path: root/plip/test/pdb/4alw.pdb

HEADER    TRANSFERASE                             05-MAR-12   4ALW              
TITLE     BENZOFUROPYRIMIDINONE INHIBITORS OF PIM-1                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PIM-1 KINASE;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PROTEIN KINASE DOMAIN, RESIDUES 406-717;                   
COMPND   5 EC: 2.7.1.37;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    TRANSFERASE, PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE PIM-1     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.J.STOUT,L.ADAMS                                                     
REVDAT   1   16-JAN-13 4ALW    0                                                
JRNL        AUTH   A.L.TSUHAKO,D.S.BROWN,E.S.KOLTUN,N.AAY,A.ARCALAS,V.CHAN,     
JRNL        AUTH 2 H.DU,S.ENGST,M.FRANZINI,A.GALAN,P.HUANG,S.JOHNSTON,B.KANE,   
JRNL        AUTH 3 M.H.KIM,A.D.LAIRD,R.LIN,L.MOCK,I.NGAN,M.PACK,G.STOTT,        
JRNL        AUTH 4 T.J.STOUT,P.YU,C.ZAHARIA,W.ZHANG,P.ZHOU,J.M.NUSS,            
JRNL        AUTH 5 P.C.KEARNEY,W.XU                                             
JRNL        TITL   THE DESIGN, SYNTHESIS, AND BIOLOGICAL EVALUATION OF PIM      
JRNL        TITL 2 KINASE INHIBITORS.                                           
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  3732 2012              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   22542012                                                     
JRNL        DOI    10.1016/J.BMCL.2012.04.025                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.92 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.32                          
REMARK   3   NUMBER OF REFLECTIONS             : 31220                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.15781                         
REMARK   3   R VALUE            (WORKING SET) : 0.15516                         
REMARK   3   FREE R VALUE                     : 0.20731                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1670                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.920                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.970                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2214                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.36                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.368                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 142                          
REMARK   3   BIN FREE R VALUE                    : 0.474                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2263                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 337                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.685                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00                                                 
REMARK   3    B22 (A**2) : 0.00                                                 
REMARK   3    B33 (A**2) : 0.00                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.109         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.086         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.009         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2363 ; 0.031 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3211 ; 2.238 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   280 ; 6.771 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;33.585 ;23.065       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   395 ;13.795 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;17.316 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   339 ; 0.191 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1841 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1238 ; 0.236 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1614 ; 0.320 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   298 ; 0.231 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.213 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.278 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1427 ; 1.845 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2231 ; 2.715 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1141 ; 4.345 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   976 ; 6.036 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4ALW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-51570.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 155                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-325)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33275                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.92                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.42                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 7.4                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.33                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.92                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.28                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.60                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: IN-HOUSE PIM1 STRUCTURE                              
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.9                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.00200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       27.00100            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.50150            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       13.50050            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       67.50250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     CYS A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     ASP A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     LEU A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     LEU A   307                                                      
REMARK 465     SER A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     GLY A   310                                                      
REMARK 465     PRO A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     LYS A   313                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A    72     O    HOH A  2047              2.14            
REMARK 500   OG   SER A   222     C2   IMD A  1309              2.03            
REMARK 500   O    HOH A  2016     O    HOH A  2336              2.17            
REMARK 500   O    HOH A  2025     O    HOH A  2064              1.78            
REMARK 500   O    HOH A  2026     O    HOH A  2064              1.78            
REMARK 500   O    HOH A  2058     O    HOH A  2214              2.10            
REMARK 500   O    HOH A  2117     O    HOH A  2123              2.11            
REMARK 500   O    HOH A  2138     O    HOH A  2295              1.97            
REMARK 500   O    HOH A  2194     O    HOH A  2196              2.04            
REMARK 500   O    HOH A  2238     O    HOH A  2243              2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2078     O    HOH A  2289     2544     2.13            
REMARK 500   O    HOH A  2114     O    HOH A  2270     2544     2.19            
REMARK 500   O    HOH A  2277     O    HOH A  2325     3655     1.99            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A 147   CD1   PHE A 147   CE1     0.126                       
REMARK 500    TYR A 207   CD1   TYR A 207   CE1     0.091                       
REMARK 500    GLU A 262   CD    GLU A 262   OE1     0.077                       
REMARK 500    GLU A 262   CG    GLU A 262   CD      0.120                       
REMARK 500    TRP A 269   CG    TRP A 269   CD1     0.092                       
REMARK 500    PHE A 281   CD1   PHE A 281   CE1     0.129                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  57   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    LEU A 118   CB  -  CG  -  CD1 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG A 145   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    CYS A 158   CA  -  CB  -  SG  ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG A 250   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 268   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    CYS A 270   CA  -  CB  -  SG  ANGL. DEV. =  -8.3 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    ASP A 167       46.78   -140.86                                   
REMARK 500    ASP A 186       81.46     71.12                                   
REMARK 500    ASP A 202       32.20   -140.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A   35     SER A   36                  146.50                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A1307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HY7 A1308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A1309                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XQZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HPIM-1 KINASE AT 2.1 A                         
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1XR1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HPIM-1 KINASE IN COMPLEX WITH                  
REMARK 900  AMP-PNPAT 2.1 A RESOLUTION                                          
REMARK 900 RELATED ID: 1XWS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 KINASE DOMAIN                   
REMARK 900 RELATED ID: 1YHS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PIM-1 BOUND TO STAUROSPORINE                   
REMARK 900 RELATED ID: 1YI3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PIM-1 BOUND TO LY294002                        
REMARK 900 RELATED ID: 1YI4   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF PIM-1 BOUND TO ADENOSINE                               
REMARK 900 RELATED ID: 1YWV   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURES OF PROTO-ONCOGENE KINASE PIM1: A                 
REMARK 900  TARGETOF ABERRANT SOMATIC HYPERMUTATIONS IN DIFFUSE LARGE           
REMARK 900   CELLLYMPHOMA                                                       
REMARK 900 RELATED ID: 1YXS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 WITH P123M MUTATION                
REMARK 900 RELATED ID: 1YXT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH                    
REMARK 900  AMPPNP                                                              
REMARK 900 RELATED ID: 1YXU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH AMP                
REMARK 900 RELATED ID: 1YXV   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH 3,4                
REMARK 900  -DIHYDROXY-1-METHYLQUINOLIN-2(1H)-ONE                               
REMARK 900 RELATED ID: 1YXX   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH (3E                
REMARK 900  )-3-[(4-HYDROXYPHENYL)IMINO]-1H-INDOL-2(3H)-ONE                     
REMARK 900 RELATED ID: 2BIK   RELATED DB: PDB                                   
REMARK 900  HUMAN PIM1 PHOSPHORYLATED ON SER261                                 
REMARK 900 RELATED ID: 2BIL   RELATED DB: PDB                                   
REMARK 900  THE HUMAN PROTEIN KINASE PIM1 IN COMPLEX WITH ITS                   
REMARK 900  CONSENSUS PEPTIDE PIMTIDE                                           
REMARK 900 RELATED ID: 2BZH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH                 
REMARK 900  A RUTHENIUM ORGANOMETALLIC LIGAND RU1                               
REMARK 900 RELATED ID: 2BZI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH                 
REMARK 900  A RUTHENIUM ORGANOMETALLIC LIGAND RU2                               
REMARK 900 RELATED ID: 2BZJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH                 
REMARK 900  A RUTHENIUM ORGANOMETALLIC LIGAND RU3                               
REMARK 900 RELATED ID: 2BZK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH                 
REMARK 900  AMPPNP AND PIMTIDE                                                  
REMARK 900 RELATED ID: 2C3I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN PIM1 IN COMPLEX WITH                     
REMARK 900  IMIDAZOPYRIDAZIN I                                                  
REMARK 900 RELATED ID: 2J2I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAB PIM1 IN COMPLEX WITH                 
REMARK 900  LY333531                                                            
REMARK 900 RELATED ID: 2XIX   RELATED DB: PDB                                   
REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-1 FROM                
REMARK 900   CRYSTALLOGRAPHIC FRAGMENT SCREEN                                   
REMARK 900 RELATED ID: 2XIY   RELATED DB: PDB                                   
REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-2 FROM                
REMARK 900   CRYSTALLOGRAPHIC FRAGMENT SCREEN                                   
REMARK 900 RELATED ID: 2XIZ   RELATED DB: PDB                                   
REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-3 FROM                
REMARK 900   CRYSTALLOGRAPHIC FRAGMENT SCREEN                                   
REMARK 900 RELATED ID: 2XJ0   RELATED DB: PDB                                   
REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-4 FROM                
REMARK 900   CRYSTALLOGRAPHIC FRAGMENT SCREEN                                   
REMARK 900 RELATED ID: 2XJ1   RELATED DB: PDB                                   
REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE                 
REMARK 900  INIBITOR                                                            
REMARK 900 RELATED ID: 2XJ2   RELATED DB: PDB                                   
REMARK 900  PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE                 
REMARK 900  INHIBITOR                                                           
REMARK 900 RELATED ID: 4A7C   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PIM1 KINASE WITH ETP46546                      
DBREF  4ALW A    2   313  UNP    P11309   PIM1_HUMAN       2    213             
SEQADV 4ALW MET A  -14  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW HIS A  -13  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW HIS A  -12  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW HIS A  -11  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW HIS A  -10  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW HIS A   -9  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW HIS A   -8  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW GLY A   -7  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW GLU A   -6  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW ASN A   -5  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW LEU A   -4  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW TYR A   -3  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW PHE A   -2  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW GLN A   -1  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW GLY A    0  UNP  P11309              EXPRESSION TAG                 
SEQADV 4ALW SER A    1  UNP  P11309              EXPRESSION TAG                 
SEQRES   1 A  328  MET HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE          
SEQRES   2 A  328  GLN GLY SER LEU LEU SER LYS ILE ASN SER LEU ALA HIS          
SEQRES   3 A  328  LEU ARG ALA ALA PRO CYS ASN ASP LEU HIS ALA THR LYS          
SEQRES   4 A  328  LEU ALA PRO GLY LYS GLU LYS GLU PRO LEU GLU SER GLN          
SEQRES   5 A  328  TYR GLN VAL GLY PRO LEU LEU GLY SER GLY GLY PHE GLY          
SEQRES   6 A  328  SER VAL TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO          
SEQRES   7 A  328  VAL ALA ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP          
SEQRES   8 A  328  TRP GLY GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU          
SEQRES   9 A  328  VAL VAL LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY          
SEQRES  10 A  328  VAL ILE ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER          
SEQRES  11 A  328  PHE VAL LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP          
SEQRES  12 A  328  LEU PHE ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU          
SEQRES  13 A  328  GLU LEU ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA          
SEQRES  14 A  328  VAL ARG HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP          
SEQRES  15 A  328  ILE LYS ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY          
SEQRES  16 A  328  GLU LEU LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU          
SEQRES  17 A  328  LYS ASP THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL          
SEQRES  18 A  328  TYR SER PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS          
SEQRES  19 A  328  GLY ARG SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU          
SEQRES  20 A  328  TYR ASP MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP          
SEQRES  21 A  328  GLU GLU ILE ILE ARG GLY GLN VAL PHE PHE ARG GLN ARG          
SEQRES  22 A  328  VAL SER SER GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU          
SEQRES  23 A  328  ALA LEU ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE          
SEQRES  24 A  328  GLN ASN HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN          
SEQRES  25 A  328  GLU THR ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY          
SEQRES  26 A  328  PRO SER LYS                                                  
HET    IMD  A1307       5                                                       
HET    HY7  A1308      23                                                       
HET    IMD  A1309       5                                                       
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     HY7 8-BROMANYL-2-[(4-METHYLPIPERAZIN-1-YL)METHYL]                    
HETNAM   2 HY7  -3H-[1]BENZOFURO[3,2-D]PYRIMIDIN-4-ONE                          
FORMUL   2  IMD    2(C3 H5 N2 1+)                                               
FORMUL   3  HY7    C16 H17 BR N4 O2                                             
FORMUL   4  HOH   *337(H2 O)                                                    
HELIX    1   1 ASP A   72  ILE A   74  5                                   3    
HELIX    2   2 MET A   88  SER A   97  1                                  10    
HELIX    3   3 LEU A  129  GLY A  137  1                                   9    
HELIX    4   4 GLN A  140  CYS A  161  1                                  22    
HELIX    5   5 LYS A  169  GLU A  171  5                                   3    
HELIX    6   6 ASP A  186  GLY A  190  5                                   5    
HELIX    7   7 THR A  204  SER A  208  5                                   5    
HELIX    8   8 PRO A  209  HIS A  216  1                                   8    
HELIX    9   9 HIS A  219  GLY A  238  1                                  20    
HELIX   10  10 HIS A  244  GLY A  251  1                                   8    
HELIX   11  11 SER A  260  LEU A  271  1                                  12    
HELIX   12  12 ARG A  274  ARG A  278  5                                   5    
HELIX   13  13 THR A  280  ASN A  286  1                                   7    
HELIX   14  14 HIS A  287  GLN A  291  5                                   5    
HELIX   15  15 LEU A  295  LEU A  304  1                                  10    
SHEET    1  AA 5 TYR A  38  GLY A  47  0                                        
SHEET    2  AA 5 GLY A  50  ARG A  57 -1  O  GLY A  50   N  GLY A  47           
SHEET    3  AA 5 LEU A  62  GLU A  70 -1  O  LEU A  62   N  ARG A  57           
SHEET    4  AA 5 SER A 115  GLU A 121 -1  O  PHE A 116   N  VAL A  69           
SHEET    5  AA 5 LEU A 106  GLU A 111 -1  N  LEU A 107   O  ILE A 119           
SHEET    1  AB 2 TRP A  77  GLU A  79  0                                        
SHEET    2  AB 2 ARG A  85  PRO A  87 -1  O  VAL A  86   N  GLY A  78           
SHEET    1  AC 3 VAL A 126  ASP A 128  0                                        
SHEET    2  AC 3 ILE A 173  ASP A 176 -1  O  ILE A 175   N  GLN A 127           
SHEET    3  AC 3 GLU A 181  LEU A 184 -1  O  GLU A 181   N  ASP A 176           
SHEET    1  AD 2 VAL A 163  LEU A 164  0                                        
SHEET    2  AD 2 ALA A 191  LEU A 192 -1  O  ALA A 191   N  LEU A 164           
CISPEP   1 GLU A  124    PRO A  125          0         0.04                     
SITE     1 AC1  7 PHE A 130  ILE A 133  THR A 134  ASP A 170                    
SITE     2 AC1  7 ASP A 234  GLY A 238  ASP A 239                               
SITE     1 AC2 13 PHE A  49  VAL A  52  ALA A  65  LYS A  67                    
SITE     2 AC2 13 LEU A 120  GLU A 121  ASN A 172  LEU A 174                    
SITE     3 AC2 13 ILE A 185  ASP A 186  HOH A2213  HOH A2336                    
SITE     4 AC2 13 HOH A2337                                                     
SITE     1 AC3  5 HIS A 219  ARG A 221  SER A 222  HOH A2249                    
SITE     2 AC3  5 HOH A2302                                                     
CRYST1   97.449   97.449   81.003  90.00  90.00 120.00 P 65          6          
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      0.010262  0.005925  0.000000        0.00000                         
SCALE2      0.000000  0.011849  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012345        0.00000                         
ATOM      1  N   LEU A  34       7.313 -40.565 -13.432  1.00 82.72           N  
ATOM      2  CA  LEU A  34       6.965 -40.395 -11.961  1.00 83.44           C  
ATOM      3  C   LEU A  34       7.884 -41.192 -10.992  1.00 83.01           C  
ATOM      4  O   LEU A  34       8.703 -41.979 -11.452  1.00 83.89           O  
ATOM      5  CB  LEU A  34       5.479 -40.728 -11.705  1.00 83.29           C  
ATOM      6  CG  LEU A  34       5.078 -42.198 -11.565  1.00 83.23           C  
ATOM      7  CD1 LEU A  34       4.052 -42.341 -10.444  1.00 83.91           C  
ATOM      8  CD2 LEU A  34       4.568 -42.753 -12.892  1.00 82.22           C  
ATOM      9  N   GLU A  35       7.761 -40.987  -9.671  1.00 82.39           N  
ATOM     10  CA  GLU A  35       8.551 -41.769  -8.685  1.00 81.26           C  
ATOM     11  C   GLU A  35       7.776 -42.994  -8.257  1.00 79.77           C  
ATOM     12  O   GLU A  35       7.352 -43.138  -7.099  1.00 79.72           O  
ATOM     13  CB  GLU A  35       8.952 -40.969  -7.447  1.00 82.22           C  
ATOM     14  CG  GLU A  35       9.944 -39.814  -7.674  1.00 85.51           C  
ATOM     15  CD  GLU A  35       9.304 -38.566  -8.350  1.00 88.82           C  
ATOM     16  OE1 GLU A  35       8.499 -38.715  -9.312  1.00 88.93           O  
ATOM     17  OE2 GLU A  35       9.632 -37.427  -7.923  1.00 88.92           O  
ATOM     18  N   SER A  36       7.528 -43.830  -9.254  1.00 77.44           N  
ATOM     19  CA  SER A  36       7.471 -45.275  -9.086  1.00 74.71           C  
ATOM     20  C   SER A  36       8.861 -45.839  -9.500  1.00 72.05           C  
ATOM     21  O   SER A  36       9.134 -47.036  -9.322  1.00 71.74           O  
ATOM     22  CB  SER A  36       6.305 -45.888  -9.898  1.00 75.36           C  
ATOM     23  OG  SER A  36       6.175 -45.291 -11.201  1.00 76.24           O  
ATOM     24  N   GLN A  37       9.744 -44.961 -10.007  1.00 68.22           N  
ATOM     25  CA  GLN A  37      11.112 -45.363 -10.388  1.00 64.70           C  
ATOM     26  C   GLN A  37      12.053 -45.487  -9.202  1.00 61.12           C  
ATOM     27  O   GLN A  37      13.144 -46.058  -9.349  1.00 60.46           O  
ATOM     28  CB  GLN A  37      11.740 -44.397 -11.359  1.00 65.23           C  
ATOM     29  CG  GLN A  37      10.796 -43.771 -12.337  1.00 67.99           C  
ATOM     30  CD  GLN A  37      11.521 -42.776 -13.225  1.00 73.03           C  
ATOM     31  OE1 GLN A  37      12.713 -42.968 -13.558  1.00 72.75           O  
ATOM     32  NE2 GLN A  37      10.823 -41.693 -13.601  1.00 72.74           N  
ATOM     33  N   TYR A  38      11.612 -44.988  -8.038  1.00 57.40           N  
ATOM     34  CA  TYR A  38      12.410 -44.965  -6.810  1.00 54.24           C  
ATOM     35  C   TYR A  38      11.716 -45.526  -5.596  1.00 53.47           C  
ATOM     36  O   TYR A  38      10.604 -45.130  -5.296  1.00 53.03           O  
ATOM     37  CB  TYR A  38      12.895 -43.527  -6.498  1.00 53.14           C  
ATOM     38  CG  TYR A  38      13.722 -42.973  -7.614  1.00 49.32           C  
ATOM     39  CD1 TYR A  38      15.036 -43.369  -7.779  1.00 48.19           C  
ATOM     40  CD2 TYR A  38      13.185 -42.068  -8.512  1.00 48.26           C  
ATOM     41  CE1 TYR A  38      15.793 -42.911  -8.852  1.00 48.46           C  
ATOM     42  CE2 TYR A  38      13.939 -41.592  -9.592  1.00 48.12           C  
ATOM     43  CZ  TYR A  38      15.227 -42.026  -9.751  1.00 47.94           C  
ATOM     44  OH  TYR A  38      15.969 -41.535 -10.789  1.00 50.20           O  
ATOM     45  N   GLN A  39      12.396 -46.413  -4.877  1.00 51.30           N  
ATOM     46  CA  GLN A  39      11.944 -46.739  -3.562  1.00 51.65           C  
ATOM     47  C   GLN A  39      12.509 -45.687  -2.555  1.00 50.48           C  
ATOM     48  O   GLN A  39      13.736 -45.611  -2.362  1.00 50.32           O  
ATOM     49  CB  GLN A  39      12.457 -48.106  -3.238  1.00 51.56           C  
ATOM     50  CG  GLN A  39      11.844 -48.807  -2.095  1.00 58.61           C  
ATOM     51  CD  GLN A  39      12.710 -50.025  -1.689  1.00 68.02           C  
ATOM     52  OE1 GLN A  39      13.650 -49.899  -0.883  1.00 73.23           O  
ATOM     53  NE2 GLN A  39      12.424 -51.197  -2.283  1.00 69.47           N  
ATOM     54  N   VAL A  40      11.635 -44.916  -1.906  1.00 48.43           N  
ATOM     55  CA  VAL A  40      12.026 -44.022  -0.832  1.00 45.82           C  
ATOM     56  C   VAL A  40      12.453 -44.755   0.468  1.00 46.04           C  
ATOM     57  O   VAL A  40      11.707 -45.597   0.998  1.00 44.89           O  
ATOM     58  CB  VAL A  40      10.930 -43.012  -0.544  1.00 46.73           C  
ATOM     59  CG1 VAL A  40      11.339 -42.041   0.548  1.00 45.57           C  
ATOM     60  CG2 VAL A  40      10.646 -42.211  -1.771  1.00 45.82           C  
ATOM     61  N   GLY A  41      13.634 -44.429   1.015  1.00 42.27           N  
ATOM     62  CA  GLY A  41      14.066 -45.013   2.313  1.00 40.23           C  
ATOM     63  C   GLY A  41      13.969 -43.912   3.361  1.00 38.17           C  
ATOM     64  O   GLY A  41      13.176 -43.006   3.216  1.00 39.09           O  
ATOM     65  N   PRO A  42      14.756 -43.988   4.434  1.00 37.65           N  
ATOM     66  CA  PRO A  42      14.645 -43.047   5.571  1.00 38.13           C  
ATOM     67  C   PRO A  42      15.018 -41.569   5.230  1.00 38.64           C  
ATOM     68  O   PRO A  42      15.822 -41.311   4.296  1.00 37.19           O  
ATOM     69  CB  PRO A  42      15.685 -43.556   6.551  1.00 38.55           C  
ATOM     70  CG  PRO A  42      16.155 -44.857   6.078  1.00 39.95           C  
ATOM     71  CD  PRO A  42      15.743 -45.057   4.659  1.00 38.97           C  
ATOM     72  N   LEU A  43      14.408 -40.645   5.956  1.00 37.16           N  
ATOM     73  CA  LEU A  43      14.760 -39.263   5.891  1.00 36.56           C  
ATOM     74  C   LEU A  43      16.258 -39.157   6.287  1.00 38.01           C  
ATOM     75  O   LEU A  43      16.628 -39.706   7.314  1.00 38.49           O  
ATOM     76  CB  LEU A  43      13.900 -38.492   6.864  1.00 35.96           C  
ATOM     77  CG  LEU A  43      14.065 -36.967   6.935  1.00 36.63           C  
ATOM     78  CD1 LEU A  43      13.590 -36.305   5.658  1.00 36.69           C  
ATOM     79  CD2 LEU A  43      13.269 -36.402   8.072  1.00 36.06           C  
ATOM     80  N   LEU A  44      17.089 -38.444   5.511  1.00 35.66           N  
ATOM     81  CA  LEU A  44      18.502 -38.199   5.891  1.00 34.35           C  
ATOM     82  C   LEU A  44      18.681 -36.853   6.556  1.00 35.42           C  
ATOM     83  O   LEU A  44      19.590 -36.688   7.329  1.00 36.50           O  
ATOM     84  CB  LEU A  44      19.402 -38.278   4.648  1.00 34.68           C  
ATOM     85  CG  LEU A  44      19.450 -39.666   3.999  1.00 35.01           C  
ATOM     86  CD1 LEU A  44      20.154 -39.646   2.597  1.00 37.08           C  
ATOM     87  CD2 LEU A  44      20.212 -40.646   4.890  1.00 35.43           C  
ATOM     88  N   GLY A  45      17.858 -35.866   6.272  1.00 35.33           N  
ATOM     89  CA  GLY A  45      18.041 -34.533   6.835  1.00 35.06           C  
ATOM     90  C   GLY A  45      16.955 -33.610   6.321  1.00 36.25           C  
ATOM     91  O   GLY A  45      16.307 -33.932   5.275  1.00 32.98           O  
ATOM     92  N   SER A  46      16.743 -32.489   7.014  1.00 35.82           N  
ATOM     93  CA  SER A  46      15.868 -31.463   6.497  1.00 39.50           C  
ATOM     94  C   SER A  46      16.227 -30.064   7.026  1.00 39.81           C  
ATOM     95  O   SER A  46      16.969 -29.952   7.986  1.00 39.77           O  
ATOM     96  CB  SER A  46      14.432 -31.771   6.898  1.00 41.56           C  
ATOM     97  OG  SER A  46      14.283 -31.596   8.285  1.00 45.24           O  
ATOM     98  N   GLY A  47      15.649 -28.994   6.478  1.00 40.37           N  
ATOM     99  CA  GLY A  47      16.050 -27.674   6.965  1.00 41.10           C  
ATOM    100  C   GLY A  47      15.360 -26.580   6.231  1.00 42.93           C  
ATOM    101  O   GLY A  47      14.287 -26.829   5.684  1.00 42.13           O  
