HEADER    FUSION PROTEIN                          14-MAY-99   1QCS              
TITLE     N-TERMINAL DOMAIN OF N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF)          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-ETHYLMALEIMIDE SENSITIVE FACTOR (NSF-N);                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN OF NSF;                                  
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: THIS PROTEIN IS ONE DOMAIN OF THREE IN THE            
COMPND   7 NSF PROTOMER. BIOLOGICALLY NSF IS A HEXAMER.                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;                             
SOURCE   3 ORGANISM_COMMON: CHINESE HAMSTER;                                    
SOURCE   4 ORGANISM_TAXID: 10029;                                               
SOURCE   5 TISSUE: OVARY;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET-15B                                    
KEYWDS    DOUBLE-PSI BETA BARREL ALPHA BETA ROLL, FUSION PROTEIN                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.C.YU,R.JAHN,A.T.BRUNGER                                             
REVDAT   3   24-FEB-09 1QCS    1       VERSN                                    
REVDAT   2   08-DEC-99 1QCS    1       COMPND JRNL   REMARK                     
REVDAT   1   18-MAY-99 1QCS    0                                                
JRNL        AUTH   R.C.YU,R.JAHN,A.T.BRUNGER                                    
JRNL        TITL   NSF N-TERMINAL DOMAIN CRYSTAL STRUCTURE: MODELS OF           
JRNL        TITL 2 NSF FUNCTION.                                                
JRNL        REF    MOL.CELL                      V.   4    97 1999              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   10445031                                                     
JRNL        DOI    10.1016/S1097-2765(00)80191-4                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.5                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH AND HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2145257.790                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 32739                          
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 10%                      
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3195                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4359                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE                    : 0.2590                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 478                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1517                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.53000                                             
REMARK   3    B22 (A**2) : -3.62000                                             
REMARK   3    B33 (A**2) : 9.16000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.110 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.820 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.700 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.730 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 46.28                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MLHL TARGET FUNCTION AND DENSITY          
REMARK   3  MODIFIED, COMBINED PHASES USED IN REFINEMENTS. WAVELENGTH 3         
REMARK   3  (LOW ENERGY REMOTE, 0.9998 ANGSTROM) DATA USED FOR REFINEMENT.      
REMARK   4                                                                      
REMARK   4 1QCS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009092.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9799, 0.9801, 0.9998, 0.9537     
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADSC                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32752                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.05100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP, 100       
REMARK 280  MM TRIS PH 8.7, 2.0 M AMMONIUM SULFATE, 10 MM DITHIOTHREITOL        
REMARK 280  (DTT), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.83150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.83150            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       16.02100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       87.68100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       16.02100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       87.68100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.83150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       16.02100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       87.68100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       39.83150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       16.02100            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       87.68100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: IS ONE DOMAIN OF THREE IN THE NSF PROTOMER. BIOLOGICALLY     
REMARK 300 NSF IS A HEXAMER. SYMMETRY OPERATORS AND RELEVANT TRANSLATIONS       
REMARK 300 FOR HEXAMERIZATION ARE UNKNOWN. NSF CONTAINS 3 DOMAINS: N, D1,       
REMARK 300 AND D2. D2 IS THE HEXAMERIZATION DOMAIN. BOTH THE SPATIAL            
REMARK 300 ORIENTATION OF N RELATIVE TO D2, AND THE STRUCTURE OF IN THE         
REMARK 300 INTERMEDIATE D1 DOMAIN ARE NOT KNOWN.                                
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     PRO A   164                                                      
REMARK 465     ALA A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     GLY A   167                                                      
REMARK 465     LYS A   168                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     GLU A   203                                                      
REMARK 465     ASN A   204                                                      
REMARK 465     ARG A   205                                                      
REMARK 465     LEU A   206                                                      
REMARK 465     GLU A   207                                                      
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  67   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 127       31.72     70.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 408        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH A 423        DISTANCE =  6.22 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NSF   RELATED DB: PDB                                   
REMARK 900 D2 DOMAIN OF NSF                                                     
REMARK 900 RELATED ID: 1D2N   RELATED DB: PDB                                   
REMARK 900 D2 DOMAIN OF NSF                                                     
DBREF  1QCS A    1   205  UNP    P18708   NSF_CRIGR        1    205             
SEQADV 1QCS GLY A   -3  UNP  P18708              SEE REMARK 999                 
SEQADV 1QCS SER A   -2  UNP  P18708              SEE REMARK 999                 
SEQADV 1QCS HIS A   -1  UNP  P18708              SEE REMARK 999                 
SEQADV 1QCS ASN A    0  UNP  P18708              SEE REMARK 999                 
SEQADV 1QCS MSE A    1  UNP  P18708    MET     1 MODIFIED RESIDUE               
SEQADV 1QCS MSE A    6  UNP  P18708    MET     6 MODIFIED RESIDUE               
SEQADV 1QCS MSE A   95  UNP  P18708    MET    95 MODIFIED RESIDUE               
SEQADV 1QCS MSE A  117  UNP  P18708    MET   117 MODIFIED RESIDUE               
SEQADV 1QCS MSE A  155  UNP  P18708    MET   155 MODIFIED RESIDUE               
SEQADV 1QCS LEU A  206  UNP  P18708              SEE REMARK 999                 
SEQADV 1QCS GLU A  207  UNP  P18708              SEE REMARK 999                 
SEQRES   1 A  211  GLY SER HIS ASN MSE ALA GLY ARG SER MSE GLN ALA ALA          
SEQRES   2 A  211  ARG CYS PRO THR ASP GLU LEU SER LEU SER ASN CYS ALA          
SEQRES   3 A  211  VAL VAL SER GLU LYS ASP TYR GLN SER GLY GLN HIS VAL          
SEQRES   4 A  211  ILE VAL ARG THR SER PRO ASN HIS LYS TYR ILE PHE THR          
SEQRES   5 A  211  LEU ARG THR HIS PRO SER VAL VAL PRO GLY SER VAL ALA          
SEQRES   6 A  211  PHE SER LEU PRO GLN ARG LYS TRP ALA GLY LEU SER ILE          
SEQRES   7 A  211  GLY GLN GLU ILE GLU VAL ALA LEU TYR SER PHE ASP LYS          
SEQRES   8 A  211  ALA LYS GLN CYS ILE GLY THR MSE THR ILE GLU ILE ASP          
SEQRES   9 A  211  PHE LEU GLN LYS LYS ASN ILE ASP SER ASN PRO TYR ASP          
SEQRES  10 A  211  THR ASP LYS MSE ALA ALA GLU PHE ILE GLN GLN PHE ASN          
SEQRES  11 A  211  ASN GLN ALA PHE SER VAL GLY GLN GLN LEU VAL PHE SER          
SEQRES  12 A  211  PHE ASN ASP LYS LEU PHE GLY LEU LEU VAL LYS ASP ILE          
SEQRES  13 A  211  GLU ALA MSE ASP PRO SER ILE LEU LYS GLY GLU PRO ALA          
SEQRES  14 A  211  SER GLY LYS ARG GLN LYS ILE GLU VAL GLY LEU VAL VAL          
SEQRES  15 A  211  GLY ASN SER GLN VAL ALA PHE GLU LYS ALA GLU ASN SER          
SEQRES  16 A  211  SER LEU ASN LEU ILE GLY LYS ALA LYS THR LYS GLU ASN          
SEQRES  17 A  211  ARG LEU GLU                                                  
MODRES 1QCS MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1QCS MSE A    6  MET  SELENOMETHIONINE                                   
MODRES 1QCS MSE A   95  MET  SELENOMETHIONINE                                   
MODRES 1QCS MSE A  117  MET  SELENOMETHIONINE                                   
MODRES 1QCS MSE A  155  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A   6       8                                                       
HET    MSE  A  95       8                                                       
HET    MSE  A 117       8                                                       
HET    MSE  A 155       8                                                       
HET    SO4  A 500       5                                                       
HET    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   2  SO4    3(O4 S 2-)                                                   
FORMUL   5  HOH   *130(H2 O)                                                    
HELIX    1   1 THR A   13  SER A   19  1                                   7    
HELIX    2   2 SER A   63  GLY A   71  1                                   9    
HELIX    3   3 ASP A   86  CYS A   91  1                                   6    
HELIX    4   4 GLN A  103  ILE A  107  5                                   5    
HELIX    5   5 THR A  114  ASN A  126  1                                  13    
SHEET    1   A 7 ARG A   4  ARG A  10  0                                        
SHEET    2   A 7 SER A  59  PHE A  62  1  O  VAL A  60   N  ALA A   9           
SHEET    3   A 7 ARG A   4  ARG A  10  1  O  GLN A   7   N  VAL A  60           
SHEET    4   A 7 GLU A  77  TYR A  83 -1  O  ILE A  78   N  MSE A   6           
SHEET    5   A 7 HIS A  34  SER A  40 -1  O  HIS A  34   N  TYR A  83           
SHEET    6   A 7 HIS A  43  THR A  51 -1  O  HIS A  43   N  THR A  39           
SHEET    7   A 7 ALA A  22  VAL A  24  1  N  ALA A  22   O  THR A  48           
SHEET    1   B 4 GLN A 135  PHE A 140  0                                        
SHEET    2   B 4 LYS A 143  ALA A 154 -1  O  LYS A 143   N  PHE A 140           
SHEET    3   B 4 ILE A  92  PHE A 101 -1  N  GLY A  93   O  GLU A 153           
SHEET    4   B 4 GLN A 182  LYS A 187  1  N  GLN A 182   O  GLY A  93           
SHEET    1   C 2 PRO A 111  ASP A 113  0                                        
SHEET    2   C 2 ASN A 194  ILE A 196  1  O  ASN A 194   N  TYR A 112           
SHEET    1   D 2 ALA A 129  SER A 131  0                                        
SHEET    2   D 2 VAL A 174  LEU A 176 -1  N  GLY A 175   O  PHE A 130           
LINK         C   ASN A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   ALA A   2     1555   1555  1.33  
LINK         C   SER A   5                 N   MSE A   6     1555   1555  1.33  
LINK         C   MSE A   6                 N   GLN A   7     1555   1555  1.33  
LINK         C   THR A  94                 N   MSE A  95     1555   1555  1.33  
LINK         C   MSE A  95                 N   THR A  96     1555   1555  1.33  
LINK         C   LYS A 116                 N   MSE A 117     1555   1555  1.33  
LINK         C   MSE A 117                 N   ALA A 118     1555   1555  1.33  
LINK         C   ALA A 154                 N   MSE A 155     1555   1555  1.33  
LINK         C   MSE A 155                 N   ASP A 156     1555   1555  1.33  
SITE     1 AC1  6 GLN A  76  GLU A  77  LYS A  87  ASN A 127                    
SITE     2 AC1  6 HOH A 371  HOH A 408                                          
SITE     1 AC2  3 THR A  13  ARG A  50  HIS A  52                               
SITE     1 AC3  4 ARG A  10  CYS A  11  LEU A  64  ARG A  67                    
CRYST1   32.042  175.362   79.663  90.00  90.00  90.00 C 2 2 21      8          
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      0.031209  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005702  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012553        0.00000                         
ATOM      1  N   ASN A   0       6.461   2.442 -30.173  1.00 52.56           N  
ATOM      2  CA  ASN A   0       6.322   1.121 -30.783  1.00 52.71           C  
ATOM      3  C   ASN A   0       5.950   1.224 -32.253  1.00 51.92           C  
ATOM      4  O   ASN A   0       6.372   0.401 -33.064  1.00 51.23           O  
ATOM      5  CB  ASN A   0       5.266   0.298 -30.044  1.00 53.81           C  
ATOM      6  CG  ASN A   0       5.661   0.005 -28.621  1.00 55.04           C  
ATOM      7  OD1 ASN A   0       6.794  -0.409 -28.352  1.00 55.80           O  
ATOM      8  ND2 ASN A   0       4.727   0.202 -27.693  1.00 55.62           N  
HETATM    9  N   MSE A   1       5.150   2.231 -32.588  1.00 51.56           N  
HETATM   10  CA  MSE A   1       4.732   2.458 -33.966  1.00 50.97           C  
HETATM   11  C   MSE A   1       5.962   2.862 -34.781  1.00 48.20           C  
HETATM   12  O   MSE A   1       6.147   2.431 -35.920  1.00 47.21           O  
HETATM   13  CB  MSE A   1       3.694   3.578 -34.024  1.00 55.57           C  
HETATM   14  CG  MSE A   1       4.095   4.822 -33.238  1.00 60.95           C  
HETATM   15 SE   MSE A   1       3.400   6.364 -33.917  1.00 70.06          SE  
HETATM   16  CE  MSE A   1       4.859   7.007 -34.799  1.00 66.98           C  
ATOM     17  N   ALA A   2       6.806   3.688 -34.175  1.00 44.88           N  
ATOM     18  CA  ALA A   2       8.025   4.152 -34.823  1.00 42.42           C  
ATOM     19  C   ALA A   2       9.053   3.026 -34.872  1.00 40.07           C  
ATOM     20  O   ALA A   2       9.859   2.944 -35.801  1.00 39.79           O  
ATOM     21  CB  ALA A   2       8.598   5.350 -34.064  1.00 41.96           C  
ATOM     22  N   GLY A   3       9.014   2.153 -33.871  1.00 37.21           N  
ATOM     23  CA  GLY A   3       9.958   1.058 -33.828  1.00 35.26           C  
ATOM     24  C   GLY A   3      11.031   1.323 -32.793  1.00 33.85           C  
ATOM     25  O   GLY A   3      11.496   2.453 -32.655  1.00 33.67           O  
ATOM     26  N   ARG A   4      11.435   0.286 -32.069  1.00 31.34           N  
ATOM     27  CA  ARG A   4      12.447   0.443 -31.033  1.00 29.75           C  
ATOM     28  C   ARG A   4      13.485  -0.682 -31.026  1.00 27.10           C  
ATOM     29  O   ARG A   4      13.263  -1.750 -31.589  1.00 25.32           O  
ATOM     30  CB  ARG A   4      11.756   0.541 -29.670  1.00 31.27           C  
ATOM     31  CG  ARG A   4      10.578  -0.401 -29.510  1.00 34.08           C  
ATOM     32  CD  ARG A   4       9.797  -0.122 -28.230  1.00 36.52           C  
ATOM     33  NE  ARG A   4      10.606  -0.375 -27.042  1.00 39.67           N  
ATOM     34  CZ  ARG A   4      10.170  -0.274 -25.790  1.00 40.53           C  
ATOM     35  NH1 ARG A   4       8.914   0.085 -25.536  1.00 40.45           N  
ATOM     36  NH2 ARG A   4      10.995  -0.549 -24.789  1.00 41.40           N  
ATOM     37  N   SER A   5      14.619  -0.426 -30.385  1.00 25.19           N  
ATOM     38  CA  SER A   5      15.694  -1.408 -30.300  1.00 24.01           C  
ATOM     39  C   SER A   5      15.413  -2.361 -29.139  1.00 22.63           C  
ATOM     40  O   SER A   5      15.008  -1.937 -28.059  1.00 20.80           O  
ATOM     41  CB  SER A   5      17.026  -0.691 -30.100  1.00 25.40           C  
ATOM     42  OG  SER A   5      17.248   0.224 -31.166  1.00 26.74           O  
HETATM   43  N   MSE A   6      15.615  -3.653 -29.367  1.00 21.19           N  
HETATM   44  CA  MSE A   6      15.356  -4.651 -28.338  1.00 21.34           C  
HETATM   45  C   MSE A   6      16.448  -5.709 -28.411  1.00 20.80           C  
HETATM   46  O   MSE A   6      17.208  -5.749 -29.380  1.00 20.60           O  
HETATM   47  CB  MSE A   6      13.994  -5.325 -28.581  1.00 24.74           C  
HETATM   48  CG  MSE A   6      12.804  -4.383 -28.699  1.00 29.78           C  
HETATM   49 SE   MSE A   6      12.259  -3.649 -27.083  1.00 43.03          SE  
HETATM   50  CE  MSE A   6      11.180  -4.989 -26.454  1.00 34.62           C  
ATOM     51  N   GLN A   7      16.519  -6.571 -27.400  1.00 18.66           N  
ATOM     52  CA  GLN A   7      17.520  -7.629 -27.391  1.00 17.65           C  
ATOM     53  C   GLN A   7      16.801  -8.964 -27.514  1.00 16.89           C  
ATOM     54  O   GLN A   7      15.804  -9.202 -26.825  1.00 16.04           O  
ATOM     55  CB  GLN A   7      18.323  -7.589 -26.092  1.00 19.48           C  
ATOM     56  CG  GLN A   7      19.500  -8.561 -26.072  1.00 22.07           C  
ATOM     57  CD  GLN A   7      20.457  -8.290 -24.915  1.00 23.31           C  
ATOM     58  OE1 GLN A   7      20.937  -7.169 -24.755  1.00 25.23           O  
ATOM     59  NE2 GLN A   7      20.755  -9.319 -24.128  1.00 23.31           N  
ATOM     60  N   ALA A   8      17.287  -9.833 -28.393  1.00 15.55           N  
ATOM     61  CA  ALA A   8      16.672 -11.137 -28.582  1.00 16.24           C  
ATOM     62  C   ALA A   8      16.989 -12.069 -27.409  1.00 16.70           C  
ATOM     63  O   ALA A   8      18.142 -12.205 -26.983  1.00 17.06           O  
ATOM     64  CB  ALA A   8      17.144 -11.761 -29.910  1.00 16.85           C  
ATOM     65  N   ALA A   9      15.951 -12.717 -26.894  1.00 16.50           N  
ATOM     66  CA  ALA A   9      16.104 -13.614 -25.767  1.00 17.37           C  
ATOM     67  C   ALA A   9      15.517 -14.994 -26.047  1.00 18.57           C  
ATOM     68  O   ALA A   9      14.913 -15.249 -27.099  1.00 17.86           O  
ATOM     69  CB  ALA A   9      15.450 -12.995 -24.532  1.00 16.97           C  
ATOM     70  N   ARG A  10      15.696 -15.883 -25.085  1.00 20.25           N  
ATOM     71  CA  ARG A  10      15.214 -17.235 -25.203  1.00 22.77           C  
ATOM     72  C   ARG A  10      13.788 -17.394 -24.673  1.00 22.21           C  
ATOM     73  O   ARG A  10      13.422 -16.813 -23.654  1.00 21.97           O  
ATOM     74  CB  ARG A  10      16.176 -18.150 -24.446  1.00 25.49           C  
