CNRS Nantes University UFIP UFIP
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***  1q18  ***

elNémo ID: 22042405255378885

Job options:

ID        	=	 22042405255378885
JOBID     	=	 1q18
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 1q18

HEADER    TRANSFERASE                             18-JUL-03   1Q18              
TITLE     CRYSTAL STRUCTURE OF E.COLI GLUCOKINASE (GLK)                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOKINASE;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GLUCOSE KINASE;                                             
COMPND   5 EC: 2.7.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: GLK OR B2388 OR Z3654 OR ECS3268;                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFO4                                      
KEYWDS    GLUCOKINASE, ATP, KINASE, PHOSPHOTRANSFER, MONTREAL-                  
KEYWDS   2 KINGSTON BACTERIAL STRUCTURAL GENOMICS INITIATIVE, BSGI,             
KEYWDS   3 STRUCTURAL GENOMICS, TRANSFERASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.V.LUNIN,Y.LI,J.D.SCHRAG,A.MATTE,M.CYGLER,MONTREAL-                  
AUTHOR   2 KINGSTON BACTERIAL STRUCTURAL GENOMICS INITIATIVE (BSGI)             
REVDAT   3   24-FEB-09 1Q18    1       VERSN                                    
REVDAT   2   23-NOV-04 1Q18    1       JRNL                                     
REVDAT   1   27-JUL-04 1Q18    0                                                
JRNL        AUTH   V.V.LUNIN,Y.LI,J.D.SCHRAG,P.IANNUZZI,M.CYGLER,               
JRNL        AUTH 2 A.MATTE                                                      
JRNL        TITL   CRYSTAL STRUCTURES OF ESCHERICHIA COLI                       
JRNL        TITL 2 ATP-DEPENDENT GLUCOKINASE AND ITS COMPLEX WITH               
JRNL        TITL 3 GLUCOSE.                                                     
JRNL        REF    J.BACTERIOL.                  V. 186  6915 2004              
JRNL        REFN                   ISSN 0021-9193                               
JRNL        PMID   15466045                                                     
JRNL        DOI    10.1128/JB.186.20.6915-6927.2004                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.36 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30408                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1657                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.36                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.42                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2029                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 117                          
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4908                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 387                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.375         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.270         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.177         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.238         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4994 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6765 ; 1.226 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   640 ; 5.892 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   761 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3768 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2487 ; 0.208 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   366 ; 0.165 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    35 ; 0.218 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3161 ; 0.606 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5055 ; 1.156 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1833 ; 1.648 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1710 ; 2.704 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Q18 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019788.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.964711, 0.979962, 0.980178       
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30408                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.360                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.760                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.1M TRIS-HCL, 0.2M        
REMARK 280  MGCL2, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      117.35500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       40.73700            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       40.73700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      176.03250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       40.73700            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       40.73700            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.67750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       40.73700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.73700            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      176.03250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       40.73700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.73700            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       58.67750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      117.35500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER                               
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     MSE B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG A   178     O    ILE A   181              2.06            
REMARK 500   CB   ASP A   293     O    HOH A   541              2.09            
REMARK 500   O    ARG B   178     O    ILE B   181              2.15            
REMARK 500   NZ   LYS B   128     O    HOH B   404              2.16            
REMARK 500   C    ALA B    43     O    HOH B   397              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  85   CG    GLU A  85   CD      0.094                       
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    CYS A  65   CA  -  CB  -  SG  ANGL. DEV. =   7.3 DEGREES          
REMARK 500    GLY A  91   C   -  N   -  CA  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ARG A 188   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 243   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    LEU A 307   CA  -  CB  -  CG  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    ASP B 148   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 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    ASN A  76       64.25     79.08                                   
REMARK 500    SER A 191      172.84    176.92                                   
REMARK 500    LYS B   3      118.22    177.43                                   
REMARK 500    VAL B  44      -36.73   -150.20                                   
REMARK 500    HIS B  52      -26.57   -142.05                                   
REMARK 500    THR B  68      -87.82   -115.27                                   
REMARK 500    ALA B 122     -125.87    -80.52                                   
REMARK 500    ASP B 148       59.70     38.00                                   
REMARK 500    LYS B 149      -18.61     80.41                                   
REMARK 500    LEU B 190       74.48   -116.63                                   
REMARK 500    PHE B 268       39.94   -151.90                                   
REMARK 500    SER B 275      173.68    -59.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A   75     ASN A   76                 -143.95                    
REMARK 500 GLY B   91     PHE B   92                 -139.10                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SZ2   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH LIGAND                                             
REMARK 900 RELATED ID: GLK_ECO57   RELATED DB: TARGETDB                         
DBREF  1Q18 A    2   321  UNP    P0A6V8   GLK_ECOLI        2    321             
DBREF  1Q18 B    2   321  UNP    P0A6V8   GLK_ECOLI        2    321             
SEQADV 1Q18 MSE A  -10  UNP  P0A6V8              MODIFIED RESIDUE               
SEQADV 1Q18 GLY A   -9  UNP  P0A6V8              CLONING ARTIFACT               
SEQADV 1Q18 SER A   -8  UNP  P0A6V8              CLONING ARTIFACT               
SEQADV 1Q18 SER A   -7  UNP  P0A6V8              CLONING ARTIFACT               
SEQADV 1Q18 HIS A   -6  UNP  P0A6V8              EXPRESSION TAG                 
SEQADV 1Q18 HIS A   -5  UNP  P0A6V8              EXPRESSION TAG                 
SEQADV 1Q18 HIS A   -4  UNP  P0A6V8              EXPRESSION TAG                 
SEQADV 1Q18 HIS A   -3  UNP  P0A6V8              EXPRESSION TAG                 
SEQADV 1Q18 HIS A   -2  UNP  P0A6V8              EXPRESSION TAG                 
SEQADV 1Q18 HIS A   -1  UNP  P0A6V8              EXPRESSION TAG                 
SEQADV 1Q18 GLY A   11  UNP  P0A6V8              CLONING ARTIFACT               
SEQADV 1Q18 SER A    1  UNP  P0A6V8              CLONING ARTIFACT               
SEQADV 1Q18 MSE A   74  UNP  P0A6V8    MET    74 MODIFIED RESIDUE               
SEQADV 1Q18 MSE A   86  UNP  P0A6V8    MET    86 MODIFIED RESIDUE               
SEQADV 1Q18 MSE A  106  UNP  P0A6V8    MET   106 MODIFIED RESIDUE               
SEQADV 1Q18 MSE A  110  UNP  P0A6V8    MET   110 MODIFIED RESIDUE               
SEQADV 1Q18 MSE A  241  UNP  P0A6V8    MET   241 MODIFIED RESIDUE               
SEQRES   1 A  332  MSE GLY SER SER HIS HIS HIS HIS HIS HIS GLY SER THR          
SEQRES   2 A  332  LYS TYR ALA LEU VAL GLY ASP VAL GLY GLY THR ASN ALA          
SEQRES   3 A  332  ARG LEU ALA LEU CYS ASP ILE ALA SER GLY GLU ILE SER          
SEQRES   4 A  332  GLN ALA LYS THR TYR SER GLY LEU ASP TYR PRO SER LEU          
SEQRES   5 A  332  GLU ALA VAL ILE ARG VAL TYR LEU GLU GLU HIS LYS VAL          
SEQRES   6 A  332  GLU VAL LYS ASP GLY CYS ILE ALA ILE ALA CYS PRO ILE          
SEQRES   7 A  332  THR GLY ASP TRP VAL ALA MSE THR ASN HIS THR TRP ALA          
SEQRES   8 A  332  PHE SER ILE ALA GLU MSE LYS LYS ASN LEU GLY PHE SER          
SEQRES   9 A  332  HIS LEU GLU ILE ILE ASN ASP PHE THR ALA VAL SER MSE          
SEQRES  10 A  332  ALA ILE PRO MSE LEU LYS LYS GLU HIS LEU ILE GLN PHE          
SEQRES  11 A  332  GLY GLY ALA GLU PRO VAL GLU GLY LYS PRO ILE ALA VAL          
SEQRES  12 A  332  TYR GLY ALA GLY THR GLY LEU GLY VAL ALA HIS LEU VAL          
SEQRES  13 A  332  HIS VAL ASP LYS ARG TRP VAL SER LEU PRO GLY GLU GLY          
SEQRES  14 A  332  GLY HIS VAL ASP PHE ALA PRO ASN SER GLU GLU GLU ALA          
SEQRES  15 A  332  ILE ILE LEU GLU ILE LEU ARG ALA GLU ILE GLY HIS VAL          
SEQRES  16 A  332  SER ALA GLU ARG VAL LEU SER GLY PRO GLY LEU VAL ASN          
SEQRES  17 A  332  LEU TYR ARG ALA ILE VAL LYS ALA ASP ASN ARG LEU PRO          
SEQRES  18 A  332  GLU ASN LEU LYS PRO LYS ASP ILE THR GLU ARG ALA LEU          
SEQRES  19 A  332  ALA ASP SER CYS THR ASP CYS ARG ARG ALA LEU SER LEU          
SEQRES  20 A  332  PHE CYS VAL ILE MSE GLY ARG PHE GLY GLY ASN LEU ALA          
SEQRES  21 A  332  LEU ASN LEU GLY THR PHE GLY GLY VAL PHE ILE ALA GLY          
SEQRES  22 A  332  GLY ILE VAL PRO ARG PHE LEU GLU PHE PHE LYS ALA SER          
SEQRES  23 A  332  GLY PHE ARG ALA ALA PHE GLU ASP LYS GLY ARG PHE LYS          
SEQRES  24 A  332  GLU TYR VAL HIS ASP ILE PRO VAL TYR LEU ILE VAL HIS          
SEQRES  25 A  332  ASP ASN PRO GLY LEU LEU GLY SER GLY ALA HIS LEU ARG          
SEQRES  26 A  332  GLN THR LEU GLY HIS ILE LEU                                  
MODRES 1Q18 MSE A   74  MET  SELENOMETHIONINE                                   
MODRES 1Q18 MSE A   86  MET  SELENOMETHIONINE                                   
MODRES 1Q18 MSE A  106  MET  SELENOMETHIONINE                                   
MODRES 1Q18 MSE A  110  MET  SELENOMETHIONINE                                   
MODRES 1Q18 MSE A  241  MET  SELENOMETHIONINE                                   
HET    MSE  A  74       8                                                       
HET    MSE  A  86       8                                                       
HET    MSE  A 106       8                                                       
HET    MSE  A 110       8                                                       
HET    MSE  A 241       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    10(C5 H11 N O2 SE)                                           
FORMUL   3  HOH   *387(H2 O)                                                    
HELIX    1   1 LEU A   36  TYR A   38  5                                   3    
HELIX    2   2 SER A   40  LYS A   53  1                                  14    
HELIX    3   3 ASN A   76  ALA A   80  5                                   5    
HELIX    4   4 ILE A   83  LEU A   90  1                                   8    
HELIX    5   5 ASP A  100  ILE A  108  1                                   9    
HELIX    6   6 PRO A  109  LEU A  111  5                                   3    
HELIX    7   7 LYS A  112  GLU A  114  5                                   3    
HELIX    8   8 GLU A  157  VAL A  161  5                                   5    
HELIX    9   9 SER A  167  ILE A  181  1                                  15    
HELIX   10  10 SER A  191  ASP A  206  1                                  16    
HELIX   11  11 LYS A  214  ALA A  224  1                                  11    
HELIX   12  12 CYS A  227  GLY A  253  1                                  27    
HELIX   13  13 ILE A  264  ARG A  267  5                                   4    
HELIX   14  14 PHE A  268  ALA A  274  1                                   7    
HELIX   15  15 GLY A  276  ASP A  283  1                                   8    
HELIX   16  16 LYS A  284  ARG A  286  5                                   3    
HELIX   17  17 PHE A  287  HIS A  292  1                                   6    
HELIX   18  18 ASN A  303  LEU A  317  1                                  15    
SHEET    1   A 5 ILE A  27  SER A  34  0                                        
SHEET    2   A 5 ASN A  14  ASP A  21 -1  N  ALA A  15   O  TYR A  33           
SHEET    3   A 5 TYR A   4  VAL A  10 -1  N  ALA A   5   O  CYS A  20           
SHEET    4   A 5 ASP A  58  ILE A  63  1  O  ALA A  62   N  VAL A  10           
SHEET    5   A 5 HIS A  94  ASN A  99  1  O  GLU A  96   N  GLY A  59           
SHEET    1   B 2 TRP A  71  VAL A  72  0                                        
SHEET    2   B 2 PHE A  81  SER A  82 -1  O  PHE A  81   N  VAL A  72           
SHEET    1   C 6 LEU A 116  GLN A 118  0                                        
SHEET    2   C 6 VAL A 296  ILE A 299 -1  O  LEU A 298   N  ILE A 117           
SHEET    3   C 6 VAL A 258  ILE A 260  1  N  ILE A 260   O  TYR A 297           
SHEET    4   C 6 ILE A 130  ALA A 135  1  N  ALA A 131   O  PHE A 259           
SHEET    5   C 6 LEU A 139  VAL A 147 -1  O  ALA A 142   N  VAL A 132           
SHEET    6   C 6 ARG A 150  LEU A 154 -1  O  LEU A 154   N  HIS A 143           
LINK         C   ALA A  73                 N   MSE A  74     1555   1555  1.31  
LINK         C   MSE A  74                 N   THR A  75     1555   1555  1.32  
LINK         C   GLU A  85                 N   MSE A  86     1555   1555  1.35  
LINK         C   MSE A  86                 N   LYS A  87     1555   1555  1.33  
LINK         C   SER A 105                 N   MSE A 106     1555   1555  1.34  
LINK         C   MSE A 106                 N   ALA A 107     1555   1555  1.34  
LINK         C   PRO A 109                 N   MSE A 110     1555   1555  1.32  
LINK         C   MSE A 110                 N   LEU A 111     1555   1555  1.32  
LINK         C   ILE A 240                 N   MSE A 241     1555   1555  1.34  
LINK         C   MSE A 241                 N   GLY A 242     1555   1555  1.35  
CISPEP   1 THR B    2    LYS B    3          0       -18.52                     
CRYST1   81.474   81.474  234.710  90.00  90.00  90.00 P 43 21 2    16          
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      0.012274  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012274  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004261        0.00000                         
ATOM      1  N   THR A   2      18.729 -11.073  20.207  1.00 43.09           N  
ATOM      2  CA  THR A   2      18.567  -9.606  19.790  1.00 42.18           C  
ATOM      3  C   THR A   2      19.785  -8.730  20.073  1.00 40.31           C  
ATOM      4  O   THR A   2      19.983  -8.301  21.206  1.00 41.84           O  
ATOM      5  CB  THR A   2      17.374  -9.018  20.543  1.00 42.93           C  
ATOM      6  OG1 THR A   2      17.225  -9.720  21.799  1.00 44.92           O  
ATOM      7  CG2 THR A   2      16.127  -9.373  19.809  1.00 43.97           C  
ATOM      8  N   LYS A   3      20.599  -8.440  19.072  1.00 37.66           N  
ATOM      9  CA  LYS A   3      21.814  -7.672  19.322  1.00 34.96           C  
ATOM     10  C   LYS A   3      21.594  -6.136  19.494  1.00 34.37           C  
ATOM     11  O   LYS A   3      22.257  -5.471  20.304  1.00 34.32           O  
ATOM     12  CB  LYS A   3      22.810  -7.904  18.193  1.00 34.64           C  
ATOM     13  CG  LYS A   3      24.070  -7.070  18.317  1.00 32.19           C  
ATOM     14  CD  LYS A   3      25.252  -7.808  17.741  1.00 34.72           C  
ATOM     15  CE  LYS A   3      26.323  -6.847  17.244  1.00 38.94           C  
ATOM     16  NZ  LYS A   3      27.284  -6.514  18.352  1.00 37.59           N  
ATOM     17  N   TYR A   4      20.700  -5.573  18.698  1.00 31.66           N  
ATOM     18  CA  TYR A   4      20.617  -4.129  18.612  1.00 30.44           C  
ATOM     19  C   TYR A   4      19.293  -3.667  19.106  1.00 27.91           C  
ATOM     20  O   TYR A   4      18.331  -4.413  18.987  1.00 27.01           O  
ATOM     21  CB  TYR A   4      20.710  -3.703  17.155  1.00 30.89           C  
ATOM     22  CG  TYR A   4      22.075  -3.899  16.598  1.00 32.95           C  
ATOM     23  CD1 TYR A   4      22.273  -4.719  15.483  1.00 33.18           C  
ATOM     24  CD2 TYR A   4      23.170  -3.234  17.152  1.00 30.94           C  
ATOM     25  CE1 TYR A   4      23.535  -4.865  14.939  1.00 35.75           C  
ATOM     26  CE2 TYR A   4      24.414  -3.383  16.611  1.00 34.55           C  
ATOM     27  CZ  TYR A   4      24.574  -4.213  15.509  1.00 36.09           C  
ATOM     28  OH  TYR A   4      25.805  -4.389  14.981  1.00 44.54           O  
ATOM     29  N   ALA A   5      19.250  -2.433  19.624  1.00 25.77           N  
ATOM     30  CA  ALA A   5      17.968  -1.715  19.786  1.00 24.96           C  
ATOM     31  C   ALA A   5      18.007  -0.435  18.969  1.00 24.12           C  
ATOM     32  O   ALA A   5      19.071   0.027  18.584  1.00 24.64           O  
ATOM     33  CB  ALA A   5      17.677  -1.427  21.276  1.00 23.93           C  
ATOM     34  N   LEU A   6      16.861   0.184  18.711  1.00 23.99           N  
ATOM     35  CA  LEU A   6      16.862   1.410  17.895  1.00 22.36           C  
ATOM     36  C   LEU A   6      16.906   2.611  18.833  1.00 21.63           C  
ATOM     37  O   LEU A   6      16.182   2.661  19.838  1.00 21.01           O  
ATOM     38  CB  LEU A   6      15.587   1.464  17.063  1.00 22.45           C  
ATOM     39  CG  LEU A   6      15.343   2.351  15.829  1.00 26.79           C  
ATOM     40  CD1 LEU A   6      14.155   3.232  16.010  1.00 32.03           C  
ATOM     41  CD2 LEU A   6      16.522   3.091  15.243  1.00 24.34           C  
ATOM     42  N   VAL A   7      17.752   3.569  18.521  1.00 19.90           N  
ATOM     43  CA  VAL A   7      17.680   4.821  19.225  1.00 20.06           C  
ATOM     44  C   VAL A   7      17.464   5.979  18.239  1.00 21.16           C  
ATOM     45  O   VAL A   7      17.707   5.862  17.031  1.00 20.78           O  
ATOM     46  CB  VAL A   7      18.898   5.044  20.148  1.00 19.16           C  
ATOM     47  CG1 VAL A   7      18.843   4.037  21.314  1.00 18.09           C  
ATOM     48  CG2 VAL A   7      20.213   4.904  19.386  1.00 18.59           C  
ATOM     49  N   GLY A   8      16.999   7.106  18.769  1.00 22.29           N  
ATOM     50  CA  GLY A   8      16.709   8.263  17.934  1.00 22.34           C  
ATOM     51  C   GLY A   8      16.813   9.543  18.715  1.00 23.03           C  
ATOM     52  O   GLY A   8      16.798   9.556  19.971  1.00 21.73           O  
ATOM     53  N   ASP A   9      16.923  10.623  17.964  1.00 23.72           N  
ATOM     54  CA  ASP A   9      16.990  11.957  18.547  1.00 26.93           C  
ATOM     55  C   ASP A   9      16.351  12.850  17.491  1.00 27.53           C  
ATOM     56  O   ASP A   9      16.906  13.042  16.382  1.00 27.03           O  
ATOM     57  CB  ASP A   9      18.444  12.349  18.779  1.00 27.63           C  
ATOM     58  CG  ASP A   9      18.601  13.652  19.565  1.00 30.43           C  
ATOM     59  OD1 ASP A   9      17.632  14.120  20.209  1.00 32.86           O  
ATOM     60  OD2 ASP A   9      19.707  14.245  19.626  1.00 31.40           O  
ATOM     61  N   VAL A  10      15.144  13.282  17.804  1.00 26.91           N  
ATOM     62  CA  VAL A  10      14.309  13.989  16.866  1.00 27.67           C  
ATOM     63  C   VAL A  10      14.059  15.425  17.337  1.00 29.27           C  
ATOM     64  O   VAL A  10      13.587  15.660  18.437  1.00 27.83           O  
ATOM     65  CB  VAL A  10      12.977  13.220  16.603  1.00 27.16           C  
ATOM     66  CG1 VAL A  10      12.213  13.815  15.393  1.00 26.88           C  
ATOM     67  CG2 VAL A  10      13.263  11.746  16.322  1.00 26.67           C  
ATOM     68  N   GLY A  11      14.410  16.383  16.482  1.00 31.85           N  
ATOM     69  CA  GLY A  11      14.071  17.780  16.701  1.00 34.54           C  
ATOM     70  C   GLY A  11      13.058  18.286  15.687  1.00 36.54           C  
ATOM     71  O   GLY A  11      12.357  17.505  15.021  1.00 36.35           O  
ATOM     72  N   GLY A  12      12.973  19.614  15.573  1.00 38.11           N  
ATOM     73  CA  GLY A  12      11.992  20.234  14.696  1.00 39.17           C  
ATOM     74  C   GLY A  12      12.159  19.982  13.208  1.00 40.27           C  
ATOM     75  O   GLY A  12      11.147  19.956  12.488  1.00 41.73           O  
ATOM     76  N   THR A  13      13.391  19.850  12.714  1.00 39.63           N  
ATOM     77  CA  THR A  13      13.571  19.601  11.279  1.00 39.85           C  
ATOM     78  C   THR A  13      14.249  18.259  10.948  1.00 38.60           C  
ATOM     79  O   THR A  13      14.104  17.754   9.840  1.00 39.46           O  
ATOM     80  CB  THR A  13      14.269  20.811  10.513  1.00 41.24           C  
ATOM     81  OG1 THR A  13      15.013  21.628  11.427  1.00 42.72           O  
ATOM     82  CG2 THR A  13      13.187  21.806   9.952  1.00 43.46           C  
ATOM     83  N   ASN A  14      14.963  17.674  11.899  1.00 36.80           N  
ATOM     84  CA  ASN A  14      15.713  16.475  11.626  1.00 36.01           C  
ATOM     85  C   ASN A  14      15.471  15.351  12.623  1.00 34.22           C  
ATOM     86  O   ASN A  14      15.310  15.575  13.824  1.00 33.62           O  
ATOM     87  CB  ASN A  14      17.210  16.786  11.478  1.00 37.17           C  
ATOM     88  CG  ASN A  14      17.499  17.695  10.269  1.00 39.84           C  
ATOM     89  OD1 ASN A  14      17.036  17.439   9.153  1.00 43.50           O  
ATOM     90  ND2 ASN A  14      18.225  18.782  10.507  1.00 42.75           N  
ATOM     91  N   ALA A  15      15.424  14.143  12.075  1.00 31.58           N  
ATOM     92  CA  ALA A  15      15.338  12.936  12.853  1.00 30.06           C  
ATOM     93  C   ALA A  15      16.637  12.143  12.663  1.00 29.63           C  
ATOM     94  O   ALA A  15      17.007  11.786  11.535  1.00 29.13           O  
ATOM     95  CB  ALA A  15      14.095  12.118  12.440  1.00 29.59           C  
ATOM     96  N   ARG A  16      17.331  11.882  13.767  1.00 28.22           N  
ATOM     97  CA  ARG A  16      18.596  11.161  13.725  1.00 28.53           C  
ATOM     98  C   ARG A  16      18.337   9.772  14.349  1.00 27.27           C  
ATOM     99  O   ARG A  16      17.758   9.659  15.412  1.00 26.07           O  
ATOM    100  CB  ARG A  16      19.727  11.988  14.419  1.00 28.61           C  
ATOM    101  CG  ARG A  16      21.078  11.249  14.566  1.00 35.11           C  
ATOM    102  CD  ARG A  16      22.412  12.047  14.420  1.00 42.26           C  
ATOM    103  NE  ARG A  16      23.098  11.671  13.160  1.00 52.16           N  
ATOM    104  CZ  ARG A  16      24.432  11.561  12.938  1.00 54.09           C  
ATOM    105  NH1 ARG A  16      25.342  11.793  13.887  1.00 55.44           N  
ATOM    106  NH2 ARG A  16      24.849  11.211  11.732  1.00 52.73           N  
ATOM    107  N   LEU A  17      18.722   8.708  13.646  1.00 27.16           N  
ATOM    108  CA  LEU A  17      18.444   7.366  14.110  1.00 25.48           C  
ATOM    109  C   LEU A  17      19.757   6.574  14.115  1.00 25.73           C  
ATOM    110  O   LEU A  17      20.693   6.930  13.426  1.00 25.53           O  
ATOM    111  CB  LEU A  17      17.352   6.703  13.236  1.00 25.05           C  
ATOM    112  CG  LEU A  17      15.931   7.277  13.232  1.00 24.55           C  
ATOM    113  CD1 LEU A  17      15.109   6.479  12.263  1.00 24.61           C  
ATOM    114  CD2 LEU A  17      15.204   7.230  14.624  1.00 23.04           C  
ATOM    115  N   ALA A  18      19.806   5.492  14.897  1.00 24.71           N  
ATOM    116  CA  ALA A  18      21.012   4.715  15.095  1.00 24.34           C  
ATOM    117  C   ALA A  18      20.682   3.410  15.835  1.00 24.86           C  
ATOM    118  O   ALA A  18      19.542   3.177  16.231  1.00 25.01           O  
ATOM    119  CB  ALA A  18      22.062   5.503  15.873  1.00 22.44           C  
ATOM    120  N   LEU A  19      21.705   2.594  16.041  1.00 24.57           N  
ATOM    121  CA  LEU A  19      21.563   1.275  16.611  1.00 25.05           C  
ATOM    122  C   LEU A  19      22.342   1.349  17.882  1.00 25.03           C  
ATOM    123  O   LEU A  19      23.454   1.946  17.909  1.00 24.70           O  
ATOM    124  CB  LEU A  19      22.216   0.224  15.706  1.00 24.21           C  
ATOM    125  CG  LEU A  19      21.450  -0.183  14.439  1.00 25.90           C  
ATOM    126  CD1 LEU A  19      22.219  -1.252  13.699  1.00 25.13           C  
ATOM    127  CD2 LEU A  19      19.997  -0.646  14.782  1.00 25.82           C  
ATOM    128  N   CYS A  20      21.783   0.755  18.928  1.00 25.34           N  
ATOM    129  CA  CYS A  20      22.466   0.750  20.227  1.00 26.52           C  
ATOM    130  C   CYS A  20      22.718  -0.709  20.531  1.00 26.76           C  
ATOM    131  O   CYS A  20      21.795  -1.485  20.539  1.00 26.84           O  
ATOM    132  CB  CYS A  20      21.604   1.388  21.332  1.00 26.05           C  
ATOM    133  SG  CYS A  20      22.161   1.023  23.012  1.00 27.70           S  
ATOM    134  N   ASP A  21      23.980  -1.076  20.721  1.00 28.60           N  
ATOM    135  CA  ASP A  21      24.351  -2.461  21.007  1.00 29.96           C  
ATOM    136  C   ASP A  21      23.859  -2.773  22.412  1.00 29.55           C  
ATOM    137  O   ASP A  21      24.292  -2.168  23.383  1.00 29.78           O  