ATOM    102  N   GLY A  48      15.980 -25.383   6.168  1.00 42.41           N  
ATOM    103  CA  GLY A  48      15.325 -24.290   5.443  1.00 43.42           C  
ATOM    104  C   GLY A  48      14.998 -24.669   3.975  1.00 43.46           C  
ATOM    105  O   GLY A  48      13.974 -24.244   3.417  1.00 44.50           O  
ATOM    106  N   PHE A  49      15.868 -25.475   3.350  1.00 40.22           N  
ATOM    107  CA  PHE A  49      15.738 -25.731   1.942  1.00 38.73           C  
ATOM    108  C   PHE A  49      14.561 -26.666   1.609  1.00 37.94           C  
ATOM    109  O   PHE A  49      14.027 -26.551   0.502  1.00 36.12           O  
ATOM    110  CB  PHE A  49      16.989 -26.403   1.418  1.00 38.99           C  
ATOM    111  CG  PHE A  49      17.157 -27.790   1.921  1.00 39.57           C  
ATOM    112  CD1 PHE A  49      17.789 -28.012   3.144  1.00 33.86           C  
ATOM    113  CD2 PHE A  49      16.640 -28.880   1.176  1.00 37.87           C  
ATOM    114  CE1 PHE A  49      17.993 -29.327   3.627  1.00 39.80           C  
ATOM    115  CE2 PHE A  49      16.814 -30.223   1.675  1.00 37.90           C  
ATOM    116  CZ  PHE A  49      17.494 -30.425   2.882  1.00 38.08           C  
ATOM    117  N   GLY A  50      14.245 -27.628   2.527  1.00 36.11           N  
ATOM    118  CA  GLY A  50      13.285 -28.787   2.254  1.00 35.22           C  
ATOM    119  C   GLY A  50      13.834 -30.028   3.007  1.00 33.94           C  
ATOM    120  O   GLY A  50      14.359 -29.871   4.131  1.00 33.36           O  
ATOM    121  N   SER A  51      13.813 -31.201   2.369  1.00 33.44           N  
ATOM    122  CA  SER A  51      14.153 -32.515   3.010  1.00 32.38           C  
ATOM    123  C   SER A  51      14.805 -33.453   2.061  1.00 31.16           C  
ATOM    124  O   SER A  51      14.477 -33.426   0.871  1.00 32.99           O  
ATOM    125  CB  SER A  51      12.793 -33.217   3.466  1.00 30.30           C  
ATOM    126  OG  SER A  51      12.075 -32.353   4.342  1.00 31.61           O  
ATOM    127  N   VAL A  52      15.646 -34.381   2.559  1.00 29.02           N  
ATOM    128  CA  VAL A  52      16.279 -35.310   1.731  1.00 27.20           C  
ATOM    129  C   VAL A  52      16.182 -36.668   2.319  1.00 29.34           C  
ATOM    130  O   VAL A  52      16.292 -36.814   3.577  1.00 30.08           O  
ATOM    131  CB  VAL A  52      17.848 -34.946   1.544  1.00 26.61           C  
ATOM    132  CG1AVAL A  52      18.320 -35.380   0.158  0.50 27.91           C  
ATOM    133  CG2AVAL A  52      18.005 -33.565   1.689  0.50 28.09           C  
ATOM    134  CG1BVAL A  52      18.440 -34.489   2.889  0.50 22.94           C  
ATOM    135  CG2BVAL A  52      18.635 -36.131   0.950  0.50 29.31           C  
ATOM    136  N   TYR A  53      15.941 -37.637   1.423  1.00 29.85           N  
ATOM    137  CA  TYR A  53      15.736 -39.073   1.740  1.00 30.76           C  
ATOM    138  C   TYR A  53      16.729 -39.904   1.045  1.00 31.96           C  
ATOM    139  O   TYR A  53      17.183 -39.565  -0.102  1.00 33.32           O  
ATOM    140  CB  TYR A  53      14.392 -39.563   1.180  1.00 30.41           C  
ATOM    141  CG  TYR A  53      13.201 -38.876   1.865  1.00 29.23           C  
ATOM    142  CD1 TYR A  53      12.776 -37.609   1.465  1.00 30.63           C  
ATOM    143  CD2 TYR A  53      12.530 -39.499   2.985  1.00 29.97           C  
ATOM    144  CE1 TYR A  53      11.720 -36.968   2.102  1.00 29.06           C  
ATOM    145  CE2 TYR A  53      11.408 -38.853   3.617  1.00 30.30           C  
ATOM    146  CZ  TYR A  53      11.002 -37.620   3.162  1.00 31.70           C  
ATOM    147  OH  TYR A  53       9.949 -36.904   3.794  1.00 31.69           O  
ATOM    148  N   SER A  54      16.989 -41.044   1.657  1.00 29.38           N  
ATOM    149  CA  SER A  54      17.736 -42.129   1.052  1.00 34.10           C  
ATOM    150  C   SER A  54      16.759 -42.808   0.115  1.00 36.79           C  
ATOM    151  O   SER A  54      15.541 -42.769   0.367  1.00 38.53           O  
ATOM    152  CB  SER A  54      18.220 -43.080   2.136  1.00 32.31           C  
ATOM    153  OG  SER A  54      18.977 -44.106   1.573  1.00 37.01           O  
ATOM    154  N   GLY A  55      17.247 -43.335  -1.003  1.00 36.95           N  
ATOM    155  CA  GLY A  55      16.376 -43.935  -1.956  1.00 38.44           C  
ATOM    156  C   GLY A  55      17.169 -44.915  -2.753  1.00 40.12           C  
ATOM    157  O   GLY A  55      18.402 -45.047  -2.592  1.00 36.85           O  
ATOM    158  N   ILE A  56      16.464 -45.618  -3.624  1.00 40.93           N  
ATOM    159  CA  ILE A  56      17.096 -46.655  -4.444  1.00 44.58           C  
ATOM    160  C   ILE A  56      16.394 -46.597  -5.766  1.00 45.04           C  
ATOM    161  O   ILE A  56      15.166 -46.536  -5.813  1.00 44.35           O  
ATOM    162  CB  ILE A  56      16.935 -48.027  -3.821  1.00 44.47           C  
ATOM    163  CG1 ILE A  56      17.941 -48.184  -2.681  1.00 47.46           C  
ATOM    164  CG2 ILE A  56      17.111 -49.138  -4.866  1.00 47.78           C  
ATOM    165  CD1 ILE A  56      17.788 -49.534  -1.854  1.00 47.80           C  
ATOM    166  N   ARG A  57      17.165 -46.537  -6.838  1.00 45.68           N  
ATOM    167  CA  ARG A  57      16.535 -46.506  -8.147  1.00 48.30           C  
ATOM    168  C   ARG A  57      16.104 -47.934  -8.486  1.00 49.46           C  
ATOM    169  O   ARG A  57      16.937 -48.870  -8.489  1.00 47.86           O  
ATOM    170  CB  ARG A  57      17.489 -46.005  -9.172  1.00 48.05           C  
ATOM    171  CG  ARG A  57      16.887 -45.882 -10.509  1.00 49.51           C  
ATOM    172  CD  ARG A  57      18.076 -46.157 -11.457  1.00 56.12           C  
ATOM    173  NE  ARG A  57      18.627 -44.910 -11.910  1.00 53.20           N  
ATOM    174  CZ  ARG A  57      19.851 -44.709 -12.388  1.00 54.48           C  
ATOM    175  NH1 ARG A  57      20.770 -45.669 -12.486  1.00 52.72           N  
ATOM    176  NH2 ARG A  57      20.129 -43.489 -12.785  1.00 50.86           N  
ATOM    177  N   VAL A  58      14.800 -48.061  -8.717  1.00 51.28           N  
ATOM    178  CA  VAL A  58      14.085 -49.366  -8.807  1.00 54.00           C  
ATOM    179  C   VAL A  58      14.662 -50.239  -9.927  1.00 55.45           C  
ATOM    180  O   VAL A  58      15.016 -51.386  -9.694  1.00 56.42           O  
ATOM    181  CB  VAL A  58      12.568 -49.112  -8.907  1.00 53.57           C  
ATOM    182  CG1 VAL A  58      11.804 -50.283  -9.559  1.00 57.42           C  
ATOM    183  CG2 VAL A  58      12.005 -48.784  -7.530  1.00 52.94           C  
ATOM    184  N   SER A  59      14.850 -49.653 -11.107  1.00 57.12           N  
ATOM    185  CA  SER A  59      15.355 -50.369 -12.278  1.00 57.82           C  
ATOM    186  C   SER A  59      16.659 -51.084 -11.992  1.00 58.63           C  
ATOM    187  O   SER A  59      16.704 -52.316 -12.037  1.00 59.28           O  
ATOM    188  CB  SER A  59      15.519 -49.414 -13.454  1.00 58.71           C  
ATOM    189  OG  SER A  59      16.546 -48.492 -13.172  1.00 58.93           O  
ATOM    190  N   ASP A  60      17.718 -50.347 -11.649  1.00 57.80           N  
ATOM    191  CA  ASP A  60      19.009 -51.009 -11.333  1.00 56.42           C  
ATOM    192  C   ASP A  60      19.421 -51.150  -9.875  1.00 54.90           C  
ATOM    193  O   ASP A  60      20.545 -51.567  -9.630  1.00 53.83           O  
ATOM    194  CB  ASP A  60      20.176 -50.346 -12.074  1.00 56.39           C  
ATOM    195  CG  ASP A  60      20.277 -48.857 -11.798  1.00 56.96           C  
ATOM    196  OD1 ASP A  60      19.365 -48.282 -11.175  1.00 55.30           O  
ATOM    197  OD2 ASP A  60      21.242 -48.229 -12.270  1.00 61.13           O  
ATOM    198  N   ASN A  61      18.567 -50.805  -8.924  1.00 53.71           N  
ATOM    199  CA  ASN A  61      19.016 -50.704  -7.508  1.00 53.91           C  
ATOM    200  C   ASN A  61      20.141 -49.673  -7.148  1.00 51.20           C  
ATOM    201  O   ASN A  61      20.836 -49.802  -6.138  1.00 50.71           O  
ATOM    202  CB  ASN A  61      19.421 -52.055  -6.985  1.00 55.68           C  
ATOM    203  CG  ASN A  61      18.226 -52.911  -6.738  1.00 61.89           C  
ATOM    204  OD1 ASN A  61      17.206 -52.429  -6.237  1.00 66.14           O  
ATOM    205  ND2 ASN A  61      18.305 -54.176  -7.166  1.00 67.16           N  
ATOM    206  N   LEU A  62      20.335 -48.679  -7.982  1.00 47.38           N  
ATOM    207  CA  LEU A  62      21.403 -47.726  -7.725  1.00 44.37           C  
ATOM    208  C   LEU A  62      21.057 -46.971  -6.465  1.00 41.59           C  
ATOM    209  O   LEU A  62      19.969 -46.422  -6.380  1.00 39.80           O  
ATOM    210  CB  LEU A  62      21.456 -46.725  -8.867  1.00 45.16           C  
ATOM    211  CG  LEU A  62      22.568 -45.702  -8.656  1.00 42.02           C  
ATOM    212  CD1 LEU A  62      23.993 -46.420  -8.708  1.00 45.42           C  
ATOM    213  CD2 LEU A  62      22.448 -44.504  -9.608  1.00 41.34           C  
ATOM    214  N   PRO A  63      21.982 -46.892  -5.493  1.00 39.37           N  
ATOM    215  CA  PRO A  63      21.674 -45.934  -4.374  1.00 38.76           C  
ATOM    216  C   PRO A  63      21.599 -44.431  -4.801  1.00 39.28           C  
ATOM    217  O   PRO A  63      22.474 -43.918  -5.550  1.00 39.77           O  
ATOM    218  CB  PRO A  63      22.776 -46.173  -3.367  1.00 37.35           C  
ATOM    219  CG  PRO A  63      23.827 -47.034  -4.079  1.00 39.72           C  
ATOM    220  CD  PRO A  63      23.269 -47.579  -5.350  1.00 39.66           C  
ATOM    221  N   VAL A  64      20.566 -43.735  -4.353  1.00 36.35           N  
ATOM    222  CA  VAL A  64      20.389 -42.300  -4.665  1.00 34.56           C  
ATOM    223  C   VAL A  64      19.944 -41.510  -3.427  1.00 34.33           C  
ATOM    224  O   VAL A  64      19.553 -42.096  -2.365  1.00 35.69           O  
ATOM    225  CB  VAL A  64      19.326 -42.065  -5.788  1.00 34.58           C  
ATOM    226  CG1 VAL A  64      19.752 -42.791  -7.140  1.00 35.49           C  
ATOM    227  CG2 VAL A  64      17.928 -42.545  -5.323  1.00 35.41           C  
ATOM    228  N   ALA A  65      19.895 -40.197  -3.549  1.00 31.92           N  
ATOM    229  CA  ALA A  65      19.362 -39.398  -2.451  1.00 32.34           C  
ATOM    230  C   ALA A  65      18.289 -38.634  -3.170  1.00 31.15           C  
ATOM    231  O   ALA A  65      18.481 -38.285  -4.321  1.00 30.96           O  
ATOM    232  CB  ALA A  65      20.418 -38.397  -1.854  1.00 30.70           C  
ATOM    233  N   ILE A  66      17.207 -38.309  -2.497  1.00 30.17           N  
ATOM    234  CA  ILE A  66      16.084 -37.703  -3.135  1.00 30.95           C  
ATOM    235  C   ILE A  66      15.813 -36.457  -2.402  1.00 30.11           C  
ATOM    236  O   ILE A  66      15.404 -36.502  -1.218  1.00 32.75           O  
ATOM    237  CB  ILE A  66      14.867 -38.648  -3.073  1.00 31.43           C  
ATOM    238  CG1 ILE A  66      15.197 -39.934  -3.799  1.00 32.64           C  
ATOM    239  CG2 ILE A  66      13.596 -37.871  -3.657  1.00 28.22           C  
ATOM    240  CD1 ILE A  66      14.215 -41.138  -3.626  1.00 33.21           C  
ATOM    241  N   LYS A  67      16.123 -35.327  -3.029  1.00 28.89           N  
ATOM    242  CA  LYS A  67      16.028 -34.045  -2.354  1.00 30.15           C  
ATOM    243  C   LYS A  67      14.842 -33.242  -2.836  1.00 32.03           C  
ATOM    244  O   LYS A  67      14.723 -32.899  -4.062  1.00 33.17           O  
ATOM    245  CB  LYS A  67      17.322 -33.234  -2.603  1.00 29.65           C  
ATOM    246  CG  LYS A  67      17.238 -31.846  -2.025  1.00 29.26           C  
ATOM    247  CD  LYS A  67      18.672 -31.147  -2.278  1.00 30.54           C  
ATOM    248  CE  LYS A  67      18.918 -29.968  -1.322  1.00 33.75           C  
ATOM    249  NZ  LYS A  67      20.147 -29.237  -1.840  1.00 29.98           N  
ATOM    250  N   HIS A  68      13.997 -32.863  -1.881  1.00 31.75           N  
ATOM    251  CA  HIS A  68      12.794 -32.067  -2.111  1.00 32.95           C  
ATOM    252  C   HIS A  68      13.038 -30.649  -1.769  1.00 33.91           C  
ATOM    253  O   HIS A  68      13.326 -30.353  -0.620  1.00 31.81           O  
ATOM    254  CB  HIS A  68      11.654 -32.545  -1.215  1.00 32.12           C  
ATOM    255  CG  HIS A  68      11.292 -33.948  -1.448  1.00 31.13           C  
ATOM    256  ND1 HIS A  68      10.168 -34.311  -2.153  1.00 33.22           N  
ATOM    257  CD2 HIS A  68      11.918 -35.105  -1.105  1.00 31.70           C  
ATOM    258  CE1 HIS A  68      10.127 -35.629  -2.264  1.00 27.32           C  
ATOM    259  NE2 HIS A  68      11.190 -36.130  -1.646  1.00 28.18           N  
ATOM    260  N   VAL A  69      12.904 -29.765  -2.756  1.00 33.96           N  
ATOM    261  CA  VAL A  69      13.271 -28.344  -2.609  1.00 38.00           C  
ATOM    262  C   VAL A  69      11.930 -27.599  -2.698  1.00 40.98           C  
ATOM    263  O   VAL A  69      11.242 -27.706  -3.728  1.00 41.22           O  
ATOM    264  CB  VAL A  69      14.195 -27.891  -3.765  1.00 38.59           C  
ATOM    265  CG1 VAL A  69      14.417 -26.355  -3.699  1.00 42.08           C  
ATOM    266  CG2 VAL A  69      15.579 -28.687  -3.723  1.00 40.03           C  
ATOM    267  N   GLU A  70      11.562 -26.918  -1.621  1.00 42.96           N  
ATOM    268  CA  GLU A  70      10.318 -26.163  -1.545  1.00 46.58           C  
ATOM    269  C   GLU A  70      10.477 -24.876  -2.344  1.00 45.09           C  
ATOM    270  O   GLU A  70      11.451 -24.102  -2.159  1.00 44.48           O  
ATOM    271  CB  GLU A  70       9.964 -25.845  -0.080  1.00 46.91           C  
ATOM    272  CG  GLU A  70       9.228 -27.003   0.566  1.00 56.07           C  
ATOM    273  CD  GLU A  70       7.717 -27.050   0.226  1.00 62.43           C  
ATOM    274  OE1 GLU A  70       7.046 -25.987   0.420  1.00 68.33           O  
ATOM    275  OE2 GLU A  70       7.194 -28.143  -0.192  1.00 62.54           O  
ATOM    276  N   LYS A  71       9.559 -24.685  -3.266  1.00 45.67           N  
ATOM    277  CA  LYS A  71       9.538 -23.407  -4.102  1.00 47.07           C  
ATOM    278  C   LYS A  71       9.720 -22.082  -3.361  1.00 49.59           C  
ATOM    279  O   LYS A  71      10.584 -21.280  -3.753  1.00 48.65           O  
ATOM    280  CB  LYS A  71       8.323 -23.363  -4.986  1.00 46.04           C  
ATOM    281  CG  LYS A  71       8.362 -24.515  -5.949  1.00 41.47           C  
ATOM    282  CD  LYS A  71       7.339 -24.393  -7.065  1.00 39.26           C  
ATOM    283  CE  LYS A  71       7.671 -25.367  -8.153  1.00 43.96           C  
ATOM    284  NZ  LYS A  71       6.483 -25.813  -9.005  1.00 44.67           N  
ATOM    285  N   ASP A  72       8.996 -21.888  -2.242  1.00 51.86           N  
ATOM    286  CA  ASP A  72       8.934 -20.586  -1.629  1.00 55.13           C  
ATOM    287  C   ASP A  72      10.189 -20.311  -0.911  1.00 56.35           C  
ATOM    288  O   ASP A  72      10.335 -19.224  -0.362  1.00 55.99           O  
ATOM    289  CB  ASP A  72       7.885 -20.535  -0.570  1.00 57.42           C  
ATOM    290  CG  ASP A  72       6.749 -21.426  -0.871  1.00 65.65           C  
ATOM    291  OD1 ASP A  72       6.941 -22.310  -1.761  1.00 72.25           O  
ATOM    292  OD2 ASP A  72       5.677 -21.249  -0.206  1.00 72.56           O  
ATOM    293  N   ARG A  73      11.064 -21.302  -0.814  1.00 56.95           N  
ATOM    294  C   ARG A  73      13.477 -20.960  -1.115  1.00 58.13           C  
ATOM    295  O   ARG A  73      14.630 -20.711  -0.722  1.00 58.54           O  
ATOM    296  CA AARG A  73      12.327 -21.102  -0.114  0.50 58.30           C  
ATOM    297  CB AARG A  73      12.584 -22.215   0.930  0.50 58.35           C  
ATOM    298  CG AARG A  73      11.767 -22.088   2.233  0.50 60.52           C  
ATOM    299  CD AARG A  73      10.604 -23.081   2.340  0.50 62.69           C  
ATOM    300  NE AARG A  73      10.983 -24.265   3.121  0.50 65.56           N  
ATOM    301  CZ AARG A  73      10.215 -25.345   3.275  0.50 66.70           C  
ATOM    302  NH1AARG A  73       9.017 -25.378   2.707  0.50 65.76           N  
ATOM    303  NH2AARG A  73      10.634 -26.392   3.992  0.50 65.70           N  
ATOM    304  CA BARG A  73      12.324 -21.071  -0.127  0.50 57.95           C  
ATOM    305  CB BARG A  73      12.561 -22.131   0.964  0.50 57.73           C  
ATOM    306  CG BARG A  73      11.541 -22.057   2.111  0.50 58.46           C  
ATOM    307  CD BARG A  73      11.607 -20.681   2.810  0.50 57.96           C  
ATOM    308  NE BARG A  73      12.904 -20.517   3.439  0.50 55.90           N  
ATOM    309  CZ BARG A  73      13.127 -20.728   4.725  0.50 55.37           C  
ATOM    310  NH1BARG A  73      12.116 -21.065   5.518  0.50 55.94           N  
ATOM    311  NH2BARG A  73      14.350 -20.578   5.213  0.50 52.65           N  
ATOM    312  N   ILE A  74      13.160 -21.093  -2.403  1.00 58.28           N  
ATOM    313  CA  ILE A  74      14.189 -20.975  -3.424  1.00 59.10           C  
ATOM    314  C   ILE A  74      14.741 -19.534  -3.490  1.00 60.60           C  
ATOM    315  O   ILE A  74      14.068 -18.630  -4.016  1.00 61.40           O  
ATOM    316  CB  ILE A  74      13.680 -21.477  -4.787  1.00 58.93           C  
ATOM    317  CG1 ILE A  74      13.384 -22.973  -4.709  1.00 56.78           C  
ATOM    318  CG2 ILE A  74      14.699 -21.199  -5.898  1.00 57.75           C  
ATOM    319  CD1 ILE A  74      12.895 -23.538  -5.970  1.00 55.76           C  
ATOM    320  N   SER A  75      15.958 -19.313  -2.972  1.00 61.31           N  
ATOM    321  CA  SER A  75      16.533 -17.933  -3.006  1.00 62.40           C  
ATOM    322  C   SER A  75      16.859 -17.371  -4.419  1.00 62.87           C  
ATOM    323  O   SER A  75      16.985 -16.146  -4.544  1.00 63.55           O  
ATOM    324  CB  SER A  75      17.720 -17.724  -2.024  1.00 62.46           C  
ATOM    325  OG  SER A  75      18.748 -18.729  -2.153  1.00 65.00           O  
ATOM    326  N   ASP A  76      17.010 -18.256  -5.443  1.00 62.72           N  
ATOM    327  CA  ASP A  76      17.332 -17.920  -6.855  1.00 60.72           C  
ATOM    328  C   ASP A  76      16.842 -18.916  -7.914  1.00 58.95           C  
ATOM    329  O   ASP A  76      16.990 -20.140  -7.790  1.00 56.34           O  
ATOM    330  CB  ASP A  76      18.847 -17.757  -7.030  1.00 61.56           C  
ATOM    331  CG  ASP A  76      19.405 -16.587  -6.219  1.00 66.63           C  
ATOM    332  OD1 ASP A  76      18.780 -15.480  -6.263  1.00 69.46           O  
ATOM    333  OD2 ASP A  76      20.464 -16.760  -5.521  1.00 68.92           O  
ATOM    334  N   TRP A  77      16.312 -18.373  -8.996  1.00 56.97           N  
ATOM    335  CA  TRP A  77      15.851 -19.187 -10.079  1.00 57.12           C  
ATOM    336  C   TRP A  77      16.713 -18.939 -11.275  1.00 58.41           C  
ATOM    337  O   TRP A  77      17.365 -17.904 -11.367  1.00 58.48           O  
ATOM    338  CB  TRP A  77      14.418 -18.829 -10.448  1.00 55.41           C  
ATOM    339  CG  TRP A  77      13.416 -19.104  -9.413  1.00 53.69           C  
ATOM    340  CD1 TRP A  77      13.153 -18.359  -8.279  1.00 54.03           C  
ATOM    341  CD2 TRP A  77      12.508 -20.213  -9.388  1.00 51.26           C  
ATOM    342  NE1 TRP A  77      12.131 -18.962  -7.556  1.00 51.94           N  
ATOM    343  CE2 TRP A  77      11.714 -20.084  -8.227  1.00 51.05           C  
ATOM    344  CE3 TRP A  77      12.306 -21.316 -10.225  1.00 52.93           C  
ATOM    345  CZ2 TRP A  77      10.704 -21.003  -7.905  1.00 52.07           C  
ATOM    346  CZ3 TRP A  77      11.306 -22.240  -9.900  1.00 53.57           C  
ATOM    347  CH2 TRP A  77      10.515 -22.070  -8.754  1.00 52.64           C  
ATOM    348  N   GLY A  78      16.704 -19.885 -12.198  1.00 59.62           N  
ATOM    349  CA  GLY A  78      17.488 -19.794 -13.397  1.00 62.41           C  
ATOM    350  C   GLY A  78      16.674 -20.476 -14.433  1.00 65.42           C  
ATOM    351  O   GLY A  78      15.483 -20.745 -14.218  1.00 65.93           O  
ATOM    352  N   GLU A  79      17.265 -20.738 -15.585  1.00 69.01           N  
ATOM    353  CA  GLU A  79      16.534 -21.528 -16.564  1.00 73.31           C  
ATOM    354  C   GLU A  79      17.461 -22.277 -17.464  1.00 74.89           C  
ATOM    355  O   GLU A  79      18.652 -21.980 -17.523  1.00 75.38           O  
ATOM    356  CB  GLU A  79      15.535 -20.712 -17.366  1.00 73.98           C  
ATOM    357  CG  GLU A  79      16.168 -19.846 -18.415  1.00 79.11           C  
ATOM    358  CD  GLU A  79      15.213 -18.755 -18.854  1.00 85.37           C  
ATOM    359  OE1 GLU A  79      13.975 -19.026 -18.920  1.00 84.99           O  
ATOM    360  OE2 GLU A  79      15.714 -17.627 -19.113  1.00 88.07           O  
ATOM    361  N   LEU A  80      16.895 -23.254 -18.160  1.00 77.51           N  
ATOM    362  CA  LEU A  80      17.683 -24.313 -18.777  1.00 79.71           C  
ATOM    363  C   LEU A  80      18.185 -23.904 -20.171  1.00 82.03           C  
ATOM    364  O   LEU A  80      17.621 -22.947 -20.754  1.00 81.79           O  
ATOM    365  CB  LEU A  80      16.847 -25.599 -18.809  1.00 79.36           C  
ATOM    366  CG  LEU A  80      16.570 -26.134 -17.404  1.00 77.58           C  
ATOM    367  CD1 LEU A  80      15.703 -27.367 -17.484  1.00 76.56           C  
ATOM    368  CD2 LEU A  80      17.915 -26.423 -16.719  1.00 75.88           C  
ATOM    369  N   PRO A  81      19.261 -24.588 -20.691  1.00 83.82           N  
ATOM    370  CA  PRO A  81      19.612 -24.333 -22.116  1.00 84.88           C  
ATOM    371  C   PRO A  81      18.350 -24.222 -23.022  1.00 85.24           C  
ATOM    372  O   PRO A  81      18.133 -23.144 -23.586  1.00 86.01           O  
ATOM    373  CB  PRO A  81      20.572 -25.491 -22.474  1.00 85.06           C  
ATOM    374  CG  PRO A  81      21.319 -25.766 -21.124  1.00 85.04           C  
ATOM    375  CD  PRO A  81      20.202 -25.557 -20.056  1.00 84.44           C  
ATOM    376  N   ASN A  82      17.498 -25.253 -23.118  1.00 85.03           N  
ATOM    377  CA  ASN A  82      16.175 -25.021 -23.739  1.00 84.83           C  
ATOM    378  C   ASN A  82      15.501 -23.770 -23.119  1.00 83.63           C  
ATOM    379  O   ASN A  82      15.140 -22.838 -23.832  1.00 83.61           O  
ATOM    380  CB  ASN A  82      15.260 -26.276 -23.750  1.00 85.22           C  
ATOM    381  CG  ASN A  82      14.844 -26.740 -22.333  1.00 87.09           C  
ATOM    382  OD1 ASN A  82      15.688 -27.149 -21.518  1.00 86.95           O  
ATOM    383  ND2 ASN A  82      13.537 -26.699 -22.053  1.00 87.09           N  
ATOM    384  N   GLY A  83      15.399 -23.722 -21.797  1.00 82.64           N  
ATOM    385  CA  GLY A  83      14.890 -22.531 -21.137  1.00 81.23           C  
ATOM    386  C   GLY A  83      13.640 -22.738 -20.300  1.00 80.48           C  
ATOM    387  O   GLY A  83      12.721 -21.903 -20.357  1.00 80.38           O  
ATOM    388  N   THR A  84      13.612 -23.837 -19.524  1.00 78.59           N  
ATOM    389  CA  THR A  84      12.557 -24.101 -18.497  1.00 76.59           C  
ATOM    390  C   THR A  84      12.872 -23.425 -17.127  1.00 73.93           C  
ATOM    391  O   THR A  84      14.029 -23.425 -16.675  1.00 74.25           O  
ATOM    392  CB  THR A  84      12.383 -25.617 -18.254  1.00 76.83           C  
ATOM    393  OG1 THR A  84      12.442 -26.299 -19.513  1.00 79.30           O  
ATOM    394  CG2 THR A  84      11.064 -25.929 -17.512  1.00 76.30           C  
ATOM    395  N   ARG A  85      11.859 -22.882 -16.458  1.00 69.93           N  
ATOM    396  CA  ARG A  85      12.121 -22.218 -15.181  1.00 65.59           C  
ATOM    397  C   ARG A  85      12.360 -23.194 -13.951  1.00 64.57           C  
ATOM    398  O   ARG A  85      11.409 -23.793 -13.396  1.00 64.55           O  
ATOM    399  CB  ARG A  85      11.074 -21.133 -14.944  1.00 66.97           C  
ATOM    400  CG  ARG A  85      11.047 -20.534 -13.578  1.00 68.60           C  
ATOM    401  CD  ARG A  85       9.819 -19.645 -13.491  1.00 73.68           C  
ATOM    402  NE  ARG A  85       9.637 -19.086 -12.154  1.00 74.44           N  
ATOM    403  CZ  ARG A  85      10.377 -18.103 -11.650  1.00 76.37           C  
ATOM    404  NH1 ARG A  85      11.376 -17.584 -12.366  1.00 76.23           N  
ATOM    405  NH2 ARG A  85      10.124 -17.650 -10.419  1.00 76.43           N  
ATOM    406  N   VAL A  86      13.641 -23.347 -13.576  1.00 60.44           N  
ATOM    407  CA  VAL A  86      14.116 -24.297 -12.542  1.00 57.31           C  
ATOM    408  C   VAL A  86      14.882 -23.578 -11.397  1.00 51.99           C  
ATOM    409  O   VAL A  86      15.358 -22.450 -11.569  1.00 51.59           O  
ATOM    410  CB  VAL A  86      15.037 -25.328 -13.183  1.00 57.19           C  
ATOM    411  CG1 VAL A  86      14.287 -26.086 -14.290  1.00 57.21           C  
ATOM    412  CG2 VAL A  86      16.262 -24.630 -13.782  1.00 57.46           C  
ATOM    413  N   PRO A  87      14.974 -24.206 -10.202  1.00 46.53           N  
ATOM    414  CA  PRO A  87      15.902 -23.622  -9.254  1.00 44.26           C  
ATOM    415  C   PRO A  87      17.313 -23.439  -9.869  1.00 40.15           C  
ATOM    416  O   PRO A  87      17.808 -24.288 -10.638  1.00 40.09           O  
ATOM    417  CB  PRO A  87      15.902 -24.620  -8.073  1.00 43.08           C  
ATOM    418  CG  PRO A  87      14.689 -25.398  -8.216  1.00 44.06           C  
ATOM    419  CD  PRO A  87      14.284 -25.376  -9.661  1.00 46.08           C  
ATOM    420  N   MET A  88      17.945 -22.340  -9.522  1.00 38.64           N  
ATOM    421  CA  MET A  88      19.369 -22.149  -9.863  1.00 36.71           C  
ATOM    422  C   MET A  88      20.183 -23.402  -9.475  1.00 35.87           C  
ATOM    423  O   MET A  88      21.099 -23.855 -10.186  1.00 35.36           O  
ATOM    424  CB  MET A  88      19.877 -20.876  -9.178  1.00 37.76           C  
ATOM    425  CG  MET A  88      21.345 -20.565  -9.451  1.00 42.40           C  
ATOM    426  SD  MET A  88      21.681 -20.294 -11.237  1.00 52.99           S  
ATOM    427  CE  MET A  88      20.390 -19.090 -11.606  1.00 46.76           C  
ATOM    428  N   GLU A  89      19.866 -23.989  -8.344  1.00 34.65           N  
ATOM    429  CA  GLU A  89      20.564 -25.191  -7.907  1.00 34.88           C  
ATOM    430  C   GLU A  89      20.648 -26.239  -9.036  1.00 34.80           C  
ATOM    431  O   GLU A  89      21.654 -26.926  -9.222  1.00 34.56           O  
ATOM    432  CB  GLU A  89      19.721 -25.771  -6.735  1.00 35.76           C  
ATOM    433  CG  GLU A  89      20.274 -26.982  -6.168  1.00 35.10           C  
ATOM    434  CD  GLU A  89      19.651 -27.420  -4.828  1.00 33.27           C  
ATOM    435  OE1 GLU A  89      18.740 -26.779  -4.249  1.00 35.93           O  
ATOM    436  OE2 GLU A  89      20.107 -28.484  -4.338  1.00 35.19           O  
ATOM    437  N   VAL A  90      19.529 -26.443  -9.760  1.00 34.01           N  
ATOM    438  CA  VAL A  90      19.546 -27.376 -10.929  1.00 32.69           C  
ATOM    439  C   VAL A  90      20.427 -26.871 -12.069  1.00 31.01           C  
ATOM    440  O   VAL A  90      21.226 -27.623 -12.622  1.00 31.61           O  
ATOM    441  CB  VAL A  90      18.089 -27.588 -11.430  1.00 34.57           C  
ATOM    442  CG1 VAL A  90      18.064 -28.340 -12.777  1.00 34.42           C  
ATOM    443  CG2 VAL A  90      17.316 -28.263 -10.336  1.00 33.20           C  
ATOM    444  N   VAL A  91      20.398 -25.574 -12.342  1.00 30.82           N  
ATOM    445  CA  VAL A  91      21.283 -25.080 -13.372  1.00 32.12           C  
ATOM    446  C   VAL A  91      22.744 -25.347 -12.971  1.00 32.86           C  
ATOM    447  O   VAL A  91      23.563 -25.797 -13.783  1.00 30.50           O  
ATOM    448  CB  VAL A  91      21.073 -23.531 -13.539  1.00 34.16           C  
ATOM    449  CG1 VAL A  91      22.176 -23.001 -14.394  1.00 33.76           C  
ATOM    450  CG2 VAL A  91      19.697 -23.298 -14.240  1.00 35.36           C  
ATOM    451  N   LEU A  92      23.071 -25.065 -11.675  1.00 31.09           N  
ATOM    452  CA  LEU A  92      24.457 -25.185 -11.236  1.00 30.77           C  
ATOM    453  C   LEU A  92      24.887 -26.632 -11.252  1.00 29.57           C  
ATOM    454  O   LEU A  92      25.952 -26.931 -11.690  1.00 28.10           O  
ATOM    455  CB  LEU A  92      24.664 -24.545  -9.831  1.00 30.81           C  
ATOM    456  CG  LEU A  92      24.182 -23.115  -9.799  1.00 27.34           C  
ATOM    457  CD1 LEU A  92      24.240 -22.599  -8.369  1.00 29.78           C  
ATOM    458  CD2 LEU A  92      24.907 -22.207 -10.826  1.00 29.69           C  
ATOM    459  N   LEU A  93      24.041 -27.547 -10.786  1.00 29.86           N  
ATOM    460  CA  LEU A  93      24.392 -28.940 -10.770  1.00 30.72           C  
ATOM    461  C   LEU A  93      24.657 -29.447 -12.197  1.00 31.22           C  
ATOM    462  O   LEU A  93      25.578 -30.259 -12.410  1.00 30.78           O  
ATOM    463  CB  LEU A  93      23.272 -29.768 -10.127  1.00 29.80           C  
ATOM    464  CG  LEU A  93      23.262 -29.758  -8.577  1.00 30.57           C  
ATOM    465  CD1 LEU A  93      21.877 -30.133  -8.013  1.00 30.01           C  
ATOM    466  CD2 LEU A  93      24.281 -30.688  -8.063  1.00 27.90           C  
ATOM    467  N   LYS A  94      23.875 -28.982 -13.170  1.00 33.09           N  
ATOM    468  CA  LYS A  94      24.087 -29.417 -14.583  1.00 33.30           C  
