path: root/plip/test/pdb/1bma.pdb

HEADER    HYDROLASE/HYDROLASE INHIBITOR           01-MAY-95   1BMA              
TITLE     BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC     
TITLE    2 ELASTASE                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHYMOTRYPSIN-LIKE ELASTASE FAMILY MEMBER 1;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ELASTASE-1;                                                 
COMPND   5 EC: 3.4.21.36                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIGS,SWINE,WILD BOAR;                               
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: PANCREAS                                                      
KEYWDS    SERINE PROTEASE,METAL-BINDING, PROTEASE, SECRETED, ZYMOGEN,           
KEYWDS   2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.PEISACH,D.CASEBIER,S.L.GALLION,P.FURTH,G.A.PETSKO,J.C.HOGAN JR.,    
AUTHOR   2 D.RINGE                                                              
REVDAT   4   13-JUL-11 1BMA    1       VERSN                                    
REVDAT   3   24-FEB-09 1BMA    1       VERSN                                    
REVDAT   2   01-APR-03 1BMA    1       JRNL                                     
REVDAT   1   07-DEC-95 1BMA    0                                                
JRNL        AUTH   E.PEISACH,D.CASEBIER,S.L.GALLION,P.FURTH,G.A.PETSKO,         
JRNL        AUTH 2 J.C.HOGAN JR.,D.RINGE                                        
JRNL        TITL   INTERACTION OF A PEPTIDOMIMETIC AMINIMIDE INHIBITOR WITH     
JRNL        TITL 2 ELASTASE.                                                    
JRNL        REF    SCIENCE                       V. 269    66 1995              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   7604279                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.MATTOS,D.A.GIAMMONA,G.A.PETSKO,D.RINGE                     
REMARK   1  TITL   STRUCTURAL ANALYSIS OF THE ACTIVE SITE OF PORCINE PANCREATIC 
REMARK   1  TITL 2 ELASTASE BASED ON THE X-RAY CRYSTAL STRUCTURES OF COMPLEXES  
REMARK   1  TITL 3 WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS            
REMARK   1  REF    BIOCHEMISTRY                  V.  34  3193 1995              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   I.LI DE LA SIERRA,E.PAPAMICHAEL,C.SAKARELOS,J.-L.DIMICOLI,   
REMARK   1  AUTH 2 T.PRANGE                                                     
REMARK   1  TITL   INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3 (TFLA)    
REMARK   1  TITL 2 WITH PORCINE PANCREATIC ELASTASE. X-RAY STUDIES AT 1.8       
REMARK   1  TITL 3 ANGSTROMS                                                    
REMARK   1  REF    J.MOL.RECOG.                  V.   3    36 1990              
REMARK   1  REFN                   ISSN 0952-3499                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   E.MEYER,G.COLE,R.RADHAKRISHNAN,O.EPP                         
REMARK   1  TITL   STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT 1.65      
REMARK   1  TITL 2 ANGSTROMS RESOLUTION                                         
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.B      V.  44    26 1988              
REMARK   1  REFN                   ISSN 0108-7681                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   E.MEYER,R.RADHAKRISHNAN,G.COLE,L.G.PRESTA                    
REMARK   1  TITL   STRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH  
REMARK   1  TITL 2 PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTION     
REMARK   1  REF    J.MOL.BIOL.                   V. 189   533 1986              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   D.L.HUGHES,L.C.DIECKER,L.C.BIETH,J.-L.DIMICOLI               
REMARK   1  TITL   CRYSTALLOGRAPHIC STUDY OF THE BINDING OF A TRI-FLUOROACETYL  
REMARK   1  TITL 2 DIPEPTIDE ANILIDE INHIBITOR WITH ELASTASE                    
REMARK   1  REF    J.MOL.BIOL.                   V. 162   645 1982              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   J.-L.DIMICOLI,A.RENAUD,J.BIETH                               
REMARK   1  TITL   THE INDIRECT MECHANISM OF ACTION OF THE TRIFLUOROACETYL      
REMARK   1  TITL 2 PEPTIDES ON ELASTASE                                         
REMARK   1  REF    EUR.J.BIOCHEM.                V. 107   423 1980              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   L.SAWYER,C.M.SHOTTON,J.W.CAMPBELL,P.L.WENDELL,H.MUIRHEAD,    
REMARK   1  AUTH 2 H.C.WATSON,R.DIAMOND,R.C.LADNER                              
REMARK   1  TITL   THE ATOMIC STRUCTURE OF CRYSTALLINE PORCINE PANCREATIC       
REMARK   1  TITL 2 ELASTASE AT 2.5 ANGSTROMS RESOLUTION. COMPARISONS WITH THE   
REMARK   1  TITL 3 STRUCTURE OF ALPHA-CHYMOTRYPSIN                              
REMARK   1  REF    J.MOL.BIOL.                   V. 118   137 1978              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 58.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 44505                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1822                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 134                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.01                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-94                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5148                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39545                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 58.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> 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  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE INHIBITOR WAS SOAKED INTO THE        
REMARK 280  GROWN CRYSTALS USING A 4 MM STOCK SOLUTION OF THE INHIBITOR IN      
REMARK 280  10% ACETONITRILE.                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.08000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.76000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.84000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.76000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.08000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.84000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    HIS A  60   NE2   HIS A  60   CD2    -0.073                       
REMARK 500    HIS A  75   NE2   HIS A  75   CD2    -0.070                       
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    TRP A  27   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP A  27   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A  36   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    TRP A  41   CD1 -  CG  -  CD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    TRP A  41   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A  51   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    TRP A  54   CD1 -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    TRP A  54   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A  64   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    TRP A  98   CD1 -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    TRP A  98   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    TRP A 147   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP A 147   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 151   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG A 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    TRP A 179   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP A 179   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A 226   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 240   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    TRP A 247   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    TRP A 247   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 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    HIS A  75      -55.40   -129.50                                   
REMARK 500    TYR A 178     -113.73   -104.95                                   
REMARK 500    SER A 203      135.31    -37.60                                   
REMARK 500    SER A 222      -56.81   -120.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 NOTE THAT SUBCOMPONENT MBH IS REFERRED TO AS MBA IN THE PAPER        
REMARK 600 CITED IN THE JRNL RECORDS ABOVE.                                     
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 280  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  84   OE2                                                    
REMARK 620 2 GLN A  79   O    93.3                                              
REMARK 620 3 HOH A 355   O    84.6  90.9                                        
REMARK 620 4 ASN A  81   OD1  83.2  93.3 167.3                                  
REMARK 620 5 GLU A  74   OE1  94.5 163.5 104.3  73.2                            
REMARK 620 6 ASN A  76   O   169.8  87.8 105.6  86.5  82.0                      
REMARK 620 7 GLU A  74   OE2  95.9 150.8  62.5 115.3  42.2  88.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: (1R)-1-BENZYL-1-METHYL-1-(2-{[4-(1-METHYLETHYL)       
REMARK 630 PHENYL]AMINO}-2-OXOETHYL)-2-{(2S)-4-METHYL-2-[(TRIFLUOROACETYL)      
REMARK 630 AMINO]PENTANOYL}DIAZANIUM                                            
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     0QH A   256                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    TFA LEU MBH ISO                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEETS PRESENTED AS *S1* AND *S2* IN SHEET RECORDS               
REMARK 700 BELOW ARE ACTUALLY TWO SIX-STRANDED BETA-BARRELS.  THIS IS           
REMARK 700 REPRESENTED BY TWO SEVEN-STRANDED SHEETS IN WHICH THE FIRST          
REMARK 700 AND LAST STRANDS OF EACH SHEET ARE IDENTICAL.                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 280                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QH A 256                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD                                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE RESIDUE NUMBERING SCHEME FOR THE PROTEIN IS SEQUENTIAL           
REMARK 999 STARTING WITH VAL A 16 AND ENDING WITH ASN A 255.                    
REMARK 999                                                                      
REMARK 999 THE IDENTITY OF ASN A 81 AGREES WITH THE SEQUENCES OF                
REMARK 999 SEVERAL OTHER ELASTASE STRUCTURES.  THE AUTHORS, THEREFORE,          
REMARK 999 BELIEVE IT TO BE CORRECT.                                            
DBREF  1BMA A   16   255  UNP    P00772   CELA1_PIG       27    266             
SEQADV 1BMA ASN A   81  UNP  P00772    ASP    92 CONFLICT                       
SEQRES   1 A  240  VAL VAL GLY GLY THR GLU ALA GLN ARG ASN SER TRP PRO          
SEQRES   2 A  240  SER GLN ILE SER LEU GLN TYR ARG SER GLY SER SER TRP          
SEQRES   3 A  240  ALA HIS THR CYS GLY GLY THR LEU ILE ARG GLN ASN TRP          
SEQRES   4 A  240  VAL MET THR ALA ALA HIS CYS VAL ASP ARG GLU LEU THR          
SEQRES   5 A  240  PHE ARG VAL VAL VAL GLY GLU HIS ASN LEU ASN GLN ASN          
SEQRES   6 A  240  ASN GLY THR GLU GLN TYR VAL GLY VAL GLN LYS ILE VAL          
SEQRES   7 A  240  VAL HIS PRO TYR TRP ASN THR ASP ASP VAL ALA ALA GLY          
SEQRES   8 A  240  TYR ASP ILE ALA LEU LEU ARG LEU ALA GLN SER VAL THR          
SEQRES   9 A  240  LEU ASN SER TYR VAL GLN LEU GLY VAL LEU PRO ARG ALA          
SEQRES  10 A  240  GLY THR ILE LEU ALA ASN ASN SER PRO CYS TYR ILE THR          
SEQRES  11 A  240  GLY TRP GLY LEU THR ARG THR ASN GLY GLN LEU ALA GLN          
SEQRES  12 A  240  THR LEU GLN GLN ALA TYR LEU PRO THR VAL ASP TYR ALA          
SEQRES  13 A  240  ILE CYS SER SER SER SER TYR TRP GLY SER THR VAL LYS          
SEQRES  14 A  240  ASN SER MET VAL CYS ALA GLY GLY ASP GLY VAL ARG SER          
SEQRES  15 A  240  GLY CYS GLN GLY ASP SER GLY GLY PRO LEU HIS CYS LEU          
SEQRES  16 A  240  VAL ASN GLY GLN TYR ALA VAL HIS GLY VAL THR SER PHE          
SEQRES  17 A  240  VAL SER ARG LEU GLY CYS ASN VAL THR ARG LYS PRO THR          
SEQRES  18 A  240  VAL PHE THR ARG VAL SER ALA TYR ILE SER TRP ILE ASN          
SEQRES  19 A  240  ASN VAL ILE ALA SER ASN                                      
HET     CA  A 280       1                                                       
HET    SO4  A 290       5                                                       
HET    0QH  A 256      37                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     0QH (1R)-1-BENZYL-1-METHYL-1-(2-{[4-(1-METHYLETHYL)                  
HETNAM   2 0QH  PHENYL]AMINO}-2-OXOETHYL)-2-{(2S)-4-METHYL-2-                   
HETNAM   3 0QH  [(TRIFLUOROACETYL)AMINO]PENTANOYL}DIAZANIUM                     
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  0QH    C27 H36 F3 N4 O3 1+                                          
FORMUL   5  HOH   *134(H2 O)                                                    
HELIX    1  H1 ASP A  169  SER A  175  1                                   7    
HELIX    2  H2 TYR A  244  ASN A  255  1                                  12    
SHEET    1  S1 7 SER A  29  SER A  37  0                                        
SHEET    2  S1 7 SER A  40  ILE A  50 -1                                        
SHEET    3  S1 7 ASN A  53  ALA A  59 -1                                        
SHEET    4  S1 7 ASP A 108  GLN A 116 -1                                        
SHEET    5  S1 7 GLU A  84  HIS A  95 -1                                        
SHEET    6  S1 7 PHE A  68  GLY A  73 -1                                        
SHEET    7  S1 7 SER A  29  SER A  37 -1                                        
SHEET    1  S2 7 ASN A 139  THR A 150  0                                        
SHEET    2  S2 7 GLY A 154  VAL A 168 -1                                        
SHEET    3  S2 7 SER A 186  VAL A 195 -1                                        
SHEET    4  S2 7 ASN A 230  VAL A 241 -1                                        
SHEET    5  S2 7 HIS A 218  VAL A 224 -1                                        
SHEET    6  S2 7 SER A 203  CYS A 209 -1                                        
SHEET    7  S2 7 SER A 140  THR A 150 -1                                        
SHEET    1  S3 3 GLY A 154  ALA A 157  0                                        
SHEET    2  S3 3 TRP A 147  LEU A 149 -1                                        
SHEET    3  S3 3 GLN A 200  ASP A 202 -1                                        
SSBOND   1 CYS A   45    CYS A   61                          1555   1555  2.02  
SSBOND   2 CYS A  142    CYS A  209                          1555   1555  2.01  
SSBOND   3 CYS A  173    CYS A  189                          1555   1555  2.01  
SSBOND   4 CYS A  199    CYS A  229                          1555   1555  2.01  
LINK        CA    CA A 280                 OE2 GLU A  84     1555   1555  2.51  
LINK        CA    CA A 280                 O   GLN A  79     1555   1555  2.37  
LINK        CA    CA A 280                 O   HOH A 355     1555   1555  2.53  
LINK        CA    CA A 280                 OD1 ASN A  81     1555   1555  2.52  
LINK        CA    CA A 280                 OE1 GLU A  74     1555   1555  2.50  
LINK        CA    CA A 280                 O   ASN A  76     1555   1555  2.37  
LINK        CA    CA A 280                 OE2 GLU A  74     1555   1555  3.09  
SITE     1 AC1  6 GLU A  74  ASN A  76  GLN A  79  ASN A  81                    
SITE     2 AC1  6 GLU A  84  HOH A 355                                          
SITE     1 AC2  5 GLY A 133  ARG A 151  ARG A 240  HOH A 340                    
SITE     2 AC2  5 HOH A 345                                                     
SITE     1 AC3 17 GLU A  65  LEU A  66  THR A  67  VAL A 103                    
SITE     2 AC3 17 THR A 152  THR A 182  CYS A 199  GLN A 200                    
SITE     3 AC3 17 SER A 203  THR A 221  SER A 222  PHE A 223                    
SITE     4 AC3 17 VAL A 224  SER A 225  ARG A 226  GLY A 228                    
SITE     5 AC3 17 CYS A 229                                                     
SITE     1 CAT  3 ASP A 108  HIS A  60  SER A 203                               
CRYST1   52.160   57.680   75.520  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019172  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017337  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013242        0.00000                         
ATOM      1  N   VAL A  16      41.593  32.726  35.179  1.00  5.92           N  
ATOM      2  CA  VAL A  16      40.667  33.462  36.045  1.00  5.90           C  
ATOM      3  C   VAL A  16      39.544  34.005  35.167  1.00  9.05           C  
ATOM      4  O   VAL A  16      39.830  34.764  34.220  1.00 10.48           O  
ATOM      5  CB  VAL A  16      41.446  34.646  36.763  1.00  3.34           C  
ATOM      6  CG1 VAL A  16      40.479  35.497  37.575  1.00  5.02           C  
ATOM      7  CG2 VAL A  16      42.485  34.116  37.761  1.00  7.03           C  
ATOM      8  N   VAL A  17      38.276  33.667  35.460  1.00  9.38           N  
ATOM      9  CA  VAL A  17      37.124  34.221  34.774  1.00  8.32           C  
ATOM     10  C   VAL A  17      36.701  35.486  35.515  1.00 10.66           C  
ATOM     11  O   VAL A  17      36.731  35.504  36.741  1.00 10.27           O  
ATOM     12  CB  VAL A  17      35.956  33.225  34.766  1.00  6.81           C  
ATOM     13  CG1 VAL A  17      34.839  33.738  33.857  1.00  6.95           C  
ATOM     14  CG2 VAL A  17      36.405  31.908  34.179  1.00  7.97           C  
ATOM     15  N   GLY A  18      36.334  36.574  34.832  1.00  9.48           N  
ATOM     16  CA  GLY A  18      35.822  37.755  35.533  1.00 10.87           C  
ATOM     17  C   GLY A  18      36.915  38.523  36.270  1.00 12.24           C  
ATOM     18  O   GLY A  18      36.678  39.227  37.249  1.00 14.40           O  
ATOM     19  N   GLY A  19      38.145  38.374  35.824  1.00 12.48           N  
ATOM     20  CA  GLY A  19      39.268  39.043  36.456  1.00 14.94           C  
ATOM     21  C   GLY A  19      39.626  40.361  35.784  1.00 16.65           C  
ATOM     22  O   GLY A  19      38.950  40.814  34.852  1.00 18.12           O  
ATOM     23  N   THR A  20      40.656  41.023  36.329  1.00 17.53           N  
ATOM     24  CA  THR A  20      41.215  42.247  35.786  1.00 18.60           C  
ATOM     25  C   THR A  20      42.711  42.021  35.745  1.00 18.76           C  
ATOM     26  O   THR A  20      43.229  41.126  36.410  1.00 18.06           O  
ATOM     27  CB  THR A  20      40.854  43.488  36.671  1.00 18.53           C  
ATOM     28  OG1 THR A  20      41.161  43.234  38.028  1.00 21.90           O  
ATOM     29  CG2 THR A  20      39.362  43.783  36.615  1.00 20.28           C  
ATOM     30  N   GLU A  21      43.465  42.806  34.977  1.00 17.36           N  
ATOM     31  CA  GLU A  21      44.865  42.555  34.859  1.00 16.71           C  
ATOM     32  C   GLU A  21      45.574  42.977  36.145  1.00 17.00           C  
ATOM     33  O   GLU A  21      45.219  44.002  36.718  1.00 16.14           O  
ATOM     34  CB  GLU A  21      45.362  43.317  33.667  1.00 20.43           C  
ATOM     35  CG  GLU A  21      46.829  43.020  33.446  1.00 24.72           C  
ATOM     36  CD  GLU A  21      47.475  43.832  32.343  1.00 30.35           C  
ATOM     37  OE1 GLU A  21      46.815  44.064  31.332  1.00 32.22           O  
ATOM     38  OE2 GLU A  21      48.640  44.213  32.503  1.00 34.58           O  
ATOM     39  N   ALA A  22      46.507  42.201  36.690  1.00 13.57           N  
ATOM     40  CA  ALA A  22      47.254  42.613  37.877  1.00 16.53           C  
ATOM     41  C   ALA A  22      48.413  43.574  37.541  1.00 19.25           C  
ATOM     42  O   ALA A  22      48.936  43.546  36.410  1.00 19.34           O  
ATOM     43  CB  ALA A  22      47.850  41.387  38.565  1.00 12.65           C  
ATOM     44  N   GLN A  23      48.800  44.479  38.475  1.00 22.53           N  
ATOM     45  CA  GLN A  23      50.009  45.296  38.310  1.00 26.37           C  
ATOM     46  C   GLN A  23      51.263  44.409  38.378  1.00 27.67           C  
ATOM     47  O   GLN A  23      51.187  43.347  38.997  1.00 23.66           O  
ATOM     48  CB  GLN A  23      50.168  46.320  39.400  1.00 31.17           C  
ATOM     49  CG  GLN A  23      49.159  47.429  39.421  1.00 42.19           C  
ATOM     50  CD  GLN A  23      49.687  48.673  40.142  1.00 49.58           C  
ATOM     51  OE1 GLN A  23      50.904  48.913  40.285  1.00 52.36           O  
ATOM     52  NE2 GLN A  23      48.727  49.492  40.591  1.00 51.67           N  
ATOM     53  N   ARG A  24      52.431  44.788  37.800  1.00 29.51           N  
ATOM     54  CA  ARG A  24      53.641  43.953  37.789  1.00 30.30           C  
ATOM     55  C   ARG A  24      54.183  43.386  39.081  1.00 31.38           C  
ATOM     56  O   ARG A  24      54.587  42.235  39.151  1.00 34.00           O  
ATOM     57  CB  ARG A  24      54.840  44.668  37.206  1.00 30.16           C  
ATOM     58  CG  ARG A  24      54.679  44.883  35.770  1.00 28.35           C  
ATOM     59  CD  ARG A  24      55.881  45.609  35.209  1.00 27.43           C  
ATOM     60  NE  ARG A  24      55.515  45.740  33.820  1.00 28.29           N  
ATOM     61  CZ  ARG A  24      55.724  44.756  32.944  1.00 28.28           C  
ATOM     62  NH1 ARG A  24      56.320  43.610  33.293  1.00 27.96           N  
ATOM     63  NH2 ARG A  24      55.172  44.852  31.736  1.00 28.73           N  
ATOM     64  N   ASN A  25      54.279  44.201  40.117  1.00 32.39           N  
ATOM     65  CA  ASN A  25      54.869  43.760  41.380  1.00 33.61           C  
ATOM     66  C   ASN A  25      53.824  43.580  42.473  1.00 31.97           C  
ATOM     67  O   ASN A  25      54.141  43.602  43.671  1.00 29.55           O  
ATOM     68  CB  ASN A  25      55.929  44.795  41.809  1.00 37.80           C  
ATOM     69  CG  ASN A  25      55.409  46.225  41.994  1.00 40.56           C  
ATOM     70  OD1 ASN A  25      54.300  46.613  41.600  1.00 42.11           O  
ATOM     71  ND2 ASN A  25      56.249  47.031  42.633  1.00 44.06           N  
ATOM     72  N   SER A  26      52.568  43.425  42.030  1.00 28.95           N  
ATOM     73  CA  SER A  26      51.480  43.244  42.956  1.00 27.48           C  
ATOM     74  C   SER A  26      51.550  41.881  43.640  1.00 24.98           C  
ATOM     75  O   SER A  26      51.345  41.838  44.862  1.00 24.86           O  
ATOM     76  CB  SER A  26      50.145  43.400  42.220  1.00 29.77           C  
ATOM     77  OG  SER A  26      49.576  44.692  42.384  1.00 32.18           O  
ATOM     78  N   TRP A  27      51.894  40.773  42.943  1.00 19.00           N  
ATOM     79  CA  TRP A  27      51.827  39.462  43.577  1.00 15.63           C  
ATOM     80  C   TRP A  27      53.117  38.694  43.339  1.00 13.92           C  