ATOM    138  CB  ASP A  21      25.875  -2.625  20.913  1.00 31.18           C  
ATOM    139  CG  ASP A  21      26.341  -4.053  21.201  1.00 34.15           C  
ATOM    140  OD1 ASP A  21      26.000  -4.635  22.257  1.00 37.20           O  
ATOM    141  OD2 ASP A  21      27.035  -4.687  20.396  1.00 38.01           O  
ATOM    142  N   ILE A  22      22.948  -3.713  22.540  1.00 30.56           N  
ATOM    143  CA  ILE A  22      22.349  -3.946  23.855  1.00 31.55           C  
ATOM    144  C   ILE A  22      23.326  -4.447  24.936  1.00 32.45           C  
ATOM    145  O   ILE A  22      23.155  -4.131  26.101  1.00 32.83           O  
ATOM    146  CB  ILE A  22      21.086  -4.804  23.723  1.00 31.48           C  
ATOM    147  CG1 ILE A  22      19.947  -3.950  23.141  1.00 31.07           C  
ATOM    148  CG2 ILE A  22      20.634  -5.325  25.067  1.00 32.79           C  
ATOM    149  CD1 ILE A  22      18.764  -4.784  22.596  1.00 30.95           C  
ATOM    150  N   ALA A  23      24.385  -5.158  24.565  1.00 33.38           N  
ATOM    151  CA  ALA A  23      25.274  -5.672  25.589  1.00 34.87           C  
ATOM    152  C   ALA A  23      26.171  -4.572  26.102  1.00 35.28           C  
ATOM    153  O   ALA A  23      26.439  -4.501  27.306  1.00 37.52           O  
ATOM    154  CB  ALA A  23      26.119  -6.867  25.079  1.00 34.87           C  
ATOM    155  N   SER A  24      26.608  -3.699  25.210  1.00 34.62           N  
ATOM    156  CA  SER A  24      27.603  -2.696  25.566  1.00 34.53           C  
ATOM    157  C   SER A  24      27.131  -1.225  25.630  1.00 33.94           C  
ATOM    158  O   SER A  24      27.825  -0.395  26.227  1.00 32.98           O  
ATOM    159  CB  SER A  24      28.780  -2.791  24.602  1.00 34.31           C  
ATOM    160  OG  SER A  24      28.464  -2.140  23.409  1.00 36.33           O  
ATOM    161  N   GLY A  25      25.996  -0.900  24.993  1.00 33.34           N  
ATOM    162  CA  GLY A  25      25.513   0.468  24.969  1.00 32.03           C  
ATOM    163  C   GLY A  25      26.189   1.307  23.916  1.00 32.35           C  
ATOM    164  O   GLY A  25      25.908   2.494  23.784  1.00 30.95           O  
ATOM    165  N   GLU A  26      27.083   0.684  23.150  1.00 33.05           N  
ATOM    166  CA  GLU A  26      27.722   1.335  22.017  1.00 34.05           C  
ATOM    167  C   GLU A  26      26.683   1.784  20.988  1.00 32.95           C  
ATOM    168  O   GLU A  26      25.807   1.003  20.623  1.00 34.03           O  
ATOM    169  CB  GLU A  26      28.706   0.353  21.345  1.00 34.78           C  
ATOM    170  CG  GLU A  26      29.434   0.969  20.147  1.00 40.93           C  
ATOM    171  CD  GLU A  26      30.425   0.026  19.442  1.00 49.89           C  
ATOM    172  OE1 GLU A  26      30.855   0.381  18.283  1.00 48.25           O  
ATOM    173  OE2 GLU A  26      30.774  -1.047  20.054  1.00 51.48           O  
ATOM    174  N   ILE A  27      26.822   3.004  20.475  1.00 31.99           N  
ATOM    175  CA  ILE A  27      25.977   3.523  19.390  1.00 31.53           C  
ATOM    176  C   ILE A  27      26.663   3.444  18.012  1.00 32.20           C  
ATOM    177  O   ILE A  27      27.841   3.796  17.868  1.00 32.41           O  
ATOM    178  CB  ILE A  27      25.566   5.033  19.655  1.00 30.77           C  
ATOM    179  CG1 ILE A  27      24.919   5.220  21.043  1.00 30.31           C  
ATOM    180  CG2 ILE A  27      24.607   5.493  18.645  1.00 30.11           C  
ATOM    181  CD1 ILE A  27      23.716   4.386  21.286  1.00 26.36           C  
ATOM    182  N   SER A  28      25.913   3.047  16.985  1.00 31.58           N  
ATOM    183  CA  SER A  28      26.492   2.963  15.654  1.00 31.76           C  
ATOM    184  C   SER A  28      25.446   3.137  14.527  1.00 32.19           C  
ATOM    185  O   SER A  28      24.220   3.115  14.752  1.00 30.67           O  
ATOM    186  CB  SER A  28      27.239   1.624  15.472  1.00 31.08           C  
ATOM    187  OG  SER A  28      26.316   0.535  15.369  1.00 31.60           O  
ATOM    188  N   GLN A  29      25.988   3.305  13.322  1.00 32.47           N  
ATOM    189  CA  GLN A  29      25.243   3.404  12.080  1.00 32.82           C  
ATOM    190  C   GLN A  29      24.240   4.563  12.159  1.00 32.68           C  
ATOM    191  O   GLN A  29      23.123   4.459  11.701  1.00 32.18           O  
ATOM    192  CB  GLN A  29      24.617   2.055  11.748  1.00 33.06           C  
ATOM    193  CG  GLN A  29      25.653   0.980  11.277  1.00 37.21           C  
ATOM    194  CD  GLN A  29      25.030  -0.096  10.369  1.00 43.96           C  
ATOM    195  OE1 GLN A  29      24.698  -1.205  10.826  1.00 46.45           O  
ATOM    196  NE2 GLN A  29      24.885   0.225   9.079  1.00 46.95           N  
ATOM    197  N   ALA A  30      24.666   5.652  12.792  1.00 33.06           N  
ATOM    198  CA  ALA A  30      23.867   6.853  12.917  1.00 33.81           C  
ATOM    199  C   ALA A  30      23.527   7.413  11.539  1.00 34.83           C  
ATOM    200  O   ALA A  30      24.396   7.451  10.649  1.00 36.45           O  
ATOM    201  CB  ALA A  30      24.625   7.882  13.700  1.00 33.08           C  
ATOM    202  N   LYS A  31      22.284   7.869  11.354  1.00 34.12           N  
ATOM    203  CA  LYS A  31      21.900   8.535  10.121  1.00 33.27           C  
ATOM    204  C   LYS A  31      20.850   9.590  10.402  1.00 32.62           C  
ATOM    205  O   LYS A  31      19.969   9.335  11.205  1.00 32.41           O  
ATOM    206  CB  LYS A  31      21.368   7.529   9.090  1.00 32.65           C  
ATOM    207  CG  LYS A  31      21.461   8.081   7.663  1.00 34.74           C  
ATOM    208  CD  LYS A  31      20.894   7.190   6.562  1.00 40.37           C  
ATOM    209  CE  LYS A  31      20.558   8.032   5.280  1.00 40.31           C  
ATOM    210  NZ  LYS A  31      19.820   7.193   4.295  1.00 41.89           N  
ATOM    211  N   THR A  32      20.940  10.745   9.721  1.00 32.45           N  
ATOM    212  CA  THR A  32      20.016  11.880   9.899  1.00 32.59           C  
ATOM    213  C   THR A  32      19.044  12.039   8.719  1.00 33.30           C  
ATOM    214  O   THR A  32      19.454  12.039   7.586  1.00 32.59           O  
ATOM    215  CB  THR A  32      20.804  13.182  10.033  1.00 32.29           C  
ATOM    216  OG1 THR A  32      21.637  13.112  11.181  1.00 32.90           O  
ATOM    217  CG2 THR A  32      19.870  14.405  10.325  1.00 31.25           C  
ATOM    218  N   TYR A  33      17.757  12.194   8.993  1.00 34.05           N  
ATOM    219  CA  TYR A  33      16.788  12.362   7.933  1.00 34.70           C  
ATOM    220  C   TYR A  33      16.120  13.683   8.089  1.00 35.92           C  
ATOM    221  O   TYR A  33      15.942  14.161   9.206  1.00 36.85           O  
ATOM    222  CB  TYR A  33      15.723  11.274   7.972  1.00 33.67           C  
ATOM    223  CG  TYR A  33      16.280   9.915   7.784  1.00 33.56           C  
ATOM    224  CD1 TYR A  33      16.667   9.150   8.892  1.00 31.89           C  
ATOM    225  CD2 TYR A  33      16.453   9.379   6.504  1.00 30.69           C  
ATOM    226  CE1 TYR A  33      17.154   7.890   8.747  1.00 29.53           C  
ATOM    227  CE2 TYR A  33      16.971   8.101   6.333  1.00 30.76           C  
ATOM    228  CZ  TYR A  33      17.332   7.354   7.469  1.00 31.98           C  
ATOM    229  OH  TYR A  33      17.867   6.074   7.348  1.00 31.34           O  
ATOM    230  N   SER A  34      15.715  14.261   6.963  1.00 37.02           N  
ATOM    231  CA  SER A  34      15.006  15.522   6.992  1.00 38.90           C  
ATOM    232  C   SER A  34      13.508  15.287   7.220  1.00 39.22           C  
ATOM    233  O   SER A  34      12.881  14.516   6.507  1.00 39.44           O  
ATOM    234  CB  SER A  34      15.262  16.338   5.715  1.00 38.88           C  
ATOM    235  OG  SER A  34      14.540  17.552   5.826  1.00 42.59           O  
ATOM    236  N   GLY A  35      12.952  15.933   8.240  1.00 39.77           N  
ATOM    237  CA  GLY A  35      11.547  15.765   8.564  1.00 41.31           C  
ATOM    238  C   GLY A  35      10.576  16.115   7.443  1.00 42.83           C  
ATOM    239  O   GLY A  35       9.558  15.435   7.299  1.00 43.54           O  
ATOM    240  N   LEU A  36      10.879  17.149   6.643  1.00 43.37           N  
ATOM    241  CA  LEU A  36       9.998  17.546   5.543  1.00 43.57           C  
ATOM    242  C   LEU A  36       9.840  16.427   4.509  1.00 43.47           C  
ATOM    243  O   LEU A  36       8.814  16.358   3.821  1.00 44.61           O  
ATOM    244  CB  LEU A  36      10.541  18.768   4.807  1.00 44.49           C  
ATOM    245  CG  LEU A  36      11.179  20.027   5.391  1.00 46.25           C  
ATOM    246  CD1 LEU A  36      12.091  20.653   4.297  1.00 48.52           C  
ATOM    247  CD2 LEU A  36      10.125  21.058   5.893  1.00 49.33           C  
ATOM    248  N   ASP A  37      10.857  15.567   4.376  1.00 41.85           N  
ATOM    249  CA  ASP A  37      10.835  14.482   3.391  1.00 40.05           C  
ATOM    250  C   ASP A  37       9.920  13.274   3.743  1.00 38.94           C  
ATOM    251  O   ASP A  37       9.821  12.335   2.942  1.00 38.49           O  
ATOM    252  CB  ASP A  37      12.239  13.922   3.180  1.00 40.59           C  
ATOM    253  CG  ASP A  37      13.193  14.883   2.458  1.00 43.15           C  
ATOM    254  OD1 ASP A  37      12.767  15.921   1.898  1.00 43.94           O  
ATOM    255  OD2 ASP A  37      14.427  14.648   2.406  1.00 44.06           O  
ATOM    256  N   TYR A  38       9.278  13.265   4.914  1.00 36.84           N  
ATOM    257  CA  TYR A  38       8.584  12.056   5.401  1.00 35.55           C  
ATOM    258  C   TYR A  38       7.252  12.397   6.073  1.00 35.58           C  
ATOM    259  O   TYR A  38       7.146  13.415   6.723  1.00 35.59           O  
ATOM    260  CB  TYR A  38       9.506  11.247   6.335  1.00 34.77           C  
ATOM    261  CG  TYR A  38      10.721  10.645   5.619  1.00 34.52           C  
ATOM    262  CD1 TYR A  38      11.948  11.295   5.626  1.00 34.89           C  
ATOM    263  CD2 TYR A  38      10.621   9.444   4.896  1.00 33.92           C  
ATOM    264  CE1 TYR A  38      13.065  10.772   4.931  1.00 35.42           C  
ATOM    265  CE2 TYR A  38      11.729   8.892   4.234  1.00 34.35           C  
ATOM    266  CZ  TYR A  38      12.955   9.572   4.245  1.00 36.66           C  
ATOM    267  OH  TYR A  38      14.083   9.058   3.569  1.00 38.15           O  
ATOM    268  N   PRO A  39       6.226  11.561   5.940  1.00 35.92           N  
ATOM    269  CA  PRO A  39       4.903  11.891   6.528  1.00 35.90           C  
ATOM    270  C   PRO A  39       4.799  11.724   8.064  1.00 35.47           C  
ATOM    271  O   PRO A  39       3.889  12.322   8.701  1.00 35.07           O  
ATOM    272  CB  PRO A  39       3.949  10.886   5.859  1.00 35.81           C  
ATOM    273  CG  PRO A  39       4.812   9.781   5.347  1.00 36.63           C  
ATOM    274  CD  PRO A  39       6.250  10.245   5.268  1.00 35.67           C  
ATOM    275  N   SER A  40       5.723  10.936   8.642  1.00 33.78           N  
ATOM    276  CA  SER A  40       5.693  10.592  10.064  1.00 32.39           C  
ATOM    277  C   SER A  40       7.025  10.041  10.588  1.00 31.42           C  
ATOM    278  O   SER A  40       7.932   9.691   9.806  1.00 31.65           O  
ATOM    279  CB  SER A  40       4.592   9.568  10.308  1.00 31.78           C  
ATOM    280  OG  SER A  40       4.953   8.324   9.737  1.00 34.14           O  
ATOM    281  N   LEU A  41       7.146   9.964  11.910  1.00 29.28           N  
ATOM    282  CA  LEU A  41       8.332   9.398  12.545  1.00 27.52           C  
ATOM    283  C   LEU A  41       8.359   7.905  12.230  1.00 27.12           C  
ATOM    284  O   LEU A  41       9.412   7.320  11.988  1.00 27.09           O  
ATOM    285  CB  LEU A  41       8.236   9.590  14.063  1.00 27.53           C  
ATOM    286  CG  LEU A  41       9.448   9.687  15.009  1.00 26.71           C  
ATOM    287  CD1 LEU A  41       9.102   9.040  16.312  1.00 23.77           C  
ATOM    288  CD2 LEU A  41      10.785   9.204  14.440  1.00 20.41           C  
ATOM    289  N   GLU A  42       7.201   7.280  12.273  1.00 25.99           N  
ATOM    290  CA  GLU A  42       7.114   5.857  11.964  1.00 26.79           C  
ATOM    291  C   GLU A  42       7.735   5.545  10.583  1.00 27.74           C  
ATOM    292  O   GLU A  42       8.607   4.659  10.449  1.00 28.84           O  
ATOM    293  CB AGLU A  42       5.629   5.489  11.936  0.50 26.58           C  
ATOM    294  CB BGLU A  42       5.687   5.346  12.069  0.50 26.36           C  
ATOM    295  CG AGLU A  42       5.011   5.258  13.293  0.50 25.12           C  
ATOM    296  CG BGLU A  42       5.538   3.841  11.904  0.50 23.88           C  
ATOM    297  CD AGLU A  42       4.039   6.342  13.768  0.50 23.36           C  
ATOM    298  CD BGLU A  42       4.099   3.419  12.160  0.50 23.45           C  
ATOM    299  OE1AGLU A  42       4.359   7.605  13.725  0.50 20.54           O  
ATOM    300  OE1BGLU A  42       3.492   3.934  13.132  0.50 26.99           O  
ATOM    301  OE2AGLU A  42       2.979   5.885  14.253  0.50 16.22           O  
ATOM    302  OE2BGLU A  42       3.561   2.589  11.412  0.50 21.02           O  
ATOM    303  N   ALA A  43       7.316   6.307   9.570  1.00 28.55           N  
ATOM    304  CA  ALA A  43       7.854   6.148   8.243  1.00 29.62           C  
ATOM    305  C   ALA A  43       9.379   6.375   8.186  1.00 30.59           C  
ATOM    306  O   ALA A  43      10.092   5.655   7.451  1.00 32.44           O  
ATOM    307  CB  ALA A  43       7.096   7.049   7.235  1.00 29.55           C  
ATOM    308  N   VAL A  44       9.902   7.348   8.931  1.00 29.95           N  
ATOM    309  CA  VAL A  44      11.353   7.493   8.988  1.00 30.30           C  
ATOM    310  C   VAL A  44      11.972   6.273   9.659  1.00 29.57           C  
ATOM    311  O   VAL A  44      13.047   5.856   9.271  1.00 30.21           O  
ATOM    312  CB  VAL A  44      11.856   8.735   9.769  1.00 30.91           C  
ATOM    313  CG1 VAL A  44      13.375   8.708   9.780  1.00 30.40           C  
ATOM    314  CG2 VAL A  44      11.423  10.005   9.112  1.00 32.19           C  
ATOM    315  N   ILE A  45      11.310   5.704  10.659  1.00 28.56           N  
ATOM    316  CA  ILE A  45      11.854   4.503  11.328  1.00 28.92           C  
ATOM    317  C   ILE A  45      11.957   3.281  10.364  1.00 29.28           C  
ATOM    318  O   ILE A  45      13.006   2.594  10.305  1.00 29.08           O  
ATOM    319  CB  ILE A  45      11.031   4.164  12.628  1.00 28.32           C  
ATOM    320  CG1 ILE A  45      11.221   5.285  13.695  1.00 27.47           C  
ATOM    321  CG2 ILE A  45      11.339   2.706  13.135  1.00 26.69           C  
ATOM    322  CD1 ILE A  45      10.602   4.994  15.079  1.00 23.36           C  
ATOM    323  N   ARG A  46      10.876   3.019   9.614  1.00 28.67           N  
ATOM    324  CA  ARG A  46      10.846   1.880   8.666  1.00 28.69           C  
ATOM    325  C   ARG A  46      11.927   2.029   7.579  1.00 28.85           C  
ATOM    326  O   ARG A  46      12.708   1.094   7.303  1.00 28.29           O  
ATOM    327  CB  ARG A  46       9.481   1.694   8.050  1.00 28.64           C  
ATOM    328  CG  ARG A  46       8.417   1.297   9.056  1.00 28.77           C  
ATOM    329  CD  ARG A  46       6.988   1.486   8.479  1.00 31.86           C  
ATOM    330  NE  ARG A  46       5.967   1.026   9.420  1.00 34.11           N  
ATOM    331  CZ  ARG A  46       5.808  -0.234   9.801  1.00 35.52           C  
ATOM    332  NH1 ARG A  46       6.608  -1.203   9.315  1.00 32.59           N  
ATOM    333  NH2 ARG A  46       4.841  -0.527  10.673  1.00 38.32           N  
ATOM    334  N   VAL A  47      12.025   3.232   7.045  1.00 28.44           N  
ATOM    335  CA  VAL A  47      13.096   3.554   6.124  1.00 29.40           C  
ATOM    336  C   VAL A  47      14.444   3.194   6.707  1.00 29.02           C  
ATOM    337  O   VAL A  47      15.240   2.507   6.057  1.00 31.06           O  
ATOM    338  CB  VAL A  47      13.068   5.063   5.669  1.00 28.84           C  
ATOM    339  CG1 VAL A  47      14.338   5.432   4.960  1.00 31.08           C  
ATOM    340  CG2 VAL A  47      11.942   5.300   4.705  1.00 29.02           C  
ATOM    341  N   TYR A  48      14.727   3.656   7.915  1.00 28.77           N  
ATOM    342  CA  TYR A  48      16.042   3.431   8.508  1.00 28.10           C  
ATOM    343  C   TYR A  48      16.300   1.940   8.618  1.00 29.10           C  
ATOM    344  O   TYR A  48      17.428   1.479   8.374  1.00 29.22           O  
ATOM    345  CB  TYR A  48      16.141   4.068   9.903  1.00 27.67           C  
ATOM    346  CG  TYR A  48      17.453   3.807  10.588  1.00 26.16           C  
ATOM    347  CD1 TYR A  48      18.546   4.630  10.377  1.00 24.30           C  
ATOM    348  CD2 TYR A  48      17.595   2.737  11.475  1.00 26.37           C  
ATOM    349  CE1 TYR A  48      19.791   4.365  11.013  1.00 26.41           C  
ATOM    350  CE2 TYR A  48      18.824   2.470  12.112  1.00 26.95           C  
ATOM    351  CZ  TYR A  48      19.913   3.281  11.858  1.00 29.64           C  
ATOM    352  OH  TYR A  48      21.128   2.998  12.473  1.00 32.50           O  
ATOM    353  N   LEU A  49      15.271   1.187   9.017  1.00 29.67           N  
ATOM    354  CA  LEU A  49      15.469  -0.225   9.291  1.00 30.52           C  
ATOM    355  C   LEU A  49      15.640  -1.030   8.006  1.00 32.35           C  
ATOM    356  O   LEU A  49      16.369  -2.022   8.018  1.00 32.43           O  
ATOM    357  CB  LEU A  49      14.386  -0.805  10.193  1.00 29.32           C  
ATOM    358  CG  LEU A  49      14.351  -0.217  11.635  1.00 28.82           C  
ATOM    359  CD1 LEU A  49      13.048  -0.616  12.319  1.00 27.86           C  
ATOM    360  CD2 LEU A  49      15.570  -0.624  12.529  1.00 24.30           C  
ATOM    361  N   GLU A  50      15.025  -0.585   6.908  1.00 33.98           N  
ATOM    362  CA  GLU A  50      15.184  -1.272   5.622  1.00 36.49           C  
ATOM    363  C   GLU A  50      16.535  -0.958   5.025  1.00 35.78           C  
ATOM    364  O   GLU A  50      17.183  -1.853   4.564  1.00 35.73           O  
ATOM    365  CB  GLU A  50      14.093  -0.901   4.592  1.00 37.42           C  
ATOM    366  CG  GLU A  50      12.734  -1.522   4.866  1.00 44.14           C  
ATOM    367  CD  GLU A  50      12.776  -3.034   5.109  1.00 51.43           C  
ATOM    368  OE1 GLU A  50      13.224  -3.760   4.173  1.00 52.89           O  
ATOM    369  OE2 GLU A  50      12.376  -3.484   6.241  1.00 52.42           O  
ATOM    370  N   GLU A  51      16.938   0.313   5.029  1.00 35.90           N  
ATOM    371  CA  GLU A  51      18.229   0.713   4.506  1.00 36.02           C  
ATOM    372  C   GLU A  51      19.373   0.005   5.252  1.00 37.19           C  
ATOM    373  O   GLU A  51      20.442  -0.236   4.667  1.00 37.08           O  
ATOM    374  CB  GLU A  51      18.421   2.236   4.631  1.00 37.02           C  
ATOM    375  CG  GLU A  51      17.553   3.104   3.701  1.00 38.97           C  
ATOM    376  CD  GLU A  51      17.787   4.619   3.851  1.00 41.19           C  
ATOM    377  OE1 GLU A  51      18.390   5.074   4.853  1.00 36.35           O  
ATOM    378  OE2 GLU A  51      17.373   5.376   2.941  1.00 43.57           O  
ATOM    379  N   HIS A  52      19.191  -0.283   6.548  1.00 36.26           N  
ATOM    380  CA  HIS A  52      20.300  -0.861   7.316  1.00 35.99           C  
ATOM    381  C   HIS A  52      20.239  -2.385   7.422  1.00 36.72           C  
ATOM    382  O   HIS A  52      21.166  -2.989   7.923  1.00 37.23           O  
ATOM    383  CB  HIS A  52      20.442  -0.149   8.649  1.00 34.75           C  
ATOM    384  CG  HIS A  52      20.843   1.281   8.472  1.00 33.20           C  
ATOM    385  ND1 HIS A  52      19.944   2.268   8.130  1.00 31.93           N  
ATOM    386  CD2 HIS A  52      22.060   1.868   8.466  1.00 31.34           C  
ATOM    387  CE1 HIS A  52      20.592   3.408   7.962  1.00 31.43           C  
ATOM    388  NE2 HIS A  52      21.875   3.196   8.175  1.00 29.17           N  
ATOM    389  N   LYS A  53      19.157  -2.965   6.890  1.00 36.60           N  
ATOM    390  CA  LYS A  53      18.845  -4.381   6.933  1.00 37.47           C  
ATOM    391  C   LYS A  53      19.116  -5.028   8.303  1.00 37.59           C  
ATOM    392  O   LYS A  53      19.922  -5.983   8.431  1.00 36.83           O  
ATOM    393  CB  LYS A  53      19.492  -5.167   5.764  1.00 38.56           C  
ATOM    394  CG  LYS A  53      19.442  -4.496   4.359  1.00 41.61           C  
ATOM    395  CD  LYS A  53      18.174  -4.839   3.552  1.00 48.55           C  
ATOM    396  CE  LYS A  53      18.155  -4.086   2.186  1.00 52.79           C  
ATOM    397  NZ  LYS A  53      16.884  -3.280   1.942  1.00 53.88           N  
ATOM    398  N   VAL A  54      18.399  -4.504   9.308  1.00 36.86           N  
ATOM    399  CA  VAL A  54      18.512  -4.914  10.715  1.00 35.95           C  
ATOM    400  C   VAL A  54      17.163  -5.093  11.349  1.00 34.38           C  
ATOM    401  O   VAL A  54      16.194  -4.482  10.934  1.00 35.11           O  
ATOM    402  CB  VAL A  54      19.231  -3.872  11.585  1.00 36.36           C  
ATOM    403  CG1 VAL A  54      20.679  -4.179  11.657  1.00 37.06           C  
ATOM    404  CG2 VAL A  54      18.945  -2.427  11.098  1.00 36.44           C  
ATOM    405  N   GLU A  55      17.098  -5.944  12.361  1.00 33.28           N  
ATOM    406  CA  GLU A  55      15.856  -6.128  13.085  1.00 31.97           C  
ATOM    407  C   GLU A  55      16.067  -5.817  14.530  1.00 30.90           C  
ATOM    408  O   GLU A  55      17.132  -6.137  15.078  1.00 29.22           O  
ATOM    409  CB  GLU A  55      15.316  -7.542  12.879  1.00 32.66           C  
ATOM    410  CG  GLU A  55      15.116  -7.824  11.395  1.00 35.73           C  
ATOM    411  CD  GLU A  55      14.325  -9.074  11.152  1.00 42.44           C  
ATOM    412  OE1 GLU A  55      14.956 -10.121  10.810  1.00 41.79           O  
ATOM    413  OE2 GLU A  55      13.088  -9.001  11.334  1.00 43.98           O  
ATOM    414  N   VAL A  56      15.048  -5.176  15.130  1.00 29.57           N  
ATOM    415  CA  VAL A  56      15.081  -4.777  16.529  1.00 29.10           C  
ATOM    416  C   VAL A  56      13.723  -5.072  17.136  1.00 30.06           C  
ATOM    417  O   VAL A  56      12.739  -5.129  16.421  1.00 29.47           O  
ATOM    418  CB  VAL A  56      15.418  -3.246  16.715  1.00 29.98           C  
ATOM    419  CG1 VAL A  56      16.787  -2.891  16.193  1.00 28.33           C  
ATOM    420  CG2 VAL A  56      14.360  -2.329  16.080  1.00 26.38           C  
ATOM    421  N   LYS A  57      13.655  -5.279  18.450  1.00 30.16           N  
ATOM    422  CA  LYS A  57      12.336  -5.361  19.106  1.00 31.15           C  
ATOM    423  C   LYS A  57      12.110  -4.226  20.103  1.00 29.51           C  
ATOM    424  O   LYS A  57      11.019  -4.069  20.622  1.00 30.33           O  
ATOM    425  CB  LYS A  57      12.103  -6.713  19.792  1.00 32.20           C  
ATOM    426  CG  LYS A  57      12.975  -7.864  19.278  1.00 38.05           C  
ATOM    427  CD  LYS A  57      12.632  -9.194  19.971  1.00 46.54           C  
ATOM    428  CE  LYS A  57      12.520 -10.380  18.947  1.00 51.94           C  
ATOM    429  NZ  LYS A  57      12.009 -11.677  19.579  1.00 53.12           N  
ATOM    430  N   ASP A  58      13.138  -3.427  20.351  1.00 28.10           N  
ATOM    431  CA  ASP A  58      13.046  -2.351  21.324  1.00 26.67           C  
ATOM    432  C   ASP A  58      13.538  -1.049  20.774  1.00 24.92           C  
ATOM    433  O   ASP A  58      14.482  -1.024  19.965  1.00 23.44           O  
ATOM    434  CB  ASP A  58      13.913  -2.681  22.543  1.00 27.43           C  
ATOM    435  CG  ASP A  58      13.629  -4.047  23.096  1.00 28.98           C  
ATOM    436  OD1 ASP A  58      12.502  -4.266  23.529  1.00 30.63           O  
ATOM    437  OD2 ASP A  58      14.468  -4.974  23.114  1.00 37.27           O  
ATOM    438  N   GLY A  59      12.931   0.049  21.250  1.00 23.32           N  
ATOM    439  CA  GLY A  59      13.417   1.356  20.866  1.00 21.71           C  
ATOM    440  C   GLY A  59      13.274   2.434  21.906  1.00 21.32           C  
ATOM    441  O   GLY A  59      12.422   2.336  22.797  1.00 20.90           O  
ATOM    442  N   CYS A  60      14.117   3.461  21.797  1.00 19.59           N  
ATOM    443  CA  CYS A  60      13.968   4.633  22.632  1.00 20.28           C  
ATOM    444  C   CYS A  60      14.292   5.827  21.781  1.00 19.59           C  
ATOM    445  O   CYS A  60      15.400   5.908  21.289  1.00 19.58           O  
ATOM    446  CB  CYS A  60      14.979   4.619  23.806  1.00 21.40           C  
ATOM    447  SG  CYS A  60      14.786   6.093  24.842  1.00 23.10           S  
ATOM    448  N   ILE A  61      13.350   6.755  21.630  1.00 19.06           N  
ATOM    449  CA  ILE A  61      13.533   7.951  20.847  1.00 19.10           C  
ATOM    450  C   ILE A  61      13.458   9.203  21.718  1.00 20.53           C  
ATOM    451  O   ILE A  61      12.518   9.365  22.493  1.00 20.18           O  
ATOM    452  CB  ILE A  61      12.408   8.069  19.806  1.00 19.74           C  
ATOM    453  CG1 ILE A  61      12.184   6.765  19.017  1.00 19.72           C  
ATOM    454  CG2 ILE A  61      12.653   9.247  18.891  1.00 19.24           C  
ATOM    455  CD1 ILE A  61      13.379   6.239  18.257  1.00 22.09           C  
ATOM    456  N   ALA A  62      14.454  10.087  21.576  1.00 20.91           N  
ATOM    457  CA  ALA A  62      14.472  11.336  22.289  1.00 21.04           C  
ATOM    458  C   ALA A  62      13.832  12.387  21.384  1.00 21.92           C  
ATOM    459  O   ALA A  62      14.151  12.461  20.193  1.00 21.26           O  
ATOM    460  CB  ALA A  62      15.899  11.715  22.644  1.00 20.75           C  
ATOM    461  N   ILE A  63      12.931  13.196  21.945  1.00 23.15           N  
ATOM    462  CA  ILE A  63      12.132  14.131  21.147  1.00 25.65           C  
ATOM    463  C   ILE A  63      12.148  15.472  21.799  1.00 26.86           C  
ATOM    464  O   ILE A  63      11.973  15.559  23.014  1.00 28.25           O  
ATOM    465  CB  ILE A  63      10.683  13.680  21.109  1.00 26.60           C  
ATOM    466  CG1 ILE A  63      10.604  12.201  20.716  1.00 28.34           C  
ATOM    467  CG2 ILE A  63       9.882  14.557  20.124  1.00 28.25           C  
ATOM    468  CD1 ILE A  63      10.220  11.972  19.303  1.00 30.18           C  
ATOM    469  N   ALA A  64      12.293  16.521  21.022  1.00 28.06           N  
ATOM    470  CA  ALA A  64      12.403  17.832  21.624  1.00 31.82           C  
ATOM    471  C   ALA A  64      11.012  18.372  22.003  1.00 34.22           C  
ATOM    472  O   ALA A  64      10.552  19.380  21.459  1.00 34.86           O  
ATOM    473  CB  ALA A  64      13.214  18.812  20.730  1.00 30.07           C  
ATOM    474  N   CYS A  65      10.347  17.666  22.919  1.00 36.42           N  
ATOM    475  CA  CYS A  65       9.098  18.158  23.533  1.00 39.77           C  