ATOM    469  C   LYS A  94      25.403 -28.902 -15.087  1.00 34.02           C  
ATOM    470  O   LYS A  94      26.169 -29.662 -15.690  1.00 33.23           O  
ATOM    471  CB  LYS A  94      22.977 -28.944 -15.497  1.00 35.91           C  
ATOM    472  CG  LYS A  94      21.644 -29.721 -15.216  1.00 38.15           C  
ATOM    473  CD  LYS A  94      20.468 -29.051 -15.976  1.00 46.08           C  
ATOM    474  CE  LYS A  94      20.193 -29.856 -17.271  1.00 54.15           C  
ATOM    475  NZ  LYS A  94      19.287 -31.070 -17.002  1.00 56.43           N  
ATOM    476  N   LYS A  95      25.737 -27.652 -14.747  1.00 33.45           N  
ATOM    477  CA  LYS A  95      27.067 -27.109 -15.206  1.00 33.29           C  
ATOM    478  C   LYS A  95      28.223 -27.935 -14.663  1.00 31.99           C  
ATOM    479  O   LYS A  95      29.206 -28.095 -15.344  1.00 33.94           O  
ATOM    480  CB  LYS A  95      27.211 -25.642 -14.837  1.00 34.42           C  
ATOM    481  CG  LYS A  95      26.259 -24.729 -15.709  1.00 37.46           C  
ATOM    482  CD  LYS A  95      26.300 -23.244 -15.247  1.00 36.38           C  
ATOM    483  CE  LYS A  95      27.647 -22.597 -15.417  1.00 39.74           C  
ATOM    484  NZ  LYS A  95      28.069 -22.383 -16.851  1.00 39.74           N  
ATOM    485  N   VAL A  96      28.115 -28.434 -13.440  1.00 32.66           N  
ATOM    486  CA  VAL A  96      29.267 -29.139 -12.855  1.00 35.38           C  
ATOM    487  C   VAL A  96      29.256 -30.654 -13.056  1.00 37.41           C  
ATOM    488  O   VAL A  96      30.244 -31.356 -12.671  1.00 36.73           O  
ATOM    489  CB  VAL A  96      29.475 -28.855 -11.339  1.00 35.07           C  
ATOM    490  CG1 VAL A  96      29.763 -27.351 -11.095  1.00 34.70           C  
ATOM    491  CG2 VAL A  96      28.253 -29.292 -10.567  1.00 29.57           C  
ATOM    492  N   SER A  97      28.140 -31.167 -13.590  1.00 40.65           N  
ATOM    493  CA  SER A  97      28.044 -32.628 -13.876  1.00 42.06           C  
ATOM    494  C   SER A  97      29.188 -33.129 -14.757  1.00 42.74           C  
ATOM    495  O   SER A  97      29.508 -32.567 -15.807  1.00 43.09           O  
ATOM    496  CB  SER A  97      26.759 -32.995 -14.550  1.00 42.44           C  
ATOM    497  OG  SER A  97      26.880 -34.410 -14.729  1.00 50.01           O  
ATOM    498  N   SER A  98      29.880 -34.154 -14.291  1.00 44.12           N  
ATOM    499  CA  SER A  98      30.944 -34.761 -15.120  1.00 44.70           C  
ATOM    500  C   SER A  98      31.312 -36.084 -14.416  1.00 44.35           C  
ATOM    501  O   SER A  98      30.722 -36.407 -13.366  1.00 44.19           O  
ATOM    502  CB  SER A  98      32.164 -33.862 -15.197  1.00 45.66           C  
ATOM    503  OG  SER A  98      32.942 -34.022 -14.000  1.00 46.64           O  
ATOM    504  N   GLY A  99      32.288 -36.813 -14.957  1.00 43.76           N  
ATOM    505  CA  GLY A  99      32.765 -38.072 -14.323  1.00 43.99           C  
ATOM    506  C   GLY A  99      33.727 -37.793 -13.154  1.00 43.81           C  
ATOM    507  O   GLY A  99      34.189 -38.726 -12.473  1.00 43.25           O  
ATOM    508  N   PHE A 100      34.013 -36.499 -12.919  1.00 41.24           N  
ATOM    509  CA  PHE A 100      34.806 -36.111 -11.768  1.00 39.64           C  
ATOM    510  C   PHE A 100      34.046 -36.393 -10.482  1.00 39.71           C  
ATOM    511  O   PHE A 100      33.023 -35.817 -10.259  1.00 41.56           O  
ATOM    512  CB  PHE A 100      35.204 -34.632 -11.817  1.00 37.11           C  
ATOM    513  CG  PHE A 100      35.965 -34.164 -10.528  1.00 36.37           C  
ATOM    514  CD1 PHE A 100      37.135 -34.866 -10.076  1.00 31.89           C  
ATOM    515  CD2 PHE A 100      35.545 -33.040  -9.788  1.00 36.41           C  
ATOM    516  CE1 PHE A 100      37.877 -34.384  -8.967  1.00 32.72           C  
ATOM    517  CE2 PHE A 100      36.294 -32.558  -8.594  1.00 32.24           C  
ATOM    518  CZ  PHE A 100      37.436 -33.185  -8.221  1.00 31.70           C  
ATOM    519  N   SER A 101      34.563 -37.277  -9.622  1.00 39.42           N  
ATOM    520  CA  SER A 101      33.786 -37.710  -8.492  1.00 39.43           C  
ATOM    521  C   SER A 101      33.780 -36.718  -7.313  1.00 38.44           C  
ATOM    522  O   SER A 101      33.114 -37.031  -6.225  1.00 38.01           O  
ATOM    523  CB  SER A 101      34.263 -39.087  -8.022  1.00 41.29           C  
ATOM    524  OG  SER A 101      35.603 -39.017  -7.557  1.00 39.35           O  
ATOM    525  N   GLY A 102      34.488 -35.553  -7.477  1.00 35.81           N  
ATOM    526  CA  GLY A 102      34.630 -34.634  -6.317  1.00 29.65           C  
ATOM    527  C   GLY A 102      33.437 -33.722  -6.088  1.00 28.48           C  
ATOM    528  O   GLY A 102      33.336 -32.995  -5.065  1.00 26.79           O  
ATOM    529  N   VAL A 103      32.544 -33.672  -7.074  1.00 27.81           N  
ATOM    530  CA  VAL A 103      31.322 -32.902  -6.939  1.00 27.83           C  
ATOM    531  C   VAL A 103      30.144 -33.896  -7.167  1.00 29.36           C  
ATOM    532  O   VAL A 103      30.258 -34.769  -8.070  1.00 32.11           O  
ATOM    533  CB  VAL A 103      31.216 -31.742  -7.914  1.00 30.07           C  
ATOM    534  CG1 VAL A 103      29.837 -31.108  -7.778  1.00 27.44           C  
ATOM    535  CG2 VAL A 103      32.337 -30.691  -7.583  1.00 26.10           C  
ATOM    536  N   ILE A 104      29.088 -33.797  -6.356  1.00 26.75           N  
ATOM    537  CA  ILE A 104      27.939 -34.738  -6.460  1.00 30.84           C  
ATOM    538  C   ILE A 104      27.311 -34.642  -7.850  1.00 30.69           C  
ATOM    539  O   ILE A 104      27.323 -33.535  -8.495  1.00 31.18           O  
ATOM    540  CB  ILE A 104      26.768 -34.508  -5.454  1.00 27.33           C  
ATOM    541  CG1AILE A 104      25.951 -35.800  -5.197  0.50 25.24           C  
ATOM    542  CG2AILE A 104      25.918 -33.241  -5.825  0.50 25.75           C  
ATOM    543  CD1AILE A 104      26.890 -36.859  -4.402  0.50 20.87           C  
ATOM    544  CG1BILE A 104      26.708 -33.096  -4.953  0.50 34.41           C  
ATOM    545  CG2BILE A 104      26.481 -35.762  -4.497  0.50 33.95           C  
ATOM    546  CD1BILE A 104      25.969 -32.225  -5.865  0.50 31.92           C  
ATOM    547  N   ARG A 105      26.823 -35.800  -8.334  1.00 31.97           N  
ATOM    548  CA  ARG A 105      26.178 -35.834  -9.636  1.00 33.72           C  
ATOM    549  C   ARG A 105      24.633 -35.767  -9.549  1.00 32.49           C  
ATOM    550  O   ARG A 105      24.059 -36.567  -8.811  1.00 34.33           O  
ATOM    551  CB  ARG A 105      26.551 -37.149 -10.314  1.00 34.73           C  
ATOM    552  CG  ARG A 105      26.483 -37.011 -11.790  1.00 46.12           C  
ATOM    553  CD  ARG A 105      27.485 -37.943 -12.439  1.00 60.19           C  
ATOM    554  NE  ARG A 105      27.591 -37.579 -13.847  1.00 69.78           N  
ATOM    555  CZ  ARG A 105      28.558 -37.998 -14.655  1.00 74.70           C  
ATOM    556  NH1 ARG A 105      29.514 -38.799 -14.177  1.00 77.45           N  
ATOM    557  NH2 ARG A 105      28.576 -37.604 -15.931  1.00 77.10           N  
ATOM    558  N   LEU A 106      24.017 -34.813 -10.230  1.00 29.52           N  
ATOM    559  CA  LEU A 106      22.542 -34.777 -10.418  1.00 32.73           C  
ATOM    560  C   LEU A 106      22.171 -35.871 -11.472  1.00 33.48           C  
ATOM    561  O   LEU A 106      22.681 -35.858 -12.615  1.00 34.00           O  
ATOM    562  CB  LEU A 106      22.040 -33.447 -10.944  1.00 30.94           C  
ATOM    563  CG  LEU A 106      20.516 -33.272 -11.058  1.00 31.54           C  
ATOM    564  CD1 LEU A 106      19.785 -33.566  -9.733  1.00 30.06           C  
ATOM    565  CD2 LEU A 106      20.248 -31.838 -11.594  1.00 31.66           C  
ATOM    566  N   LEU A 107      21.405 -36.854 -11.064  1.00 34.91           N  
ATOM    567  CA  LEU A 107      20.942 -37.927 -11.936  1.00 36.57           C  
ATOM    568  C   LEU A 107      19.629 -37.604 -12.667  1.00 38.07           C  
ATOM    569  O   LEU A 107      19.402 -38.039 -13.815  1.00 40.00           O  
ATOM    570  CB  LEU A 107      20.763 -39.236 -11.114  1.00 36.28           C  
ATOM    571  CG  LEU A 107      22.060 -39.726 -10.501  1.00 36.75           C  
ATOM    572  CD1 LEU A 107      21.953 -40.971  -9.601  1.00 37.78           C  
ATOM    573  CD2 LEU A 107      23.151 -39.918 -11.524  1.00 44.83           C  
ATOM    574  N   ASP A 108      18.758 -36.845 -12.039  1.00 38.65           N  
ATOM    575  CA  ASP A 108      17.481 -36.574 -12.649  1.00 39.91           C  
ATOM    576  C   ASP A 108      16.788 -35.613 -11.781  1.00 39.26           C  
ATOM    577  O   ASP A 108      17.249 -35.325 -10.702  1.00 38.80           O  
ATOM    578  CB  ASP A 108      16.677 -37.885 -12.780  1.00 41.52           C  
ATOM    579  CG  ASP A 108      15.530 -37.774 -13.818  1.00 45.70           C  
ATOM    580  OD1 ASP A 108      15.161 -36.678 -14.294  1.00 49.10           O  
ATOM    581  OD2 ASP A 108      14.975 -38.815 -14.114  1.00 54.18           O  
ATOM    582  N   TRP A 109      15.685 -35.060 -12.249  1.00 39.91           N  
ATOM    583  CA  TRP A 109      14.903 -34.116 -11.458  1.00 40.46           C  
ATOM    584  C   TRP A 109      13.469 -34.091 -12.005  1.00 42.34           C  
ATOM    585  O   TRP A 109      13.273 -34.414 -13.179  1.00 40.62           O  
ATOM    586  CB  TRP A 109      15.479 -32.688 -11.461  1.00 39.42           C  
ATOM    587  CG  TRP A 109      15.512 -31.999 -12.815  1.00 41.04           C  
ATOM    588  CD1 TRP A 109      16.485 -32.132 -13.832  1.00 43.92           C  
ATOM    589  CD2 TRP A 109      14.577 -31.033 -13.284  1.00 41.70           C  
ATOM    590  NE1 TRP A 109      16.167 -31.278 -14.888  1.00 43.68           N  
ATOM    591  CE2 TRP A 109      14.997 -30.618 -14.584  1.00 44.52           C  
ATOM    592  CE3 TRP A 109      13.402 -30.483 -12.738  1.00 46.95           C  
ATOM    593  CZ2 TRP A 109      14.269 -29.687 -15.346  1.00 47.16           C  
ATOM    594  CZ3 TRP A 109      12.653 -29.517 -13.508  1.00 47.20           C  
ATOM    595  CH2 TRP A 109      13.106 -29.143 -14.803  1.00 46.61           C  
ATOM    596  N   PHE A 110      12.517 -33.647 -11.161  1.00 43.51           N  
ATOM    597  CA  PHE A 110      11.051 -33.607 -11.435  1.00 44.50           C  
ATOM    598  C   PHE A 110      10.549 -32.334 -10.851  1.00 44.80           C  
ATOM    599  O   PHE A 110      11.104 -31.858  -9.851  1.00 43.59           O  
ATOM    600  CB  PHE A 110      10.325 -34.796 -10.761  1.00 45.06           C  
ATOM    601  CG  PHE A 110      10.910 -36.110 -11.141  1.00 49.35           C  
ATOM    602  CD1 PHE A 110      10.499 -36.772 -12.333  1.00 56.67           C  
ATOM    603  CD2 PHE A 110      11.946 -36.683 -10.388  1.00 50.52           C  
ATOM    604  CE1 PHE A 110      11.109 -38.008 -12.733  1.00 58.32           C  
ATOM    605  CE2 PHE A 110      12.570 -37.917 -10.776  1.00 53.02           C  
ATOM    606  CZ  PHE A 110      12.156 -38.569 -11.949  1.00 55.73           C  
ATOM    607  N   GLU A 111       9.537 -31.746 -11.504  1.00 43.96           N  
ATOM    608  CA  GLU A 111       8.783 -30.659 -10.977  1.00 45.26           C  
ATOM    609  C   GLU A 111       7.443 -31.122 -10.368  1.00 46.10           C  
ATOM    610  O   GLU A 111       6.835 -32.077 -10.863  1.00 46.88           O  
ATOM    611  CB  GLU A 111       8.477 -29.646 -12.066  1.00 45.62           C  
ATOM    612  CG  GLU A 111       7.729 -28.495 -11.464  1.00 46.08           C  
ATOM    613  CD  GLU A 111       7.803 -27.244 -12.256  1.00 48.06           C  
ATOM    614  OE1 GLU A 111       8.312 -27.316 -13.348  1.00 49.46           O  
ATOM    615  OE2 GLU A 111       7.361 -26.170 -11.795  1.00 50.56           O  
ATOM    616  N   ARG A 112       7.015 -30.430  -9.304  1.00 45.88           N  
ATOM    617  CA  ARG A 112       5.716 -30.638  -8.629  1.00 44.99           C  
ATOM    618  C   ARG A 112       5.156 -29.269  -8.268  1.00 46.47           C  
ATOM    619  O   ARG A 112       5.889 -28.236  -8.302  1.00 46.76           O  
ATOM    620  CB  ARG A 112       5.876 -31.413  -7.298  1.00 43.68           C  
ATOM    621  CG  ARG A 112       6.097 -32.902  -7.420  1.00 40.52           C  
ATOM    622  CD  ARG A 112       6.454 -33.462  -6.064  1.00 43.52           C  
ATOM    623  NE  ARG A 112       6.474 -34.930  -6.094  1.00 46.93           N  
ATOM    624  CZ  ARG A 112       6.613 -35.738  -5.035  1.00 45.06           C  
ATOM    625  NH1 ARG A 112       6.856 -35.257  -3.814  1.00 39.93           N  
ATOM    626  NH2 ARG A 112       6.591 -37.046  -5.232  1.00 42.09           N  
ATOM    627  N   PRO A 113       3.842 -29.210  -7.943  1.00 46.67           N  
ATOM    628  CA  PRO A 113       3.245 -27.938  -7.656  1.00 46.16           C  
ATOM    629  C   PRO A 113       3.992 -27.076  -6.648  1.00 46.96           C  
ATOM    630  O   PRO A 113       4.030 -25.856  -6.856  1.00 46.27           O  
ATOM    631  CB  PRO A 113       1.858 -28.315  -7.073  1.00 46.71           C  
ATOM    632  CG  PRO A 113       1.581 -29.673  -7.633  1.00 46.85           C  
ATOM    633  CD  PRO A 113       2.853 -30.316  -8.028  1.00 46.67           C  
ATOM    634  N   ASP A 114       4.569 -27.637  -5.564  1.00 45.21           N  
ATOM    635  CA  ASP A 114       5.163 -26.716  -4.552  1.00 46.02           C  
ATOM    636  C   ASP A 114       6.621 -26.909  -4.337  1.00 43.52           C  
ATOM    637  O   ASP A 114       7.243 -26.216  -3.519  1.00 45.02           O  
ATOM    638  CB  ASP A 114       4.416 -26.742  -3.187  1.00 47.63           C  
ATOM    639  CG  ASP A 114       3.055 -25.999  -3.259  1.00 54.33           C  
ATOM    640  OD1 ASP A 114       2.915 -25.091  -4.136  1.00 56.21           O  
ATOM    641  OD2 ASP A 114       2.148 -26.320  -2.438  1.00 57.73           O  
ATOM    642  N   SER A 115       7.172 -27.824  -5.123  1.00 42.80           N  
ATOM    643  CA  SER A 115       8.524 -28.294  -4.890  1.00 41.08           C  
ATOM    644  C   SER A 115       9.190 -28.809  -6.217  1.00 39.61           C  
ATOM    645  O   SER A 115       8.491 -29.177  -7.209  1.00 38.22           O  
ATOM    646  CB  SER A 115       8.430 -29.416  -3.831  1.00 39.40           C  
ATOM    647  OG  SER A 115       7.897 -30.593  -4.408  1.00 37.58           O  
ATOM    648  N   PHE A 116      10.527 -28.875  -6.211  1.00 38.66           N  
ATOM    649  CA  PHE A 116      11.202 -29.836  -7.110  1.00 37.11           C  
ATOM    650  C   PHE A 116      11.768 -31.046  -6.424  1.00 37.67           C  
ATOM    651  O   PHE A 116      12.101 -30.961  -5.257  1.00 36.96           O  
ATOM    652  CB  PHE A 116      12.343 -29.116  -7.829  1.00 39.44           C  
ATOM    653  CG  PHE A 116      11.853 -28.063  -8.797  1.00 39.54           C  
ATOM    654  CD1 PHE A 116      11.429 -26.832  -8.341  1.00 40.96           C  
ATOM    655  CD2 PHE A 116      11.785 -28.356 -10.182  1.00 43.25           C  
ATOM    656  CE1 PHE A 116      10.994 -25.857  -9.278  1.00 46.87           C  
ATOM    657  CE2 PHE A 116      11.313 -27.380 -11.099  1.00 41.46           C  
ATOM    658  CZ  PHE A 116      10.947 -26.171 -10.646  1.00 39.92           C  
ATOM    659  N   VAL A 117      12.037 -32.102  -7.175  1.00 35.40           N  
ATOM    660  CA  VAL A 117      12.629 -33.264  -6.583  1.00 35.69           C  
ATOM    661  C   VAL A 117      13.870 -33.575  -7.366  1.00 35.93           C  
ATOM    662  O   VAL A 117      13.818 -33.828  -8.615  1.00 35.59           O  
ATOM    663  CB  VAL A 117      11.640 -34.466  -6.531  1.00 35.93           C  
ATOM    664  CG1 VAL A 117      12.229 -35.602  -5.778  1.00 33.66           C  
ATOM    665  CG2 VAL A 117      10.335 -34.004  -5.803  1.00 36.43           C  
ATOM    666  N   LEU A 118      15.005 -33.502  -6.662  1.00 33.56           N  
ATOM    667  CA  LEU A 118      16.307 -33.783  -7.269  1.00 32.68           C  
ATOM    668  C   LEU A 118      16.721 -35.154  -6.913  1.00 31.32           C  
ATOM    669  O   LEU A 118      16.706 -35.501  -5.725  1.00 30.55           O  
ATOM    670  CB  LEU A 118      17.334 -32.767  -6.756  1.00 31.02           C  
ATOM    671  CG  LEU A 118      17.305 -31.368  -7.397  1.00 36.47           C  
ATOM    672  CD1 LEU A 118      15.968 -30.713  -7.887  1.00 35.81           C  
ATOM    673  CD2 LEU A 118      18.234 -30.355  -6.627  1.00 36.38           C  
ATOM    674  N   ILE A 119      17.221 -35.902  -7.893  1.00 29.95           N  
ATOM    675  CA  ILE A 119      17.759 -37.231  -7.656  1.00 31.00           C  
ATOM    676  C   ILE A 119      19.274 -37.183  -7.789  1.00 31.33           C  
ATOM    677  O   ILE A 119      19.774 -36.813  -8.882  1.00 31.05           O  
ATOM    678  CB  ILE A 119      17.258 -38.315  -8.709  1.00 29.91           C  
ATOM    679  CG1 ILE A 119      15.752 -38.256  -8.931  1.00 34.32           C  
ATOM    680  CG2 ILE A 119      17.666 -39.708  -8.305  1.00 35.14           C  
ATOM    681  CD1 ILE A 119      14.915 -38.665  -7.731  1.00 33.60           C  
ATOM    682  N   LEU A 120      19.987 -37.563  -6.711  1.00 30.24           N  
ATOM    683  CA  LEU A 120      21.393 -37.326  -6.650  1.00 29.10           C  
ATOM    684  C   LEU A 120      22.025 -38.631  -6.361  1.00 31.47           C  
ATOM    685  O   LEU A 120      21.469 -39.478  -5.695  1.00 28.99           O  
ATOM    686  CB  LEU A 120      21.763 -36.350  -5.506  1.00 30.47           C  
ATOM    687  CG  LEU A 120      21.164 -34.995  -5.712  1.00 27.09           C  
ATOM    688  CD1 LEU A 120      20.714 -34.312  -4.430  1.00 30.85           C  
ATOM    689  CD2 LEU A 120      22.133 -34.071  -6.492  1.00 32.14           C  
ATOM    690  N   GLU A 121      23.267 -38.740  -6.800  1.00 31.19           N  
ATOM    691  CA  GLU A 121      24.188 -39.798  -6.457  1.00 32.74           C  
ATOM    692  C   GLU A 121      24.217 -39.987  -4.964  1.00 32.04           C  
ATOM    693  O   GLU A 121      24.180 -39.023  -4.214  1.00 30.33           O  
ATOM    694  CB  GLU A 121      25.549 -39.221  -6.916  1.00 33.59           C  
ATOM    695  CG  GLU A 121      26.661 -40.028  -6.610  1.00 38.65           C  
ATOM    696  CD  GLU A 121      28.002 -39.454  -7.163  1.00 44.57           C  
ATOM    697  OE1 GLU A 121      28.168 -38.238  -7.510  1.00 36.26           O  
ATOM    698  OE2 GLU A 121      28.913 -40.273  -7.167  1.00 48.00           O  
ATOM    699  N   ARG A 122      24.377 -41.220  -4.513  1.00 31.29           N  
ATOM    700  CA  ARG A 122      24.544 -41.473  -3.106  1.00 32.95           C  
ATOM    701  C   ARG A 122      25.596 -42.508  -2.877  1.00 34.08           C  
ATOM    702  O   ARG A 122      25.428 -43.678  -3.207  1.00 34.66           O  
ATOM    703  CB  ARG A 122      23.296 -41.913  -2.408  1.00 33.09           C  
ATOM    704  CG  ARG A 122      23.527 -42.467  -1.022  1.00 32.27           C  
ATOM    705  CD  ARG A 122      22.111 -42.470  -0.211  1.00 33.99           C  
ATOM    706  NE  ARG A 122      21.186 -43.573  -0.695  1.00 34.76           N  
ATOM    707  CZ  ARG A 122      21.349 -44.891  -0.444  1.00 38.82           C  
ATOM    708  NH1 ARG A 122      22.319 -45.357   0.363  1.00 32.36           N  
ATOM    709  NH2 ARG A 122      20.470 -45.771  -0.924  1.00 33.50           N  
ATOM    710  N   PRO A 123      26.727 -42.071  -2.334  1.00 35.79           N  
ATOM    711  CA  PRO A 123      27.853 -42.992  -1.961  1.00 35.31           C  
ATOM    712  C   PRO A 123      27.381 -43.874  -0.772  1.00 35.06           C  
ATOM    713  O   PRO A 123      26.520 -43.487   0.017  1.00 32.73           O  
ATOM    714  CB  PRO A 123      28.922 -42.045  -1.477  1.00 32.60           C  
ATOM    715  CG  PRO A 123      28.502 -40.651  -1.926  1.00 36.05           C  
ATOM    716  CD  PRO A 123      27.040 -40.639  -2.088  1.00 36.77           C  
ATOM    717  N   GLU A 124      27.962 -45.034  -0.636  1.00 35.65           N  
ATOM    718  CA  GLU A 124      27.506 -45.922   0.418  1.00 38.41           C  
ATOM    719  C   GLU A 124      28.610 -46.912   0.791  1.00 37.52           C  
ATOM    720  O   GLU A 124      29.065 -47.622  -0.073  1.00 39.61           O  
ATOM    721  CB  GLU A 124      26.226 -46.648  -0.028  1.00 39.56           C  
ATOM    722  CG  GLU A 124      25.920 -47.940   0.749  1.00 46.07           C  
ATOM    723  CD  GLU A 124      25.499 -47.671   2.195  1.00 56.42           C  
ATOM    724  OE1 GLU A 124      24.568 -46.855   2.380  1.00 65.68           O  
ATOM    725  OE2 GLU A 124      26.065 -48.268   3.155  1.00 59.55           O  
ATOM    726  N   PRO A 125      29.061 -46.936   2.062  1.00 35.19           N  
ATOM    727  CA  PRO A 125      28.669 -46.159   3.184  1.00 33.83           C  
ATOM    728  C   PRO A 125      29.240 -44.708   3.029  1.00 33.95           C  
ATOM    729  O   PRO A 125      30.266 -44.533   2.343  1.00 32.44           O  
ATOM    730  CB  PRO A 125      29.373 -46.862   4.327  1.00 33.97           C  
ATOM    731  CG  PRO A 125      30.641 -47.411   3.698  1.00 34.94           C  
ATOM    732  CD  PRO A 125      30.155 -47.889   2.394  1.00 36.85           C  
ATOM    733  N   VAL A 126      28.543 -43.730   3.612  1.00 32.82           N  
ATOM    734  CA  VAL A 126      28.914 -42.316   3.487  1.00 32.52           C  
ATOM    735  C   VAL A 126      28.701 -41.691   4.854  1.00 33.44           C  
ATOM    736  O   VAL A 126      27.868 -42.164   5.688  1.00 31.70           O  
ATOM    737  CB  VAL A 126      28.027 -41.624   2.411  1.00 32.95           C  
ATOM    738  CG1 VAL A 126      26.587 -41.581   2.832  1.00 33.28           C  
ATOM    739  CG2 VAL A 126      28.489 -40.219   2.002  1.00 32.16           C  
ATOM    740  N   GLN A 127      29.415 -40.573   5.122  1.00 29.07           N  
ATOM    741  CA  GLN A 127      29.145 -39.795   6.300  1.00 28.55           C  
ATOM    742  C   GLN A 127      29.575 -38.366   5.969  1.00 27.50           C  
ATOM    743  O   GLN A 127      30.593 -38.197   5.287  1.00 24.75           O  
ATOM    744  CB  GLN A 127      29.979 -40.286   7.483  1.00 27.16           C  
ATOM    745  CG  GLN A 127      29.743 -39.455   8.748  1.00 32.40           C  
ATOM    746  CD  GLN A 127      30.546 -40.025   9.910  1.00 33.10           C  
ATOM    747  OE1 GLN A 127      31.737 -40.324   9.776  1.00 32.71           O  
ATOM    748  NE2 GLN A 127      29.868 -40.241  11.044  1.00 39.51           N  
ATOM    749  N   ASP A 128      28.773 -37.397   6.345  1.00 26.27           N  
ATOM    750  CA  ASP A 128      29.159 -36.006   6.077  1.00 27.29           C  
ATOM    751  C   ASP A 128      30.283 -35.579   7.020  1.00 26.03           C  
ATOM    752  O   ASP A 128      30.566 -36.178   8.138  1.00 25.21           O  
ATOM    753  CB  ASP A 128      27.939 -35.047   5.961  1.00 25.66           C  
ATOM    754  CG  ASP A 128      27.304 -34.635   7.331  1.00 33.64           C  
ATOM    755  OD1 ASP A 128      27.961 -34.644   8.390  1.00 30.69           O  
ATOM    756  OD2 ASP A 128      26.161 -34.137   7.244  1.00 36.75           O  
ATOM    757  N   LEU A 129      30.963 -34.540   6.615  1.00 25.11           N  
ATOM    758  CA  LEU A 129      32.138 -34.211   7.343  1.00 25.33           C  
ATOM    759  C   LEU A 129      31.803 -33.618   8.717  1.00 25.78           C  
ATOM    760  O   LEU A 129      32.596 -33.686   9.621  1.00 25.97           O  
ATOM    761  CB  LEU A 129      33.049 -33.254   6.534  1.00 23.08           C  
ATOM    762  CG  LEU A 129      34.308 -32.802   7.302  1.00 23.42           C  
ATOM    763  CD1 LEU A 129      35.411 -33.905   7.484  1.00 20.46           C  
ATOM    764  CD2 LEU A 129      34.938 -31.745   6.310  1.00 24.99           C  
ATOM    765  N   PHE A 130      30.652 -32.970   8.866  1.00 29.13           N  
ATOM    766  CA  PHE A 130      30.264 -32.446  10.173  1.00 29.96           C  
ATOM    767  C   PHE A 130      30.138 -33.584  11.204  1.00 29.66           C  
ATOM    768  O   PHE A 130      30.637 -33.478  12.323  1.00 28.61           O  
ATOM    769  CB  PHE A 130      28.894 -31.756  10.019  1.00 31.02           C  
ATOM    770  CG  PHE A 130      28.397 -31.151  11.299  1.00 34.71           C  
ATOM    771  CD1 PHE A 130      27.602 -31.924  12.182  1.00 40.18           C  
ATOM    772  CD2 PHE A 130      28.702 -29.818  11.640  1.00 34.72           C  
ATOM    773  CE1 PHE A 130      27.152 -31.392  13.393  1.00 40.40           C  
ATOM    774  CE2 PHE A 130      28.233 -29.266  12.858  1.00 38.60           C  
ATOM    775  CZ  PHE A 130      27.485 -30.090  13.735  1.00 38.86           C  
ATOM    776  N   ASP A 131      29.497 -34.699  10.803  1.00 30.16           N  
ATOM    777  CA  ASP A 131      29.301 -35.825  11.725  1.00 30.32           C  
ATOM    778  C   ASP A 131      30.605 -36.553  11.982  1.00 30.52           C  
ATOM    779  O   ASP A 131      30.894 -37.024  13.099  1.00 29.18           O  
ATOM    780  CB  ASP A 131      28.310 -36.837  11.078  1.00 29.43           C  
ATOM    781  CG  ASP A 131      26.887 -36.321  11.074  1.00 35.90           C  
ATOM    782  OD1 ASP A 131      26.625 -35.350  11.774  1.00 37.73           O  
ATOM    783  OD2 ASP A 131      26.052 -36.835  10.298  1.00 39.80           O  
ATOM    784  N   PHE A 132      31.409 -36.658  10.934  1.00 28.53           N  
ATOM    785  CA  PHE A 132      32.750 -37.228  11.091  1.00 27.38           C  
ATOM    786  C   PHE A 132      33.567 -36.511  12.133  1.00 30.02           C  
ATOM    787  O   PHE A 132      34.182 -37.134  13.040  1.00 30.75           O  
ATOM    788  CB  PHE A 132      33.400 -37.208   9.724  1.00 26.47           C  
ATOM    789  CG  PHE A 132      34.708 -37.930   9.669  1.00 28.90           C  
ATOM    790  CD1 PHE A 132      34.732 -39.303   9.431  1.00 29.70           C  
ATOM    791  CD2 PHE A 132      35.908 -37.242   9.826  1.00 29.64           C  
ATOM    792  CE1 PHE A 132      35.969 -39.977   9.316  1.00 31.52           C  
ATOM    793  CE2 PHE A 132      37.158 -37.913   9.755  1.00 30.60           C  
ATOM    794  CZ  PHE A 132      37.204 -39.292   9.503  1.00 30.16           C  
ATOM    795  N   ILE A 133      33.622 -35.180  12.027  1.00 28.28           N  
ATOM    796  CA  ILE A 133      34.284 -34.336  13.054  1.00 27.77           C  
ATOM    797  C   ILE A 133      33.596 -34.430  14.424  1.00 30.62           C  
ATOM    798  O   ILE A 133      34.276 -34.504  15.403  1.00 31.56           O  
ATOM    799  CB  ILE A 133      34.410 -32.840  12.606  1.00 26.40           C  
ATOM    800  CG1 ILE A 133      35.422 -32.804  11.413  1.00 24.61           C  
ATOM    801  CG2 ILE A 133      34.870 -31.926  13.826  1.00 29.10           C  
ATOM    802  CD1 ILE A 133      35.503 -31.455  10.542  1.00 26.63           C  
ATOM    803  N   THR A 134      32.272 -34.453  14.488  1.00 31.85           N  
ATOM    804  CA  THR A 134      31.595 -34.653  15.797  1.00 35.11           C  
ATOM    805  C   THR A 134      32.050 -35.938  16.439  1.00 37.09           C  
ATOM    806  O   THR A 134      32.253 -36.000  17.610  1.00 39.29           O  
ATOM    807  CB  THR A 134      30.062 -34.708  15.579  1.00 35.29           C  
ATOM    808  OG1 THR A 134      29.651 -33.474  15.033  1.00 33.57           O  
ATOM    809  CG2 THR A 134      29.284 -34.894  16.892  1.00 37.26           C  
ATOM    810  N   GLU A 135      32.298 -36.961  15.663  1.00 38.46           N  
ATOM    811  CA  GLU A 135      32.514 -38.259  16.209  1.00 41.85           C  
ATOM    812  C   GLU A 135      33.978 -38.411  16.521  1.00 42.40           C  
ATOM    813  O   GLU A 135      34.339 -38.955  17.596  1.00 43.22           O  
ATOM    814  CB  GLU A 135      32.040 -39.190  15.140  1.00 42.25           C  
ATOM    815  CG  GLU A 135      32.454 -40.575  15.187  1.00 50.18           C  
ATOM    816  CD  GLU A 135      31.466 -41.402  14.346  1.00 58.63           C  
ATOM    817  OE1 GLU A 135      30.242 -41.013  14.283  1.00 60.41           O  
ATOM    818  OE2 GLU A 135      31.936 -42.393  13.745  1.00 60.86           O  
ATOM    819  N   ARG A 136      34.836 -37.824  15.679  1.00 39.32           N  
ATOM    820  CA  ARG A 136      36.258 -38.026  15.833  1.00 39.36           C  
ATOM    821  C   ARG A 136      37.112 -36.902  16.422  1.00 37.79           C  
ATOM    822  O   ARG A 136      38.311 -37.114  16.687  1.00 38.90           O  
ATOM    823  CB  ARG A 136      36.849 -38.562  14.510  1.00 39.99           C  
ATOM    824  CG  ARG A 136      36.182 -39.865  14.158  1.00 45.81           C  
ATOM    825  CD  ARG A 136      36.689 -40.506  12.872  1.00 54.30           C  
ATOM    826  NE  ARG A 136      38.164 -40.525  12.689  1.00 53.36           N  
ATOM    827  CZ  ARG A 136      38.782 -41.378  11.854  1.00 48.64           C  
ATOM    828  NH1 ARG A 136      38.053 -42.311  11.188  1.00 45.04           N  
ATOM    829  NH2 ARG A 136      40.117 -41.325  11.699  1.00 47.92           N  
ATOM    830  N   GLY A 137      36.499 -35.757  16.673  1.00 35.01           N  
ATOM    831  CA  GLY A 137      37.180 -34.545  17.080  1.00 32.95           C  
ATOM    832  C   GLY A 137      38.076 -33.954  15.994  1.00 32.78           C  
ATOM    833  O   GLY A 137      37.942 -34.317  14.800  1.00 31.00           O  
ATOM    834  N   ALA A 138      39.051 -33.124  16.424  1.00 31.60           N  