ATOM     81  O   TRP A  27      53.144  37.728  42.595  1.00 12.13           O  
ATOM     82  CB  TRP A  27      50.596  38.703  43.019  1.00 11.96           C  
ATOM     83  CG  TRP A  27      49.263  39.463  43.147  1.00 11.14           C  
ATOM     84  CD1 TRP A  27      48.655  40.009  42.035  1.00 11.57           C  
ATOM     85  CD2 TRP A  27      48.540  39.681  44.301  1.00 13.48           C  
ATOM     86  NE1 TRP A  27      47.556  40.562  42.482  1.00 10.27           N  
ATOM     87  CE2 TRP A  27      47.439  40.401  43.808  1.00 10.92           C  
ATOM     88  CE3 TRP A  27      48.623  39.397  45.681  1.00 13.18           C  
ATOM     89  CZ2 TRP A  27      46.423  40.836  44.680  1.00 10.34           C  
ATOM     90  CZ3 TRP A  27      47.605  39.840  46.538  1.00 11.90           C  
ATOM     91  CH2 TRP A  27      46.513  40.551  46.040  1.00 10.77           C  
ATOM     92  N   PRO A  28      54.229  39.090  43.951  1.00 11.86           N  
ATOM     93  CA  PRO A  28      55.548  38.663  43.566  1.00 12.64           C  
ATOM     94  C   PRO A  28      55.962  37.263  44.017  1.00 11.81           C  
ATOM     95  O   PRO A  28      57.054  36.803  43.660  1.00 11.52           O  
ATOM     96  CB  PRO A  28      56.413  39.809  44.089  1.00 14.52           C  
ATOM     97  CG  PRO A  28      55.730  40.196  45.376  1.00 12.82           C  
ATOM     98  CD  PRO A  28      54.281  40.117  44.984  1.00 11.25           C  
ATOM     99  N   SER A  29      55.096  36.568  44.781  1.00  9.76           N  
ATOM    100  CA  SER A  29      55.334  35.159  45.098  1.00  9.96           C  
ATOM    101  C   SER A  29      54.674  34.231  44.069  1.00  9.91           C  
ATOM    102  O   SER A  29      54.900  33.017  44.093  1.00  9.94           O  
ATOM    103  CB  SER A  29      54.789  34.832  46.503  1.00  8.62           C  
ATOM    104  OG  SER A  29      53.364  34.849  46.566  1.00 12.43           O  
ATOM    105  N   GLN A  30      53.845  34.765  43.154  1.00  8.00           N  
ATOM    106  CA  GLN A  30      53.241  33.980  42.087  1.00  8.57           C  
ATOM    107  C   GLN A  30      54.294  33.417  41.123  1.00 10.02           C  
ATOM    108  O   GLN A  30      55.207  34.132  40.697  1.00 10.78           O  
ATOM    109  CB  GLN A  30      52.264  34.846  41.275  1.00 10.17           C  
ATOM    110  CG  GLN A  30      51.653  34.201  40.027  1.00  8.01           C  
ATOM    111  CD  GLN A  30      50.507  33.288  40.306  1.00  9.07           C  
ATOM    112  OE1 GLN A  30      49.469  33.711  40.810  1.00 10.33           O  
ATOM    113  NE2 GLN A  30      50.621  32.014  39.953  1.00 10.31           N  
ATOM    114  N   ILE A  31      54.210  32.116  40.793  1.00  8.92           N  
ATOM    115  CA  ILE A  31      55.088  31.545  39.777  1.00  6.99           C  
ATOM    116  C   ILE A  31      54.240  30.889  38.673  1.00  7.32           C  
ATOM    117  O   ILE A  31      53.032  30.629  38.858  1.00  6.13           O  
ATOM    118  CB  ILE A  31      56.136  30.486  40.429  1.00  9.28           C  
ATOM    119  CG1 ILE A  31      55.501  29.162  40.903  1.00  7.00           C  
ATOM    120  CG2 ILE A  31      56.814  31.169  41.627  1.00  8.47           C  
ATOM    121  CD1 ILE A  31      55.220  28.102  39.818  1.00  8.11           C  
ATOM    122  N   SER A  32      54.850  30.664  37.482  1.00  8.48           N  
ATOM    123  CA  SER A  32      54.240  29.916  36.392  1.00  9.14           C  
ATOM    124  C   SER A  32      54.994  28.595  36.331  1.00  7.06           C  
ATOM    125  O   SER A  32      56.212  28.571  36.246  1.00  8.01           O  
ATOM    126  CB  SER A  32      54.410  30.660  35.057  1.00  9.53           C  
ATOM    127  OG  SER A  32      54.099  29.861  33.919  1.00 10.59           O  
ATOM    128  N   LEU A  33      54.275  27.494  36.373  1.00  9.59           N  
ATOM    129  CA  LEU A  33      54.858  26.166  36.265  1.00  9.76           C  
ATOM    130  C   LEU A  33      54.588  25.764  34.825  1.00 10.03           C  
ATOM    131  O   LEU A  33      53.451  25.728  34.380  1.00  8.61           O  
ATOM    132  CB  LEU A  33      54.176  25.127  37.197  1.00 10.56           C  
ATOM    133  CG  LEU A  33      54.678  23.658  37.079  1.00  9.91           C  
ATOM    134  CD1 LEU A  33      56.085  23.543  37.617  1.00  7.64           C  
ATOM    135  CD2 LEU A  33      53.734  22.732  37.820  1.00 12.30           C  
ATOM    136  N   GLN A  34      55.645  25.383  34.129  1.00 12.13           N  
ATOM    137  CA  GLN A  34      55.609  25.150  32.694  1.00 13.18           C  
ATOM    138  C   GLN A  34      56.151  23.795  32.353  1.00 11.91           C  
ATOM    139  O   GLN A  34      57.055  23.357  33.054  1.00 13.44           O  
ATOM    140  CB  GLN A  34      56.479  26.194  31.955  1.00 12.93           C  
ATOM    141  CG  GLN A  34      55.982  27.572  32.291  1.00 12.27           C  
ATOM    142  CD  GLN A  34      56.605  28.671  31.492  1.00 13.36           C  
ATOM    143  OE1 GLN A  34      57.616  28.521  30.808  1.00 13.40           O  
ATOM    144  NE2 GLN A  34      55.926  29.794  31.626  1.00 11.34           N  
ATOM    145  N   TYR A  35      55.675  23.147  31.306  1.00 11.44           N  
ATOM    146  CA  TYR A  35      56.313  21.907  30.895  1.00 14.14           C  
ATOM    147  C   TYR A  35      56.852  22.024  29.466  1.00 14.38           C  
ATOM    148  O   TYR A  35      56.391  22.859  28.695  1.00 13.75           O  
ATOM    149  CB  TYR A  35      55.327  20.761  30.987  1.00 13.02           C  
ATOM    150  CG  TYR A  35      54.128  20.842  30.062  1.00 19.19           C  
ATOM    151  CD1 TYR A  35      53.089  21.733  30.324  1.00 20.94           C  
ATOM    152  CD2 TYR A  35      54.087  20.023  28.922  1.00 22.45           C  
ATOM    153  CE1 TYR A  35      52.006  21.816  29.452  1.00 23.87           C  
ATOM    154  CE2 TYR A  35      52.999  20.103  28.049  1.00 22.05           C  
ATOM    155  CZ  TYR A  35      51.964  20.998  28.321  1.00 24.06           C  
ATOM    156  OH  TYR A  35      50.865  21.061  27.476  1.00 25.35           O  
ATOM    157  N   ARG A  36      57.832  21.217  29.075  1.00 16.04           N  
ATOM    158  CA  ARG A  36      58.391  21.298  27.740  1.00 19.73           C  
ATOM    159  C   ARG A  36      57.462  20.582  26.795  1.00 22.34           C  
ATOM    160  O   ARG A  36      56.908  19.520  27.036  1.00 22.37           O  
ATOM    161  CB  ARG A  36      59.757  20.698  27.755  1.00 21.39           C  
ATOM    162  CG  ARG A  36      60.578  21.142  26.575  1.00 24.73           C  
ATOM    163  CD  ARG A  36      62.004  20.688  26.765  1.00 30.91           C  
ATOM    164  NE  ARG A  36      62.103  19.297  27.236  1.00 38.05           N  
ATOM    165  CZ  ARG A  36      61.826  18.166  26.523  1.00 39.47           C  
ATOM    166  NH1 ARG A  36      61.391  18.177  25.242  1.00 43.28           N  
ATOM    167  NH2 ARG A  36      62.026  16.974  27.092  1.00 37.49           N  
ATOM    168  N   SER A  37      57.147  21.355  25.786  1.00 25.25           N  
ATOM    169  CA  SER A  37      56.184  20.971  24.794  1.00 32.58           C  
ATOM    170  C   SER A  37      56.928  21.157  23.477  1.00 37.49           C  
ATOM    171  O   SER A  37      57.067  22.276  22.947  1.00 38.55           O  
ATOM    172  CB  SER A  37      55.010  21.909  24.986  1.00 34.35           C  
ATOM    173  OG  SER A  37      53.918  21.576  24.154  1.00 39.18           O  
ATOM    174  N   GLY A  38      57.490  20.028  23.009  1.00 39.31           N  
ATOM    175  CA  GLY A  38      58.282  19.988  21.792  1.00 40.50           C  
ATOM    176  C   GLY A  38      59.594  20.740  21.968  1.00 42.41           C  
ATOM    177  O   GLY A  38      60.516  20.339  22.693  1.00 42.97           O  
ATOM    178  N   SER A  39      59.595  21.879  21.277  1.00 42.87           N  
ATOM    179  CA  SER A  39      60.731  22.796  21.262  1.00 44.46           C  
ATOM    180  C   SER A  39      60.594  23.962  22.239  1.00 43.55           C  
ATOM    181  O   SER A  39      61.551  24.647  22.607  1.00 45.39           O  
ATOM    182  CB  SER A  39      60.874  23.321  19.850  1.00 47.58           C  
ATOM    183  OG  SER A  39      59.583  23.585  19.282  1.00 51.23           O  
ATOM    184  N   SER A  40      59.345  24.174  22.644  1.00 41.15           N  
ATOM    185  CA  SER A  40      58.971  25.266  23.518  1.00 38.12           C  
ATOM    186  C   SER A  40      58.493  24.800  24.901  1.00 33.55           C  
ATOM    187  O   SER A  40      58.634  23.624  25.245  1.00 32.42           O  
ATOM    188  CB  SER A  40      57.905  26.050  22.768  1.00 40.19           C  
ATOM    189  OG  SER A  40      56.915  25.159  22.253  1.00 45.65           O  
ATOM    190  N   TRP A  41      57.967  25.752  25.687  1.00 27.38           N  
ATOM    191  CA  TRP A  41      57.496  25.523  27.043  1.00 22.42           C  
ATOM    192  C   TRP A  41      56.114  26.091  27.135  1.00 19.86           C  
ATOM    193  O   TRP A  41      55.904  27.195  26.677  1.00 21.58           O  
ATOM    194  CB  TRP A  41      58.348  26.242  28.014  1.00 22.39           C  
ATOM    195  CG  TRP A  41      59.743  25.673  28.140  1.00 23.61           C  
ATOM    196  CD1 TRP A  41      60.790  26.138  27.371  1.00 22.48           C  
ATOM    197  CD2 TRP A  41      60.106  24.685  29.028  1.00 24.55           C  
ATOM    198  NE1 TRP A  41      61.828  25.437  27.779  1.00 25.26           N  
ATOM    199  CE2 TRP A  41      61.481  24.564  28.756  1.00 25.15           C  
ATOM    200  CE3 TRP A  41      59.498  23.894  30.019  1.00 24.05           C  
ATOM    201  CZ2 TRP A  41      62.247  23.644  29.482  1.00 24.19           C  
ATOM    202  CZ3 TRP A  41      60.279  22.981  30.736  1.00 21.92           C  
ATOM    203  CH2 TRP A  41      61.635  22.859  30.471  1.00 23.76           C  
ATOM    204  N   ALA A  42      55.153  25.389  27.704  1.00 16.35           N  
ATOM    205  CA  ALA A  42      53.776  25.840  27.824  1.00 15.04           C  
ATOM    206  C   ALA A  42      53.388  25.995  29.315  1.00 14.44           C  
ATOM    207  O   ALA A  42      53.767  25.155  30.145  1.00 13.83           O  
ATOM    208  CB  ALA A  42      52.825  24.815  27.202  1.00 13.91           C  
ATOM    209  N   HIS A  43      52.632  27.039  29.679  1.00 11.49           N  
ATOM    210  CA  HIS A  43      52.146  27.185  31.048  1.00 12.37           C  
ATOM    211  C   HIS A  43      51.090  26.108  31.347  1.00 10.74           C  
ATOM    212  O   HIS A  43      50.169  25.878  30.566  1.00 11.37           O  
ATOM    213  CB  HIS A  43      51.548  28.584  31.205  1.00 12.11           C  
ATOM    214  CG  HIS A  43      50.789  28.830  32.491  1.00 11.84           C  
ATOM    215  ND1 HIS A  43      51.312  29.320  33.609  1.00 11.21           N  
ATOM    216  CD2 HIS A  43      49.454  28.549  32.701  1.00 12.94           C  
ATOM    217  CE1 HIS A  43      50.340  29.340  34.491  1.00 12.11           C  
ATOM    218  NE2 HIS A  43      49.227  28.879  33.948  1.00 10.55           N  
ATOM    219  N   THR A  44      51.215  25.400  32.464  1.00  9.11           N  
ATOM    220  CA  THR A  44      50.175  24.476  32.872  1.00  9.74           C  
ATOM    221  C   THR A  44      49.510  24.819  34.228  1.00  7.13           C  
ATOM    222  O   THR A  44      48.329  24.556  34.440  1.00  7.38           O  
ATOM    223  CB  THR A  44      50.822  23.066  32.851  1.00 10.48           C  
ATOM    224  OG1 THR A  44      49.727  22.191  32.998  1.00 14.23           O  
ATOM    225  CG2 THR A  44      51.867  22.787  33.920  1.00 12.75           C  
ATOM    226  N   CYS A  45      50.235  25.490  35.116  1.00  6.51           N  
ATOM    227  CA  CYS A  45      49.773  25.700  36.485  1.00  6.29           C  
ATOM    228  C   CYS A  45      50.423  26.923  37.125  1.00  5.70           C  
ATOM    229  O   CYS A  45      51.443  27.401  36.620  1.00  4.80           O  
ATOM    230  CB  CYS A  45      50.122  24.446  37.382  1.00  8.42           C  
ATOM    231  SG  CYS A  45      48.919  23.107  37.188  1.00 10.15           S  
ATOM    232  N   GLY A  46      49.794  27.434  38.193  1.00  6.07           N  
ATOM    233  CA  GLY A  46      50.444  28.450  38.978  1.00  7.86           C  
ATOM    234  C   GLY A  46      51.105  27.748  40.178  1.00 10.78           C  
ATOM    235  O   GLY A  46      51.065  26.510  40.318  1.00 11.22           O  
ATOM    236  N   GLY A  47      51.711  28.548  41.043  1.00  6.54           N  
ATOM    237  CA  GLY A  47      52.285  28.063  42.289  1.00  6.80           C  
ATOM    238  C   GLY A  47      52.661  29.272  43.136  1.00  7.93           C  
ATOM    239  O   GLY A  47      52.493  30.423  42.702  1.00  9.16           O  
ATOM    240  N   THR A  48      53.219  29.016  44.305  1.00  7.69           N  
ATOM    241  CA  THR A  48      53.681  30.047  45.215  1.00  8.22           C  
ATOM    242  C   THR A  48      55.117  29.798  45.606  1.00  9.03           C  
ATOM    243  O   THR A  48      55.466  28.710  46.049  1.00 10.78           O  
ATOM    244  CB  THR A  48      52.811  30.066  46.470  1.00 10.32           C  
ATOM    245  OG1 THR A  48      51.476  30.319  46.073  1.00  9.40           O  
ATOM    246  CG2 THR A  48      53.206  31.179  47.448  1.00  9.14           C  
ATOM    247  N   LEU A  49      56.018  30.767  45.471  1.00  9.93           N  
ATOM    248  CA  LEU A  49      57.386  30.650  45.934  1.00 10.04           C  
ATOM    249  C   LEU A  49      57.389  30.698  47.474  1.00 10.76           C  
ATOM    250  O   LEU A  49      56.894  31.661  48.042  1.00  9.70           O  
ATOM    251  CB  LEU A  49      58.216  31.805  45.323  1.00  9.80           C  
ATOM    252  CG  LEU A  49      59.709  31.758  45.631  1.00 12.10           C  
ATOM    253  CD1 LEU A  49      60.337  30.629  44.818  1.00 10.75           C  
ATOM    254  CD2 LEU A  49      60.348  33.111  45.320  1.00 12.86           C  
ATOM    255  N   ILE A  50      57.843  29.663  48.187  1.00 10.28           N  
ATOM    256  CA  ILE A  50      57.774  29.700  49.641  1.00 11.21           C  
ATOM    257  C   ILE A  50      59.150  29.768  50.263  1.00 10.60           C  
ATOM    258  O   ILE A  50      59.280  30.150  51.428  1.00 11.17           O  
ATOM    259  CB  ILE A  50      57.008  28.470  50.241  1.00 10.84           C  
ATOM    260  CG1 ILE A  50      57.635  27.146  49.819  1.00 12.83           C  
ATOM    261  CG2 ILE A  50      55.545  28.694  49.943  1.00  8.94           C  
ATOM    262  CD1 ILE A  50      56.887  25.953  50.437  1.00 19.56           C  
ATOM    263  N   ARG A  51      60.179  29.331  49.538  1.00 11.39           N  
ATOM    264  CA  ARG A  51      61.572  29.479  49.921  1.00 14.84           C  
ATOM    265  C   ARG A  51      62.311  29.843  48.642  1.00 14.15           C  
ATOM    266  O   ARG A  51      61.754  29.654  47.574  1.00 15.83           O  
ATOM    267  CB  ARG A  51      62.252  28.189  50.447  1.00 15.49           C  
ATOM    268  CG  ARG A  51      61.749  27.603  51.730  1.00 20.57           C  
ATOM    269  CD  ARG A  51      61.836  28.700  52.749  1.00 26.75           C  
ATOM    270  NE  ARG A  51      61.483  28.198  54.067  1.00 36.70           N  
ATOM    271  CZ  ARG A  51      60.229  28.103  54.521  1.00 40.23           C  
ATOM    272  NH1 ARG A  51      59.155  28.467  53.810  1.00 44.96           N  
ATOM    273  NH2 ARG A  51      60.048  27.549  55.715  1.00 45.37           N  
ATOM    274  N   GLN A  52      63.559  30.313  48.677  1.00 14.77           N  
ATOM    275  CA  GLN A  52      64.315  30.613  47.475  1.00 17.69           C  
ATOM    276  C   GLN A  52      64.508  29.415  46.557  1.00 17.94           C  
ATOM    277  O   GLN A  52      64.717  29.568  45.362  1.00 16.30           O  
ATOM    278  CB  GLN A  52      65.684  31.156  47.836  1.00 22.60           C  
ATOM    279  CG  GLN A  52      65.565  32.611  48.259  1.00 31.18           C  
ATOM    280  CD  GLN A  52      66.887  33.323  48.580  1.00 38.73           C  
ATOM    281  OE1 GLN A  52      67.126  33.760  49.719  1.00 43.53           O  
ATOM    282  NE2 GLN A  52      67.782  33.472  47.599  1.00 39.25           N  
ATOM    283  N   ASN A  53      64.408  28.203  47.090  1.00 15.33           N  
ATOM    284  CA  ASN A  53      64.510  27.011  46.265  1.00 16.68           C  
ATOM    285  C   ASN A  53      63.330  26.053  46.454  1.00 14.98           C  
ATOM    286  O   ASN A  53      63.459  24.884  46.119  1.00 13.92           O  
ATOM    287  CB  ASN A  53      65.830  26.296  46.572  1.00 17.35           C  
ATOM    288  CG  ASN A  53      66.052  25.916  48.036  1.00 18.96           C  
ATOM    289  OD1 ASN A  53      66.934  25.116  48.326  1.00 24.48           O  
ATOM    290  ND2 ASN A  53      65.351  26.389  49.059  1.00 19.62           N  
ATOM    291  N   TRP A  54      62.187  26.485  47.000  1.00 11.60           N  
ATOM    292  CA  TRP A  54      61.013  25.626  47.134  1.00 11.68           C  
ATOM    293  C   TRP A  54      59.781  26.386  46.654  1.00 10.70           C  
ATOM    294  O   TRP A  54      59.648  27.594  46.913  1.00 11.59           O  
ATOM    295  CB  TRP A  54      60.775  25.158  48.617  1.00 11.66           C  
ATOM    296  CG  TRP A  54      61.683  24.023  49.131  1.00 14.01           C  
ATOM    297  CD1 TRP A  54      62.831  24.286  49.837  1.00 16.95           C  
ATOM    298  CD2 TRP A  54      61.487  22.654  48.953  1.00 16.32           C  
ATOM    299  NE1 TRP A  54      63.376  23.106  50.101  1.00 17.14           N  
ATOM    300  CE2 TRP A  54      62.619  22.108  49.598  1.00 16.55           C  
ATOM    301  CE3 TRP A  54      60.541  21.809  48.355  1.00 14.98           C  
ATOM    302  CZ2 TRP A  54      62.823  20.732  49.657  1.00 14.78           C  
ATOM    303  CZ3 TRP A  54      60.753  20.430  48.420  1.00 18.60           C  
ATOM    304  CH2 TRP A  54      61.880  19.901  49.063  1.00 16.24           C  
ATOM    305  N   VAL A  55      58.943  25.673  45.877  1.00  9.81           N  
ATOM    306  CA  VAL A  55      57.666  26.154  45.334  1.00 10.27           C  
ATOM    307  C   VAL A  55      56.517  25.268  45.825  1.00 10.57           C  
ATOM    308  O   VAL A  55      56.636  24.045  45.875  1.00 11.53           O  
ATOM    309  CB  VAL A  55      57.697  26.160  43.748  1.00 11.35           C  
ATOM    310  CG1 VAL A  55      56.318  26.081  43.062  1.00 11.56           C  
ATOM    311  CG2 VAL A  55      58.243  27.503  43.327  1.00 10.32           C  
ATOM    312  N   MET A  56      55.386  25.846  46.219  1.00  8.66           N  
ATOM    313  CA  MET A  56      54.227  25.076  46.603  1.00  7.44           C  
ATOM    314  C   MET A  56      53.219  25.081  45.458  1.00 10.16           C  
ATOM    315  O   MET A  56      52.927  26.154  44.924  1.00  9.25           O  
ATOM    316  CB  MET A  56      53.670  25.703  47.875  1.00  9.29           C  
ATOM    317  CG  MET A  56      52.377  25.079  48.372  1.00 10.71           C  
ATOM    318  SD  MET A  56      51.700  25.886  49.852  1.00 13.02           S  
ATOM    319  CE  MET A  56      51.288  27.566  49.430  1.00  9.38           C  
ATOM    320  N   THR A  57      52.628  23.952  45.055  1.00  8.68           N  
ATOM    321  CA  THR A  57      51.655  23.921  43.955  1.00  6.91           C  
ATOM    322  C   THR A  57      50.646  22.812  44.262  1.00  7.86           C  
ATOM    323  O   THR A  57      50.679  22.256  45.374  1.00  7.97           O  
ATOM    324  CB  THR A  57      52.436  23.702  42.597  1.00  5.11           C  
ATOM    325  OG1 THR A  57      51.496  23.956  41.567  1.00  5.03           O  
ATOM    326  CG2 THR A  57      52.996  22.303  42.379  1.00  5.45           C  
ATOM    327  N   ALA A  58      49.721  22.481  43.359  1.00  8.02           N  
ATOM    328  CA  ALA A  58      48.786  21.380  43.583  1.00  8.76           C  
ATOM    329  C   ALA A  58      49.418  20.058  43.095  1.00 10.42           C  
ATOM    330  O   ALA A  58      50.202  20.041  42.128  1.00  8.70           O  
ATOM    331  CB  ALA A  58      47.485  21.629  42.817  1.00  7.33           C  
ATOM    332  N   ALA A  59      49.157  18.938  43.792  1.00  9.16           N  
ATOM    333  CA  ALA A  59      49.627  17.641  43.341  1.00  8.74           C  
ATOM    334  C   ALA A  59      49.083  17.230  41.957  1.00  9.94           C  
ATOM    335  O   ALA A  59      49.797  16.613  41.149  1.00  9.40           O  
ATOM    336  CB  ALA A  59      49.212  16.591  44.328  1.00  9.97           C  
ATOM    337  N   HIS A  60      47.853  17.606  41.585  1.00  9.12           N  
ATOM    338  CA  HIS A  60      47.349  17.225  40.272  1.00 10.21           C  
ATOM    339  C   HIS A  60      48.119  17.919  39.140  1.00  9.84           C  
ATOM    340  O   HIS A  60      48.018  17.452  38.006  1.00 10.59           O  
ATOM    341  CB  HIS A  60      45.823  17.534  40.124  1.00  9.52           C  
ATOM    342  CG  HIS A  60      45.355  18.977  39.952  1.00 12.03           C  
ATOM    343  ND1 HIS A  60      44.765  19.764  40.861  1.00 13.28           N  
ATOM    344  CD2 HIS A  60      45.448  19.698  38.779  1.00 11.66           C  
ATOM    345  CE1 HIS A  60      44.505  20.915  40.306  1.00 12.79           C  
ATOM    346  NE2 HIS A  60      44.916  20.850  39.061  1.00 13.95           N  
ATOM    347  N   CYS A  61      48.885  18.995  39.406  1.00  7.85           N  
ATOM    348  CA  CYS A  61      49.713  19.651  38.388  1.00  9.63           C  
ATOM    349  C   CYS A  61      50.914  18.793  37.965  1.00 11.75           C  
ATOM    350  O   CYS A  61      51.460  18.975  36.873  1.00 11.07           O  
ATOM    351  CB  CYS A  61      50.279  20.995  38.878  1.00  9.53           C  
ATOM    352  SG  CYS A  61      48.981  22.231  39.006  1.00  9.56           S  
ATOM    353  N   VAL A  62      51.372  17.885  38.838  1.00 11.98           N  
ATOM    354  CA  VAL A  62      52.538  17.079  38.543  1.00 13.47           C  
ATOM    355  C   VAL A  62      52.177  15.599  38.430  1.00 14.50           C  
ATOM    356  O   VAL A  62      53.049  14.733  38.528  1.00 15.98           O  
ATOM    357  CB  VAL A  62      53.637  17.283  39.615  1.00 14.34           C  
ATOM    358  CG1 VAL A  62      54.198  18.694  39.437  1.00 14.68           C  
ATOM    359  CG2 VAL A  62      53.117  17.128  41.041  1.00 15.60           C  
ATOM    360  N   ASP A  63      50.899  15.278  38.187  1.00 14.73           N  
ATOM    361  CA  ASP A  63      50.545  13.889  37.961  1.00 19.22           C  
ATOM    362  C   ASP A  63      51.208  13.313  36.716  1.00 20.60           C  
ATOM    363  O   ASP A  63      51.656  12.159  36.748  1.00 22.54           O  
ATOM    364  CB  ASP A  63      49.029  13.724  37.841  1.00 18.62           C  