ATOM     75  CG  ARG A  10      15.869 -19.624 -24.552  1.00 30.32           C  
ATOM     76  CD  ARG A  10      17.067 -20.454 -24.105  1.00 33.39           C  
ATOM     77  NE  ARG A  10      16.839 -21.868 -24.370  1.00 37.21           N  
ATOM     78  CZ  ARG A  10      17.718 -22.830 -24.109  1.00 39.33           C  
ATOM     79  NH1 ARG A  10      18.894 -22.531 -23.566  1.00 40.11           N  
ATOM     80  NH2 ARG A  10      17.423 -24.091 -24.401  1.00 40.26           N  
ATOM     81  N   CYS A  11      12.987 -18.188 -25.373  1.00 23.19           N  
ATOM     82  CA  CYS A  11      11.606 -18.459 -24.963  1.00 23.88           C  
ATOM     83  C   CYS A  11      11.562 -18.989 -23.516  1.00 23.91           C  
ATOM     84  O   CYS A  11      12.292 -19.924 -23.167  1.00 23.53           O  
ATOM     85  CB  CYS A  11      10.982 -19.475 -25.916  1.00 24.15           C  
ATOM     86  SG  CYS A  11       9.226 -19.687 -25.619  1.00 27.33           S  
ATOM     87  N   PRO A  12      10.677 -18.424 -22.669  1.00 24.26           N  
ATOM     88  CA  PRO A  12      10.500 -18.779 -21.247  1.00 25.04           C  
ATOM     89  C   PRO A  12       9.904 -20.130 -20.867  1.00 25.23           C  
ATOM     90  O   PRO A  12      10.313 -20.716 -19.868  1.00 26.25           O  
ATOM     91  CB  PRO A  12       9.625 -17.640 -20.694  1.00 24.95           C  
ATOM     92  CG  PRO A  12       9.514 -16.632 -21.823  1.00 25.53           C  
ATOM     93  CD  PRO A  12       9.650 -17.450 -23.071  1.00 24.71           C  
ATOM     94  N   THR A  13       8.931 -20.621 -21.630  1.00 25.68           N  
ATOM     95  CA  THR A  13       8.298 -21.898 -21.294  1.00 26.09           C  
ATOM     96  C   THR A  13       8.061 -22.785 -22.509  1.00 27.00           C  
ATOM     97  O   THR A  13       8.028 -22.308 -23.642  1.00 26.16           O  
ATOM     98  CB  THR A  13       6.917 -21.696 -20.607  1.00 27.29           C  
ATOM     99  OG1 THR A  13       5.977 -21.175 -21.555  1.00 27.19           O  
ATOM    100  CG2 THR A  13       7.025 -20.732 -19.420  1.00 26.50           C  
ATOM    101  N   ASP A  14       7.885 -24.080 -22.267  1.00 27.43           N  
ATOM    102  CA  ASP A  14       7.622 -25.011 -23.353  1.00 28.82           C  
ATOM    103  C   ASP A  14       6.296 -24.698 -24.029  1.00 27.91           C  
ATOM    104  O   ASP A  14       6.186 -24.779 -25.252  1.00 27.22           O  
ATOM    105  CB  ASP A  14       7.582 -26.448 -22.833  1.00 30.86           C  
ATOM    106  CG  ASP A  14       8.898 -26.880 -22.237  1.00 33.62           C  
ATOM    107  OD1 ASP A  14       9.953 -26.601 -22.855  1.00 34.99           O  
ATOM    108  OD2 ASP A  14       8.879 -27.505 -21.153  1.00 35.79           O  
ATOM    109  N   GLU A  15       5.290 -24.353 -23.232  1.00 27.87           N  
ATOM    110  CA  GLU A  15       3.967 -24.028 -23.765  1.00 28.41           C  
ATOM    111  C   GLU A  15       4.041 -22.830 -24.707  1.00 27.42           C  
ATOM    112  O   GLU A  15       3.397 -22.816 -25.759  1.00 26.37           O  
ATOM    113  CB  GLU A  15       2.979 -23.719 -22.627  1.00 31.12           C  
ATOM    114  CG  GLU A  15       1.584 -23.308 -23.113  1.00 34.88           C  
ATOM    115  CD  GLU A  15       0.612 -22.973 -21.980  1.00 39.05           C  
ATOM    116  OE1 GLU A  15       0.892 -22.046 -21.172  1.00 39.91           O  
ATOM    117  OE2 GLU A  15      -0.447 -23.641 -21.902  1.00 41.36           O  
ATOM    118  N   LEU A  16       4.803 -21.810 -24.324  1.00 25.73           N  
ATOM    119  CA  LEU A  16       4.929 -20.641 -25.189  1.00 25.16           C  
ATOM    120  C   LEU A  16       5.728 -20.987 -26.443  1.00 23.87           C  
ATOM    121  O   LEU A  16       5.506 -20.424 -27.514  1.00 23.19           O  
ATOM    122  CB  LEU A  16       5.579 -19.478 -24.432  1.00 25.96           C  
ATOM    123  CG  LEU A  16       4.600 -18.858 -23.436  1.00 26.75           C  
ATOM    124  CD1 LEU A  16       5.285 -17.777 -22.614  1.00 27.95           C  
ATOM    125  CD2 LEU A  16       3.413 -18.292 -24.207  1.00 27.93           C  
ATOM    126  N   SER A  17       6.647 -21.931 -26.315  1.00 23.99           N  
ATOM    127  CA  SER A  17       7.444 -22.339 -27.464  1.00 24.21           C  
ATOM    128  C   SER A  17       6.502 -22.911 -28.538  1.00 23.83           C  
ATOM    129  O   SER A  17       6.649 -22.632 -29.736  1.00 24.22           O  
ATOM    130  CB  SER A  17       8.478 -23.385 -27.033  1.00 25.21           C  
ATOM    131  OG  SER A  17       9.399 -23.642 -28.084  1.00 27.72           O  
ATOM    132  N   LEU A  18       5.508 -23.673 -28.110  1.00 21.92           N  
ATOM    133  CA  LEU A  18       4.573 -24.263 -29.060  1.00 22.00           C  
ATOM    134  C   LEU A  18       3.533 -23.295 -29.626  1.00 21.34           C  
ATOM    135  O   LEU A  18       2.828 -23.636 -30.570  1.00 22.40           O  
ATOM    136  CB  LEU A  18       3.863 -25.451 -28.418  1.00 22.80           C  
ATOM    137  CG  LEU A  18       4.784 -26.649 -28.159  1.00 24.56           C  
ATOM    138  CD1 LEU A  18       4.088 -27.660 -27.270  1.00 26.10           C  
ATOM    139  CD2 LEU A  18       5.178 -27.273 -29.491  1.00 26.06           C  
ATOM    140  N   SER A  19       3.440 -22.096 -29.062  1.00 18.42           N  
ATOM    141  CA  SER A  19       2.465 -21.117 -29.531  1.00 17.63           C  
ATOM    142  C   SER A  19       2.892 -20.373 -30.805  1.00 16.32           C  
ATOM    143  O   SER A  19       2.057 -19.742 -31.456  1.00 16.20           O  
ATOM    144  CB  SER A  19       2.204 -20.075 -28.442  1.00 18.80           C  
ATOM    145  OG  SER A  19       3.323 -19.189 -28.331  1.00 19.90           O  
ATOM    146  N   ASN A  20       4.181 -20.451 -31.137  1.00 15.37           N  
ATOM    147  CA  ASN A  20       4.792 -19.758 -32.274  1.00 15.12           C  
ATOM    148  C   ASN A  20       4.683 -18.230 -32.147  1.00 15.63           C  
ATOM    149  O   ASN A  20       4.806 -17.501 -33.139  1.00 14.72           O  
ATOM    150  CB  ASN A  20       4.212 -20.186 -33.634  1.00 15.77           C  
ATOM    151  CG  ASN A  20       5.111 -19.754 -34.814  1.00 15.03           C  
ATOM    152  OD1 ASN A  20       4.627 -19.251 -35.846  1.00 17.88           O  
ATOM    153  ND2 ASN A  20       6.415 -19.956 -34.671  1.00 13.15           N  
ATOM    154  N   CYS A  21       4.465 -17.735 -30.934  1.00 14.81           N  
ATOM    155  CA  CYS A  21       4.388 -16.286 -30.734  1.00 15.41           C  
ATOM    156  C   CYS A  21       5.743 -15.795 -30.241  1.00 15.24           C  
ATOM    157  O   CYS A  21       6.513 -16.563 -29.678  1.00 15.87           O  
ATOM    158  CB  CYS A  21       3.337 -15.926 -29.666  1.00 17.05           C  
ATOM    159  SG  CYS A  21       1.594 -16.082 -30.160  1.00 21.55           S  
ATOM    160  N   ALA A  22       6.050 -14.524 -30.463  1.00 15.00           N  
ATOM    161  CA  ALA A  22       7.284 -13.960 -29.931  1.00 14.63           C  
ATOM    162  C   ALA A  22       6.794 -13.541 -28.537  1.00 15.01           C  
ATOM    163  O   ALA A  22       5.690 -13.000 -28.412  1.00 14.91           O  
ATOM    164  CB  ALA A  22       7.714 -12.739 -30.737  1.00 15.20           C  
ATOM    165  N   VAL A  23       7.598 -13.786 -27.503  1.00 13.28           N  
ATOM    166  CA  VAL A  23       7.187 -13.479 -26.129  1.00 12.28           C  
ATOM    167  C   VAL A  23       7.791 -12.187 -25.598  1.00 11.68           C  
ATOM    168  O   VAL A  23       9.000 -11.970 -25.703  1.00 10.93           O  
ATOM    169  CB  VAL A  23       7.558 -14.652 -25.209  1.00 10.72           C  
ATOM    170  CG1 VAL A  23       6.969 -14.433 -23.815  1.00 12.94           C  
ATOM    171  CG2 VAL A  23       7.031 -15.946 -25.824  1.00 11.77           C  
ATOM    172  N   VAL A  24       6.942 -11.356 -24.993  1.00 11.73           N  
ATOM    173  CA  VAL A  24       7.345 -10.034 -24.520  1.00 13.03           C  
ATOM    174  C   VAL A  24       6.883  -9.651 -23.120  1.00 13.69           C  
ATOM    175  O   VAL A  24       6.063 -10.336 -22.512  1.00 13.07           O  
ATOM    176  CB  VAL A  24       6.816  -8.968 -25.486  1.00 14.03           C  
ATOM    177  CG1 VAL A  24       7.482  -9.131 -26.847  1.00 13.84           C  
ATOM    178  CG2 VAL A  24       5.297  -9.139 -25.654  1.00 14.58           C  
ATOM    179  N   SER A  25       7.418  -8.534 -22.628  1.00 13.56           N  
ATOM    180  CA  SER A  25       7.065  -8.015 -21.311  1.00 15.42           C  
ATOM    181  C   SER A  25       5.754  -7.229 -21.408  1.00 15.73           C  
ATOM    182  O   SER A  25       5.503  -6.547 -22.400  1.00 15.57           O  
ATOM    183  CB  SER A  25       8.181  -7.085 -20.792  1.00 15.66           C  
ATOM    184  OG  SER A  25       7.700  -6.254 -19.736  1.00 16.99           O  
ATOM    185  N   GLU A  26       4.922  -7.330 -20.375  1.00 16.11           N  
ATOM    186  CA  GLU A  26       3.656  -6.607 -20.329  1.00 17.87           C  
ATOM    187  C   GLU A  26       3.951  -5.106 -20.261  1.00 18.01           C  
ATOM    188  O   GLU A  26       3.081  -4.280 -20.523  1.00 17.82           O  
ATOM    189  CB  GLU A  26       2.839  -7.009 -19.086  1.00 19.83           C  
ATOM    190  CG  GLU A  26       2.627  -8.521 -18.921  1.00 23.26           C  
ATOM    191  CD  GLU A  26       1.721  -8.887 -17.734  1.00 24.68           C  
ATOM    192  OE1 GLU A  26       1.532  -8.053 -16.826  1.00 24.81           O  
ATOM    193  OE2 GLU A  26       1.210 -10.023 -17.709  1.00 26.18           O  
ATOM    194  N   LYS A  27       5.184  -4.755 -19.907  1.00 18.87           N  
ATOM    195  CA  LYS A  27       5.570  -3.357 -19.826  1.00 20.99           C  
ATOM    196  C   LYS A  27       5.837  -2.744 -21.214  1.00 21.52           C  
ATOM    197  O   LYS A  27       5.794  -1.519 -21.377  1.00 21.66           O  
ATOM    198  CB  LYS A  27       6.806  -3.216 -18.931  1.00 23.37           C  
ATOM    199  CG  LYS A  27       6.519  -3.566 -17.465  1.00 26.86           C  
ATOM    200  CD  LYS A  27       7.757  -3.448 -16.595  1.00 29.91           C  
ATOM    201  CE  LYS A  27       7.457  -3.846 -15.141  1.00 32.07           C  
ATOM    202  NZ  LYS A  27       6.461  -2.938 -14.513  1.00 33.38           N  
ATOM    203  N   ASP A  28       6.084  -3.589 -22.211  1.00 20.33           N  
ATOM    204  CA  ASP A  28       6.381  -3.099 -23.560  1.00 20.32           C  
ATOM    205  C   ASP A  28       5.217  -3.219 -24.567  1.00 20.07           C  
ATOM    206  O   ASP A  28       5.008  -2.323 -25.393  1.00 19.94           O  
ATOM    207  CB  ASP A  28       7.610  -3.837 -24.123  1.00 21.30           C  
ATOM    208  CG  ASP A  28       8.894  -3.588 -23.315  1.00 23.11           C  
ATOM    209  OD1 ASP A  28       9.128  -2.437 -22.871  1.00 22.75           O  
ATOM    210  OD2 ASP A  28       9.690  -4.546 -23.158  1.00 22.26           O  
ATOM    211  N   TYR A  29       4.456  -4.309 -24.500  1.00 19.02           N  
ATOM    212  CA  TYR A  29       3.346  -4.531 -25.439  1.00 20.68           C  
ATOM    213  C   TYR A  29       2.166  -5.258 -24.818  1.00 20.88           C  
ATOM    214  O   TYR A  29       2.180  -5.590 -23.629  1.00 20.71           O  
ATOM    215  CB  TYR A  29       3.784  -5.399 -26.622  1.00 20.93           C  
ATOM    216  CG  TYR A  29       5.049  -4.975 -27.312  1.00 22.96           C  
ATOM    217  CD1 TYR A  29       6.283  -5.459 -26.890  1.00 23.52           C  
ATOM    218  CD2 TYR A  29       5.012  -4.094 -28.394  1.00 22.98           C  
ATOM    219  CE1 TYR A  29       7.454  -5.083 -27.521  1.00 25.08           C  
ATOM    220  CE2 TYR A  29       6.189  -3.702 -29.039  1.00 24.74           C  
ATOM    221  CZ  TYR A  29       7.405  -4.203 -28.594  1.00 25.33           C  
ATOM    222  OH  TYR A  29       8.587  -3.817 -29.198  1.00 27.09           O  
ATOM    223  N   GLN A  30       1.160  -5.523 -25.658  1.00 20.55           N  
ATOM    224  CA  GLN A  30      -0.031  -6.275 -25.257  1.00 20.74           C  
ATOM    225  C   GLN A  30      -0.145  -7.513 -26.144  1.00 19.46           C  
ATOM    226  O   GLN A  30       0.135  -7.451 -27.348  1.00 18.18           O  
ATOM    227  CB  GLN A  30      -1.305  -5.426 -25.408  1.00 23.10           C  
ATOM    228  CG  GLN A  30      -1.273  -4.145 -24.582  1.00 27.34           C  
ATOM    229  CD  GLN A  30      -2.652  -3.565 -24.320  1.00 30.14           C  
ATOM    230  OE1 GLN A  30      -3.605  -3.811 -25.068  1.00 31.12           O  
ATOM    231  NE2 GLN A  30      -2.762  -2.777 -23.250  1.00 32.07           N  
ATOM    232  N   SER A  31      -0.539  -8.637 -25.554  1.00 18.10           N  
ATOM    233  CA  SER A  31      -0.692  -9.884 -26.307  1.00 17.90           C  
ATOM    234  C   SER A  31      -1.653  -9.671 -27.480  1.00 18.37           C  
ATOM    235  O   SER A  31      -2.644  -8.921 -27.376  1.00 17.29           O  
ATOM    236  CB  SER A  31      -1.249 -10.998 -25.410  1.00 17.78           C  
ATOM    237  OG  SER A  31      -0.412 -11.217 -24.295  1.00 17.84           O  
ATOM    238  N   GLY A  32      -1.351 -10.307 -28.605  1.00 17.11           N  
ATOM    239  CA  GLY A  32      -2.219 -10.158 -29.758  1.00 17.48           C  
ATOM    240  C   GLY A  32      -1.747  -9.119 -30.761  1.00 17.82           C  
ATOM    241  O   GLY A  32      -2.207  -9.124 -31.910  1.00 18.06           O  
ATOM    242  N   GLN A  33      -0.862  -8.210 -30.349  1.00 17.16           N  
ATOM    243  CA  GLN A  33      -0.339  -7.223 -31.287  1.00 17.43           C  
ATOM    244  C   GLN A  33       0.617  -7.956 -32.221  1.00 17.03           C  
ATOM    245  O   GLN A  33       1.119  -9.049 -31.889  1.00 16.31           O  
ATOM    246  CB  GLN A  33       0.413  -6.104 -30.555  1.00 17.37           C  
ATOM    247  CG  GLN A  33      -0.544  -5.172 -29.769  1.00 20.27           C  
ATOM    248  CD  GLN A  33       0.175  -4.036 -29.103  1.00 21.15           C  
ATOM    249  OE1 GLN A  33       1.056  -4.253 -28.284  1.00 20.82           O  
ATOM    250  NE2 GLN A  33      -0.182  -2.810 -29.464  1.00 23.28           N  
ATOM    251  N   HIS A  34       0.838  -7.390 -33.401  1.00 15.23           N  
ATOM    252  CA  HIS A  34       1.768  -7.995 -34.349  1.00 15.17           C  
ATOM    253  C   HIS A  34       2.924  -7.020 -34.527  1.00 14.58           C  
ATOM    254  O   HIS A  34       2.754  -5.804 -34.377  1.00 15.46           O  
ATOM    255  CB  HIS A  34       1.080  -8.252 -35.696  1.00 14.18           C  
ATOM    256  CG  HIS A  34      -0.234  -8.963 -35.577  1.00 14.96           C  
ATOM    257  ND1 HIS A  34      -0.327 -10.311 -35.301  1.00 13.85           N  
ATOM    258  CD2 HIS A  34      -1.508  -8.509 -35.672  1.00 14.12           C  
ATOM    259  CE1 HIS A  34      -1.599 -10.656 -35.229  1.00 15.87           C  
ATOM    260  NE2 HIS A  34      -2.337  -9.582 -35.451  1.00 15.91           N  
ATOM    261  N   VAL A  35       4.102  -7.540 -34.845  1.00 15.14           N  
ATOM    262  CA  VAL A  35       5.250  -6.675 -35.052  1.00 14.07           C  
ATOM    263  C   VAL A  35       6.082  -7.154 -36.217  1.00 14.87           C  
ATOM    264  O   VAL A  35       6.003  -8.304 -36.650  1.00 14.33           O  
ATOM    265  CB  VAL A  35       6.208  -6.643 -33.832  1.00 14.79           C  
ATOM    266  CG1 VAL A  35       5.493  -6.109 -32.592  1.00 13.83           C  
ATOM    267  CG2 VAL A  35       6.753  -8.061 -33.560  1.00 13.88           C  
ATOM    268  N   ILE A  36       6.879  -6.240 -36.736  1.00 14.48           N  
ATOM    269  CA  ILE A  36       7.800  -6.590 -37.773  1.00 16.00           C  
ATOM    270  C   ILE A  36       9.158  -6.482 -37.049  1.00 15.19           C  
ATOM    271  O   ILE A  36       9.427  -5.519 -36.317  1.00 15.01           O  
ATOM    272  CB  ILE A  36       7.676  -5.632 -38.987  1.00 17.49           C  
ATOM    273  CG1 ILE A  36       8.593  -6.106 -40.111  1.00 19.82           C  
ATOM    274  CG2 ILE A  36       8.035  -4.208 -38.584  1.00 21.71           C  
ATOM    275  CD1 ILE A  36       7.970  -5.914 -41.508  1.00 22.32           C  
ATOM    276  N   VAL A  37       9.971  -7.518 -37.191  1.00 14.43           N  
ATOM    277  CA  VAL A  37      11.287  -7.569 -36.575  1.00 14.61           C  
ATOM    278  C   VAL A  37      12.291  -7.380 -37.707  1.00 15.58           C  
ATOM    279  O   VAL A  37      12.255  -8.121 -38.704  1.00 15.51           O  
ATOM    280  CB  VAL A  37      11.555  -8.928 -35.905  1.00 15.34           C  
ATOM    281  CG1 VAL A  37      13.031  -8.993 -35.445  1.00 17.68           C  
ATOM    282  CG2 VAL A  37      10.631  -9.110 -34.682  1.00 15.19           C  
ATOM    283  N   ARG A  38      13.177  -6.400 -37.539  1.00 14.31           N  
ATOM    284  CA  ARG A  38      14.198  -6.065 -38.537  1.00 15.85           C  
ATOM    285  C   ARG A  38      15.595  -6.459 -38.080  1.00 16.13           C  
ATOM    286  O   ARG A  38      16.024  -6.073 -36.985  1.00 16.49           O  
ATOM    287  CB  ARG A  38      14.177  -4.550 -38.811  1.00 15.31           C  
ATOM    288  CG  ARG A  38      15.335  -4.028 -39.700  1.00 17.63           C  
ATOM    289  CD  ARG A  38      15.275  -2.503 -39.803  1.00 19.96           C  
ATOM    290  NE  ARG A  38      16.250  -1.910 -40.725  1.00 21.92           N  
ATOM    291  CZ  ARG A  38      17.570  -1.934 -40.557  1.00 22.66           C  
ATOM    292  NH1 ARG A  38      18.101  -2.535 -39.502  1.00 24.04           N  
ATOM    293  NH2 ARG A  38      18.364  -1.322 -41.436  1.00 23.41           N  
ATOM    294  N   THR A  39      16.292  -7.246 -38.896  1.00 17.16           N  
ATOM    295  CA  THR A  39      17.663  -7.627 -38.585  1.00 17.96           C  
ATOM    296  C   THR A  39      18.604  -6.924 -39.562  1.00 18.54           C  
ATOM    297  O   THR A  39      19.811  -6.855 -39.324  1.00 19.97           O  
ATOM    298  CB  THR A  39      17.901  -9.166 -38.652  1.00 19.42           C  
ATOM    299  OG1 THR A  39      17.481  -9.679 -39.924  1.00 19.67           O  
ATOM    300  CG2 THR A  39      17.122  -9.882 -37.539  1.00 18.96           C  
ATOM    301  N   SER A  40      18.061  -6.425 -40.675  1.00 18.01           N  
ATOM    302  CA  SER A  40      18.861  -5.690 -41.663  1.00 18.67           C  
ATOM    303  C   SER A  40      17.924  -5.030 -42.673  1.00 19.72           C  
ATOM    304  O   SER A  40      16.703  -5.249 -42.637  1.00 18.61           O  
ATOM    305  CB  SER A  40      19.834  -6.632 -42.410  1.00 18.35           C  
ATOM    306  OG  SER A  40      19.319  -7.043 -43.671  1.00 18.61           O  
ATOM    307  N   PRO A  41      18.469  -4.192 -43.571  1.00 20.62           N  
ATOM    308  CA  PRO A  41      17.610  -3.546 -44.573  1.00 22.01           C  
ATOM    309  C   PRO A  41      16.824  -4.554 -45.435  1.00 21.57           C  
ATOM    310  O   PRO A  41      15.724  -4.260 -45.903  1.00 23.50           O  
ATOM    311  CB  PRO A  41      18.612  -2.740 -45.413  1.00 22.65           C  
