET A 373      28.785  37.627  19.158  1.00194.29           C  
ATOM   1959  N   LEU A 374      28.169  41.061  16.007  1.00 95.42           N  
ATOM   1960  CA  LEU A 374      26.916  41.699  15.650  1.00 95.42           C  
ATOM   1961  C   LEU A 374      26.847  43.099  16.251  1.00 95.42           C  
ATOM   1962  O   LEU A 374      26.300  44.024  15.646  1.00 95.42           O  
ATOM   1963  CB  LEU A 374      25.742  40.831  16.123  1.00130.55           C  
ATOM   1964  CG  LEU A 374      25.707  39.409  15.536  1.00130.55           C  
ATOM   1965  CD1 LEU A 374      26.245  38.414  16.542  1.00130.55           C  
ATOM   1966  CD2 LEU A 374      24.288  39.037  15.168  1.00130.55           C  
ATOM   1967  N   ARG A 375      27.430  43.258  17.435  1.00112.34           N  
ATOM   1968  CA  ARG A 375      27.476  44.563  18.079  1.00112.34           C  
ATOM   1969  C   ARG A 375      28.299  45.525  17.231  1.00112.34           C  
ATOM   1970  O   ARG A 375      27.923  46.684  17.057  1.00112.34           O  
ATOM   1971  CB  ARG A 375      28.072  44.446  19.491  1.00120.63           C  
ATOM   1972  CG  ARG A 375      27.047  44.172  20.598  1.00120.63           C  
ATOM   1973  CD  ARG A 375      25.803  43.455  20.066  1.00120.63           C  
ATOM   1974  NE  ARG A 375      25.731  42.051  20.474  1.00120.63           N  
ATOM   1975  CZ  ARG A 375      26.620  41.117  20.135  1.00120.63           C  
ATOM   1976  NH1 ARG A 375      27.665  41.430  19.380  1.00120.63           N  
ATOM   1977  NH2 ARG A 375      26.461  39.864  20.547  1.00120.63           N  
ATOM   1978  N   GLU A 376      29.414  45.043  16.693  1.00 92.12           N  
ATOM   1979  CA  GLU A 376      30.219  45.858  15.794  1.00 92.12           C  
ATOM   1980  C   GLU A 376      29.339  46.258  14.621  1.00 92.12           C  
ATOM   1981  O   GLU A 376      29.336  47.416  14.187  1.00 92.12           O  
ATOM   1982  CB  GLU A 376      31.417  45.068  15.268  1.00162.69           C  
ATOM   1983  CG  GLU A 376      32.484  44.764  16.299  1.00162.69           C  
ATOM   1984  CD  GLU A 376      33.568  43.845  15.762  1.00162.69           C  
ATOM   1985  OE1 GLU A 376      34.452  44.327  15.017  1.00162.69           O  
ATOM   1986  OE2 GLU A 376      33.534  42.639  16.087  1.00162.69           O  
ATOM   1987  N   VAL A 377      28.594  45.274  14.119  1.00126.73           N  
ATOM   1988  CA  VAL A 377      27.756  45.435  12.936  1.00126.73           C  
ATOM   1989  C   VAL A 377      26.724  46.508  13.215  1.00126.73           C  
ATOM   1990  O   VAL A 377      26.598  47.476  12.471  1.00126.73           O  
ATOM   1991  CB  VAL A 377      27.009  44.123  12.593  1.00110.52           C  
ATOM   1992  CG1 VAL A 377      26.281  44.272  11.276  1.00110.52           C  
ATOM   1993  CG2 VAL A 377      27.984  42.959  12.535  1.00110.52           C  
ATOM   1994  N   LEU A 378      25.992  46.328  14.305  1.00132.07           N  
ATOM   1995  CA  LEU A 378      24.978  47.288  14.703  1.00132.07           C  
ATOM   1996  C   LEU A 378      25.603  48.655  14.931  1.00132.07           C  
ATOM   1997  O   LEU A 378      24.904  49.664  14.997  1.00132.07           O  
ATOM   1998  CB  LEU A 378      24.274  46.798  15.968  1.00 76.59           C  
ATOM   1999  CG  LEU A 378      23.360  45.608  15.663  1.00 76.59           C  
ATOM   2000  CD1 LEU A 378      23.177  44.699  16.887  1.00 76.59           C  
ATOM   2001  CD2 LEU A 378      22.038  46.148  15.153  1.00 76.59           C  
ATOM   2002  N   GLU A 379      26.926  48.687  15.041  1.00 94.39           N  
ATOM   2003  CA  GLU A 379      27.622  49.948  15.196  1.00 94.39           C  
ATOM   2004  C   GLU A 379      27.866  50.617  13.847  1.00 94.39           C  
ATOM   2005  O   GLU A 379      27.574  51.794  13.686  1.00 94.39           O  
ATOM   2006  CB  GLU A 379      28.940  49.734  15.942  1.00203.22           C  
ATOM   2007  CG  GLU A 379      28.750  49.442  17.425  1.00203.22           C  
