CNRS Nantes University UFIP UFIP
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***  HYDROLASE 27-MAR-06 2GHU  ***

elNémo ID: 22032617252046561

Job options:

ID        	=	 22032617252046561
JOBID     	=	 HYDROLASE 27-MAR-06 2GHU
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE                               27-MAR-06   2GHU              
TITLE     CRYSTAL STRUCTURE OF FALCIPAIN-2 FROM PLASMODIUM FALCIPARUM           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FALCIPAIN 2;                                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: MATURE WILD-TYPE ENZYME (RESIDUES 1-241);                  
COMPND   5 EC: 3.4.22.-;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;                          
SOURCE   3 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM;                     
SOURCE   4 ORGANISM_TAXID: 5833;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE-30                                    
KEYWDS    PAPAIN-LIKE CYSTEINE PROTEASE, L-DOMAIN, R-DOMAIN, ALPHA              
KEYWDS   2 HELIX, RANDOM COIL, TWISTED ANTIPARALLEL BETA-SHEET,                 
KEYWDS   3 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.HOGG,K.NAGARAJAN,C.L.SCHMIDT,R.HILGENFELD                           
REVDAT   4   24-FEB-09 2GHU    1       VERSN                                    
REVDAT   3   12-SEP-06 2GHU    1       JRNL                                     
REVDAT   2   11-JUL-06 2GHU    1       JRNL                                     
REVDAT   1   06-JUN-06 2GHU    0                                                
JRNL        AUTH   T.HOGG,K.NAGARAJAN,S.HERZBERG,L.CHEN,X.SHEN,                 
JRNL        AUTH 2 H.JIANG,M.WECKE,C.BLOHMKE,R.HILGENFELD,C.L.SCHMIDT           
JRNL        TITL   STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF                
JRNL        TITL 2 FALCIPAIN-2, A HEMOGLOBINASE FROM THE MALARIAL               
JRNL        TITL 3 PARASITE PLASMODIUM FALCIPARUM.                              
JRNL        REF    J.BIOL.CHEM.                  V. 281 25425 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16777845                                                     
JRNL        DOI    10.1074/JBC.M603776200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 37950                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2010                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3970                       
REMARK   3   BIN FREE R VALUE                    : 0.4050                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 323                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.023                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7614                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 40                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.77000                                             
REMARK   3    B22 (A**2) : 2.25000                                              
REMARK   3    B33 (A**2) : -3.04300                                             
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.96                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUPED                                   
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2GHU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037136.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8045                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI (111)         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40840                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.030                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.15200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: MIXED MODEL DERIVED FROM PDB ENTRY 1S4V              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4-0.8 M AMMONIUM SULFATE, 100 MM       
REMARK 280  SODIUM CITRATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 298.0K                                                  
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       89.04500            
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       89.04500            
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       72.91500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       84.14000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       72.91500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       84.14000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.04500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       72.91500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       84.14000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.04500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       72.91500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       84.14000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS PRESUMED TO BE A MONOMER.         
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU C    14                                                      
REMARK 465     GLU C    15                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     PRO A  189                                                       
REMARK 475     LEU A  190                                                       
REMARK 475     PRO C  189                                                       
REMARK 475     LEU C  190                                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A   133     OD2  ASP A   133     4555     1.77            
REMARK 500   OD1  ASN C    16     OD1  ASN C    16     3554     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR A 191   N   -  CA  -  C   ANGL. DEV. =  17.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A   4      -72.74    -49.89                                   
REMARK 500    ARG A  12      -74.62    -98.38                                   
REMARK 500    LEU A  26       48.20    -96.08                                   
REMARK 500    HIS A  27       19.84   -153.15                                   
REMARK 500    LYS A  37     -155.26     54.31                                   
REMARK 500    ASN A  38       25.25    -76.01                                   
REMARK 500    ILE A  57      -85.45    -90.01                                   
REMARK 500    ARG A  58      -77.66    -41.74                                   
REMARK 500    LYS A  59       21.37    -73.03                                   
REMARK 500    ASN A  60       58.69     23.81                                   
REMARK 500    SER A 108     -126.30     41.14                                   
REMARK 500    PRO A 111      148.61    -37.74                                   
REMARK 500    ASN A 112      119.01   -173.55                                   
REMARK 500    ARG A 118        4.21    -58.12                                   
REMARK 500    ASP A 133      -12.71    -49.24                                   
REMARK 500    TYR A 159      119.45    -38.48                                   
REMARK 500    GLU A 161      175.99    177.00                                   
REMARK 500    ASP A 165       25.79   -155.50                                   
REMARK 500    VAL A 187     -110.15    -98.47                                   
REMARK 500    ASN A 188       93.67   -170.94                                   
REMARK 500    PRO A 189       -5.85    -59.23                                   
REMARK 500    LEU A 190       60.61   -116.48                                   
REMARK 500    THR A 191      -18.93     69.76                                   
REMARK 500    LYS A 192     -114.04    -97.30                                   
REMARK 500    LYS A 193     -119.26   -142.66                                   
REMARK 500    GLU A 195      149.84    172.93                                   
REMARK 500    GLN A 209       11.48    -58.72                                   
REMARK 500    ARG A 213       28.70     49.86                                   
REMARK 500    CYS A 229       27.64     46.66                                   
REMARK 500    LEU A 231      135.07    -19.89                                   
REMARK 500    MET B   2     -174.53   -172.91                                   
REMARK 500    TYR B   4      -71.70    -51.01                                   
REMARK 500    GLU B   5      -37.09    -38.34                                   
REMARK 500    ARG B  12      -71.61   -107.98                                   
REMARK 500    HIS B  27       34.23   -142.49                                   
REMARK 500    PRO B  32      154.91    -44.96                                   
REMARK 500    LYS B  37     -151.14     67.79                                   
REMARK 500    ASN B  38       30.01    -85.81                                   
REMARK 500    ILE B  57      -71.35    -87.56                                   
REMARK 500    LYS B  59       26.99    -76.29                                   
REMARK 500    ASN B  60       55.26     19.75                                   
REMARK 500    GLU B  90      -70.03    -47.49                                   
REMARK 500    VAL B 107       17.62   -149.08                                   
REMARK 500    SER B 108     -134.38     44.73                                   
REMARK 500    ASN B 127     -172.77   -177.79                                   
REMARK 500    GLU B 161      174.49    172.40                                   
REMARK 500    ASP B 165       27.37   -147.19                                   
REMARK 500    ASP B 170      -91.10    -46.64                                   
REMARK 500    LEU B 172      114.65    -39.13                                   
REMARK 500    VAL B 179       13.66   -142.74                                   
REMARK 500    MET B 183      101.52   -164.03                                   
REMARK 500    VAL B 187     -106.16    -97.29                                   
REMARK 500    ASN B 188      -68.71   -150.55                                   
REMARK 500    LEU B 190      -99.92    -55.23                                   
REMARK 500    THR B 191      -28.60    -38.53                                   
REMARK 500    LYS B 192      -18.60     67.50                                   
REMARK 500    GLN B 209       31.77    -68.22                                   
REMARK 500    GLU B 212       94.55    -66.92                                   
REMARK 500    ARG B 227       78.03   -107.34                                   
REMARK 500    ARG C  12      -76.79   -119.22                                   
REMARK 500    LEU C  26       52.56    -96.42                                   
REMARK 500    HIS C  27       22.44   -159.68                                   
REMARK 500    PRO C  32      163.62    -45.78                                   
REMARK 500    LYS C  37     -157.72     54.63                                   
REMARK 500    ASN C  38       20.21    -73.62                                   
REMARK 500    ILE C  57      -73.00    -89.16                                   
REMARK 500    ASN C  60       60.57     35.22                                   
REMARK 500    ASP C 101      -37.29    -34.19                                   
REMARK 500    VAL C 107       20.64   -147.45                                   
REMARK 500    SER C 108     -130.29     45.20                                   
REMARK 500    ASN C 115       82.55   -152.67                                   
REMARK 500    ILE C 116       -9.24    -55.11                                   
REMARK 500    ASN C 127     -170.87   -178.97                                   
REMARK 500    TYR C 159      118.84    -36.35                                   
REMARK 500    ASP C 165       19.04   -163.91                                   
REMARK 500    ASP C 170      -86.68    -47.98                                   
REMARK 500    ASN C 173       32.24   -144.93                                   
REMARK 500    MET C 183      106.98   -168.06                                   
REMARK 500    PRO C 189      -71.87    -48.52                                   
REMARK 500    LEU C 190       95.84    -66.54                                   
REMARK 500    THR C 191     -166.69     53.33                                   
REMARK 500    LYS C 192     -172.01     65.88                                   
REMARK 500    GLN C 209       29.27    -69.35                                   
REMARK 500    ARG C 213       29.32     43.19                                   
REMARK 500    LEU C 231      136.03    -27.89                                   
REMARK 500    TYR D   4      -71.51    -50.51                                   
REMARK 500    ARG D  12      -57.15   -121.00                                   
REMARK 500    LYS D  37     -144.13     59.53                                   
REMARK 500    CYS D  42      -61.42    -26.75                                   
REMARK 500    ILE D  57      -70.26    -96.28                                   
REMARK 500    ASN D  60       65.59     32.08                                   
REMARK 500    CYS D  80       -0.72    -57.11                                   
REMARK 500    SER D 108     -136.56     59.62                                   
REMARK 500    ASN D 127     -175.57   -177.12                                   
REMARK 500    LEU D 136      -71.64    -66.37                                   
REMARK 500    ASP D 165       17.01   -160.30                                   
REMARK 500    ASP D 170      -91.26    -50.45                                   
REMARK 500    LEU D 172      108.02    -58.80                                   
REMARK 500    MET D 183      105.76   -162.48                                   
REMARK 500    GLN D 209       21.03    -65.79                                   
REMARK 500    LEU D 231      143.57    -34.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2GHU A    1   241  UNP    Q9N6S8   Q9N6S8_PLAFA   244    484             
DBREF  2GHU B    1   241  UNP    Q9N6S8   Q9N6S8_PLAFA   244    484             
DBREF  2GHU C    1   241  UNP    Q9N6S8   Q9N6S8_PLAFA   244    484             
DBREF  2GHU D    1   241  UNP    Q9N6S8   Q9N6S8_PLAFA   244    484             
SEQRES   1 A  241  GLN MET ASN TYR GLU GLU VAL ILE LYS LYS TYR ARG GLY          
SEQRES   2 A  241  GLU GLU ASN PHE ASP HIS ALA ALA TYR ASP TRP ARG LEU          
SEQRES   3 A  241  HIS SER GLY VAL THR PRO VAL LYS ASP GLN LYS ASN CYS          
SEQRES   4 A  241  GLY SER CYS TRP ALA PHE SER SER ILE GLY SER VAL GLU          
SEQRES   5 A  241  SER GLN TYR ALA ILE ARG LYS ASN LYS LEU ILE THR LEU          
SEQRES   6 A  241  SER GLU GLN GLU LEU VAL ASP CYS SER PHE LYS ASN TYR          
SEQRES   7 A  241  GLY CYS ASN GLY GLY LEU ILE ASN ASN ALA PHE GLU ASP          
SEQRES   8 A  241  MET ILE GLU LEU GLY GLY ILE CYS PRO ASP GLY ASP TYR          
SEQRES   9 A  241  PRO TYR VAL SER ASP ALA PRO ASN LEU CYS ASN ILE ASP          
SEQRES  10 A  241  ARG CYS THR GLU LYS TYR GLY ILE LYS ASN TYR LEU SER          
SEQRES  11 A  241  VAL PRO ASP ASN LYS LEU LYS GLU ALA LEU ARG PHE LEU          
SEQRES  12 A  241  GLY PRO ILE SER ILE SER VAL ALA VAL SER ASP ASP PHE          
SEQRES  13 A  241  ALA PHE TYR LYS GLU GLY ILE PHE ASP GLY GLU CYS GLY          
SEQRES  14 A  241  ASP GLN LEU ASN HIS ALA VAL MET LEU VAL GLY PHE GLY          
SEQRES  15 A  241  MET LYS GLU ILE VAL ASN PRO LEU THR LYS LYS GLY GLU          
SEQRES  16 A  241  LYS HIS TYR TYR TYR ILE ILE LYS ASN SER TRP GLY GLN          
SEQRES  17 A  241  GLN TRP GLY GLU ARG GLY PHE ILE ASN ILE GLU THR ASP          
SEQRES  18 A  241  GLU SER GLY LEU MET ARG LYS CYS GLY LEU GLY THR ASP          
SEQRES  19 A  241  ALA PHE ILE PRO LEU ILE GLU                                  
SEQRES   1 B  241  GLN MET ASN TYR GLU GLU VAL ILE LYS LYS TYR ARG GLY          
SEQRES   2 B  241  GLU GLU ASN PHE ASP HIS ALA ALA TYR ASP TRP ARG LEU          
SEQRES   3 B  241  HIS SER GLY VAL THR PRO VAL LYS ASP GLN LYS ASN CYS          
SEQRES   4 B  241  GLY SER CYS TRP ALA PHE SER SER ILE GLY SER VAL GLU          
SEQRES   5 B  241  SER GLN TYR ALA ILE ARG LYS ASN LYS LEU ILE THR LEU          
SEQRES   6 B  241  SER GLU GLN GLU LEU VAL ASP CYS SER PHE LYS ASN TYR          
SEQRES   7 B  241  GLY CYS ASN GLY GLY LEU ILE ASN ASN ALA PHE GLU ASP          
SEQRES   8 B  241  MET ILE GLU LEU GLY GLY ILE CYS PRO ASP GLY ASP TYR          
SEQRES   9 B  241  PRO TYR VAL SER ASP ALA PRO ASN LEU CYS ASN ILE ASP          
SEQRES  10 B  241  ARG CYS THR GLU LYS TYR GLY ILE LYS ASN TYR LEU SER          
SEQRES  11 B  241  VAL PRO ASP ASN LYS LEU LYS GLU ALA LEU ARG PHE LEU          
SEQRES  12 B  241  GLY PRO ILE SER ILE SER VAL ALA VAL SER ASP ASP PHE          
SEQRES  13 B  241  ALA PHE TYR LYS GLU GLY ILE PHE ASP GLY GLU CYS GLY          
SEQRES  14 B  241  ASP GLN LEU ASN HIS ALA VAL MET LEU VAL GLY PHE GLY          
SEQRES  15 B  241  MET LYS GLU ILE VAL ASN PRO LEU THR LYS LYS GLY GLU          
SEQRES  16 B  241  LYS HIS TYR TYR TYR ILE ILE LYS ASN SER TRP GLY GLN          
SEQRES  17 B  241  GLN TRP GLY GLU ARG GLY PHE ILE ASN ILE GLU THR ASP          
SEQRES  18 B  241  GLU SER GLY LEU MET ARG LYS CYS GLY LEU GLY THR ASP          
SEQRES  19 B  241  ALA PHE ILE PRO LEU ILE GLU                                  
SEQRES   1 C  241  GLN MET ASN TYR GLU GLU VAL ILE LYS LYS TYR ARG GLY          
SEQRES   2 C  241  GLU GLU ASN PHE ASP HIS ALA ALA TYR ASP TRP ARG LEU          
SEQRES   3 C  241  HIS SER GLY VAL THR PRO VAL LYS ASP GLN LYS ASN CYS          
SEQRES   4 C  241  GLY SER CYS TRP ALA PHE SER SER ILE GLY SER VAL GLU          
SEQRES   5 C  241  SER GLN TYR ALA ILE ARG LYS ASN LYS LEU ILE THR LEU          
SEQRES   6 C  241  SER GLU GLN GLU LEU VAL ASP CYS SER PHE LYS ASN TYR          
SEQRES   7 C  241  GLY CYS ASN GLY GLY LEU ILE ASN ASN ALA PHE GLU ASP          