ATOM    835  CA  ALA A 138      40.004 -32.500  15.553  1.00 29.42           C  
ATOM    836  C   ALA A 138      40.753 -33.573  14.758  1.00 30.65           C  
ATOM    837  O   ALA A 138      41.155 -34.642  15.298  1.00 29.49           O  
ATOM    838  CB  ALA A 138      40.998 -31.688  16.381  1.00 31.08           C  
ATOM    839  N   LEU A 139      40.962 -33.331  13.469  1.00 26.44           N  
ATOM    840  CA  LEU A 139      41.533 -34.345  12.599  1.00 27.14           C  
ATOM    841  C   LEU A 139      43.066 -34.238  12.637  1.00 27.80           C  
ATOM    842  O   LEU A 139      43.601 -33.125  12.648  1.00 27.42           O  
ATOM    843  CB  LEU A 139      41.025 -34.089  11.181  1.00 26.24           C  
ATOM    844  CG  LEU A 139      39.494 -34.170  11.040  1.00 27.13           C  
ATOM    845  CD1 LEU A 139      39.285 -34.159   9.540  1.00 27.40           C  
ATOM    846  CD2 LEU A 139      38.887 -35.447  11.758  1.00 25.71           C  
ATOM    847  N   GLN A 140      43.785 -35.376  12.614  1.00 27.62           N  
ATOM    848  CA  GLN A 140      45.240 -35.335  12.428  1.00 29.70           C  
ATOM    849  C   GLN A 140      45.548 -34.525  11.148  1.00 28.73           C  
ATOM    850  O   GLN A 140      44.792 -34.611  10.157  1.00 25.59           O  
ATOM    851  CB  GLN A 140      45.733 -36.759  12.209  1.00 29.89           C  
ATOM    852  CG  GLN A 140      45.740 -37.655  13.494  1.00 38.19           C  
ATOM    853  CD  GLN A 140      46.332 -39.071  13.092  1.00 38.73           C  
ATOM    854  OE1 GLN A 140      47.198 -39.169  12.143  1.00 49.24           O  
ATOM    855  NE2 GLN A 140      45.879 -40.141  13.794  1.00 54.11           N  
ATOM    856  N   GLU A 141      46.676 -33.785  11.129  1.00 27.08           N  
ATOM    857  CA  GLU A 141      46.985 -32.921   9.948  1.00 26.52           C  
ATOM    858  C   GLU A 141      47.031 -33.680   8.660  1.00 27.40           C  
ATOM    859  O   GLU A 141      46.584 -33.219   7.670  1.00 25.05           O  
ATOM    860  CB  GLU A 141      48.234 -32.074  10.193  1.00 27.30           C  
ATOM    861  CG  GLU A 141      47.956 -31.058  11.362  1.00 28.63           C  
ATOM    862  CD  GLU A 141      49.024 -29.999  11.494  1.00 30.12           C  
ATOM    863  OE1 GLU A 141      49.841 -29.781  10.557  1.00 27.43           O  
ATOM    864  OE2 GLU A 141      49.098 -29.471  12.609  1.00 30.70           O  
ATOM    865  N   GLU A 142      47.581 -34.903   8.667  1.00 26.74           N  
ATOM    866  CA  GLU A 142      47.675 -35.621   7.408  1.00 27.41           C  
ATOM    867  C   GLU A 142      46.313 -35.920   6.825  1.00 25.55           C  
ATOM    868  O   GLU A 142      46.142 -35.943   5.606  1.00 23.97           O  
ATOM    869  CB  GLU A 142      48.387 -36.985   7.693  1.00 30.08           C  
ATOM    870  CG  GLU A 142      48.590 -37.864   6.492  1.00 28.60           C  
ATOM    871  CD  GLU A 142      49.167 -39.294   6.914  1.00 33.18           C  
ATOM    872  OE1 GLU A 142      48.442 -40.143   7.485  1.00 34.97           O  
ATOM    873  OE2 GLU A 142      50.367 -39.475   6.664  1.00 35.79           O  
ATOM    874  N   LEU A 143      45.376 -36.244   7.695  1.00 23.17           N  
ATOM    875  CA  LEU A 143      44.006 -36.484   7.237  1.00 23.84           C  
ATOM    876  C   LEU A 143      43.362 -35.177   6.786  1.00 24.15           C  
ATOM    877  O   LEU A 143      42.753 -35.129   5.685  1.00 25.29           O  
ATOM    878  CB  LEU A 143      43.144 -37.028   8.353  1.00 23.11           C  
ATOM    879  CG  LEU A 143      41.698 -37.370   7.974  1.00 25.36           C  
ATOM    880  CD1 LEU A 143      41.658 -38.324   6.711  1.00 25.33           C  
ATOM    881  CD2 LEU A 143      41.097 -38.033   9.169  1.00 25.01           C  
ATOM    882  N   ALA A 144      43.528 -34.139   7.579  1.00 22.86           N  
ATOM    883  CA  ALA A 144      43.014 -32.795   7.157  1.00 22.68           C  
ATOM    884  C   ALA A 144      43.597 -32.353   5.820  1.00 22.68           C  
ATOM    885  O   ALA A 144      42.877 -31.776   5.024  1.00 23.92           O  
ATOM    886  CB  ALA A 144      43.285 -31.747   8.141  1.00 21.64           C  
ATOM    887  N   ARG A 145      44.919 -32.585   5.558  1.00 24.59           N  
ATOM    888  CA  ARG A 145      45.545 -32.201   4.323  1.00 22.45           C  
ATOM    889  C   ARG A 145      44.886 -32.916   3.160  1.00 22.52           C  
ATOM    890  O   ARG A 145      44.567 -32.328   2.122  1.00 21.79           O  
ATOM    891  CB  ARG A 145      47.075 -32.602   4.381  1.00 21.31           C  
ATOM    892  CG  ARG A 145      47.857 -32.312   3.038  1.00 25.01           C  
ATOM    893  CD  ARG A 145      49.391 -32.700   3.237  1.00 24.23           C  
ATOM    894  NE  ARG A 145      49.951 -32.057   4.416  1.00 27.14           N  
ATOM    895  CZ  ARG A 145      50.346 -32.652   5.530  1.00 28.55           C  
ATOM    896  NH1 ARG A 145      50.391 -33.990   5.712  1.00 26.72           N  
ATOM    897  NH2 ARG A 145      50.755 -31.885   6.483  1.00 33.03           N  
ATOM    898  N   SER A 146      44.633 -34.210   3.315  1.00 23.58           N  
ATOM    899  CA  SER A 146      44.034 -35.016   2.253  1.00 22.98           C  
ATOM    900  C   SER A 146      42.629 -34.504   1.985  1.00 25.29           C  
ATOM    901  O   SER A 146      42.246 -34.287   0.841  1.00 24.96           O  
ATOM    902  CB  SER A 146      43.901 -36.478   2.747  1.00 23.14           C  
ATOM    903  OG  SER A 146      43.324 -37.235   1.655  1.00 26.82           O  
ATOM    904  N   PHE A 147      41.849 -34.256   3.033  1.00 23.43           N  
ATOM    905  CA  PHE A 147      40.470 -33.831   2.836  1.00 20.83           C  
ATOM    906  C   PHE A 147      40.463 -32.415   2.237  1.00 21.53           C  
ATOM    907  O   PHE A 147      39.697 -32.097   1.359  1.00 23.08           O  
ATOM    908  CB  PHE A 147      39.835 -33.768   4.207  1.00 23.16           C  
ATOM    909  CG  PHE A 147      39.280 -35.122   4.668  1.00 25.29           C  
ATOM    910  CD1 PHE A 147      39.541 -36.284   3.910  1.00 26.75           C  
ATOM    911  CD2 PHE A 147      38.465 -35.178   5.801  1.00 23.55           C  
ATOM    912  CE1 PHE A 147      38.958 -37.612   4.344  1.00 30.21           C  
ATOM    913  CE2 PHE A 147      37.954 -36.420   6.237  1.00 27.52           C  
ATOM    914  CZ  PHE A 147      38.152 -37.604   5.472  1.00 26.48           C  
ATOM    915  N   PHE A 148      41.287 -31.542   2.822  1.00 21.31           N  
ATOM    916  CA  PHE A 148      41.271 -30.136   2.327  1.00 20.47           C  
ATOM    917  C   PHE A 148      41.678 -30.061   0.874  1.00 23.13           C  
ATOM    918  O   PHE A 148      41.179 -29.268   0.156  1.00 22.57           O  
ATOM    919  CB  PHE A 148      42.219 -29.305   3.184  1.00 18.27           C  
ATOM    920  CG  PHE A 148      42.025 -27.796   3.021  1.00 22.88           C  
ATOM    921  CD1 PHE A 148      40.765 -27.196   3.264  1.00 23.16           C  
ATOM    922  CD2 PHE A 148      43.101 -27.012   2.633  1.00 19.06           C  
ATOM    923  CE1 PHE A 148      40.651 -25.819   3.101  1.00 23.62           C  
ATOM    924  CE2 PHE A 148      42.973 -25.585   2.479  1.00 20.88           C  
ATOM    925  CZ  PHE A 148      41.759 -25.041   2.701  1.00 20.95           C  
ATOM    926  N   TRP A 149      42.733 -30.790   0.481  1.00 22.32           N  
ATOM    927  CA  TRP A 149      43.184 -30.865  -0.937  1.00 20.82           C  
ATOM    928  C   TRP A 149      42.022 -31.284  -1.813  1.00 20.64           C  
ATOM    929  O   TRP A 149      41.741 -30.667  -2.849  1.00 21.97           O  
ATOM    930  CB  TRP A 149      44.287 -31.988  -1.031  1.00 20.43           C  
ATOM    931  CG  TRP A 149      44.842 -32.115  -2.505  1.00 21.15           C  
ATOM    932  CD1 TRP A 149      44.469 -33.007  -3.495  1.00 24.06           C  
ATOM    933  CD2 TRP A 149      45.873 -31.279  -3.073  1.00 23.65           C  
ATOM    934  NE1 TRP A 149      45.237 -32.757  -4.658  1.00 25.56           N  
ATOM    935  CE2 TRP A 149      46.103 -31.722  -4.414  1.00 24.09           C  
ATOM    936  CE3 TRP A 149      46.652 -30.205  -2.552  1.00 26.82           C  
ATOM    937  CZ2 TRP A 149      47.081 -31.103  -5.263  1.00 24.33           C  
ATOM    938  CZ3 TRP A 149      47.699 -29.615  -3.402  1.00 24.25           C  
ATOM    939  CH2 TRP A 149      47.823 -30.035  -4.741  1.00 26.48           C  
ATOM    940  N   GLN A 150      41.335 -32.394  -1.448  1.00 18.88           N  
ATOM    941  CA  GLN A 150      40.228 -32.807  -2.234  1.00 20.76           C  
ATOM    942  C   GLN A 150      39.126 -31.748  -2.328  1.00 22.67           C  
ATOM    943  O   GLN A 150      38.431 -31.620  -3.373  1.00 21.86           O  
ATOM    944  CB  GLN A 150      39.621 -34.113  -1.656  1.00 23.39           C  
ATOM    945  CG  GLN A 150      40.561 -35.314  -1.910  1.00 24.59           C  
ATOM    946  CD  GLN A 150      39.819 -36.644  -1.566  1.00 25.61           C  
ATOM    947  OE1 GLN A 150      38.692 -36.864  -1.995  1.00 28.87           O  
ATOM    948  NE2 GLN A 150      40.406 -37.418  -0.688  1.00 30.09           N  
ATOM    949  N   VAL A 151      38.894 -31.026  -1.255  1.00 23.16           N  
ATOM    950  CA  VAL A 151      37.839 -30.030  -1.365  1.00 22.31           C  
ATOM    951  C   VAL A 151      38.307 -28.969  -2.357  1.00 23.03           C  
ATOM    952  O   VAL A 151      37.478 -28.335  -3.018  1.00 22.95           O  
ATOM    953  CB  VAL A 151      37.609 -29.343  -0.026  1.00 22.73           C  
ATOM    954  CG1 VAL A 151      36.751 -27.981  -0.093  1.00 21.65           C  
ATOM    955  CG2 VAL A 151      36.924 -30.333   1.048  1.00 19.33           C  
ATOM    956  N   LEU A 152      39.571 -28.556  -2.245  1.00 21.56           N  
ATOM    957  CA  LEU A 152      40.090 -27.508  -3.175  1.00 23.37           C  
ATOM    958  C   LEU A 152      39.993 -27.959  -4.641  1.00 22.39           C  
ATOM    959  O   LEU A 152      39.640 -27.184  -5.487  1.00 21.99           O  
ATOM    960  CB  LEU A 152      41.648 -27.307  -2.884  1.00 24.79           C  
ATOM    961  CG  LEU A 152      42.041 -26.090  -1.979  1.00 28.96           C  
ATOM    962  CD1 LEU A 152      41.858 -24.692  -2.642  1.00 29.37           C  
ATOM    963  CD2 LEU A 152      41.257 -25.913  -0.843  1.00 28.91           C  
ATOM    964  N   GLU A 153      40.233 -29.245  -4.941  1.00 21.28           N  
ATOM    965  CA  GLU A 153      40.091 -29.756  -6.299  1.00 21.77           C  
ATOM    966  C   GLU A 153      38.592 -29.655  -6.729  1.00 22.81           C  
ATOM    967  O   GLU A 153      38.313 -29.212  -7.863  1.00 21.05           O  
ATOM    968  CB  GLU A 153      40.561 -31.252  -6.393  1.00 23.87           C  
ATOM    969  CG  GLU A 153      42.067 -31.365  -6.293  1.00 23.88           C  
ATOM    970  CD  GLU A 153      42.794 -30.777  -7.481  1.00 30.87           C  
ATOM    971  OE1 GLU A 153      42.390 -31.140  -8.555  1.00 29.83           O  
ATOM    972  OE2 GLU A 153      43.859 -30.111  -7.372  1.00 29.42           O  
ATOM    973  N   ALA A 154      37.652 -29.977  -5.796  1.00 22.82           N  
ATOM    974  CA  ALA A 154      36.167 -29.921  -6.077  1.00 20.17           C  
ATOM    975  C   ALA A 154      35.744 -28.444  -6.329  1.00 22.74           C  
ATOM    976  O   ALA A 154      34.998 -28.134  -7.240  1.00 23.12           O  
ATOM    977  CB  ALA A 154      35.365 -30.474  -4.826  1.00 20.21           C  
ATOM    978  N   VAL A 155      36.178 -27.522  -5.472  1.00 22.86           N  
ATOM    979  CA  VAL A 155      35.848 -26.085  -5.677  1.00 21.95           C  
ATOM    980  C   VAL A 155      36.427 -25.531  -6.951  1.00 22.92           C  
ATOM    981  O   VAL A 155      35.738 -24.835  -7.697  1.00 23.13           O  
ATOM    982  CB  VAL A 155      36.323 -25.249  -4.434  1.00 20.73           C  
ATOM    983  CG1 VAL A 155      35.932 -23.759  -4.559  1.00 22.62           C  
ATOM    984  CG2 VAL A 155      35.575 -25.815  -3.159  1.00 20.11           C  
ATOM    985  N   ARG A 156      37.726 -25.781  -7.229  1.00 22.83           N  
ATOM    986  CA  ARG A 156      38.326 -25.393  -8.546  1.00 23.82           C  
ATOM    987  C   ARG A 156      37.513 -25.953  -9.702  1.00 25.67           C  
ATOM    988  O   ARG A 156      37.305 -25.256 -10.704  1.00 28.03           O  
ATOM    989  CB  ARG A 156      39.733 -25.972  -8.635  1.00 24.26           C  
ATOM    990  CG  ARG A 156      40.717 -25.239  -7.768  1.00 23.59           C  
ATOM    991  CD  ARG A 156      42.176 -25.863  -7.941  1.00 22.05           C  
ATOM    992  NE  ARG A 156      42.522 -25.802  -9.349  1.00 25.12           N  
ATOM    993  CZ  ARG A 156      43.408 -26.590  -9.980  1.00 24.97           C  
ATOM    994  NH1 ARG A 156      44.148 -27.503  -9.307  1.00 21.71           N  
ATOM    995  NH2 ARG A 156      43.562 -26.426 -11.300  1.00 22.49           N  
ATOM    996  N   HIS A 157      37.100 -27.224  -9.655  1.00 25.34           N  
ATOM    997  CA  HIS A 157      36.184 -27.738 -10.726  1.00 26.16           C  
ATOM    998  C   HIS A 157      34.896 -26.841 -10.819  1.00 26.22           C  
ATOM    999  O   HIS A 157      34.497 -26.455 -11.937  1.00 24.14           O  
ATOM   1000  CB  HIS A 157      35.807 -29.220 -10.494  1.00 29.01           C  
ATOM   1001  CG  HIS A 157      34.756 -29.752 -11.414  1.00 27.83           C  
ATOM   1002  ND1 HIS A 157      35.060 -30.126 -12.691  1.00 28.14           N  
ATOM   1003  CD2 HIS A 157      33.446 -30.019 -11.235  1.00 31.11           C  
ATOM   1004  CE1 HIS A 157      33.968 -30.616 -13.264  1.00 33.40           C  
ATOM   1005  NE2 HIS A 157      32.970 -30.530 -12.415  1.00 32.14           N  
ATOM   1006  N   CYS A 158      34.237 -26.550  -9.702  1.00 22.79           N  
ATOM   1007  CA  CYS A 158      33.012 -25.730  -9.753  1.00 24.22           C  
ATOM   1008  C   CYS A 158      33.350 -24.417 -10.443  1.00 24.38           C  
ATOM   1009  O   CYS A 158      32.645 -24.004 -11.413  1.00 23.43           O  
ATOM   1010  CB  CYS A 158      32.531 -25.329  -8.288  1.00 24.35           C  
ATOM   1011  SG  CYS A 158      31.771 -26.833  -7.557  1.00 28.68           S  
ATOM   1012  N   HIS A 159      34.457 -23.800 -10.028  1.00 23.35           N  
ATOM   1013  CA  HIS A 159      34.817 -22.439 -10.615  1.00 25.21           C  
ATOM   1014  C   HIS A 159      35.186 -22.538 -12.084  1.00 26.01           C  
ATOM   1015  O   HIS A 159      34.826 -21.685 -12.869  1.00 25.38           O  
ATOM   1016  CB  HIS A 159      35.989 -21.842  -9.841  1.00 24.19           C  
ATOM   1017  CG  HIS A 159      35.586 -21.371  -8.457  1.00 30.31           C  
ATOM   1018  ND1 HIS A 159      36.233 -20.351  -7.816  1.00 33.32           N  
ATOM   1019  CD2 HIS A 159      34.555 -21.727  -7.624  1.00 29.25           C  
ATOM   1020  CE1 HIS A 159      35.655 -20.107  -6.639  1.00 39.57           C  
ATOM   1021  NE2 HIS A 159      34.642 -20.936  -6.490  1.00 32.75           N  
ATOM   1022  N   ASN A 160      35.737 -23.664 -12.491  1.00 26.25           N  
ATOM   1023  CA  ASN A 160      36.197 -23.830 -13.907  1.00 29.77           C  
ATOM   1024  C   ASN A 160      34.945 -24.014 -14.742  1.00 30.29           C  
ATOM   1025  O   ASN A 160      34.943 -23.640 -15.911  1.00 30.77           O  
ATOM   1026  CB  ASN A 160      36.914 -25.143 -14.134  1.00 29.48           C  
ATOM   1027  CG AASN A 160      38.248 -25.204 -13.599  0.50 30.78           C  
ATOM   1028  OD1AASN A 160      38.850 -24.214 -13.264  0.50 39.73           O  
ATOM   1029  ND2AASN A 160      38.737 -26.438 -13.437  0.50 35.30           N  
ATOM   1030  CG BASN A 160      37.768 -25.137 -15.409  0.50 25.98           C  
ATOM   1031  OD1BASN A 160      38.453 -24.177 -15.728  0.50 22.31           O  
ATOM   1032  ND2BASN A 160      37.730 -26.215 -16.098  0.50 21.71           N  
ATOM   1033  N   CYS A 161      33.872 -24.554 -14.139  1.00 29.89           N  
ATOM   1034  CA  CYS A 161      32.550 -24.762 -14.769  1.00 30.63           C  
ATOM   1035  C   CYS A 161      31.657 -23.537 -14.670  1.00 30.60           C  
ATOM   1036  O   CYS A 161      30.487 -23.560 -15.143  1.00 32.73           O  
ATOM   1037  CB  CYS A 161      31.776 -26.001 -14.162  1.00 30.83           C  
ATOM   1038  SG  CYS A 161      32.661 -27.484 -14.621  1.00 34.43           S  
ATOM   1039  N   GLY A 162      32.201 -22.455 -14.120  1.00 30.24           N  
ATOM   1040  CA  GLY A 162      31.432 -21.192 -14.003  1.00 27.08           C  
ATOM   1041  C   GLY A 162      30.432 -21.194 -12.868  1.00 27.33           C  
ATOM   1042  O   GLY A 162      29.443 -20.445 -12.936  1.00 25.45           O  
ATOM   1043  N   VAL A 163      30.661 -22.006 -11.795  1.00 25.84           N  
ATOM   1044  CA  VAL A 163      29.745 -22.080 -10.630  1.00 26.26           C  
ATOM   1045  C   VAL A 163      30.514 -21.698  -9.341  1.00 24.46           C  
ATOM   1046  O   VAL A 163      31.635 -22.181  -9.085  1.00 25.77           O  
ATOM   1047  CB  VAL A 163      29.276 -23.505 -10.475  1.00 25.95           C  
ATOM   1048  CG1 VAL A 163      28.470 -23.757  -9.213  1.00 22.61           C  
ATOM   1049  CG2 VAL A 163      28.502 -23.942 -11.851  1.00 26.26           C  
ATOM   1050  N   LEU A 164      29.899 -20.812  -8.602  1.00 26.07           N  
ATOM   1051  CA  LEU A 164      30.280 -20.381  -7.230  1.00 25.38           C  
ATOM   1052  C   LEU A 164      29.359 -21.088  -6.196  1.00 27.89           C  
ATOM   1053  O   LEU A 164      28.089 -20.909  -6.214  1.00 26.98           O  
ATOM   1054  CB  LEU A 164      30.143 -18.858  -7.208  1.00 25.80           C  
ATOM   1055  CG  LEU A 164      30.620 -18.252  -5.882  1.00 24.34           C  
ATOM   1056  CD1 LEU A 164      32.212 -18.378  -5.872  1.00 24.36           C  
ATOM   1057  CD2 LEU A 164      30.222 -16.712  -5.642  1.00 22.47           C  
ATOM   1058  N   HIS A 165      29.945 -21.894  -5.293  1.00 23.86           N  
ATOM   1059  CA  HIS A 165      29.092 -22.696  -4.391  1.00 25.70           C  
ATOM   1060  C   HIS A 165      28.395 -21.837  -3.286  1.00 25.03           C  
ATOM   1061  O   HIS A 165      27.148 -22.023  -2.989  1.00 26.34           O  
ATOM   1062  CB  HIS A 165      29.980 -23.775  -3.644  1.00 25.67           C  
ATOM   1063  CG  HIS A 165      29.189 -24.761  -2.851  1.00 24.89           C  
ATOM   1064  ND1 HIS A 165      28.821 -24.536  -1.541  1.00 23.45           N  
ATOM   1065  CD2 HIS A 165      28.813 -26.038  -3.142  1.00 21.86           C  
ATOM   1066  CE1 HIS A 165      28.161 -25.594  -1.080  1.00 24.76           C  
ATOM   1067  NE2 HIS A 165      28.164 -26.531  -2.025  1.00 21.81           N  
ATOM   1068  N   ARG A 166      29.162 -20.908  -2.675  1.00 21.37           N  
ATOM   1069  CA  ARG A 166      28.708 -20.036  -1.616  1.00 24.04           C  
ATOM   1070  C   ARG A 166      28.251 -20.647  -0.276  1.00 25.62           C  
ATOM   1071  O   ARG A 166      27.753 -19.929   0.575  1.00 26.92           O  
ATOM   1072  CB  ARG A 166      27.567 -19.102  -2.157  1.00 24.21           C  
ATOM   1073  CG  ARG A 166      28.054 -18.245  -3.360  1.00 24.75           C  
ATOM   1074  CD  ARG A 166      27.157 -16.943  -3.502  1.00 26.20           C  
ATOM   1075  NE  ARG A 166      25.774 -17.217  -3.870  1.00 26.20           N  
ATOM   1076  CZ  ARG A 166      24.876 -16.248  -4.146  1.00 31.72           C  
ATOM   1077  NH1 ARG A 166      25.227 -14.922  -4.052  1.00 26.43           N  
ATOM   1078  NH2 ARG A 166      23.632 -16.617  -4.489  1.00 31.35           N  
ATOM   1079  N   ASP A 167      28.342 -21.966  -0.099  1.00 24.26           N  
ATOM   1080  CA  ASP A 167      28.104 -22.493   1.268  1.00 25.13           C  
ATOM   1081  C   ASP A 167      29.074 -23.627   1.579  1.00 24.16           C  
ATOM   1082  O   ASP A 167      28.711 -24.715   2.027  1.00 24.64           O  
ATOM   1083  CB  ASP A 167      26.626 -22.958   1.344  1.00 27.62           C  
ATOM   1084  CG  ASP A 167      26.132 -23.108   2.787  1.00 32.49           C  
ATOM   1085  OD1 ASP A 167      26.805 -22.472   3.670  1.00 29.84           O  
ATOM   1086  OD2 ASP A 167      25.058 -23.794   2.970  1.00 30.59           O  
ATOM   1087  N   ILE A 168      30.364 -23.431   1.286  1.00 23.39           N  
ATOM   1088  CA  ILE A 168      31.342 -24.523   1.544  1.00 24.00           C  
ATOM   1089  C   ILE A 168      31.432 -24.665   3.070  1.00 24.14           C  
ATOM   1090  O   ILE A 168      31.712 -23.695   3.759  1.00 24.74           O  
ATOM   1091  CB  ILE A 168      32.754 -24.129   0.970  1.00 23.31           C  
ATOM   1092  CG1 ILE A 168      32.672 -23.967  -0.565  1.00 24.67           C  
ATOM   1093  CG2 ILE A 168      33.793 -25.160   1.480  1.00 21.61           C  
ATOM   1094  CD1 ILE A 168      33.838 -23.113  -1.130  1.00 26.98           C  
ATOM   1095  N   LYS A 169      31.225 -25.868   3.606  1.00 24.35           N  
ATOM   1096  CA  LYS A 169      31.291 -26.041   5.034  1.00 25.00           C  
ATOM   1097  C   LYS A 169      31.188 -27.550   5.272  1.00 24.75           C  
ATOM   1098  O   LYS A 169      30.830 -28.333   4.340  1.00 23.20           O  
ATOM   1099  CB  LYS A 169      30.128 -25.308   5.743  1.00 23.48           C  
ATOM   1100  CG  LYS A 169      28.751 -25.835   5.359  1.00 26.54           C  
ATOM   1101  CD  LYS A 169      27.788 -25.086   6.242  1.00 31.09           C  
ATOM   1102  CE  LYS A 169      26.404 -25.378   5.956  1.00 39.50           C  
ATOM   1103  NZ  LYS A 169      25.749 -24.786   7.258  1.00 40.65           N  
ATOM   1104  N   ASP A 170      31.536 -27.963   6.492  1.00 24.88           N  
ATOM   1105  CA  ASP A 170      31.576 -29.374   6.747  1.00 25.56           C  
ATOM   1106  C   ASP A 170      30.301 -30.142   6.421  1.00 26.80           C  
ATOM   1107  O   ASP A 170      30.403 -31.215   5.894  1.00 26.25           O  
ATOM   1108  CB  ASP A 170      32.132 -29.727   8.164  1.00 26.29           C  
ATOM   1109  CG  ASP A 170      31.414 -29.020   9.300  1.00 30.62           C  
ATOM   1110  OD1 ASP A 170      30.344 -28.350   9.092  1.00 36.77           O  
ATOM   1111  OD2 ASP A 170      31.958 -29.176  10.439  1.00 36.67           O  
ATOM   1112  N   GLU A 171      29.122 -29.589   6.684  1.00 26.53           N  
ATOM   1113  CA  GLU A 171      27.865 -30.312   6.452  1.00 29.58           C  
ATOM   1114  C   GLU A 171      27.556 -30.413   4.950  1.00 28.48           C  
ATOM   1115  O   GLU A 171      26.697 -31.222   4.576  1.00 28.32           O  
ATOM   1116  CB  GLU A 171      26.675 -29.505   6.917  1.00 29.87           C  
ATOM   1117  CG  GLU A 171      26.500 -29.278   8.322  1.00 41.57           C  
ATOM   1118  CD  GLU A 171      25.349 -28.261   8.453  1.00 51.15           C  
ATOM   1119  OE1 GLU A 171      24.315 -28.478   7.737  1.00 43.90           O  
ATOM   1120  OE2 GLU A 171      25.587 -27.254   9.190  1.00 55.57           O  
ATOM   1121  N   ASN A 172      28.239 -29.639   4.114  1.00 25.88           N  
ATOM   1122  CA  ASN A 172      28.052 -29.766   2.663  1.00 23.17           C  
ATOM   1123  C   ASN A 172      29.193 -30.549   1.981  1.00 24.59           C  
ATOM   1124  O   ASN A 172      29.406 -30.402   0.771  1.00 27.78           O  
ATOM   1125  CB  ASN A 172      27.921 -28.413   2.032  1.00 22.24           C  
ATOM   1126  CG  ASN A 172      26.575 -27.792   2.275  1.00 27.22           C  
ATOM   1127  OD1 ASN A 172      25.613 -28.541   2.465  1.00 26.19           O  
ATOM   1128  ND2 ASN A 172      26.496 -26.443   2.298  1.00 22.07           N  
ATOM   1129  N   ILE A 173      29.845 -31.448   2.701  1.00 25.04           N  
ATOM   1130  CA  ILE A 173      30.869 -32.319   2.197  1.00 22.60           C  
ATOM   1131  C   ILE A 173      30.590 -33.764   2.634  1.00 24.04           C  
ATOM   1132  O   ILE A 173      30.454 -34.026   3.864  1.00 24.29           O  
ATOM   1133  CB  ILE A 173      32.247 -31.904   2.761  1.00 23.90           C  
ATOM   1134  CG1 ILE A 173      32.658 -30.495   2.122  1.00 20.17           C  
ATOM   1135  CG2 ILE A 173      33.336 -32.925   2.372  1.00 21.74           C  
ATOM   1136  CD1 ILE A 173      33.854 -29.794   2.913  1.00 26.07           C  
ATOM   1137  N   LEU A 174      30.499 -34.683   1.664  1.00 22.77           N  
ATOM   1138  CA  LEU A 174      30.244 -36.079   2.033  1.00 25.29           C  
ATOM   1139  C   LEU A 174      31.527 -36.844   1.927  1.00 26.90           C  
ATOM   1140  O   LEU A 174      32.344 -36.552   1.012  1.00 28.03           O  
ATOM   1141  CB  LEU A 174      29.156 -36.684   1.110  1.00 24.84           C  
ATOM   1142  CG  LEU A 174      27.744 -36.104   1.085  1.00 30.57           C  
ATOM   1143  CD1 LEU A 174      26.948 -36.963   0.060  1.00 30.70           C  
ATOM   1144  CD2 LEU A 174      27.233 -36.147   2.542  1.00 30.28           C  
ATOM   1145  N   ILE A 175      31.737 -37.838   2.788  1.00 27.06           N  
ATOM   1146  CA  ILE A 175      32.902 -38.725   2.673  1.00 26.72           C  
ATOM   1147  C   ILE A 175      32.485 -40.111   2.209  1.00 30.44           C  
ATOM   1148  O   ILE A 175      31.644 -40.721   2.872  1.00 27.31           O  
ATOM   1149  CB  ILE A 175      33.624 -38.858   4.040  1.00 27.41           C  
ATOM   1150  CG1 ILE A 175      33.986 -37.511   4.674  1.00 27.02           C  
ATOM   1151  CG2 ILE A 175      34.887 -39.770   3.843  1.00 24.32           C  
ATOM   1152  CD1 ILE A 175      34.280 -37.637   6.256  1.00 25.65           C  
ATOM   1153  N   ASP A 176      33.004 -40.557   1.045  1.00 30.99           N  
ATOM   1154  CA  ASP A 176      32.759 -41.896   0.479  1.00 32.94           C  
ATOM   1155  C   ASP A 176      33.779 -42.677   1.271  1.00 34.86           C  
ATOM   1156  O   ASP A 176      34.983 -42.689   0.931  1.00 37.46           O  
ATOM   1157  CB  ASP A 176      33.079 -41.782  -1.031  1.00 34.09           C  
ATOM   1158  CG  ASP A 176      32.900 -43.118  -1.840  1.00 37.09           C  
ATOM   1159  OD1 ASP A 176      32.970 -44.164  -1.222  1.00 36.07           O  
ATOM   1160  OD2 ASP A 176      32.737 -43.027  -3.106  1.00 36.11           O  
ATOM   1161  N   LEU A 177      33.344 -43.251   2.400  1.00 34.86           N  
ATOM   1162  CA  LEU A 177      34.244 -43.948   3.324  1.00 35.99           C  
ATOM   1163  C   LEU A 177      35.036 -45.094   2.652  1.00 37.79           C  
ATOM   1164  O   LEU A 177      36.217 -45.236   2.931  1.00 41.08           O  
ATOM   1165  CB  LEU A 177      33.540 -44.423   4.607  1.00 34.43           C  
ATOM   1166  CG  LEU A 177      32.754 -43.313   5.363  1.00 35.19           C  
ATOM   1167  CD1 LEU A 177      31.530 -43.961   6.139  1.00 29.99           C  
ATOM   1168  CD2 LEU A 177      33.700 -42.428   6.284  1.00 29.36           C  
ATOM   1169  N   ASN A 178      34.460 -45.846   1.725  1.00 37.88           N  
ATOM   1170  CA  ASN A 178      35.260 -46.969   1.207  1.00 38.39           C  
ATOM   1171  C   ASN A 178      36.454 -46.472   0.407  1.00 37.35           C  
ATOM   1172  O   ASN A 178      37.553 -46.979   0.563  1.00 35.87           O  
ATOM   1173  CB  ASN A 178      34.380 -47.921   0.410  1.00 38.58           C  
ATOM   1174  CG  ASN A 178      33.609 -48.882   1.344  1.00 43.86           C  
ATOM   1175  OD1 ASN A 178      33.938 -48.982   2.531  1.00 45.17           O  
ATOM   1176  ND2 ASN A 178      32.587 -49.543   0.820  1.00 46.79           N  
ATOM   1177  N   ARG A 179      36.227 -45.407  -0.362  1.00 35.16           N  
ATOM   1178  CA  ARG A 179      37.217 -44.917  -1.332  1.00 35.60           C  
ATOM   1179  C   ARG A 179      38.081 -43.731  -0.845  1.00 34.90           C  
ATOM   1180  O   ARG A 179      39.049 -43.365  -1.528  1.00 36.23           O  
ATOM   1181  CB  ARG A 179      36.462 -44.466  -2.539  1.00 35.81           C  
ATOM   1182  CG  ARG A 179      35.624 -45.588  -3.169  1.00 37.98           C  
ATOM   1183  CD  ARG A 179      35.336 -45.197  -4.604  1.00 37.69           C  
ATOM   1184  NE  ARG A 179      34.711 -46.248  -5.410  1.00 44.70           N  
ATOM   1185  CZ  ARG A 179      35.380 -47.267  -5.998  1.00 46.64           C  
ATOM   1186  NH1 ARG A 179      36.700 -47.425  -5.875  1.00 44.32           N  
ATOM   1187  NH2 ARG A 179      34.704 -48.129  -6.741  1.00 49.67           N  
ATOM   1188  N   GLY A 180      37.770 -43.191   0.317  1.00 32.15           N  
ATOM   1189  CA  GLY A 180      38.465 -41.993   0.900  1.00 31.61           C  
ATOM   1190  C   GLY A 180      38.240 -40.702   0.044  1.00 31.12           C  
ATOM   1191  O   GLY A 180      39.125 -39.826   0.003  1.00 32.72           O  
ATOM   1192  N   GLU A 181      37.121 -40.638  -0.684  1.00 28.50           N  
ATOM   1193  CA  GLU A 181      36.882 -39.574  -1.672  1.00 27.41           C  
ATOM   1194  C   GLU A 181      35.851 -38.652  -1.076  1.00 28.88           C  
ATOM   1195  O   GLU A 181      34.804 -39.125  -0.648  1.00 28.97           O  
ATOM   1196  CB  GLU A 181      36.407 -40.136  -3.044  1.00 26.21           C  
ATOM   1197  CG  GLU A 181      37.525 -40.973  -3.662  1.00 27.40           C  
ATOM   1198  CD  GLU A 181      37.135 -41.456  -5.050  1.00 37.04           C  
ATOM   1199  OE1 GLU A 181      35.993 -41.147  -5.493  1.00 32.70           O  
ATOM   1200  OE2 GLU A 181      38.000 -42.127  -5.691  1.00 38.22           O  
ATOM   1201  N   LEU A 182      36.095 -37.338  -1.100  1.00 26.52           N  