ATOM    312  CG  PRO A  41      19.668  -2.384 -44.429  1.00 22.59           C  
ATOM    313  CD  PRO A  41      19.848  -3.676 -43.657  1.00 21.85           C  
ATOM    314  N   ASN A  42      17.377  -5.748 -45.630  1.00 21.48           N  
ATOM    315  CA  ASN A  42      16.740  -6.772 -46.472  1.00 21.04           C  
ATOM    316  C   ASN A  42      16.094  -7.926 -45.736  1.00 20.13           C  
ATOM    317  O   ASN A  42      15.571  -8.851 -46.371  1.00 19.36           O  
ATOM    318  CB  ASN A  42      17.766  -7.371 -47.436  1.00 23.60           C  
ATOM    319  CG  ASN A  42      18.056  -6.472 -48.612  1.00 26.40           C  
ATOM    320  OD1 ASN A  42      17.345  -5.502 -48.849  1.00 29.52           O  
ATOM    321  ND2 ASN A  42      19.099  -6.798 -49.366  1.00 27.57           N  
ATOM    322  N   HIS A  43      16.106  -7.881 -44.407  1.00 18.61           N  
ATOM    323  CA  HIS A  43      15.547  -8.980 -43.629  1.00 17.72           C  
ATOM    324  C   HIS A  43      14.580  -8.512 -42.552  1.00 16.98           C  
ATOM    325  O   HIS A  43      14.998  -7.957 -41.529  1.00 16.21           O  
ATOM    326  CB  HIS A  43      16.709  -9.775 -43.021  1.00 18.10           C  
ATOM    327  CG  HIS A  43      17.692 -10.254 -44.044  1.00 20.36           C  
ATOM    328  ND1 HIS A  43      17.593 -11.485 -44.659  1.00 22.40           N  
ATOM    329  CD2 HIS A  43      18.757  -9.638 -44.605  1.00 19.83           C  
ATOM    330  CE1 HIS A  43      18.560 -11.605 -45.553  1.00 20.79           C  
ATOM    331  NE2 HIS A  43      19.278 -10.499 -45.539  1.00 21.37           N  
ATOM    332  N   LYS A  44      13.293  -8.734 -42.810  1.00 17.39           N  
ATOM    333  CA  LYS A  44      12.201  -8.355 -41.910  1.00 17.69           C  
ATOM    334  C   LYS A  44      11.301  -9.578 -41.742  1.00 17.40           C  
ATOM    335  O   LYS A  44      11.055 -10.307 -42.710  1.00 16.95           O  
ATOM    336  CB  LYS A  44      11.357  -7.234 -42.523  1.00 20.64           C  
ATOM    337  CG  LYS A  44      12.110  -6.009 -43.040  1.00 24.92           C  
ATOM    338  CD  LYS A  44      12.654  -5.180 -41.924  1.00 28.03           C  
ATOM    339  CE  LYS A  44      12.800  -3.710 -42.354  1.00 30.15           C  
ATOM    340  NZ  LYS A  44      13.626  -3.539 -43.581  1.00 31.57           N  
ATOM    341  N   TYR A  45      10.782  -9.779 -40.532  1.00 15.07           N  
ATOM    342  CA  TYR A  45       9.923 -10.931 -40.245  1.00 14.35           C  
ATOM    343  C   TYR A  45       8.765 -10.514 -39.361  1.00 13.73           C  
ATOM    344  O   TYR A  45       8.953  -9.771 -38.398  1.00 12.78           O  
ATOM    345  CB  TYR A  45      10.716 -12.004 -39.503  1.00 14.38           C  
ATOM    346  CG  TYR A  45      11.982 -12.397 -40.217  1.00 16.63           C  
ATOM    347  CD1 TYR A  45      13.159 -11.649 -40.063  1.00 17.12           C  
ATOM    348  CD2 TYR A  45      11.982 -13.455 -41.119  1.00 16.58           C  
ATOM    349  CE1 TYR A  45      14.300 -11.954 -40.809  1.00 18.37           C  
ATOM    350  CE2 TYR A  45      13.117 -13.760 -41.866  1.00 17.99           C  
ATOM    351  CZ  TYR A  45      14.262 -13.005 -41.706  1.00 18.50           C  
ATOM    352  OH  TYR A  45      15.368 -13.298 -42.478  1.00 21.02           O  
ATOM    353  N   ILE A  46       7.577 -11.013 -39.667  1.00 12.47           N  
ATOM    354  CA  ILE A  46       6.412 -10.668 -38.875  1.00 13.20           C  
ATOM    355  C   ILE A  46       6.020 -11.759 -37.874  1.00 13.09           C  
ATOM    356  O   ILE A  46       5.935 -12.938 -38.222  1.00 12.70           O  
ATOM    357  CB  ILE A  46       5.239 -10.284 -39.821  1.00 14.30           C  
ATOM    358  CG1 ILE A  46       5.648  -9.031 -40.603  1.00 15.88           C  
ATOM    359  CG2 ILE A  46       3.952  -9.983 -39.013  1.00 13.51           C  
ATOM    360  CD1 ILE A  46       4.715  -8.668 -41.705  1.00 18.11           C  
ATOM    361  N   PHE A  47       5.836 -11.348 -36.615  1.00 12.40           N  
ATOM    362  CA  PHE A  47       5.446 -12.240 -35.515  1.00 13.16           C  
ATOM    363  C   PHE A  47       4.266 -11.661 -34.754  1.00 12.62           C  
ATOM    364  O   PHE A  47       4.041 -10.444 -34.736  1.00 13.60           O  
ATOM    365  CB  PHE A  47       6.554 -12.399 -34.458  1.00 13.05           C  
ATOM    366  CG  PHE A  47       7.825 -13.025 -34.965  1.00 15.35           C  
ATOM    367  CD1 PHE A  47       8.809 -12.246 -35.589  1.00 15.24           C  
ATOM    368  CD2 PHE A  47       8.050 -14.394 -34.799  1.00 15.76           C  
ATOM    369  CE1 PHE A  47       9.996 -12.816 -36.035  1.00 14.79           C  
ATOM    370  CE2 PHE A  47       9.247 -14.975 -35.245  1.00 16.54           C  
ATOM    371  CZ  PHE A  47      10.220 -14.181 -35.862  1.00 15.94           C  
ATOM    372  N   THR A  48       3.527 -12.541 -34.101  1.00 12.85           N  
ATOM    373  CA  THR A  48       2.411 -12.132 -33.262  1.00 12.98           C  
ATOM    374  C   THR A  48       2.951 -12.289 -31.829  1.00 14.15           C  
ATOM    375  O   THR A  48       3.689 -13.225 -31.547  1.00 13.04           O  
ATOM    376  CB  THR A  48       1.209 -13.043 -33.501  1.00 13.95           C  
ATOM    377  OG1 THR A  48       0.764 -12.848 -34.853  1.00 12.89           O  
ATOM    378  CG2 THR A  48       0.061 -12.715 -32.526  1.00 14.51           C  
ATOM    379  N   LEU A  49       2.597 -11.362 -30.944  1.00 14.34           N  
ATOM    380  CA  LEU A  49       3.081 -11.368 -29.564  1.00 14.58           C  
ATOM    381  C   LEU A  49       2.187 -11.983 -28.500  1.00 14.73           C  
ATOM    382  O   LEU A  49       0.949 -11.978 -28.617  1.00 15.59           O  
ATOM    383  CB  LEU A  49       3.362  -9.927 -29.115  1.00 15.77           C  
ATOM    384  CG  LEU A  49       4.219  -9.043 -30.027  1.00 15.43           C  
ATOM    385  CD1 LEU A  49       4.320  -7.635 -29.424  1.00 16.51           C  
ATOM    386  CD2 LEU A  49       5.587  -9.657 -30.182  1.00 16.13           C  
ATOM    387  N   ARG A  50       2.833 -12.491 -27.452  1.00 13.80           N  
ATOM    388  CA  ARG A  50       2.146 -13.026 -26.272  1.00 14.59           C  
ATOM    389  C   ARG A  50       3.007 -12.561 -25.080  1.00 13.53           C  
ATOM    390  O   ARG A  50       4.232 -12.695 -25.099  1.00 12.58           O  
ATOM    391  CB  ARG A  50       2.076 -14.571 -26.323  1.00 15.53           C  
ATOM    392  CG  ARG A  50       1.385 -15.230 -25.117  1.00 19.61           C  
ATOM    393  CD  ARG A  50      -0.076 -14.781 -24.997  1.00 20.84           C  
ATOM    394  NE  ARG A  50      -0.713 -15.245 -23.763  1.00 24.72           N  
ATOM    395  CZ  ARG A  50      -1.334 -16.411 -23.628  1.00 26.66           C  
ATOM    396  NH1 ARG A  50      -1.412 -17.247 -24.659  1.00 27.42           N  
ATOM    397  NH2 ARG A  50      -1.874 -16.748 -22.456  1.00 27.27           N  
ATOM    398  N   THR A  51       2.394 -11.993 -24.047  1.00 13.59           N  
ATOM    399  CA  THR A  51       3.196 -11.571 -22.902  1.00 13.63           C  
ATOM    400  C   THR A  51       3.405 -12.726 -21.921  1.00 13.77           C  
ATOM    401  O   THR A  51       2.653 -13.710 -21.931  1.00 12.81           O  
ATOM    402  CB  THR A  51       2.533 -10.395 -22.111  1.00 14.57           C  
ATOM    403  OG1 THR A  51       1.230 -10.793 -21.663  1.00 16.99           O  
ATOM    404  CG2 THR A  51       2.415  -9.139 -22.965  1.00 15.00           C  
ATOM    405  N   HIS A  52       4.456 -12.614 -21.105  1.00 15.61           N  
ATOM    406  CA  HIS A  52       4.758 -13.571 -20.028  1.00 16.11           C  
ATOM    407  C   HIS A  52       5.443 -12.742 -18.932  1.00 16.28           C  
ATOM    408  O   HIS A  52       6.318 -11.910 -19.217  1.00 16.25           O  
ATOM    409  CB  HIS A  52       5.662 -14.720 -20.484  1.00 16.92           C  
ATOM    410  CG  HIS A  52       5.824 -15.799 -19.451  1.00 17.57           C  
ATOM    411  ND1 HIS A  52       6.815 -15.770 -18.492  1.00 18.54           N  
ATOM    412  CD2 HIS A  52       5.093 -16.912 -19.201  1.00 19.30           C  
ATOM    413  CE1 HIS A  52       6.688 -16.819 -17.697  1.00 19.45           C  
ATOM    414  NE2 HIS A  52       5.651 -17.528 -18.105  1.00 19.07           N  
ATOM    415  N   PRO A  53       5.063 -12.954 -17.663  1.00 17.33           N  
ATOM    416  CA  PRO A  53       5.660 -12.190 -16.552  1.00 18.24           C  
ATOM    417  C   PRO A  53       7.185 -12.244 -16.429  1.00 19.24           C  
ATOM    418  O   PRO A  53       7.804 -11.308 -15.909  1.00 19.89           O  
ATOM    419  CB  PRO A  53       4.962 -12.774 -15.304  1.00 18.40           C  
ATOM    420  CG  PRO A  53       3.673 -13.293 -15.835  1.00 18.12           C  
ATOM    421  CD  PRO A  53       4.083 -13.928 -17.160  1.00 17.91           C  
ATOM    422  N   SER A  54       7.798 -13.325 -16.911  1.00 19.00           N  
ATOM    423  CA  SER A  54       9.248 -13.487 -16.790  1.00 19.67           C  
ATOM    424  C   SER A  54      10.139 -12.710 -17.757  1.00 19.17           C  
ATOM    425  O   SER A  54      11.355 -12.595 -17.528  1.00 18.39           O  
ATOM    426  CB  SER A  54       9.609 -14.974 -16.899  1.00 21.61           C  
ATOM    427  OG  SER A  54       9.538 -15.404 -18.256  1.00 24.64           O  
ATOM    428  N   VAL A  55       9.567 -12.190 -18.841  1.00 16.87           N  
ATOM    429  CA  VAL A  55      10.368 -11.455 -19.826  1.00 16.45           C  
ATOM    430  C   VAL A  55      10.866 -10.114 -19.296  1.00 15.73           C  
ATOM    431  O   VAL A  55      10.106  -9.343 -18.707  1.00 15.78           O  
ATOM    432  CB  VAL A  55       9.573 -11.194 -21.126  1.00 15.74           C  
ATOM    433  CG1 VAL A  55      10.435 -10.383 -22.131  1.00 14.98           C  
ATOM    434  CG2 VAL A  55       9.155 -12.510 -21.740  1.00 17.25           C  
ATOM    435  N   VAL A  56      12.150  -9.847 -19.508  1.00 14.64           N  
ATOM    436  CA  VAL A  56      12.744  -8.596 -19.069  1.00 14.83           C  
ATOM    437  C   VAL A  56      12.415  -7.495 -20.084  1.00 15.38           C  
ATOM    438  O   VAL A  56      12.583  -7.686 -21.294  1.00 16.04           O  
ATOM    439  CB  VAL A  56      14.299  -8.734 -18.925  1.00 14.68           C  
ATOM    440  CG1 VAL A  56      14.897  -7.464 -18.299  1.00 13.74           C  
ATOM    441  CG2 VAL A  56      14.641  -9.964 -18.059  1.00 13.13           C  
ATOM    442  N   PRO A  57      11.906  -6.345 -19.611  1.00 15.73           N  
ATOM    443  CA  PRO A  57      11.572  -5.238 -20.514  1.00 16.49           C  
ATOM    444  C   PRO A  57      12.773  -4.918 -21.410  1.00 16.50           C  
ATOM    445  O   PRO A  57      13.927  -4.936 -20.956  1.00 17.04           O  
ATOM    446  CB  PRO A  57      11.256  -4.091 -19.558  1.00 15.78           C  
ATOM    447  CG  PRO A  57      10.668  -4.820 -18.349  1.00 16.63           C  
ATOM    448  CD  PRO A  57      11.584  -6.014 -18.204  1.00 16.05           C  
ATOM    449  N   GLY A  58      12.519  -4.629 -22.681  1.00 16.19           N  
ATOM    450  CA  GLY A  58      13.629  -4.332 -23.566  1.00 16.47           C  
ATOM    451  C   GLY A  58      14.137  -5.563 -24.300  1.00 16.35           C  
ATOM    452  O   GLY A  58      15.164  -5.512 -24.976  1.00 16.92           O  
ATOM    453  N   SER A  59      13.450  -6.689 -24.146  1.00 15.55           N  
ATOM    454  CA  SER A  59      13.861  -7.890 -24.854  1.00 15.25           C  
ATOM    455  C   SER A  59      12.628  -8.575 -25.421  1.00 14.38           C  
ATOM    456  O   SER A  59      11.501  -8.345 -24.963  1.00 15.08           O  
ATOM    457  CB  SER A  59      14.617  -8.870 -23.917  1.00 15.38           C  
ATOM    458  OG  SER A  59      13.742  -9.500 -22.973  1.00 15.59           O  
ATOM    459  N   VAL A  60      12.851  -9.393 -26.439  1.00 14.16           N  
ATOM    460  CA  VAL A  60      11.801 -10.183 -27.072  1.00 14.40           C  
ATOM    461  C   VAL A  60      12.357 -11.603 -27.107  1.00 14.69           C  
ATOM    462  O   VAL A  60      13.482 -11.833 -27.565  1.00 13.60           O  
ATOM    463  CB  VAL A  60      11.499  -9.707 -28.509  1.00 15.28           C  
ATOM    464  CG1 VAL A  60      10.376 -10.577 -29.121  1.00 14.10           C  
ATOM    465  CG2 VAL A  60      11.071  -8.237 -28.477  1.00 16.22           C  
ATOM    466  N   ALA A  61      11.573 -12.555 -26.618  1.00 13.93           N  
ATOM    467  CA  ALA A  61      12.023 -13.940 -26.572  1.00 14.94           C  
ATOM    468  C   ALA A  61      11.488 -14.751 -27.755  1.00 15.06           C  
ATOM    469  O   ALA A  61      10.305 -14.635 -28.129  1.00 15.16           O  
ATOM    470  CB  ALA A  61      11.585 -14.579 -25.252  1.00 14.60           C  
ATOM    471  N   PHE A  62      12.370 -15.570 -28.325  1.00 14.65           N  
ATOM    472  CA  PHE A  62      12.057 -16.428 -29.467  1.00 15.84           C  
ATOM    473  C   PHE A  62      12.460 -17.864 -29.188  1.00 16.63           C  
ATOM    474  O   PHE A  62      13.422 -18.118 -28.466  1.00 16.50           O  
ATOM    475  CB  PHE A  62      12.814 -15.971 -30.725  1.00 15.10           C  
ATOM    476  CG  PHE A  62      12.574 -14.531 -31.101  1.00 13.35           C  
ATOM    477  CD1 PHE A  62      13.353 -13.513 -30.539  1.00 14.50           C  
ATOM    478  CD2 PHE A  62      11.581 -14.195 -32.028  1.00 13.48           C  
ATOM    479  CE1 PHE A  62      13.148 -12.167 -30.897  1.00 14.76           C  
ATOM    480  CE2 PHE A  62      11.359 -12.845 -32.401  1.00 14.10           C  
ATOM    481  CZ  PHE A  62      12.144 -11.835 -31.836  1.00 15.23           C  
ATOM    482  N   SER A  63      11.727 -18.793 -29.786  1.00 17.09           N  
ATOM    483  CA  SER A  63      11.997 -20.210 -29.632  1.00 17.64           C  
ATOM    484  C   SER A  63      13.015 -20.609 -30.683  1.00 17.74           C  
ATOM    485  O   SER A  63      13.294 -19.853 -31.618  1.00 14.61           O  
ATOM    486  CB  SER A  63      10.718 -21.014 -29.828  1.00 19.38           C  
ATOM    487  OG  SER A  63      10.265 -20.916 -31.173  1.00 23.08           O  
ATOM    488  N   LEU A  64      13.572 -21.803 -30.531  1.00 17.10           N  
ATOM    489  CA  LEU A  64      14.570 -22.281 -31.469  1.00 18.67           C  
ATOM    490  C   LEU A  64      14.093 -22.272 -32.928  1.00 18.11           C  
ATOM    491  O   LEU A  64      14.822 -21.816 -33.819  1.00 17.33           O  
ATOM    492  CB  LEU A  64      15.029 -23.683 -31.053  1.00 21.12           C  
ATOM    493  CG  LEU A  64      15.999 -24.363 -32.015  1.00 21.94           C  
ATOM    494  CD1 LEU A  64      17.263 -23.536 -32.115  1.00 22.51           C  
ATOM    495  CD2 LEU A  64      16.309 -25.779 -31.496  1.00 24.48           C  
ATOM    496  N   PRO A  65      12.866 -22.762 -33.202  1.00 17.84           N  
ATOM    497  CA  PRO A  65      12.367 -22.767 -34.586  1.00 18.52           C  
ATOM    498  C   PRO A  65      12.302 -21.359 -35.184  1.00 17.06           C  
ATOM    499  O   PRO A  65      12.628 -21.147 -36.359  1.00 16.38           O  
ATOM    500  CB  PRO A  65      10.971 -23.383 -34.458  1.00 19.36           C  
ATOM    501  CG  PRO A  65      11.087 -24.253 -33.254  1.00 19.77           C  
ATOM    502  CD  PRO A  65      11.909 -23.424 -32.300  1.00 19.93           C  
ATOM    503  N   GLN A  66      11.883 -20.394 -34.372  1.00 16.65           N  
ATOM    504  CA  GLN A  66      11.782 -19.009 -34.838  1.00 15.61           C  
ATOM    505  C   GLN A  66      13.176 -18.440 -35.095  1.00 15.81           C  
ATOM    506  O   GLN A  66      13.395 -17.720 -36.082  1.00 14.85           O  
ATOM    507  CB  GLN A  66      11.048 -18.150 -33.803  1.00 17.30           C  
ATOM    508  CG  GLN A  66       9.604 -18.570 -33.550  1.00 18.09           C  
ATOM    509  CD  GLN A  66       8.991 -17.790 -32.412  1.00 20.37           C  
ATOM    510  OE1 GLN A  66       9.667 -17.504 -31.427  1.00 22.02           O  
ATOM    511  NE2 GLN A  66       7.705 -17.458 -32.524  1.00 19.91           N  
ATOM    512  N   ARG A  67      14.119 -18.767 -34.214  1.00 15.17           N  
ATOM    513  CA  ARG A  67      15.489 -18.284 -34.369  1.00 16.75           C  
ATOM    514  C   ARG A  67      16.120 -18.856 -35.651  1.00 16.87           C  
ATOM    515  O   ARG A  67      16.862 -18.161 -36.357  1.00 17.25           O  
ATOM    516  CB  ARG A  67      16.346 -18.683 -33.156  1.00 16.52           C  
ATOM    517  CG  ARG A  67      16.249 -17.773 -31.920  1.00 20.22           C  
ATOM    518  CD  ARG A  67      17.228 -18.279 -30.838  1.00 21.86           C  
ATOM    519  NE  ARG A  67      16.412 -18.787 -29.757  1.00 28.51           N  
ATOM    520  CZ  ARG A  67      16.525 -19.960 -29.159  1.00 26.69           C  
ATOM    521  NH1 ARG A  67      17.456 -20.850 -29.486  1.00 27.83           N  
ATOM    522  NH2 ARG A  67      15.647 -20.238 -28.230  1.00 29.12           N  
ATOM    523  N   LYS A  68      15.830 -20.116 -35.952  1.00 17.19           N  
ATOM    524  CA  LYS A  68      16.386 -20.754 -37.147  1.00 19.13           C  
ATOM    525  C   LYS A  68      15.733 -20.269 -38.439  1.00 18.92           C  
ATOM    526  O   LYS A  68      16.339 -20.338 -39.520  1.00 20.48           O  
ATOM    527  CB  LYS A  68      16.264 -22.272 -37.033  1.00 20.76           C  
ATOM    528  CG  LYS A  68      16.929 -22.806 -35.777  1.00 25.53           C  
ATOM    529  CD  LYS A  68      16.574 -24.268 -35.512  1.00 28.60           C  
ATOM    530  CE  LYS A  68      17.475 -25.224 -36.272  1.00 32.19           C  
ATOM    531  NZ  LYS A  68      17.168 -26.662 -35.935  1.00 32.92           N  
ATOM    532  N   TRP A  69      14.498 -19.786 -38.343  1.00 17.67           N  
ATOM    533  CA  TRP A  69      13.832 -19.267 -39.530  1.00 16.82           C  
ATOM    534  C   TRP A  69      14.221 -17.817 -39.787  1.00 16.41           C  
ATOM    535  O   TRP A  69      14.601 -17.458 -40.901  1.00 17.10           O  
ATOM    536  CB  TRP A  69      12.308 -19.356 -39.400  1.00 16.63           C  
ATOM    537  CG  TRP A  69      11.568 -18.545 -40.470  1.00 15.64           C  
ATOM    538  CD1 TRP A  69      11.634 -18.721 -41.831  1.00 16.06           C  
ATOM    539  CD2 TRP A  69      10.624 -17.493 -40.249  1.00 15.93           C  
ATOM    540  NE1 TRP A  69      10.776 -17.846 -42.463  1.00 14.90           N  
ATOM    541  CE2 TRP A  69      10.143 -17.085 -41.516  1.00 15.12           C  
ATOM    542  CE3 TRP A  69      10.124 -16.858 -39.097  1.00 16.00           C  
ATOM    543  CZ2 TRP A  69       9.185 -16.069 -41.667  1.00 15.46           C  
ATOM    544  CZ3 TRP A  69       9.175 -15.851 -39.244  1.00 15.92           C  
ATOM    545  CH2 TRP A  69       8.713 -15.466 -40.526  1.00 14.75           C  
ATOM    546  N   ALA A  70      14.138 -16.974 -38.767  1.00 15.87           N  
ATOM    547  CA  ALA A  70      14.462 -15.556 -38.962  1.00 16.18           C  