ATOM   2008  CD  GLU A 379      30.017  48.947  18.094  1.00203.22           C  
ATOM   2009  OE1 GLU A 379      30.887  48.397  17.386  1.00203.22           O  
ATOM   2010  OE2 GLU A 379      30.144  49.108  19.327  1.00203.22           O  
ATOM   2011  N   HIS A 380      28.380  49.866  12.878  1.00 84.43           N  
ATOM   2012  CA  HIS A 380      28.639  50.408  11.546  1.00 84.43           C  
ATOM   2013  C   HIS A 380      27.663  51.524  11.192  1.00 84.43           C  
ATOM   2014  O   HIS A 380      26.454  51.376  11.353  1.00 84.43           O  
ATOM   2015  CB  HIS A 380      28.546  49.305  10.488  1.00 93.91           C  
ATOM   2016  CG  HIS A 380      28.945  49.757   9.117  1.00 93.91           C  
ATOM   2017  ND1 HIS A 380      30.182  49.482   8.572  1.00 93.91           N  
ATOM   2018  CD2 HIS A 380      28.285  50.499   8.195  1.00 93.91           C  
ATOM   2019  CE1 HIS A 380      30.268  50.036   7.377  1.00 93.91           C  
ATOM   2020  NE2 HIS A 380      29.131  50.659   7.124  1.00 93.91           N  
ATOM   2021  N   PRO A 381      28.182  52.659  10.695  1.00103.29           N  
ATOM   2022  CA  PRO A 381      27.426  53.913  10.568  1.00103.29           C  
ATOM   2023  C   PRO A 381      26.266  53.806   9.597  1.00103.29           C  
ATOM   2024  O   PRO A 381      25.114  54.084   9.945  1.00103.29           O  
ATOM   2025  CB  PRO A 381      28.467  54.911  10.081  1.00102.82           C  
ATOM   2026  CG  PRO A 381      29.465  54.078   9.365  1.00102.82           C  
ATOM   2027  CD  PRO A 381      29.534  52.781  10.125  1.00102.82           C  
ATOM   2028  N   TRP A 382      26.590  53.415   8.372  1.00 81.76           N  
ATOM   2029  CA  TRP A 382      25.581  53.088   7.379  1.00 81.76           C  
ATOM   2030  C   TRP A 382      24.440  52.252   8.013  1.00 81.76           C  
ATOM   2031  O   TRP A 382      23.261  52.441   7.693  1.00 81.76           O  
ATOM   2032  CB  TRP A 382      26.264  52.331   6.237  1.00 95.04           C  
ATOM   2033  CG  TRP A 382      25.369  51.954   5.127  1.00 95.04           C  
ATOM   2034  CD1 TRP A 382      25.202  52.614   3.949  1.00 95.04           C  
ATOM   2035  CD2 TRP A 382      24.501  50.821   5.084  1.00 95.04           C  
ATOM   2036  NE1 TRP A 382      24.280  51.961   3.173  1.00 95.04           N  
ATOM   2037  CE2 TRP A 382      23.834  50.856   3.850  1.00 95.04           C  
ATOM   2038  CE3 TRP A 382      24.223  49.779   5.973  1.00 95.04           C  
ATOM   2039  CZ2 TRP A 382      22.902  49.887   3.481  1.00 95.04           C  
ATOM   2040  CZ3 TRP A 382      23.298  48.820   5.607  1.00 95.04           C  
ATOM   2041  CH2 TRP A 382      22.649  48.881   4.373  1.00 95.04           C  
ATOM   2042  N   ILE A 383      24.804  51.356   8.932  1.00 86.15           N  
ATOM   2043  CA  ILE A 383      23.846  50.474   9.596  1.00 86.15           C  
ATOM   2044  C   ILE A 383      22.965  51.157  10.640  1.00 86.15           C  
ATOM   2045  O   ILE A 383      22.033  50.549  11.175  1.00 86.15           O  
ATOM   2046  CB  ILE A 383      24.570  49.260  10.266  1.00109.21           C  
ATOM   2047  CG1 ILE A 383      24.468  48.025   9.363  1.00109.21           C  
ATOM   2048  CG2 ILE A 383      23.980  48.960  11.639  1.00109.21           C  
ATOM   2049  CD1 ILE A 383      23.043  47.564   9.085  1.00109.21           C  
ATOM   2050  N   THR A 384      23.244  52.421  10.929  1.00110.15           N  
ATOM   2051  CA  THR A 384      22.559  53.098  12.025  1.00110.15           C  
ATOM   2052  C   THR A 384      21.932  54.389  11.524  1.00110.15           C  
ATOM   2053  O   THR A 384      20.804  54.738  11.872  1.00110.15           O  
ATOM   2054  CB  THR A 384      23.543  53.434  13.138  1.00101.78           C  
ATOM   2055  OG1 THR A 384      24.473  54.406  12.655  1.00101.78           O  
ATOM   2056  CG2 THR A 384      24.319  52.190  13.555  1.00101.78           C  
ATOM   2057  N   ALA A 385      22.682  55.100  10.700  1.00 87.39           N  