SEQRES   8 C  241  MET ILE GLU LEU GLY GLY ILE CYS PRO ASP GLY ASP TYR          
SEQRES   9 C  241  PRO TYR VAL SER ASP ALA PRO ASN LEU CYS ASN ILE ASP          
SEQRES  10 C  241  ARG CYS THR GLU LYS TYR GLY ILE LYS ASN TYR LEU SER          
SEQRES  11 C  241  VAL PRO ASP ASN LYS LEU LYS GLU ALA LEU ARG PHE LEU          
SEQRES  12 C  241  GLY PRO ILE SER ILE SER VAL ALA VAL SER ASP ASP PHE          
SEQRES  13 C  241  ALA PHE TYR LYS GLU GLY ILE PHE ASP GLY GLU CYS GLY          
SEQRES  14 C  241  ASP GLN LEU ASN HIS ALA VAL MET LEU VAL GLY PHE GLY          
SEQRES  15 C  241  MET LYS GLU ILE VAL ASN PRO LEU THR LYS LYS GLY GLU          
SEQRES  16 C  241  LYS HIS TYR TYR TYR ILE ILE LYS ASN SER TRP GLY GLN          
SEQRES  17 C  241  GLN TRP GLY GLU ARG GLY PHE ILE ASN ILE GLU THR ASP          
SEQRES  18 C  241  GLU SER GLY LEU MET ARG LYS CYS GLY LEU GLY THR ASP          
SEQRES  19 C  241  ALA PHE ILE PRO LEU ILE GLU                                  
SEQRES   1 D  241  GLN MET ASN TYR GLU GLU VAL ILE LYS LYS TYR ARG GLY          
SEQRES   2 D  241  GLU GLU ASN PHE ASP HIS ALA ALA TYR ASP TRP ARG LEU          
SEQRES   3 D  241  HIS SER GLY VAL THR PRO VAL LYS ASP GLN LYS ASN CYS          
SEQRES   4 D  241  GLY SER CYS TRP ALA PHE SER SER ILE GLY SER VAL GLU          
SEQRES   5 D  241  SER GLN TYR ALA ILE ARG LYS ASN LYS LEU ILE THR LEU          
SEQRES   6 D  241  SER GLU GLN GLU LEU VAL ASP CYS SER PHE LYS ASN TYR          
SEQRES   7 D  241  GLY CYS ASN GLY GLY LEU ILE ASN ASN ALA PHE GLU ASP          
SEQRES   8 D  241  MET ILE GLU LEU GLY GLY ILE CYS PRO ASP GLY ASP TYR          
SEQRES   9 D  241  PRO TYR VAL SER ASP ALA PRO ASN LEU CYS ASN ILE ASP          
SEQRES  10 D  241  ARG CYS THR GLU LYS TYR GLY ILE LYS ASN TYR LEU SER          
SEQRES  11 D  241  VAL PRO ASP ASN LYS LEU LYS GLU ALA LEU ARG PHE LEU          
SEQRES  12 D  241  GLY PRO ILE SER ILE SER VAL ALA VAL SER ASP ASP PHE          
SEQRES  13 D  241  ALA PHE TYR LYS GLU GLY ILE PHE ASP GLY GLU CYS GLY          
SEQRES  14 D  241  ASP GLN LEU ASN HIS ALA VAL MET LEU VAL GLY PHE GLY          
SEQRES  15 D  241  MET LYS GLU ILE VAL ASN PRO LEU THR LYS LYS GLY GLU          
SEQRES  16 D  241  LYS HIS TYR TYR TYR ILE ILE LYS ASN SER TRP GLY GLN          
SEQRES  17 D  241  GLN TRP GLY GLU ARG GLY PHE ILE ASN ILE GLU THR ASP          
SEQRES  18 D  241  GLU SER GLY LEU MET ARG LYS CYS GLY LEU GLY THR ASP          
SEQRES  19 D  241  ALA PHE ILE PRO LEU ILE GLU                                  
FORMUL   5  HOH   *40(H2 O)                                                     
HELIX    1   1 ASN A    3  ARG A   12  1                                  10    
HELIX    2   2 ARG A   25  SER A   28  5                                   4    
HELIX    3   3 SER A   41  ARG A   58  1                                  18    
HELIX    4   4 SER A   66  SER A   74  1                                   9    
HELIX    5   5 TYR A   78  GLY A   82  5                                   5    
HELIX    6   6 LEU A   84  GLY A   96  1                                  13    
HELIX    7   7 LYS A  135  GLY A  144  1                                  10    
HELIX    8   8 SER A  153  TYR A  159  1                                   7    
HELIX    9   9 ARG A  227  LEU A  231  5                                   5    
HELIX   10  10 ASN B    3  LYS B   10  1                                   8    
HELIX   11  11 ARG B   25  SER B   28  5                                   4    
HELIX   12  12 SER B   41  ARG B   58  1                                  18    
HELIX   13  13 SER B   66  SER B   74  1                                   9    
HELIX   14  14 TYR B   78  GLY B   82  5                                   5    
HELIX   15  15 LEU B   84  GLY B   96  1                                  13    
HELIX   16  16 ASN B  115  CYS B  119  5                                   5    
HELIX   17  17 LYS B  135  GLY B  144  1                                  10    
HELIX   18  18 ASP B  154  TYR B  159  5                                   6    
HELIX   19  19 ARG B  227  LEU B  231  5                                   5    
HELIX   20  20 ASN C    3  ARG C   12  1                                  10    
HELIX   21  21 ARG C   25  SER C   28  5                                   4    
HELIX   22  22 SER C   41  LYS C   59  1                                  19    
HELIX   23  23 SER C   66  SER C   74  1                                   9    
HELIX   24  24 TYR C   78  GLY C   82  5                                   5    
HELIX   25  25 LEU C   84  LEU C   95  1                                  12    
HELIX   26  26 LYS C  135  LEU C  143  1                                   9    
HELIX   27  27 SER C  153  TYR C  159  1                                   7    
HELIX   28  28 ARG C  227  LEU C  231  5                                   5    
HELIX   29  29 ASN D    3  ARG D   12  1                                  10    
HELIX   30  30 ARG D   25  SER D   28  5                                   4    
HELIX   31  31 SER D   41  LYS D   59  1                                  19    
HELIX   32  32 SER D   66  SER D   74  1                                   9    
HELIX   33  33 TYR D   78  GLY D   82  5                                   5    
HELIX   34  34 LEU D   84  LEU D   95  1                                  12    
HELIX   35  35 LYS D  135  LEU D  143  1                                   9    
HELIX   36  36 SER D  153  TYR D  159  1                                   7    
HELIX   37  37 ARG D  227  LEU D  231  5                                   5    
SHEET    1   A 5 TYR A  22  ASP A  23  0                                        
SHEET    2   A 5 ALA A 175  ILE A 186 -1  O  PHE A 181   N  TYR A  22           
SHEET    3   A 5 ILE A 146  SER A 149 -1  N  ILE A 146   O  LEU A 178           
SHEET    4   A 5 ALA A 235  LEU A 239 -1  O  PHE A 236   N  SER A 147           
SHEET    5   A 5 ASN A 127  SER A 130 -1  N  ASN A 127   O  LEU A 239           
SHEET    1   B 4 TYR A  22  ASP A  23  0                                        
SHEET    2   B 4 ALA A 175  ILE A 186 -1  O  PHE A 181   N  TYR A  22           
SHEET    3   B 4 GLU A 195  LYS A 203 -1  O  ILE A 201   N  GLY A 180           
SHEET    4   B 4 PHE A 215  THR A 220 -1  O  ILE A 216   N  ILE A 202           
SHEET    1   C 5 TYR B  22  ASP B  23  0                                        
SHEET    2   C 5 ALA B 175  ILE B 186 -1  O  PHE B 181   N  TYR B  22           
SHEET    3   C 5 ILE B 146  SER B 149 -1  N  ILE B 148   O  VAL B 176           
SHEET    4   C 5 ALA B 235  LEU B 239 -1  O  PHE B 236   N  SER B 147           
SHEET    5   C 5 ASN B 127  SER B 130 -1  N  ASN B 127   O  LEU B 239           
SHEET    1   D 5 TYR B  22  ASP B  23  0                                        
SHEET    2   D 5 ALA B 175  ILE B 186 -1  O  PHE B 181   N  TYR B  22           
SHEET    3   D 5 GLU B 195  LYS B 203 -1  O  GLU B 195   N  ILE B 186           
SHEET    4   D 5 PHE B 215  GLU B 219 -1  O  ILE B 216   N  ILE B 202           
SHEET    5   D 5 ILE B 163  PHE B 164  1  N  PHE B 164   O  ASN B 217           
SHEET    1   E 5 TYR C  22  ASP C  23  0                                        
SHEET    2   E 5 ALA C 175  VAL C 187 -1  O  PHE C 181   N  TYR C  22           
SHEET    3   E 5 ILE C 146  SER C 149 -1  N  ILE C 148   O  VAL C 176           
SHEET    4   E 5 ALA C 235  LEU C 239 -1  O  PHE C 236   N  SER C 147           
SHEET    5   E 5 ASN C 127  SER C 130 -1  N  ASN C 127   O  LEU C 239           
SHEET    1   F 5 TYR C  22  ASP C  23  0                                        
SHEET    2   F 5 ALA C 175  VAL C 187 -1  O  PHE C 181   N  TYR C  22           
SHEET    3   F 5 GLY C 194  LYS C 203 -1  O  ILE C 201   N  GLY C 180           
SHEET    4   F 5 PHE C 215  GLU C 219 -1  O  ILE C 216   N  ILE C 202           
SHEET    5   F 5 ILE C 163  PHE C 164  1  N  PHE C 164   O  GLU C 219           
SHEET    1   G 5 TYR D  22  ASP D  23  0                                        
SHEET    2   G 5 ALA D 175  ASN D 188 -1  O  PHE D 181   N  TYR D  22           
SHEET    3   G 5 ILE D 146  SER D 149 -1  N  ILE D 146   O  LEU D 178           
SHEET    4   G 5 ALA D 235  LEU D 239 -1  O  PHE D 236   N  SER D 147           
SHEET    5   G 5 ASN D 127  SER D 130 -1  N  ASN D 127   O  LEU D 239           
SHEET    1   H 5 TYR D  22  ASP D  23  0                                        
SHEET    2   H 5 ALA D 175  ASN D 188 -1  O  PHE D 181   N  TYR D  22           
SHEET    3   H 5 LYS D 193  LYS D 203 -1  O  ILE D 201   N  GLY D 180           
SHEET    4   H 5 PHE D 215  THR D 220 -1  O  ILE D 216   N  ILE D 202           
SHEET    5   H 5 ILE D 163  PHE D 164  1  N  PHE D 164   O  GLU D 219           
SSBOND   1 CYS A   39    CYS A   80                          1555   1555  2.04  
SSBOND   2 CYS A   73    CYS A  114                          1555   1555  2.03  
SSBOND   3 CYS A   99    CYS A  119                          1555   1555  2.05  
SSBOND   4 CYS A  168    CYS A  229                          1555   1555  2.04  
SSBOND   5 CYS B   39    CYS B   80                          1555   1555  2.04  
SSBOND   6 CYS B   73    CYS B  114                          1555   1555  2.04  
SSBOND   7 CYS B   99    CYS B  119                          1555   1555  2.04  
SSBOND   8 CYS B  168    CYS B  229                          1555   1555  2.04  
SSBOND   9 CYS C   39    CYS C   80                          1555   1555  2.05  
SSBOND  10 CYS C   73    CYS C  114                          1555   1555  2.03  
SSBOND  11 CYS C   99    CYS C  119                          1555   1555  2.04  
SSBOND  12 CYS C  168    CYS C  229                          1555   1555  2.03  
SSBOND  13 CYS D   39    CYS D   80                          1555   1555  2.04  
SSBOND  14 CYS D   73    CYS D  114                          1555   1555  2.04  
SSBOND  15 CYS D   99    CYS D  119                          1555   1555  2.03  
SSBOND  16 CYS D  168    CYS D  229                          1555   1555  2.04  
CISPEP   1 ASN B  188    PRO B  189          0        -0.22                     
CRYST1  145.830  168.280  178.090  90.00  90.00  90.00 C 2 2 21     32          
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      0.006857  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005942  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005615        0.00000                         
ATOM      1  N   GLN A   1      57.080  10.906  -0.154  1.00116.46           N  
ATOM      2  CA  GLN A   1      58.233  11.356   0.671  1.00116.46           C  
ATOM      3  C   GLN A   1      57.803  12.375   1.733  1.00116.46           C  
ATOM      4  O   GLN A   1      58.547  13.299   2.061  1.00116.46           O  
ATOM      5  CB  GLN A   1      59.305  11.973  -0.222  1.00125.46           C  
ATOM      6  CG  GLN A   1      60.701  11.889   0.362  1.00125.46           C  
ATOM      7  CD  GLN A   1      61.707  12.740  -0.388  1.00125.46           C  
ATOM      8  OE1 GLN A   1      62.915  12.495  -0.332  1.00125.46           O  
ATOM      9  NE2 GLN A   1      61.217  13.757  -1.084  1.00125.46           N  
ATOM     10  N   MET A   2      56.592  12.204   2.253  1.00168.62           N  
ATOM     11  CA  MET A   2      56.049  13.073   3.295  1.00168.62           C  
ATOM     12  C   MET A   2      54.906  12.366   4.003  1.00168.62           C  
ATOM     13  O   MET A   2      54.473  11.293   3.580  1.00175.39           O  
ATOM     14  CB  MET A   2      55.533  14.392   2.717  1.00116.85           C  
ATOM     15  CG  MET A   2      56.579  15.476   2.646  1.00116.85           C  
ATOM     16  SD  MET A   2      55.870  17.134   2.505  1.00116.85           S  
ATOM     17  CE  MET A   2      56.250  17.851   4.158  1.00116.85           C  
ATOM     18  N   ASN A   3      54.419  12.961   5.085  1.00167.35           N  
ATOM     19  CA  ASN A   3      53.315  12.353   5.805  1.00167.35           C  
ATOM     20  C   ASN A   3      52.016  12.997   5.356  1.00167.35           C  
ATOM     21  O   ASN A   3      51.773  14.186   5.580  1.00183.25           O  
ATOM     22  CB  ASN A   3      53.490  12.499   7.312  1.00133.92           C  
ATOM     23  CG  ASN A   3      52.493  11.667   8.082  1.00133.92           C  
ATOM     24  OD1 ASN A   3      51.302  11.966   8.090  1.00133.92           O  
ATOM     25  ND2 ASN A   3      52.971  10.603   8.720  1.00133.92           N  
ATOM     26  N   TYR A   4      51.190  12.185   4.711  1.00101.13           N  
ATOM     27  CA  TYR A   4      49.917  12.632   4.179  1.00101.13           C  
ATOM     28  C   TYR A   4      49.041  13.407   5.172  1.00101.13           C  
ATOM     29  O   TYR A   4      48.893  14.630   5.050  1.00125.67           O  
ATOM     30  CB  TYR A   4      49.156  11.422   3.616  1.00123.62           C  
ATOM     31  CG  TYR A   4      47.815  11.772   3.023  1.00123.62           C  
ATOM     32  CD1 TYR A   4      47.707  12.703   1.994  1.00123.62           C  
ATOM     33  CD2 TYR A   4      46.646  11.217   3.531  1.00123.62           C  
ATOM     34  CE1 TYR A   4      46.469  13.076   1.496  1.00123.62           C  
ATOM     35  CE2 TYR A   4      45.409  11.582   3.038  1.00123.62           C  
ATOM     36  CZ  TYR A   4      45.326  12.510   2.027  1.00123.62           C  
ATOM     37  OH  TYR A   4      44.095  12.883   1.566  1.00123.62           O  
ATOM     38  N   GLU A   5      48.466  12.692   6.144  1.00119.33           N  
ATOM     39  CA  GLU A   5      47.589  13.285   7.156  1.00119.33           C  
ATOM     40  C   GLU A   5      48.111  14.632   7.632  1.00119.33           C  
ATOM     41  O   GLU A   5      47.338  15.548   7.914  1.00129.37           O  
ATOM     42  CB  GLU A   5      47.434  12.349   8.358  1.00157.00           C  
ATOM     43  CG  GLU A   5      46.888  10.969   8.026  1.00157.00           C  
ATOM     44  CD  GLU A   5      47.974   9.985   7.633  1.00157.00           C  
ATOM     45  OE1 GLU A   5      48.658  10.215   6.614  1.00157.00           O  
ATOM     46  OE2 GLU A   5      48.147   8.976   8.351  1.00157.00           O  
ATOM     47  N   GLU A   6      49.430  14.743   7.715  1.00 95.13           N  
ATOM     48  CA  GLU A   6      50.064  15.972   8.148  1.00 95.13           C  
ATOM     49  C   GLU A   6      49.763  17.100   7.165  1.00 95.13           C  
ATOM     50  O   GLU A   6      49.536  18.246   7.567  1.00100.44           O  
ATOM     51  CB  GLU A   6      51.579  15.772   8.245  1.00177.84           C  
ATOM     52  CG  GLU A   6      52.345  17.003   8.707  1.00177.84           C  
ATOM     53  CD  GLU A   6      53.847  16.833   8.581  1.00177.84           C  
ATOM     54  OE1 GLU A   6      54.335  16.686   7.441  1.00177.84           O  
ATOM     55  OE2 GLU A   6      54.540  16.844   9.621  1.00177.84           O  
ATOM     56  N   VAL A   7      49.752  16.768   5.875  1.00114.95           N  
ATOM     57  CA  VAL A   7      49.514  17.766   4.835  1.00114.95           C  
ATOM     58  C   VAL A   7      48.056  17.938   4.461  1.00114.95           C  
ATOM     59  O   VAL A   7      47.603  19.055   4.193  1.00113.22           O  
ATOM     60  CB  VAL A   7      50.279  17.425   3.552  1.00 73.67           C  
ATOM     61  CG1 VAL A   7      50.573  18.710   2.777  1.00 73.67           C  
ATOM     62  CG2 VAL A   7      51.554  16.664   3.889  1.00 73.67           C  
ATOM     63  N   ILE A   8      47.328  16.828   4.427  1.00112.51           N  
ATOM     64  CA  ILE A   8      45.918  16.863   4.074  1.00112.51           C  
ATOM     65  C   ILE A   8      45.185  17.872   4.967  1.00112.51           C  
ATOM     66  O   ILE A   8      44.224  18.510   4.530  1.00119.88           O  
ATOM     67  CB  ILE A   8      45.286  15.453   4.207  1.00 80.34           C  
ATOM     68  CG1 ILE A   8      43.896  15.429   3.575  1.00 80.34           C  
ATOM     69  CG2 ILE A   8      45.170  15.071   5.660  1.00 80.34           C  
ATOM     70  CD1 ILE A   8      43.887  15.646   2.094  1.00 80.34           C  
ATOM     71  N   LYS A   9      45.660  18.021   6.207  1.00 89.23           N  
ATOM     72  CA  LYS A   9      45.084  18.952   7.186  1.00 89.23           C  
ATOM     73  C   LYS A   9      45.301  20.410   6.796  1.00 89.23           C  
ATOM     74  O   LYS A   9      44.401  21.242   6.924  1.00107.58           O  
ATOM     75  CB  LYS A   9      45.705  18.708   8.559  1.00143.89           C  
ATOM     76  CG  LYS A   9      44.911  17.780   9.460  1.00143.89           C  
ATOM     77  CD  LYS A   9      43.738  18.512  10.099  1.00143.89           C  
ATOM     78  CE  LYS A   9      43.127  17.694  11.228  1.00143.89           C  
ATOM     79  NZ  LYS A   9      42.029  18.429  11.917  1.00143.89           N  
ATOM     80  N   LYS A  10      46.507  20.700   6.318  1.00107.86           N  
ATOM     81  CA  LYS A  10      46.904  22.042   5.894  1.00107.86           C  
ATOM     82  C   LYS A  10      46.067  22.550   4.712  1.00107.86           C  
ATOM     83  O   LYS A  10      46.093  23.743   4.377  1.00107.86           O  
ATOM     84  CB  LYS A  10      48.383  22.024   5.489  1.00126.36           C  
ATOM     85  CG  LYS A  10      49.279  21.224   6.439  1.00126.36           C  
ATOM     86  CD  LYS A  10      50.703  21.081   5.902  1.00126.36           C  
ATOM     87  CE  LYS A  10      51.581  20.253   6.841  1.00126.36           C  
ATOM     88  NZ  LYS A  10      52.961  20.032   6.308  1.00126.36           N  
ATOM     89  N   TYR A  11      45.330  21.633   4.086  1.00163.49           N  
ATOM     90  CA  TYR A  11      44.503  21.949   2.924  1.00163.49           C  
ATOM     91  C   TYR A  11      43.005  21.700   3.098  1.00163.49           C  
ATOM     92  O   TYR A  11      42.183  22.415   2.528  1.00163.49           O  