ATOM    548  C   ALA A  70      15.964 -15.231 -38.849  1.00 16.61           C  
ATOM    549  O   ALA A  70      16.374 -14.094 -39.086  1.00 17.96           O  
ATOM    550  CB  ALA A  70      13.641 -14.693 -37.974  1.00 14.45           C  
ATOM    551  N   GLY A  71      16.781 -16.218 -38.479  1.00 15.97           N  
ATOM    552  CA  GLY A  71      18.214 -15.992 -38.372  1.00 15.97           C  
ATOM    553  C   GLY A  71      18.586 -15.074 -37.222  1.00 17.45           C  
ATOM    554  O   GLY A  71      19.316 -14.089 -37.407  1.00 18.19           O  
ATOM    555  N   LEU A  72      18.073 -15.399 -36.040  1.00 16.79           N  
ATOM    556  CA  LEU A  72      18.298 -14.622 -34.832  1.00 18.24           C  
ATOM    557  C   LEU A  72      19.203 -15.352 -33.850  1.00 18.50           C  
ATOM    558  O   LEU A  72      19.144 -16.578 -33.730  1.00 19.50           O  
ATOM    559  CB  LEU A  72      16.956 -14.344 -34.137  1.00 18.17           C  
ATOM    560  CG  LEU A  72      15.882 -13.598 -34.938  1.00 19.51           C  
ATOM    561  CD1 LEU A  72      14.603 -13.570 -34.140  1.00 20.62           C  
ATOM    562  CD2 LEU A  72      16.333 -12.168 -35.246  1.00 20.52           C  
ATOM    563  N   SER A  73      20.026 -14.585 -33.145  1.00 18.72           N  
ATOM    564  CA  SER A  73      20.940 -15.123 -32.140  1.00 18.57           C  
ATOM    565  C   SER A  73      20.553 -14.559 -30.779  1.00 17.77           C  
ATOM    566  O   SER A  73      20.183 -13.399 -30.676  1.00 16.51           O  
ATOM    567  CB  SER A  73      22.382 -14.703 -32.441  1.00 19.61           C  
ATOM    568  OG  SER A  73      22.854 -15.312 -33.631  1.00 23.06           O  
ATOM    569  N   ILE A  74      20.632 -15.381 -29.740  1.00 18.03           N  
ATOM    570  CA  ILE A  74      20.310 -14.913 -28.394  1.00 18.45           C  
ATOM    571  C   ILE A  74      21.328 -13.831 -28.038  1.00 19.17           C  
ATOM    572  O   ILE A  74      22.542 -14.012 -28.223  1.00 18.75           O  
ATOM    573  CB  ILE A  74      20.380 -16.068 -27.360  1.00 18.86           C  
ATOM    574  CG1 ILE A  74      19.253 -17.072 -27.641  1.00 19.76           C  
ATOM    575  CG2 ILE A  74      20.229 -15.516 -25.935  1.00 18.43           C  
ATOM    576  CD1 ILE A  74      19.316 -18.353 -26.811  1.00 21.43           C  
ATOM    577  N   GLY A  75      20.823 -12.696 -27.559  1.00 17.68           N  
ATOM    578  CA  GLY A  75      21.689 -11.590 -27.197  1.00 19.39           C  
ATOM    579  C   GLY A  75      21.869 -10.527 -28.266  1.00 19.79           C  
ATOM    580  O   GLY A  75      22.429  -9.469 -27.991  1.00 20.63           O  
ATOM    581  N   GLN A  76      21.391 -10.773 -29.483  1.00 19.38           N  
ATOM    582  CA  GLN A  76      21.578  -9.785 -30.526  1.00 20.14           C  
ATOM    583  C   GLN A  76      20.577  -8.624 -30.466  1.00 20.80           C  
ATOM    584  O   GLN A  76      19.474  -8.746 -29.924  1.00 19.37           O  
ATOM    585  CB  GLN A  76      21.535 -10.459 -31.905  1.00 21.48           C  
ATOM    586  CG  GLN A  76      20.230 -10.384 -32.646  1.00 22.16           C  
ATOM    587  CD  GLN A  76      20.347 -10.889 -34.080  1.00 23.76           C  
ATOM    588  OE1 GLN A  76      20.601 -12.072 -34.316  1.00 21.73           O  
ATOM    589  NE2 GLN A  76      20.162  -9.989 -35.047  1.00 24.85           N  
ATOM    590  N   GLU A  77      20.981  -7.493 -31.024  1.00 20.54           N  
ATOM    591  CA  GLU A  77      20.127  -6.320 -31.058  1.00 22.30           C  
ATOM    592  C   GLU A  77      19.251  -6.419 -32.300  1.00 21.58           C  
ATOM    593  O   GLU A  77      19.727  -6.819 -33.375  1.00 21.40           O  
ATOM    594  CB  GLU A  77      20.988  -5.048 -31.102  1.00 25.34           C  
ATOM    595  CG  GLU A  77      20.203  -3.744 -31.220  1.00 30.76           C  
ATOM    596  CD  GLU A  77      21.069  -2.507 -30.972  1.00 34.48           C  
ATOM    597  OE1 GLU A  77      22.191  -2.412 -31.529  1.00 36.83           O  
ATOM    598  OE2 GLU A  77      20.624  -1.613 -30.221  1.00 37.29           O  
ATOM    599  N   ILE A  78      17.970  -6.094 -32.144  1.00 18.96           N  
ATOM    600  CA  ILE A  78      17.019  -6.117 -33.257  1.00 19.38           C  
ATOM    601  C   ILE A  78      16.148  -4.872 -33.169  1.00 18.75           C  
ATOM    602  O   ILE A  78      16.080  -4.222 -32.125  1.00 19.28           O  
ATOM    603  CB  ILE A  78      16.041  -7.321 -33.180  1.00 18.97           C  
ATOM    604  CG1 ILE A  78      15.395  -7.348 -31.787  1.00 19.82           C  
ATOM    605  CG2 ILE A  78      16.767  -8.641 -33.501  1.00 20.62           C  
ATOM    606  CD1 ILE A  78      14.230  -8.291 -31.644  1.00 20.03           C  
ATOM    607  N   GLU A  79      15.490  -4.522 -34.267  1.00 17.95           N  
ATOM    608  CA  GLU A  79      14.578  -3.392 -34.237  1.00 17.43           C  
ATOM    609  C   GLU A  79      13.189  -3.987 -34.398  1.00 16.44           C  
ATOM    610  O   GLU A  79      12.973  -4.874 -35.236  1.00 14.82           O  
ATOM    611  CB  GLU A  79      14.884  -2.393 -35.347  1.00 20.06           C  
ATOM    612  CG  GLU A  79      15.923  -1.384 -34.925  1.00 26.35           C  
ATOM    613  CD  GLU A  79      16.220  -0.347 -35.995  1.00 28.08           C  
ATOM    614  OE1 GLU A  79      15.272   0.309 -36.495  1.00 30.75           O  
ATOM    615  OE2 GLU A  79      17.412  -0.189 -36.317  1.00 31.44           O  
ATOM    616  N   VAL A  80      12.260  -3.502 -33.581  1.00 14.38           N  
ATOM    617  CA  VAL A  80      10.893  -4.010 -33.577  1.00 14.55           C  
ATOM    618  C   VAL A  80       9.867  -2.887 -33.698  1.00 15.70           C  
ATOM    619  O   VAL A  80       9.916  -1.921 -32.946  1.00 15.52           O  
ATOM    620  CB  VAL A  80      10.607  -4.768 -32.259  1.00 14.50           C  
ATOM    621  CG1 VAL A  80       9.241  -5.409 -32.319  1.00 14.11           C  
ATOM    622  CG2 VAL A  80      11.704  -5.822 -32.003  1.00 15.08           C  
ATOM    623  N   ALA A  81       8.922  -3.032 -34.625  1.00 15.86           N  
ATOM    624  CA  ALA A  81       7.884  -2.025 -34.815  1.00 16.15           C  
ATOM    625  C   ALA A  81       6.506  -2.694 -34.898  1.00 16.07           C  
ATOM    626  O   ALA A  81       6.376  -3.803 -35.415  1.00 14.13           O  
ATOM    627  CB  ALA A  81       8.163  -1.215 -36.100  1.00 15.66           C  
ATOM    628  N   LEU A  82       5.487  -2.024 -34.372  1.00 15.66           N  
ATOM    629  CA  LEU A  82       4.128  -2.550 -34.441  1.00 17.55           C  
ATOM    630  C   LEU A  82       3.691  -2.635 -35.898  1.00 18.42           C  
ATOM    631  O   LEU A  82       3.963  -1.730 -36.709  1.00 17.93           O  
ATOM    632  CB  LEU A  82       3.155  -1.649 -33.662  1.00 18.53           C  
ATOM    633  CG  LEU A  82       3.316  -1.755 -32.143  1.00 20.00           C  
ATOM    634  CD1 LEU A  82       2.407  -0.747 -31.436  1.00 21.22           C  
ATOM    635  CD2 LEU A  82       2.966  -3.186 -31.715  1.00 20.14           C  
ATOM    636  N   TYR A  83       3.005  -3.722 -36.222  1.00 18.20           N  
ATOM    637  CA  TYR A  83       2.524  -3.978 -37.574  1.00 19.77           C  
ATOM    638  C   TYR A  83       1.010  -4.164 -37.550  1.00 20.67           C  
ATOM    639  O   TYR A  83       0.472  -4.836 -36.664  1.00 20.85           O  
ATOM    640  CB  TYR A  83       3.189  -5.253 -38.105  1.00 20.25           C  
ATOM    641  CG  TYR A  83       2.784  -5.666 -39.501  1.00 22.63           C  
ATOM    642  CD1 TYR A  83       3.436  -5.146 -40.621  1.00 23.41           C  
ATOM    643  CD2 TYR A  83       1.767  -6.606 -39.700  1.00 23.32           C  
ATOM    644  CE1 TYR A  83       3.088  -5.551 -41.907  1.00 25.16           C  
ATOM    645  CE2 TYR A  83       1.406  -7.021 -40.984  1.00 25.15           C  
ATOM    646  CZ  TYR A  83       2.072  -6.488 -42.082  1.00 26.41           C  
ATOM    647  OH  TYR A  83       1.721  -6.891 -43.348  1.00 27.18           O  
ATOM    648  N   SER A  84       0.324  -3.556 -38.512  1.00 21.72           N  
ATOM    649  CA  SER A  84      -1.127  -3.684 -38.600  1.00 23.28           C  
ATOM    650  C   SER A  84      -1.520  -4.360 -39.901  1.00 22.10           C  
ATOM    651  O   SER A  84      -1.142  -3.908 -40.978  1.00 22.58           O  
ATOM    652  CB  SER A  84      -1.804  -2.308 -38.545  1.00 25.19           C  
ATOM    653  OG  SER A  84      -2.011  -1.881 -37.206  1.00 30.47           O  
ATOM    654  N   PHE A  85      -2.265  -5.452 -39.813  1.00 22.02           N  
ATOM    655  CA  PHE A  85      -2.720  -6.115 -41.025  1.00 21.89           C  
ATOM    656  C   PHE A  85      -3.911  -5.362 -41.627  1.00 23.55           C  
ATOM    657  O   PHE A  85      -4.673  -4.706 -40.910  1.00 22.67           O  
ATOM    658  CB  PHE A  85      -3.219  -7.534 -40.741  1.00 20.51           C  
ATOM    659  CG  PHE A  85      -2.140  -8.539 -40.523  1.00 19.69           C  
ATOM    660  CD1 PHE A  85      -1.695  -8.838 -39.235  1.00 18.76           C  
ATOM    661  CD2 PHE A  85      -1.604  -9.231 -41.600  1.00 19.54           C  
ATOM    662  CE1 PHE A  85      -0.735  -9.814 -39.023  1.00 18.56           C  
ATOM    663  CE2 PHE A  85      -0.642 -10.213 -41.408  1.00 19.76           C  
ATOM    664  CZ  PHE A  85      -0.202 -10.511 -40.113  1.00 19.04           C  
ATOM    665  N   ASP A  86      -4.067  -5.476 -42.943  1.00 24.20           N  
ATOM    666  CA  ASP A  86      -5.224  -4.906 -43.636  1.00 25.67           C  
ATOM    667  C   ASP A  86      -6.112  -6.151 -43.779  1.00 25.06           C  
ATOM    668  O   ASP A  86      -5.952  -6.941 -44.709  1.00 23.50           O  
ATOM    669  CB  ASP A  86      -4.822  -4.374 -45.012  1.00 27.11           C  
ATOM    670  CG  ASP A  86      -6.020  -3.969 -45.851  1.00 29.38           C  
ATOM    671  OD1 ASP A  86      -5.818  -3.361 -46.923  1.00 31.19           O  
ATOM    672  OD2 ASP A  86      -7.165  -4.263 -45.446  1.00 30.56           O  
ATOM    673  N   LYS A  87      -7.031  -6.336 -42.839  1.00 25.74           N  
ATOM    674  CA  LYS A  87      -7.896  -7.520 -42.829  1.00 27.35           C  
ATOM    675  C   LYS A  87      -8.785  -7.770 -44.053  1.00 28.45           C  
ATOM    676  O   LYS A  87      -9.286  -8.884 -44.249  1.00 29.21           O  
ATOM    677  CB  LYS A  87      -8.750  -7.530 -41.555  1.00 28.42           C  
ATOM    678  CG  LYS A  87      -7.928  -7.760 -40.276  1.00 30.29           C  
ATOM    679  CD  LYS A  87      -8.831  -7.998 -39.064  1.00 31.61           C  
ATOM    680  CE  LYS A  87      -7.993  -8.273 -37.812  1.00 33.58           C  
ATOM    681  NZ  LYS A  87      -8.855  -8.435 -36.604  1.00 35.10           N  
ATOM    682  N   ALA A  88      -8.977  -6.759 -44.885  1.00 28.98           N  
ATOM    683  CA  ALA A  88      -9.789  -6.957 -46.077  1.00 29.10           C  
ATOM    684  C   ALA A  88      -8.969  -7.670 -47.150  1.00 28.60           C  
ATOM    685  O   ALA A  88      -9.525  -8.252 -48.090  1.00 29.96           O  
ATOM    686  CB  ALA A  88     -10.288  -5.612 -46.598  1.00 29.21           C  
ATOM    687  N   LYS A  89      -7.647  -7.638 -47.013  1.00 27.09           N  
ATOM    688  CA  LYS A  89      -6.777  -8.266 -48.002  1.00 26.18           C  
ATOM    689  C   LYS A  89      -5.815  -9.337 -47.494  1.00 24.66           C  
ATOM    690  O   LYS A  89      -5.318 -10.154 -48.284  1.00 23.06           O  
ATOM    691  CB  LYS A  89      -5.943  -7.199 -48.715  1.00 28.11           C  
ATOM    692  CG  LYS A  89      -6.765  -6.165 -49.473  1.00 31.09           C  
ATOM    693  CD  LYS A  89      -5.916  -5.495 -50.543  1.00 34.34           C  
ATOM    694  CE  LYS A  89      -6.691  -4.403 -51.269  1.00 36.53           C  
ATOM    695  NZ  LYS A  89      -5.792  -3.608 -52.158  1.00 38.80           N  
ATOM    696  N   GLN A  90      -5.548  -9.353 -46.191  1.00 22.36           N  
ATOM    697  CA  GLN A  90      -4.583 -10.313 -45.669  1.00 21.28           C  
ATOM    698  C   GLN A  90      -5.075 -11.464 -44.795  1.00 20.76           C  
ATOM    699  O   GLN A  90      -4.258 -12.210 -44.280  1.00 19.72           O  
ATOM    700  CB  GLN A  90      -3.462  -9.561 -44.937  1.00 21.11           C  
ATOM    701  CG  GLN A  90      -2.728  -8.538 -45.797  1.00 22.40           C  
ATOM    702  CD  GLN A  90      -1.620  -7.825 -45.035  1.00 22.29           C  
ATOM    703  OE1 GLN A  90      -0.464  -8.274 -45.007  1.00 24.39           O  
ATOM    704  NE2 GLN A  90      -1.969  -6.726 -44.400  1.00 20.57           N  
ATOM    705  N   CYS A  91      -6.384 -11.618 -44.611  1.00 20.04           N  
ATOM    706  CA  CYS A  91      -6.860 -12.743 -43.817  1.00 20.27           C  
ATOM    707  C   CYS A  91      -6.704 -13.974 -44.696  1.00 19.84           C  
ATOM    708  O   CYS A  91      -6.996 -13.935 -45.897  1.00 19.46           O  
ATOM    709  CB  CYS A  91      -8.326 -12.571 -43.404  1.00 20.76           C  
ATOM    710  SG  CYS A  91      -8.579 -11.307 -42.140  1.00 23.89           S  
ATOM    711  N   ILE A  92      -6.236 -15.059 -44.090  1.00 18.15           N  
ATOM    712  CA  ILE A  92      -5.997 -16.301 -44.794  1.00 17.86           C  
ATOM    713  C   ILE A  92      -7.239 -17.135 -45.096  1.00 18.92           C  
ATOM    714  O   ILE A  92      -8.004 -17.482 -44.199  1.00 18.69           O  
ATOM    715  CB  ILE A  92      -4.964 -17.157 -44.002  1.00 17.18           C  
ATOM    716  CG1 ILE A  92      -3.624 -16.399 -43.968  1.00 16.72           C  
ATOM    717  CG2 ILE A  92      -4.820 -18.545 -44.634  1.00 17.57           C  
ATOM    718  CD1 ILE A  92      -2.555 -16.998 -43.090  1.00 14.52           C  
ATOM    719  N   GLY A  93      -7.447 -17.425 -46.377  1.00 18.49           N  
ATOM    720  CA  GLY A  93      -8.567 -18.249 -46.788  1.00 20.46           C  
ATOM    721  C   GLY A  93      -8.083 -19.685 -46.782  1.00 20.76           C  
ATOM    722  O   GLY A  93      -8.710 -20.560 -46.192  1.00 21.96           O  
ATOM    723  N   THR A  94      -6.951 -19.932 -47.427  1.00 20.98           N  
ATOM    724  CA  THR A  94      -6.388 -21.276 -47.463  1.00 22.62           C  
ATOM    725  C   THR A  94      -4.858 -21.195 -47.365  1.00 21.70           C  
ATOM    726  O   THR A  94      -4.238 -20.268 -47.886  1.00 20.84           O  
ATOM    727  CB  THR A  94      -6.768 -22.027 -48.775  1.00 24.45           C  
ATOM    728  OG1 THR A  94      -8.189 -21.961 -48.982  1.00 27.33           O  
ATOM    729  CG2 THR A  94      -6.363 -23.496 -48.676  1.00 25.07           C  
HETATM  730  N   MSE A  95      -4.265 -22.155 -46.669  1.00 22.14           N  
HETATM  731  CA  MSE A  95      -2.820 -22.218 -46.508  1.00 22.82           C  
HETATM  732  C   MSE A  95      -2.408 -23.672 -46.662  1.00 21.91           C  
HETATM  733  O   MSE A  95      -3.086 -24.582 -46.167  1.00 21.96           O  
HETATM  734  CB  MSE A  95      -2.400 -21.686 -45.126  1.00 25.22           C  
HETATM  735  CG  MSE A  95      -0.881 -21.756 -44.813  1.00 30.27           C  
HETATM  736 SE   MSE A  95      -0.371 -20.708 -43.334  1.00 39.40          SE  
HETATM  737  CE  MSE A  95      -1.823 -21.086 -42.216  1.00 31.97           C  
ATOM    738  N   THR A  96      -1.311 -23.887 -47.375  1.00 20.15           N  
ATOM    739  CA  THR A  96      -0.784 -25.227 -47.598  1.00 19.89           C  
ATOM    740  C   THR A  96       0.443 -25.327 -46.725  1.00 19.28           C  
ATOM    741  O   THR A  96       1.307 -24.451 -46.786  1.00 17.80           O  
ATOM    742  CB  THR A  96      -0.362 -25.428 -49.073  1.00 21.68           C  
ATOM    743  OG1 THR A  96      -1.506 -25.258 -49.919  1.00 25.01           O  
ATOM    744  CG2 THR A  96       0.217 -26.829 -49.276  1.00 22.43           C  
ATOM    745  N   ILE A  97       0.510 -26.400 -45.936  1.00 18.21           N  
ATOM    746  CA  ILE A  97       1.598 -26.638 -44.991  1.00 19.49           C  
ATOM    747  C   ILE A  97       2.250 -28.008 -45.164  1.00 19.52           C  
ATOM    748  O   ILE A  97       1.560 -29.038 -45.179  1.00 19.14           O  
ATOM    749  CB  ILE A  97       1.059 -26.537 -43.540  1.00 20.09           C  
ATOM    750  CG1 ILE A  97       0.540 -25.113 -43.295  1.00 20.56           C  
ATOM    751  CG2 ILE A  97       2.130 -26.943 -42.531  1.00 20.47           C  
ATOM    752  CD1 ILE A  97      -0.197 -24.953 -41.977  1.00 23.40           C  
ATOM    753  N   GLU A  98       3.574 -28.007 -45.288  1.00 19.70           N  
ATOM    754  CA  GLU A  98       4.346 -29.233 -45.412  1.00 20.57           C  
ATOM    755  C   GLU A  98       4.616 -29.701 -43.981  1.00 20.41           C  
ATOM    756  O   GLU A  98       5.028 -28.913 -43.125  1.00 18.99           O  
ATOM    757  CB  GLU A  98       5.665 -28.968 -46.158  1.00 22.65           C  
ATOM    758  CG  GLU A  98       6.533 -30.211 -46.364  1.00 27.11           C  
ATOM    759  CD  GLU A  98       7.840 -29.906 -47.097  1.00 30.41           C  
ATOM    760  OE1 GLU A  98       7.788 -29.430 -48.251  1.00 32.69           O  
ATOM    761  OE2 GLU A  98       8.926 -30.136 -46.519  1.00 32.95           O  
ATOM    762  N   ILE A  99       4.389 -30.983 -43.722  1.00 19.29           N  
ATOM    763  CA  ILE A  99       4.556 -31.520 -42.387  1.00 19.95           C  
ATOM    764  C   ILE A  99       5.368 -32.816 -42.358  1.00 21.54           C  
ATOM    765  O   ILE A  99       5.360 -33.589 -43.326  1.00 21.43           O  
ATOM    766  CB  ILE A  99       3.162 -31.771 -41.759  1.00 20.67           C  
ATOM    767  CG1 ILE A  99       3.288 -32.328 -40.344  1.00 20.95           C  
ATOM    768  CG2 ILE A  99       2.365 -32.743 -42.642  1.00 20.63           C  
ATOM    769  CD1 ILE A  99       1.954 -32.359 -39.603  1.00 23.17           C  
ATOM    770  N   ASP A 100       6.058 -33.035 -41.241  1.00 21.03           N  
ATOM    771  CA  ASP A 100       6.867 -34.233 -41.034  1.00 21.89           C  
ATOM    772  C   ASP A 100       7.109 -34.340 -39.537  1.00 21.66           C  
ATOM    773  O   ASP A 100       6.867 -33.381 -38.788  1.00 21.36           O  
ATOM    774  CB  ASP A 100       8.216 -34.121 -41.771  1.00 23.42           C  
ATOM    775  CG  ASP A 100       8.876 -35.489 -42.029  1.00 26.45           C  
ATOM    776  OD1 ASP A 100       8.413 -36.528 -41.486  1.00 26.09           O  
ATOM    777  OD2 ASP A 100       9.877 -35.516 -42.778  1.00 26.04           O  
ATOM    778  N   PHE A 101       7.562 -35.509 -39.096  1.00 21.02           N  
ATOM    779  CA  PHE A 101       7.867 -35.721 -37.694  1.00 21.98           C  
ATOM    780  C   PHE A 101       9.037 -34.795 -37.377  1.00 22.97           C  
ATOM    781  O   PHE A 101       9.895 -34.566 -38.234  1.00 22.47           O  
ATOM    782  CB  PHE A 101       8.275 -37.180 -37.446  1.00 22.13           C  
ATOM    783  CG  PHE A 101       7.137 -38.165 -37.580  1.00 21.50           C  
ATOM    784  CD1 PHE A 101       6.969 -38.897 -38.751  1.00 21.99           C  