ATOM    365  CG  ASP A  63      48.279  13.565  39.174  1.00 18.39           C  
ATOM    366  OD1 ASP A  63      48.843  13.089  40.164  1.00 18.09           O  
ATOM    367  OD2 ASP A  63      47.100  13.916  39.199  1.00 18.27           O  
ATOM    368  N   ARG A  64      51.318  14.065  35.615  1.00 20.95           N  
ATOM    369  CA  ARG A  64      52.016  13.547  34.448  1.00 21.05           C  
ATOM    370  C   ARG A  64      53.499  13.775  34.581  1.00 20.06           C  
ATOM    371  O   ARG A  64      53.971  14.823  35.033  1.00 22.98           O  
ATOM    372  CB  ARG A  64      51.526  14.202  33.157  1.00 25.12           C  
ATOM    373  CG  ARG A  64      50.231  13.593  32.567  1.00 34.24           C  
ATOM    374  CD  ARG A  64      50.160  12.057  32.234  1.00 44.22           C  
ATOM    375  NE  ARG A  64      51.129  11.521  31.257  1.00 53.66           N  
ATOM    376  CZ  ARG A  64      50.832  11.172  29.978  1.00 57.48           C  
ATOM    377  NH1 ARG A  64      49.601  11.283  29.442  1.00 58.71           N  
ATOM    378  NH2 ARG A  64      51.800  10.675  29.203  1.00 57.72           N  
ATOM    379  N   GLU A  65      54.238  12.753  34.165  1.00 17.07           N  
ATOM    380  CA  GLU A  65      55.679  12.742  34.250  1.00 17.82           C  
ATOM    381  C   GLU A  65      56.333  13.452  33.078  1.00 19.64           C  
ATOM    382  O   GLU A  65      56.778  12.820  32.122  1.00 20.83           O  
ATOM    383  CB  GLU A  65      56.143  11.299  34.335  1.00 18.50           C  
ATOM    384  CG  GLU A  65      55.616  10.706  35.633  1.00 20.29           C  
ATOM    385  CD  GLU A  65      56.362   9.473  36.085  1.00 17.04           C  
ATOM    386  OE1 GLU A  65      57.553   9.583  36.382  1.00 17.50           O  
ATOM    387  OE2 GLU A  65      55.729   8.427  36.140  1.00 19.42           O  
ATOM    388  N   LEU A  66      56.420  14.785  33.220  1.00 15.92           N  
ATOM    389  CA  LEU A  66      56.848  15.716  32.176  1.00 15.64           C  
ATOM    390  C   LEU A  66      58.095  16.424  32.660  1.00 16.72           C  
ATOM    391  O   LEU A  66      58.454  16.286  33.833  1.00 16.69           O  
ATOM    392  CB  LEU A  66      55.757  16.768  31.946  1.00 17.74           C  
ATOM    393  CG  LEU A  66      54.328  16.332  31.660  1.00 18.78           C  
ATOM    394  CD1 LEU A  66      53.378  17.487  31.846  1.00 21.80           C  
ATOM    395  CD2 LEU A  66      54.222  15.831  30.257  1.00 20.48           C  
ATOM    396  N   THR A  67      58.774  17.160  31.774  1.00 13.72           N  
ATOM    397  CA  THR A  67      59.883  18.010  32.146  1.00 15.03           C  
ATOM    398  C   THR A  67      59.310  19.379  32.563  1.00 15.54           C  
ATOM    399  O   THR A  67      58.695  20.086  31.764  1.00 16.15           O  
ATOM    400  CB  THR A  67      60.871  18.249  30.983  1.00 16.91           C  
ATOM    401  OG1 THR A  67      61.456  17.006  30.642  1.00 19.43           O  
ATOM    402  CG2 THR A  67      61.986  19.202  31.361  1.00 16.06           C  
ATOM    403  N   PHE A  68      59.563  19.798  33.809  1.00 14.23           N  
ATOM    404  CA  PHE A  68      58.984  21.009  34.356  1.00 12.00           C  
ATOM    405  C   PHE A  68      60.057  22.023  34.658  1.00 11.66           C  
ATOM    406  O   PHE A  68      61.182  21.699  35.038  1.00 12.35           O  
ATOM    407  CB  PHE A  68      58.227  20.727  35.660  1.00 10.94           C  
ATOM    408  CG  PHE A  68      56.966  19.891  35.537  1.00 10.22           C  
ATOM    409  CD1 PHE A  68      55.824  20.423  34.932  1.00 10.34           C  
ATOM    410  CD2 PHE A  68      56.952  18.589  36.055  1.00 13.17           C  
ATOM    411  CE1 PHE A  68      54.669  19.641  34.855  1.00 12.14           C  
ATOM    412  CE2 PHE A  68      55.785  17.811  35.969  1.00  8.93           C  
ATOM    413  CZ  PHE A  68      54.648  18.339  35.372  1.00 12.34           C  
ATOM    414  N   ARG A  69      59.656  23.281  34.477  1.00 11.68           N  
ATOM    415  CA  ARG A  69      60.474  24.403  34.916  1.00 11.50           C  
ATOM    416  C   ARG A  69      59.529  25.414  35.583  1.00  8.81           C  
ATOM    417  O   ARG A  69      58.320  25.415  35.394  1.00 10.24           O  
ATOM    418  CB  ARG A  69      61.213  25.098  33.743  1.00 11.76           C  
ATOM    419  CG  ARG A  69      60.364  25.979  32.846  1.00 14.86           C  
ATOM    420  CD  ARG A  69      61.293  26.707  31.895  1.00 16.28           C  
ATOM    421  NE  ARG A  69      60.420  27.583  31.120  1.00 19.92           N  
ATOM    422  CZ  ARG A  69      60.875  28.394  30.165  1.00 21.52           C  
ATOM    423  NH1 ARG A  69      62.162  28.451  29.840  1.00 20.39           N  
ATOM    424  NH2 ARG A  69      60.016  29.192  29.543  1.00 20.72           N  
ATOM    425  N   VAL A  70      60.129  26.315  36.347  1.00 11.12           N  
ATOM    426  CA  VAL A  70      59.422  27.336  37.099  1.00 10.60           C  
ATOM    427  C   VAL A  70      59.950  28.655  36.558  1.00  9.31           C  
ATOM    428  O   VAL A  70      61.156  28.828  36.334  1.00 10.93           O  
ATOM    429  CB  VAL A  70      59.753  27.097  38.634  1.00  9.18           C  
ATOM    430  CG1 VAL A  70      59.743  28.373  39.455  1.00 13.34           C  
ATOM    431  CG2 VAL A  70      58.721  26.109  39.166  1.00  6.24           C  
ATOM    432  N   VAL A  71      58.992  29.549  36.368  1.00  8.89           N  
ATOM    433  CA  VAL A  71      59.338  30.909  36.017  1.00 11.93           C  
ATOM    434  C   VAL A  71      58.852  31.852  37.120  1.00 11.92           C  
ATOM    435  O   VAL A  71      57.655  31.937  37.432  1.00 12.15           O  
ATOM    436  CB  VAL A  71      58.702  31.317  34.647  1.00 14.02           C  
ATOM    437  CG1 VAL A  71      59.272  32.677  34.251  1.00 10.96           C  
ATOM    438  CG2 VAL A  71      59.011  30.289  33.563  1.00 13.43           C  
ATOM    439  N   VAL A  72      59.804  32.566  37.744  1.00 13.18           N  
ATOM    440  CA  VAL A  72      59.451  33.594  38.734  1.00 12.34           C  
ATOM    441  C   VAL A  72      59.636  34.991  38.089  1.00 14.36           C  
ATOM    442  O   VAL A  72      60.312  35.152  37.048  1.00 13.27           O  
ATOM    443  CB  VAL A  72      60.327  33.453  40.043  1.00 11.92           C  
ATOM    444  CG1 VAL A  72      60.168  32.062  40.595  1.00 12.55           C  
ATOM    445  CG2 VAL A  72      61.794  33.651  39.807  1.00 11.27           C  
ATOM    446  N   GLY A  73      58.974  36.008  38.646  1.00 11.87           N  
ATOM    447  CA  GLY A  73      59.073  37.371  38.121  1.00 14.08           C  
ATOM    448  C   GLY A  73      58.387  37.512  36.773  1.00 15.09           C  
ATOM    449  O   GLY A  73      58.735  38.353  35.952  1.00 13.12           O  
ATOM    450  N   GLU A  74      57.377  36.673  36.557  1.00 14.89           N  
ATOM    451  CA  GLU A  74      56.680  36.658  35.300  1.00 15.18           C  
ATOM    452  C   GLU A  74      55.441  37.519  35.345  1.00 15.13           C  
ATOM    453  O   GLU A  74      54.729  37.580  36.343  1.00 15.30           O  
ATOM    454  CB  GLU A  74      56.305  35.201  34.918  1.00 15.63           C  
ATOM    455  CG  GLU A  74      55.658  34.857  33.578  1.00 14.24           C  
ATOM    456  CD  GLU A  74      56.448  35.409  32.404  1.00 17.13           C  
ATOM    457  OE1 GLU A  74      56.479  36.597  32.299  1.00 16.38           O  
ATOM    458  OE2 GLU A  74      57.040  34.708  31.606  1.00 19.38           O  
ATOM    459  N   HIS A  75      55.228  38.237  34.232  1.00 15.92           N  
ATOM    460  CA  HIS A  75      53.987  38.963  34.068  1.00 14.16           C  
ATOM    461  C   HIS A  75      53.300  38.688  32.718  1.00 15.24           C  
ATOM    462  O   HIS A  75      52.114  38.343  32.754  1.00 13.71           O  
ATOM    463  CB  HIS A  75      54.285  40.426  34.247  1.00 16.58           C  
ATOM    464  CG  HIS A  75      53.004  41.234  34.238  1.00 18.47           C  
ATOM    465  ND1 HIS A  75      52.022  41.152  35.121  1.00 19.99           N  
ATOM    466  CD2 HIS A  75      52.667  42.159  33.285  1.00 19.29           C  
ATOM    467  CE1 HIS A  75      51.097  41.991  34.744  1.00 21.94           C  
ATOM    468  NE2 HIS A  75      51.491  42.588  33.645  1.00 23.35           N  
ATOM    469  N   ASN A  76      53.936  38.875  31.533  1.00 12.62           N  
ATOM    470  CA  ASN A  76      53.282  38.553  30.275  1.00 12.88           C  
ATOM    471  C   ASN A  76      53.830  37.233  29.786  1.00 13.49           C  
ATOM    472  O   ASN A  76      55.021  37.202  29.520  1.00 14.57           O  
ATOM    473  CB  ASN A  76      53.557  39.636  29.227  1.00 14.38           C  
ATOM    474  CG  ASN A  76      52.816  39.356  27.917  1.00 16.99           C  
ATOM    475  OD1 ASN A  76      52.985  38.314  27.303  1.00 18.07           O  
ATOM    476  ND2 ASN A  76      51.957  40.205  27.375  1.00 18.06           N  
ATOM    477  N   LEU A  77      53.074  36.138  29.618  1.00 13.10           N  
ATOM    478  CA  LEU A  77      53.654  34.856  29.191  1.00 16.26           C  
ATOM    479  C   LEU A  77      54.349  34.840  27.835  1.00 18.78           C  
ATOM    480  O   LEU A  77      55.335  34.135  27.607  1.00 16.87           O  
ATOM    481  CB  LEU A  77      52.587  33.746  29.171  1.00 12.97           C  
ATOM    482  CG  LEU A  77      52.036  33.309  30.510  1.00 12.19           C  
ATOM    483  CD1 LEU A  77      50.886  32.342  30.314  1.00 10.63           C  
ATOM    484  CD2 LEU A  77      53.160  32.685  31.334  1.00 11.40           C  
ATOM    485  N   ASN A  78      53.889  35.718  26.964  1.00 22.18           N  
ATOM    486  CA  ASN A  78      54.380  35.717  25.614  1.00 27.02           C  
ATOM    487  C   ASN A  78      55.407  36.791  25.304  1.00 29.22           C  
ATOM    488  O   ASN A  78      55.888  36.812  24.167  1.00 31.27           O  
ATOM    489  CB  ASN A  78      53.136  35.808  24.724  1.00 30.95           C  
ATOM    490  CG  ASN A  78      52.153  34.665  24.993  1.00 34.09           C  
ATOM    491  OD1 ASN A  78      51.008  34.856  25.420  1.00 36.04           O  
ATOM    492  ND2 ASN A  78      52.594  33.422  24.807  1.00 35.73           N  
ATOM    493  N   GLN A  79      55.796  37.686  26.230  1.00 29.09           N  
ATOM    494  CA  GLN A  79      56.730  38.787  25.929  1.00 27.70           C  
ATOM    495  C   GLN A  79      57.879  38.885  26.904  1.00 26.60           C  
ATOM    496  O   GLN A  79      57.615  38.583  28.052  1.00 20.79           O  
ATOM    497  CB  GLN A  79      56.043  40.128  25.981  1.00 31.97           C  
ATOM    498  CG  GLN A  79      55.124  40.432  24.818  1.00 40.38           C  
ATOM    499  CD  GLN A  79      54.257  41.660  25.083  1.00 45.18           C  
ATOM    500  OE1 GLN A  79      54.605  42.525  25.898  1.00 49.79           O  
ATOM    501  NE2 GLN A  79      53.099  41.765  24.418  1.00 45.59           N  
ATOM    502  N   ASN A  80      59.125  39.256  26.607  1.00 24.38           N  
ATOM    503  CA  ASN A  80      60.093  39.436  27.672  1.00 26.13           C  
ATOM    504  C   ASN A  80      59.733  40.691  28.492  1.00 24.82           C  
ATOM    505  O   ASN A  80      59.459  41.770  27.975  1.00 24.22           O  
ATOM    506  CB  ASN A  80      61.525  39.577  27.110  1.00 31.06           C  
ATOM    507  CG  ASN A  80      62.609  39.916  28.160  1.00 36.12           C  
ATOM    508  OD1 ASN A  80      62.814  39.231  29.174  1.00 37.74           O  
ATOM    509  ND2 ASN A  80      63.332  41.026  27.967  1.00 40.37           N  
ATOM    510  N   ASN A  81      59.733  40.517  29.813  1.00 20.88           N  
ATOM    511  CA  ASN A  81      59.400  41.570  30.751  1.00 20.77           C  
ATOM    512  C   ASN A  81      60.699  42.125  31.344  1.00 18.80           C  
ATOM    513  O   ASN A  81      60.704  43.163  31.979  1.00 19.83           O  
ATOM    514  CB  ASN A  81      58.474  40.983  31.844  1.00 19.80           C  
ATOM    515  CG  ASN A  81      57.062  40.605  31.402  1.00 20.20           C  
ATOM    516  OD1 ASN A  81      56.685  39.438  31.377  1.00 20.33           O  
ATOM    517  ND2 ASN A  81      56.187  41.530  31.047  1.00 19.34           N  
ATOM    518  N   GLY A  82      61.862  41.502  31.165  1.00 18.50           N  
ATOM    519  CA  GLY A  82      63.105  41.965  31.737  1.00 17.86           C  
ATOM    520  C   GLY A  82      63.188  41.609  33.213  1.00 19.09           C  
ATOM    521  O   GLY A  82      64.088  42.084  33.890  1.00 20.72           O  
ATOM    522  N   THR A  83      62.286  40.781  33.764  1.00 19.40           N  
ATOM    523  CA  THR A  83      62.275  40.417  35.187  1.00 19.01           C  
ATOM    524  C   THR A  83      62.283  38.924  35.505  1.00 18.98           C  
ATOM    525  O   THR A  83      62.373  38.506  36.664  1.00 19.69           O  
ATOM    526  CB  THR A  83      61.045  41.054  35.821  1.00 16.10           C  
ATOM    527  OG1 THR A  83      59.922  40.569  35.104  1.00 14.11           O  
ATOM    528  CG2 THR A  83      61.070  42.588  35.751  1.00 16.91           C  
ATOM    529  N   GLU A  84      62.245  38.082  34.466  1.00 17.88           N  
ATOM    530  CA  GLU A  84      62.045  36.648  34.637  1.00 14.65           C  
ATOM    531  C   GLU A  84      63.292  35.900  35.014  1.00 13.47           C  
ATOM    532  O   GLU A  84      64.387  36.258  34.588  1.00 13.80           O  
ATOM    533  CB  GLU A  84      61.499  35.997  33.363  1.00 12.10           C  
ATOM    534  CG  GLU A  84      60.237  36.570  32.736  1.00 14.64           C  
ATOM    535  CD  GLU A  84      60.445  37.752  31.775  1.00 16.56           C  
ATOM    536  OE1 GLU A  84      61.402  38.528  31.859  1.00 15.47           O  
ATOM    537  OE2 GLU A  84      59.621  37.917  30.905  1.00 16.61           O  
ATOM    538  N   GLN A  85      63.147  34.915  35.913  1.00 12.34           N  
ATOM    539  CA  GLN A  85      64.221  33.966  36.198  1.00 12.18           C  
ATOM    540  C   GLN A  85      63.605  32.598  35.922  1.00 13.70           C  
ATOM    541  O   GLN A  85      62.467  32.345  36.316  1.00 13.20           O  
ATOM    542  CB  GLN A  85      64.674  34.008  37.637  1.00 14.90           C  
ATOM    543  CG  GLN A  85      65.380  35.285  38.054  1.00 17.26           C  
ATOM    544  CD  GLN A  85      65.518  35.351  39.570  1.00 20.93           C  
ATOM    545  OE1 GLN A  85      66.202  34.524  40.171  1.00 22.56           O  
ATOM    546  NE2 GLN A  85      64.883  36.312  40.242  1.00 20.29           N  
ATOM    547  N   TYR A  86      64.354  31.744  35.217  1.00 14.34           N  
ATOM    548  CA  TYR A  86      63.891  30.436  34.741  1.00 16.35           C  
ATOM    549  C   TYR A  86      64.717  29.364  35.424  1.00 16.89           C  
ATOM    550  O   TYR A  86      65.946  29.361  35.275  1.00 18.78           O  
ATOM    551  CB  TYR A  86      64.096  30.294  33.259  1.00 16.32           C  
ATOM    552  CG  TYR A  86      63.416  31.357  32.429  1.00 19.72           C  
ATOM    553  CD1 TYR A  86      62.099  31.182  32.060  1.00 18.48           C  
ATOM    554  CD2 TYR A  86      64.098  32.516  32.052  1.00 20.37           C  
ATOM    555  CE1 TYR A  86      61.448  32.162  31.315  1.00 20.31           C  
ATOM    556  CE2 TYR A  86      63.451  33.499  31.301  1.00 19.67           C  
ATOM    557  CZ  TYR A  86      62.128  33.308  30.944  1.00 20.73           C  
ATOM    558  OH  TYR A  86      61.442  34.288  30.249  1.00 27.36           O  
ATOM    559  N   VAL A  87      64.095  28.450  36.183  1.00 15.67           N  
ATOM    560  CA  VAL A  87      64.884  27.451  36.906  1.00 15.58           C  
ATOM    561  C   VAL A  87      64.223  26.079  36.822  1.00 14.33           C  
ATOM    562  O   VAL A  87      63.008  25.999  36.714  1.00 12.05           O  
ATOM    563  CB  VAL A  87      65.089  27.968  38.386  1.00 15.09           C  
ATOM    564  CG1 VAL A  87      63.770  28.218  39.073  1.00 17.81           C  
ATOM    565  CG2 VAL A  87      65.878  26.938  39.180  1.00 14.82           C  
ATOM    566  N   GLY A  88      65.029  25.001  36.778  1.00 15.60           N  
ATOM    567  CA  GLY A  88      64.545  23.626  36.675  1.00 15.91           C  
ATOM    568  C   GLY A  88      64.036  23.095  38.002  1.00 15.26           C  
ATOM    569  O   GLY A  88      64.387  23.586  39.078  1.00 13.64           O  
ATOM    570  N   VAL A  89      63.131  22.124  37.918  1.00 14.94           N  
ATOM    571  CA  VAL A  89      62.621  21.446  39.101  1.00 16.34           C  
ATOM    572  C   VAL A  89      63.521  20.237  39.296  1.00 19.56           C  
ATOM    573  O   VAL A  89      63.700  19.406  38.406  1.00 21.89           O  
ATOM    574  CB  VAL A  89      61.175  21.005  38.884  1.00 11.51           C  
ATOM    575  CG1 VAL A  89      60.647  20.192  40.048  1.00 13.75           C  
ATOM    576  CG2 VAL A  89      60.328  22.252  38.793  1.00  9.94           C  
ATOM    577  N   GLN A  90      64.189  20.204  40.429  1.00 20.26           N  
ATOM    578  CA  GLN A  90      65.034  19.096  40.765  1.00 22.28           C  
ATOM    579  C   GLN A  90      64.294  17.969  41.535  1.00 24.14           C  
ATOM    580  O   GLN A  90      64.680  16.807  41.382  1.00 25.96           O  
ATOM    581  CB  GLN A  90      66.142  19.683  41.550  1.00 23.58           C  
ATOM    582  CG  GLN A  90      67.113  18.705  42.144  1.00 30.44           C  
ATOM    583  CD  GLN A  90      68.064  19.491  43.008  1.00 33.80           C  
ATOM    584  OE1 GLN A  90      67.753  19.879  44.134  1.00 36.82           O  
ATOM    585  NE2 GLN A  90      69.237  19.779  42.454  1.00 36.91           N  
ATOM    586  N   LYS A  91      63.262  18.187  42.371  1.00 20.69           N  
ATOM    587  CA  LYS A  91      62.648  17.102  43.128  1.00 18.40           C  
ATOM    588  C   LYS A  91      61.197  17.458  43.376  1.00 17.81           C  
ATOM    589  O   LYS A  91      60.920  18.610  43.681  1.00 17.02           O  
ATOM    590  CB  LYS A  91      63.404  16.948  44.427  1.00 20.25           C  
ATOM    591  CG  LYS A  91      62.840  15.904  45.357  1.00 26.29           C  
ATOM    592  CD  LYS A  91      63.591  15.895  46.677  1.00 29.77           C  
ATOM    593  CE  LYS A  91      63.339  14.527  47.326  1.00 32.95           C  
ATOM    594  NZ  LYS A  91      64.038  13.442  46.641  1.00 36.98           N  
ATOM    595  N   ILE A  92      60.266  16.514  43.214  1.00 14.26           N  
ATOM    596  CA  ILE A  92      58.838  16.726  43.403  1.00 16.37           C  
ATOM    597  C   ILE A  92      58.401  15.863  44.592  1.00 16.51           C  
ATOM    598  O   ILE A  92      58.598  14.641  44.563  1.00 17.95           O  
ATOM    599  CB  ILE A  92      58.097  16.311  42.112  1.00 15.64           C  
ATOM    600  CG1 ILE A  92      58.510  17.276  40.968  1.00 16.74           C  
ATOM    601  CG2 ILE A  92      56.580  16.304  42.348  1.00 14.98           C  
ATOM    602  CD1 ILE A  92      57.997  16.971  39.532  1.00 20.78           C  
ATOM    603  N   VAL A  93      57.797  16.491  45.617  1.00 13.52           N  
ATOM    604  CA  VAL A  93      57.362  15.804  46.824  1.00 12.48           C  
ATOM    605  C   VAL A  93      55.886  16.028  46.841  1.00 12.62           C  
ATOM    606  O   VAL A  93      55.421  17.117  47.128  1.00 14.90           O  
ATOM    607  CB  VAL A  93      58.034  16.409  48.107  1.00  8.83           C  
ATOM    608  CG1 VAL A  93      57.629  15.621  49.341  1.00  9.55           C  
ATOM    609  CG2 VAL A  93      59.555  16.361  47.987  1.00 10.27           C  
ATOM    610  N   VAL A  94      55.103  15.022  46.489  1.00 12.74           N  
ATOM    611  CA  VAL A  94      53.657  15.132  46.518  1.00 13.20           C  
ATOM    612  C   VAL A  94      53.193  14.687  47.910  1.00 14.69           C  
ATOM    613  O   VAL A  94      53.896  13.885  48.542  1.00 12.47           O  
ATOM    614  CB  VAL A  94      53.061  14.222  45.373  1.00 16.43           C  
ATOM    615  CG1 VAL A  94      51.556  14.174  45.405  1.00 15.01           C  
ATOM    616  CG2 VAL A  94      53.417  14.836  44.013  1.00 15.46           C  
ATOM    617  N   HIS A  95      52.081  15.208  48.467  1.00 12.87           N  
ATOM    618  CA  HIS A  95      51.562  14.729  49.747  1.00 14.54           C  
ATOM    619  C   HIS A  95      51.364  13.200  49.686  1.00 15.11           C  
ATOM    620  O   HIS A  95      50.773  12.732  48.701  1.00 13.56           O  
ATOM    621  CB  HIS A  95      50.230  15.412  50.049  1.00 13.95           C  
ATOM    622  CG  HIS A  95      49.864  15.175  51.497  1.00 16.11           C  
ATOM    623  ND1 HIS A  95      49.373  14.062  52.040  1.00 14.83           N  
ATOM    624  CD2 HIS A  95      50.077  16.080  52.510  1.00 16.56           C  
ATOM    625  CE1 HIS A  95      49.288  14.251  53.348  1.00 16.92           C  
ATOM    626  NE2 HIS A  95      49.711  15.458  53.612  1.00 17.35           N  
ATOM    627  N   PRO A  96      51.849  12.377  50.656  1.00 15.94           N  
ATOM    628  CA  PRO A  96      51.682  10.906  50.715  1.00 16.06           C  
ATOM    629  C   PRO A  96      50.288  10.339  50.474  1.00 15.65           C  
ATOM    630  O   PRO A  96      50.147   9.247  49.935  1.00 17.84           O  
ATOM    631  CB  PRO A  96      52.206  10.520  52.097  1.00 16.71           C  
ATOM    632  CG  PRO A  96      53.231  11.588  52.459  1.00 16.31           C  
ATOM    633  CD  PRO A  96      52.671  12.844  51.797  1.00 16.37           C  
ATOM    634  N   TYR A  97      49.246  11.060  50.904  1.00 12.74           N  
ATOM    635  CA  TYR A  97      47.875  10.656  50.747  1.00 12.92           C  
ATOM    636  C   TYR A  97      47.122  11.114  49.509  1.00 14.08           C  
ATOM    637  O   TYR A  97      45.918  10.844  49.445  1.00 12.62           O  
ATOM    638  CB  TYR A  97      47.086  11.125  51.937  1.00 19.96           C  
ATOM    639  CG  TYR A  97      47.419  10.449  53.244  1.00 24.42           C  
ATOM    640  CD1 TYR A  97      47.972   9.169  53.262  1.00 29.05           C  
ATOM    641  CD2 TYR A  97      47.116  11.098  54.441  1.00 28.57           C  
ATOM    642  CE1 TYR A  97      48.214   8.515  54.478  1.00 30.89           C  
ATOM    643  CE2 TYR A  97      47.357  10.458  55.662  1.00 31.11           C  
ATOM    644  CZ  TYR A  97      47.899   9.168  55.673  1.00 31.62           C  
ATOM    645  OH  TYR A  97      48.088   8.514  56.878  1.00 33.38           O  
ATOM    646  N   TRP A  98      47.783  11.833  48.568  1.00 13.04           N  
ATOM    647  CA  TRP A  98      47.155  12.347  47.348  1.00 12.00           C  
ATOM    648  C   TRP A  98      46.665  11.184  46.522  1.00 12.60           C  