ATOM    476  C   CYS A  65       8.892  17.595  24.956  1.00 40.28           C  
ATOM    477  O   CYS A  65       9.508  16.578  25.312  1.00 39.86           O  
ATOM    478  CB  CYS A  65       7.854  17.974  22.632  1.00 38.88           C  
ATOM    479  SG ACYS A  65       7.561  16.434  21.725  0.50 38.94           S  
ATOM    480  SG BCYS A  65       6.309  18.549  23.363  0.50 44.04           S  
ATOM    481  N   PRO A  66       8.082  18.235  25.800  1.00 41.05           N  
ATOM    482  CA  PRO A  66       7.726  17.540  27.057  1.00 41.63           C  
ATOM    483  C   PRO A  66       6.990  16.235  26.731  1.00 41.78           C  
ATOM    484  O   PRO A  66       6.155  16.153  25.797  1.00 41.24           O  
ATOM    485  CB  PRO A  66       6.843  18.540  27.841  1.00 42.04           C  
ATOM    486  CG  PRO A  66       7.023  19.934  27.148  1.00 41.50           C  
ATOM    487  CD  PRO A  66       7.502  19.595  25.708  1.00 42.09           C  
ATOM    488  N   ILE A  67       7.374  15.182  27.451  1.00 41.86           N  
ATOM    489  CA  ILE A  67       6.649  13.921  27.353  1.00 41.19           C  
ATOM    490  C   ILE A  67       5.788  13.853  28.611  1.00 41.47           C  
ATOM    491  O   ILE A  67       6.307  13.750  29.735  1.00 42.06           O  
ATOM    492  CB  ILE A  67       7.605  12.705  27.180  1.00 40.98           C  
ATOM    493  CG1 ILE A  67       8.676  12.979  26.077  1.00 38.68           C  
ATOM    494  CG2 ILE A  67       6.802  11.402  26.931  1.00 40.71           C  
ATOM    495  CD1 ILE A  67       8.142  13.251  24.665  1.00 31.82           C  
ATOM    496  N   THR A  68       4.471  13.988  28.428  1.00 40.73           N  
ATOM    497  CA  THR A  68       3.563  13.918  29.566  1.00 39.52           C  
ATOM    498  C   THR A  68       2.369  12.975  29.425  1.00 38.39           C  
ATOM    499  O   THR A  68       1.597  12.875  30.371  1.00 38.98           O  
ATOM    500  CB  THR A  68       3.068  15.325  29.955  1.00 39.70           C  
ATOM    501  OG1 THR A  68       2.381  15.901  28.843  1.00 40.53           O  
ATOM    502  CG2 THR A  68       4.274  16.311  30.250  1.00 39.97           C  
ATOM    503  N   GLY A  69       2.191  12.319  28.268  1.00 35.52           N  
ATOM    504  CA  GLY A  69       1.172  11.315  28.123  1.00 31.73           C  
ATOM    505  C   GLY A  69       1.466  10.319  27.016  1.00 30.96           C  
ATOM    506  O   GLY A  69       2.580  10.259  26.476  1.00 29.22           O  
ATOM    507  N   ASP A  70       0.449   9.520  26.668  1.00 28.97           N  
ATOM    508  CA  ASP A  70       0.517   8.724  25.476  1.00 26.71           C  
ATOM    509  C   ASP A  70       0.659   9.551  24.185  1.00 25.98           C  
ATOM    510  O   ASP A  70       1.278   9.105  23.224  1.00 24.27           O  
ATOM    511  CB  ASP A  70      -0.682   7.808  25.333  1.00 26.86           C  
ATOM    512  CG  ASP A  70      -0.547   6.934  24.118  1.00 26.41           C  
ATOM    513  OD1 ASP A  70      -1.267   7.188  23.124  1.00 28.80           O  
ATOM    514  OD2 ASP A  70       0.352   6.045  24.036  1.00 24.15           O  
ATOM    515  N   TRP A  71       0.066  10.740  24.158  1.00 25.81           N  
ATOM    516  CA  TRP A  71       0.139  11.573  22.972  1.00 25.41           C  
ATOM    517  C   TRP A  71       1.401  12.466  22.966  1.00 26.21           C  
ATOM    518  O   TRP A  71       1.604  13.216  23.883  1.00 26.37           O  
ATOM    519  CB  TRP A  71      -1.093  12.461  22.864  1.00 23.60           C  
ATOM    520  CG  TRP A  71      -1.142  13.065  21.453  1.00 21.97           C  
ATOM    521  CD1 TRP A  71      -0.817  14.361  21.069  1.00 16.19           C  
ATOM    522  CD2 TRP A  71      -1.463  12.358  20.253  1.00 17.61           C  
ATOM    523  NE1 TRP A  71      -0.974  14.496  19.701  1.00 18.53           N  
ATOM    524  CE2 TRP A  71      -1.366  13.287  19.173  1.00 19.88           C  
ATOM    525  CE3 TRP A  71      -1.861  11.036  19.977  1.00 18.36           C  
ATOM    526  CZ2 TRP A  71      -1.644  12.930  17.844  1.00 18.29           C  
ATOM    527  CZ3 TRP A  71      -2.130  10.668  18.638  1.00 20.18           C  
ATOM    528  CH2 TRP A  71      -2.013  11.623  17.591  1.00 19.32           C  
ATOM    529  N   VAL A  72       2.201  12.384  21.925  1.00 27.68           N  
ATOM    530  CA  VAL A  72       3.406  13.195  21.781  1.00 30.21           C  
ATOM    531  C   VAL A  72       3.153  14.336  20.809  1.00 31.62           C  
ATOM    532  O   VAL A  72       3.043  14.139  19.596  1.00 31.18           O  
ATOM    533  CB  VAL A  72       4.610  12.352  21.290  1.00 30.31           C  
ATOM    534  CG1 VAL A  72       5.825  13.211  21.105  1.00 29.75           C  
ATOM    535  CG2 VAL A  72       4.908  11.282  22.328  1.00 32.04           C  
ATOM    536  N   ALA A  73       3.054  15.525  21.383  1.00 34.17           N  
ATOM    537  CA  ALA A  73       2.591  16.702  20.684  1.00 37.66           C  
ATOM    538  C   ALA A  73       3.827  17.309  20.044  1.00 40.28           C  
ATOM    539  O   ALA A  73       4.523  18.182  20.590  1.00 40.54           O  
ATOM    540  CB  ALA A  73       1.901  17.682  21.674  1.00 37.25           C  
HETATM  541  N   MSE A  74       4.134  16.757  18.902  1.00 43.47           N  
HETATM  542  CA  MSE A  74       5.234  17.221  18.124  1.00 48.20           C  
HETATM  543  C   MSE A  74       4.917  18.530  17.451  1.00 50.10           C  
HETATM  544  O   MSE A  74       3.824  18.722  16.900  1.00 49.96           O  
HETATM  545  CB  MSE A  74       5.538  16.164  17.069  1.00 48.84           C  
HETATM  546  CG  MSE A  74       6.084  14.923  17.742  1.00 52.57           C  
HETATM  547 SE   MSE A  74       7.362  13.977  16.700  1.00 65.13          SE  
HETATM  548  CE  MSE A  74       8.695  15.631  16.159  1.00 55.84           C  
ATOM    549  N   THR A  75       5.863  19.448  17.507  1.00 52.69           N  
ATOM    550  CA  THR A  75       5.884  20.442  16.448  1.00 55.46           C  
ATOM    551  C   THR A  75       6.534  19.763  15.214  1.00 56.16           C  
ATOM    552  O   THR A  75       7.443  18.908  15.349  1.00 56.64           O  
ATOM    553  CB  THR A  75       6.481  21.790  16.894  1.00 56.13           C  
ATOM    554  OG1 THR A  75       6.337  22.740  15.818  1.00 59.81           O  
ATOM    555  CG2 THR A  75       8.025  21.705  17.216  1.00 57.39           C  
ATOM    556  N   ASN A  76       6.049  20.131  14.028  1.00 56.40           N  
ATOM    557  CA  ASN A  76       5.911  19.195  12.909  1.00 56.53           C  
ATOM    558  C   ASN A  76       4.633  18.476  13.314  1.00 56.09           C  
ATOM    559  O   ASN A  76       4.550  17.276  13.631  1.00 55.87           O  
ATOM    560  CB  ASN A  76       7.108  18.241  12.709  1.00 57.38           C  
ATOM    561  CG  ASN A  76       7.307  17.840  11.233  1.00 59.34           C  
ATOM    562  OD1 ASN A  76       8.431  17.497  10.795  1.00 59.48           O  
ATOM    563  ND2 ASN A  76       6.209  17.889  10.459  1.00 60.49           N  
ATOM    564  N   HIS A  77       3.608  19.287  13.330  1.00 55.13           N  
ATOM    565  CA  HIS A  77       2.413  18.911  13.995  1.00 53.37           C  
ATOM    566  C   HIS A  77       1.690  17.756  13.330  1.00 51.68           C  
ATOM    567  O   HIS A  77       0.944  17.010  13.985  1.00 51.74           O  
ATOM    568  CB  HIS A  77       1.523  20.123  14.089  1.00 54.77           C  
ATOM    569  CG  HIS A  77       0.182  19.772  14.565  1.00 55.86           C  
ATOM    570  ND1 HIS A  77      -0.802  19.344  13.705  1.00 56.98           N  
ATOM    571  CD2 HIS A  77      -0.298  19.626  15.817  1.00 58.70           C  
ATOM    572  CE1 HIS A  77      -1.867  19.017  14.409  1.00 60.80           C  
ATOM    573  NE2 HIS A  77      -1.591  19.187  15.693  1.00 62.44           N  
ATOM    574  N   THR A  78       1.888  17.599  12.026  1.00 49.16           N  
ATOM    575  CA  THR A  78       1.377  16.408  11.355  1.00 46.04           C  
ATOM    576  C   THR A  78       2.127  15.129  11.827  1.00 42.69           C  
ATOM    577  O   THR A  78       1.679  14.042  11.536  1.00 41.47           O  
ATOM    578  CB  THR A  78       1.402  16.577   9.798  1.00 47.20           C  
ATOM    579  OG1 THR A  78       0.860  15.395   9.178  1.00 49.79           O  
ATOM    580  CG2 THR A  78       2.851  16.621   9.279  1.00 44.80           C  
ATOM    581  N   TRP A  79       3.254  15.291  12.541  1.00 39.65           N  
ATOM    582  CA  TRP A  79       4.031  14.176  13.140  1.00 37.02           C  
ATOM    583  C   TRP A  79       3.596  13.713  14.544  1.00 34.88           C  
ATOM    584  O   TRP A  79       4.099  12.683  15.031  1.00 35.15           O  
ATOM    585  CB  TRP A  79       5.523  14.510  13.212  1.00 36.22           C  
ATOM    586  CG  TRP A  79       6.286  14.247  11.918  1.00 37.26           C  
ATOM    587  CD1 TRP A  79       5.850  14.495  10.619  1.00 37.82           C  
ATOM    588  CD2 TRP A  79       7.616  13.721  11.791  1.00 34.29           C  
ATOM    589  NE1 TRP A  79       6.828  14.137   9.722  1.00 37.59           N  
ATOM    590  CE2 TRP A  79       7.914  13.651  10.408  1.00 35.64           C  
ATOM    591  CE3 TRP A  79       8.583  13.288  12.703  1.00 34.04           C  
ATOM    592  CZ2 TRP A  79       9.125  13.160   9.930  1.00 34.48           C  
ATOM    593  CZ3 TRP A  79       9.792  12.794  12.218  1.00 34.11           C  
ATOM    594  CH2 TRP A  79      10.051  12.740  10.852  1.00 32.82           C  
ATOM    595  N   ALA A  80       2.714  14.477  15.189  1.00 31.19           N  
ATOM    596  CA  ALA A  80       2.218  14.146  16.531  1.00 29.21           C  
ATOM    597  C   ALA A  80       1.748  12.713  16.524  1.00 26.08           C  
ATOM    598  O   ALA A  80       1.168  12.288  15.567  1.00 26.43           O  
ATOM    599  CB  ALA A  80       1.090  15.111  16.956  1.00 27.85           C  
ATOM    600  N   PHE A  81       2.022  11.934  17.554  1.00 24.13           N  
ATOM    601  CA  PHE A  81       1.652  10.513  17.448  1.00 22.56           C  
ATOM    602  C   PHE A  81       1.345   9.937  18.834  1.00 22.53           C  
ATOM    603  O   PHE A  81       1.738  10.501  19.869  1.00 21.97           O  
ATOM    604  CB  PHE A  81       2.762   9.699  16.731  1.00 21.28           C  
ATOM    605  CG  PHE A  81       4.054   9.611  17.540  1.00 22.35           C  
ATOM    606  CD1 PHE A  81       4.295   8.513  18.388  1.00 23.28           C  
ATOM    607  CD2 PHE A  81       4.999  10.654  17.486  1.00 22.88           C  
ATOM    608  CE1 PHE A  81       5.435   8.464  19.210  1.00 20.62           C  
ATOM    609  CE2 PHE A  81       6.173  10.638  18.274  1.00 20.95           C  
ATOM    610  CZ  PHE A  81       6.384   9.513  19.172  1.00 21.63           C  
ATOM    611  N   SER A  82       0.686   8.786  18.831  1.00 21.88           N  
ATOM    612  CA  SER A  82       0.473   7.998  20.031  1.00 22.52           C  
ATOM    613  C   SER A  82       1.624   7.005  20.235  1.00 23.19           C  
ATOM    614  O   SER A  82       1.928   6.157  19.370  1.00 21.43           O  
ATOM    615  CB  SER A  82      -0.811   7.190  19.854  1.00 22.30           C  
ATOM    616  OG  SER A  82      -0.863   6.108  20.765  1.00 22.60           O  
ATOM    617  N   ILE A  83       2.238   7.077  21.400  1.00 23.89           N  
ATOM    618  CA  ILE A  83       3.248   6.087  21.730  1.00 23.13           C  
ATOM    619  C   ILE A  83       2.681   4.652  21.619  1.00 23.94           C  
ATOM    620  O   ILE A  83       3.310   3.793  21.016  1.00 24.50           O  
ATOM    621  CB  ILE A  83       3.798   6.326  23.147  1.00 22.64           C  
ATOM    622  CG1 ILE A  83       4.515   7.689  23.219  1.00 22.79           C  
ATOM    623  CG2 ILE A  83       4.707   5.110  23.553  1.00 21.55           C  
ATOM    624  CD1 ILE A  83       4.827   8.182  24.656  1.00 20.84           C  
ATOM    625  N   ALA A  84       1.547   4.359  22.247  1.00 24.21           N  
ATOM    626  CA  ALA A  84       1.022   2.991  22.137  1.00 26.72           C  
ATOM    627  C   ALA A  84       0.759   2.574  20.664  1.00 27.05           C  
ATOM    628  O   ALA A  84       1.093   1.442  20.308  1.00 27.76           O  
ATOM    629  CB  ALA A  84      -0.248   2.723  23.063  1.00 24.78           C  
ATOM    630  N   GLU A  85       0.189   3.485  19.861  1.00 28.35           N  
ATOM    631  CA  GLU A  85      -0.094   3.268  18.420  1.00 31.24           C  
ATOM    632  C   GLU A  85       1.189   2.847  17.728  1.00 31.56           C  
ATOM    633  O   GLU A  85       1.237   1.769  17.089  1.00 32.59           O  
ATOM    634  CB  GLU A  85      -0.717   4.551  17.736  1.00 31.93           C  
ATOM    635  CG  GLU A  85      -0.387   4.848  16.239  1.00 39.04           C  
ATOM    636  CD  GLU A  85       0.046   6.331  15.791  1.00 46.02           C  
ATOM    637  OE1 GLU A  85       0.826   6.391  14.793  1.00 47.76           O  
ATOM    638  OE2 GLU A  85      -0.408   7.448  16.295  1.00 41.30           O  
HETATM  639  N   MSE A  86       2.236   3.684  17.855  1.00 30.30           N  
HETATM  640  CA  MSE A  86       3.508   3.389  17.204  1.00 29.70           C  
HETATM  641  C   MSE A  86       4.155   2.075  17.667  1.00 28.99           C  
HETATM  642  O   MSE A  86       4.728   1.359  16.872  1.00 28.82           O  
HETATM  643  CB  MSE A  86       4.504   4.522  17.425  1.00 29.26           C  
HETATM  644  CG  MSE A  86       5.660   4.417  16.447  1.00 34.94           C  
HETATM  645 SE   MSE A  86       7.037   5.831  16.632  1.00 50.27          SE  
HETATM  646  CE  MSE A  86       6.437   6.843  15.453  1.00 36.38           C  
ATOM    647  N   LYS A  87       4.122   1.804  18.967  1.00 28.71           N  
ATOM    648  CA  LYS A  87       4.712   0.594  19.521  1.00 29.87           C  
ATOM    649  C   LYS A  87       4.050  -0.608  18.863  1.00 30.33           C  
ATOM    650  O   LYS A  87       4.723  -1.527  18.429  1.00 29.84           O  
ATOM    651  CB  LYS A  87       4.466   0.523  21.029  1.00 28.83           C  
ATOM    652  CG  LYS A  87       5.161  -0.660  21.685  1.00 29.95           C  
ATOM    653  CD  LYS A  87       4.684  -0.846  23.118  1.00 29.25           C  
ATOM    654  CE  LYS A  87       5.077  -2.208  23.646  1.00 32.65           C  
ATOM    655  NZ  LYS A  87       5.344  -2.238  25.137  1.00 32.56           N  
ATOM    656  N   LYS A  88       2.721  -0.566  18.789  1.00 31.54           N  
ATOM    657  CA  LYS A  88       1.967  -1.629  18.160  1.00 33.25           C  
ATOM    658  C   LYS A  88       2.232  -1.699  16.644  1.00 32.87           C  
ATOM    659  O   LYS A  88       2.536  -2.762  16.161  1.00 32.85           O  
ATOM    660  CB  LYS A  88       0.489  -1.537  18.489  1.00 33.08           C  
ATOM    661  CG  LYS A  88      -0.335  -2.448  17.634  1.00 37.88           C  
ATOM    662  CD  LYS A  88      -1.750  -2.585  18.203  1.00 44.04           C  
ATOM    663  CE  LYS A  88      -2.064  -4.069  18.442  1.00 47.98           C  
ATOM    664  NZ  LYS A  88      -2.984  -4.678  17.402  1.00 47.84           N  
ATOM    665  N   ASN A  89       2.159  -0.587  15.911  1.00 32.56           N  
ATOM    666  CA  ASN A  89       2.510  -0.613  14.473  1.00 32.39           C  
ATOM    667  C   ASN A  89       3.878  -1.240  14.135  1.00 32.99           C  
ATOM    668  O   ASN A  89       3.993  -1.975  13.155  1.00 33.51           O  
ATOM    669  CB  ASN A  89       2.463   0.792  13.861  1.00 31.92           C  
ATOM    670  CG  ASN A  89       1.053   1.330  13.745  1.00 30.47           C  
ATOM    671  OD1 ASN A  89       0.081   0.623  14.027  1.00 29.83           O  
ATOM    672  ND2 ASN A  89       0.938   2.595  13.355  1.00 25.41           N  
ATOM    673  N   LEU A  90       4.920  -0.898  14.897  1.00 32.65           N  
ATOM    674  CA  LEU A  90       6.245  -1.514  14.749  1.00 33.14           C  
ATOM    675  C   LEU A  90       6.065  -2.775  15.573  1.00 34.00           C  
ATOM    676  O   LEU A  90       5.050  -2.949  16.254  1.00 36.30           O  
ATOM    677  CB  LEU A  90       7.323  -0.628  15.387  1.00 32.68           C  
ATOM    678  CG  LEU A  90       7.977   0.606  14.745  1.00 33.69           C  
ATOM    679  CD1 LEU A  90       7.428   0.990  13.415  1.00 35.99           C  
ATOM    680  CD2 LEU A  90       7.942   1.838  15.675  1.00 32.05           C  
ATOM    681  N   GLY A  91       6.939  -3.725  15.595  1.00 33.52           N  
ATOM    682  CA  GLY A  91       6.406  -4.806  16.437  1.00 34.11           C  
ATOM    683  C   GLY A  91       7.086  -4.846  17.769  1.00 33.93           C  
ATOM    684  O   GLY A  91       7.565  -5.886  18.158  1.00 35.44           O  
ATOM    685  N   PHE A  92       7.167  -3.708  18.447  1.00 33.46           N  
ATOM    686  CA  PHE A  92       8.166  -3.532  19.496  1.00 32.04           C  
ATOM    687  C   PHE A  92       7.692  -4.113  20.793  1.00 31.45           C  
ATOM    688  O   PHE A  92       6.527  -3.969  21.123  1.00 31.87           O  
ATOM    689  CB  PHE A  92       8.512  -2.035  19.695  1.00 30.59           C  
ATOM    690  CG  PHE A  92       9.527  -1.510  18.722  1.00 30.95           C  
ATOM    691  CD1 PHE A  92       9.848  -2.234  17.549  1.00 30.14           C  
ATOM    692  CD2 PHE A  92      10.187  -0.301  18.970  1.00 29.01           C  
ATOM    693  CE1 PHE A  92      10.781  -1.736  16.629  1.00 31.52           C  
ATOM    694  CE2 PHE A  92      11.127   0.200  18.065  1.00 29.82           C  
ATOM    695  CZ  PHE A  92      11.430  -0.517  16.887  1.00 31.14           C  
ATOM    696  N   SER A  93       8.598  -4.708  21.559  1.00 30.60           N  
ATOM    697  CA  SER A  93       8.257  -5.119  22.923  1.00 30.41           C  
ATOM    698  C   SER A  93       8.385  -3.938  23.864  1.00 29.19           C  
ATOM    699  O   SER A  93       7.648  -3.849  24.819  1.00 28.30           O  
ATOM    700  CB  SER A  93       9.175  -6.266  23.399  1.00 32.06           C  
ATOM    701  OG  SER A  93       9.450  -7.189  22.338  1.00 35.58           O  
ATOM    702  N   HIS A  94       9.332  -3.026  23.606  1.00 28.62           N  
ATOM    703  CA  HIS A  94       9.444  -1.801  24.408  1.00 27.34           C  
ATOM    704  C   HIS A  94       9.657  -0.603  23.510  1.00 26.40           C  
ATOM    705  O   HIS A  94      10.540  -0.632  22.646  1.00 25.60           O  
ATOM    706  CB  HIS A  94      10.635  -1.854  25.370  1.00 28.22           C  
ATOM    707  CG  HIS A  94      10.630  -3.032  26.275  1.00 31.23           C  
ATOM    708  ND1 HIS A  94      10.160  -2.970  27.578  1.00 36.36           N  
ATOM    709  CD2 HIS A  94      11.000  -4.314  26.065  1.00 30.18           C  
ATOM    710  CE1 HIS A  94      10.274  -4.163  28.138  1.00 33.78           C  
ATOM    711  NE2 HIS A  94      10.774  -4.996  27.241  1.00 31.79           N  
ATOM    712  N   LEU A  95       8.880   0.460  23.739  1.00 24.36           N  
ATOM    713  CA  LEU A  95       9.101   1.712  23.046  1.00 23.58           C  
ATOM    714  C   LEU A  95       9.097   2.770  24.131  1.00 23.24           C  
ATOM    715  O   LEU A  95       8.017   3.120  24.688  1.00 22.64           O  
ATOM    716  CB  LEU A  95       7.971   2.028  22.055  1.00 23.12           C  
ATOM    717  CG  LEU A  95       8.121   2.857  20.750  1.00 24.88           C  
ATOM    718  CD1 LEU A  95       6.987   3.849  20.456  1.00 17.42           C  
ATOM    719  CD2 LEU A  95       9.524   3.418  20.486  1.00 21.71           C  
ATOM    720  N   GLU A  96      10.286   3.260  24.442  1.00 21.07           N  
ATOM    721  CA  GLU A  96      10.438   4.381  25.340  1.00 22.16           C  
ATOM    722  C   GLU A  96      10.525   5.672  24.527  1.00 22.95           C  
ATOM    723  O   GLU A  96      11.279   5.760  23.522  1.00 24.28           O  
ATOM    724  CB  GLU A  96      11.721   4.234  26.180  1.00 20.44           C  
ATOM    725  CG  GLU A  96      11.634   3.142  27.235  1.00 24.27           C  
ATOM    726  CD  GLU A  96      10.554   3.455  28.271  1.00 28.16           C  
ATOM    727  OE1 GLU A  96       9.650   2.597  28.412  1.00 32.42           O  
ATOM    728  OE2 GLU A  96      10.594   4.567  28.914  1.00 27.05           O  
ATOM    729  N  AILE A  97       9.774   6.689  24.910  0.40 22.96           N  
ATOM    730  N  BILE A  97       9.773   6.675  24.956  0.60 22.37           N  
ATOM    731  CA AILE A  97      10.037   7.992  24.298  0.40 23.00           C  
ATOM    732  CA BILE A  97       9.912   8.005  24.361  0.60 21.97           C  
ATOM    733  C  AILE A  97      10.218   9.068  25.354  0.40 22.97           C  
ATOM    734  C  BILE A  97      10.235   9.041  25.428  0.60 22.47           C  
ATOM    735  O  AILE A  97       9.373   9.261  26.231  0.40 22.61           O  
ATOM    736  O  BILE A  97       9.486   9.189  26.392  0.60 22.02           O  
ATOM    737  CB AILE A  97       9.008   8.383  23.195  0.40 22.99           C  
ATOM    738  CB BILE A  97       8.650   8.417  23.583  0.60 21.41           C  
ATOM    739  CG1AILE A  97       8.510   9.810  23.418  0.40 22.08           C  
ATOM    740  CG1BILE A  97       8.248   7.317  22.581  0.60 20.57           C  
ATOM    741  CG2AILE A  97       7.885   7.364  23.108  0.40 23.42           C  
ATOM    742  CG2BILE A  97       8.893   9.752  22.886  0.60 18.56           C  
ATOM    743  CD1AILE A  97       8.160  10.555  22.180  0.40 21.32           C  
ATOM    744  CD1BILE A  97       8.991   7.313  21.258  0.60 14.94           C  
ATOM    745  N   ILE A  98      11.355   9.749  25.256  1.00 22.67           N  
ATOM    746  CA  ILE A  98      11.802  10.661  26.296  1.00 22.32           C  
ATOM    747  C   ILE A  98      12.120  12.015  25.726  1.00 21.71           C  
ATOM    748  O   ILE A  98      12.364  12.155  24.543  1.00 21.41           O  
ATOM    749  CB  ILE A  98      13.043  10.081  27.032  1.00 23.14           C  
ATOM    750  CG1 ILE A  98      14.256   9.942  26.080  1.00 19.14           C  
ATOM    751  CG2 ILE A  98      12.711   8.771  27.683  1.00 23.68           C  
ATOM    752  CD1 ILE A  98      15.431   9.318  26.747  1.00 19.12           C  
ATOM    753  N   ASN A  99      12.090  13.012  26.593  1.00 22.48           N  
ATOM    754  CA  ASN A  99      12.425  14.354  26.245  1.00 22.46           C  
ATOM    755  C   ASN A  99      13.915  14.397  25.873  1.00 22.82           C  
ATOM    756  O   ASN A  99      14.744  13.641  26.412  1.00 21.69           O  
ATOM    757  CB  ASN A  99      12.125  15.247  27.438  1.00 22.77           C  
ATOM    758  CG  ASN A  99      12.674  16.634  27.244  1.00 25.93           C  
ATOM    759  OD1 ASN A  99      12.070  17.455  26.522  1.00 26.90           O  
ATOM    760  ND2 ASN A  99      13.859  16.890  27.800  1.00 20.33           N  
ATOM    761  N   ASP A 100      14.247  15.252  24.922  1.00 23.23           N  
ATOM    762  CA  ASP A 100      15.606  15.293  24.388  1.00 24.39           C  
ATOM    763  C   ASP A 100      16.664  15.714  25.449  1.00 24.63           C  
ATOM    764  O   ASP A 100      17.763  15.173  25.499  1.00 24.57           O  
ATOM    765  CB  ASP A 100      15.665  16.208  23.190  1.00 23.84           C  
ATOM    766  CG  ASP A 100      15.399  17.639  23.544  1.00 26.51           C  
ATOM    767  OD1 ASP A 100      14.465  17.971  24.314  1.00 30.89           O  
ATOM    768  OD2 ASP A 100      16.074  18.551  23.082  1.00 34.88           O  
ATOM    769  N   PHE A 101      16.304  16.655  26.313  1.00 25.49           N  
ATOM    770  CA  PHE A 101      17.252  17.133  27.289  1.00 25.08           C  
ATOM    771  C   PHE A 101      17.446  16.099  28.378  1.00 24.35           C  
ATOM    772  O   PHE A 101      18.541  15.891  28.835  1.00 25.43           O  
ATOM    773  CB  PHE A 101      16.884  18.505  27.838  1.00 24.41           C  
ATOM    774  CG  PHE A 101      18.020  19.137  28.592  1.00 27.02           C  
ATOM    775  CD1 PHE A 101      18.133  18.981  29.968  1.00 23.85           C  
ATOM    776  CD2 PHE A 101      19.056  19.787  27.903  1.00 25.92           C  
ATOM    777  CE1 PHE A 101      19.232  19.547  30.668  1.00 23.05           C  
ATOM    778  CE2 PHE A 101      20.143  20.342  28.620  1.00 25.57           C  
ATOM    779  CZ  PHE A 101      20.219  20.201  29.996  1.00 21.43           C  
ATOM    780  N   THR A 102      16.385  15.409  28.765  1.00 24.88           N  
ATOM    781  CA  THR A 102      16.495  14.172  29.565  1.00 24.13           C  
ATOM    782  C   THR A 102      17.452  13.135  28.969  1.00 23.94           C  
ATOM    783  O   THR A 102      18.243  12.521  29.706  1.00 24.90           O  
ATOM    784  CB  THR A 102      15.091  13.537  29.734  1.00 23.93           C  
ATOM    785  OG1 THR A 102      14.240  14.483  30.386  1.00 24.61           O  
ATOM    786  CG2 THR A 102      15.129  12.305  30.712  1.00 23.54           C  
ATOM    787  N   ALA A 103      17.325  12.874  27.663  1.00 22.38           N  
ATOM    788  CA  ALA A 103      18.228  11.941  27.028  1.00 22.84           C  
ATOM    789  C   ALA A 103      19.702  12.409  27.160  1.00 22.69           C  
ATOM    790  O   ALA A 103      20.566  11.604  27.438  1.00 21.23           O  
ATOM    791  CB  ALA A 103      17.872  11.721  25.575  1.00 21.57           C  
ATOM    792  N   VAL A 104      19.968  13.696  26.919  1.00 22.90           N  
ATOM    793  CA  VAL A 104      21.314  14.216  27.092  1.00 24.05           C  
ATOM    794  C   VAL A 104      21.836  13.919  28.522  1.00 24.15           C  
ATOM    795  O   VAL A 104      23.005  13.563  28.673  1.00 23.51           O  
ATOM    796  CB  VAL A 104      21.444  15.726  26.721  1.00 24.87           C  
ATOM    797  CG1 VAL A 104      22.874  16.250  27.052  1.00 24.55           C  
ATOM    798  CG2 VAL A 104      21.159  15.974  25.153  1.00 25.48           C  
ATOM    799  N   SER A 105      20.959  14.026  29.539  1.00 23.77           N  
ATOM    800  CA  SER A 105      21.339  13.845  30.947  1.00 23.23           C  
ATOM    801  C   SER A 105      21.664  12.388  31.175  1.00 24.47           C  
ATOM    802  O   SER A 105      22.606  12.070  31.930  1.00 24.74           O  
ATOM    803  CB  SER A 105      20.203  14.263  31.901  1.00 22.60           C  
ATOM    804  OG  SER A 105      19.221  13.222  32.010  1.00 19.46           O  
HETATM  805  N   MSE A 106      20.879  11.499  30.545  1.00 23.71           N  
HETATM  806  CA  MSE A 106      21.122  10.047  30.636  1.00 23.69           C  
HETATM  807  C   MSE A 106      22.433   9.578  29.910  1.00 24.01           C  
HETATM  808  O   MSE A 106      22.944   8.485  30.191  1.00 22.78           O  
HETATM  809  CB  MSE A 106      19.885   9.256  30.131  1.00 23.53           C  
HETATM  810  CG  MSE A 106      18.680   9.372  31.048  1.00 26.46           C  
HETATM  811 SE   MSE A 106      19.127   8.649  32.821  1.00 42.87          SE  
HETATM  812  CE  MSE A 106      19.906   6.860  32.328  1.00 36.28           C  
ATOM    813  N   ALA A 107      22.973  10.402  29.001  1.00 23.72           N  