ATOM   1202  CA  LEU A 182      35.070 -36.358  -0.645  1.00 26.68           C  
ATOM   1203  C   LEU A 182      34.210 -35.894  -1.798  1.00 27.11           C  
ATOM   1204  O   LEU A 182      34.701 -35.808  -2.944  1.00 28.38           O  
ATOM   1205  CB  LEU A 182      35.829 -35.165  -0.023  1.00 28.70           C  
ATOM   1206  CG  LEU A 182      36.060 -35.278   1.470  1.00 29.04           C  
ATOM   1207  CD1 LEU A 182      36.659 -36.511   2.019  1.00 32.63           C  
ATOM   1208  CD2 LEU A 182      36.963 -34.032   1.841  1.00 29.82           C  
ATOM   1209  N   LYS A 183      32.942 -35.568  -1.535  1.00 27.11           N  
ATOM   1210  CA  LYS A 183      32.107 -34.978  -2.547  1.00 27.27           C  
ATOM   1211  C   LYS A 183      31.472 -33.720  -2.033  1.00 26.19           C  
ATOM   1212  O   LYS A 183      30.860 -33.752  -0.932  1.00 25.94           O  
ATOM   1213  CB  LYS A 183      30.953 -35.971  -2.865  1.00 26.31           C  
ATOM   1214  CG  LYS A 183      31.437 -37.238  -3.506  1.00 34.31           C  
ATOM   1215  CD  LYS A 183      30.232 -38.022  -4.061  1.00 41.92           C  
ATOM   1216  CE  LYS A 183      30.452 -38.590  -5.447  1.00 47.42           C  
ATOM   1217  NZ  LYS A 183      31.745 -39.209  -5.677  1.00 43.81           N  
ATOM   1218  N   LEU A 184      31.473 -32.641  -2.815  1.00 24.47           N  
ATOM   1219  CA  LEU A 184      30.791 -31.398  -2.418  1.00 23.71           C  
ATOM   1220  C   LEU A 184      29.353 -31.560  -2.853  1.00 25.36           C  
ATOM   1221  O   LEU A 184      29.093 -32.017  -4.039  1.00 25.64           O  
ATOM   1222  CB  LEU A 184      31.467 -30.261  -3.210  1.00 25.53           C  
ATOM   1223  CG  LEU A 184      31.120 -28.827  -3.038  1.00 29.08           C  
ATOM   1224  CD1 LEU A 184      31.378 -28.408  -1.527  1.00 30.06           C  
ATOM   1225  CD2 LEU A 184      32.108 -27.986  -3.993  1.00 29.09           C  
ATOM   1226  N   ILE A 185      28.437 -31.205  -1.962  1.00 24.15           N  
ATOM   1227  CA  ILE A 185      27.015 -31.296  -2.237  1.00 26.43           C  
ATOM   1228  C   ILE A 185      26.415 -29.907  -2.046  1.00 27.47           C  
ATOM   1229  O   ILE A 185      27.033 -29.007  -1.496  1.00 27.26           O  
ATOM   1230  CB  ILE A 185      26.301 -32.356  -1.309  1.00 23.47           C  
ATOM   1231  CG1 ILE A 185      26.534 -32.088   0.185  1.00 25.53           C  
ATOM   1232  CG2 ILE A 185      26.841 -33.838  -1.566  1.00 21.78           C  
ATOM   1233  CD1 ILE A 185      25.499 -32.726   1.142  1.00 28.98           C  
ATOM   1234  N   ASP A 186      25.142 -29.768  -2.420  1.00 28.15           N  
ATOM   1235  CA  ASP A 186      24.279 -28.651  -2.026  1.00 27.44           C  
ATOM   1236  C   ASP A 186      24.607 -27.296  -2.669  1.00 27.24           C  
ATOM   1237  O   ASP A 186      25.211 -26.365  -2.037  1.00 29.19           O  
ATOM   1238  CB  ASP A 186      24.140 -28.497  -0.506  1.00 26.16           C  
ATOM   1239  CG  ASP A 186      23.181 -27.366  -0.153  1.00 33.13           C  
ATOM   1240  OD1 ASP A 186      22.357 -26.993  -1.033  1.00 31.21           O  
ATOM   1241  OD2 ASP A 186      23.230 -26.819   0.972  1.00 32.30           O  
ATOM   1242  N   PHE A 187      24.127 -27.124  -3.897  1.00 26.52           N  
ATOM   1243  CA  PHE A 187      24.311 -25.856  -4.560  1.00 26.83           C  
ATOM   1244  C   PHE A 187      23.124 -24.949  -4.362  1.00 28.73           C  
ATOM   1245  O   PHE A 187      22.964 -23.953  -5.115  1.00 28.77           O  
ATOM   1246  CB  PHE A 187      24.623 -26.065  -6.059  1.00 27.24           C  
ATOM   1247  CG  PHE A 187      25.985 -26.704  -6.271  1.00 27.39           C  
ATOM   1248  CD1 PHE A 187      26.148 -28.073  -6.126  1.00 30.55           C  
ATOM   1249  CD2 PHE A 187      27.107 -25.928  -6.594  1.00 23.57           C  
ATOM   1250  CE1 PHE A 187      27.423 -28.648  -6.343  1.00 29.73           C  
ATOM   1251  CE2 PHE A 187      28.387 -26.535  -6.746  1.00 29.19           C  
ATOM   1252  CZ  PHE A 187      28.544 -27.837  -6.575  1.00 25.95           C  
ATOM   1253  N   GLY A 188      22.316 -25.256  -3.342  1.00 27.99           N  
ATOM   1254  CA  GLY A 188      21.163 -24.401  -2.989  1.00 27.35           C  
ATOM   1255  C   GLY A 188      21.381 -22.971  -2.620  1.00 29.84           C  
ATOM   1256  O   GLY A 188      20.427 -22.192  -2.654  1.00 29.10           O  
ATOM   1257  N   SER A 189      22.608 -22.582  -2.229  1.00 29.44           N  
ATOM   1258  CA  SER A 189      22.936 -21.161  -2.010  1.00 30.94           C  
ATOM   1259  C   SER A 189      23.850 -20.567  -3.097  1.00 31.10           C  
ATOM   1260  O   SER A 189      24.330 -19.426  -2.945  1.00 27.58           O  
ATOM   1261  CB  SER A 189      23.682 -20.981  -0.698  1.00 31.60           C  
ATOM   1262  OG  SER A 189      22.919 -21.528   0.354  1.00 32.08           O  
ATOM   1263  N   GLY A 190      24.080 -21.348  -4.152  1.00 29.71           N  
ATOM   1264  CA  GLY A 190      25.133 -21.027  -5.138  1.00 29.90           C  
ATOM   1265  C   GLY A 190      24.722 -19.971  -6.161  1.00 30.42           C  
ATOM   1266  O   GLY A 190      23.576 -19.517  -6.153  1.00 28.93           O  
ATOM   1267  N   ALA A 191      25.608 -19.643  -7.077  1.00 28.81           N  
ATOM   1268  CA  ALA A 191      25.278 -18.685  -8.130  1.00 28.72           C  
ATOM   1269  C   ALA A 191      26.207 -18.948  -9.262  1.00 29.58           C  
ATOM   1270  O   ALA A 191      27.240 -19.644  -9.095  1.00 29.87           O  
ATOM   1271  CB  ALA A 191      25.521 -17.227  -7.627  1.00 26.35           C  
ATOM   1272  N   LEU A 192      25.897 -18.370 -10.444  1.00 27.58           N  
ATOM   1273  CA  LEU A 192      26.881 -18.377 -11.514  1.00 27.73           C  
ATOM   1274  C   LEU A 192      28.063 -17.498 -11.008  1.00 26.68           C  
ATOM   1275  O   LEU A 192      27.859 -16.424 -10.383  1.00 24.84           O  
ATOM   1276  CB  LEU A 192      26.253 -17.695 -12.764  1.00 29.41           C  
ATOM   1277  CG  LEU A 192      24.979 -18.339 -13.190  1.00 31.29           C  
ATOM   1278  CD1 LEU A 192      24.389 -17.613 -14.477  1.00 42.53           C  
ATOM   1279  CD2 LEU A 192      25.389 -19.806 -13.515  1.00 36.02           C  
ATOM   1280  N   LEU A 193      29.283 -17.935 -11.326  1.00 26.06           N  
ATOM   1281  CA  LEU A 193      30.481 -17.224 -10.981  1.00 28.64           C  
ATOM   1282  C   LEU A 193      30.573 -15.973 -11.901  1.00 30.75           C  
ATOM   1283  O   LEU A 193      30.317 -16.068 -13.127  1.00 32.26           O  
ATOM   1284  CB  LEU A 193      31.693 -18.127 -11.250  1.00 26.93           C  
ATOM   1285  CG  LEU A 193      33.088 -17.593 -10.894  1.00 31.95           C  
ATOM   1286  CD1 LEU A 193      33.149 -17.171  -9.377  1.00 27.94           C  
ATOM   1287  CD2 LEU A 193      34.092 -18.660 -11.165  1.00 29.17           C  
ATOM   1288  N   LYS A 194      30.960 -14.840 -11.345  1.00 31.51           N  
ATOM   1289  CA  LYS A 194      31.122 -13.589 -12.098  1.00 30.51           C  
ATOM   1290  C   LYS A 194      32.309 -12.850 -11.473  1.00 31.82           C  
ATOM   1291  O   LYS A 194      32.725 -13.155 -10.315  1.00 34.00           O  
ATOM   1292  CB  LYS A 194      29.819 -12.761 -11.991  1.00 29.31           C  
ATOM   1293  CG  LYS A 194      29.428 -12.233 -10.575  1.00 28.12           C  
ATOM   1294  CD  LYS A 194      28.066 -11.520 -10.579  1.00 28.11           C  
ATOM   1295  CE  LYS A 194      27.834 -10.836  -9.336  1.00 28.85           C  
ATOM   1296  NZ  LYS A 194      26.449 -10.245  -9.205  1.00 34.23           N  
ATOM   1297  N   ASP A 195      32.830 -11.833 -12.164  1.00 30.15           N  
ATOM   1298  CA  ASP A 195      34.024 -11.107 -11.683  1.00 30.55           C  
ATOM   1299  C   ASP A 195      33.692  -9.830 -10.935  1.00 31.52           C  
ATOM   1300  O   ASP A 195      34.594  -9.140 -10.444  1.00 32.37           O  
ATOM   1301  CB  ASP A 195      34.865 -10.799 -12.869  1.00 31.44           C  
ATOM   1302  CG  ASP A 195      35.357 -12.065 -13.554  1.00 38.20           C  
ATOM   1303  OD1 ASP A 195      35.837 -12.886 -12.823  1.00 34.76           O  
ATOM   1304  OD2 ASP A 195      35.283 -12.210 -14.766  1.00 37.96           O  
ATOM   1305  N   THR A 196      32.399  -9.496 -10.853  1.00 31.46           N  
ATOM   1306  CA  THR A 196      31.933  -8.274 -10.191  1.00 33.03           C  
ATOM   1307  C   THR A 196      31.370  -8.670  -8.831  1.00 34.02           C  
ATOM   1308  O   THR A 196      31.389  -9.878  -8.479  1.00 32.68           O  
ATOM   1309  CB  THR A 196      30.905  -7.571 -11.111  1.00 32.79           C  
ATOM   1310  OG1 THR A 196      29.913  -8.531 -11.468  1.00 36.58           O  
ATOM   1311  CG2 THR A 196      31.690  -7.056 -12.423  1.00 34.00           C  
ATOM   1312  N   VAL A 197      30.828  -7.713  -8.082  1.00 33.30           N  
ATOM   1313  CA  VAL A 197      30.490  -7.916  -6.652  1.00 32.66           C  
ATOM   1314  C   VAL A 197      29.153  -8.582  -6.484  1.00 32.93           C  
ATOM   1315  O   VAL A 197      28.205  -8.350  -7.264  1.00 32.01           O  
ATOM   1316  CB  VAL A 197      30.539  -6.553  -5.886  1.00 35.40           C  
ATOM   1317  CG1 VAL A 197      29.268  -5.692  -6.203  1.00 39.18           C  
ATOM   1318  CG2 VAL A 197      30.675  -6.764  -4.384  1.00 36.94           C  
ATOM   1319  N   TYR A 198      29.057  -9.484  -5.517  1.00 29.58           N  
ATOM   1320  CA  TYR A 198      27.760 -10.008  -5.096  1.00 31.16           C  
ATOM   1321  C   TYR A 198      27.229  -9.169  -3.924  1.00 33.62           C  
ATOM   1322  O   TYR A 198      28.003  -8.714  -3.096  1.00 33.68           O  
ATOM   1323  CB  TYR A 198      27.948 -11.443  -4.599  1.00 28.29           C  
ATOM   1324  CG  TYR A 198      28.368 -12.369  -5.700  1.00 29.52           C  
ATOM   1325  CD1 TYR A 198      29.687 -12.502  -6.048  1.00 24.11           C  
ATOM   1326  CD2 TYR A 198      27.392 -13.216  -6.319  1.00 23.96           C  
ATOM   1327  CE1 TYR A 198      30.086 -13.392  -7.081  1.00 24.20           C  
ATOM   1328  CE2 TYR A 198      27.753 -14.132  -7.358  1.00 28.83           C  
ATOM   1329  CZ  TYR A 198      29.116 -14.266  -7.677  1.00 25.51           C  
ATOM   1330  OH  TYR A 198      29.474 -15.086  -8.707  1.00 25.93           O  
ATOM   1331  N   THR A 199      25.911  -8.940  -3.851  1.00 35.11           N  
ATOM   1332  CA  THR A 199      25.333  -8.118  -2.811  1.00 36.95           C  
ATOM   1333  C   THR A 199      24.195  -8.924  -2.193  1.00 37.80           C  
ATOM   1334  O   THR A 199      23.507  -8.468  -1.321  1.00 37.51           O  
ATOM   1335  CB  THR A 199      24.798  -6.829  -3.369  1.00 39.09           C  
ATOM   1336  OG1 THR A 199      23.813  -7.148  -4.336  1.00 39.61           O  
ATOM   1337  CG2 THR A 199      25.899  -5.980  -4.096  1.00 39.03           C  
ATOM   1338  N   ASP A 200      24.047 -10.180  -2.587  1.00 37.56           N  
ATOM   1339  CA  ASP A 200      23.104 -11.037  -1.952  1.00 39.28           C  
ATOM   1340  C   ASP A 200      23.882 -12.195  -1.367  1.00 37.35           C  
ATOM   1341  O   ASP A 200      24.914 -12.538  -1.938  1.00 36.86           O  
ATOM   1342  CB  ASP A 200      22.126 -11.617  -3.029  1.00 41.98           C  
ATOM   1343  CG  ASP A 200      22.827 -12.583  -4.081  1.00 46.93           C  
ATOM   1344  OD1 ASP A 200      23.713 -12.069  -4.860  1.00 52.31           O  
ATOM   1345  OD2 ASP A 200      22.452 -13.807  -4.160  1.00 46.98           O  
ATOM   1346  N   PHE A 201      23.396 -12.796  -0.287  1.00 34.67           N  
ATOM   1347  CA  PHE A 201      24.052 -13.986   0.235  1.00 35.70           C  
ATOM   1348  C   PHE A 201      23.139 -14.733   1.142  1.00 36.10           C  
ATOM   1349  O   PHE A 201      22.561 -14.135   1.999  1.00 38.23           O  
ATOM   1350  CB  PHE A 201      25.265 -13.577   1.065  1.00 32.84           C  
ATOM   1351  CG  PHE A 201      25.887 -14.712   1.800  1.00 34.82           C  
ATOM   1352  CD1 PHE A 201      26.721 -15.625   1.129  1.00 31.36           C  
ATOM   1353  CD2 PHE A 201      25.757 -14.822   3.177  1.00 35.09           C  
ATOM   1354  CE1 PHE A 201      27.380 -16.703   1.824  1.00 34.67           C  
ATOM   1355  CE2 PHE A 201      26.416 -15.856   3.887  1.00 37.38           C  
ATOM   1356  CZ  PHE A 201      27.211 -16.817   3.185  1.00 36.58           C  
ATOM   1357  N   ASP A 202      23.002 -16.038   1.016  1.00 36.68           N  
ATOM   1358  C   ASP A 202      22.796 -18.068   2.269  1.00 35.25           C  
ATOM   1359  O   ASP A 202      22.140 -19.060   2.475  1.00 35.36           O  
ATOM   1360  CA AASP A 202      22.121 -16.756   1.939  0.50 35.94           C  
ATOM   1361  CB AASP A 202      20.727 -17.025   1.307  0.50 37.33           C  
ATOM   1362  CG AASP A 202      19.696 -17.559   2.324  0.50 38.82           C  
ATOM   1363  OD1AASP A 202      19.448 -16.906   3.364  0.50 38.99           O  
ATOM   1364  OD2AASP A 202      19.164 -18.676   2.097  0.50 42.59           O  
ATOM   1365  CA BASP A 202      22.116 -16.771   1.882  0.50 36.07           C  
ATOM   1366  CB BASP A 202      20.800 -17.050   1.124  0.50 37.52           C  
ATOM   1367  CG BASP A 202      19.898 -15.819   1.069  0.50 38.99           C  
ATOM   1368  OD1BASP A 202      19.351 -15.478   2.121  0.50 43.89           O  
ATOM   1369  OD2BASP A 202      19.767 -15.173  -0.001  0.50 44.15           O  
ATOM   1370  N   GLY A 203      24.130 -18.095   2.302  1.00 33.90           N  
ATOM   1371  CA  GLY A 203      24.750 -19.338   2.778  1.00 30.96           C  
ATOM   1372  C   GLY A 203      24.967 -19.210   4.274  1.00 32.56           C  
ATOM   1373  O   GLY A 203      24.206 -18.530   4.961  1.00 33.14           O  
ATOM   1374  N   THR A 204      26.040 -19.780   4.814  1.00 31.59           N  
ATOM   1375  CA  THR A 204      26.125 -19.856   6.284  1.00 30.28           C  
ATOM   1376  C   THR A 204      26.879 -18.618   6.884  1.00 30.69           C  
ATOM   1377  O   THR A 204      28.096 -18.348   6.545  1.00 30.45           O  
ATOM   1378  CB  THR A 204      26.730 -21.184   6.741  1.00 26.72           C  
ATOM   1379  OG1 THR A 204      25.985 -22.323   6.250  1.00 30.91           O  
ATOM   1380  CG2 THR A 204      26.837 -21.218   8.320  1.00 28.02           C  
ATOM   1381  N   ARG A 205      26.219 -17.897   7.831  1.00 31.24           N  
ATOM   1382  CA  ARG A 205      26.831 -16.607   8.307  1.00 33.11           C  
ATOM   1383  C   ARG A 205      28.240 -16.817   8.936  1.00 30.52           C  
ATOM   1384  O   ARG A 205      29.136 -16.025   8.649  1.00 32.83           O  
ATOM   1385  CB  ARG A 205      25.970 -15.850   9.329  1.00 31.37           C  
ATOM   1386  CG  ARG A 205      26.332 -14.375   9.434  1.00 36.04           C  
ATOM   1387  CD  ARG A 205      25.244 -13.537  10.268  1.00 34.02           C  
ATOM   1388  NE  ARG A 205      25.611 -12.104  10.443  1.00 34.75           N  
ATOM   1389  CZ  ARG A 205      25.400 -11.100   9.581  1.00 39.40           C  
ATOM   1390  NH1 ARG A 205      24.887 -11.295   8.381  1.00 40.09           N  
ATOM   1391  NH2 ARG A 205      25.782  -9.854   9.875  1.00 38.02           N  
ATOM   1392  N   VAL A 206      28.448 -17.861   9.749  1.00 31.45           N  
ATOM   1393  CA  VAL A 206      29.735 -17.950  10.478  1.00 28.92           C  
ATOM   1394  C   VAL A 206      30.868 -18.413   9.522  1.00 30.79           C  
ATOM   1395  O   VAL A 206      32.019 -18.524   9.964  1.00 30.21           O  
ATOM   1396  CB  VAL A 206      29.608 -18.876  11.681  1.00 32.09           C  
ATOM   1397  CG1 VAL A 206      28.688 -18.253  12.759  1.00 28.59           C  
ATOM   1398  CG2 VAL A 206      29.045 -20.352  11.291  1.00 26.34           C  
ATOM   1399  N   TYR A 207      30.547 -18.720   8.239  1.00 30.09           N  
ATOM   1400  CA  TYR A 207      31.559 -18.987   7.187  1.00 27.30           C  
ATOM   1401  C   TYR A 207      31.734 -17.810   6.259  1.00 28.28           C  
ATOM   1402  O   TYR A 207      32.557 -17.882   5.289  1.00 24.77           O  
ATOM   1403  CB  TYR A 207      31.195 -20.193   6.351  1.00 28.61           C  
ATOM   1404  CG  TYR A 207      31.479 -21.553   7.002  1.00 30.11           C  
ATOM   1405  CD1 TYR A 207      30.648 -22.037   8.033  1.00 27.82           C  
ATOM   1406  CD2 TYR A 207      32.648 -22.310   6.619  1.00 25.21           C  
ATOM   1407  CE1 TYR A 207      30.881 -23.343   8.689  1.00 27.26           C  
ATOM   1408  CE2 TYR A 207      32.897 -23.552   7.221  1.00 25.37           C  
ATOM   1409  CZ  TYR A 207      32.024 -24.045   8.262  1.00 27.91           C  
ATOM   1410  OH  TYR A 207      32.337 -25.334   8.713  1.00 34.67           O  
ATOM   1411  N   SER A 208      30.890 -16.767   6.437  1.00 27.04           N  
ATOM   1412  CA  SER A 208      30.923 -15.616   5.513  1.00 27.04           C  
ATOM   1413  C   SER A 208      31.963 -14.549   5.996  1.00 27.63           C  
ATOM   1414  O   SER A 208      32.288 -14.481   7.140  1.00 26.43           O  
ATOM   1415  CB  SER A 208      29.526 -14.986   5.455  1.00 27.97           C  
ATOM   1416  OG  SER A 208      29.362 -14.173   6.547  1.00 29.49           O  
ATOM   1417  N   PRO A 209      32.551 -13.800   5.057  1.00 26.11           N  
ATOM   1418  CA  PRO A 209      33.711 -13.052   5.309  1.00 27.80           C  
ATOM   1419  C   PRO A 209      33.336 -11.674   5.855  1.00 28.61           C  
ATOM   1420  O   PRO A 209      32.141 -11.227   5.783  1.00 29.03           O  
ATOM   1421  CB  PRO A 209      34.340 -12.932   3.895  1.00 25.59           C  
ATOM   1422  CG  PRO A 209      33.131 -12.807   2.982  1.00 27.07           C  
ATOM   1423  CD  PRO A 209      32.144 -13.792   3.629  1.00 27.19           C  
ATOM   1424  N   PRO A 210      34.335 -10.992   6.326  1.00 30.48           N  
ATOM   1425  CA  PRO A 210      34.051  -9.750   7.039  1.00 29.56           C  
ATOM   1426  C   PRO A 210      33.456  -8.688   6.128  1.00 31.24           C  
ATOM   1427  O   PRO A 210      32.627  -7.895   6.604  1.00 30.70           O  
ATOM   1428  CB  PRO A 210      35.415  -9.332   7.617  1.00 32.27           C  
ATOM   1429  CG  PRO A 210      36.459 -10.197   6.982  1.00 31.07           C  
ATOM   1430  CD  PRO A 210      35.777 -11.395   6.365  1.00 28.84           C  
ATOM   1431  N   GLU A 211      33.853  -8.672   4.857  1.00 30.19           N  
ATOM   1432  CA  GLU A 211      33.276  -7.710   3.936  1.00 31.88           C  
ATOM   1433  C   GLU A 211      31.780  -7.991   3.736  1.00 30.44           C  
ATOM   1434  O   GLU A 211      31.068  -7.060   3.522  1.00 34.12           O  
ATOM   1435  CB  GLU A 211      33.964  -7.628   2.602  1.00 29.78           C  
ATOM   1436  CG  GLU A 211      33.949  -8.980   1.755  1.00 31.45           C  
ATOM   1437  CD  GLU A 211      35.087  -9.994   2.137  1.00 31.09           C  
ATOM   1438  OE1 GLU A 211      35.684  -9.853   3.249  1.00 28.41           O  
ATOM   1439  OE2 GLU A 211      35.387 -10.878   1.268  1.00 28.21           O  
ATOM   1440  N   TRP A 212      31.313  -9.216   3.832  1.00 29.95           N  
ATOM   1441  CA  TRP A 212      29.882  -9.454   3.806  1.00 31.71           C  
ATOM   1442  C   TRP A 212      29.246  -8.882   5.099  1.00 34.05           C  
ATOM   1443  O   TRP A 212      28.192  -8.159   5.050  1.00 34.57           O  
ATOM   1444  CB  TRP A 212      29.514 -10.936   3.689  1.00 32.41           C  
ATOM   1445  CG  TRP A 212      28.022 -11.127   3.924  1.00 29.88           C  
ATOM   1446  CD1 TRP A 212      27.441 -11.746   5.009  1.00 36.25           C  
ATOM   1447  CD2 TRP A 212      26.916 -10.681   3.076  1.00 32.50           C  
ATOM   1448  NE1 TRP A 212      26.051 -11.700   4.887  1.00 35.66           N  
ATOM   1449  CE2 TRP A 212      25.720 -11.025   3.739  1.00 34.86           C  
ATOM   1450  CE3 TRP A 212      26.835 -10.007   1.830  1.00 27.19           C  
ATOM   1451  CZ2 TRP A 212      24.459 -10.738   3.208  1.00 34.53           C  
ATOM   1452  CZ3 TRP A 212      25.535  -9.714   1.301  1.00 35.80           C  
ATOM   1453  CH2 TRP A 212      24.398 -10.114   1.982  1.00 32.98           C  
ATOM   1454  N   ILE A 213      29.848  -9.198   6.248  1.00 32.51           N  
ATOM   1455  CA  ILE A 213      29.247  -8.773   7.513  1.00 34.99           C  
ATOM   1456  C   ILE A 213      29.180  -7.250   7.569  1.00 36.57           C  
ATOM   1457  O   ILE A 213      28.154  -6.715   7.940  1.00 36.30           O  
ATOM   1458  CB  ILE A 213      30.053  -9.285   8.724  1.00 34.48           C  
ATOM   1459  CG1 ILE A 213      30.251 -10.790   8.620  1.00 33.77           C  
ATOM   1460  CG2 ILE A 213      29.498  -8.752  10.089  1.00 32.73           C  
ATOM   1461  CD1 ILE A 213      29.017 -11.620   8.878  1.00 34.29           C  
ATOM   1462  N   ARG A 214      30.265  -6.578   7.211  1.00 37.50           N  
ATOM   1463  CA  ARG A 214      30.312  -5.126   7.351  1.00 39.61           C  
ATOM   1464  C   ARG A 214      29.536  -4.398   6.242  1.00 40.71           C  
ATOM   1465  O   ARG A 214      28.830  -3.490   6.560  1.00 42.68           O  
ATOM   1466  CB  ARG A 214      31.736  -4.642   7.254  1.00 41.30           C  
ATOM   1467  CG  ARG A 214      32.555  -5.012   8.462  1.00 48.46           C  
ATOM   1468  CD  ARG A 214      34.013  -4.556   8.294  1.00 58.35           C  
ATOM   1469  NE  ARG A 214      34.213  -3.255   8.916  1.00 68.10           N  
ATOM   1470  CZ  ARG A 214      35.214  -2.436   8.603  1.00 75.02           C  
ATOM   1471  NH1 ARG A 214      36.100  -2.793   7.661  1.00 77.35           N  
ATOM   1472  NH2 ARG A 214      35.328  -1.245   9.206  1.00 75.61           N  
ATOM   1473  N   TYR A 215      29.660  -4.788   4.962  1.00 39.37           N  
ATOM   1474  CA  TYR A 215      29.210  -3.997   3.803  1.00 38.81           C  
ATOM   1475  C   TYR A 215      28.181  -4.686   2.929  1.00 38.22           C  
ATOM   1476  O   TYR A 215      27.716  -4.124   1.913  1.00 37.59           O  
ATOM   1477  CB  TYR A 215      30.379  -3.728   2.939  1.00 40.00           C  
ATOM   1478  CG  TYR A 215      31.502  -3.108   3.699  1.00 44.33           C  
ATOM   1479  CD1 TYR A 215      31.334  -1.871   4.338  1.00 47.59           C  
ATOM   1480  CD2 TYR A 215      32.770  -3.714   3.744  1.00 45.27           C  
ATOM   1481  CE1 TYR A 215      32.396  -1.264   5.033  1.00 49.39           C  
ATOM   1482  CE2 TYR A 215      33.840  -3.128   4.467  1.00 47.34           C  
ATOM   1483  CZ  TYR A 215      33.634  -1.910   5.094  1.00 49.06           C  
ATOM   1484  OH  TYR A 215      34.688  -1.328   5.780  1.00 52.33           O  
ATOM   1485  N   HIS A 216      27.851  -5.911   3.282  1.00 35.56           N  
ATOM   1486  CA  HIS A 216      27.023  -6.655   2.417  1.00 37.76           C  
ATOM   1487  C   HIS A 216      27.516  -6.731   0.952  1.00 36.07           C  
ATOM   1488  O   HIS A 216      26.731  -6.604  -0.009  1.00 36.66           O  
ATOM   1489  CB  HIS A 216      25.596  -6.078   2.576  1.00 39.21           C  
ATOM   1490  CG  HIS A 216      24.916  -6.643   3.768  1.00 48.72           C  
ATOM   1491  ND1 HIS A 216      23.568  -6.925   3.799  1.00 55.53           N  
ATOM   1492  CD2 HIS A 216      25.431  -7.090   4.947  1.00 53.76           C  
ATOM   1493  CE1 HIS A 216      23.282  -7.497   4.961  1.00 59.76           C  
ATOM   1494  NE2 HIS A 216      24.397  -7.621   5.668  1.00 57.84           N  
ATOM   1495  N   ARG A 217      28.834  -6.878   0.741  1.00 34.36           N  
ATOM   1496  CA  ARG A 217      29.344  -7.018  -0.601  1.00 34.09           C  
ATOM   1497  C   ARG A 217      30.502  -7.964  -0.489  1.00 33.19           C  
ATOM   1498  O   ARG A 217      31.273  -7.884   0.477  1.00 29.91           O  
ATOM   1499  CB  ARG A 217      29.942  -5.669  -1.028  1.00 32.32           C  
ATOM   1500  CG  ARG A 217      28.829  -4.608  -1.164  1.00 40.11           C  
ATOM   1501  CD  ARG A 217      29.436  -3.143  -1.156  1.00 42.87           C  
ATOM   1502  NE  ARG A 217      30.375  -3.008  -2.275  1.00 50.59           N  
ATOM   1503  CZ  ARG A 217      30.022  -2.741  -3.537  1.00 55.47           C  
ATOM   1504  NH1 ARG A 217      28.713  -2.568  -3.884  1.00 51.41           N  
ATOM   1505  NH2 ARG A 217      31.004  -2.688  -4.459  1.00 55.34           N  
ATOM   1506  N   TYR A 218      30.698  -8.799  -1.497  1.00 30.45           N  
ATOM   1507  CA  TYR A 218      31.943  -9.641  -1.534  1.00 29.48           C  
ATOM   1508  C   TYR A 218      32.187 -10.028  -3.021  1.00 28.03           C  
ATOM   1509  O   TYR A 218      31.292  -9.893  -3.867  1.00 29.39           O  
ATOM   1510  CB  TYR A 218      31.775 -10.884  -0.662  1.00 28.41           C  
ATOM   1511  CG  TYR A 218      30.590 -11.695  -1.054  1.00 30.49           C  
ATOM   1512  CD1 TYR A 218      29.300 -11.346  -0.577  1.00 30.51           C  
ATOM   1513  CD2 TYR A 218      30.716 -12.829  -1.920  1.00 27.99           C  
ATOM   1514  CE1 TYR A 218      28.198 -12.095  -0.853  1.00 31.20           C  
ATOM   1515  CE2 TYR A 218      29.561 -13.564  -2.285  1.00 26.32           C  
ATOM   1516  CZ  TYR A 218      28.313 -13.179  -1.798  1.00 32.60           C  
ATOM   1517  OH  TYR A 218      27.177 -13.952  -2.103  1.00 31.16           O  
ATOM   1518  N   HIS A 219      33.397 -10.473  -3.330  1.00 27.40           N  
ATOM   1519  CA  HIS A 219      33.691 -11.062  -4.616  1.00 27.69           C  
ATOM   1520  C   HIS A 219      33.746 -12.582  -4.389  1.00 27.95           C  
ATOM   1521  O   HIS A 219      34.016 -13.057  -3.281  1.00 25.79           O  
ATOM   1522  CB  HIS A 219      35.005 -10.531  -5.138  1.00 28.43           C  
ATOM   1523  CG  HIS A 219      34.861  -9.139  -5.726  1.00 30.38           C  
ATOM   1524  ND1 HIS A 219      34.864  -8.012  -4.943  1.00 31.84           N  
ATOM   1525  CD2 HIS A 219      34.616  -8.722  -6.988  1.00 31.00           C  
ATOM   1526  CE1 HIS A 219      34.645  -6.941  -5.699  1.00 39.00           C  
ATOM   1527  NE2 HIS A 219      34.485  -7.342  -6.947  1.00 35.03           N  
ATOM   1528  N   GLY A 220      33.521 -13.302  -5.449  1.00 26.43           N  
ATOM   1529  CA  GLY A 220      33.224 -14.768  -5.380  1.00 26.49           C  
ATOM   1530  C   GLY A 220      34.412 -15.542  -4.835  1.00 24.92           C  
ATOM   1531  O   GLY A 220      34.304 -16.212  -3.829  1.00 23.46           O  
ATOM   1532  N   ARG A 221      35.544 -15.403  -5.510  1.00 23.30           N  
ATOM   1533  CA  ARG A 221      36.722 -16.256  -5.201  1.00 28.19           C  
ATOM   1534  C   ARG A 221      37.255 -15.938  -3.822  1.00 27.80           C  
ATOM   1535  O   ARG A 221      37.497 -16.840  -3.084  1.00 24.48           O  
ATOM   1536  CB  ARG A 221      37.750 -15.999  -6.264  1.00 26.84           C  
ATOM   1537  CG  ARG A 221      37.211 -16.432  -7.742  1.00 33.60           C  
ATOM   1538  CD  ARG A 221      38.117 -15.783  -8.962  1.00 34.93           C  
ATOM   1539  NE  ARG A 221      37.632 -16.061 -10.326  1.00 39.54           N  
ATOM   1540  CZ  ARG A 221      36.644 -15.380 -10.922  1.00 46.20           C  
ATOM   1541  NH1 ARG A 221      36.014 -14.446 -10.213  1.00 47.27           N  
ATOM   1542  NH2 ARG A 221      36.334 -15.593 -12.226  1.00 36.95           N  
ATOM   1543  N   SER A 222      37.481 -14.648  -3.455  1.00 24.39           N  
ATOM   1544  CA  SER A 222      38.019 -14.407  -2.145  1.00 24.93           C  
ATOM   1545  C   SER A 222      37.039 -14.706  -1.022  1.00 23.57           C  
ATOM   1546  O   SER A 222      37.431 -15.047   0.103  1.00 23.11           O  
ATOM   1547  CB  SER A 222      38.516 -12.922  -2.071  1.00 29.88           C  
ATOM   1548  OG  SER A 222      37.434 -12.092  -2.464  1.00 26.74           O  
ATOM   1549  N   ALA A 223      35.730 -14.641  -1.245  1.00 23.74           N  
ATOM   1550  CA  ALA A 223      34.796 -15.082  -0.201  1.00 23.31           C  
ATOM   1551  C   ALA A 223      34.924 -16.639  -0.083  1.00 21.83           C  
ATOM   1552  O   ALA A 223      34.846 -17.156   1.047  1.00 24.55           O  
ATOM   1553  CB  ALA A 223      33.374 -14.779  -0.578  1.00 23.72           C  
ATOM   1554  N   ALA A 224      35.097 -17.344  -1.222  1.00 23.56           N  
ATOM   1555  CA  ALA A 224      35.254 -18.838  -1.262  1.00 21.36           C  
ATOM   1556  C   ALA A 224      36.506 -19.152  -0.373  1.00 22.00           C  
ATOM   1557  O   ALA A 224      36.468 -20.019   0.438  1.00 21.52           O  
ATOM   1558  CB  ALA A 224      35.456 -19.325  -2.653  1.00 21.37           C  
ATOM   1559  N   VAL A 225      37.569 -18.414  -0.553  1.00 20.82           N  
ATOM   1560  CA  VAL A 225      38.823 -18.715   0.111  1.00 19.04           C  
ATOM   1561  C   VAL A 225      38.642 -18.446   1.603  1.00 20.90           C  
ATOM   1562  O   VAL A 225      39.084 -19.220   2.373  1.00 20.75           O  
ATOM   1563  CB  VAL A 225      40.031 -17.857  -0.502  1.00 19.35           C  
ATOM   1564  CG1 VAL A 225      41.225 -17.949   0.490  1.00 20.11           C  
ATOM   1565  CG2 VAL A 225      40.398 -18.399  -1.972  1.00 19.52           C  
ATOM   1566  N   TRP A 226      37.927 -17.375   2.052  1.00 21.33           N  
ATOM   1567  CA  TRP A 226      37.634 -17.201   3.493  1.00 21.45           C  
ATOM   1568  C   TRP A 226      36.945 -18.430   4.009  1.00 21.39           C  