ATOM    785  CD2 PHE A 101       6.260 -38.379 -36.524  1.00 22.50           C  
ATOM    786  CE1 PHE A 101       5.950 -39.837 -38.872  1.00 20.65           C  
ATOM    787  CE2 PHE A 101       5.226 -39.320 -36.625  1.00 22.50           C  
ATOM    788  CZ  PHE A 101       5.073 -40.053 -37.805  1.00 22.29           C  
ATOM    789  N   LEU A 102       9.062 -34.242 -36.167  1.00 24.61           N  
ATOM    790  CA  LEU A 102      10.141 -33.338 -35.788  1.00 27.38           C  
ATOM    791  C   LEU A 102      11.374 -34.116 -35.320  1.00 29.57           C  
ATOM    792  O   LEU A 102      12.501 -33.715 -35.581  1.00 29.53           O  
ATOM    793  CB  LEU A 102       9.693 -32.387 -34.669  1.00 27.11           C  
ATOM    794  CG  LEU A 102      10.739 -31.337 -34.246  1.00 27.20           C  
ATOM    795  CD1 LEU A 102      10.835 -30.262 -35.312  1.00 27.03           C  
ATOM    796  CD2 LEU A 102      10.348 -30.715 -32.912  1.00 28.00           C  
ATOM    797  N   GLN A 103      11.148 -35.228 -34.633  1.00 32.42           N  
ATOM    798  CA  GLN A 103      12.238 -36.048 -34.100  1.00 35.47           C  
ATOM    799  C   GLN A 103      12.248 -37.442 -34.748  1.00 36.83           C  
ATOM    800  O   GLN A 103      11.312 -38.225 -34.567  1.00 35.19           O  
ATOM    801  CB  GLN A 103      12.068 -36.155 -32.580  1.00 37.00           C  
ATOM    802  CG  GLN A 103      11.931 -34.788 -31.902  1.00 39.90           C  
ATOM    803  CD  GLN A 103      11.567 -34.871 -30.426  1.00 41.88           C  
ATOM    804  OE1 GLN A 103      10.467 -35.305 -30.060  1.00 43.48           O  
ATOM    805  NE2 GLN A 103      12.490 -34.451 -29.568  1.00 42.79           N  
ATOM    806  N   LYS A 104      13.299 -37.738 -35.514  1.00 39.21           N  
ATOM    807  CA  LYS A 104      13.399 -39.034 -36.189  1.00 41.34           C  
ATOM    808  C   LYS A 104      13.251 -40.188 -35.212  1.00 41.83           C  
ATOM    809  O   LYS A 104      12.824 -41.287 -35.577  1.00 42.02           O  
ATOM    810  CB  LYS A 104      14.718 -39.142 -36.953  1.00 42.26           C  
ATOM    811  CG  LYS A 104      15.850 -38.318 -36.389  1.00 44.15           C  
ATOM    812  CD  LYS A 104      16.958 -38.172 -37.432  1.00 45.96           C  
ATOM    813  CE  LYS A 104      16.412 -37.550 -38.716  1.00 46.35           C  
ATOM    814  NZ  LYS A 104      17.441 -37.456 -39.792  1.00 47.24           N  
ATOM    815  N   LYS A 105      13.584 -39.919 -33.957  1.00 42.71           N  
ATOM    816  CA  LYS A 105      13.467 -40.922 -32.913  1.00 42.93           C  
ATOM    817  C   LYS A 105      12.025 -41.385 -32.779  1.00 42.46           C  
ATOM    818  O   LYS A 105      11.756 -42.576 -32.598  1.00 43.08           O  
ATOM    819  CB  LYS A 105      13.898 -40.348 -31.556  1.00 43.86           C  
ATOM    820  CG  LYS A 105      15.335 -39.890 -31.469  1.00 45.55           C  
ATOM    821  CD  LYS A 105      16.293 -41.013 -31.835  1.00 46.63           C  
ATOM    822  CE  LYS A 105      17.738 -40.602 -31.608  1.00 47.22           C  
ATOM    823  NZ  LYS A 105      18.678 -41.601 -32.180  1.00 47.48           N  
ATOM    824  N   ASN A 106      11.097 -40.438 -32.887  1.00 41.30           N  
ATOM    825  CA  ASN A 106       9.683 -40.729 -32.685  1.00 39.52           C  
ATOM    826  C   ASN A 106       8.799 -41.010 -33.891  1.00 37.37           C  
ATOM    827  O   ASN A 106       7.573 -40.966 -33.792  1.00 36.29           O  
ATOM    828  CB  ASN A 106       9.095 -39.601 -31.847  1.00 41.60           C  
ATOM    829  CG  ASN A 106       9.999 -39.233 -30.686  1.00 43.36           C  
ATOM    830  OD1 ASN A 106      10.463 -40.110 -29.948  1.00 44.49           O  
ATOM    831  ND2 ASN A 106      10.267 -37.937 -30.521  1.00 44.40           N  
ATOM    832  N   ILE A 107       9.420 -41.309 -35.024  1.00 35.33           N  
ATOM    833  CA  ILE A 107       8.683 -41.625 -36.236  1.00 33.08           C  
ATOM    834  C   ILE A 107       7.909 -42.946 -36.082  1.00 32.58           C  
ATOM    835  O   ILE A 107       8.391 -43.887 -35.449  1.00 31.54           O  
ATOM    836  CB  ILE A 107       9.657 -41.753 -37.424  1.00 32.77           C  
ATOM    837  CG1 ILE A 107      10.272 -40.380 -37.737  1.00 32.16           C  
ATOM    838  CG2 ILE A 107       8.945 -42.338 -38.627  1.00 31.97           C  
ATOM    839  CD1 ILE A 107      11.313 -40.402 -38.843  1.00 31.04           C  
ATOM    840  N   ASP A 108       6.701 -43.002 -36.637  1.00 31.82           N  
ATOM    841  CA  ASP A 108       5.892 -44.219 -36.598  1.00 31.80           C  
ATOM    842  C   ASP A 108       5.017 -44.254 -37.835  1.00 30.48           C  
ATOM    843  O   ASP A 108       4.854 -43.242 -38.513  1.00 29.55           O  
ATOM    844  CB  ASP A 108       5.029 -44.302 -35.330  1.00 34.27           C  
ATOM    845  CG  ASP A 108       3.920 -43.259 -35.289  1.00 36.55           C  
ATOM    846  OD1 ASP A 108       3.115 -43.169 -36.247  1.00 36.95           O  
ATOM    847  OD2 ASP A 108       3.848 -42.531 -34.278  1.00 38.99           O  
ATOM    848  N   SER A 109       4.457 -45.420 -38.132  1.00 29.75           N  
ATOM    849  CA  SER A 109       3.627 -45.586 -39.321  1.00 28.74           C  
ATOM    850  C   SER A 109       2.126 -45.468 -39.061  1.00 28.36           C  
ATOM    851  O   SER A 109       1.319 -45.766 -39.944  1.00 28.06           O  
ATOM    852  CB  SER A 109       3.922 -46.942 -39.969  1.00 28.94           C  
ATOM    853  OG  SER A 109       3.548 -48.001 -39.113  1.00 29.95           O  
ATOM    854  N   ASN A 110       1.746 -45.032 -37.864  1.00 27.52           N  
ATOM    855  CA  ASN A 110       0.325 -44.882 -37.544  1.00 27.73           C  
ATOM    856  C   ASN A 110      -0.327 -43.730 -38.325  1.00 26.49           C  
ATOM    857  O   ASN A 110       0.340 -42.795 -38.755  1.00 24.99           O  
ATOM    858  CB  ASN A 110       0.136 -44.662 -36.041  1.00 30.49           C  
ATOM    859  CG  ASN A 110       0.548 -45.878 -35.215  1.00 33.21           C  
ATOM    860  OD1 ASN A 110       0.166 -47.014 -35.521  1.00 36.41           O  
ATOM    861  ND2 ASN A 110       1.318 -45.643 -34.156  1.00 33.86           N  
ATOM    862  N   PRO A 111      -1.651 -43.800 -38.528  1.00 26.07           N  
ATOM    863  CA  PRO A 111      -2.373 -42.758 -39.261  1.00 25.49           C  
ATOM    864  C   PRO A 111      -2.604 -41.503 -38.418  1.00 24.87           C  
ATOM    865  O   PRO A 111      -2.816 -41.589 -37.207  1.00 23.75           O  
ATOM    866  CB  PRO A 111      -3.684 -43.445 -39.618  1.00 26.52           C  
ATOM    867  CG  PRO A 111      -3.932 -44.285 -38.376  1.00 26.52           C  
ATOM    868  CD  PRO A 111      -2.557 -44.906 -38.156  1.00 26.05           C  
ATOM    869  N   TYR A 112      -2.542 -40.349 -39.073  1.00 23.42           N  
ATOM    870  CA  TYR A 112      -2.777 -39.059 -38.436  1.00 22.52           C  
ATOM    871  C   TYR A 112      -3.896 -38.395 -39.229  1.00 21.78           C  
ATOM    872  O   TYR A 112      -3.778 -38.188 -40.433  1.00 20.95           O  
ATOM    873  CB  TYR A 112      -1.490 -38.214 -38.432  1.00 22.53           C  
ATOM    874  CG  TYR A 112      -0.461 -38.782 -37.483  1.00 23.73           C  
ATOM    875  CD1 TYR A 112       0.416 -39.788 -37.885  1.00 23.12           C  
ATOM    876  CD2 TYR A 112      -0.444 -38.390 -36.143  1.00 25.19           C  
ATOM    877  CE1 TYR A 112       1.275 -40.394 -36.975  1.00 25.41           C  
ATOM    878  CE2 TYR A 112       0.412 -38.986 -35.223  1.00 26.07           C  
ATOM    879  CZ  TYR A 112       1.263 -39.988 -35.643  1.00 25.97           C  
ATOM    880  OH  TYR A 112       2.074 -40.601 -34.718  1.00 28.34           O  
ATOM    881  N   ASP A 113      -4.992 -38.095 -38.540  1.00 22.10           N  
ATOM    882  CA  ASP A 113      -6.187 -37.509 -39.145  1.00 23.25           C  
ATOM    883  C   ASP A 113      -6.005 -36.014 -39.441  1.00 23.00           C  
ATOM    884  O   ASP A 113      -5.954 -35.203 -38.513  1.00 22.31           O  
ATOM    885  CB  ASP A 113      -7.369 -37.738 -38.188  1.00 24.60           C  
ATOM    886  CG  ASP A 113      -8.715 -37.562 -38.854  1.00 27.61           C  
ATOM    887  OD1 ASP A 113      -8.866 -36.634 -39.681  1.00 28.37           O  
ATOM    888  OD2 ASP A 113      -9.636 -38.353 -38.533  1.00 28.60           O  
ATOM    889  N   THR A 114      -5.917 -35.655 -40.726  1.00 22.68           N  
ATOM    890  CA  THR A 114      -5.707 -34.260 -41.116  1.00 23.04           C  
ATOM    891  C   THR A 114      -6.883 -33.353 -40.796  1.00 23.87           C  
ATOM    892  O   THR A 114      -6.712 -32.148 -40.655  1.00 21.76           O  
ATOM    893  CB  THR A 114      -5.397 -34.088 -42.633  1.00 23.57           C  
ATOM    894  OG1 THR A 114      -6.488 -34.583 -43.422  1.00 23.74           O  
ATOM    895  CG2 THR A 114      -4.106 -34.797 -43.008  1.00 22.34           C  
ATOM    896  N   ASP A 115      -8.081 -33.922 -40.685  1.00 24.59           N  
ATOM    897  CA  ASP A 115      -9.239 -33.102 -40.382  1.00 26.30           C  
ATOM    898  C   ASP A 115      -9.164 -32.685 -38.917  1.00 25.91           C  
ATOM    899  O   ASP A 115      -9.495 -31.552 -38.561  1.00 25.39           O  
ATOM    900  CB  ASP A 115     -10.531 -33.861 -40.703  1.00 28.69           C  
ATOM    901  CG  ASP A 115     -10.645 -34.196 -42.190  1.00 31.57           C  
ATOM    902  OD1 ASP A 115     -10.463 -33.274 -43.010  1.00 33.93           O  
ATOM    903  OD2 ASP A 115     -10.900 -35.373 -42.550  1.00 33.92           O  
ATOM    904  N   LYS A 116      -8.695 -33.586 -38.067  1.00 25.11           N  
ATOM    905  CA  LYS A 116      -8.564 -33.245 -36.658  1.00 25.03           C  
ATOM    906  C   LYS A 116      -7.359 -32.319 -36.496  1.00 23.24           C  
ATOM    907  O   LYS A 116      -7.387 -31.390 -35.694  1.00 22.07           O  
ATOM    908  CB  LYS A 116      -8.398 -34.517 -35.817  1.00 26.79           C  
ATOM    909  CG  LYS A 116      -9.651 -35.390 -35.798  1.00 29.26           C  
ATOM    910  CD  LYS A 116      -9.338 -36.740 -35.178  1.00 32.88           C  
ATOM    911  CE  LYS A 116     -10.522 -37.706 -35.220  1.00 35.15           C  
ATOM    912  NZ  LYS A 116     -10.082 -39.108 -34.891  1.00 36.41           N  
HETATM  913  N   MSE A 117      -6.309 -32.579 -37.269  1.00 22.05           N  
HETATM  914  CA  MSE A 117      -5.099 -31.760 -37.231  1.00 23.11           C  
HETATM  915  C   MSE A 117      -5.407 -30.324 -37.658  1.00 21.59           C  
HETATM  916  O   MSE A 117      -4.933 -29.377 -37.046  1.00 20.76           O  
HETATM  917  CB  MSE A 117      -4.026 -32.322 -38.169  1.00 27.21           C  
HETATM  918  CG  MSE A 117      -3.341 -33.614 -37.713  1.00 34.72           C  
HETATM  919 SE   MSE A 117      -2.060 -34.200 -38.931  1.00 47.52          SE  
HETATM  920  CE  MSE A 117      -1.394 -32.584 -39.532  1.00 40.55           C  
ATOM    921  N   ALA A 118      -6.201 -30.175 -38.710  1.00 19.42           N  
ATOM    922  CA  ALA A 118      -6.556 -28.855 -39.223  1.00 20.18           C  
ATOM    923  C   ALA A 118      -7.364 -28.077 -38.186  1.00 19.92           C  
ATOM    924  O   ALA A 118      -7.180 -26.872 -38.016  1.00 19.94           O  
ATOM    925  CB  ALA A 118      -7.352 -29.001 -40.538  1.00 20.04           C  
ATOM    926  N   ALA A 119      -8.241 -28.777 -37.473  1.00 19.33           N  
ATOM    927  CA  ALA A 119      -9.066 -28.145 -36.447  1.00 19.45           C  
ATOM    928  C   ALA A 119      -8.214 -27.702 -35.266  1.00 19.43           C  
ATOM    929  O   ALA A 119      -8.405 -26.598 -34.740  1.00 19.06           O  
ATOM    930  CB  ALA A 119     -10.167 -29.110 -35.971  1.00 19.41           C  
ATOM    931  N   GLU A 120      -7.292 -28.558 -34.834  1.00 18.09           N  
ATOM    932  CA  GLU A 120      -6.416 -28.214 -33.725  1.00 19.89           C  
ATOM    933  C   GLU A 120      -5.488 -27.057 -34.133  1.00 18.11           C  
ATOM    934  O   GLU A 120      -5.182 -26.177 -33.326  1.00 17.69           O  
ATOM    935  CB  GLU A 120      -5.588 -29.432 -33.294  1.00 22.50           C  
ATOM    936  CG  GLU A 120      -4.927 -29.245 -31.927  1.00 29.45           C  
ATOM    937  CD  GLU A 120      -4.285 -30.515 -31.385  1.00 33.63           C  
ATOM    938  OE1 GLU A 120      -4.906 -31.601 -31.517  1.00 36.80           O  
ATOM    939  OE2 GLU A 120      -3.173 -30.431 -30.808  1.00 35.16           O  
ATOM    940  N   PHE A 121      -5.034 -27.072 -35.382  1.00 17.55           N  
ATOM    941  CA  PHE A 121      -4.169 -26.012 -35.891  1.00 17.59           C  
ATOM    942  C   PHE A 121      -4.870 -24.649 -35.756  1.00 17.44           C  
ATOM    943  O   PHE A 121      -4.271 -23.667 -35.294  1.00 16.21           O  
ATOM    944  CB  PHE A 121      -3.823 -26.282 -37.363  1.00 17.24           C  
ATOM    945  CG  PHE A 121      -2.859 -25.291 -37.951  1.00 17.35           C  
ATOM    946  CD1 PHE A 121      -1.487 -25.536 -37.941  1.00 17.58           C  
ATOM    947  CD2 PHE A 121      -3.318 -24.083 -38.460  1.00 16.89           C  
ATOM    948  CE1 PHE A 121      -0.595 -24.581 -38.429  1.00 17.99           C  
ATOM    949  CE2 PHE A 121      -2.435 -23.125 -38.946  1.00 17.78           C  
ATOM    950  CZ  PHE A 121      -1.074 -23.373 -38.930  1.00 19.02           C  
ATOM    951  N   ILE A 122      -6.137 -24.585 -36.164  1.00 17.03           N  
ATOM    952  CA  ILE A 122      -6.884 -23.333 -36.070  1.00 18.15           C  
ATOM    953  C   ILE A 122      -7.081 -22.923 -34.606  1.00 18.91           C  
ATOM    954  O   ILE A 122      -6.876 -21.757 -34.247  1.00 18.76           O  
ATOM    955  CB  ILE A 122      -8.270 -23.454 -36.761  1.00 18.75           C  
ATOM    956  CG1 ILE A 122      -8.082 -23.703 -38.264  1.00 17.99           C  
ATOM    957  CG2 ILE A 122      -9.094 -22.196 -36.503  1.00 18.62           C  
ATOM    958  CD1 ILE A 122      -7.270 -22.631 -39.000  1.00 21.48           C  
ATOM    959  N   GLN A 123      -7.449 -23.887 -33.760  1.00 18.48           N  
ATOM    960  CA  GLN A 123      -7.679 -23.625 -32.340  1.00 20.14           C  
ATOM    961  C   GLN A 123      -6.419 -23.047 -31.684  1.00 19.84           C  
ATOM    962  O   GLN A 123      -6.489 -22.169 -30.831  1.00 19.41           O  
ATOM    963  CB  GLN A 123      -8.079 -24.926 -31.633  1.00 23.60           C  
ATOM    964  CG  GLN A 123      -8.601 -24.750 -30.206  1.00 28.51           C  
ATOM    965  CD  GLN A 123      -9.971 -24.080 -30.153  1.00 32.51           C  
ATOM    966  OE1 GLN A 123     -10.824 -24.294 -31.036  1.00 34.88           O  
ATOM    967  NE2 GLN A 123     -10.200 -23.279 -29.109  1.00 34.21           N  
ATOM    968  N   GLN A 124      -5.255 -23.523 -32.104  1.00 19.52           N  
ATOM    969  CA  GLN A 124      -4.014 -23.044 -31.524  1.00 18.96           C  
ATOM    970  C   GLN A 124      -3.431 -21.740 -32.067  1.00 17.53           C  
ATOM    971  O   GLN A 124      -2.882 -20.934 -31.306  1.00 17.39           O  
ATOM    972  CB  GLN A 124      -2.942 -24.124 -31.646  1.00 21.18           C  
ATOM    973  CG  GLN A 124      -1.547 -23.583 -31.436  1.00 26.51           C  
ATOM    974  CD  GLN A 124      -0.737 -24.394 -30.452  1.00 29.91           C  
ATOM    975  OE1 GLN A 124      -0.490 -25.591 -30.675  1.00 31.80           O  
ATOM    976  NE2 GLN A 124      -0.314 -23.754 -29.353  1.00 29.51           N  
ATOM    977  N   PHE A 125      -3.547 -21.532 -33.370  1.00 15.90           N  
ATOM    978  CA  PHE A 125      -2.920 -20.384 -34.010  1.00 16.26           C  
ATOM    979  C   PHE A 125      -3.827 -19.288 -34.555  1.00 15.89           C  
ATOM    980  O   PHE A 125      -3.363 -18.407 -35.281  1.00 16.41           O  
ATOM    981  CB  PHE A 125      -2.020 -20.910 -35.139  1.00 15.52           C  
ATOM    982  CG  PHE A 125      -0.999 -21.937 -34.686  1.00 16.09           C  
ATOM    983  CD1 PHE A 125      -0.997 -23.215 -35.226  1.00 14.09           C  
ATOM    984  CD2 PHE A 125      -0.012 -21.601 -33.753  1.00 16.51           C  
ATOM    985  CE1 PHE A 125      -0.032 -24.151 -34.867  1.00 15.70           C  
ATOM    986  CE2 PHE A 125       0.964 -22.523 -33.378  1.00 16.94           C  
ATOM    987  CZ  PHE A 125       0.956 -23.819 -33.947  1.00 16.63           C  
ATOM    988  N   ASN A 126      -5.117 -19.320 -34.229  1.00 16.75           N  
ATOM    989  CA  ASN A 126      -5.992 -18.282 -34.757  1.00 15.73           C  
ATOM    990  C   ASN A 126      -5.554 -16.886 -34.297  1.00 15.80           C  
ATOM    991  O   ASN A 126      -5.080 -16.687 -33.164  1.00 14.14           O  
ATOM    992  CB  ASN A 126      -7.465 -18.564 -34.382  1.00 18.46           C  
ATOM    993  CG  ASN A 126      -7.723 -18.483 -32.898  1.00 20.59           C  
ATOM    994  OD1 ASN A 126      -8.009 -17.407 -32.363  1.00 21.03           O  
ATOM    995  ND2 ASN A 126      -7.619 -19.620 -32.214  1.00 21.87           N  
ATOM    996  N   ASN A 127      -5.684 -15.934 -35.220  1.00 15.14           N  
ATOM    997  CA  ASN A 127      -5.336 -14.532 -35.007  1.00 16.19           C  
ATOM    998  C   ASN A 127      -3.828 -14.307 -34.895  1.00 15.00           C  
ATOM    999  O   ASN A 127      -3.374 -13.400 -34.195  1.00 14.31           O  
ATOM   1000  CB  ASN A 127      -6.072 -13.977 -33.778  1.00 19.13           C  
ATOM   1001  CG  ASN A 127      -6.439 -12.491 -33.930  1.00 23.84           C  
ATOM   1002  OD1 ASN A 127      -6.392 -11.933 -35.032  1.00 25.29           O  
ATOM   1003  ND2 ASN A 127      -6.816 -11.852 -32.817  1.00 24.01           N  
ATOM   1004  N   GLN A 128      -3.067 -15.137 -35.608  1.00 13.54           N  
ATOM   1005  CA  GLN A 128      -1.608 -15.059 -35.635  1.00 12.95           C  
ATOM   1006  C   GLN A 128      -1.097 -14.958 -37.072  1.00 12.26           C  
ATOM   1007  O   GLN A 128      -1.728 -15.461 -38.006  1.00 11.32           O  
ATOM   1008  CB  GLN A 128      -0.979 -16.297 -34.977  1.00 13.77           C  
ATOM   1009  CG  GLN A 128      -1.204 -16.366 -33.478  1.00 14.46           C  
ATOM   1010  CD  GLN A 128      -0.463 -17.524 -32.800  1.00 15.67           C  
ATOM   1011  OE1 GLN A 128       0.595 -17.994 -33.271  1.00 17.28           O  
ATOM   1012  NE2 GLN A 128      -0.992 -17.965 -31.671  1.00 15.20           N  
ATOM   1013  N   ALA A 129       0.070 -14.333 -37.221  1.00 11.96           N  
ATOM   1014  CA  ALA A 129       0.721 -14.138 -38.517  1.00 12.30           C  
ATOM   1015  C   ALA A 129       1.542 -15.332 -38.993  1.00 12.35           C  
ATOM   1016  O   ALA A 129       2.278 -15.949 -38.225  1.00 13.15           O  
ATOM   1017  CB  ALA A 129       1.636 -12.909 -38.458  1.00 12.30           C  
ATOM   1018  N   PHE A 130       1.425 -15.643 -40.277  1.00 12.17           N  
ATOM   1019  CA  PHE A 130       2.213 -16.725 -40.888  1.00 13.62           C  
ATOM   1020  C   PHE A 130       2.715 -16.203 -42.223  1.00 13.73           C  