ATOM    814  CA  ALA A 107      24.275  10.105  28.386  1.00 25.67           C  
ATOM    815  C   ALA A 107      25.427  10.126  29.409  1.00 27.22           C  
ATOM    816  O   ALA A 107      26.428   9.392  29.265  1.00 25.60           O  
ATOM    817  CB  ALA A 107      24.579  11.053  27.266  1.00 24.89           C  
ATOM    818  N   ILE A 108      25.260  10.946  30.443  1.00 27.87           N  
ATOM    819  CA  ILE A 108      26.388  11.289  31.299  1.00 29.18           C  
ATOM    820  C   ILE A 108      27.141  10.087  31.882  1.00 30.29           C  
ATOM    821  O   ILE A 108      28.375  10.078  31.827  1.00 30.91           O  
ATOM    822  CB  ILE A 108      25.978  12.326  32.352  1.00 28.58           C  
ATOM    823  CG1 ILE A 108      25.820  13.679  31.666  1.00 26.83           C  
ATOM    824  CG2 ILE A 108      26.936  12.340  33.527  1.00 29.25           C  
ATOM    825  CD1 ILE A 108      25.143  14.731  32.549  1.00 30.25           C  
ATOM    826  N   PRO A 109      26.453   9.067  32.399  1.00 31.09           N  
ATOM    827  CA  PRO A 109      27.174   7.882  32.879  1.00 31.71           C  
ATOM    828  C   PRO A 109      27.860   7.102  31.762  1.00 32.88           C  
ATOM    829  O   PRO A 109      28.651   6.223  32.044  1.00 34.26           O  
ATOM    830  CB  PRO A 109      26.080   7.044  33.562  1.00 31.32           C  
ATOM    831  CG  PRO A 109      24.989   8.068  33.825  1.00 32.71           C  
ATOM    832  CD  PRO A 109      25.006   8.975  32.643  1.00 30.18           C  
HETATM  833  N   MSE A 110      27.595   7.414  30.508  1.00 32.38           N  
HETATM  834  CA  MSE A 110      28.277   6.696  29.447  1.00 33.15           C  
HETATM  835  C   MSE A 110      29.482   7.492  28.924  1.00 33.51           C  
HETATM  836  O   MSE A 110      30.231   7.038  28.075  1.00 33.64           O  
HETATM  837  CB  MSE A 110      27.288   6.422  28.299  1.00 33.18           C  
HETATM  838  CG  MSE A 110      26.121   5.550  28.658  1.00 33.32           C  
HETATM  839 SE   MSE A 110      26.690   3.805  29.305  1.00 43.49          SE  
HETATM  840  CE  MSE A 110      27.618   3.139  27.530  1.00 36.79           C  
ATOM    841  N   LEU A 111      29.671   8.694  29.432  1.00 35.09           N  
ATOM    842  CA  LEU A 111      30.606   9.612  28.784  1.00 36.74           C  
ATOM    843  C   LEU A 111      32.019   9.321  29.232  1.00 37.89           C  
ATOM    844  O   LEU A 111      32.244   9.102  30.417  1.00 38.73           O  
ATOM    845  CB  LEU A 111      30.241  11.066  29.092  1.00 35.49           C  
ATOM    846  CG  LEU A 111      29.011  11.595  28.359  1.00 34.37           C  
ATOM    847  CD1 LEU A 111      28.789  13.034  28.747  1.00 27.56           C  
ATOM    848  CD2 LEU A 111      29.175  11.437  26.839  1.00 29.14           C  
ATOM    849  N   LYS A 112      32.941   9.326  28.278  1.00 39.15           N  
ATOM    850  CA  LYS A 112      34.368   9.133  28.534  1.00 41.07           C  
ATOM    851  C   LYS A 112      35.101  10.480  28.654  1.00 41.47           C  
ATOM    852  O   LYS A 112      34.609  11.540  28.172  1.00 40.21           O  
ATOM    853  CB  LYS A 112      35.006   8.269  27.422  1.00 41.34           C  
ATOM    854  CG  LYS A 112      34.548   6.755  27.440  1.00 43.64           C  
ATOM    855  CD  LYS A 112      35.419   5.874  26.490  1.00 50.34           C  
ATOM    856  CE  LYS A 112      34.620   4.710  25.828  1.00 51.63           C  
ATOM    857  NZ  LYS A 112      34.503   4.844  24.318  1.00 49.11           N  
ATOM    858  N   LYS A 113      36.296  10.429  29.258  1.00 41.53           N  
ATOM    859  CA  LYS A 113      37.037  11.660  29.563  1.00 41.40           C  
ATOM    860  C   LYS A 113      37.268  12.468  28.314  1.00 39.84           C  
ATOM    861  O   LYS A 113      37.178  13.679  28.356  1.00 38.84           O  
ATOM    862  CB  LYS A 113      38.326  11.413  30.384  1.00 42.61           C  
ATOM    863  CG  LYS A 113      38.095  10.814  31.811  1.00 45.66           C  
ATOM    864  CD  LYS A 113      36.943  11.505  32.644  1.00 54.59           C  
ATOM    865  CE  LYS A 113      37.192  11.491  34.196  1.00 57.69           C  
ATOM    866  NZ  LYS A 113      35.895  11.588  34.996  1.00 61.57           N  
ATOM    867  N   GLU A 114      37.449  11.799  27.184  1.00 39.09           N  
ATOM    868  CA  GLU A 114      37.527  12.506  25.911  1.00 38.44           C  
ATOM    869  C   GLU A 114      36.233  13.175  25.424  1.00 37.13           C  
ATOM    870  O   GLU A 114      36.255  13.930  24.453  1.00 36.86           O  
ATOM    871  CB  GLU A 114      38.124  11.598  24.813  1.00 40.36           C  
ATOM    872  CG  GLU A 114      37.219  10.495  24.254  1.00 42.41           C  
ATOM    873  CD  GLU A 114      37.593   9.162  24.839  1.00 43.18           C  
ATOM    874  OE1 GLU A 114      38.147   9.198  25.969  1.00 46.22           O  
ATOM    875  OE2 GLU A 114      37.353   8.108  24.194  1.00 43.01           O  
ATOM    876  N   HIS A 115      35.108  12.920  26.093  1.00 35.88           N  
ATOM    877  CA  HIS A 115      33.855  13.583  25.708  1.00 34.66           C  
ATOM    878  C   HIS A 115      33.574  14.813  26.544  1.00 33.77           C  
ATOM    879  O   HIS A 115      32.553  15.458  26.359  1.00 32.79           O  
ATOM    880  CB  HIS A 115      32.679  12.631  25.868  1.00 34.72           C  
ATOM    881  CG  HIS A 115      32.823  11.366  25.088  1.00 34.39           C  
ATOM    882  ND1 HIS A 115      33.232  11.349  23.767  1.00 33.53           N  
ATOM    883  CD2 HIS A 115      32.601  10.076  25.437  1.00 34.48           C  
ATOM    884  CE1 HIS A 115      33.249  10.096  23.338  1.00 36.37           C  
ATOM    885  NE2 HIS A 115      32.872   9.304  24.330  1.00 36.02           N  
ATOM    886  N   LEU A 116      34.492  15.113  27.466  1.00 32.06           N  
ATOM    887  CA  LEU A 116      34.238  16.049  28.538  1.00 31.03           C  
ATOM    888  C   LEU A 116      35.346  17.101  28.587  1.00 29.91           C  
ATOM    889  O   LEU A 116      36.475  16.752  28.501  1.00 29.27           O  
ATOM    890  CB  LEU A 116      34.225  15.235  29.838  1.00 31.76           C  
ATOM    891  CG  LEU A 116      32.944  14.803  30.579  1.00 31.04           C  
ATOM    892  CD1 LEU A 116      31.696  14.786  29.728  1.00 24.44           C  
ATOM    893  CD2 LEU A 116      33.184  13.469  31.313  1.00 28.46           C  
ATOM    894  N   ILE A 117      35.039  18.398  28.666  1.00 29.37           N  
ATOM    895  CA  ILE A 117      36.106  19.377  28.930  1.00 27.76           C  
ATOM    896  C   ILE A 117      35.913  19.916  30.335  1.00 27.37           C  
ATOM    897  O   ILE A 117      34.897  20.533  30.619  1.00 27.80           O  
ATOM    898  CB  ILE A 117      36.077  20.513  27.895  1.00 28.57           C  
ATOM    899  CG1 ILE A 117      36.313  19.932  26.491  1.00 29.95           C  
ATOM    900  CG2 ILE A 117      37.139  21.609  28.258  1.00 24.92           C  
ATOM    901  CD1 ILE A 117      36.162  20.975  25.360  1.00 31.40           C  
ATOM    902  N   GLN A 118      36.844  19.632  31.236  1.00 26.26           N  
ATOM    903  CA  GLN A 118      36.673  20.021  32.637  1.00 24.43           C  
ATOM    904  C   GLN A 118      36.862  21.490  32.892  1.00 24.05           C  
ATOM    905  O   GLN A 118      37.720  22.121  32.303  1.00 23.05           O  
ATOM    906  CB  GLN A 118      37.630  19.249  33.559  1.00 24.75           C  
ATOM    907  CG  GLN A 118      37.317  19.458  35.037  1.00 24.29           C  
ATOM    908  CD  GLN A 118      38.010  18.457  35.916  1.00 26.35           C  
ATOM    909  OE1 GLN A 118      38.704  17.579  35.415  1.00 27.40           O  
ATOM    910  NE2 GLN A 118      37.817  18.572  37.227  1.00 26.07           N  
ATOM    911  N   PHE A 119      36.069  22.037  33.806  1.00 23.63           N  
ATOM    912  CA  PHE A 119      36.269  23.420  34.212  1.00 23.62           C  
ATOM    913  C   PHE A 119      36.348  23.519  35.740  1.00 23.72           C  
ATOM    914  O   PHE A 119      35.349  23.885  36.402  1.00 23.33           O  
ATOM    915  CB  PHE A 119      35.128  24.286  33.649  1.00 23.81           C  
ATOM    916  CG  PHE A 119      35.260  24.567  32.175  1.00 24.39           C  
ATOM    917  CD1 PHE A 119      34.786  23.654  31.223  1.00 27.33           C  
ATOM    918  CD2 PHE A 119      35.855  25.724  31.740  1.00 23.52           C  
ATOM    919  CE1 PHE A 119      34.877  23.901  29.847  1.00 25.81           C  
ATOM    920  CE2 PHE A 119      35.971  25.987  30.373  1.00 27.10           C  
ATOM    921  CZ  PHE A 119      35.470  25.065  29.426  1.00 28.62           C  
ATOM    922  N   GLY A 120      37.514  23.162  36.302  1.00 23.60           N  
ATOM    923  CA  GLY A 120      37.757  23.253  37.745  1.00 22.38           C  
ATOM    924  C   GLY A 120      37.211  22.074  38.527  1.00 22.80           C  
ATOM    925  O   GLY A 120      36.617  21.170  37.940  1.00 21.77           O  
ATOM    926  N   GLY A 121      37.410  22.091  39.852  1.00 22.77           N  
ATOM    927  CA  GLY A 121      36.983  21.026  40.744  1.00 25.36           C  
ATOM    928  C   GLY A 121      37.882  19.786  40.774  1.00 26.97           C  
ATOM    929  O   GLY A 121      38.780  19.614  39.952  1.00 26.54           O  
ATOM    930  N   ALA A 122      37.619  18.891  41.720  1.00 29.20           N  
ATOM    931  CA  ALA A 122      38.327  17.600  41.773  1.00 30.32           C  
ATOM    932  C   ALA A 122      37.525  16.521  41.058  1.00 32.31           C  
ATOM    933  O   ALA A 122      36.597  16.791  40.308  1.00 33.54           O  
ATOM    934  CB  ALA A 122      38.603  17.166  43.225  1.00 29.46           C  
ATOM    935  N   GLU A 123      37.892  15.277  41.311  1.00 33.59           N  
ATOM    936  CA  GLU A 123      37.205  14.158  40.716  1.00 34.25           C  
ATOM    937  C   GLU A 123      35.811  14.039  41.331  1.00 32.62           C  
ATOM    938  O   GLU A 123      35.620  14.378  42.515  1.00 31.64           O  
ATOM    939  CB  GLU A 123      38.046  12.877  40.887  1.00 34.52           C  
ATOM    940  CG  GLU A 123      39.373  12.974  40.103  1.00 37.79           C  
ATOM    941  CD  GLU A 123      39.178  13.027  38.569  1.00 41.66           C  
ATOM    942  OE1 GLU A 123      38.314  12.296  38.045  1.00 42.82           O  
ATOM    943  OE2 GLU A 123      39.901  13.773  37.866  1.00 42.32           O  
ATOM    944  N   PRO A 124      34.841  13.600  40.519  1.00 31.63           N  
ATOM    945  CA  PRO A 124      33.469  13.360  41.009  1.00 31.30           C  
ATOM    946  C   PRO A 124      33.437  12.354  42.152  1.00 31.84           C  
ATOM    947  O   PRO A 124      34.274  11.440  42.147  1.00 31.78           O  
ATOM    948  CB  PRO A 124      32.720  12.771  39.798  1.00 31.08           C  
ATOM    949  CG  PRO A 124      33.605  12.818  38.600  1.00 30.20           C  
ATOM    950  CD  PRO A 124      34.986  13.344  39.070  1.00 31.59           C  
ATOM    951  N   VAL A 125      32.519  12.523  43.118  1.00 31.41           N  
ATOM    952  CA  VAL A 125      32.253  11.461  44.063  1.00 31.90           C  
ATOM    953  C   VAL A 125      31.261  10.510  43.367  1.00 32.96           C  
ATOM    954  O   VAL A 125      30.165  10.908  42.951  1.00 32.58           O  
ATOM    955  CB  VAL A 125      31.700  11.981  45.415  1.00 32.71           C  
ATOM    956  CG1 VAL A 125      31.620  10.848  46.430  1.00 31.51           C  
ATOM    957  CG2 VAL A 125      32.581  13.169  45.961  1.00 32.86           C  
ATOM    958  N   GLU A 126      31.660   9.258  43.229  1.00 33.60           N  
ATOM    959  CA  GLU A 126      30.859   8.281  42.510  1.00 34.75           C  
ATOM    960  C   GLU A 126      29.500   8.020  43.173  1.00 32.91           C  
ATOM    961  O   GLU A 126      29.385   7.816  44.374  1.00 31.93           O  
ATOM    962  CB  GLU A 126      31.641   6.964  42.292  1.00 35.80           C  
ATOM    963  CG  GLU A 126      32.858   7.095  41.357  1.00 42.21           C  
ATOM    964  CD  GLU A 126      32.499   7.251  39.855  1.00 52.04           C  
ATOM    965  OE1 GLU A 126      31.562   6.542  39.349  1.00 52.55           O  
ATOM    966  OE2 GLU A 126      33.157   8.102  39.165  1.00 53.34           O  
ATOM    967  N   GLY A 127      28.469   8.054  42.339  1.00 31.89           N  
ATOM    968  CA  GLY A 127      27.108   7.799  42.771  1.00 30.06           C  
ATOM    969  C   GLY A 127      26.434   8.938  43.496  1.00 28.26           C  
ATOM    970  O   GLY A 127      25.304   8.763  43.943  1.00 27.63           O  
ATOM    971  N   LYS A 128      27.102  10.083  43.623  1.00 26.36           N  
ATOM    972  CA  LYS A 128      26.465  11.259  44.220  1.00 26.06           C  
ATOM    973  C   LYS A 128      25.695  12.056  43.139  1.00 24.51           C  
ATOM    974  O   LYS A 128      25.911  11.853  41.956  1.00 24.74           O  
ATOM    975  CB  LYS A 128      27.513  12.116  44.924  1.00 27.72           C  
ATOM    976  CG  LYS A 128      27.570  11.882  46.452  1.00 30.07           C  
ATOM    977  CD  LYS A 128      28.166  10.540  46.768  1.00 36.89           C  
ATOM    978  CE  LYS A 128      27.862  10.072  48.203  1.00 41.53           C  
ATOM    979  NZ  LYS A 128      28.387   8.653  48.293  1.00 44.30           N  
ATOM    980  N   PRO A 129      24.770  12.911  43.518  1.00 22.92           N  
ATOM    981  CA  PRO A 129      23.906  13.552  42.518  1.00 22.18           C  
ATOM    982  C   PRO A 129      24.642  14.368  41.474  1.00 21.84           C  
ATOM    983  O   PRO A 129      25.757  14.862  41.733  1.00 22.92           O  
ATOM    984  CB  PRO A 129      22.963  14.433  43.380  1.00 21.99           C  
ATOM    985  CG  PRO A 129      22.990  13.739  44.759  1.00 21.43           C  
ATOM    986  CD  PRO A 129      24.370  13.240  44.904  1.00 21.94           C  
ATOM    987  N   ILE A 130      23.999  14.547  40.336  1.00 20.60           N  
ATOM    988  CA  ILE A 130      24.538  15.274  39.213  1.00 21.82           C  
ATOM    989  C   ILE A 130      23.505  16.303  38.752  1.00 22.34           C  
ATOM    990  O   ILE A 130      22.316  16.031  38.720  1.00 22.17           O  
ATOM    991  CB  ILE A 130      24.808  14.321  38.050  1.00 22.15           C  
ATOM    992  CG1 ILE A 130      25.925  13.332  38.379  1.00 23.01           C  
ATOM    993  CG2 ILE A 130      25.103  15.071  36.733  1.00 22.77           C  
ATOM    994  CD1 ILE A 130      25.883  12.098  37.376  1.00 24.74           C  
ATOM    995  N   ALA A 131      23.976  17.487  38.392  1.00 22.27           N  
ATOM    996  CA  ALA A 131      23.150  18.487  37.743  1.00 22.56           C  
ATOM    997  C   ALA A 131      23.700  18.642  36.361  1.00 23.10           C  
ATOM    998  O   ALA A 131      24.904  18.496  36.167  1.00 23.60           O  
ATOM    999  CB  ALA A 131      23.285  19.811  38.478  1.00 23.03           C  
ATOM   1000  N   VAL A 132      22.819  18.970  35.412  1.00 22.88           N  
ATOM   1001  CA  VAL A 132      23.130  19.167  34.041  1.00 22.20           C  
ATOM   1002  C   VAL A 132      22.328  20.370  33.643  1.00 21.96           C  
ATOM   1003  O   VAL A 132      21.161  20.446  34.018  1.00 24.44           O  
ATOM   1004  CB  VAL A 132      22.557  17.989  33.198  1.00 24.02           C  
ATOM   1005  CG1 VAL A 132      23.100  17.996  31.723  1.00 22.72           C  
ATOM   1006  CG2 VAL A 132      22.783  16.656  33.882  1.00 25.87           C  
ATOM   1007  N   TYR A 133      22.884  21.283  32.848  1.00 21.24           N  
ATOM   1008  CA  TYR A 133      22.122  22.405  32.293  1.00 21.14           C  
ATOM   1009  C   TYR A 133      22.687  22.816  30.964  1.00 21.83           C  
ATOM   1010  O   TYR A 133      23.789  22.462  30.644  1.00 22.53           O  
ATOM   1011  CB  TYR A 133      22.047  23.632  33.233  1.00 20.75           C  
ATOM   1012  CG  TYR A 133      23.355  24.297  33.629  1.00 20.31           C  
ATOM   1013  CD1 TYR A 133      23.562  25.653  33.347  1.00 23.09           C  
ATOM   1014  CD2 TYR A 133      24.343  23.611  34.355  1.00 19.79           C  
ATOM   1015  CE1 TYR A 133      24.757  26.313  33.733  1.00 23.02           C  
ATOM   1016  CE2 TYR A 133      25.539  24.259  34.764  1.00 19.14           C  
ATOM   1017  CZ  TYR A 133      25.727  25.603  34.449  1.00 21.17           C  
ATOM   1018  OH  TYR A 133      26.850  26.277  34.836  1.00 18.86           O  
ATOM   1019  N   GLY A 134      21.936  23.544  30.164  1.00 22.50           N  
ATOM   1020  CA  GLY A 134      22.399  23.760  28.811  1.00 23.95           C  
ATOM   1021  C   GLY A 134      21.701  24.938  28.232  1.00 26.00           C  
ATOM   1022  O   GLY A 134      20.477  25.000  28.282  1.00 26.95           O  
ATOM   1023  N   ALA A 135      22.479  25.887  27.715  1.00 27.05           N  
ATOM   1024  CA  ALA A 135      21.945  27.073  27.065  1.00 27.70           C  
ATOM   1025  C   ALA A 135      21.953  26.887  25.551  1.00 29.03           C  
ATOM   1026  O   ALA A 135      23.012  26.875  24.938  1.00 30.52           O  
ATOM   1027  CB  ALA A 135      22.764  28.246  27.435  1.00 26.99           C  
ATOM   1028  N   GLY A 136      20.777  26.699  24.965  1.00 29.09           N  
ATOM   1029  CA  GLY A 136      20.613  26.628  23.530  1.00 29.50           C  
ATOM   1030  C   GLY A 136      19.556  27.652  23.119  1.00 30.39           C  
ATOM   1031  O   GLY A 136      19.675  28.873  23.441  1.00 31.41           O  
ATOM   1032  N   THR A 137      18.546  27.187  22.408  1.00 28.93           N  
ATOM   1033  CA  THR A 137      17.397  28.023  22.114  1.00 30.56           C  
ATOM   1034  C   THR A 137      16.735  28.429  23.410  1.00 30.40           C  
ATOM   1035  O   THR A 137      16.312  29.554  23.538  1.00 31.79           O  
ATOM   1036  CB  THR A 137      16.371  27.332  21.143  1.00 31.32           C  
ATOM   1037  OG1 THR A 137      16.958  27.206  19.832  1.00 30.33           O  
ATOM   1038  CG2 THR A 137      15.191  28.317  20.850  1.00 35.32           C  
ATOM   1039  N   GLY A 138      16.669  27.518  24.378  1.00 29.80           N  
ATOM   1040  CA  GLY A 138      16.260  27.867  25.728  1.00 28.80           C  
ATOM   1041  C   GLY A 138      17.307  27.371  26.733  1.00 27.76           C  
ATOM   1042  O   GLY A 138      18.404  27.032  26.372  1.00 27.67           O  
ATOM   1043  N   LEU A 139      16.944  27.325  27.993  1.00 27.40           N  
ATOM   1044  CA  LEU A 139      17.808  26.844  29.050  1.00 27.00           C  
ATOM   1045  C   LEU A 139      17.237  25.553  29.626  1.00 25.82           C  
ATOM   1046  O   LEU A 139      16.200  25.587  30.277  1.00 27.03           O  
ATOM   1047  CB  LEU A 139      17.871  27.879  30.173  1.00 26.59           C  
ATOM   1048  CG  LEU A 139      18.715  27.559  31.430  1.00 26.73           C  
ATOM   1049  CD1 LEU A 139      20.174  27.201  31.047  1.00 22.32           C  
ATOM   1050  CD2 LEU A 139      18.660  28.846  32.370  1.00 22.10           C  
ATOM   1051  N   GLY A 140      17.902  24.434  29.423  1.00 23.77           N  
ATOM   1052  CA  GLY A 140      17.427  23.197  30.009  1.00 22.39           C  
ATOM   1053  C   GLY A 140      18.161  22.933  31.306  1.00 21.84           C  
ATOM   1054  O   GLY A 140      19.324  23.287  31.397  1.00 21.35           O  
ATOM   1055  N   VAL A 141      17.502  22.314  32.284  1.00 20.73           N  
ATOM   1056  CA  VAL A 141      18.133  21.890  33.509  1.00 20.50           C  
ATOM   1057  C   VAL A 141      17.612  20.502  33.911  1.00 21.00           C  
ATOM   1058  O   VAL A 141      16.410  20.272  33.875  1.00 22.01           O  
ATOM   1059  CB  VAL A 141      17.774  22.820  34.659  1.00 19.88           C  
ATOM   1060  CG1 VAL A 141      18.194  22.234  35.938  1.00 17.08           C  
ATOM   1061  CG2 VAL A 141      18.368  24.254  34.464  1.00 23.44           C  
ATOM   1062  N   ALA A 142      18.472  19.587  34.368  1.00 19.86           N  
ATOM   1063  CA  ALA A 142      17.961  18.286  34.827  1.00 18.79           C  
ATOM   1064  C   ALA A 142      18.900  17.829  35.937  1.00 19.59           C  
ATOM   1065  O   ALA A 142      20.042  18.344  36.025  1.00 19.90           O  
ATOM   1066  CB  ALA A 142      18.010  17.281  33.681  1.00 19.02           C  
ATOM   1067  N   HIS A 143      18.477  16.870  36.750  1.00 19.00           N  
ATOM   1068  CA  HIS A 143      19.400  16.254  37.705  1.00 21.43           C  
ATOM   1069  C   HIS A 143      19.397  14.753  37.561  1.00 22.04           C  
ATOM   1070  O   HIS A 143      18.419  14.198  36.993  1.00 23.72           O  
ATOM   1071  CB  HIS A 143      19.105  16.669  39.149  1.00 20.31           C  
ATOM   1072  CG  HIS A 143      19.125  18.148  39.354  1.00 23.55           C  
ATOM   1073  ND1 HIS A 143      18.151  18.984  38.834  1.00 22.20           N  
ATOM   1074  CD2 HIS A 143      20.001  18.947  40.020  1.00 22.78           C  
ATOM   1075  CE1 HIS A 143      18.429  20.234  39.176  1.00 22.89           C  
ATOM   1076  NE2 HIS A 143      19.538  20.239  39.902  1.00 24.18           N  
ATOM   1077  N   LEU A 144      20.457  14.102  38.060  1.00 21.22           N  
ATOM   1078  CA  LEU A 144      20.518  12.634  38.140  1.00 22.67           C  
ATOM   1079  C   LEU A 144      20.937  12.184  39.521  1.00 23.36           C  
ATOM   1080  O   LEU A 144      21.804  12.785  40.134  1.00 22.70           O  
ATOM   1081  CB  LEU A 144      21.504  11.998  37.132  1.00 22.15           C  
ATOM   1082  CG  LEU A 144      21.479  12.118  35.606  1.00 26.19           C  
ATOM   1083  CD1 LEU A 144      22.826  11.546  34.949  1.00 25.38           C  
ATOM   1084  CD2 LEU A 144      20.313  11.302  35.008  1.00 28.02           C  
ATOM   1085  N   VAL A 145      20.288  11.135  40.020  1.00 24.46           N  
ATOM   1086  CA  VAL A 145      20.637  10.531  41.290  1.00 26.47           C  
ATOM   1087  C   VAL A 145      20.805   9.039  41.081  1.00 28.04           C  
ATOM   1088  O   VAL A 145      20.182   8.448  40.204  1.00 28.52           O  
ATOM   1089  CB  VAL A 145      19.591  10.790  42.350  1.00 26.33           C  
ATOM   1090  CG1 VAL A 145      19.526  12.300  42.646  1.00 26.62           C  
ATOM   1091  CG2 VAL A 145      18.197  10.238  41.888  1.00 26.00           C  
ATOM   1092  N   HIS A 146      21.666   8.440  41.879  1.00 29.26           N  
ATOM   1093  CA  HIS A 146      21.992   7.061  41.689  1.00 31.52           C  
ATOM   1094  C   HIS A 146      21.306   6.277  42.781  1.00 32.53           C  
ATOM   1095  O   HIS A 146      21.651   6.423  43.924  1.00 31.82           O  
ATOM   1096  CB  HIS A 146      23.506   6.847  41.790  1.00 31.30           C  
ATOM   1097  CG  HIS A 146      23.955   5.488  41.354  1.00 33.09           C  
ATOM   1098  ND1 HIS A 146      24.406   4.534  42.239  1.00 35.50           N  
ATOM   1099  CD2 HIS A 146      24.049   4.928  40.120  1.00 35.82           C  
ATOM   1100  CE1 HIS A 146      24.767   3.447  41.574  1.00 35.20           C  
ATOM   1101  NE2 HIS A 146      24.571   3.664  40.284  1.00 35.80           N  
ATOM   1102  N   VAL A 147      20.356   5.422  42.410  1.00 33.64           N  
ATOM   1103  CA  VAL A 147      19.615   4.646  43.395  1.00 35.26           C  
ATOM   1104  C   VAL A 147      19.551   3.228  42.941  1.00 36.09           C  
ATOM   1105  O   VAL A 147      19.140   2.954  41.816  1.00 36.63           O  
ATOM   1106  CB  VAL A 147      18.190   5.130  43.549  1.00 35.12           C  
ATOM   1107  CG1 VAL A 147      17.463   4.255  44.571  1.00 34.87           C  
ATOM   1108  CG2 VAL A 147      18.187   6.636  43.959  1.00 36.32           C  
ATOM   1109  N   ASP A 148      20.010   2.328  43.802  1.00 38.00           N  
ATOM   1110  CA  ASP A 148      19.931   0.906  43.512  1.00 39.70           C  
ATOM   1111  C   ASP A 148      20.578   0.482  42.206  1.00 38.27           C  
ATOM   1112  O   ASP A 148      19.980  -0.264  41.441  1.00 36.57           O  
ATOM   1113  CB  ASP A 148      18.471   0.506  43.466  1.00 41.29           C  
ATOM   1114  CG  ASP A 148      18.143  -0.467  44.526  1.00 47.56           C  
ATOM   1115  OD1 ASP A 148      18.505  -1.659  44.308  1.00 51.75           O  
ATOM   1116  OD2 ASP A 148      17.559  -0.117  45.603  1.00 53.09           O  
ATOM   1117  N   LYS A 149      21.794   0.967  41.975  1.00 38.35           N  
ATOM   1118  CA  LYS A 149      22.539   0.735  40.726  1.00 39.03           C  
ATOM   1119  C   LYS A 149      21.864   1.253  39.451  1.00 38.02           C  
ATOM   1120  O   LYS A 149      22.214   0.806  38.342  1.00 38.18           O  
ATOM   1121  CB  LYS A 149      22.889  -0.745  40.567  1.00 39.43           C  
ATOM   1122  CG  LYS A 149      24.333  -1.035  41.045  1.00 45.00           C  
ATOM   1123  CD  LYS A 149      24.320  -1.852  42.317  1.00 48.52           C  
ATOM   1124  CE  LYS A 149      23.584  -3.148  42.081  1.00 51.42           C  
ATOM   1125  NZ  LYS A 149      23.852  -4.088  43.207  1.00 53.76           N  
ATOM   1126  N   ARG A 150      20.902   2.173  39.600  1.00 36.28           N  
ATOM   1127  CA  ARG A 150      20.242   2.774  38.445  1.00 35.29           C  
ATOM   1128  C   ARG A 150      20.424   4.265  38.514  1.00 32.81           C  
ATOM   1129  O   ARG A 150      20.238   4.857  39.590  1.00 31.06           O  
ATOM   1130  CB  ARG A 150      18.744   2.526  38.485  1.00 35.93           C  
ATOM   1131  CG  ARG A 150      18.221   1.305  37.765  1.00 41.92           C  
ATOM   1132  CD  ARG A 150      16.652   1.221  37.816  1.00 49.59           C  
ATOM   1133  NE  ARG A 150      15.972   2.478  37.425  1.00 51.62           N  
ATOM   1134  CZ  ARG A 150      14.975   3.072  38.102  1.00 52.84           C  
ATOM   1135  NH1 ARG A 150      14.510   2.547  39.238  1.00 52.25           N  
ATOM   1136  NH2 ARG A 150      14.429   4.196  37.627  1.00 52.25           N  
ATOM   1137  N   TRP A 151      20.731   4.874  37.368  1.00 30.77           N  
ATOM   1138  CA  TRP A 151      20.669   6.322  37.288  1.00 30.81           C  
ATOM   1139  C   TRP A 151      19.252   6.777  36.977  1.00 30.34           C  
ATOM   1140  O   TRP A 151      18.684   6.394  35.972  1.00 28.79           O  
ATOM   1141  CB  TRP A 151      21.654   6.893  36.284  1.00 29.86           C  
ATOM   1142  CG  TRP A 151      23.047   6.841  36.777  1.00 30.65           C  
ATOM   1143  CD1 TRP A 151      24.012   5.880  36.485  1.00 30.58           C  
ATOM   1144  CD2 TRP A 151      23.653   7.759  37.686  1.00 29.00           C  
ATOM   1145  NE1 TRP A 151      25.179   6.181  37.150  1.00 29.63           N  
ATOM   1146  CE2 TRP A 151      24.993   7.322  37.894  1.00 28.11           C  
ATOM   1147  CE3 TRP A 151      23.194   8.918  38.369  1.00 27.12           C  
ATOM   1148  CZ2 TRP A 151      25.891   8.013  38.728  1.00 29.55           C  
ATOM   1149  CZ3 TRP A 151      24.084   9.599  39.222  1.00 29.65           C  
ATOM   1150  CH2 TRP A 151      25.419   9.144  39.390  1.00 30.05           C  
ATOM   1151  N   VAL A 152      18.722   7.617  37.857  1.00 29.57           N  
