CNRS Nantes University UFIP UFIP
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***  miaA  ***

elNémo ID: 200528152247133928

Job options:

ID        	=	 200528152247133928
JOBID     	=	 miaA
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -200
DQMAX     	=	 200
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER miaA

HEADER    TRANSFERASE                             16-OCT-08   3EXA              
TITLE     CRYSTAL STRUCTURE OF THE FULL-LENGTH TRNA ISOPENTENYLPYROPHOSPHATE    
TITLE    2 TRANSFERASE (BH2366) FROM BACILLUS HALODURANS, NORTHEAST STRUCTURAL  
TITLE    3 GENOMICS CONSORTIUM TARGET BHR41.                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRNA DELTA(2)-ISOPENTENYLPYROPHOSPHATE TRANSFERASE;        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: IPP TRANSFERASE, ISOPENTENYL-DIPHOSPHATE:TRNA               
COMPND   5 ISOPENTENYLTRANSFERASE, IPTASE, IPPT;                                
COMPND   6 EC: 2.5.1.8;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS;                            
SOURCE   3 ORGANISM_TAXID: 86665;                                               
SOURCE   4 STRAIN: C-125;                                                       
SOURCE   5 GENE: BH2366, MIAA;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE     
KEYWDS   2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, ATP-     
KEYWDS   3 BINDING, NUCLEOTIDE-BINDING, NUCLEOTIDYLTRANSFERASE, TRANSFERASE,    
KEYWDS   4 TRNA PROCESSING                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FOROUHAR,M.ABASHIDZE,H.NEELY,J.SEETHARAMAN,R.SHASTRY,H.JANJUA,      
AUTHOR   2 K.CUNNINGHAM,L.-C.MA,R.XIAO,J.LIU,M.C.BARAN,T.B.ACTON,B.ROST,        
AUTHOR   3 G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST STRUCTURAL GENOMICS         
AUTHOR   4 CONSORTIUM (NESG)                                                    
REVDAT   4   24-JAN-18 3EXA    1       AUTHOR JRNL                              
REVDAT   3   25-OCT-17 3EXA    1       REMARK                                   
REVDAT   2   24-FEB-09 3EXA    1       VERSN                                    
REVDAT   1   11-NOV-08 3EXA    0                                                
JRNL        AUTH   F.FOROUHAR,M.ABASHIDZE,H.NEELY,J.SEETHARAMAN,R.SHASTRY,      
JRNL        AUTH 2 H.JANJUA,K.CUNNINGHAM,L.-C.MA,R.XIAO,J.LIU,M.C.BARAN,        
JRNL        AUTH 3 T.B.ACTON,B.ROST,G.T.MONTELIONE,L.TONG,J.F.HUNT              
JRNL        TITL   CRYSTAL STRUCTURE OF THE FULL-LENGTH TRNA                    
JRNL        TITL 2 ISOPENTENYLPYROPHOSPHATE TRANSFERASE (BH2366) FROM BACILLUS  
JRNL        TITL 3 HALODURANS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET  
JRNL        TITL 4 BHR41.                                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 375722.410                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 68.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 85837                          
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) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3936                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 50.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6088                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 286                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9684                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 565                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -10.72000                                            
REMARK   3    B22 (A**2) : 11.26000                                             
REMARK   3    B33 (A**2) : -0.54000                                             
REMARK   3    B12 (A**2) : -0.33000                                             
REMARK   3    B13 (A**2) : -3.68000                                             
REMARK   3    B23 (A**2) : 0.18000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
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) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.33                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.30                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 36.92                                                
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3EXA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049882.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9788                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89734                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.700                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 70.7                               
REMARK 200  DATA REDUNDANCY                : 1.500                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : 0.03800                            
REMARK 200   FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.08300                            
REMARK 200   FOR SHELL         : 5.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SNB THEN SOLVE/RESOLVE                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MM TRIS-HCL PH      
REMARK 280  (7.5), 100 MM NACL, 5 MM DTT, AND 0.025% (W/V) NAN3. RESERVOIR      
REMARK 280  SOLUTION: 16% PEG 3350 AND 200 MM AMMONIUM TARTRATE, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 7.5                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 300 REMARK: POSSIBLY MONOMER. HOWEVER IN BOTH CRYSTAL AND SOLUTION, THE  
REMARK 300 BH2366 MOLECULES PREDOMINANTLY EXIST AS DIMERS. AT PRESENT, IT IS    
REMARK 300 UNKNOWN WHAT ROLE AN APO BH266 DIMER PLAYS.                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 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     MSE A     1                                                      
REMARK 465     LYS A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     VAL A   176                                                      
REMARK 465     THR A   177                                                      
REMARK 465     GLU A   178                                                      
REMARK 465     GLN A   179                                                      
REMARK 465     ALA A   180                                                      
REMARK 465     ARG A   181                                                      
REMARK 465     HIS A   182                                                      
REMARK 465     GLU A   183                                                      
REMARK 465     GLU A   184                                                      
REMARK 465     GLU A   185                                                      
REMARK 465     THR A   186                                                      
REMARK 465     PRO A   187                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     LYS B   174                                                      
REMARK 465     THR B   175                                                      
REMARK 465     VAL B   176                                                      
REMARK 465     THR B   177                                                      
REMARK 465     GLU B   178                                                      
REMARK 465     GLN B   179                                                      
REMARK 465     ALA B   180                                                      
REMARK 465     ARG B   181                                                      
REMARK 465     HIS B   182                                                      
REMARK 465     GLU B   183                                                      
REMARK 465     GLU B   184                                                      
REMARK 465     GLU B   185                                                      
REMARK 465     THR B   186                                                      
REMARK 465     PRO B   187                                                      
REMARK 465     HIS B   318                                                      
REMARK 465     HIS B   319                                                      
REMARK 465     HIS B   320                                                      
REMARK 465     HIS B   321                                                      
REMARK 465     HIS B   322                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     LYS C   174                                                      
REMARK 465     THR C   175                                                      
REMARK 465     VAL C   176                                                      
REMARK 465     THR C   177                                                      
REMARK 465     GLU C   178                                                      
REMARK 465     GLN C   179                                                      
REMARK 465     ALA C   180                                                      
REMARK 465     ARG C   181                                                      
REMARK 465     HIS C   182                                                      
REMARK 465     GLU C   183                                                      
REMARK 465     GLU C   184                                                      
REMARK 465     GLU C   185                                                      
REMARK 465     THR C   186                                                      
REMARK 465     PRO C   187                                                      
REMARK 465     HIS C   319                                                      
REMARK 465     HIS C   320                                                      
REMARK 465     HIS C   321                                                      
REMARK 465     HIS C   322                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     LYS D   174                                                      
REMARK 465     THR D   175                                                      
REMARK 465     VAL D   176                                                      
REMARK 465     THR D   177                                                      
REMARK 465     GLU D   178                                                      
REMARK 465     GLN D   179                                                      
REMARK 465     ALA D   180                                                      
REMARK 465     ARG D   181                                                      
REMARK 465     HIS D   182                                                      
REMARK 465     GLU D   183                                                      
REMARK 465     GLU D   184                                                      
REMARK 465     GLU D   185                                                      
REMARK 465     THR D   186                                                      
REMARK 465     PRO D   187                                                      
REMARK 465     HIS D   318                                                      
REMARK 465     HIS D   319                                                      
REMARK 465     HIS D   320                                                      
REMARK 465     HIS D   321                                                      
REMARK 465     HIS D   322                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU D   128     O    HOH D   374              2.05            
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    ARG B 160   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG B 160   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG B 160   NE  -  CZ  -  NH2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG B 161   CD  -  NE  -  CZ  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG B 161   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG B 161   NE  -  CZ  -  NH2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG B 164   CD  -  NE  -  CZ  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG B 164   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG B 164   NE  -  CZ  -  NH2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG D 160   CD  -  NE  -  CZ  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG D 160   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG D 160   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG D 161   CD  -  NE  -  CZ  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG D 161   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG D 161   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG D 164   CD  -  NE  -  CZ  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG D 164   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG D 164   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.0 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    PRO A  11     -173.02    -65.48                                   
REMARK 500    ASN A  28       62.21     38.90                                   
REMARK 500    MSE A  43       78.85   -116.45                                   
REMARK 500    LEU A  62       30.95     72.68                                   
REMARK 500    ASP A 147       81.50    178.09                                   
REMARK 500    ALA A 152       -7.60    -57.67                                   
REMARK 500    ARG A 201      -70.33    -40.25                                   
REMARK 500    ILE A 241       50.89    -67.95                                   
REMARK 500    ASN A 283       19.56     82.84                                   
REMARK 500    THR A 290      102.47    -53.64                                   
REMARK 500    ASP A 291       58.96     21.66                                   
REMARK 500    PRO B  11     -173.23    -64.73                                   
REMARK 500    ASN B 113      -71.97    -68.36                                   
REMARK 500    TYR B 134     -142.81   -102.15                                   
REMARK 500    ASP B 147       75.95    173.85                                   
REMARK 500    THR B 172      -72.70    -50.36                                   
REMARK 500    MSE B 199      148.15   -175.36                                   
REMARK 500    ILE B 241       51.00    -67.21                                   
REMARK 500    VAL B 292       27.94    -77.82                                   
REMARK 500    PRO C  11     -172.70    -65.39                                   
REMARK 500    ASN C  28       62.96     38.49                                   
REMARK 500    MSE C  43       79.10   -115.79                                   
REMARK 500    LEU C  62       31.38     72.13                                   
REMARK 500    ASP C 147       81.72    178.20                                   
REMARK 500    ALA C 152       -7.39    -58.46                                   
REMARK 500    ASN C 158       59.96    -95.94                                   
REMARK 500    ARG C 201      -70.47    -40.93                                   
REMARK 500    ILE C 241       50.37    -67.28                                   
REMARK 500    ASN C 283       19.64     83.02                                   
REMARK 500    THR C 290      102.40    -54.39                                   
REMARK 500    ASP C 291       59.35     21.90                                   
REMARK 500    PRO D  11     -173.78    -64.79                                   
REMARK 500    ASN D 113      -72.34    -68.35                                   
REMARK 500    TYR D 134     -143.22   -101.94                                   
REMARK 500    ASP D 147       75.97    173.15                                   
REMARK 500    THR D 172      -72.46    -50.42                                   
REMARK 500    MSE D 199      148.91   -175.56                                   
REMARK 500    ILE D 241       51.90    -68.19                                   
REMARK 500    VAL D 292       28.05    -77.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QGN   RELATED DB: PDB                                   
REMARK 900 THE CURRENT STRUCTURE IS THE FULL-LENGTH STRUCTURE CONTAINING BOTH   
REMARK 900 THE CATALYTIC AND TRNA-BINDING DOMAINS, WHEREAS 2QGN IS THE          
REMARK 900 STRUCTURE OF THE CATALYTIC DOMAIN.                                   
REMARK 900 RELATED ID: BHR41   RELATED DB: TARGETDB                             
DBREF  3EXA A    1   314  UNP    Q9KAC3   MIAA_BACHD       1    314             
DBREF  3EXA B    1   314  UNP    Q9KAC3   MIAA_BACHD       1    314             
DBREF  3EXA C    1   314  UNP    Q9KAC3   MIAA_BACHD       1    314             
DBREF  3EXA D    1   314  UNP    Q9KAC3   MIAA_BACHD       1    314             
SEQADV 3EXA LEU A  315  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA GLU A  316  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS A  317  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS A  318  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS A  319  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS A  320  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS A  321  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS A  322  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA LEU B  315  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA GLU B  316  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS B  317  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS B  318  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS B  319  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS B  320  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS B  321  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS B  322  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA LEU C  315  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA GLU C  316  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS C  317  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS C  318  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS C  319  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS C  320  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS C  321  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS C  322  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA LEU D  315  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA GLU D  316  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS D  317  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS D  318  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS D  319  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS D  320  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS D  321  UNP  Q9KAC3              EXPRESSION TAG                 
SEQADV 3EXA HIS D  322  UNP  Q9KAC3              EXPRESSION TAG                 
SEQRES   1 A  322  MSE LYS GLU LYS LEU VAL ALA ILE VAL GLY PRO THR ALA          
SEQRES   2 A  322  VAL GLY LYS THR LYS THR SER VAL MSE LEU ALA LYS ARG          
SEQRES   3 A  322  LEU ASN GLY GLU VAL ILE SER GLY ASP SER MSE GLN VAL          
SEQRES   4 A  322  TYR ARG GLY MSE ASP ILE GLY THR ALA LYS ILE THR ALA          
SEQRES   5 A  322  GLU GLU MSE ASP GLY VAL PRO HIS HIS LEU ILE ASP ILE          
SEQRES   6 A  322  LYS ASP PRO SER GLU SER PHE SER VAL ALA ASP PHE GLN          
SEQRES   7 A  322  ASP LEU ALA THR PRO LEU ILE THR GLU ILE HIS GLU ARG          
SEQRES   8 A  322  GLY ARG LEU PRO PHE LEU VAL GLY GLY THR GLY LEU TYR          
SEQRES   9 A  322  VAL ASN ALA VAL ILE HIS GLN PHE ASN LEU GLY ASP ILE          
SEQRES  10 A  322  ARG ALA ASP GLU ASP TYR ARG HIS GLU LEU GLU ALA PHE          
SEQRES  11 A  322  VAL ASN SER TYR GLY VAL GLN ALA LEU HIS ASP LYS LEU          
SEQRES  12 A  322  SER LYS ILE ASP PRO LYS ALA ALA ALA ALA ILE HIS PRO          
SEQRES  13 A  322  ASN ASN TYR ARG ARG VAL ILE ARG ALA LEU GLU ILE ILE          
SEQRES  14 A  322  LYS LEU THR GLY LYS THR VAL THR GLU GLN ALA ARG HIS          
SEQRES  15 A  322  GLU GLU GLU THR PRO SER PRO TYR ASN LEU VAL MSE ILE          
SEQRES  16 A  322  GLY LEU THR MSE GLU ARG ASP VAL LEU TYR ASP ARG ILE          
SEQRES  17 A  322  ASN ARG ARG VAL ASP GLN MSE VAL GLU GLU GLY LEU ILE          
SEQRES  18 A  322  ASP GLU ALA LYS LYS LEU TYR ASP ARG GLY ILE ARG ASP          
SEQRES  19 A  322  CYS GLN SER VAL GLN ALA ILE GLY TYR LYS GLU MSE TYR          
SEQRES  20 A  322  ASP TYR LEU ASP GLY ASN VAL THR LEU GLU GLU ALA ILE          
SEQRES  21 A  322  ASP THR LEU LYS ARG ASN SER ARG ARG TYR ALA LYS ARG          
SEQRES  22 A  322  GLN LEU THR TRP PHE ARG ASN LYS ALA ASN VAL THR TRP          
SEQRES  23 A  322  PHE ASP MSE THR ASP VAL ASP PHE ASP LYS LYS ILE MSE          
SEQRES  24 A  322  GLU ILE HIS ASN PHE ILE ALA GLY LYS LEU GLU GLU LYS          
SEQRES  25 A  322  SER LYS LEU GLU HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  322  MSE LYS GLU LYS LEU VAL ALA ILE VAL GLY PRO THR ALA          
SEQRES   2 B  322  VAL GLY LYS THR LYS THR SER VAL MSE LEU ALA LYS ARG          
SEQRES   3 B  322  LEU ASN GLY GLU VAL ILE SER GLY ASP SER MSE GLN VAL          
SEQRES   4 B  322  TYR ARG GLY MSE ASP ILE GLY THR ALA LYS ILE THR ALA          
SEQRES   5 B  322  GLU GLU MSE ASP GLY VAL PRO HIS HIS LEU ILE ASP ILE          
SEQRES   6 B  322  LYS ASP PRO SER GLU SER PHE SER VAL ALA ASP PHE GLN          
SEQRES   7 B  322  ASP LEU ALA THR PRO LEU ILE THR GLU ILE HIS GLU ARG          
SEQRES   8 B  322  GLY ARG LEU PRO PHE LEU VAL GLY GLY THR GLY LEU TYR          
SEQRES   9 B  322  VAL ASN ALA VAL ILE HIS GLN PHE ASN LEU GLY ASP ILE          
SEQRES  10 B  322  ARG ALA ASP GLU ASP TYR ARG HIS GLU LEU GLU ALA PHE          
SEQRES  11 B  322  VAL ASN SER TYR GLY VAL GLN ALA LEU HIS ASP LYS LEU          
SEQRES  12 B  322  SER LYS ILE ASP PRO LYS ALA ALA ALA ALA ILE HIS PRO          
SEQRES  13 B  322  ASN ASN TYR ARG ARG VAL ILE ARG ALA LEU GLU ILE ILE          
SEQRES  14 B  322  LYS LEU THR GLY LYS THR VAL THR GLU GLN ALA ARG HIS          
SEQRES  15 B  322  GLU GLU GLU THR PRO SER PRO TYR ASN LEU VAL MSE ILE          
SEQRES  16 B  322  GLY LEU THR MSE GLU ARG ASP VAL LEU TYR ASP ARG ILE          
SEQRES  17 B  322  ASN ARG ARG VAL ASP GLN MSE VAL GLU GLU GLY LEU ILE          
SEQRES  18 B  322  ASP GLU ALA LYS LYS LEU TYR ASP ARG GLY ILE ARG ASP          
SEQRES  19 B  322  CYS GLN SER VAL GLN ALA ILE GLY TYR LYS GLU MSE TYR          
SEQRES  20 B  322  ASP TYR LEU ASP GLY ASN VAL THR LEU GLU GLU ALA ILE          
SEQRES  21 B  322  ASP THR LEU LYS ARG ASN SER ARG ARG TYR ALA LYS ARG          
SEQRES  22 B  322  GLN LEU THR TRP PHE ARG ASN LYS ALA ASN VAL THR TRP          
SEQRES  23 B  322  PHE ASP MSE THR ASP VAL ASP PHE ASP LYS LYS ILE MSE          
SEQRES  24 B  322  GLU ILE HIS ASN PHE ILE ALA GLY LYS LEU GLU GLU LYS          
SEQRES  25 B  322  SER LYS LEU GLU HIS HIS HIS HIS HIS HIS                      
SEQRES   1 C  322  MSE LYS GLU LYS LEU VAL ALA ILE VAL GLY PRO THR ALA          
SEQRES   2 C  322  VAL GLY LYS THR LYS THR SER VAL MSE LEU ALA LYS ARG          
SEQRES   3 C  322  LEU ASN GLY GLU VAL ILE SER GLY ASP SER MSE GLN VAL          
SEQRES   4 C  322  TYR ARG GLY MSE ASP ILE GLY THR ALA LYS ILE THR ALA          
SEQRES   5 C  322  GLU GLU MSE ASP GLY VAL PRO HIS HIS LEU ILE ASP ILE          
SEQRES   6 C  322  LYS ASP PRO SER GLU SER PHE SER VAL ALA ASP PHE GLN          
SEQRES   7 C  322  ASP LEU ALA THR PRO LEU ILE THR GLU ILE HIS GLU ARG          
SEQRES   8 C  322  GLY ARG LEU PRO PHE LEU VAL GLY GLY THR GLY LEU TYR          
SEQRES   9 C  322  VAL ASN ALA VAL ILE HIS GLN PHE ASN LEU GLY ASP ILE          
SEQRES  10 C  322  ARG ALA ASP GLU ASP TYR ARG HIS GLU LEU GLU ALA PHE          
SEQRES  11 C  322  VAL ASN SER TYR GLY VAL GLN ALA LEU HIS ASP LYS LEU          
SEQRES  12 C  322  SER LYS ILE ASP PRO LYS ALA ALA ALA ALA ILE HIS PRO          
SEQRES  13 C  322  ASN ASN TYR ARG ARG VAL ILE ARG ALA LEU GLU ILE ILE          
SEQRES  14 C  322  LYS LEU THR GLY LYS THR VAL THR GLU GLN ALA ARG HIS          
SEQRES  15 C  322  GLU GLU GLU THR PRO SER PRO TYR ASN LEU VAL MSE ILE          
SEQRES  16 C  322  GLY LEU THR MSE GLU ARG ASP VAL LEU TYR ASP ARG ILE          
SEQRES  17 C  322  ASN ARG ARG VAL ASP GLN MSE VAL GLU GLU GLY LEU ILE          
SEQRES  18 C  322  ASP GLU ALA LYS LYS LEU TYR ASP ARG GLY ILE ARG ASP          
SEQRES  19 C  322  CYS GLN SER VAL GLN ALA ILE GLY TYR LYS GLU MSE TYR          
SEQRES  20 C  322  ASP TYR LEU ASP GLY ASN VAL THR LEU GLU GLU ALA ILE          
SEQRES  21 C  322  ASP THR LEU LYS ARG ASN SER ARG ARG TYR ALA LYS ARG          
SEQRES  22 C  322  GLN LEU THR TRP PHE ARG ASN LYS ALA ASN VAL THR TRP          
SEQRES  23 C  322  PHE ASP MSE THR ASP VAL ASP PHE ASP LYS LYS ILE MSE          
SEQRES  24 C  322  GLU ILE HIS ASN PHE ILE ALA GLY LYS LEU GLU GLU LYS          
SEQRES  25 C  322  SER LYS LEU GLU HIS HIS HIS HIS HIS HIS                      
SEQRES   1 D  322  MSE LYS GLU LYS LEU VAL ALA ILE VAL GLY PRO THR ALA          
SEQRES   2 D  322  VAL GLY LYS THR LYS THR SER VAL MSE LEU ALA LYS ARG          
SEQRES   3 D  322  LEU ASN GLY GLU VAL ILE SER GLY ASP SER MSE GLN VAL          
SEQRES   4 D  322  TYR ARG GLY MSE ASP ILE GLY THR ALA LYS ILE THR ALA          
SEQRES   5 D  322  GLU GLU MSE ASP GLY VAL PRO HIS HIS LEU ILE ASP ILE          
SEQRES   6 D  322  LYS ASP PRO SER GLU SER PHE SER VAL ALA ASP PHE GLN          
SEQRES   7 D  322  ASP LEU ALA THR PRO LEU ILE THR GLU ILE HIS GLU ARG          
SEQRES   8 D  322  GLY ARG LEU PRO PHE LEU VAL GLY GLY THR GLY LEU TYR          
SEQRES   9 D  322  VAL ASN ALA VAL ILE HIS GLN PHE ASN LEU GLY ASP ILE          
SEQRES  10 D  322  ARG ALA ASP GLU ASP TYR ARG HIS GLU LEU GLU ALA PHE          
SEQRES  11 D  322  VAL ASN SER TYR GLY VAL GLN ALA LEU HIS ASP LYS LEU          
SEQRES  12 D  322  SER LYS ILE ASP PRO LYS ALA ALA ALA ALA ILE HIS PRO          
SEQRES  13 D  322  ASN ASN TYR ARG ARG VAL ILE ARG ALA LEU GLU ILE ILE          
SEQRES  14 D  322  LYS LEU THR GLY LYS THR VAL THR GLU GLN ALA ARG HIS          
SEQRES  15 D  322  GLU GLU GLU THR PRO SER PRO TYR ASN LEU VAL MSE ILE          
SEQRES  16 D  322  GLY LEU THR MSE GLU ARG ASP VAL LEU TYR ASP ARG ILE          
SEQRES  17 D  322  ASN ARG ARG VAL ASP GLN MSE VAL GLU GLU GLY LEU ILE          
SEQRES  18 D  322  ASP GLU ALA LYS LYS LEU TYR ASP ARG GLY ILE ARG ASP          
SEQRES  19 D  322  CYS GLN SER VAL GLN ALA ILE GLY TYR LYS GLU MSE TYR          
SEQRES  20 D  322  ASP TYR LEU ASP GLY ASN VAL THR LEU GLU GLU ALA ILE          
SEQRES  21 D  322  ASP THR LEU LYS ARG ASN SER ARG ARG TYR ALA LYS ARG          
SEQRES  22 D  322  GLN LEU THR TRP PHE ARG ASN LYS ALA ASN VAL THR TRP          
SEQRES  23 D  322  PHE ASP MSE THR ASP VAL ASP PHE ASP LYS LYS ILE MSE          
SEQRES  24 D  322  GLU ILE HIS ASN PHE ILE ALA GLY LYS LEU GLU GLU LYS          
SEQRES  25 D  322  SER LYS LEU GLU HIS HIS HIS HIS HIS HIS                      
MODRES 3EXA MSE A   22  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE A   37  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE A   43  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE A   55  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE A  194  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE A  199  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE A  215  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE A  246  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE A  289  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE A  299  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B   22  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B   37  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B   43  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B   55  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B  194  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B  199  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B  215  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B  246  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B  289  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE B  299  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C   22  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C   37  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C   43  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C   55  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C  194  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C  199  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C  215  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C  246  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C  289  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE C  299  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D   22  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D   37  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D   43  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D   55  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D  194  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D  199  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D  215  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D  246  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D  289  MET  SELENOMETHIONINE                                   
MODRES 3EXA MSE D  299  MET  SELENOMETHIONINE                                   
HET    MSE  A  22       8                                                       
HET    MSE  A  37       8                                                       
HET    MSE  A  43       8                                                       
HET    MSE  A  55       8                                                       
HET    MSE  A 194       8                                                       
HET    MSE  A 199       8                                                       
HET    MSE  A 215       8                                                       
HET    MSE  A 246       8                                                       
HET    MSE  A 289       8                                                       
HET    MSE  A 299       8                                                       
HET    MSE  B  22       8                                                       
HET    MSE  B  37       8                                                       