ATOM     93  CB  TYR A  11      45.000  21.158   1.711  1.00101.85           C  
ATOM     94  CG  TYR A  11      46.305  21.661   1.122  1.00101.85           C  
ATOM     95  CD1 TYR A  11      47.510  20.976   1.323  1.00101.85           C  
ATOM     96  CD2 TYR A  11      46.327  22.811   0.329  1.00101.85           C  
ATOM     97  CE1 TYR A  11      48.698  21.422   0.740  1.00101.85           C  
ATOM     98  CE2 TYR A  11      47.509  23.264  -0.257  1.00101.85           C  
ATOM     99  CZ  TYR A  11      48.687  22.566  -0.051  1.00101.85           C  
ATOM    100  OH  TYR A  11      49.837  23.008  -0.667  1.00101.85           O  
ATOM    101  N   ARG A  12      42.649  20.679   3.868  1.00133.14           N  
ATOM    102  CA  ARG A  12      41.246  20.358   4.098  1.00133.14           C  
ATOM    103  C   ARG A  12      40.723  20.910   5.418  1.00133.14           C  
ATOM    104  O   ARG A  12      39.972  21.888   5.446  1.00133.14           O  
ATOM    105  CB  ARG A  12      41.025  18.843   4.084  1.00103.81           C  
ATOM    106  CG  ARG A  12      39.629  18.434   4.568  1.00103.81           C  
ATOM    107  CD  ARG A  12      39.387  16.921   4.550  1.00103.81           C  
ATOM    108  NE  ARG A  12      37.994  16.596   4.885  1.00103.81           N  
ATOM    109  CZ  ARG A  12      37.456  15.375   4.837  1.00103.81           C  
ATOM    110  NH1 ARG A  12      38.186  14.330   4.466  1.00103.81           N  
ATOM    111  NH2 ARG A  12      36.177  15.196   5.154  1.00103.81           N  
ATOM    112  N   GLY A  13      41.121  20.267   6.511  1.00179.53           N  
ATOM    113  CA  GLY A  13      40.668  20.683   7.823  1.00179.53           C  
ATOM    114  C   GLY A  13      39.421  19.902   8.195  1.00179.53           C  
ATOM    115  O   GLY A  13      39.443  18.669   8.232  1.00179.53           O  
ATOM    116  N   GLU A  14      38.331  20.614   8.462  1.00199.00           N  
ATOM    117  CA  GLU A  14      37.072  19.975   8.828  1.00199.00           C  
ATOM    118  C   GLU A  14      36.048  20.077   7.704  1.00199.00           C  
ATOM    119  O   GLU A  14      34.919  19.604   7.838  1.00199.00           O  
ATOM    120  CB  GLU A  14      36.504  20.607  10.103  1.00186.18           C  
ATOM    121  CG  GLU A  14      37.341  20.359  11.353  1.00186.18           C  
ATOM    122  CD  GLU A  14      37.405  18.890  11.744  1.00186.18           C  
ATOM    123  OE1 GLU A  14      38.104  18.567  12.727  1.00186.18           O  
ATOM    124  OE2 GLU A  14      36.756  18.058  11.073  1.00186.18           O  
ATOM    125  N   GLU A  15      36.447  20.695   6.596  1.00159.64           N  
ATOM    126  CA  GLU A  15      35.563  20.854   5.444  1.00159.64           C  
ATOM    127  C   GLU A  15      35.091  19.504   4.902  1.00159.64           C  
ATOM    128  O   GLU A  15      35.906  18.636   4.590  1.00159.64           O  
ATOM    129  CB  GLU A  15      36.283  21.614   4.326  1.00138.83           C  
ATOM    130  CG  GLU A  15      36.673  23.041   4.666  1.00138.83           C  
ATOM    131  CD  GLU A  15      37.454  23.712   3.544  1.00138.83           C  
ATOM    132  OE1 GLU A  15      37.752  24.922   3.657  1.00138.83           O  
ATOM    133  OE2 GLU A  15      37.775  23.027   2.548  1.00138.83           O  
ATOM    134  N   ASN A  16      33.777  19.327   4.797  1.00150.24           N  
ATOM    135  CA  ASN A  16      33.215  18.088   4.266  1.00150.24           C  
ATOM    136  C   ASN A  16      33.149  18.254   2.758  1.00150.24           C  
ATOM    137  O   ASN A  16      33.221  19.380   2.254  1.00150.24           O  
ATOM    138  CB  ASN A  16      31.808  17.847   4.810  1.00138.62           C  
ATOM    139  CG  ASN A  16      31.770  17.809   6.317  1.00138.62           C  
ATOM    140  OD1 ASN A  16      32.482  17.027   6.948  1.00138.62           O  
ATOM    141  ND2 ASN A  16      30.934  18.656   6.908  1.00138.62           N  
ATOM    142  N   PHE A  17      33.010  17.147   2.033  1.00 87.49           N  
ATOM    143  CA  PHE A  17      32.953  17.244   0.581  1.00 87.49           C  
ATOM    144  C   PHE A  17      32.128  16.176  -0.094  1.00 87.49           C  
ATOM    145  O   PHE A  17      31.988  15.054   0.411  1.00 87.49           O  
ATOM    146  CB  PHE A  17      34.366  17.235  -0.009  1.00 93.47           C  
ATOM    147  CG  PHE A  17      35.016  15.874  -0.043  1.00 93.47           C  
ATOM    148  CD1 PHE A  17      34.647  14.934  -0.992  1.00 93.47           C  
ATOM    149  CD2 PHE A  17      36.023  15.550   0.853  1.00 93.47           C  
ATOM    150  CE1 PHE A  17      35.272  13.707  -1.048  1.00 93.47           C  
ATOM    151  CE2 PHE A  17      36.652  14.320   0.801  1.00 93.47           C  
ATOM    152  CZ  PHE A  17      36.278  13.400  -0.151  1.00 93.47           C  
ATOM    153  N   ASP A  18      31.605  16.543  -1.259  1.00 70.96           N  
ATOM    154  CA  ASP A  18      30.784  15.650  -2.055  1.00 70.96           C  
ATOM    155  C   ASP A  18      31.638  14.503  -2.597  1.00 70.96           C  
ATOM    156  O   ASP A  18      32.585  14.736  -3.366  1.00 70.96           O  
ATOM    157  CB  ASP A  18      30.165  16.418  -3.217  1.00119.40           C  
ATOM    158  CG  ASP A  18      29.075  15.639  -3.899  1.00119.40           C  
ATOM    159  OD1 ASP A  18      29.275  14.430  -4.130  1.00119.40           O  
ATOM    160  OD2 ASP A  18      28.022  16.232  -4.206  1.00119.40           O  
ATOM    161  N   HIS A  19      31.299  13.273  -2.196  1.00 43.50           N  
ATOM    162  CA  HIS A  19      32.031  12.083  -2.626  1.00 43.50           C  
ATOM    163  C   HIS A  19      31.578  11.550  -3.977  1.00 43.50           C  
ATOM    164  O   HIS A  19      32.145  10.596  -4.502  1.00 43.50           O  
ATOM    165  CB  HIS A  19      31.888  10.972  -1.592  1.00 77.76           C  
ATOM    166  CG  HIS A  19      32.874  11.058  -0.475  1.00 77.76           C  
ATOM    167  ND1 HIS A  19      33.013  12.181   0.311  1.00 77.76           N  
ATOM    168  CD2 HIS A  19      33.747  10.144   0.013  1.00 77.76           C  
ATOM    169  CE1 HIS A  19      33.927  11.954   1.238  1.00 77.76           C  
ATOM    170  NE2 HIS A  19      34.388  10.726   1.079  1.00 77.76           N  
ATOM    171  N   ALA A  20      30.548  12.152  -4.546  1.00 72.04           N  
ATOM    172  CA  ALA A  20      30.073  11.670  -5.824  1.00 72.04           C  
ATOM    173  C   ALA A  20      30.871  12.275  -6.948  1.00 72.04           C  
ATOM    174  O   ALA A  20      31.145  11.610  -7.950  1.00 72.04           O  
ATOM    175  CB  ALA A  20      28.611  12.001  -6.005  1.00 47.45           C  
ATOM    176  N   ALA A  21      31.272  13.529  -6.793  1.00 41.43           N  
ATOM    177  CA  ALA A  21      31.996  14.136  -7.884  1.00 41.43           C  
ATOM    178  C   ALA A  21      32.728  15.445  -7.675  1.00 41.43           C  
ATOM    179  O   ALA A  21      32.258  16.321  -6.958  1.00 41.43           O  
ATOM    180  CB  ALA A  21      31.052  14.295  -9.002  1.00 13.52           C  
ATOM    181  N   TYR A  22      33.884  15.553  -8.318  1.00 49.52           N  
ATOM    182  CA  TYR A  22      34.699  16.760  -8.342  1.00 49.52           C  
ATOM    183  C   TYR A  22      35.559  16.552  -9.568  1.00 49.52           C  
ATOM    184  O   TYR A  22      36.182  15.496  -9.703  1.00 49.52           O  
ATOM    185  CB  TYR A  22      35.607  16.912  -7.137  1.00 75.21           C  
ATOM    186  CG  TYR A  22      36.271  18.263  -7.183  1.00 75.21           C  
ATOM    187  CD1 TYR A  22      35.496  19.418  -7.173  1.00 75.21           C  
ATOM    188  CD2 TYR A  22      37.653  18.401  -7.312  1.00 75.21           C  
ATOM    189  CE1 TYR A  22      36.067  20.689  -7.297  1.00 75.21           C  
ATOM    190  CE2 TYR A  22      38.246  19.673  -7.439  1.00 75.21           C  
ATOM    191  CZ  TYR A  22      37.438  20.819  -7.433  1.00 75.21           C  
ATOM    192  OH  TYR A  22      37.958  22.098  -7.581  1.00 75.21           O  
ATOM    193  N   ASP A  23      35.612  17.523 -10.473  1.00 45.96           N  
ATOM    194  CA  ASP A  23      36.397  17.323 -11.694  1.00 45.96           C  
ATOM    195  C   ASP A  23      37.423  18.422 -11.926  1.00 45.96           C  
ATOM    196  O   ASP A  23      37.106  19.482 -12.456  1.00 45.96           O  
ATOM    197  CB  ASP A  23      35.444  17.234 -12.896  1.00 36.13           C  
ATOM    198  CG  ASP A  23      36.154  16.868 -14.186  1.00 36.13           C  
ATOM    199  OD1 ASP A  23      37.364  17.162 -14.319  1.00 36.13           O  
ATOM    200  OD2 ASP A  23      35.491  16.297 -15.078  1.00 36.13           O  
ATOM    201  N   TRP A  24      38.665  18.172 -11.550  1.00 40.34           N  
ATOM    202  CA  TRP A  24      39.692  19.182 -11.737  1.00 40.34           C  
ATOM    203  C   TRP A  24      39.790  19.725 -13.136  1.00 40.34           C  
ATOM    204  O   TRP A  24      40.300  20.832 -13.330  1.00 40.34           O  
ATOM    205  CB  TRP A  24      41.044  18.647 -11.328  1.00 53.58           C  
ATOM    206  CG  TRP A  24      41.268  18.838  -9.911  1.00 53.58           C  
ATOM    207  CD1 TRP A  24      41.432  17.877  -8.973  1.00 53.58           C  
ATOM    208  CD2 TRP A  24      41.351  20.082  -9.239  1.00 53.58           C  
ATOM    209  NE1 TRP A  24      41.620  18.448  -7.746  1.00 53.58           N  
ATOM    210  CE2 TRP A  24      41.575  19.809  -7.884  1.00 53.58           C  
ATOM    211  CE3 TRP A  24      41.260  21.412  -9.651  1.00 53.58           C  
ATOM    212  CZ2 TRP A  24      41.710  20.810  -6.933  1.00 53.58           C  
ATOM    213  CZ3 TRP A  24      41.395  22.412  -8.706  1.00 53.58           C  
ATOM    214  CH2 TRP A  24      41.618  22.105  -7.365  1.00 53.58           C  
ATOM    215  N   ARG A  25      39.317  18.954 -14.112  1.00 56.99           N  
ATOM    216  CA  ARG A  25      39.360  19.390 -15.503  1.00 56.99           C  
ATOM    217  C   ARG A  25      38.670  20.710 -15.699  1.00 56.99           C  
ATOM    218  O   ARG A  25      39.226  21.643 -16.265  1.00 56.99           O  
ATOM    219  CB  ARG A  25      38.684  18.389 -16.411  1.00 36.47           C  
ATOM    220  CG  ARG A  25      39.619  17.344 -16.937  1.00 36.47           C  
ATOM    221  CD  ARG A  25      38.861  16.395 -17.836  1.00 36.47           C  
ATOM    222  NE  ARG A  25      37.658  15.917 -17.178  1.00 36.47           N  
ATOM    223  CZ  ARG A  25      36.903  14.971 -17.692  1.00 36.47           C  
ATOM    224  NH1 ARG A  25      37.262  14.440 -18.852  1.00 36.47           N  
ATOM    225  NH2 ARG A  25      35.817  14.555 -17.060  1.00 36.47           N  
ATOM    226  N   LEU A  26      37.442  20.784 -15.225  1.00 45.67           N  
ATOM    227  CA  LEU A  26      36.689  21.995 -15.380  1.00 45.67           C  
ATOM    228  C   LEU A  26      36.732  22.927 -14.183  1.00 45.67           C  
ATOM    229  O   LEU A  26      35.715  23.394 -13.723  1.00 45.67           O  
ATOM    230  CB  LEU A  26      35.256  21.635 -15.772  1.00 29.34           C  
ATOM    231  CG  LEU A  26      34.654  20.454 -15.032  1.00 29.34           C  
ATOM    232  CD1 LEU A  26      34.349  20.885 -13.647  1.00 29.34           C  
ATOM    233  CD2 LEU A  26      33.417  19.985 -15.723  1.00 29.34           C  
ATOM    234  N   HIS A  27      37.926  23.179 -13.673  1.00 38.44           N  
ATOM    235  CA  HIS A  27      38.128  24.114 -12.567  1.00 38.44           C  
ATOM    236  C   HIS A  27      39.550  24.613 -12.748  1.00 38.44           C  
ATOM    237  O   HIS A  27      40.178  25.136 -11.833  1.00 38.44           O  
ATOM    238  CB  HIS A  27      37.924  23.460 -11.190  1.00 43.49           C  
ATOM    239  CG  HIS A  27      36.491  23.140 -10.894  1.00 43.49           C  
ATOM    240  ND1 HIS A  27      35.488  24.079 -11.006  1.00 43.49           N  
ATOM    241  CD2 HIS A  27      35.877  21.969 -10.590  1.00 43.49           C  
ATOM    242  CE1 HIS A  27      34.317  23.497 -10.796  1.00 43.49           C  
ATOM    243  NE2 HIS A  27      34.524  22.216 -10.542  1.00 43.49           N  
ATOM    244  N   SER A  28      40.037  24.446 -13.969  1.00 48.11           N  
ATOM    245  CA  SER A  28      41.358  24.895 -14.324  1.00 48.11           C  
ATOM    246  C   SER A  28      42.477  24.153 -13.576  1.00 48.11           C  
ATOM    247  O   SER A  28      43.427  24.763 -13.073  1.00 48.11           O  
ATOM    248  CB  SER A  28      41.441  26.402 -14.085  1.00 53.10           C  
ATOM    249  OG  SER A  28      42.749  26.890 -14.321  1.00 53.10           O  
ATOM    250  N   GLY A  29      42.385  22.832 -13.515  1.00 59.00           N  
ATOM    251  CA  GLY A  29      43.432  22.094 -12.831  1.00 59.00           C  
ATOM    252  C   GLY A  29      44.059  20.986 -13.661  1.00 59.00           C  
ATOM    253  O   GLY A  29      44.890  20.228 -13.177  1.00 59.00           O  
ATOM    254  N   VAL A  30      43.688  20.900 -14.924  1.00 56.06           N  
ATOM    255  CA  VAL A  30      44.209  19.842 -15.756  1.00 56.06           C  
ATOM    256  C   VAL A  30      44.691  20.395 -17.081  1.00 56.06           C  
ATOM    257  O   VAL A  30      43.870  20.803 -17.905  1.00 56.06           O  
ATOM    258  CB  VAL A  30      43.101  18.815 -16.040  1.00 40.65           C  
ATOM    259  CG1 VAL A  30      43.665  17.604 -16.759  1.00 40.65           C  
ATOM    260  CG2 VAL A  30      42.433  18.425 -14.758  1.00 40.65           C  
ATOM    261  N   THR A  31      46.005  20.413 -17.301  1.00 39.85           N  
ATOM    262  CA  THR A  31      46.549  20.911 -18.566  1.00 39.85           C  
ATOM    263  C   THR A  31      46.164  19.880 -19.626  1.00 39.85           C  
ATOM    264  O   THR A  31      45.842  18.749 -19.287  1.00 39.85           O  
ATOM    265  CB  THR A  31      48.055  21.052 -18.471  1.00 61.17           C  
ATOM    266  OG1 THR A  31      48.604  19.843 -17.942  1.00 61.17           O  
ATOM    267  CG2 THR A  31      48.412  22.209 -17.552  1.00 61.17           C  
ATOM    268  N   PRO A  32      46.197  20.246 -20.921  1.00 44.51           N  
ATOM    269  CA  PRO A  32      45.830  19.346 -22.033  1.00 44.51           C  
ATOM    270  C   PRO A  32      46.574  18.029 -22.056  1.00 44.51           C  
ATOM    271  O   PRO A  32      47.736  17.985 -21.693  1.00 44.51           O  
ATOM    272  CB  PRO A  32      46.143  20.174 -23.275  1.00 39.48           C  
ATOM    273  CG  PRO A  32      46.094  21.579 -22.795  1.00 39.48           C  
ATOM    274  CD  PRO A  32      46.743  21.508 -21.443  1.00 39.48           C  
ATOM    275  N   VAL A  33      45.908  16.967 -22.498  1.00 36.62           N  
ATOM    276  CA  VAL A  33      46.543  15.643 -22.573  1.00 36.62           C  
ATOM    277  C   VAL A  33      47.599  15.632 -23.668  1.00 36.62           C  
ATOM    278  O   VAL A  33      47.447  16.309 -24.662  1.00 36.62           O  
ATOM    279  CB  VAL A  33      45.505  14.473 -22.867  1.00 37.51           C  
ATOM    280  CG1 VAL A  33      44.084  15.029 -22.933  1.00 37.51           C  
ATOM    281  CG2 VAL A  33      45.860  13.721 -24.157  1.00 37.51           C  
ATOM    282  N   LYS A  34      48.655  14.853 -23.491  1.00 44.07           N  
ATOM    283  CA  LYS A  34      49.702  14.791 -24.489  1.00 44.07           C  
ATOM    284  C   LYS A  34      49.762  13.406 -25.114  1.00 44.07           C  
ATOM    285  O   LYS A  34      48.877  12.598 -24.885  1.00 44.07           O  
ATOM    286  CB  LYS A  34      51.031  15.143 -23.852  1.00 12.88           C  
ATOM    287  CG  LYS A  34      51.048  16.517 -23.192  1.00 12.88           C  
ATOM    288  CD  LYS A  34      52.467  16.904 -22.730  1.00 12.88           C  
ATOM    289  CE  LYS A  34      52.397  18.085 -21.748  1.00 12.88           C  
ATOM    290  NZ  LYS A  34      53.670  18.518 -21.024  1.00 12.88           N  
ATOM    291  N   ASP A  35      50.786  13.120 -25.911  1.00 48.12           N  
ATOM    292  CA  ASP A  35      50.871  11.809 -26.543  1.00 48.12           C  
ATOM    293  C   ASP A  35      52.293  11.307 -26.480  1.00 48.12           C  
ATOM    294  O   ASP A  35      53.169  11.853 -27.149  1.00 48.12           O  
ATOM    295  CB  ASP A  35      50.449  11.893 -28.000  1.00 71.46           C  
ATOM    296  CG  ASP A  35      50.366  10.534 -28.656  1.00 71.46           C  
ATOM    297  OD1 ASP A  35      50.926   9.565 -28.091  1.00 71.46           O  
ATOM    298  OD2 ASP A  35      49.746  10.440 -29.743  1.00 71.46           O  
ATOM    299  N   GLN A  36      52.520  10.262 -25.687  1.00 46.03           N  
ATOM    300  CA  GLN A  36      53.850   9.693 -25.518  1.00 46.03           C  
ATOM    301  C   GLN A  36      54.296   8.958 -26.772  1.00 46.03           C  
ATOM    302  O   GLN A  36      55.444   8.532 -26.878  1.00 46.03           O  
ATOM    303  CB  GLN A  36      53.869   8.741 -24.318  1.00 59.97           C  
ATOM    304  CG  GLN A  36      53.155   7.416 -24.543  1.00 59.97           C  
ATOM    305  CD  GLN A  36      52.875   6.670 -23.241  1.00 59.97           C  
ATOM    306  OE1 GLN A  36      51.744   6.660 -22.749  1.00 59.97           O  
ATOM    307  NE2 GLN A  36      53.909   6.051 -22.671  1.00 59.97           N  
ATOM    308  N   LYS A  37      53.388   8.800 -27.727  1.00 47.66           N  
ATOM    309  CA  LYS A  37      53.732   8.125 -28.969  1.00 47.66           C  
ATOM    310  C   LYS A  37      54.328   6.738 -28.679  1.00 47.66           C  
ATOM    311  O   LYS A  37      54.074   6.155 -27.626  1.00 47.66           O  
ATOM    312  CB  LYS A  37      54.742   8.968 -29.754  1.00 50.81           C  
ATOM    313  CG  LYS A  37      54.407  10.463 -29.867  1.00 50.81           C  