ATOM    649  O   TRP A  98      47.422  10.250  46.298  1.00 13.84           O  
ATOM    650  CB  TRP A  98      48.157  13.169  46.445  1.00 10.27           C  
ATOM    651  CG  TRP A  98      47.633  13.510  45.018  1.00  9.10           C  
ATOM    652  CD1 TRP A  98      48.301  13.079  43.898  1.00  9.83           C  
ATOM    653  CD2 TRP A  98      46.490  14.212  44.682  1.00  8.83           C  
ATOM    654  NE1 TRP A  98      47.583  13.495  42.864  1.00  7.05           N  
ATOM    655  CE2 TRP A  98      46.512  14.161  43.285  1.00  8.87           C  
ATOM    656  CE3 TRP A  98      45.436  14.874  45.319  1.00  9.49           C  
ATOM    657  CZ2 TRP A  98      45.512  14.741  42.521  1.00 10.25           C  
ATOM    658  CZ3 TRP A  98      44.425  15.458  44.549  1.00 12.16           C  
ATOM    659  CH2 TRP A  98      44.462  15.398  43.155  1.00 11.86           C  
ATOM    660  N   ASN A  99      45.457  11.209  46.028  1.00 14.58           N  
ATOM    661  CA  ASN A  99      45.017  10.129  45.157  1.00 16.39           C  
ATOM    662  C   ASN A  99      44.429  10.790  43.941  1.00 14.46           C  
ATOM    663  O   ASN A  99      43.391  11.435  44.072  1.00 14.41           O  
ATOM    664  CB  ASN A  99      43.966   9.302  45.883  1.00 18.94           C  
ATOM    665  CG  ASN A  99      43.326   8.185  45.093  1.00 20.89           C  
ATOM    666  OD1 ASN A  99      43.688   7.903  43.951  1.00 24.09           O  
ATOM    667  ND2 ASN A  99      42.336   7.557  45.732  1.00 24.14           N  
ATOM    668  N   THR A 100      45.076  10.624  42.786  1.00 15.80           N  
ATOM    669  CA  THR A 100      44.608  11.181  41.502  1.00 18.40           C  
ATOM    670  C   THR A 100      43.146  10.900  41.123  1.00 19.39           C  
ATOM    671  O   THR A 100      42.462  11.748  40.532  1.00 20.77           O  
ATOM    672  CB  THR A 100      45.432  10.654  40.351  1.00 19.59           C  
ATOM    673  OG1 THR A 100      46.784  10.591  40.746  1.00 26.80           O  
ATOM    674  CG2 THR A 100      45.218  11.522  39.143  1.00 22.76           C  
ATOM    675  N   ASP A 101      42.670   9.693  41.471  1.00 20.22           N  
ATOM    676  CA  ASP A 101      41.285   9.239  41.235  1.00 22.75           C  
ATOM    677  C   ASP A 101      40.234   9.804  42.210  1.00 25.03           C  
ATOM    678  O   ASP A 101      39.035   9.498  42.075  1.00 23.02           O  
ATOM    679  CB  ASP A 101      41.132   7.708  41.349  1.00 24.56           C  
ATOM    680  CG  ASP A 101      42.027   6.808  40.511  1.00 28.77           C  
ATOM    681  OD1 ASP A 101      42.446   7.214  39.420  1.00 29.77           O  
ATOM    682  OD2 ASP A 101      42.279   5.687  40.975  1.00 31.95           O  
ATOM    683  N   ASP A 102      40.685  10.572  43.235  1.00 23.36           N  
ATOM    684  CA  ASP A 102      39.788  11.180  44.201  1.00 22.91           C  
ATOM    685  C   ASP A 102      40.272  12.575  44.630  1.00 22.59           C  
ATOM    686  O   ASP A 102      40.711  12.725  45.774  1.00 21.87           O  
ATOM    687  CB  ASP A 102      39.715  10.218  45.352  1.00 22.88           C  
ATOM    688  CG  ASP A 102      38.567  10.408  46.325  1.00 26.98           C  
ATOM    689  OD1 ASP A 102      37.798  11.372  46.219  1.00 22.46           O  
ATOM    690  OD2 ASP A 102      38.468   9.544  47.203  1.00 28.88           O  
ATOM    691  N   VAL A 103      40.207  13.631  43.770  1.00 20.22           N  
ATOM    692  CA  VAL A 103      40.590  14.990  44.190  1.00 18.18           C  
ATOM    693  C   VAL A 103      39.676  15.478  45.338  1.00 15.07           C  
ATOM    694  O   VAL A 103      40.099  16.273  46.166  1.00 14.46           O  
ATOM    695  CB  VAL A 103      40.533  15.972  42.915  1.00 19.44           C  
ATOM    696  CG1 VAL A 103      39.125  16.374  42.552  1.00 19.05           C  
ATOM    697  CG2 VAL A 103      41.252  17.269  43.206  1.00 17.32           C  
ATOM    698  N   ALA A 104      38.442  14.967  45.449  1.00 12.49           N  
ATOM    699  CA  ALA A 104      37.510  15.367  46.482  1.00 13.00           C  
ATOM    700  C   ALA A 104      37.913  14.831  47.846  1.00 11.56           C  
ATOM    701  O   ALA A 104      37.409  15.291  48.867  1.00 11.63           O  
ATOM    702  CB  ALA A 104      36.125  14.865  46.138  1.00 13.61           C  
ATOM    703  N   ALA A 105      38.850  13.880  47.903  1.00 12.38           N  
ATOM    704  CA  ALA A 105      39.424  13.466  49.171  1.00 12.37           C  
ATOM    705  C   ALA A 105      40.428  14.478  49.778  1.00 12.90           C  
ATOM    706  O   ALA A 105      40.738  14.402  50.975  1.00 13.39           O  
ATOM    707  CB  ALA A 105      40.153  12.138  48.997  1.00 12.90           C  
ATOM    708  N   GLY A 106      40.932  15.450  49.004  1.00 11.80           N  
ATOM    709  CA  GLY A 106      41.878  16.431  49.511  1.00 11.28           C  
ATOM    710  C   GLY A 106      43.291  16.009  49.180  1.00 10.14           C  
ATOM    711  O   GLY A 106      43.517  15.221  48.264  1.00 10.55           O  
ATOM    712  N   TYR A 107      44.221  16.539  49.991  1.00  6.45           N  
ATOM    713  CA  TYR A 107      45.660  16.363  49.895  1.00  7.59           C  
ATOM    714  C   TYR A 107      46.191  16.831  48.550  1.00  5.93           C  
ATOM    715  O   TYR A 107      47.220  16.349  48.084  1.00  8.21           O  
ATOM    716  CB  TYR A 107      46.098  14.873  50.119  1.00 10.07           C  
ATOM    717  CG  TYR A 107      45.495  14.301  51.410  1.00 14.76           C  
ATOM    718  CD1 TYR A 107      45.975  14.689  52.667  1.00 14.99           C  
ATOM    719  CD2 TYR A 107      44.403  13.430  51.318  1.00 16.34           C  
ATOM    720  CE1 TYR A 107      45.347  14.211  53.819  1.00 19.58           C  
ATOM    721  CE2 TYR A 107      43.772  12.941  52.449  1.00 16.99           C  
ATOM    722  CZ  TYR A 107      44.250  13.342  53.691  1.00 21.33           C  
ATOM    723  OH  TYR A 107      43.601  12.881  54.828  1.00 28.40           O  
ATOM    724  N   ASP A 108      45.542  17.824  47.956  1.00  6.59           N  
ATOM    725  CA  ASP A 108      46.017  18.293  46.666  1.00  6.83           C  
ATOM    726  C   ASP A 108      47.061  19.380  46.853  1.00  7.13           C  
ATOM    727  O   ASP A 108      46.795  20.575  46.695  1.00  7.22           O  
ATOM    728  CB  ASP A 108      44.835  18.832  45.808  1.00  5.74           C  
ATOM    729  CG  ASP A 108      45.130  18.984  44.297  1.00  7.46           C  
ATOM    730  OD1 ASP A 108      46.207  18.606  43.862  1.00  6.32           O  
ATOM    731  OD2 ASP A 108      44.261  19.453  43.571  1.00  7.77           O  
ATOM    732  N   ILE A 109      48.278  18.894  47.151  1.00  6.43           N  
ATOM    733  CA  ILE A 109      49.434  19.753  47.427  1.00  7.64           C  
ATOM    734  C   ILE A 109      50.714  18.997  47.168  1.00  7.56           C  
ATOM    735  O   ILE A 109      50.848  17.790  47.384  1.00  9.28           O  
ATOM    736  CB  ILE A 109      49.313  20.299  48.927  1.00  8.14           C  
ATOM    737  CG1 ILE A 109      50.424  21.328  49.224  1.00  8.97           C  
ATOM    738  CG2 ILE A 109      49.366  19.129  49.951  1.00  6.47           C  
ATOM    739  CD1 ILE A 109      50.035  22.216  50.449  1.00 10.00           C  
ATOM    740  N   ALA A 110      51.673  19.768  46.661  1.00  7.57           N  
ATOM    741  CA  ALA A 110      52.975  19.254  46.297  1.00  8.22           C  
ATOM    742  C   ALA A 110      54.005  20.354  46.456  1.00  9.78           C  
ATOM    743  O   ALA A 110      53.710  21.540  46.305  1.00 10.61           O  
ATOM    744  CB  ALA A 110      52.957  18.783  44.842  1.00  7.05           C  
ATOM    745  N   LEU A 111      55.214  19.961  46.827  1.00  8.38           N  
ATOM    746  CA  LEU A 111      56.315  20.876  46.979  1.00 11.26           C  
ATOM    747  C   LEU A 111      57.401  20.545  45.961  1.00 11.28           C  
ATOM    748  O   LEU A 111      57.808  19.398  45.844  1.00 11.78           O  
ATOM    749  CB  LEU A 111      56.900  20.778  48.401  1.00 11.52           C  
ATOM    750  CG  LEU A 111      55.944  21.119  49.543  1.00 14.90           C  
ATOM    751  CD1 LEU A 111      56.650  20.874  50.874  1.00 16.48           C  
ATOM    752  CD2 LEU A 111      55.506  22.572  49.439  1.00 13.34           C  
ATOM    753  N   LEU A 112      57.916  21.532  45.234  1.00 12.10           N  
ATOM    754  CA  LEU A 112      58.928  21.349  44.211  1.00 11.77           C  
ATOM    755  C   LEU A 112      60.230  21.991  44.671  1.00 13.64           C  
ATOM    756  O   LEU A 112      60.290  23.170  45.037  1.00 10.84           O  
ATOM    757  CB  LEU A 112      58.482  22.015  42.905  1.00 12.17           C  
ATOM    758  CG  LEU A 112      57.063  21.837  42.415  1.00 15.40           C  
ATOM    759  CD1 LEU A 112      56.876  22.538  41.085  1.00 15.49           C  
ATOM    760  CD2 LEU A 112      56.775  20.368  42.294  1.00 15.15           C  
ATOM    761  N   ARG A 113      61.283  21.186  44.757  1.00 13.46           N  
ATOM    762  CA  ARG A 113      62.589  21.715  45.050  1.00 15.28           C  
ATOM    763  C   ARG A 113      63.244  22.124  43.733  1.00 16.51           C  
ATOM    764  O   ARG A 113      63.374  21.346  42.790  1.00 15.93           O  
ATOM    765  CB  ARG A 113      63.388  20.649  45.748  1.00 19.45           C  
ATOM    766  CG  ARG A 113      64.692  21.189  46.234  1.00 24.78           C  
ATOM    767  CD  ARG A 113      65.510  19.963  46.464  1.00 35.00           C  
ATOM    768  NE  ARG A 113      66.833  20.308  46.929  1.00 44.46           N  
ATOM    769  CZ  ARG A 113      67.054  20.648  48.211  1.00 50.93           C  
ATOM    770  NH1 ARG A 113      66.056  20.699  49.111  1.00 53.94           N  
ATOM    771  NH2 ARG A 113      68.294  20.957  48.614  1.00 52.42           N  
ATOM    772  N   LEU A 114      63.656  23.382  43.675  1.00 14.59           N  
ATOM    773  CA  LEU A 114      64.286  23.948  42.517  1.00 12.96           C  
ATOM    774  C   LEU A 114      65.750  23.621  42.431  1.00 14.45           C  
ATOM    775  O   LEU A 114      66.429  23.426  43.427  1.00 15.35           O  
ATOM    776  CB  LEU A 114      64.085  25.448  42.528  1.00 14.52           C  
ATOM    777  CG  LEU A 114      62.643  25.929  42.734  1.00 13.04           C  
ATOM    778  CD1 LEU A 114      62.618  27.433  42.664  1.00 13.89           C  
ATOM    779  CD2 LEU A 114      61.727  25.354  41.681  1.00 15.27           C  
ATOM    780  N   ALA A 115      66.225  23.591  41.180  1.00 15.90           N  
ATOM    781  CA  ALA A 115      67.574  23.190  40.869  1.00 16.86           C  
ATOM    782  C   ALA A 115      68.522  24.228  41.395  1.00 19.93           C  
ATOM    783  O   ALA A 115      69.664  23.887  41.715  1.00 22.92           O  
ATOM    784  CB  ALA A 115      67.763  23.068  39.383  1.00 14.10           C  
ATOM    785  N   GLN A 116      68.097  25.490  41.479  1.00 21.12           N  
ATOM    786  CA  GLN A 116      68.882  26.472  42.201  1.00 24.08           C  
ATOM    787  C   GLN A 116      68.024  27.514  42.898  1.00 20.84           C  
ATOM    788  O   GLN A 116      66.823  27.610  42.679  1.00 18.27           O  
ATOM    789  CB  GLN A 116      69.904  27.171  41.267  1.00 30.47           C  
ATOM    790  CG  GLN A 116      69.588  28.237  40.206  1.00 40.70           C  
ATOM    791  CD  GLN A 116      70.645  29.381  40.178  1.00 48.56           C  
ATOM    792  OE1 GLN A 116      71.846  29.204  40.474  1.00 51.81           O  
ATOM    793  NE2 GLN A 116      70.236  30.621  39.855  1.00 50.77           N  
ATOM    794  N   SER A 117      68.648  28.236  43.834  1.00 20.21           N  
ATOM    795  CA  SER A 117      67.993  29.326  44.525  1.00 22.03           C  
ATOM    796  C   SER A 117      67.726  30.546  43.645  1.00 20.51           C  
ATOM    797  O   SER A 117      68.607  30.978  42.906  1.00 21.61           O  
ATOM    798  CB  SER A 117      68.848  29.713  45.693  1.00 23.40           C  
ATOM    799  OG  SER A 117      68.736  28.667  46.645  1.00 29.17           O  
ATOM    800  N   VAL A 118      66.505  31.076  43.634  1.00 18.92           N  
ATOM    801  CA  VAL A 118      66.219  32.272  42.862  1.00 17.04           C  
ATOM    802  C   VAL A 118      66.682  33.466  43.689  1.00 18.16           C  
ATOM    803  O   VAL A 118      66.958  33.359  44.893  1.00 18.57           O  
ATOM    804  CB  VAL A 118      64.691  32.408  42.520  1.00 15.99           C  
ATOM    805  CG1 VAL A 118      64.306  31.212  41.662  1.00 13.34           C  
ATOM    806  CG2 VAL A 118      63.798  32.454  43.740  1.00 14.89           C  
ATOM    807  N   THR A 119      66.874  34.578  42.987  1.00 17.98           N  
ATOM    808  CA  THR A 119      67.293  35.837  43.544  1.00 18.88           C  
ATOM    809  C   THR A 119      66.071  36.651  43.921  1.00 18.24           C  
ATOM    810  O   THR A 119      65.197  36.845  43.074  1.00 19.28           O  
ATOM    811  CB  THR A 119      68.136  36.574  42.489  1.00 22.39           C  
ATOM    812  OG1 THR A 119      69.324  35.787  42.316  1.00 24.41           O  
ATOM    813  CG2 THR A 119      68.409  38.046  42.866  1.00 23.47           C  
ATOM    814  N   LEU A 120      65.997  37.164  45.156  1.00 17.66           N  
ATOM    815  CA  LEU A 120      64.844  37.945  45.535  1.00 17.16           C  
ATOM    816  C   LEU A 120      65.043  39.410  45.223  1.00 17.89           C  
ATOM    817  O   LEU A 120      66.140  39.954  45.375  1.00 21.02           O  
ATOM    818  CB  LEU A 120      64.553  37.758  47.023  1.00 17.06           C  
ATOM    819  CG  LEU A 120      64.308  36.343  47.568  1.00 19.10           C  
ATOM    820  CD1 LEU A 120      63.883  36.470  49.023  1.00 18.54           C  
ATOM    821  CD2 LEU A 120      63.208  35.620  46.823  1.00 18.38           C  
ATOM    822  N   ASN A 121      63.967  40.037  44.751  1.00 17.23           N  
ATOM    823  CA  ASN A 121      63.949  41.455  44.410  1.00 18.56           C  
ATOM    824  C   ASN A 121      62.526  41.982  44.418  1.00 18.33           C  
ATOM    825  O   ASN A 121      61.669  41.268  44.947  1.00 19.10           O  
ATOM    826  CB  ASN A 121      64.608  41.669  43.030  1.00 18.33           C  
ATOM    827  CG  ASN A 121      64.039  40.875  41.875  1.00 18.25           C  
ATOM    828  OD1 ASN A 121      62.827  40.853  41.666  1.00 19.36           O  
ATOM    829  ND2 ASN A 121      64.922  40.227  41.111  1.00 18.49           N  
ATOM    830  N   SER A 122      62.109  43.135  43.864  1.00 20.06           N  
ATOM    831  CA  SER A 122      60.701  43.535  44.000  1.00 21.56           C  
ATOM    832  C   SER A 122      59.689  42.720  43.200  1.00 21.71           C  
ATOM    833  O   SER A 122      58.476  42.816  43.410  1.00 23.08           O  
ATOM    834  CB  SER A 122      60.540  44.987  43.627  1.00 25.51           C  
ATOM    835  OG  SER A 122      61.304  45.281  42.466  1.00 35.65           O  
ATOM    836  N   TYR A 123      60.216  41.903  42.277  1.00 19.93           N  
ATOM    837  CA  TYR A 123      59.418  41.039  41.431  1.00 17.77           C  
ATOM    838  C   TYR A 123      59.332  39.622  41.935  1.00 15.04           C  
ATOM    839  O   TYR A 123      58.436  38.902  41.513  1.00 14.16           O  
ATOM    840  CB  TYR A 123      60.006  40.982  40.052  1.00 19.11           C  
ATOM    841  CG  TYR A 123      60.098  42.388  39.530  1.00 21.65           C  
ATOM    842  CD1 TYR A 123      58.899  43.020  39.158  1.00 25.24           C  
ATOM    843  CD2 TYR A 123      61.335  43.032  39.445  1.00 21.72           C  
ATOM    844  CE1 TYR A 123      58.945  44.334  38.689  1.00 25.01           C  
ATOM    845  CE2 TYR A 123      61.380  44.348  38.971  1.00 22.05           C  
ATOM    846  CZ  TYR A 123      60.184  44.980  38.603  1.00 24.94           C  
ATOM    847  OH  TYR A 123      60.168  46.280  38.139  1.00 26.91           O  
ATOM    848  N   VAL A 124      60.314  39.232  42.751  1.00 14.56           N  
ATOM    849  CA  VAL A 124      60.462  37.886  43.301  1.00 15.79           C  
ATOM    850  C   VAL A 124      60.566  37.920  44.837  1.00 13.33           C  
ATOM    851  O   VAL A 124      61.586  38.272  45.424  1.00 13.49           O  
ATOM    852  CB  VAL A 124      61.736  37.207  42.666  1.00 14.02           C  
ATOM    853  CG1 VAL A 124      61.857  35.756  43.122  1.00 14.00           C  
ATOM    854  CG2 VAL A 124      61.628  37.221  41.137  1.00 12.98           C  
ATOM    855  N   GLN A 125      59.480  37.525  45.504  1.00 15.12           N  
ATOM    856  CA  GLN A 125      59.396  37.532  46.964  1.00 14.25           C  
ATOM    857  C   GLN A 125      58.761  36.258  47.480  1.00 14.18           C  
ATOM    858  O   GLN A 125      57.963  35.658  46.781  1.00 12.99           O  
ATOM    859  CB  GLN A 125      58.540  38.710  47.464  1.00 16.30           C  
ATOM    860  CG  GLN A 125      59.202  40.063  47.285  1.00 22.28           C  
ATOM    861  CD  GLN A 125      60.382  40.270  48.215  1.00 27.01           C  
ATOM    862  OE1 GLN A 125      60.210  40.216  49.432  1.00 32.30           O  
ATOM    863  NE2 GLN A 125      61.614  40.482  47.752  1.00 30.01           N  
ATOM    864  N   LEU A 126      59.072  35.839  48.699  1.00 12.49           N  
ATOM    865  CA  LEU A 126      58.465  34.650  49.243  1.00 13.35           C  
ATOM    866  C   LEU A 126      57.043  34.954  49.700  1.00 12.59           C  
ATOM    867  O   LEU A 126      56.705  36.045  50.161  1.00 11.18           O  
ATOM    868  CB  LEU A 126      59.297  34.118  50.426  1.00 12.23           C  
ATOM    869  CG  LEU A 126      60.799  33.912  50.317  1.00 13.20           C  
ATOM    870  CD1 LEU A 126      61.319  33.196  51.553  1.00 14.55           C  
ATOM    871  CD2 LEU A 126      61.109  33.120  49.080  1.00 15.07           C  
ATOM    872  N   GLY A 127      56.200  33.941  49.540  1.00 11.33           N  
ATOM    873  CA  GLY A 127      54.836  33.975  49.957  1.00 11.54           C  
ATOM    874  C   GLY A 127      54.753  33.786  51.454  1.00 13.23           C  
ATOM    875  O   GLY A 127      55.547  33.052  52.038  1.00 14.89           O  
ATOM    876  N   VAL A 128      53.807  34.474  52.086  1.00 12.47           N  
ATOM    877  CA  VAL A 128      53.651  34.406  53.529  1.00 12.66           C  
ATOM    878  C   VAL A 128      52.649  33.269  53.788  1.00 10.38           C  
ATOM    879  O   VAL A 128      51.526  33.321  53.297  1.00 12.45           O  
ATOM    880  CB  VAL A 128      53.125  35.792  54.025  1.00 12.62           C  
ATOM    881  CG1 VAL A 128      52.798  35.658  55.512  1.00 16.46           C  
ATOM    882  CG2 VAL A 128      54.153  36.918  53.813  1.00 12.26           C  
ATOM    883  N   LEU A 129      53.000  32.231  54.574  1.00 12.38           N  
ATOM    884  CA  LEU A 129      52.053  31.181  54.933  1.00 12.53           C  
ATOM    885  C   LEU A 129      51.234  31.506  56.197  1.00 14.42           C  
ATOM    886  O   LEU A 129      51.762  32.177  57.100  1.00 14.93           O  
ATOM    887  CB  LEU A 129      52.850  29.870  55.106  1.00 13.25           C  
ATOM    888  CG  LEU A 129      53.533  29.362  53.833  1.00 14.57           C  
ATOM    889  CD1 LEU A 129      54.094  28.008  54.108  1.00 16.71           C  
ATOM    890  CD2 LEU A 129      52.563  29.223  52.681  1.00 14.81           C  
ATOM    891  N   PRO A 130      49.960  31.099  56.339  1.00 12.78           N  
ATOM    892  CA  PRO A 130      49.205  31.212  57.581  1.00 14.50           C  
ATOM    893  C   PRO A 130      49.726  30.305  58.703  1.00 14.51           C  
ATOM    894  O   PRO A 130      50.451  29.329  58.494  1.00 13.22           O  
ATOM    895  CB  PRO A 130      47.772  30.904  57.177  1.00 12.12           C  
ATOM    896  CG  PRO A 130      47.960  29.939  56.033  1.00 13.92           C  
ATOM    897  CD  PRO A 130      49.144  30.506  55.289  1.00 13.35           C  
ATOM    898  N   ARG A 131      49.411  30.670  59.949  1.00 16.06           N  
ATOM    899  CA  ARG A 131      49.723  29.766  61.050  1.00 17.91           C  
ATOM    900  C   ARG A 131      48.784  28.578  60.973  1.00 13.67           C  
ATOM    901  O   ARG A 131      47.649  28.714  60.483  1.00 12.92           O  
ATOM    902  CB  ARG A 131      49.560  30.491  62.409  1.00 25.93           C  
ATOM    903  CG  ARG A 131      50.680  31.554  62.612  1.00 39.42           C  
ATOM    904  CD  ARG A 131      52.152  31.030  62.666  1.00 50.12           C  
ATOM    905  NE  ARG A 131      53.162  32.110  62.659  1.00 60.31           N  
ATOM    906  CZ  ARG A 131      54.278  32.132  63.441  1.00 65.68           C  
ATOM    907  NH1 ARG A 131      54.577  31.147  64.316  1.00 66.88           N  
ATOM    908  NH2 ARG A 131      55.123  33.181  63.366  1.00 68.80           N  
ATOM    909  N   ALA A 132      49.280  27.411  61.418  1.00 14.22           N  
ATOM    910  CA  ALA A 132      48.519  26.156  61.393  1.00 14.01           C  
ATOM    911  C   ALA A 132      47.173  26.231  62.081  1.00 15.78           C  
ATOM    912  O   ALA A 132      47.078  26.816  63.162  1.00 14.01           O  
ATOM    913  CB  ALA A 132      49.287  25.045  62.070  1.00 16.06           C  
ATOM    914  N   GLY A 133      46.109  25.699  61.454  1.00 12.42           N  
ATOM    915  CA  GLY A 133      44.789  25.646  62.036  1.00 11.40           C  
ATOM    916  C   GLY A 133      43.905  26.836  61.751  1.00 11.68           C  
ATOM    917  O   GLY A 133      42.712  26.772  62.027  1.00 12.16           O  
ATOM    918  N   THR A 134      44.469  27.938  61.230  1.00 12.27           N  
ATOM    919  CA  THR A 134      43.715  29.150  60.918  1.00 12.85           C  
ATOM    920  C   THR A 134      42.583  28.894  59.957  1.00 11.47           C  
ATOM    921  O   THR A 134      42.803  28.385  58.867  1.00 11.69           O  
ATOM    922  CB  THR A 134      44.648  30.227  60.295  1.00 13.66           C  
ATOM    923  OG1 THR A 134      45.687  30.503  61.219  1.00 17.97           O  
ATOM    924  CG2 THR A 134      43.926  31.533  60.032  1.00 17.08           C  
ATOM    925  N   ILE A 135      41.384  29.252  60.348  1.00  9.47           N  
ATOM    926  CA  ILE A 135      40.189  29.186  59.540  1.00 10.97           C  
ATOM    927  C   ILE A 135      39.715  30.642  59.371  1.00 14.31           C  
ATOM    928  O   ILE A 135      39.593  31.399  60.338  1.00 14.95           O  
ATOM    929  CB  ILE A 135      39.094  28.352  60.262  1.00 11.95           C  
ATOM    930  CG1 ILE A 135      39.633  26.968  60.584  1.00 14.79           C  
ATOM    931  CG2 ILE A 135      37.824  28.320  59.428  1.00 14.04           C  
ATOM    932  CD1 ILE A 135      39.932  26.005  59.446  1.00 18.18           C  