HET    MSE  B  43       8                                                       
HET    MSE  B  55       8                                                       
HET    MSE  B 194       8                                                       
HET    MSE  B 199       8                                                       
HET    MSE  B 215       8                                                       
HET    MSE  B 246       8                                                       
HET    MSE  B 289       8                                                       
HET    MSE  B 299       8                                                       
HET    MSE  C  22       8                                                       
HET    MSE  C  37       8                                                       
HET    MSE  C  43       8                                                       
HET    MSE  C  55       8                                                       
HET    MSE  C 194       8                                                       
HET    MSE  C 199       8                                                       
HET    MSE  C 215       8                                                       
HET    MSE  C 246       8                                                       
HET    MSE  C 289       8                                                       
HET    MSE  C 299       8                                                       
HET    MSE  D  22       8                                                       
HET    MSE  D  37       8                                                       
HET    MSE  D  43       8                                                       
HET    MSE  D  55       8                                                       
HET    MSE  D 194       8                                                       
HET    MSE  D 199       8                                                       
HET    MSE  D 215       8                                                       
HET    MSE  D 246       8                                                       
HET    MSE  D 289       8                                                       
HET    MSE  D 299       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    40(C5 H11 N O2 SE)                                           
FORMUL   5  HOH   *565(H2 O)                                                    
HELIX    1   1 GLY A   15  ARG A   26  1                                  12    
HELIX    2   2 ASP A   35  TYR A   40  5                                   6    
HELIX    3   3 THR A   51  ASP A   56  1                                   6    
HELIX    4   4 SER A   73  ARG A   91  1                                  19    
HELIX    5   5 THR A  101  GLN A  111  1                                  11    
HELIX    6   6 ASP A  120  TYR A  134  1                                  15    
HELIX    7   7 GLY A  135  LYS A  145  1                                  11    
HELIX    8   8 ASP A  147  ALA A  152  1                                   6    
HELIX    9   9 ASN A  158  THR A  172  1                                  15    
HELIX   10  10 GLU A  200  GLY A  219  1                                  20    
HELIX   11  11 GLY A  219  ARG A  230  1                                  12    
HELIX   12  12 GLN A  236  ALA A  240  5                                   5    
HELIX   13  13 TYR A  243  ASP A  251  1                                   9    
HELIX   14  14 THR A  255  ASN A  280  1                                  26    
HELIX   15  15 ASP A  293  HIS A  318  1                                  26    
HELIX   16  16 GLY B   15  ARG B   26  1                                  12    
HELIX   17  17 THR B   51  ASP B   56  1                                   6    
HELIX   18  18 SER B   73  ARG B   91  1                                  19    
HELIX   19  19 THR B  101  HIS B  110  1                                  10    
HELIX   20  20 ASP B  120  TYR B  134  1                                  15    
HELIX   21  21 GLY B  135  LYS B  145  1                                  11    
HELIX   22  22 ASP B  147  ALA B  152  1                                   6    
HELIX   23  23 ASN B  158  GLY B  173  1                                  16    
HELIX   24  24 GLU B  200  GLY B  219  1                                  20    
HELIX   25  25 GLY B  219  ARG B  230  1                                  12    
HELIX   26  26 CYS B  235  ALA B  240  1                                   6    
HELIX   27  27 TYR B  243  ASP B  251  1                                   9    
HELIX   28  28 THR B  255  ASN B  280  1                                  26    
HELIX   29  29 ASP B  293  HIS B  317  1                                  25    
HELIX   30  30 GLY C   15  ARG C   26  1                                  12    
HELIX   31  31 ASP C   35  TYR C   40  5                                   6    
HELIX   32  32 THR C   51  ASP C   56  1                                   6    
HELIX   33  33 SER C   73  ARG C   91  1                                  19    
HELIX   34  34 THR C  101  GLN C  111  1                                  11    
HELIX   35  35 ASP C  120  TYR C  134  1                                  15    
HELIX   36  36 GLY C  135  LYS C  145  1                                  11    
HELIX   37  37 ASP C  147  ALA C  152  1                                   6    
HELIX   38  38 ASN C  158  THR C  172  1                                  15    
HELIX   39  39 GLU C  200  GLY C  219  1                                  20    
HELIX   40  40 GLY C  219  ARG C  230  1                                  12    
HELIX   41  41 GLN C  236  ALA C  240  5                                   5    
HELIX   42  42 TYR C  243  ASP C  251  1                                   9    
HELIX   43  43 THR C  255  ASN C  280  1                                  26    
HELIX   44  44 ASP C  293  HIS C  318  1                                  26    
HELIX   45  45 GLY D   15  ARG D   26  1                                  12    
HELIX   46  46 THR D   51  ASP D   56  1                                   6    
HELIX   47  47 SER D   73  ARG D   91  1                                  19    
HELIX   48  48 THR D  101  HIS D  110  1                                  10    
HELIX   49  49 ASP D  120  TYR D  134  1                                  15    
HELIX   50  50 GLY D  135  LYS D  145  1                                  11    
HELIX   51  51 ASP D  147  ALA D  152  1                                   6    
HELIX   52  52 ASN D  158  GLY D  173  1                                  16    
HELIX   53  53 GLU D  200  GLY D  219  1                                  20    
HELIX   54  54 GLY D  219  ARG D  230  1                                  12    
HELIX   55  55 CYS D  235  ALA D  240  1                                   6    
HELIX   56  56 TYR D  243  ASP D  251  1                                   9    
HELIX   57  57 THR D  255  ASN D  280  1                                  26    
HELIX   58  58 ASP D  293  HIS D  317  1                                  25    
SHEET    1   A 6 HIS A  60  HIS A  61  0                                        
SHEET    2   A 6 GLY A  29  SER A  33  1  N  VAL A  31   O  HIS A  61           
SHEET    3   A 6 LEU A  94  VAL A  98  1  O  PHE A  96   N  ILE A  32           
SHEET    4   A 6 LYS A   4  VAL A   9  1  N  VAL A   6   O  LEU A  97           
SHEET    5   A 6 ASN A 191  THR A 198  1  O  VAL A 193   N  ALA A   7           
SHEET    6   A 6 VAL A 284  ASP A 288  1  O  THR A 285   N  GLY A 196           
SHEET    1   B 6 HIS B  60  HIS B  61  0                                        
SHEET    2   B 6 GLY B  29  SER B  33  1  N  VAL B  31   O  HIS B  61           
SHEET    3   B 6 LEU B  94  VAL B  98  1  O  PHE B  96   N  ILE B  32           
SHEET    4   B 6 LYS B   4  VAL B   9  1  N  VAL B   6   O  LEU B  97           
SHEET    5   B 6 ASN B 191  THR B 198  1  O  VAL B 193   N  ALA B   7           
SHEET    6   B 6 THR B 285  ASP B 288  1  O  THR B 285   N  MSE B 194           
SHEET    1   C 6 HIS C  60  HIS C  61  0                                        
SHEET    2   C 6 GLY C  29  SER C  33  1  N  VAL C  31   O  HIS C  61           
SHEET    3   C 6 LEU C  94  VAL C  98  1  O  PHE C  96   N  ILE C  32           
SHEET    4   C 6 LYS C   4  VAL C   9  1  N  VAL C   6   O  LEU C  97           
SHEET    5   C 6 ASN C 191  THR C 198  1  O  VAL C 193   N  ALA C   7           
SHEET    6   C 6 VAL C 284  ASP C 288  1  O  THR C 285   N  GLY C 196           
SHEET    1   D 6 HIS D  60  HIS D  61  0                                        
SHEET    2   D 6 GLY D  29  SER D  33  1  N  SER D  33   O  HIS D  61           
SHEET    3   D 6 LEU D  94  VAL D  98  1  O  PHE D  96   N  ILE D  32           
SHEET    4   D 6 LYS D   4  VAL D   9  1  N  VAL D   6   O  LEU D  97           
SHEET    5   D 6 ASN D 191  THR D 198  1  O  VAL D 193   N  ALA D   7           
SHEET    6   D 6 THR D 285  ASP D 288  1  O  PHE D 287   N  GLY D 196           
LINK         C   VAL A  21                 N   MSE A  22     1555   1555  1.33  
LINK         C   MSE A  22                 N   LEU A  23     1555   1555  1.33  
LINK         C   SER A  36                 N   MSE A  37     1555   1555  1.33  
LINK         C   MSE A  37                 N   GLN A  38     1555   1555  1.33  
LINK         C   GLY A  42                 N   MSE A  43     1555   1555  1.33  
LINK         C   MSE A  43                 N   ASP A  44     1555   1555  1.33  
LINK         C   GLU A  54                 N   MSE A  55     1555   1555  1.33  
LINK         C   MSE A  55                 N   ASP A  56     1555   1555  1.33  
LINK         C   VAL A 193                 N   MSE A 194     1555   1555  1.33  
LINK         C   MSE A 194                 N   ILE A 195     1555   1555  1.33  
LINK         C   THR A 198                 N   MSE A 199     1555   1555  1.33  
LINK         C   MSE A 199                 N   GLU A 200     1555   1555  1.33  
LINK         C   GLN A 214                 N   MSE A 215     1555   1555  1.33  
LINK         C   MSE A 215                 N   VAL A 216     1555   1555  1.33  
LINK         C   GLU A 245                 N   MSE A 246     1555   1555  1.33  
LINK         C   MSE A 246                 N   TYR A 247     1555   1555  1.33  
LINK         C   ASP A 288                 N   MSE A 289     1555   1555  1.33  
LINK         C   MSE A 289                 N   THR A 290     1555   1555  1.33  
LINK         C   ILE A 298                 N   MSE A 299     1555   1555  1.33  
LINK         C   MSE A 299                 N   GLU A 300     1555   1555  1.33  
LINK         C   VAL B  21                 N   MSE B  22     1555   1555  1.33  
LINK         C   MSE B  22                 N   LEU B  23     1555   1555  1.33  
LINK         C   SER B  36                 N   MSE B  37     1555   1555  1.33  
LINK         C   MSE B  37                 N   GLN B  38     1555   1555  1.33  
LINK         C   GLY B  42                 N   MSE B  43     1555   1555  1.33  
LINK         C   MSE B  43                 N   ASP B  44     1555   1555  1.33  
LINK         C   GLU B  54                 N   MSE B  55     1555   1555  1.33  
LINK         C   MSE B  55                 N   ASP B  56     1555   1555  1.33  
LINK         C   VAL B 193                 N   MSE B 194     1555   1555  1.33  
LINK         C   MSE B 194                 N   ILE B 195     1555   1555  1.33  
LINK         C   THR B 198                 N   MSE B 199     1555   1555  1.33  
LINK         C   MSE B 199                 N   GLU B 200     1555   1555  1.33  
LINK         C   GLN B 214                 N   MSE B 215     1555   1555  1.33  
LINK         C   MSE B 215                 N   VAL B 216     1555   1555  1.33  
LINK         C   GLU B 245                 N   MSE B 246     1555   1555  1.33  
LINK         C   MSE B 246                 N   TYR B 247     1555   1555  1.33  
LINK         C   ASP B 288                 N   MSE B 289     1555   1555  1.33  
LINK         C   MSE B 289                 N   THR B 290     1555   1555  1.33  
LINK         C   ILE B 298                 N   MSE B 299     1555   1555  1.33  
LINK         C   MSE B 299                 N   GLU B 300     1555   1555  1.33  
LINK         C   VAL C  21                 N   MSE C  22     1555   1555  1.33  
LINK         C   MSE C  22                 N   LEU C  23     1555   1555  1.33  
LINK         C   SER C  36                 N   MSE C  37     1555   1555  1.33  
LINK         C   MSE C  37                 N   GLN C  38     1555   1555  1.33  
LINK         C   GLY C  42                 N   MSE C  43     1555   1555  1.33  
LINK         C   MSE C  43                 N   ASP C  44     1555   1555  1.33  
LINK         C   GLU C  54                 N   MSE C  55     1555   1555  1.33  
LINK         C   MSE C  55                 N   ASP C  56     1555   1555  1.33  
LINK         C   VAL C 193                 N   MSE C 194     1555   1555  1.33  
LINK         C   MSE C 194                 N   ILE C 195     1555   1555  1.33  
LINK         C   THR C 198                 N   MSE C 199     1555   1555  1.33  
LINK         C   MSE C 199                 N   GLU C 200     1555   1555  1.33  
LINK         C   GLN C 214                 N   MSE C 215     1555   1555  1.33  
LINK         C   MSE C 215                 N   VAL C 216     1555   1555  1.33  
LINK         C   GLU C 245                 N   MSE C 246     1555   1555  1.33  
LINK         C   MSE C 246                 N   TYR C 247     1555   1555  1.33  
LINK         C   ASP C 288                 N   MSE C 289     1555   1555  1.33  
LINK         C   MSE C 289                 N   THR C 290     1555   1555  1.33  
LINK         C   ILE C 298                 N   MSE C 299     1555   1555  1.33  
LINK         C   MSE C 299                 N   GLU C 300     1555   1555  1.33  
LINK         C   VAL D  21                 N   MSE D  22     1555   1555  1.33  
LINK         C   MSE D  22                 N   LEU D  23     1555   1555  1.33  
LINK         C   SER D  36                 N   MSE D  37     1555   1555  1.33  
LINK         C   MSE D  37                 N   GLN D  38     1555   1555  1.33  
LINK         C   GLY D  42                 N   MSE D  43     1555   1555  1.33  
LINK         C   MSE D  43                 N   ASP D  44     1555   1555  1.33  
LINK         C   GLU D  54                 N   MSE D  55     1555   1555  1.33  
LINK         C   MSE D  55                 N   ASP D  56     1555   1555  1.33  
LINK         C   VAL D 193                 N   MSE D 194     1555   1555  1.33  
LINK         C   MSE D 194                 N   ILE D 195     1555   1555  1.33  
LINK         C   THR D 198                 N   MSE D 199     1555   1555  1.33  
LINK         C   MSE D 199                 N   GLU D 200     1555   1555  1.33  
LINK         C   GLN D 214                 N   MSE D 215     1555   1555  1.33  
LINK         C   MSE D 215                 N   VAL D 216     1555   1555  1.33  
LINK         C   GLU D 245                 N   MSE D 246     1555   1555  1.33  
LINK         C   MSE D 246                 N   TYR D 247     1555   1555  1.33  
LINK         C   ASP D 288                 N   MSE D 289     1555   1555  1.33  
LINK         C   MSE D 289                 N   THR D 290     1555   1555  1.33  
LINK         C   ILE D 298                 N   MSE D 299     1555   1555  1.33  
LINK         C   MSE D 299                 N   GLU D 300     1555   1555  1.33  
CRYST1   51.805   73.824   95.561  89.99  93.73  90.02 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019303  0.000007  0.001259        0.00000                         
SCALE2      0.000000  0.013546 -0.000003        0.00000                         
SCALE3      0.000000  0.000000  0.010487        0.00000                         
ATOM      1  N   LYS A   2      13.226  46.397  33.422  1.00 31.24           N  
ATOM      2  CA  LYS A   2      14.645  46.092  33.082  1.00 34.73           C  
ATOM      3  C   LYS A   2      15.067  46.747  31.773  1.00 33.92           C  
ATOM      4  O   LYS A   2      14.235  47.003  30.901  1.00 37.10           O  
ATOM      5  CB  LYS A   2      14.857  44.583  32.926  1.00 39.37           C  
ATOM      6  CG  LYS A   2      14.499  43.721  34.119  1.00 35.51           C  
ATOM      7  CD  LYS A   2      14.805  42.259  33.798  1.00 41.31           C  
ATOM      8  CE  LYS A   2      14.443  41.335  34.951  1.00 51.61           C  
ATOM      9  NZ  LYS A   2      12.975  41.363  35.225  1.00 51.04           N  
ATOM     10  N   GLU A   3      16.362  47.027  31.651  1.00 35.72           N  
ATOM     11  CA  GLU A   3      16.927  47.584  30.423  1.00 32.49           C  
ATOM     12  C   GLU A   3      16.794  46.509  29.340  1.00 29.01           C  
ATOM     13  O   GLU A   3      17.077  45.332  29.582  1.00 21.48           O  
ATOM     14  CB  GLU A   3      18.416  47.906  30.600  1.00 33.88           C  
ATOM     15  CG  GLU A   3      18.746  49.220  31.289  1.00 31.21           C  
ATOM     16  CD  GLU A   3      20.244  49.408  31.494  1.00 32.56           C  
ATOM     17  OE1 GLU A   3      21.024  49.060  30.583  1.00 35.98           O  
ATOM     18  OE2 GLU A   3      20.650  49.913  32.563  1.00 47.14           O  
ATOM     19  N   LYS A   4      16.378  46.931  28.148  1.00 27.91           N  
ATOM     20  CA  LYS A   4      16.188  46.039  27.007  1.00 20.97           C  
ATOM     21  C   LYS A   4      17.475  45.871  26.208  1.00 21.83           C  
ATOM     22  O   LYS A   4      18.199  46.837  25.980  1.00 19.05           O  
ATOM     23  CB  LYS A   4      15.106  46.590  26.081  1.00 22.09           C  
ATOM     24  CG  LYS A   4      13.727  46.665  26.694  1.00 21.98           C  
ATOM     25  CD  LYS A   4      12.743  47.269  25.709  1.00 15.42           C  
ATOM     26  CE  LYS A   4      11.374  47.442  26.346  1.00 27.05           C  
ATOM     27  NZ  LYS A   4      10.423  48.185  25.465  1.00 23.77           N  
ATOM     28  N   LEU A   5      17.745  44.643  25.771  1.00 21.21           N  
ATOM     29  CA  LEU A   5      18.948  44.358  24.997  1.00 15.36           C  
ATOM     30  C   LEU A   5      18.721  43.285  23.943  1.00 22.31           C  
ATOM     31  O   LEU A   5      18.319  42.164  24.261  1.00 14.78           O  
ATOM     32  CB  LEU A   5      20.067  43.911  25.928  1.00 15.38           C  
ATOM     33  CG  LEU A   5      21.336  43.371  25.284  1.00 16.93           C  
ATOM     34  CD1 LEU A   5      21.889  44.351  24.259  1.00 12.04           C  
ATOM     35  CD2 LEU A   5      22.343  43.111  26.386  1.00 10.79           C  
ATOM     36  N   VAL A   6      18.981  43.627  22.684  1.00 18.93           N  
ATOM     37  CA  VAL A   6      18.823  42.664  21.600  1.00 21.16           C  
ATOM     38  C   VAL A   6      20.196  42.114  21.228  1.00 22.58           C  
ATOM     39  O   VAL A   6      21.135  42.882  21.035  1.00 22.31           O  
ATOM     40  CB  VAL A   6      18.202  43.309  20.331  1.00 26.48           C  
ATOM     41  CG1 VAL A   6      18.115  42.264  19.219  1.00 18.81           C  
ATOM     42  CG2 VAL A   6      16.813  43.870  20.637  1.00 15.98           C  
ATOM     43  N   ALA A   7      20.323  40.790  21.145  1.00 15.84           N  
ATOM     44  CA  ALA A   7      21.599  40.191  20.764  1.00 12.34           C  
ATOM     45  C   ALA A   7      21.437  39.400  19.474  1.00 17.51           C  
ATOM     46  O   ALA A   7      20.481  38.641  19.319  1.00 21.12           O  
ATOM     47  CB  ALA A   7      22.121  39.286  21.869  1.00 13.22           C  
ATOM     48  N   ILE A   8      22.357  39.612  18.538  1.00 17.73           N  
ATOM     49  CA  ILE A   8      22.346  38.908  17.266  1.00 14.34           C  
ATOM     50  C   ILE A   8      23.660  38.151  17.216  1.00 11.85           C  
ATOM     51  O   ILE A   8      24.730  38.742  17.107  1.00 16.77           O  
ATOM     52  CB  ILE A   8      22.271  39.880  16.073  1.00 18.66           C  
ATOM     53  CG1 ILE A   8      21.032  40.758  16.196  1.00 17.81           C  
ATOM     54  CG2 ILE A   8      22.236  39.099  14.763  1.00 17.94           C  
ATOM     55  CD1 ILE A   8      20.934  41.815  15.130  1.00 22.30           C  
ATOM     56  N   VAL A   9      23.567  36.833  17.313  1.00 19.20           N  
ATOM     57  CA  VAL A   9      24.735  35.973  17.322  1.00 16.59           C  
ATOM     58  C   VAL A   9      24.687  35.016  16.137  1.00 20.32           C  
ATOM     59  O   VAL A   9      23.645  34.858  15.505  1.00 25.92           O  
ATOM     60  CB  VAL A   9      24.745  35.149  18.588  1.00 13.70           C  
ATOM     61  CG1 VAL A   9      24.617  36.071  19.801  1.00  5.92           C  
ATOM     62  CG2 VAL A   9      23.576  34.169  18.546  1.00  9.40           C  
ATOM     63  N   GLY A  10      25.809  34.359  15.867  1.00 19.56           N  
ATOM     64  CA  GLY A  10      25.887  33.424  14.759  1.00 20.48           C  
ATOM     65  C   GLY A  10      27.302  33.411  14.206  1.00 21.44           C  
ATOM     66  O   GLY A  10      28.082  34.308  14.512  1.00 15.76           O  
ATOM     67  N   PRO A  11      27.671  32.404  13.402  1.00 19.63           N  
ATOM     68  CA  PRO A  11      29.012  32.294  12.813  1.00 25.42           C  
ATOM     69  C   PRO A  11      29.305  33.421  11.824  1.00 25.17           C  
ATOM     70  O   PRO A  11      28.515  34.352  11.691  1.00 28.98           O  
ATOM     71  CB  PRO A  11      28.974  30.929  12.134  1.00 18.19           C  
ATOM     72  CG  PRO A  11      27.541  30.817  11.720  1.00 23.06           C  
ATOM     73  CD  PRO A  11      26.817  31.290  12.961  1.00 18.85           C  
ATOM     74  N   THR A  12      30.437  33.333  11.129  1.00 28.16           N  
ATOM     75  CA  THR A  12      30.819  34.350  10.147  1.00 21.06           C  
ATOM     76  C   THR A  12      30.197  34.059   8.791  1.00 21.92           C  
ATOM     77  O   THR A  12      30.000  32.902   8.428  1.00 20.96           O  
ATOM     78  CB  THR A  12      32.347  34.390   9.889  1.00 28.45           C  
ATOM     79  OG1 THR A  12      33.056  33.904  11.035  1.00 25.24           O  
ATOM     80  CG2 THR A  12      32.797  35.825   9.572  1.00 30.93           C  
ATOM     81  N   ALA A  13      29.910  35.125   8.051  1.00 25.19           N  
ATOM     82  CA  ALA A  13      29.357  35.042   6.710  1.00 21.62           C  
ATOM     83  C   ALA A  13      27.866  34.750   6.595  1.00 22.42           C  
ATOM     84  O   ALA A  13      27.367  34.510   5.495  1.00 19.93           O  
ATOM     85  CB  ALA A  13      30.153  34.027   5.894  1.00 24.11           C  
ATOM     86  N   VAL A  14      27.147  34.786   7.711  1.00 25.89           N  
ATOM     87  CA  VAL A  14      25.706  34.536   7.679  1.00 18.70           C  
ATOM     88  C   VAL A  14      24.887  35.815   7.516  1.00 18.63           C  
ATOM     89  O   VAL A  14      23.665  35.777   7.581  1.00 15.19           O  
ATOM     90  CB  VAL A  14      25.210  33.824   8.963  1.00 20.40           C  
ATOM     91  CG1 VAL A  14      25.637  32.371   8.958  1.00 19.96           C  
ATOM     92  CG2 VAL A  14      25.755  34.528  10.190  1.00 20.91           C  
ATOM     93  N   GLY A  15      25.547  36.952   7.331  1.00 13.75           N  
ATOM     94  CA  GLY A  15      24.798  38.183   7.141  1.00 17.70           C  
ATOM     95  C   GLY A  15      24.370  38.872   8.415  1.00 16.92           C  
ATOM     96  O   GLY A  15      23.326  39.519   8.461  1.00 23.24           O  
ATOM     97  N   LYS A  16      25.197  38.742   9.443  1.00 16.97           N  
ATOM     98  CA  LYS A  16      24.946  39.336  10.738  1.00 14.67           C  
ATOM     99  C   LYS A  16      24.982  40.867  10.686  1.00 23.60           C  
ATOM    100  O   LYS A  16      24.237  41.538  11.405  1.00 18.56           O  
ATOM    101  CB  LYS A  16      25.980  38.810  11.723  1.00  4.13           C  
ATOM    102  CG  LYS A  16      25.384  38.286  13.009  1.00 24.86           C  
ATOM    103  CD  LYS A  16      26.039  36.986  13.504  1.00 21.37           C  
ATOM    104  CE  LYS A  16      27.521  37.141  13.792  1.00 27.62           C  
ATOM    105  NZ  LYS A  16      28.351  36.944  12.577  1.00 23.58           N  
ATOM    106  N   THR A  17      25.834  41.427   9.833  1.00 25.14           N  
ATOM    107  CA  THR A  17      25.923  42.883   9.731  1.00 28.14           C  
ATOM    108  C   THR A  17      24.670  43.507   9.127  1.00 29.16           C  
ATOM    109  O   THR A  17      24.002  44.332   9.758  1.00 20.60           O  
ATOM    110  CB  THR A  17      27.138  43.317   8.886  1.00 32.02           C  
ATOM    111  OG1 THR A  17      28.343  42.905   9.545  1.00 32.60           O  
ATOM    112  CG2 THR A  17      27.153  44.835   8.714  1.00 26.90           C  
ATOM    113  N   LYS A  18      24.353  43.102   7.901  1.00 29.57           N  
ATOM    114  CA  LYS A  18      23.192  43.637   7.202  1.00 26.35           C  
ATOM    115  C   LYS A  18      21.876  43.440   7.949  1.00 29.01           C  
ATOM    116  O   LYS A  18      21.087  44.377   8.076  1.00 28.52           O  
ATOM    117  CB  LYS A  18      23.089  43.027   5.797  1.00 31.45           C  
ATOM    118  CG  LYS A  18      21.939  43.580   4.958  1.00 32.28           C  
ATOM    119  CD  LYS A  18      21.925  42.975   3.565  1.00 36.72           C  
ATOM    120  CE  LYS A  18      20.678  43.395   2.777  1.00 48.04           C  
ATOM    121  NZ  LYS A  18      20.489  44.885   2.715  1.00 46.66           N  
ATOM    122  N   THR A  19      21.626  42.243   8.461  1.00 15.79           N  
ATOM    123  CA  THR A  19      20.368  42.051   9.146  1.00 20.82           C  
ATOM    124  C   THR A  19      20.295  42.897  10.405  1.00 18.35           C  
ATOM    125  O   THR A  19      19.215  43.325  10.804  1.00 29.27           O  
ATOM    126  CB  THR A  19      20.098  40.564   9.472  1.00 19.81           C  
ATOM    127  OG1 THR A  19      20.970  40.122  10.511  1.00 39.14           O  
ATOM    128  CG2 THR A  19      20.332  39.724   8.245  1.00 20.92           C  
ATOM    129  N   SER A  20      21.441  43.177  11.012  1.00 15.08           N  
ATOM    130  CA  SER A  20      21.455  43.985  12.222  1.00 15.28           C  
ATOM    131  C   SER A  20      21.256  45.480  11.970  1.00 19.59           C  
ATOM    132  O   SER A  20      20.607  46.150  12.763  1.00 18.93           O  
ATOM    133  CB  SER A  20      22.754  43.763  13.011  1.00 23.70           C  
ATOM    134  OG  SER A  20      23.895  44.094  12.244  1.00 23.76           O  
ATOM    135  N   VAL A  21      21.799  46.020  10.885  1.00 21.06           N  
ATOM    136  CA  VAL A  21      21.615  47.443  10.644  1.00 17.44           C  
ATOM    137  C   VAL A  21      20.188  47.724  10.204  1.00 17.60           C  
ATOM    138  O   VAL A  21      19.660  48.799  10.471  1.00 17.40           O  
ATOM    139  CB  VAL A  21      22.577  47.986   9.567  1.00 17.90           C  
ATOM    140  CG1 VAL A  21      23.995  47.484   9.835  1.00 15.23           C  
ATOM    141  CG2 VAL A  21      22.110  47.568   8.193  1.00 21.18           C  
HETATM  142  N   MSE A  22      19.570  46.759   9.526  1.00 24.71           N  
HETATM  143  CA  MSE A  22      18.194  46.913   9.049  1.00 26.05           C  
HETATM  144  C   MSE A  22      17.224  46.800  10.217  1.00 24.06           C  
HETATM  145  O   MSE A  22      16.181  47.441  10.230  1.00 25.40           O  
HETATM  146  CB  MSE A  22      17.858  45.850   7.994  1.00 38.52           C  
HETATM  147  CG  MSE A  22      18.551  46.031   6.621  1.00 54.06           C  
HETATM  148 SE   MSE A  22      18.207  47.711   5.645  1.00 68.06          SE  
HETATM  149  CE  MSE A  22      20.008  48.468   5.585  1.00 53.99           C  
ATOM    150  N   LEU A  23      17.575  45.975  11.193  1.00 23.85           N  
ATOM    151  CA  LEU A  23      16.746  45.812  12.360  1.00 20.45           C  
ATOM    152  C   LEU A  23      16.852  47.051  13.235  1.00 21.34           C  
ATOM    153  O   LEU A  23      15.870  47.492  13.826  1.00 20.34           O  
ATOM    154  CB  LEU A  23      17.189  44.590  13.154  1.00 17.95           C  
ATOM    155  CG  LEU A  23      16.697  43.257  12.611  1.00 19.44           C  
ATOM    156  CD1 LEU A  23      17.244  42.136  13.465  1.00 18.60           C  
ATOM    157  CD2 LEU A  23      15.173  43.230  12.618  1.00 17.99           C  
ATOM    158  N   ALA A  24      18.048  47.618  13.311  1.00 17.62           N  
ATOM    159  CA  ALA A  24      18.276  48.797  14.141  1.00 18.51           C  
ATOM    160  C   ALA A  24      17.658  50.062  13.556  1.00 23.73           C  
ATOM    161  O   ALA A  24      17.421  51.038  14.274  1.00 24.81           O  
ATOM    162  CB  ALA A  24      19.770  48.999  14.360  1.00 14.85           C  
ATOM    163  N   LYS A  25      17.396  50.042  12.255  1.00 26.69           N  
ATOM    164  CA  LYS A  25      16.798  51.185  11.582  1.00 29.52           C  
ATOM    165  C   LYS A  25      15.337  51.353  11.975  1.00 33.73           C  
ATOM    166  O   LYS A  25      14.916  52.423  12.419  1.00 36.83           O  
ATOM    167  CB  LYS A  25      16.907  51.023  10.066  1.00 28.98           C  
ATOM    168  CG  LYS A  25      18.298  51.252   9.514  1.00 22.94           C  
ATOM    169  CD  LYS A  25      18.340  50.911   8.039  1.00 30.60           C  
ATOM    170  CE  LYS A  25      19.683  51.261   7.427  1.00 35.33           C  
ATOM    171  NZ  LYS A  25      19.907  52.737   7.406  1.00 38.78           N  
ATOM    172  N   ARG A  26      14.559  50.293  11.819  1.00 33.68           N  
ATOM    173  CA  ARG A  26      13.147  50.367  12.162  1.00 34.72           C  
ATOM    174  C   ARG A  26      12.892  50.132  13.649  1.00 32.54           C  
ATOM    175  O   ARG A  26      11.746  50.077  14.085  1.00 35.50           O  
ATOM    176  CB  ARG A  26      12.361  49.362  11.320  1.00 42.58           C  
ATOM    177  CG  ARG A  26      12.933  47.970  11.365  1.00 42.23           C  
ATOM    178  CD  ARG A  26      12.887  47.298   9.996  1.00 54.53           C  
ATOM    179  NE  ARG A  26      11.583  46.748   9.630  1.00 51.10           N  