ATOM    314  CD  LYS A  37      53.592  10.809 -31.111  1.00 50.81           C  
ATOM    315  CE  LYS A  37      53.487  12.331 -31.330  1.00 50.81           C  
ATOM    316  NZ  LYS A  37      54.798  13.048 -31.413  1.00 50.81           N  
ATOM    317  N   ASN A  38      55.132   6.227 -29.609  1.00 70.85           N  
ATOM    318  CA  ASN A  38      55.731   4.902 -29.491  1.00 70.85           C  
ATOM    319  C   ASN A  38      56.908   4.769 -28.530  1.00 70.85           C  
ATOM    320  O   ASN A  38      57.736   3.873 -28.694  1.00 70.85           O  
ATOM    321  CB  ASN A  38      56.154   4.413 -30.872  1.00130.30           C  
ATOM    322  CG  ASN A  38      57.062   5.396 -31.576  1.00130.30           C  
ATOM    323  OD1 ASN A  38      57.549   5.133 -32.674  1.00130.30           O  
ATOM    324  ND2 ASN A  38      57.294   6.545 -30.944  1.00130.30           N  
ATOM    325  N   CYS A  39      56.985   5.641 -27.531  1.00 64.07           N  
ATOM    326  CA  CYS A  39      58.063   5.581 -26.537  1.00 64.07           C  
ATOM    327  C   CYS A  39      57.483   5.295 -25.155  1.00 64.07           C  
ATOM    328  O   CYS A  39      56.494   5.908 -24.761  1.00 64.07           O  
ATOM    329  CB  CYS A  39      58.825   6.902 -26.514  1.00 69.50           C  
ATOM    330  SG  CYS A  39      59.718   7.254 -24.965  1.00 69.50           S  
ATOM    331  N   GLY A  40      58.104   4.385 -24.410  1.00 51.14           N  
ATOM    332  CA  GLY A  40      57.573   4.020 -23.098  1.00 51.14           C  
ATOM    333  C   GLY A  40      57.815   5.002 -21.972  1.00 51.14           C  
ATOM    334  O   GLY A  40      58.444   4.680 -20.956  1.00 51.14           O  
ATOM    335  N   SER A  41      57.270   6.199 -22.130  1.00 44.58           N  
ATOM    336  CA  SER A  41      57.485   7.253 -21.155  1.00 44.58           C  
ATOM    337  C   SER A  41      56.343   7.583 -20.218  1.00 44.58           C  
ATOM    338  O   SER A  41      56.441   8.558 -19.481  1.00 44.58           O  
ATOM    339  CB  SER A  41      57.903   8.512 -21.897  1.00 44.21           C  
ATOM    340  OG  SER A  41      57.030   8.713 -22.999  1.00 44.21           O  
ATOM    341  N   CYS A  42      55.272   6.791 -20.229  1.00 51.71           N  
ATOM    342  CA  CYS A  42      54.138   7.062 -19.339  1.00 51.71           C  
ATOM    343  C   CYS A  42      54.556   7.707 -18.011  1.00 51.71           C  
ATOM    344  O   CYS A  42      54.030   8.744 -17.621  1.00 51.71           O  
ATOM    345  CB  CYS A  42      53.324   5.782 -19.074  1.00 56.31           C  
ATOM    346  SG  CYS A  42      54.246   4.271 -18.931  1.00 56.31           S  
ATOM    347  N   TRP A  43      55.515   7.110 -17.326  1.00 39.50           N  
ATOM    348  CA  TRP A  43      55.989   7.671 -16.059  1.00 39.50           C  
ATOM    349  C   TRP A  43      56.365   9.151 -16.101  1.00 39.50           C  
ATOM    350  O   TRP A  43      56.095   9.901 -15.174  1.00 39.50           O  
ATOM    351  CB  TRP A  43      57.216   6.920 -15.587  1.00 29.96           C  
ATOM    352  CG  TRP A  43      58.285   6.966 -16.580  1.00 29.96           C  
ATOM    353  CD1 TRP A  43      58.389   6.204 -17.707  1.00 29.96           C  
ATOM    354  CD2 TRP A  43      59.441   7.790 -16.535  1.00 29.96           C  
ATOM    355  NE1 TRP A  43      59.557   6.498 -18.362  1.00 29.96           N  
ATOM    356  CE2 TRP A  43      60.226   7.469 -17.659  1.00 29.96           C  
ATOM    357  CE3 TRP A  43      59.891   8.772 -15.656  1.00 29.96           C  
ATOM    358  CZ2 TRP A  43      61.451   8.094 -17.926  1.00 29.96           C  
ATOM    359  CZ3 TRP A  43      61.109   9.400 -15.927  1.00 29.96           C  
ATOM    360  CH2 TRP A  43      61.874   9.054 -17.052  1.00 29.96           C  
ATOM    361  N   ALA A  44      57.046   9.551 -17.158  1.00 46.82           N  
ATOM    362  CA  ALA A  44      57.450  10.930 -17.293  1.00 46.82           C  
ATOM    363  C   ALA A  44      56.181  11.753 -17.543  1.00 46.82           C  
ATOM    364  O   ALA A  44      55.958  12.793 -16.918  1.00 46.82           O  
ATOM    365  CB  ALA A  44      58.419  11.053 -18.449  1.00 46.69           C  
ATOM    366  N   PHE A  45      55.332  11.285 -18.447  1.00 33.28           N  
ATOM    367  CA  PHE A  45      54.109  12.012 -18.717  1.00 33.28           C  
ATOM    368  C   PHE A  45      53.213  12.127 -17.495  1.00 33.28           C  
ATOM    369  O   PHE A  45      52.586  13.157 -17.276  1.00 33.28           O  
ATOM    370  CB  PHE A  45      53.334  11.357 -19.855  1.00 52.01           C  
ATOM    371  CG  PHE A  45      53.858  11.709 -21.202  1.00 52.01           C  
ATOM    372  CD1 PHE A  45      55.054  11.191 -21.643  1.00 52.01           C  
ATOM    373  CD2 PHE A  45      53.180  12.606 -22.012  1.00 52.01           C  
ATOM    374  CE1 PHE A  45      55.573  11.558 -22.872  1.00 52.01           C  
ATOM    375  CE2 PHE A  45      53.694  12.976 -23.237  1.00 52.01           C  
ATOM    376  CZ  PHE A  45      54.895  12.448 -23.664  1.00 52.01           C  
ATOM    377  N   SER A  46      53.150  11.073 -16.690  1.00 39.87           N  
ATOM    378  CA  SER A  46      52.288  11.124 -15.523  1.00 39.87           C  
ATOM    379  C   SER A  46      52.818  12.096 -14.514  1.00 39.87           C  
ATOM    380  O   SER A  46      52.095  12.964 -14.065  1.00 39.87           O  
ATOM    381  CB  SER A  46      52.120   9.750 -14.865  1.00 33.14           C  
ATOM    382  OG  SER A  46      50.983   9.770 -14.007  1.00 33.14           O  
ATOM    383  N   SER A  47      54.078  11.964 -14.149  1.00 53.51           N  
ATOM    384  CA  SER A  47      54.592  12.887 -13.173  1.00 53.51           C  
ATOM    385  C   SER A  47      54.517  14.300 -13.707  1.00 53.51           C  
ATOM    386  O   SER A  47      53.999  15.178 -13.033  1.00 53.51           O  
ATOM    387  CB  SER A  47      56.020  12.539 -12.780  1.00 42.18           C  
ATOM    388  OG  SER A  47      56.771  12.172 -13.910  1.00 42.18           O  
ATOM    389  N   ILE A  48      55.005  14.546 -14.912  1.00 36.85           N  
ATOM    390  CA  ILE A  48      54.941  15.908 -15.425  1.00 36.85           C  
ATOM    391  C   ILE A  48      53.508  16.448 -15.321  1.00 36.85           C  
ATOM    392  O   ILE A  48      53.274  17.526 -14.784  1.00 36.85           O  
ATOM    393  CB  ILE A  48      55.416  15.962 -16.883  1.00 39.90           C  
ATOM    394  CG1 ILE A  48      56.936  15.899 -16.923  1.00 39.90           C  
ATOM    395  CG2 ILE A  48      54.946  17.233 -17.548  1.00 39.90           C  
ATOM    396  CD1 ILE A  48      57.598  17.043 -16.214  1.00 39.90           C  
ATOM    397  N   GLY A  49      52.551  15.680 -15.818  1.00 30.45           N  
ATOM    398  CA  GLY A  49      51.173  16.107 -15.767  1.00 30.45           C  
ATOM    399  C   GLY A  49      50.693  16.553 -14.401  1.00 30.45           C  
ATOM    400  O   GLY A  49      50.035  17.578 -14.284  1.00 30.45           O  
ATOM    401  N   SER A  50      50.991  15.792 -13.361  1.00 46.52           N  
ATOM    402  CA  SER A  50      50.583  16.196 -12.032  1.00 46.52           C  
ATOM    403  C   SER A  50      51.293  17.485 -11.622  1.00 46.52           C  
ATOM    404  O   SER A  50      50.749  18.270 -10.850  1.00 46.52           O  
ATOM    405  CB  SER A  50      50.890  15.102 -11.034  1.00 65.66           C  
ATOM    406  OG  SER A  50      50.135  13.959 -11.349  1.00 65.66           O  
ATOM    407  N   VAL A  51      52.505  17.709 -12.118  1.00 44.66           N  
ATOM    408  CA  VAL A  51      53.208  18.940 -11.785  1.00 44.66           C  
ATOM    409  C   VAL A  51      52.508  20.093 -12.487  1.00 44.66           C  
ATOM    410  O   VAL A  51      52.270  21.129 -11.870  1.00 44.66           O  
ATOM    411  CB  VAL A  51      54.671  18.940 -12.250  1.00 35.53           C  
ATOM    412  CG1 VAL A  51      55.235  20.333 -12.143  1.00 35.53           C  
ATOM    413  CG2 VAL A  51      55.485  18.011 -11.402  1.00 35.53           C  
ATOM    414  N   GLU A  52      52.183  19.914 -13.769  1.00 55.19           N  
ATOM    415  CA  GLU A  52      51.498  20.953 -14.540  1.00 55.19           C  
ATOM    416  C   GLU A  52      50.238  21.411 -13.818  1.00 55.19           C  
ATOM    417  O   GLU A  52      49.917  22.603 -13.796  1.00 55.19           O  
ATOM    418  CB  GLU A  52      51.134  20.448 -15.946  1.00 46.98           C  
ATOM    419  CG  GLU A  52      52.350  20.035 -16.746  1.00 46.98           C  
ATOM    420  CD  GLU A  52      52.093  19.822 -18.235  1.00 46.98           C  
ATOM    421  OE1 GLU A  52      51.038  19.253 -18.598  1.00 46.98           O  
ATOM    422  OE2 GLU A  52      52.970  20.199 -19.051  1.00 46.98           O  
ATOM    423  N   SER A  53      49.533  20.464 -13.214  1.00 42.79           N  
ATOM    424  CA  SER A  53      48.315  20.774 -12.493  1.00 42.79           C  
ATOM    425  C   SER A  53      48.555  21.555 -11.218  1.00 42.79           C  
ATOM    426  O   SER A  53      47.769  22.441 -10.886  1.00 42.79           O  
ATOM    427  CB  SER A  53      47.569  19.499 -12.168  1.00 39.63           C  
ATOM    428  OG  SER A  53      47.239  18.844 -13.372  1.00 39.63           O  
ATOM    429  N   GLN A  54      49.614  21.234 -10.482  1.00 62.29           N  
ATOM    430  CA  GLN A  54      49.877  21.981  -9.264  1.00 62.29           C  
ATOM    431  C   GLN A  54      50.057  23.452  -9.602  1.00 62.29           C  
ATOM    432  O   GLN A  54      49.596  24.323  -8.862  1.00 62.29           O  
ATOM    433  CB  GLN A  54      51.114  21.457  -8.559  1.00 59.38           C  
ATOM    434  CG  GLN A  54      50.830  20.214  -7.765  1.00 59.38           C  
ATOM    435  CD  GLN A  54      49.634  20.390  -6.870  1.00 59.38           C  
ATOM    436  OE1 GLN A  54      49.678  21.139  -5.885  1.00 59.38           O  
ATOM    437  NE2 GLN A  54      48.541  19.707  -7.213  1.00 59.38           N  
ATOM    438  N   TYR A  55      50.730  23.730 -10.718  1.00 53.10           N  
ATOM    439  CA  TYR A  55      50.929  25.104 -11.154  1.00 53.10           C  
ATOM    440  C   TYR A  55      49.588  25.654 -11.601  1.00 53.10           C  
ATOM    441  O   TYR A  55      49.172  26.713 -11.160  1.00 53.10           O  
ATOM    442  CB  TYR A  55      51.927  25.172 -12.308  1.00 57.21           C  
ATOM    443  CG  TYR A  55      53.360  25.185 -11.857  1.00 57.21           C  
ATOM    444  CD1 TYR A  55      53.950  24.055 -11.318  1.00 57.21           C  
ATOM    445  CD2 TYR A  55      54.116  26.341 -11.938  1.00 57.21           C  
ATOM    446  CE1 TYR A  55      55.259  24.078 -10.872  1.00 57.21           C  
ATOM    447  CE2 TYR A  55      55.423  26.378 -11.492  1.00 57.21           C  
ATOM    448  CZ  TYR A  55      55.991  25.245 -10.963  1.00 57.21           C  
ATOM    449  OH  TYR A  55      57.299  25.272 -10.546  1.00 57.21           O  
ATOM    450  N   ALA A  56      48.897  24.934 -12.471  1.00 55.04           N  
ATOM    451  CA  ALA A  56      47.605  25.412 -12.916  1.00 55.04           C  
ATOM    452  C   ALA A  56      46.701  25.726 -11.724  1.00 55.04           C  
ATOM    453  O   ALA A  56      45.865  26.628 -11.791  1.00 55.04           O  
ATOM    454  CB  ALA A  56      46.956  24.398 -13.796  1.00 40.36           C  
ATOM    455  N   ILE A  57      46.856  24.991 -10.631  1.00 52.11           N  
ATOM    456  CA  ILE A  57      46.030  25.249  -9.462  1.00 52.11           C  
ATOM    457  C   ILE A  57      46.686  26.258  -8.551  1.00 52.11           C  
ATOM    458  O   ILE A  57      46.408  27.437  -8.663  1.00 52.11           O  
ATOM    459  CB  ILE A  57      45.749  23.979  -8.659  1.00 40.06           C  
ATOM    460  CG1 ILE A  57      44.762  23.090  -9.437  1.00 40.06           C  
ATOM    461  CG2 ILE A  57      45.227  24.364  -7.271  1.00 40.06           C  
ATOM    462  CD1 ILE A  57      44.576  21.700  -8.864  1.00 40.06           C  
ATOM    463  N   ARG A  58      47.566  25.806  -7.665  1.00 64.72           N  
ATOM    464  CA  ARG A  58      48.247  26.698  -6.729  1.00 64.72           C  
ATOM    465  C   ARG A  58      48.742  28.049  -7.293  1.00 64.72           C  
ATOM    466  O   ARG A  58      48.129  29.090  -7.058  1.00 64.72           O  
ATOM    467  CB  ARG A  58      49.418  25.967  -6.092  1.00 56.11           C  
ATOM    468  CG  ARG A  58      49.081  24.579  -5.612  1.00 56.11           C  
ATOM    469  CD  ARG A  58      47.869  24.523  -4.691  1.00 56.11           C  
ATOM    470  NE  ARG A  58      47.625  23.139  -4.290  1.00 56.11           N  
ATOM    471  CZ  ARG A  58      46.544  22.717  -3.641  1.00 56.11           C  
ATOM    472  NH1 ARG A  58      45.584  23.580  -3.303  1.00 56.11           N  
ATOM    473  NH2 ARG A  58      46.414  21.424  -3.344  1.00 56.11           N  
ATOM    474  N   LYS A  59      49.856  28.038  -8.016  1.00 53.97           N  
ATOM    475  CA  LYS A  59      50.415  29.261  -8.588  1.00 53.97           C  
ATOM    476  C   LYS A  59      49.601  29.776  -9.772  1.00 53.97           C  
ATOM    477  O   LYS A  59      50.114  30.556 -10.586  1.00 53.97           O  
ATOM    478  CB  LYS A  59      51.850  29.008  -9.047  1.00113.42           C  
ATOM    479  CG  LYS A  59      52.837  28.760  -7.925  1.00113.42           C  
ATOM    480  CD  LYS A  59      53.105  30.034  -7.143  1.00113.42           C  
ATOM    481  CE  LYS A  59      54.221  29.833  -6.135  1.00113.42           C  
ATOM    482  NZ  LYS A  59      53.886  28.740  -5.179  1.00113.42           N  
ATOM    483  N   ASN A  60      48.334  29.363  -9.849  1.00 51.10           N  
ATOM    484  CA  ASN A  60      47.441  29.726 -10.955  1.00 51.10           C  
ATOM    485  C   ASN A  60      48.182  30.097 -12.240  1.00 51.10           C  
ATOM    486  O   ASN A  60      48.051  31.206 -12.756  1.00 51.10           O  
ATOM    487  CB  ASN A  60      46.501  30.874 -10.579  1.00102.76           C  
ATOM    488  CG  ASN A  60      45.441  31.126 -11.651  1.00102.76           C  
ATOM    489  OD1 ASN A  60      44.554  30.295 -11.880  1.00102.76           O  
ATOM    490  ND2 ASN A  60      45.539  32.269 -12.321  1.00102.76           N  
ATOM    491  N   LYS A  61      48.977  29.164 -12.743  1.00 66.17           N  
ATOM    492  CA  LYS A  61      49.713  29.398 -13.965  1.00 66.17           C  
ATOM    493  C   LYS A  61      49.644  28.192 -14.859  1.00 66.17           C  
ATOM    494  O   LYS A  61      49.771  27.049 -14.405  1.00 66.17           O  
ATOM    495  CB  LYS A  61      51.180  29.701 -13.698  1.00 64.85           C  
ATOM    496  CG  LYS A  61      51.957  29.784 -14.999  1.00 64.85           C  
ATOM    497  CD  LYS A  61      53.329  30.382 -14.819  1.00 64.85           C  
ATOM    498  CE  LYS A  61      53.970  30.677 -16.170  1.00 64.85           C  
ATOM    499  NZ  LYS A  61      55.266  31.397 -15.999  1.00 64.85           N  
ATOM    500  N   LEU A  62      49.440  28.444 -16.143  1.00 54.12           N  
ATOM    501  CA  LEU A  62      49.380  27.351 -17.086  1.00 54.12           C  
ATOM    502  C   LEU A  62      50.759  27.259 -17.691  1.00 54.12           C  
ATOM    503  O   LEU A  62      51.269  28.237 -18.237  1.00 54.12           O  
ATOM    504  CB  LEU A  62      48.347  27.631 -18.160  1.00 24.47           C  
ATOM    505  CG  LEU A  62      48.154  26.463 -19.112  1.00 24.47           C  
ATOM    506  CD1 LEU A  62      46.949  26.731 -19.980  1.00 24.47           C  
ATOM    507  CD2 LEU A  62      49.380  26.283 -19.967  1.00 24.47           C  
ATOM    508  N   ILE A  63      51.358  26.079 -17.590  1.00 51.77           N  
ATOM    509  CA  ILE A  63      52.704  25.851 -18.101  1.00 51.77           C  
ATOM    510  C   ILE A  63      52.790  24.397 -18.473  1.00 51.77           C  
ATOM    511  O   ILE A  63      52.332  23.550 -17.723  1.00 51.77           O  
ATOM    512  CB  ILE A  63      53.768  26.138 -16.991  1.00 46.53           C  
ATOM    513  CG1 ILE A  63      55.156  25.669 -17.407  1.00 46.53           C  
ATOM    514  CG2 ILE A  63      53.393  25.422 -15.719  1.00 46.53           C  
ATOM    515  CD1 ILE A  63      55.834  26.584 -18.368  1.00 46.53           C  
ATOM    516  N   THR A  64      53.343  24.085 -19.630  1.00 74.01           N  
ATOM    517  CA  THR A  64      53.493  22.681 -19.968  1.00 74.01           C  
ATOM    518  C   THR A  64      54.990  22.396 -19.900  1.00 74.01           C  
ATOM    519  O   THR A  64      55.791  23.166 -20.432  1.00 74.01           O  
ATOM    520  CB  THR A  64      52.956  22.392 -21.331  1.00 54.47           C  
ATOM    521  OG1 THR A  64      53.598  23.247 -22.267  1.00 54.47           O  
ATOM    522  CG2 THR A  64      51.486  22.654 -21.364  1.00 54.47           C  
ATOM    523  N   LEU A  65      55.368  21.304 -19.238  1.00 36.84           N  
ATOM    524  CA  LEU A  65      56.775  20.989 -19.055  1.00 36.84           C  
ATOM    525  C   LEU A  65      57.290  19.853 -19.893  1.00 36.84           C  
ATOM    526  O   LEU A  65      56.528  19.007 -20.352  1.00 36.84           O  
ATOM    527  CB  LEU A  65      57.018  20.698 -17.596  1.00 49.11           C  
ATOM    528  CG  LEU A  65      56.613  21.926 -16.803  1.00 49.11           C  
ATOM    529  CD1 LEU A  65      56.311  21.552 -15.376  1.00 49.11           C  
ATOM    530  CD2 LEU A  65      57.729  22.942 -16.903  1.00 49.11           C  
ATOM    531  N   SER A  66      58.599  19.807 -20.065  1.00 34.10           N  
ATOM    532  CA  SER A  66      59.175  18.783 -20.908  1.00 34.10           C  
ATOM    533  C   SER A  66      59.244  17.326 -20.431  1.00 34.10           C  
ATOM    534  O   SER A  66      60.031  16.988 -19.549  1.00 34.10           O  
ATOM    535  CB  SER A  66      60.567  19.217 -21.336  1.00 45.95           C  