ATOM    933  N   LEU A 136      39.430  31.092  58.150  1.00 15.33           N  
ATOM    934  CA  LEU A 136      38.900  32.423  57.908  1.00 15.29           C  
ATOM    935  C   LEU A 136      37.394  32.465  58.111  1.00 16.06           C  
ATOM    936  O   LEU A 136      36.653  31.499  57.870  1.00 15.28           O  
ATOM    937  CB  LEU A 136      39.216  32.880  56.461  1.00 16.04           C  
ATOM    938  CG  LEU A 136      40.704  32.930  56.113  1.00 18.11           C  
ATOM    939  CD1 LEU A 136      40.897  33.096  54.617  1.00 21.51           C  
ATOM    940  CD2 LEU A 136      41.353  34.040  56.921  1.00 19.80           C  
ATOM    941  N   ALA A 137      36.917  33.627  58.553  1.00 16.01           N  
ATOM    942  CA  ALA A 137      35.481  33.798  58.649  1.00 17.87           C  
ATOM    943  C   ALA A 137      34.844  33.866  57.247  1.00 18.01           C  
ATOM    944  O   ALA A 137      35.507  34.108  56.239  1.00 16.27           O  
ATOM    945  CB  ALA A 137      35.174  35.088  59.415  1.00 18.28           C  
ATOM    946  N   ASN A 138      33.532  33.622  57.203  1.00 18.60           N  
ATOM    947  CA  ASN A 138      32.733  33.695  56.001  1.00 18.18           C  
ATOM    948  C   ASN A 138      32.894  35.101  55.484  1.00 19.27           C  
ATOM    949  O   ASN A 138      32.994  36.085  56.229  1.00 17.88           O  
ATOM    950  CB  ASN A 138      31.262  33.470  56.276  1.00 17.20           C  
ATOM    951  CG  ASN A 138      30.433  33.247  55.024  1.00 20.09           C  
ATOM    952  OD1 ASN A 138      30.676  32.313  54.261  1.00 19.28           O  
ATOM    953  ND2 ASN A 138      29.436  34.094  54.767  1.00 20.96           N  
ATOM    954  N   ASN A 139      32.995  35.108  54.165  1.00 18.73           N  
ATOM    955  CA  ASN A 139      33.154  36.302  53.365  1.00 20.28           C  
ATOM    956  C   ASN A 139      34.413  37.113  53.609  1.00 19.05           C  
ATOM    957  O   ASN A 139      34.368  38.332  53.490  1.00 19.23           O  
ATOM    958  CB  ASN A 139      31.929  37.170  53.556  1.00 25.51           C  
ATOM    959  CG  ASN A 139      31.584  37.807  52.234  1.00 34.05           C  
ATOM    960  OD1 ASN A 139      30.958  37.179  51.377  1.00 40.16           O  
ATOM    961  ND2 ASN A 139      32.015  39.048  52.015  1.00 40.04           N  
ATOM    962  N   SER A 140      35.543  36.481  53.963  1.00 15.70           N  
ATOM    963  CA  SER A 140      36.798  37.186  54.122  1.00 14.52           C  
ATOM    964  C   SER A 140      37.315  37.619  52.773  1.00 15.11           C  
ATOM    965  O   SER A 140      37.031  36.951  51.785  1.00 14.47           O  
ATOM    966  CB  SER A 140      37.867  36.321  54.772  1.00 16.20           C  
ATOM    967  OG  SER A 140      37.468  36.086  56.112  1.00 18.16           O  
ATOM    968  N   PRO A 141      38.003  38.759  52.678  1.00 14.63           N  
ATOM    969  CA  PRO A 141      38.577  39.279  51.444  1.00 13.41           C  
ATOM    970  C   PRO A 141      39.807  38.525  51.000  1.00 10.55           C  
ATOM    971  O   PRO A 141      40.833  38.470  51.675  1.00 11.01           O  
ATOM    972  CB  PRO A 141      38.831  40.740  51.769  1.00 14.54           C  
ATOM    973  CG  PRO A 141      39.189  40.734  53.232  1.00 15.28           C  
ATOM    974  CD  PRO A 141      38.095  39.783  53.731  1.00 16.40           C  
ATOM    975  N   CYS A 142      39.669  37.908  49.826  1.00 11.19           N  
ATOM    976  CA  CYS A 142      40.765  37.156  49.211  1.00 10.27           C  
ATOM    977  C   CYS A 142      40.805  37.452  47.732  1.00 10.86           C  
ATOM    978  O   CYS A 142      39.767  37.785  47.149  1.00 12.76           O  
ATOM    979  CB  CYS A 142      40.548  35.673  49.362  1.00 12.32           C  
ATOM    980  SG  CYS A 142      40.395  35.106  51.066  1.00 11.55           S  
ATOM    981  N   TYR A 143      41.991  37.399  47.132  1.00  9.25           N  
ATOM    982  CA  TYR A 143      42.160  37.538  45.699  1.00  7.77           C  
ATOM    983  C   TYR A 143      42.678  36.232  45.103  1.00  9.84           C  
ATOM    984  O   TYR A 143      43.627  35.658  45.663  1.00  9.61           O  
ATOM    985  CB  TYR A 143      43.191  38.602  45.349  1.00  8.46           C  
ATOM    986  CG  TYR A 143      42.556  39.960  45.490  1.00 15.49           C  
ATOM    987  CD1 TYR A 143      42.505  40.616  46.728  1.00 20.51           C  
ATOM    988  CD2 TYR A 143      41.972  40.533  44.365  1.00 18.94           C  
ATOM    989  CE1 TYR A 143      41.852  41.855  46.833  1.00 22.21           C  
ATOM    990  CE2 TYR A 143      41.327  41.768  44.467  1.00 25.19           C  
ATOM    991  CZ  TYR A 143      41.275  42.414  45.699  1.00 25.16           C  
ATOM    992  OH  TYR A 143      40.644  43.636  45.777  1.00 31.74           O  
ATOM    993  N   ILE A 144      42.116  35.757  43.968  1.00  8.83           N  
ATOM    994  CA  ILE A 144      42.751  34.637  43.247  1.00  8.16           C  
ATOM    995  C   ILE A 144      43.617  35.210  42.158  1.00  8.94           C  
ATOM    996  O   ILE A 144      43.264  36.216  41.529  1.00  9.58           O  
ATOM    997  CB  ILE A 144      41.669  33.658  42.648  1.00  7.84           C  
ATOM    998  CG1 ILE A 144      42.414  32.453  42.000  1.00  9.60           C  
ATOM    999  CG2 ILE A 144      40.755  34.349  41.648  1.00  5.35           C  
ATOM   1000  CD1 ILE A 144      41.552  31.284  41.473  1.00  6.07           C  
ATOM   1001  N   THR A 145      44.789  34.652  41.924  1.00  7.93           N  
ATOM   1002  CA  THR A 145      45.569  35.137  40.804  1.00  7.74           C  
ATOM   1003  C   THR A 145      45.991  34.012  39.845  1.00 10.60           C  
ATOM   1004  O   THR A 145      46.172  32.873  40.276  1.00  9.17           O  
ATOM   1005  CB  THR A 145      46.858  35.918  41.281  1.00  5.71           C  
ATOM   1006  OG1 THR A 145      47.622  35.116  42.173  1.00  5.47           O  
ATOM   1007  CG2 THR A 145      46.444  37.275  41.846  1.00  8.19           C  
ATOM   1008  N   GLY A 146      46.149  34.299  38.540  1.00  8.12           N  
ATOM   1009  CA  GLY A 146      46.676  33.295  37.629  1.00  9.19           C  
ATOM   1010  C   GLY A 146      46.537  33.671  36.155  1.00  9.69           C  
ATOM   1011  O   GLY A 146      45.903  34.677  35.803  1.00  8.92           O  
ATOM   1012  N   TRP A 147      47.140  32.807  35.319  1.00  7.68           N  
ATOM   1013  CA  TRP A 147      47.144  32.956  33.862  1.00  7.80           C  
ATOM   1014  C   TRP A 147      46.212  31.971  33.164  1.00  9.38           C  
ATOM   1015  O   TRP A 147      46.263  31.821  31.952  1.00 11.53           O  
ATOM   1016  CB  TRP A 147      48.558  32.739  33.306  1.00  8.48           C  
ATOM   1017  CG  TRP A 147      49.620  33.790  33.632  1.00  9.39           C  
ATOM   1018  CD1 TRP A 147      49.780  34.882  32.834  1.00 10.04           C  
ATOM   1019  CD2 TRP A 147      50.541  33.740  34.652  1.00 10.02           C  
ATOM   1020  NE1 TRP A 147      50.813  35.519  33.335  1.00  8.45           N  
ATOM   1021  CE2 TRP A 147      51.303  34.896  34.408  1.00  9.41           C  
ATOM   1022  CE3 TRP A 147      50.865  32.913  35.729  1.00  7.37           C  
ATOM   1023  CZ2 TRP A 147      52.386  35.235  35.229  1.00 11.23           C  
ATOM   1024  CZ3 TRP A 147      51.953  33.253  36.548  1.00  7.18           C  
ATOM   1025  CH2 TRP A 147      52.716  34.408  36.308  1.00  8.91           C  
ATOM   1026  N   GLY A 148      45.346  31.299  33.929  1.00  9.69           N  
ATOM   1027  CA  GLY A 148      44.410  30.330  33.395  1.00  7.88           C  
ATOM   1028  C   GLY A 148      43.335  30.928  32.510  1.00  9.49           C  
ATOM   1029  O   GLY A 148      43.270  32.144  32.321  1.00 10.20           O  
ATOM   1030  N   LEU A 149      42.438  30.060  32.037  1.00  7.76           N  
ATOM   1031  CA  LEU A 149      41.387  30.425  31.092  1.00  7.74           C  
ATOM   1032  C   LEU A 149      40.533  31.537  31.615  1.00  8.88           C  
ATOM   1033  O   LEU A 149      40.138  31.552  32.795  1.00  9.52           O  
ATOM   1034  CB  LEU A 149      40.429  29.279  30.782  1.00  7.94           C  
ATOM   1035  CG  LEU A 149      40.950  27.945  30.363  1.00  9.90           C  
ATOM   1036  CD1 LEU A 149      39.772  27.102  29.900  1.00 12.79           C  
ATOM   1037  CD2 LEU A 149      42.009  28.104  29.318  1.00 10.28           C  
ATOM   1038  N   THR A 150      40.270  32.468  30.710  1.00  8.87           N  
ATOM   1039  CA  THR A 150      39.468  33.607  31.094  1.00 10.03           C  
ATOM   1040  C   THR A 150      37.977  33.426  30.858  1.00 10.87           C  
ATOM   1041  O   THR A 150      37.150  34.270  31.235  1.00 10.66           O  
ATOM   1042  CB  THR A 150      40.028  34.863  30.362  1.00 10.23           C  
ATOM   1043  OG1 THR A 150      39.856  34.692  28.967  1.00 14.19           O  
ATOM   1044  CG2 THR A 150      41.491  35.069  30.621  1.00  9.13           C  
ATOM   1045  N   ARG A 151      37.589  32.297  30.250  1.00 11.55           N  
ATOM   1046  CA  ARG A 151      36.199  31.916  30.057  1.00 12.27           C  
ATOM   1047  C   ARG A 151      36.241  30.399  30.140  1.00 10.58           C  
ATOM   1048  O   ARG A 151      37.274  29.796  29.839  1.00 11.78           O  
ATOM   1049  CB  ARG A 151      35.622  32.208  28.642  1.00 19.17           C  
ATOM   1050  CG  ARG A 151      35.542  33.557  27.934  1.00 26.69           C  
ATOM   1051  CD  ARG A 151      34.361  34.465  28.283  1.00 34.03           C  
ATOM   1052  NE  ARG A 151      33.052  33.811  28.152  1.00 39.13           N  
ATOM   1053  CZ  ARG A 151      32.061  34.233  27.333  1.00 39.58           C  
ATOM   1054  NH1 ARG A 151      32.169  35.307  26.524  1.00 40.73           N  
ATOM   1055  NH2 ARG A 151      30.897  33.581  27.372  1.00 38.69           N  
ATOM   1056  N   THR A 152      35.125  29.758  30.488  1.00 11.92           N  
ATOM   1057  CA  THR A 152      34.967  28.299  30.424  1.00 12.16           C  
ATOM   1058  C   THR A 152      35.237  27.895  28.963  1.00 14.05           C  
ATOM   1059  O   THR A 152      34.671  28.486  28.039  1.00 14.86           O  
ATOM   1060  CB  THR A 152      33.536  27.922  30.815  1.00  9.41           C  
ATOM   1061  OG1 THR A 152      33.409  28.313  32.174  1.00 14.56           O  
ATOM   1062  CG2 THR A 152      33.199  26.458  30.680  1.00 11.59           C  
ATOM   1063  N   ASN A 153      36.126  26.926  28.749  1.00 14.23           N  
ATOM   1064  CA  ASN A 153      36.538  26.475  27.424  1.00 14.96           C  
ATOM   1065  C   ASN A 153      37.083  27.596  26.559  1.00 14.95           C  
ATOM   1066  O   ASN A 153      36.934  27.509  25.339  1.00 15.11           O  
ATOM   1067  CB  ASN A 153      35.370  25.809  26.676  1.00 19.04           C  
ATOM   1068  CG  ASN A 153      34.910  24.544  27.381  1.00 23.80           C  
ATOM   1069  OD1 ASN A 153      35.706  23.653  27.729  1.00 24.64           O  
ATOM   1070  ND2 ASN A 153      33.596  24.510  27.614  1.00 25.16           N  
ATOM   1071  N   GLY A 154      37.682  28.633  27.180  1.00 13.63           N  
ATOM   1072  CA  GLY A 154      38.293  29.745  26.469  1.00 11.62           C  
ATOM   1073  C   GLY A 154      39.772  29.503  26.257  1.00 13.55           C  
ATOM   1074  O   GLY A 154      40.259  28.392  25.990  1.00 15.18           O  
ATOM   1075  N   GLN A 155      40.527  30.570  26.353  1.00 14.43           N  
ATOM   1076  CA  GLN A 155      41.966  30.447  26.288  1.00 15.79           C  
ATOM   1077  C   GLN A 155      42.712  31.081  27.468  1.00 13.66           C  
ATOM   1078  O   GLN A 155      42.148  31.866  28.224  1.00 10.24           O  
ATOM   1079  CB  GLN A 155      42.494  31.050  24.978  1.00 21.59           C  
ATOM   1080  CG  GLN A 155      42.034  32.419  24.521  1.00 29.39           C  
ATOM   1081  CD  GLN A 155      42.764  32.889  23.260  1.00 34.23           C  
ATOM   1082  OE1 GLN A 155      43.277  32.111  22.451  1.00 36.53           O  
ATOM   1083  NE2 GLN A 155      42.853  34.200  23.067  1.00 36.81           N  
ATOM   1084  N   LEU A 156      43.990  30.734  27.655  1.00 14.13           N  
ATOM   1085  CA  LEU A 156      44.836  31.289  28.717  1.00 14.79           C  
ATOM   1086  C   LEU A 156      44.989  32.798  28.626  1.00 16.90           C  
ATOM   1087  O   LEU A 156      44.858  33.409  27.550  1.00 16.83           O  
ATOM   1088  CB  LEU A 156      46.234  30.698  28.671  1.00 15.94           C  
ATOM   1089  CG  LEU A 156      46.337  29.193  28.964  1.00 19.73           C  
ATOM   1090  CD1 LEU A 156      47.807  28.814  28.724  1.00 20.30           C  
ATOM   1091  CD2 LEU A 156      45.865  28.823  30.392  1.00 16.92           C  
ATOM   1092  N   ALA A 157      45.223  33.437  29.764  1.00 15.33           N  
ATOM   1093  CA  ALA A 157      45.495  34.858  29.753  1.00 15.51           C  
ATOM   1094  C   ALA A 157      46.947  35.040  29.333  1.00 16.07           C  
ATOM   1095  O   ALA A 157      47.813  34.194  29.633  1.00 17.90           O  
ATOM   1096  CB  ALA A 157      45.296  35.403  31.140  1.00 12.82           C  
ATOM   1097  N   GLN A 158      47.257  36.120  28.610  1.00 15.47           N  
ATOM   1098  CA  GLN A 158      48.664  36.437  28.362  1.00 17.41           C  
ATOM   1099  C   GLN A 158      49.301  37.143  29.552  1.00 13.63           C  
ATOM   1100  O   GLN A 158      50.479  36.973  29.807  1.00 14.94           O  
ATOM   1101  CB  GLN A 158      48.861  37.368  27.215  1.00 24.31           C  
ATOM   1102  CG  GLN A 158      48.408  36.857  25.859  1.00 36.06           C  
ATOM   1103  CD  GLN A 158      48.489  37.906  24.729  1.00 42.49           C  
ATOM   1104  OE1 GLN A 158      47.839  37.725  23.689  1.00 46.00           O  
ATOM   1105  NE2 GLN A 158      49.244  39.021  24.843  1.00 44.51           N  
ATOM   1106  N   THR A 159      48.564  37.994  30.273  1.00 14.16           N  
ATOM   1107  CA  THR A 159      49.082  38.719  31.431  1.00 13.59           C  
ATOM   1108  C   THR A 159      48.386  38.250  32.721  1.00 12.30           C  
ATOM   1109  O   THR A 159      47.212  37.843  32.687  1.00 13.30           O  
ATOM   1110  CB  THR A 159      48.863  40.238  31.206  1.00 14.21           C  
ATOM   1111  OG1 THR A 159      47.474  40.482  31.134  1.00 16.33           O  
ATOM   1112  CG2 THR A 159      49.479  40.707  29.901  1.00 15.33           C  
ATOM   1113  N   LEU A 160      49.072  38.369  33.880  1.00 11.84           N  
ATOM   1114  CA  LEU A 160      48.496  37.890  35.143  1.00 12.23           C  
ATOM   1115  C   LEU A 160      47.179  38.597  35.455  1.00 11.95           C  
ATOM   1116  O   LEU A 160      47.063  39.809  35.272  1.00 12.78           O  
ATOM   1117  CB  LEU A 160      49.509  38.104  36.293  1.00 11.08           C  
ATOM   1118  CG  LEU A 160      49.146  37.580  37.676  1.00 10.58           C  
ATOM   1119  CD1 LEU A 160      49.052  36.061  37.608  1.00  8.70           C  
ATOM   1120  CD2 LEU A 160      50.203  37.943  38.681  1.00 10.14           C  
ATOM   1121  N   GLN A 161      46.164  37.806  35.817  1.00  8.13           N  
ATOM   1122  CA  GLN A 161      44.839  38.318  36.151  1.00  9.83           C  
ATOM   1123  C   GLN A 161      44.583  38.159  37.638  1.00 10.91           C  
ATOM   1124  O   GLN A 161      45.180  37.282  38.280  1.00 11.00           O  
ATOM   1125  CB  GLN A 161      43.691  37.548  35.461  1.00 10.26           C  
ATOM   1126  CG  GLN A 161      43.752  37.452  33.946  1.00 12.31           C  
ATOM   1127  CD  GLN A 161      43.575  38.796  33.267  1.00 13.11           C  
ATOM   1128  OE1 GLN A 161      42.483  39.358  33.324  1.00 15.12           O  
ATOM   1129  NE2 GLN A 161      44.620  39.310  32.628  1.00 15.95           N  
ATOM   1130  N   GLN A 162      43.699  38.982  38.181  1.00 10.49           N  
ATOM   1131  CA  GLN A 162      43.262  38.785  39.556  1.00 13.38           C  
ATOM   1132  C   GLN A 162      41.767  39.000  39.660  1.00 12.98           C  
ATOM   1133  O   GLN A 162      41.156  39.715  38.864  1.00 13.63           O  
ATOM   1134  CB  GLN A 162      43.981  39.738  40.506  1.00 14.26           C  
ATOM   1135  CG  GLN A 162      43.684  41.172  40.198  1.00 18.96           C  
ATOM   1136  CD  GLN A 162      44.422  42.100  41.114  1.00 17.04           C  
ATOM   1137  OE1 GLN A 162      45.636  42.113  41.175  1.00 18.54           O  
ATOM   1138  NE2 GLN A 162      43.661  42.902  41.825  1.00 19.42           N  
ATOM   1139  N   ALA A 163      41.127  38.327  40.599  1.00 13.23           N  
ATOM   1140  CA  ALA A 163      39.695  38.494  40.792  1.00 13.22           C  
ATOM   1141  C   ALA A 163      39.435  38.497  42.288  1.00 11.36           C  
ATOM   1142  O   ALA A 163      40.101  37.777  43.036  1.00 11.21           O  
ATOM   1143  CB  ALA A 163      38.880  37.350  40.176  1.00 14.42           C  
ATOM   1144  N   TYR A 164      38.474  39.311  42.731  1.00 11.67           N  
ATOM   1145  CA  TYR A 164      38.141  39.408  44.130  1.00 11.56           C  
ATOM   1146  C   TYR A 164      37.231  38.243  44.395  1.00 10.80           C  
ATOM   1147  O   TYR A 164      36.176  38.123  43.775  1.00 12.70           O  
ATOM   1148  CB  TYR A 164      37.448  40.710  44.359  1.00 12.54           C  
ATOM   1149  CG  TYR A 164      37.040  40.933  45.788  1.00 13.95           C  
ATOM   1150  CD1 TYR A 164      38.014  41.027  46.791  1.00 17.97           C  
ATOM   1151  CD2 TYR A 164      35.687  41.029  46.070  1.00 16.75           C  
ATOM   1152  CE1 TYR A 164      37.615  41.220  48.101  1.00 18.03           C  
ATOM   1153  CE2 TYR A 164      35.281  41.224  47.391  1.00 21.27           C  
ATOM   1154  CZ  TYR A 164      36.248  41.318  48.402  1.00 22.57           C  
ATOM   1155  OH  TYR A 164      35.833  41.496  49.724  1.00 26.64           O  
ATOM   1156  N   LEU A 165      37.643  37.397  45.335  1.00  9.07           N  
ATOM   1157  CA  LEU A 165      36.957  36.131  45.560  1.00 10.37           C  
ATOM   1158  C   LEU A 165      36.810  35.914  47.063  1.00 11.29           C  
ATOM   1159  O   LEU A 165      37.644  35.248  47.661  1.00 11.27           O  
ATOM   1160  CB  LEU A 165      37.787  34.976  44.930  1.00 12.38           C  
ATOM   1161  CG  LEU A 165      37.093  33.893  44.101  1.00 11.95           C  
ATOM   1162  CD1 LEU A 165      36.540  34.532  42.852  1.00  9.43           C  
ATOM   1163  CD2 LEU A 165      38.062  32.782  43.751  1.00  8.65           C  
ATOM   1164  N   PRO A 166      35.818  36.492  47.729  1.00 11.82           N  
ATOM   1165  CA  PRO A 166      35.583  36.361  49.163  1.00 13.01           C  
ATOM   1166  C   PRO A 166      35.260  34.957  49.614  1.00 13.63           C  
ATOM   1167  O   PRO A 166      34.616  34.224  48.863  1.00 12.83           O  
ATOM   1168  CB  PRO A 166      34.462  37.318  49.422  1.00 15.56           C  
ATOM   1169  CG  PRO A 166      33.694  37.392  48.119  1.00 16.69           C  
ATOM   1170  CD  PRO A 166      34.823  37.368  47.118  1.00 14.04           C  
ATOM   1171  N   THR A 167      35.620  34.550  50.821  1.00 14.28           N  
ATOM   1172  CA  THR A 167      35.421  33.166  51.166  1.00 12.03           C  
ATOM   1173  C   THR A 167      33.984  32.783  51.463  1.00 13.99           C  
ATOM   1174  O   THR A 167      33.121  33.622  51.727  1.00 13.60           O  
ATOM   1175  CB  THR A 167      36.327  32.814  52.346  1.00 14.28           C  
ATOM   1176  OG1 THR A 167      35.813  33.542  53.453  1.00 12.69           O  
ATOM   1177  CG2 THR A 167      37.805  33.108  52.083  1.00 14.31           C  
ATOM   1178  N   VAL A 168      33.710  31.477  51.351  1.00 12.25           N  
ATOM   1179  CA  VAL A 168      32.398  30.889  51.637  1.00 13.80           C  
ATOM   1180  C   VAL A 168      32.787  29.872  52.697  1.00 16.47           C  
ATOM   1181  O   VAL A 168      33.563  28.951  52.386  1.00 16.50           O  
ATOM   1182  CB  VAL A 168      31.794  30.139  50.415  1.00 11.38           C  
ATOM   1183  CG1 VAL A 168      30.432  29.638  50.754  1.00 12.27           C  
ATOM   1184  CG2 VAL A 168      31.689  31.048  49.222  1.00 14.01           C  
ATOM   1185  N   ASP A 169      32.285  29.980  53.941  1.00 16.38           N  
ATOM   1186  CA  ASP A 169      32.769  29.053  54.947  1.00 18.65           C  
ATOM   1187  C   ASP A 169      32.266  27.632  54.746  1.00 17.74           C  
ATOM   1188  O   ASP A 169      31.359  27.388  53.953  1.00 17.72           O  
ATOM   1189  CB  ASP A 169      32.409  29.582  56.344  1.00 19.48           C  
ATOM   1190  CG  ASP A 169      30.968  29.641  56.817  1.00 24.59           C  
ATOM   1191  OD1 ASP A 169      30.079  29.046  56.217  1.00 26.31           O  
ATOM   1192  OD2 ASP A 169      30.738  30.291  57.834  1.00 24.58           O  
ATOM   1193  N   TYR A 170      32.844  26.713  55.507  1.00 18.85           N  
ATOM   1194  CA  TYR A 170      32.610  25.308  55.315  1.00 19.40           C  
ATOM   1195  C   TYR A 170      31.175  24.909  55.488  1.00 20.05           C  
ATOM   1196  O   TYR A 170      30.680  24.097  54.705  1.00 18.83           O  
ATOM   1197  CB  TYR A 170      33.506  24.536  56.265  1.00 21.04           C  
ATOM   1198  CG  TYR A 170      33.214  23.051  56.250  1.00 23.14           C  
ATOM   1199  CD1 TYR A 170      33.602  22.282  55.145  1.00 26.72           C  
ATOM   1200  CD2 TYR A 170      32.532  22.469  57.332  1.00 26.68           C  
ATOM   1201  CE1 TYR A 170      33.314  20.920  55.119  1.00 25.93           C  
ATOM   1202  CE2 TYR A 170      32.241  21.102  57.307  1.00 27.72           C  
ATOM   1203  CZ  TYR A 170      32.645  20.334  56.199  1.00 28.85           C  
ATOM   1204  OH  TYR A 170      32.446  18.960  56.205  1.00 27.20           O  
ATOM   1205  N   ALA A 171      30.485  25.483  56.457  1.00 19.61           N  
ATOM   1206  CA  ALA A 171      29.101  25.118  56.673  1.00 21.92           C  
ATOM   1207  C   ALA A 171      28.224  25.480  55.490  1.00 23.01           C  
ATOM   1208  O   ALA A 171      27.300  24.738  55.163  1.00 24.62           O  
ATOM   1209  CB  ALA A 171      28.552  25.819  57.901  1.00 22.12           C  
ATOM   1210  N   ILE A 172      28.501  26.598  54.811  1.00 22.62           N  
ATOM   1211  CA  ILE A 172      27.740  26.953  53.626  1.00 22.20           C  
ATOM   1212  C   ILE A 172      28.229  26.155  52.417  1.00 21.87           C  
ATOM   1213  O   ILE A 172      27.414  25.602  51.661  1.00 23.60           O  
ATOM   1214  CB  ILE A 172      27.877  28.447  53.367  1.00 23.58           C  
ATOM   1215  CG1 ILE A 172      27.265  29.244  54.528  1.00 26.43           C  
ATOM   1216  CG2 ILE A 172      27.127  28.796  52.093  1.00 23.26           C  