ATOM   1152  CA  VAL A 152      17.366   8.094  37.737  1.00 29.46           C  
ATOM   1153  C   VAL A 152      17.400   9.562  37.369  1.00 29.92           C  
ATOM   1154  O   VAL A 152      18.116  10.362  37.996  1.00 28.58           O  
ATOM   1155  CB  VAL A 152      16.594   7.949  39.064  1.00 29.96           C  
ATOM   1156  CG1 VAL A 152      15.143   8.462  38.871  1.00 31.40           C  
ATOM   1157  CG2 VAL A 152      16.635   6.500  39.567  1.00 28.24           C  
ATOM   1158  N   SER A 153      16.645   9.924  36.337  1.00 29.71           N  
ATOM   1159  CA  SER A 153      16.640  11.301  35.916  1.00 30.44           C  
ATOM   1160  C   SER A 153      15.476  12.020  36.549  1.00 28.83           C  
ATOM   1161  O   SER A 153      14.373  11.463  36.619  1.00 29.52           O  
ATOM   1162  CB  SER A 153      16.528  11.403  34.416  1.00 31.65           C  
ATOM   1163  OG  SER A 153      15.152  11.581  34.043  1.00 35.80           O  
ATOM   1164  N   LEU A 154      15.740  13.261  36.960  1.00 26.80           N  
ATOM   1165  CA  LEU A 154      14.765  14.143  37.601  1.00 25.90           C  
ATOM   1166  C   LEU A 154      14.615  15.362  36.751  1.00 25.57           C  
ATOM   1167  O   LEU A 154      15.417  16.297  36.862  1.00 24.82           O  
ATOM   1168  CB  LEU A 154      15.171  14.576  39.036  1.00 24.36           C  
ATOM   1169  CG  LEU A 154      15.764  13.471  39.926  1.00 23.87           C  
ATOM   1170  CD1 LEU A 154      16.292  14.053  41.237  1.00 21.77           C  
ATOM   1171  CD2 LEU A 154      14.702  12.399  40.182  1.00 22.67           C  
ATOM   1172  N   PRO A 155      13.582  15.355  35.902  1.00 25.89           N  
ATOM   1173  CA  PRO A 155      13.297  16.473  35.008  1.00 24.76           C  
ATOM   1174  C   PRO A 155      12.713  17.659  35.768  1.00 24.59           C  
ATOM   1175  O   PRO A 155      12.301  17.516  36.912  1.00 23.66           O  
ATOM   1176  CB  PRO A 155      12.241  15.887  34.080  1.00 25.38           C  
ATOM   1177  CG  PRO A 155      11.526  14.898  34.936  1.00 25.86           C  
ATOM   1178  CD  PRO A 155      12.628  14.234  35.712  1.00 26.40           C  
ATOM   1179  N   GLY A 156      12.701  18.819  35.118  1.00 23.80           N  
ATOM   1180  CA  GLY A 156      11.961  19.955  35.599  1.00 23.62           C  
ATOM   1181  C   GLY A 156      12.148  21.114  34.638  1.00 23.83           C  
ATOM   1182  O   GLY A 156      12.656  20.942  33.511  1.00 23.66           O  
ATOM   1183  N   GLU A 157      11.750  22.284  35.114  1.00 24.44           N  
ATOM   1184  CA  GLU A 157      11.772  23.518  34.331  1.00 26.27           C  
ATOM   1185  C   GLU A 157      12.644  24.567  35.045  1.00 25.49           C  
ATOM   1186  O   GLU A 157      12.360  25.763  35.066  1.00 24.82           O  
ATOM   1187  CB  GLU A 157      10.337  24.004  33.983  1.00 25.99           C  
ATOM   1188  CG  GLU A 157       9.546  23.076  33.044  1.00 28.20           C  
ATOM   1189  CD  GLU A 157       9.987  23.117  31.574  1.00 32.04           C  
ATOM   1190  OE1 GLU A 157      10.831  23.953  31.153  1.00 35.69           O  
ATOM   1191  OE2 GLU A 157       9.511  22.271  30.804  1.00 36.77           O  
ATOM   1192  N   GLY A 158      13.782  24.093  35.562  1.00 26.39           N  
ATOM   1193  CA  GLY A 158      14.682  24.924  36.366  1.00 25.53           C  
ATOM   1194  C   GLY A 158      15.386  26.017  35.585  1.00 25.20           C  
ATOM   1195  O   GLY A 158      16.013  26.908  36.179  1.00 25.25           O  
ATOM   1196  N   GLY A 159      15.247  25.977  34.263  1.00 25.02           N  
ATOM   1197  CA  GLY A 159      15.662  27.069  33.411  1.00 25.23           C  
ATOM   1198  C   GLY A 159      14.799  28.296  33.598  1.00 25.91           C  
ATOM   1199  O   GLY A 159      15.218  29.430  33.286  1.00 25.74           O  
ATOM   1200  N   HIS A 160      13.586  28.078  34.105  1.00 24.82           N  
ATOM   1201  CA  HIS A 160      12.618  29.176  34.236  1.00 25.36           C  
ATOM   1202  C   HIS A 160      12.538  29.860  35.608  1.00 25.06           C  
ATOM   1203  O   HIS A 160      11.706  30.731  35.820  1.00 25.37           O  
ATOM   1204  CB  HIS A 160      11.246  28.709  33.710  1.00 25.38           C  
ATOM   1205  CG  HIS A 160      11.337  28.201  32.317  1.00 27.10           C  
ATOM   1206  ND1 HIS A 160      11.536  29.044  31.241  1.00 27.35           N  
ATOM   1207  CD2 HIS A 160      11.411  26.941  31.832  1.00 28.89           C  
ATOM   1208  CE1 HIS A 160      11.675  28.323  30.142  1.00 26.40           C  
ATOM   1209  NE2 HIS A 160      11.615  27.044  30.479  1.00 31.34           N  
ATOM   1210  N   VAL A 161      13.436  29.514  36.527  1.00 25.06           N  
ATOM   1211  CA  VAL A 161      13.549  30.216  37.810  1.00 23.86           C  
ATOM   1212  C   VAL A 161      13.957  31.670  37.605  1.00 24.43           C  
ATOM   1213  O   VAL A 161      14.430  32.022  36.490  1.00 23.35           O  
ATOM   1214  CB  VAL A 161      14.568  29.521  38.715  1.00 24.84           C  
ATOM   1215  CG1 VAL A 161      14.182  28.021  38.871  1.00 23.67           C  
ATOM   1216  CG2 VAL A 161      16.015  29.713  38.171  1.00 22.38           C  
ATOM   1217  N   ASP A 162      13.766  32.528  38.644  1.00 24.80           N  
ATOM   1218  CA  ASP A 162      14.197  33.934  38.552  1.00 25.06           C  
ATOM   1219  C   ASP A 162      15.681  34.107  38.168  1.00 25.88           C  
ATOM   1220  O   ASP A 162      16.566  33.408  38.697  1.00 25.70           O  
ATOM   1221  CB  ASP A 162      13.934  34.671  39.848  1.00 24.94           C  
ATOM   1222  CG  ASP A 162      12.540  34.381  40.429  1.00 28.30           C  
ATOM   1223  OD1 ASP A 162      11.577  34.280  39.624  1.00 29.77           O  
ATOM   1224  OD2 ASP A 162      12.312  34.262  41.675  1.00 27.54           O  
ATOM   1225  N   PHE A 163      15.960  35.024  37.252  1.00 26.26           N  
ATOM   1226  CA  PHE A 163      17.330  35.469  37.045  1.00 27.66           C  
ATOM   1227  C   PHE A 163      17.831  36.108  38.356  1.00 28.14           C  
ATOM   1228  O   PHE A 163      17.156  36.963  38.955  1.00 28.83           O  
ATOM   1229  CB  PHE A 163      17.345  36.514  35.927  1.00 28.57           C  
ATOM   1230  CG  PHE A 163      18.618  37.246  35.805  1.00 27.68           C  
ATOM   1231  CD1 PHE A 163      19.846  36.574  35.940  1.00 27.19           C  
ATOM   1232  CD2 PHE A 163      18.614  38.611  35.519  1.00 26.03           C  
ATOM   1233  CE1 PHE A 163      21.044  37.249  35.848  1.00 23.57           C  
ATOM   1234  CE2 PHE A 163      19.815  39.313  35.412  1.00 26.78           C  
ATOM   1235  CZ  PHE A 163      21.047  38.614  35.566  1.00 26.34           C  
ATOM   1236  N   ALA A 164      18.990  35.647  38.829  1.00 28.06           N  
ATOM   1237  CA  ALA A 164      19.640  36.206  40.010  1.00 26.90           C  
ATOM   1238  C   ALA A 164      20.812  37.160  39.710  1.00 26.53           C  
ATOM   1239  O   ALA A 164      21.958  36.747  39.736  1.00 25.24           O  
ATOM   1240  CB  ALA A 164      20.086  35.099  40.890  1.00 26.65           C  
ATOM   1241  N   PRO A 165      20.553  38.455  39.537  1.00 27.42           N  
ATOM   1242  CA  PRO A 165      21.653  39.403  39.259  1.00 27.51           C  
ATOM   1243  C   PRO A 165      22.546  39.540  40.493  1.00 27.91           C  
ATOM   1244  O   PRO A 165      22.037  39.366  41.592  1.00 26.30           O  
ATOM   1245  CB  PRO A 165      20.943  40.717  39.033  1.00 26.89           C  
ATOM   1246  CG  PRO A 165      19.609  40.575  39.825  1.00 27.23           C  
ATOM   1247  CD  PRO A 165      19.246  39.130  39.735  1.00 27.49           C  
ATOM   1248  N   ASN A 166      23.839  39.816  40.321  1.00 29.55           N  
ATOM   1249  CA  ASN A 166      24.736  39.971  41.478  1.00 31.63           C  
ATOM   1250  C   ASN A 166      25.522  41.285  41.485  1.00 33.19           C  
ATOM   1251  O   ASN A 166      26.488  41.374  42.270  1.00 34.83           O  
ATOM   1252  CB  ASN A 166      25.778  38.837  41.521  1.00 31.60           C  
ATOM   1253  CG  ASN A 166      26.891  39.058  40.493  1.00 34.97           C  
ATOM   1254  OD1 ASN A 166      26.729  39.880  39.596  1.00 39.35           O  
ATOM   1255  ND2 ASN A 166      28.016  38.346  40.620  1.00 37.89           N  
ATOM   1256  N   SER A 167      25.194  42.239  40.593  1.00 34.00           N  
ATOM   1257  CA  SER A 167      25.808  43.590  40.561  1.00 35.88           C  
ATOM   1258  C   SER A 167      24.783  44.677  40.182  1.00 37.19           C  
ATOM   1259  O   SER A 167      23.680  44.371  39.688  1.00 38.93           O  
ATOM   1260  CB  SER A 167      26.969  43.636  39.561  1.00 35.77           C  
ATOM   1261  OG  SER A 167      26.476  43.522  38.216  1.00 36.59           O  
ATOM   1262  N   GLU A 168      25.135  45.943  40.378  1.00 37.60           N  
ATOM   1263  CA  GLU A 168      24.244  47.035  39.946  1.00 38.50           C  
ATOM   1264  C   GLU A 168      24.010  47.028  38.425  1.00 36.98           C  
ATOM   1265  O   GLU A 168      22.884  47.252  37.965  1.00 37.28           O  
ATOM   1266  CB  GLU A 168      24.751  48.427  40.404  1.00 38.30           C  
ATOM   1267  CG  GLU A 168      24.894  48.544  41.914  1.00 41.85           C  
ATOM   1268  CD  GLU A 168      25.160  49.968  42.394  1.00 45.93           C  
ATOM   1269  OE1 GLU A 168      26.262  50.517  42.128  1.00 47.40           O  
ATOM   1270  OE2 GLU A 168      24.272  50.532  43.068  1.00 46.79           O  
ATOM   1271  N   GLU A 169      25.078  46.800  37.664  1.00 35.70           N  
ATOM   1272  CA  GLU A 169      24.977  46.659  36.176  1.00 35.08           C  
ATOM   1273  C   GLU A 169      23.966  45.550  35.792  1.00 33.27           C  
ATOM   1274  O   GLU A 169      23.068  45.771  34.984  1.00 32.41           O  
ATOM   1275  CB  GLU A 169      26.353  46.380  35.540  1.00 34.18           C  
ATOM   1276  CG  GLU A 169      26.288  46.193  34.031  1.00 36.27           C  
ATOM   1277  CD  GLU A 169      27.557  45.614  33.426  1.00 39.26           C  
ATOM   1278  OE1 GLU A 169      27.759  45.744  32.191  1.00 35.34           O  
ATOM   1279  OE2 GLU A 169      28.359  45.004  34.185  1.00 43.06           O  
ATOM   1280  N   GLU A 170      24.125  44.385  36.411  1.00 31.98           N  
ATOM   1281  CA  GLU A 170      23.181  43.269  36.240  1.00 32.40           C  
ATOM   1282  C   GLU A 170      21.740  43.515  36.741  1.00 32.42           C  
ATOM   1283  O   GLU A 170      20.818  43.000  36.138  1.00 32.33           O  
ATOM   1284  CB  GLU A 170      23.718  41.981  36.830  1.00 30.62           C  
ATOM   1285  CG  GLU A 170      24.698  41.303  35.920  1.00 31.32           C  
ATOM   1286  CD  GLU A 170      25.173  39.970  36.482  1.00 34.69           C  
ATOM   1287  OE1 GLU A 170      24.388  39.192  37.103  1.00 37.85           O  
ATOM   1288  OE2 GLU A 170      26.359  39.696  36.311  1.00 34.17           O  
ATOM   1289  N   ALA A 171      21.572  44.291  37.812  1.00 32.11           N  
ATOM   1290  CA  ALA A 171      20.249  44.659  38.324  1.00 31.92           C  
ATOM   1291  C   ALA A 171      19.551  45.644  37.368  1.00 32.58           C  
ATOM   1292  O   ALA A 171      18.322  45.529  37.110  1.00 34.22           O  
ATOM   1293  CB  ALA A 171      20.373  45.254  39.715  1.00 31.41           C  
ATOM   1294  N   ILE A 172      20.322  46.585  36.820  1.00 31.38           N  
ATOM   1295  CA  ILE A 172      19.856  47.437  35.723  1.00 31.28           C  
ATOM   1296  C   ILE A 172      19.368  46.629  34.511  1.00 31.44           C  
ATOM   1297  O   ILE A 172      18.299  46.921  33.966  1.00 33.94           O  
ATOM   1298  CB  ILE A 172      20.963  48.491  35.343  1.00 31.85           C  
ATOM   1299  CG1 ILE A 172      21.082  49.551  36.457  1.00 32.53           C  
ATOM   1300  CG2 ILE A 172      20.651  49.206  34.030  1.00 30.43           C  
ATOM   1301  CD1 ILE A 172      22.405  50.359  36.429  1.00 35.88           C  
ATOM   1302  N   ILE A 173      20.108  45.593  34.111  1.00 30.48           N  
ATOM   1303  CA  ILE A 173      19.700  44.720  33.015  1.00 29.10           C  
ATOM   1304  C   ILE A 173      18.420  43.986  33.397  1.00 29.13           C  
ATOM   1305  O   ILE A 173      17.496  43.868  32.582  1.00 29.24           O  
ATOM   1306  CB  ILE A 173      20.849  43.726  32.614  1.00 28.62           C  
ATOM   1307  CG1 ILE A 173      21.982  44.493  31.889  1.00 28.95           C  
ATOM   1308  CG2 ILE A 173      20.282  42.550  31.762  1.00 27.58           C  
ATOM   1309  CD1 ILE A 173      23.319  43.741  31.690  1.00 22.52           C  
ATOM   1310  N   LEU A 174      18.375  43.490  34.630  1.00 28.89           N  
ATOM   1311  CA  LEU A 174      17.156  42.919  35.222  1.00 29.88           C  
ATOM   1312  C   LEU A 174      15.913  43.815  35.024  1.00 30.69           C  
ATOM   1313  O   LEU A 174      14.920  43.389  34.450  1.00 30.49           O  
ATOM   1314  CB  LEU A 174      17.360  42.702  36.714  1.00 29.51           C  
ATOM   1315  CG  LEU A 174      16.509  41.631  37.454  1.00 31.34           C  
ATOM   1316  CD1 LEU A 174      16.333  41.920  38.962  1.00 25.53           C  
ATOM   1317  CD2 LEU A 174      15.200  41.320  36.842  1.00 26.12           C  
ATOM   1318  N   GLU A 175      15.993  45.057  35.503  1.00 32.64           N  
ATOM   1319  CA  GLU A 175      14.878  45.993  35.407  1.00 34.64           C  
ATOM   1320  C   GLU A 175      14.508  46.401  33.951  1.00 34.59           C  
ATOM   1321  O   GLU A 175      13.322  46.474  33.612  1.00 34.65           O  
ATOM   1322  CB  GLU A 175      15.127  47.191  36.303  1.00 35.09           C  
ATOM   1323  CG  GLU A 175      14.411  47.064  37.670  1.00 40.12           C  
ATOM   1324  CD  GLU A 175      14.832  45.848  38.541  1.00 42.23           C  
ATOM   1325  OE1 GLU A 175      13.918  44.979  38.780  1.00 34.33           O  
ATOM   1326  OE2 GLU A 175      16.057  45.786  38.976  1.00 39.76           O  
ATOM   1327  N   ILE A 176      15.506  46.588  33.091  1.00 34.41           N  
ATOM   1328  CA  ILE A 176      15.231  46.886  31.700  1.00 33.89           C  
ATOM   1329  C   ILE A 176      14.412  45.767  31.084  1.00 35.03           C  
ATOM   1330  O   ILE A 176      13.369  46.020  30.427  1.00 34.39           O  
ATOM   1331  CB  ILE A 176      16.519  47.090  30.929  1.00 34.34           C  
ATOM   1332  CG1 ILE A 176      17.069  48.493  31.233  1.00 33.63           C  
ATOM   1333  CG2 ILE A 176      16.257  46.931  29.433  1.00 32.07           C  
ATOM   1334  CD1 ILE A 176      18.517  48.653  30.999  1.00 29.95           C  
ATOM   1335  N   LEU A 177      14.847  44.527  31.343  1.00 35.00           N  
ATOM   1336  CA  LEU A 177      14.099  43.341  30.892  1.00 34.62           C  
ATOM   1337  C   LEU A 177      12.724  43.199  31.575  1.00 34.51           C  
ATOM   1338  O   LEU A 177      11.718  42.796  30.935  1.00 32.87           O  
ATOM   1339  CB  LEU A 177      14.926  42.052  31.075  1.00 34.28           C  
ATOM   1340  CG  LEU A 177      16.192  41.885  30.224  1.00 35.06           C  
ATOM   1341  CD1 LEU A 177      16.876  40.585  30.534  1.00 34.22           C  
ATOM   1342  CD2 LEU A 177      15.884  41.959  28.738  1.00 34.84           C  
ATOM   1343  N   ARG A 178      12.687  43.491  32.877  1.00 35.13           N  
ATOM   1344  CA  ARG A 178      11.403  43.427  33.589  1.00 36.32           C  
ATOM   1345  C   ARG A 178      10.427  44.454  32.976  1.00 37.31           C  
ATOM   1346  O   ARG A 178       9.266  44.110  32.776  1.00 36.95           O  
ATOM   1347  CB  ARG A 178      11.519  43.618  35.089  1.00 35.24           C  
ATOM   1348  CG  ARG A 178      10.169  43.373  35.857  1.00 37.35           C  
ATOM   1349  CD  ARG A 178      10.037  44.216  37.137  1.00 36.53           C  
ATOM   1350  NE  ARG A 178      10.315  45.627  36.840  1.00 42.69           N  
ATOM   1351  CZ  ARG A 178       9.432  46.511  36.319  1.00 44.06           C  
ATOM   1352  NH1 ARG A 178       8.171  46.166  36.063  1.00 43.96           N  
ATOM   1353  NH2 ARG A 178       9.822  47.758  36.061  1.00 46.40           N  
ATOM   1354  N   ALA A 179      10.902  45.656  32.608  1.00 37.93           N  
ATOM   1355  CA  ALA A 179      10.000  46.639  31.971  1.00 39.59           C  
ATOM   1356  C   ALA A 179       9.432  46.175  30.621  1.00 40.95           C  
ATOM   1357  O   ALA A 179       8.369  46.613  30.250  1.00 42.05           O  
ATOM   1358  CB  ALA A 179      10.636  48.034  31.876  1.00 38.94           C  
ATOM   1359  N   GLU A 180      10.112  45.276  29.907  1.00 42.19           N  
ATOM   1360  CA  GLU A 180       9.643  44.800  28.601  1.00 43.96           C  
ATOM   1361  C   GLU A 180       8.748  43.541  28.636  1.00 43.86           C  
ATOM   1362  O   GLU A 180       7.676  43.519  28.032  1.00 43.48           O  
ATOM   1363  CB  GLU A 180      10.805  44.699  27.599  1.00 44.15           C  
ATOM   1364  CG  GLU A 180      11.716  45.948  27.657  1.00 51.75           C  
ATOM   1365  CD  GLU A 180      11.889  46.757  26.336  1.00 61.72           C  
ATOM   1366  OE1 GLU A 180      11.016  46.697  25.412  1.00 65.23           O  
ATOM   1367  OE2 GLU A 180      12.925  47.493  26.216  1.00 64.06           O  
ATOM   1368  N   ILE A 181       9.184  42.484  29.322  1.00 43.93           N  
ATOM   1369  CA  ILE A 181       8.267  41.403  29.662  1.00 43.42           C  
ATOM   1370  C   ILE A 181       8.048  41.510  31.157  1.00 43.23           C  
ATOM   1371  O   ILE A 181       8.444  42.517  31.764  1.00 44.44           O  
ATOM   1372  CB  ILE A 181       8.772  40.051  29.136  1.00 43.91           C  
ATOM   1373  CG1 ILE A 181       9.837  39.385  30.052  1.00 45.23           C  
ATOM   1374  CG2 ILE A 181       9.239  40.231  27.692  1.00 43.89           C  
ATOM   1375  CD1 ILE A 181      11.236  39.846  29.893  1.00 45.70           C  
ATOM   1376  N   GLY A 182       7.381  40.577  31.795  1.00 41.69           N  
ATOM   1377  CA  GLY A 182       7.286  40.758  33.233  1.00 40.00           C  
ATOM   1378  C   GLY A 182       8.433  40.002  33.885  1.00 38.93           C  
ATOM   1379  O   GLY A 182       9.526  40.524  34.130  1.00 39.18           O  
ATOM   1380  N   HIS A 183       8.174  38.736  34.137  1.00 36.96           N  
ATOM   1381  CA  HIS A 183       9.089  37.903  34.889  1.00 35.49           C  
ATOM   1382  C   HIS A 183      10.372  37.635  34.078  1.00 33.52           C  
ATOM   1383  O   HIS A 183      10.325  37.304  32.915  1.00 32.75           O  
ATOM   1384  CB  HIS A 183       8.381  36.609  35.237  1.00 34.91           C  
ATOM   1385  CG  HIS A 183       9.265  35.604  35.904  1.00 36.66           C  
ATOM   1386  ND1 HIS A 183       9.749  34.488  35.248  1.00 34.99           N  
ATOM   1387  CD2 HIS A 183       9.725  35.532  37.174  1.00 34.79           C  
ATOM   1388  CE1 HIS A 183      10.474  33.774  36.089  1.00 36.99           C  
ATOM   1389  NE2 HIS A 183      10.477  34.386  37.262  1.00 38.41           N  
ATOM   1390  N   VAL A 184      11.520  37.854  34.695  1.00 32.24           N  
ATOM   1391  CA  VAL A 184      12.791  37.594  34.028  1.00 30.16           C  
ATOM   1392  C   VAL A 184      13.390  36.360  34.652  1.00 29.57           C  
ATOM   1393  O   VAL A 184      13.867  36.374  35.788  1.00 28.83           O  
ATOM   1394  CB  VAL A 184      13.753  38.772  34.150  1.00 30.62           C  
ATOM   1395  CG1 VAL A 184      15.028  38.500  33.363  1.00 26.25           C  
ATOM   1396  CG2 VAL A 184      13.056  40.059  33.638  1.00 29.60           C  
ATOM   1397  N   SER A 185      13.312  35.278  33.894  1.00 29.08           N  
ATOM   1398  CA  SER A 185      13.915  33.996  34.231  1.00 28.80           C  
ATOM   1399  C   SER A 185      15.400  33.980  33.857  1.00 28.01           C  
ATOM   1400  O   SER A 185      15.875  34.824  33.094  1.00 27.69           O  
ATOM   1401  CB  SER A 185      13.167  32.895  33.464  1.00 28.48           C  
ATOM   1402  OG  SER A 185      13.275  33.118  32.064  1.00 29.88           O  
ATOM   1403  N   ALA A 186      16.127  33.018  34.412  1.00 27.28           N  
ATOM   1404  CA  ALA A 186      17.485  32.719  33.981  1.00 26.01           C  
ATOM   1405  C   ALA A 186      17.569  32.512  32.454  1.00 25.81           C  
ATOM   1406  O   ALA A 186      18.517  33.001  31.819  1.00 25.14           O  
ATOM   1407  CB  ALA A 186      17.969  31.492  34.688  1.00 24.61           C  
ATOM   1408  N   GLU A 187      16.602  31.788  31.876  1.00 25.69           N  
ATOM   1409  CA  GLU A 187      16.558  31.543  30.406  1.00 26.74           C  
ATOM   1410  C   GLU A 187      16.557  32.828  29.567  1.00 26.82           C  
ATOM   1411  O   GLU A 187      17.184  32.892  28.502  1.00 27.65           O  
ATOM   1412  CB  GLU A 187      15.329  30.703  29.999  1.00 26.59           C  
ATOM   1413  CG  GLU A 187      15.305  30.432  28.515  1.00 27.62           C  
ATOM   1414  CD  GLU A 187      14.160  29.532  28.125  1.00 31.14           C  
ATOM   1415  OE1 GLU A 187      13.136  30.059  27.635  1.00 32.70           O  
ATOM   1416  OE2 GLU A 187      14.274  28.303  28.309  1.00 30.60           O  
ATOM   1417  N   ARG A 188      15.873  33.839  30.071  1.00 27.62           N  
ATOM   1418  CA  ARG A 188      15.751  35.130  29.411  1.00 30.17           C  
ATOM   1419  C   ARG A 188      17.121  35.743  29.202  1.00 30.40           C  
ATOM   1420  O   ARG A 188      17.290  36.687  28.428  1.00 30.22           O  
ATOM   1421  CB  ARG A 188      14.944  36.084  30.281  1.00 30.42           C  
ATOM   1422  CG  ARG A 188      14.058  36.996  29.488  1.00 35.54           C  
ATOM   1423  CD  ARG A 188      12.650  36.444  29.343  1.00 37.46           C  
ATOM   1424  NE  ARG A 188      12.248  36.790  28.016  1.00 42.05           N  
ATOM   1425  CZ  ARG A 188      11.039  36.717  27.523  1.00 39.05           C  
ATOM   1426  NH1 ARG A 188      10.000  36.310  28.247  1.00 37.97           N  
ATOM   1427  NH2 ARG A 188      10.904  37.086  26.271  1.00 40.11           N  
ATOM   1428  N   VAL A 189      18.100  35.175  29.892  1.00 30.25           N  
ATOM   1429  CA  VAL A 189      19.456  35.681  29.819  1.00 30.76           C  
ATOM   1430  C   VAL A 189      20.474  34.593  29.387  1.00 29.46           C  
ATOM   1431  O   VAL A 189      21.441  34.905  28.708  1.00 30.68           O  
ATOM   1432  CB  VAL A 189      19.744  36.450  31.169  1.00 31.71           C  
ATOM   1433  CG1 VAL A 189      20.579  35.686  32.101  1.00 30.51           C  
ATOM   1434  CG2 VAL A 189      20.201  37.856  30.914  1.00 32.96           C  
ATOM   1435  N   LEU A 190      20.213  33.324  29.712  1.00 27.29           N  
ATOM   1436  CA  LEU A 190      21.103  32.210  29.396  1.00 25.27           C  
ATOM   1437  C   LEU A 190      20.519  31.322  28.331  1.00 25.04           C  
ATOM   1438  O   LEU A 190      19.943  30.268  28.623  1.00 24.90           O  
ATOM   1439  CB  LEU A 190      21.394  31.332  30.634  1.00 25.00           C  
ATOM   1440  CG  LEU A 190      22.106  31.955  31.830  1.00 24.53           C  
ATOM   1441  CD1 LEU A 190      22.340  30.936  32.964  1.00 21.02           C  
ATOM   1442  CD2 LEU A 190      23.429  32.569  31.377  1.00 22.45           C  
ATOM   1443  N   SER A 191      20.738  31.734  27.094  1.00 23.72           N  
ATOM   1444  CA  SER A 191      20.335  31.019  25.926  1.00 23.93           C  
ATOM   1445  C   SER A 191      20.741  31.932  24.784  1.00 24.36           C  
ATOM   1446  O   SER A 191      21.153  33.077  25.003  1.00 23.40           O  
ATOM   1447  CB  SER A 191      18.822  30.803  25.872  1.00 22.84           C  
ATOM   1448  OG  SER A 191      18.136  32.024  25.988  1.00 22.11           O  
ATOM   1449  N   GLY A 192      20.604  31.421  23.567  1.00 25.29           N  
ATOM   1450  CA  GLY A 192      20.799  32.226  22.348  1.00 25.41           C  
ATOM   1451  C   GLY A 192      19.971  33.497  22.339  1.00 26.24           C  
ATOM   1452  O   GLY A 192      20.560  34.533  22.160  1.00 26.73           O  
ATOM   1453  N   PRO A 193      18.633  33.447  22.473  1.00 26.30           N  
ATOM   1454  CA  PRO A 193      17.838  34.677  22.616  1.00 27.35           C  
ATOM   1455  C   PRO A 193      18.279  35.527  23.828  1.00 28.40           C  
ATOM   1456  O   PRO A 193      18.141  36.788  23.770  1.00 29.02           O  
ATOM   1457  CB  PRO A 193      16.387  34.140  22.808  1.00 27.14           C  
ATOM   1458  CG  PRO A 193      16.412  32.825  21.957  1.00 25.61           C  
ATOM   1459  CD  PRO A 193      17.758  32.259  22.441  1.00 26.88           C  
ATOM   1460  N   GLY A 194      18.822  34.853  24.874  1.00 27.70           N  
ATOM   1461  CA  GLY A 194      19.296  35.477  26.095  1.00 25.47           C  
ATOM   1462  C   GLY A 194      20.458  36.388  25.792  1.00 25.05           C  
ATOM   1463  O   GLY A 194      20.537  37.474  26.343  1.00 25.01           O  
ATOM   1464  N   LEU A 195      21.367  35.960  24.914  1.00 25.80           N  
ATOM   1465  CA  LEU A 195      22.461  36.837  24.443  1.00 26.22           C  
ATOM   1466  C   LEU A 195      21.960  38.121  23.780  1.00 26.35           C  
ATOM   1467  O   LEU A 195      22.568  39.181  23.956  1.00 27.24           O  
ATOM   1468  CB  LEU A 195      23.362  36.108  23.460  1.00 26.49           C  
ATOM   1469  CG  LEU A 195      24.148  34.896  23.971  1.00 29.74           C  
ATOM   1470  CD1 LEU A 195      24.966  34.353  22.816  1.00 30.58           C  
ATOM   1471  CD2 LEU A 195      25.068  35.209  25.139  1.00 29.08           C  
ATOM   1472  N   VAL A 196      20.872  38.034  23.007  1.00 25.92           N  
ATOM   1473  CA  VAL A 196      20.344  39.211  22.317  1.00 25.89           C  
ATOM   1474  C   VAL A 196      19.719  40.161  23.341  1.00 26.83           C  
ATOM   1475  O   VAL A 196      19.946  41.376  23.288  1.00 27.13           O  
ATOM   1476  CB  VAL A 196      19.372  38.808  21.190  1.00 26.78           C  
ATOM   1477  CG1 VAL A 196      18.662  40.040  20.603  1.00 26.46           C  
ATOM   1478  CG2 VAL A 196      20.130  38.030  20.092  1.00 24.73           C  
ATOM   1479  N   ASN A 197      19.027  39.584  24.330  1.00 26.66           N  
ATOM   1480  CA  ASN A 197      18.478  40.324  25.452  1.00 26.62           C  
ATOM   1481  C   ASN A 197      19.536  41.087  26.224  1.00 25.85           C  
ATOM   1482  O   ASN A 197      19.335  42.298  26.554  1.00 25.17           O  
ATOM   1483  CB  ASN A 197      17.674  39.376  26.401  1.00 27.69           C  
ATOM   1484  CG  ASN A 197      16.376  38.861  25.749  1.00 30.56           C  
ATOM   1485  OD1 ASN A 197      15.938  39.389  24.720  1.00 31.76           O  
ATOM   1486  ND2 ASN A 197      15.787  37.818  26.324  1.00 29.95           N  
ATOM   1487  N   LEU A 198      20.645  40.393  26.507  1.00 24.39           N  
ATOM   1488  CA  LEU A 198      21.762  40.986  27.235  1.00 24.85           C  
ATOM   1489  C   LEU A 198      22.333  42.162  26.443  1.00 24.76           C  