ATOM    536  OG  SER A  66      61.025  18.331 -22.338  1.00 45.95           O  
ATOM    537  N   GLU A  67      58.432  16.446 -21.008  1.00 41.44           N  
ATOM    538  CA  GLU A  67      58.539  15.044 -20.618  1.00 41.44           C  
ATOM    539  C   GLU A  67      59.866  14.579 -21.213  1.00 41.44           C  
ATOM    540  O   GLU A  67      60.556  13.738 -20.649  1.00 41.44           O  
ATOM    541  CB  GLU A  67      57.416  14.188 -21.212  1.00 58.06           C  
ATOM    542  CG  GLU A  67      56.084  14.305 -20.519  1.00 58.06           C  
ATOM    543  CD  GLU A  67      55.253  15.474 -21.011  1.00 58.06           C  
ATOM    544  OE1 GLU A  67      55.802  16.344 -21.736  1.00 58.06           O  
ATOM    545  OE2 GLU A  67      54.048  15.520 -20.657  1.00 58.06           O  
ATOM    546  N   GLN A  68      60.233  15.140 -22.359  1.00 65.54           N  
ATOM    547  CA  GLN A  68      61.473  14.731 -22.991  1.00 65.54           C  
ATOM    548  C   GLN A  68      62.691  14.993 -22.140  1.00 65.54           C  
ATOM    549  O   GLN A  68      63.644  14.235 -22.221  1.00 65.54           O  
ATOM    550  CB  GLN A  68      61.674  15.419 -24.324  1.00 46.34           C  
ATOM    551  CG  GLN A  68      62.833  14.838 -25.105  1.00 46.34           C  
ATOM    552  CD  GLN A  68      62.560  13.419 -25.562  1.00 46.34           C  
ATOM    553  OE1 GLN A  68      61.576  13.147 -26.252  1.00 46.34           O  
ATOM    554  NE2 GLN A  68      63.433  12.508 -25.184  1.00 46.34           N  
ATOM    555  N   GLU A  69      62.683  16.064 -21.345  1.00 65.39           N  
ATOM    556  CA  GLU A  69      63.837  16.354 -20.491  1.00 65.39           C  
ATOM    557  C   GLU A  69      63.910  15.324 -19.379  1.00 65.39           C  
ATOM    558  O   GLU A  69      64.982  15.065 -18.839  1.00 65.39           O  
ATOM    559  CB  GLU A  69      63.778  17.752 -19.871  1.00 67.92           C  
ATOM    560  CG  GLU A  69      64.955  18.010 -18.934  1.00 67.92           C  
ATOM    561  CD  GLU A  69      64.941  19.392 -18.296  1.00 67.92           C  
ATOM    562  OE1 GLU A  69      65.187  20.392 -19.002  1.00 67.92           O  
ATOM    563  OE2 GLU A  69      64.685  19.492 -17.082  1.00 67.92           O  
ATOM    564  N   LEU A  70      62.770  14.744 -19.023  1.00 61.68           N  
ATOM    565  CA  LEU A  70      62.769  13.719 -17.998  1.00 61.68           C  
ATOM    566  C   LEU A  70      63.254  12.435 -18.632  1.00 61.68           C  
ATOM    567  O   LEU A  70      64.095  11.729 -18.069  1.00 61.68           O  
ATOM    568  CB  LEU A  70      61.379  13.478 -17.443  1.00 28.38           C  
ATOM    569  CG  LEU A  70      60.939  14.207 -16.186  1.00 28.38           C  
ATOM    570  CD1 LEU A  70      59.651  13.527 -15.695  1.00 28.38           C  
ATOM    571  CD2 LEU A  70      62.032  14.149 -15.127  1.00 28.38           C  
ATOM    572  N   VAL A  71      62.724  12.115 -19.804  1.00 34.49           N  
ATOM    573  CA  VAL A  71      63.162  10.900 -20.453  1.00 34.49           C  
ATOM    574  C   VAL A  71      64.660  10.969 -20.696  1.00 34.49           C  
ATOM    575  O   VAL A  71      65.343   9.954 -20.696  1.00 34.49           O  
ATOM    576  CB  VAL A  71      62.463  10.667 -21.789  1.00 21.43           C  
ATOM    577  CG1 VAL A  71      63.154   9.566 -22.532  1.00 21.43           C  
ATOM    578  CG2 VAL A  71      61.005  10.259 -21.563  1.00 21.43           C  
ATOM    579  N   ASP A  72      65.193  12.165 -20.882  1.00 46.44           N  
ATOM    580  CA  ASP A  72      66.616  12.274 -21.133  1.00 46.44           C  
ATOM    581  C   ASP A  72      67.460  12.443 -19.893  1.00 46.44           C  
ATOM    582  O   ASP A  72      68.603  12.026 -19.885  1.00 46.44           O  
ATOM    583  CB  ASP A  72      66.914  13.432 -22.094  1.00 54.29           C  
ATOM    584  CG  ASP A  72      66.299  13.222 -23.469  1.00 54.29           C  
ATOM    585  OD1 ASP A  72      65.976  12.056 -23.811  1.00 54.29           O  
ATOM    586  OD2 ASP A  72      66.150  14.218 -24.211  1.00 54.29           O  
ATOM    587  N   CYS A  73      66.920  13.016 -18.827  1.00 54.39           N  
ATOM    588  CA  CYS A  73      67.766  13.243 -17.668  1.00 54.39           C  
ATOM    589  C   CYS A  73      67.445  12.542 -16.358  1.00 54.39           C  
ATOM    590  O   CYS A  73      68.287  12.521 -15.456  1.00 54.39           O  
ATOM    591  CB  CYS A  73      67.860  14.737 -17.393  1.00 63.29           C  
ATOM    592  SG  CYS A  73      67.982  15.845 -18.842  1.00 63.29           S  
ATOM    593  N   SER A  74      66.241  11.998 -16.207  1.00 56.89           N  
ATOM    594  CA  SER A  74      65.939  11.309 -14.960  1.00 56.89           C  
ATOM    595  C   SER A  74      66.724  10.011 -15.010  1.00 56.89           C  
ATOM    596  O   SER A  74      66.356   9.067 -15.711  1.00 56.89           O  
ATOM    597  CB  SER A  74      64.454  11.018 -14.833  1.00 53.82           C  
ATOM    598  OG  SER A  74      64.216  10.334 -13.616  1.00 53.82           O  
ATOM    599  N   PHE A  75      67.825   9.961 -14.282  1.00 80.38           N  
ATOM    600  CA  PHE A  75      68.641   8.772 -14.312  1.00 80.38           C  
ATOM    601  C   PHE A  75      68.147   7.652 -13.411  1.00 80.38           C  
ATOM    602  O   PHE A  75      68.578   6.505 -13.550  1.00 80.38           O  
ATOM    603  CB  PHE A  75      70.079   9.159 -14.000  1.00 51.60           C  
ATOM    604  CG  PHE A  75      70.678  10.087 -15.024  1.00 51.60           C  
ATOM    605  CD1 PHE A  75      70.716   9.724 -16.368  1.00 51.60           C  
ATOM    606  CD2 PHE A  75      71.168  11.337 -14.658  1.00 51.60           C  
ATOM    607  CE1 PHE A  75      71.224  10.588 -17.326  1.00 51.60           C  
ATOM    608  CE2 PHE A  75      71.685  12.212 -15.622  1.00 51.60           C  
ATOM    609  CZ  PHE A  75      71.708  11.837 -16.951  1.00 51.60           C  
ATOM    610  N   LYS A  76      67.234   7.970 -12.496  1.00 58.62           N  
ATOM    611  CA  LYS A  76      66.702   6.939 -11.626  1.00 58.62           C  
ATOM    612  C   LYS A  76      65.611   6.210 -12.376  1.00 58.62           C  
ATOM    613  O   LYS A  76      64.864   5.420 -11.798  1.00 58.62           O  
ATOM    614  CB  LYS A  76      66.153   7.525 -10.328  1.00 61.81           C  
ATOM    615  CG  LYS A  76      67.216   8.153  -9.449  1.00 61.81           C  
ATOM    616  CD  LYS A  76      66.770   8.211  -7.991  1.00 61.81           C  
ATOM    617  CE  LYS A  76      67.576   9.234  -7.179  1.00 61.81           C  
ATOM    618  NZ  LYS A  76      67.296  10.666  -7.569  1.00 61.81           N  
ATOM    619  N   ASN A  77      65.523   6.483 -13.671  1.00 47.12           N  
ATOM    620  CA  ASN A  77      64.530   5.837 -14.516  1.00 47.12           C  
ATOM    621  C   ASN A  77      65.226   5.321 -15.765  1.00 47.12           C  
ATOM    622  O   ASN A  77      66.449   5.402 -15.860  1.00 47.12           O  
ATOM    623  CB  ASN A  77      63.421   6.822 -14.876  1.00 46.07           C  
ATOM    624  CG  ASN A  77      62.542   7.150 -13.695  1.00 46.07           C  
ATOM    625  OD1 ASN A  77      61.767   6.304 -13.233  1.00 46.07           O  
ATOM    626  ND2 ASN A  77      62.661   8.374 -13.180  1.00 46.07           N  
ATOM    627  N   TYR A  78      64.473   4.800 -16.726  1.00 45.80           N  
ATOM    628  CA  TYR A  78      65.106   4.266 -17.920  1.00 45.80           C  
ATOM    629  C   TYR A  78      64.545   4.800 -19.212  1.00 45.80           C  
ATOM    630  O   TYR A  78      64.233   4.026 -20.135  1.00 45.80           O  
ATOM    631  CB  TYR A  78      65.006   2.745 -17.926  1.00 62.55           C  
ATOM    632  CG  TYR A  78      65.613   2.145 -16.696  1.00 62.55           C  
ATOM    633  CD1 TYR A  78      64.905   2.114 -15.502  1.00 62.55           C  
ATOM    634  CD2 TYR A  78      66.931   1.709 -16.694  1.00 62.55           C  
ATOM    635  CE1 TYR A  78      65.496   1.677 -14.336  1.00 62.55           C  
ATOM    636  CE2 TYR A  78      67.529   1.269 -15.534  1.00 62.55           C  
ATOM    637  CZ  TYR A  78      66.806   1.261 -14.358  1.00 62.55           C  
ATOM    638  OH  TYR A  78      67.399   0.874 -13.186  1.00 62.55           O  
ATOM    639  N   GLY A  79      64.394   6.117 -19.277  1.00 31.45           N  
ATOM    640  CA  GLY A  79      63.889   6.716 -20.496  1.00 31.45           C  
ATOM    641  C   GLY A  79      62.771   5.937 -21.135  1.00 31.45           C  
ATOM    642  O   GLY A  79      61.871   5.491 -20.420  1.00 31.45           O  
ATOM    643  N   CYS A  80      62.833   5.733 -22.458  1.00 40.25           N  
ATOM    644  CA  CYS A  80      61.735   5.049 -23.136  1.00 40.25           C  
ATOM    645  C   CYS A  80      61.476   3.666 -22.643  1.00 40.25           C  
ATOM    646  O   CYS A  80      60.422   3.108 -22.918  1.00 40.25           O  
ATOM    647  CB  CYS A  80      61.896   5.064 -24.656  1.00 90.99           C  
ATOM    648  SG  CYS A  80      61.664   6.747 -25.319  1.00 90.99           S  
ATOM    649  N   ASN A  81      62.407   3.132 -21.862  1.00 70.33           N  
ATOM    650  CA  ASN A  81      62.245   1.786 -21.343  1.00 70.33           C  
ATOM    651  C   ASN A  81      61.550   1.683 -19.998  1.00 70.33           C  
ATOM    652  O   ASN A  81      61.538   0.615 -19.387  1.00 70.33           O  
ATOM    653  CB  ASN A  81      63.591   1.068 -21.291  1.00 78.48           C  
ATOM    654  CG  ASN A  81      64.048   0.603 -22.661  1.00 78.48           C  
ATOM    655  OD1 ASN A  81      63.240   0.131 -23.469  1.00 78.48           O  
ATOM    656  ND2 ASN A  81      65.349   0.719 -22.925  1.00 78.48           N  
ATOM    657  N   GLY A  82      60.970   2.786 -19.536  1.00 51.52           N  
ATOM    658  CA  GLY A  82      60.247   2.741 -18.277  1.00 51.52           C  
ATOM    659  C   GLY A  82      60.812   3.517 -17.108  1.00 51.52           C  
ATOM    660  O   GLY A  82      61.962   3.967 -17.127  1.00 51.52           O  
ATOM    661  N   GLY A  83      59.999   3.665 -16.067  1.00 44.81           N  
ATOM    662  CA  GLY A  83      60.460   4.416 -14.914  1.00 44.81           C  
ATOM    663  C   GLY A  83      59.437   4.415 -13.803  1.00 44.81           C  
ATOM    664  O   GLY A  83      58.375   3.818 -13.953  1.00 44.81           O  
ATOM    665  N   LEU A  84      59.745   5.077 -12.692  1.00 42.85           N  
ATOM    666  CA  LEU A  84      58.824   5.125 -11.558  1.00 42.85           C  
ATOM    667  C   LEU A  84      58.467   6.545 -11.189  1.00 42.85           C  
ATOM    668  O   LEU A  84      59.355   7.390 -11.021  1.00 42.85           O  
ATOM    669  CB  LEU A  84      59.418   4.455 -10.301  1.00 55.96           C  
ATOM    670  CG  LEU A  84      59.509   2.939 -10.114  1.00 55.96           C  
ATOM    671  CD1 LEU A  84      58.627   2.191 -11.117  1.00 55.96           C  
ATOM    672  CD2 LEU A  84      60.951   2.546 -10.272  1.00 55.96           C  
ATOM    673  N   ILE A  85      57.167   6.776 -11.008  1.00 40.75           N  
ATOM    674  CA  ILE A  85      56.664   8.090 -10.675  1.00 40.75           C  
ATOM    675  C   ILE A  85      57.487   8.866  -9.663  1.00 40.75           C  
ATOM    676  O   ILE A  85      57.937   9.984  -9.941  1.00 40.75           O  
ATOM    677  CB  ILE A  85      55.269   8.011 -10.152  1.00 26.82           C  
ATOM    678  CG1 ILE A  85      54.363   7.373 -11.198  1.00 26.82           C  
ATOM    679  CG2 ILE A  85      54.788   9.397  -9.844  1.00 26.82           C  
ATOM    680  CD1 ILE A  85      52.871   7.374 -10.833  1.00 26.82           C  
ATOM    681  N   ASN A  86      57.680   8.286  -8.484  1.00 58.07           N  
ATOM    682  CA  ASN A  86      58.441   8.968  -7.439  1.00 58.07           C  
ATOM    683  C   ASN A  86      59.878   9.211  -7.884  1.00 58.07           C  
ATOM    684  O   ASN A  86      60.477  10.229  -7.557  1.00 58.07           O  
ATOM    685  CB  ASN A  86      58.406   8.150  -6.158  1.00 73.32           C  
ATOM    686  CG  ASN A  86      58.848   6.739  -6.381  1.00 73.32           C  
ATOM    687  OD1 ASN A  86      58.375   6.061  -7.299  1.00 73.32           O  
ATOM    688  ND2 ASN A  86      59.763   6.276  -5.548  1.00 73.32           N  
ATOM    689  N   ASN A  87      60.436   8.278  -8.638  1.00 53.25           N  
ATOM    690  CA  ASN A  87      61.793   8.468  -9.114  1.00 53.25           C  
ATOM    691  C   ASN A  87      61.787   9.744  -9.923  1.00 53.25           C  
ATOM    692  O   ASN A  87      62.672  10.590  -9.784  1.00 53.25           O  
ATOM    693  CB  ASN A  87      62.229   7.314 -10.013  1.00 73.05           C  
ATOM    694  CG  ASN A  87      62.598   6.087  -9.233  1.00 73.05           C  
ATOM    695  OD1 ASN A  87      62.935   6.178  -8.050  1.00 73.05           O  
ATOM    696  ND2 ASN A  87      62.557   4.928  -9.887  1.00 73.05           N  
ATOM    697  N   ALA A  88      60.779   9.875 -10.779  1.00 37.60           N  
ATOM    698  CA  ALA A  88      60.656  11.057 -11.613  1.00 37.60           C  
ATOM    699  C   ALA A  88      60.684  12.306 -10.718  1.00 37.60           C  
ATOM    700  O   ALA A  88      61.602  13.129 -10.820  1.00 37.60           O  
ATOM    701  CB  ALA A  88      59.378  10.985 -12.413  1.00 25.35           C  
ATOM    702  N   PHE A  89      59.705  12.439  -9.827  1.00 48.28           N  
ATOM    703  CA  PHE A  89      59.687  13.587  -8.920  1.00 48.28           C  
ATOM    704  C   PHE A  89      61.047  13.735  -8.252  1.00 48.28           C  
ATOM    705  O   PHE A  89      61.531  14.839  -8.053  1.00 48.28           O  
ATOM    706  CB  PHE A  89      58.618  13.409  -7.846  1.00 43.52           C  
ATOM    707  CG  PHE A  89      57.230  13.446  -8.379  1.00 43.52           C  
ATOM    708  CD1 PHE A  89      56.818  14.489  -9.200  1.00 43.52           C  
ATOM    709  CD2 PHE A  89      56.323  12.454  -8.061  1.00 43.52           C  
ATOM    710  CE1 PHE A  89      55.510  14.540  -9.702  1.00 43.52           C  
ATOM    711  CE2 PHE A  89      55.008  12.499  -8.557  1.00 43.52           C  
ATOM    712  CZ  PHE A  89      54.603  13.549  -9.382  1.00 43.52           C  
ATOM    713  N   GLU A  90      61.656  12.610  -7.900  1.00 56.98           N  
ATOM    714  CA  GLU A  90      62.964  12.630  -7.274  1.00 56.98           C  
ATOM    715  C   GLU A  90      63.878  13.406  -8.209  1.00 56.98           C  
ATOM    716  O   GLU A  90      64.280  14.526  -7.891  1.00 56.98           O  
ATOM    717  CB  GLU A  90      63.494  11.206  -7.100  1.00103.38           C  
ATOM    718  CG  GLU A  90      64.168  10.924  -5.759  1.00103.38           C  
ATOM    719  CD  GLU A  90      63.173  10.821  -4.612  1.00103.38           C  
ATOM    720  OE1 GLU A  90      62.776  11.872  -4.062  1.00103.38           O  
ATOM    721  OE2 GLU A  90      62.782   9.682  -4.272  1.00103.38           O  
ATOM    722  N   ASP A  91      64.186  12.821  -9.370  1.00 65.42           N  
ATOM    723  CA  ASP A  91      65.058  13.474 -10.343  1.00 65.42           C  
ATOM    724  C   ASP A  91      64.641  14.909 -10.663  1.00 65.42           C  
ATOM    725  O   ASP A  91      65.473  15.742 -11.015  1.00 65.42           O  
ATOM    726  CB  ASP A  91      65.138  12.661 -11.632  1.00 81.10           C  
ATOM    727  CG  ASP A  91      66.255  11.647 -11.603  1.00 81.10           C  
ATOM    728  OD1 ASP A  91      66.130  10.670 -10.849  1.00 81.10           O  
ATOM    729  OD2 ASP A  91      67.267  11.828 -12.318  1.00 81.10           O  
ATOM    730  N   MET A  92      63.353  15.202 -10.554  1.00 50.61           N  
ATOM    731  CA  MET A  92      62.896  16.552 -10.812  1.00 50.61           C  
ATOM    732  C   MET A  92      63.547  17.475  -9.797  1.00 50.61           C  
ATOM    733  O   MET A  92      64.018  18.565 -10.110  1.00 50.61           O  
ATOM    734  CB  MET A  92      61.390  16.635 -10.663  1.00 46.78           C  
ATOM    735  CG  MET A  92      60.657  16.191 -11.866  1.00 46.78           C  
ATOM    736  SD  MET A  92      59.084  16.975 -11.855  1.00 46.78           S  
ATOM    737  CE  MET A  92      57.960  15.591 -12.333  1.00 46.78           C  
ATOM    738  N   ILE A  93      63.562  17.025  -8.558  1.00 89.27           N  
ATOM    739  CA  ILE A  93      64.143  17.801  -7.489  1.00 89.27           C  
ATOM    740  C   ILE A  93      65.644  17.885  -7.683  1.00 89.27           C  
ATOM    741  O   ILE A  93      66.231  18.948  -7.519  1.00 89.27           O  
ATOM    742  CB  ILE A  93      63.770  17.163  -6.154  1.00 49.76           C  
ATOM    743  CG1 ILE A  93      62.332  17.557  -5.827  1.00 49.76           C  
ATOM    744  CG2 ILE A  93      64.745  17.557  -5.081  1.00 49.76           C  
ATOM    745  CD1 ILE A  93      61.694  16.701  -4.799  1.00 49.76           C  
ATOM    746  N   GLU A  94      66.251  16.761  -8.049  1.00 73.46           N  
ATOM    747  CA  GLU A  94      67.690  16.698  -8.294  1.00 73.46           C  
ATOM    748  C   GLU A  94      68.076  17.734  -9.343  1.00 73.46           C  
ATOM    749  O   GLU A  94      69.062  18.456  -9.190  1.00 73.46           O  
ATOM    750  CB  GLU A  94      68.081  15.312  -8.820  1.00135.27           C  
ATOM    751  CG  GLU A  94      68.220  14.231  -7.772  1.00135.27           C  
ATOM    752  CD  GLU A  94      69.522  14.338  -7.015  1.00135.27           C  
ATOM    753  OE1 GLU A  94      70.584  14.319  -7.672  1.00135.27           O  
ATOM    754  OE2 GLU A  94      69.484  14.438  -5.769  1.00135.27           O  
ATOM    755  N   LEU A  95      67.284  17.787 -10.413  1.00 65.55           N  
ATOM    756  CA  LEU A  95      67.507  18.696 -11.529  1.00 65.55           C  