ATOM   1217  CD1 ILE A 172      27.460  30.777  54.480  1.00 29.86           C  
ATOM   1218  N   CYS A 173      29.550  26.023  52.248  1.00 20.25           N  
ATOM   1219  CA  CYS A 173      30.085  25.356  51.077  1.00 19.04           C  
ATOM   1220  C   CYS A 173      29.723  23.876  50.994  1.00 18.75           C  
ATOM   1221  O   CYS A 173      29.491  23.342  49.908  1.00 16.80           O  
ATOM   1222  CB  CYS A 173      31.593  25.525  51.061  1.00 17.25           C  
ATOM   1223  SG  CYS A 173      32.221  25.307  49.374  1.00 14.89           S  
ATOM   1224  N   SER A 174      29.611  23.206  52.138  1.00 18.61           N  
ATOM   1225  CA  SER A 174      29.246  21.819  52.096  1.00 19.62           C  
ATOM   1226  C   SER A 174      27.756  21.616  52.240  1.00 19.20           C  
ATOM   1227  O   SER A 174      27.318  20.478  52.376  1.00 20.88           O  
ATOM   1228  CB  SER A 174      30.015  21.085  53.173  1.00 19.00           C  
ATOM   1229  OG  SER A 174      29.675  21.542  54.466  1.00 23.92           O  
ATOM   1230  N   SER A 175      26.928  22.660  52.158  1.00 19.31           N  
ATOM   1231  CA  SER A 175      25.500  22.463  52.244  1.00 19.81           C  
ATOM   1232  C   SER A 175      25.071  21.940  50.890  1.00 22.90           C  
ATOM   1233  O   SER A 175      25.757  22.156  49.872  1.00 22.99           O  
ATOM   1234  CB  SER A 175      24.782  23.757  52.557  1.00 17.66           C  
ATOM   1235  OG  SER A 175      24.702  24.666  51.472  1.00 22.90           O  
ATOM   1236  N   SER A 176      23.950  21.222  50.843  1.00 25.07           N  
ATOM   1237  CA  SER A 176      23.537  20.574  49.607  1.00 27.40           C  
ATOM   1238  C   SER A 176      23.314  21.487  48.400  1.00 26.86           C  
ATOM   1239  O   SER A 176      23.465  21.041  47.265  1.00 28.07           O  
ATOM   1240  CB  SER A 176      22.275  19.739  49.916  1.00 30.02           C  
ATOM   1241  OG  SER A 176      21.199  20.458  50.511  1.00 36.25           O  
ATOM   1242  N   SER A 177      23.023  22.778  48.556  1.00 27.00           N  
ATOM   1243  CA  SER A 177      22.851  23.663  47.403  1.00 27.03           C  
ATOM   1244  C   SER A 177      24.156  24.169  46.760  1.00 25.15           C  
ATOM   1245  O   SER A 177      24.150  24.736  45.662  1.00 24.45           O  
ATOM   1246  CB  SER A 177      21.947  24.858  47.831  1.00 29.12           C  
ATOM   1247  OG  SER A 177      22.066  25.296  49.188  1.00 35.57           O  
ATOM   1248  N   TYR A 178      25.282  23.972  47.467  1.00 22.58           N  
ATOM   1249  CA  TYR A 178      26.628  24.306  47.009  1.00 19.15           C  
ATOM   1250  C   TYR A 178      27.369  23.040  46.614  1.00 17.43           C  
ATOM   1251  O   TYR A 178      26.943  22.403  45.659  1.00 16.91           O  
ATOM   1252  CB  TYR A 178      27.403  25.033  48.110  1.00 19.85           C  
ATOM   1253  CG  TYR A 178      26.936  26.453  48.295  1.00 19.44           C  
ATOM   1254  CD1 TYR A 178      25.648  26.697  48.769  1.00 20.35           C  
ATOM   1255  CD2 TYR A 178      27.804  27.490  47.954  1.00 21.19           C  
ATOM   1256  CE1 TYR A 178      25.208  28.000  48.907  1.00 23.84           C  
ATOM   1257  CE2 TYR A 178      27.372  28.796  48.082  1.00 21.78           C  
ATOM   1258  CZ  TYR A 178      26.078  29.036  48.552  1.00 25.26           C  
ATOM   1259  OH  TYR A 178      25.630  30.337  48.640  1.00 29.53           O  
ATOM   1260  N   TRP A 179      28.438  22.590  47.283  1.00 15.81           N  
ATOM   1261  CA  TRP A 179      29.178  21.425  46.843  1.00 14.58           C  
ATOM   1262  C   TRP A 179      28.825  20.158  47.577  1.00 15.60           C  
ATOM   1263  O   TRP A 179      29.259  19.074  47.206  1.00 15.80           O  
ATOM   1264  CB  TRP A 179      30.638  21.704  47.014  1.00 10.68           C  
ATOM   1265  CG  TRP A 179      31.306  22.452  45.874  1.00 13.09           C  
ATOM   1266  CD1 TRP A 179      31.641  23.789  45.945  1.00 12.92           C  
ATOM   1267  CD2 TRP A 179      31.699  21.873  44.701  1.00 13.86           C  
ATOM   1268  NE1 TRP A 179      32.262  24.051  44.808  1.00 12.64           N  
ATOM   1269  CE2 TRP A 179      32.326  22.956  44.034  1.00 12.99           C  
ATOM   1270  CE3 TRP A 179      31.605  20.616  44.123  1.00 13.14           C  
ATOM   1271  CZ2 TRP A 179      32.881  22.776  42.753  1.00 12.21           C  
ATOM   1272  CZ3 TRP A 179      32.149  20.444  42.847  1.00 15.91           C  
ATOM   1273  CH2 TRP A 179      32.782  21.503  42.166  1.00 14.09           C  
ATOM   1274  N   GLY A 180      28.074  20.277  48.664  1.00 15.83           N  
ATOM   1275  CA  GLY A 180      27.719  19.125  49.483  1.00 16.58           C  
ATOM   1276  C   GLY A 180      28.944  18.478  50.082  1.00 18.19           C  
ATOM   1277  O   GLY A 180      29.944  19.129  50.416  1.00 18.94           O  
ATOM   1278  N   SER A 181      28.839  17.145  50.120  1.00 19.51           N  
ATOM   1279  CA  SER A 181      29.881  16.222  50.565  1.00 20.26           C  
ATOM   1280  C   SER A 181      31.235  16.299  49.891  1.00 17.73           C  
ATOM   1281  O   SER A 181      32.232  15.824  50.432  1.00 18.28           O  
ATOM   1282  CB  SER A 181      29.466  14.766  50.390  1.00 22.21           C  
ATOM   1283  OG  SER A 181      28.769  14.312  51.523  1.00 28.46           O  
ATOM   1284  N   THR A 182      31.291  16.821  48.682  1.00 16.34           N  
ATOM   1285  CA  THR A 182      32.539  16.864  47.951  1.00 15.15           C  
ATOM   1286  C   THR A 182      33.515  17.765  48.670  1.00 13.10           C  
ATOM   1287  O   THR A 182      34.690  17.421  48.625  1.00 14.50           O  
ATOM   1288  CB  THR A 182      32.200  17.336  46.539  1.00 17.28           C  
ATOM   1289  OG1 THR A 182      31.377  16.291  46.046  1.00 18.72           O  
ATOM   1290  CG2 THR A 182      33.375  17.574  45.620  1.00 17.98           C  
ATOM   1291  N   VAL A 183      33.120  18.855  49.356  1.00 11.33           N  
ATOM   1292  CA  VAL A 183      34.165  19.646  50.033  1.00 12.21           C  
ATOM   1293  C   VAL A 183      34.349  19.158  51.448  1.00 12.41           C  
ATOM   1294  O   VAL A 183      33.427  18.725  52.124  1.00 15.19           O  
ATOM   1295  CB  VAL A 183      33.888  21.174  50.102  1.00 14.68           C  
ATOM   1296  CG1 VAL A 183      33.857  21.630  48.660  1.00 16.16           C  
ATOM   1297  CG2 VAL A 183      32.628  21.552  50.801  1.00 16.59           C  
ATOM   1298  N   LYS A 184      35.610  19.128  51.798  1.00 11.85           N  
ATOM   1299  CA  LYS A 184      36.046  18.708  53.104  1.00 12.76           C  
ATOM   1300  C   LYS A 184      36.480  19.966  53.849  1.00 14.30           C  
ATOM   1301  O   LYS A 184      36.728  21.024  53.275  1.00 12.58           O  
ATOM   1302  CB  LYS A 184      37.248  17.747  53.006  1.00 10.65           C  
ATOM   1303  CG  LYS A 184      37.052  16.560  52.054  1.00 14.86           C  
ATOM   1304  CD  LYS A 184      35.784  15.804  52.402  1.00 15.58           C  
ATOM   1305  CE  LYS A 184      35.466  14.618  51.488  1.00 18.57           C  
ATOM   1306  NZ  LYS A 184      35.004  15.001  50.158  1.00 16.58           N  
ATOM   1307  N   ASN A 185      36.630  19.812  55.162  1.00 15.07           N  
ATOM   1308  CA  ASN A 185      37.134  20.869  56.020  1.00 17.39           C  
ATOM   1309  C   ASN A 185      38.643  21.147  55.792  1.00 14.69           C  
ATOM   1310  O   ASN A 185      39.116  22.198  56.234  1.00 14.25           O  
ATOM   1311  CB  ASN A 185      36.834  20.492  57.497  1.00 22.38           C  
ATOM   1312  CG  ASN A 185      37.098  21.662  58.459  1.00 29.56           C  
ATOM   1313  OD1 ASN A 185      37.642  21.428  59.538  1.00 34.55           O  
ATOM   1314  ND2 ASN A 185      36.810  22.950  58.173  1.00 31.07           N  
ATOM   1315  N   SER A 186      39.416  20.274  55.081  1.00 10.71           N  
ATOM   1316  CA  SER A 186      40.789  20.543  54.657  1.00  9.08           C  
ATOM   1317  C   SER A 186      40.816  21.433  53.386  1.00  8.56           C  
ATOM   1318  O   SER A 186      41.870  21.577  52.757  1.00  8.90           O  
ATOM   1319  CB  SER A 186      41.531  19.237  54.341  1.00  9.04           C  
ATOM   1320  OG  SER A 186      40.846  18.549  53.296  1.00 10.97           O  
ATOM   1321  N   MET A 187      39.692  22.023  52.979  1.00  7.52           N  
ATOM   1322  CA  MET A 187      39.585  22.867  51.804  1.00 10.21           C  
ATOM   1323  C   MET A 187      38.993  24.237  52.154  1.00 12.42           C  
ATOM   1324  O   MET A 187      38.270  24.386  53.138  1.00 11.96           O  
ATOM   1325  CB  MET A 187      38.671  22.216  50.791  1.00 10.94           C  
ATOM   1326  CG  MET A 187      39.204  20.911  50.205  1.00 11.39           C  
ATOM   1327  SD  MET A 187      37.858  20.000  49.438  1.00 10.12           S  
ATOM   1328  CE  MET A 187      38.604  18.454  49.020  1.00 10.58           C  
ATOM   1329  N   VAL A 188      39.304  25.263  51.350  1.00 12.50           N  
ATOM   1330  CA  VAL A 188      38.697  26.598  51.432  1.00 13.07           C  
ATOM   1331  C   VAL A 188      37.879  26.815  50.155  1.00 11.00           C  
ATOM   1332  O   VAL A 188      38.297  26.453  49.077  1.00 13.48           O  
ATOM   1333  CB  VAL A 188      39.768  27.717  51.529  1.00 13.39           C  
ATOM   1334  CG1 VAL A 188      39.170  29.107  51.572  1.00 13.79           C  
ATOM   1335  CG2 VAL A 188      40.536  27.482  52.798  1.00 12.84           C  
ATOM   1336  N   CYS A 189      36.697  27.373  50.265  1.00 12.00           N  
ATOM   1337  CA  CYS A 189      35.841  27.710  49.152  1.00 11.22           C  
ATOM   1338  C   CYS A 189      35.862  29.210  49.013  1.00 12.82           C  
ATOM   1339  O   CYS A 189      35.793  29.898  50.024  1.00 11.42           O  
ATOM   1340  CB  CYS A 189      34.411  27.300  49.402  1.00 13.78           C  
ATOM   1341  SG  CYS A 189      34.212  25.515  49.558  1.00 12.57           S  
ATOM   1342  N   ALA A 190      35.977  29.752  47.793  1.00 11.38           N  
ATOM   1343  CA  ALA A 190      35.901  31.199  47.611  1.00 10.48           C  
ATOM   1344  C   ALA A 190      35.139  31.493  46.321  1.00 10.01           C  
ATOM   1345  O   ALA A 190      35.229  30.723  45.356  1.00 10.78           O  
ATOM   1346  CB  ALA A 190      37.304  31.764  47.552  1.00  7.99           C  
ATOM   1347  N   GLY A 191      34.278  32.528  46.318  1.00  9.54           N  
ATOM   1348  CA  GLY A 191      33.535  32.923  45.138  1.00 10.94           C  
ATOM   1349  C   GLY A 191      32.145  32.340  45.049  1.00 11.49           C  
ATOM   1350  O   GLY A 191      31.391  32.402  46.015  1.00 15.03           O  
ATOM   1351  N   GLY A 192      31.795  31.810  43.883  1.00 11.09           N  
ATOM   1352  CA  GLY A 192      30.468  31.222  43.705  1.00 11.75           C  
ATOM   1353  C   GLY A 192      29.407  32.187  43.205  1.00 13.13           C  
ATOM   1354  O   GLY A 192      28.250  31.816  43.138  1.00 12.39           O  
ATOM   1355  N   ASP A 193      29.761  33.422  42.839  1.00 14.59           N  
ATOM   1356  CA  ASP A 193      28.770  34.392  42.363  1.00 16.42           C  
ATOM   1357  C   ASP A 193      28.282  34.182  40.922  1.00 17.95           C  
ATOM   1358  O   ASP A 193      27.339  34.831  40.484  1.00 20.10           O  
ATOM   1359  CB  ASP A 193      29.326  35.854  42.519  1.00 17.13           C  
ATOM   1360  CG  ASP A 193      30.544  36.360  41.725  1.00 19.55           C  
ATOM   1361  OD1 ASP A 193      31.034  35.665  40.846  1.00 19.13           O  
ATOM   1362  OD2 ASP A 193      31.043  37.457  41.995  1.00 20.30           O  
ATOM   1363  N   GLY A 194      28.878  33.264  40.170  1.00 17.24           N  
ATOM   1364  CA  GLY A 194      28.495  33.016  38.790  1.00 17.43           C  
ATOM   1365  C   GLY A 194      29.245  33.916  37.820  1.00 18.50           C  
ATOM   1366  O   GLY A 194      29.095  33.748  36.617  1.00 21.56           O  
ATOM   1367  N   VAL A 195      30.084  34.850  38.281  1.00 16.91           N  
ATOM   1368  CA  VAL A 195      30.838  35.793  37.447  1.00 16.26           C  
ATOM   1369  C   VAL A 195      32.346  35.605  37.463  1.00 15.66           C  
ATOM   1370  O   VAL A 195      33.052  35.707  36.457  1.00 15.31           O  
ATOM   1371  CB  VAL A 195      30.553  37.275  37.882  1.00 15.62           C  
ATOM   1372  CG1 VAL A 195      31.218  38.227  36.885  1.00 12.84           C  
ATOM   1373  CG2 VAL A 195      29.042  37.511  37.993  1.00 17.52           C  
ATOM   1374  N   ARG A 196      32.829  35.354  38.673  1.00 14.43           N  
ATOM   1375  CA  ARG A 196      34.244  35.333  38.967  1.00 13.75           C  
ATOM   1376  C   ARG A 196      34.619  33.972  39.483  1.00 10.11           C  
ATOM   1377  O   ARG A 196      33.910  33.436  40.322  1.00 11.55           O  
ATOM   1378  CB  ARG A 196      34.598  36.365  40.036  1.00 16.23           C  
ATOM   1379  CG  ARG A 196      34.460  37.700  39.378  1.00 21.25           C  
ATOM   1380  CD  ARG A 196      34.743  38.820  40.316  1.00 20.80           C  
ATOM   1381  NE  ARG A 196      33.700  38.932  41.323  1.00 21.73           N  
ATOM   1382  CZ  ARG A 196      33.610  40.024  42.086  1.00 22.00           C  
ATOM   1383  NH1 ARG A 196      34.467  41.054  41.927  1.00 20.62           N  
ATOM   1384  NH2 ARG A 196      32.717  40.033  43.077  1.00 21.75           N  
ATOM   1385  N   SER A 197      35.713  33.421  38.988  1.00 10.11           N  
ATOM   1386  CA  SER A 197      36.198  32.147  39.479  1.00  9.45           C  
ATOM   1387  C   SER A 197      37.592  31.883  39.001  1.00  6.91           C  
ATOM   1388  O   SER A 197      38.159  32.562  38.140  1.00  9.22           O  
ATOM   1389  CB  SER A 197      35.297  31.007  38.996  1.00 12.93           C  
ATOM   1390  OG  SER A 197      35.336  30.935  37.577  1.00 20.65           O  
ATOM   1391  N   GLY A 198      38.160  30.827  39.565  1.00  7.32           N  
ATOM   1392  CA  GLY A 198      39.364  30.208  39.003  1.00  8.03           C  
ATOM   1393  C   GLY A 198      38.972  29.406  37.764  1.00  7.77           C  
ATOM   1394  O   GLY A 198      37.780  29.191  37.521  1.00 11.00           O  
ATOM   1395  N   CYS A 199      39.901  28.961  36.939  1.00  8.22           N  
ATOM   1396  CA  CYS A 199      39.509  28.154  35.759  1.00  8.73           C  
ATOM   1397  C   CYS A 199      40.744  27.340  35.398  1.00  8.78           C  
ATOM   1398  O   CYS A 199      41.796  27.568  35.999  1.00 10.58           O  
ATOM   1399  CB  CYS A 199      39.096  29.056  34.534  1.00  9.70           C  
ATOM   1400  SG  CYS A 199      37.954  28.233  33.374  1.00 10.88           S  
ATOM   1401  N   GLN A 200      40.713  26.389  34.451  1.00 10.41           N  
ATOM   1402  CA  GLN A 200      41.885  25.592  34.095  1.00  9.08           C  
ATOM   1403  C   GLN A 200      43.107  26.415  33.856  1.00  9.28           C  
ATOM   1404  O   GLN A 200      42.942  27.456  33.234  1.00 10.66           O  
ATOM   1405  CB  GLN A 200      41.655  24.810  32.835  1.00 15.06           C  
ATOM   1406  CG  GLN A 200      40.680  23.683  33.098  1.00 23.03           C  
ATOM   1407  CD  GLN A 200      39.292  24.017  32.633  1.00 28.01           C  
ATOM   1408  OE1 GLN A 200      38.840  23.535  31.590  1.00 34.19           O  
ATOM   1409  NE2 GLN A 200      38.569  24.812  33.404  1.00 30.17           N  
ATOM   1410  N   GLY A 201      44.286  26.022  34.354  1.00  5.85           N  
ATOM   1411  CA  GLY A 201      45.546  26.785  34.241  1.00  7.92           C  
ATOM   1412  C   GLY A 201      45.821  27.690  35.457  1.00  5.59           C  
ATOM   1413  O   GLY A 201      46.904  28.245  35.569  1.00  8.61           O  
ATOM   1414  N   ASP A 202      44.808  27.926  36.298  1.00  7.47           N  
ATOM   1415  CA  ASP A 202      44.988  28.610  37.575  1.00  6.56           C  
ATOM   1416  C   ASP A 202      45.353  27.604  38.678  1.00  9.54           C  
ATOM   1417  O   ASP A 202      45.887  27.999  39.703  1.00  6.94           O  
ATOM   1418  CB  ASP A 202      43.733  29.345  38.003  1.00  6.07           C  
ATOM   1419  CG  ASP A 202      43.380  30.501  37.103  1.00  4.86           C  
ATOM   1420  OD1 ASP A 202      44.282  31.198  36.652  1.00  8.85           O  
ATOM   1421  OD2 ASP A 202      42.199  30.695  36.860  1.00  7.20           O  
ATOM   1422  N   SER A 203      45.120  26.301  38.460  1.00 12.03           N  
ATOM   1423  CA  SER A 203      45.496  25.184  39.340  1.00 11.28           C  
ATOM   1424  C   SER A 203      46.832  25.356  40.015  1.00  8.97           C  
ATOM   1425  O   SER A 203      47.781  25.791  39.370  1.00  7.68           O  
ATOM   1426  CB  SER A 203      45.580  23.890  38.534  1.00 13.93           C  
ATOM   1427  OG  SER A 203      44.314  23.381  38.110  1.00 16.67           O  
ATOM   1428  N   GLY A 204      46.951  25.077  41.300  1.00  7.04           N  
ATOM   1429  CA  GLY A 204      48.247  25.158  41.935  1.00  6.36           C  
ATOM   1430  C   GLY A 204      48.566  26.524  42.502  1.00  7.46           C  
ATOM   1431  O   GLY A 204      49.417  26.631  43.396  1.00  6.58           O  
ATOM   1432  N   GLY A 205      47.878  27.567  41.978  1.00  7.72           N  
ATOM   1433  CA  GLY A 205      48.228  28.922  42.354  1.00  6.49           C  
ATOM   1434  C   GLY A 205      47.653  29.337  43.694  1.00  7.96           C  
ATOM   1435  O   GLY A 205      46.865  28.597  44.306  1.00  9.08           O  
ATOM   1436  N   PRO A 206      48.010  30.549  44.151  1.00  7.38           N  
ATOM   1437  CA  PRO A 206      47.538  31.146  45.403  1.00  6.75           C  
ATOM   1438  C   PRO A 206      46.131  31.751  45.478  1.00  7.46           C  
ATOM   1439  O   PRO A 206      45.570  32.262  44.485  1.00  6.98           O  
ATOM   1440  CB  PRO A 206      48.619  32.164  45.712  1.00  3.94           C  
ATOM   1441  CG  PRO A 206      48.841  32.717  44.308  1.00  7.28           C  
ATOM   1442  CD  PRO A 206      48.937  31.463  43.457  1.00  4.71           C  
ATOM   1443  N   LEU A 207      45.556  31.637  46.682  1.00  6.01           N  
ATOM   1444  CA  LEU A 207      44.400  32.439  47.073  1.00  6.18           C  
ATOM   1445  C   LEU A 207      45.077  33.308  48.157  1.00  7.30           C  
ATOM   1446  O   LEU A 207      45.624  32.791  49.148  1.00  7.76           O  
ATOM   1447  CB  LEU A 207      43.247  31.589  47.693  1.00  5.97           C  
ATOM   1448  CG  LEU A 207      41.992  32.358  48.218  1.00  4.05           C  
ATOM   1449  CD1 LEU A 207      41.246  33.024  47.068  1.00  6.67           C  
ATOM   1450  CD2 LEU A 207      41.077  31.399  48.970  1.00  7.99           C  
ATOM   1451  N   HIS A 208      45.156  34.627  47.931  1.00  7.62           N  
ATOM   1452  CA  HIS A 208      45.818  35.576  48.844  1.00  7.94           C  
ATOM   1453  C   HIS A 208      44.728  36.187  49.672  1.00  8.26           C  
ATOM   1454  O   HIS A 208      43.806  36.778  49.103  1.00  8.96           O  
ATOM   1455  CB  HIS A 208      46.483  36.740  48.138  1.00  6.17           C  
ATOM   1456  CG  HIS A 208      47.324  36.319  46.959  1.00  9.32           C  
ATOM   1457  ND1 HIS A 208      48.604  35.971  46.999  1.00  8.26           N  
ATOM   1458  CD2 HIS A 208      46.916  36.270  45.636  1.00 10.85           C  
ATOM   1459  CE1 HIS A 208      49.011  35.724  45.759  1.00 10.58           C  
ATOM   1460  NE2 HIS A 208      47.979  35.909  44.963  1.00 12.70           N  
ATOM   1461  N   CYS A 209      44.794  36.094  51.003  1.00 10.31           N  
ATOM   1462  CA  CYS A 209      43.768  36.662  51.874  1.00  9.59           C  
ATOM   1463  C   CYS A 209      44.396  37.619  52.867  1.00 10.04           C  
ATOM   1464  O   CYS A 209      45.472  37.361  53.397  1.00  9.32           O  
ATOM   1465  CB  CYS A 209      43.045  35.584  52.653  1.00 10.10           C  
ATOM   1466  SG  CYS A 209      42.199  34.388  51.566  1.00 10.46           S  
ATOM   1467  N   LEU A 210      43.710  38.746  53.064  1.00 12.01           N  
ATOM   1468  CA  LEU A 210      44.150  39.791  53.975  1.00 16.22           C  
ATOM   1469  C   LEU A 210      43.758  39.469  55.432  1.00 16.11           C  
ATOM   1470  O   LEU A 210      42.593  39.391  55.823  1.00 16.56           O  
ATOM   1471  CB  LEU A 210      43.540  41.143  53.518  1.00 18.02           C  
ATOM   1472  CG  LEU A 210      44.065  42.433  54.201  1.00 21.65           C  
ATOM   1473  CD1 LEU A 210      45.570  42.555  53.951  1.00 22.49           C  
ATOM   1474  CD2 LEU A 210      43.335  43.663  53.655  1.00 21.54           C  
ATOM   1475  N   VAL A 211      44.793  39.255  56.242  1.00 16.99           N  
ATOM   1476  CA  VAL A 211      44.675  38.906  57.646  1.00 19.04           C  
ATOM   1477  C   VAL A 211      45.700  39.779  58.367  1.00 18.36           C  
ATOM   1478  O   VAL A 211      46.889  39.687  58.062  1.00 18.05           O  
ATOM   1479  CB  VAL A 211      45.020  37.417  57.848  1.00 22.08           C  
ATOM   1480  CG1 VAL A 211      45.077  37.062  59.313  1.00 23.93           C  
ATOM   1481  CG2 VAL A 211      43.955  36.568  57.209  1.00 22.44           C  
ATOM   1482  N   ASN A 212      45.276  40.627  59.315  1.00 18.74           N  
ATOM   1483  CA  ASN A 212      46.155  41.475  60.132  1.00 19.98           C  
ATOM   1484  C   ASN A 212      47.094  42.352  59.310  1.00 17.73           C  
ATOM   1485  O   ASN A 212      48.302  42.401  59.529  1.00 18.87           O  
ATOM   1486  CB  ASN A 212      47.006  40.618  61.097  1.00 23.71           C  
ATOM   1487  CG  ASN A 212      46.182  39.752  62.055  1.00 29.76           C  
ATOM   1488  OD1 ASN A 212      46.465  38.561  62.278  1.00 32.63           O  
ATOM   1489  ND2 ASN A 212      45.134  40.342  62.634  1.00 31.27           N  
ATOM   1490  N   GLY A 213      46.493  42.964  58.294  1.00 14.91           N  
ATOM   1491  CA  GLY A 213      47.178  43.897  57.444  1.00 11.87           C  
ATOM   1492  C   GLY A 213      48.185  43.275  56.525  1.00 14.76           C  
ATOM   1493  O   GLY A 213      48.959  43.999  55.912  1.00 15.07           O  
ATOM   1494  N   GLN A 214      48.179  41.950  56.359  1.00 14.17           N  
ATOM   1495  CA  GLN A 214      49.205  41.263  55.586  1.00 15.43           C  
ATOM   1496  C   GLN A 214      48.533  40.284  54.615  1.00 14.62           C  
ATOM   1497  O   GLN A 214      47.610  39.603  55.041  1.00 14.30           O  
ATOM   1498  CB  GLN A 214      50.066  40.555  56.605  1.00 15.94           C  
ATOM   1499  CG  GLN A 214      51.264  39.860  56.048  1.00 19.80           C  