ATOM   1569  O   TRP A 226      37.236 -18.919   5.118  1.00 22.43           O  
ATOM   1570  CB  TRP A 226      36.662 -15.969   3.720  1.00 22.84           C  
ATOM   1571  CG  TRP A 226      36.343 -15.776   5.137  1.00 22.26           C  
ATOM   1572  CD1 TRP A 226      35.298 -16.341   5.845  1.00 27.26           C  
ATOM   1573  CD2 TRP A 226      37.032 -14.940   6.005  1.00 25.55           C  
ATOM   1574  NE1 TRP A 226      35.324 -15.911   7.150  1.00 28.12           N  
ATOM   1575  CE2 TRP A 226      36.373 -15.007   7.262  1.00 26.00           C  
ATOM   1576  CE3 TRP A 226      38.133 -14.076   5.849  1.00 23.21           C  
ATOM   1577  CZ2 TRP A 226      36.809 -14.310   8.365  1.00 26.62           C  
ATOM   1578  CZ3 TRP A 226      38.558 -13.336   7.018  1.00 26.74           C  
ATOM   1579  CH2 TRP A 226      37.916 -13.524   8.224  1.00 27.34           C  
ATOM   1580  N   SER A 227      35.905 -18.879   3.317  1.00 19.60           N  
ATOM   1581  CA  SER A 227      35.212 -20.031   3.865  1.00 19.39           C  
ATOM   1582  C   SER A 227      36.112 -21.238   3.927  1.00 20.14           C  
ATOM   1583  O   SER A 227      35.971 -22.083   4.864  1.00 21.35           O  
ATOM   1584  CB  SER A 227      33.922 -20.291   3.052  1.00 21.24           C  
ATOM   1585  OG  SER A 227      34.256 -20.809   1.744  1.00 23.90           O  
ATOM   1586  N   LEU A 228      37.012 -21.391   2.956  1.00 21.45           N  
ATOM   1587  CA  LEU A 228      37.995 -22.574   2.966  1.00 21.75           C  
ATOM   1588  C   LEU A 228      38.869 -22.466   4.234  1.00 21.27           C  
ATOM   1589  O   LEU A 228      39.250 -23.479   4.856  1.00 21.01           O  
ATOM   1590  CB  LEU A 228      38.918 -22.558   1.729  1.00 20.39           C  
ATOM   1591  CG  LEU A 228      37.963 -23.079   0.528  1.00 20.32           C  
ATOM   1592  CD1 LEU A 228      38.670 -22.765  -0.840  1.00 25.25           C  
ATOM   1593  CD2 LEU A 228      37.563 -24.573   0.656  1.00 21.62           C  
ATOM   1594  N   GLY A 229      39.219 -21.249   4.606  1.00 19.21           N  
ATOM   1595  CA  GLY A 229      40.037 -21.022   5.880  1.00 19.93           C  
ATOM   1596  C   GLY A 229      39.214 -21.401   7.131  1.00 21.66           C  
ATOM   1597  O   GLY A 229      39.744 -22.009   8.075  1.00 20.79           O  
ATOM   1598  N   ILE A 230      37.885 -21.094   7.167  1.00 20.05           N  
ATOM   1599  CA  ILE A 230      37.086 -21.456   8.318  1.00 19.41           C  
ATOM   1600  C   ILE A 230      37.010 -23.013   8.292  1.00 20.85           C  
ATOM   1601  O   ILE A 230      37.138 -23.651   9.349  1.00 20.61           O  
ATOM   1602  CB  ILE A 230      35.594 -20.933   8.104  1.00 18.52           C  
ATOM   1603  CG1 ILE A 230      35.611 -19.370   8.032  1.00 18.50           C  
ATOM   1604  CG2 ILE A 230      34.667 -21.400   9.277  1.00 19.60           C  
ATOM   1605  CD1 ILE A 230      36.214 -18.668   9.354  1.00 21.01           C  
ATOM   1606  N   LEU A 231      36.857 -23.592   7.091  1.00 21.63           N  
ATOM   1607  CA  LEU A 231      36.756 -25.088   7.003  1.00 20.40           C  
ATOM   1608  C   LEU A 231      38.042 -25.740   7.459  1.00 22.51           C  
ATOM   1609  O   LEU A 231      37.999 -26.778   8.122  1.00 22.01           O  
ATOM   1610  CB  LEU A 231      36.544 -25.439   5.541  1.00 19.97           C  
ATOM   1611  CG  LEU A 231      36.442 -26.962   5.307  1.00 21.52           C  
ATOM   1612  CD1 LEU A 231      35.311 -27.621   6.089  1.00 26.40           C  
ATOM   1613  CD2 LEU A 231      36.396 -27.250   3.827  1.00 20.28           C  
ATOM   1614  N   LEU A 232      39.221 -25.190   7.080  1.00 20.70           N  
ATOM   1615  CA  LEU A 232      40.438 -25.934   7.419  1.00 21.20           C  
ATOM   1616  C   LEU A 232      40.573 -25.751   8.929  1.00 23.42           C  
ATOM   1617  O   LEU A 232      40.978 -26.693   9.581  1.00 22.27           O  
ATOM   1618  CB  LEU A 232      41.673 -25.305   6.758  1.00 21.92           C  
ATOM   1619  CG  LEU A 232      43.083 -25.836   7.113  1.00 18.92           C  
ATOM   1620  CD1 LEU A 232      43.005 -27.503   6.921  1.00 19.32           C  
ATOM   1621  CD2 LEU A 232      44.109 -25.142   6.096  1.00 21.78           C  
ATOM   1622  N   TYR A 233      40.329 -24.543   9.513  1.00 20.30           N  
ATOM   1623  CA  TYR A 233      40.329 -24.441  10.993  1.00 19.08           C  
ATOM   1624  C   TYR A 233      39.468 -25.494  11.623  1.00 22.70           C  
ATOM   1625  O   TYR A 233      39.839 -26.166  12.591  1.00 24.07           O  
ATOM   1626  CB  TYR A 233      39.948 -22.980  11.477  1.00 20.97           C  
ATOM   1627  CG  TYR A 233      40.083 -22.732  13.009  1.00 20.95           C  
ATOM   1628  CD1 TYR A 233      39.102 -23.243  13.922  1.00 25.13           C  
ATOM   1629  CD2 TYR A 233      41.240 -22.070  13.534  1.00 23.74           C  
ATOM   1630  CE1 TYR A 233      39.253 -23.038  15.297  1.00 28.17           C  
ATOM   1631  CE2 TYR A 233      41.347 -21.837  14.948  1.00 24.96           C  
ATOM   1632  CZ  TYR A 233      40.397 -22.351  15.765  1.00 25.18           C  
ATOM   1633  OH  TYR A 233      40.457 -22.213  17.152  1.00 29.28           O  
ATOM   1634  N   ASP A 234      38.262 -25.623  11.113  1.00 23.89           N  
ATOM   1635  CA  ASP A 234      37.324 -26.561  11.701  1.00 25.49           C  
ATOM   1636  C   ASP A 234      37.857 -27.954  11.662  1.00 25.42           C  
ATOM   1637  O   ASP A 234      37.714 -28.684  12.676  1.00 25.35           O  
ATOM   1638  CB  ASP A 234      35.998 -26.401  10.917  1.00 22.26           C  
ATOM   1639  CG  ASP A 234      34.890 -27.359  11.365  1.00 30.82           C  
ATOM   1640  OD1 ASP A 234      34.570 -27.443  12.583  1.00 26.64           O  
ATOM   1641  OD2 ASP A 234      34.309 -27.973  10.428  1.00 31.57           O  
ATOM   1642  N   MET A 235      38.582 -28.345  10.586  1.00 23.97           N  
ATOM   1643  CA  MET A 235      39.055 -29.676  10.528  1.00 25.18           C  
ATOM   1644  C   MET A 235      40.161 -29.896  11.563  1.00 25.17           C  
ATOM   1645  O   MET A 235      40.200 -30.960  12.200  1.00 26.91           O  
ATOM   1646  CB  MET A 235      39.667 -30.007   9.120  1.00 25.74           C  
ATOM   1647  CG  MET A 235      38.508 -30.142   7.990  1.00 27.57           C  
ATOM   1648  SD  MET A 235      39.409 -30.564   6.466  1.00 32.94           S  
ATOM   1649  CE  MET A 235      38.363 -30.178   5.059  1.00 29.18           C  
ATOM   1650  N   VAL A 236      41.101 -28.953  11.703  1.00 23.33           N  
ATOM   1651  CA  VAL A 236      42.305 -29.236  12.520  1.00 22.59           C  
ATOM   1652  C   VAL A 236      42.007 -28.897  14.008  1.00 24.86           C  
ATOM   1653  O   VAL A 236      42.771 -29.249  14.900  1.00 25.84           O  
ATOM   1654  CB  VAL A 236      43.581 -28.542  11.957  1.00 25.10           C  
ATOM   1655  CG1 VAL A 236      43.953 -29.148  10.544  1.00 21.03           C  
ATOM   1656  CG2 VAL A 236      43.487 -26.922  11.943  1.00 22.76           C  
ATOM   1657  N   CYS A 237      40.978 -28.065  14.283  1.00 23.10           N  
ATOM   1658  CA  CYS A 237      40.692 -27.708  15.666  1.00 25.18           C  
ATOM   1659  C   CYS A 237      39.395 -28.368  16.162  1.00 28.23           C  
ATOM   1660  O   CYS A 237      39.173 -28.399  17.393  1.00 28.79           O  
ATOM   1661  CB  CYS A 237      40.554 -26.195  15.834  1.00 23.04           C  
ATOM   1662  SG  CYS A 237      42.100 -25.365  15.688  1.00 31.24           S  
ATOM   1663  N   GLY A 238      38.567 -28.868  15.250  1.00 26.40           N  
ATOM   1664  CA  GLY A 238      37.370 -29.631  15.643  1.00 29.85           C  
ATOM   1665  C   GLY A 238      36.154 -28.732  15.867  1.00 31.21           C  
ATOM   1666  O   GLY A 238      35.106 -29.222  16.293  1.00 33.63           O  
ATOM   1667  N   ASP A 239      36.270 -27.429  15.574  1.00 29.50           N  
ATOM   1668  CA  ASP A 239      35.177 -26.455  15.669  1.00 31.76           C  
ATOM   1669  C   ASP A 239      35.541 -25.230  14.852  1.00 30.05           C  
ATOM   1670  O   ASP A 239      36.730 -24.958  14.608  1.00 27.37           O  
ATOM   1671  CB  ASP A 239      34.910 -25.981  17.081  1.00 34.65           C  
ATOM   1672  CG  ASP A 239      33.848 -26.829  17.743  1.00 47.06           C  
ATOM   1673  OD1 ASP A 239      32.640 -26.759  17.313  1.00 52.18           O  
ATOM   1674  OD2 ASP A 239      34.244 -27.640  18.654  1.00 53.23           O  
ATOM   1675  N   ILE A 240      34.550 -24.425  14.458  1.00 29.16           N  
ATOM   1676  CA  ILE A 240      34.859 -23.218  13.712  1.00 29.28           C  
ATOM   1677  C   ILE A 240      35.486 -22.104  14.591  1.00 29.64           C  
ATOM   1678  O   ILE A 240      35.311 -22.127  15.820  1.00 30.87           O  
ATOM   1679  CB  ILE A 240      33.565 -22.710  12.985  1.00 28.70           C  
ATOM   1680  CG1 ILE A 240      32.453 -22.484  14.022  1.00 28.80           C  
ATOM   1681  CG2 ILE A 240      33.067 -23.753  12.025  1.00 30.42           C  
ATOM   1682  CD1 ILE A 240      31.155 -21.723  13.458  1.00 34.32           C  
ATOM   1683  N   PRO A 241      36.224 -21.149  13.997  1.00 27.37           N  
ATOM   1684  CA  PRO A 241      36.895 -20.194  14.891  1.00 26.76           C  
ATOM   1685  C   PRO A 241      36.058 -19.014  15.409  1.00 30.23           C  
ATOM   1686  O   PRO A 241      36.431 -18.502  16.448  1.00 30.98           O  
ATOM   1687  CB  PRO A 241      38.089 -19.670  14.053  1.00 25.35           C  
ATOM   1688  CG  PRO A 241      37.552 -19.679  12.576  1.00 26.12           C  
ATOM   1689  CD  PRO A 241      36.540 -20.891  12.561  1.00 25.27           C  
ATOM   1690  N   PHE A 242      34.972 -18.625  14.708  1.00 29.79           N  
ATOM   1691  CA  PHE A 242      34.219 -17.378  14.997  1.00 30.16           C  
ATOM   1692  C   PHE A 242      32.773 -17.785  15.182  1.00 32.46           C  
ATOM   1693  O   PHE A 242      32.309 -18.568  14.441  1.00 33.22           O  
ATOM   1694  CB  PHE A 242      34.331 -16.370  13.886  1.00 27.38           C  
ATOM   1695  CG  PHE A 242      35.732 -16.076  13.484  1.00 26.67           C  
ATOM   1696  CD1 PHE A 242      36.752 -15.818  14.462  1.00 29.59           C  
ATOM   1697  CD2 PHE A 242      36.078 -16.126  12.102  1.00 27.62           C  
ATOM   1698  CE1 PHE A 242      38.098 -15.496  14.027  1.00 27.79           C  
ATOM   1699  CE2 PHE A 242      37.422 -15.802  11.632  1.00 27.49           C  
ATOM   1700  CZ  PHE A 242      38.423 -15.531  12.620  1.00 27.79           C  
ATOM   1701  N   GLU A 243      32.121 -17.355  16.272  1.00 36.56           N  
ATOM   1702  CA  GLU A 243      30.666 -17.437  16.361  1.00 39.97           C  
ATOM   1703  C   GLU A 243      29.973 -16.080  16.143  1.00 39.54           C  
ATOM   1704  O   GLU A 243      28.948 -16.010  15.487  1.00 41.98           O  
ATOM   1705  CB  GLU A 243      30.288 -18.001  17.701  1.00 42.14           C  
ATOM   1706  CG  GLU A 243      30.834 -19.407  17.930  1.00 52.79           C  
ATOM   1707  CD  GLU A 243      30.001 -20.503  17.221  1.00 64.90           C  
ATOM   1708  OE1 GLU A 243      28.846 -20.208  16.767  1.00 69.07           O  
ATOM   1709  OE2 GLU A 243      30.503 -21.658  17.132  1.00 67.52           O  
ATOM   1710  N   HIS A 244      30.538 -14.989  16.604  1.00 38.24           N  
ATOM   1711  CA  HIS A 244      29.817 -13.684  16.556  1.00 37.76           C  
ATOM   1712  C   HIS A 244      30.344 -12.813  15.427  1.00 35.78           C  
ATOM   1713  O   HIS A 244      31.536 -12.947  14.989  1.00 31.05           O  
ATOM   1714  CB  HIS A 244      29.904 -13.010  17.958  1.00 38.56           C  
ATOM   1715  CG  HIS A 244      29.311 -13.895  19.020  1.00 47.13           C  
ATOM   1716  ND1 HIS A 244      30.035 -14.393  20.085  1.00 53.00           N  
ATOM   1717  CD2 HIS A 244      28.089 -14.482  19.093  1.00 51.24           C  
ATOM   1718  CE1 HIS A 244      29.262 -15.192  20.807  1.00 55.25           C  
ATOM   1719  NE2 HIS A 244      28.086 -15.286  20.210  1.00 54.47           N  
ATOM   1720  N   ASP A 245      29.475 -11.941  14.926  1.00 33.38           N  
ATOM   1721  CA  ASP A 245      29.864 -11.000  13.894  1.00 34.80           C  
ATOM   1722  C   ASP A 245      31.122 -10.250  14.309  1.00 34.85           C  
ATOM   1723  O   ASP A 245      31.993  -9.943  13.515  1.00 32.63           O  
ATOM   1724  CB  ASP A 245      28.735  -9.966  13.753  1.00 35.46           C  
ATOM   1725  CG  ASP A 245      27.547 -10.489  12.918  1.00 39.80           C  
ATOM   1726  OD1 ASP A 245      27.405 -11.749  12.611  1.00 38.51           O  
ATOM   1727  OD2 ASP A 245      26.732  -9.597  12.554  1.00 44.59           O  
ATOM   1728  N   GLU A 246      31.218  -9.912  15.600  1.00 35.20           N  
ATOM   1729  CA  GLU A 246      32.347  -9.063  16.035  1.00 35.54           C  
ATOM   1730  C   GLU A 246      33.662  -9.857  15.857  1.00 32.96           C  
ATOM   1731  O   GLU A 246      34.668  -9.313  15.539  1.00 33.12           O  
ATOM   1732  CB  GLU A 246      32.176  -8.725  17.557  1.00 36.78           C  
ATOM   1733  CG  GLU A 246      30.764  -8.066  17.892  1.00 46.59           C  
ATOM   1734  CD  GLU A 246      29.486  -8.993  17.638  1.00 58.06           C  
ATOM   1735  OE1 GLU A 246      29.483 -10.219  17.906  1.00 59.42           O  
ATOM   1736  OE2 GLU A 246      28.439  -8.444  17.201  1.00 65.92           O  
ATOM   1737  N   GLU A 247      33.613 -11.154  16.175  1.00 31.82           N  
ATOM   1738  C   GLU A 247      35.178 -12.127  14.545  1.00 30.03           C  
ATOM   1739  O   GLU A 247      36.365 -12.107  14.176  1.00 28.18           O  
ATOM   1740  CA AGLU A 247      34.809 -12.009  16.021  0.50 31.10           C  
ATOM   1741  CB AGLU A 247      34.539 -13.382  16.605  0.50 30.17           C  
ATOM   1742  CG AGLU A 247      34.463 -13.423  18.121  0.50 30.88           C  
ATOM   1743  CD AGLU A 247      33.567 -14.539  18.593  0.50 33.46           C  
ATOM   1744  OE1AGLU A 247      32.827 -15.115  17.771  0.50 33.78           O  
ATOM   1745  OE2AGLU A 247      33.606 -14.874  19.792  0.50 31.49           O  
ATOM   1746  CA BGLU A 247      34.784 -12.037  16.017  0.50 30.91           C  
ATOM   1747  CB BGLU A 247      34.409 -13.420  16.492  0.50 29.71           C  
ATOM   1748  CG BGLU A 247      34.477 -13.664  17.969  0.50 29.77           C  
ATOM   1749  CD BGLU A 247      34.468 -15.135  18.198  0.50 30.16           C  
ATOM   1750  OE1BGLU A 247      33.360 -15.741  18.198  0.50 30.16           O  
ATOM   1751  OE2BGLU A 247      35.578 -15.704  18.246  0.50 30.76           O  
ATOM   1752  N   ILE A 248      34.162 -12.263  13.661  1.00 29.34           N  
ATOM   1753  CA  ILE A 248      34.445 -12.314  12.189  1.00 28.96           C  
ATOM   1754  C   ILE A 248      35.177 -11.069  11.735  1.00 31.47           C  
ATOM   1755  O   ILE A 248      36.228 -11.112  11.087  1.00 29.21           O  
ATOM   1756  CB  ILE A 248      33.167 -12.567  11.348  1.00 29.87           C  
ATOM   1757  CG1 ILE A 248      32.617 -13.935  11.704  1.00 24.74           C  
ATOM   1758  CG2 ILE A 248      33.490 -12.433   9.834  1.00 29.11           C  
ATOM   1759  CD1 ILE A 248      31.161 -14.255  11.337  1.00 31.00           C  
ATOM   1760  N   ILE A 249      34.632  -9.887  12.114  1.00 30.36           N  
ATOM   1761  CA  ILE A 249      35.188  -8.636  11.637  1.00 33.25           C  
ATOM   1762  C   ILE A 249      36.562  -8.371  12.218  1.00 31.60           C  
ATOM   1763  O   ILE A 249      37.385  -7.742  11.540  1.00 34.03           O  
ATOM   1764  CB  ILE A 249      34.226  -7.440  12.058  1.00 33.88           C  
ATOM   1765  CG1 ILE A 249      32.939  -7.503  11.243  1.00 35.16           C  
ATOM   1766  CG2 ILE A 249      34.926  -6.072  11.823  1.00 40.10           C  
ATOM   1767  CD1 ILE A 249      31.880  -6.463  11.829  1.00 41.06           C  
ATOM   1768  N   ARG A 250      36.808  -8.791  13.482  1.00 30.81           N  
ATOM   1769  CA  ARG A 250      38.170  -8.604  14.035  1.00 31.65           C  
ATOM   1770  C   ARG A 250      39.162  -9.609  13.361  1.00 32.37           C  
ATOM   1771  O   ARG A 250      40.311  -9.235  13.049  1.00 32.71           O  
ATOM   1772  CB  ARG A 250      38.174  -8.787  15.557  1.00 30.07           C  
ATOM   1773  CG  ARG A 250      39.620  -8.591  16.182  1.00 29.41           C  
ATOM   1774  CD  ARG A 250      39.431  -8.373  17.697  1.00 35.20           C  
ATOM   1775  NE  ARG A 250      40.789  -8.309  18.349  1.00 33.41           N  
ATOM   1776  CZ  ARG A 250      41.329  -9.247  19.117  1.00 34.90           C  
ATOM   1777  NH1 ARG A 250      40.667 -10.409  19.359  1.00 27.60           N  
ATOM   1778  NH2 ARG A 250      42.576  -9.018  19.554  1.00 35.23           N  
ATOM   1779  N   GLY A 251      38.689 -10.843  13.059  1.00 33.51           N  
ATOM   1780  CA  GLY A 251      39.551 -11.722  12.224  1.00 31.37           C  
ATOM   1781  C   GLY A 251      40.761 -12.306  13.005  1.00 31.45           C  
ATOM   1782  O   GLY A 251      41.738 -12.792  12.366  1.00 32.02           O  
ATOM   1783  N   GLN A 252      40.706 -12.358  14.354  1.00 31.16           N  
ATOM   1784  CA  GLN A 252      41.923 -12.732  15.146  1.00 30.03           C  
ATOM   1785  C   GLN A 252      41.765 -14.213  15.355  1.00 30.47           C  
ATOM   1786  O   GLN A 252      40.785 -14.622  15.947  1.00 32.64           O  
ATOM   1787  CB  GLN A 252      41.908 -12.130  16.539  1.00 29.70           C  
ATOM   1788  CG  GLN A 252      43.117 -12.567  17.403  1.00 34.29           C  
ATOM   1789  CD  GLN A 252      44.449 -12.201  16.758  1.00 38.00           C  
ATOM   1790  OE1 GLN A 252      44.609 -11.061  16.222  1.00 42.18           O  
ATOM   1791  NE2 GLN A 252      45.408 -13.146  16.774  1.00 33.44           N  
ATOM   1792  N   VAL A 253      42.696 -15.023  14.933  1.00 27.69           N  
ATOM   1793  CA  VAL A 253      42.491 -16.486  15.055  1.00 28.02           C  
ATOM   1794  C   VAL A 253      43.227 -17.032  16.270  1.00 26.37           C  
ATOM   1795  O   VAL A 253      44.405 -16.782  16.346  1.00 27.17           O  
ATOM   1796  CB  VAL A 253      43.133 -17.132  13.705  1.00 26.97           C  
ATOM   1797  CG1 VAL A 253      43.073 -18.699  13.702  1.00 26.68           C  
ATOM   1798  CG2 VAL A 253      42.419 -16.592  12.406  1.00 28.28           C  
ATOM   1799  N   PHE A 254      42.605 -17.806  17.162  1.00 25.86           N  
ATOM   1800  CA  PHE A 254      43.246 -18.425  18.304  1.00 27.91           C  
ATOM   1801  C   PHE A 254      43.173 -19.942  18.042  1.00 28.98           C  
ATOM   1802  O   PHE A 254      42.058 -20.501  17.754  1.00 28.45           O  
ATOM   1803  CB  PHE A 254      42.438 -18.089  19.583  1.00 28.72           C  
ATOM   1804  CG  PHE A 254      42.806 -18.949  20.765  1.00 32.21           C  
ATOM   1805  CD1 PHE A 254      43.970 -18.655  21.565  1.00 33.32           C  
ATOM   1806  CD2 PHE A 254      42.008 -20.075  21.104  1.00 30.22           C  
ATOM   1807  CE1 PHE A 254      44.323 -19.536  22.727  1.00 24.56           C  
ATOM   1808  CE2 PHE A 254      42.362 -20.954  22.242  1.00 31.72           C  
ATOM   1809  CZ  PHE A 254      43.539 -20.651  23.017  1.00 34.00           C  
ATOM   1810  N   PHE A 255      44.332 -20.600  18.126  1.00 29.77           N  
ATOM   1811  CA  PHE A 255      44.370 -22.075  18.003  1.00 31.00           C  
ATOM   1812  C   PHE A 255      44.167 -22.710  19.344  1.00 31.59           C  
ATOM   1813  O   PHE A 255      44.874 -22.435  20.291  1.00 35.07           O  
ATOM   1814  CB  PHE A 255      45.598 -22.544  17.268  1.00 28.75           C  
ATOM   1815  CG  PHE A 255      45.514 -22.268  15.845  1.00 30.14           C  
ATOM   1816  CD1 PHE A 255      45.840 -21.028  15.330  1.00 25.75           C  
ATOM   1817  CD2 PHE A 255      44.949 -23.224  14.989  1.00 27.52           C  
ATOM   1818  CE1 PHE A 255      45.658 -20.750  13.892  1.00 24.74           C  
ATOM   1819  CE2 PHE A 255      44.838 -22.986  13.624  1.00 22.77           C  
ATOM   1820  CZ  PHE A 255      45.136 -21.720  13.058  1.00 29.33           C  
ATOM   1821  N   ARG A 256      43.103 -23.516  19.426  1.00 33.11           N  
ATOM   1822  CA  ARG A 256      42.692 -24.127  20.665  1.00 34.58           C  
ATOM   1823  C   ARG A 256      43.254 -25.583  20.787  1.00 34.72           C  
ATOM   1824  O   ARG A 256      43.203 -26.170  21.910  1.00 35.38           O  
ATOM   1825  CB  ARG A 256      41.150 -24.203  20.690  1.00 36.35           C  
ATOM   1826  CG  ARG A 256      40.515 -24.851  19.436  1.00 35.01           C  
ATOM   1827  CD  ARG A 256      38.936 -24.654  19.447  1.00 38.74           C  
ATOM   1828  NE  ARG A 256      38.524 -23.363  18.854  1.00 46.04           N  
ATOM   1829  CZ  ARG A 256      37.255 -22.919  18.903  1.00 50.68           C  
ATOM   1830  NH1 ARG A 256      36.318 -23.663  19.521  1.00 51.37           N  
ATOM   1831  NH2 ARG A 256      36.917 -21.760  18.372  1.00 42.28           N  
ATOM   1832  N   GLN A 257      43.825 -26.113  19.677  1.00 31.46           N  
ATOM   1833  CA  GLN A 257      44.485 -27.451  19.632  1.00 30.89           C  
ATOM   1834  C   GLN A 257      45.938 -27.144  19.123  1.00 26.54           C  
ATOM   1835  O   GLN A 257      46.213 -26.140  18.542  1.00 24.28           O  
ATOM   1836  CB  GLN A 257      43.807 -28.347  18.560  1.00 31.47           C  
ATOM   1837  CG  GLN A 257      42.342 -28.543  18.841  1.00 41.53           C  
ATOM   1838  CD  GLN A 257      42.149 -29.497  19.968  1.00 52.37           C  
ATOM   1839  OE1 GLN A 257      42.972 -30.397  20.167  1.00 54.69           O  
ATOM   1840  NE2 GLN A 257      41.081 -29.292  20.752  1.00 56.06           N  
ATOM   1841  N   ARG A 258      46.791 -28.112  19.259  1.00 24.66           N  
ATOM   1842  CA  ARG A 258      48.143 -28.005  18.754  1.00 23.21           C  
ATOM   1843  C   ARG A 258      48.011 -28.213  17.255  1.00 24.03           C  
ATOM   1844  O   ARG A 258      47.529 -29.279  16.821  1.00 24.78           O  
ATOM   1845  CB  ARG A 258      48.938 -29.133  19.357  1.00 20.61           C  
ATOM   1846  CG AARG A 258      50.116 -29.551  18.534  0.50 25.17           C  
ATOM   1847  CD AARG A 258      51.150 -28.465  18.734  0.50 22.88           C  
ATOM   1848  NE AARG A 258      52.155 -28.554  17.673  0.50 25.23           N  
ATOM   1849  CZ AARG A 258      53.268 -27.851  17.678  0.50 23.89           C  
ATOM   1850  NH1AARG A 258      53.543 -27.062  18.744  0.50 15.07           N  
ATOM   1851  NH2AARG A 258      54.131 -28.039  16.671  0.50 20.47           N  
ATOM   1852  CG BARG A 258      50.487 -28.903  19.109  0.50 19.32           C  
ATOM   1853  CD BARG A 258      50.844 -29.291  17.569  0.50 18.97           C  
ATOM   1854  NE BARG A 258      52.206 -28.887  17.067  0.50 18.66           N  
ATOM   1855  CZ BARG A 258      52.716 -29.353  15.930  0.50 21.10           C  
ATOM   1856  NH1BARG A 258      52.017 -30.218  15.186  0.50 14.70           N  
ATOM   1857  NH2BARG A 258      53.875 -28.918  15.519  0.50 28.51           N  
ATOM   1858  N   VAL A 259      48.444 -27.226  16.494  1.00 21.36           N  
ATOM   1859  CA  VAL A 259      48.401 -27.282  15.051  1.00 23.73           C  
ATOM   1860  C   VAL A 259      49.752 -26.708  14.632  1.00 23.85           C  
ATOM   1861  O   VAL A 259      50.256 -25.687  15.245  1.00 26.47           O  
ATOM   1862  CB  VAL A 259      47.258 -26.317  14.543  1.00 22.49           C  
ATOM   1863  CG1 VAL A 259      47.314 -26.116  13.026  1.00 25.62           C  
ATOM   1864  CG2 VAL A 259      45.872 -26.918  14.964  1.00 21.99           C  
ATOM   1865  N   SER A 260      50.309 -27.269  13.546  1.00 22.12           N  
ATOM   1866  CA  SER A 260      51.719 -26.935  13.089  1.00 23.95           C  
ATOM   1867  C   SER A 260      51.760 -25.507  12.616  1.00 25.13           C  
ATOM   1868  O   SER A 260      50.749 -24.968  12.223  1.00 21.70           O  
ATOM   1869  CB  SER A 260      52.093 -27.904  11.948  1.00 23.48           C  
ATOM   1870  OG  SER A 260      51.268 -27.618  10.806  1.00 23.91           O  
ATOM   1871  N   SER A 261      52.922 -24.841  12.672  1.00 24.58           N  
ATOM   1872  CA  SER A 261      52.965 -23.447  12.283  1.00 24.82           C  
ATOM   1873  C   SER A 261      52.667 -23.295  10.827  1.00 26.95           C  
ATOM   1874  O   SER A 261      52.169 -22.271  10.431  1.00 25.30           O  
ATOM   1875  CB  SER A 261      54.340 -22.814  12.563  1.00 26.89           C  
ATOM   1876  OG  SER A 261      54.616 -22.908  13.968  1.00 27.84           O  
ATOM   1877  N   GLU A 262      52.962 -24.295  10.020  1.00 25.76           N  
ATOM   1878  CA  GLU A 262      52.674 -24.155   8.540  1.00 30.16           C  
ATOM   1879  C   GLU A 262      51.174 -24.140   8.323  1.00 24.48           C  
ATOM   1880  O   GLU A 262      50.675 -23.328   7.538  1.00 24.67           O  
ATOM   1881  CB  GLU A 262      53.275 -25.303   7.707  1.00 28.93           C  
ATOM   1882  CG  GLU A 262      54.778 -25.240   7.484  1.00 34.66           C  
ATOM   1883  CD  GLU A 262      55.233 -26.588   6.679  1.00 44.00           C  
ATOM   1884  OE1 GLU A 262      54.484 -27.685   6.727  1.00 54.71           O  
ATOM   1885  OE2 GLU A 262      56.324 -26.541   5.986  1.00 60.34           O  
ATOM   1886  N   CYS A 263      50.482 -25.037   8.993  1.00 24.97           N  
ATOM   1887  CA  CYS A 263      48.985 -25.060   8.890  1.00 24.07           C  
ATOM   1888  C   CYS A 263      48.407 -23.747   9.394  1.00 24.22           C  
ATOM   1889  O   CYS A 263      47.480 -23.175   8.755  1.00 23.65           O  
ATOM   1890  CB  CYS A 263      48.439 -26.247   9.650  1.00 24.66           C  
ATOM   1891  SG  CYS A 263      46.684 -26.473   9.432  1.00 27.65           S  
ATOM   1892  N   GLN A 264      48.885 -23.247  10.564  1.00 23.67           N  
ATOM   1893  CA  GLN A 264      48.364 -22.008  11.138  1.00 22.73           C  
ATOM   1894  C   GLN A 264      48.571 -20.884  10.146  1.00 23.69           C  
ATOM   1895  O   GLN A 264      47.681 -20.068   9.967  1.00 25.71           O  
ATOM   1896  CB  GLN A 264      49.153 -21.685  12.430  1.00 24.62           C  
ATOM   1897  CG  GLN A 264      48.781 -22.588  13.647  1.00 22.29           C  
ATOM   1898  CD  GLN A 264      49.184 -21.937  14.942  1.00 27.76           C  
ATOM   1899  OE1 GLN A 264      49.459 -20.728  14.974  1.00 29.31           O  
ATOM   1900  NE2 GLN A 264      49.221 -22.725  16.041  1.00 25.38           N  
ATOM   1901  N   HIS A 265      49.756 -20.859   9.487  1.00 24.49           N  
ATOM   1902  CA  HIS A 265      50.135 -19.789   8.534  1.00 26.14           C  
ATOM   1903  C   HIS A 265      49.079 -19.819   7.349  1.00 25.77           C  
ATOM   1904  O   HIS A 265      48.532 -18.797   6.920  1.00 22.25           O  
ATOM   1905  CB  HIS A 265      51.505 -20.058   7.922  1.00 26.52           C  
ATOM   1906  CG  HIS A 265      51.812 -19.095   6.804  1.00 30.55           C  
ATOM   1907  ND1 HIS A 265      52.298 -17.803   7.039  1.00 32.39           N  
ATOM   1908  CD2 HIS A 265      51.561 -19.168   5.476  1.00 22.79           C  
ATOM   1909  CE1 HIS A 265      52.452 -17.178   5.869  1.00 27.85           C  
ATOM   1910  NE2 HIS A 265      51.959 -17.952   4.916  1.00 35.61           N  
ATOM   1911  N   LEU A 266      48.756 -21.021   6.897  1.00 23.63           N  
ATOM   1912  CA  LEU A 266      47.837 -21.120   5.729  1.00 23.39           C  
ATOM   1913  C   LEU A 266      46.474 -20.626   6.166  1.00 22.88           C  
ATOM   1914  O   LEU A 266      45.783 -19.939   5.356  1.00 24.52           O  
ATOM   1915  CB  LEU A 266      47.731 -22.581   5.229  1.00 22.42           C  
ATOM   1916  CG  LEU A 266      46.725 -22.850   4.024  1.00 22.22           C  
ATOM   1917  CD1 LEU A 266      46.851 -21.876   2.845  1.00 21.76           C  
ATOM   1918  CD2 LEU A 266      46.819 -24.288   3.600  1.00 23.33           C  
ATOM   1919  N   ILE A 267      46.038 -21.046   7.388  1.00 23.92           N  
ATOM   1920  CA  ILE A 267      44.654 -20.714   7.853  1.00 22.08           C  
ATOM   1921  C   ILE A 267      44.605 -19.198   7.964  1.00 24.11           C  
ATOM   1922  O   ILE A 267      43.665 -18.580   7.522  1.00 23.09           O  
ATOM   1923  CB  ILE A 267      44.332 -21.318   9.205  1.00 22.82           C  
ATOM   1924  CG1 ILE A 267      44.072 -22.851   8.981  1.00 20.69           C  
ATOM   1925  CG2 ILE A 267      43.094 -20.633   9.852  1.00 19.77           C  
ATOM   1926  CD1 ILE A 267      44.146 -23.696  10.258  1.00 25.12           C  
ATOM   1927  N   ARG A 268      45.617 -18.599   8.563  1.00 23.13           N  
ATOM   1928  CA  ARG A 268      45.531 -17.133   8.842  1.00 25.50           C  
ATOM   1929  C   ARG A 268      45.662 -16.418   7.479  1.00 24.13           C  
ATOM   1930  O   ARG A 268      45.185 -15.291   7.325  1.00 26.48           O  
ATOM   1931  CB  ARG A 268      46.672 -16.744   9.777  1.00 23.59           C  
ATOM   1932  CG  ARG A 268      46.500 -17.200  11.208  1.00 24.88           C  
ATOM   1933  CD  ARG A 268      47.433 -16.355  12.188  1.00 28.65           C  
ATOM   1934  NE  ARG A 268      46.976 -16.547  13.584  1.00 28.83           N  
ATOM   1935  CZ  ARG A 268      47.461 -17.504  14.371  1.00 34.20           C  