ATOM    180  CZ  ARG A  26      11.401  45.921   8.602  1.00 54.78           C  
ATOM    181  NH1 ARG A  26      10.192  45.445   8.315  1.00 46.92           N  
ATOM    182  NH2 ARG A  26      12.444  45.565   7.861  1.00 43.50           N  
ATOM    183  N   LEU A  27      13.959  50.015  14.431  1.00 30.32           N  
ATOM    184  CA  LEU A  27      13.822  49.790  15.859  1.00 22.57           C  
ATOM    185  C   LEU A  27      14.592  50.856  16.626  1.00 23.79           C  
ATOM    186  O   LEU A  27      14.838  50.712  17.822  1.00 25.66           O  
ATOM    187  CB  LEU A  27      14.350  48.400  16.213  1.00 26.37           C  
ATOM    188  CG  LEU A  27      13.396  47.412  16.905  1.00 31.32           C  
ATOM    189  CD1 LEU A  27      12.081  47.330  16.159  1.00 32.37           C  
ATOM    190  CD2 LEU A  27      14.050  46.044  16.966  1.00 24.81           C  
ATOM    191  N   ASN A  28      14.966  51.922  15.920  1.00 24.14           N  
ATOM    192  CA  ASN A  28      15.725  53.046  16.482  1.00 26.54           C  
ATOM    193  C   ASN A  28      16.790  52.579  17.472  1.00 22.32           C  
ATOM    194  O   ASN A  28      16.737  52.945  18.639  1.00 31.14           O  
ATOM    195  CB  ASN A  28      14.762  54.035  17.176  1.00 29.19           C  
ATOM    196  CG  ASN A  28      15.448  55.332  17.615  1.00 31.78           C  
ATOM    197  OD1 ASN A  28      16.173  55.962  16.842  1.00 35.13           O  
ATOM    198  ND2 ASN A  28      15.201  55.742  18.853  1.00 28.49           N  
ATOM    199  N   GLY A  29      17.761  51.791  17.014  1.00 17.81           N  
ATOM    200  CA  GLY A  29      18.782  51.307  17.927  1.00 19.88           C  
ATOM    201  C   GLY A  29      20.226  51.607  17.559  1.00 23.83           C  
ATOM    202  O   GLY A  29      20.497  52.133  16.482  1.00 19.20           O  
ATOM    203  N   GLU A  30      21.155  51.295  18.464  1.00 15.04           N  
ATOM    204  CA  GLU A  30      22.575  51.512  18.205  1.00 20.17           C  
ATOM    205  C   GLU A  30      23.268  50.163  18.317  1.00 22.63           C  
ATOM    206  O   GLU A  30      22.801  49.296  19.052  1.00 28.64           O  
ATOM    207  CB  GLU A  30      23.170  52.486  19.214  1.00 19.10           C  
ATOM    208  CG  GLU A  30      22.373  53.757  19.364  1.00 23.84           C  
ATOM    209  CD  GLU A  30      23.173  54.859  20.025  1.00 27.81           C  
ATOM    210  OE1 GLU A  30      24.072  54.548  20.832  1.00 29.51           O  
ATOM    211  OE2 GLU A  30      22.904  56.042  19.739  1.00 31.61           O  
ATOM    212  N   VAL A  31      24.374  49.964  17.605  1.00 14.54           N  
ATOM    213  CA  VAL A  31      25.034  48.664  17.677  1.00  6.99           C  
ATOM    214  C   VAL A  31      26.296  48.622  18.502  1.00 11.69           C  
ATOM    215  O   VAL A  31      27.178  49.469  18.363  1.00 16.33           O  
ATOM    216  CB  VAL A  31      25.412  48.104  16.281  1.00 10.39           C  
ATOM    217  CG1 VAL A  31      26.079  46.741  16.448  1.00  4.58           C  
ATOM    218  CG2 VAL A  31      24.189  47.992  15.390  1.00  1.00           C  
ATOM    219  N   ILE A  32      26.387  47.625  19.367  1.00  8.83           N  
ATOM    220  CA  ILE A  32      27.589  47.451  20.159  1.00  9.57           C  
ATOM    221  C   ILE A  32      28.262  46.228  19.560  1.00 19.18           C  
ATOM    222  O   ILE A  32      27.700  45.126  19.592  1.00 17.53           O  
ATOM    223  CB  ILE A  32      27.295  47.160  21.621  1.00 20.45           C  
ATOM    224  CG1 ILE A  32      26.418  48.269  22.208  1.00 19.84           C  
ATOM    225  CG2 ILE A  32      28.612  47.047  22.375  1.00 20.29           C  
ATOM    226  CD1 ILE A  32      26.033  48.023  23.648  1.00 19.65           C  
ATOM    227  N   SER A  33      29.456  46.428  19.005  1.00 15.84           N  
ATOM    228  CA  SER A  33      30.214  45.355  18.378  1.00 20.34           C  
ATOM    229  C   SER A  33      30.683  44.357  19.417  1.00 24.56           C  
ATOM    230  O   SER A  33      31.356  44.725  20.377  1.00 17.86           O  
ATOM    231  CB  SER A  33      31.428  45.915  17.635  1.00 18.64           C  
ATOM    232  OG  SER A  33      32.211  44.853  17.097  1.00 22.34           O  
ATOM    233  N   GLY A  34      30.320  43.094  19.229  1.00 25.87           N  
ATOM    234  CA  GLY A  34      30.731  42.077  20.179  1.00 24.85           C  
ATOM    235  C   GLY A  34      31.972  41.331  19.728  1.00 26.70           C  
ATOM    236  O   GLY A  34      32.453  40.446  20.432  1.00 34.63           O  
ATOM    237  N   ASP A  35      32.497  41.693  18.560  1.00 28.05           N  
ATOM    238  CA  ASP A  35      33.679  41.042  17.998  1.00 24.42           C  
ATOM    239  C   ASP A  35      34.979  41.683  18.491  1.00 22.03           C  
ATOM    240  O   ASP A  35      35.384  42.743  18.023  1.00 26.41           O  
ATOM    241  CB  ASP A  35      33.587  41.085  16.468  1.00 26.88           C  
ATOM    242  CG  ASP A  35      34.790  40.477  15.787  1.00 25.97           C  
ATOM    243  OD1 ASP A  35      34.674  40.137  14.593  1.00 31.01           O  
ATOM    244  OD2 ASP A  35      35.848  40.343  16.431  1.00 25.24           O  
ATOM    245  N   SER A  36      35.627  41.007  19.432  1.00 25.50           N  
ATOM    246  CA  SER A  36      36.867  41.467  20.039  1.00 26.67           C  
ATOM    247  C   SER A  36      37.963  41.900  19.072  1.00 29.51           C  
ATOM    248  O   SER A  36      38.815  42.716  19.430  1.00 34.56           O  
ATOM    249  CB  SER A  36      37.416  40.381  20.960  1.00 31.03           C  
ATOM    250  OG  SER A  36      37.671  39.189  20.230  1.00 33.87           O  
HETATM  251  N   MSE A  37      37.968  41.361  17.858  1.00 27.82           N  
HETATM  252  CA  MSE A  37      38.998  41.743  16.897  1.00 25.47           C  
HETATM  253  C   MSE A  37      38.728  43.087  16.243  1.00 21.97           C  
HETATM  254  O   MSE A  37      39.655  43.746  15.779  1.00 23.71           O  
HETATM  255  CB  MSE A  37      39.162  40.665  15.823  1.00 30.18           C  
HETATM  256  CG  MSE A  37      39.930  39.452  16.308  1.00 45.06           C  
HETATM  257 SE   MSE A  37      41.713  39.910  16.986  1.00 62.62          SE  
HETATM  258  CE  MSE A  37      41.407  39.595  18.894  1.00 63.95           C  
ATOM    259  N   GLN A  38      37.461  43.487  16.217  1.00 13.63           N  
ATOM    260  CA  GLN A  38      37.056  44.754  15.624  1.00 22.33           C  
ATOM    261  C   GLN A  38      37.600  45.946  16.399  1.00 24.13           C  
ATOM    262  O   GLN A  38      37.543  47.073  15.909  1.00 25.22           O  
ATOM    263  CB  GLN A  38      35.532  44.877  15.601  1.00 34.37           C  
ATOM    264  CG  GLN A  38      34.805  43.789  14.848  1.00 44.35           C  
ATOM    265  CD  GLN A  38      35.021  43.883  13.364  1.00 38.86           C  
ATOM    266  OE1 GLN A  38      36.148  43.771  12.885  1.00 47.42           O  
ATOM    267  NE2 GLN A  38      33.943  44.094  12.622  1.00 31.49           N  
ATOM    268  N   VAL A  39      38.106  45.716  17.608  1.00 22.21           N  
ATOM    269  CA  VAL A  39      38.614  46.828  18.410  1.00 21.15           C  
ATOM    270  C   VAL A  39      39.952  47.356  17.925  1.00 20.48           C  
ATOM    271  O   VAL A  39      40.236  48.547  18.064  1.00 20.10           O  
ATOM    272  CB  VAL A  39      38.764  46.457  19.923  1.00 19.98           C  
ATOM    273  CG1 VAL A  39      37.495  45.758  20.427  1.00 11.27           C  
ATOM    274  CG2 VAL A  39      40.006  45.604  20.150  1.00 12.09           C  
ATOM    275  N   TYR A  40      40.761  46.478  17.338  1.00 19.85           N  
ATOM    276  CA  TYR A  40      42.096  46.855  16.867  1.00 22.26           C  
ATOM    277  C   TYR A  40      42.113  47.668  15.586  1.00 20.39           C  
ATOM    278  O   TYR A  40      41.716  47.190  14.529  1.00 26.58           O  
ATOM    279  CB  TYR A  40      42.952  45.597  16.685  1.00 16.68           C  
ATOM    280  CG  TYR A  40      43.171  44.830  17.970  1.00  9.54           C  
ATOM    281  CD1 TYR A  40      44.001  45.339  18.974  1.00 14.21           C  
ATOM    282  CD2 TYR A  40      42.532  43.622  18.197  1.00  3.96           C  
ATOM    283  CE1 TYR A  40      44.185  44.659  20.173  1.00  9.93           C  
ATOM    284  CE2 TYR A  40      42.705  42.934  19.391  1.00  9.14           C  
ATOM    285  CZ  TYR A  40      43.530  43.455  20.372  1.00 12.33           C  
ATOM    286  OH  TYR A  40      43.704  42.776  21.559  1.00 19.15           O  
ATOM    287  N   ARG A  41      42.588  48.901  15.679  1.00 22.82           N  
ATOM    288  CA  ARG A  41      42.655  49.748  14.503  1.00 33.79           C  
ATOM    289  C   ARG A  41      43.857  49.442  13.626  1.00 34.65           C  
ATOM    290  O   ARG A  41      44.924  49.073  14.118  1.00 39.36           O  
ATOM    291  CB  ARG A  41      42.653  51.223  14.905  1.00 39.43           C  
ATOM    292  CG  ARG A  41      43.199  51.480  16.270  1.00 38.13           C  
ATOM    293  CD  ARG A  41      42.783  52.848  16.717  1.00 39.01           C  
ATOM    294  NE  ARG A  41      42.921  52.970  18.159  1.00 53.13           N  
ATOM    295  CZ  ARG A  41      42.577  54.046  18.854  1.00 58.54           C  
ATOM    296  NH1 ARG A  41      42.071  55.106  18.237  1.00 56.91           N  
ATOM    297  NH2 ARG A  41      42.738  54.058  20.170  1.00 63.69           N  
ATOM    298  N   GLY A  42      43.659  49.596  12.318  1.00 37.67           N  
ATOM    299  CA  GLY A  42      44.708  49.328  11.351  1.00 38.57           C  
ATOM    300  C   GLY A  42      44.585  47.911  10.826  1.00 39.22           C  
ATOM    301  O   GLY A  42      45.304  47.514   9.909  1.00 41.76           O  
HETATM  302  N   MSE A  43      43.672  47.156  11.434  1.00 33.39           N  
HETATM  303  CA  MSE A  43      43.395  45.772  11.071  1.00 33.32           C  
HETATM  304  C   MSE A  43      41.957  45.741  10.576  1.00 30.48           C  
HETATM  305  O   MSE A  43      41.044  45.354  11.303  1.00 34.41           O  
HETATM  306  CB  MSE A  43      43.562  44.872  12.303  1.00 33.20           C  
HETATM  307  CG  MSE A  43      45.023  44.711  12.737  1.00 35.92           C  
HETATM  308 SE   MSE A  43      45.319  43.964  14.500  1.00 35.48          SE  
HETATM  309  CE  MSE A  43      45.336  42.073  14.117  1.00 29.17           C  
ATOM    310  N   ASP A  44      41.754  46.166   9.337  1.00 29.38           N  
ATOM    311  CA  ASP A  44      40.413  46.218   8.777  1.00 26.40           C  
ATOM    312  C   ASP A  44      40.084  45.014   7.905  1.00 27.08           C  
ATOM    313  O   ASP A  44      38.997  44.442   8.001  1.00 24.68           O  
ATOM    314  CB  ASP A  44      40.249  47.505   7.964  1.00 32.46           C  
ATOM    315  CG  ASP A  44      40.671  48.744   8.738  1.00 34.61           C  
ATOM    316  OD1 ASP A  44      40.259  48.881   9.912  1.00 41.58           O  
ATOM    317  OD2 ASP A  44      41.405  49.585   8.171  1.00 32.75           O  
ATOM    318  N   ILE A  45      41.028  44.623   7.059  1.00 23.64           N  
ATOM    319  CA  ILE A  45      40.814  43.498   6.162  1.00 21.86           C  
ATOM    320  C   ILE A  45      40.740  42.163   6.875  1.00 17.79           C  
ATOM    321  O   ILE A  45      39.734  41.464   6.788  1.00 24.90           O  
ATOM    322  CB  ILE A  45      41.915  43.432   5.115  1.00 18.88           C  
ATOM    323  CG1 ILE A  45      41.915  44.730   4.308  1.00 16.88           C  
ATOM    324  CG2 ILE A  45      41.705  42.229   4.227  1.00 20.31           C  
ATOM    325  CD1 ILE A  45      43.140  44.933   3.470  1.00 12.50           C  
ATOM    326  N   GLY A  46      41.800  41.808   7.588  1.00 22.98           N  
ATOM    327  CA  GLY A  46      41.813  40.534   8.290  1.00 20.88           C  
ATOM    328  C   GLY A  46      40.675  40.340   9.276  1.00 25.41           C  
ATOM    329  O   GLY A  46      40.343  39.214   9.627  1.00 22.27           O  
ATOM    330  N   THR A  47      40.059  41.422   9.730  1.00 23.41           N  
ATOM    331  CA  THR A  47      38.986  41.262  10.695  1.00 27.96           C  
ATOM    332  C   THR A  47      37.597  41.491  10.110  1.00 31.38           C  
ATOM    333  O   THR A  47      36.606  41.504  10.845  1.00 36.57           O  
ATOM    334  CB  THR A  47      39.185  42.192  11.901  1.00 23.51           C  
ATOM    335  OG1 THR A  47      38.882  43.539  11.527  1.00 30.53           O  
ATOM    336  CG2 THR A  47      40.627  42.130  12.380  1.00 26.17           C  
ATOM    337  N   ALA A  48      37.521  41.656   8.790  1.00 30.91           N  
ATOM    338  CA  ALA A  48      36.244  41.887   8.118  1.00 25.40           C  
ATOM    339  C   ALA A  48      35.486  42.998   8.831  1.00 29.62           C  
ATOM    340  O   ALA A  48      34.287  42.877   9.106  1.00 29.00           O  
ATOM    341  CB  ALA A  48      35.413  40.609   8.107  1.00 28.86           C  
ATOM    342  N   LYS A  49      36.203  44.077   9.131  1.00 25.81           N  
ATOM    343  CA  LYS A  49      35.635  45.228   9.824  1.00 21.89           C  
ATOM    344  C   LYS A  49      34.499  45.849   9.019  1.00 27.29           C  
ATOM    345  O   LYS A  49      34.592  45.998   7.796  1.00 29.76           O  
ATOM    346  CB  LYS A  49      36.732  46.266  10.083  1.00 11.83           C  
ATOM    347  CG  LYS A  49      36.358  47.333  11.097  1.00 15.07           C  
ATOM    348  CD  LYS A  49      37.581  48.133  11.544  1.00 14.79           C  
ATOM    349  CE  LYS A  49      38.546  47.286  12.365  1.00 23.92           C  
ATOM    350  NZ  LYS A  49      39.836  47.983  12.609  1.00 13.75           N  
ATOM    351  N   ILE A  50      33.422  46.208   9.711  1.00 28.91           N  
ATOM    352  CA  ILE A  50      32.276  46.823   9.056  1.00 31.00           C  
ATOM    353  C   ILE A  50      32.650  48.209   8.540  1.00 28.46           C  
ATOM    354  O   ILE A  50      33.371  48.953   9.199  1.00 26.43           O  
ATOM    355  CB  ILE A  50      31.072  46.972  10.021  1.00 33.41           C  
ATOM    356  CG1 ILE A  50      29.928  47.695   9.302  1.00 34.15           C  
ATOM    357  CG2 ILE A  50      31.480  47.765  11.256  1.00 27.06           C  
ATOM    358  CD1 ILE A  50      28.634  47.734  10.077  1.00 44.82           C  
ATOM    359  N   THR A  51      32.149  48.555   7.363  1.00 26.83           N  
ATOM    360  CA  THR A  51      32.445  49.853   6.780  1.00 29.48           C  
ATOM    361  C   THR A  51      31.396  50.890   7.172  1.00 30.30           C  
ATOM    362  O   THR A  51      30.294  50.543   7.590  1.00 24.95           O  
ATOM    363  CB  THR A  51      32.504  49.755   5.253  1.00 28.34           C  
ATOM    364  OG1 THR A  51      31.223  49.351   4.752  1.00 26.15           O  
ATOM    365  CG2 THR A  51      33.557  48.730   4.834  1.00 23.28           C  
ATOM    366  N   ALA A  52      31.743  52.166   7.036  1.00 32.45           N  
ATOM    367  CA  ALA A  52      30.808  53.232   7.375  1.00 32.09           C  
ATOM    368  C   ALA A  52      29.563  53.118   6.496  1.00 35.38           C  
ATOM    369  O   ALA A  52      28.453  53.447   6.926  1.00 35.17           O  
ATOM    370  CB  ALA A  52      31.472  54.596   7.190  1.00 27.22           C  
ATOM    371  N   GLU A  53      29.758  52.638   5.270  1.00 36.79           N  
ATOM    372  CA  GLU A  53      28.670  52.471   4.316  1.00 37.99           C  
ATOM    373  C   GLU A  53      27.741  51.324   4.739  1.00 35.55           C  
ATOM    374  O   GLU A  53      26.526  51.407   4.561  1.00 34.62           O  
ATOM    375  CB  GLU A  53      29.249  52.219   2.918  1.00 42.35           C  
ATOM    376  CG  GLU A  53      28.303  52.546   1.773  1.00 58.23           C  
ATOM    377  CD  GLU A  53      28.964  52.399   0.409  1.00 67.52           C  
ATOM    378  OE1 GLU A  53      28.338  52.773  -0.611  1.00 67.29           O  
ATOM    379  OE2 GLU A  53      30.112  51.907   0.358  1.00 72.94           O  
ATOM    380  N   GLU A  54      28.309  50.257   5.297  1.00 32.06           N  
ATOM    381  CA  GLU A  54      27.496  49.133   5.756  1.00 32.13           C  
ATOM    382  C   GLU A  54      26.684  49.539   6.993  1.00 27.36           C  
ATOM    383  O   GLU A  54      25.596  49.023   7.220  1.00 25.72           O  
ATOM    384  CB  GLU A  54      28.380  47.931   6.103  1.00 37.20           C  
ATOM    385  CG  GLU A  54      29.245  47.436   4.955  1.00 44.42           C  
ATOM    386  CD  GLU A  54      30.141  46.274   5.353  1.00 43.31           C  
ATOM    387  OE1 GLU A  54      29.644  45.131   5.409  1.00 38.88           O  
ATOM    388  OE2 GLU A  54      31.335  46.513   5.628  1.00 43.84           O  
HETATM  389  N   MSE A  55      27.224  50.462   7.788  1.00 29.08           N  
HETATM  390  CA  MSE A  55      26.539  50.936   8.987  1.00 26.84           C  
HETATM  391  C   MSE A  55      25.282  51.677   8.570  1.00 29.77           C  
HETATM  392  O   MSE A  55      24.290  51.735   9.304  1.00 22.09           O  
HETATM  393  CB  MSE A  55      27.427  51.887   9.777  1.00 25.10           C  
HETATM  394  CG  MSE A  55      28.660  51.236  10.355  1.00 37.40           C  
HETATM  395 SE   MSE A  55      29.736  52.441  11.409  1.00 40.91          SE  
HETATM  396  CE  MSE A  55      31.144  51.213  11.916  1.00 38.91           C  
ATOM    397  N   ASP A  56      25.352  52.257   7.380  1.00 32.57           N  
ATOM    398  CA  ASP A  56      24.248  52.998   6.807  1.00 35.12           C  
ATOM    399  C   ASP A  56      23.575  53.868   7.859  1.00 35.18           C  
ATOM    400  O   ASP A  56      22.389  53.715   8.141  1.00 41.15           O  
ATOM    401  CB  ASP A  56      23.249  52.019   6.185  1.00 42.55           C  
ATOM    402  CG  ASP A  56      22.267  52.696   5.246  1.00 51.32           C  
ATOM    403  OD1 ASP A  56      22.650  53.690   4.593  1.00 58.85           O  
ATOM    404  OD2 ASP A  56      21.114  52.220   5.144  1.00 55.87           O  
ATOM    405  N   GLY A  57      24.348  54.774   8.455  1.00 33.40           N  
ATOM    406  CA  GLY A  57      23.799  55.675   9.457  1.00 31.98           C  
ATOM    407  C   GLY A  57      23.712  55.161  10.883  1.00 31.54           C  
ATOM    408  O   GLY A  57      23.829  55.938  11.834  1.00 31.28           O  
ATOM    409  N   VAL A  58      23.492  53.862  11.041  1.00 27.95           N  
ATOM    410  CA  VAL A  58      23.394  53.293  12.374  1.00 25.61           C  
ATOM    411  C   VAL A  58      24.727  53.458  13.081  1.00 26.85           C  
ATOM    412  O   VAL A  58      25.778  53.130  12.533  1.00 37.51           O  
ATOM    413  CB  VAL A  58      23.047  51.796  12.332  1.00 28.06           C  
ATOM    414  CG1 VAL A  58      22.945  51.252  13.751  1.00 30.74           C  
ATOM    415  CG2 VAL A  58      21.740  51.582  11.582  1.00 26.89           C  
ATOM    416  N   PRO A  59      24.706  53.991  14.304  1.00 21.98           N  
ATOM    417  CA  PRO A  59      25.942  54.186  15.067  1.00 27.59           C  
ATOM    418  C   PRO A  59      26.496  52.890  15.670  1.00 23.94           C  
ATOM    419  O   PRO A  59      25.748  52.065  16.208  1.00 15.65           O  
ATOM    420  CB  PRO A  59      25.526  55.187  16.141  1.00 28.40           C  
ATOM    421  CG  PRO A  59      24.090  54.828  16.374  1.00 31.32           C  
ATOM    422  CD  PRO A  59      23.568  54.637  14.974  1.00 20.90           C  
ATOM    423  N   HIS A  60      27.809  52.718  15.568  1.00 13.97           N  
ATOM    424  CA  HIS A  60      28.456  51.536  16.102  1.00 18.96           C  
ATOM    425  C   HIS A  60      29.527  51.872  17.130  1.00 18.53           C  
ATOM    426  O   HIS A  60      30.292  52.826  16.966  1.00 23.76           O  
ATOM    427  CB  HIS A  60      29.055  50.702  14.965  1.00 19.86           C  
ATOM    428  CG  HIS A  60      28.031  50.080  14.075  1.00 17.38           C  
ATOM    429  ND1 HIS A  60      28.143  48.791  13.593  1.00 25.70           N  
ATOM    430  CD2 HIS A  60      26.873  50.567  13.567  1.00 16.84           C  
ATOM    431  CE1 HIS A  60      27.104  48.514  12.832  1.00 20.94           C  
ATOM    432  NE2 HIS A  60      26.317  49.580  12.799  1.00 21.88           N  
ATOM    433  N   HIS A  61      29.582  51.076  18.192  1.00 18.53           N  
ATOM    434  CA  HIS A  61      30.550  51.303  19.254  1.00 17.12           C  
ATOM    435  C   HIS A  61      31.551  50.174  19.435  1.00 16.09           C  
ATOM    436  O   HIS A  61      31.291  49.024  19.071  1.00 11.94           O  
ATOM    437  CB  HIS A  61      29.826  51.514  20.584  1.00 20.50           C  
ATOM    438  CG  HIS A  61      28.734  52.533  20.528  1.00 17.74           C  
ATOM    439  ND1 HIS A  61      27.526  52.294  19.914  1.00 24.37           N  
ATOM    440  CD2 HIS A  61      28.680  53.803  20.990  1.00 22.13           C  
ATOM    441  CE1 HIS A  61      26.771  53.375  19.997  1.00 20.82           C  
ATOM    442  NE2 HIS A  61      27.448  54.305  20.644  1.00 26.54           N  
ATOM    443  N   LEU A  62      32.690  50.526  20.026  1.00 15.11           N  
ATOM    444  CA  LEU A  62      33.752  49.578  20.314  1.00 10.75           C  
ATOM    445  C   LEU A  62      34.513  49.120  19.078  1.00 20.88           C  
ATOM    446  O   LEU A  62      35.000  47.990  19.001  1.00 16.86           O  
ATOM    447  CB  LEU A  62      33.171  48.386  21.069  1.00 15.07           C  
ATOM    448  CG  LEU A  62      33.137  48.509  22.603  1.00 20.44           C  
ATOM    449  CD1 LEU A  62      32.910  49.949  23.067  1.00  7.59           C  
ATOM    450  CD2 LEU A  62      32.059  47.595  23.118  1.00 11.12           C  
ATOM    451  N   ILE A  63      34.599  50.010  18.101  1.00 18.29           N  
ATOM    452  CA  ILE A  63      35.328  49.720  16.885  1.00 20.78           C  
ATOM    453  C   ILE A  63      36.512  50.672  16.829  1.00 28.71           C  
ATOM    454  O   ILE A  63      36.353  51.884  17.004  1.00 29.86           O  
ATOM    455  CB  ILE A  63      34.478  49.955  15.637  1.00 19.03           C  
ATOM    456  CG1 ILE A  63      33.197  49.137  15.714  1.00 20.82           C  
ATOM    457  CG2 ILE A  63      35.268  49.566  14.403  1.00 14.54           C  
ATOM    458  CD1 ILE A  63      33.407  47.660  15.598  1.00 23.96           C  
ATOM    459  N   ASP A  64      37.698  50.122  16.596  1.00 23.23           N  
ATOM    460  CA  ASP A  64      38.887  50.943  16.502  1.00 21.23           C  
ATOM    461  C   ASP A  64      39.163  51.722  17.781  1.00 17.07           C  
ATOM    462  O   ASP A  64      39.326  52.936  17.745  1.00 23.68           O  
ATOM    463  CB  ASP A  64      38.728  51.896  15.312  1.00 14.96           C  
ATOM    464  CG  ASP A  64      38.792  51.168  13.992  1.00 14.04           C  
ATOM    465  OD1 ASP A  64      38.314  51.691  12.969  1.00 22.29           O  
ATOM    466  OD2 ASP A  64      39.343  50.052  13.970  1.00 23.01           O  
ATOM    467  N   ILE A  65      39.238  51.020  18.907  1.00 17.13           N  
ATOM    468  CA  ILE A  65      39.489  51.664  20.196  1.00 23.17           C  
ATOM    469  C   ILE A  65      40.779  51.200  20.888  1.00 27.01           C  
ATOM    470  O   ILE A  65      41.142  51.718  21.947  1.00 26.09           O  
ATOM    471  CB  ILE A  65      38.338  51.391  21.170  1.00 21.51           C  
ATOM    472  CG1 ILE A  65      38.152  49.878  21.302  1.00 18.82           C  
ATOM    473  CG2 ILE A  65      37.063  52.059  20.680  1.00 23.48           C  
ATOM    474  CD1 ILE A  65      37.250  49.470  22.436  1.00 13.27           C  
ATOM    475  N   LYS A  66      41.461  50.220  20.304  1.00 25.32           N  
ATOM    476  CA  LYS A  66      42.692  49.687  20.885  1.00 27.97           C  
ATOM    477  C   LYS A  66      43.788  49.443  19.851  1.00 29.03           C  
ATOM    478  O   LYS A  66      43.537  48.865  18.796  1.00 37.18           O  
ATOM    479  CB  LYS A  66      42.396  48.372  21.611  1.00 25.16           C  
ATOM    480  CG  LYS A  66      41.728  48.525  22.961  1.00 19.29           C  
ATOM    481  CD  LYS A  66      42.756  48.809  24.028  1.00 23.22           C  
ATOM    482  CE  LYS A  66      42.119  48.875  25.392  1.00 27.90           C  
ATOM    483  NZ  LYS A  66      43.170  49.063  26.421  1.00 34.60           N  
ATOM    484  N   ASP A  67      45.002  49.884  20.159  1.00 26.66           N  
ATOM    485  CA  ASP A  67      46.146  49.693  19.269  1.00 23.96           C  
ATOM    486  C   ASP A  67      46.486  48.202  19.236  1.00 19.17           C  
ATOM    487  O   ASP A  67      46.465  47.544  20.266  1.00 18.12           O  
ATOM    488  CB  ASP A  67      47.343  50.494  19.786  1.00 25.56           C  
ATOM    489  CG  ASP A  67      48.620  50.187  19.031  1.00 27.87           C  
ATOM    490  OD1 ASP A  67      49.308  49.212  19.389  1.00 25.51           O  
ATOM    491  OD2 ASP A  67      48.927  50.917  18.068  1.00 30.53           O  
ATOM    492  N   PRO A  68      46.821  47.656  18.054  1.00 20.20           N  
ATOM    493  CA  PRO A  68      47.154  46.230  17.924  1.00 21.59           C  
ATOM    494  C   PRO A  68      48.189  45.661  18.887  1.00 22.76           C  
ATOM    495  O   PRO A  68      48.333  44.443  18.981  1.00 21.70           O  
ATOM    496  CB  PRO A  68      47.561  46.084  16.452  1.00 16.77           C  
ATOM    497  CG  PRO A  68      47.932  47.484  16.033  1.00 27.07           C  
ATOM    498  CD  PRO A  68      46.946  48.348  16.760  1.00 22.30           C  
ATOM    499  N   SER A  69      48.893  46.526  19.615  1.00 23.36           N  
ATOM    500  CA  SER A  69      49.884  46.051  20.582  1.00 20.95           C  
ATOM    501  C   SER A  69      49.248  45.840  21.956  1.00 22.65           C  
ATOM    502  O   SER A  69      49.813  45.154  22.809  1.00 22.92           O  
ATOM    503  CB  SER A  69      51.046  47.046  20.709  1.00 22.11           C  
ATOM    504  OG  SER A  69      50.642  48.231  21.371  1.00 26.44           O  
ATOM    505  N   GLU A  70      48.071  46.429  22.163  1.00 21.42           N  
ATOM    506  CA  GLU A  70      47.358  46.323  23.436  1.00 23.88           C  
ATOM    507  C   GLU A  70      46.498  45.077  23.530  1.00 25.59           C  
ATOM    508  O   GLU A  70      46.145  44.469  22.519  1.00 31.08           O  
ATOM    509  CB  GLU A  70      46.455  47.537  23.647  1.00 23.28           C  
ATOM    510  CG  GLU A  70      47.115  48.870  23.361  1.00 30.93           C  
ATOM    511  CD  GLU A  70      46.196  50.046  23.648  1.00 40.45           C  
ATOM    512  OE1 GLU A  70      45.965  50.348  24.840  1.00 45.69           O  
ATOM    513  OE2 GLU A  70      45.698  50.665  22.682  1.00 33.76           O  
ATOM    514  N   SER A  71      46.149  44.705  24.755  1.00 30.93           N  
ATOM    515  CA  SER A  71      45.305  43.538  24.979  1.00 31.75           C  
ATOM    516  C   SER A  71      43.892  44.016  25.289  1.00 31.07           C  
ATOM    517  O   SER A  71      43.700  45.128  25.780  1.00 32.75           O  
ATOM    518  CB  SER A  71      45.822  42.725  26.157  1.00 35.61           C  
ATOM    519  OG  SER A  71      45.609  43.433  27.358  1.00 24.07           O  
ATOM    520  N   PHE A  72      42.910  43.164  25.012  1.00 28.32           N  
ATOM    521  CA  PHE A  72      41.507  43.489  25.245  1.00 26.76           C  
ATOM    522  C   PHE A  72      40.768  42.256  25.760  1.00 26.07           C  
ATOM    523  O   PHE A  72      40.188  41.493  24.983  1.00 20.06           O  
ATOM    524  CB  PHE A  72      40.856  43.975  23.942  1.00 29.22           C  
ATOM    525  CG  PHE A  72      39.544  44.676  24.148  1.00 32.18           C  
ATOM    526  CD1 PHE A  72      39.501  45.920  24.768  1.00 28.26           C  
ATOM    527  CD2 PHE A  72      38.349  44.076  23.765  1.00 23.73           C  
ATOM    528  CE1 PHE A  72      38.288  46.552  25.007  1.00 29.74           C  
ATOM    529  CE2 PHE A  72      37.136  44.703  24.001  1.00 25.56           C  
ATOM    530  CZ  PHE A  72      37.104  45.944  24.625  1.00 19.49           C  
ATOM    531  N   SER A  73      40.784  42.074  27.076  1.00 21.87           N  
ATOM    532  CA  SER A  73      40.137  40.928  27.697  1.00 23.14           C  
ATOM    533  C   SER A  73      38.622  41.055  27.763  1.00 25.76           C  
ATOM    534  O   SER A  73      38.048  42.117  27.504  1.00 27.88           O  
ATOM    535  CB  SER A  73      40.664  40.724  29.121  1.00 25.96           C  
ATOM    536  OG  SER A  73      40.167  41.730  29.992  1.00 27.38           O  
ATOM    537  N   VAL A  74      37.978  39.955  28.129  1.00 27.08           N  
ATOM    538  CA  VAL A  74      36.538  39.934  28.257  1.00 30.19           C  
ATOM    539  C   VAL A  74      36.127  40.995  29.275  1.00 26.50           C  
ATOM    540  O   VAL A  74      35.157  41.723  29.074  1.00 29.59           O  
ATOM    541  CB  VAL A  74      36.060  38.560  28.729  1.00 21.89           C  
ATOM    542  CG1 VAL A  74      36.543  38.308  30.135  1.00 28.49           C  
ATOM    543  CG2 VAL A  74      34.561  38.488  28.657  1.00 29.35           C  
ATOM    544  N   ALA A  75      36.882  41.087  30.364  1.00 28.82           N  
ATOM    545  CA  ALA A  75      36.592  42.058  31.407  1.00 28.74           C  
ATOM    546  C   ALA A  75      36.642  43.474  30.839  1.00 30.47           C  
ATOM    547  O   ALA A  75      35.799  44.302  31.176  1.00 30.46           O  
ATOM    548  CB  ALA A  75      37.584  41.915  32.554  1.00 16.79           C  
ATOM    549  N   ASP A  76      37.625  43.753  29.983  1.00 27.53           N  
ATOM    550  CA  ASP A  76      37.729  45.077  29.388  1.00 23.71           C  
ATOM    551  C   ASP A  76      36.454  45.321  28.583  1.00 27.05           C  
ATOM    552  O   ASP A  76      35.855  46.388  28.663  1.00 27.10           O  
ATOM    553  CB  ASP A  76      38.941  45.201  28.442  1.00 25.12           C  
ATOM    554  CG  ASP A  76      40.284  45.012  29.146  1.00 31.59           C  