ATOM    757  C   LEU A  95      67.084  20.121 -11.234  1.00 65.55           C  
ATOM    758  O   LEU A  95      67.394  21.036 -11.998  1.00 65.55           O  
ATOM    759  CB  LEU A  95      66.741  18.199 -12.747  1.00 41.86           C  
ATOM    760  CG  LEU A  95      67.328  16.953 -13.389  1.00 41.86           C  
ATOM    761  CD1 LEU A  95      66.421  16.431 -14.473  1.00 41.86           C  
ATOM    762  CD2 LEU A  95      68.681  17.303 -13.953  1.00 41.86           C  
ATOM    763  N   GLY A  96      66.364  20.306 -10.134  1.00 80.92           N  
ATOM    764  CA  GLY A  96      65.900  21.632  -9.782  1.00 80.92           C  
ATOM    765  C   GLY A  96      65.063  22.244 -10.892  1.00 80.92           C  
ATOM    766  O   GLY A  96      65.414  23.292 -11.445  1.00 80.92           O  
ATOM    767  N   GLY A  97      63.957  21.582 -11.224  1.00 61.43           N  
ATOM    768  CA  GLY A  97      63.078  22.078 -12.269  1.00 61.43           C  
ATOM    769  C   GLY A  97      63.259  21.456 -13.643  1.00 61.43           C  
ATOM    770  O   GLY A  97      64.298  20.888 -13.953  1.00 61.43           O  
ATOM    771  N   ILE A  98      62.228  21.575 -14.468  1.00 45.42           N  
ATOM    772  CA  ILE A  98      62.243  21.039 -15.817  1.00 45.42           C  
ATOM    773  C   ILE A  98      61.932  22.133 -16.825  1.00 45.42           C  
ATOM    774  O   ILE A  98      61.121  23.025 -16.574  1.00 45.42           O  
ATOM    775  CB  ILE A  98      61.185  19.950 -16.009  1.00 58.66           C  
ATOM    776  CG1 ILE A  98      61.577  18.692 -15.260  1.00 58.66           C  
ATOM    777  CG2 ILE A  98      61.030  19.640 -17.470  1.00 58.66           C  
ATOM    778  CD1 ILE A  98      61.458  18.838 -13.794  1.00 58.66           C  
ATOM    779  N   CYS A  99      62.563  22.051 -17.984  1.00 59.41           N  
ATOM    780  CA  CYS A  99      62.322  23.029 -19.026  1.00 59.41           C  
ATOM    781  C   CYS A  99      60.900  22.975 -19.536  1.00 59.41           C  
ATOM    782  O   CYS A  99      60.189  21.990 -19.348  1.00 59.41           O  
ATOM    783  CB  CYS A  99      63.262  22.798 -20.201  1.00 98.59           C  
ATOM    784  SG  CYS A  99      64.948  23.402 -19.906  1.00 98.59           S  
ATOM    785  N   PRO A 100      60.450  24.062 -20.161  1.00 34.24           N  
ATOM    786  CA  PRO A 100      59.097  24.087 -20.701  1.00 34.24           C  
ATOM    787  C   PRO A 100      58.942  23.207 -21.943  1.00 34.24           C  
ATOM    788  O   PRO A 100      59.828  23.131 -22.793  1.00 34.24           O  
ATOM    789  CB  PRO A 100      58.884  25.558 -21.008  1.00 58.74           C  
ATOM    790  CG  PRO A 100      59.601  26.201 -19.894  1.00 58.74           C  
ATOM    791  CD  PRO A 100      60.898  25.432 -19.872  1.00 58.74           C  
ATOM    792  N   ASP A 101      57.795  22.532 -21.989  1.00 41.22           N  
ATOM    793  CA  ASP A 101      57.356  21.655 -23.064  1.00 41.22           C  
ATOM    794  C   ASP A 101      57.862  22.293 -24.346  1.00 41.22           C  
ATOM    795  O   ASP A 101      58.352  21.618 -25.258  1.00 41.22           O  
ATOM    796  CB  ASP A 101      55.828  21.651 -23.037  1.00 98.15           C  
ATOM    797  CG  ASP A 101      55.223  20.383 -23.569  1.00 98.15           C  
ATOM    798  OD1 ASP A 101      55.771  19.292 -23.297  1.00 98.15           O  
ATOM    799  OD2 ASP A 101      54.170  20.478 -24.239  1.00 98.15           O  
ATOM    800  N   GLY A 102      57.751  23.626 -24.373  1.00 51.83           N  
ATOM    801  CA  GLY A 102      58.152  24.434 -25.514  1.00 51.83           C  
ATOM    802  C   GLY A 102      59.624  24.584 -25.829  1.00 51.83           C  
ATOM    803  O   GLY A 102      59.982  24.497 -26.982  1.00 51.83           O  
ATOM    804  N   ASP A 103      60.477  24.816 -24.839  1.00 57.30           N  
ATOM    805  CA  ASP A 103      61.899  24.978 -25.126  1.00 57.30           C  
ATOM    806  C   ASP A 103      62.605  23.636 -25.292  1.00 57.30           C  
ATOM    807  O   ASP A 103      63.751  23.594 -25.736  1.00 57.30           O  
ATOM    808  CB  ASP A 103      62.620  25.737 -24.001  1.00 85.17           C  
ATOM    809  CG  ASP A 103      61.885  26.986 -23.549  1.00 85.17           C  
ATOM    810  OD1 ASP A 103      61.408  27.763 -24.398  1.00 85.17           O  
ATOM    811  OD2 ASP A 103      61.802  27.208 -22.326  1.00 85.17           O  
ATOM    812  N   TYR A 104      61.918  22.547 -24.949  1.00 51.43           N  
ATOM    813  CA  TYR A 104      62.505  21.197 -24.967  1.00 51.43           C  
ATOM    814  C   TYR A 104      61.423  20.235 -25.404  1.00 51.43           C  
ATOM    815  O   TYR A 104      60.967  19.393 -24.631  1.00 51.43           O  
ATOM    816  CB  TYR A 104      62.952  20.839 -23.540  1.00 39.25           C  
ATOM    817  CG  TYR A 104      64.007  19.783 -23.402  1.00 39.25           C  
ATOM    818  CD1 TYR A 104      65.017  19.924 -22.460  1.00 39.25           C  
ATOM    819  CD2 TYR A 104      64.009  18.655 -24.201  1.00 39.25           C  
ATOM    820  CE1 TYR A 104      66.019  18.969 -22.319  1.00 39.25           C  
ATOM    821  CE2 TYR A 104      65.007  17.682 -24.067  1.00 39.25           C  
ATOM    822  CZ  TYR A 104      66.016  17.850 -23.125  1.00 39.25           C  
ATOM    823  OH  TYR A 104      67.043  16.929 -23.013  1.00 39.25           O  
ATOM    824  N   PRO A 105      61.002  20.343 -26.662  1.00 45.09           N  
ATOM    825  CA  PRO A 105      59.958  19.506 -27.258  1.00 45.09           C  
ATOM    826  C   PRO A 105      60.180  18.014 -27.111  1.00 45.09           C  
ATOM    827  O   PRO A 105      61.305  17.547 -27.039  1.00 45.09           O  
ATOM    828  CB  PRO A 105      59.973  19.939 -28.707  1.00 56.59           C  
ATOM    829  CG  PRO A 105      61.426  20.226 -28.917  1.00 56.59           C  
ATOM    830  CD  PRO A 105      61.745  21.059 -27.706  1.00 56.59           C  
ATOM    831  N   TYR A 106      59.081  17.278 -27.078  1.00 62.55           N  
ATOM    832  CA  TYR A 106      59.108  15.832 -26.950  1.00 62.55           C  
ATOM    833  C   TYR A 106      59.430  15.236 -28.302  1.00 62.55           C  
ATOM    834  O   TYR A 106      58.948  15.726 -29.319  1.00 62.55           O  
ATOM    835  CB  TYR A 106      57.737  15.344 -26.504  1.00 41.47           C  
ATOM    836  CG  TYR A 106      57.626  13.853 -26.330  1.00 41.47           C  
ATOM    837  CD1 TYR A 106      58.520  13.156 -25.513  1.00 41.47           C  
ATOM    838  CD2 TYR A 106      56.574  13.142 -26.923  1.00 41.47           C  
ATOM    839  CE1 TYR A 106      58.356  11.788 -25.288  1.00 41.47           C  
ATOM    840  CE2 TYR A 106      56.406  11.780 -26.706  1.00 41.47           C  
ATOM    841  CZ  TYR A 106      57.292  11.113 -25.890  1.00 41.47           C  
ATOM    842  OH  TYR A 106      57.111   9.775 -25.656  1.00 41.47           O  
ATOM    843  N   VAL A 107      60.227  14.174 -28.314  1.00 33.04           N  
ATOM    844  CA  VAL A 107      60.598  13.519 -29.564  1.00 33.04           C  
ATOM    845  C   VAL A 107      60.507  11.993 -29.427  1.00 33.04           C  
ATOM    846  O   VAL A 107      61.184  11.266 -30.161  1.00 33.04           O  
ATOM    847  CB  VAL A 107      62.055  13.874 -29.962  1.00 29.26           C  
ATOM    848  CG1 VAL A 107      62.358  15.317 -29.655  1.00 29.26           C  
ATOM    849  CG2 VAL A 107      63.028  13.003 -29.207  1.00 29.26           C  
ATOM    850  N   SER A 108      59.683  11.524 -28.484  1.00 51.31           N  
ATOM    851  CA  SER A 108      59.489  10.093 -28.174  1.00 51.31           C  
ATOM    852  C   SER A 108      60.759   9.228 -28.165  1.00 51.31           C  
ATOM    853  O   SER A 108      61.730   9.568 -27.474  1.00 51.31           O  
ATOM    854  CB  SER A 108      58.440   9.459 -29.096  1.00 58.55           C  
ATOM    855  OG  SER A 108      58.964   9.165 -30.372  1.00 58.55           O  
ATOM    856  N   ASP A 109      60.754   8.133 -28.933  1.00 54.68           N  
ATOM    857  CA  ASP A 109      61.887   7.187 -28.989  1.00 54.68           C  
ATOM    858  C   ASP A 109      63.154   7.577 -29.776  1.00 54.68           C  
ATOM    859  O   ASP A 109      64.149   6.837 -29.768  1.00 54.68           O  
ATOM    860  CB  ASP A 109      61.409   5.821 -29.493  1.00 69.12           C  
ATOM    861  CG  ASP A 109      60.848   5.893 -30.884  1.00 69.12           C  
ATOM    862  OD1 ASP A 109      60.435   4.842 -31.421  1.00 69.12           O  
ATOM    863  OD2 ASP A 109      60.821   7.011 -31.440  1.00 69.12           O  
ATOM    864  N   ALA A 110      63.131   8.728 -30.437  1.00 46.68           N  
ATOM    865  CA  ALA A 110      64.285   9.184 -31.200  1.00 46.68           C  
ATOM    866  C   ALA A 110      65.446   9.530 -30.275  1.00 46.68           C  
ATOM    867  O   ALA A 110      65.325  10.462 -29.476  1.00 46.68           O  
ATOM    868  CB  ALA A 110      63.904  10.401 -31.996  1.00 56.15           C  
ATOM    869  N   PRO A 111      66.596   8.815 -30.386  1.00 41.15           N  
ATOM    870  CA  PRO A 111      67.748   9.113 -29.517  1.00 41.15           C  
ATOM    871  C   PRO A 111      67.881  10.613 -29.289  1.00 41.15           C  
ATOM    872  O   PRO A 111      67.544  11.425 -30.148  1.00 41.15           O  
ATOM    873  CB  PRO A 111      68.934   8.504 -30.269  1.00 66.38           C  
ATOM    874  CG  PRO A 111      68.487   8.496 -31.669  1.00 66.38           C  
ATOM    875  CD  PRO A 111      67.045   8.045 -31.552  1.00 66.38           C  
ATOM    876  N   ASN A 112      68.379  10.991 -28.129  1.00 36.02           N  
ATOM    877  CA  ASN A 112      68.424  12.405 -27.839  1.00 36.02           C  
ATOM    878  C   ASN A 112      69.173  12.648 -26.532  1.00 36.02           C  
ATOM    879  O   ASN A 112      68.752  12.171 -25.492  1.00 36.02           O  
ATOM    880  CB  ASN A 112      66.965  12.890 -27.741  1.00 53.34           C  
ATOM    881  CG  ASN A 112      66.835  14.386 -27.787  1.00 53.34           C  
ATOM    882  OD1 ASN A 112      66.888  15.068 -26.762  1.00 53.34           O  
ATOM    883  ND2 ASN A 112      66.666  14.913 -28.991  1.00 53.34           N  
ATOM    884  N   LEU A 113      70.276  13.385 -26.573  1.00 42.08           N  
ATOM    885  CA  LEU A 113      71.014  13.643 -25.345  1.00 42.08           C  
ATOM    886  C   LEU A 113      70.258  14.525 -24.337  1.00 42.08           C  
ATOM    887  O   LEU A 113      69.287  15.188 -24.671  1.00 42.08           O  
ATOM    888  CB  LEU A 113      72.370  14.267 -25.663  1.00 37.97           C  
ATOM    889  CG  LEU A 113      73.240  13.498 -26.663  1.00 37.97           C  
ATOM    890  CD1 LEU A 113      74.702  13.958 -26.523  1.00 37.97           C  
ATOM    891  CD2 LEU A 113      73.127  12.009 -26.415  1.00 37.97           C  
ATOM    892  N   CYS A 114      70.686  14.511 -23.085  1.00 50.68           N  
ATOM    893  CA  CYS A 114      70.019  15.326 -22.090  1.00 50.68           C  
ATOM    894  C   CYS A 114      70.722  16.676 -22.002  1.00 50.68           C  
ATOM    895  O   CYS A 114      71.919  16.751 -21.708  1.00 50.68           O  
ATOM    896  CB  CYS A 114      70.049  14.638 -20.722  1.00 40.38           C  
ATOM    897  SG  CYS A 114      69.949  15.835 -19.347  1.00 40.38           S  
ATOM    898  N   ASN A 115      69.986  17.748 -22.261  1.00 39.25           N  
ATOM    899  CA  ASN A 115      70.585  19.070 -22.170  1.00 39.25           C  
ATOM    900  C   ASN A 115      69.791  19.947 -21.232  1.00 39.25           C  
ATOM    901  O   ASN A 115      68.807  20.546 -21.649  1.00 39.25           O  
ATOM    902  CB  ASN A 115      70.615  19.737 -23.525  1.00 62.98           C  
ATOM    903  CG  ASN A 115      71.466  20.964 -23.525  1.00 62.98           C  
ATOM    904  OD1 ASN A 115      71.435  21.759 -22.588  1.00 62.98           O  
ATOM    905  ND2 ASN A 115      72.239  21.132 -24.575  1.00 62.98           N  
ATOM    906  N   ILE A 116      70.211  20.053 -19.977  1.00 51.55           N  
ATOM    907  CA  ILE A 116      69.446  20.860 -19.038  1.00 51.55           C  
ATOM    908  C   ILE A 116      69.439  22.332 -19.385  1.00 51.55           C  
ATOM    909  O   ILE A 116      68.611  23.077 -18.866  1.00 51.55           O  
ATOM    910  CB  ILE A 116      69.968  20.730 -17.609  1.00 62.83           C  
ATOM    911  CG1 ILE A 116      71.374  21.301 -17.535  1.00 62.83           C  
ATOM    912  CG2 ILE A 116      69.955  19.282 -17.179  1.00 62.83           C  
ATOM    913  CD1 ILE A 116      71.948  21.306 -16.155  1.00 62.83           C  
ATOM    914  N   ASP A 117      70.354  22.748 -20.262  1.00 57.35           N  
ATOM    915  CA  ASP A 117      70.472  24.154 -20.664  1.00 57.35           C  
ATOM    916  C   ASP A 117      69.540  24.637 -21.759  1.00 57.35           C  
ATOM    917  O   ASP A 117      69.551  25.818 -22.087  1.00 57.35           O  
ATOM    918  CB  ASP A 117      71.896  24.469 -21.112  1.00 76.91           C  
ATOM    919  CG  ASP A 117      72.837  24.669 -19.961  1.00 76.91           C  
ATOM    920  OD1 ASP A 117      72.360  24.951 -18.837  1.00 76.91           O  
ATOM    921  OD2 ASP A 117      74.060  24.563 -20.195  1.00 76.91           O  
ATOM    922  N   ARG A 118      68.749  23.743 -22.338  1.00 44.55           N  
ATOM    923  CA  ARG A 118      67.838  24.135 -23.402  1.00 44.55           C  
ATOM    924  C   ARG A 118      66.834  25.223 -23.021  1.00 44.55           C  
ATOM    925  O   ARG A 118      65.964  25.538 -23.830  1.00 44.55           O  
ATOM    926  CB  ARG A 118      67.058  22.934 -23.922  1.00 64.75           C  
ATOM    927  CG  ARG A 118      67.760  22.070 -24.914  1.00 64.75           C  
ATOM    928  CD  ARG A 118      66.720  21.553 -25.867  1.00 64.75           C  
ATOM    929  NE  ARG A 118      67.135  20.338 -26.559  1.00 64.75           N  
ATOM    930  CZ  ARG A 118      66.342  19.618 -27.362  1.00 64.75           C  
ATOM    931  NH1 ARG A 118      65.082  19.996 -27.581  1.00 64.75           N  
ATOM    932  NH2 ARG A 118      66.797  18.504 -27.939  1.00 64.75           N  
ATOM    933  N   CYS A 119      66.928  25.772 -21.807  1.00 69.88           N  
ATOM    934  CA  CYS A 119      66.013  26.833 -21.359  1.00 69.88           C  
ATOM    935  C   CYS A 119      66.571  27.633 -20.183  1.00 69.88           C  
ATOM    936  O   CYS A 119      67.648  27.327 -19.659  1.00 69.88           O  
ATOM    937  CB  CYS A 119      64.664  26.260 -20.946  1.00 86.01           C  
ATOM    938  SG  CYS A 119      64.688  25.358 -19.362  1.00 86.01           S  
ATOM    939  N   THR A 120      65.829  28.647 -19.753  1.00102.52           N  
ATOM    940  CA  THR A 120      66.281  29.482 -18.650  1.00102.52           C  
ATOM    941  C   THR A 120      65.266  29.587 -17.527  1.00102.52           C  
ATOM    942  O   THR A 120      65.596  30.029 -16.428  1.00102.52           O  
ATOM    943  CB  THR A 120      66.613  30.879 -19.146  1.00 71.69           C  
ATOM    944  OG1 THR A 120      66.181  31.004 -20.507  1.00 71.69           O  
ATOM    945  CG2 THR A 120      68.115  31.131 -19.059  1.00 71.69           C  
ATOM    946  N   GLU A 121      64.028  29.195 -17.811  1.00105.72           N  
ATOM    947  CA  GLU A 121      62.970  29.215 -16.806  1.00105.72           C  
ATOM    948  C   GLU A 121      62.619  27.767 -16.475  1.00105.72           C  
ATOM    949  O   GLU A 121      61.835  27.131 -17.173  1.00105.72           O  
ATOM    950  CB  GLU A 121      61.732  29.956 -17.335  1.00131.92           C  
ATOM    951  CG  GLU A 121      61.596  31.415 -16.866  1.00131.92           C  
ATOM    952  CD  GLU A 121      61.091  31.545 -15.431  1.00131.92           C  
ATOM    953  OE1 GLU A 121      59.906  31.233 -15.174  1.00131.92           O  
ATOM    954  OE2 GLU A 121      61.881  31.961 -14.558  1.00131.92           O  
ATOM    955  N   LYS A 122      63.216  27.242 -15.415  1.00 81.97           N  
ATOM    956  CA  LYS A 122      62.962  25.869 -15.014  1.00 81.97           C  
ATOM    957  C   LYS A 122      61.850  25.861 -13.993  1.00 81.97           C  
ATOM    958  O   LYS A 122      61.916  26.610 -13.027  1.00 81.97           O  
ATOM    959  CB  LYS A 122      64.221  25.269 -14.397  1.00101.64           C  
ATOM    960  CG  LYS A 122      65.392  25.250 -15.337  1.00101.64           C  
ATOM    961  CD  LYS A 122      66.635  24.725 -14.660  1.00101.64           C  
ATOM    962  CE  LYS A 122      67.700  24.395 -15.698  1.00101.64           C  
ATOM    963  NZ  LYS A 122      67.993  25.551 -16.594  1.00101.64           N  
ATOM    964  N   TYR A 123      60.827  25.035 -14.202  1.00 67.05           N  
ATOM    965  CA  TYR A 123      59.711  24.934 -13.254  1.00 67.05           C  
ATOM    966  C   TYR A 123      59.969  23.700 -12.435  1.00 67.05           C  
ATOM    967  O   TYR A 123      60.169  22.635 -12.997  1.00 67.05           O  
ATOM    968  CB  TYR A 123      58.386  24.821 -14.001  1.00 64.06           C  
ATOM    969  CG  TYR A 123      58.125  26.061 -14.811  1.00 64.06           C  
ATOM    970  CD1 TYR A 123      57.098  26.938 -14.472  1.00 64.06           C  
ATOM    971  CD2 TYR A 123      58.977  26.418 -15.852  1.00 64.06           C  
ATOM    972  CE1 TYR A 123      56.934  28.145 -15.141  1.00 64.06           C  
ATOM    973  CE2 TYR A 123      58.823  27.611 -16.523  1.00 64.06           C  
ATOM    974  CZ  TYR A 123      57.803  28.478 -16.165  1.00 64.06           C  
ATOM    975  OH  TYR A 123      57.677  29.689 -16.816  1.00 64.06           O  
ATOM    976  N   GLY A 124      59.989  23.837 -11.115  1.00 40.77           N  
ATOM    977  CA  GLY A 124      60.285  22.682 -10.284  1.00 40.77           C  