ATOM   1021  O   PHE A 130       2.008 -15.473 -42.904  1.00 14.33           O  
ATOM   1022  CB  PHE A 130       1.365 -17.984 -41.126  1.00 15.22           C  
ATOM   1023  CG  PHE A 130       1.116 -18.767 -39.890  1.00 15.37           C  
ATOM   1024  CD1 PHE A 130       0.064 -18.440 -39.042  1.00 17.23           C  
ATOM   1025  CD2 PHE A 130       1.986 -19.779 -39.519  1.00 17.03           C  
ATOM   1026  CE1 PHE A 130      -0.106 -19.110 -37.841  1.00 16.84           C  
ATOM   1027  CE2 PHE A 130       1.825 -20.457 -38.321  1.00 17.45           C  
ATOM   1028  CZ  PHE A 130       0.780 -20.122 -37.476  1.00 17.02           C  
ATOM   1029  N   SER A 131       3.940 -16.567 -42.584  1.00 14.17           N  
ATOM   1030  CA  SER A 131       4.525 -16.131 -43.849  1.00 15.15           C  
ATOM   1031  C   SER A 131       4.923 -17.353 -44.657  1.00 15.04           C  
ATOM   1032  O   SER A 131       5.210 -18.407 -44.101  1.00 13.83           O  
ATOM   1033  CB  SER A 131       5.786 -15.285 -43.597  1.00 15.92           C  
ATOM   1034  OG  SER A 131       5.477 -14.065 -42.942  1.00 16.46           O  
ATOM   1035  N   VAL A 132       4.965 -17.200 -45.974  1.00 16.26           N  
ATOM   1036  CA  VAL A 132       5.391 -18.298 -46.835  1.00 16.69           C  
ATOM   1037  C   VAL A 132       6.848 -18.597 -46.463  1.00 16.07           C  
ATOM   1038  O   VAL A 132       7.647 -17.677 -46.254  1.00 16.34           O  
ATOM   1039  CB  VAL A 132       5.283 -17.883 -48.333  1.00 17.40           C  
ATOM   1040  CG1 VAL A 132       5.898 -18.960 -49.233  1.00 18.41           C  
ATOM   1041  CG2 VAL A 132       3.816 -17.684 -48.699  1.00 18.64           C  
ATOM   1042  N   GLY A 133       7.189 -19.876 -46.338  1.00 15.82           N  
ATOM   1043  CA  GLY A 133       8.553 -20.233 -45.987  1.00 15.27           C  
ATOM   1044  C   GLY A 133       8.800 -20.320 -44.486  1.00 15.19           C  
ATOM   1045  O   GLY A 133       9.839 -20.793 -44.041  1.00 15.34           O  
ATOM   1046  N   GLN A 134       7.849 -19.863 -43.687  1.00 15.11           N  
ATOM   1047  CA  GLN A 134       8.020 -19.911 -42.236  1.00 15.14           C  
ATOM   1048  C   GLN A 134       8.027 -21.351 -41.674  1.00 16.03           C  
ATOM   1049  O   GLN A 134       7.234 -22.204 -42.077  1.00 15.38           O  
ATOM   1050  CB  GLN A 134       6.929 -19.073 -41.559  1.00 14.83           C  
ATOM   1051  CG  GLN A 134       7.051 -18.965 -40.040  1.00 13.31           C  
ATOM   1052  CD  GLN A 134       6.194 -17.836 -39.455  1.00 13.73           C  
ATOM   1053  OE1 GLN A 134       5.370 -17.225 -40.146  1.00 11.07           O  
ATOM   1054  NE2 GLN A 134       6.393 -17.557 -38.172  1.00 12.82           N  
ATOM   1055  N   GLN A 135       8.929 -21.592 -40.735  1.00 16.59           N  
ATOM   1056  CA  GLN A 135       9.085 -22.880 -40.064  1.00 18.97           C  
ATOM   1057  C   GLN A 135       8.591 -22.760 -38.630  1.00 18.77           C  
ATOM   1058  O   GLN A 135       8.806 -21.731 -37.989  1.00 19.31           O  
ATOM   1059  CB  GLN A 135      10.569 -23.270 -40.025  1.00 21.06           C  
ATOM   1060  CG  GLN A 135      11.241 -23.369 -41.391  1.00 24.83           C  
ATOM   1061  CD  GLN A 135      12.726 -23.011 -41.338  1.00 27.59           C  
ATOM   1062  OE1 GLN A 135      13.410 -23.256 -40.336  1.00 30.28           O  
ATOM   1063  NE2 GLN A 135      13.229 -22.436 -42.418  1.00 29.48           N  
ATOM   1064  N   LEU A 136       7.916 -23.792 -38.130  1.00 18.13           N  
ATOM   1065  CA  LEU A 136       7.447 -23.803 -36.742  1.00 18.40           C  
ATOM   1066  C   LEU A 136       7.181 -25.236 -36.295  1.00 19.08           C  
ATOM   1067  O   LEU A 136       7.241 -26.177 -37.108  1.00 17.25           O  
ATOM   1068  CB  LEU A 136       6.168 -22.975 -36.555  1.00 19.70           C  
ATOM   1069  CG  LEU A 136       4.903 -23.528 -37.211  1.00 20.33           C  
ATOM   1070  CD1 LEU A 136       3.666 -23.128 -36.397  1.00 21.03           C  
ATOM   1071  CD2 LEU A 136       4.832 -23.020 -38.643  1.00 20.05           C  
ATOM   1072  N   VAL A 137       6.922 -25.406 -35.001  1.00 18.93           N  
ATOM   1073  CA  VAL A 137       6.637 -26.729 -34.468  1.00 20.80           C  
ATOM   1074  C   VAL A 137       5.167 -26.772 -34.077  1.00 21.71           C  
ATOM   1075  O   VAL A 137       4.585 -25.772 -33.622  1.00 21.25           O  
ATOM   1076  CB  VAL A 137       7.536 -27.078 -33.263  1.00 22.11           C  
ATOM   1077  CG1 VAL A 137       8.989 -27.093 -33.708  1.00 23.60           C  
ATOM   1078  CG2 VAL A 137       7.346 -26.070 -32.140  1.00 26.05           C  
ATOM   1079  N   PHE A 138       4.568 -27.937 -34.266  1.00 20.67           N  
ATOM   1080  CA  PHE A 138       3.149 -28.124 -33.997  1.00 21.87           C  
ATOM   1081  C   PHE A 138       2.983 -29.367 -33.144  1.00 22.50           C  
ATOM   1082  O   PHE A 138       3.460 -30.440 -33.512  1.00 21.82           O  
ATOM   1083  CB  PHE A 138       2.426 -28.298 -35.344  1.00 21.90           C  
ATOM   1084  CG  PHE A 138       0.954 -28.612 -35.235  1.00 23.08           C  
ATOM   1085  CD1 PHE A 138       0.385 -29.597 -36.051  1.00 23.39           C  
ATOM   1086  CD2 PHE A 138       0.132 -27.904 -34.360  1.00 23.21           C  
ATOM   1087  CE1 PHE A 138      -0.992 -29.874 -35.997  1.00 23.70           C  
ATOM   1088  CE2 PHE A 138      -1.239 -28.168 -34.292  1.00 23.96           C  
ATOM   1089  CZ  PHE A 138      -1.807 -29.154 -35.111  1.00 24.50           C  
ATOM   1090  N   SER A 139       2.331 -29.220 -31.997  1.00 22.77           N  
ATOM   1091  CA  SER A 139       2.097 -30.360 -31.121  1.00 24.47           C  
ATOM   1092  C   SER A 139       0.689 -30.862 -31.381  1.00 25.03           C  
ATOM   1093  O   SER A 139      -0.282 -30.118 -31.231  1.00 24.02           O  
ATOM   1094  CB  SER A 139       2.231 -29.960 -29.657  1.00 25.19           C  
ATOM   1095  OG  SER A 139       1.967 -31.075 -28.827  1.00 26.71           O  
ATOM   1096  N   PHE A 140       0.583 -32.118 -31.799  1.00 26.22           N  
ATOM   1097  CA  PHE A 140      -0.712 -32.709 -32.088  1.00 27.67           C  
ATOM   1098  C   PHE A 140      -0.794 -34.065 -31.406  1.00 29.91           C  
ATOM   1099  O   PHE A 140      -0.040 -34.980 -31.726  1.00 29.14           O  
ATOM   1100  CB  PHE A 140      -0.896 -32.863 -33.594  1.00 25.87           C  
ATOM   1101  CG  PHE A 140      -2.174 -33.553 -33.974  1.00 25.99           C  
ATOM   1102  CD1 PHE A 140      -3.401 -32.934 -33.761  1.00 25.74           C  
ATOM   1103  CD2 PHE A 140      -2.150 -34.829 -34.531  1.00 25.58           C  
ATOM   1104  CE1 PHE A 140      -4.592 -33.568 -34.099  1.00 26.09           C  
ATOM   1105  CE2 PHE A 140      -3.335 -35.478 -34.874  1.00 26.65           C  
ATOM   1106  CZ  PHE A 140      -4.564 -34.842 -34.657  1.00 26.60           C  
ATOM   1107  N   ASN A 141      -1.710 -34.174 -30.452  1.00 33.58           N  
ATOM   1108  CA  ASN A 141      -1.885 -35.407 -29.701  1.00 36.76           C  
ATOM   1109  C   ASN A 141      -0.574 -35.865 -29.063  1.00 37.63           C  
ATOM   1110  O   ASN A 141      -0.166 -37.018 -29.207  1.00 38.12           O  
ATOM   1111  CB  ASN A 141      -2.444 -36.489 -30.618  1.00 37.98           C  
ATOM   1112  CG  ASN A 141      -3.954 -36.555 -30.567  1.00 39.71           C  
ATOM   1113  OD1 ASN A 141      -4.534 -36.848 -29.517  1.00 41.06           O  
ATOM   1114  ND2 ASN A 141      -4.601 -36.279 -31.690  1.00 40.25           N  
ATOM   1115  N   ASP A 142       0.083 -34.934 -28.376  1.00 38.49           N  
ATOM   1116  CA  ASP A 142       1.343 -35.198 -27.688  1.00 39.02           C  
ATOM   1117  C   ASP A 142       2.514 -35.583 -28.577  1.00 37.51           C  
ATOM   1118  O   ASP A 142       3.550 -36.031 -28.077  1.00 38.91           O  
ATOM   1119  CB  ASP A 142       1.141 -36.282 -26.629  1.00 41.59           C  
ATOM   1120  CG  ASP A 142       0.215 -35.836 -25.531  1.00 43.76           C  
ATOM   1121  OD1 ASP A 142       0.546 -34.833 -24.852  1.00 45.14           O  
ATOM   1122  OD2 ASP A 142      -0.843 -36.482 -25.351  1.00 45.42           O  
ATOM   1123  N   LYS A 143       2.355 -35.410 -29.884  1.00 34.41           N  
ATOM   1124  CA  LYS A 143       3.411 -35.723 -30.838  1.00 31.65           C  
ATOM   1125  C   LYS A 143       3.907 -34.413 -31.455  1.00 28.94           C  
ATOM   1126  O   LYS A 143       3.104 -33.555 -31.794  1.00 27.05           O  
ATOM   1127  CB  LYS A 143       2.862 -36.599 -31.949  1.00 32.77           C  
ATOM   1128  CG  LYS A 143       3.909 -37.376 -32.686  1.00 34.41           C  
ATOM   1129  CD  LYS A 143       4.197 -38.656 -31.933  1.00 35.76           C  
ATOM   1130  CE  LYS A 143       5.131 -39.562 -32.706  1.00 36.59           C  
ATOM   1131  NZ  LYS A 143       5.292 -40.872 -32.016  1.00 37.27           N  
ATOM   1132  N   LEU A 144       5.217 -34.261 -31.617  1.00 26.38           N  
ATOM   1133  CA  LEU A 144       5.738 -33.035 -32.214  1.00 24.58           C  
ATOM   1134  C   LEU A 144       6.012 -33.144 -33.721  1.00 23.06           C  
ATOM   1135  O   LEU A 144       6.657 -34.086 -34.189  1.00 22.69           O  
ATOM   1136  CB  LEU A 144       7.011 -32.596 -31.486  1.00 24.41           C  
ATOM   1137  CG  LEU A 144       6.870 -32.202 -30.013  1.00 24.87           C  
ATOM   1138  CD1 LEU A 144       8.239 -31.775 -29.511  1.00 25.65           C  
ATOM   1139  CD2 LEU A 144       5.860 -31.056 -29.830  1.00 23.99           C  
ATOM   1140  N   PHE A 145       5.515 -32.167 -34.475  1.00 21.59           N  
ATOM   1141  CA  PHE A 145       5.709 -32.125 -35.919  1.00 20.63           C  
ATOM   1142  C   PHE A 145       6.368 -30.833 -36.347  1.00 21.05           C  
ATOM   1143  O   PHE A 145       6.176 -29.788 -35.712  1.00 19.95           O  
ATOM   1144  CB  PHE A 145       4.370 -32.236 -36.658  1.00 20.91           C  
ATOM   1145  CG  PHE A 145       3.651 -33.528 -36.408  1.00 21.87           C  
ATOM   1146  CD1 PHE A 145       2.844 -33.678 -35.292  1.00 22.50           C  
ATOM   1147  CD2 PHE A 145       3.851 -34.617 -37.244  1.00 22.72           C  
ATOM   1148  CE1 PHE A 145       2.244 -34.905 -35.002  1.00 24.05           C  
ATOM   1149  CE2 PHE A 145       3.258 -35.853 -36.962  1.00 23.89           C  
ATOM   1150  CZ  PHE A 145       2.458 -35.996 -35.846  1.00 23.18           C  
ATOM   1151  N   GLY A 146       7.147 -30.911 -37.427  1.00 20.68           N  
ATOM   1152  CA  GLY A 146       7.785 -29.729 -37.979  1.00 20.54           C  
ATOM   1153  C   GLY A 146       6.915 -29.273 -39.144  1.00 20.28           C  
ATOM   1154  O   GLY A 146       6.510 -30.104 -39.978  1.00 20.33           O  
ATOM   1155  N   LEU A 147       6.615 -27.977 -39.212  1.00 18.00           N  
ATOM   1156  CA  LEU A 147       5.778 -27.440 -40.287  1.00 18.02           C  
ATOM   1157  C   LEU A 147       6.514 -26.399 -41.111  1.00 18.78           C  
ATOM   1158  O   LEU A 147       7.348 -25.660 -40.592  1.00 18.52           O  
ATOM   1159  CB  LEU A 147       4.515 -26.771 -39.732  1.00 17.90           C  
ATOM   1160  CG  LEU A 147       3.595 -27.537 -38.779  1.00 18.10           C  
ATOM   1161  CD1 LEU A 147       2.395 -26.658 -38.449  1.00 18.08           C  
ATOM   1162  CD2 LEU A 147       3.137 -28.846 -39.425  1.00 20.15           C  
ATOM   1163  N   LEU A 148       6.174 -26.345 -42.392  1.00 18.36           N  
ATOM   1164  CA  LEU A 148       6.746 -25.386 -43.328  1.00 19.25           C  
ATOM   1165  C   LEU A 148       5.605 -24.835 -44.179  1.00 19.28           C  
ATOM   1166  O   LEU A 148       4.918 -25.590 -44.875  1.00 19.14           O  
ATOM   1167  CB  LEU A 148       7.781 -26.069 -44.221  1.00 20.34           C  
ATOM   1168  CG  LEU A 148       8.210 -25.295 -45.475  1.00 22.10           C  
ATOM   1169  CD1 LEU A 148       8.889 -23.979 -45.083  1.00 21.82           C  
ATOM   1170  CD2 LEU A 148       9.161 -26.183 -46.304  1.00 22.88           C  
ATOM   1171  N   VAL A 149       5.385 -23.524 -44.113  1.00 19.16           N  
ATOM   1172  CA  VAL A 149       4.324 -22.899 -44.893  1.00 18.85           C  
ATOM   1173  C   VAL A 149       4.750 -22.833 -46.374  1.00 19.78           C  
ATOM   1174  O   VAL A 149       5.749 -22.199 -46.715  1.00 18.76           O  
ATOM   1175  CB  VAL A 149       4.039 -21.463 -44.400  1.00 19.06           C  
ATOM   1176  CG1 VAL A 149       2.886 -20.873 -45.202  1.00 18.54           C  
ATOM   1177  CG2 VAL A 149       3.708 -21.466 -42.882  1.00 17.30           C  
ATOM   1178  N   LYS A 150       3.983 -23.480 -47.245  1.00 20.82           N  
ATOM   1179  CA  LYS A 150       4.311 -23.505 -48.673  1.00 23.15           C  
ATOM   1180  C   LYS A 150       3.535 -22.486 -49.483  1.00 24.09           C  
ATOM   1181  O   LYS A 150       4.064 -21.903 -50.438  1.00 24.36           O  
ATOM   1182  CB  LYS A 150       4.034 -24.898 -49.254  1.00 24.22           C  
ATOM   1183  CG  LYS A 150       4.768 -26.030 -48.558  1.00 25.41           C  
ATOM   1184  CD  LYS A 150       6.282 -25.869 -48.669  1.00 27.73           C  
ATOM   1185  CE  LYS A 150       6.740 -25.906 -50.121  1.00 29.16           C  
ATOM   1186  NZ  LYS A 150       8.230 -25.859 -50.217  1.00 31.15           N  
ATOM   1187  N   ASP A 151       2.278 -22.262 -49.110  1.00 24.17           N  
ATOM   1188  CA  ASP A 151       1.448 -21.342 -49.868  1.00 25.26           C  
ATOM   1189  C   ASP A 151       0.327 -20.760 -49.010  1.00 24.05           C  
ATOM   1190  O   ASP A 151      -0.155 -21.424 -48.082  1.00 22.57           O  
ATOM   1191  CB  ASP A 151       0.868 -22.078 -51.085  1.00 28.13           C  
ATOM   1192  CG  ASP A 151       0.090 -21.160 -52.011  1.00 32.34           C  
ATOM   1193  OD1 ASP A 151      -1.168 -21.174 -51.973  1.00 34.64           O  
ATOM   1194  OD2 ASP A 151       0.737 -20.405 -52.774  1.00 36.07           O  
ATOM   1195  N   ILE A 152      -0.056 -19.520 -49.324  1.00 22.66           N  
ATOM   1196  CA  ILE A 152      -1.112 -18.795 -48.615  1.00 21.82           C  
ATOM   1197  C   ILE A 152      -1.996 -18.040 -49.604  1.00 22.64           C  
ATOM   1198  O   ILE A 152      -1.498 -17.317 -50.464  1.00 22.32           O  
ATOM   1199  CB  ILE A 152      -0.525 -17.742 -47.634  1.00 21.29           C  
ATOM   1200  CG1 ILE A 152       0.486 -18.405 -46.685  1.00 20.70           C  
ATOM   1201  CG2 ILE A 152      -1.663 -17.071 -46.867  1.00 19.90           C  
ATOM   1202  CD1 ILE A 152       1.288 -17.425 -45.817  1.00 22.27           C  
ATOM   1203  N   GLU A 153      -3.311 -18.204 -49.480  1.00 24.11           N  
ATOM   1204  CA  GLU A 153      -4.258 -17.507 -50.354  1.00 26.03           C  
ATOM   1205  C   GLU A 153      -5.240 -16.720 -49.493  1.00 26.05           C  
ATOM   1206  O   GLU A 153      -5.708 -17.245 -48.480  1.00 24.50           O  
ATOM   1207  CB  GLU A 153      -5.025 -18.515 -51.217  1.00 29.66           C  
ATOM   1208  CG  GLU A 153      -4.228 -19.061 -52.393  1.00 33.76           C  
ATOM   1209  CD  GLU A 153      -5.015 -20.077 -53.195  1.00 36.49           C  
ATOM   1210  OE1 GLU A 153      -6.254 -19.925 -53.284  1.00 38.75           O  
ATOM   1211  OE2 GLU A 153      -4.400 -21.019 -53.745  1.00 37.71           O  
ATOM   1212  N   ALA A 154      -5.569 -15.486 -49.900  1.00 25.52           N  
ATOM   1213  CA  ALA A 154      -6.494 -14.637 -49.136  1.00 27.88           C  
ATOM   1214  C   ALA A 154      -7.951 -15.117 -49.180  1.00 29.53           C  
ATOM   1215  O   ALA A 154      -8.368 -15.759 -50.139  1.00 28.22           O  
ATOM   1216  CB  ALA A 154      -6.410 -13.194 -49.621  1.00 26.53           C  
HETATM 1217  N   MSE A 155      -8.716 -14.792 -48.136  1.00 32.20           N  
HETATM 1218  CA  MSE A 155     -10.114 -15.206 -48.049  1.00 35.54           C  
HETATM 1219  C   MSE A 155     -11.029 -14.358 -48.898  1.00 34.46           C  
HETATM 1220  O   MSE A 155     -10.692 -13.234 -49.266  1.00 33.32           O  
HETATM 1221  CB  MSE A 155     -10.639 -15.122 -46.612  1.00 42.05           C  
HETATM 1222  CG  MSE A 155      -9.790 -15.817 -45.577  1.00 51.11           C  
HETATM 1223 SE   MSE A 155     -10.740 -16.615 -44.227  1.00 64.14          SE  
HETATM 1224  CE  MSE A 155     -11.397 -15.089 -43.417  1.00 59.93           C  
ATOM   1225  N   ASP A 156     -12.206 -14.913 -49.174  1.00 34.26           N  
ATOM   1226  CA  ASP A 156     -13.242 -14.235 -49.946  1.00 34.49           C  
ATOM   1227  C   ASP A 156     -13.945 -13.286 -48.986  1.00 33.28           C  
ATOM   1228  O   ASP A 156     -13.812 -13.419 -47.770  1.00 33.06           O  
ATOM   1229  CB  ASP A 156     -14.297 -15.228 -50.454  1.00 35.97           C  
ATOM   1230  CG  ASP A 156     -13.711 -16.333 -51.310  1.00 38.40           C  
ATOM   1231  OD1 ASP A 156     -13.023 -16.013 -52.306  1.00 38.52           O  
ATOM   1232  OD2 ASP A 156     -13.954 -17.522 -50.987  1.00 38.99           O  
ATOM   1233  N   PRO A 157     -14.700 -12.313 -49.521  1.00 32.65           N  
ATOM   1234  CA  PRO A 157     -15.406 -11.385 -48.635  1.00 31.58           C  
ATOM   1235  C   PRO A 157     -16.584 -12.190 -48.065  1.00 31.06           C  
ATOM   1236  O   PRO A 157     -16.855 -13.302 -48.541  1.00 29.85           O  
ATOM   1237  CB  PRO A 157     -15.865 -10.273 -49.584  1.00 32.59           C  
ATOM   1238  CG  PRO A 157     -14.953 -10.418 -50.799  1.00 32.75           C  
ATOM   1239  CD  PRO A 157     -14.847 -11.912 -50.928  1.00 32.53           C  
ATOM   1240  N   SER A 158     -17.270 -11.652 -47.057  1.00 29.60           N  
ATOM   1241  CA  SER A 158     -18.408 -12.347 -46.454  1.00 29.59           C  
ATOM   1242  C   SER A 158     -19.555 -12.380 -47.454  1.00 29.88           C  
ATOM   1243  O   SER A 158     -19.525 -11.655 -48.455  1.00 28.56           O  
ATOM   1244  CB  SER A 158     -18.870 -11.630 -45.172  1.00 28.99           C  
ATOM   1245  OG  SER A 158     -19.372 -10.330 -45.454  1.00 29.38           O  
ATOM   1246  N   ILE A 159     -20.573 -13.199 -47.173  1.00 30.86           N  
ATOM   1247  CA  ILE A 159     -21.727 -13.320 -48.070  1.00 32.53           C  
ATOM   1248  C   ILE A 159     -22.515 -12.005 -48.221  1.00 33.83           C  
ATOM   1249  O   ILE A 159     -23.144 -11.779 -49.259  1.00 33.95           O  
ATOM   1250  CB  ILE A 159     -22.705 -14.441 -47.597  1.00 32.95           C  
ATOM   1251  CG1 ILE A 159     -23.618 -14.876 -48.750  1.00 33.44           C  
ATOM   1252  CG2 ILE A 159     -23.577 -13.934 -46.447  1.00 32.01           C  
ATOM   1253  CD1 ILE A 159     -22.889 -15.561 -49.896  1.00 34.49           C  
ATOM   1254  N   LEU A 160     -22.491 -11.146 -47.198  1.00 35.08           N  
ATOM   1255  CA  LEU A 160     -23.214  -9.868 -47.270  1.00 37.42           C  
ATOM   1256  C   LEU A 160     -22.545  -8.920 -48.264  1.00 38.81           C  
ATOM   1257  O   LEU A 160     -23.065  -7.846 -48.569  1.00 39.15           O  