ATOM    555  OD1 ASP A  76      40.520  45.639  30.206  1.00 25.66           O  
ATOM    556  OD2 ASP A  76      41.122  44.240  28.614  1.00 34.81           O  
ATOM    557  N   PHE A  77      36.036  44.327  27.806  1.00 23.84           N  
ATOM    558  CA  PHE A  77      34.835  44.474  26.991  1.00 22.26           C  
ATOM    559  C   PHE A  77      33.589  44.745  27.831  1.00 25.42           C  
ATOM    560  O   PHE A  77      32.824  45.662  27.533  1.00 25.13           O  
ATOM    561  CB  PHE A  77      34.610  43.229  26.136  1.00 21.63           C  
ATOM    562  CG  PHE A  77      33.300  43.234  25.399  1.00 22.09           C  
ATOM    563  CD1 PHE A  77      32.309  42.313  25.717  1.00 16.20           C  
ATOM    564  CD2 PHE A  77      33.042  44.183  24.417  1.00 18.08           C  
ATOM    565  CE1 PHE A  77      31.077  42.342  25.072  1.00 24.69           C  
ATOM    566  CE2 PHE A  77      31.809  44.218  23.768  1.00 21.89           C  
ATOM    567  CZ  PHE A  77      30.825  43.295  24.097  1.00 13.19           C  
ATOM    568  N   GLN A  78      33.396  43.947  28.878  1.00 21.55           N  
ATOM    569  CA  GLN A  78      32.249  44.081  29.767  1.00 21.05           C  
ATOM    570  C   GLN A  78      32.169  45.460  30.438  1.00 23.40           C  
ATOM    571  O   GLN A  78      31.086  46.039  30.537  1.00 22.73           O  
ATOM    572  CB  GLN A  78      32.297  42.971  30.824  1.00 21.25           C  
ATOM    573  CG  GLN A  78      31.154  42.988  31.834  1.00 25.52           C  
ATOM    574  CD  GLN A  78      31.293  41.898  32.893  1.00 34.27           C  
ATOM    575  OE1 GLN A  78      31.096  40.716  32.614  1.00 40.32           O  
ATOM    576  NE2 GLN A  78      31.650  42.295  34.113  1.00 42.40           N  
ATOM    577  N   ASP A  79      33.302  45.985  30.900  1.00 24.99           N  
ATOM    578  CA  ASP A  79      33.313  47.300  31.542  1.00 31.08           C  
ATOM    579  C   ASP A  79      32.970  48.411  30.536  1.00 34.12           C  
ATOM    580  O   ASP A  79      32.541  49.501  30.926  1.00 33.55           O  
ATOM    581  CB  ASP A  79      34.681  47.609  32.181  1.00 28.80           C  
ATOM    582  CG  ASP A  79      35.053  46.640  33.295  1.00 33.53           C  
ATOM    583  OD1 ASP A  79      34.140  46.037  33.906  1.00 32.92           O  
ATOM    584  OD2 ASP A  79      36.266  46.497  33.571  1.00 30.38           O  
ATOM    585  N   LEU A  80      33.165  48.148  29.245  1.00 31.27           N  
ATOM    586  CA  LEU A  80      32.844  49.150  28.228  1.00 32.10           C  
ATOM    587  C   LEU A  80      31.432  48.976  27.672  1.00 29.70           C  
ATOM    588  O   LEU A  80      30.768  49.958  27.355  1.00 31.48           O  
ATOM    589  CB  LEU A  80      33.851  49.096  27.074  1.00 35.80           C  
ATOM    590  CG  LEU A  80      35.266  49.617  27.351  1.00 28.62           C  
ATOM    591  CD1 LEU A  80      36.156  49.269  26.183  1.00 28.17           C  
ATOM    592  CD2 LEU A  80      35.234  51.123  27.578  1.00 28.11           C  
ATOM    593  N   ALA A  81      30.966  47.736  27.564  1.00 24.70           N  
ATOM    594  CA  ALA A  81      29.635  47.485  27.027  1.00 18.09           C  
ATOM    595  C   ALA A  81      28.508  47.804  27.997  1.00 20.84           C  
ATOM    596  O   ALA A  81      27.534  48.477  27.637  1.00 20.98           O  
ATOM    597  CB  ALA A  81      29.517  46.043  26.577  1.00 18.96           C  
ATOM    598  N   THR A  82      28.631  47.325  29.228  1.00 17.64           N  
ATOM    599  CA  THR A  82      27.585  47.545  30.214  1.00 18.88           C  
ATOM    600  C   THR A  82      27.202  49.025  30.311  1.00 23.47           C  
ATOM    601  O   THR A  82      26.043  49.377  30.135  1.00 20.91           O  
ATOM    602  CB  THR A  82      28.011  46.978  31.593  1.00 19.34           C  
ATOM    603  OG1 THR A  82      28.347  45.590  31.448  1.00 24.62           O  
ATOM    604  CG2 THR A  82      26.880  47.089  32.594  1.00 20.93           C  
ATOM    605  N   PRO A  83      28.172  49.915  30.562  1.00 23.32           N  
ATOM    606  CA  PRO A  83      27.816  51.334  30.657  1.00 25.14           C  
ATOM    607  C   PRO A  83      27.201  51.867  29.358  1.00 30.50           C  
ATOM    608  O   PRO A  83      26.302  52.716  29.381  1.00 23.50           O  
ATOM    609  CB  PRO A  83      29.150  52.006  30.984  1.00 25.71           C  
ATOM    610  CG  PRO A  83      29.914  50.924  31.699  1.00 26.28           C  
ATOM    611  CD  PRO A  83      29.597  49.708  30.861  1.00 24.09           C  
ATOM    612  N   LEU A  84      27.681  51.361  28.223  1.00 33.96           N  
ATOM    613  CA  LEU A  84      27.180  51.805  26.923  1.00 28.44           C  
ATOM    614  C   LEU A  84      25.710  51.467  26.730  1.00 25.62           C  
ATOM    615  O   LEU A  84      24.962  52.250  26.153  1.00 28.60           O  
ATOM    616  CB  LEU A  84      28.009  51.194  25.791  1.00 24.08           C  
ATOM    617  CG  LEU A  84      28.747  52.210  24.911  1.00 29.43           C  
ATOM    618  CD1 LEU A  84      29.662  51.481  23.948  1.00 33.39           C  
ATOM    619  CD2 LEU A  84      27.755  53.068  24.158  1.00 22.06           C  
ATOM    620  N   ILE A  85      25.295  50.301  27.206  1.00 19.62           N  
ATOM    621  CA  ILE A  85      23.900  49.905  27.077  1.00 13.91           C  
ATOM    622  C   ILE A  85      23.010  50.918  27.782  1.00 19.17           C  
ATOM    623  O   ILE A  85      21.921  51.243  27.306  1.00 22.15           O  
ATOM    624  CB  ILE A  85      23.681  48.517  27.668  1.00 14.77           C  
ATOM    625  CG1 ILE A  85      24.256  47.470  26.710  1.00 17.24           C  
ATOM    626  CG2 ILE A  85      22.216  48.279  27.953  1.00  7.29           C  
ATOM    627  CD1 ILE A  85      24.294  46.073  27.295  1.00 31.06           C  
ATOM    628  N   THR A  86      23.490  51.428  28.912  1.00 24.86           N  
ATOM    629  CA  THR A  86      22.751  52.420  29.683  1.00 23.32           C  
ATOM    630  C   THR A  86      22.737  53.761  28.957  1.00 22.85           C  
ATOM    631  O   THR A  86      21.716  54.437  28.926  1.00 25.13           O  
ATOM    632  CB  THR A  86      23.375  52.628  31.076  1.00 21.36           C  
ATOM    633  OG1 THR A  86      23.461  51.369  31.750  1.00 23.93           O  
ATOM    634  CG2 THR A  86      22.514  53.576  31.912  1.00 19.36           C  
ATOM    635  N   GLU A  87      23.872  54.139  28.374  1.00 25.45           N  
ATOM    636  CA  GLU A  87      23.977  55.405  27.655  1.00 29.21           C  
ATOM    637  C   GLU A  87      23.087  55.391  26.409  1.00 30.32           C  
ATOM    638  O   GLU A  87      22.571  56.426  25.984  1.00 30.48           O  
ATOM    639  CB  GLU A  87      25.441  55.672  27.275  1.00 30.39           C  
ATOM    640  CG  GLU A  87      26.381  55.829  28.482  1.00 31.47           C  
ATOM    641  CD  GLU A  87      27.861  55.702  28.117  1.00 27.31           C  
ATOM    642  OE1 GLU A  87      28.307  56.381  27.166  1.00 27.05           O  
ATOM    643  OE2 GLU A  87      28.579  54.930  28.795  1.00 28.70           O  
ATOM    644  N   ILE A  88      22.912  54.208  25.827  1.00 28.26           N  
ATOM    645  CA  ILE A  88      22.063  54.047  24.654  1.00 19.92           C  
ATOM    646  C   ILE A  88      20.598  54.157  25.095  1.00 23.81           C  
ATOM    647  O   ILE A  88      19.756  54.692  24.365  1.00 21.57           O  
ATOM    648  CB  ILE A  88      22.333  52.681  23.973  1.00 23.43           C  
ATOM    649  CG1 ILE A  88      23.737  52.702  23.353  1.00 19.68           C  
ATOM    650  CG2 ILE A  88      21.260  52.381  22.918  1.00 17.00           C  
ATOM    651  CD1 ILE A  88      24.176  51.383  22.737  1.00 13.37           C  
ATOM    652  N   HIS A  89      20.297  53.668  26.297  1.00 22.56           N  
ATOM    653  CA  HIS A  89      18.934  53.756  26.819  1.00 27.17           C  
ATOM    654  C   HIS A  89      18.615  55.176  27.244  1.00 26.64           C  
ATOM    655  O   HIS A  89      17.464  55.596  27.190  1.00 30.22           O  
ATOM    656  CB  HIS A  89      18.740  52.816  28.001  1.00 23.96           C  
ATOM    657  CG  HIS A  89      18.294  51.449  27.597  1.00 32.85           C  
ATOM    658  ND1 HIS A  89      17.058  51.206  27.047  1.00 38.90           N  
ATOM    659  CD2 HIS A  89      18.943  50.261  27.621  1.00 36.89           C  
ATOM    660  CE1 HIS A  89      16.961  49.919  26.742  1.00 35.13           C  
ATOM    661  NE2 HIS A  89      18.088  49.328  27.080  1.00 38.53           N  
ATOM    662  N   GLU A  90      19.644  55.905  27.667  1.00 25.32           N  
ATOM    663  CA  GLU A  90      19.493  57.294  28.085  1.00 24.97           C  
ATOM    664  C   GLU A  90      19.107  58.146  26.873  1.00 21.25           C  
ATOM    665  O   GLU A  90      18.493  59.201  27.024  1.00 23.21           O  
ATOM    666  CB  GLU A  90      20.805  57.826  28.667  1.00 34.20           C  
ATOM    667  CG  GLU A  90      21.379  57.018  29.821  1.00 45.38           C  
ATOM    668  CD  GLU A  90      20.966  57.536  31.178  1.00 52.53           C  
ATOM    669  OE1 GLU A  90      21.348  56.908  32.190  1.00 49.84           O  
ATOM    670  OE2 GLU A  90      20.265  58.573  31.239  1.00 63.13           O  
ATOM    671  N   ARG A  91      19.486  57.694  25.678  1.00 21.93           N  
ATOM    672  CA  ARG A  91      19.172  58.410  24.442  1.00 19.14           C  
ATOM    673  C   ARG A  91      17.826  57.984  23.894  1.00 19.84           C  
ATOM    674  O   ARG A  91      17.354  58.535  22.904  1.00 22.46           O  
ATOM    675  CB  ARG A  91      20.231  58.149  23.367  1.00 25.57           C  
ATOM    676  CG  ARG A  91      21.497  58.966  23.499  1.00 22.90           C  
ATOM    677  CD  ARG A  91      22.428  58.710  22.317  1.00 28.79           C  
ATOM    678  NE  ARG A  91      23.107  57.413  22.367  1.00 29.80           N  
ATOM    679  CZ  ARG A  91      24.101  57.112  23.202  1.00 36.01           C  
ATOM    680  NH1 ARG A  91      24.538  58.012  24.070  1.00 38.34           N  
ATOM    681  NH2 ARG A  91      24.678  55.916  23.158  1.00 34.40           N  
ATOM    682  N   GLY A  92      17.217  56.990  24.536  1.00 25.46           N  
ATOM    683  CA  GLY A  92      15.924  56.496  24.095  1.00 20.89           C  
ATOM    684  C   GLY A  92      16.043  55.562  22.904  1.00 29.58           C  
ATOM    685  O   GLY A  92      15.105  55.417  22.125  1.00 32.10           O  
ATOM    686  N   ARG A  93      17.205  54.931  22.773  1.00 29.69           N  
ATOM    687  CA  ARG A  93      17.485  54.009  21.684  1.00 25.96           C  
ATOM    688  C   ARG A  93      17.575  52.592  22.221  1.00 21.99           C  
ATOM    689  O   ARG A  93      17.729  52.381  23.427  1.00 15.70           O  
ATOM    690  CB  ARG A  93      18.824  54.356  21.042  1.00 33.44           C  
ATOM    691  CG  ARG A  93      18.953  55.783  20.594  1.00 29.24           C  
ATOM    692  CD  ARG A  93      18.326  55.962  19.247  1.00 39.17           C  
ATOM    693  NE  ARG A  93      18.623  57.272  18.689  1.00 45.40           N  
ATOM    694  CZ  ARG A  93      19.836  57.673  18.322  1.00 45.34           C  
ATOM    695  NH1 ARG A  93      20.874  56.862  18.458  1.00 49.73           N  
ATOM    696  NH2 ARG A  93      20.011  58.883  17.801  1.00 49.21           N  
ATOM    697  N   LEU A  94      17.508  51.624  21.313  1.00 14.89           N  
ATOM    698  CA  LEU A  94      17.598  50.219  21.685  1.00 13.91           C  
ATOM    699  C   LEU A  94      18.993  49.664  21.387  1.00 19.27           C  
ATOM    700  O   LEU A  94      19.432  49.643  20.233  1.00 21.47           O  
ATOM    701  CB  LEU A  94      16.544  49.416  20.924  1.00 15.76           C  
ATOM    702  CG  LEU A  94      16.599  47.903  21.102  1.00 10.25           C  
ATOM    703  CD1 LEU A  94      16.407  47.546  22.567  1.00  8.38           C  
ATOM    704  CD2 LEU A  94      15.528  47.272  20.250  1.00 13.21           C  
ATOM    705  N   PRO A  95      19.708  49.206  22.427  1.00 17.70           N  
ATOM    706  CA  PRO A  95      21.054  48.654  22.257  1.00 19.98           C  
ATOM    707  C   PRO A  95      21.085  47.268  21.619  1.00 18.27           C  
ATOM    708  O   PRO A  95      20.351  46.362  22.019  1.00 14.23           O  
ATOM    709  CB  PRO A  95      21.599  48.645  23.680  1.00 23.02           C  
ATOM    710  CG  PRO A  95      20.386  48.315  24.472  1.00 20.84           C  
ATOM    711  CD  PRO A  95      19.337  49.225  23.851  1.00 15.39           C  
ATOM    712  N   PHE A  96      21.961  47.128  20.629  1.00 17.51           N  
ATOM    713  CA  PHE A  96      22.152  45.894  19.871  1.00 15.38           C  
ATOM    714  C   PHE A  96      23.572  45.325  20.062  1.00 17.17           C  
ATOM    715  O   PHE A  96      24.562  45.997  19.767  1.00 13.17           O  
ATOM    716  CB  PHE A  96      21.925  46.182  18.374  1.00 23.10           C  
ATOM    717  CG  PHE A  96      20.485  46.077  17.923  1.00 21.11           C  
ATOM    718  CD1 PHE A  96      20.010  44.899  17.344  1.00 25.59           C  
ATOM    719  CD2 PHE A  96      19.615  47.155  18.053  1.00 18.77           C  
ATOM    720  CE1 PHE A  96      18.684  44.790  16.902  1.00 24.20           C  
ATOM    721  CE2 PHE A  96      18.289  47.056  17.614  1.00 25.43           C  
ATOM    722  CZ  PHE A  96      17.824  45.867  17.034  1.00 19.70           C  
ATOM    723  N   LEU A  97      23.664  44.098  20.566  1.00 14.11           N  
ATOM    724  CA  LEU A  97      24.948  43.435  20.746  1.00 14.07           C  
ATOM    725  C   LEU A  97      25.043  42.472  19.569  1.00 19.40           C  
ATOM    726  O   LEU A  97      24.326  41.458  19.517  1.00 13.12           O  
ATOM    727  CB  LEU A  97      24.994  42.664  22.071  1.00 17.55           C  
ATOM    728  CG  LEU A  97      26.322  41.995  22.464  1.00 11.86           C  
ATOM    729  CD1 LEU A  97      27.416  43.027  22.597  1.00  7.35           C  
ATOM    730  CD2 LEU A  97      26.149  41.266  23.772  1.00 22.65           C  
ATOM    731  N   VAL A  98      25.929  42.807  18.629  1.00 17.40           N  
ATOM    732  CA  VAL A  98      26.114  42.036  17.395  1.00 24.20           C  
ATOM    733  C   VAL A  98      27.451  41.328  17.219  1.00 23.15           C  
ATOM    734  O   VAL A  98      28.508  41.884  17.517  1.00 28.91           O  
ATOM    735  CB  VAL A  98      25.890  42.941  16.143  1.00 15.10           C  
ATOM    736  CG1 VAL A  98      26.023  42.117  14.858  1.00 13.48           C  
ATOM    737  CG2 VAL A  98      24.523  43.569  16.208  1.00 10.01           C  
ATOM    738  N   GLY A  99      27.373  40.097  16.717  1.00 27.93           N  
ATOM    739  CA  GLY A  99      28.548  39.288  16.464  1.00 32.87           C  
ATOM    740  C   GLY A  99      29.301  38.961  17.726  1.00 40.47           C  
ATOM    741  O   GLY A  99      28.732  39.006  18.818  1.00 41.87           O  
ATOM    742  N   GLY A 100      30.582  38.623  17.572  1.00 44.88           N  
ATOM    743  CA  GLY A 100      31.425  38.305  18.715  1.00 43.71           C  
ATOM    744  C   GLY A 100      31.470  36.842  19.116  1.00 41.24           C  
ATOM    745  O   GLY A 100      30.731  36.014  18.587  1.00 43.65           O  
ATOM    746  N   THR A 101      32.359  36.518  20.048  1.00 40.42           N  
ATOM    747  CA  THR A 101      32.467  35.147  20.527  1.00 43.84           C  
ATOM    748  C   THR A 101      31.609  35.026  21.776  1.00 37.70           C  
ATOM    749  O   THR A 101      31.354  36.019  22.462  1.00 27.73           O  
ATOM    750  CB  THR A 101      33.913  34.770  20.914  1.00 49.98           C  
ATOM    751  OG1 THR A 101      34.249  35.399  22.158  1.00 60.67           O  
ATOM    752  CG2 THR A 101      34.892  35.223  19.844  1.00 48.25           C  
ATOM    753  N   GLY A 102      31.187  33.801  22.071  1.00 38.18           N  
ATOM    754  CA  GLY A 102      30.348  33.554  23.227  1.00 41.28           C  
ATOM    755  C   GLY A 102      30.877  34.130  24.521  1.00 42.43           C  
ATOM    756  O   GLY A 102      30.109  34.575  25.373  1.00 46.37           O  
ATOM    757  N   LEU A 103      32.194  34.126  24.669  1.00 40.44           N  
ATOM    758  CA  LEU A 103      32.825  34.647  25.871  1.00 38.46           C  
ATOM    759  C   LEU A 103      32.473  36.095  26.171  1.00 36.20           C  
ATOM    760  O   LEU A 103      32.170  36.440  27.314  1.00 41.10           O  
ATOM    761  CB  LEU A 103      34.339  34.525  25.760  1.00 40.71           C  
ATOM    762  CG  LEU A 103      34.990  33.424  26.579  1.00 41.88           C  
ATOM    763  CD1 LEU A 103      36.485  33.443  26.305  1.00 44.26           C  
ATOM    764  CD2 LEU A 103      34.707  33.641  28.058  1.00 34.08           C  
ATOM    765  N   TYR A 104      32.519  36.941  25.148  1.00 32.10           N  
ATOM    766  CA  TYR A 104      32.225  38.359  25.323  1.00 28.53           C  
ATOM    767  C   TYR A 104      30.734  38.649  25.461  1.00 30.57           C  
ATOM    768  O   TYR A 104      30.337  39.529  26.231  1.00 29.08           O  
ATOM    769  CB  TYR A 104      32.818  39.170  24.158  1.00 33.20           C  
ATOM    770  CG  TYR A 104      34.336  39.283  24.179  1.00 32.80           C  
ATOM    771  CD1 TYR A 104      35.145  38.143  24.262  1.00 46.69           C  
ATOM    772  CD2 TYR A 104      34.963  40.529  24.114  1.00 38.18           C  
ATOM    773  CE1 TYR A 104      36.547  38.240  24.282  1.00 41.20           C  
ATOM    774  CE2 TYR A 104      36.364  40.642  24.133  1.00 40.25           C  
ATOM    775  CZ  TYR A 104      37.147  39.492  24.218  1.00 43.80           C  
ATOM    776  OH  TYR A 104      38.528  39.583  24.257  1.00 42.95           O  
ATOM    777  N   VAL A 105      29.908  37.907  24.727  1.00 25.93           N  
ATOM    778  CA  VAL A 105      28.467  38.103  24.795  1.00 26.89           C  
ATOM    779  C   VAL A 105      27.898  37.581  26.108  1.00 25.50           C  
ATOM    780  O   VAL A 105      27.087  38.258  26.737  1.00 34.05           O  
ATOM    781  CB  VAL A 105      27.721  37.418  23.606  1.00 26.54           C  
ATOM    782  CG1 VAL A 105      28.232  37.964  22.286  1.00 20.91           C  
ATOM    783  CG2 VAL A 105      27.902  35.914  23.663  1.00 36.38           C  
ATOM    784  N   ASN A 106      28.319  36.393  26.539  1.00 26.58           N  
ATOM    785  CA  ASN A 106      27.807  35.847  27.798  1.00 26.39           C  
ATOM    786  C   ASN A 106      28.205  36.678  28.994  1.00 24.15           C  
ATOM    787  O   ASN A 106      27.446  36.787  29.949  1.00 25.29           O  
ATOM    788  CB  ASN A 106      28.285  34.421  28.021  1.00 24.58           C  
ATOM    789  CG  ASN A 106      27.589  33.445  27.125  1.00 39.64           C  
ATOM    790  OD1 ASN A 106      26.654  33.804  26.410  1.00 48.03           O  
ATOM    791  ND2 ASN A 106      28.027  32.198  27.158  1.00 49.44           N  
ATOM    792  N   ALA A 107      29.392  37.266  28.944  1.00 24.65           N  
ATOM    793  CA  ALA A 107      29.852  38.075  30.053  1.00 27.50           C  
ATOM    794  C   ALA A 107      28.999  39.328  30.218  1.00 26.05           C  
ATOM    795  O   ALA A 107      28.816  39.814  31.329  1.00 25.68           O  
ATOM    796  CB  ALA A 107      31.307  38.449  29.849  1.00 30.84           C  
ATOM    797  N   VAL A 108      28.476  39.843  29.109  1.00 27.51           N  
ATOM    798  CA  VAL A 108      27.645  41.046  29.127  1.00 22.48           C  
ATOM    799  C   VAL A 108      26.196  40.750  29.490  1.00 23.64           C  
ATOM    800  O   VAL A 108      25.595  41.453  30.294  1.00 24.26           O  
ATOM    801  CB  VAL A 108      27.644  41.739  27.753  1.00 22.05           C  
ATOM    802  CG1 VAL A 108      26.532  42.773  27.688  1.00 15.25           C  
ATOM    803  CG2 VAL A 108      28.995  42.379  27.502  1.00 18.49           C  
ATOM    804  N   ILE A 109      25.639  39.704  28.894  1.00 25.28           N  
ATOM    805  CA  ILE A 109      24.254  39.384  29.152  1.00 26.59           C  
ATOM    806  C   ILE A 109      24.024  38.763  30.514  1.00 34.56           C  
ATOM    807  O   ILE A 109      22.880  38.620  30.940  1.00 43.49           O  
ATOM    808  CB  ILE A 109      23.678  38.440  28.088  1.00 25.30           C  
ATOM    809  CG1 ILE A 109      24.352  37.072  28.173  1.00 33.32           C  
ATOM    810  CG2 ILE A 109      23.867  39.032  26.717  1.00  8.93           C  
ATOM    811  CD1 ILE A 109      23.690  36.042  27.271  1.00 34.29           C  
ATOM    812  N   HIS A 110      25.099  38.391  31.201  1.00 30.37           N  
ATOM    813  CA  HIS A 110      24.971  37.778  32.520  1.00 29.27           C  
ATOM    814  C   HIS A 110      25.625  38.612  33.610  1.00 33.12           C  
ATOM    815  O   HIS A 110      25.496  38.306  34.794  1.00 35.40           O  
ATOM    816  CB  HIS A 110      25.581  36.372  32.517  1.00 19.29           C  
ATOM    817  CG  HIS A 110      24.787  35.372  31.738  1.00 25.35           C  
ATOM    818  ND1 HIS A 110      25.331  34.623  30.714  1.00 32.37           N  
ATOM    819  CD2 HIS A 110      23.494  34.982  31.839  1.00 32.20           C  
ATOM    820  CE1 HIS A 110      24.409  33.817  30.221  1.00 35.84           C  
ATOM    821  NE2 HIS A 110      23.283  34.014  30.887  1.00 35.03           N  
ATOM    822  N   GLN A 111      26.326  39.668  33.216  1.00 37.28           N  
ATOM    823  CA  GLN A 111      26.990  40.526  34.190  1.00 42.05           C  
ATOM    824  C   GLN A 111      27.882  39.725  35.138  1.00 43.47           C  
ATOM    825  O   GLN A 111      27.846  39.938  36.351  1.00 43.86           O  
ATOM    826  CB  GLN A 111      25.953  41.295  35.015  1.00 42.06           C  
ATOM    827  CG  GLN A 111      25.248  42.392  34.267  1.00 43.26           C  
ATOM    828  CD  GLN A 111      26.214  43.389  33.673  1.00 48.98           C  
ATOM    829  OE1 GLN A 111      26.859  43.125  32.654  1.00 53.67           O  
ATOM    830  NE2 GLN A 111      26.330  44.543  34.312  1.00 55.31           N  
ATOM    831  N   PHE A 112      28.679  38.808  34.594  1.00 46.79           N  
ATOM    832  CA  PHE A 112      29.575  37.996  35.421  1.00 49.26           C  
ATOM    833  C   PHE A 112      30.470  38.859  36.304  1.00 51.91           C  
ATOM    834  O   PHE A 112      30.999  39.877  35.858  1.00 43.68           O  
ATOM    835  CB  PHE A 112      30.467  37.103  34.553  1.00 48.71           C  
ATOM    836  CG  PHE A 112      29.742  35.969  33.890  1.00 43.05           C  
ATOM    837  CD1 PHE A 112      28.823  35.202  34.594  1.00 45.33           C  
ATOM    838  CD2 PHE A 112      30.014  35.640  32.567  1.00 44.89           C  
ATOM    839  CE1 PHE A 112      28.178  34.121  33.988  1.00 39.97           C  
ATOM    840  CE2 PHE A 112      29.377  34.561  31.951  1.00 37.00           C  
ATOM    841  CZ  PHE A 112      28.461  33.801  32.665  1.00 34.45           C  
ATOM    842  N   ASN A 113      30.644  38.439  37.555  1.00 61.52           N  
ATOM    843  CA  ASN A 113      31.480  39.174  38.502  1.00 70.04           C  
ATOM    844  C   ASN A 113      32.813  39.582  37.883  1.00 73.50           C  
ATOM    845  O   ASN A 113      33.124  40.771  37.787  1.00 78.72           O  
ATOM    846  CB  ASN A 113      31.768  38.328  39.744  1.00 72.36           C  
ATOM    847  CG  ASN A 113      32.681  39.042  40.732  1.00 79.35           C  
ATOM    848  OD1 ASN A 113      33.364  38.407  41.540  1.00 81.61           O  
ATOM    849  ND2 ASN A 113      32.691  40.373  40.674  1.00 81.38           N  
ATOM    850  N   LEU A 114      33.593  38.580  37.477  1.00 73.55           N  
ATOM    851  CA  LEU A 114      34.914  38.778  36.878  1.00 71.36           C  
ATOM    852  C   LEU A 114      35.886  39.400  37.878  1.00 69.07           C  
ATOM    853  O   LEU A 114      36.735  40.222  37.519  1.00 66.47           O  
ATOM    854  CB  LEU A 114      34.819  39.653  35.621  1.00 69.55           C  
ATOM    855  CG  LEU A 114      34.244  38.999  34.361  1.00 68.65           C  
ATOM    856  CD1 LEU A 114      34.195  40.032  33.252  1.00 69.14           C  
ATOM    857  CD2 LEU A 114      35.097  37.803  33.938  1.00 68.20           C  
ATOM    858  N   GLY A 115      35.747  38.996  39.137  1.00 68.08           N  
ATOM    859  CA  GLY A 115      36.608  39.500  40.189  1.00 68.12           C  
ATOM    860  C   GLY A 115      37.838  38.627  40.354  1.00 67.01           C  
ATOM    861  O   GLY A 115      37.811  37.432  40.044  1.00 64.14           O  
ATOM    862  N   ASP A 116      38.918  39.232  40.841  1.00 65.74           N  
ATOM    863  CA  ASP A 116      40.178  38.529  41.051  1.00 64.37           C  
ATOM    864  C   ASP A 116      40.022  37.401  42.067  1.00 59.20           C  
ATOM    865  O   ASP A 116      38.957  37.226  42.664  1.00 56.12           O  
ATOM    866  CB  ASP A 116      41.256  39.503  41.546  1.00 68.67           C  
ATOM    867  CG  ASP A 116      41.489  40.660  40.591  1.00 70.10           C  
ATOM    868  OD1 ASP A 116      41.796  40.403  39.406  1.00 69.29           O  
ATOM    869  OD2 ASP A 116      41.372  41.826  41.032  1.00 68.68           O  
ATOM    870  N   ILE A 117      41.093  36.636  42.254  1.00 52.44           N  
ATOM    871  CA  ILE A 117      41.093  35.533  43.206  1.00 51.30           C  
ATOM    872  C   ILE A 117      42.272  35.663  44.170  1.00 45.96           C  
ATOM    873  O   ILE A 117      43.415  35.394  43.803  1.00 47.32           O  
ATOM    874  CB  ILE A 117      41.181  34.157  42.490  1.00 57.09           C  
ATOM    875  CG1 ILE A 117      39.910  33.897  41.669  1.00 62.54           C  
ATOM    876  CG2 ILE A 117      41.363  33.050  43.517  1.00 57.14           C  
ATOM    877  CD1 ILE A 117      39.806  34.699  40.374  1.00 73.49           C  
ATOM    878  N   ARG A 118      41.988  36.084  45.400  1.00 39.35           N  
ATOM    879  CA  ARG A 118      43.025  36.246  46.418  1.00 39.16           C  
ATOM    880  C   ARG A 118      42.665  35.507  47.703  1.00 34.53           C  
ATOM    881  O   ARG A 118      41.491  35.347  48.041  1.00 26.81           O  
ATOM    882  CB  ARG A 118      43.251  37.731  46.727  1.00 38.43           C  
ATOM    883  CG  ARG A 118      44.293  37.987  47.813  1.00 49.66           C  
ATOM    884  CD  ARG A 118      44.498  39.478  48.056  1.00 53.48           C  
ATOM    885  NE  ARG A 118      43.236  40.156  48.351  1.00 63.71           N  
ATOM    886  CZ  ARG A 118      42.520  39.974  49.458  1.00 66.17           C  
ATOM    887  NH1 ARG A 118      41.381  40.636  49.629  1.00 65.69           N  
ATOM    888  NH2 ARG A 118      42.944  39.141  50.400  1.00 65.94           N  
ATOM    889  N   ALA A 119      43.693  35.060  48.413  1.00 41.81           N  
ATOM    890  CA  ALA A 119      43.517  34.336  49.664  1.00 43.59           C  
ATOM    891  C   ALA A 119      43.249  35.295  50.825  1.00 45.34           C  
ATOM    892  O   ALA A 119      44.005  36.238  51.057  1.00 40.42           O  
ATOM    893  CB  ALA A 119      44.755  33.488  49.956  1.00 46.75           C  
ATOM    894  N   ASP A 120      42.165  35.033  51.549  1.00 43.59           N  
ATOM    895  CA  ASP A 120      41.764  35.843  52.693  1.00 45.97           C  
ATOM    896  C   ASP A 120      42.909  35.930  53.707  1.00 44.24           C  
ATOM    897  O   ASP A 120      43.380  34.908  54.204  1.00 51.60           O  
ATOM    898  CB  ASP A 120      40.522  35.217  53.341  1.00 44.62           C  
ATOM    899  CG  ASP A 120      39.894  36.106  54.395  1.00 54.97           C  
ATOM    900  OD1 ASP A 120      38.761  35.800  54.836  1.00 58.08           O  
ATOM    901  OD2 ASP A 120      40.526  37.110  54.789  1.00 61.28           O  
ATOM    902  N   GLU A 121      43.357  37.148  54.005  1.00 39.01           N  
ATOM    903  CA  GLU A 121      44.440  37.341  54.964  1.00 41.87           C  
ATOM    904  C   GLU A 121      44.053  36.838  56.361  1.00 38.61           C  
ATOM    905  O   GLU A 121      44.919  36.546  57.189  1.00 34.16           O  
ATOM    906  CB  GLU A 121      44.848  38.826  55.044  1.00 51.04           C  
ATOM    907  CG  GLU A 121      43.742  39.798  55.475  1.00 54.34           C  
ATOM    908  CD  GLU A 121      42.762  40.124  54.355  1.00 61.05           C  
ATOM    909  OE1 GLU A 121      41.654  40.628  54.659  1.00 64.17           O  
ATOM    910  OE2 GLU A 121      43.099  39.888  53.172  1.00 57.35           O  
ATOM    911  N   ASP A 122      42.753  36.724  56.617  1.00 33.50           N  
ATOM    912  CA  ASP A 122      42.283  36.264  57.916  1.00 33.55           C  
ATOM    913  C   ASP A 122      42.499  34.772  58.139  1.00 32.61           C  
ATOM    914  O   ASP A 122      42.914  34.357  59.224  1.00 32.13           O  
ATOM    915  CB  ASP A 122      40.801  36.602  58.106  1.00 33.30           C  
ATOM    916  CG  ASP A 122      40.529  38.094  58.033  1.00 29.77           C  
ATOM    917  OD1 ASP A 122      41.391  38.888  58.470  1.00 35.34           O  
ATOM    918  OD2 ASP A 122      39.447  38.471  57.547  1.00 37.83           O  
ATOM    919  N   TYR A 123      42.224  33.965  57.118  1.00 28.47           N  
ATOM    920  CA  TYR A 123      42.403  32.522  57.235  1.00 25.15           C  
ATOM    921  C   TYR A 123      43.871  32.188  57.453  1.00 26.07           C  
ATOM    922  O   TYR A 123      44.211  31.261  58.194  1.00 24.91           O  
ATOM    923  CB  TYR A 123      41.899  31.816  55.976  1.00 21.60           C  
ATOM    924  CG  TYR A 123      41.998  30.308  56.041  1.00 25.85           C  
ATOM    925  CD1 TYR A 123      42.885  29.613  55.225  1.00 20.70           C  
ATOM    926  CD2 TYR A 123      41.191  29.574  56.910  1.00 31.18           C  
ATOM    927  CE1 TYR A 123      42.961  28.224  55.270  1.00 29.47           C  
ATOM    928  CE2 TYR A 123      41.262  28.185  56.966  1.00 26.73           C  
ATOM    929  CZ  TYR A 123      42.146  27.515  56.144  1.00 27.09           C  