ATOM   1936  NH1 ARG A 268      48.433 -18.225  13.882  1.00 31.34           N  
ATOM   1937  NH2 ARG A 268      46.969 -17.709  15.606  1.00 29.96           N  
ATOM   1938  N   TRP A 269      46.338 -17.051   6.493  1.00 24.70           N  
ATOM   1939  CA  TRP A 269      46.364 -16.443   5.135  1.00 23.81           C  
ATOM   1940  C   TRP A 269      44.972 -16.459   4.489  1.00 23.67           C  
ATOM   1941  O   TRP A 269      44.487 -15.428   4.005  1.00 22.96           O  
ATOM   1942  CB  TRP A 269      47.428 -17.101   4.269  1.00 23.08           C  
ATOM   1943  CG  TRP A 269      47.807 -16.419   3.037  1.00 25.43           C  
ATOM   1944  CD1 TRP A 269      47.517 -15.047   2.648  1.00 28.17           C  
ATOM   1945  CD2 TRP A 269      48.597 -16.960   1.975  1.00 25.28           C  
ATOM   1946  NE1 TRP A 269      48.057 -14.810   1.366  1.00 28.74           N  
ATOM   1947  CE2 TRP A 269      48.738 -15.941   0.964  1.00 26.90           C  
ATOM   1948  CE3 TRP A 269      49.216 -18.195   1.779  1.00 22.85           C  
ATOM   1949  CZ2 TRP A 269      49.493 -16.137  -0.185  1.00 29.28           C  
ATOM   1950  CZ3 TRP A 269      49.936 -18.386   0.640  1.00 26.94           C  
ATOM   1951  CH2 TRP A 269      50.089 -17.363  -0.327  1.00 29.19           C  
ATOM   1952  N   CYS A 270      44.317 -17.642   4.469  1.00 21.06           N  
ATOM   1953  CA  CYS A 270      42.940 -17.722   3.944  1.00 21.50           C  
ATOM   1954  C   CYS A 270      42.058 -16.700   4.652  1.00 21.20           C  
ATOM   1955  O   CYS A 270      41.121 -16.209   4.041  1.00 21.71           O  
ATOM   1956  CB  CYS A 270      42.352 -19.150   4.211  1.00 20.96           C  
ATOM   1957  SG  CYS A 270      43.216 -20.283   3.034  1.00 25.55           S  
ATOM   1958  N   LEU A 271      42.296 -16.404   5.967  1.00 22.35           N  
ATOM   1959  CA  LEU A 271      41.401 -15.514   6.734  1.00 25.65           C  
ATOM   1960  C   LEU A 271      41.978 -14.068   6.806  1.00 26.09           C  
ATOM   1961  O   LEU A 271      41.672 -13.378   7.744  1.00 28.50           O  
ATOM   1962  CB  LEU A 271      41.228 -15.983   8.179  1.00 23.31           C  
ATOM   1963  CG  LEU A 271      40.547 -17.433   8.187  1.00 22.82           C  
ATOM   1964  CD1 LEU A 271      40.389 -18.008   9.574  1.00 24.49           C  
ATOM   1965  CD2 LEU A 271      39.102 -17.435   7.453  1.00 22.62           C  
ATOM   1966  N   ALA A 272      42.733 -13.662   5.809  1.00 26.95           N  
ATOM   1967  CA  ALA A 272      43.187 -12.234   5.704  1.00 28.13           C  
ATOM   1968  C   ALA A 272      41.956 -11.351   5.657  1.00 29.23           C  
ATOM   1969  O   ALA A 272      40.964 -11.613   4.929  1.00 27.47           O  
ATOM   1970  CB  ALA A 272      44.031 -12.011   4.500  1.00 27.21           C  
ATOM   1971  N   LEU A 273      41.969 -10.317   6.524  1.00 30.14           N  
ATOM   1972  CA  LEU A 273      40.807  -9.391   6.605  1.00 30.27           C  
ATOM   1973  C   LEU A 273      40.531  -8.751   5.221  1.00 29.36           C  
ATOM   1974  O   LEU A 273      39.387  -8.660   4.770  1.00 28.91           O  
ATOM   1975  CB  LEU A 273      41.093  -8.306   7.690  1.00 32.54           C  
ATOM   1976  CG  LEU A 273      40.877  -8.745   9.134  1.00 34.75           C  
ATOM   1977  CD1 LEU A 273      41.119  -7.604  10.161  1.00 36.69           C  
ATOM   1978  CD2 LEU A 273      39.450  -9.243   9.285  1.00 38.63           C  
ATOM   1979  N   ARG A 274      41.544  -8.265   4.557  1.00 28.72           N  
ATOM   1980  CA  ARG A 274      41.375  -7.680   3.246  1.00 32.64           C  
ATOM   1981  C   ARG A 274      41.320  -8.771   2.189  1.00 31.01           C  
ATOM   1982  O   ARG A 274      42.277  -9.567   2.063  1.00 29.63           O  
ATOM   1983  CB  ARG A 274      42.587  -6.821   2.882  1.00 32.57           C  
ATOM   1984  CG  ARG A 274      42.606  -5.426   3.496  1.00 43.03           C  
ATOM   1985  CD  ARG A 274      44.129  -4.846   3.544  1.00 42.93           C  
ATOM   1986  NE  ARG A 274      44.676  -4.113   2.391  1.00 61.14           N  
ATOM   1987  CZ  ARG A 274      44.474  -4.350   1.083  1.00 69.28           C  
ATOM   1988  NH1 ARG A 274      43.700  -5.353   0.628  1.00 69.85           N  
ATOM   1989  NH2 ARG A 274      45.090  -3.554   0.196  1.00 72.60           N  
ATOM   1990  N   PRO A 275      40.239  -8.794   1.396  1.00 29.78           N  
ATOM   1991  CA  PRO A 275      40.043  -9.791   0.400  1.00 30.95           C  
ATOM   1992  C   PRO A 275      41.266  -9.995  -0.501  1.00 30.57           C  
ATOM   1993  O   PRO A 275      41.574 -11.098  -0.858  1.00 29.07           O  
ATOM   1994  CB  PRO A 275      38.827  -9.296  -0.398  1.00 30.86           C  
ATOM   1995  CG  PRO A 275      38.006  -8.538   0.697  1.00 29.92           C  
ATOM   1996  CD  PRO A 275      39.089  -7.833   1.464  1.00 30.86           C  
ATOM   1997  N   SER A 276      41.939  -8.927  -0.913  1.00 32.19           N  
ATOM   1998  CA  SER A 276      42.956  -9.081  -1.931  1.00 31.30           C  
ATOM   1999  C   SER A 276      44.232  -9.616  -1.223  1.00 31.87           C  
ATOM   2000  O   SER A 276      45.192  -9.917  -1.879  1.00 33.47           O  
ATOM   2001  CB  SER A 276      43.235  -7.683  -2.524  1.00 33.24           C  
ATOM   2002  OG  SER A 276      43.703  -6.795  -1.454  1.00 35.94           O  
ATOM   2003  N   ASP A 277      44.244  -9.656   0.105  1.00 31.97           N  
ATOM   2004  CA  ASP A 277      45.336 -10.297   0.883  1.00 31.07           C  
ATOM   2005  C   ASP A 277      45.223 -11.832   0.992  1.00 30.73           C  
ATOM   2006  O   ASP A 277      46.205 -12.454   1.445  1.00 31.03           O  
ATOM   2007  CB  ASP A 277      45.383  -9.747   2.292  1.00 29.07           C  
ATOM   2008  CG  ASP A 277      46.176  -8.357   2.325  1.00 37.49           C  
ATOM   2009  OD1 ASP A 277      46.766  -7.981   1.299  1.00 32.25           O  
ATOM   2010  OD2 ASP A 277      46.137  -7.713   3.343  1.00 38.70           O  
ATOM   2011  N   ARG A 278      44.071 -12.428   0.555  1.00 26.93           N  
ATOM   2012  CA  ARG A 278      43.961 -13.889   0.654  1.00 23.85           C  
ATOM   2013  C   ARG A 278      44.601 -14.600  -0.522  1.00 26.41           C  
ATOM   2014  O   ARG A 278      44.803 -14.013  -1.634  1.00 25.56           O  
ATOM   2015  CB  ARG A 278      42.459 -14.258   0.709  1.00 24.63           C  
ATOM   2016  CG  ARG A 278      41.790 -13.464   1.782  1.00 25.64           C  
ATOM   2017  CD  ARG A 278      40.253 -13.807   1.883  1.00 22.52           C  
ATOM   2018  NE  ARG A 278      39.704 -12.824   2.837  1.00 25.74           N  
ATOM   2019  CZ  ARG A 278      38.491 -12.269   2.750  1.00 24.49           C  
ATOM   2020  NH1 ARG A 278      37.626 -12.630   1.763  1.00 27.96           N  
ATOM   2021  NH2 ARG A 278      38.202 -11.257   3.597  1.00 26.13           N  
ATOM   2022  N   PRO A 279      45.032 -15.872  -0.299  1.00 24.09           N  
ATOM   2023  CA  PRO A 279      45.730 -16.575  -1.387  1.00 23.59           C  
ATOM   2024  C   PRO A 279      44.745 -16.916  -2.547  1.00 27.00           C  
ATOM   2025  O   PRO A 279      43.536 -17.016  -2.294  1.00 25.49           O  
ATOM   2026  CB  PRO A 279      46.153 -17.895  -0.684  1.00 23.81           C  
ATOM   2027  CG  PRO A 279      45.071 -18.073   0.494  1.00 23.67           C  
ATOM   2028  CD  PRO A 279      44.940 -16.645   0.989  1.00 20.60           C  
ATOM   2029  N   THR A 280      45.226 -17.142  -3.774  1.00 26.15           N  
ATOM   2030  CA  THR A 280      44.363 -17.707  -4.806  1.00 25.58           C  
ATOM   2031  C   THR A 280      44.402 -19.236  -4.605  1.00 27.06           C  
ATOM   2032  O   THR A 280      45.225 -19.713  -3.779  1.00 26.17           O  
ATOM   2033  CB  THR A 280      45.028 -17.477  -6.147  1.00 25.46           C  
ATOM   2034  OG1 THR A 280      46.331 -18.115  -6.139  1.00 26.39           O  
ATOM   2035  CG2 THR A 280      45.173 -15.900  -6.381  1.00 26.26           C  
ATOM   2036  N   PHE A 281      43.606 -19.983  -5.376  1.00 25.16           N  
ATOM   2037  CA  PHE A 281      43.663 -21.522  -5.242  1.00 25.18           C  
ATOM   2038  C   PHE A 281      45.017 -22.033  -5.482  1.00 26.49           C  
ATOM   2039  O   PHE A 281      45.502 -22.981  -4.830  1.00 25.64           O  
ATOM   2040  CB  PHE A 281      42.624 -22.209  -6.136  1.00 27.80           C  
ATOM   2041  CG  PHE A 281      41.192 -21.802  -5.802  1.00 29.08           C  
ATOM   2042  CD1 PHE A 281      40.760 -21.702  -4.501  1.00 36.55           C  
ATOM   2043  CD2 PHE A 281      40.237 -21.609  -6.841  1.00 37.39           C  
ATOM   2044  CE1 PHE A 281      39.348 -21.272  -4.152  1.00 34.94           C  
ATOM   2045  CE2 PHE A 281      38.888 -21.253  -6.546  1.00 39.89           C  
ATOM   2046  CZ  PHE A 281      38.477 -21.047  -5.145  1.00 37.37           C  
ATOM   2047  N   GLU A 282      45.692 -21.464  -6.477  1.00 24.11           N  
ATOM   2048  CA  GLU A 282      46.998 -21.923  -6.813  1.00 26.49           C  
ATOM   2049  C   GLU A 282      47.925 -21.704  -5.659  1.00 25.98           C  
ATOM   2050  O   GLU A 282      48.713 -22.611  -5.336  1.00 27.27           O  
ATOM   2051  CB  GLU A 282      47.504 -21.187  -8.111  1.00 26.28           C  
ATOM   2052  CG  GLU A 282      48.948 -21.692  -8.471  1.00 26.60           C  
ATOM   2053  CD  GLU A 282      49.463 -20.942  -9.754  1.00 34.44           C  
ATOM   2054  OE1 GLU A 282      48.859 -19.884 -10.101  1.00 36.17           O  
ATOM   2055  OE2 GLU A 282      50.451 -21.415 -10.366  1.00 38.68           O  
ATOM   2056  N   GLU A 283      47.888 -20.552  -5.019  1.00 23.93           N  
ATOM   2057  CA  GLU A 283      48.755 -20.246  -3.839  1.00 25.06           C  
ATOM   2058  C   GLU A 283      48.425 -21.153  -2.653  1.00 25.44           C  
ATOM   2059  O   GLU A 283      49.331 -21.625  -1.929  1.00 27.97           O  
ATOM   2060  CB  GLU A 283      48.543 -18.823  -3.413  1.00 26.49           C  
ATOM   2061  CG  GLU A 283      49.427 -17.855  -4.307  1.00 25.65           C  
ATOM   2062  CD  GLU A 283      49.152 -16.439  -3.969  1.00 32.85           C  
ATOM   2063  OE1 GLU A 283      48.000 -16.060  -3.713  1.00 27.11           O  
ATOM   2064  OE2 GLU A 283      50.131 -15.713  -3.910  1.00 32.72           O  
ATOM   2065  N   ILE A 284      47.160 -21.502  -2.509  1.00 22.66           N  
ATOM   2066  CA  ILE A 284      46.836 -22.479  -1.410  1.00 23.24           C  
ATOM   2067  C   ILE A 284      47.470 -23.818  -1.786  1.00 23.06           C  
ATOM   2068  O   ILE A 284      48.143 -24.386  -0.924  1.00 25.71           O  
ATOM   2069  CB  ILE A 284      45.351 -22.624  -1.208  1.00 21.07           C  
ATOM   2070  CG1 ILE A 284      44.725 -21.286  -0.729  1.00 23.60           C  
ATOM   2071  CG2 ILE A 284      44.955 -23.870  -0.238  1.00 22.09           C  
ATOM   2072  CD1 ILE A 284      43.165 -21.426  -0.796  1.00 22.89           C  
ATOM   2073  N   GLN A 285      47.277 -24.315  -3.029  1.00 22.98           N  
ATOM   2074  CA  GLN A 285      47.767 -25.694  -3.300  1.00 24.49           C  
ATOM   2075  C   GLN A 285      49.317 -25.785  -3.416  1.00 26.08           C  
ATOM   2076  O   GLN A 285      49.894 -26.855  -3.325  1.00 25.03           O  
ATOM   2077  CB  GLN A 285      47.041 -26.265  -4.516  1.00 25.05           C  
ATOM   2078  CG  GLN A 285      45.511 -26.461  -4.253  1.00 26.77           C  
ATOM   2079  CD  GLN A 285      44.931 -27.257  -5.389  1.00 26.70           C  
ATOM   2080  OE1 GLN A 285      44.848 -26.759  -6.494  1.00 27.34           O  
ATOM   2081  NE2 GLN A 285      44.623 -28.547  -5.148  1.00 25.02           N  
ATOM   2082  N   ASN A 286      49.971 -24.644  -3.592  1.00 25.87           N  
ATOM   2083  CA  ASN A 286      51.460 -24.585  -3.521  1.00 27.92           C  
ATOM   2084  C   ASN A 286      52.014 -24.288  -2.164  1.00 27.34           C  
ATOM   2085  O   ASN A 286      53.278 -24.261  -1.985  1.00 27.31           O  
ATOM   2086  CB  ASN A 286      51.998 -23.565  -4.531  1.00 28.00           C  
ATOM   2087  CG  ASN A 286      51.806 -24.057  -5.996  1.00 30.89           C  
ATOM   2088  OD1 ASN A 286      51.825 -25.241  -6.277  1.00 33.28           O  
ATOM   2089  ND2 ASN A 286      51.629 -23.172  -6.869  1.00 30.20           N  
ATOM   2090  N   HIS A 287      51.123 -24.105  -1.170  1.00 25.02           N  
ATOM   2091  CA  HIS A 287      51.609 -23.818   0.169  1.00 25.01           C  
ATOM   2092  C   HIS A 287      52.421 -24.970   0.741  1.00 26.14           C  
ATOM   2093  O   HIS A 287      52.083 -26.150   0.456  1.00 27.56           O  
ATOM   2094  CB  HIS A 287      50.437 -23.399   1.060  1.00 24.52           C  
ATOM   2095  CG  HIS A 287      50.849 -23.015   2.429  1.00 24.25           C  
ATOM   2096  ND1 HIS A 287      50.919 -21.700   2.860  1.00 26.11           N  
ATOM   2097  CD2 HIS A 287      51.182 -23.788   3.490  1.00 18.69           C  
ATOM   2098  CE1 HIS A 287      51.315 -21.667   4.124  1.00 20.62           C  
ATOM   2099  NE2 HIS A 287      51.501 -22.933   4.519  1.00 29.24           N  
ATOM   2100  N   PRO A 288      53.483 -24.692   1.503  1.00 27.53           N  
ATOM   2101  CA  PRO A 288      54.277 -25.815   2.069  1.00 29.17           C  
ATOM   2102  C   PRO A 288      53.351 -26.784   2.829  1.00 29.21           C  
ATOM   2103  O   PRO A 288      53.652 -27.990   2.856  1.00 27.89           O  
ATOM   2104  CB  PRO A 288      55.137 -25.128   3.115  1.00 30.22           C  
ATOM   2105  CG  PRO A 288      55.433 -23.764   2.476  1.00 31.64           C  
ATOM   2106  CD  PRO A 288      54.083 -23.395   1.828  1.00 29.06           C  
ATOM   2107  N   TRP A 289      52.270 -26.305   3.483  1.00 26.19           N  
ATOM   2108  CA  TRP A 289      51.508 -27.287   4.268  1.00 27.06           C  
ATOM   2109  C   TRP A 289      50.857 -28.324   3.373  1.00 26.07           C  
ATOM   2110  O   TRP A 289      50.528 -29.427   3.871  1.00 27.33           O  
ATOM   2111  CB  TRP A 289      50.458 -26.609   5.206  1.00 26.02           C  
ATOM   2112  CG  TRP A 289      49.791 -27.583   6.111  1.00 22.73           C  
ATOM   2113  CD1 TRP A 289      50.342 -28.210   7.195  1.00 24.11           C  
ATOM   2114  CD2 TRP A 289      48.459 -28.049   5.968  1.00 23.06           C  
ATOM   2115  NE1 TRP A 289      49.360 -29.067   7.798  1.00 25.38           N  
ATOM   2116  CE2 TRP A 289      48.220 -29.003   7.034  1.00 25.98           C  
ATOM   2117  CE3 TRP A 289      47.430 -27.749   5.056  1.00 24.74           C  
ATOM   2118  CZ2 TRP A 289      46.995 -29.681   7.177  1.00 27.44           C  
ATOM   2119  CZ3 TRP A 289      46.200 -28.420   5.175  1.00 24.50           C  
ATOM   2120  CH2 TRP A 289      46.007 -29.403   6.222  1.00 23.91           C  
ATOM   2121  N   MET A 290      50.610 -27.980   2.108  1.00 26.29           N  
ATOM   2122  CA  MET A 290      49.798 -28.781   1.184  1.00 27.55           C  
ATOM   2123  C   MET A 290      50.596 -29.878   0.431  1.00 30.72           C  
ATOM   2124  O   MET A 290      50.036 -30.540  -0.454  1.00 30.18           O  
ATOM   2125  CB  MET A 290      49.013 -27.962   0.172  1.00 24.10           C  
ATOM   2126  CG  MET A 290      47.916 -26.999   0.926  1.00 27.61           C  
ATOM   2127  SD  MET A 290      46.243 -27.671   0.719  1.00 33.24           S  
ATOM   2128  CE  MET A 290      46.430 -28.942   1.761  1.00 22.99           C  
ATOM   2129  N   GLN A 291      51.884 -30.053   0.759  1.00 31.04           N  
ATOM   2130  CA  GLN A 291      52.736 -30.850  -0.132  1.00 31.49           C  
ATOM   2131  C   GLN A 291      52.605 -32.309   0.326  1.00 32.36           C  
ATOM   2132  O   GLN A 291      52.216 -32.530   1.488  1.00 31.38           O  
ATOM   2133  CB  GLN A 291      54.174 -30.332  -0.013  1.00 32.80           C  
ATOM   2134  CG  GLN A 291      54.364 -28.841  -0.677  1.00 37.32           C  
ATOM   2135  CD  GLN A 291      53.459 -28.574  -1.986  1.00 47.80           C  
ATOM   2136  OE1 GLN A 291      53.715 -29.165  -3.048  1.00 49.95           O  
ATOM   2137  NE2 GLN A 291      52.381 -27.714  -1.874  1.00 42.93           N  
ATOM   2138  N   ASP A 292      52.803 -33.265  -0.603  1.00 31.67           N  
ATOM   2139  CA  ASP A 292      52.856 -34.667  -0.235  1.00 34.37           C  
ATOM   2140  C   ASP A 292      51.541 -35.174   0.268  1.00 33.05           C  
ATOM   2141  O   ASP A 292      51.517 -35.908   1.251  1.00 34.01           O  
ATOM   2142  CB  ASP A 292      53.856 -34.872   0.882  1.00 35.14           C  
ATOM   2143  CG  ASP A 292      55.307 -34.607   0.396  1.00 46.98           C  
ATOM   2144  OD1 ASP A 292      55.581 -34.789  -0.860  1.00 54.27           O  
ATOM   2145  OD2 ASP A 292      56.163 -34.183   1.239  1.00 56.06           O  
ATOM   2146  N   VAL A 293      50.460 -34.800  -0.410  1.00 30.23           N  
ATOM   2147  CA  VAL A 293      49.131 -35.168   0.061  1.00 28.74           C  
ATOM   2148  C   VAL A 293      48.982 -36.660  -0.217  1.00 28.48           C  
ATOM   2149  O   VAL A 293      49.526 -37.148  -1.199  1.00 27.02           O  
ATOM   2150  CB  VAL A 293      48.076 -34.421  -0.767  1.00 28.20           C  
ATOM   2151  CG1 VAL A 293      48.065 -34.921  -2.272  1.00 28.79           C  
ATOM   2152  CG2 VAL A 293      46.655 -34.559  -0.164  1.00 30.25           C  
ATOM   2153  N   LEU A 294      48.221 -37.356   0.625  1.00 29.33           N  
ATOM   2154  CA  LEU A 294      47.873 -38.745   0.419  1.00 29.62           C  
ATOM   2155  C   LEU A 294      46.904 -38.874  -0.766  1.00 30.64           C  
ATOM   2156  O   LEU A 294      46.034 -38.011  -0.992  1.00 29.76           O  
ATOM   2157  CB  LEU A 294      47.182 -39.367   1.623  1.00 25.65           C  
ATOM   2158  CG  LEU A 294      47.896 -39.541   2.966  1.00 26.87           C  
ATOM   2159  CD1 LEU A 294      46.978 -40.096   4.103  1.00 26.50           C  
ATOM   2160  CD2 LEU A 294      49.223 -40.380   2.713  1.00 29.88           C  
ATOM   2161  N   LEU A 295      46.949 -40.060  -1.398  1.00 28.96           N  
ATOM   2162  CA  LEU A 295      45.949 -40.363  -2.366  1.00 29.02           C  
ATOM   2163  C   LEU A 295      44.655 -40.716  -1.642  1.00 27.52           C  
ATOM   2164  O   LEU A 295      44.686 -41.136  -0.479  1.00 27.45           O  
ATOM   2165  CB  LEU A 295      46.390 -41.588  -3.233  1.00 32.63           C  
ATOM   2166  CG  LEU A 295      47.644 -41.494  -4.114  1.00 35.70           C  
ATOM   2167  CD1 LEU A 295      47.834 -42.849  -4.887  1.00 41.04           C  
ATOM   2168  CD2 LEU A 295      47.677 -40.362  -5.059  1.00 35.35           C  
ATOM   2169  N   PRO A 296      43.502 -40.578  -2.294  1.00 28.83           N  
ATOM   2170  CA  PRO A 296      42.262 -40.941  -1.519  1.00 29.41           C  
ATOM   2171  C   PRO A 296      42.264 -42.413  -0.952  1.00 34.26           C  
ATOM   2172  O   PRO A 296      41.956 -42.596   0.273  1.00 33.37           O  
ATOM   2173  CB  PRO A 296      41.179 -40.811  -2.550  1.00 30.24           C  
ATOM   2174  CG  PRO A 296      41.679 -39.684  -3.469  1.00 27.25           C  
ATOM   2175  CD  PRO A 296      43.174 -39.989  -3.632  1.00 28.92           C  
ATOM   2176  N   GLN A 297      42.632 -43.419  -1.805  1.00 34.44           N  
ATOM   2177  CA  GLN A 297      42.616 -44.801  -1.316  1.00 36.31           C  
ATOM   2178  C   GLN A 297      43.491 -44.962  -0.096  1.00 35.60           C  
ATOM   2179  O   GLN A 297      43.042 -45.643   0.868  1.00 37.62           O  
ATOM   2180  CB  GLN A 297      42.998 -45.886  -2.373  1.00 36.80           C  
ATOM   2181  CG  GLN A 297      42.474 -47.385  -1.935  1.00 40.17           C  
ATOM   2182  CD  GLN A 297      40.954 -47.381  -1.518  1.00 48.30           C  
ATOM   2183  OE1 GLN A 297      40.083 -47.036  -2.312  1.00 53.82           O  
ATOM   2184  NE2 GLN A 297      40.667 -47.742  -0.268  1.00 51.23           N  
ATOM   2185  N   GLU A 298      44.708 -44.388  -0.146  1.00 34.09           N  
ATOM   2186  CA  GLU A 298      45.639 -44.396   1.003  1.00 37.30           C  
ATOM   2187  C   GLU A 298      45.003 -43.715   2.219  1.00 35.19           C  
ATOM   2188  O   GLU A 298      45.159 -44.159   3.399  1.00 35.28           O  
ATOM   2189  CB  GLU A 298      46.944 -43.650   0.771  1.00 36.82           C  
ATOM   2190  CG  GLU A 298      47.732 -43.864  -0.479  1.00 41.71           C  
ATOM   2191  CD  GLU A 298      48.900 -42.829  -0.502  1.00 44.09           C  
ATOM   2192  OE1 GLU A 298      49.910 -43.058   0.180  1.00 61.60           O  
ATOM   2193  OE2 GLU A 298      48.852 -41.764  -1.124  1.00 42.45           O  
ATOM   2194  N   THR A 299      44.278 -42.632   1.943  1.00 31.23           N  
ATOM   2195  CA  THR A 299      43.566 -41.960   3.001  1.00 29.91           C  
ATOM   2196  C   THR A 299      42.533 -42.880   3.660  1.00 30.13           C  
ATOM   2197  O   THR A 299      42.404 -42.955   4.906  1.00 29.69           O  
ATOM   2198  CB  THR A 299      42.893 -40.620   2.439  1.00 29.25           C  
ATOM   2199  OG1 THR A 299      43.916 -39.775   1.830  1.00 29.26           O  
ATOM   2200  CG2 THR A 299      42.223 -39.900   3.637  1.00 30.72           C  
ATOM   2201  N   ALA A 300      41.819 -43.623   2.840  1.00 31.42           N  
ATOM   2202  CA  ALA A 300      40.786 -44.545   3.394  1.00 33.24           C  
ATOM   2203  C   ALA A 300      41.465 -45.670   4.271  1.00 35.52           C  
ATOM   2204  O   ALA A 300      41.019 -46.014   5.385  1.00 35.82           O  
ATOM   2205  CB  ALA A 300      40.003 -45.147   2.276  1.00 33.58           C  
ATOM   2206  N   GLU A 301      42.543 -46.211   3.724  1.00 36.21           N  
ATOM   2207  CA  GLU A 301      43.263 -47.285   4.366  1.00 39.75           C  
ATOM   2208  C   GLU A 301      43.873 -46.873   5.703  1.00 39.64           C  
ATOM   2209  O   GLU A 301      43.697 -47.602   6.687  1.00 40.16           O  
ATOM   2210  CB  GLU A 301      44.315 -47.848   3.439  1.00 39.93           C  
ATOM   2211  CG  GLU A 301      43.670 -48.689   2.342  1.00 47.86           C  
ATOM   2212  CD  GLU A 301      44.672 -49.005   1.228  1.00 60.63           C  
ATOM   2213  OE1 GLU A 301      45.847 -48.521   1.333  1.00 63.40           O  
ATOM   2214  OE2 GLU A 301      44.274 -49.707   0.245  1.00 64.67           O  
ATOM   2215  N   ILE A 302      44.557 -45.723   5.747  1.00 37.07           N  
ATOM   2216  CA  ILE A 302      45.143 -45.260   6.979  1.00 37.90           C  
ATOM   2217  C   ILE A 302      44.147 -44.709   7.986  1.00 38.64           C  
ATOM   2218  O   ILE A 302      44.263 -44.963   9.182  1.00 39.52           O  
ATOM   2219  CB  ILE A 302      46.214 -44.223   6.657  1.00 38.45           C  
ATOM   2220  CG1 ILE A 302      47.184 -44.814   5.580  1.00 38.77           C  
ATOM   2221  CG2 ILE A 302      46.829 -43.690   7.963  1.00 40.86           C  
ATOM   2222  CD1 ILE A 302      48.292 -43.892   5.066  1.00 39.14           C  
ATOM   2223  N   HIS A 303      43.165 -43.929   7.530  1.00 37.64           N  
ATOM   2224  CA  HIS A 303      42.389 -43.118   8.450  1.00 36.71           C  
ATOM   2225  C   HIS A 303      40.952 -43.529   8.536  1.00 36.75           C  
ATOM   2226  O   HIS A 303      40.244 -43.190   9.527  1.00 37.96           O  
ATOM   2227  CB  HIS A 303      42.482 -41.645   7.995  1.00 33.44           C  
ATOM   2228  CG  HIS A 303      43.837 -41.057   8.219  1.00 30.15           C  
ATOM   2229  ND1 HIS A 303      44.272 -40.696   9.468  1.00 30.67           N  
ATOM   2230  CD2 HIS A 303      44.840 -40.769   7.366  1.00 29.44           C  
ATOM   2231  CE1 HIS A 303      45.514 -40.231   9.395  1.00 29.22           C  
ATOM   2232  NE2 HIS A 303      45.874 -40.230   8.111  1.00 30.29           N  
ATOM   2233  N   LEU A 304      40.440 -44.182   7.506  1.00 38.92           N  
ATOM   2234  CA  LEU A 304      39.007 -44.457   7.539  1.00 41.57           C  
ATOM   2235  C   LEU A 304      38.720 -45.951   7.746  1.00 48.74           C  
ATOM   2236  O   LEU A 304      37.572 -46.315   7.944  1.00 48.50           O  
ATOM   2237  CB  LEU A 304      38.250 -43.900   6.319  1.00 40.49           C  
ATOM   2238  CG  LEU A 304      38.572 -42.444   5.897  1.00 33.49           C  
ATOM   2239  CD1 LEU A 304      37.892 -42.158   4.491  1.00 33.84           C  
ATOM   2240  CD2 LEU A 304      38.042 -41.589   6.955  1.00 35.37           C  
ATOM   2241  N   HIS A 305      39.799 -46.734   7.793  1.00 53.89           N  
ATOM   2242  C   HIS A 305      38.853 -48.829   6.839  1.00 59.44           C  
ATOM   2243  O   HIS A 305      37.872 -49.541   7.200  1.00 61.16           O  
ATOM   2244  CA AHIS A 305      39.787 -48.210   7.873  0.50 57.47           C  
ATOM   2245  CB AHIS A 305      39.549 -48.759   9.305  0.50 57.64           C  
ATOM   2246  CG AHIS A 305      38.329 -48.224   9.977  0.50 58.55           C  
ATOM   2247  ND1AHIS A 305      37.088 -48.798   9.824  0.50 60.58           N  
ATOM   2248  CD2AHIS A 305      38.160 -47.172  10.816  0.50 60.77           C  
ATOM   2249  CE1AHIS A 305      36.200 -48.119  10.537  0.50 62.17           C  
ATOM   2250  NE2AHIS A 305      36.825 -47.125  11.146  0.50 63.17           N  
ATOM   2251  CA BHIS A 305      39.771 -48.198   7.896  0.50 57.68           C  
ATOM   2252  CB BHIS A 305      39.490 -48.639   9.356  0.50 57.96           C  
ATOM   2253  CG BHIS A 305      40.477 -48.065  10.330  0.50 59.95           C  
ATOM   2254  ND1BHIS A 305      41.723 -48.622  10.544  0.50 61.26           N  
ATOM   2255  CD2BHIS A 305      40.435 -46.938  11.080  0.50 62.19           C  
ATOM   2256  CE1BHIS A 305      42.391 -47.879  11.406  0.50 63.36           C  
ATOM   2257  NE2BHIS A 305      41.636 -46.847  11.742  0.50 64.64           N  
ATOM   2258  N   SER A 306      39.201 -48.573   5.554  1.00 60.65           N  
ATOM   2259  CA  SER A 306      38.369 -48.806   4.327  1.00 62.85           C  
ATOM   2260  C   SER A 306      39.236 -48.918   3.093  1.00 62.25           C  
ATOM   2261  O   SER A 306      40.459 -48.927   3.222  1.00 63.29           O  
ATOM   2262  CB  SER A 306      37.406 -47.635   4.052  1.00 62.59           C  
ATOM   2263  OG  SER A 306      36.600 -47.267   5.189  1.00 67.72           O  
TER    2264      SER A 306                                                      
HETATM 2265  N1  IMD A1307      31.859 -30.260  13.196  1.00 44.91           N  
HETATM 2266  C2  IMD A1307      32.442 -29.210  13.758  1.00 42.62           C  
HETATM 2267  N3  IMD A1307      32.238 -29.353  15.085  1.00 42.76           N  
HETATM 2268  C4  IMD A1307      31.516 -30.469  15.340  1.00 39.06           C  
HETATM 2269  C5  IMD A1307      31.245 -31.044  14.112  1.00 44.28           C  
HETATM 2270  C5  HY7 A1308      21.011 -29.247   2.375  1.00 32.86           C  
HETATM 2271  C6  HY7 A1308      21.502 -27.932   3.082  1.00 33.65           C  
HETATM 2272  N3  HY7 A1308      22.942 -28.128   3.429  1.00 29.60           N  
HETATM 2273  C7  HY7 A1308      23.487 -26.997   4.252  1.00 34.50           C  
HETATM 2274  C8  HY7 A1308      23.248 -29.318   4.280  1.00 29.19           C  
HETATM 2275  C9  HY7 A1308      22.876 -30.571   3.458  1.00 29.72           C  
HETATM 2276  N2  HY7 A1308      21.406 -30.422   3.159  1.00 30.89           N  
HETATM 2277  C4  HY7 A1308      20.831 -31.658   2.600  1.00 31.48           C  
HETATM 2278  C3  HY7 A1308      21.450 -32.287   1.392  1.00 27.84           C  
HETATM 2279  N4  HY7 A1308      21.817 -33.527   1.423  1.00 29.98           N  
HETATM 2280  C10 HY7 A1308      22.304 -34.156   0.307  1.00 25.66           C  
HETATM 2281  C11 HY7 A1308      22.794 -35.432   0.041  1.00 27.76           C  
HETATM 2282  C12 HY7 A1308      22.893 -36.578   0.817  1.00 29.77           C  
HETATM 2283  C13 HY7 A1308      23.435 -37.635   0.123  1.00 30.61           C  
HETATM 2284 BR1  HY7 A1308      23.732 -39.255   1.085  1.00 44.83          BR  
HETATM 2285  C14 HY7 A1308      23.841 -37.673  -1.244  1.00 27.22           C  
HETATM 2286  C15 HY7 A1308      23.713 -36.510  -2.002  1.00 28.95           C  
HETATM 2287  C16 HY7 A1308      23.172 -35.457  -1.301  1.00 28.95           C  
HETATM 2288  O2  HY7 A1308      22.949 -34.208  -1.763  1.00 29.50           O  
HETATM 2289  C1  HY7 A1308      22.373 -33.434  -0.866  1.00 28.37           C  
HETATM 2290  C2  HY7 A1308      22.012 -32.073  -0.900  1.00 29.57           C  
HETATM 2291  O1  HY7 A1308      22.109 -31.353  -1.906  1.00 31.12           O  
HETATM 2292  N1  HY7 A1308      21.456 -31.581   0.237  1.00 27.98           N  
HETATM 2293  N1  IMD A1309      37.488 -12.588  -5.602  1.00 29.42           N  
HETATM 2294  C2  IMD A1309      37.759 -11.978  -4.461  1.00 39.74           C  
HETATM 2295  N3  IMD A1309      38.504 -10.888  -4.620  1.00 35.95           N  
HETATM 2296  C4  IMD A1309      38.757 -10.844  -5.994  1.00 43.18           C  
HETATM 2297  C5  IMD A1309      38.085 -11.867  -6.597  1.00 44.12           C  
HETATM 2298  O   HOH A2001       5.666 -41.010  -6.898  1.00 77.98           O  
HETATM 2299  O   HOH A2002       5.446 -38.917  -7.881  1.00 71.95           O  
HETATM 2300  O   HOH A2003       7.511 -45.949  -6.622  1.00 70.31           O  
HETATM 2301  O   HOH A2004       6.244 -36.486  -8.673  1.00 73.72           O  