ATOM   1258  CB  LEU A 160     -23.282  -9.189 -45.896  1.00 36.64           C  
ATOM   1259  CG  LEU A 160     -24.050  -9.911 -44.785  1.00 36.00           C  
ATOM   1260  CD1 LEU A 160     -24.136  -8.994 -43.566  1.00 35.35           C  
ATOM   1261  CD2 LEU A 160     -25.446 -10.291 -45.264  1.00 35.91           C  
ATOM   1262  N   LYS A 161     -21.378  -9.325 -48.751  1.00 40.68           N  
ATOM   1263  CA  LYS A 161     -20.625  -8.555 -49.734  1.00 42.35           C  
ATOM   1264  C   LYS A 161     -19.997  -9.485 -50.763  1.00 42.80           C  
ATOM   1265  O   LYS A 161     -20.151  -9.283 -51.965  1.00 43.72           O  
ATOM   1266  CB  LYS A 161     -19.533  -7.742 -49.053  1.00 43.22           C  
ATOM   1267  CG  LYS A 161     -20.076  -6.640 -48.187  1.00 45.11           C  
ATOM   1268  CD  LYS A 161     -18.956  -5.916 -47.510  1.00 46.25           C  
ATOM   1269  CE  LYS A 161     -19.477  -5.124 -46.351  1.00 46.67           C  
ATOM   1270  NZ  LYS A 161     -18.467  -5.143 -45.271  1.00 48.16           N  
ATOM   1271  N   ARG A 169      -8.651 -15.904 -56.488  1.00 47.55           N  
ATOM   1272  CA  ARG A 169      -7.876 -16.147 -55.270  1.00 46.98           C  
ATOM   1273  C   ARG A 169      -6.495 -15.502 -55.386  1.00 45.62           C  
ATOM   1274  O   ARG A 169      -5.691 -15.881 -56.246  1.00 45.86           O  
ATOM   1275  CB  ARG A 169      -7.682 -17.647 -55.039  1.00 48.63           C  
ATOM   1276  CG  ARG A 169      -8.835 -18.536 -55.474  1.00 50.73           C  
ATOM   1277  CD  ARG A 169      -8.513 -19.969 -55.093  1.00 52.29           C  
ATOM   1278  NE  ARG A 169      -9.432 -20.949 -55.660  1.00 54.32           N  
ATOM   1279  CZ  ARG A 169      -9.292 -22.263 -55.502  1.00 55.06           C  
ATOM   1280  NH1 ARG A 169      -8.269 -22.736 -54.795  1.00 55.69           N  
ATOM   1281  NH2 ARG A 169     -10.165 -23.103 -56.047  1.00 55.69           N  
ATOM   1282  N   GLN A 170      -6.220 -14.538 -54.515  1.00 43.06           N  
ATOM   1283  CA  GLN A 170      -4.939 -13.846 -54.517  1.00 40.73           C  
ATOM   1284  C   GLN A 170      -3.939 -14.535 -53.583  1.00 38.62           C  
ATOM   1285  O   GLN A 170      -4.278 -14.895 -52.454  1.00 37.36           O  
ATOM   1286  CB  GLN A 170      -5.154 -12.394 -54.077  1.00 42.17           C  
ATOM   1287  CG  GLN A 170      -3.892 -11.562 -53.923  1.00 43.98           C  
ATOM   1288  CD  GLN A 170      -4.201 -10.162 -53.414  1.00 45.70           C  
ATOM   1289  OE1 GLN A 170      -5.077  -9.481 -53.951  1.00 46.75           O  
ATOM   1290  NE2 GLN A 170      -3.487  -9.724 -52.377  1.00 45.86           N  
ATOM   1291  N   LYS A 171      -2.716 -14.734 -54.065  1.00 36.49           N  
ATOM   1292  CA  LYS A 171      -1.664 -15.351 -53.261  1.00 34.38           C  
ATOM   1293  C   LYS A 171      -0.971 -14.228 -52.504  1.00 32.66           C  
ATOM   1294  O   LYS A 171      -0.721 -13.153 -53.067  1.00 31.63           O  
ATOM   1295  CB  LYS A 171      -0.643 -16.063 -54.157  1.00 36.67           C  
ATOM   1296  CG  LYS A 171      -1.185 -17.293 -54.870  1.00 39.30           C  
ATOM   1297  CD  LYS A 171      -0.105 -17.952 -55.730  1.00 41.83           C  
ATOM   1298  CE  LYS A 171      -0.659 -19.145 -56.501  1.00 43.16           C  
ATOM   1299  NZ  LYS A 171       0.360 -19.774 -57.395  1.00 44.48           N  
ATOM   1300  N   ILE A 172      -0.663 -14.467 -51.233  1.00 29.40           N  
ATOM   1301  CA  ILE A 172      -0.004 -13.455 -50.414  1.00 27.24           C  
ATOM   1302  C   ILE A 172       1.208 -14.070 -49.723  1.00 26.00           C  
ATOM   1303  O   ILE A 172       1.249 -15.281 -49.506  1.00 25.63           O  
ATOM   1304  CB  ILE A 172      -0.997 -12.852 -49.364  1.00 26.13           C  
ATOM   1305  CG1 ILE A 172      -1.692 -13.969 -48.575  1.00 24.94           C  
ATOM   1306  CG2 ILE A 172      -2.049 -11.995 -50.075  1.00 25.85           C  
ATOM   1307  CD1 ILE A 172      -2.751 -13.479 -47.553  1.00 24.21           C  
ATOM   1308  N   GLU A 173       2.191 -13.236 -49.395  1.00 25.56           N  
ATOM   1309  CA  GLU A 173       3.426 -13.672 -48.733  1.00 24.95           C  
ATOM   1310  C   GLU A 173       3.266 -13.802 -47.216  1.00 22.70           C  
ATOM   1311  O   GLU A 173       3.931 -14.615 -46.592  1.00 20.25           O  
ATOM   1312  CB  GLU A 173       4.560 -12.671 -49.000  1.00 28.54           C  
ATOM   1313  CG  GLU A 173       4.926 -12.502 -50.463  1.00 34.37           C  
ATOM   1314  CD  GLU A 173       5.578 -11.153 -50.736  1.00 37.93           C  
ATOM   1315  OE1 GLU A 173       6.627 -10.849 -50.110  1.00 39.97           O  
ATOM   1316  OE2 GLU A 173       5.032 -10.394 -51.575  1.00 40.17           O  
ATOM   1317  N   VAL A 174       2.422 -12.959 -46.635  1.00 20.80           N  
ATOM   1318  CA  VAL A 174       2.180 -12.978 -45.197  1.00 19.61           C  
ATOM   1319  C   VAL A 174       0.696 -12.725 -44.965  1.00 18.90           C  
ATOM   1320  O   VAL A 174       0.066 -11.939 -45.673  1.00 19.76           O  
ATOM   1321  CB  VAL A 174       3.055 -11.909 -44.450  1.00 19.78           C  
ATOM   1322  CG1 VAL A 174       2.888 -10.545 -45.091  1.00 21.57           C  
ATOM   1323  CG2 VAL A 174       2.655 -11.825 -42.961  1.00 19.86           C  
ATOM   1324  N   GLY A 175       0.123 -13.433 -44.005  1.00 17.69           N  
ATOM   1325  CA  GLY A 175      -1.284 -13.259 -43.737  1.00 16.77           C  
ATOM   1326  C   GLY A 175      -1.651 -13.611 -42.315  1.00 15.96           C  
ATOM   1327  O   GLY A 175      -0.839 -14.123 -41.548  1.00 14.89           O  
ATOM   1328  N   LEU A 176      -2.902 -13.342 -41.979  1.00 15.17           N  
ATOM   1329  CA  LEU A 176      -3.416 -13.601 -40.652  1.00 15.56           C  
ATOM   1330  C   LEU A 176      -4.353 -14.804 -40.645  1.00 15.17           C  
ATOM   1331  O   LEU A 176      -5.335 -14.843 -41.385  1.00 16.10           O  
ATOM   1332  CB  LEU A 176      -4.163 -12.354 -40.168  1.00 17.52           C  
ATOM   1333  CG  LEU A 176      -4.721 -12.369 -38.743  1.00 18.11           C  
ATOM   1334  CD1 LEU A 176      -3.555 -12.228 -37.754  1.00 16.83           C  
ATOM   1335  CD2 LEU A 176      -5.716 -11.192 -38.582  1.00 18.31           C  
ATOM   1336  N   VAL A 177      -4.052 -15.791 -39.808  1.00 14.51           N  
ATOM   1337  CA  VAL A 177      -4.910 -16.960 -39.694  1.00 15.98           C  
ATOM   1338  C   VAL A 177      -6.126 -16.538 -38.875  1.00 15.61           C  
ATOM   1339  O   VAL A 177      -5.988 -15.929 -37.812  1.00 16.14           O  
ATOM   1340  CB  VAL A 177      -4.198 -18.134 -38.953  1.00 16.07           C  
ATOM   1341  CG1 VAL A 177      -5.229 -19.237 -38.595  1.00 17.56           C  
ATOM   1342  CG2 VAL A 177      -3.121 -18.732 -39.851  1.00 16.87           C  
ATOM   1343  N   VAL A 178      -7.316 -16.842 -39.374  1.00 15.13           N  
ATOM   1344  CA  VAL A 178      -8.527 -16.492 -38.646  1.00 15.80           C  
ATOM   1345  C   VAL A 178      -9.415 -17.723 -38.422  1.00 15.93           C  
ATOM   1346  O   VAL A 178      -9.128 -18.828 -38.918  1.00 15.08           O  
ATOM   1347  CB  VAL A 178      -9.333 -15.364 -39.355  1.00 16.99           C  
ATOM   1348  CG1 VAL A 178      -8.552 -14.024 -39.284  1.00 17.42           C  
ATOM   1349  CG2 VAL A 178      -9.603 -15.733 -40.795  1.00 15.96           C  
ATOM   1350  N   GLY A 179     -10.503 -17.519 -37.686  1.00 15.53           N  
ATOM   1351  CA  GLY A 179     -11.387 -18.622 -37.336  1.00 17.01           C  
ATOM   1352  C   GLY A 179     -11.915 -19.465 -38.475  1.00 17.23           C  
ATOM   1353  O   GLY A 179     -12.149 -20.668 -38.311  1.00 17.87           O  
ATOM   1354  N   ASN A 180     -12.124 -18.845 -39.627  1.00 17.07           N  
ATOM   1355  CA  ASN A 180     -12.640 -19.590 -40.755  1.00 18.38           C  
ATOM   1356  C   ASN A 180     -11.609 -19.945 -41.830  1.00 18.49           C  
ATOM   1357  O   ASN A 180     -11.987 -20.318 -42.934  1.00 17.50           O  
ATOM   1358  CB  ASN A 180     -13.848 -18.852 -41.375  1.00 19.58           C  
ATOM   1359  CG  ASN A 180     -13.549 -17.410 -41.718  1.00 21.97           C  
ATOM   1360  OD1 ASN A 180     -12.411 -16.956 -41.630  1.00 22.41           O  
ATOM   1361  ND2 ASN A 180     -14.587 -16.672 -42.107  1.00 23.46           N  
ATOM   1362  N   SER A 181     -10.316 -19.854 -41.498  1.00 17.89           N  
ATOM   1363  CA  SER A 181      -9.244 -20.201 -42.438  1.00 19.61           C  
ATOM   1364  C   SER A 181      -9.213 -21.722 -42.632  1.00 21.41           C  
ATOM   1365  O   SER A 181      -9.529 -22.470 -41.711  1.00 20.41           O  
ATOM   1366  CB  SER A 181      -7.863 -19.767 -41.890  1.00 19.87           C  
ATOM   1367  OG  SER A 181      -7.741 -18.358 -41.766  1.00 18.05           O  
ATOM   1368  N   GLN A 182      -8.833 -22.171 -43.825  1.00 22.02           N  
ATOM   1369  CA  GLN A 182      -8.726 -23.603 -44.105  1.00 25.04           C  
ATOM   1370  C   GLN A 182      -7.259 -23.981 -44.289  1.00 24.54           C  
ATOM   1371  O   GLN A 182      -6.490 -23.246 -44.923  1.00 24.69           O  
ATOM   1372  CB  GLN A 182      -9.502 -23.955 -45.372  1.00 27.77           C  
ATOM   1373  CG  GLN A 182     -11.002 -23.858 -45.200  1.00 32.38           C  
ATOM   1374  CD  GLN A 182     -11.726 -23.962 -46.521  1.00 36.15           C  
ATOM   1375  OE1 GLN A 182     -11.776 -22.997 -47.294  1.00 38.04           O  
ATOM   1376  NE2 GLN A 182     -12.277 -25.141 -46.804  1.00 36.70           N  
ATOM   1377  N   VAL A 183      -6.860 -25.110 -43.717  1.00 23.94           N  
ATOM   1378  CA  VAL A 183      -5.479 -25.555 -43.849  1.00 24.68           C  
ATOM   1379  C   VAL A 183      -5.434 -26.916 -44.508  1.00 24.04           C  
ATOM   1380  O   VAL A 183      -6.263 -27.776 -44.229  1.00 24.03           O  
ATOM   1381  CB  VAL A 183      -4.753 -25.659 -42.481  1.00 25.62           C  
ATOM   1382  CG1 VAL A 183      -3.417 -26.370 -42.659  1.00 26.93           C  
ATOM   1383  CG2 VAL A 183      -4.493 -24.281 -41.928  1.00 27.43           C  
ATOM   1384  N   ALA A 184      -4.470 -27.095 -45.399  1.00 22.62           N  
ATOM   1385  CA  ALA A 184      -4.305 -28.367 -46.080  1.00 22.31           C  
ATOM   1386  C   ALA A 184      -2.869 -28.804 -45.824  1.00 22.21           C  
ATOM   1387  O   ALA A 184      -1.940 -27.999 -45.918  1.00 21.97           O  
ATOM   1388  CB  ALA A 184      -4.566 -28.200 -47.571  1.00 23.24           C  
ATOM   1389  N   PHE A 185      -2.689 -30.076 -45.486  1.00 22.13           N  
ATOM   1390  CA  PHE A 185      -1.365 -30.600 -45.200  1.00 22.02           C  
ATOM   1391  C   PHE A 185      -0.832 -31.523 -46.299  1.00 24.00           C  
ATOM   1392  O   PHE A 185      -1.610 -32.174 -47.017  1.00 23.02           O  
ATOM   1393  CB  PHE A 185      -1.388 -31.383 -43.888  1.00 21.38           C  
ATOM   1394  CG  PHE A 185      -1.701 -30.553 -42.684  1.00 21.21           C  
ATOM   1395  CD1 PHE A 185      -3.010 -30.420 -42.229  1.00 20.28           C  
ATOM   1396  CD2 PHE A 185      -0.673 -29.930 -41.976  1.00 21.82           C  
ATOM   1397  CE1 PHE A 185      -3.295 -29.678 -41.079  1.00 21.36           C  
ATOM   1398  CE2 PHE A 185      -0.940 -29.181 -40.823  1.00 21.74           C  
ATOM   1399  CZ  PHE A 185      -2.257 -29.057 -40.372  1.00 21.82           C  
ATOM   1400  N   GLU A 186       0.493 -31.568 -46.426  1.00 24.65           N  
ATOM   1401  CA  GLU A 186       1.165 -32.458 -47.382  1.00 26.88           C  
ATOM   1402  C   GLU A 186       2.455 -32.909 -46.713  1.00 26.06           C  
ATOM   1403  O   GLU A 186       3.198 -32.085 -46.182  1.00 24.62           O  
ATOM   1404  CB  GLU A 186       1.470 -31.747 -48.712  1.00 29.05           C  
ATOM   1405  CG  GLU A 186       2.438 -30.581 -48.632  1.00 33.63           C  
ATOM   1406  CD  GLU A 186       2.722 -29.963 -49.996  1.00 36.93           C  
ATOM   1407  OE1 GLU A 186       1.763 -29.494 -50.657  1.00 37.89           O  
ATOM   1408  OE2 GLU A 186       3.908 -29.945 -50.409  1.00 38.87           O  
ATOM   1409  N   LYS A 187       2.716 -34.213 -46.706  1.00 25.79           N  
ATOM   1410  CA  LYS A 187       3.929 -34.713 -46.065  1.00 26.58           C  
ATOM   1411  C   LYS A 187       5.170 -34.321 -46.854  1.00 26.37           C  
ATOM   1412  O   LYS A 187       5.121 -34.125 -48.068  1.00 25.21           O  
ATOM   1413  CB  LYS A 187       3.886 -36.239 -45.904  1.00 27.60           C  
ATOM   1414  CG  LYS A 187       4.054 -37.010 -47.198  1.00 29.51           C  
ATOM   1415  CD  LYS A 187       4.157 -38.510 -46.933  1.00 32.31           C  
ATOM   1416  CE  LYS A 187       4.368 -39.286 -48.227  1.00 33.96           C  
ATOM   1417  NZ  LYS A 187       4.472 -40.752 -47.970  1.00 36.80           N  
ATOM   1418  N   ALA A 188       6.286 -34.192 -46.155  1.00 27.59           N  
ATOM   1419  CA  ALA A 188       7.536 -33.825 -46.805  1.00 29.46           C  
ATOM   1420  C   ALA A 188       7.999 -34.996 -47.657  1.00 31.49           C  
ATOM   1421  O   ALA A 188       7.662 -36.150 -47.368  1.00 30.64           O  
ATOM   1422  CB  ALA A 188       8.592 -33.509 -45.759  1.00 29.63           C  
ATOM   1423  N   GLU A 189       8.769 -34.697 -48.699  1.00 33.36           N  
ATOM   1424  CA  GLU A 189       9.301 -35.735 -49.574  1.00 36.25           C  
ATOM   1425  C   GLU A 189      10.005 -36.819 -48.757  1.00 36.40           C  
ATOM   1426  O   GLU A 189      10.752 -36.521 -47.828  1.00 36.98           O  
ATOM   1427  CB  GLU A 189      10.300 -35.132 -50.564  1.00 38.79           C  
ATOM   1428  CG  GLU A 189       9.667 -34.404 -51.740  1.00 42.49           C  
ATOM   1429  CD  GLU A 189       8.705 -35.291 -52.506  1.00 44.42           C  
ATOM   1430  OE1 GLU A 189       9.111 -36.415 -52.882  1.00 46.26           O  
ATOM   1431  OE2 GLU A 189       7.545 -34.869 -52.729  1.00 45.84           O  
ATOM   1432  N   ASN A 190       9.752 -38.073 -49.111  1.00 36.64           N  
ATOM   1433  CA  ASN A 190      10.355 -39.223 -48.446  1.00 36.87           C  
ATOM   1434  C   ASN A 190       9.971 -39.382 -46.974  1.00 35.75           C  
ATOM   1435  O   ASN A 190      10.634 -40.097 -46.231  1.00 35.81           O  
ATOM   1436  CB  ASN A 190      11.882 -39.163 -48.582  1.00 39.05           C  
ATOM   1437  CG  ASN A 190      12.325 -38.883 -50.007  1.00 40.22           C  
ATOM   1438  OD1 ASN A 190      11.802 -39.464 -50.959  1.00 40.84           O  
ATOM   1439  ND2 ASN A 190      13.293 -37.981 -50.160  1.00 42.24           N  
ATOM   1440  N   SER A 191       8.904 -38.714 -46.554  1.00 34.10           N  
ATOM   1441  CA  SER A 191       8.445 -38.816 -45.176  1.00 33.21           C  
ATOM   1442  C   SER A 191       7.660 -40.115 -45.009  1.00 32.83           C  
ATOM   1443  O   SER A 191       6.983 -40.562 -45.931  1.00 33.38           O  
ATOM   1444  CB  SER A 191       7.542 -37.627 -44.829  1.00 32.37           C  
ATOM   1445  OG  SER A 191       6.909 -37.828 -43.577  1.00 31.77           O  
ATOM   1446  N   SER A 192       7.752 -40.729 -43.838  1.00 32.46           N  
ATOM   1447  CA  SER A 192       7.011 -41.959 -43.602  1.00 32.26           C  
ATOM   1448  C   SER A 192       5.683 -41.634 -42.912  1.00 31.34           C  
ATOM   1449  O   SER A 192       4.951 -42.531 -42.481  1.00 31.35           O  
ATOM   1450  CB  SER A 192       7.832 -42.914 -42.744  1.00 33.61           C  
ATOM   1451  OG  SER A 192       7.967 -42.411 -41.428  1.00 36.85           O  
ATOM   1452  N   LEU A 193       5.368 -40.345 -42.819  1.00 29.20           N  
ATOM   1453  CA  LEU A 193       4.128 -39.906 -42.180  1.00 27.55           C  
ATOM   1454  C   LEU A 193       2.900 -40.366 -42.972  1.00 26.76           C  
ATOM   1455  O   LEU A 193       2.777 -40.098 -44.168  1.00 27.65           O  
ATOM   1456  CB  LEU A 193       4.132 -38.376 -42.040  1.00 26.60           C  
ATOM   1457  CG  LEU A 193       2.961 -37.742 -41.288  1.00 27.19           C  
ATOM   1458  CD1 LEU A 193       2.875 -38.323 -39.889  1.00 25.96           C  
ATOM   1459  CD2 LEU A 193       3.140 -36.213 -41.251  1.00 26.30           C  
ATOM   1460  N   ASN A 194       1.995 -41.062 -42.291  1.00 25.75           N  
ATOM   1461  CA  ASN A 194       0.771 -41.584 -42.889  1.00 25.36           C  
ATOM   1462  C   ASN A 194      -0.395 -40.634 -42.589  1.00 24.75           C  
ATOM   1463  O   ASN A 194      -0.954 -40.667 -41.487  1.00 23.90           O  
ATOM   1464  CB  ASN A 194       0.490 -42.977 -42.294  1.00 26.15           C  
ATOM   1465  CG  ASN A 194      -0.755 -43.625 -42.860  1.00 27.96           C  
ATOM   1466  OD1 ASN A 194      -1.275 -44.594 -42.289  1.00 30.31           O  
ATOM   1467  ND2 ASN A 194      -1.238 -43.112 -43.988  1.00 27.67           N  
ATOM   1468  N   LEU A 195      -0.753 -39.794 -43.563  1.00 24.58           N  
ATOM   1469  CA  LEU A 195      -1.845 -38.826 -43.408  1.00 24.97           C  
ATOM   1470  C   LEU A 195      -3.146 -39.325 -44.026  1.00 25.66           C  
ATOM   1471  O   LEU A 195      -3.156 -39.803 -45.165  1.00 25.58           O  
ATOM   1472  CB  LEU A 195      -1.496 -37.494 -44.086  1.00 25.52           C  
ATOM   1473  CG  LEU A 195      -0.308 -36.649 -43.618  1.00 24.62           C  
ATOM   1474  CD1 LEU A 195      -0.256 -35.373 -44.433  1.00 24.05           C  
ATOM   1475  CD2 LEU A 195      -0.460 -36.327 -42.135  1.00 24.66           C  
ATOM   1476  N   ILE A 196      -4.235 -39.206 -43.278  1.00 25.79           N  
ATOM   1477  CA  ILE A 196      -5.551 -39.615 -43.750  1.00 27.08           C  
ATOM   1478  C   ILE A 196      -6.484 -38.407 -43.613  1.00 28.52           C  
ATOM   1479  O   ILE A 196      -6.145 -37.416 -42.957  1.00 28.39           O  
ATOM   1480  CB  ILE A 196      -6.130 -40.792 -42.905  1.00 27.01           C  
ATOM   1481  CG1 ILE A 196      -6.352 -40.342 -41.453  1.00 27.09           C  
ATOM   1482  CG2 ILE A 196      -5.181 -41.980 -42.965  1.00 27.53           C  
ATOM   1483  CD1 ILE A 196      -7.150 -41.309 -40.592  1.00 27.31           C  
ATOM   1484  N   GLY A 197      -7.658 -38.480 -44.223  1.00 29.00           N  
ATOM   1485  CA  GLY A 197      -8.576 -37.363 -44.108  1.00 30.29           C  
ATOM   1486  C   GLY A 197      -8.610 -36.467 -45.325  1.00 31.53           C  
ATOM   1487  O   GLY A 197      -7.835 -36.634 -46.266  1.00 30.73           O  
ATOM   1488  N   LYS A 198      -9.496 -35.482 -45.291  1.00 33.32           N  
ATOM   1489  CA  LYS A 198      -9.661 -34.587 -46.419  1.00 35.23           C  
ATOM   1490  C   LYS A 198      -8.881 -33.274 -46.399  1.00 35.74           C  
ATOM   1491  O   LYS A 198      -8.862 -32.562 -47.398  1.00 35.84           O  
ATOM   1492  CB  LYS A 198     -11.156 -34.315 -46.617  1.00 36.79           C  
ATOM   1493  CG  LYS A 198     -11.926 -35.547 -47.093  1.00 38.84           C  