ATOM    930  OH  TYR A 123      42.208  26.140  56.186  1.00 21.74           O  
ATOM    931  N   ARG A 124      44.746  32.946  56.800  1.00 27.43           N  
ATOM    932  CA  ARG A 124      46.170  32.707  56.951  1.00 25.40           C  
ATOM    933  C   ARG A 124      46.518  33.025  58.398  1.00 31.53           C  
ATOM    934  O   ARG A 124      47.279  32.299  59.042  1.00 30.10           O  
ATOM    935  CB  ARG A 124      46.969  33.596  56.001  1.00 33.01           C  
ATOM    936  CG  ARG A 124      48.396  33.128  55.787  1.00 34.30           C  
ATOM    937  CD  ARG A 124      49.391  34.220  56.132  1.00 39.48           C  
ATOM    938  NE  ARG A 124      50.405  34.381  55.088  1.00 49.12           N  
ATOM    939  CZ  ARG A 124      50.174  34.913  53.891  1.00 44.89           C  
ATOM    940  NH1 ARG A 124      48.962  35.345  53.572  1.00 50.42           N  
ATOM    941  NH2 ARG A 124      51.154  35.014  53.009  1.00 53.23           N  
ATOM    942  N   HIS A 125      45.948  34.114  58.908  1.00 32.01           N  
ATOM    943  CA  HIS A 125      46.174  34.518  60.292  1.00 32.65           C  
ATOM    944  C   HIS A 125      45.683  33.388  61.205  1.00 35.81           C  
ATOM    945  O   HIS A 125      46.311  33.071  62.216  1.00 33.78           O  
ATOM    946  CB  HIS A 125      45.397  35.802  60.596  1.00 35.40           C  
ATOM    947  CG  HIS A 125      45.588  36.319  61.990  1.00 35.68           C  
ATOM    948  ND1 HIS A 125      44.637  37.078  62.636  1.00 37.03           N  
ATOM    949  CD2 HIS A 125      46.626  36.205  62.855  1.00 38.07           C  
ATOM    950  CE1 HIS A 125      45.077  37.407  63.838  1.00 37.69           C  
ATOM    951  NE2 HIS A 125      46.283  36.889  63.994  1.00 36.78           N  
ATOM    952  N   GLU A 126      44.557  32.782  60.835  1.00 34.45           N  
ATOM    953  CA  GLU A 126      43.971  31.689  61.608  1.00 29.01           C  
ATOM    954  C   GLU A 126      44.909  30.490  61.685  1.00 27.31           C  
ATOM    955  O   GLU A 126      45.059  29.883  62.742  1.00 20.28           O  
ATOM    956  CB  GLU A 126      42.649  31.266  60.972  1.00 36.83           C  
ATOM    957  CG  GLU A 126      41.961  30.080  61.621  1.00 42.09           C  
ATOM    958  CD  GLU A 126      40.674  29.717  60.902  1.00 48.96           C  
ATOM    959  OE1 GLU A 126      39.822  30.618  60.721  1.00 50.12           O  
ATOM    960  OE2 GLU A 126      40.514  28.534  60.520  1.00 51.48           O  
ATOM    961  N   LEU A 127      45.531  30.148  60.560  1.00 21.48           N  
ATOM    962  CA  LEU A 127      46.446  29.018  60.527  1.00 23.02           C  
ATOM    963  C   LEU A 127      47.706  29.286  61.343  1.00 30.68           C  
ATOM    964  O   LEU A 127      48.199  28.401  62.044  1.00 30.10           O  
ATOM    965  CB  LEU A 127      46.841  28.679  59.092  1.00 18.91           C  
ATOM    966  CG  LEU A 127      45.687  28.224  58.200  1.00 26.61           C  
ATOM    967  CD1 LEU A 127      46.199  27.996  56.793  1.00 26.38           C  
ATOM    968  CD2 LEU A 127      45.067  26.962  58.771  1.00 18.84           C  
ATOM    969  N   GLU A 128      48.232  30.503  61.261  1.00 29.04           N  
ATOM    970  CA  GLU A 128      49.436  30.824  62.006  1.00 25.77           C  
ATOM    971  C   GLU A 128      49.151  30.702  63.496  1.00 24.22           C  
ATOM    972  O   GLU A 128      49.940  30.112  64.236  1.00 18.49           O  
ATOM    973  CB  GLU A 128      49.931  32.224  61.625  1.00 22.06           C  
ATOM    974  CG  GLU A 128      50.353  32.279  60.149  1.00 27.25           C  
ATOM    975  CD  GLU A 128      50.704  33.669  59.659  1.00 27.95           C  
ATOM    976  OE1 GLU A 128      49.985  34.630  60.007  1.00 33.77           O  
ATOM    977  OE2 GLU A 128      51.688  33.799  58.899  1.00 24.76           O  
ATOM    978  N   ALA A 129      48.007  31.228  63.924  1.00 21.48           N  
ATOM    979  CA  ALA A 129      47.606  31.165  65.323  1.00 22.27           C  
ATOM    980  C   ALA A 129      47.421  29.705  65.727  1.00 26.71           C  
ATOM    981  O   ALA A 129      47.701  29.311  66.860  1.00 30.05           O  
ATOM    982  CB  ALA A 129      46.302  31.932  65.526  1.00 24.98           C  
ATOM    983  N   PHE A 130      46.957  28.899  64.783  1.00 26.04           N  
ATOM    984  CA  PHE A 130      46.735  27.489  65.038  1.00 21.62           C  
ATOM    985  C   PHE A 130      48.054  26.760  65.258  1.00 26.41           C  
ATOM    986  O   PHE A 130      48.208  25.999  66.220  1.00 31.71           O  
ATOM    987  CB  PHE A 130      46.014  26.860  63.852  1.00 22.58           C  
ATOM    988  CG  PHE A 130      45.645  25.429  64.062  1.00 23.07           C  
ATOM    989  CD1 PHE A 130      44.388  25.088  64.541  1.00 17.30           C  
ATOM    990  CD2 PHE A 130      46.569  24.417  63.817  1.00 25.53           C  
ATOM    991  CE1 PHE A 130      44.052  23.761  64.774  1.00 26.37           C  
ATOM    992  CE2 PHE A 130      46.241  23.081  64.049  1.00 28.13           C  
ATOM    993  CZ  PHE A 130      44.981  22.752  64.529  1.00 17.48           C  
ATOM    994  N   VAL A 131      49.003  26.989  64.356  1.00 20.80           N  
ATOM    995  CA  VAL A 131      50.298  26.337  64.443  1.00 24.26           C  
ATOM    996  C   VAL A 131      51.064  26.754  65.704  1.00 27.52           C  
ATOM    997  O   VAL A 131      51.935  26.024  66.178  1.00 31.45           O  
ATOM    998  CB  VAL A 131      51.151  26.606  63.155  1.00 23.74           C  
ATOM    999  CG1 VAL A 131      51.548  28.065  63.062  1.00 24.06           C  
ATOM   1000  CG2 VAL A 131      52.383  25.723  63.155  1.00 33.06           C  
ATOM   1001  N   ASN A 132      50.723  27.913  66.263  1.00 32.07           N  
ATOM   1002  CA  ASN A 132      51.376  28.394  67.481  1.00 32.39           C  
ATOM   1003  C   ASN A 132      50.665  27.911  68.746  1.00 33.52           C  
ATOM   1004  O   ASN A 132      51.285  27.730  69.795  1.00 30.33           O  
ATOM   1005  CB  ASN A 132      51.443  29.918  67.491  1.00 32.04           C  
ATOM   1006  CG  ASN A 132      52.007  30.454  68.787  1.00 33.69           C  
ATOM   1007  OD1 ASN A 132      51.258  30.870  69.675  1.00 33.61           O  
ATOM   1008  ND2 ASN A 132      53.335  30.425  68.916  1.00 26.76           N  
ATOM   1009  N   SER A 133      49.355  27.725  68.635  1.00 31.12           N  
ATOM   1010  CA  SER A 133      48.550  27.244  69.746  1.00 28.88           C  
ATOM   1011  C   SER A 133      48.690  25.727  69.882  1.00 30.43           C  
ATOM   1012  O   SER A 133      48.541  25.195  70.973  1.00 31.07           O  
ATOM   1013  CB  SER A 133      47.076  27.604  69.529  1.00 16.53           C  
ATOM   1014  OG  SER A 133      46.679  28.670  70.361  1.00 26.41           O  
ATOM   1015  N   TYR A 134      48.980  25.043  68.774  1.00 30.63           N  
ATOM   1016  CA  TYR A 134      49.119  23.586  68.770  1.00 33.35           C  
ATOM   1017  C   TYR A 134      50.371  23.115  68.021  1.00 38.75           C  
ATOM   1018  O   TYR A 134      51.022  23.899  67.327  1.00 37.85           O  
ATOM   1019  CB  TYR A 134      47.875  22.961  68.146  1.00 34.19           C  
ATOM   1020  CG  TYR A 134      46.600  23.397  68.824  1.00 41.61           C  
ATOM   1021  CD1 TYR A 134      46.322  23.016  70.136  1.00 42.54           C  
ATOM   1022  CD2 TYR A 134      45.668  24.192  68.156  1.00 43.87           C  
ATOM   1023  CE1 TYR A 134      45.147  23.411  70.765  1.00 36.10           C  
ATOM   1024  CE2 TYR A 134      44.489  24.593  68.778  1.00 45.12           C  
ATOM   1025  CZ  TYR A 134      44.235  24.194  70.082  1.00 39.76           C  
ATOM   1026  OH  TYR A 134      43.050  24.549  70.683  1.00 40.75           O  
ATOM   1027  N   GLY A 135      50.708  21.835  68.149  1.00 35.16           N  
ATOM   1028  CA  GLY A 135      51.898  21.335  67.476  1.00 42.37           C  
ATOM   1029  C   GLY A 135      52.024  21.715  66.006  1.00 43.53           C  
ATOM   1030  O   GLY A 135      51.061  22.165  65.377  1.00 39.50           O  
ATOM   1031  N   VAL A 136      53.221  21.547  65.451  1.00 41.05           N  
ATOM   1032  CA  VAL A 136      53.422  21.847  64.046  1.00 31.15           C  
ATOM   1033  C   VAL A 136      52.895  20.636  63.283  1.00 31.98           C  
ATOM   1034  O   VAL A 136      52.471  20.750  62.133  1.00 36.68           O  
ATOM   1035  CB  VAL A 136      54.908  22.091  63.701  1.00 29.17           C  
ATOM   1036  CG1 VAL A 136      55.688  20.791  63.726  1.00 27.32           C  
ATOM   1037  CG2 VAL A 136      55.011  22.757  62.354  1.00 30.10           C  
ATOM   1038  N   GLN A 137      52.898  19.471  63.921  1.00 26.67           N  
ATOM   1039  CA  GLN A 137      52.379  18.293  63.243  1.00 31.58           C  
ATOM   1040  C   GLN A 137      50.849  18.282  63.338  1.00 27.59           C  
ATOM   1041  O   GLN A 137      50.181  17.585  62.569  1.00 28.62           O  
ATOM   1042  CB  GLN A 137      52.951  17.003  63.836  1.00 35.44           C  
ATOM   1043  CG  GLN A 137      52.303  16.586  65.127  1.00 44.65           C  
ATOM   1044  CD  GLN A 137      52.521  15.121  65.442  1.00 54.59           C  
ATOM   1045  OE1 GLN A 137      52.058  14.627  66.471  1.00 60.43           O  
ATOM   1046  NE2 GLN A 137      53.224  14.416  64.558  1.00 51.64           N  
ATOM   1047  N   ALA A 138      50.293  19.044  64.281  1.00 21.49           N  
ATOM   1048  CA  ALA A 138      48.834  19.130  64.414  1.00 19.57           C  
ATOM   1049  C   ALA A 138      48.293  19.880  63.191  1.00 23.77           C  
ATOM   1050  O   ALA A 138      47.238  19.542  62.640  1.00 24.33           O  
ATOM   1051  CB  ALA A 138      48.450  19.867  65.691  1.00  9.14           C  
ATOM   1052  N   LEU A 139      49.031  20.904  62.771  1.00 24.72           N  
ATOM   1053  CA  LEU A 139      48.658  21.696  61.605  1.00 26.21           C  
ATOM   1054  C   LEU A 139      48.818  20.799  60.380  1.00 31.38           C  
ATOM   1055  O   LEU A 139      48.142  20.965  59.359  1.00 32.40           O  
ATOM   1056  CB  LEU A 139      49.578  22.905  61.468  1.00 17.04           C  
ATOM   1057  CG  LEU A 139      49.315  23.716  60.204  1.00 18.55           C  
ATOM   1058  CD1 LEU A 139      47.952  24.331  60.307  1.00 13.02           C  
ATOM   1059  CD2 LEU A 139      50.374  24.783  60.023  1.00 26.26           C  
ATOM   1060  N   HIS A 140      49.731  19.844  60.517  1.00 30.08           N  
ATOM   1061  CA  HIS A 140      50.030  18.880  59.481  1.00 32.86           C  
ATOM   1062  C   HIS A 140      48.893  17.868  59.447  1.00 35.63           C  
ATOM   1063  O   HIS A 140      48.441  17.457  58.376  1.00 33.03           O  
ATOM   1064  CB  HIS A 140      51.362  18.193  59.794  1.00 32.62           C  
ATOM   1065  CG  HIS A 140      51.925  17.415  58.648  1.00 37.16           C  
ATOM   1066  ND1 HIS A 140      51.629  16.086  58.431  1.00 37.87           N  
ATOM   1067  CD2 HIS A 140      52.748  17.786  57.639  1.00 35.23           C  
ATOM   1068  CE1 HIS A 140      52.246  15.673  57.338  1.00 33.92           C  
ATOM   1069  NE2 HIS A 140      52.930  16.686  56.838  1.00 37.53           N  
ATOM   1070  N   ASP A 141      48.418  17.472  60.622  1.00 37.12           N  
ATOM   1071  CA  ASP A 141      47.316  16.520  60.670  1.00 37.28           C  
ATOM   1072  C   ASP A 141      46.072  17.174  60.078  1.00 37.24           C  
ATOM   1073  O   ASP A 141      45.252  16.503  59.451  1.00 33.09           O  
ATOM   1074  CB  ASP A 141      47.045  16.056  62.105  1.00 29.62           C  
ATOM   1075  CG  ASP A 141      48.180  15.214  62.670  1.00 33.72           C  
ATOM   1076  OD1 ASP A 141      48.738  14.379  61.922  1.00 28.24           O  
ATOM   1077  OD2 ASP A 141      48.511  15.378  63.864  1.00 35.52           O  
ATOM   1078  N   LYS A 142      45.944  18.487  60.268  1.00 34.73           N  
ATOM   1079  CA  LYS A 142      44.799  19.224  59.739  1.00 29.94           C  
ATOM   1080  C   LYS A 142      44.742  19.089  58.224  1.00 33.14           C  
ATOM   1081  O   LYS A 142      43.685  18.837  57.647  1.00 34.27           O  
ATOM   1082  CB  LYS A 142      44.890  20.709  60.108  1.00 26.78           C  
ATOM   1083  CG  LYS A 142      43.790  21.567  59.472  1.00 33.26           C  
ATOM   1084  CD  LYS A 142      43.940  23.048  59.823  1.00 34.45           C  
ATOM   1085  CE  LYS A 142      43.523  23.351  61.266  1.00 37.98           C  
ATOM   1086  NZ  LYS A 142      42.041  23.234  61.499  1.00 35.74           N  
ATOM   1087  N   LEU A 143      45.890  19.258  57.582  1.00 33.28           N  
ATOM   1088  CA  LEU A 143      45.965  19.165  56.137  1.00 31.63           C  
ATOM   1089  C   LEU A 143      45.849  17.710  55.680  1.00 33.70           C  
ATOM   1090  O   LEU A 143      45.264  17.427  54.637  1.00 29.09           O  
ATOM   1091  CB  LEU A 143      47.277  19.803  55.670  1.00 32.49           C  
ATOM   1092  CG  LEU A 143      47.620  19.894  54.184  1.00 35.77           C  
ATOM   1093  CD1 LEU A 143      48.326  18.627  53.752  1.00 38.08           C  
ATOM   1094  CD2 LEU A 143      46.362  20.144  53.369  1.00 32.56           C  
ATOM   1095  N   SER A 144      46.386  16.796  56.487  1.00 34.97           N  
ATOM   1096  CA  SER A 144      46.371  15.355  56.199  1.00 33.56           C  
ATOM   1097  C   SER A 144      44.942  14.792  56.166  1.00 33.03           C  
ATOM   1098  O   SER A 144      44.658  13.819  55.464  1.00 31.84           O  
ATOM   1099  CB  SER A 144      47.208  14.615  57.260  1.00 34.06           C  
ATOM   1100  OG  SER A 144      47.466  13.269  56.909  1.00 35.74           O  
ATOM   1101  N   LYS A 145      44.048  15.411  56.931  1.00 33.53           N  
ATOM   1102  CA  LYS A 145      42.656  14.984  56.988  1.00 37.93           C  
ATOM   1103  C   LYS A 145      41.845  15.583  55.832  1.00 45.74           C  
ATOM   1104  O   LYS A 145      40.733  15.133  55.543  1.00 44.87           O  
ATOM   1105  CB  LYS A 145      42.026  15.409  58.321  1.00 29.72           C  
ATOM   1106  CG  LYS A 145      40.549  15.066  58.448  1.00 28.94           C  
ATOM   1107  CD  LYS A 145      39.861  15.938  59.473  1.00 40.97           C  
ATOM   1108  CE  LYS A 145      38.341  15.832  59.364  1.00 47.26           C  
ATOM   1109  NZ  LYS A 145      37.640  16.888  60.176  1.00 43.62           N  
ATOM   1110  N   ILE A 146      42.407  16.598  55.177  1.00 48.81           N  
ATOM   1111  CA  ILE A 146      41.742  17.275  54.060  1.00 49.90           C  
ATOM   1112  C   ILE A 146      42.408  16.898  52.728  1.00 49.18           C  
ATOM   1113  O   ILE A 146      41.896  17.202  51.652  1.00 50.06           O  
ATOM   1114  CB  ILE A 146      41.787  18.829  54.258  1.00 47.92           C  
ATOM   1115  CG1 ILE A 146      40.517  19.485  53.705  1.00 52.55           C  
ATOM   1116  CG2 ILE A 146      43.000  19.409  53.565  1.00 48.31           C  
ATOM   1117  CD1 ILE A 146      40.390  19.462  52.190  1.00 52.65           C  
ATOM   1118  N   ASP A 147      43.548  16.223  52.812  1.00 51.98           N  
ATOM   1119  CA  ASP A 147      44.288  15.803  51.626  1.00 52.74           C  
ATOM   1120  C   ASP A 147      45.568  15.096  52.068  1.00 55.61           C  
ATOM   1121  O   ASP A 147      46.649  15.689  52.092  1.00 54.58           O  
ATOM   1122  CB  ASP A 147      44.642  17.015  50.758  1.00 54.78           C  
ATOM   1123  CG  ASP A 147      45.464  16.640  49.537  1.00 58.77           C  
ATOM   1124  OD1 ASP A 147      45.901  17.557  48.807  1.00 62.01           O  
ATOM   1125  OD2 ASP A 147      45.673  15.429  49.307  1.00 62.01           O  
ATOM   1126  N   PRO A 148      45.461  13.808  52.421  1.00 53.79           N  
ATOM   1127  CA  PRO A 148      46.626  13.038  52.864  1.00 53.20           C  
ATOM   1128  C   PRO A 148      47.766  12.969  51.854  1.00 52.22           C  
ATOM   1129  O   PRO A 148      48.933  12.928  52.238  1.00 52.74           O  
ATOM   1130  CB  PRO A 148      46.031  11.667  53.175  1.00 56.55           C  
ATOM   1131  CG  PRO A 148      44.884  11.574  52.209  1.00 62.42           C  
ATOM   1132  CD  PRO A 148      44.269  12.950  52.310  1.00 55.21           C  
ATOM   1133  N   LYS A 149      47.428  12.958  50.567  1.00 53.81           N  
ATOM   1134  CA  LYS A 149      48.437  12.885  49.506  1.00 54.32           C  
ATOM   1135  C   LYS A 149      49.455  14.026  49.598  1.00 52.05           C  
ATOM   1136  O   LYS A 149      50.666  13.793  49.604  1.00 53.54           O  
ATOM   1137  CB  LYS A 149      47.755  12.909  48.128  1.00 58.67           C  
ATOM   1138  CG  LYS A 149      48.727  12.891  46.940  1.00 64.86           C  
ATOM   1139  CD  LYS A 149      48.060  13.248  45.601  1.00 63.99           C  
ATOM   1140  CE  LYS A 149      47.013  12.222  45.142  1.00 63.05           C  
ATOM   1141  NZ  LYS A 149      47.566  10.867  44.832  1.00 63.18           N  
ATOM   1142  N   ALA A 150      48.957  15.259  49.667  1.00 52.55           N  
ATOM   1143  CA  ALA A 150      49.813  16.437  49.758  1.00 48.83           C  
ATOM   1144  C   ALA A 150      50.565  16.424  51.082  1.00 49.61           C  
ATOM   1145  O   ALA A 150      51.756  16.747  51.138  1.00 49.79           O  
ATOM   1146  CB  ALA A 150      48.972  17.701  49.644  1.00 42.55           C  
ATOM   1147  N   ALA A 151      49.859  16.044  52.143  1.00 48.05           N  
ATOM   1148  CA  ALA A 151      50.439  15.972  53.480  1.00 49.23           C  
ATOM   1149  C   ALA A 151      51.696  15.112  53.486  1.00 46.82           C  
ATOM   1150  O   ALA A 151      52.781  15.588  53.813  1.00 44.77           O  
ATOM   1151  CB  ALA A 151      49.415  15.405  54.462  1.00 52.06           C  
ATOM   1152  N   ALA A 152      51.546  13.843  53.120  1.00 47.67           N  
ATOM   1153  CA  ALA A 152      52.673  12.917  53.088  1.00 47.29           C  
ATOM   1154  C   ALA A 152      53.779  13.422  52.172  1.00 48.02           C  
ATOM   1155  O   ALA A 152      54.866  12.849  52.128  1.00 48.31           O  
ATOM   1156  CB  ALA A 152      52.209  11.548  52.625  1.00 46.04           C  
ATOM   1157  N   ALA A 153      53.496  14.499  51.447  1.00 45.43           N  
ATOM   1158  CA  ALA A 153      54.460  15.070  50.523  1.00 45.04           C  
ATOM   1159  C   ALA A 153      55.247  16.233  51.119  1.00 45.78           C  
ATOM   1160  O   ALA A 153      56.127  16.793  50.464  1.00 50.75           O  
ATOM   1161  CB  ALA A 153      53.743  15.521  49.264  1.00 44.41           C  
ATOM   1162  N   ILE A 154      54.943  16.591  52.362  1.00 43.66           N  
ATOM   1163  CA  ILE A 154      55.626  17.703  53.021  1.00 41.54           C  
ATOM   1164  C   ILE A 154      55.986  17.373  54.468  1.00 44.63           C  
ATOM   1165  O   ILE A 154      55.131  16.930  55.233  1.00 45.40           O  
ATOM   1166  CB  ILE A 154      54.736  18.959  53.037  1.00 38.99           C  
ATOM   1167  CG1 ILE A 154      54.256  19.280  51.620  1.00 34.96           C  
ATOM   1168  CG2 ILE A 154      55.504  20.131  53.624  1.00 37.48           C  
ATOM   1169  CD1 ILE A 154      53.077  20.234  51.589  1.00 27.64           C  
ATOM   1170  N   HIS A 155      57.248  17.595  54.837  1.00 47.57           N  
ATOM   1171  CA  HIS A 155      57.713  17.336  56.204  1.00 44.34           C  
ATOM   1172  C   HIS A 155      56.919  18.226  57.147  1.00 38.60           C  
ATOM   1173  O   HIS A 155      56.789  19.425  56.918  1.00 29.52           O  
ATOM   1174  CB  HIS A 155      59.195  17.678  56.348  1.00 48.55           C  
ATOM   1175  CG  HIS A 155      59.851  17.067  57.549  1.00 57.50           C  
ATOM   1176  ND1 HIS A 155      60.904  17.667  58.206  1.00 64.13           N  
ATOM   1177  CD2 HIS A 155      59.661  15.873  58.162  1.00 62.32           C  
ATOM   1178  CE1 HIS A 155      61.337  16.870  59.168  1.00 64.39           C  
ATOM   1179  NE2 HIS A 155      60.599  15.774  59.161  1.00 64.50           N  
ATOM   1180  N   PRO A 156      56.390  17.648  58.234  1.00 42.36           N  
ATOM   1181  CA  PRO A 156      55.604  18.424  59.199  1.00 43.70           C  
ATOM   1182  C   PRO A 156      56.294  19.671  59.785  1.00 38.34           C  
ATOM   1183  O   PRO A 156      55.616  20.609  60.205  1.00 38.73           O  
ATOM   1184  CB  PRO A 156      55.212  17.375  60.252  1.00 41.93           C  
ATOM   1185  CG  PRO A 156      56.259  16.313  60.116  1.00 38.96           C  
ATOM   1186  CD  PRO A 156      56.493  16.235  58.642  1.00 38.34           C  
ATOM   1187  N   ASN A 157      57.626  19.689  59.794  1.00 33.91           N  
ATOM   1188  CA  ASN A 157      58.388  20.837  60.311  1.00 32.97           C  
ATOM   1189  C   ASN A 157      58.373  22.003  59.309  1.00 31.53           C  
ATOM   1190  O   ASN A 157      58.815  23.114  59.614  1.00 27.84           O  
ATOM   1191  CB  ASN A 157      59.855  20.445  60.597  1.00 32.92           C  
ATOM   1192  CG  ASN A 157      60.047  19.767  61.958  1.00 32.95           C  
ATOM   1193  OD1 ASN A 157      59.451  18.732  62.242  1.00 35.69           O  
ATOM   1194  ND2 ASN A 157      60.897  20.355  62.798  1.00 36.74           N  
ATOM   1195  N   ASN A 158      57.875  21.750  58.106  1.00 30.44           N  
ATOM   1196  CA  ASN A 158      57.818  22.799  57.096  1.00 32.86           C  
ATOM   1197  C   ASN A 158      56.428  23.432  57.133  1.00 28.95           C  
ATOM   1198  O   ASN A 158      55.712  23.412  56.142  1.00 28.84           O  
ATOM   1199  CB  ASN A 158      58.079  22.203  55.710  1.00 33.30           C  
ATOM   1200  CG  ASN A 158      58.446  23.255  54.680  1.00 37.90           C  
ATOM   1201  OD1 ASN A 158      58.368  24.459  54.944  1.00 46.28           O  
ATOM   1202  ND2 ASN A 158      58.847  22.806  53.495  1.00 32.74           N  
ATOM   1203  N   TYR A 159      56.064  23.999  58.282  1.00 31.66           N  
ATOM   1204  CA  TYR A 159      54.759  24.617  58.478  1.00 28.45           C  
ATOM   1205  C   TYR A 159      54.430  25.702  57.464  1.00 34.40           C  
ATOM   1206  O   TYR A 159      53.257  25.959  57.176  1.00 37.11           O  
ATOM   1207  CB  TYR A 159      54.653  25.218  59.875  1.00 26.86           C  
ATOM   1208  CG  TYR A 159      55.501  26.460  60.077  1.00 31.56           C  
ATOM   1209  CD1 TYR A 159      56.804  26.371  60.575  1.00 26.39           C  
ATOM   1210  CD2 TYR A 159      54.992  27.731  59.778  1.00 33.39           C  
ATOM   1211  CE1 TYR A 159      57.578  27.513  60.776  1.00 23.84           C  
ATOM   1212  CE2 TYR A 159      55.758  28.880  59.970  1.00 29.44           C  
ATOM   1213  CZ  TYR A 159      57.048  28.766  60.473  1.00 32.64           C  
ATOM   1214  OH  TYR A 159      57.786  29.913  60.693  1.00 22.38           O  
ATOM   1215  N   ARG A 160      55.456  26.353  56.934  1.00 30.79           N  
ATOM   1216  CA  ARG A 160      55.239  27.407  55.956  1.00 34.33           C  
ATOM   1217  C   ARG A 160      54.598  26.828  54.700  1.00 33.01           C  
ATOM   1218  O   ARG A 160      53.663  27.405  54.141  1.00 32.85           O  
ATOM   1219  CB  ARG A 160      56.564  28.080  55.593  1.00 45.20           C  
ATOM   1220  CG  ARG A 160      56.392  29.542  55.259  1.00 51.58           C  
ATOM   1221  CD  ARG A 160      55.884  30.278  56.486  1.00 56.45           C  
ATOM   1222  NE  ARG A 160      54.892  31.297  56.151  1.00 53.62           N  
ATOM   1223  CZ  ARG A 160      54.306  32.085  57.045  1.00 49.72           C  
ATOM   1224  NH1 ARG A 160      54.608  31.975  58.335  1.00 41.44           N  
ATOM   1225  NH2 ARG A 160      53.419  32.983  56.649  1.00 45.69           N  
ATOM   1226  N   ARG A 161      55.106  25.680  54.267  1.00 32.57           N  
ATOM   1227  CA  ARG A 161      54.595  25.010  53.081  1.00 34.32           C  
ATOM   1228  C   ARG A 161      53.248  24.338  53.371  1.00 30.91           C  
ATOM   1229  O   ARG A 161      52.448  24.121  52.465  1.00 23.13           O  
ATOM   1230  CB  ARG A 161      55.619  23.984  52.591  1.00 37.02           C  
ATOM   1231  CG  ARG A 161      55.278  23.320  51.270  1.00 48.52           C  
ATOM   1232  CD  ARG A 161      56.440  22.453  50.795  1.00 60.90           C  
ATOM   1233  NE  ARG A 161      56.100  21.650  49.620  1.00 62.32           N  
ATOM   1234  CZ  ARG A 161      56.964  20.874  48.970  1.00 66.59           C  
ATOM   1235  NH1 ARG A 161      58.226  20.793  49.376  1.00 63.24           N  
ATOM   1236  NH2 ARG A 161      56.565  20.177  47.914  1.00 65.97           N  
ATOM   1237  N   VAL A 162      52.998  24.014  54.637  1.00 31.02           N  
ATOM   1238  CA  VAL A 162      51.734  23.399  55.019  1.00 26.78           C  
ATOM   1239  C   VAL A 162      50.661  24.480  55.049  1.00 23.51           C  
ATOM   1240  O   VAL A 162      49.529  24.253  54.638  1.00 30.43           O  
ATOM   1241  CB  VAL A 162      51.839  22.721  56.399  1.00 26.46           C  
ATOM   1242  CG1 VAL A 162      50.459  22.289  56.892  1.00 27.58           C  
ATOM   1243  CG2 VAL A 162      52.762  21.515  56.300  1.00 23.80           C  
ATOM   1244  N   ILE A 163      51.009  25.664  55.527  1.00 20.51           N  
ATOM   1245  CA  ILE A 163      50.030  26.743  55.549  1.00 28.22           C  
ATOM   1246  C   ILE A 163      49.631  27.087  54.113  1.00 22.37           C  
ATOM   1247  O   ILE A 163      48.471  27.363  53.827  1.00 19.58           O  
ATOM   1248  CB  ILE A 163      50.599  28.002  56.233  1.00 27.75           C  
ATOM   1249  CG1 ILE A 163      50.628  27.783  57.748  1.00 32.24           C  
ATOM   1250  CG2 ILE A 163      49.768  29.229  55.860  1.00 26.80           C  
ATOM   1251  CD1 ILE A 163      51.217  28.915  58.522  1.00 24.52           C  
ATOM   1252  N   ARG A 164      50.609  27.075  53.217  1.00 30.20           N  
ATOM   1253  CA  ARG A 164      50.368  27.383  51.814  1.00 27.56           C  
ATOM   1254  C   ARG A 164      49.359  26.400  51.221  1.00 28.56           C  
ATOM   1255  O   ARG A 164      48.439  26.794  50.508  1.00 29.33           O  
ATOM   1256  CB  ARG A 164      51.691  27.316  51.051  1.00 31.21           C  
ATOM   1257  CG  ARG A 164      51.561  27.225  49.541  1.00 41.60           C  
ATOM   1258  CD  ARG A 164      51.009  28.501  48.929  1.00 49.34           C  
ATOM   1259  NE  ARG A 164      51.917  29.047  47.922  1.00 55.25           N  
ATOM   1260  CZ  ARG A 164      52.360  28.377  46.861  1.00 62.55           C  
ATOM   1261  NH1 ARG A 164      51.985  27.120  46.652  1.00 64.47           N  
ATOM   1262  NH2 ARG A 164      53.187  28.963  46.006  1.00 64.55           N  
ATOM   1263  N   ALA A 165      49.536  25.118  51.523  1.00 31.48           N  
ATOM   1264  CA  ALA A 165      48.643  24.078  51.016  1.00 25.51           C  
ATOM   1265  C   ALA A 165      47.208  24.273  51.491  1.00 23.71           C  
ATOM   1266  O   ALA A 165      46.264  24.106  50.721  1.00 26.71           O  
ATOM   1267  CB  ALA A 165      49.144  22.707  51.447  1.00 23.07           C  
ATOM   1268  N   LEU A 166      47.044  24.621  52.761  1.00 16.69           N  
ATOM   1269  CA  LEU A 166      45.712  24.816  53.308  1.00 21.14           C  
ATOM   1270  C   LEU A 166      45.034  26.062  52.734  1.00 27.20           C  
ATOM   1271  O   LEU A 166      43.810  26.106  52.623  1.00 24.64           O  
ATOM   1272  CB  LEU A 166      45.772  24.903  54.840  1.00 21.59           C  
ATOM   1273  CG  LEU A 166      46.346  23.681  55.590  1.00 28.07           C  
ATOM   1274  CD1 LEU A 166      46.700  24.059  57.027  1.00 21.39           C  
ATOM   1275  CD2 LEU A 166      45.342  22.543  55.570  1.00 27.66           C  
ATOM   1276  N   GLU A 167      45.814  27.076  52.363  1.00 27.34           N  
ATOM   1277  CA  GLU A 167      45.212  28.287  51.813  1.00 30.23           C  
ATOM   1278  C   GLU A 167      44.735  28.026  50.391  1.00 29.79           C  
ATOM   1279  O   GLU A 167      43.663  28.479  49.994  1.00 23.61           O  
ATOM   1280  CB  GLU A 167      46.204  29.460  51.794  1.00 32.17           C  
ATOM   1281  CG  GLU A 167      46.782  29.886  53.141  1.00 34.09           C  
ATOM   1282  CD  GLU A 167      47.591  31.179  53.041  1.00 32.25           C  
ATOM   1283  OE1 GLU A 167      46.979  32.264  52.998  1.00 43.01           O  
ATOM   1284  OE2 GLU A 167      48.836  31.118  52.987  1.00 28.22           O  
ATOM   1285  N   ILE A 168      45.546  27.302  49.626  1.00 32.43           N  
ATOM   1286  CA  ILE A 168      45.200  26.982  48.249  1.00 32.42           C  
ATOM   1287  C   ILE A 168      43.912  26.165  48.202  1.00 35.12           C  
ATOM   1288  O   ILE A 168      43.060  26.383  47.337  1.00 38.47           O  
ATOM   1289  CB  ILE A 168      46.327  26.196  47.558  1.00 30.75           C  
ATOM   1290  CG1 ILE A 168      47.524  27.129  47.308  1.00 37.79           C  
ATOM   1291  CG2 ILE A 168      45.818  25.590  46.260  1.00 36.14           C  
ATOM   1292  CD1 ILE A 168      48.715  26.470  46.606  1.00 20.96           C  
ATOM   1293  N   ILE A 169      43.768  25.237  49.146  1.00 36.95           N  
ATOM   1294  CA  ILE A 169      42.587  24.376  49.226  1.00 28.46           C  
ATOM   1295  C   ILE A 169      41.347  25.201  49.548  1.00 30.78           C  
ATOM   1296  O   ILE A 169      40.299  25.044  48.911  1.00 33.88           O  
ATOM   1297  CB  ILE A 169      42.783  23.267  50.300  1.00 27.25           C  
ATOM   1298  CG1 ILE A 169      43.871  22.292  49.828  1.00 23.20           C  
ATOM   1299  CG2 ILE A 169      41.462  22.541  50.568  1.00 26.60           C  
ATOM   1300  CD1 ILE A 169      44.303  21.249  50.856  1.00 19.59           C  
ATOM   1301  N   LYS A 170      41.476  26.086  50.532  1.00 30.89           N  
ATOM   1302  CA  LYS A 170      40.380  26.958  50.938  1.00 30.86           C  
ATOM   1303  C   LYS A 170      39.920  27.813  49.754  1.00 30.85           C  
ATOM   1304  O   LYS A 170      38.781  28.266  49.718  1.00 30.67           O  