ATOM    978  C   GLY A 124      59.249  22.354  -9.233  1.00 40.77           C  
ATOM    979  O   GLY A 124      58.118  22.819  -9.306  1.00 40.77           O  
ATOM    980  N   ILE A 125      59.625  21.544  -8.254  1.00 95.11           N  
ATOM    981  CA  ILE A 125      58.696  21.186  -7.202  1.00 95.11           C  
ATOM    982  C   ILE A 125      59.458  21.213  -5.896  1.00 95.11           C  
ATOM    983  O   ILE A 125      60.611  20.777  -5.844  1.00 95.11           O  
ATOM    984  CB  ILE A 125      58.149  19.787  -7.416  1.00 48.69           C  
ATOM    985  CG1 ILE A 125      59.255  18.763  -7.179  1.00 48.69           C  
ATOM    986  CG2 ILE A 125      57.666  19.644  -8.833  1.00 48.69           C  
ATOM    987  CD1 ILE A 125      58.797  17.300  -7.260  1.00 48.69           C  
ATOM    988  N   LYS A 126      58.833  21.736  -4.844  1.00 80.92           N  
ATOM    989  CA  LYS A 126      59.494  21.790  -3.550  1.00 80.92           C  
ATOM    990  C   LYS A 126      59.668  20.365  -3.026  1.00 80.92           C  
ATOM    991  O   LYS A 126      60.724  20.004  -2.504  1.00 80.92           O  
ATOM    992  CB  LYS A 126      58.679  22.622  -2.557  1.00141.86           C  
ATOM    993  CG  LYS A 126      59.397  22.825  -1.231  1.00141.86           C  
ATOM    994  CD  LYS A 126      58.669  23.783  -0.311  1.00141.86           C  
ATOM    995  CE  LYS A 126      59.485  24.026   0.949  1.00141.86           C  
ATOM    996  NZ  LYS A 126      58.871  25.058   1.827  1.00141.86           N  
ATOM    997  N   ASN A 127      58.628  19.556  -3.179  1.00 65.76           N  
ATOM    998  CA  ASN A 127      58.668  18.173  -2.731  1.00 65.76           C  
ATOM    999  C   ASN A 127      57.450  17.413  -3.258  1.00 65.76           C  
ATOM   1000  O   ASN A 127      56.692  17.931  -4.084  1.00 65.76           O  
ATOM   1001  CB  ASN A 127      58.729  18.124  -1.204  1.00 99.39           C  
ATOM   1002  CG  ASN A 127      58.763  16.714  -0.673  1.00 99.39           C  
ATOM   1003  OD1 ASN A 127      59.534  15.880  -1.138  1.00 99.39           O  
ATOM   1004  ND2 ASN A 127      57.923  16.438   0.312  1.00 99.39           N  
ATOM   1005  N   TYR A 128      57.269  16.182  -2.800  1.00 52.12           N  
ATOM   1006  CA  TYR A 128      56.147  15.390  -3.259  1.00 52.12           C  
ATOM   1007  C   TYR A 128      55.702  14.377  -2.222  1.00 52.12           C  
ATOM   1008  O   TYR A 128      56.508  13.646  -1.641  1.00 52.12           O  
ATOM   1009  CB  TYR A 128      56.505  14.648  -4.537  1.00 48.72           C  
ATOM   1010  CG  TYR A 128      57.383  13.449  -4.306  1.00 48.72           C  
ATOM   1011  CD1 TYR A 128      58.746  13.591  -4.148  1.00 48.72           C  
ATOM   1012  CD2 TYR A 128      56.838  12.171  -4.248  1.00 48.72           C  
ATOM   1013  CE1 TYR A 128      59.554  12.490  -3.940  1.00 48.72           C  
ATOM   1014  CE2 TYR A 128      57.633  11.063  -4.042  1.00 48.72           C  
ATOM   1015  CZ  TYR A 128      58.995  11.226  -3.889  1.00 48.72           C  
ATOM   1016  OH  TYR A 128      59.809  10.126  -3.686  1.00 48.72           O  
ATOM   1017  N   LEU A 129      54.395  14.321  -2.032  1.00 74.58           N  
ATOM   1018  CA  LEU A 129      53.780  13.436  -1.069  1.00 74.58           C  
ATOM   1019  C   LEU A 129      53.287  12.154  -1.713  1.00 74.58           C  
ATOM   1020  O   LEU A 129      53.114  12.088  -2.933  1.00 74.58           O  
ATOM   1021  CB  LEU A 129      52.612  14.188  -0.430  1.00 72.66           C  
ATOM   1022  CG  LEU A 129      51.409  13.468   0.179  1.00 72.66           C  
ATOM   1023  CD1 LEU A 129      50.532  14.499   0.875  1.00 72.66           C  
ATOM   1024  CD2 LEU A 129      50.606  12.747  -0.891  1.00 72.66           C  
ATOM   1025  N   SER A 130      53.082  11.124  -0.898  1.00 62.52           N  
ATOM   1026  CA  SER A 130      52.525   9.891  -1.423  1.00 62.52           C  
ATOM   1027  C   SER A 130      51.151   9.786  -0.793  1.00 62.52           C  
ATOM   1028  O   SER A 130      51.017   9.891   0.413  1.00 62.52           O  
ATOM   1029  CB  SER A 130      53.343   8.669  -1.038  1.00 48.13           C  
ATOM   1030  OG  SER A 130      52.754   7.504  -1.623  1.00 48.13           O  
ATOM   1031  N   VAL A 131      50.122   9.598  -1.603  1.00 50.76           N  
ATOM   1032  CA  VAL A 131      48.773   9.501  -1.074  1.00 50.76           C  
ATOM   1033  C   VAL A 131      48.392   8.031  -0.826  1.00 50.76           C  
ATOM   1034  O   VAL A 131      48.693   7.151  -1.640  1.00 50.76           O  
ATOM   1035  CB  VAL A 131      47.772  10.204  -2.036  1.00 56.46           C  
ATOM   1036  CG1 VAL A 131      47.954   9.682  -3.432  1.00 56.46           C  
ATOM   1037  CG2 VAL A 131      46.356   9.988  -1.581  1.00 56.46           C  
ATOM   1038  N   PRO A 132      47.736   7.759   0.325  1.00 37.62           N  
ATOM   1039  CA  PRO A 132      47.254   6.463   0.831  1.00 37.62           C  
ATOM   1040  C   PRO A 132      46.417   5.710  -0.184  1.00 37.62           C  
ATOM   1041  O   PRO A 132      45.574   6.303  -0.824  1.00 37.62           O  
ATOM   1042  CB  PRO A 132      46.428   6.861   2.038  1.00 60.68           C  
ATOM   1043  CG  PRO A 132      47.102   8.118   2.510  1.00 60.68           C  
ATOM   1044  CD  PRO A 132      47.338   8.847   1.240  1.00 60.68           C  
ATOM   1045  N   ASP A 133      46.627   4.403  -0.318  1.00 53.68           N  
ATOM   1046  CA  ASP A 133      45.868   3.600  -1.292  1.00 53.68           C  
ATOM   1047  C   ASP A 133      44.358   3.829  -1.212  1.00 53.68           C  
ATOM   1048  O   ASP A 133      43.609   3.400  -2.080  1.00 53.68           O  
ATOM   1049  CB  ASP A 133      46.161   2.104  -1.115  1.00150.70           C  
ATOM   1050  CG  ASP A 133      45.644   1.556   0.200  1.00150.70           C  
ATOM   1051  OD1 ASP A 133      46.278   1.822   1.243  1.00150.70           O  
ATOM   1052  OD2 ASP A 133      44.599   0.864   0.192  1.00150.70           O  
ATOM   1053  N   ASN A 134      43.920   4.483  -0.150  1.00 84.23           N  
ATOM   1054  CA  ASN A 134      42.517   4.799   0.051  1.00 84.23           C  
ATOM   1055  C   ASN A 134      42.594   6.276   0.351  1.00 84.23           C  
ATOM   1056  O   ASN A 134      43.682   6.844   0.350  1.00 84.23           O  
ATOM   1057  CB  ASN A 134      41.969   4.060   1.268  1.00119.49           C  
ATOM   1058  CG  ASN A 134      42.612   4.519   2.559  1.00119.49           C  
ATOM   1059  OD1 ASN A 134      42.535   5.702   2.925  1.00119.49           O  
ATOM   1060  ND2 ASN A 134      43.255   3.588   3.261  1.00119.49           N  
ATOM   1061  N   LYS A 135      41.475   6.914   0.639  1.00 83.27           N  
ATOM   1062  CA  LYS A 135      41.558   8.335   0.908  1.00 83.27           C  
ATOM   1063  C   LYS A 135      42.046   9.031  -0.393  1.00 83.27           C  
ATOM   1064  O   LYS A 135      42.627  10.121  -0.372  1.00 83.27           O  
ATOM   1065  CB  LYS A 135      42.535   8.548   2.068  1.00119.22           C  
ATOM   1066  CG  LYS A 135      42.508   9.920   2.678  1.00119.22           C  
ATOM   1067  CD  LYS A 135      42.930   9.863   4.135  1.00119.22           C  
ATOM   1068  CE  LYS A 135      41.908   9.118   4.981  1.00119.22           C  
ATOM   1069  NZ  LYS A 135      40.592   9.812   4.983  1.00119.22           N  
ATOM   1070  N   LEU A 136      41.793   8.367  -1.524  1.00 67.59           N  
ATOM   1071  CA  LEU A 136      42.163   8.859  -2.849  1.00 67.59           C  
ATOM   1072  C   LEU A 136      41.347  10.100  -3.153  1.00 67.59           C  
ATOM   1073  O   LEU A 136      41.887  11.204  -3.192  1.00 67.59           O  
ATOM   1074  CB  LEU A 136      41.879   7.778  -3.891  1.00 30.64           C  
ATOM   1075  CG  LEU A 136      42.997   7.454  -4.887  1.00 30.64           C  
ATOM   1076  CD1 LEU A 136      44.374   7.751  -4.312  1.00 30.64           C  
ATOM   1077  CD2 LEU A 136      42.889   5.998  -5.270  1.00 30.64           C  
ATOM   1078  N   LYS A 137      40.044   9.909  -3.362  1.00 49.93           N  
ATOM   1079  CA  LYS A 137      39.139  11.031  -3.623  1.00 49.93           C  
ATOM   1080  C   LYS A 137      39.449  12.189  -2.692  1.00 49.93           C  
ATOM   1081  O   LYS A 137      39.442  13.337  -3.105  1.00 49.93           O  
ATOM   1082  CB  LYS A 137      37.673  10.643  -3.412  1.00 32.45           C  
ATOM   1083  CG  LYS A 137      37.165   9.614  -4.369  1.00 32.45           C  
ATOM   1084  CD  LYS A 137      35.670   9.600  -4.361  1.00 32.45           C  
ATOM   1085  CE  LYS A 137      35.149   8.573  -5.353  1.00 32.45           C  
ATOM   1086  NZ  LYS A 137      33.641   8.466  -5.375  1.00 32.45           N  
ATOM   1087  N   GLU A 138      39.714  11.887  -1.428  1.00 48.27           N  
ATOM   1088  CA  GLU A 138      40.023  12.945  -0.494  1.00 48.27           C  
ATOM   1089  C   GLU A 138      41.221  13.773  -0.971  1.00 48.27           C  
ATOM   1090  O   GLU A 138      41.162  15.015  -0.991  1.00 48.27           O  
ATOM   1091  CB  GLU A 138      40.324  12.372   0.894  1.00112.73           C  
ATOM   1092  CG  GLU A 138      40.444  13.452   1.985  1.00112.73           C  
ATOM   1093  CD  GLU A 138      41.082  12.943   3.268  1.00112.73           C  
ATOM   1094  OE1 GLU A 138      42.306  12.698   3.257  1.00112.73           O  
ATOM   1095  OE2 GLU A 138      40.366  12.784   4.282  1.00112.73           O  
ATOM   1096  N   ALA A 139      42.306  13.089  -1.344  1.00 57.00           N  
ATOM   1097  CA  ALA A 139      43.525  13.769  -1.792  1.00 57.00           C  
ATOM   1098  C   ALA A 139      43.216  14.560  -3.053  1.00 57.00           C  
ATOM   1099  O   ALA A 139      43.529  15.758  -3.192  1.00 57.00           O  
ATOM   1100  CB  ALA A 139      44.610  12.748  -2.075  1.00105.19           C  
ATOM   1101  N   LEU A 140      42.583  13.841  -3.967  1.00 52.60           N  
ATOM   1102  CA  LEU A 140      42.165  14.362  -5.243  1.00 52.60           C  
ATOM   1103  C   LEU A 140      41.384  15.665  -5.071  1.00 52.60           C  
ATOM   1104  O   LEU A 140      41.607  16.628  -5.783  1.00 52.60           O  
ATOM   1105  CB  LEU A 140      41.312  13.293  -5.916  1.00 49.62           C  
ATOM   1106  CG  LEU A 140      40.972  13.482  -7.379  1.00 49.62           C  
ATOM   1107  CD1 LEU A 140      42.106  14.218  -8.086  1.00 49.62           C  
ATOM   1108  CD2 LEU A 140      40.732  12.110  -8.006  1.00 49.62           C  
ATOM   1109  N   ARG A 141      40.497  15.686  -4.085  1.00 55.93           N  
ATOM   1110  CA  ARG A 141      39.634  16.828  -3.794  1.00 55.93           C  
ATOM   1111  C   ARG A 141      40.315  18.092  -3.263  1.00 55.93           C  
ATOM   1112  O   ARG A 141      39.894  19.219  -3.568  1.00 55.93           O  
ATOM   1113  CB  ARG A 141      38.564  16.393  -2.792  1.00 71.47           C  
ATOM   1114  CG  ARG A 141      37.219  17.052  -2.973  1.00 71.47           C  
ATOM   1115  CD  ARG A 141      37.330  18.545  -2.932  1.00 71.47           C  
ATOM   1116  NE  ARG A 141      36.082  19.175  -3.325  1.00 71.47           N  
ATOM   1117  CZ  ARG A 141      35.998  20.422  -3.769  1.00 71.47           C  
ATOM   1118  NH1 ARG A 141      37.101  21.163  -3.873  1.00 71.47           N  
ATOM   1119  NH2 ARG A 141      34.817  20.925  -4.114  1.00 71.47           N  
ATOM   1120  N   PHE A 142      41.360  17.921  -2.464  1.00 72.72           N  
ATOM   1121  CA  PHE A 142      42.012  19.086  -1.900  1.00 72.72           C  
ATOM   1122  C   PHE A 142      43.436  19.327  -2.362  1.00 72.72           C  
ATOM   1123  O   PHE A 142      43.874  20.480  -2.433  1.00 72.72           O  
ATOM   1124  CB  PHE A 142      41.950  19.012  -0.374  1.00 72.22           C  
ATOM   1125  CG  PHE A 142      40.542  18.934   0.171  1.00 72.22           C  
ATOM   1126  CD1 PHE A 142      39.998  17.706   0.576  1.00 72.22           C  
ATOM   1127  CD2 PHE A 142      39.742  20.080   0.239  1.00 72.22           C  
ATOM   1128  CE1 PHE A 142      38.676  17.618   1.037  1.00 72.22           C  
ATOM   1129  CE2 PHE A 142      38.424  20.005   0.696  1.00 72.22           C  
ATOM   1130  CZ  PHE A 142      37.890  18.769   1.097  1.00 72.22           C  
ATOM   1131  N   LEU A 143      44.152  18.252  -2.686  1.00 52.83           N  
ATOM   1132  CA  LEU A 143      45.536  18.380  -3.145  1.00 52.83           C  
ATOM   1133  C   LEU A 143      45.665  18.592  -4.652  1.00 52.83           C  
ATOM   1134  O   LEU A 143      46.594  19.255  -5.102  1.00 52.83           O  
ATOM   1135  CB  LEU A 143      46.359  17.144  -2.771  1.00 74.27           C  
ATOM   1136  CG  LEU A 143      46.649  16.808  -1.312  1.00 74.27           C  
ATOM   1137  CD1 LEU A 143      47.153  18.055  -0.594  1.00 74.27           C  
ATOM   1138  CD2 LEU A 143      45.389  16.264  -0.672  1.00 74.27           C  
ATOM   1139  N   GLY A 144      44.755  18.015  -5.434  1.00 62.74           N  
ATOM   1140  CA  GLY A 144      44.833  18.179  -6.878  1.00 62.74           C  
ATOM   1141  C   GLY A 144      45.015  16.856  -7.600  1.00 62.74           C  
ATOM   1142  O   GLY A 144      45.021  15.820  -6.959  1.00 62.74           O  
ATOM   1143  N   PRO A 145      45.179  16.851  -8.929  1.00 50.60           N  
ATOM   1144  CA  PRO A 145      45.351  15.591  -9.656  1.00 50.60           C  
ATOM   1145  C   PRO A 145      46.495  14.762  -9.082  1.00 50.60           C  
ATOM   1146  O   PRO A 145      47.454  15.312  -8.536  1.00 50.60           O  
ATOM   1147  CB  PRO A 145      45.637  16.052 -11.082  1.00 55.83           C  
ATOM   1148  CG  PRO A 145      44.977  17.391 -11.158  1.00 55.83           C  
ATOM   1149  CD  PRO A 145      45.329  18.000  -9.834  1.00 55.83           C  
ATOM   1150  N   ILE A 146      46.401  13.442  -9.230  1.00 43.90           N  
ATOM   1151  CA  ILE A 146      47.416  12.529  -8.703  1.00 43.90           C  
ATOM   1152  C   ILE A 146      48.025  11.611  -9.753  1.00 43.90           C  
ATOM   1153  O   ILE A 146      47.300  10.992 -10.537  1.00 43.90           O  
ATOM   1154  CB  ILE A 146      46.824  11.585  -7.646  1.00 39.13           C  
ATOM   1155  CG1 ILE A 146      45.934  12.354  -6.681  1.00 39.13           C  
ATOM   1156  CG2 ILE A 146      47.946  10.897  -6.894  1.00 39.13           C  
ATOM   1157  CD1 ILE A 146      44.837  11.509  -6.073  1.00 39.13           C  
ATOM   1158  N   SER A 147      49.353  11.513  -9.751  1.00 34.99           N  
ATOM   1159  CA  SER A 147      50.052  10.609 -10.654  1.00 34.99           C  
ATOM   1160  C   SER A 147      49.829   9.227 -10.054  1.00 34.99           C  
ATOM   1161  O   SER A 147      50.134   9.009  -8.885  1.00 34.99           O  
ATOM   1162  CB  SER A 147      51.543  10.903 -10.652  1.00 38.18           C  
ATOM   1163  OG  SER A 147      51.857  11.887 -11.601  1.00 38.18           O  
ATOM   1164  N   ILE A 148      49.303   8.289 -10.823  1.00 38.41           N  
ATOM   1165  CA  ILE A 148      49.072   6.967 -10.271  1.00 38.41           C  
ATOM   1166  C   ILE A 148      49.478   5.865 -11.225  1.00 38.41           C  
ATOM   1167  O   ILE A 148      49.868   6.130 -12.347  1.00 38.41           O  
ATOM   1168  CB  ILE A 148      47.616   6.789  -9.945  1.00 31.52           C  
ATOM   1169  CG1 ILE A 148      46.814   6.846 -11.242  1.00 31.52           C  
ATOM   1170  CG2 ILE A 148      47.173   7.868  -8.951  1.00 31.52           C  
ATOM   1171  CD1 ILE A 148      45.356   6.481 -11.069  1.00 31.52           C  
ATOM   1172  N   SER A 149      49.371   4.622 -10.787  1.00 39.80           N  
ATOM   1173  CA  SER A 149      49.739   3.490 -11.630  1.00 39.80           C  
ATOM   1174  C   SER A 149      48.542   2.594 -11.846  1.00 39.80           C  
ATOM   1175  O   SER A 149      47.603   2.656 -11.070  1.00 39.80           O  
ATOM   1176  CB  SER A 149      50.835   2.703 -10.937  1.00 45.13           C  
ATOM   1177  OG  SER A 149      50.597   2.645  -9.539  1.00 45.13           O  
ATOM   1178  N   VAL A 150      48.548   1.772 -12.882  1.00 67.51           N  
ATOM   1179  CA  VAL A 150      47.424   0.864 -13.087  1.00 67.51           C  
ATOM   1180  C   VAL A 150      47.765  -0.270 -14.005  1.00 67.51           C  
ATOM   1181  O   VAL A 150      48.655  -0.142 -14.844  1.00 67.51           O  
ATOM   1182  CB  VAL A 150      46.196   1.534 -13.707  1.00 35.64           C  
ATOM   1183  CG1 VAL A 150      45.511   2.384 -12.686  1.00 35.64           C  
ATOM   1184  CG2 VAL A 150      46.585   2.342 -14.912  1.00 35.64           C  
ATOM   1185  N   ALA A 151      47.052  -1.381 -13.860  1.00 61.78           N  
ATOM   1186  CA  ALA A 151      47.284  -2.529 -14.726  1.00 61.78           C  
ATOM   1187  C   ALA A 151      46.413  -2.359 -15.969  1.00 61.78           C  
ATOM   1188  O   ALA A 151      45.209  -2.513 -15.898  1.00 61.78           O  
ATOM   1189  CB  ALA A 151      46.925  -3.817 -14.000  1.00200.00           C  
ATOM   1190  N   VAL A 152      47.010  -2.024 -17.105  1.00 60.71           N  
ATOM   1191  CA  VAL A 152      46.220  -1.848 -18.313  1.00 60.71           C  
ATOM   1192  C   VAL A 152      46.106  -3.113 -19.128  1.00 60.71           C  
ATOM   1193  O   VAL A 152      47.105  -3.669 -19.588  1.00 60.71           O  
ATOM   1194  CB  VAL A 152      46.796  -0.760 -19.226  1.00 87.39           C  
ATOM   1195  CG1 VAL A 152      46.140  -0.829 -20.588  1.00 87.39           C  
ATOM   1196  CG2 VAL A 152      46.546   0.599 -18.623  1.00 87.39           C  
ATOM   1197  N   SER A 153      44.872  -3.561 -19.308  1.00 91.86           N  
ATOM   1198  CA  SER A 153      44.604  -4.751 -20.096  1.00 91.86           C  