ATOM   1490  O   LEU A 198      22.501  43.281  26.972  1.00 25.04           O  
ATOM   1491  CB  LEU A 198      22.870  39.939  27.573  1.00 23.47           C  
ATOM   1492  CG  LEU A 198      22.749  38.950  28.744  1.00 23.56           C  
ATOM   1493  CD1 LEU A 198      23.833  37.844  28.670  1.00 21.96           C  
ATOM   1494  CD2 LEU A 198      22.800  39.600  30.144  1.00 21.44           C  
ATOM   1495  N   TYR A 199      22.602  41.916  25.170  1.00 26.22           N  
ATOM   1496  CA  TYR A 199      23.107  42.976  24.259  1.00 27.37           C  
ATOM   1497  C   TYR A 199      22.152  44.177  24.197  1.00 27.00           C  
ATOM   1498  O   TYR A 199      22.577  45.329  24.353  1.00 27.53           O  
ATOM   1499  CB  TYR A 199      23.398  42.419  22.855  1.00 26.46           C  
ATOM   1500  CG  TYR A 199      23.245  43.441  21.733  1.00 30.01           C  
ATOM   1501  CD1 TYR A 199      24.335  44.211  21.329  1.00 29.43           C  
ATOM   1502  CD2 TYR A 199      22.019  43.629  21.068  1.00 30.84           C  
ATOM   1503  CE1 TYR A 199      24.215  45.147  20.333  1.00 32.82           C  
ATOM   1504  CE2 TYR A 199      21.892  44.592  20.028  1.00 30.39           C  
ATOM   1505  CZ  TYR A 199      22.994  45.343  19.682  1.00 33.62           C  
ATOM   1506  OH  TYR A 199      22.964  46.293  18.673  1.00 35.02           O  
ATOM   1507  N   ARG A 200      20.859  43.925  24.034  1.00 28.57           N  
ATOM   1508  CA  ARG A 200      19.883  45.045  23.985  1.00 29.33           C  
ATOM   1509  C   ARG A 200      19.837  45.883  25.277  1.00 29.66           C  
ATOM   1510  O   ARG A 200      19.923  47.121  25.258  1.00 30.02           O  
ATOM   1511  CB  ARG A 200      18.518  44.517  23.672  1.00 30.19           C  
ATOM   1512  CG  ARG A 200      18.345  44.073  22.248  1.00 32.38           C  
ATOM   1513  CD  ARG A 200      16.993  43.364  22.018  1.00 39.26           C  
ATOM   1514  NE  ARG A 200      15.908  44.100  22.649  1.00 47.16           N  
ATOM   1515  CZ  ARG A 200      15.163  43.669  23.668  1.00 50.61           C  
ATOM   1516  NH1 ARG A 200      15.324  42.454  24.211  1.00 49.68           N  
ATOM   1517  NH2 ARG A 200      14.225  44.478  24.141  1.00 53.47           N  
ATOM   1518  N   ALA A 201      19.795  45.190  26.408  1.00 30.22           N  
ATOM   1519  CA  ALA A 201      19.797  45.809  27.716  1.00 29.54           C  
ATOM   1520  C   ALA A 201      21.118  46.551  28.014  1.00 29.72           C  
ATOM   1521  O   ALA A 201      21.122  47.620  28.613  1.00 30.03           O  
ATOM   1522  CB  ALA A 201      19.509  44.746  28.765  1.00 29.93           C  
ATOM   1523  N   ILE A 202      22.246  46.017  27.571  1.00 29.97           N  
ATOM   1524  CA  ILE A 202      23.517  46.712  27.766  1.00 28.79           C  
ATOM   1525  C   ILE A 202      23.536  48.019  26.964  1.00 30.16           C  
ATOM   1526  O   ILE A 202      23.995  49.059  27.442  1.00 30.45           O  
ATOM   1527  CB  ILE A 202      24.666  45.790  27.314  1.00 28.78           C  
ATOM   1528  CG1 ILE A 202      24.819  44.649  28.327  1.00 26.84           C  
ATOM   1529  CG2 ILE A 202      26.019  46.600  27.037  1.00 27.47           C  
ATOM   1530  CD1 ILE A 202      25.605  43.506  27.797  1.00 23.17           C  
ATOM   1531  N   VAL A 203      23.086  47.947  25.714  1.00 30.85           N  
ATOM   1532  CA  VAL A 203      23.050  49.137  24.843  1.00 31.21           C  
ATOM   1533  C   VAL A 203      22.130  50.228  25.451  1.00 31.89           C  
ATOM   1534  O   VAL A 203      22.530  51.382  25.582  1.00 30.83           O  
ATOM   1535  CB  VAL A 203      22.597  48.739  23.420  1.00 31.09           C  
ATOM   1536  CG1 VAL A 203      22.190  49.972  22.608  1.00 30.53           C  
ATOM   1537  CG2 VAL A 203      23.672  47.913  22.736  1.00 27.29           C  
ATOM   1538  N   LYS A 204      20.925  49.822  25.864  1.00 33.61           N  
ATOM   1539  CA  LYS A 204      19.955  50.728  26.500  1.00 35.06           C  
ATOM   1540  C   LYS A 204      20.478  51.352  27.766  1.00 35.34           C  
ATOM   1541  O   LYS A 204      20.199  52.527  28.030  1.00 35.41           O  
ATOM   1542  CB  LYS A 204      18.607  50.022  26.778  1.00 35.37           C  
ATOM   1543  CG  LYS A 204      17.873  49.618  25.470  1.00 39.06           C  
ATOM   1544  CD  LYS A 204      16.378  49.279  25.652  1.00 43.26           C  
ATOM   1545  CE  LYS A 204      15.747  48.846  24.283  1.00 43.88           C  
ATOM   1546  NZ  LYS A 204      14.232  48.781  24.323  1.00 43.40           N  
ATOM   1547  N   ALA A 205      21.224  50.569  28.556  1.00 34.94           N  
ATOM   1548  CA  ALA A 205      21.772  51.067  29.839  1.00 34.38           C  
ATOM   1549  C   ALA A 205      22.843  52.132  29.575  1.00 33.73           C  
ATOM   1550  O   ALA A 205      23.197  52.926  30.442  1.00 33.71           O  
ATOM   1551  CB  ALA A 205      22.360  49.894  30.702  1.00 33.48           C  
ATOM   1552  N   ASP A 206      23.396  52.126  28.376  1.00 34.23           N  
ATOM   1553  CA  ASP A 206      24.361  53.136  28.027  1.00 34.29           C  
ATOM   1554  C   ASP A 206      23.710  54.224  27.133  1.00 34.66           C  
ATOM   1555  O   ASP A 206      24.401  54.976  26.408  1.00 34.34           O  
ATOM   1556  CB  ASP A 206      25.540  52.452  27.366  1.00 35.26           C  
ATOM   1557  CG  ASP A 206      26.760  53.361  27.243  1.00 35.66           C  
ATOM   1558  OD1 ASP A 206      27.068  54.116  28.187  1.00 35.75           O  
ATOM   1559  OD2 ASP A 206      27.450  53.386  26.206  1.00 36.64           O  
ATOM   1560  N   ASN A 207      22.376  54.305  27.193  1.00 34.21           N  
ATOM   1561  CA  ASN A 207      21.625  55.375  26.518  1.00 34.94           C  
ATOM   1562  C   ASN A 207      21.790  55.403  24.993  1.00 34.69           C  
ATOM   1563  O   ASN A 207      22.011  56.458  24.392  1.00 35.26           O  
ATOM   1564  CB  ASN A 207      21.952  56.736  27.159  1.00 35.06           C  
ATOM   1565  CG  ASN A 207      21.382  56.854  28.581  1.00 36.14           C  
ATOM   1566  OD1 ASN A 207      20.184  56.673  28.798  1.00 35.95           O  
ATOM   1567  ND2 ASN A 207      22.241  57.175  29.548  1.00 37.11           N  
ATOM   1568  N   ARG A 208      21.684  54.236  24.362  1.00 33.89           N  
ATOM   1569  CA  ARG A 208      21.926  54.138  22.946  1.00 33.10           C  
ATOM   1570  C   ARG A 208      20.824  53.258  22.417  1.00 34.01           C  
ATOM   1571  O   ARG A 208      20.026  52.745  23.203  1.00 33.46           O  
ATOM   1572  CB  ARG A 208      23.312  53.562  22.688  1.00 32.52           C  
ATOM   1573  CG  ARG A 208      24.425  54.582  22.881  1.00 31.89           C  
ATOM   1574  CD  ARG A 208      25.817  54.118  22.510  1.00 31.11           C  
ATOM   1575  NE  ARG A 208      26.387  53.183  23.490  1.00 32.13           N  
ATOM   1576  CZ  ARG A 208      26.508  51.867  23.308  1.00 29.79           C  
ATOM   1577  NH1 ARG A 208      26.075  51.312  22.170  1.00 23.58           N  
ATOM   1578  NH2 ARG A 208      27.051  51.106  24.281  1.00 28.10           N  
ATOM   1579  N   LEU A 209      20.780  53.061  21.100  1.00 34.68           N  
ATOM   1580  CA  LEU A 209      19.759  52.194  20.485  1.00 35.96           C  
ATOM   1581  C   LEU A 209      20.407  50.921  19.930  1.00 36.00           C  
ATOM   1582  O   LEU A 209      21.473  50.969  19.310  1.00 36.18           O  
ATOM   1583  CB  LEU A 209      18.991  52.938  19.361  1.00 35.40           C  
ATOM   1584  CG  LEU A 209      17.887  54.000  19.571  1.00 38.88           C  
ATOM   1585  CD1 LEU A 209      17.319  54.139  20.994  1.00 38.08           C  
ATOM   1586  CD2 LEU A 209      18.286  55.405  18.994  1.00 38.66           C  
ATOM   1587  N   PRO A 210      19.797  49.780  20.189  1.00 36.48           N  
ATOM   1588  CA  PRO A 210      20.336  48.498  19.697  1.00 37.35           C  
ATOM   1589  C   PRO A 210      20.015  48.257  18.244  1.00 37.64           C  
ATOM   1590  O   PRO A 210      18.998  48.774  17.782  1.00 38.67           O  
ATOM   1591  CB  PRO A 210      19.547  47.456  20.514  1.00 36.83           C  
ATOM   1592  CG  PRO A 210      18.204  48.161  20.785  1.00 37.89           C  
ATOM   1593  CD  PRO A 210      18.575  49.619  21.003  1.00 36.46           C  
ATOM   1594  N   GLU A 211      20.787  47.423  17.553  1.00 38.07           N  
ATOM   1595  CA  GLU A 211      20.289  46.828  16.306  1.00 38.44           C  
ATOM   1596  C   GLU A 211      19.560  45.530  16.569  1.00 38.57           C  
ATOM   1597  O   GLU A 211      19.646  44.941  17.675  1.00 37.60           O  
ATOM   1598  CB  GLU A 211      21.405  46.617  15.310  1.00 38.19           C  
ATOM   1599  CG  GLU A 211      22.129  47.919  15.017  1.00 43.32           C  
ATOM   1600  CD  GLU A 211      23.361  47.721  14.150  1.00 49.00           C  
ATOM   1601  OE1 GLU A 211      23.208  47.303  12.973  1.00 51.91           O  
ATOM   1602  OE2 GLU A 211      24.476  47.975  14.651  1.00 49.61           O  
ATOM   1603  N   ASN A 212      18.830  45.089  15.545  1.00 38.78           N  
ATOM   1604  CA  ASN A 212      18.080  43.846  15.591  1.00 39.34           C  
ATOM   1605  C   ASN A 212      19.031  42.658  15.374  1.00 39.23           C  
ATOM   1606  O   ASN A 212      18.992  41.990  14.334  1.00 40.18           O  
ATOM   1607  CB  ASN A 212      16.987  43.877  14.514  1.00 39.99           C  
ATOM   1608  CG  ASN A 212      16.165  42.598  14.450  1.00 44.26           C  
ATOM   1609  OD1 ASN A 212      15.930  41.917  15.478  1.00 48.34           O  
ATOM   1610  ND2 ASN A 212      15.707  42.251  13.234  1.00 47.56           N  
ATOM   1611  N   LEU A 213      19.891  42.392  16.346  1.00 37.84           N  
ATOM   1612  CA  LEU A 213      20.925  41.386  16.141  1.00 35.86           C  
ATOM   1613  C   LEU A 213      20.408  40.003  16.489  1.00 35.22           C  
ATOM   1614  O   LEU A 213      19.421  39.851  17.240  1.00 35.00           O  
ATOM   1615  CB  LEU A 213      22.208  41.749  16.897  1.00 34.96           C  
ATOM   1616  CG  LEU A 213      22.967  43.041  16.538  1.00 34.16           C  
ATOM   1617  CD1 LEU A 213      24.311  43.055  17.287  1.00 32.68           C  
ATOM   1618  CD2 LEU A 213      23.220  43.244  15.037  1.00 32.42           C  
ATOM   1619  N   LYS A 214      21.034  39.001  15.877  1.00 34.41           N  
ATOM   1620  CA  LYS A 214      20.713  37.606  16.114  1.00 34.98           C  
ATOM   1621  C   LYS A 214      21.727  37.005  17.102  1.00 33.32           C  
ATOM   1622  O   LYS A 214      22.842  37.545  17.197  1.00 32.75           O  
ATOM   1623  CB  LYS A 214      20.840  36.842  14.787  1.00 36.74           C  
ATOM   1624  CG  LYS A 214      19.583  36.805  13.938  1.00 42.30           C  
ATOM   1625  CD  LYS A 214      19.627  37.900  12.881  1.00 49.33           C  
ATOM   1626  CE  LYS A 214      20.459  37.514  11.664  1.00 53.18           C  
ATOM   1627  NZ  LYS A 214      21.365  38.663  11.340  1.00 55.96           N  
ATOM   1628  N   PRO A 215      21.394  35.868  17.748  1.00 31.81           N  
ATOM   1629  CA  PRO A 215      22.321  35.189  18.680  1.00 31.54           C  
ATOM   1630  C   PRO A 215      23.685  34.981  18.043  1.00 31.73           C  
ATOM   1631  O   PRO A 215      24.688  35.322  18.688  1.00 31.50           O  
ATOM   1632  CB  PRO A 215      21.622  33.830  18.979  1.00 30.32           C  
ATOM   1633  CG  PRO A 215      20.149  34.143  18.805  1.00 30.69           C  
ATOM   1634  CD  PRO A 215      20.115  35.133  17.645  1.00 31.83           C  
ATOM   1635  N   LYS A 216      23.735  34.504  16.794  1.00 31.48           N  
ATOM   1636  CA  LYS A 216      25.029  34.307  16.152  1.00 32.57           C  
ATOM   1637  C   LYS A 216      25.825  35.593  15.885  1.00 32.26           C  
ATOM   1638  O   LYS A 216      27.071  35.537  15.825  1.00 32.55           O  
ATOM   1639  CB  LYS A 216      24.921  33.459  14.879  1.00 33.53           C  
ATOM   1640  CG  LYS A 216      24.977  31.931  15.164  1.00 35.92           C  
ATOM   1641  CD  LYS A 216      24.409  31.113  13.946  1.00 43.62           C  
ATOM   1642  CE  LYS A 216      24.123  29.633  14.290  1.00 45.26           C  
ATOM   1643  NZ  LYS A 216      23.506  28.947  13.115  1.00 46.66           N  
ATOM   1644  N   ASP A 217      25.152  36.737  15.726  1.00 30.62           N  
ATOM   1645  CA  ASP A 217      25.911  37.978  15.638  1.00 30.58           C  
ATOM   1646  C   ASP A 217      26.578  38.334  16.961  1.00 28.47           C  
ATOM   1647  O   ASP A 217      27.660  38.890  16.975  1.00 26.74           O  
ATOM   1648  CB  ASP A 217      25.046  39.170  15.245  1.00 31.72           C  
ATOM   1649  CG  ASP A 217      24.473  39.028  13.888  1.00 34.72           C  
ATOM   1650  OD1 ASP A 217      25.267  38.735  12.942  1.00 35.89           O  
ATOM   1651  OD2 ASP A 217      23.234  39.157  13.711  1.00 35.72           O  
ATOM   1652  N   ILE A 218      25.904  38.040  18.067  1.00 28.00           N  
ATOM   1653  CA  ILE A 218      26.472  38.393  19.365  1.00 28.05           C  
ATOM   1654  C   ILE A 218      27.813  37.630  19.579  1.00 28.08           C  
ATOM   1655  O   ILE A 218      28.816  38.235  19.928  1.00 26.96           O  
ATOM   1656  CB  ILE A 218      25.498  38.109  20.498  1.00 27.69           C  
ATOM   1657  CG1 ILE A 218      24.078  38.620  20.149  1.00 26.80           C  
ATOM   1658  CG2 ILE A 218      26.089  38.664  21.850  1.00 27.58           C  
ATOM   1659  CD1 ILE A 218      23.949  40.141  19.999  1.00 24.88           C  
ATOM   1660  N   THR A 219      27.807  36.316  19.340  1.00 28.33           N  
ATOM   1661  CA  THR A 219      28.987  35.479  19.589  1.00 29.05           C  
ATOM   1662  C   THR A 219      30.109  35.827  18.635  1.00 29.47           C  
ATOM   1663  O   THR A 219      31.263  35.976  19.067  1.00 29.34           O  
ATOM   1664  CB  THR A 219      28.631  33.993  19.518  1.00 28.34           C  
ATOM   1665  OG1 THR A 219      28.094  33.694  18.225  1.00 29.15           O  
ATOM   1666  CG2 THR A 219      27.447  33.707  20.468  1.00 26.75           C  
ATOM   1667  N   GLU A 220      29.734  36.047  17.376  1.00 30.01           N  
ATOM   1668  CA  GLU A 220      30.652  36.350  16.299  1.00 31.67           C  
ATOM   1669  C   GLU A 220      31.447  37.599  16.580  1.00 30.96           C  
ATOM   1670  O   GLU A 220      32.677  37.594  16.493  1.00 30.73           O  
ATOM   1671  CB  GLU A 220      29.888  36.502  14.964  1.00 33.25           C  
ATOM   1672  CG  GLU A 220      30.732  36.976  13.781  1.00 39.70           C  
ATOM   1673  CD  GLU A 220      30.146  36.525  12.450  1.00 50.15           C  
ATOM   1674  OE1 GLU A 220      30.468  35.399  12.001  1.00 55.08           O  
ATOM   1675  OE2 GLU A 220      29.335  37.278  11.856  1.00 54.20           O  
ATOM   1676  N   ARG A 221      30.741  38.664  16.933  1.00 31.30           N  
ATOM   1677  CA  ARG A 221      31.375  39.935  17.253  1.00 31.54           C  
ATOM   1678  C   ARG A 221      32.080  39.951  18.623  1.00 31.51           C  
ATOM   1679  O   ARG A 221      33.056  40.692  18.803  1.00 31.27           O  
ATOM   1680  CB  ARG A 221      30.367  41.085  17.157  1.00 31.34           C  
ATOM   1681  CG  ARG A 221      29.674  41.185  15.795  1.00 32.96           C  
ATOM   1682  CD  ARG A 221      28.569  42.202  15.746  1.00 32.40           C  
ATOM   1683  NE  ARG A 221      27.839  42.078  14.489  1.00 36.06           N  
ATOM   1684  CZ  ARG A 221      26.988  42.992  14.026  1.00 35.74           C  
ATOM   1685  NH1 ARG A 221      26.754  44.107  14.711  1.00 30.03           N  
ATOM   1686  NH2 ARG A 221      26.355  42.776  12.878  1.00 36.33           N  
ATOM   1687  N   ALA A 222      31.581  39.195  19.600  1.00 30.71           N  
ATOM   1688  CA  ALA A 222      32.364  39.033  20.836  1.00 31.14           C  
ATOM   1689  C   ALA A 222      33.697  38.321  20.499  1.00 31.89           C  
ATOM   1690  O   ALA A 222      34.745  38.790  20.872  1.00 31.52           O  
ATOM   1691  CB  ALA A 222      31.594  38.274  21.873  1.00 30.81           C  
ATOM   1692  N   LEU A 223      33.653  37.212  19.754  1.00 33.37           N  
ATOM   1693  CA  LEU A 223      34.882  36.501  19.349  1.00 34.63           C  
ATOM   1694  C   LEU A 223      35.861  37.391  18.613  1.00 35.41           C  
ATOM   1695  O   LEU A 223      37.057  37.345  18.883  1.00 35.27           O  
ATOM   1696  CB  LEU A 223      34.572  35.292  18.454  1.00 34.80           C  
ATOM   1697  CG  LEU A 223      33.961  34.040  19.093  1.00 37.97           C  
ATOM   1698  CD1 LEU A 223      34.198  32.801  18.226  1.00 39.67           C  
ATOM   1699  CD2 LEU A 223      34.506  33.845  20.486  1.00 36.45           C  
ATOM   1700  N   ALA A 224      35.360  38.193  17.665  1.00 35.70           N  
ATOM   1701  CA  ALA A 224      36.256  38.955  16.803  1.00 35.11           C  
ATOM   1702  C   ALA A 224      36.721  40.187  17.546  1.00 35.74           C  
ATOM   1703  O   ALA A 224      37.540  40.949  17.017  1.00 36.85           O  
ATOM   1704  CB  ALA A 224      35.583  39.319  15.530  1.00 35.26           C  
ATOM   1705  N   ASP A 225      36.257  40.365  18.790  1.00 34.02           N  
ATOM   1706  CA  ASP A 225      36.489  41.615  19.511  1.00 34.25           C  
ATOM   1707  C   ASP A 225      36.074  42.876  18.676  1.00 33.46           C  
ATOM   1708  O   ASP A 225      36.689  43.945  18.800  1.00 32.17           O  
ATOM   1709  CB  ASP A 225      37.950  41.719  20.025  1.00 34.81           C  
ATOM   1710  CG  ASP A 225      38.092  42.690  21.198  1.00 38.11           C  
ATOM   1711  OD1 ASP A 225      39.216  43.233  21.444  1.00 41.96           O  
ATOM   1712  OD2 ASP A 225      37.121  43.003  21.925  1.00 39.28           O  
ATOM   1713  N   SER A 226      34.991  42.743  17.891  1.00 32.16           N  
ATOM   1714  CA  SER A 226      34.513  43.822  17.013  1.00 32.27           C  
ATOM   1715  C   SER A 226      33.261  44.589  17.501  1.00 32.39           C  
ATOM   1716  O   SER A 226      32.734  45.401  16.772  1.00 32.74           O  
ATOM   1717  CB  SER A 226      34.265  43.304  15.619  1.00 31.53           C  
ATOM   1718  OG  SER A 226      33.112  42.467  15.611  1.00 33.02           O  
ATOM   1719  N   CYS A 227      32.795  44.331  18.730  1.00 32.32           N  
ATOM   1720  CA  CYS A 227      31.725  45.116  19.316  1.00 30.77           C  
ATOM   1721  C   CYS A 227      31.800  45.079  20.821  1.00 30.78           C  
ATOM   1722  O   CYS A 227      31.626  44.010  21.418  1.00 30.13           O  
ATOM   1723  CB  CYS A 227      30.354  44.629  18.836  1.00 31.36           C  
ATOM   1724  SG  CYS A 227      28.986  45.470  19.710  1.00 31.26           S  
ATOM   1725  N   THR A 228      32.027  46.233  21.459  1.00 30.64           N  
ATOM   1726  CA  THR A 228      32.053  46.228  22.910  1.00 30.54           C  
ATOM   1727  C   THR A 228      30.733  45.780  23.553  1.00 30.03           C  
ATOM   1728  O   THR A 228      30.761  45.193  24.617  1.00 29.80           O  
ATOM   1729  CB  THR A 228      32.477  47.573  23.507  1.00 31.58           C  
ATOM   1730  OG1 THR A 228      31.602  48.591  23.008  1.00 29.85           O  
ATOM   1731  CG2 THR A 228      33.918  47.946  23.068  1.00 30.36           C  
ATOM   1732  N   ASP A 229      29.598  46.054  22.920  1.00 29.60           N  
ATOM   1733  CA  ASP A 229      28.312  45.645  23.481  1.00 29.20           C  
ATOM   1734  C   ASP A 229      28.204  44.135  23.437  1.00 28.84           C  
ATOM   1735  O   ASP A 229      27.848  43.524  24.434  1.00 27.93           O  
ATOM   1736  CB  ASP A 229      27.118  46.306  22.780  1.00 28.81           C  
ATOM   1737  CG  ASP A 229      27.183  47.841  22.831  1.00 32.43           C  
ATOM   1738  OD1 ASP A 229      27.458  48.419  23.927  1.00 30.39           O  
ATOM   1739  OD2 ASP A 229      26.969  48.548  21.810  1.00 33.79           O  
ATOM   1740  N   CYS A 230      28.508  43.542  22.283  1.00 28.36           N  
ATOM   1741  CA  CYS A 230      28.450  42.091  22.159  1.00 28.33           C  
ATOM   1742  C   CYS A 230      29.471  41.398  23.078  1.00 27.64           C  
ATOM   1743  O   CYS A 230      29.144  40.427  23.710  1.00 26.50           O  
ATOM   1744  CB  CYS A 230      28.647  41.658  20.696  1.00 28.55           C  
ATOM   1745  SG  CYS A 230      27.271  42.242  19.670  1.00 28.45           S  
ATOM   1746  N   ARG A 231      30.690  41.916  23.156  1.00 27.65           N  
ATOM   1747  CA  ARG A 231      31.686  41.328  24.042  1.00 29.11           C  
ATOM   1748  C   ARG A 231      31.217  41.290  25.503  1.00 28.14           C  
ATOM   1749  O   ARG A 231      31.279  40.253  26.182  1.00 27.79           O  
ATOM   1750  CB  ARG A 231      33.019  42.068  23.942  1.00 29.00           C  
ATOM   1751  CG  ARG A 231      34.143  41.181  24.401  1.00 30.34           C  
ATOM   1752  CD  ARG A 231      35.456  41.824  24.304  1.00 34.45           C  
ATOM   1753  NE  ARG A 231      35.720  42.607  25.497  1.00 39.72           N  
ATOM   1754  CZ  ARG A 231      36.657  43.550  25.568  1.00 43.72           C  
ATOM   1755  NH1 ARG A 231      37.397  43.851  24.488  1.00 45.00           N  
ATOM   1756  NH2 ARG A 231      36.839  44.217  26.701  1.00 42.25           N  
ATOM   1757  N   ARG A 232      30.713  42.436  25.949  1.00 28.41           N  
ATOM   1758  CA  ARG A 232      30.120  42.558  27.280  1.00 28.32           C  
ATOM   1759  C   ARG A 232      28.934  41.603  27.466  1.00 27.75           C  
ATOM   1760  O   ARG A 232      28.822  40.935  28.499  1.00 27.09           O  
ATOM   1761  CB  ARG A 232      29.690  43.997  27.571  1.00 27.72           C  
ATOM   1762  CG  ARG A 232      29.228  44.142  29.014  1.00 30.45           C  
ATOM   1763  CD  ARG A 232      30.369  44.088  30.022  1.00 34.25           C  
ATOM   1764  NE  ARG A 232      30.247  45.305  30.800  1.00 43.80           N  
ATOM   1765  CZ  ARG A 232      31.117  46.293  30.864  1.00 44.85           C  
ATOM   1766  NH1 ARG A 232      32.288  46.254  30.234  1.00 43.28           N  
ATOM   1767  NH2 ARG A 232      30.804  47.339  31.615  1.00 50.83           N  
ATOM   1768  N   ALA A 233      28.056  41.536  26.466  1.00 27.04           N  
ATOM   1769  CA  ALA A 233      26.944  40.559  26.500  1.00 27.04           C  
ATOM   1770  C   ALA A 233      27.490  39.180  26.781  1.00 26.03           C  
ATOM   1771  O   ALA A 233      27.005  38.526  27.695  1.00 26.25           O  
ATOM   1772  CB  ALA A 233      26.107  40.537  25.170  1.00 25.75           C  
ATOM   1773  N   LEU A 234      28.523  38.760  26.027  1.00 24.97           N  
ATOM   1774  CA  LEU A 234      29.039  37.383  26.151  1.00 23.78           C  
ATOM   1775  C   LEU A 234      29.784  37.109  27.478  1.00 23.00           C  
ATOM   1776  O   LEU A 234      29.718  35.992  28.068  1.00 22.24           O  
ATOM   1777  CB  LEU A 234      29.964  37.058  24.982  1.00 24.29           C  
ATOM   1778  CG  LEU A 234      29.786  35.717  24.266  1.00 23.41           C  
ATOM   1779  CD1 LEU A 234      31.099  35.187  23.840  1.00 20.48           C  
ATOM   1780  CD2 LEU A 234      28.998  34.685  24.976  1.00 23.49           C  
ATOM   1781  N   SER A 235      30.514  38.119  27.918  1.00 22.26           N  
ATOM   1782  CA  SER A 235      31.201  38.060  29.197  1.00 22.88           C  
ATOM   1783  C   SER A 235      30.228  37.882  30.341  1.00 22.78           C  
ATOM   1784  O   SER A 235      30.483  37.120  31.274  1.00 23.06           O  
ATOM   1785  CB  SER A 235      32.001  39.340  29.414  1.00 22.82           C  
ATOM   1786  OG  SER A 235      33.092  39.338  28.517  1.00 23.23           O  
ATOM   1787  N   LEU A 236      29.088  38.543  30.262  1.00 22.82           N  
ATOM   1788  CA  LEU A 236      28.138  38.436  31.360  1.00 22.63           C  
ATOM   1789  C   LEU A 236      27.454  37.084  31.249  1.00 23.22           C  
ATOM   1790  O   LEU A 236      27.137  36.454  32.285  1.00 23.39           O  
ATOM   1791  CB  LEU A 236      27.103  39.548  31.298  1.00 22.95           C  
ATOM   1792  CG  LEU A 236      27.582  40.988  31.607  1.00 24.17           C  
ATOM   1793  CD1 LEU A 236      26.418  42.034  31.415  1.00 19.47           C  
ATOM   1794  CD2 LEU A 236      28.080  41.042  32.987  1.00 26.09           C  
ATOM   1795  N   PHE A 237      27.248  36.599  30.009  1.00 21.57           N  
ATOM   1796  CA  PHE A 237      26.639  35.281  29.900  1.00 21.77           C  
ATOM   1797  C   PHE A 237      27.516  34.236  30.625  1.00 21.17           C  
ATOM   1798  O   PHE A 237      27.008  33.399  31.349  1.00 19.94           O  
ATOM   1799  CB  PHE A 237      26.426  34.918  28.447  1.00 20.59           C  
ATOM   1800  CG  PHE A 237      26.106  33.473  28.206  1.00 22.38           C  
ATOM   1801  CD1 PHE A 237      24.777  33.052  28.039  1.00 21.60           C  
ATOM   1802  CD2 PHE A 237      27.142  32.533  28.055  1.00 20.36           C  
ATOM   1803  CE1 PHE A 237      24.489  31.692  27.758  1.00 22.85           C  
ATOM   1804  CE2 PHE A 237      26.883  31.212  27.803  1.00 19.66           C  
ATOM   1805  CZ  PHE A 237      25.551  30.762  27.650  1.00 22.98           C  
ATOM   1806  N   CYS A 238      28.830  34.311  30.418  1.00 21.99           N  
ATOM   1807  CA  CYS A 238      29.759  33.321  30.971  1.00 21.63           C  
ATOM   1808  C   CYS A 238      29.774  33.327  32.464  1.00 21.17           C  
ATOM   1809  O   CYS A 238      29.727  32.242  33.082  1.00 21.99           O  
ATOM   1810  CB  CYS A 238      31.157  33.537  30.449  1.00 21.66           C  
ATOM   1811  SG  CYS A 238      31.289  33.283  28.647  1.00 25.99           S  
ATOM   1812  N   VAL A 239      29.812  34.518  33.077  1.00 21.78           N  
ATOM   1813  CA  VAL A 239      29.727  34.606  34.530  1.00 21.06           C  
ATOM   1814  C   VAL A 239      28.372  34.200  35.085  1.00 20.63           C  
ATOM   1815  O   VAL A 239      28.282  33.474  36.092  1.00 19.67           O  
ATOM   1816  CB  VAL A 239      30.269  35.971  35.165  1.00 22.66           C  
ATOM   1817  CG1 VAL A 239      31.660  36.311  34.653  1.00 22.25           C  
ATOM   1818  CG2 VAL A 239      29.330  37.139  35.001  1.00 22.48           C  
ATOM   1819  N   ILE A 240      27.302  34.650  34.443  1.00 20.50           N  
ATOM   1820  CA  ILE A 240      25.960  34.305  34.918  1.00 21.16           C  
ATOM   1821  C   ILE A 240      25.774  32.798  34.820  1.00 21.24           C  
ATOM   1822  O   ILE A 240      25.164  32.191  35.691  1.00 21.81           O  
ATOM   1823  CB  ILE A 240      24.854  35.067  34.107  1.00 21.30           C  
ATOM   1824  CG1 ILE A 240      24.884  36.569  34.430  1.00 21.90           C  
ATOM   1825  CG2 ILE A 240      23.480  34.479  34.386  1.00 18.51           C  
ATOM   1826  CD1 ILE A 240      24.239  37.507  33.254  1.00 24.46           C  
HETATM 1827  N   MSE A 241      26.309  32.194  33.756  1.00 22.25           N  