ATOM   1305  CB  LYS A 170      40.821  27.868  52.090  1.00 34.60           C  
ATOM   1306  CG  LYS A 170      39.711  28.764  52.644  1.00 42.00           C  
ATOM   1307  CD  LYS A 170      40.201  30.198  52.879  1.00 50.12           C  
ATOM   1308  CE  LYS A 170      40.570  30.897  51.565  1.00 55.63           C  
ATOM   1309  NZ  LYS A 170      41.285  32.194  51.771  1.00 47.57           N  
ATOM   1310  N   LEU A 171      40.804  28.045  48.789  1.00 36.14           N  
ATOM   1311  CA  LEU A 171      40.421  28.839  47.631  1.00 45.11           C  
ATOM   1312  C   LEU A 171      39.416  28.094  46.767  1.00 47.95           C  
ATOM   1313  O   LEU A 171      38.436  28.674  46.306  1.00 51.41           O  
ATOM   1314  CB  LEU A 171      41.639  29.196  46.787  1.00 38.16           C  
ATOM   1315  CG  LEU A 171      42.374  30.472  47.193  1.00 37.40           C  
ATOM   1316  CD1 LEU A 171      43.586  30.651  46.293  1.00 30.42           C  
ATOM   1317  CD2 LEU A 171      41.443  31.674  47.069  1.00 41.73           C  
ATOM   1318  N   THR A 172      39.654  26.804  46.564  1.00 51.34           N  
ATOM   1319  CA  THR A 172      38.773  25.990  45.740  1.00 56.54           C  
ATOM   1320  C   THR A 172      37.555  25.455  46.490  1.00 58.07           C  
ATOM   1321  O   THR A 172      36.935  24.485  46.057  1.00 60.19           O  
ATOM   1322  CB  THR A 172      39.538  24.797  45.141  1.00 58.17           C  
ATOM   1323  OG1 THR A 172      38.709  24.135  44.178  1.00 60.05           O  
ATOM   1324  CG2 THR A 172      39.920  23.812  46.234  1.00 56.07           C  
ATOM   1325  N   GLY A 173      37.215  26.087  47.608  1.00 57.38           N  
ATOM   1326  CA  GLY A 173      36.073  25.641  48.387  1.00 57.37           C  
ATOM   1327  C   GLY A 173      34.867  26.555  48.268  1.00 59.80           C  
ATOM   1328  O   GLY A 173      34.908  27.572  47.574  1.00 62.28           O  
ATOM   1329  N   SER A 188      19.912  36.615  33.563  1.00 35.32           N  
ATOM   1330  CA  SER A 188      20.141  37.888  32.900  1.00 34.45           C  
ATOM   1331  C   SER A 188      19.361  39.044  33.512  1.00 34.62           C  
ATOM   1332  O   SER A 188      18.158  38.937  33.758  1.00 38.36           O  
ATOM   1333  CB  SER A 188      19.769  37.800  31.424  1.00 32.47           C  
ATOM   1334  OG  SER A 188      20.038  39.037  30.784  1.00 36.80           O  
ATOM   1335  N   PRO A 189      20.040  40.174  33.761  1.00 26.47           N  
ATOM   1336  CA  PRO A 189      19.388  41.346  34.338  1.00 26.91           C  
ATOM   1337  C   PRO A 189      18.669  42.174  33.275  1.00 27.90           C  
ATOM   1338  O   PRO A 189      17.933  43.097  33.608  1.00 36.13           O  
ATOM   1339  CB  PRO A 189      20.552  42.112  34.949  1.00 26.96           C  
ATOM   1340  CG  PRO A 189      21.627  41.879  33.936  1.00 25.98           C  
ATOM   1341  CD  PRO A 189      21.500  40.373  33.718  1.00 24.27           C  
ATOM   1342  N   TYR A 190      18.889  41.862  31.999  1.00 25.65           N  
ATOM   1343  CA  TYR A 190      18.242  42.616  30.918  1.00 26.26           C  
ATOM   1344  C   TYR A 190      16.960  41.959  30.389  1.00 23.11           C  
ATOM   1345  O   TYR A 190      16.682  40.784  30.654  1.00 22.59           O  
ATOM   1346  CB  TYR A 190      19.194  42.795  29.717  1.00 17.80           C  
ATOM   1347  CG  TYR A 190      20.489  43.527  29.985  1.00 23.28           C  
ATOM   1348  CD1 TYR A 190      21.672  42.833  30.186  1.00 20.39           C  
ATOM   1349  CD2 TYR A 190      20.525  44.921  30.039  1.00 28.23           C  
ATOM   1350  CE1 TYR A 190      22.860  43.501  30.436  1.00 29.32           C  
ATOM   1351  CE2 TYR A 190      21.709  45.605  30.291  1.00 28.01           C  
ATOM   1352  CZ  TYR A 190      22.878  44.886  30.490  1.00 32.20           C  
ATOM   1353  OH  TYR A 190      24.057  45.550  30.748  1.00 28.54           O  
ATOM   1354  N   ASN A 191      16.180  42.748  29.653  1.00 17.92           N  
ATOM   1355  CA  ASN A 191      14.972  42.258  28.993  1.00 26.15           C  
ATOM   1356  C   ASN A 191      15.635  41.876  27.678  1.00 21.29           C  
ATOM   1357  O   ASN A 191      15.647  42.657  26.723  1.00 23.06           O  
ATOM   1358  CB  ASN A 191      13.970  43.401  28.764  1.00 27.14           C  
ATOM   1359  CG  ASN A 191      12.764  42.974  27.938  1.00 25.49           C  
ATOM   1360  OD1 ASN A 191      12.780  41.928  27.280  1.00 22.32           O  
ATOM   1361  ND2 ASN A 191      11.720  43.796  27.952  1.00 19.77           N  
ATOM   1362  N   LEU A 192      16.230  40.690  27.658  1.00 23.72           N  
ATOM   1363  CA  LEU A 192      16.954  40.229  26.493  1.00 16.53           C  
ATOM   1364  C   LEU A 192      16.199  39.341  25.517  1.00 21.69           C  
ATOM   1365  O   LEU A 192      15.377  38.501  25.897  1.00 20.09           O  
ATOM   1366  CB  LEU A 192      18.242  39.524  26.938  1.00 19.93           C  
ATOM   1367  CG  LEU A 192      19.225  39.007  25.868  1.00 25.54           C  
ATOM   1368  CD1 LEU A 192      20.607  38.936  26.456  1.00 20.26           C  
ATOM   1369  CD2 LEU A 192      18.797  37.631  25.368  1.00 31.03           C  
ATOM   1370  N   VAL A 193      16.497  39.578  24.242  1.00 21.52           N  
ATOM   1371  CA  VAL A 193      15.968  38.832  23.117  1.00 18.37           C  
ATOM   1372  C   VAL A 193      17.225  38.486  22.313  1.00 20.97           C  
ATOM   1373  O   VAL A 193      17.943  39.366  21.820  1.00 25.36           O  
ATOM   1374  CB  VAL A 193      15.001  39.676  22.256  1.00 21.31           C  
ATOM   1375  CG1 VAL A 193      14.577  38.888  21.024  1.00 20.35           C  
ATOM   1376  CG2 VAL A 193      13.768  40.045  23.072  1.00 19.46           C  
HETATM 1377  N   MSE A 194      17.505  37.194  22.224  1.00 20.08           N  
HETATM 1378  CA  MSE A 194      18.674  36.711  21.522  1.00 18.81           C  
HETATM 1379  C   MSE A 194      18.254  35.911  20.295  1.00 16.61           C  
HETATM 1380  O   MSE A 194      17.500  34.948  20.409  1.00 20.57           O  
HETATM 1381  CB  MSE A 194      19.485  35.830  22.465  1.00 11.96           C  
HETATM 1382  CG  MSE A 194      20.965  35.818  22.182  1.00 36.83           C  
HETATM 1383 SE   MSE A 194      21.977  35.005  23.619  1.00 54.64          SE  
HETATM 1384  CE  MSE A 194      23.234  34.012  22.541  1.00 55.76           C  
ATOM   1385  N   ILE A 195      18.731  36.312  19.124  1.00 16.88           N  
ATOM   1386  CA  ILE A 195      18.399  35.601  17.892  1.00 17.52           C  
ATOM   1387  C   ILE A 195      19.682  35.069  17.278  1.00 16.25           C  
ATOM   1388  O   ILE A 195      20.741  35.670  17.430  1.00 19.45           O  
ATOM   1389  CB  ILE A 195      17.725  36.528  16.853  1.00 21.56           C  
ATOM   1390  CG1 ILE A 195      18.652  37.698  16.540  1.00 23.79           C  
ATOM   1391  CG2 ILE A 195      16.374  37.033  17.376  1.00 21.92           C  
ATOM   1392  CD1 ILE A 195      18.169  38.581  15.431  1.00 28.70           C  
ATOM   1393  N   GLY A 196      19.595  33.942  16.584  1.00 22.78           N  
ATOM   1394  CA  GLY A 196      20.782  33.387  15.961  1.00 19.23           C  
ATOM   1395  C   GLY A 196      20.567  33.188  14.475  1.00 19.23           C  
ATOM   1396  O   GLY A 196      19.488  32.774  14.053  1.00 21.94           O  
ATOM   1397  N   LEU A 197      21.589  33.507  13.684  1.00 20.83           N  
ATOM   1398  CA  LEU A 197      21.543  33.351  12.234  1.00 14.88           C  
ATOM   1399  C   LEU A 197      22.404  32.149  11.842  1.00 20.08           C  
ATOM   1400  O   LEU A 197      23.579  32.077  12.207  1.00 19.85           O  
ATOM   1401  CB  LEU A 197      22.063  34.620  11.553  1.00 15.55           C  
ATOM   1402  CG  LEU A 197      21.379  35.914  12.028  1.00 16.36           C  
ATOM   1403  CD1 LEU A 197      21.842  37.085  11.170  1.00  6.92           C  
ATOM   1404  CD2 LEU A 197      19.867  35.758  11.948  1.00  4.71           C  
ATOM   1405  N   THR A 198      21.802  31.202  11.121  1.00 25.06           N  
ATOM   1406  CA  THR A 198      22.479  29.987  10.680  1.00 21.19           C  
ATOM   1407  C   THR A 198      22.358  29.902   9.192  1.00 22.24           C  
ATOM   1408  O   THR A 198      21.775  30.773   8.547  1.00 21.66           O  
ATOM   1409  CB  THR A 198      21.808  28.693  11.166  1.00 25.81           C  
ATOM   1410  OG1 THR A 198      21.044  28.952  12.342  1.00 39.46           O  
ATOM   1411  CG2 THR A 198      22.855  27.625  11.442  1.00 28.68           C  
HETATM 1412  N   MSE A 199      22.851  28.789   8.664  1.00 21.83           N  
HETATM 1413  CA  MSE A 199      22.830  28.555   7.234  1.00 25.92           C  
HETATM 1414  C   MSE A 199      23.284  27.127   6.971  1.00 25.26           C  
HETATM 1415  O   MSE A 199      23.996  26.538   7.783  1.00 27.72           O  
HETATM 1416  CB  MSE A 199      23.786  29.546   6.578  1.00 27.42           C  
HETATM 1417  CG  MSE A 199      23.512  29.882   5.131  1.00 30.58           C  
HETATM 1418 SE   MSE A 199      24.771  31.255   4.528  1.00 35.33          SE  
HETATM 1419  CE  MSE A 199      23.828  32.835   5.094  1.00 24.55           C  
ATOM   1420  N   GLU A 200      22.862  26.575   5.839  1.00 29.10           N  
ATOM   1421  CA  GLU A 200      23.234  25.219   5.447  1.00 27.34           C  
ATOM   1422  C   GLU A 200      24.758  25.071   5.415  1.00 28.10           C  
ATOM   1423  O   GLU A 200      25.469  25.980   4.982  1.00 23.05           O  
ATOM   1424  CB  GLU A 200      22.632  24.896   4.072  1.00 26.88           C  
ATOM   1425  CG  GLU A 200      21.231  24.292   4.142  1.00 48.69           C  
ATOM   1426  CD  GLU A 200      20.447  24.403   2.833  1.00 56.19           C  
ATOM   1427  OE1 GLU A 200      21.027  24.162   1.747  1.00 56.76           O  
ATOM   1428  OE2 GLU A 200      19.238  24.721   2.898  1.00 57.12           O  
ATOM   1429  N   ARG A 201      25.240  23.920   5.885  1.00 32.01           N  
ATOM   1430  CA  ARG A 201      26.672  23.587   5.966  1.00 28.59           C  
ATOM   1431  C   ARG A 201      27.527  24.022   4.781  1.00 26.37           C  
ATOM   1432  O   ARG A 201      28.365  24.921   4.893  1.00 19.62           O  
ATOM   1433  CB  ARG A 201      26.836  22.067   6.155  1.00 36.95           C  
ATOM   1434  CG  ARG A 201      28.254  21.589   6.496  1.00 44.77           C  
ATOM   1435  CD  ARG A 201      28.780  22.225   7.791  1.00 54.63           C  
ATOM   1436  NE  ARG A 201      27.942  21.947   8.963  1.00 59.23           N  
ATOM   1437  CZ  ARG A 201      28.092  22.523  10.158  1.00 64.75           C  
ATOM   1438  NH1 ARG A 201      29.048  23.421  10.366  1.00 65.16           N  
ATOM   1439  NH2 ARG A 201      27.277  22.207  11.154  1.00 67.99           N  
ATOM   1440  N   ASP A 202      27.317  23.352   3.653  1.00 24.74           N  
ATOM   1441  CA  ASP A 202      28.067  23.608   2.431  1.00 27.62           C  
ATOM   1442  C   ASP A 202      28.041  25.050   1.946  1.00 28.64           C  
ATOM   1443  O   ASP A 202      29.051  25.565   1.466  1.00 32.52           O  
ATOM   1444  CB  ASP A 202      27.562  22.688   1.323  1.00 33.15           C  
ATOM   1445  CG  ASP A 202      27.754  21.226   1.655  1.00 36.68           C  
ATOM   1446  OD1 ASP A 202      27.339  20.376   0.840  1.00 46.98           O  
ATOM   1447  OD2 ASP A 202      28.321  20.927   2.730  1.00 40.03           O  
ATOM   1448  N   VAL A 203      26.883  25.692   2.059  1.00 26.64           N  
ATOM   1449  CA  VAL A 203      26.720  27.074   1.630  1.00 22.63           C  
ATOM   1450  C   VAL A 203      27.589  27.988   2.480  1.00 18.91           C  
ATOM   1451  O   VAL A 203      28.357  28.783   1.952  1.00 16.86           O  
ATOM   1452  CB  VAL A 203      25.228  27.508   1.731  1.00 27.96           C  
ATOM   1453  CG1 VAL A 203      25.091  29.000   1.532  1.00 27.65           C  
ATOM   1454  CG2 VAL A 203      24.407  26.784   0.667  1.00 26.48           C  
ATOM   1455  N   LEU A 204      27.470  27.853   3.798  1.00 19.00           N  
ATOM   1456  CA  LEU A 204      28.235  28.649   4.742  1.00 12.96           C  
ATOM   1457  C   LEU A 204      29.743  28.528   4.520  1.00 19.18           C  
ATOM   1458  O   LEU A 204      30.472  29.527   4.580  1.00 26.26           O  
ATOM   1459  CB  LEU A 204      27.900  28.223   6.172  1.00  9.02           C  
ATOM   1460  CG  LEU A 204      28.706  28.986   7.229  1.00 14.57           C  
ATOM   1461  CD1 LEU A 204      28.182  30.402   7.303  1.00 14.83           C  
ATOM   1462  CD2 LEU A 204      28.609  28.309   8.593  1.00 14.86           C  
ATOM   1463  N   TYR A 205      30.218  27.307   4.275  1.00 20.83           N  
ATOM   1464  CA  TYR A 205      31.646  27.066   4.056  1.00 16.62           C  
ATOM   1465  C   TYR A 205      32.154  27.772   2.805  1.00 16.02           C  
ATOM   1466  O   TYR A 205      33.199  28.429   2.834  1.00  8.68           O  
ATOM   1467  CB  TYR A 205      31.948  25.555   3.963  1.00 17.58           C  
ATOM   1468  CG  TYR A 205      31.970  24.827   5.299  1.00 21.62           C  
ATOM   1469  CD1 TYR A 205      31.843  25.531   6.498  1.00 25.27           C  
ATOM   1470  CD2 TYR A 205      32.123  23.439   5.366  1.00 18.51           C  
ATOM   1471  CE1 TYR A 205      31.861  24.882   7.730  1.00 17.78           C  
ATOM   1472  CE2 TYR A 205      32.146  22.772   6.606  1.00 20.88           C  
ATOM   1473  CZ  TYR A 205      32.011  23.510   7.783  1.00 25.77           C  
ATOM   1474  OH  TYR A 205      32.016  22.899   9.025  1.00 24.51           O  
ATOM   1475  N   ASP A 206      31.422  27.642   1.705  1.00 14.61           N  
ATOM   1476  CA  ASP A 206      31.843  28.293   0.465  1.00 24.98           C  
ATOM   1477  C   ASP A 206      31.920  29.793   0.654  1.00 23.26           C  
ATOM   1478  O   ASP A 206      32.847  30.438   0.163  1.00 20.89           O  
ATOM   1479  CB  ASP A 206      30.874  27.983  -0.676  1.00 25.91           C  
ATOM   1480  CG  ASP A 206      30.960  26.547  -1.134  1.00 33.73           C  
ATOM   1481  OD1 ASP A 206      30.221  26.184  -2.069  1.00 42.39           O  
ATOM   1482  OD2 ASP A 206      31.764  25.780  -0.564  1.00 35.05           O  
ATOM   1483  N   ARG A 207      30.946  30.355   1.365  1.00 19.86           N  
ATOM   1484  CA  ARG A 207      30.955  31.796   1.589  1.00 21.77           C  
ATOM   1485  C   ARG A 207      32.138  32.190   2.471  1.00 14.07           C  
ATOM   1486  O   ARG A 207      32.614  33.319   2.395  1.00  4.24           O  
ATOM   1487  CB  ARG A 207      29.634  32.260   2.224  1.00 21.45           C  
ATOM   1488  CG  ARG A 207      28.443  32.314   1.263  1.00 28.35           C  
ATOM   1489  CD  ARG A 207      27.142  32.414   2.045  1.00 21.92           C  
ATOM   1490  NE  ARG A 207      27.084  33.631   2.839  1.00 38.95           N  
ATOM   1491  CZ  ARG A 207      26.633  34.797   2.388  1.00 45.55           C  
ATOM   1492  NH1 ARG A 207      26.193  34.895   1.143  1.00 47.01           N  
ATOM   1493  NH2 ARG A 207      26.632  35.867   3.178  1.00 51.80           N  
ATOM   1494  N   ILE A 208      32.610  31.251   3.294  1.00 12.52           N  
ATOM   1495  CA  ILE A 208      33.741  31.509   4.173  1.00 11.42           C  
ATOM   1496  C   ILE A 208      35.044  31.464   3.361  1.00 13.78           C  
ATOM   1497  O   ILE A 208      35.941  32.278   3.582  1.00 11.75           O  
ATOM   1498  CB  ILE A 208      33.770  30.502   5.353  1.00 17.89           C  
ATOM   1499  CG1 ILE A 208      32.586  30.792   6.295  1.00 16.24           C  
ATOM   1500  CG2 ILE A 208      35.098  30.576   6.106  1.00  5.82           C  
ATOM   1501  CD1 ILE A 208      32.409  29.809   7.421  1.00  5.80           C  
ATOM   1502  N   ASN A 209      35.138  30.538   2.408  1.00 19.35           N  
ATOM   1503  CA  ASN A 209      36.329  30.448   1.573  1.00 14.40           C  
ATOM   1504  C   ASN A 209      36.433  31.680   0.682  1.00 13.39           C  
ATOM   1505  O   ASN A 209      37.516  32.245   0.492  1.00 14.08           O  
ATOM   1506  CB  ASN A 209      36.302  29.207   0.682  1.00 13.00           C  
ATOM   1507  CG  ASN A 209      36.267  27.917   1.468  1.00  9.22           C  
ATOM   1508  OD1 ASN A 209      36.891  27.786   2.525  1.00 13.69           O  
ATOM   1509  ND2 ASN A 209      35.546  26.944   0.944  1.00 13.67           N  
ATOM   1510  N   ARG A 210      35.310  32.095   0.123  1.00  5.30           N  
ATOM   1511  CA  ARG A 210      35.313  33.269  -0.730  1.00 17.91           C  
ATOM   1512  C   ARG A 210      35.659  34.506   0.114  1.00 20.06           C  
ATOM   1513  O   ARG A 210      36.305  35.438  -0.362  1.00 20.12           O  
ATOM   1514  CB  ARG A 210      33.949  33.429  -1.418  1.00 24.43           C  
ATOM   1515  CG  ARG A 210      33.746  34.761  -2.119  1.00 17.06           C  
ATOM   1516  CD  ARG A 210      34.853  35.027  -3.105  1.00 23.85           C  
ATOM   1517  NE  ARG A 210      34.666  36.307  -3.781  1.00 37.92           N  
ATOM   1518  CZ  ARG A 210      35.606  36.905  -4.502  1.00 41.97           C  
ATOM   1519  NH1 ARG A 210      36.797  36.334  -4.634  1.00 46.25           N  
ATOM   1520  NH2 ARG A 210      35.358  38.066  -5.091  1.00 42.71           N  
ATOM   1521  N   ARG A 211      35.240  34.512   1.371  1.00 21.31           N  
ATOM   1522  CA  ARG A 211      35.563  35.638   2.227  1.00 21.01           C  
ATOM   1523  C   ARG A 211      37.086  35.714   2.327  1.00 21.04           C  
ATOM   1524  O   ARG A 211      37.664  36.800   2.273  1.00 18.85           O  
ATOM   1525  CB  ARG A 211      34.959  35.451   3.617  1.00 27.18           C  
ATOM   1526  CG  ARG A 211      34.298  36.693   4.196  1.00 39.91           C  
ATOM   1527  CD  ARG A 211      35.005  37.198   5.451  1.00 47.31           C  
ATOM   1528  NE  ARG A 211      35.464  36.115   6.325  1.00 54.71           N  
ATOM   1529  CZ  ARG A 211      35.601  36.221   7.646  1.00 59.33           C  
ATOM   1530  NH1 ARG A 211      36.036  35.187   8.357  1.00 49.15           N  
ATOM   1531  NH2 ARG A 211      35.276  37.353   8.261  1.00 52.26           N  
ATOM   1532  N   VAL A 212      37.737  34.559   2.459  1.00 16.89           N  
ATOM   1533  CA  VAL A 212      39.199  34.518   2.569  1.00 17.27           C  
ATOM   1534  C   VAL A 212      39.878  35.061   1.317  1.00 19.14           C  
ATOM   1535  O   VAL A 212      40.785  35.896   1.395  1.00 16.03           O  
ATOM   1536  CB  VAL A 212      39.713  33.084   2.841  1.00 11.98           C  
ATOM   1537  CG1 VAL A 212      41.243  33.050   2.801  1.00  8.01           C  
ATOM   1538  CG2 VAL A 212      39.231  32.627   4.190  1.00 10.24           C  
ATOM   1539  N   ASP A 213      39.444  34.577   0.160  1.00 23.75           N  
ATOM   1540  CA  ASP A 213      40.013  35.047  -1.082  1.00 23.22           C  
ATOM   1541  C   ASP A 213      39.814  36.559  -1.119  1.00 25.08           C  
ATOM   1542  O   ASP A 213      40.734  37.304  -1.463  1.00 25.74           O  
ATOM   1543  CB  ASP A 213      39.317  34.407  -2.283  1.00 26.23           C  
ATOM   1544  CG  ASP A 213      39.318  32.894  -2.228  1.00 30.09           C  
ATOM   1545  OD1 ASP A 213      40.310  32.291  -1.767  1.00 22.85           O  
ATOM   1546  OD2 ASP A 213      38.311  32.299  -2.670  1.00 45.89           O  
ATOM   1547  N   GLN A 214      38.618  37.019  -0.762  1.00 22.76           N  
ATOM   1548  CA  GLN A 214      38.359  38.460  -0.765  1.00 26.96           C  
ATOM   1549  C   GLN A 214      39.421  39.197   0.041  1.00 21.74           C  
ATOM   1550  O   GLN A 214      39.929  40.223  -0.400  1.00 23.77           O  
ATOM   1551  CB  GLN A 214      36.993  38.772  -0.172  1.00 23.90           C  
ATOM   1552  CG  GLN A 214      35.917  39.084  -1.177  1.00 38.14           C  
ATOM   1553  CD  GLN A 214      34.569  39.223  -0.497  1.00 47.67           C  
ATOM   1554  OE1 GLN A 214      34.428  39.979   0.471  1.00 53.96           O  
ATOM   1555  NE2 GLN A 214      33.574  38.491  -0.987  1.00 45.53           N  
HETATM 1556  N   MSE A 215      39.748  38.674   1.218  1.00 11.98           N  
HETATM 1557  CA  MSE A 215      40.760  39.300   2.056  1.00 24.55           C  
HETATM 1558  C   MSE A 215      42.110  39.320   1.348  1.00 21.44           C  
HETATM 1559  O   MSE A 215      42.838  40.311   1.413  1.00 22.98           O  
HETATM 1560  CB  MSE A 215      40.917  38.558   3.383  1.00 22.92           C  
HETATM 1561  CG  MSE A 215      39.653  38.467   4.202  1.00 23.29           C  
HETATM 1562 SE   MSE A 215      39.890  37.519   5.866  1.00 33.02          SE  
HETATM 1563  CE  MSE A 215      38.725  38.631   6.952  1.00 29.05           C  
ATOM   1564  N   VAL A 216      42.449  38.224   0.679  1.00 13.73           N  
ATOM   1565  CA  VAL A 216      43.718  38.171  -0.019  1.00 17.54           C  
ATOM   1566  C   VAL A 216      43.710  39.195  -1.142  1.00 18.27           C  
ATOM   1567  O   VAL A 216      44.701  39.876  -1.363  1.00 26.48           O  
ATOM   1568  CB  VAL A 216      43.986  36.780  -0.590  1.00 13.24           C  
ATOM   1569  CG1 VAL A 216      45.286  36.785  -1.364  1.00 20.68           C  
ATOM   1570  CG2 VAL A 216      44.041  35.771   0.540  1.00 18.25           C  
ATOM   1571  N   GLU A 217      42.583  39.311  -1.833  1.00 18.41           N  
ATOM   1572  CA  GLU A 217      42.448  40.259  -2.928  1.00 20.12           C  
ATOM   1573  C   GLU A 217      42.558  41.704  -2.464  1.00 20.62           C  
ATOM   1574  O   GLU A 217      43.189  42.516  -3.135  1.00 23.32           O  
ATOM   1575  CB  GLU A 217      41.109  40.058  -3.651  1.00 16.31           C  
ATOM   1576  CG  GLU A 217      41.023  38.764  -4.464  1.00 21.92           C  
ATOM   1577  CD  GLU A 217      39.754  38.670  -5.309  1.00 23.06           C  
ATOM   1578  OE1 GLU A 217      39.421  39.649  -6.016  1.00 21.73           O  
ATOM   1579  OE2 GLU A 217      39.099  37.608  -5.280  1.00 22.44           O  
ATOM   1580  N   GLU A 218      41.952  42.024  -1.321  1.00 20.08           N  
ATOM   1581  CA  GLU A 218      41.976  43.390  -0.785  1.00 19.74           C  
ATOM   1582  C   GLU A 218      43.314  43.791  -0.189  1.00 16.88           C  
ATOM   1583  O   GLU A 218      43.592  44.975  -0.035  1.00 16.75           O  
ATOM   1584  CB  GLU A 218      40.888  43.560   0.274  1.00 25.94           C  
ATOM   1585  CG  GLU A 218      39.495  43.697  -0.303  1.00 34.86           C  
ATOM   1586  CD  GLU A 218      38.411  43.340   0.695  1.00 45.82           C  
ATOM   1587  OE1 GLU A 218      37.224  43.393   0.317  1.00 42.71           O  
ATOM   1588  OE2 GLU A 218      38.740  43.000   1.856  1.00 50.14           O  
ATOM   1589  N   GLY A 219      44.135  42.804   0.156  1.00 14.82           N  
ATOM   1590  CA  GLY A 219      45.436  43.109   0.717  1.00 20.45           C  
ATOM   1591  C   GLY A 219      45.776  42.506   2.070  1.00 19.31           C  
ATOM   1592  O   GLY A 219      46.627  43.044   2.774  1.00 24.05           O  
ATOM   1593  N   LEU A 220      45.138  41.404   2.445  1.00 18.52           N  
ATOM   1594  CA  LEU A 220      45.430  40.775   3.730  1.00 19.78           C  
ATOM   1595  C   LEU A 220      46.936  40.695   3.970  1.00 20.50           C  
ATOM   1596  O   LEU A 220      47.432  41.179   4.985  1.00 20.81           O  
ATOM   1597  CB  LEU A 220      44.845  39.363   3.779  1.00 17.76           C  
ATOM   1598  CG  LEU A 220      45.091  38.646   5.109  1.00 13.13           C  
ATOM   1599  CD1 LEU A 220      44.494  39.477   6.244  1.00  6.32           C  
ATOM   1600  CD2 LEU A 220      44.469  37.259   5.071  1.00  5.71           C  
ATOM   1601  N   ILE A 221      47.650  40.085   3.023  1.00 19.99           N  
ATOM   1602  CA  ILE A 221      49.103  39.925   3.106  1.00 24.60           C  
ATOM   1603  C   ILE A 221      49.825  41.233   3.426  1.00 20.10           C  
ATOM   1604  O   ILE A 221      50.704  41.267   4.284  1.00 20.32           O  
ATOM   1605  CB  ILE A 221      49.685  39.358   1.783  1.00 23.94           C  
ATOM   1606  CG1 ILE A 221      49.006  38.036   1.442  1.00 14.56           C  
ATOM   1607  CG2 ILE A 221      51.182  39.149   1.928  1.00 16.64           C  
ATOM   1608  CD1 ILE A 221      49.411  37.472   0.112  1.00 28.68           C  
ATOM   1609  N   ASP A 222      49.465  42.302   2.727  1.00 18.47           N  
ATOM   1610  CA  ASP A 222      50.088  43.596   2.971  1.00 21.85           C  
ATOM   1611  C   ASP A 222      49.786  44.052   4.384  1.00 25.38           C  
ATOM   1612  O   ASP A 222      50.665  44.559   5.079  1.00 23.13           O  
ATOM   1613  CB  ASP A 222      49.561  44.643   1.995  1.00 37.03           C  
ATOM   1614  CG  ASP A 222      50.100  44.456   0.609  1.00 47.77           C  
ATOM   1615  OD1 ASP A 222      51.350  44.522   0.458  1.00 51.45           O  
ATOM   1616  OD2 ASP A 222      49.282  44.247  -0.318  1.00 46.62           O  
ATOM   1617  N   GLU A 223      48.531  43.866   4.794  1.00 18.17           N  
ATOM   1618  CA  GLU A 223      48.074  44.254   6.119  1.00 17.20           C  
ATOM   1619  C   GLU A 223      48.869  43.529   7.194  1.00 17.93           C  
ATOM   1620  O   GLU A 223      49.209  44.120   8.218  1.00 26.01           O  
ATOM   1621  CB  GLU A 223      46.576  43.954   6.279  1.00 13.29           C  
ATOM   1622  CG  GLU A 223      45.993  44.440   7.601  1.00 16.37           C  
ATOM   1623  CD  GLU A 223      44.519  44.124   7.762  1.00 20.86           C  
ATOM   1624  OE1 GLU A 223      44.155  42.928   7.791  1.00 30.88           O  
ATOM   1625  OE2 GLU A 223      43.715  45.074   7.861  1.00 32.29           O  
ATOM   1626  N   ALA A 224      49.166  42.253   6.964  1.00 18.77           N  
ATOM   1627  CA  ALA A 224      49.942  41.458   7.921  1.00 20.88           C  
ATOM   1628  C   ALA A 224      51.379  41.970   7.924  1.00 17.61           C  
ATOM   1629  O   ALA A 224      51.955  42.207   8.985  1.00 18.67           O  
ATOM   1630  CB  ALA A 224      49.910  39.967   7.532  1.00 10.45           C  
ATOM   1631  N   LYS A 225      51.955  42.149   6.737  1.00 18.50           N  
ATOM   1632  CA  LYS A 225      53.328  42.641   6.633  1.00 17.22           C  
ATOM   1633  C   LYS A 225      53.556  43.945   7.373  1.00 18.26           C  
ATOM   1634  O   LYS A 225      54.638  44.169   7.918  1.00 32.07           O  
ATOM   1635  CB  LYS A 225      53.745  42.817   5.170  1.00 23.64           C  
ATOM   1636  CG  LYS A 225      53.908  41.517   4.406  1.00 23.43           C  
ATOM   1637  CD  LYS A 225      54.293  41.764   2.951  1.00 22.21           C  
ATOM   1638  CE  LYS A 225      55.637  42.449   2.816  1.00 18.53           C  
ATOM   1639  NZ  LYS A 225      55.866  42.830   1.396  1.00 26.92           N  
ATOM   1640  N   LYS A 226      52.559  44.819   7.398  1.00 25.04           N  
ATOM   1641  CA  LYS A 226      52.730  46.084   8.104  1.00 21.53           C  
ATOM   1642  C   LYS A 226      52.825  45.844   9.615  1.00 18.19           C  
ATOM   1643  O   LYS A 226      53.683  46.418  10.278  1.00 18.81           O  
ATOM   1644  CB  LYS A 226      51.578  47.037   7.776  1.00 26.20           C  
ATOM   1645  CG  LYS A 226      51.519  47.459   6.309  1.00 36.87           C  
ATOM   1646  CD  LYS A 226      50.358  48.417   6.055  1.00 46.10           C  
ATOM   1647  CE  LYS A 226      50.310  48.875   4.603  1.00 45.56           C  
ATOM   1648  NZ  LYS A 226      49.141  49.760   4.325  1.00 54.83           N  
ATOM   1649  N   LEU A 227      51.958  44.993  10.158  1.00 17.06           N  
ATOM   1650  CA  LEU A 227      51.998  44.694  11.585  1.00 19.89           C  
ATOM   1651  C   LEU A 227      53.279  43.944  11.924  1.00 24.04           C  
ATOM   1652  O   LEU A 227      53.862  44.122  12.994  1.00 25.29           O  
ATOM   1653  CB  LEU A 227      50.806  43.836  11.982  1.00 20.47           C  
ATOM   1654  CG  LEU A 227      49.445  44.523  11.843  1.00 24.74           C  
ATOM   1655  CD1 LEU A 227      48.356  43.506  12.108  1.00 30.15           C  
ATOM   1656  CD2 LEU A 227      49.341  45.691  12.821  1.00 19.65           C  
ATOM   1657  N   TYR A 228      53.704  43.098  10.997  1.00 25.42           N  
ATOM   1658  CA  TYR A 228      54.902  42.287  11.153  1.00 24.91           C  
ATOM   1659  C   TYR A 228      56.128  43.190  11.135  1.00 21.29           C  
ATOM   1660  O   TYR A 228      57.015  43.090  11.985  1.00 17.87           O  
ATOM   1661  CB  TYR A 228      54.980  41.303   9.985  1.00 27.63           C  
ATOM   1662  CG  TYR A 228      55.959  40.173  10.166  1.00 17.26           C  
ATOM   1663  CD1 TYR A 228      55.592  39.014  10.856  1.00 20.95           C  
ATOM   1664  CD2 TYR A 228      57.232  40.235   9.601  1.00 19.39           C  
ATOM   1665  CE1 TYR A 228      56.468  37.934  10.969  1.00 17.84           C  
ATOM   1666  CE2 TYR A 228      58.119  39.170   9.705  1.00 18.93           C  
ATOM   1667  CZ  TYR A 228      57.733  38.019  10.388  1.00 21.85           C  
ATOM   1668  OH  TYR A 228      58.604  36.961  10.482  1.00 13.81           O  
ATOM   1669  N   ASP A 229      56.156  44.080  10.153  1.00 19.88           N  
ATOM   1670  CA  ASP A 229      57.263  45.007   9.995  1.00 25.56           C  
ATOM   1671  C   ASP A 229      57.403  45.972  11.160  1.00 22.55           C  
ATOM   1672  O   ASP A 229      58.510  46.393  11.479  1.00 24.82           O  
ATOM   1673  CB  ASP A 229      57.101  45.798   8.701  1.00 31.55           C  
ATOM   1674  CG  ASP A 229      58.378  45.864   7.896  1.00 40.10           C  
ATOM   1675  OD1 ASP A 229      58.393  46.585   6.875  1.00 46.97           O  
ATOM   1676  OD2 ASP A 229      59.363  45.193   8.277  1.00 44.55           O  
ATOM   1677  N   ARG A 230      56.298  46.345  11.796  1.00 22.58           N  
ATOM   1678  CA  ARG A 230      56.426  47.269  12.909  1.00 23.12           C  
ATOM   1679  C   ARG A 230      56.873  46.535  14.157  1.00 22.62           C  