ATOM   1500  CD  GLN A 214      52.128  39.170  57.107  1.00 20.39           C  
ATOM   1501  OE1 GLN A 214      53.320  39.473  57.259  1.00 24.35           O  
ATOM   1502  NE2 GLN A 214      51.558  38.197  57.822  1.00 22.43           N  
ATOM   1503  N   TYR A 215      48.833  40.202  53.315  1.00 14.11           N  
ATOM   1504  CA  TYR A 215      48.265  39.149  52.483  1.00 13.61           C  
ATOM   1505  C   TYR A 215      48.968  37.829  52.723  1.00 12.39           C  
ATOM   1506  O   TYR A 215      50.180  37.793  52.619  1.00 14.64           O  
ATOM   1507  CB  TYR A 215      48.425  39.498  51.061  1.00 14.44           C  
ATOM   1508  CG  TYR A 215      47.258  40.356  50.629  1.00 17.88           C  
ATOM   1509  CD1 TYR A 215      46.036  39.744  50.371  1.00 16.16           C  
ATOM   1510  CD2 TYR A 215      47.408  41.735  50.451  1.00 21.97           C  
ATOM   1511  CE1 TYR A 215      44.961  40.494  49.925  1.00 19.19           C  
ATOM   1512  CE2 TYR A 215      46.325  42.500  50.006  1.00 24.30           C  
ATOM   1513  CZ  TYR A 215      45.117  41.856  49.746  1.00 24.11           C  
ATOM   1514  OH  TYR A 215      44.033  42.565  49.282  1.00 30.65           O  
ATOM   1515  N   ALA A 216      48.285  36.763  53.100  1.00 11.17           N  
ATOM   1516  CA  ALA A 216      48.944  35.488  53.251  1.00  8.90           C  
ATOM   1517  C   ALA A 216      48.295  34.521  52.289  1.00  9.12           C  
ATOM   1518  O   ALA A 216      47.155  34.705  51.878  1.00  6.94           O  
ATOM   1519  CB  ALA A 216      48.780  34.987  54.667  1.00  9.71           C  
ATOM   1520  N   VAL A 217      49.005  33.475  51.896  1.00  9.17           N  
ATOM   1521  CA  VAL A 217      48.483  32.483  50.937  1.00  9.15           C  
ATOM   1522  C   VAL A 217      47.743  31.400  51.731  1.00  8.85           C  
ATOM   1523  O   VAL A 217      48.356  30.558  52.388  1.00 10.09           O  
ATOM   1524  CB  VAL A 217      49.665  31.869  50.140  1.00 12.18           C  
ATOM   1525  CG1 VAL A 217      49.106  30.837  49.159  1.00 11.76           C  
ATOM   1526  CG2 VAL A 217      50.492  32.965  49.462  1.00 10.13           C  
ATOM   1527  N   HIS A 218      46.408  31.436  51.679  1.00  7.84           N  
ATOM   1528  CA  HIS A 218      45.553  30.528  52.425  1.00  7.30           C  
ATOM   1529  C   HIS A 218      45.050  29.356  51.584  1.00  8.46           C  
ATOM   1530  O   HIS A 218      44.526  28.366  52.131  1.00  8.23           O  
ATOM   1531  CB  HIS A 218      44.340  31.284  52.967  1.00  8.92           C  
ATOM   1532  CG  HIS A 218      44.628  32.019  54.279  1.00 10.64           C  
ATOM   1533  ND1 HIS A 218      44.180  31.691  55.493  1.00 10.75           N  
ATOM   1534  CD2 HIS A 218      45.483  33.092  54.419  1.00 14.34           C  
ATOM   1535  CE1 HIS A 218      44.743  32.506  56.359  1.00 14.78           C  
ATOM   1536  NE2 HIS A 218      45.531  33.354  55.706  1.00 12.41           N  
ATOM   1537  N   GLY A 219      45.180  29.445  50.250  1.00  7.23           N  
ATOM   1538  CA  GLY A 219      44.659  28.367  49.401  1.00  6.28           C  
ATOM   1539  C   GLY A 219      45.628  27.993  48.288  1.00  5.34           C  
ATOM   1540  O   GLY A 219      46.475  28.794  47.905  1.00  6.80           O  
ATOM   1541  N   VAL A 220      45.573  26.746  47.822  1.00  7.32           N  
ATOM   1542  CA  VAL A 220      46.273  26.292  46.615  1.00  5.62           C  
ATOM   1543  C   VAL A 220      45.097  25.897  45.701  1.00  6.97           C  
ATOM   1544  O   VAL A 220      44.303  25.011  46.059  1.00  5.93           O  
ATOM   1545  CB  VAL A 220      47.187  25.074  46.930  1.00  6.49           C  
ATOM   1546  CG1 VAL A 220      47.723  24.488  45.651  1.00  7.98           C  
ATOM   1547  CG2 VAL A 220      48.425  25.493  47.714  1.00  7.83           C  
ATOM   1548  N   THR A 221      44.896  26.517  44.525  1.00  6.24           N  
ATOM   1549  CA  THR A 221      43.697  26.257  43.694  1.00  7.32           C  
ATOM   1550  C   THR A 221      43.632  24.790  43.246  1.00  7.97           C  
ATOM   1551  O   THR A 221      44.609  24.220  42.746  1.00  8.36           O  
ATOM   1552  CB  THR A 221      43.699  27.186  42.439  1.00  9.07           C  
ATOM   1553  OG1 THR A 221      43.998  28.538  42.827  1.00  9.53           O  
ATOM   1554  CG2 THR A 221      42.359  27.127  41.752  1.00  5.81           C  
ATOM   1555  N   SER A 222      42.478  24.167  43.465  1.00  8.65           N  
ATOM   1556  CA  SER A 222      42.342  22.742  43.256  1.00  9.57           C  
ATOM   1557  C   SER A 222      41.283  22.365  42.225  1.00  9.40           C  
ATOM   1558  O   SER A 222      41.618  21.664  41.264  1.00 11.94           O  
ATOM   1559  CB  SER A 222      42.014  22.028  44.615  1.00 10.44           C  
ATOM   1560  OG  SER A 222      41.964  20.601  44.518  1.00  7.17           O  
ATOM   1561  N   PHE A 223      40.015  22.755  42.350  1.00  8.26           N  
ATOM   1562  CA  PHE A 223      39.055  22.358  41.358  1.00  9.14           C  
ATOM   1563  C   PHE A 223      37.867  23.321  41.302  1.00 10.35           C  
ATOM   1564  O   PHE A 223      37.628  24.147  42.198  1.00  9.64           O  
ATOM   1565  CB  PHE A 223      38.609  20.871  41.646  1.00 11.15           C  
ATOM   1566  CG  PHE A 223      37.853  20.540  42.948  1.00 11.44           C  
ATOM   1567  CD1 PHE A 223      36.468  20.640  42.988  1.00 10.26           C  
ATOM   1568  CD2 PHE A 223      38.546  20.139  44.094  1.00 12.61           C  
ATOM   1569  CE1 PHE A 223      35.764  20.354  44.151  1.00  9.32           C  
ATOM   1570  CE2 PHE A 223      37.825  19.861  45.254  1.00  9.67           C  
ATOM   1571  CZ  PHE A 223      36.444  19.968  45.285  1.00  9.35           C  
ATOM   1572  N   VAL A 224      37.205  23.238  40.143  1.00  7.66           N  
ATOM   1573  CA  VAL A 224      35.974  23.926  39.837  1.00  8.11           C  
ATOM   1574  C   VAL A 224      34.993  22.874  39.315  1.00  8.11           C  
ATOM   1575  O   VAL A 224      35.315  21.698  39.126  1.00  9.71           O  
ATOM   1576  CB  VAL A 224      36.170  25.046  38.756  1.00  8.31           C  
ATOM   1577  CG1 VAL A 224      36.999  26.192  39.339  1.00  8.77           C  
ATOM   1578  CG2 VAL A 224      36.889  24.517  37.531  1.00 10.84           C  
ATOM   1579  N   SER A 225      33.761  23.296  39.101  1.00 10.38           N  
ATOM   1580  CA  SER A 225      32.715  22.444  38.562  1.00 12.28           C  
ATOM   1581  C   SER A 225      33.063  21.936  37.174  1.00 14.77           C  
ATOM   1582  O   SER A 225      33.660  22.645  36.369  1.00 12.00           O  
ATOM   1583  CB  SER A 225      31.448  23.248  38.492  1.00 14.44           C  
ATOM   1584  OG  SER A 225      30.392  22.488  37.935  1.00 13.00           O  
ATOM   1585  N   ARG A 226      32.699  20.687  36.902  1.00 17.12           N  
ATOM   1586  CA  ARG A 226      32.858  20.143  35.565  1.00 18.88           C  
ATOM   1587  C   ARG A 226      31.826  20.845  34.693  1.00 18.19           C  
ATOM   1588  O   ARG A 226      32.024  20.845  33.488  1.00 19.46           O  
ATOM   1589  CB AARG A 226      32.636  18.611  35.532  0.50 18.28           C  
ATOM   1590  CB BARG A 226      32.590  18.632  35.482  0.50 18.93           C  
ATOM   1591  CG AARG A 226      31.274  18.031  35.871  0.50 19.97           C  
ATOM   1592  CG BARG A 226      31.198  18.143  35.851  0.50 21.01           C  
ATOM   1593  CD AARG A 226      31.123  16.550  35.440  0.50 21.61           C  
ATOM   1594  CD BARG A 226      30.827  16.839  35.111  0.50 23.47           C  
ATOM   1595  NE AARG A 226      29.720  16.126  35.490  0.50 19.41           N  
ATOM   1596  NE BARG A 226      29.972  15.985  35.932  0.50 20.33           N  
ATOM   1597  CZ AARG A 226      28.822  16.412  34.535  0.50 19.53           C  
ATOM   1598  CZ BARG A 226      30.508  15.244  36.903  0.50 19.45           C  
ATOM   1599  NH1AARG A 226      29.112  17.100  33.426  0.50 18.71           N  
ATOM   1600  NH1BARG A 226      31.826  15.276  37.111  0.50 22.46           N  
ATOM   1601  NH2AARG A 226      27.558  16.055  34.720  0.50 20.95           N  
ATOM   1602  NH2BARG A 226      29.738  14.534  37.714  0.50 11.80           N  
ATOM   1603  N   LEU A 227      30.761  21.462  35.235  1.00 17.41           N  
ATOM   1604  CA  LEU A 227      29.799  22.189  34.417  1.00 18.32           C  
ATOM   1605  C   LEU A 227      30.280  23.526  33.867  1.00 19.58           C  
ATOM   1606  O   LEU A 227      29.765  24.026  32.857  1.00 21.27           O  
ATOM   1607  CB  LEU A 227      28.570  22.446  35.200  1.00 19.76           C  
ATOM   1608  CG  LEU A 227      27.946  21.156  35.747  1.00 24.84           C  
ATOM   1609  CD1 LEU A 227      26.872  21.537  36.753  1.00 27.60           C  
ATOM   1610  CD2 LEU A 227      27.428  20.276  34.617  1.00 23.53           C  
ATOM   1611  N   GLY A 228      31.285  24.109  34.509  1.00 16.77           N  
ATOM   1612  CA  GLY A 228      31.799  25.392  34.104  1.00 13.99           C  
ATOM   1613  C   GLY A 228      32.636  25.950  35.224  1.00 10.47           C  
ATOM   1614  O   GLY A 228      32.480  25.567  36.365  1.00 10.66           O  
ATOM   1615  N   CYS A 229      33.551  26.837  34.870  1.00 10.47           N  
ATOM   1616  CA  CYS A 229      34.368  27.501  35.845  1.00  9.12           C  
ATOM   1617  C   CYS A 229      33.579  28.478  36.699  1.00  9.74           C  
ATOM   1618  O   CYS A 229      33.635  28.351  37.904  1.00 11.86           O  
ATOM   1619  CB  CYS A 229      35.461  28.201  35.116  1.00  5.24           C  
ATOM   1620  SG  CYS A 229      36.647  27.064  34.364  1.00  9.50           S  
ATOM   1621  N   ASN A 230      32.806  29.430  36.175  1.00 12.90           N  
ATOM   1622  CA  ASN A 230      32.052  30.403  36.965  1.00 11.67           C  
ATOM   1623  C   ASN A 230      30.624  29.969  37.036  1.00 13.70           C  
ATOM   1624  O   ASN A 230      29.784  30.262  36.200  1.00 18.68           O  
ATOM   1625  CB  ASN A 230      32.150  31.779  36.328  1.00 12.51           C  
ATOM   1626  CG  ASN A 230      31.776  31.810  34.847  1.00 14.26           C  
ATOM   1627  OD1 ASN A 230      32.319  31.047  34.041  1.00 13.98           O  
ATOM   1628  ND2 ASN A 230      30.828  32.648  34.433  1.00 14.78           N  
ATOM   1629  N   VAL A 231      30.309  29.176  38.027  1.00 15.22           N  
ATOM   1630  CA  VAL A 231      28.962  28.665  38.205  1.00 17.57           C  
ATOM   1631  C   VAL A 231      28.460  29.105  39.581  1.00 18.17           C  
ATOM   1632  O   VAL A 231      29.160  29.026  40.604  1.00 18.32           O  
ATOM   1633  CB  VAL A 231      29.033  27.119  38.028  1.00 18.26           C  
ATOM   1634  CG1 VAL A 231      27.718  26.430  38.416  1.00 19.20           C  
ATOM   1635  CG2 VAL A 231      29.253  26.822  36.552  1.00 18.38           C  
ATOM   1636  N   THR A 232      27.252  29.684  39.547  1.00 19.07           N  
ATOM   1637  CA  THR A 232      26.557  30.130  40.750  1.00 22.11           C  
ATOM   1638  C   THR A 232      26.427  28.953  41.724  1.00 21.83           C  
ATOM   1639  O   THR A 232      26.035  27.833  41.361  1.00 21.80           O  
ATOM   1640  CB  THR A 232      25.152  30.674  40.380  1.00 23.60           C  
ATOM   1641  OG1 THR A 232      25.324  31.816  39.534  1.00 26.85           O  
ATOM   1642  CG2 THR A 232      24.377  31.112  41.603  1.00 26.52           C  
ATOM   1643  N   ARG A 233      26.805  29.244  42.976  1.00 20.88           N  
ATOM   1644  CA  ARG A 233      26.821  28.277  44.076  1.00 21.90           C  
ATOM   1645  C   ARG A 233      27.770  27.111  43.913  1.00 19.36           C  
ATOM   1646  O   ARG A 233      27.629  26.100  44.590  1.00 18.62           O  
ATOM   1647  CB  ARG A 233      25.423  27.699  44.343  1.00 25.56           C  
ATOM   1648  CG  ARG A 233      24.583  28.792  44.884  1.00 29.13           C  
ATOM   1649  CD  ARG A 233      23.164  28.370  45.144  1.00 37.78           C  
ATOM   1650  NE  ARG A 233      22.633  29.481  45.910  1.00 47.82           N  
ATOM   1651  CZ  ARG A 233      22.098  30.584  45.350  1.00 53.44           C  
ATOM   1652  NH1 ARG A 233      21.979  30.739  44.010  1.00 54.84           N  
ATOM   1653  NH2 ARG A 233      21.777  31.606  46.168  1.00 56.42           N  
ATOM   1654  N   LYS A 234      28.756  27.231  43.015  1.00 16.50           N  
ATOM   1655  CA  LYS A 234      29.833  26.254  42.974  1.00 14.24           C  
ATOM   1656  C   LYS A 234      31.094  27.079  43.073  1.00 12.98           C  
ATOM   1657  O   LYS A 234      31.812  27.264  42.098  1.00 11.14           O  
ATOM   1658  CB  LYS A 234      29.881  25.453  41.686  1.00 13.88           C  
ATOM   1659  CG  LYS A 234      28.765  24.457  41.559  1.00 20.97           C  
ATOM   1660  CD  LYS A 234      29.059  23.243  42.404  1.00 24.77           C  
ATOM   1661  CE  LYS A 234      27.987  22.184  42.249  1.00 31.09           C  
ATOM   1662  NZ  LYS A 234      26.726  22.697  42.765  1.00 35.24           N  
ATOM   1663  N   PRO A 235      31.448  27.607  44.239  1.00 12.98           N  
ATOM   1664  CA  PRO A 235      32.662  28.391  44.392  1.00 11.47           C  
ATOM   1665  C   PRO A 235      33.895  27.618  44.007  1.00 10.04           C  
ATOM   1666  O   PRO A 235      33.837  26.388  43.918  1.00  9.33           O  
ATOM   1667  CB  PRO A 235      32.591  28.818  45.835  1.00 11.41           C  
ATOM   1668  CG  PRO A 235      31.722  27.811  46.523  1.00 13.56           C  
ATOM   1669  CD  PRO A 235      30.701  27.457  45.487  1.00 11.50           C  
ATOM   1670  N   THR A 236      34.982  28.324  43.701  1.00  7.10           N  
ATOM   1671  CA  THR A 236      36.247  27.684  43.400  1.00  7.02           C  
ATOM   1672  C   THR A 236      36.744  27.023  44.699  1.00  8.02           C  
ATOM   1673  O   THR A 236      36.590  27.597  45.793  1.00  7.37           O  
ATOM   1674  CB  THR A 236      37.265  28.728  42.925  1.00  5.25           C  
ATOM   1675  OG1 THR A 236      36.707  29.407  41.795  1.00  8.21           O  
ATOM   1676  CG2 THR A 236      38.580  28.104  42.538  1.00  2.88           C  
ATOM   1677  N   VAL A 237      37.346  25.819  44.586  1.00  6.84           N  
ATOM   1678  CA  VAL A 237      37.793  25.077  45.766  1.00  7.14           C  
ATOM   1679  C   VAL A 237      39.310  24.989  45.794  1.00  7.29           C  
ATOM   1680  O   VAL A 237      39.975  24.661  44.795  1.00  7.33           O  
ATOM   1681  CB  VAL A 237      37.184  23.639  45.789  1.00  7.85           C  
ATOM   1682  CG1 VAL A 237      37.542  22.927  47.128  1.00  8.17           C  
ATOM   1683  CG2 VAL A 237      35.682  23.721  45.640  1.00  9.59           C  
ATOM   1684  N   PHE A 238      39.836  25.268  47.011  1.00  7.55           N  
ATOM   1685  CA  PHE A 238      41.248  25.374  47.286  1.00  5.97           C  
ATOM   1686  C   PHE A 238      41.704  24.385  48.358  1.00  6.46           C  
ATOM   1687  O   PHE A 238      40.933  24.045  49.248  1.00  8.93           O  
ATOM   1688  CB  PHE A 238      41.577  26.786  47.779  1.00  7.26           C  
ATOM   1689  CG  PHE A 238      41.203  27.888  46.803  1.00  7.68           C  
ATOM   1690  CD1 PHE A 238      39.888  28.361  46.738  1.00  8.41           C  
ATOM   1691  CD2 PHE A 238      42.187  28.379  45.927  1.00  5.27           C  
ATOM   1692  CE1 PHE A 238      39.554  29.319  45.788  1.00  6.40           C  
ATOM   1693  CE2 PHE A 238      41.836  29.339  44.976  1.00  5.48           C  
ATOM   1694  CZ  PHE A 238      40.528  29.801  44.914  1.00  6.98           C  
ATOM   1695  N   THR A 239      42.930  23.878  48.300  1.00  5.52           N  
ATOM   1696  CA  THR A 239      43.525  23.120  49.397  1.00  6.64           C  
ATOM   1697  C   THR A 239      43.773  24.150  50.507  1.00  7.11           C  
ATOM   1698  O   THR A 239      44.362  25.190  50.204  1.00  7.28           O  
ATOM   1699  CB  THR A 239      44.839  22.513  48.957  1.00  5.02           C  
ATOM   1700  OG1 THR A 239      44.467  21.693  47.867  1.00  7.25           O  
ATOM   1701  CG2 THR A 239      45.551  21.690  49.984  1.00  8.52           C  
ATOM   1702  N   ARG A 240      43.355  23.877  51.761  1.00  7.86           N  
ATOM   1703  CA  ARG A 240      43.561  24.827  52.848  1.00  6.80           C  
ATOM   1704  C   ARG A 240      44.978  24.704  53.338  1.00  7.30           C  
ATOM   1705  O   ARG A 240      45.380  23.731  53.990  1.00 10.68           O  
ATOM   1706  CB  ARG A 240      42.520  24.564  53.993  1.00  8.62           C  
ATOM   1707  CG  ARG A 240      42.716  25.564  55.145  1.00  8.87           C  
ATOM   1708  CD  ARG A 240      41.536  25.653  56.067  1.00  8.61           C  
ATOM   1709  NE  ARG A 240      41.221  24.374  56.687  1.00 11.56           N  
ATOM   1710  CZ  ARG A 240      41.903  23.795  57.693  1.00  9.55           C  
ATOM   1711  NH1 ARG A 240      42.978  24.334  58.250  1.00  8.42           N  
ATOM   1712  NH2 ARG A 240      41.432  22.638  58.178  1.00  8.69           N  
ATOM   1713  N   VAL A 241      45.804  25.730  53.047  1.00  6.78           N  
ATOM   1714  CA  VAL A 241      47.224  25.673  53.358  1.00  7.67           C  
ATOM   1715  C   VAL A 241      47.477  25.524  54.872  1.00  7.96           C  
ATOM   1716  O   VAL A 241      48.393  24.794  55.248  1.00  7.52           O  
ATOM   1717  CB  VAL A 241      47.932  26.945  52.800  1.00  8.15           C  
ATOM   1718  CG1 VAL A 241      49.359  27.081  53.289  1.00  5.92           C  
ATOM   1719  CG2 VAL A 241      47.919  26.850  51.265  1.00  6.16           C  
ATOM   1720  N   SER A 242      46.633  26.129  55.732  1.00  6.90           N  
ATOM   1721  CA  SER A 242      46.862  26.061  57.180  1.00  9.87           C  
ATOM   1722  C   SER A 242      46.687  24.647  57.739  1.00 11.50           C  
ATOM   1723  O   SER A 242      47.135  24.390  58.850  1.00 10.55           O  
ATOM   1724  CB  SER A 242      45.909  27.017  57.926  1.00  6.38           C  
ATOM   1725  OG  SER A 242      44.558  26.626  57.971  1.00  7.15           O  
ATOM   1726  N   ALA A 243      46.080  23.711  56.973  1.00 11.57           N  
ATOM   1727  CA  ALA A 243      45.964  22.335  57.399  1.00 11.12           C  
ATOM   1728  C   ALA A 243      47.248  21.578  57.116  1.00 11.17           C  
ATOM   1729  O   ALA A 243      47.410  20.456  57.591  1.00 13.38           O  
ATOM   1730  CB  ALA A 243      44.809  21.659  56.669  1.00  8.87           C  
ATOM   1731  N   TYR A 244      48.231  22.171  56.442  1.00  8.71           N  
ATOM   1732  CA  TYR A 244      49.429  21.466  56.001  1.00  9.59           C  
ATOM   1733  C   TYR A 244      50.741  22.034  56.457  1.00  9.55           C  
ATOM   1734  O   TYR A 244      51.796  21.637  55.969  1.00 10.53           O  
ATOM   1735  CB  TYR A 244      49.437  21.389  54.445  1.00  9.85           C  
ATOM   1736  CG  TYR A 244      48.266  20.543  53.912  1.00 11.66           C  
ATOM   1737  CD1 TYR A 244      48.373  19.146  53.905  1.00 11.24           C  
ATOM   1738  CD2 TYR A 244      47.065  21.160  53.517  1.00  8.56           C  
ATOM   1739  CE1 TYR A 244      47.283  18.375  53.511  1.00  9.19           C  
ATOM   1740  CE2 TYR A 244      45.975  20.388  53.133  1.00  6.79           C  
ATOM   1741  CZ  TYR A 244      46.101  19.005  53.137  1.00  8.12           C  
ATOM   1742  OH  TYR A 244      45.004  18.234  52.809  1.00 10.18           O  
ATOM   1743  N   ILE A 245      50.728  22.928  57.441  1.00 11.15           N  
ATOM   1744  CA  ILE A 245      51.951  23.617  57.834  1.00 11.13           C  
ATOM   1745  C   ILE A 245      53.013  22.684  58.391  1.00 10.97           C  
ATOM   1746  O   ILE A 245      54.177  22.828  58.026  1.00 11.37           O  
ATOM   1747  CB  ILE A 245      51.557  24.735  58.842  1.00  9.25           C  
ATOM   1748  CG1 ILE A 245      50.595  25.722  58.155  1.00 10.37           C  
ATOM   1749  CG2 ILE A 245      52.831  25.389  59.412  1.00 10.03           C  
ATOM   1750  CD1 ILE A 245      51.125  26.399  56.881  1.00 11.86           C  
ATOM   1751  N   SER A 246      52.652  21.695  59.223  1.00 12.45           N  
ATOM   1752  CA  SER A 246      53.628  20.737  59.730  1.00 11.85           C  
ATOM   1753  C   SER A 246      54.232  19.877  58.649  1.00 11.14           C  
ATOM   1754  O   SER A 246      55.438  19.646  58.683  1.00 13.26           O  
ATOM   1755  CB  SER A 246      52.986  19.821  60.742  1.00 17.42           C  
ATOM   1756  OG  SER A 246      52.876  20.618  61.884  1.00 25.47           O  
ATOM   1757  N   TRP A 247      53.436  19.436  57.656  1.00 11.38           N  
ATOM   1758  CA  TRP A 247      53.987  18.615  56.574  1.00 10.46           C  
ATOM   1759  C   TRP A 247      54.981  19.446  55.762  1.00 12.43           C  
ATOM   1760  O   TRP A 247      56.126  19.023  55.545  1.00 10.24           O  
ATOM   1761  CB  TRP A 247      52.812  18.090  55.707  1.00 10.33           C  
ATOM   1762  CG  TRP A 247      53.261  17.313  54.467  1.00 14.12           C  
ATOM   1763  CD1 TRP A 247      53.714  16.023  54.550  1.00 15.22           C  
ATOM   1764  CD2 TRP A 247      53.360  17.829  53.179  1.00 14.99           C  
ATOM   1765  NE1 TRP A 247      54.129  15.729  53.320  1.00 15.11           N  
ATOM   1766  CE2 TRP A 247      53.946  16.760  52.474  1.00 14.91           C  
ATOM   1767  CE3 TRP A 247      53.042  19.022  52.516  1.00 15.78           C  
ATOM   1768  CZ2 TRP A 247      54.234  16.862  51.111  1.00 13.51           C  
ATOM   1769  CZ3 TRP A 247      53.332  19.115  51.144  1.00 16.23           C  
ATOM   1770  CH2 TRP A 247      53.922  18.049  50.455  1.00 16.23           C  
ATOM   1771  N   ILE A 248      54.572  20.698  55.405  1.00 13.24           N  
ATOM   1772  CA  ILE A 248      55.437  21.603  54.640  1.00 13.46           C  
ATOM   1773  C   ILE A 248      56.740  21.840  55.356  1.00 13.85           C  
ATOM   1774  O   ILE A 248      57.794  21.685  54.756  1.00 15.18           O  
ATOM   1775  CB  ILE A 248      54.751  22.959  54.394  1.00 11.46           C  
ATOM   1776  CG1 ILE A 248      53.573  22.727  53.471  1.00 10.52           C  
ATOM   1777  CG2 ILE A 248      55.735  23.964  53.791  1.00 13.13           C  
ATOM   1778  CD1 ILE A 248      52.650  23.931  53.358  1.00 13.12           C  
ATOM   1779  N   ASN A 249      56.708  22.167  56.643  1.00 15.66           N  
ATOM   1780  CA  ASN A 249      57.966  22.361  57.335  1.00 18.53           C  
ATOM   1781  C   ASN A 249      58.814  21.119  57.539  1.00 16.43           C  
ATOM   1782  O   ASN A 249      60.031  21.260  57.491  1.00 17.80           O  
ATOM   1783  CB  ASN A 249      57.724  23.020  58.681  1.00 21.46           C  