HETATM 2302  O   HOH A2005      14.744 -45.152 -13.429  1.00 67.31           O  
HETATM 2303  O   HOH A2006      14.612 -40.465 -12.641  1.00 64.22           O  
HETATM 2304  O   HOH A2007      14.976 -47.147  -0.028  1.00 54.74           O  
HETATM 2305  O   HOH A2008       8.533 -45.432  -2.086  1.00 61.98           O  
HETATM 2306  O   HOH A2009      12.556 -41.461   7.872  1.00 38.15           O  
HETATM 2307  O   HOH A2010      16.853 -38.406   9.592  1.00 50.98           O  
HETATM 2308  O   HOH A2011      18.539 -41.590   8.334  1.00 59.14           O  
HETATM 2309  O   HOH A2012      22.073 -37.871   7.834  1.00 55.19           O  
HETATM 2310  O   HOH A2013      15.360 -33.975   9.949  1.00 43.58           O  
HETATM 2311  O   HOH A2014      19.132 -32.483   8.977  1.00 47.38           O  
HETATM 2312  O   HOH A2015      16.246 -28.562  10.484  1.00 64.20           O  
HETATM 2313  O   HOH A2016      19.916 -29.131   6.527  1.00 55.51           O  
HETATM 2314  O   HOH A2017       2.815 -43.338  -6.625  1.00 50.55           O  
HETATM 2315  O   HOH A2018      12.287 -28.064   6.235  1.00 65.24           O  
HETATM 2316  O   HOH A2019      14.458 -24.300   8.989  1.00 68.66           O  
HETATM 2317  O   HOH A2020      18.717 -25.153   4.160  1.00 46.43           O  
HETATM 2318  O   HOH A2021      18.224 -24.883   7.872  1.00 61.37           O  
HETATM 2319  O   HOH A2022      16.417 -22.187   1.954  1.00 66.62           O  
HETATM 2320  O   HOH A2023      14.172 -24.327  -1.048  1.00 36.00           O  
HETATM 2321  O   HOH A2024      11.295 -29.648   4.473  1.00 37.52           O  
HETATM 2322  O   HOH A2025      24.090 -39.409   6.080  1.00 56.67           O  
HETATM 2323  O   HOH A2026      23.335 -37.109   5.107  1.00 54.79           O  
HETATM 2324  O   HOH A2027      13.474 -35.312  11.581  1.00 34.94           O  
HETATM 2325  O   HOH A2028      22.261 -34.080   9.433  1.00 65.37           O  
HETATM 2326  O   HOH A2029      21.154 -33.328   6.071  1.00 49.39           O  
HETATM 2327  O   HOH A2030      20.078 -26.513   6.218  1.00 48.42           O  
HETATM 2328  O   HOH A2031      20.247 -24.375   1.779  1.00 43.51           O  
HETATM 2329  O   HOH A2032      16.608 -24.009  -1.892  1.00 44.44           O  
HETATM 2330  O   HOH A2033      17.233 -46.315   1.062  1.00 44.40           O  
HETATM 2331  O   HOH A2034      20.998 -44.251   3.584  1.00 44.90           O  
HETATM 2332  O   HOH A2035      22.988 -42.266   3.277  1.00 38.36           O  
HETATM 2333  O   HOH A2036      23.044 -43.609 -13.993  1.00 54.83           O  
HETATM 2334  O   HOH A2037      21.767 -41.765 -14.437  1.00 57.37           O  
HETATM 2335  O   HOH A2038      25.402 -42.311  -9.535  1.00 55.93           O  
HETATM 2336  O   HOH A2039      21.138 -50.302  -3.557  1.00 52.36           O  
HETATM 2337  O   HOH A2040      24.116 -50.936  -6.521  1.00 65.40           O  
HETATM 2338  O   HOH A2041      24.623 -43.211  -6.748  1.00 38.67           O  
HETATM 2339  O   HOH A2042      19.986 -26.425   0.077  1.00 31.43           O  
HETATM 2340  O   HOH A2043      18.002 -26.538  -1.863  1.00 32.13           O  
HETATM 2341  O   HOH A2044       8.007 -32.804  -2.953  1.00 42.87           O  
HETATM 2342  O   HOH A2045      11.062 -38.972  -1.086  1.00 44.53           O  
HETATM 2343  O   HOH A2046      33.347 -30.974 -16.608  1.00 55.33           O  
HETATM 2344  O   HOH A2047       6.749 -24.445  -1.782  1.00 57.35           O  
HETATM 2345  O   HOH A2048       5.810 -29.663  -1.142  1.00 51.24           O  
HETATM 2346  O   HOH A2049      35.751 -36.286 -16.172  1.00 53.12           O  
HETATM 2347  O   HOH A2050      11.462 -18.918  -4.319  1.00 66.32           O  
HETATM 2348  O   HOH A2051       4.766 -22.579  -3.994  1.00 66.59           O  
HETATM 2349  O   HOH A2052       7.056 -21.959   2.471  1.00 66.18           O  
HETATM 2350  O   HOH A2053      17.708 -21.502  -2.266  1.00 52.49           O  
HETATM 2351  O   HOH A2054      11.398 -24.660   6.701  1.00 70.25           O  
HETATM 2352  O   HOH A2055       7.824 -27.048   4.387  1.00 66.34           O  
HETATM 2353  O   HOH A2056      20.920 -18.785  -4.496  1.00 55.33           O  
HETATM 2354  O   HOH A2057      21.183 -17.978  -1.937  1.00 69.68           O  
HETATM 2355  O   HOH A2058      19.661 -20.291  -0.588  1.00 51.39           O  
HETATM 2356  O   HOH A2059      18.244 -22.808  -6.232  1.00 50.67           O  
HETATM 2357  O   HOH A2060      22.074 -17.159  -7.499  1.00 61.17           O  
HETATM 2358  O   HOH A2061      27.326 -51.205   1.138  1.00 70.37           O  
HETATM 2359  O   HOH A2062      24.043 -41.926   5.941  1.00 57.64           O  
HETATM 2360  O   HOH A2063      13.541 -18.512 -14.796  1.00 74.96           O  
HETATM 2361  O   HOH A2064      24.830 -38.063   5.186  1.00 62.41           O  
HETATM 2362  O   HOH A2065      20.345 -19.324 -15.668  1.00 58.59           O  
HETATM 2363  O   HOH A2066      20.493 -23.024 -18.398  1.00 68.91           O  
HETATM 2364  O   HOH A2067      17.930 -27.623 -21.282  1.00 77.30           O  
HETATM 2365  O   HOH A2068      12.492 -24.612 -22.856  1.00 68.32           O  
HETATM 2366  O   HOH A2069      10.739 -22.151 -18.735  1.00 63.67           O  
HETATM 2367  O   HOH A2070       8.526 -23.005 -12.287  1.00 61.14           O  
HETATM 2368  O   HOH A2071      13.814 -16.586 -13.038  1.00 65.42           O  
HETATM 2369  O   HOH A2072      40.584 -34.949  -6.263  1.00 42.43           O  
HETATM 2370  O   HOH A2073      35.907 -29.710 -16.750  1.00 47.21           O  
HETATM 2371  O   HOH A2074      21.321 -21.780  -5.833  1.00 46.96           O  
HETATM 2372  O   HOH A2075      17.272 -24.698  -4.839  1.00 49.46           O  
HETATM 2373  O   HOH A2076      22.645 -29.179  -4.986  1.00 28.91           O  
HETATM 2374  O   HOH A2077      41.948 -21.711 -14.588  1.00 46.96           O  
HETATM 2375  O   HOH A2078      40.345 -25.986 -20.882  1.00 55.08           O  
HETATM 2376  O   HOH A2079      22.931 -25.613 -16.605  1.00 47.48           O  
HETATM 2377  O   HOH A2080      30.159 -16.707  -0.527  1.00 32.68           O  
HETATM 2378  O   HOH A2081      26.081 -32.618 -11.130  1.00 45.21           O  
HETATM 2379  O   HOH A2082      16.949 -31.283 -17.670  1.00 51.48           O  
HETATM 2380  O   HOH A2083      30.503 -26.440  13.465  1.00 53.71           O  
HETATM 2381  O   HOH A2084      19.928 -34.230 -14.986  1.00 53.32           O  
HETATM 2382  O   HOH A2085      24.502 -27.016 -18.035  1.00 56.59           O  
HETATM 2383  O   HOH A2086      30.765 -30.096 -16.107  1.00 51.33           O  
HETATM 2384  O   HOH A2087      29.654 -26.123 -17.622  1.00 48.22           O  
HETATM 2385  O   HOH A2088      30.320 -21.037 -17.506  1.00 47.87           O  
HETATM 2386  O   HOH A2089      31.879 -33.459 -11.761  1.00 46.99           O  
HETATM 2387  O   HOH A2090      29.292 -33.994 -11.038  1.00 50.45           O  
HETATM 2388  O   HOH A2091      30.710 -38.006 -11.319  1.00 68.99           O  
HETATM 2389  O   HOH A2092      35.547 -33.721 -14.825  1.00 54.04           O  
HETATM 2390  O   HOH A2093      33.027 -36.149 -17.057  1.00 65.90           O  
HETATM 2391  O   HOH A2094      31.697 -40.205 -10.698  1.00 59.10           O  
HETATM 2392  O   HOH A2095      30.475 -37.526  -8.500  1.00 38.21           O  
HETATM 2393  O   HOH A2096      37.178 -37.514  -6.528  1.00 46.50           O  
HETATM 2394  O   HOH A2097      21.818 -16.011 -12.438  1.00 56.09           O  
HETATM 2395  O   HOH A2098      25.997 -13.672 -13.136  1.00 47.99           O  
HETATM 2396  O   HOH A2099      31.107 -13.628 -15.992  1.00 52.36           O  
HETATM 2397  O   HOH A2100      38.888 -15.259 -16.010  1.00 52.29           O  
HETATM 2398  O   HOH A2101      39.381 -11.467 -17.803  1.00 58.55           O  
HETATM 2399  O   HOH A2102      24.312 -37.183 -14.191  1.00 57.17           O  
HETATM 2400  O   HOH A2103      13.564 -33.653 -16.394  1.00 68.45           O  
HETATM 2401  O   HOH A2104      11.338 -33.179 -15.422  1.00 58.91           O  
HETATM 2402  O   HOH A2105       9.297 -31.939 -14.260  1.00 62.51           O  
HETATM 2403  O   HOH A2106       9.048 -29.012 -15.390  1.00 67.20           O  
HETATM 2404  O   HOH A2107       3.688 -29.483 -11.395  1.00 63.72           O  
HETATM 2405  O   HOH A2108       1.627 -28.747  -4.197  1.00 69.69           O  
HETATM 2406  O   HOH A2109       5.097 -30.136  -3.924  1.00 52.92           O  
HETATM 2407  O   HOH A2110      33.971 -19.249  19.635  1.00 53.84           O  
HETATM 2408  O   HOH A2111      38.795 -17.300  20.194  1.00 43.86           O  
HETATM 2409  O   HOH A2112      27.315 -40.955  -9.845  1.00 57.97           O  
HETATM 2410  O   HOH A2113      28.913 -42.122  -5.435  1.00 48.55           O  
HETATM 2411  O   HOH A2114      31.292 -40.723  -8.089  1.00 48.09           O  
HETATM 2412  O   HOH A2115      25.654 -14.454  17.400  1.00 62.06           O  
HETATM 2413  O   HOH A2116      32.599  -5.169  16.289  1.00 56.24           O  
HETATM 2414  O   HOH A2117      36.955  -5.351  15.472  1.00 50.65           O  
HETATM 2415  O   HOH A2118      26.657 -46.174  -4.197  1.00 52.18           O  
HETATM 2416  O   HOH A2119      26.792 -44.505  -5.705  1.00 47.40           O  
HETATM 2417  O   HOH A2120      23.438 -48.562   0.401  1.00 65.04           O  
HETATM 2418  O   HOH A2121      24.598 -44.108   1.669  1.00 35.37           O  
HETATM 2419  O   HOH A2122      20.954 -48.621  -0.692  1.00 65.40           O  
HETATM 2420  O   HOH A2123      38.250  -4.958  13.849  1.00 55.05           O  
HETATM 2421  O   HOH A2124      45.956 -12.800  12.011  1.00 50.23           O  
HETATM 2422  O   HOH A2125      29.880 -45.844  -2.779  1.00 41.40           O  
HETATM 2423  O   HOH A2126      29.447 -50.833   0.251  1.00 74.60           O  
HETATM 2424  O   HOH A2127      31.776 -45.795   0.567  1.00 38.84           O  
HETATM 2425  O   HOH A2128      26.050 -44.834   5.033  1.00 40.56           O  
HETATM 2426  O   HOH A2129      25.934 -41.026   8.428  1.00 65.19           O  
HETATM 2427  O   HOH A2130      28.120 -43.673   8.464  1.00 57.07           O  
HETATM 2428  O   HOH A2131      26.936 -39.867  11.297  1.00 55.64           O  
HETATM 2429  O   HOH A2132      50.239 -14.535   5.515  1.00 60.08           O  
HETATM 2430  O   HOH A2133      53.463 -16.855   1.556  1.00 57.17           O  
HETATM 2431  O   HOH A2134      26.526 -38.122   7.995  1.00 35.14           O  
HETATM 2432  O   HOH A2135      25.287 -33.274   9.510  1.00 44.16           O  
HETATM 2433  O   HOH A2136      23.850 -35.802   8.037  1.00 56.51           O  
HETATM 2434  O   HOH A2137      24.967 -33.043   5.260  1.00 37.08           O  
HETATM 2435  O   HOH A2138      45.653 -10.119   7.258  1.00 45.97           O  
HETATM 2436  O   HOH A2139      27.198 -34.760  14.252  1.00 53.48           O  
HETATM 2437  O   HOH A2140      23.335 -36.689  10.164  1.00 53.94           O  
HETATM 2438  O   HOH A2141      40.860 -15.260  -5.678  1.00 44.83           O  
HETATM 2439  O   HOH A2142      28.405 -31.433  16.947  1.00 56.24           O  
HETATM 2440  O   HOH A2143      52.883 -19.637  -4.095  1.00 42.40           O  
HETATM 2441  O   HOH A2144      53.448 -19.845   0.582  1.00 48.29           O  
HETATM 2442  O   HOH A2145      53.956 -16.475  -1.027  1.00 67.13           O  
HETATM 2443  O   HOH A2146      35.859 -37.634  19.772  1.00 63.39           O  
HETATM 2444  O   HOH A2147      35.083 -42.637  14.509  1.00 64.77           O  
HETATM 2445  O   HOH A2148      40.607 -35.842  17.719  1.00 46.13           O  
HETATM 2446  O   HOH A2149      41.035 -37.683  14.871  1.00 50.60           O  
HETATM 2447  O   HOH A2150      42.786 -40.342  11.875  1.00 43.69           O  
HETATM 2448  O   HOH A2151      39.185 -32.775  19.142  1.00 46.42           O  
HETATM 2449  O   HOH A2152      44.409 -34.892  16.323  1.00 53.13           O  
HETATM 2450  O   HOH A2153      44.555 -31.377  14.448  1.00 37.22           O  
HETATM 2451  O   HOH A2154      42.173 -37.810  12.828  1.00 31.83           O  
HETATM 2452  O   HOH A2155      47.593 -42.088  12.160  1.00 58.76           O  
HETATM 2453  O   HOH A2156      43.301 -42.359  13.364  1.00 56.42           O  
HETATM 2454  O   HOH A2157      45.767 -43.292  12.447  1.00 58.33           O  
HETATM 2455  O   HOH A2158      49.381 -35.936  10.773  1.00 32.39           O  
HETATM 2456  O   HOH A2159      48.061 -33.493  13.698  1.00 30.94           O  
HETATM 2457  O   HOH A2160      51.921 -31.139   9.652  1.00 51.55           O  
HETATM 2458  O   HOH A2161      47.193 -31.361  14.670  1.00 44.37           O  
HETATM 2459  O   HOH A2162      49.778 -30.838  15.040  1.00 46.44           O  
HETATM 2460  O   HOH A2163      47.742 -36.019   3.216  1.00 25.53           O  
HETATM 2461  O   HOH A2164      51.226 -41.965   6.094  1.00 55.27           O  
HETATM 2462  O   HOH A2165      49.299 -41.777   9.911  1.00 61.06           O  
HETATM 2463  O   HOH A2166      51.648 -38.063   5.016  1.00 40.89           O  
HETATM 2464  O   HOH A2167      53.513 -31.874   4.145  1.00 47.92           O  
HETATM 2465  O   HOH A2168      50.459 -36.121   3.616  1.00 26.29           O  
HETATM 2466  O   HOH A2169      51.663 -34.692   8.299  1.00 44.28           O  
HETATM 2467  O   HOH A2170      43.378 -37.027  -1.064  1.00 33.87           O  
HETATM 2468  O   HOH A2171      38.288 -33.770  -5.183  1.00 25.48           O  
HETATM 2469  O   HOH A2172      37.147 -36.178  -4.121  1.00 28.14           O  
HETATM 2470  O   HOH A2173      40.073 -29.731 -10.212  1.00 30.60           O  
HETATM 2471  O   HOH A2174      39.467 -23.018 -11.026  1.00 36.14           O  
HETATM 2472  O   HOH A2175      41.751 -23.452 -10.716  1.00 31.79           O  
HETATM 2473  O   HOH A2176      37.003 -28.803 -14.348  1.00 44.44           O  
HETATM 2474  O   HOH A2177      35.460 -19.659 -14.773  1.00 48.47           O  
HETATM 2475  O   HOH A2178      38.115 -18.745  -9.633  1.00 64.61           O  
HETATM 2476  O   HOH A2179      32.767 -21.764  -4.691  1.00 25.66           O  
HETATM 2477  O   HOH A2180      32.674 -22.141 -17.712  1.00 59.67           O  
HETATM 2478  O   HOH A2181      39.497 -22.100 -14.441  1.00 46.49           O  
HETATM 2479  O   HOH A2182      39.840 -27.940 -12.077  1.00 33.57           O  
HETATM 2480  O   HOH A2183      38.957 -26.208 -18.655  1.00 55.73           O  
HETATM 2481  O   HOH A2184      28.878 -18.906 -15.071  1.00 41.77           O  
HETATM 2482  O   HOH A2185      25.251 -23.765  -2.144  1.00 28.66           O  
HETATM 2483  O   HOH A2186      31.859 -20.327  -2.481  1.00 27.58           O  
HETATM 2484  O   HOH A2187      28.748 -19.483   3.486  1.00 33.19           O  
HETATM 2485  O   HOH A2188      30.671 -18.508   1.464  1.00 32.47           O  
HETATM 2486  O   HOH A2189      23.686 -17.322  -1.268  1.00 31.94           O  
HETATM 2487  O   HOH A2190      23.942 -13.930  -6.848  1.00 57.35           O  
HETATM 2488  O   HOH A2191      21.257 -15.470  -2.126  1.00 49.97           O  
HETATM 2489  O   HOH A2192      31.747 -20.821   0.356  1.00 24.18           O  
HETATM 2490  O   HOH A2193      29.342 -21.934   4.335  1.00 25.70           O  
HETATM 2491  O   HOH A2194      22.490 -22.234   5.048  1.00 59.50           O  
HETATM 2492  O   HOH A2195      23.145 -24.211   1.094  1.00 32.70           O  
HETATM 2493  O   HOH A2196      23.549 -23.971   5.210  1.00 39.57           O  
HETATM 2494  O   HOH A2197      25.861 -24.239  10.089  1.00 61.71           O  
HETATM 2495  O   HOH A2198      23.325 -23.410   9.419  1.00 65.46           O  
HETATM 2496  O   HOH A2199      30.635 -26.172  10.769  1.00 42.98           O  
HETATM 2497  O   HOH A2200      22.377 -26.052   7.932  1.00 58.35           O  
HETATM 2498  O   HOH A2201      32.094 -46.635  -2.411  1.00 52.84           O  
HETATM 2499  O   HOH A2202      33.303 -41.134  -4.980  1.00 39.43           O  
HETATM 2500  O   HOH A2203      37.113 -50.323   1.123  1.00 69.87           O  
HETATM 2501  O   HOH A2204      31.706 -51.308   2.841  1.00 68.46           O  
HETATM 2502  O   HOH A2205      34.272 -48.306   5.097  1.00 60.61           O  
HETATM 2503  O   HOH A2206      39.458 -43.713  -4.346  1.00 37.53           O  
HETATM 2504  O   HOH A2207      31.326 -46.661  -6.084  1.00 61.90           O  
HETATM 2505  O   HOH A2208      38.913 -46.222  -4.763  1.00 39.01           O  
HETATM 2506  O   HOH A2209      39.333 -48.392  -8.039  1.00 48.64           O  
HETATM 2507  O   HOH A2210      36.814 -49.381  -8.160  1.00 54.92           O  
HETATM 2508  O   HOH A2211      35.447 -49.593  -3.024  1.00 64.66           O  
HETATM 2509  O   HOH A2212      39.959 -40.266  -6.818  1.00 33.07           O  
HETATM 2510  O   HOH A2213      23.520 -31.547  -4.026  1.00 35.21           O  
HETATM 2511  O   HOH A2214      20.726 -20.812   1.149  1.00 45.28           O  
HETATM 2512  O   HOH A2215      23.595 -16.566 -10.346  1.00 31.53           O  
HETATM 2513  O   HOH A2216      25.900 -14.686 -10.566  1.00 38.00           O  
HETATM 2514  O   HOH A2217      28.655 -14.785 -14.871  1.00 47.87           O  
HETATM 2515  O   HOH A2218      33.107 -11.943  -7.951  1.00 25.17           O  
HETATM 2516  O   HOH A2219      24.898 -12.474  -9.083  1.00 44.60           O  
HETATM 2517  O   HOH A2220      24.615 -10.014  -6.301  1.00 45.64           O  
HETATM 2518  O   HOH A2221      31.514 -11.026 -14.563  1.00 37.52           O  
HETATM 2519  O   HOH A2222      33.786 -15.489 -14.261  1.00 55.21           O  
HETATM 2520  O   HOH A2223      38.745 -12.098 -13.095  1.00 64.47           O  
HETATM 2521  O   HOH A2224      36.758 -13.822 -16.303  1.00 55.41           O  
HETATM 2522  O   HOH A2225      20.904 -11.566   0.410  1.00 40.70           O  
HETATM 2523  O   HOH A2226      23.562 -15.979   6.159  1.00 43.35           O  
HETATM 2524  O   HOH A2227      23.692 -18.456   8.695  1.00 41.43           O  
HETATM 2525  O   HOH A2228      25.789 -18.960  10.748  1.00 33.91           O  
HETATM 2526  O   HOH A2229      24.255 -13.641   6.582  1.00 34.81           O  
HETATM 2527  O   HOH A2230      23.066  -9.203   7.332  1.00 55.99           O  
HETATM 2528  O   HOH A2231      25.760  -7.729   8.335  1.00 46.06           O  
HETATM 2529  O   HOH A2232      33.546 -19.333  12.098  1.00 26.17           O  
HETATM 2530  O   HOH A2233      33.366 -16.277   9.089  1.00 27.55           O  
HETATM 2531  O   HOH A2234      32.482 -16.914   2.681  1.00 31.89           O  
HETATM 2532  O   HOH A2235      37.098  -7.452   4.513  1.00 43.39           O  
HETATM 2533  O   HOH A2236      35.512 -10.488  -1.258  1.00 27.84           O  
HETATM 2534  O   HOH A2237      29.505  -4.183  11.248  1.00 61.63           O  
HETATM 2535  O   HOH A2238      25.793  -3.096   5.066  1.00 61.61           O  
HETATM 2536  O   HOH A2239      30.011  -0.439   7.907  1.00 57.12           O  
HETATM 2537  O   HOH A2240      32.172  -1.215   8.919  1.00 68.49           O  
HETATM 2538  O   HOH A2241      25.462  -4.390  -0.603  1.00 46.67           O  
HETATM 2539  O   HOH A2242      27.968  -1.376   1.501  1.00 58.80           O  
HETATM 2540  O   HOH A2243      25.034  -4.465   6.304  1.00 68.22           O  
HETATM 2541  O   HOH A2244      33.641  -6.144  -0.733  1.00 44.89           O  
HETATM 2542  O   HOH A2245      32.882  -3.721  -1.600  1.00 49.50           O  
HETATM 2543  O   HOH A2246      30.303  -0.763   0.603  1.00 63.60           O  
HETATM 2544  O   HOH A2247      26.182  -2.857  -2.193  1.00 57.37           O  
HETATM 2545  O   HOH A2248      35.589  -7.778  -2.204  1.00 28.14           O  
HETATM 2546  O   HOH A2249      35.784 -13.488  -7.598  1.00 35.25           O  
HETATM 2547  O   HOH A2250      31.937 -17.502  -2.524  1.00 27.72           O  
HETATM 2548  O   HOH A2251      37.991 -19.137 -12.015  1.00 56.17           O  
HETATM 2549  O   HOH A2252      39.666 -13.653 -11.366  1.00 62.14           O  
HETATM 2550  O   HOH A2253      34.952 -31.566  17.830  1.00 48.94           O  
HETATM 2551  O   HOH A2254      32.092 -25.548  15.460  1.00 38.26           O  
HETATM 2552  O   HOH A2255      33.140 -22.077  17.662  1.00 49.83           O  
HETATM 2553  O   HOH A2256      38.510 -19.280  18.328  1.00 57.74           O  
HETATM 2554  O   HOH A2257      39.725 -17.985  16.803  1.00 41.12           O  
HETATM 2555  O   HOH A2258      27.690 -14.489  13.241  1.00 43.40           O  
HETATM 2556  O   HOH A2259      30.097 -23.878  16.362  1.00 45.02           O  
HETATM 2557  O   HOH A2260      29.000 -18.635  20.526  1.00 77.74           O  
HETATM 2558  O   HOH A2261      26.565 -12.079  16.025  1.00 45.80           O  
HETATM 2559  O   HOH A2262      26.946  -7.306  13.486  1.00 58.07           O  
HETATM 2560  O   HOH A2263      35.078  -6.721  16.298  1.00 41.99           O  
HETATM 2561  O   HOH A2264      33.663 -10.672  20.533  1.00 60.59           O  
HETATM 2562  O   HOH A2265      38.300 -12.471  15.951  1.00 30.01           O  
HETATM 2563  O   HOH A2266      37.849 -15.272  17.763  1.00 49.72           O  
HETATM 2564  O   HOH A2267      37.236  -6.241   9.352  1.00 41.05           O  
HETATM 2565  O   HOH A2268      41.026  -6.615  13.316  1.00 66.68           O  
HETATM 2566  O   HOH A2269      38.155 -11.457  18.608  1.00 32.69           O  
HETATM 2567  O   HOH A2270      44.374  -6.748  19.245  1.00 65.94           O  
HETATM 2568  O   HOH A2271      42.596 -12.316  10.014  1.00 29.21           O  
HETATM 2569  O   HOH A2272      44.340 -10.329  12.218  1.00 47.31           O  
HETATM 2570  O   HOH A2273      40.124 -15.310  19.072  1.00 46.85           O  
HETATM 2571  O   HOH A2274      45.206 -14.302  14.160  1.00 29.36           O  
HETATM 2572  O   HOH A2275      44.839 -15.352  19.370  1.00 37.57           O  
HETATM 2573  O   HOH A2276      46.852 -19.344  18.512  1.00 34.64           O  
HETATM 2574  O   HOH A2277      44.140 -27.371  24.507  1.00 41.39           O  
HETATM 2575  O   HOH A2278      48.573 -24.694  18.078  1.00 24.88           O  
HETATM 2576  O   HOH A2279      46.515 -30.228  21.648  1.00 51.69           O  
HETATM 2577  O   HOH A2280      55.950 -26.691  17.573  1.00 34.35           O  
HETATM 2578  O   HOH A2281      55.262 -26.128  13.814  1.00 27.26           O  
HETATM 2579  O   HOH A2282      55.357 -29.217  13.245  1.00 55.77           O  
HETATM 2580  O   HOH A2283      53.607 -28.955   8.628  1.00 49.87           O  
HETATM 2581  O   HOH A2284      54.962 -26.308  10.152  1.00 34.46           O  
HETATM 2582  O   HOH A2285      52.307 -19.950  11.977  1.00 36.37           O  
HETATM 2583  O   HOH A2286      49.510 -16.179   7.491  1.00 31.65           O  
HETATM 2584  O   HOH A2287      50.865 -16.351   9.997  1.00 38.33           O  
HETATM 2585  O   HOH A2288      52.007 -14.920   2.878  1.00 57.42           O  
HETATM 2586  O   HOH A2289      55.155 -20.600   4.513  1.00 57.87           O  
HETATM 2587  O   HOH A2290      46.892 -12.803   6.445  1.00 47.73           O  
HETATM 2588  O   HOH A2291      44.660 -13.907   9.823  1.00 34.11           O  
HETATM 2589  O   HOH A2292      50.457 -18.024  11.715  1.00 34.77           O  
HETATM 2590  O   HOH A2293      50.960 -16.342  14.081  1.00 44.07           O  
HETATM 2591  O   HOH A2294      48.778 -12.585  -0.709  1.00 37.41           O  
HETATM 2592  O   HOH A2295      44.112  -9.862   8.463  1.00 43.87           O  
HETATM 2593  O   HOH A2296      44.608  -8.246   5.299  1.00 35.13           O  
HETATM 2594  O   HOH A2297      41.371  -5.918  -0.195  1.00 53.35           O  
HETATM 2595  O   HOH A2298      47.392  -4.166  -1.291  1.00 64.46           O  
HETATM 2596  O   HOH A2299      43.427  -3.254  -2.193  1.00 53.63           O  
HETATM 2597  O   HOH A2300      40.425  -4.692   6.432  1.00 58.63           O  
HETATM 2598  O   HOH A2301      42.608 -12.711  -2.857  1.00 33.97           O  
HETATM 2599  O   HOH A2302      40.312  -9.224  -3.743  1.00 44.58           O  
HETATM 2600  O   HOH A2303      40.313  -6.500  -2.163  1.00 43.42           O  
HETATM 2601  O   HOH A2304      44.951 -10.359  -4.532  1.00 49.38           O  
HETATM 2602  O   HOH A2305      48.442 -12.044   4.091  1.00 58.49           O  
HETATM 2603  O   HOH A2306      47.051 -13.673  -3.350  1.00 40.86           O  
HETATM 2604  O   HOH A2307      41.387 -15.266  -2.974  1.00 34.88           O  
HETATM 2605  O   HOH A2308      48.095 -17.515  -8.260  1.00 35.15           O  
HETATM 2606  O   HOH A2309      42.278 -18.638  -7.787  1.00 41.11           O  
HETATM 2607  O   HOH A2310      44.347 -19.970  -8.628  1.00 28.57           O  
HETATM 2608  O   HOH A2311      46.113 -19.163 -10.380  1.00 51.85           O  
HETATM 2609  O   HOH A2312      50.237 -18.210 -12.005  1.00 59.34           O  
HETATM 2610  O   HOH A2313      50.862 -18.446  -7.709  1.00 55.78           O  
HETATM 2611  O   HOH A2314      51.859 -23.715  -9.896  1.00 43.80           O  
HETATM 2612  O   HOH A2315      51.826 -20.566  -1.812  1.00 35.76           O  
HETATM 2613  O   HOH A2316      52.519 -16.505  -3.548  1.00 48.47           O  
HETATM 2614  O   HOH A2317      50.345 -13.415  -2.452  1.00 50.90           O  
HETATM 2615  O   HOH A2318      55.318 -22.466  -1.727  1.00 49.02           O  
HETATM 2616  O   HOH A2319      54.942 -26.348  -2.904  1.00 66.10           O  
HETATM 2617  O   HOH A2320      56.028 -24.941  -1.080  1.00 60.24           O  
HETATM 2618  O   HOH A2321      52.943 -25.973  -9.110  1.00 47.76           O  
HETATM 2619  O   HOH A2322      53.100 -27.438  -5.919  1.00 54.41           O  
HETATM 2620  O   HOH A2323      51.717 -20.194  -6.303  1.00 38.32           O  
HETATM 2621  O   HOH A2324      56.361 -28.782   2.472  1.00 54.80           O  
HETATM 2622  O   HOH A2325      50.952 -30.860  -3.479  1.00 51.04           O  
HETATM 2623  O   HOH A2326      53.526 -32.283  -3.212  1.00 53.49           O  
HETATM 2624  O   HOH A2327      52.368 -39.113   0.570  1.00 63.40           O  
HETATM 2625  O   HOH A2328      51.049 -40.327  -1.485  1.00 56.98           O  
HETATM 2626  O   HOH A2329      43.843 -43.745  -4.473  1.00 44.57           O  
HETATM 2627  O   HOH A2330      52.720 -42.009   1.144  1.00 67.98           O  
HETATM 2628  O   HOH A2331      46.263 -46.481  10.520  1.00 56.74           O  
HETATM 2629  O   HOH A2332      38.382 -51.727   4.776  1.00 67.44           O  
HETATM 2630  O   HOH A2333      39.162 -51.908   9.516  1.00 71.24           O  
HETATM 2631  O   HOH A2334      34.924 -50.540  10.321  1.00 78.71           O  
HETATM 2632  O   HOH A2335      38.322 -48.753  13.467  1.00 79.48           O  
HETATM 2633  O   HOH A2336      20.311 -31.019   5.527  1.00 41.21           O  
HETATM 2634  O   HOH A2337      22.622 -34.582   3.897  1.00 38.55           O  
CONECT 2265 2266 2269                                                           
CONECT 2266 2265 2267                                                           
CONECT 2267 2266 2268                                                           
CONECT 2268 2267 2269                                                           
CONECT 2269 2265 2268                                                           
CONECT 2270 2271 2276                                                           
CONECT 2271 2270 2272                                                           
CONECT 2272 2271 2273 2274                                                      
CONECT 2273 2272                                                                
CONECT 2274 2272 2275                                                           
CONECT 2275 2274 2276                                                           
CONECT 2276 2270 2275 2277                                                      
CONECT 2277 2276 2278                                                           
CONECT 2278 2277 2279 2292                                                      
CONECT 2279 2278 2280                                                           
CONECT 2280 2279 2281 2289                                                      
CONECT 2281 2280 2282 2287                                                      
CONECT 2282 2281 2283                                                           
CONECT 2283 2282 2284 2285                                                      
CONECT 2284 2283                                                                
CONECT 2285 2283 2286                                                           
CONECT 2286 2285 2287                                                           
CONECT 2287 2281 2286 2288                                                      
CONECT 2288 2287 2289                                                           
CONECT 2289 2280 2288 2290                                                      
CONECT 2290 2289 2291 2292                                                      
CONECT 2291 2290                                                                
CONECT 2292 2278 2290                                                           
CONECT 2293 2294 2297                                                           
CONECT 2294 2293 2295                                                           
CONECT 2295 2294 2296                                                           
CONECT 2296 2295 2297                                                           
CONECT 2297 2293 2296                                                           
MASTER      511    0    3   15   12    0    8    6 2633    1   33   26          
END