ATOM   1680  O   ARG A 230      57.081  47.146  15.203  1.00 23.39           O  
ATOM   1681  CB  ARG A 230      55.120  48.032  13.164  1.00 27.38           C  
ATOM   1682  CG  ARG A 230      53.914  47.172  13.445  1.00 44.29           C  
ATOM   1683  CD  ARG A 230      52.734  48.016  13.921  1.00 46.27           C  
ATOM   1684  NE  ARG A 230      52.956  48.600  15.247  1.00 47.41           N  
ATOM   1685  CZ  ARG A 230      52.017  49.232  15.946  1.00 42.09           C  
ATOM   1686  NH1 ARG A 230      50.798  49.360  15.443  1.00 45.35           N  
ATOM   1687  NH2 ARG A 230      52.291  49.728  17.145  1.00 36.90           N  
ATOM   1688  N   GLY A 231      57.030  45.219  14.044  1.00 15.24           N  
ATOM   1689  CA  GLY A 231      57.484  44.435  15.180  1.00 13.38           C  
ATOM   1690  C   GLY A 231      56.438  43.840  16.107  1.00 13.74           C  
ATOM   1691  O   GLY A 231      56.775  43.443  17.217  1.00 17.24           O  
ATOM   1692  N   ILE A 232      55.178  43.769  15.673  1.00 18.74           N  
ATOM   1693  CA  ILE A 232      54.107  43.197  16.505  1.00 15.69           C  
ATOM   1694  C   ILE A 232      54.210  41.659  16.504  1.00 23.48           C  
ATOM   1695  O   ILE A 232      54.196  41.027  15.446  1.00 12.26           O  
ATOM   1696  CB  ILE A 232      52.697  43.596  15.970  1.00 17.54           C  
ATOM   1697  CG1 ILE A 232      52.496  45.118  16.033  1.00 17.36           C  
ATOM   1698  CG2 ILE A 232      51.623  42.920  16.781  1.00 16.18           C  
ATOM   1699  CD1 ILE A 232      52.602  45.710  17.425  1.00 19.22           C  
ATOM   1700  N   ARG A 233      54.310  41.046  17.681  1.00 23.37           N  
ATOM   1701  CA  ARG A 233      54.410  39.592  17.730  1.00 22.37           C  
ATOM   1702  C   ARG A 233      53.959  39.048  19.064  1.00 21.50           C  
ATOM   1703  O   ARG A 233      54.103  39.705  20.094  1.00 21.24           O  
ATOM   1704  CB  ARG A 233      55.855  39.147  17.444  1.00 23.44           C  
ATOM   1705  CG  ARG A 233      56.068  37.625  17.370  1.00 22.53           C  
ATOM   1706  CD  ARG A 233      57.552  37.283  17.160  1.00 26.86           C  
ATOM   1707  NE  ARG A 233      57.767  36.527  15.932  1.00 33.06           N  
ATOM   1708  CZ  ARG A 233      57.298  35.301  15.730  1.00 31.06           C  
ATOM   1709  NH1 ARG A 233      57.525  34.680  14.586  1.00 22.63           N  
ATOM   1710  NH2 ARG A 233      56.616  34.687  16.688  1.00 42.53           N  
ATOM   1711  N   ASP A 234      53.387  37.847  19.039  1.00 26.73           N  
ATOM   1712  CA  ASP A 234      52.926  37.195  20.262  1.00 27.75           C  
ATOM   1713  C   ASP A 234      51.912  38.037  21.050  1.00 29.13           C  
ATOM   1714  O   ASP A 234      51.851  37.983  22.287  1.00 24.56           O  
ATOM   1715  CB  ASP A 234      54.146  36.865  21.112  1.00 19.97           C  
ATOM   1716  CG  ASP A 234      55.087  35.929  20.395  1.00 22.67           C  
ATOM   1717  OD1 ASP A 234      56.321  36.005  20.592  1.00 25.72           O  
ATOM   1718  OD2 ASP A 234      54.568  35.101  19.623  1.00 22.16           O  
ATOM   1719  N   CYS A 235      51.115  38.811  20.321  1.00 24.59           N  
ATOM   1720  CA  CYS A 235      50.098  39.651  20.932  1.00 24.06           C  
ATOM   1721  C   CYS A 235      48.740  39.072  20.616  1.00 25.19           C  
ATOM   1722  O   CYS A 235      48.590  38.259  19.702  1.00 25.30           O  
ATOM   1723  CB  CYS A 235      50.158  41.079  20.390  1.00 27.38           C  
ATOM   1724  SG  CYS A 235      51.567  42.075  20.935  1.00 41.67           S  
ATOM   1725  N   GLN A 236      47.740  39.505  21.364  1.00 26.46           N  
ATOM   1726  CA  GLN A 236      46.394  39.018  21.133  1.00 30.59           C  
ATOM   1727  C   GLN A 236      45.998  39.241  19.671  1.00 24.51           C  
ATOM   1728  O   GLN A 236      45.627  38.300  18.961  1.00 22.90           O  
ATOM   1729  CB  GLN A 236      45.423  39.746  22.056  1.00 32.72           C  
ATOM   1730  CG  GLN A 236      44.022  39.208  22.006  1.00 33.76           C  
ATOM   1731  CD  GLN A 236      43.086  40.058  22.807  1.00 34.05           C  
ATOM   1732  OE1 GLN A 236      43.381  40.415  23.947  1.00 27.00           O  
ATOM   1733  NE2 GLN A 236      41.947  40.394  22.221  1.00 32.11           N  
ATOM   1734  N   SER A 237      46.102  40.492  19.233  1.00 17.32           N  
ATOM   1735  CA  SER A 237      45.759  40.895  17.868  1.00 21.09           C  
ATOM   1736  C   SER A 237      46.299  39.983  16.769  1.00 20.74           C  
ATOM   1737  O   SER A 237      45.565  39.554  15.880  1.00 20.99           O  
ATOM   1738  CB  SER A 237      46.293  42.299  17.597  1.00 20.45           C  
ATOM   1739  OG  SER A 237      47.717  42.266  17.506  1.00 17.61           O  
ATOM   1740  N   VAL A 238      47.597  39.720  16.837  1.00 15.33           N  
ATOM   1741  CA  VAL A 238      48.296  38.921  15.851  1.00 20.16           C  
ATOM   1742  C   VAL A 238      48.136  37.419  16.004  1.00 13.90           C  
ATOM   1743  O   VAL A 238      48.474  36.655  15.104  1.00 13.12           O  
ATOM   1744  CB  VAL A 238      49.786  39.303  15.868  1.00 23.41           C  
ATOM   1745  CG1 VAL A 238      50.637  38.185  15.321  1.00 38.73           C  
ATOM   1746  CG2 VAL A 238      49.986  40.561  15.061  1.00 19.20           C  
ATOM   1747  N   GLN A 239      47.616  36.994  17.141  1.00 17.47           N  
ATOM   1748  CA  GLN A 239      47.420  35.572  17.370  1.00 23.66           C  
ATOM   1749  C   GLN A 239      46.059  35.167  16.834  1.00 19.85           C  
ATOM   1750  O   GLN A 239      45.684  33.995  16.870  1.00 20.63           O  
ATOM   1751  CB  GLN A 239      47.521  35.257  18.868  1.00 19.19           C  
ATOM   1752  CG  GLN A 239      48.939  35.358  19.416  1.00 16.03           C  
ATOM   1753  CD  GLN A 239      49.009  35.334  20.941  1.00 15.93           C  
ATOM   1754  OE1 GLN A 239      48.257  36.033  21.619  1.00 20.82           O  
ATOM   1755  NE2 GLN A 239      49.931  34.545  21.482  1.00 12.26           N  
ATOM   1756  N   ALA A 240      45.323  36.147  16.323  1.00 17.79           N  
ATOM   1757  CA  ALA A 240      43.989  35.899  15.782  1.00 18.69           C  
ATOM   1758  C   ALA A 240      43.989  34.945  14.588  1.00 22.18           C  
ATOM   1759  O   ALA A 240      44.907  34.950  13.757  1.00 16.07           O  
ATOM   1760  CB  ALA A 240      43.330  37.217  15.392  1.00 14.31           C  
ATOM   1761  N   ILE A 241      42.929  34.148  14.521  1.00 20.89           N  
ATOM   1762  CA  ILE A 241      42.722  33.148  13.487  1.00 26.64           C  
ATOM   1763  C   ILE A 241      42.474  33.743  12.093  1.00 26.70           C  
ATOM   1764  O   ILE A 241      41.516  33.379  11.406  1.00 29.94           O  
ATOM   1765  CB  ILE A 241      41.543  32.231  13.891  1.00 29.78           C  
ATOM   1766  CG1 ILE A 241      41.406  31.078  12.908  1.00 36.80           C  
ATOM   1767  CG2 ILE A 241      40.259  33.040  13.973  1.00 41.06           C  
ATOM   1768  CD1 ILE A 241      40.380  30.058  13.337  1.00 41.34           C  
ATOM   1769  N   GLY A 242      43.369  34.648  11.701  1.00 27.49           N  
ATOM   1770  CA  GLY A 242      43.322  35.330  10.418  1.00 12.00           C  
ATOM   1771  C   GLY A 242      44.583  36.159  10.171  1.00 21.41           C  
ATOM   1772  O   GLY A 242      44.738  36.747   9.103  1.00 27.52           O  
ATOM   1773  N   TYR A 243      45.476  36.233  11.160  1.00 22.79           N  
ATOM   1774  CA  TYR A 243      46.750  36.955  11.022  1.00 15.77           C  
ATOM   1775  C   TYR A 243      47.893  35.987  11.344  1.00 16.68           C  
ATOM   1776  O   TYR A 243      49.015  36.159  10.876  1.00 15.70           O  
ATOM   1777  CB  TYR A 243      46.849  38.171  11.975  1.00 16.67           C  
ATOM   1778  CG  TYR A 243      45.964  39.347  11.604  1.00 10.82           C  
ATOM   1779  CD1 TYR A 243      44.631  39.375  11.988  1.00 19.34           C  
ATOM   1780  CD2 TYR A 243      46.437  40.380  10.792  1.00 13.63           C  
ATOM   1781  CE1 TYR A 243      43.773  40.387  11.570  1.00 18.36           C  
ATOM   1782  CE2 TYR A 243      45.593  41.407  10.359  1.00 12.88           C  
ATOM   1783  CZ  TYR A 243      44.254  41.396  10.751  1.00 24.32           C  
ATOM   1784  OH  TYR A 243      43.377  42.352  10.291  1.00 19.60           O  
ATOM   1785  N   LYS A 244      47.602  34.968  12.148  1.00 21.59           N  
ATOM   1786  CA  LYS A 244      48.626  34.002  12.514  1.00 22.82           C  
ATOM   1787  C   LYS A 244      49.070  33.177  11.303  1.00 20.27           C  
ATOM   1788  O   LYS A 244      50.248  32.892  11.154  1.00 22.07           O  
ATOM   1789  CB  LYS A 244      48.141  33.088  13.654  1.00 17.38           C  
ATOM   1790  CG  LYS A 244      47.113  32.052  13.273  1.00 24.81           C  
ATOM   1791  CD  LYS A 244      46.721  31.160  14.458  1.00 21.91           C  
ATOM   1792  CE  LYS A 244      45.499  30.315  14.064  1.00 31.36           C  
ATOM   1793  NZ  LYS A 244      45.020  29.367  15.112  1.00 32.70           N  
ATOM   1794  N   GLU A 245      48.146  32.822  10.420  1.00 20.04           N  
ATOM   1795  CA  GLU A 245      48.523  32.044   9.251  1.00 18.84           C  
ATOM   1796  C   GLU A 245      49.520  32.814   8.395  1.00 22.45           C  
ATOM   1797  O   GLU A 245      50.509  32.254   7.910  1.00 27.23           O  
ATOM   1798  CB  GLU A 245      47.303  31.693   8.419  1.00 17.40           C  
ATOM   1799  CG  GLU A 245      46.293  30.821   9.145  1.00 21.70           C  
ATOM   1800  CD  GLU A 245      45.353  31.595  10.047  1.00 26.42           C  
ATOM   1801  OE1 GLU A 245      45.246  32.840   9.905  1.00 30.13           O  
ATOM   1802  OE2 GLU A 245      44.694  30.946  10.891  1.00 30.04           O  
HETATM 1803  N   MSE A 246      49.270  34.101   8.205  1.00 22.51           N  
HETATM 1804  CA  MSE A 246      50.185  34.909   7.418  1.00 16.70           C  
HETATM 1805  C   MSE A 246      51.540  34.999   8.132  1.00 14.13           C  
HETATM 1806  O   MSE A 246      52.590  34.978   7.491  1.00 13.24           O  
HETATM 1807  CB  MSE A 246      49.600  36.305   7.181  1.00 19.46           C  
HETATM 1808  CG  MSE A 246      48.362  36.304   6.294  1.00 18.46           C  
HETATM 1809 SE   MSE A 246      48.642  35.440   4.549  1.00 36.78          SE  
HETATM 1810  CE  MSE A 246      47.568  33.837   4.839  1.00 29.52           C  
ATOM   1811  N   TYR A 247      51.530  35.078   9.458  1.00 14.22           N  
ATOM   1812  CA  TYR A 247      52.788  35.152  10.184  1.00  9.30           C  
ATOM   1813  C   TYR A 247      53.659  33.908   9.958  1.00 14.01           C  
ATOM   1814  O   TYR A 247      54.882  34.014   9.841  1.00 10.84           O  
ATOM   1815  CB  TYR A 247      52.542  35.381  11.675  1.00 11.83           C  
ATOM   1816  CG  TYR A 247      52.516  36.842  12.074  1.00 15.08           C  
ATOM   1817  CD1 TYR A 247      53.212  37.276  13.199  1.00 24.23           C  
ATOM   1818  CD2 TYR A 247      51.800  37.791  11.338  1.00 12.26           C  
ATOM   1819  CE1 TYR A 247      53.206  38.611  13.592  1.00 16.65           C  
ATOM   1820  CE2 TYR A 247      51.785  39.140  11.731  1.00 17.59           C  
ATOM   1821  CZ  TYR A 247      52.498  39.534  12.866  1.00 14.75           C  
ATOM   1822  OH  TYR A 247      52.522  40.848  13.285  1.00 18.80           O  
ATOM   1823  N   ASP A 248      53.055  32.726   9.898  1.00 13.51           N  
ATOM   1824  CA  ASP A 248      53.856  31.532   9.625  1.00 12.69           C  
ATOM   1825  C   ASP A 248      54.480  31.682   8.241  1.00 13.80           C  
ATOM   1826  O   ASP A 248      55.637  31.322   8.031  1.00 16.47           O  
ATOM   1827  CB  ASP A 248      53.000  30.264   9.662  1.00 14.55           C  
ATOM   1828  CG  ASP A 248      52.684  29.824  11.070  1.00 26.62           C  
ATOM   1829  OD1 ASP A 248      53.625  29.559  11.852  1.00 31.58           O  
ATOM   1830  OD2 ASP A 248      51.489  29.740  11.405  1.00 37.11           O  
ATOM   1831  N   TYR A 249      53.706  32.202   7.291  1.00 11.67           N  
ATOM   1832  CA  TYR A 249      54.215  32.413   5.937  1.00 15.69           C  
ATOM   1833  C   TYR A 249      55.387  33.397   5.970  1.00 13.95           C  
ATOM   1834  O   TYR A 249      56.452  33.131   5.411  1.00 13.70           O  
ATOM   1835  CB  TYR A 249      53.118  32.969   5.015  1.00  6.44           C  
ATOM   1836  CG  TYR A 249      53.673  33.632   3.768  1.00 20.20           C  
ATOM   1837  CD1 TYR A 249      54.331  32.881   2.790  1.00 14.10           C  
ATOM   1838  CD2 TYR A 249      53.584  35.019   3.586  1.00 10.63           C  
ATOM   1839  CE1 TYR A 249      54.889  33.487   1.666  1.00 15.76           C  
ATOM   1840  CE2 TYR A 249      54.141  35.637   2.463  1.00  8.62           C  
ATOM   1841  CZ  TYR A 249      54.793  34.860   1.509  1.00 19.97           C  
ATOM   1842  OH  TYR A 249      55.360  35.436   0.400  1.00 22.09           O  
ATOM   1843  N   LEU A 250      55.176  34.535   6.627  1.00 18.23           N  
ATOM   1844  CA  LEU A 250      56.201  35.570   6.740  1.00 19.51           C  
ATOM   1845  C   LEU A 250      57.462  35.047   7.437  1.00 22.24           C  
ATOM   1846  O   LEU A 250      58.565  35.499   7.146  1.00 17.24           O  
ATOM   1847  CB  LEU A 250      55.628  36.775   7.499  1.00 22.28           C  
ATOM   1848  CG  LEU A 250      55.141  38.017   6.745  1.00 24.70           C  
ATOM   1849  CD1 LEU A 250      54.790  37.711   5.307  1.00  8.68           C  
ATOM   1850  CD2 LEU A 250      53.951  38.595   7.501  1.00 20.19           C  
ATOM   1851  N   ASP A 251      57.281  34.104   8.361  1.00 19.77           N  
ATOM   1852  CA  ASP A 251      58.386  33.487   9.087  1.00 16.40           C  
ATOM   1853  C   ASP A 251      59.066  32.489   8.163  1.00 19.25           C  
ATOM   1854  O   ASP A 251      60.174  32.035   8.441  1.00 24.51           O  
ATOM   1855  CB  ASP A 251      57.884  32.725  10.318  1.00 18.58           C  
ATOM   1856  CG  ASP A 251      57.631  33.622  11.513  1.00 22.32           C  
ATOM   1857  OD1 ASP A 251      57.069  33.116  12.512  1.00 18.92           O  
ATOM   1858  OD2 ASP A 251      57.999  34.820  11.464  1.00 25.07           O  
ATOM   1859  N   GLY A 252      58.382  32.125   7.083  1.00 15.56           N  
ATOM   1860  CA  GLY A 252      58.939  31.182   6.132  1.00 11.37           C  
ATOM   1861  C   GLY A 252      58.780  29.735   6.547  1.00 14.86           C  
ATOM   1862  O   GLY A 252      59.533  28.871   6.098  1.00 29.57           O  
ATOM   1863  N   ASN A 253      57.793  29.466   7.393  1.00 14.39           N  
ATOM   1864  CA  ASN A 253      57.527  28.115   7.884  1.00 17.33           C  
ATOM   1865  C   ASN A 253      56.549  27.360   6.995  1.00 18.92           C  
ATOM   1866  O   ASN A 253      56.469  26.136   7.049  1.00 22.83           O  
ATOM   1867  CB  ASN A 253      56.950  28.175   9.302  1.00 20.75           C  
ATOM   1868  CG  ASN A 253      57.977  28.588  10.346  1.00 21.15           C  
ATOM   1869  OD1 ASN A 253      57.613  29.046  11.429  1.00 31.55           O  
ATOM   1870  ND2 ASN A 253      59.254  28.418  10.034  1.00 11.45           N  
ATOM   1871  N   VAL A 254      55.796  28.100   6.189  1.00 18.37           N  
ATOM   1872  CA  VAL A 254      54.809  27.510   5.296  1.00 17.94           C  
ATOM   1873  C   VAL A 254      54.732  28.336   4.015  1.00 20.94           C  
ATOM   1874  O   VAL A 254      54.992  29.538   4.035  1.00 18.50           O  
ATOM   1875  CB  VAL A 254      53.392  27.490   5.961  1.00 21.29           C  
ATOM   1876  CG1 VAL A 254      53.391  26.577   7.196  1.00 12.44           C  
ATOM   1877  CG2 VAL A 254      52.986  28.914   6.359  1.00  9.87           C  
ATOM   1878  N   THR A 255      54.383  27.687   2.909  1.00 17.25           N  
ATOM   1879  CA  THR A 255      54.254  28.367   1.625  1.00 21.96           C  
ATOM   1880  C   THR A 255      52.985  29.227   1.630  1.00 21.77           C  
ATOM   1881  O   THR A 255      52.051  28.953   2.383  1.00 16.59           O  
ATOM   1882  CB  THR A 255      54.123  27.355   0.474  1.00 21.32           C  
ATOM   1883  OG1 THR A 255      52.884  26.638   0.613  1.00 23.10           O  
ATOM   1884  CG2 THR A 255      55.274  26.358   0.507  1.00 20.29           C  
ATOM   1885  N   LEU A 256      52.959  30.253   0.781  1.00 22.10           N  
ATOM   1886  CA  LEU A 256      51.814  31.148   0.673  1.00 16.51           C  
ATOM   1887  C   LEU A 256      50.506  30.369   0.449  1.00 19.57           C  
ATOM   1888  O   LEU A 256      49.513  30.604   1.140  1.00 16.62           O  
ATOM   1889  CB  LEU A 256      52.032  32.145  -0.469  1.00 14.18           C  
ATOM   1890  CG  LEU A 256      50.928  33.176  -0.764  1.00 20.37           C  
ATOM   1891  CD1 LEU A 256      50.619  34.009   0.483  1.00 14.22           C  
ATOM   1892  CD2 LEU A 256      51.404  34.089  -1.890  1.00 24.54           C  
ATOM   1893  N   GLU A 257      50.504  29.445  -0.508  1.00 22.58           N  
ATOM   1894  CA  GLU A 257      49.308  28.655  -0.779  1.00 25.41           C  
ATOM   1895  C   GLU A 257      48.918  27.829   0.447  1.00 30.16           C  
ATOM   1896  O   GLU A 257      47.731  27.588   0.695  1.00 30.73           O  
ATOM   1897  CB  GLU A 257      49.516  27.742  -1.991  1.00 18.67           C  
ATOM   1898  CG  GLU A 257      50.873  27.091  -2.034  1.00 29.94           C  
ATOM   1899  CD  GLU A 257      51.895  27.917  -2.794  1.00 30.97           C  
ATOM   1900  OE1 GLU A 257      52.112  27.628  -3.987  1.00 35.58           O  
ATOM   1901  OE2 GLU A 257      52.465  28.861  -2.210  1.00 29.61           O  
ATOM   1902  N   GLU A 258      49.913  27.399   1.220  1.00 28.20           N  
ATOM   1903  CA  GLU A 258      49.653  26.627   2.433  1.00 21.89           C  
ATOM   1904  C   GLU A 258      48.969  27.512   3.468  1.00 22.00           C  
ATOM   1905  O   GLU A 258      48.044  27.070   4.144  1.00 22.76           O  
ATOM   1906  CB  GLU A 258      50.957  26.077   3.014  1.00 31.12           C  
ATOM   1907  CG  GLU A 258      51.154  24.582   2.809  1.00 38.35           C  
ATOM   1908  CD  GLU A 258      52.571  24.123   3.142  1.00 39.49           C  
ATOM   1909  OE1 GLU A 258      52.841  22.907   3.042  1.00 40.16           O  
ATOM   1910  OE2 GLU A 258      53.414  24.975   3.497  1.00 37.68           O  
ATOM   1911  N   ALA A 259      49.415  28.759   3.591  1.00 15.02           N  
ATOM   1912  CA  ALA A 259      48.814  29.677   4.554  1.00 20.44           C  
ATOM   1913  C   ALA A 259      47.343  29.922   4.211  1.00 16.81           C  
ATOM   1914  O   ALA A 259      46.466  29.760   5.063  1.00 15.22           O  
ATOM   1915  CB  ALA A 259      49.590  31.003   4.589  1.00 16.48           C  
ATOM   1916  N   ILE A 260      47.082  30.306   2.961  1.00 19.35           N  
ATOM   1917  CA  ILE A 260      45.719  30.561   2.477  1.00 14.62           C  
ATOM   1918  C   ILE A 260      44.819  29.355   2.722  1.00 11.51           C  
ATOM   1919  O   ILE A 260      43.689  29.495   3.186  1.00 20.81           O  
ATOM   1920  CB  ILE A 260      45.708  30.866   0.950  1.00 20.74           C  
ATOM   1921  CG1 ILE A 260      46.441  32.175   0.665  1.00 23.89           C  
ATOM   1922  CG2 ILE A 260      44.279  30.969   0.437  1.00 15.01           C  
ATOM   1923  CD1 ILE A 260      46.729  32.391  -0.802  1.00 19.24           C  
ATOM   1924  N   ASP A 261      45.315  28.169   2.400  1.00 14.15           N  
ATOM   1925  CA  ASP A 261      44.527  26.962   2.602  1.00 19.06           C  
ATOM   1926  C   ASP A 261      44.249  26.732   4.088  1.00 20.46           C  
ATOM   1927  O   ASP A 261      43.144  26.344   4.467  1.00 19.04           O  
ATOM   1928  CB  ASP A 261      45.259  25.758   2.012  1.00 22.85           C  
ATOM   1929  CG  ASP A 261      44.577  24.444   2.341  1.00 35.57           C  
ATOM   1930  OD1 ASP A 261      44.817  23.901   3.436  1.00 34.01           O  
ATOM   1931  OD2 ASP A 261      43.793  23.955   1.505  1.00 44.56           O  
ATOM   1932  N   THR A 262      45.251  26.992   4.925  1.00 21.43           N  
ATOM   1933  CA  THR A 262      45.128  26.810   6.370  1.00 18.49           C  
ATOM   1934  C   THR A 262      44.210  27.856   6.997  1.00 19.12           C  
ATOM   1935  O   THR A 262      43.469  27.564   7.943  1.00 19.46           O  
ATOM   1936  CB  THR A 262      46.516  26.849   7.042  1.00 19.03           C  
ATOM   1937  OG1 THR A 262      47.254  25.673   6.671  1.00 22.05           O  
ATOM   1938  CG2 THR A 262      46.382  26.905   8.567  1.00 17.58           C  
ATOM   1939  N   LEU A 263      44.257  29.068   6.460  1.00 14.01           N  
ATOM   1940  CA  LEU A 263      43.410  30.151   6.946  1.00 15.41           C  
ATOM   1941  C   LEU A 263      41.958  29.805   6.667  1.00 13.64           C  
ATOM   1942  O   LEU A 263      41.087  30.014   7.506  1.00 18.31           O  
ATOM   1943  CB  LEU A 263      43.764  31.466   6.241  1.00 18.97           C  
ATOM   1944  CG  LEU A 263      42.781  32.626   6.411  1.00 16.00           C  
ATOM   1945  CD1 LEU A 263      42.436  32.800   7.881  1.00 13.59           C  
ATOM   1946  CD2 LEU A 263      43.386  33.902   5.855  1.00 19.09           C  
ATOM   1947  N   LYS A 264      41.696  29.281   5.475  1.00 13.71           N  
ATOM   1948  CA  LYS A 264      40.341  28.912   5.116  1.00 12.13           C  
ATOM   1949  C   LYS A 264      39.815  27.826   6.046  1.00 14.11           C  
ATOM   1950  O   LYS A 264      38.685  27.902   6.539  1.00  9.88           O  
ATOM   1951  CB  LYS A 264      40.290  28.428   3.671  1.00 10.91           C  
ATOM   1952  CG  LYS A 264      40.373  29.559   2.641  1.00 12.40           C  
ATOM   1953  CD  LYS A 264      40.394  29.017   1.211  1.00 14.01           C  
ATOM   1954  CE  LYS A 264      40.316  30.139   0.177  1.00 15.74           C  
ATOM   1955  NZ  LYS A 264      40.234  29.618  -1.218  1.00 12.64           N  
ATOM   1956  N   ARG A 265      40.648  26.819   6.279  1.00 15.60           N  
ATOM   1957  CA  ARG A 265      40.292  25.708   7.138  1.00 17.49           C  
ATOM   1958  C   ARG A 265      40.028  26.208   8.551  1.00 18.54           C  
ATOM   1959  O   ARG A 265      38.970  25.934   9.123  1.00 12.24           O  
ATOM   1960  CB  ARG A 265      41.418  24.677   7.114  1.00 23.32           C  
ATOM   1961  CG  ARG A 265      41.187  23.455   7.978  1.00 38.21           C  
ATOM   1962  CD  ARG A 265      41.804  22.222   7.313  1.00 50.12           C  
ATOM   1963  NE  ARG A 265      43.144  22.493   6.795  1.00 60.02           N  
ATOM   1964  CZ  ARG A 265      44.181  22.854   7.547  1.00 72.62           C  
ATOM   1965  NH1 ARG A 265      45.365  23.083   6.989  1.00 70.44           N  
ATOM   1966  NH2 ARG A 265      44.038  22.983   8.860  1.00 77.10           N  
ATOM   1967  N   ASN A 266      40.972  26.955   9.118  1.00 18.87           N  
ATOM   1968  CA  ASN A 266      40.763  27.474  10.465  1.00 17.60           C  
ATOM   1969  C   ASN A 266      39.512  28.349  10.522  1.00 13.91           C  
ATOM   1970  O   ASN A 266      38.806  28.342  11.526  1.00 16.90           O  
ATOM   1971  CB  ASN A 266      41.967  28.290  10.943  1.00 22.78           C  
ATOM   1972  CG  ASN A 266      43.229  27.466  11.043  1.00 16.01           C  
ATOM   1973  OD1 ASN A 266      43.179  26.258  11.260  1.00 19.45           O  
ATOM   1974  ND2 ASN A 266      44.373  28.120  10.895  1.00 13.96           N  
ATOM   1975  N   SER A 267      39.233  29.100   9.457  1.00  9.89           N  
ATOM   1976  CA  SER A 267      38.048  29.954   9.442  1.00  8.68           C  
ATOM   1977  C   SER A 267      36.769  29.120   9.485  1.00 16.60           C  
ATOM   1978  O   SER A 267      35.789  29.505  10.129  1.00 18.47           O  
ATOM   1979  CB  SER A 267      38.021  30.850   8.198  1.00 17.24           C  
ATOM   1980  OG  SER A 267      38.993  31.880   8.267  1.00 12.96           O  
ATOM   1981  N   ARG A 268      36.772  27.985   8.790  1.00 11.24           N  
ATOM   1982  CA  ARG A 268      35.605  27.114   8.779  1.00 18.55           C  
ATOM   1983  C   ARG A 268      35.463  26.424  10.132  1.00 19.68           C  
ATOM   1984  O   ARG A 268      34.361  26.328  10.670  1.00 14.65           O  
ATOM   1985  CB  ARG A 268      35.718  26.054   7.678  1.00 22.60           C  
ATOM   1986  CG  ARG A 268      35.650  26.601   6.259  1.00 14.14           C  
ATOM   1987  CD  ARG A 268      35.559  25.445   5.275  1.00  9.36           C  
ATOM   1988  NE  ARG A 268      36.642  24.488   5.467  1.00  9.12           N  
ATOM   1989  CZ  ARG A 268      37.790  24.506   4.793  1.00 18.82           C  
ATOM   1990  NH1 ARG A 268      38.010  25.436   3.874  1.00 17.16           N  
ATOM   1991  NH2 ARG A 268      38.717  23.590   5.028  1.00 10.20           N  
ATOM   1992  N   ARG A 269      36.588  25.957  10.673  1.00 23.06           N  
ATOM   1993  CA  ARG A 269      36.619  25.275  11.969  1.00 27.45           C  
ATOM   1994  C   ARG A 269      36.119  26.190  13.079  1.00 27.23           C  
ATOM   1995  O   ARG A 269      35.480  25.743  14.034  1.00 24.47           O  
ATOM   1996  CB  ARG A 269      38.050  24.856  12.314  1.00 29.43           C  
ATOM   1997  CG  ARG A 269      38.227  23.400  12.688  1.00 35.32           C  
ATOM   1998  CD  ARG A 269      38.486  22.562  11.448  1.00 40.40           C  
ATOM   1999  NE  ARG A 269      39.706  21.768  11.566  1.00 47.34           N  
ATOM   2000  CZ  ARG A 269      40.930  22.273  11.692  1.00 51.67           C  
ATOM   2001  NH1 ARG A 269      41.972  21.458  11.792  1.00 52.87           N  
ATOM   2002  NH2 ARG A 269      41.118  23.587  11.717  1.00 54.41           N  
ATOM   2003  N   TYR A 270      36.440  27.472  12.956  1.00 29.85           N  
ATOM   2004  CA  TYR A 270      36.047  28.459  13.950  1.00 29.48           C  
ATOM   2005  C   TYR A 270      34.558  28.804  13.855  1.00 27.26           C  
ATOM   2006  O   TYR A 270      33.932  29.145  14.858  1.00 24.12           O  
ATOM   2007  CB  TYR A 270      36.914  29.709  13.790  1.00 29.94           C  
ATOM   2008  CG  TYR A 270      36.600  30.824  14.755  1.00 33.09           C  
ATOM   2009  CD1 TYR A 270      35.680  31.817  14.424  1.00 32.45           C  
ATOM   2010  CD2 TYR A 270      37.227  30.891  15.997  1.00 39.18           C  
ATOM   2011  CE1 TYR A 270      35.392  32.853  15.308  1.00 38.54           C  
ATOM   2012  CE2 TYR A 270      36.946  31.918  16.889  1.00 41.51           C  
ATOM   2013  CZ  TYR A 270      36.030  32.894  16.539  1.00 41.44           C  
ATOM   2014  OH  TYR A 270      35.742  33.904  17.426  1.00 53.32           O  
ATOM   2015  N   ALA A 271      33.994  28.714  12.652  1.00 23.80           N  
ATOM   2016  CA  ALA A 271      32.575  28.997  12.469  1.00 22.78           C  
ATOM   2017  C   ALA A 271      31.801  27.851  13.116  1.00 24.72           C  
ATOM   2018  O   ALA A 271      30.854  28.071  13.871  1.00 18.65           O  
ATOM   2019  CB  ALA A 271      32.230  29.088  10.978  1.00 14.45           C  
ATOM   2020  N   LYS A 272      32.220  26.623  12.819  1.00 17.88           N  
ATOM   2021  CA  LYS A 272      31.574  25.438  13.375  1.00 24.72           C  
ATOM   2022  C   LYS A 272      31.578  25.479  14.909  1.00 27.53           C  
ATOM   2023  O   LYS A 272      30.638  25.013  15.549  1.00 28.26           O  
ATOM   2024  CB  LYS A 272      32.293  24.175  12.883  1.00 28.76           C  
ATOM   2025  CG  LYS A 272      31.724  22.858  13.400  1.00 27.85           C  
ATOM   2026  CD  LYS A 272      32.691  21.710  13.099  1.00 38.53           C  
ATOM   2027  CE  LYS A 272      34.024  21.919  13.841  1.00 48.49           C  
ATOM   2028  NZ  LYS A 272      35.102  20.935  13.503  1.00 42.10           N  
ATOM   2029  N   ARG A 273      32.635  26.039  15.492  1.00 22.12           N  
ATOM   2030  CA  ARG A 273      32.733  26.132  16.936  1.00 24.05           C  
ATOM   2031  C   ARG A 273      31.858  27.245  17.482  1.00 24.76           C  
ATOM   2032  O   ARG A 273      31.299  27.124  18.568  1.00 24.29           O  
ATOM   2033  CB  ARG A 273      34.184  26.355  17.359  1.00 34.25           C  
ATOM   2034  CG  ARG A 273      34.824  25.097  17.900  1.00 37.99           C  
ATOM   2035  CD  ARG A 273      36.326  25.060  17.711  1.00 41.80           C  
ATOM   2036  NE  ARG A 273      36.835  23.760  18.133  1.00 57.83           N  
ATOM   2037  CZ  ARG A 273      36.413  22.597  17.642  1.00 63.34           C  
ATOM   2038  NH1 ARG A 273      36.930  21.460  18.090  1.00 61.12           N  
ATOM   2039  NH2 ARG A 273      35.481  22.568  16.696  1.00 59.61           N  
ATOM   2040  N   GLN A 274      31.731  28.329  16.732  1.00 16.37           N  
ATOM   2041  CA  GLN A 274      30.906  29.433  17.187  1.00 21.20           C  
ATOM   2042  C   GLN A 274      29.433  29.033  17.184  1.00 25.01           C  
ATOM   2043  O   GLN A 274      28.673  29.420  18.072  1.00 24.08           O  
ATOM   2044  CB  GLN A 274      31.146  30.660  16.309  1.00 19.43           C  
ATOM   2045  CG  GLN A 274      32.457  31.360  16.626  1.00 32.97           C  
ATOM   2046  CD  GLN A 274      32.366  32.220  17.877  1.00 50.26           C  
ATOM   2047  OE1 GLN A 274      31.700  33.261  17.875  1.00 55.66           O  
ATOM   2048  NE2 GLN A 274      33.027  31.787  18.956  1.00 52.13           N  
ATOM   2049  N   LEU A 275      29.042  28.243  16.188  1.00 23.34           N  
ATOM   2050  CA  LEU A 275      27.667  27.767  16.068  1.00 21.78           C  
ATOM   2051  C   LEU A 275      27.347  26.806  17.210  1.00 22.36           C  
ATOM   2052  O   LEU A 275      26.283  26.888  17.826  1.00 22.12           O  
ATOM   2053  CB  LEU A 275      27.472  27.065  14.721  1.00 18.27           C  
ATOM   2054  CG  LEU A 275      26.799  27.896  13.620  1.00 21.18           C  