HETATM 1828  CA  MSE A 241      26.283  30.723  33.582  1.00 22.90           C  
HETATM 1829  C   MSE A 241      27.024  30.002  34.747  1.00 22.64           C  
HETATM 1830  O   MSE A 241      26.542  28.967  35.271  1.00 22.25           O  
HETATM 1831  CB  MSE A 241      26.880  30.395  32.227  1.00 23.19           C  
HETATM 1832  CG  MSE A 241      26.596  29.055  31.702  1.00 30.13           C  
HETATM 1833 SE   MSE A 241      24.736  28.808  31.013  1.00 44.61          SE  
HETATM 1834  CE  MSE A 241      25.077  26.957  30.275  1.00 38.99           C  
ATOM   1835  N   GLY A 242      28.174  30.555  35.171  1.00 21.77           N  
ATOM   1836  CA  GLY A 242      28.887  30.018  36.330  1.00 21.14           C  
ATOM   1837  C   GLY A 242      28.106  30.142  37.628  1.00 22.35           C  
ATOM   1838  O   GLY A 242      27.998  29.179  38.398  1.00 21.53           O  
ATOM   1839  N   ARG A 243      27.545  31.329  37.899  1.00 22.70           N  
ATOM   1840  CA  ARG A 243      26.779  31.511  39.131  1.00 23.22           C  
ATOM   1841  C   ARG A 243      25.628  30.497  39.197  1.00 22.87           C  
ATOM   1842  O   ARG A 243      25.378  29.852  40.238  1.00 22.48           O  
ATOM   1843  CB  ARG A 243      26.199  32.910  39.178  1.00 24.01           C  
ATOM   1844  CG  ARG A 243      27.166  33.989  39.561  1.00 25.85           C  
ATOM   1845  CD  ARG A 243      26.440  35.280  39.920  1.00 26.96           C  
ATOM   1846  NE  ARG A 243      26.845  36.197  38.935  1.00 31.13           N  
ATOM   1847  CZ  ARG A 243      26.062  36.809  38.097  1.00 32.33           C  
ATOM   1848  NH1 ARG A 243      24.731  36.727  38.157  1.00 29.48           N  
ATOM   1849  NH2 ARG A 243      26.653  37.573  37.211  1.00 34.74           N  
ATOM   1850  N   PHE A 244      24.973  30.328  38.050  1.00 21.39           N  
ATOM   1851  CA  PHE A 244      23.799  29.478  37.949  1.00 20.73           C  
ATOM   1852  C   PHE A 244      24.143  28.047  38.226  1.00 20.09           C  
ATOM   1853  O   PHE A 244      23.475  27.410  38.994  1.00 21.77           O  
ATOM   1854  CB  PHE A 244      23.144  29.628  36.561  1.00 20.27           C  
ATOM   1855  CG  PHE A 244      21.850  28.903  36.420  1.00 20.05           C  
ATOM   1856  CD1 PHE A 244      20.629  29.554  36.704  1.00 23.33           C  
ATOM   1857  CD2 PHE A 244      21.820  27.585  35.945  1.00 22.75           C  
ATOM   1858  CE1 PHE A 244      19.390  28.867  36.567  1.00 19.27           C  
ATOM   1859  CE2 PHE A 244      20.603  26.890  35.791  1.00 22.29           C  
ATOM   1860  CZ  PHE A 244      19.375  27.558  36.083  1.00 20.04           C  
ATOM   1861  N   GLY A 245      25.187  27.511  37.622  1.00 21.24           N  
ATOM   1862  CA  GLY A 245      25.618  26.146  37.975  1.00 20.33           C  
ATOM   1863  C   GLY A 245      25.962  25.978  39.452  1.00 20.35           C  
ATOM   1864  O   GLY A 245      25.717  24.930  40.082  1.00 19.25           O  
ATOM   1865  N   GLY A 246      26.572  27.008  40.032  1.00 20.10           N  
ATOM   1866  CA  GLY A 246      26.966  26.864  41.425  1.00 19.76           C  
ATOM   1867  C   GLY A 246      25.728  26.783  42.316  1.00 19.08           C  
ATOM   1868  O   GLY A 246      25.745  26.081  43.313  1.00 18.94           O  
ATOM   1869  N   ASN A 247      24.649  27.479  41.937  1.00 18.80           N  
ATOM   1870  CA  ASN A 247      23.362  27.375  42.661  1.00 19.34           C  
ATOM   1871  C   ASN A 247      22.757  25.982  42.561  1.00 18.91           C  
ATOM   1872  O   ASN A 247      22.377  25.410  43.567  1.00 19.42           O  
ATOM   1873  CB  ASN A 247      22.369  28.431  42.159  1.00 20.11           C  
ATOM   1874  CG  ASN A 247      22.801  29.846  42.498  1.00 19.87           C  
ATOM   1875  OD1 ASN A 247      23.486  30.062  43.474  1.00 18.81           O  
ATOM   1876  ND2 ASN A 247      22.356  30.822  41.708  1.00 18.93           N  
ATOM   1877  N   LEU A 248      22.735  25.391  41.362  1.00 19.19           N  
ATOM   1878  CA  LEU A 248      22.341  23.982  41.209  1.00 18.57           C  
ATOM   1879  C   LEU A 248      23.129  23.021  42.106  1.00 19.82           C  
ATOM   1880  O   LEU A 248      22.565  22.065  42.716  1.00 19.83           O  
ATOM   1881  CB  LEU A 248      22.499  23.541  39.759  1.00 19.93           C  
ATOM   1882  CG  LEU A 248      21.699  24.295  38.676  1.00 20.11           C  
ATOM   1883  CD1 LEU A 248      22.137  23.763  37.294  1.00 17.76           C  
ATOM   1884  CD2 LEU A 248      20.236  24.013  38.877  1.00 19.13           C  
ATOM   1885  N   ALA A 249      24.445  23.260  42.164  1.00 19.79           N  
ATOM   1886  CA  ALA A 249      25.365  22.448  42.945  1.00 19.66           C  
ATOM   1887  C   ALA A 249      25.052  22.522  44.433  1.00 19.95           C  
ATOM   1888  O   ALA A 249      24.982  21.505  45.100  1.00 19.31           O  
ATOM   1889  CB  ALA A 249      26.842  22.833  42.624  1.00 17.85           C  
ATOM   1890  N   LEU A 250      24.833  23.733  44.956  1.00 21.65           N  
ATOM   1891  CA  LEU A 250      24.441  23.878  46.370  1.00 21.07           C  
ATOM   1892  C   LEU A 250      23.093  23.226  46.671  1.00 21.66           C  
ATOM   1893  O   LEU A 250      22.888  22.615  47.727  1.00 20.84           O  
ATOM   1894  CB  LEU A 250      24.370  25.355  46.764  1.00 21.05           C  
ATOM   1895  CG  LEU A 250      25.737  26.064  46.799  1.00 20.73           C  
ATOM   1896  CD1 LEU A 250      25.593  27.575  46.583  1.00 19.56           C  
ATOM   1897  CD2 LEU A 250      26.463  25.763  48.106  1.00 16.93           C  
ATOM   1898  N   ASN A 251      22.164  23.411  45.749  1.00 22.10           N  
ATOM   1899  CA  ASN A 251      20.773  23.094  45.977  1.00 22.15           C  
ATOM   1900  C   ASN A 251      20.560  21.606  46.080  1.00 23.15           C  
ATOM   1901  O   ASN A 251      19.820  21.144  46.960  1.00 23.02           O  
ATOM   1902  CB  ASN A 251      19.907  23.742  44.890  1.00 22.60           C  
ATOM   1903  CG  ASN A 251      18.427  23.348  45.006  1.00 25.12           C  
ATOM   1904  OD1 ASN A 251      17.941  22.519  44.220  1.00 31.29           O  
ATOM   1905  ND2 ASN A 251      17.717  23.927  45.983  1.00 21.76           N  
ATOM   1906  N   LEU A 252      21.245  20.815  45.243  1.00 23.03           N  
ATOM   1907  CA  LEU A 252      21.075  19.374  45.387  1.00 23.19           C  
ATOM   1908  C   LEU A 252      22.350  18.594  45.776  1.00 23.81           C  
ATOM   1909  O   LEU A 252      22.409  17.365  45.563  1.00 23.40           O  
ATOM   1910  CB  LEU A 252      20.374  18.784  44.126  1.00 23.55           C  
ATOM   1911  CG  LEU A 252      19.315  17.679  44.436  1.00 24.78           C  
ATOM   1912  CD1 LEU A 252      18.004  18.243  44.927  1.00 25.71           C  
ATOM   1913  CD2 LEU A 252      19.086  16.811  43.194  1.00 26.04           C  
ATOM   1914  N   GLY A 253      23.370  19.282  46.332  1.00 23.64           N  
ATOM   1915  CA  GLY A 253      24.517  18.568  46.890  1.00 23.30           C  
ATOM   1916  C   GLY A 253      25.173  17.697  45.834  1.00 23.77           C  
ATOM   1917  O   GLY A 253      25.444  16.508  45.971  1.00 24.41           O  
ATOM   1918  N   THR A 254      25.492  18.337  44.747  1.00 24.10           N  
ATOM   1919  CA  THR A 254      25.732  17.659  43.473  1.00 24.08           C  
ATOM   1920  C   THR A 254      27.207  17.199  43.283  1.00 24.11           C  
ATOM   1921  O   THR A 254      27.924  17.608  42.347  1.00 23.89           O  
ATOM   1922  CB  THR A 254      25.256  18.736  42.519  1.00 24.55           C  
ATOM   1923  OG1 THR A 254      23.987  18.363  41.906  1.00 28.95           O  
ATOM   1924  CG2 THR A 254      26.224  19.106  41.525  1.00 21.96           C  
ATOM   1925  N   PHE A 255      27.660  16.323  44.172  1.00 23.86           N  
ATOM   1926  CA  PHE A 255      29.082  15.976  44.246  1.00 24.21           C  
ATOM   1927  C   PHE A 255      29.425  15.027  43.176  1.00 24.57           C  
ATOM   1928  O   PHE A 255      30.617  14.811  42.924  1.00 24.82           O  
ATOM   1929  CB  PHE A 255      29.534  15.397  45.608  1.00 24.45           C  
ATOM   1930  CG  PHE A 255      29.018  16.175  46.814  1.00 26.70           C  
ATOM   1931  CD1 PHE A 255      28.189  15.551  47.755  1.00 28.92           C  
ATOM   1932  CD2 PHE A 255      29.366  17.510  47.010  1.00 27.48           C  
ATOM   1933  CE1 PHE A 255      27.722  16.245  48.913  1.00 29.67           C  
ATOM   1934  CE2 PHE A 255      28.928  18.215  48.135  1.00 28.35           C  
ATOM   1935  CZ  PHE A 255      28.081  17.590  49.080  1.00 30.92           C  
ATOM   1936  N   GLY A 256      28.408  14.473  42.508  1.00 24.14           N  
ATOM   1937  CA  GLY A 256      28.680  13.746  41.286  1.00 23.60           C  
ATOM   1938  C   GLY A 256      29.146  14.612  40.106  1.00 23.76           C  
ATOM   1939  O   GLY A 256      29.501  14.074  39.062  1.00 24.31           O  
ATOM   1940  N   GLY A 257      29.126  15.941  40.206  1.00 22.93           N  
ATOM   1941  CA  GLY A 257      29.463  16.698  39.001  1.00 22.30           C  
ATOM   1942  C   GLY A 257      28.338  17.608  38.544  1.00 22.58           C  
ATOM   1943  O   GLY A 257      27.147  17.378  38.829  1.00 21.73           O  
ATOM   1944  N   VAL A 258      28.753  18.689  37.907  1.00 21.99           N  
ATOM   1945  CA  VAL A 258      27.877  19.607  37.190  1.00 21.44           C  
ATOM   1946  C   VAL A 258      28.278  19.542  35.688  1.00 21.88           C  
ATOM   1947  O   VAL A 258      29.476  19.665  35.347  1.00 21.66           O  
ATOM   1948  CB  VAL A 258      28.004  21.029  37.760  1.00 21.21           C  
ATOM   1949  CG1 VAL A 258      27.146  22.026  36.973  1.00 21.70           C  
ATOM   1950  CG2 VAL A 258      27.504  21.044  39.194  1.00 20.61           C  
ATOM   1951  N   PHE A 259      27.298  19.266  34.814  1.00 22.15           N  
ATOM   1952  CA  PHE A 259      27.558  19.114  33.371  1.00 22.74           C  
ATOM   1953  C   PHE A 259      26.834  20.154  32.576  1.00 23.61           C  
ATOM   1954  O   PHE A 259      25.693  20.483  32.880  1.00 24.87           O  
ATOM   1955  CB  PHE A 259      27.194  17.723  32.875  1.00 21.93           C  
ATOM   1956  CG  PHE A 259      28.034  16.645  33.486  1.00 23.08           C  
ATOM   1957  CD1 PHE A 259      27.897  16.327  34.842  1.00 22.69           C  
ATOM   1958  CD2 PHE A 259      29.019  15.994  32.736  1.00 20.33           C  
ATOM   1959  CE1 PHE A 259      28.698  15.334  35.423  1.00 21.67           C  
ATOM   1960  CE2 PHE A 259      29.838  14.997  33.324  1.00 19.52           C  
ATOM   1961  CZ  PHE A 259      29.672  14.660  34.641  1.00 21.76           C  
ATOM   1962  N   ILE A 260      27.509  20.722  31.593  1.00 23.63           N  
ATOM   1963  CA  ILE A 260      26.872  21.675  30.723  1.00 24.25           C  
ATOM   1964  C   ILE A 260      26.639  20.934  29.406  1.00 25.34           C  
ATOM   1965  O   ILE A 260      27.586  20.467  28.773  1.00 24.70           O  
ATOM   1966  CB  ILE A 260      27.767  22.947  30.555  1.00 24.11           C  
ATOM   1967  CG1 ILE A 260      27.996  23.621  31.907  1.00 24.44           C  
ATOM   1968  CG2 ILE A 260      27.167  23.959  29.524  1.00 23.81           C  
ATOM   1969  CD1 ILE A 260      29.110  24.648  31.874  1.00 24.77           C  
ATOM   1970  N   ALA A 261      25.384  20.812  28.994  1.00 27.47           N  
ATOM   1971  CA  ALA A 261      25.099  20.322  27.639  1.00 29.94           C  
ATOM   1972  C   ALA A 261      25.493  21.409  26.632  1.00 31.72           C  
ATOM   1973  O   ALA A 261      25.306  22.606  26.892  1.00 33.23           O  
ATOM   1974  CB  ALA A 261      23.675  19.957  27.499  1.00 29.16           C  
ATOM   1975  N   GLY A 262      26.134  21.016  25.531  1.00 32.74           N  
ATOM   1976  CA  GLY A 262      26.390  21.963  24.459  1.00 33.24           C  
ATOM   1977  C   GLY A 262      25.116  22.354  23.699  1.00 33.78           C  
ATOM   1978  O   GLY A 262      24.345  21.507  23.092  1.00 36.44           O  
ATOM   1979  N   GLY A 263      24.855  23.635  23.757  1.00 31.96           N  
ATOM   1980  CA  GLY A 263      24.004  24.309  22.812  1.00 29.75           C  
ATOM   1981  C   GLY A 263      24.964  25.340  22.256  1.00 29.18           C  
ATOM   1982  O   GLY A 263      25.843  25.003  21.462  1.00 28.62           O  
ATOM   1983  N   ILE A 264      24.886  26.564  22.753  1.00 27.43           N  
ATOM   1984  CA  ILE A 264      25.690  27.632  22.162  1.00 28.14           C  
ATOM   1985  C   ILE A 264      27.178  27.707  22.569  1.00 27.87           C  
ATOM   1986  O   ILE A 264      27.959  28.368  21.926  1.00 26.68           O  
ATOM   1987  CB  ILE A 264      25.002  28.995  22.388  1.00 27.31           C  
ATOM   1988  CG1 ILE A 264      24.960  29.328  23.870  1.00 28.62           C  
ATOM   1989  CG2 ILE A 264      23.625  28.949  21.811  1.00 28.27           C  
ATOM   1990  CD1 ILE A 264      24.536  30.776  24.145  1.00 30.29           C  
ATOM   1991  N   VAL A 265      27.570  27.047  23.653  1.00 29.44           N  
ATOM   1992  CA  VAL A 265      28.900  27.278  24.205  1.00 29.47           C  
ATOM   1993  C   VAL A 265      30.038  26.828  23.280  1.00 30.93           C  
ATOM   1994  O   VAL A 265      30.999  27.598  23.147  1.00 32.01           O  
ATOM   1995  CB  VAL A 265      29.064  26.719  25.605  1.00 29.02           C  
ATOM   1996  CG1 VAL A 265      30.530  26.786  26.051  1.00 27.45           C  
ATOM   1997  CG2 VAL A 265      28.155  27.471  26.596  1.00 29.13           C  
ATOM   1998  N   PRO A 266      29.968  25.625  22.671  1.00 32.20           N  
ATOM   1999  CA  PRO A 266      31.065  25.131  21.799  1.00 33.33           C  
ATOM   2000  C   PRO A 266      31.431  26.096  20.675  1.00 34.84           C  
ATOM   2001  O   PRO A 266      32.556  26.033  20.150  1.00 35.64           O  
ATOM   2002  CB  PRO A 266      30.510  23.814  21.246  1.00 32.72           C  
ATOM   2003  CG  PRO A 266      29.642  23.322  22.344  1.00 31.69           C  
ATOM   2004  CD  PRO A 266      28.923  24.588  22.822  1.00 31.48           C  
ATOM   2005  N   ARG A 267      30.511  27.009  20.360  1.00 35.52           N  
ATOM   2006  CA  ARG A 267      30.725  27.959  19.289  1.00 36.63           C  
ATOM   2007  C   ARG A 267      31.644  29.099  19.763  1.00 35.94           C  
ATOM   2008  O   ARG A 267      32.222  29.828  18.938  1.00 35.93           O  
ATOM   2009  CB  ARG A 267      29.368  28.408  18.693  1.00 37.12           C  
ATOM   2010  CG  ARG A 267      29.197  29.861  18.272  1.00 41.98           C  
ATOM   2011  CD  ARG A 267      27.834  30.139  17.529  1.00 46.79           C  
ATOM   2012  NE  ARG A 267      26.929  31.092  18.198  1.00 47.94           N  
ATOM   2013  CZ  ARG A 267      25.664  30.831  18.547  1.00 48.59           C  
ATOM   2014  NH1 ARG A 267      25.136  29.633  18.312  1.00 50.05           N  
ATOM   2015  NH2 ARG A 267      24.919  31.767  19.139  1.00 44.30           N  
ATOM   2016  N   PHE A 268      31.833  29.216  21.081  1.00 34.08           N  
ATOM   2017  CA  PHE A 268      32.755  30.229  21.629  1.00 32.06           C  
ATOM   2018  C   PHE A 268      33.617  29.646  22.740  1.00 31.73           C  
ATOM   2019  O   PHE A 268      33.907  30.300  23.774  1.00 30.18           O  
ATOM   2020  CB  PHE A 268      32.029  31.498  22.091  1.00 31.10           C  
ATOM   2021  CG  PHE A 268      30.849  31.260  22.980  1.00 29.13           C  
ATOM   2022  CD1 PHE A 268      30.992  31.314  24.378  1.00 29.19           C  
ATOM   2023  CD2 PHE A 268      29.576  31.056  22.433  1.00 28.40           C  
ATOM   2024  CE1 PHE A 268      29.902  31.128  25.212  1.00 27.55           C  
ATOM   2025  CE2 PHE A 268      28.450  30.879  23.252  1.00 27.85           C  
ATOM   2026  CZ  PHE A 268      28.617  30.897  24.653  1.00 30.29           C  
ATOM   2027  N   LEU A 269      34.030  28.404  22.487  1.00 30.97           N  
ATOM   2028  CA  LEU A 269      34.745  27.624  23.463  1.00 30.52           C  
ATOM   2029  C   LEU A 269      35.959  28.364  24.040  1.00 30.15           C  
ATOM   2030  O   LEU A 269      36.124  28.409  25.257  1.00 30.53           O  
ATOM   2031  CB  LEU A 269      35.104  26.255  22.906  1.00 29.60           C  
ATOM   2032  CG  LEU A 269      35.853  25.336  23.889  1.00 29.39           C  
ATOM   2033  CD1 LEU A 269      35.006  25.000  25.128  1.00 30.10           C  
ATOM   2034  CD2 LEU A 269      36.305  24.068  23.203  1.00 30.60           C  
ATOM   2035  N   GLU A 270      36.774  28.968  23.179  1.00 30.59           N  
ATOM   2036  CA  GLU A 270      37.975  29.683  23.614  1.00 30.83           C  
ATOM   2037  C   GLU A 270      37.613  30.936  24.414  1.00 29.94           C  
ATOM   2038  O   GLU A 270      38.251  31.255  25.436  1.00 30.44           O  
ATOM   2039  CB  GLU A 270      38.913  30.004  22.437  1.00 31.47           C  
ATOM   2040  CG  GLU A 270      39.223  28.817  21.490  1.00 37.96           C  
ATOM   2041  CD  GLU A 270      39.682  27.541  22.212  1.00 45.39           C  
ATOM   2042  OE1 GLU A 270      40.549  27.665  23.118  1.00 49.11           O  
ATOM   2043  OE2 GLU A 270      39.173  26.418  21.887  1.00 45.97           O  
ATOM   2044  N   PHE A 271      36.557  31.615  24.002  1.00 28.22           N  
ATOM   2045  CA  PHE A 271      36.084  32.760  24.757  1.00 26.87           C  
ATOM   2046  C   PHE A 271      35.619  32.371  26.169  1.00 26.62           C  
ATOM   2047  O   PHE A 271      35.926  33.074  27.135  1.00 25.96           O  
ATOM   2048  CB  PHE A 271      35.008  33.504  23.979  1.00 26.92           C  
ATOM   2049  CG  PHE A 271      34.538  34.789  24.644  1.00 26.65           C  
ATOM   2050  CD1 PHE A 271      34.979  36.041  24.176  1.00 29.20           C  
ATOM   2051  CD2 PHE A 271      33.658  34.745  25.731  1.00 21.51           C  
ATOM   2052  CE1 PHE A 271      34.545  37.226  24.780  1.00 25.77           C  
ATOM   2053  CE2 PHE A 271      33.211  35.914  26.334  1.00 21.02           C  
ATOM   2054  CZ  PHE A 271      33.639  37.152  25.853  1.00 23.73           C  
ATOM   2055  N   PHE A 272      34.949  31.218  26.254  1.00 25.84           N  
ATOM   2056  CA  PHE A 272      34.363  30.665  27.473  1.00 25.26           C  
ATOM   2057  C   PHE A 272      35.463  30.262  28.478  1.00 25.34           C  
ATOM   2058  O   PHE A 272      35.321  30.532  29.696  1.00 25.20           O  
ATOM   2059  CB  PHE A 272      33.447  29.459  27.118  1.00 23.87           C  
ATOM   2060  CG  PHE A 272      32.743  28.824  28.310  1.00 23.54           C  
ATOM   2061  CD1 PHE A 272      31.642  29.436  28.891  1.00 20.14           C  
ATOM   2062  CD2 PHE A 272      33.168  27.581  28.813  1.00 21.91           C  
ATOM   2063  CE1 PHE A 272      30.959  28.853  29.970  1.00 22.02           C  
ATOM   2064  CE2 PHE A 272      32.507  26.992  29.881  1.00 24.26           C  
ATOM   2065  CZ  PHE A 272      31.392  27.630  30.478  1.00 19.95           C  
ATOM   2066  N   LYS A 273      36.528  29.630  27.961  1.00 24.79           N  
ATOM   2067  CA  LYS A 273      37.680  29.160  28.763  1.00 24.46           C  
ATOM   2068  C   LYS A 273      38.419  30.357  29.348  1.00 24.80           C  
ATOM   2069  O   LYS A 273      38.938  30.307  30.488  1.00 23.89           O  
ATOM   2070  CB  LYS A 273      38.651  28.364  27.873  1.00 25.07           C  
ATOM   2071  CG  LYS A 273      38.277  26.857  27.670  1.00 24.59           C  
ATOM   2072  CD  LYS A 273      39.233  26.266  26.599  1.00 27.19           C  
ATOM   2073  CE  LYS A 273      39.338  24.777  26.708  1.00 30.21           C  
ATOM   2074  NZ  LYS A 273      39.986  24.188  25.502  1.00 33.85           N  
ATOM   2075  N   ALA A 274      38.466  31.421  28.546  1.00 23.16           N  
ATOM   2076  CA  ALA A 274      39.112  32.649  28.926  1.00 23.84           C  
ATOM   2077  C   ALA A 274      38.217  33.489  29.855  1.00 23.61           C  
ATOM   2078  O   ALA A 274      38.675  34.519  30.389  1.00 23.31           O  
ATOM   2079  CB  ALA A 274      39.511  33.485  27.648  1.00 23.78           C  
ATOM   2080  N   SER A 275      36.958  33.065  30.059  1.00 22.52           N  
ATOM   2081  CA  SER A 275      36.010  33.894  30.839  1.00 21.38           C  
ATOM   2082  C   SER A 275      36.095  33.699  32.352  1.00 21.53           C  
ATOM   2083  O   SER A 275      36.817  32.795  32.834  1.00 21.32           O  
ATOM   2084  CB  SER A 275      34.599  33.531  30.432  1.00 22.62           C  
ATOM   2085  OG  SER A 275      34.173  32.376  31.147  1.00 20.12           O  
ATOM   2086  N   GLY A 276      35.299  34.482  33.093  1.00 20.95           N  
ATOM   2087  CA  GLY A 276      35.191  34.384  34.547  1.00 20.26           C  
ATOM   2088  C   GLY A 276      34.261  33.273  35.062  1.00 20.81           C  
ATOM   2089  O   GLY A 276      33.852  33.294  36.245  1.00 20.55           O  
ATOM   2090  N   PHE A 277      33.952  32.307  34.195  1.00 20.28           N  
ATOM   2091  CA  PHE A 277      33.037  31.207  34.511  1.00 21.10           C  
ATOM   2092  C   PHE A 277      33.290  30.471  35.842  1.00 21.10           C  
ATOM   2093  O   PHE A 277      32.411  30.409  36.716  1.00 21.84           O  
ATOM   2094  CB  PHE A 277      32.988  30.129  33.378  1.00 19.92           C  
ATOM   2095  CG  PHE A 277      32.109  28.918  33.735  1.00 20.16           C  
ATOM   2096  CD1 PHE A 277      30.713  28.956  33.533  1.00 18.80           C  
ATOM   2097  CD2 PHE A 277      32.665  27.769  34.242  1.00 17.47           C  
ATOM   2098  CE1 PHE A 277      29.914  27.872  33.849  1.00 20.20           C  
ATOM   2099  CE2 PHE A 277      31.859  26.648  34.583  1.00 20.08           C  
ATOM   2100  CZ  PHE A 277      30.480  26.707  34.398  1.00 17.10           C  
ATOM   2101  N   ARG A 278      34.449  29.836  35.960  1.00 20.25           N  
ATOM   2102  CA  ARG A 278      34.723  29.072  37.166  1.00 20.07           C  
ATOM   2103  C   ARG A 278      34.755  29.948  38.448  1.00 20.80           C  
ATOM   2104  O   ARG A 278      34.143  29.559  39.445  1.00 20.80           O  
ATOM   2105  CB  ARG A 278      35.972  28.199  37.019  1.00 19.05           C  
ATOM   2106  CG  ARG A 278      36.186  27.296  38.202  1.00 17.21           C  
ATOM   2107  CD  ARG A 278      35.131  26.223  38.399  1.00 16.26           C  
ATOM   2108  NE  ARG A 278      35.268  25.629  39.728  1.00 17.17           N  
ATOM   2109  CZ  ARG A 278      34.842  24.413  40.071  1.00 19.88           C  
ATOM   2110  NH1 ARG A 278      34.270  23.621  39.150  1.00 17.71           N  
ATOM   2111  NH2 ARG A 278      34.945  24.006  41.356  1.00 17.55           N  
ATOM   2112  N   ALA A 279      35.397  31.134  38.408  1.00 20.74           N  
ATOM   2113  CA  ALA A 279      35.375  32.043  39.573  1.00 21.34           C  
ATOM   2114  C   ALA A 279      33.936  32.382  39.990  1.00 21.99           C  
ATOM   2115  O   ALA A 279      33.620  32.441  41.183  1.00 23.86           O  
ATOM   2116  CB  ALA A 279      36.172  33.338  39.302  1.00 20.99           C  
ATOM   2117  N   ALA A 280      33.057  32.579  39.016  1.00 20.64           N  
ATOM   2118  CA  ALA A 280      31.649  32.876  39.316  1.00 20.53           C  
ATOM   2119  C   ALA A 280      30.866  31.652  39.841  1.00 20.71           C  
ATOM   2120  O   ALA A 280      29.930  31.807  40.635  1.00 22.06           O  
ATOM   2121  CB  ALA A 280      30.969  33.434  38.078  1.00 19.64           C  
ATOM   2122  N   PHE A 281      31.230  30.455  39.391  1.00 19.16           N  
ATOM   2123  CA  PHE A 281      30.669  29.218  39.978  1.00 19.70           C  
ATOM   2124  C   PHE A 281      31.012  29.093  41.489  1.00 19.68           C  
ATOM   2125  O   PHE A 281      30.191  28.624  42.268  1.00 18.61           O  
ATOM   2126  CB  PHE A 281      31.175  28.003  39.168  1.00 17.54           C  
ATOM   2127  CG  PHE A 281      30.779  26.651  39.706  1.00 19.39           C  
ATOM   2128  CD1 PHE A 281      29.653  25.991  39.216  1.00 19.63           C  
ATOM   2129  CD2 PHE A 281      31.608  25.953  40.602  1.00 21.77           C  
ATOM   2130  CE1 PHE A 281      29.306  24.684  39.669  1.00 18.70           C  
ATOM   2131  CE2 PHE A 281      31.260  24.655  41.049  1.00 19.68           C  
ATOM   2132  CZ  PHE A 281      30.102  24.037  40.587  1.00 15.58           C  
ATOM   2133  N   GLU A 282      32.204  29.559  41.878  1.00 20.02           N  
ATOM   2134  CA  GLU A 282      32.677  29.400  43.262  1.00 21.79           C  
ATOM   2135  C   GLU A 282      32.379  30.636  44.088  1.00 22.38           C  
ATOM   2136  O   GLU A 282      32.626  30.662  45.282  1.00 23.75           O  
ATOM   2137  CB  GLU A 282      34.187  29.083  43.321  1.00 20.91           C  
ATOM   2138  CG  GLU A 282      34.577  27.937  42.416  1.00 21.52           C  
ATOM   2139  CD  GLU A 282      35.905  27.340  42.808  1.00 22.68           C  
ATOM   2140  OE1 GLU A 282      36.564  27.947  43.666  1.00 23.28           O  
ATOM   2141  OE2 GLU A 282      36.288  26.291  42.250  1.00 19.82           O  
ATOM   2142  N   ASP A 283      31.821  31.648  43.463  1.00 22.57           N  
ATOM   2143  CA  ASP A 283      31.565  32.902  44.159  1.00 24.13           C  
ATOM   2144  C   ASP A 283      30.295  32.895  45.037  1.00 24.09           C  
ATOM   2145  O   ASP A 283      29.341  33.584  44.760  1.00 24.85           O  
ATOM   2146  CB  ASP A 283      31.591  34.029  43.151  1.00 23.80           C  
ATOM   2147  CG  ASP A 283      31.391  35.358  43.760  1.00 26.02           C  
ATOM   2148  OD1 ASP A 283      31.801  35.575  44.920  1.00 28.03           O  
ATOM   2149  OD2 ASP A 283      30.816  36.256  43.123  1.00 24.71           O  
ATOM   2150  N   LYS A 284      30.353  32.156  46.143  1.00 25.01           N  
ATOM   2151  CA  LYS A 284      29.208  31.872  47.017  1.00 24.86           C  
ATOM   2152  C   LYS A 284      29.522  32.172  48.479  1.00 26.36           C  
ATOM   2153  O   LYS A 284      29.032  31.425  49.371  1.00 26.65           O  
ATOM   2154  CB  LYS A 284      28.885  30.350  46.942  1.00 25.50           C  
ATOM   2155  CG  LYS A 284      28.498  29.811  45.475  1.00 22.95           C  
ATOM   2156  CD  LYS A 284      27.327  30.629  44.836  1.00 17.30           C  
ATOM   2157  CE  LYS A 284      26.985  30.028  43.449  1.00 19.19           C  
ATOM   2158  NZ  LYS A 284      26.186  30.922  42.604  1.00 17.18           N  
ATOM   2159  N   GLY A 285      30.337  33.213  48.739  1.00 26.18           N  
ATOM   2160  CA  GLY A 285      30.753  33.583  50.089  1.00 27.07           C  
ATOM   2161  C   GLY A 285      31.330  32.447  50.914  1.00 27.80           C  
ATOM   2162  O   GLY A 285      32.219  31.738  50.474  1.00 28.79           O  
ATOM   2163  N   ARG A 286      30.792  32.180  52.088  1.00 28.42           N  
ATOM   2164  CA  ARG A 286      31.394  31.090  52.862  1.00 29.96           C  
ATOM   2165  C   ARG A 286      31.147  29.669  52.306  1.00 28.97           C  
ATOM   2166  O   ARG A 286      31.774  28.726  52.776  1.00 28.98           O  