ATOM   2058  CA  ALA A 385      22.151  56.268  10.038  1.00 87.39           C  
ATOM   2059  C   ALA A 385      21.183  55.812   8.961  1.00 87.39           C  
ATOM   2060  O   ALA A 385      20.823  56.595   8.082  1.00 87.39           O  
ATOM   2061  CB  ALA A 385      23.278  57.067   9.417  1.00115.24           C  
ATOM   2062  N   ASN A 386      20.781  54.539   9.014  1.00104.06           N  
ATOM   2063  CA  ASN A 386      19.869  53.978   8.014  1.00104.06           C  
ATOM   2064  C   ASN A 386      18.851  53.010   8.574  1.00104.06           C  
ATOM   2065  O   ASN A 386      17.846  52.724   7.927  1.00104.06           O  
ATOM   2066  CB  ASN A 386      20.640  53.267   6.912  1.00 80.00           C  
ATOM   2067  CG  ASN A 386      21.109  54.206   5.848  1.00 80.00           C  
ATOM   2068  OD1 ASN A 386      22.287  54.214   5.499  1.00 80.00           O  
ATOM   2069  ND2 ASN A 386      20.195  55.013   5.320  1.00 80.00           N  
ATOM   2070  N   SER A 387      19.120  52.496   9.767  1.00 98.80           N  
ATOM   2071  CA  SER A 387      18.198  51.580  10.427  1.00 98.80           C  
ATOM   2072  C   SER A 387      16.956  52.288  11.004  1.00 98.80           C  
ATOM   2073  O   SER A 387      16.315  53.103  10.332  1.00 98.80           O  
ATOM   2074  CB  SER A 387      18.933  50.830  11.539  1.00115.42           C  
ATOM   2075  OG  SER A 387      18.064  49.944  12.218  1.00115.42           O  
ATOM   2076  N   SER A 388      16.623  51.961  12.250  1.00192.23           N  
ATOM   2077  CA  SER A 388      15.442  52.499  12.917  1.00192.23           C  
ATOM   2078  C   SER A 388      15.412  52.016  14.357  1.00192.23           C  
ATOM   2079  O   SER A 388      15.148  52.835  15.266  1.00192.23           O  
ATOM   2080  CB  SER A 388      14.169  52.043  12.207  1.00 87.43           C  
ATOM   2081  OG  SER A 388      14.011  52.716  10.974  1.00 87.43           O  
ATOM   2082  N   LYS A 389      15.644  50.808  14.546  1.00 87.43           N  
TER    2083      LYS A 389                                                      
HETATM 2084  C1  400 A1389       3.747  31.647   7.932  1.00 44.10           C  
HETATM 2085  N2  400 A1389       3.563  31.950   9.242  1.00 44.10           N  
HETATM 2086  N3  400 A1389       4.381  31.243  10.000  1.00 44.10           N  
HETATM 2087  C4  400 A1389       4.755  30.678   7.885  1.00 44.10           C  
HETATM 2088  C5  400 A1389       5.137  30.446   9.194  1.00 44.10           C  
HETATM 2089  C6  400 A1389       6.165  29.503   9.318  1.00 44.10           C  
HETATM 2090  C7  400 A1389       6.571  29.016   8.049  1.00 44.10           C  
HETATM 2091  S8  400 A1389       5.642  29.720   6.727  1.00 44.10           S  
HETATM 2092  N9  400 A1389       3.009  32.269   7.000  1.00 44.10           N  
HETATM 2093  C10 400 A1389       3.183  32.386   5.641  1.00 44.10           C  
HETATM 2094  C11 400 A1389       2.554  33.451   4.855  1.00 44.10           C  
HETATM 2095  O12 400 A1389       3.906  31.514   5.041  1.00 44.10           O  
HETATM 2096  C13 400 A1389       1.611  34.390   5.417  1.00 44.10           C  
HETATM 2097  C14 400 A1389       1.024  35.408   4.620  1.00 44.10           C  
HETATM 2098  C15 400 A1389       1.332  35.562   3.199  1.00 44.10           C  
HETATM 2099  C16 400 A1389       2.267  34.622   2.643  1.00 44.10           C  
HETATM 2100  C17 400 A1389       2.855  33.605   3.441  1.00 44.10           C  
HETATM 2101  N18 400 A1389       0.751  36.581   2.435  1.00 44.10           N  
HETATM 2102  C19 400 A1389      -0.159  36.302   1.254  1.00 44.10           C  
HETATM 2103  C20 400 A1389      -0.035  37.364   0.085  1.00 44.10           C  
HETATM 2104  N21 400 A1389       0.044  38.780   0.677  1.00 44.10           N  
HETATM 2105  C22 400 A1389       1.247  38.878   1.589  1.00 44.10           C  
HETATM 2106  C23 400 A1389       0.974  37.995   2.821  1.00 44.10           C  
HETATM 2107  C24 400 A1389       0.098  39.848  -0.394  1.00 44.10           C  