ATOM   1494  CD  LYS A 198     -13.403 -35.243 -47.296  1.00 40.77           C  
ATOM   1495  CE  LYS A 198     -14.098 -36.343 -48.090  1.00 41.55           C  
ATOM   1496  NZ  LYS A 198     -15.561 -36.055 -48.250  1.00 42.63           N  
ATOM   1497  N   ALA A 199      -8.237 -32.949 -45.282  1.00 36.08           N  
ATOM   1498  CA  ALA A 199      -7.459 -31.711 -45.207  1.00 36.57           C  
ATOM   1499  C   ALA A 199      -6.037 -31.961 -45.722  1.00 37.13           C  
ATOM   1500  O   ALA A 199      -5.061 -31.697 -45.020  1.00 35.78           O  
ATOM   1501  CB  ALA A 199      -7.419 -31.202 -43.766  1.00 35.25           C  
ATOM   1502  N   LYS A 200      -5.929 -32.464 -46.950  1.00 39.12           N  
ATOM   1503  CA  LYS A 200      -4.618 -32.769 -47.539  1.00 41.49           C  
ATOM   1504  C   LYS A 200      -4.381 -32.242 -48.957  1.00 43.02           C  
ATOM   1505  O   LYS A 200      -5.317 -31.819 -49.635  1.00 43.43           O  
ATOM   1506  CB  LYS A 200      -4.383 -34.281 -47.558  1.00 41.40           C  
ATOM   1507  CG  LYS A 200      -4.822 -35.019 -46.308  1.00 41.85           C  
ATOM   1508  CD  LYS A 200      -4.180 -36.397 -46.226  1.00 42.15           C  
ATOM   1509  CE  LYS A 200      -4.363 -37.199 -47.502  1.00 42.28           C  
ATOM   1510  NZ  LYS A 200      -3.712 -38.545 -47.394  1.00 41.89           N  
ATOM   1511  N   THR A 201      -3.108 -32.305 -49.364  1.00 44.60           N  
ATOM   1512  CA  THR A 201      -2.546 -31.913 -50.672  1.00 46.20           C  
ATOM   1513  C   THR A 201      -1.502 -30.810 -50.557  1.00 46.29           C  
ATOM   1514  O   THR A 201      -1.910 -29.662 -50.279  1.00 47.15           O  
ATOM   1515  CB  THR A 201      -3.597 -31.448 -51.702  1.00 46.43           C  
ATOM   1516  OG1 THR A 201      -4.417 -30.431 -51.123  1.00 48.28           O  
ATOM   1517  CG2 THR A 201      -4.438 -32.616 -52.186  1.00 46.27           C  
TER    1518      THR A 201                                                      
HETATM 1519  S   SO4 A 500      24.478  -7.702 -32.793  1.00 56.61           S  
HETATM 1520  O1  SO4 A 500      23.585  -8.689 -33.426  1.00 57.74           O  
HETATM 1521  O2  SO4 A 500      25.729  -8.369 -32.398  1.00 57.95           O  
HETATM 1522  O3  SO4 A 500      23.840  -7.128 -31.592  1.00 57.15           O  
HETATM 1523  O4  SO4 A 500      24.774  -6.632 -33.768  1.00 57.66           O  
HETATM 1524  S   SO4 A 501       3.690 -20.128 -16.621  1.00 45.77           S  
HETATM 1525  O1  SO4 A 501       3.144 -19.305 -17.713  1.00 46.65           O  
HETATM 1526  O2  SO4 A 501       3.530 -21.554 -16.967  1.00 46.54           O  
HETATM 1527  O3  SO4 A 501       2.952 -19.850 -15.369  1.00 46.59           O  
HETATM 1528  O4  SO4 A 501       5.114 -19.812 -16.424  1.00 46.04           O  
HETATM 1529  S   SO4 A 502      14.827 -22.737 -26.926  1.00 50.92           S  
HETATM 1530  O1  SO4 A 502      14.670 -23.760 -25.877  1.00 52.40           O  
HETATM 1531  O2  SO4 A 502      14.362 -21.439 -26.410  1.00 51.02           O  
HETATM 1532  O3  SO4 A 502      14.006 -23.122 -28.092  1.00 52.18           O  
HETATM 1533  O4  SO4 A 502      16.246 -22.664 -27.312  1.00 51.03           O  
HETATM 1534  O   HOH A 300     -13.967 -23.550 -41.143  1.00 36.12           O  
HETATM 1535  O   HOH A 301      -9.216 -31.557 -33.449  1.00 40.26           O  
HETATM 1536  O   HOH A 302      20.240  -4.074 -25.365  1.00 44.68           O  
HETATM 1537  O   HOH A 303     -10.795 -25.342 -34.955  1.00 31.87           O  
HETATM 1538  O   HOH A 304      14.820   2.167 -29.158  1.00 30.31           O  
HETATM 1539  O   HOH A 305      -9.203 -11.143 -48.981  1.00 46.60           O  
HETATM 1540  O   HOH A 306      12.212 -15.152 -19.565  1.00 36.16           O  
HETATM 1541  O   HOH A 307      19.958 -37.310 -37.714  1.00 50.47           O  
HETATM 1542  O   HOH A 308       4.564 -45.272 -42.402  1.00 35.26           O  
HETATM 1543  O   HOH A 309      -9.558 -40.512 -37.199  1.00 37.57           O  
HETATM 1544  O   HOH A 310       6.944 -22.453 -51.291  1.00 40.10           O  
HETATM 1545  O   HOH A 311       8.168 -39.333 -51.258  1.00 46.07           O  
HETATM 1546  O   HOH A 312      12.010 -36.258 -39.328  1.00 39.40           O  
HETATM 1547  O   HOH A 313       7.244 -19.001 -29.088  1.00 35.35           O  
HETATM 1548  O   HOH A 314       3.887 -31.889 -26.729  1.00 45.69           O  
HETATM 1549  O   HOH A 315     -10.930 -37.439 -41.158  1.00 38.42           O  
HETATM 1550  O   HOH A 316      -3.935 -12.956 -28.068  1.00 40.85           O  
HETATM 1551  O   HOH A 317      11.038  -1.111 -21.778  1.00 41.91           O  
HETATM 1552  O   HOH A 318      20.555  -7.616 -36.537  1.00 32.51           O  
HETATM 1553  O   HOH A 319      -8.083  -4.244 -41.496  1.00 38.33           O  
HETATM 1554  O   HOH A 320      -0.840 -16.763 -27.447  1.00 36.57           O  
HETATM 1555  O   HOH A 321      11.527 -36.705 -44.329  1.00 41.83           O  
HETATM 1556  O   HOH A 322      -1.549 -42.407 -34.510  1.00 41.79           O  
HETATM 1557  O   HOH A 323       4.929 -14.380 -40.277  1.00 12.54           O  
HETATM 1558  O   HOH A 324       9.219  -6.899 -24.213  1.00 16.39           O  
HETATM 1559  O   HOH A 325       7.613 -12.460 -42.247  1.00 15.70           O  
HETATM 1560  O   HOH A 326      13.725 -11.803 -21.139  1.00 15.02           O  
HETATM 1561  O   HOH A 327      -4.874 -38.468 -35.598  1.00 28.56           O  
HETATM 1562  O   HOH A 328      21.736 -15.322 -35.971  1.00 19.98           O  
HETATM 1563  O   HOH A 329      -0.505  -4.950 -34.233  1.00 19.16           O  
HETATM 1564  O   HOH A 330       4.208 -15.361 -34.529  1.00 16.70           O  
HETATM 1565  O   HOH A 331       2.639 -42.161 -39.799  1.00 20.00           O  
HETATM 1566  O   HOH A 332      -0.133 -13.855 -21.685  1.00 24.72           O  
HETATM 1567  O   HOH A 333      12.839 -11.551 -15.423  1.00 31.91           O  
HETATM 1568  O   HOH A 334      17.663 -15.629 -23.047  1.00 30.19           O  
HETATM 1569  O   HOH A 335       5.585  -9.125 -18.437  1.00 22.05           O  
HETATM 1570  O   HOH A 336      10.217 -17.243 -45.241  1.00 20.55           O  
HETATM 1571  O   HOH A 337      21.840 -17.922 -30.362  1.00 20.87           O  
HETATM 1572  O   HOH A 338      17.710  -3.903 -37.212  1.00 24.30           O  
HETATM 1573  O   HOH A 339      -4.208  -6.772 -29.024  1.00 41.36           O  
HETATM 1574  O   HOH A 340       2.196 -17.329 -35.641  1.00 18.77           O  
HETATM 1575  O   HOH A 341       7.244  -9.618 -13.976  1.00 35.49           O  
HETATM 1576  O   HOH A 342       1.450 -17.542 -51.316  1.00 25.31           O  
HETATM 1577  O   HOH A 343       1.039 -23.797 -26.635  1.00 36.77           O  
HETATM 1578  O   HOH A 344      -0.562 -20.274 -30.080  1.00 33.93           O  
HETATM 1579  O   HOH A 345      -3.747 -18.002 -31.051  1.00 26.57           O  
HETATM 1580  O   HOH A 346      -3.201 -14.341 -30.678  1.00 39.50           O  
HETATM 1581  O   HOH A 347       8.040  -8.153 -17.620  1.00 31.11           O  
HETATM 1582  O   HOH A 348       9.265 -39.390 -41.701  1.00 33.50           O  
HETATM 1583  O   HOH A 349       1.756 -26.535 -31.124  1.00 21.25           O  
HETATM 1584  O   HOH A 350       0.354  -5.796 -21.547  1.00 35.36           O  
HETATM 1585  O   HOH A 351       8.251 -19.286 -36.719  1.00 15.82           O  
HETATM 1586  O   HOH A 352       4.800 -15.360 -37.124  1.00 12.91           O  
HETATM 1587  O   HOH A 353       9.871 -12.628 -43.799  1.00 22.90           O  
HETATM 1588  O   HOH A 354       1.900 -11.889 -19.084  1.00 24.00           O  
HETATM 1589  O   HOH A 355      -5.073  -9.393 -35.235  1.00 26.26           O  
HETATM 1590  O   HOH A 356       1.820 -15.993 -20.330  1.00 28.91           O  
HETATM 1591  O   HOH A 357       0.102  -9.788 -47.447  1.00 29.98           O  
HETATM 1592  O   HOH A 358     -11.669 -22.834 -39.847  1.00 22.50           O  
HETATM 1593  O   HOH A 359      -1.102 -13.988 -28.556  1.00 28.75           O  
HETATM 1594  O   HOH A 360       1.810  -1.742 -40.376  1.00 25.83           O  
HETATM 1595  O   HOH A 361      16.235 -21.678 -42.166  1.00 35.65           O  
HETATM 1596  O   HOH A 362       0.877 -35.907 -48.486  1.00 35.56           O  
HETATM 1597  O   HOH A 363       7.858  -1.706 -31.101  1.00 36.99           O  
HETATM 1598  O   HOH A 364      12.864 -14.139 -21.752  1.00 28.60           O  
HETATM 1599  O   HOH A 365      17.877 -12.534 -40.493  1.00 25.88           O  
HETATM 1600  O   HOH A 366      11.544 -14.992 -44.820  1.00 24.52           O  
HETATM 1601  O   HOH A 367      12.168 -18.339 -47.365  1.00 39.96           O  
HETATM 1602  O   HOH A 369      11.383  -2.642 -37.330  1.00 41.48           O  
HETATM 1603  O   HOH A 370      19.530 -17.452 -22.403  1.00 31.35           O  
HETATM 1604  O   HOH A 371      28.166  -6.920 -33.009  1.00 33.11           O  
HETATM 1605  O   HOH A 372      12.032 -21.597 -45.052  1.00 26.31           O  
HETATM 1606  O   HOH A 373       8.399  -6.669 -15.293  1.00 35.75           O  
HETATM 1607  O   HOH A 374       8.632 -35.982 -33.504  1.00 30.48           O  
HETATM 1608  O   HOH A 375     -13.826 -13.886 -42.735  1.00 32.73           O  
HETATM 1609  O   HOH A 376      20.035 -19.095 -31.499  1.00 38.31           O  
HETATM 1610  O   HOH A 377       4.723 -23.463 -32.740  1.00 27.49           O  
HETATM 1611  O   HOH A 378      20.113 -12.094 -39.006  1.00 29.71           O  
HETATM 1612  O   HOH A 379       5.456 -47.658 -36.215  1.00 32.17           O  
HETATM 1613  O   HOH A 380      -3.765 -11.615 -32.186  1.00 27.54           O  
HETATM 1614  O   HOH A 381      10.677 -31.896 -39.526  1.00 51.82           O  
HETATM 1615  O   HOH A 382       1.043  -0.842 -42.714  1.00 47.39           O  
HETATM 1616  O   HOH A 383      13.152 -23.699 -37.926  1.00 34.57           O  
HETATM 1617  O   HOH A 384       6.931 -35.840 -29.889  1.00 34.21           O  
HETATM 1618  O   HOH A 385      -1.116  -2.354 -32.282  1.00 45.00           O  
HETATM 1619  O   HOH A 386      -0.508  -4.609 -44.062  1.00 42.88           O  
HETATM 1620  O   HOH A 387      -2.879 -22.379 -50.228  1.00 36.13           O  
HETATM 1621  O   HOH A 388      -9.023 -26.290 -42.331  1.00 29.96           O  
HETATM 1622  O   HOH A 389      -3.722  -5.993 -37.279  1.00 29.14           O  
HETATM 1623  O   HOH A 390       3.565 -19.085 -52.251  1.00 51.71           O  
HETATM 1624  O   HOH A 391       8.225 -22.731 -48.570  1.00 30.95           O  
HETATM 1625  O   HOH A 392     -11.201 -29.842 -39.859  1.00 37.66           O  
HETATM 1626  O   HOH A 393     -11.780  -9.901 -48.625  1.00 38.68           O  
HETATM 1627  O   HOH A 394      -0.811 -31.879 -28.391  1.00 35.47           O  
HETATM 1628  O   HOH A 395      -8.701 -10.545 -46.139  1.00 45.86           O  
HETATM 1629  O   HOH A 396      -5.519 -15.303 -30.380  1.00 40.58           O  
HETATM 1630  O   HOH A 397       5.268 -24.986 -20.205  1.00 38.60           O  
HETATM 1631  O   HOH A 398       0.744 -39.541 -46.133  1.00 34.06           O  
HETATM 1632  O   HOH A 399      15.226 -31.671 -34.902  1.00 47.60           O  
HETATM 1633  O   HOH A 400       3.395 -20.723 -20.519  1.00 33.57           O  
HETATM 1634  O   HOH A 402      -4.220  -8.418 -24.626  1.00 33.32           O  
HETATM 1635  O   HOH A 403      12.164 -39.572 -42.283  1.00 38.33           O  
HETATM 1636  O   HOH A 404      -2.928  -5.265 -34.640  1.00 35.04           O  
HETATM 1637  O   HOH A 405       7.207 -23.354 -32.963  1.00 38.98           O  
HETATM 1638  O   HOH A 406       1.784  -1.922 -22.861  1.00 39.60           O  
HETATM 1639  O   HOH A 407     -11.554 -25.349 -38.626  1.00 36.26           O  
HETATM 1640  O   HOH A 408      -6.992  -4.411 -32.134  1.00 45.77           O  
HETATM 1641  O   HOH A 409      11.350 -41.479 -43.868  1.00 39.70           O  
HETATM 1642  O   HOH A 410      -7.479 -12.813 -30.320  1.00 44.71           O  
HETATM 1643  O   HOH A 411      -5.785  -9.947 -50.978  1.00 35.91           O  
HETATM 1644  O   HOH A 412      -6.891 -37.582 -34.284  1.00 33.11           O  
HETATM 1645  O   HOH A 413      20.784 -19.264 -33.917  1.00 42.89           O  
HETATM 1646  O   HOH A 414      -0.197 -27.007 -27.468  1.00 46.45           O  
HETATM 1647  O   HOH A 415      14.362 -15.803 -44.335  1.00 37.96           O  
HETATM 1648  O   HOH A 416     -11.883  -9.420 -52.019  1.00 42.56           O  
HETATM 1649  O   HOH A 417      22.322 -18.700 -23.854  1.00 41.69           O  
HETATM 1650  O   HOH A 418      12.662 -25.997 -36.932  1.00 45.77           O  
HETATM 1651  O   HOH A 419       0.889  -1.890 -26.034  1.00 45.98           O  
HETATM 1652  O   HOH A 420      -7.820  -2.549 -48.689  1.00 47.87           O  
HETATM 1653  O   HOH A 421      12.588   0.096 -38.126  1.00 48.49           O  
HETATM 1654  O   HOH A 422     -11.185 -22.507 -33.092  1.00 46.90           O  
HETATM 1655  O   HOH A 423       4.724   8.705 -31.153  1.00 40.42           O  
HETATM 1656  O   HOH A 424       4.109 -42.016 -45.722  1.00 46.36           O  
HETATM 1657  O   HOH A 425     -16.138 -40.027 -47.871  1.00 53.37           O  
HETATM 1658  O   HOH A 426      -1.608  -8.595 -49.056  1.00 43.52           O  
HETATM 1659  O   HOH A 427       7.933   0.464 -22.418  1.00 42.13           O  
HETATM 1660  O   HOH A 428       9.086 -28.895 -41.416  1.00 47.87           O  
HETATM 1661  O   HOH A 429      -2.199 -14.317 -56.953  1.00 44.84           O  
HETATM 1662  O   HOH A 430      10.970  -2.166 -40.237  1.00 50.23           O  
HETATM 1663  O   HOH A 431     -15.374 -15.249 -45.738  1.00 47.83           O  
CONECT    3    9                                                                
CONECT    9    3   10                                                           
CONECT   10    9   11   13                                                      
CONECT   11   10   12   17                                                      
CONECT   12   11                                                                
CONECT   13   10   14                                                           
CONECT   14   13   15                                                           
CONECT   15   14   16                                                           
CONECT   16   15                                                                
CONECT   17   11                                                                
CONECT   39   43                                                                
CONECT   43   39   44                                                           
CONECT   44   43   45   47                                                      
CONECT   45   44   46   51                                                      
CONECT   46   45                                                                
CONECT   47   44   48                                                           
CONECT   48   47   49                                                           
CONECT   49   48   50                                                           
CONECT   50   49                                                                
CONECT   51   45                                                                
CONECT  725  730                                                                
CONECT  730  725  731                                                           
CONECT  731  730  732  734                                                      
CONECT  732  731  733  738                                                      
CONECT  733  732                                                                
CONECT  734  731  735                                                           
CONECT  735  734  736                                                           
CONECT  736  735  737                                                           
CONECT  737  736                                                                
CONECT  738  732                                                                
CONECT  906  913                                                                
CONECT  913  906  914                                                           
CONECT  914  913  915  917                                                      
CONECT  915  914  916  921                                                      
CONECT  916  915                                                                
CONECT  917  914  918                                                           
CONECT  918  917  919                                                           
CONECT  919  918  920                                                           
CONECT  920  919                                                                
CONECT  921  915                                                                
CONECT 1214 1217                                                                
CONECT 1217 1214 1218                                                           
CONECT 1218 1217 1219 1221                                                      
CONECT 1219 1218 1220 1225                                                      
CONECT 1220 1219                                                                
CONECT 1221 1218 1222                                                           
CONECT 1222 1221 1223                                                           
CONECT 1223 1222 1224                                                           
CONECT 1224 1223                                                                
CONECT 1225 1219                                                                
CONECT 1519 1520 1521 1522 1523                                                 
CONECT 1520 1519                                                                
CONECT 1521 1519                                                                
CONECT 1522 1519                                                                
CONECT 1523 1519                                                                
CONECT 1524 1525 1526 1527 1528                                                 
CONECT 1525 1524                                                                
CONECT 1526 1524                                                                
CONECT 1527 1524                                                                
CONECT 1528 1524                                                                
CONECT 1529 1530 1531 1532 1533                                                 
CONECT 1530 1529                                                                
CONECT 1531 1529                                                                
CONECT 1532 1529                                                                
CONECT 1533 1529                                                                
MASTER      331    0    8    5   15    0    4    6 1662    1   65   17          
END                                                                             