ATOM   2167  CB  ARG A 286      31.058  31.186  54.356  1.00 30.61           C  
ATOM   2168  CG  ARG A 286      29.604  30.924  54.657  1.00 35.30           C  
ATOM   2169  CD  ARG A 286      29.208  31.255  56.080  1.00 41.83           C  
ATOM   2170  NE  ARG A 286      29.028  30.009  56.808  1.00 46.81           N  
ATOM   2171  CZ  ARG A 286      27.895  29.625  57.386  1.00 46.02           C  
ATOM   2172  NH1 ARG A 286      26.812  30.399  57.366  1.00 44.02           N  
ATOM   2173  NH2 ARG A 286      27.867  28.466  58.014  1.00 47.92           N  
ATOM   2174  N   PHE A 287      30.261  29.535  51.308  1.00 27.29           N  
ATOM   2175  CA  PHE A 287      29.976  28.235  50.688  1.00 25.70           C  
ATOM   2176  C   PHE A 287      30.826  28.014  49.430  1.00 25.43           C  
ATOM   2177  O   PHE A 287      30.621  27.071  48.689  1.00 24.62           O  
ATOM   2178  CB  PHE A 287      28.443  27.999  50.512  1.00 25.40           C  
ATOM   2179  CG  PHE A 287      27.769  27.623  51.824  1.00 24.14           C  
ATOM   2180  CD1 PHE A 287      27.468  28.614  52.790  1.00 25.29           C  
ATOM   2181  CD2 PHE A 287      27.592  26.291  52.164  1.00 19.41           C  
ATOM   2182  CE1 PHE A 287      26.933  28.276  54.055  1.00 25.56           C  
ATOM   2183  CE2 PHE A 287      27.058  25.917  53.426  1.00 22.06           C  
ATOM   2184  CZ  PHE A 287      26.721  26.926  54.384  1.00 22.92           C  
ATOM   2185  N   LYS A 288      31.810  28.888  49.228  1.00 26.16           N  
ATOM   2186  CA  LYS A 288      32.893  28.665  48.268  1.00 28.13           C  
ATOM   2187  C   LYS A 288      33.527  27.273  48.446  1.00 28.92           C  
ATOM   2188  O   LYS A 288      33.771  26.530  47.455  1.00 28.67           O  
ATOM   2189  CB  LYS A 288      33.974  29.735  48.444  1.00 28.47           C  
ATOM   2190  CG  LYS A 288      35.076  29.687  47.412  1.00 31.37           C  
ATOM   2191  CD  LYS A 288      36.287  30.463  47.893  1.00 36.51           C  
ATOM   2192  CE  LYS A 288      36.650  31.556  46.923  1.00 44.98           C  
ATOM   2193  NZ  LYS A 288      35.802  32.837  46.980  1.00 48.38           N  
ATOM   2194  N   GLU A 289      33.762  26.918  49.707  1.00 29.27           N  
ATOM   2195  CA  GLU A 289      34.431  25.671  50.037  1.00 31.10           C  
ATOM   2196  C   GLU A 289      33.521  24.445  49.855  1.00 29.63           C  
ATOM   2197  O   GLU A 289      33.987  23.349  49.634  1.00 28.55           O  
ATOM   2198  CB  GLU A 289      35.080  25.746  51.443  1.00 31.99           C  
ATOM   2199  CG  GLU A 289      36.598  26.056  51.311  1.00 42.26           C  
ATOM   2200  CD  GLU A 289      37.079  27.502  51.698  1.00 51.80           C  
ATOM   2201  OE1 GLU A 289      37.955  27.612  52.625  1.00 55.81           O  
ATOM   2202  OE2 GLU A 289      36.650  28.532  51.074  1.00 52.70           O  
ATOM   2203  N   TYR A 290      32.214  24.650  49.912  1.00 27.99           N  
ATOM   2204  CA  TYR A 290      31.316  23.604  49.515  1.00 26.82           C  
ATOM   2205  C   TYR A 290      31.476  23.244  48.016  1.00 26.94           C  
ATOM   2206  O   TYR A 290      31.522  22.045  47.701  1.00 27.50           O  
ATOM   2207  CB  TYR A 290      29.906  24.010  49.878  1.00 26.06           C  
ATOM   2208  CG  TYR A 290      28.869  22.956  49.768  1.00 26.91           C  
ATOM   2209  CD1 TYR A 290      28.447  22.227  50.889  1.00 27.21           C  
ATOM   2210  CD2 TYR A 290      28.260  22.701  48.518  1.00 25.90           C  
ATOM   2211  CE1 TYR A 290      27.452  21.238  50.771  1.00 27.22           C  
ATOM   2212  CE2 TYR A 290      27.292  21.755  48.379  1.00 26.24           C  
ATOM   2213  CZ  TYR A 290      26.853  21.051  49.497  1.00 29.78           C  
ATOM   2214  OH  TYR A 290      25.856  20.143  49.283  1.00 28.53           O  
ATOM   2215  N   VAL A 291      31.575  24.236  47.116  1.00 26.00           N  
ATOM   2216  CA  VAL A 291      31.569  23.949  45.675  1.00 26.43           C  
ATOM   2217  C   VAL A 291      32.971  23.876  45.013  1.00 27.95           C  
ATOM   2218  O   VAL A 291      33.079  23.497  43.847  1.00 27.73           O  
ATOM   2219  CB  VAL A 291      30.645  24.907  44.841  1.00 26.16           C  
ATOM   2220  CG1 VAL A 291      29.155  24.915  45.347  1.00 24.91           C  
ATOM   2221  CG2 VAL A 291      31.203  26.300  44.764  1.00 25.91           C  
ATOM   2222  N   HIS A 292      34.024  24.254  45.767  1.00 28.47           N  
ATOM   2223  CA  HIS A 292      35.370  24.376  45.247  1.00 28.70           C  
ATOM   2224  C   HIS A 292      35.851  23.070  44.667  1.00 27.60           C  
ATOM   2225  O   HIS A 292      36.636  23.073  43.710  1.00 25.72           O  
ATOM   2226  CB  HIS A 292      36.355  24.867  46.339  1.00 30.04           C  
ATOM   2227  CG  HIS A 292      37.667  25.340  45.789  1.00 36.67           C  
ATOM   2228  ND1 HIS A 292      38.855  24.658  45.988  1.00 41.41           N  
ATOM   2229  CD2 HIS A 292      37.977  26.414  45.007  1.00 41.55           C  
ATOM   2230  CE1 HIS A 292      39.834  25.288  45.344  1.00 42.85           C  
ATOM   2231  NE2 HIS A 292      39.332  26.368  44.754  1.00 43.05           N  
ATOM   2232  N   ASP A 293      35.436  21.960  45.271  1.00 26.88           N  
ATOM   2233  CA  ASP A 293      35.926  20.662  44.834  1.00 28.49           C  
ATOM   2234  C   ASP A 293      34.982  20.029  43.808  1.00 27.15           C  
ATOM   2235  O   ASP A 293      35.287  18.949  43.316  1.00 25.79           O  
ATOM   2236  CB  ASP A 293      36.080  19.638  45.980  1.00 30.07           C  
ATOM   2237  CG  ASP A 293      36.984  20.108  47.087  1.00 37.82           C  
ATOM   2238  OD1 ASP A 293      38.129  20.552  46.786  1.00 46.92           O  
ATOM   2239  OD2 ASP A 293      36.633  20.058  48.307  1.00 42.20           O  
ATOM   2240  N   ILE A 294      33.823  20.660  43.551  1.00 26.16           N  
ATOM   2241  CA  ILE A 294      32.855  20.083  42.613  1.00 24.04           C  
ATOM   2242  C   ILE A 294      33.241  20.400  41.183  1.00 23.08           C  
ATOM   2243  O   ILE A 294      33.277  21.583  40.780  1.00 24.71           O  
ATOM   2244  CB  ILE A 294      31.406  20.522  42.894  1.00 24.46           C  
ATOM   2245  CG1 ILE A 294      30.963  20.066  44.299  1.00 23.71           C  
ATOM   2246  CG2 ILE A 294      30.491  19.926  41.852  1.00 21.78           C  
ATOM   2247  CD1 ILE A 294      29.547  20.590  44.689  1.00 20.26           C  
ATOM   2248  N   PRO A 295      33.499  19.356  40.410  1.00 21.05           N  
ATOM   2249  CA  PRO A 295      33.913  19.525  39.022  1.00 21.06           C  
ATOM   2250  C   PRO A 295      32.760  20.000  38.100  1.00 20.53           C  
ATOM   2251  O   PRO A 295      31.611  19.653  38.293  1.00 20.01           O  
ATOM   2252  CB  PRO A 295      34.397  18.133  38.650  1.00 20.95           C  
ATOM   2253  CG  PRO A 295      33.538  17.197  39.523  1.00 21.49           C  
ATOM   2254  CD  PRO A 295      33.344  17.937  40.788  1.00 20.87           C  
ATOM   2255  N   VAL A 296      33.081  20.858  37.144  1.00 21.25           N  
ATOM   2256  CA  VAL A 296      32.162  21.186  36.056  1.00 20.67           C  
ATOM   2257  C   VAL A 296      32.770  20.589  34.798  1.00 21.82           C  
ATOM   2258  O   VAL A 296      34.000  20.698  34.611  1.00 22.10           O  
ATOM   2259  CB  VAL A 296      32.007  22.703  35.869  1.00 20.27           C  
ATOM   2260  CG1 VAL A 296      31.249  23.003  34.545  1.00 17.58           C  
ATOM   2261  CG2 VAL A 296      31.210  23.330  37.060  1.00 17.84           C  
ATOM   2262  N   TYR A 297      31.938  19.999  33.932  1.00 22.79           N  
ATOM   2263  CA  TYR A 297      32.372  19.609  32.573  1.00 23.91           C  
ATOM   2264  C   TYR A 297      31.445  20.102  31.472  1.00 24.63           C  
ATOM   2265  O   TYR A 297      30.239  20.059  31.605  1.00 26.19           O  
ATOM   2266  CB  TYR A 297      32.454  18.082  32.425  1.00 23.46           C  
ATOM   2267  CG  TYR A 297      33.243  17.346  33.486  1.00 25.08           C  
ATOM   2268  CD1 TYR A 297      32.608  16.830  34.621  1.00 23.18           C  
ATOM   2269  CD2 TYR A 297      34.626  17.098  33.332  1.00 25.36           C  
ATOM   2270  CE1 TYR A 297      33.334  16.126  35.605  1.00 24.39           C  
ATOM   2271  CE2 TYR A 297      35.343  16.369  34.307  1.00 23.83           C  
ATOM   2272  CZ  TYR A 297      34.687  15.909  35.427  1.00 23.10           C  
ATOM   2273  OH  TYR A 297      35.357  15.234  36.414  1.00 29.47           O  
ATOM   2274  N   LEU A 298      32.009  20.551  30.365  1.00 25.52           N  
ATOM   2275  CA  LEU A 298      31.248  20.762  29.148  1.00 24.89           C  
ATOM   2276  C   LEU A 298      31.192  19.413  28.407  1.00 24.75           C  
ATOM   2277  O   LEU A 298      32.197  18.757  28.278  1.00 25.16           O  
ATOM   2278  CB  LEU A 298      31.933  21.826  28.308  1.00 24.04           C  
ATOM   2279  CG  LEU A 298      31.228  22.240  27.016  1.00 26.10           C  
ATOM   2280  CD1 LEU A 298      29.891  22.960  27.292  1.00 22.85           C  
ATOM   2281  CD2 LEU A 298      32.206  23.097  26.206  1.00 24.01           C  
ATOM   2282  N   ILE A 299      29.999  18.970  28.007  1.00 25.33           N  
ATOM   2283  CA  ILE A 299      29.818  17.742  27.231  1.00 24.12           C  
ATOM   2284  C   ILE A 299      30.119  18.098  25.790  1.00 25.62           C  
ATOM   2285  O   ILE A 299      29.519  19.034  25.228  1.00 23.10           O  
ATOM   2286  CB  ILE A 299      28.363  17.225  27.336  1.00 24.71           C  
ATOM   2287  CG1 ILE A 299      28.017  16.821  28.787  1.00 23.33           C  
ATOM   2288  CG2 ILE A 299      28.091  16.028  26.357  1.00 21.05           C  
ATOM   2289  CD1 ILE A 299      26.534  16.773  29.054  1.00 24.26           C  
ATOM   2290  N   VAL A 300      31.073  17.381  25.186  1.00 26.98           N  
ATOM   2291  CA  VAL A 300      31.376  17.616  23.771  1.00 28.91           C  
ATOM   2292  C   VAL A 300      31.176  16.381  22.900  1.00 30.33           C  
ATOM   2293  O   VAL A 300      31.601  16.360  21.776  1.00 31.52           O  
ATOM   2294  CB  VAL A 300      32.796  18.295  23.519  1.00 28.82           C  
ATOM   2295  CG1 VAL A 300      32.851  19.697  24.091  1.00 27.44           C  
ATOM   2296  CG2 VAL A 300      33.956  17.405  24.044  1.00 30.04           C  
ATOM   2297  N   HIS A 301      30.517  15.350  23.412  1.00 33.01           N  
ATOM   2298  CA  HIS A 301      30.019  14.268  22.551  1.00 33.93           C  
ATOM   2299  C   HIS A 301      29.249  14.798  21.352  1.00 35.15           C  
ATOM   2300  O   HIS A 301      28.602  15.849  21.421  1.00 35.34           O  
ATOM   2301  CB  HIS A 301      29.120  13.358  23.341  1.00 33.97           C  
ATOM   2302  CG  HIS A 301      29.100  11.945  22.853  1.00 32.85           C  
ATOM   2303  ND1 HIS A 301      28.395  11.551  21.734  1.00 33.27           N  
ATOM   2304  CD2 HIS A 301      29.635  10.820  23.377  1.00 32.95           C  
ATOM   2305  CE1 HIS A 301      28.530  10.250  21.564  1.00 30.12           C  
ATOM   2306  NE2 HIS A 301      29.269   9.779  22.556  1.00 36.59           N  
ATOM   2307  N   ASP A 302      29.351  14.079  20.233  1.00 36.20           N  
ATOM   2308  CA  ASP A 302      28.665  14.455  19.000  1.00 36.80           C  
ATOM   2309  C   ASP A 302      27.176  14.049  19.034  1.00 34.93           C  
ATOM   2310  O   ASP A 302      26.319  14.644  18.357  1.00 34.34           O  
ATOM   2311  CB  ASP A 302      29.377  13.761  17.805  1.00 38.68           C  
ATOM   2312  CG  ASP A 302      30.907  14.021  17.794  1.00 44.05           C  
ATOM   2313  OD1 ASP A 302      31.698  13.072  17.501  1.00 49.74           O  
ATOM   2314  OD2 ASP A 302      31.406  15.140  18.096  1.00 47.30           O  
ATOM   2315  N   ASN A 303      26.867  13.017  19.801  1.00 32.36           N  
ATOM   2316  CA  ASN A 303      25.493  12.536  19.801  1.00 31.29           C  
ATOM   2317  C   ASN A 303      25.100  12.000  21.136  1.00 29.71           C  
ATOM   2318  O   ASN A 303      24.821  10.815  21.225  1.00 28.86           O  
ATOM   2319  CB  ASN A 303      25.284  11.461  18.738  1.00 31.23           C  
ATOM   2320  CG  ASN A 303      25.069  12.046  17.379  1.00 32.42           C  
ATOM   2321  OD1 ASN A 303      25.874  11.831  16.484  1.00 38.17           O  
ATOM   2322  ND2 ASN A 303      23.999  12.821  17.214  1.00 29.33           N  
ATOM   2323  N   PRO A 304      25.066  12.884  22.155  1.00 28.70           N  
ATOM   2324  CA  PRO A 304      24.744  12.473  23.535  1.00 27.52           C  
ATOM   2325  C   PRO A 304      23.259  12.130  23.683  1.00 26.99           C  
ATOM   2326  O   PRO A 304      22.938  11.300  24.546  1.00 28.02           O  
ATOM   2327  CB  PRO A 304      25.122  13.711  24.379  1.00 27.70           C  
ATOM   2328  CG  PRO A 304      24.958  14.909  23.390  1.00 28.06           C  
ATOM   2329  CD  PRO A 304      25.306  14.346  22.035  1.00 26.77           C  
ATOM   2330  N   GLY A 305      22.373  12.716  22.865  1.00 25.35           N  
ATOM   2331  CA  GLY A 305      20.987  12.263  22.843  1.00 24.83           C  
ATOM   2332  C   GLY A 305      20.829  10.785  22.469  1.00 24.75           C  
ATOM   2333  O   GLY A 305      20.087  10.036  23.124  1.00 25.80           O  
ATOM   2334  N   LEU A 306      21.512  10.334  21.426  1.00 23.68           N  
ATOM   2335  CA  LEU A 306      21.444   8.922  21.064  1.00 23.48           C  
ATOM   2336  C   LEU A 306      22.049   8.013  22.124  1.00 23.52           C  
ATOM   2337  O   LEU A 306      21.498   6.938  22.435  1.00 23.29           O  
ATOM   2338  CB  LEU A 306      22.087   8.648  19.701  1.00 23.85           C  
ATOM   2339  CG  LEU A 306      21.527   9.349  18.467  1.00 24.27           C  
ATOM   2340  CD1 LEU A 306      22.471   9.146  17.296  1.00 25.27           C  
ATOM   2341  CD2 LEU A 306      20.105   8.864  18.126  1.00 19.64           C  
ATOM   2342  N   LEU A 307      23.165   8.433  22.707  1.00 23.65           N  
ATOM   2343  CA  LEU A 307      23.830   7.627  23.752  1.00 22.97           C  
ATOM   2344  C   LEU A 307      22.971   7.519  25.032  1.00 22.91           C  
ATOM   2345  O   LEU A 307      22.794   6.397  25.646  1.00 21.90           O  
ATOM   2346  CB  LEU A 307      25.141   8.292  24.072  1.00 22.83           C  
ATOM   2347  CG  LEU A 307      26.562   7.750  24.324  1.00 27.23           C  
ATOM   2348  CD1 LEU A 307      27.266   8.509  25.492  1.00 22.52           C  
ATOM   2349  CD2 LEU A 307      26.739   6.212  24.398  1.00 28.41           C  
ATOM   2350  N   GLY A 308      22.434   8.684  25.444  1.00 22.55           N  
ATOM   2351  CA  GLY A 308      21.488   8.764  26.558  1.00 21.04           C  
ATOM   2352  C   GLY A 308      20.191   8.004  26.302  1.00 21.23           C  
ATOM   2353  O   GLY A 308      19.669   7.342  27.209  1.00 20.84           O  
ATOM   2354  N   SER A 309      19.681   8.047  25.070  1.00 20.66           N  
ATOM   2355  CA  SER A 309      18.524   7.182  24.722  1.00 21.83           C  
ATOM   2356  C   SER A 309      18.874   5.715  24.909  1.00 20.89           C  
ATOM   2357  O   SER A 309      18.092   4.957  25.470  1.00 21.33           O  
ATOM   2358  CB  SER A 309      18.002   7.457  23.275  1.00 21.45           C  
ATOM   2359  OG  SER A 309      17.460   8.774  23.229  1.00 21.71           O  
ATOM   2360  N   GLY A 310      20.067   5.320  24.473  1.00 21.58           N  
ATOM   2361  CA  GLY A 310      20.521   3.951  24.657  1.00 21.64           C  
ATOM   2362  C   GLY A 310      20.602   3.597  26.128  1.00 22.52           C  
ATOM   2363  O   GLY A 310      20.063   2.576  26.566  1.00 22.55           O  
ATOM   2364  N   ALA A 311      21.246   4.460  26.913  1.00 21.96           N  
ATOM   2365  CA  ALA A 311      21.355   4.193  28.343  1.00 22.53           C  
ATOM   2366  C   ALA A 311      19.995   4.050  29.057  1.00 23.66           C  
ATOM   2367  O   ALA A 311      19.804   3.135  29.872  1.00 24.40           O  
ATOM   2368  CB  ALA A 311      22.215   5.253  29.022  1.00 21.44           C  
ATOM   2369  N   HIS A 312      19.072   4.979  28.801  1.00 22.82           N  
ATOM   2370  CA  HIS A 312      17.731   4.866  29.354  1.00 23.20           C  
ATOM   2371  C   HIS A 312      17.026   3.520  28.998  1.00 22.15           C  
ATOM   2372  O   HIS A 312      16.497   2.819  29.853  1.00 22.53           O  
ATOM   2373  CB  HIS A 312      16.858   6.045  28.882  1.00 21.83           C  
ATOM   2374  CG  HIS A 312      15.419   5.847  29.190  1.00 23.21           C  
ATOM   2375  ND1 HIS A 312      14.913   5.964  30.466  1.00 26.72           N  
ATOM   2376  CD2 HIS A 312      14.394   5.425  28.414  1.00 25.94           C  
ATOM   2377  CE1 HIS A 312      13.620   5.718  30.452  1.00 25.93           C  
ATOM   2378  NE2 HIS A 312      13.280   5.372  29.219  1.00 28.19           N  
ATOM   2379  N   LEU A 313      17.029   3.189  27.724  1.00 22.55           N  
ATOM   2380  CA  LEU A 313      16.507   1.920  27.265  1.00 22.91           C  
ATOM   2381  C   LEU A 313      17.209   0.712  27.932  1.00 24.02           C  
ATOM   2382  O   LEU A 313      16.548  -0.206  28.409  1.00 24.68           O  
ATOM   2383  CB  LEU A 313      16.609   1.829  25.748  1.00 21.50           C  
ATOM   2384  CG  LEU A 313      15.907   0.581  25.159  1.00 22.25           C  
ATOM   2385  CD1 LEU A 313      14.396   0.519  25.544  1.00 17.03           C  
ATOM   2386  CD2 LEU A 313      16.092   0.473  23.631  1.00 18.70           C  
ATOM   2387  N   ARG A 314      18.533   0.707  27.975  1.00 24.52           N  
ATOM   2388  CA  ARG A 314      19.227  -0.438  28.563  1.00 25.56           C  
ATOM   2389  C   ARG A 314      18.909  -0.616  30.039  1.00 26.51           C  
ATOM   2390  O   ARG A 314      18.899  -1.737  30.511  1.00 27.92           O  
ATOM   2391  CB  ARG A 314      20.735  -0.374  28.315  1.00 23.82           C  
ATOM   2392  CG  ARG A 314      21.091  -0.559  26.865  1.00 27.34           C  
ATOM   2393  CD  ARG A 314      22.591  -0.372  26.510  1.00 29.45           C  
ATOM   2394  NE  ARG A 314      23.384  -1.427  27.157  1.00 33.08           N  
ATOM   2395  CZ  ARG A 314      24.269  -1.224  28.110  1.00 32.53           C  
ATOM   2396  NH1 ARG A 314      24.531   0.010  28.517  1.00 29.94           N  
ATOM   2397  NH2 ARG A 314      24.926  -2.259  28.617  1.00 32.55           N  
ATOM   2398  N   GLN A 315      18.652   0.463  30.777  1.00 26.54           N  
ATOM   2399  CA  GLN A 315      18.244   0.322  32.195  1.00 27.36           C  
ATOM   2400  C   GLN A 315      16.803  -0.180  32.300  1.00 27.77           C  
ATOM   2401  O   GLN A 315      16.473  -0.995  33.171  1.00 27.05           O  
ATOM   2402  CB  GLN A 315      18.338   1.650  32.961  1.00 26.90           C  
ATOM   2403  CG  GLN A 315      19.744   2.117  33.278  1.00 27.90           C  
ATOM   2404  CD  GLN A 315      19.743   3.248  34.312  1.00 30.71           C  
ATOM   2405  OE1 GLN A 315      18.805   4.077  34.354  1.00 33.10           O  
ATOM   2406  NE2 GLN A 315      20.780   3.311  35.106  1.00 25.46           N  
ATOM   2407  N   THR A 316      15.947   0.326  31.416  1.00 28.36           N  
ATOM   2408  CA  THR A 316      14.581  -0.190  31.318  1.00 30.01           C  
ATOM   2409  C   THR A 316      14.574  -1.703  31.034  1.00 31.32           C  
ATOM   2410  O   THR A 316      13.676  -2.396  31.513  1.00 32.54           O  
ATOM   2411  CB  THR A 316      13.769   0.529  30.192  1.00 29.89           C  
ATOM   2412  OG1 THR A 316      13.722   1.942  30.428  1.00 29.46           O  
ATOM   2413  CG2 THR A 316      12.310   0.102  30.246  1.00 28.53           C  
ATOM   2414  N   LEU A 317      15.538  -2.205  30.252  1.00 31.48           N  
ATOM   2415  CA  LEU A 317      15.611  -3.638  29.973  1.00 32.53           C  
ATOM   2416  C   LEU A 317      16.330  -4.460  31.071  1.00 33.80           C  
ATOM   2417  O   LEU A 317      16.567  -5.658  30.870  1.00 33.93           O  
ATOM   2418  CB  LEU A 317      16.287  -3.891  28.636  1.00 32.34           C  
ATOM   2419  CG  LEU A 317      15.650  -3.225  27.399  1.00 35.00           C  
ATOM   2420  CD1 LEU A 317      16.555  -3.435  26.183  1.00 33.80           C  
ATOM   2421  CD2 LEU A 317      14.247  -3.774  27.138  1.00 36.46           C  
ATOM   2422  N   GLY A 318      16.709  -3.820  32.188  1.00 33.48           N  
ATOM   2423  CA  GLY A 318      17.385  -4.496  33.285  1.00 34.01           C  
ATOM   2424  C   GLY A 318      18.906  -4.514  33.272  1.00 34.66           C  
ATOM   2425  O   GLY A 318      19.517  -5.254  34.036  1.00 35.45           O  
ATOM   2426  N   HIS A 319      19.544  -3.729  32.413  1.00 33.61           N  
ATOM   2427  CA  HIS A 319      20.971  -3.609  32.477  1.00 33.17           C  
ATOM   2428  C   HIS A 319      21.426  -2.538  33.480  1.00 33.18           C  
ATOM   2429  O   HIS A 319      20.756  -1.535  33.663  1.00 32.53           O  
ATOM   2430  CB  HIS A 319      21.483  -3.233  31.102  1.00 33.74           C  
ATOM   2431  CG  HIS A 319      21.473  -4.365  30.123  1.00 36.79           C  
ATOM   2432  ND1 HIS A 319      20.309  -4.852  29.555  1.00 33.50           N  
ATOM   2433  CD2 HIS A 319      22.491  -5.103  29.611  1.00 38.03           C  
ATOM   2434  CE1 HIS A 319      20.610  -5.855  28.750  1.00 38.69           C  
ATOM   2435  NE2 HIS A 319      21.925  -6.030  28.767  1.00 40.86           N  
ATOM   2436  N   ILE A 320      22.603  -2.740  34.072  1.00 33.64           N  
ATOM   2437  CA  ILE A 320      23.330  -1.710  34.847  1.00 33.53           C  
ATOM   2438  C   ILE A 320      24.403  -1.063  33.945  1.00 33.40           C  
ATOM   2439  O   ILE A 320      25.214  -1.744  33.273  1.00 34.18           O  
ATOM   2440  CB  ILE A 320      23.985  -2.357  36.132  1.00 34.29           C  
ATOM   2441  CG1 ILE A 320      22.912  -2.895  37.093  1.00 34.56           C  
ATOM   2442  CG2 ILE A 320      24.897  -1.372  36.864  1.00 32.13           C  
ATOM   2443  CD1 ILE A 320      23.369  -4.157  37.903  1.00 39.55           C  
ATOM   2444  N   LEU A 321      24.413   0.249  33.911  1.00 32.22           N  
ATOM   2445  CA  LEU A 321      25.250   0.932  32.991  1.00 32.11           C  
ATOM   2446  C   LEU A 321      26.754   0.725  33.312  1.00 33.92           C  
ATOM   2447  O   LEU A 321      27.138   0.675  34.489  1.00 35.19           O  
ATOM   2448  CB  LEU A 321      24.867   2.410  32.957  1.00 31.89           C  
ATOM   2449  CG  LEU A 321      23.406   2.690  32.591  1.00 29.09           C  
ATOM   2450  CD1 LEU A 321      23.177   4.156  32.464  1.00 24.69           C  
ATOM   2451  CD2 LEU A 321      23.060   1.962  31.297  1.00 26.80           C  
TER    2452      LEU A 321                                                      
CONECT  538  541                                                                
CONECT  541  538  542                                                           
CONECT  542  541  543  545                                                      
CONECT  543  542  544  549                                                      
CONECT  544  543                                                                
CONECT  545  542  546                                                           
CONECT  546  545  547                                                           
CONECT  547  546  548                                                           
CONECT  548  547                                                                
CONECT  549  543                                                                
CONECT  632  639                                                                
CONECT  639  632  640                                                           
CONECT  640  639  641  643                                                      
CONECT  641  640  642  647                                                      
CONECT  642  641                                                                
CONECT  643  640  644                                                           
CONECT  644  643  645                                                           
CONECT  645  644  646                                                           
CONECT  646  645                                                                
CONECT  647  641                                                                
CONECT  801  805                                                                
CONECT  805  801  806                                                           
CONECT  806  805  807  809                                                      
CONECT  807  806  808  813                                                      
CONECT  808  807                                                                
CONECT  809  806  810                                                           
CONECT  810  809  811                                                           
CONECT  811  810  812                                                           
CONECT  812  811                                                                
CONECT  813  807                                                                
CONECT  828  833                                                                
CONECT  833  828  834                                                           
CONECT  834  833  835  837                                                      
CONECT  835  834  836  841                                                      
CONECT  836  835                                                                
CONECT  837  834  838                                                           
CONECT  838  837  839                                                           
CONECT  839  838  840                                                           
CONECT  840  839                                                                
CONECT  841  835                                                                
CONECT 1821 1827                                                                
CONECT 1827 1821 1828                                                           
CONECT 1828 1827 1829 1831                                                      
CONECT 1829 1828 1830 1835                                                      
CONECT 1830 1829                                                                
CONECT 1831 1828 1832                                                           
CONECT 1832 1831 1833                                                           
CONECT 1833 1832 1834                                                           
CONECT 1834 1833                                                                
CONECT 1835 1829                                                                
MASTER      385    0   10   36   26    0    0    6 5295    2  104   52          
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.