ATOM   2055  CD1 LEU A 275      27.097  27.309  12.250  1.00 22.23           C  
ATOM   2056  CD2 LEU A 275      25.298  27.914  13.876  1.00  7.59           C  
ATOM   2057  N   THR A 276      28.277  25.900  17.491  1.00 12.20           N  
ATOM   2058  CA  THR A 276      28.090  24.938  18.559  1.00 17.00           C  
ATOM   2059  C   THR A 276      27.878  25.658  19.885  1.00 20.52           C  
ATOM   2060  O   THR A 276      26.966  25.330  20.645  1.00 30.04           O  
ATOM   2061  CB  THR A 276      29.297  23.979  18.652  1.00 14.82           C  
ATOM   2062  OG1 THR A 276      29.189  22.996  17.612  1.00 22.80           O  
ATOM   2063  CG2 THR A 276      29.344  23.284  20.007  1.00  9.06           C  
ATOM   2064  N   TRP A 277      28.696  26.661  20.153  1.00 17.16           N  
ATOM   2065  CA  TRP A 277      28.550  27.398  21.383  1.00 18.19           C  
ATOM   2066  C   TRP A 277      27.183  28.058  21.500  1.00 18.69           C  
ATOM   2067  O   TRP A 277      26.534  27.925  22.528  1.00 18.13           O  
ATOM   2068  CB  TRP A 277      29.628  28.461  21.498  1.00 26.53           C  
ATOM   2069  CG  TRP A 277      29.565  29.193  22.784  1.00 45.39           C  
ATOM   2070  CD1 TRP A 277      29.693  30.533  22.961  1.00 43.63           C  
ATOM   2071  CD2 TRP A 277      29.399  28.623  24.091  1.00 58.59           C  
ATOM   2072  NE1 TRP A 277      29.615  30.844  24.297  1.00 51.69           N  
ATOM   2073  CE2 TRP A 277      29.425  29.691  25.015  1.00 58.29           C  
ATOM   2074  CE3 TRP A 277      29.208  27.315  24.575  1.00 58.96           C  
ATOM   2075  CZ2 TRP A 277      29.298  29.494  26.396  1.00 60.48           C  
ATOM   2076  CZ3 TRP A 277      29.078  27.119  25.952  1.00 54.14           C  
ATOM   2077  CH2 TRP A 277      29.114  28.207  26.843  1.00 58.93           C  
ATOM   2078  N   PHE A 278      26.730  28.765  20.466  1.00 15.57           N  
ATOM   2079  CA  PHE A 278      25.430  29.422  20.557  1.00 16.57           C  
ATOM   2080  C   PHE A 278      24.250  28.459  20.527  1.00 17.90           C  
ATOM   2081  O   PHE A 278      23.228  28.712  21.164  1.00 14.18           O  
ATOM   2082  CB  PHE A 278      25.290  30.485  19.465  1.00 22.50           C  
ATOM   2083  CG  PHE A 278      26.173  31.668  19.684  1.00 22.21           C  
ATOM   2084  CD1 PHE A 278      27.096  32.049  18.722  1.00 27.64           C  
ATOM   2085  CD2 PHE A 278      26.134  32.359  20.894  1.00 27.54           C  
ATOM   2086  CE1 PHE A 278      27.985  33.097  18.965  1.00 36.92           C  
ATOM   2087  CE2 PHE A 278      27.018  33.410  21.152  1.00 26.20           C  
ATOM   2088  CZ  PHE A 278      27.947  33.781  20.185  1.00 25.30           C  
ATOM   2089  N   ARG A 279      24.399  27.360  19.793  1.00 18.13           N  
ATOM   2090  CA  ARG A 279      23.354  26.347  19.712  1.00 23.59           C  
ATOM   2091  C   ARG A 279      23.148  25.768  21.102  1.00 25.11           C  
ATOM   2092  O   ARG A 279      22.071  25.265  21.432  1.00 33.79           O  
ATOM   2093  CB  ARG A 279      23.757  25.217  18.757  1.00 22.96           C  
ATOM   2094  CG  ARG A 279      23.435  25.472  17.300  1.00 22.76           C  
ATOM   2095  CD  ARG A 279      21.929  25.553  17.105  1.00 33.28           C  
ATOM   2096  NE  ARG A 279      21.537  25.693  15.703  1.00 45.01           N  
ATOM   2097  CZ  ARG A 279      20.277  25.649  15.278  1.00 50.46           C  
ATOM   2098  NH1 ARG A 279      19.288  25.466  16.147  1.00 54.92           N  
ATOM   2099  NH2 ARG A 279      20.002  25.785  13.990  1.00 51.23           N  
ATOM   2100  N   ASN A 280      24.192  25.849  21.916  1.00 28.57           N  
ATOM   2101  CA  ASN A 280      24.149  25.327  23.275  1.00 30.26           C  
ATOM   2102  C   ASN A 280      23.572  26.347  24.247  1.00 33.33           C  
ATOM   2103  O   ASN A 280      23.419  26.057  25.433  1.00 33.26           O  
ATOM   2104  CB  ASN A 280      25.557  24.933  23.725  1.00 32.75           C  
ATOM   2105  CG  ASN A 280      25.561  23.705  24.605  1.00 37.26           C  
ATOM   2106  OD1 ASN A 280      26.558  23.391  25.249  1.00 47.10           O  
ATOM   2107  ND2 ASN A 280      24.442  22.991  24.625  1.00 46.14           N  
ATOM   2108  N   LYS A 281      23.259  27.544  23.758  1.00 29.17           N  
ATOM   2109  CA  LYS A 281      22.684  28.573  24.628  1.00 31.26           C  
ATOM   2110  C   LYS A 281      21.156  28.579  24.528  1.00 26.75           C  
ATOM   2111  O   LYS A 281      20.603  28.772  23.453  1.00 32.90           O  
ATOM   2112  CB  LYS A 281      23.232  29.957  24.259  1.00 27.40           C  
ATOM   2113  CG  LYS A 281      24.727  30.117  24.483  1.00 36.94           C  
ATOM   2114  CD  LYS A 281      25.019  31.248  25.447  1.00 28.40           C  
ATOM   2115  CE  LYS A 281      24.405  30.983  26.815  1.00 35.72           C  
ATOM   2116  NZ  LYS A 281      24.614  32.129  27.750  1.00 29.39           N  
ATOM   2117  N   ALA A 282      20.478  28.358  25.648  1.00 30.23           N  
ATOM   2118  CA  ALA A 282      19.019  28.354  25.655  1.00 40.27           C  
ATOM   2119  C   ALA A 282      18.502  29.789  25.529  1.00 37.98           C  
ATOM   2120  O   ALA A 282      19.174  30.735  25.950  1.00 34.71           O  
ATOM   2121  CB  ALA A 282      18.495  27.710  26.947  1.00 44.28           C  
ATOM   2122  N   ASN A 283      17.311  29.941  24.952  1.00 34.71           N  
ATOM   2123  CA  ASN A 283      16.701  31.254  24.752  1.00 36.68           C  
ATOM   2124  C   ASN A 283      17.224  31.950  23.485  1.00 36.63           C  
ATOM   2125  O   ASN A 283      17.115  33.170  23.342  1.00 37.82           O  
ATOM   2126  CB  ASN A 283      16.934  32.136  25.980  1.00 30.57           C  
ATOM   2127  CG  ASN A 283      16.306  31.558  27.231  1.00 41.16           C  
ATOM   2128  OD1 ASN A 283      16.635  31.954  28.350  1.00 50.18           O  
ATOM   2129  ND2 ASN A 283      15.385  30.618  27.046  1.00 40.39           N  
ATOM   2130  N   VAL A 284      17.796  31.166  22.571  1.00 31.69           N  
ATOM   2131  CA  VAL A 284      18.307  31.691  21.309  1.00 22.19           C  
ATOM   2132  C   VAL A 284      17.412  31.216  20.168  1.00 23.32           C  
ATOM   2133  O   VAL A 284      17.417  30.038  19.797  1.00 28.01           O  
ATOM   2134  CB  VAL A 284      19.758  31.225  21.033  1.00 26.19           C  
ATOM   2135  CG1 VAL A 284      20.232  31.779  19.688  1.00 14.58           C  
ATOM   2136  CG2 VAL A 284      20.684  31.702  22.147  1.00 25.76           C  
ATOM   2137  N   THR A 285      16.635  32.139  19.625  1.00 17.49           N  
ATOM   2138  CA  THR A 285      15.729  31.837  18.529  1.00 11.58           C  
ATOM   2139  C   THR A 285      16.519  31.902  17.222  1.00 12.27           C  
ATOM   2140  O   THR A 285      17.103  32.931  16.883  1.00 12.16           O  
ATOM   2141  CB  THR A 285      14.578  32.845  18.546  1.00  7.24           C  
ATOM   2142  OG1 THR A 285      14.001  32.849  19.860  1.00  7.14           O  
ATOM   2143  CG2 THR A 285      13.507  32.476  17.527  1.00  5.47           C  
ATOM   2144  N   TRP A 286      16.558  30.795  16.493  1.00 13.70           N  
ATOM   2145  CA  TRP A 286      17.328  30.784  15.268  1.00 12.69           C  
ATOM   2146  C   TRP A 286      16.549  31.087  14.004  1.00 17.23           C  
ATOM   2147  O   TRP A 286      15.329  30.942  13.938  1.00 21.18           O  
ATOM   2148  CB  TRP A 286      18.059  29.451  15.113  1.00 12.33           C  
ATOM   2149  CG  TRP A 286      19.103  29.214  16.165  1.00 16.90           C  
ATOM   2150  CD1 TRP A 286      18.913  28.672  17.409  1.00 15.67           C  
ATOM   2151  CD2 TRP A 286      20.499  29.520  16.071  1.00 13.76           C  
ATOM   2152  NE1 TRP A 286      20.104  28.619  18.086  1.00 13.94           N  
ATOM   2153  CE2 TRP A 286      21.096  29.131  17.289  1.00 14.79           C  
ATOM   2154  CE3 TRP A 286      21.307  30.080  15.070  1.00 16.51           C  
ATOM   2155  CZ2 TRP A 286      22.465  29.291  17.539  1.00 13.42           C  
ATOM   2156  CZ3 TRP A 286      22.672  30.238  15.320  1.00 12.73           C  
ATOM   2157  CH2 TRP A 286      23.233  29.841  16.543  1.00 13.32           C  
ATOM   2158  N   PHE A 287      17.281  31.539  13.001  1.00 18.42           N  
ATOM   2159  CA  PHE A 287      16.696  31.850  11.725  1.00 15.95           C  
ATOM   2160  C   PHE A 287      17.648  31.366  10.666  1.00 17.33           C  
ATOM   2161  O   PHE A 287      18.859  31.587  10.753  1.00 21.42           O  
ATOM   2162  CB  PHE A 287      16.461  33.350  11.584  1.00 19.23           C  
ATOM   2163  CG  PHE A 287      15.319  33.870  12.416  1.00 24.23           C  
ATOM   2164  CD1 PHE A 287      15.499  34.193  13.760  1.00 22.58           C  
ATOM   2165  CD2 PHE A 287      14.057  34.045  11.847  1.00 21.14           C  
ATOM   2166  CE1 PHE A 287      14.442  34.690  14.522  1.00 22.06           C  
ATOM   2167  CE2 PHE A 287      12.997  34.539  12.600  1.00 16.68           C  
ATOM   2168  CZ  PHE A 287      13.187  34.861  13.940  1.00 17.84           C  
ATOM   2169  N   ASP A 288      17.097  30.685   9.670  1.00 23.78           N  
ATOM   2170  CA  ASP A 288      17.894  30.155   8.577  1.00 22.08           C  
ATOM   2171  C   ASP A 288      18.002  31.211   7.484  1.00 23.68           C  
ATOM   2172  O   ASP A 288      16.996  31.697   6.976  1.00 20.25           O  
ATOM   2173  CB  ASP A 288      17.236  28.890   8.032  1.00 28.88           C  
ATOM   2174  CG  ASP A 288      18.159  28.094   7.138  1.00 31.94           C  
ATOM   2175  OD1 ASP A 288      17.852  26.907   6.911  1.00 36.83           O  
ATOM   2176  OD2 ASP A 288      19.180  28.651   6.658  1.00 21.44           O  
HETATM 2177  N   MSE A 289      19.233  31.558   7.130  1.00 22.61           N  
HETATM 2178  CA  MSE A 289      19.485  32.562   6.110  1.00 23.55           C  
HETATM 2179  C   MSE A 289      19.897  31.935   4.788  1.00 20.51           C  
HETATM 2180  O   MSE A 289      20.337  32.635   3.879  1.00 19.20           O  
HETATM 2181  CB  MSE A 289      20.588  33.519   6.576  1.00 24.14           C  
HETATM 2182  CG  MSE A 289      20.320  34.152   7.932  1.00 20.78           C  
HETATM 2183 SE   MSE A 289      18.599  35.027   8.000  1.00 39.42          SE  
HETATM 2184  CE  MSE A 289      19.176  36.793   7.411  1.00 19.84           C  
ATOM   2185  N   THR A 290      19.767  30.617   4.690  1.00 22.69           N  
ATOM   2186  CA  THR A 290      20.142  29.902   3.476  1.00 32.70           C  
ATOM   2187  C   THR A 290      19.479  30.454   2.217  1.00 39.99           C  
ATOM   2188  O   THR A 290      18.303  30.182   1.951  1.00 37.74           O  
ATOM   2189  CB  THR A 290      19.788  28.421   3.569  1.00 27.88           C  
ATOM   2190  OG1 THR A 290      20.476  27.842   4.678  1.00 32.85           O  
ATOM   2191  CG2 THR A 290      20.198  27.702   2.291  1.00 31.13           C  
ATOM   2192  N   ASP A 291      20.259  31.215   1.452  1.00 45.23           N  
ATOM   2193  CA  ASP A 291      19.823  31.836   0.207  1.00 50.72           C  
ATOM   2194  C   ASP A 291      18.312  31.980   0.124  1.00 49.64           C  
ATOM   2195  O   ASP A 291      17.667  31.452  -0.784  1.00 45.00           O  
ATOM   2196  CB  ASP A 291      20.349  31.033  -0.992  1.00 61.31           C  
ATOM   2197  CG  ASP A 291      21.885  30.967  -1.041  1.00 67.63           C  
ATOM   2198  OD1 ASP A 291      22.415  30.294  -1.952  1.00 74.24           O  
ATOM   2199  OD2 ASP A 291      22.559  31.580  -0.181  1.00 60.06           O  
ATOM   2200  N   VAL A 292      17.753  32.698   1.088  1.00 51.40           N  
ATOM   2201  CA  VAL A 292      16.320  32.915   1.125  1.00 53.18           C  
ATOM   2202  C   VAL A 292      16.016  34.388   0.848  1.00 47.80           C  
ATOM   2203  O   VAL A 292      16.928  35.206   0.662  1.00 32.03           O  
ATOM   2204  CB  VAL A 292      15.710  32.459   2.498  1.00 57.87           C  
ATOM   2205  CG1 VAL A 292      16.040  33.454   3.600  1.00 58.18           C  
ATOM   2206  CG2 VAL A 292      14.201  32.269   2.370  1.00 63.83           C  
ATOM   2207  N   ASP A 293      14.726  34.709   0.802  1.00 40.38           N  
ATOM   2208  CA  ASP A 293      14.270  36.060   0.513  1.00 37.49           C  
ATOM   2209  C   ASP A 293      14.561  36.991   1.679  1.00 28.23           C  
ATOM   2210  O   ASP A 293      13.974  36.856   2.745  1.00 27.44           O  
ATOM   2211  CB  ASP A 293      12.771  36.028   0.201  1.00 34.88           C  
ATOM   2212  CG  ASP A 293      12.249  37.361  -0.239  1.00 41.54           C  
ATOM   2213  OD1 ASP A 293      12.858  37.979  -1.141  1.00 51.51           O  
ATOM   2214  OD2 ASP A 293      11.222  37.795   0.310  1.00 51.28           O  
ATOM   2215  N   PHE A 294      15.474  37.935   1.478  1.00 23.23           N  
ATOM   2216  CA  PHE A 294      15.822  38.861   2.545  1.00 24.02           C  
ATOM   2217  C   PHE A 294      14.663  39.710   3.034  1.00 17.54           C  
ATOM   2218  O   PHE A 294      14.350  39.686   4.213  1.00 31.71           O  
ATOM   2219  CB  PHE A 294      16.969  39.781   2.123  1.00 27.83           C  
ATOM   2220  CG  PHE A 294      17.430  40.696   3.221  1.00 25.00           C  
ATOM   2221  CD1 PHE A 294      16.829  41.936   3.413  1.00 25.12           C  
ATOM   2222  CD2 PHE A 294      18.416  40.284   4.115  1.00 24.30           C  
ATOM   2223  CE1 PHE A 294      17.197  42.749   4.480  1.00 29.36           C  
ATOM   2224  CE2 PHE A 294      18.793  41.089   5.188  1.00 24.96           C  
ATOM   2225  CZ  PHE A 294      18.183  42.324   5.372  1.00 29.73           C  
ATOM   2226  N   ASP A 295      14.050  40.483   2.143  1.00 19.50           N  
ATOM   2227  CA  ASP A 295      12.916  41.336   2.495  1.00 18.64           C  
ATOM   2228  C   ASP A 295      11.869  40.613   3.346  1.00 28.20           C  
ATOM   2229  O   ASP A 295      11.238  41.219   4.215  1.00 30.51           O  
ATOM   2230  CB  ASP A 295      12.256  41.873   1.227  1.00 24.11           C  
ATOM   2231  CG  ASP A 295      13.135  42.863   0.492  1.00 35.25           C  
ATOM   2232  OD1 ASP A 295      12.701  43.359  -0.569  1.00 43.53           O  
ATOM   2233  OD2 ASP A 295      14.258  43.152   0.970  1.00 33.49           O  
ATOM   2234  N   LYS A 296      11.681  39.324   3.085  1.00 19.86           N  
ATOM   2235  CA  LYS A 296      10.724  38.530   3.840  1.00 28.12           C  
ATOM   2236  C   LYS A 296      11.282  38.102   5.207  1.00 24.42           C  
ATOM   2237  O   LYS A 296      10.568  38.162   6.203  1.00 31.88           O  
ATOM   2238  CB  LYS A 296      10.304  37.291   3.034  1.00 19.28           C  
ATOM   2239  CG  LYS A 296       9.124  36.512   3.625  1.00 26.64           C  
ATOM   2240  CD  LYS A 296       8.842  35.239   2.828  1.00 21.03           C  
ATOM   2241  CE  LYS A 296       7.719  34.412   3.444  1.00 27.85           C  
ATOM   2242  NZ  LYS A 296       6.396  35.095   3.353  1.00 21.44           N  
ATOM   2243  N   LYS A 297      12.545  37.679   5.264  1.00 23.54           N  
ATOM   2244  CA  LYS A 297      13.149  37.248   6.531  1.00 21.90           C  
ATOM   2245  C   LYS A 297      13.283  38.364   7.541  1.00 19.77           C  
ATOM   2246  O   LYS A 297      12.876  38.227   8.694  1.00 28.00           O  
ATOM   2247  CB  LYS A 297      14.547  36.664   6.322  1.00 12.67           C  
ATOM   2248  CG  LYS A 297      14.585  35.166   6.158  1.00 25.18           C  
ATOM   2249  CD  LYS A 297      14.059  34.437   7.383  1.00 23.19           C  
ATOM   2250  CE  LYS A 297      13.721  32.996   7.027  1.00 21.22           C  
ATOM   2251  NZ  LYS A 297      12.896  32.342   8.073  1.00 23.85           N  
ATOM   2252  N   ILE A 298      13.881  39.464   7.110  1.00 15.58           N  
ATOM   2253  CA  ILE A 298      14.088  40.592   7.999  1.00 19.66           C  
ATOM   2254  C   ILE A 298      12.760  41.064   8.582  1.00 18.84           C  
ATOM   2255  O   ILE A 298      12.703  41.520   9.724  1.00 24.98           O  
ATOM   2256  CB  ILE A 298      14.798  41.744   7.260  1.00 17.72           C  
ATOM   2257  CG1 ILE A 298      15.709  42.491   8.231  1.00 25.43           C  
ATOM   2258  CG2 ILE A 298      13.782  42.686   6.634  1.00 18.95           C  
ATOM   2259  CD1 ILE A 298      14.988  43.305   9.273  1.00 35.97           C  
HETATM 2260  N   MSE A 299      11.691  40.940   7.803  1.00 11.37           N  
HETATM 2261  CA  MSE A 299      10.379  41.349   8.274  1.00 20.19           C  
HETATM 2262  C   MSE A 299       9.895  40.344   9.321  1.00 16.98           C  
HETATM 2263  O   MSE A 299       9.247  40.721  10.295  1.00 24.49           O  
HETATM 2264  CB  MSE A 299       9.403  41.428   7.092  1.00 28.17           C  
HETATM 2265  CG  MSE A 299       8.075  42.115   7.384  1.00 43.22           C  
HETATM 2266 SE   MSE A 299       7.047  42.505   5.751  1.00 60.98          SE  
HETATM 2267  CE  MSE A 299       6.611  40.680   5.202  1.00 49.55           C  
ATOM   2268  N   GLU A 300      10.231  39.071   9.133  1.00 13.33           N  
ATOM   2269  CA  GLU A 300       9.833  38.030  10.076  1.00 10.75           C  
ATOM   2270  C   GLU A 300      10.614  38.167  11.371  1.00 13.75           C  
ATOM   2271  O   GLU A 300      10.073  37.961  12.458  1.00 15.13           O  
ATOM   2272  CB  GLU A 300      10.094  36.638   9.495  1.00 14.37           C  
ATOM   2273  CG  GLU A 300       9.797  35.488  10.462  1.00 10.35           C  
ATOM   2274  CD  GLU A 300      10.518  34.198  10.091  1.00 23.83           C  
ATOM   2275  OE1 GLU A 300      10.914  34.049   8.909  1.00 20.80           O  
ATOM   2276  OE2 GLU A 300      10.684  33.326  10.982  1.00 24.44           O  
ATOM   2277  N   ILE A 301      11.894  38.508  11.249  1.00 12.12           N  
ATOM   2278  CA  ILE A 301      12.763  38.656  12.410  1.00  8.82           C  
ATOM   2279  C   ILE A 301      12.390  39.876  13.235  1.00 13.90           C  
ATOM   2280  O   ILE A 301      12.465  39.832  14.458  1.00  8.55           O  
ATOM   2281  CB  ILE A 301      14.245  38.797  11.997  1.00 14.65           C  
ATOM   2282  CG1 ILE A 301      14.747  37.483  11.403  1.00 13.07           C  
ATOM   2283  CG2 ILE A 301      15.091  39.178  13.214  1.00 20.35           C  
ATOM   2284  CD1 ILE A 301      16.147  37.564  10.867  1.00  3.22           C  
ATOM   2285  N   HIS A 302      12.011  40.965  12.562  1.00 11.81           N  
ATOM   2286  CA  HIS A 302      11.635  42.192  13.247  1.00 13.14           C  
ATOM   2287  C   HIS A 302      10.347  41.994  14.024  1.00 20.91           C  
ATOM   2288  O   HIS A 302      10.202  42.471  15.153  1.00 20.41           O  
ATOM   2289  CB  HIS A 302      11.437  43.330  12.259  1.00 13.66           C  
ATOM   2290  CG  HIS A 302      10.710  44.506  12.842  1.00 18.61           C  
ATOM   2291  ND1 HIS A 302       9.338  44.556  12.942  1.00 19.40           N  
ATOM   2292  CD2 HIS A 302      11.174  45.657  13.388  1.00 21.71           C  
ATOM   2293  CE1 HIS A 302       8.982  45.694  13.523  1.00 11.54           C  
ATOM   2294  NE2 HIS A 302      10.074  46.375  13.802  1.00 22.44           N  
ATOM   2295  N   ASN A 303       9.401  41.309  13.405  1.00 12.49           N  
ATOM   2296  CA  ASN A 303       8.149  41.055  14.071  1.00 20.78           C  
ATOM   2297  C   ASN A 303       8.414  40.273  15.350  1.00 23.72           C  
ATOM   2298  O   ASN A 303       7.943  40.660  16.417  1.00 30.62           O  
ATOM   2299  CB  ASN A 303       7.204  40.279  13.156  1.00 10.99           C  
ATOM   2300  CG  ASN A 303       5.898  39.958  13.830  1.00 19.85           C  
ATOM   2301  OD1 ASN A 303       5.675  38.833  14.279  1.00 13.18           O  
ATOM   2302  ND2 ASN A 303       5.025  40.956  13.931  1.00 14.81           N  
ATOM   2303  N   PHE A 304       9.190  39.194  15.253  1.00 22.33           N  
ATOM   2304  CA  PHE A 304       9.491  38.385  16.432  1.00 20.89           C  
ATOM   2305  C   PHE A 304      10.205  39.152  17.545  1.00 17.90           C  
ATOM   2306  O   PHE A 304       9.842  39.047  18.718  1.00 17.32           O  
ATOM   2307  CB  PHE A 304      10.332  37.166  16.066  1.00 12.36           C  
ATOM   2308  CG  PHE A 304      10.822  36.417  17.261  1.00 14.80           C  
ATOM   2309  CD1 PHE A 304      12.044  36.743  17.854  1.00 10.33           C  
ATOM   2310  CD2 PHE A 304      10.047  35.412  17.827  1.00 14.17           C  
ATOM   2311  CE1 PHE A 304      12.494  36.082  19.013  1.00  5.27           C  
ATOM   2312  CE2 PHE A 304      10.477  34.741  18.983  1.00 18.66           C  
ATOM   2313  CZ  PHE A 304      11.714  35.081  19.576  1.00 13.10           C  
ATOM   2314  N   ILE A 305      11.229  39.909  17.167  1.00 15.99           N  
ATOM   2315  CA  ILE A 305      11.995  40.703  18.112  1.00 20.42           C  
ATOM   2316  C   ILE A 305      11.122  41.772  18.755  1.00 18.82           C  
ATOM   2317  O   ILE A 305      11.004  41.834  19.980  1.00 21.61           O  
ATOM   2318  CB  ILE A 305      13.196  41.371  17.412  1.00 17.81           C  
ATOM   2319  CG1 ILE A 305      14.241  40.312  17.067  1.00 17.31           C  
ATOM   2320  CG2 ILE A 305      13.789  42.445  18.295  1.00 14.66           C  
ATOM   2321  CD1 ILE A 305      15.460  40.863  16.344  1.00 24.62           C  
ATOM   2322  N   ALA A 306      10.507  42.607  17.926  1.00 18.57           N  
ATOM   2323  CA  ALA A 306       9.636  43.669  18.415  1.00 20.86           C  
ATOM   2324  C   ALA A 306       8.559  43.111  19.344  1.00 23.21           C  
ATOM   2325  O   ALA A 306       8.275  43.695  20.389  1.00 19.17           O  
ATOM   2326  CB  ALA A 306       8.982  44.408  17.238  1.00 18.03           C  
ATOM   2327  N   GLY A 307       7.967  41.978  18.966  1.00 28.40           N  
ATOM   2328  CA  GLY A 307       6.936  41.371  19.791  1.00 15.22           C  
ATOM   2329  C   GLY A 307       7.442  40.887  21.139  1.00 19.91           C  
ATOM   2330  O   GLY A 307       6.908  41.281  22.176  1.00 21.12           O  
ATOM   2331  N   LYS A 308       8.477  40.050  21.142  1.00 22.60           N  
ATOM   2332  CA  LYS A 308       9.009  39.519  22.400  1.00 26.26           C  
ATOM   2333  C   LYS A 308       9.426  40.628  23.359  1.00 25.51           C  
ATOM   2334  O   LYS A 308       9.197  40.519  24.561  1.00 31.27           O  
ATOM   2335  CB  LYS A 308      10.194  38.581  22.145  1.00 20.75           C  
ATOM   2336  CG  LYS A 308      10.625  37.761  23.362  1.00 15.94           C  
ATOM   2337  CD  LYS A 308      11.841  36.897  23.028  1.00 43.31           C  
ATOM   2338  CE  LYS A 308      12.330  36.052  24.216  1.00 42.89           C  
ATOM   2339  NZ  LYS A 308      13.523  35.220  23.863  1.00 32.72           N  
ATOM   2340  N   LEU A 309      10.033  41.694  22.844  1.00 30.64           N  
ATOM   2341  CA  LEU A 309      10.437  42.799  23.712  1.00 25.23           C  
ATOM   2342  C   LEU A 309       9.224  43.405  24.411  1.00 24.66           C  
ATOM   2343  O   LEU A 309       9.276  43.711  25.601  1.00 26.67           O  
ATOM   2344  CB  LEU A 309      11.161  43.884  22.914  1.00 25.25           C  
ATOM   2345  CG  LEU A 309      12.619  43.594  22.558  1.00 23.59           C  
ATOM   2346  CD1 LEU A 309      13.151  44.699  21.660  1.00 20.41           C  
ATOM   2347  CD2 LEU A 309      13.435  43.485  23.837  1.00 19.61           C  
ATOM   2348  N   GLU A 310       8.134  43.566  23.666  1.00 25.05           N  
ATOM   2349  CA  GLU A 310       6.904  44.137  24.206  1.00 23.60           C  
ATOM   2350  C   GLU A 310       6.175  43.229  25.183  1.00 21.99           C  
ATOM   2351  O   GLU A 310       5.648  43.705  26.183  1.00 20.59           O  
ATOM   2352  CB  GLU A 310       5.929  44.496  23.089  1.00 25.21           C  
ATOM   2353  CG  GLU A 310       4.667  45.170  23.600  1.00 24.83           C  
ATOM   2354  CD  GLU A 310       4.966  46.499  24.266  1.00 36.86           C  
ATOM   2355  OE1 GLU A 310       4.020  47.163  24.750  1.00 38.51           O  
ATOM   2356  OE2 GLU A 310       6.156  46.880  24.303  1.00 37.06           O  
ATOM   2357  N   GLU A 311       6.110  41.934  24.896  1.00 20.35           N  
ATOM   2358  CA  GLU A 311       5.417  41.050  25.816  1.00 25.74           C  
ATOM   2359  C   GLU A 311       6.223  40.858  27.100  1.00 24.17           C  
ATOM   2360  O   GLU A 311       5.646  40.613  28.162  1.00 26.49           O  
ATOM   2361  CB  GLU A 311       5.122  39.695  25.173  1.00 30.53           C  
ATOM   2362  CG  GLU A 311       6.316  38.793  25.088  1.00 34.13           C  
ATOM   2363  CD  GLU A 311       5.945  37.397  24.642  1.00 29.55           C  
ATOM   2364  OE1 GLU A 311       5.012  36.815  25.231  1.00 26.61           O  
ATOM   2365  OE2 GLU A 311       6.592  36.880  23.710  1.00 36.73           O  
ATOM   2366  N   LYS A 312       7.548  40.971  27.016  1.00 21.13           N  
ATOM   2367  CA  LYS A 312       8.379  40.827  28.211  1.00 24.10           C  
ATOM   2368  C   LYS A 312       8.211  42.097  29.028  1.00 22.27           C  
ATOM   2369  O   LYS A 312       8.135  42.053  30.253  1.00 28.92           O  
ATOM   2370  CB  LYS A 312       9.857  40.621  27.842  1.00 24.83           C  
ATOM   2371  CG  LYS A 312      10.160  39.246  27.258  1.00 27.82           C  
ATOM   2372  CD  LYS A 312      11.579  39.159  26.714  1.00 36.38           C  
ATOM   2373  CE  LYS A 312      12.628  39.128  27.813  1.00 39.44           C  
ATOM   2374  NZ  LYS A 312      12.709  37.797  28.473  1.00 37.85           N  
ATOM   2375  N   SER A 313       8.142  43.229  28.339  1.00 18.41           N  
ATOM   2376  CA  SER A 313       7.958  44.498  29.017  1.00 24.11           C  
ATOM   2377  C   SER A 313       6.601  44.498  29.728  1.00 28.57           C  
ATOM   2378  O   SER A 313       6.512  44.887  30.892  1.00 30.30           O  
ATOM   2379  CB  SER A 313       8.037  45.654  28.018  1.00 20.71           C  
ATOM   2380  OG  SER A 313       7.912  46.903  28.675  1.00 34.06           O  
ATOM   2381  N   LYS A 314       5.547  44.051  29.046  1.00 32.06           N  
ATOM   2382  CA  LYS A 314       4.218  44.013  29.663  1.00 37.06           C  
ATOM   2383  C   LYS A 314       4.184  43.073  30.864  1.00 39.81           C  
ATOM   2384  O   LYS A 314       3.615  43.406  31.903  1.00 41.93           O  
ATOM   2385  CB  LYS A 314       3.153  43.567  28.656  1.00 39.64           C  
ATOM   2386  CG  LYS A 314       2.680  44.649  27.703  1.00 41.99           C  
ATOM   2387  CD  LYS A 314       1.682  44.090  26.694  1.00 46.70           C  
ATOM   2388  CE  LYS A 314       1.313  45.127  25.637  1.00 51.69           C  
ATOM   2389  NZ  LYS A 314       0.634  44.518  24.456  1.00 51.59           N  
ATOM   2390  N   LEU A 315       4.793  41.900  30.707  1.00 41.98           N  
ATOM   2391  CA  LEU A 315       4.839  40.899  31.766  1.00 42.49           C  
ATOM   2392  C   LEU A 315       5.523  41.479  32.994  1.00 45.58           C  
ATOM   2393  O   LEU A 315       5.109  41.232  34.126  1.00 49.80           O  
ATOM   2394  CB  LEU A 315       5.609  39.670  31.291  1.00 42.18           C  
ATOM   2395  CG  LEU A 315       5.576  38.451  32.207  1.00 44.44           C  
ATOM   2396  CD1 LEU A 315       4.218  37.768  32.093  1.00 40.81           C  
ATOM   2397  CD2 LEU A 315       6.681  37.493  31.811  1.00 43.15           C  
ATOM   2398  N   GLU A 316       6.579  42.249  32.761  1.00 47.64           N  
ATOM   2399  CA  GLU A 316       7.323  42.879  33.841  1.00 54.67           C  
ATOM   2400  C   GLU A 316       6.465  43.921  34.562  1.00 55.79           C  
ATOM   2401  O   GLU A 316       6.613  44.127  35.764  1.00 55.44           O  
ATOM   2402  CB  GLU A 316       8.606  43.515  33.283  1.00 57.02           C  
ATOM   2403  CG  GLU A 316       9.368  44.408  34.257  1.00 66.27           C  
ATOM   2404  CD  GLU A 316       8.851  45.841  34.275  1.00 74.53           C  
ATOM   2405  OE1 GLU A 316       9.304  46.625  35.138  1.00 78.65           O  
ATOM   2406  OE2 GLU A 316       8.002  46.187  33.423  1.00 73.76           O  
ATOM   2407  N   HIS A 317       5.551  44.562  33.842  1.00 60.37           N  
ATOM   2408  CA  HIS A 317       4.693  45.568  34.462  1.00 70.24           C  
ATOM   2409  C   HIS A 317       3.708  44.922  35.435  1.00 74.32           C  
ATOM   2410  O   HIS A 317       3.321  45.528  36.437  1.00 75.46           O  
ATOM   2411  CB  HIS A 317       3.921  46.349  33.392  1.00 72.25           C  
ATOM   2412  CG  HIS A 317       3.077  47.454  33.946  1.00 75.24           C  
ATOM   2413  ND1 HIS A 317       3.611  48.529  34.625  1.00 75.61           N  
ATOM   2414  CD2 HIS A 317       1.736  47.643  33.941  1.00 77.59           C  
ATOM   2415  CE1 HIS A 317       2.636  49.330  35.015  1.00 75.69           C  
ATOM   2416  NE2 HIS A 317       1.488  48.815  34.612  1.00 76.36           N  
ATOM   2417  N   HIS A 318       3.325  43.683  35.130  1.00 78.33           N  
ATOM   2418  CA  HIS A 318       2.378  42.907  35.934  1.00 83.00           C  
ATOM   2419  C   HIS A 318       1.427  43.761  36.768  1.00 85.86           C  
ATOM   2420  O   HIS A 318       1.392  43.572  38.002  1.00 87.96           O  
ATOM   2421  CB  HIS A 318       3.122  41.908  36.841  1.00 79.98           C  
ATOM   2422  CG  HIS A 318       4.234  42.513  37.645  1.00 80.09           C  
ATOM   2423  ND1 HIS A 318       4.085  43.673  38.376  1.00 79.10           N  
ATOM   2424  CD2 HIS A 318       5.504  42.094  37.860  1.00 74.84           C  
ATOM   2425  CE1 HIS A 318       5.215  43.943  39.006  1.00 76.50           C  
ATOM   2426  NE2 HIS A 318       6.091  43.000  38.710  1.00 78.32           N  
TER    2427      HIS A 318                                                      
END                                                                             



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