ATOM   1784  CG  ASN A 249      57.244  24.449  58.519  1.00 22.86           C  
ATOM   1785  OD1 ASN A 249      56.449  24.895  59.330  1.00 29.97           O  
ATOM   1786  ND2 ASN A 249      57.638  25.244  57.531  1.00 26.91           N  
ATOM   1787  N   ASN A 250      58.213  19.930  57.696  1.00 16.83           N  
ATOM   1788  CA  ASN A 250      58.941  18.651  57.807  1.00 16.47           C  
ATOM   1789  C   ASN A 250      59.611  18.253  56.486  1.00 16.56           C  
ATOM   1790  O   ASN A 250      60.651  17.609  56.494  1.00 16.74           O  
ATOM   1791  CB  ASN A 250      57.970  17.526  58.243  1.00 13.56           C  
ATOM   1792  CG  ASN A 250      57.466  17.622  59.681  1.00 15.43           C  
ATOM   1793  OD1 ASN A 250      56.398  17.164  60.074  1.00 18.41           O  
ATOM   1794  ND2 ASN A 250      58.233  18.199  60.557  1.00 14.31           N  
ATOM   1795  N   VAL A 251      59.059  18.618  55.314  1.00 17.64           N  
ATOM   1796  CA  VAL A 251      59.696  18.335  54.019  1.00 16.18           C  
ATOM   1797  C   VAL A 251      60.857  19.283  53.790  1.00 17.67           C  
ATOM   1798  O   VAL A 251      61.933  18.839  53.397  1.00 18.03           O  
ATOM   1799  CB  VAL A 251      58.690  18.486  52.860  1.00 15.59           C  
ATOM   1800  CG1 VAL A 251      59.319  18.240  51.489  1.00 12.59           C  
ATOM   1801  CG2 VAL A 251      57.588  17.488  53.087  1.00 13.13           C  
ATOM   1802  N   ILE A 252      60.702  20.573  54.053  1.00 19.04           N  
ATOM   1803  CA  ILE A 252      61.769  21.530  53.775  1.00 25.61           C  
ATOM   1804  C   ILE A 252      63.003  21.300  54.650  1.00 29.58           C  
ATOM   1805  O   ILE A 252      64.137  21.321  54.168  1.00 31.98           O  
ATOM   1806  CB  ILE A 252      61.160  22.946  53.947  1.00 25.94           C  
ATOM   1807  CG1 ILE A 252      60.223  23.219  52.786  1.00 26.02           C  
ATOM   1808  CG2 ILE A 252      62.248  24.007  53.990  1.00 28.18           C  
ATOM   1809  CD1 ILE A 252      59.431  24.496  53.108  1.00 31.12           C  
ATOM   1810  N   ALA A 253      62.773  21.069  55.941  1.00 33.64           N  
ATOM   1811  CA  ALA A 253      63.826  20.729  56.888  1.00 39.90           C  
ATOM   1812  C   ALA A 253      64.486  19.356  56.643  1.00 44.78           C  
ATOM   1813  O   ALA A 253      65.631  19.154  57.073  1.00 46.42           O  
ATOM   1814  CB  ALA A 253      63.273  20.715  58.302  1.00 37.88           C  
ATOM   1815  N   SER A 254      63.845  18.359  55.999  1.00 48.99           N  
ATOM   1816  CA  SER A 254      64.540  17.101  55.772  1.00 52.68           C  
ATOM   1817  C   SER A 254      65.070  16.922  54.351  1.00 55.19           C  
ATOM   1818  O   SER A 254      65.847  15.987  54.133  1.00 56.64           O  
ATOM   1819  CB  SER A 254      63.621  15.919  56.142  1.00 53.68           C  
ATOM   1820  OG  SER A 254      62.413  15.811  55.394  1.00 55.52           O  
ATOM   1821  N   ASN A 255      64.721  17.786  53.381  1.00 57.18           N  
ATOM   1822  CA  ASN A 255      65.204  17.656  52.004  1.00 59.60           C  
ATOM   1823  C   ASN A 255      66.166  18.765  51.639  1.00 60.68           C  
ATOM   1824  O   ASN A 255      65.878  19.922  51.956  1.00 63.35           O  
ATOM   1825  CB  ASN A 255      64.083  17.715  50.981  1.00 60.00           C  
ATOM   1826  CG  ASN A 255      63.104  16.556  51.026  1.00 60.85           C  
ATOM   1827  OD1 ASN A 255      63.035  15.771  50.087  1.00 61.78           O  
ATOM   1828  ND2 ASN A 255      62.301  16.382  52.075  1.00 60.59           N  
ATOM   1829  OXT ASN A 255      67.187  18.458  51.029  1.00 62.36           O  
TER    1830      ASN A 255                                                      
HETATM 1831 CA    CA A 280      57.314  37.378  30.072  1.00 20.84          CA  
HETATM 1832  S   SO4 A 290      43.528  21.842  61.312  1.00 42.65           S  
HETATM 1833  O1  SO4 A 290      43.862  22.938  60.486  1.00 41.10           O  
HETATM 1834  O2  SO4 A 290      44.637  20.950  61.397  1.00 43.95           O  
HETATM 1835  O3  SO4 A 290      42.382  21.153  60.795  1.00 41.19           O  
HETATM 1836  O4  SO4 A 290      43.258  22.304  62.628  1.00 44.27           O  
HETATM 1837  C1  0QH A 256      41.149  23.354  37.644  1.00 31.55           C  
HETATM 1838  C2  0QH A 256      41.347  24.616  38.562  1.00 29.79           C  
HETATM 1839  O   0QH A 256      40.738  23.466  36.483  1.00 31.48           O  
HETATM 1840  F1  0QH A 256      41.871  24.392  39.754  1.00 30.45           F  
HETATM 1841  F2  0QH A 256      42.130  25.537  38.058  1.00 27.87           F  
HETATM 1842  F3  0QH A 256      40.210  25.231  38.787  1.00 30.74           F  
HETATM 1843  N   0QH A 256      41.428  22.136  38.149  1.00 32.72           N  
HETATM 1844  CA  0QH A 256      40.800  20.919  37.702  1.00 35.06           C  
HETATM 1845  C   0QH A 256      39.307  21.048  37.435  1.00 37.47           C  
HETATM 1846  O1  0QH A 256      38.514  21.565  38.211  1.00 36.15           O  
HETATM 1847  CB  0QH A 256      41.100  19.869  38.747  1.00 34.44           C  
HETATM 1848  CG  0QH A 256      41.280  18.443  38.288  1.00 36.76           C  
HETATM 1849  CD1 0QH A 256      42.225  18.333  37.087  1.00 36.80           C  
HETATM 1850  CD2 0QH A 256      41.811  17.676  39.479  1.00 38.25           C  
HETATM 1851  N1  0QH A 256      37.773  20.686  35.406  1.00 44.05           N  
HETATM 1852  N2  0QH A 256      39.121  20.568  36.190  1.00 41.52           N  
HETATM 1853  C3  0QH A 256      37.712  22.117  34.940  1.00 46.64           C  
HETATM 1854  C11 0QH A 256      36.522  22.554  34.080  1.00 51.49           C  
HETATM 1855  C21 0QH A 256      35.753  23.641  34.490  1.00 50.39           C  
HETATM 1856  C31 0QH A 256      34.724  24.077  33.677  1.00 52.00           C  
HETATM 1857  C4  0QH A 256      34.426  23.461  32.459  1.00 53.48           C  
HETATM 1858  C5  0QH A 256      35.179  22.373  32.039  1.00 54.08           C  
HETATM 1859  C6  0QH A 256      36.225  21.923  32.850  1.00 54.40           C  
HETATM 1860  C1M 0QH A 256      38.160  19.713  34.316  1.00 46.35           C  
HETATM 1861  CA2 0QH A 256      36.531  20.238  36.106  1.00 42.79           C  
HETATM 1862  CA1 0QH A 256      36.544  18.892  36.812  1.00 41.97           C  
HETATM 1863  O2  0QH A 256      36.668  17.792  36.251  1.00 40.89           O  
HETATM 1864  C12 0QH A 256      36.195  18.351  39.070  1.00 41.34           C  
HETATM 1865  N11 0QH A 256      36.432  19.241  38.103  1.00 41.27           N  
HETATM 1866  C22 0QH A 256      36.820  17.094  39.138  1.00 41.18           C  
HETATM 1867  C32 0QH A 256      36.529  16.229  40.207  1.00 42.70           C  
HETATM 1868  C41 0QH A 256      35.613  16.613  41.216  1.00 40.91           C  
HETATM 1869  C51 0QH A 256      35.007  17.872  41.125  1.00 42.28           C  
HETATM 1870  C61 0QH A 256      35.290  18.723  40.059  1.00 41.35           C  
HETATM 1871  C1' 0QH A 256      35.273  15.697  42.414  1.00 38.52           C  
HETATM 1872  C2' 0QH A 256      35.742  14.242  42.251  1.00 36.76           C  
HETATM 1873  C3' 0QH A 256      33.777  15.691  42.501  1.00 38.27           C  
HETATM 1874  O   HOH A 301      32.882  26.020  39.606  1.00 17.65           O  
HETATM 1875  O   HOH A 302      32.442  29.522  40.356  1.00 21.49           O  
HETATM 1876  O   HOH A 303      31.364  32.109  40.271  1.00 14.39           O  
HETATM 1877  O   HOH A 304      34.013  31.083  41.939  1.00 14.29           O  
HETATM 1878  O   HOH A 305      35.685  27.451  53.086  1.00 14.08           O  
HETATM 1879  O   HOH A 306      35.231  24.442  53.127  1.00 28.89           O  
HETATM 1880  O   HOH A 307      35.490  31.094  55.192  1.00 19.23           O  
HETATM 1881  O   HOH A 308      39.761  29.106  55.841  1.00 14.63           O  
HETATM 1882  O   HOH A 309      53.144  39.621  37.336  1.00 26.14           O  
HETATM 1883  O   HOH A 310      57.464  42.102  35.337  1.00 30.84           O  
HETATM 1884  O   HOH A 311      56.295  39.174  39.811  1.00 21.08           O  
HETATM 1885  O   HOH A 312      45.452  30.812  42.008  1.00  6.92           O  
HETATM 1886  O   HOH A 313      47.449  30.520  39.380  1.00  6.92           O  
HETATM 1887  O   HOH A 314      48.283  30.372  36.744  1.00 10.12           O  
HETATM 1888  O   HOH A 315      50.127  28.060  45.624  1.00  9.45           O  
HETATM 1889  O   HOH A 316      42.549  29.375  56.136  1.00 12.87           O  
HETATM 1890  O   HOH A 317      45.102  28.273  54.960  1.00  9.55           O  
HETATM 1891  O   HOH A 318      41.167  18.810  46.507  1.00 11.18           O  
HETATM 1892  O   HOH A 319      42.862  19.540  48.578  1.00  9.49           O  
HETATM 1893  O   HOH A 320      42.969  19.206  51.337  1.00 13.03           O  
HETATM 1894  O   HOH A 321      57.440  35.699  40.935  1.00 14.74           O  
HETATM 1895  O   HOH A 322      55.936  34.579  38.033  1.00 23.30           O  
HETATM 1896  O   HOH A 323      52.785  39.989  40.333  1.00 25.89           O  
HETATM 1897  O   HOH A 324      33.689  36.733  43.984  1.00 22.09           O  
HETATM 1898  O   HOH A 325      32.752  34.434  42.638  1.00 19.00           O  
HETATM 1899  O   HOH A 326      61.296  18.059  35.669  1.00 30.78           O  
HETATM 1900  O   HOH A 327      60.418  37.615  50.653  1.00 26.97           O  
HETATM 1901  O   HOH A 328      52.092  36.358  50.688  1.00 17.16           O  
HETATM 1902  O   HOH A 329      32.883  31.561  31.264  1.00 23.33           O  
HETATM 1903  O   HOH A 330      43.307  12.818  47.113  1.00 10.74           O  
HETATM 1904  O   HOH A 331      36.720  37.088  32.045  1.00 23.95           O  
HETATM 1905  O   HOH A 332      43.583  34.271  34.093  1.00  8.71           O  
HETATM 1906  O   HOH A 333      64.151  38.662  38.603  1.00 17.67           O  
HETATM 1907  O   HOH A 334      52.858  37.863  46.914  1.00 23.65           O  
HETATM 1908  O   HOH A 335      50.321  18.976  58.535  1.00 26.76           O  
HETATM 1909  O   HOH A 336      40.093  37.345  33.628  1.00 25.03           O  
HETATM 1910  O   HOH A 337      32.158  36.439  33.842  1.00 28.27           O  
HETATM 1911  O   HOH A 338      54.965  37.964  49.272  1.00 44.50           O  
HETATM 1912  O   HOH A 339      48.863  37.454  57.934  1.00 30.43           O  
HETATM 1913  O   HOH A 340      41.448  24.662  62.587  1.00 24.01           O  
HETATM 1914  O   HOH A 341      61.601  23.704  58.048  1.00 33.41           O  
HETATM 1915  O   HOH A 342      66.904  32.764  34.214  1.00 30.56           O  
HETATM 1916  O   HOH A 343      49.238  33.132  26.847  1.00 35.15           O  
HETATM 1917  O   HOH A 344      47.105  44.440  40.996  1.00 20.82           O  
HETATM 1918  O   HOH A 345      47.069  22.275  61.044  1.00 31.32           O  
HETATM 1919  O   HOH A 346      34.646  30.080  59.205  1.00 27.77           O  
HETATM 1920  O   HOH A 347      43.223  10.806  49.056  1.00 30.40           O  
HETATM 1921  O   HOH A 348      67.980  25.297  36.489  1.00 28.90           O  
HETATM 1922  O   HOH A 349      68.279  36.872  47.286  1.00 33.84           O  
HETATM 1923  O   HOH A 350      52.212  27.533  62.384  1.00 28.11           O  
HETATM 1924  O   HOH A 351      57.507  31.607  53.559  1.00 40.44           O  
HETATM 1925  O   HOH A 352      50.195  37.258  48.866  1.00 31.37           O  
HETATM 1926  O   HOH A 353      64.855  31.038  51.212  1.00 39.73           O  
HETATM 1927  O   HOH A 354      48.078  43.679  46.695  1.00 44.90           O  
HETATM 1928  O   HOH A 355      58.415  35.335  29.066  1.00 27.17           O  
HETATM 1929  O   HOH A 356      45.710  38.988  29.308  1.00 38.47           O  
HETATM 1930  O   HOH A 357      51.043  14.003  41.579  1.00 21.25           O  
HETATM 1931  O   HOH A 358      67.908  23.479  45.499  1.00 32.89           O  
HETATM 1932  O   HOH A 359      61.233  13.914  42.154  1.00 33.27           O  
HETATM 1933  O   HOH A 360      36.842  25.273  30.915  1.00 13.93           O  
HETATM 1934  O   HOH A 361      56.471  41.206  37.704  1.00 27.85           O  
HETATM 1935  O   HOH A 362      44.959  29.044  25.226  1.00 33.57           O  
HETATM 1936  O   HOH A 363      38.998  33.020  26.805  1.00 20.64           O  
HETATM 1937  O   HOH A 364      64.429  26.904  30.756  1.00 27.82           O  
HETATM 1938  O   HOH A 365      49.235  16.475  56.392  1.00 29.93           O  
HETATM 1939  O   HOH A 366      44.125  17.192  55.905  1.00 39.61           O  
HETATM 1940  O   HOH A 367      49.797  21.805  60.380  1.00 27.84           O  
HETATM 1941  O   HOH A 368      50.024  19.785  34.563  1.00 30.97           O  
HETATM 1942  O   HOH A 369      46.429  32.844  24.842  1.00 41.62           O  
HETATM 1943  O   HOH A 370      47.931  33.256  60.045  1.00 28.11           O  
HETATM 1944  O   HOH A 371      41.806  45.255  34.043  1.00 30.30           O  
HETATM 1945  O   HOH A 372      63.874  21.873  33.271  1.00 41.07           O  
HETATM 1946  O   HOH A 373      56.782  32.378  30.107  1.00 26.11           O  
HETATM 1947  O   HOH A 374      47.243  34.732  57.808  1.00 23.62           O  
HETATM 1948  O   HOH A 375      37.066  28.697  55.048  1.00 34.12           O  
HETATM 1949  O   HOH A 376      37.249  25.085  56.044  1.00 40.37           O  
HETATM 1950  O   HOH A 377      28.275  17.000  45.695  1.00 37.97           O  
HETATM 1951  O   HOH A 378      42.408  40.137  59.903  1.00 44.03           O  
HETATM 1952  O   HOH A 379      49.251  46.251  34.415  1.00 43.84           O  
HETATM 1953  O   HOH A 380      54.093  37.592  39.323  1.00 34.41           O  
HETATM 1954  O   HOH A 381      48.187  22.582  30.415  1.00 39.01           O  
HETATM 1955  O   HOH A 382      51.483  31.033  26.492  1.00 51.83           O  
HETATM 1956  O   HOH A 383      56.607  12.499  46.037  1.00 23.19           O  
HETATM 1957  O   HOH A 384      55.626  11.776  48.780  1.00 40.69           O  
HETATM 1958  O   HOH A 385      52.534  35.789  59.363  1.00 38.05           O  
HETATM 1959  O   HOH A 386      35.031  27.253  57.241  1.00 29.30           O  
HETATM 1960  O   HOH A 387      32.125  31.879  59.654  1.00 34.45           O  
HETATM 1961  O   HOH A 388      28.198  29.575  58.752  1.00 42.72           O  
HETATM 1962  O   HOH A 389      45.086  35.683  25.607  1.00 31.08           O  
HETATM 1963  O   HOH A 390      32.348  34.623  31.387  1.00 31.83           O  
HETATM 1964  O   HOH A 391      38.765  35.716  59.975  1.00 31.57           O  
HETATM 1965  O   HOH A 392      44.103  41.461  30.834  1.00 49.81           O  
HETATM 1966  O   HOH A 393      41.972  15.911  53.072  1.00 32.93           O  
HETATM 1967  O   HOH A 394      28.002  18.208  53.733  1.00 35.56           O  
HETATM 1968  O   HOH A 395      44.375  23.297  35.373  1.00 22.03           O  
HETATM 1969  O   HOH A 396      30.702  31.211  29.539  1.00 51.18           O  
HETATM 1970  O   HOH A 397      30.494  28.541  32.709  1.00 49.36           O  
HETATM 1971  O   HOH A 398      56.412  21.054  62.131  1.00 43.25           O  
HETATM 1972  O   HOH A 399      44.542  44.447  44.699  1.00 48.81           O  
HETATM 1973  O   HOH A 400      31.898  26.937  58.945  1.00 37.09           O  
HETATM 1974  O   HOH A 401      37.218  41.186  40.473  1.00 38.21           O  
HETATM 1975  O   HOH A 402      26.032  29.330  36.708  1.00 41.30           O  
HETATM 1976  O   HOH A 403      26.133  32.573  45.021  1.00 40.73           O  
HETATM 1977  O   HOH A 404      55.838  42.729  28.694  1.00 41.47           O  
HETATM 1978  O   HOH A 405      42.852  35.753  27.210  1.00 41.44           O  
HETATM 1979  O   HOH A 406      52.225  44.186  55.156  1.00 45.19           O  
HETATM 1980  O   HOH A 407      41.877  18.854  58.058  1.00 45.51           O  
HETATM 1981  O   HOH A 408      26.732  21.589  55.886  1.00 47.70           O  
HETATM 1982  O   HOH A 409      32.690  16.791  53.773  1.00 39.34           O  
HETATM 1983  O   HOH A 410      58.623  17.123  24.197  1.00 44.44           O  
HETATM 1984  O   HOH A 411      65.260  20.092  24.330  1.00 37.78           O  
HETATM 1985  O   HOH A 412      45.751   7.536  49.944  1.00 45.48           O  
HETATM 1986  O   HOH A 413      57.867  17.562  29.038  1.00 39.83           O  
HETATM 1987  O   HOH A 414      28.283  22.782  30.998  1.00 43.50           O  
HETATM 1988  O   HOH A 415      67.326  26.052  33.737  1.00 65.89           O  
HETATM 1989  O   HOH A 416      58.019  14.849  36.117  1.00 20.44           O  
HETATM 1990  O   HOH A 417      51.753  33.322  44.908  1.00 39.55           O  
HETATM 1991  O   HOH A 418      56.671  43.846  45.568  1.00 48.93           O  
HETATM 1992  O   HOH A 419      39.120  23.034  61.598  1.00 42.00           O  
HETATM 1993  O   HOH A 420      41.306  15.026  56.005  1.00 47.08           O  
HETATM 1994  O   HOH A 421      26.653  15.602  48.462  1.00 44.38           O  
HETATM 1995  O   HOH A 422      25.367  17.571  33.210  1.00 40.94           O  
HETATM 1996  O   HOH A 423      42.962  20.877  34.581  1.00 39.92           O  
HETATM 1997  O   HOH A 424      63.325  17.648  23.374  1.00 51.93           O  
HETATM 1998  O   HOH A 425      51.125  42.005  52.466  1.00 33.24           O  
HETATM 1999  O   HOH A 426      44.781   6.738  38.029  1.00 35.75           O  
HETATM 2000  O   HOH A 427      40.801  45.034  42.972  1.00 37.80           O  
HETATM 2001  O   HOH A 428      41.185  41.488  32.038  1.00 41.78           O  
HETATM 2002  O   HOH A 429      50.800  44.806  30.573  1.00 46.30           O  
HETATM 2003  O   HOH A 430      57.885  37.456  52.108  1.00 38.46           O  
HETATM 2004  O   HOH A 431      22.145  21.543  53.132  1.00 41.38           O  
HETATM 2005  O   HOH A 432      41.352  34.096  61.758  1.00 45.89           O  
HETATM 2006  O   HOH A 433      48.397   9.654  43.158  1.00 40.50           O  
HETATM 2007  O   HOH A 434      42.265  45.255  31.328  1.00 40.72           O  
CONECT  231  352                                                                
CONECT  352  231                                                                
CONECT  457 1831                                                                
CONECT  458 1831                                                                
CONECT  472 1831                                                                
CONECT  496 1831                                                                
CONECT  516 1831                                                                
CONECT  537 1831                                                                
CONECT  980 1466                                                                
CONECT 1223 1341                                                                
CONECT 1341 1223                                                                
CONECT 1400 1620                                                                
CONECT 1466  980                                                                
CONECT 1620 1400                                                                
CONECT 1831  457  458  472  496                                                 
CONECT 1831  516  537 1928                                                      
CONECT 1832 1833 1834 1835 1836                                                 
CONECT 1833 1832                                                                
CONECT 1834 1832                                                                
CONECT 1835 1832                                                                
CONECT 1836 1832                                                                
CONECT 1837 1838 1839 1843                                                      
CONECT 1838 1837 1840 1841 1842                                                 
CONECT 1839 1837                                                                
CONECT 1840 1838                                                                
CONECT 1841 1838                                                                
CONECT 1842 1838                                                                
CONECT 1843 1837 1844                                                           
CONECT 1844 1843 1845 1847                                                      
CONECT 1845 1844 1846 1852                                                      
CONECT 1846 1845                                                                
CONECT 1847 1844 1848                                                           
CONECT 1848 1847 1849 1850                                                      
CONECT 1849 1848                                                                
CONECT 1850 1848                                                                
CONECT 1851 1852 1853 1860 1861                                                 
CONECT 1852 1845 1851                                                           
CONECT 1853 1851 1854                                                           
CONECT 1854 1853 1855 1859                                                      
CONECT 1855 1854 1856                                                           
CONECT 1856 1855 1857                                                           
CONECT 1857 1856 1858                                                           
CONECT 1858 1857 1859                                                           
CONECT 1859 1854 1858                                                           
CONECT 1860 1851                                                                
CONECT 1861 1851 1862                                                           
CONECT 1862 1861 1863 1865                                                      
CONECT 1863 1862                                                                
CONECT 1864 1865 1866 1870                                                      
CONECT 1865 1862 1864                                                           
CONECT 1866 1864 1867                                                           
CONECT 1867 1866 1868                                                           
CONECT 1868 1867 1869 1871                                                      
CONECT 1869 1868 1870                                                           
CONECT 1870 1864 1869                                                           
CONECT 1871 1868 1872 1873                                                      
CONECT 1872 1871                                                                
CONECT 1873 1871                                                                
CONECT 1928 1831                                                                
MASTER      392    0    3    2   17    0   10    6 1999    1   59   19          
END