HETATM 2108  C25 400 A1389       7.638  28.072   7.822  1.00 44.10           C  
HETATM 2109  O26 400 A1389       8.164  27.453   8.784  1.00 44.10           O  
HETATM 2110  N27 400 A1389       8.138  27.858   6.582  1.00 44.10           N  
HETATM 2111  C28 400 A1389       9.277  27.038   6.243  1.00 44.10           C  
HETATM 2112  C29 400 A1389       8.750  25.708   5.753  1.00 44.10           C  
HETATM 2113  C30 400 A1389      10.146  27.823   5.222  1.00 44.10           C  
HETATM 2114  C31 400 A1389       7.512  25.607   4.957  1.00 44.10           C  
HETATM 2115  C32 400 A1389       7.002  24.329   4.499  1.00 44.10           C  
HETATM 2116  C33 400 A1389       7.721  23.128   4.831  1.00 44.10           C  
HETATM 2117  C34 400 A1389       8.946  23.205   5.615  1.00 44.10           C  
HETATM 2118  C35 400 A1389       9.455  24.483   6.070  1.00 44.10           C  
HETATM 2119  C36 400 A1389      11.032  28.919   5.888  1.00 44.10           C  
CONECT 2084 2085 2087 2092                                                      
CONECT 2085 2084 2086                                                           
CONECT 2086 2085 2088                                                           
CONECT 2087 2084 2088 2091                                                      
CONECT 2088 2086 2087 2089                                                      
CONECT 2089 2088 2090                                                           
CONECT 2090 2089 2091 2108                                                      
CONECT 2091 2087 2090                                                           
CONECT 2092 2084 2093                                                           
CONECT 2093 2092 2094 2095                                                      
CONECT 2094 2093 2096 2100                                                      
CONECT 2095 2093                                                                
CONECT 2096 2094 2097                                                           
CONECT 2097 2096 2098                                                           
CONECT 2098 2097 2099 2101                                                      
CONECT 2099 2098 2100                                                           
CONECT 2100 2094 2099                                                           
CONECT 2101 2098 2102 2106                                                      
CONECT 2102 2101 2103                                                           
CONECT 2103 2102 2104                                                           
CONECT 2104 2103 2105 2107                                                      
CONECT 2105 2104 2106                                                           
CONECT 2106 2101 2105                                                           
CONECT 2107 2104                                                                
CONECT 2108 2090 2109 2110                                                      
CONECT 2109 2108                                                                
CONECT 2110 2108 2111                                                           
CONECT 2111 2110 2112 2113                                                      
CONECT 2112 2111 2114 2118                                                      
CONECT 2113 2111 2119                                                           
CONECT 2114 2112 2115                                                           
CONECT 2115 2114 2116                                                           
CONECT 2116 2115 2117                                                           
CONECT 2117 2116 2118                                                           
CONECT 2118 2112 2117                                                           
CONECT 2119 2113                                                                
MASTER      424    0    1   12    7    0    5    6 2118    1   36   22          
END                                                                             