ATOM   1199  C   SER A 153      44.493  -4.299 -21.545  1.00 91.86           C  
ATOM   1200  O   SER A 153      44.330  -3.110 -21.829  1.00 91.86           O  
ATOM   1201  CB  SER A 153      43.289  -5.389 -19.674  1.00158.43           C  
ATOM   1202  OG  SER A 153      42.210  -4.567 -20.073  1.00158.43           O  
ATOM   1203  N   ASP A 154      44.570  -5.257 -22.458  1.00118.57           N  
ATOM   1204  CA  ASP A 154      44.505  -4.961 -23.883  1.00118.57           C  
ATOM   1205  C   ASP A 154      43.241  -4.172 -24.274  1.00118.57           C  
ATOM   1206  O   ASP A 154      43.309  -3.242 -25.078  1.00118.57           O  
ATOM   1207  CB  ASP A 154      44.599  -6.274 -24.681  1.00156.28           C  
ATOM   1208  CG  ASP A 154      45.193  -6.083 -26.072  1.00156.28           C  
ATOM   1209  OD1 ASP A 154      45.344  -7.091 -26.797  1.00156.28           O  
ATOM   1210  OD2 ASP A 154      45.511  -4.932 -26.442  1.00156.28           O  
ATOM   1211  N   ASP A 155      42.096  -4.529 -23.696  1.00125.38           N  
ATOM   1212  CA  ASP A 155      40.849  -3.842 -24.029  1.00125.38           C  
ATOM   1213  C   ASP A 155      40.790  -2.425 -23.480  1.00125.38           C  
ATOM   1214  O   ASP A 155      39.993  -1.608 -23.938  1.00125.38           O  
ATOM   1215  CB  ASP A 155      39.615  -4.662 -23.574  1.00148.90           C  
ATOM   1216  CG  ASP A 155      39.629  -5.014 -22.086  1.00148.90           C  
ATOM   1217  OD1 ASP A 155      40.649  -5.535 -21.591  1.00148.90           O  
ATOM   1218  OD2 ASP A 155      38.599  -4.792 -21.414  1.00148.90           O  
ATOM   1219  N   PHE A 156      41.646  -2.132 -22.508  1.00128.74           N  
ATOM   1220  CA  PHE A 156      41.690  -0.799 -21.925  1.00128.74           C  
ATOM   1221  C   PHE A 156      42.017   0.169 -23.059  1.00128.74           C  
ATOM   1222  O   PHE A 156      41.532   1.300 -23.085  1.00128.74           O  
ATOM   1223  CB  PHE A 156      42.768  -0.741 -20.838  1.00 83.12           C  
ATOM   1224  CG  PHE A 156      42.865   0.587 -20.125  1.00 83.12           C  
ATOM   1225  CD1 PHE A 156      42.686   0.660 -18.748  1.00 83.12           C  
ATOM   1226  CD2 PHE A 156      43.174   1.759 -20.818  1.00 83.12           C  
ATOM   1227  CE1 PHE A 156      42.813   1.875 -18.080  1.00 83.12           C  
ATOM   1228  CE2 PHE A 156      43.302   2.975 -20.153  1.00 83.12           C  
ATOM   1229  CZ  PHE A 156      43.122   3.032 -18.786  1.00 83.12           C  
ATOM   1230  N   ALA A 157      42.834  -0.288 -24.004  1.00 60.58           N  
ATOM   1231  CA  ALA A 157      43.218   0.542 -25.141  1.00 60.58           C  
ATOM   1232  C   ALA A 157      42.043   0.801 -26.093  1.00 60.58           C  
ATOM   1233  O   ALA A 157      41.948   1.867 -26.688  1.00 60.58           O  
ATOM   1234  CB  ALA A 157      44.372  -0.119 -25.894  1.00134.39           C  
ATOM   1235  N   PHE A 158      41.144  -0.167 -26.241  1.00122.35           N  
ATOM   1236  CA  PHE A 158      40.015   0.023 -27.149  1.00122.35           C  
ATOM   1237  C   PHE A 158      39.006   1.013 -26.614  1.00122.35           C  
ATOM   1238  O   PHE A 158      38.222   1.573 -27.374  1.00122.35           O  
ATOM   1239  CB  PHE A 158      39.283  -1.288 -27.427  1.00133.76           C  
ATOM   1240  CG  PHE A 158      40.114  -2.314 -28.112  1.00133.76           C  
ATOM   1241  CD1 PHE A 158      40.847  -3.235 -27.373  1.00133.76           C  
ATOM   1242  CD2 PHE A 158      40.152  -2.375 -29.496  1.00133.76           C  
ATOM   1243  CE1 PHE A 158      41.601  -4.209 -28.002  1.00133.76           C  
ATOM   1244  CE2 PHE A 158      40.903  -3.344 -30.136  1.00133.76           C  
ATOM   1245  CZ  PHE A 158      41.627  -4.264 -29.385  1.00133.76           C  
ATOM   1246  N   TYR A 159      39.014   1.215 -25.303  1.00 80.71           N  
ATOM   1247  CA  TYR A 159      38.078   2.138 -24.679  1.00 80.71           C  
ATOM   1248  C   TYR A 159      37.851   3.381 -25.529  1.00 80.71           C  
ATOM   1249  O   TYR A 159      38.790   4.127 -25.802  1.00 80.71           O  
ATOM   1250  CB  TYR A 159      38.592   2.539 -23.293  1.00102.62           C  
ATOM   1251  CG  TYR A 159      37.872   3.725 -22.691  1.00102.62           C  
ATOM   1252  CD1 TYR A 159      38.137   5.023 -23.133  1.00102.62           C  
ATOM   1253  CD2 TYR A 159      36.901   3.550 -21.713  1.00102.62           C  
ATOM   1254  CE1 TYR A 159      37.454   6.110 -22.625  1.00102.62           C  
ATOM   1255  CE2 TYR A 159      36.208   4.635 -21.195  1.00102.62           C  
ATOM   1256  CZ  TYR A 159      36.491   5.913 -21.660  1.00102.62           C  
ATOM   1257  OH  TYR A 159      35.804   7.000 -21.177  1.00102.62           O  
ATOM   1258  N   LYS A 160      36.609   3.611 -25.945  1.00 69.43           N  
ATOM   1259  CA  LYS A 160      36.307   4.788 -26.759  1.00 69.43           C  
ATOM   1260  C   LYS A 160      35.498   5.846 -26.013  1.00 69.43           C  
ATOM   1261  O   LYS A 160      35.515   7.019 -26.384  1.00 69.43           O  
ATOM   1262  CB  LYS A 160      35.564   4.385 -28.035  1.00140.52           C  
ATOM   1263  CG  LYS A 160      36.428   3.655 -29.043  1.00140.52           C  
ATOM   1264  CD  LYS A 160      35.590   3.115 -30.181  1.00140.52           C  
ATOM   1265  CE  LYS A 160      36.412   2.206 -31.072  1.00140.52           C  
ATOM   1266  NZ  LYS A 160      35.569   1.495 -32.071  1.00140.52           N  
ATOM   1267  N   GLU A 161      34.778   5.425 -24.976  1.00126.41           N  
ATOM   1268  CA  GLU A 161      33.967   6.340 -24.169  1.00126.41           C  
ATOM   1269  C   GLU A 161      33.210   5.554 -23.113  1.00126.41           C  
ATOM   1270  O   GLU A 161      33.264   4.322 -23.082  1.00126.41           O  
ATOM   1271  CB  GLU A 161      32.948   7.093 -25.033  1.00117.32           C  
ATOM   1272  CG  GLU A 161      31.611   6.359 -25.192  1.00117.32           C  
ATOM   1273  CD  GLU A 161      30.596   7.119 -26.043  1.00117.32           C  
ATOM   1274  OE1 GLU A 161      30.389   8.328 -25.791  1.00117.32           O  
ATOM   1275  OE2 GLU A 161      29.997   6.500 -26.956  1.00117.32           O  
ATOM   1276  N   GLY A 162      32.496   6.275 -22.255  1.00 80.00           N  
ATOM   1277  CA  GLY A 162      31.721   5.625 -21.217  1.00 80.00           C  
ATOM   1278  C   GLY A 162      32.464   5.398 -19.914  1.00 80.00           C  
ATOM   1279  O   GLY A 162      33.326   6.189 -19.541  1.00 80.00           O  
ATOM   1280  N   ILE A 163      32.128   4.317 -19.213  1.00 58.56           N  
ATOM   1281  CA  ILE A 163      32.782   4.018 -17.948  1.00 58.56           C  
ATOM   1282  C   ILE A 163      33.435   2.666 -17.989  1.00 58.56           C  
ATOM   1283  O   ILE A 163      32.875   1.690 -17.525  1.00 58.56           O  
ATOM   1284  CB  ILE A 163      31.798   4.002 -16.765  1.00 58.30           C  
ATOM   1285  CG1 ILE A 163      31.086   5.356 -16.653  1.00 58.30           C  
ATOM   1286  CG2 ILE A 163      32.554   3.647 -15.470  1.00 58.30           C  
ATOM   1287  CD1 ILE A 163      30.134   5.458 -15.475  1.00 58.30           C  
ATOM   1288  N   PHE A 164      34.628   2.610 -18.544  1.00 68.35           N  
ATOM   1289  CA  PHE A 164      35.367   1.365 -18.626  1.00 68.35           C  
ATOM   1290  C   PHE A 164      35.364   0.616 -17.289  1.00 68.35           C  
ATOM   1291  O   PHE A 164      35.575   1.208 -16.229  1.00 68.35           O  
ATOM   1292  CB  PHE A 164      36.803   1.675 -19.036  1.00 81.32           C  
ATOM   1293  CG  PHE A 164      37.717   0.507 -18.958  1.00 81.32           C  
ATOM   1294  CD1 PHE A 164      37.937  -0.282 -20.068  1.00 81.32           C  
ATOM   1295  CD2 PHE A 164      38.358   0.187 -17.760  1.00 81.32           C  
ATOM   1296  CE1 PHE A 164      38.784  -1.379 -19.992  1.00 81.32           C  
ATOM   1297  CE2 PHE A 164      39.209  -0.910 -17.667  1.00 81.32           C  
ATOM   1298  CZ  PHE A 164      39.424  -1.696 -18.785  1.00 81.32           C  
ATOM   1299  N   ASP A 165      35.123  -0.686 -17.353  1.00103.33           N  
ATOM   1300  CA  ASP A 165      35.131  -1.541 -16.173  1.00103.33           C  
ATOM   1301  C   ASP A 165      35.433  -2.943 -16.670  1.00103.33           C  
ATOM   1302  O   ASP A 165      35.055  -3.931 -16.044  1.00103.33           O  
ATOM   1303  CB  ASP A 165      33.778  -1.522 -15.456  1.00140.82           C  
ATOM   1304  CG  ASP A 165      32.635  -1.990 -16.341  1.00140.82           C  
ATOM   1305  OD1 ASP A 165      32.806  -3.003 -17.052  1.00140.82           O  
ATOM   1306  OD2 ASP A 165      31.558  -1.353 -16.313  1.00140.82           O  
ATOM   1307  N   GLY A 166      36.115  -3.004 -17.812  1.00191.40           N  
ATOM   1308  CA  GLY A 166      36.469  -4.271 -18.428  1.00191.40           C  
ATOM   1309  C   GLY A 166      37.531  -5.065 -17.696  1.00191.40           C  
ATOM   1310  O   GLY A 166      37.664  -4.966 -16.477  1.00191.40           O  
ATOM   1311  N   GLU A 167      38.293  -5.856 -18.446  1.00122.40           N  
ATOM   1312  CA  GLU A 167      39.339  -6.687 -17.862  1.00122.40           C  
ATOM   1313  C   GLU A 167      40.576  -5.847 -17.542  1.00122.40           C  
ATOM   1314  O   GLU A 167      40.851  -4.872 -18.236  1.00122.40           O  
ATOM   1315  CB  GLU A 167      39.693  -7.820 -18.835  1.00180.37           C  
ATOM   1316  CG  GLU A 167      40.708  -8.829 -18.308  1.00180.37           C  
ATOM   1317  CD  GLU A 167      40.806 -10.071 -19.179  1.00180.37           C  
ATOM   1318  OE1 GLU A 167      39.794 -10.792 -19.296  1.00180.37           O  
ATOM   1319  OE2 GLU A 167      41.890 -10.326 -19.745  1.00180.37           O  
ATOM   1320  N   CYS A 168      41.303  -6.203 -16.482  1.00 88.20           N  
ATOM   1321  CA  CYS A 168      42.506  -5.465 -16.129  1.00 88.20           C  
ATOM   1322  C   CYS A 168      43.752  -6.236 -16.570  1.00 88.20           C  
ATOM   1323  O   CYS A 168      43.653  -7.365 -17.027  1.00 88.20           O  
ATOM   1324  CB  CYS A 168      42.550  -5.189 -14.624  1.00199.22           C  
ATOM   1325  SG  CYS A 168      41.270  -4.041 -13.994  1.00199.22           S  
ATOM   1326  N   GLY A 169      44.922  -5.620 -16.458  1.00 93.13           N  
ATOM   1327  CA  GLY A 169      46.146  -6.293 -16.853  1.00 93.13           C  
ATOM   1328  C   GLY A 169      46.785  -7.142 -15.756  1.00 93.13           C  
ATOM   1329  O   GLY A 169      46.279  -7.230 -14.636  1.00 93.13           O  
ATOM   1330  N   ASP A 170      47.912  -7.763 -16.088  1.00 86.10           N  
ATOM   1331  CA  ASP A 170      48.650  -8.624 -15.174  1.00 86.10           C  
ATOM   1332  C   ASP A 170      49.042  -7.940 -13.876  1.00 86.10           C  
ATOM   1333  O   ASP A 170      48.581  -8.315 -12.787  1.00 86.10           O  
ATOM   1334  CB  ASP A 170      49.909  -9.131 -15.872  1.00123.10           C  
ATOM   1335  CG  ASP A 170      49.598  -9.869 -17.160  1.00123.10           C  
ATOM   1336  OD1 ASP A 170      49.051 -10.994 -17.094  1.00123.10           O  
ATOM   1337  OD2 ASP A 170      49.893  -9.319 -18.240  1.00123.10           O  
ATOM   1338  N   GLN A 171      49.925  -6.956 -13.999  1.00 95.49           N  
ATOM   1339  CA  GLN A 171      50.399  -6.199 -12.845  1.00 95.49           C  
ATOM   1340  C   GLN A 171      50.468  -4.729 -13.230  1.00 95.49           C  
ATOM   1341  O   GLN A 171      50.182  -4.364 -14.376  1.00 95.49           O  
ATOM   1342  CB  GLN A 171      51.789  -6.686 -12.391  1.00158.99           C  
ATOM   1343  CG  GLN A 171      52.391  -7.845 -13.203  1.00158.99           C  
ATOM   1344  CD  GLN A 171      52.994  -7.417 -14.546  1.00158.99           C  
ATOM   1345  OE1 GLN A 171      53.357  -8.259 -15.374  1.00158.99           O  
ATOM   1346  NE2 GLN A 171      53.110  -6.110 -14.758  1.00158.99           N  
ATOM   1347  N   LEU A 172      50.830  -3.891 -12.265  1.00 89.07           N  
ATOM   1348  CA  LEU A 172      50.952  -2.467 -12.516  1.00 89.07           C  
ATOM   1349  C   LEU A 172      51.867  -2.266 -13.720  1.00 89.07           C  
ATOM   1350  O   LEU A 172      53.071  -2.502 -13.639  1.00 89.07           O  
ATOM   1351  CB  LEU A 172      51.538  -1.779 -11.289  1.00 63.12           C  
ATOM   1352  CG  LEU A 172      50.606  -1.815 -10.086  1.00 63.12           C  
ATOM   1353  CD1 LEU A 172      51.183  -0.968  -8.966  1.00 63.12           C  
ATOM   1354  CD2 LEU A 172      49.232  -1.300 -10.508  1.00 63.12           C  
ATOM   1355  N   ASN A 173      51.298  -1.817 -14.831  1.00 56.50           N  
ATOM   1356  CA  ASN A 173      52.074  -1.628 -16.042  1.00 56.50           C  
ATOM   1357  C   ASN A 173      51.808  -0.281 -16.728  1.00 56.50           C  
ATOM   1358  O   ASN A 173      51.869  -0.187 -17.965  1.00 56.50           O  
ATOM   1359  CB  ASN A 173      51.704  -2.732 -17.013  1.00 60.39           C  
ATOM   1360  CG  ASN A 173      50.333  -2.508 -17.634  1.00 60.39           C  
ATOM   1361  OD1 ASN A 173      49.391  -2.123 -16.953  1.00 60.39           O  
ATOM   1362  ND2 ASN A 173      50.222  -2.745 -18.929  1.00 60.39           N  
ATOM   1363  N   HIS A 174      51.509   0.762 -15.962  1.00 66.04           N  
ATOM   1364  CA  HIS A 174      51.217   2.040 -16.596  1.00 66.04           C  
ATOM   1365  C   HIS A 174      51.011   3.139 -15.582  1.00 66.04           C  
ATOM   1366  O   HIS A 174      50.597   2.879 -14.449  1.00 66.04           O  
ATOM   1367  CB  HIS A 174      49.965   1.899 -17.458  1.00 60.34           C  
ATOM   1368  CG  HIS A 174      49.721   3.056 -18.372  1.00 60.34           C  
ATOM   1369  ND1 HIS A 174      50.712   3.605 -19.159  1.00 60.34           N  
ATOM   1370  CD2 HIS A 174      48.580   3.711 -18.694  1.00 60.34           C  
ATOM   1371  CE1 HIS A 174      50.188   4.544 -19.930  1.00 60.34           C  
ATOM   1372  NE2 HIS A 174      48.895   4.628 -19.667  1.00 60.34           N  
ATOM   1373  N   ALA A 175      51.316   4.365 -15.999  1.00 45.85           N  
ATOM   1374  CA  ALA A 175      51.152   5.541 -15.151  1.00 45.85           C  
ATOM   1375  C   ALA A 175      50.229   6.490 -15.862  1.00 45.85           C  
ATOM   1376  O   ALA A 175      50.421   6.830 -17.016  1.00 45.85           O  
ATOM   1377  CB  ALA A 175      52.464   6.220 -14.896  1.00 22.94           C  
ATOM   1378  N   VAL A 176      49.210   6.918 -15.161  1.00 28.13           N  
ATOM   1379  CA  VAL A 176      48.256   7.813 -15.742  1.00 28.13           C  
ATOM   1380  C   VAL A 176      48.019   8.728 -14.601  1.00 28.13           C  
ATOM   1381  O   VAL A 176      48.637   8.542 -13.555  1.00 28.13           O  
ATOM   1382  CB  VAL A 176      46.974   7.074 -16.056  1.00 32.24           C  
ATOM   1383  CG1 VAL A 176      47.292   5.880 -16.905  1.00 32.24           C  
ATOM   1384  CG2 VAL A 176      46.318   6.615 -14.791  1.00 32.24           C  
ATOM   1385  N   MET A 177      47.153   9.721 -14.772  1.00 32.69           N  
ATOM   1386  CA  MET A 177      46.879  10.567 -13.637  1.00 32.69           C  
ATOM   1387  C   MET A 177      45.392  10.661 -13.366  1.00 32.69           C  
ATOM   1388  O   MET A 177      44.568  10.548 -14.274  1.00 32.69           O  
ATOM   1389  CB  MET A 177      47.570  11.939 -13.773  1.00 43.27           C  
ATOM   1390  CG  MET A 177      47.046  12.950 -14.761  1.00 43.27           C  
ATOM   1391  SD  MET A 177      48.188  14.426 -14.761  1.00 43.27           S  
ATOM   1392  CE  MET A 177      49.028  14.051 -16.286  1.00 43.27           C  
ATOM   1393  N   LEU A 178      45.068  10.754 -12.080  1.00 54.20           N  
ATOM   1394  CA  LEU A 178      43.696  10.888 -11.628  1.00 54.20           C  
ATOM   1395  C   LEU A 178      43.429  12.376 -11.638  1.00 54.20           C  
ATOM   1396  O   LEU A 178      44.245  13.160 -11.147  1.00 54.20           O  
ATOM   1397  CB  LEU A 178      43.547  10.387 -10.203  1.00 39.48           C  
ATOM   1398  CG  LEU A 178      43.387   8.899  -9.940  1.00 39.48           C  
ATOM   1399  CD1 LEU A 178      43.192   8.730  -8.455  1.00 39.48           C  
ATOM   1400  CD2 LEU A 178      42.198   8.331 -10.684  1.00 39.48           C  
ATOM   1401  N   VAL A 179      42.302  12.786 -12.191  1.00 38.61           N  
ATOM   1402  CA  VAL A 179      42.051  14.208 -12.209  1.00 38.61           C  
ATOM   1403  C   VAL A 179      40.743  14.527 -11.539  1.00 38.61           C  
ATOM   1404  O   VAL A 179      40.407  15.701 -11.357  1.00 38.61           O  
ATOM   1405  CB  VAL A 179      42.056  14.768 -13.638  1.00 25.27           C  
ATOM   1406  CG1 VAL A 179      43.463  14.698 -14.199  1.00 25.27           C  
ATOM   1407  CG2 VAL A 179      41.072  13.987 -14.518  1.00 25.27           C  
ATOM   1408  N   GLY A 180      40.010  13.484 -11.159  1.00 34.23           N  
ATOM   1409  CA  GLY A 180      38.746  13.714 -10.490  1.00 34.23           C  
ATOM   1410  C   GLY A 180      37.845  12.514 -10.579  1.00 34.23           C  
ATOM   1411  O   GLY A 180      38.229  11.468 -11.088  1.00 34.23           O  
ATOM   1412  N   PHE A 181      36.632  12.658 -10.083  1.00 27.77           N  
ATOM   1413  CA  PHE A 181      35.680  11.564 -10.123  1.00 27.77           C  
ATOM   1414  C   PHE A 181      34.321  12.149 -10.446  1.00 27.77           C  
ATOM   1415  O   PHE A 181      34.131  13.374 -10.420  1.00 27.77           O  
ATOM   1416  CB  PHE A 181      35.651  10.858  -8.769  1.00 46.18           C  
ATOM   1417  CG  PHE A 181      35.725  11.799  -7.602  1.00 46.18           C  
ATOM   1418  CD1 PHE A 181      34.564  12.248  -6.984  1.00 46.18           C  
ATOM   1419  CD2 PHE A 181      36.957  12.297  -7.174  1.00 46.18           C  
ATOM   1420  CE1 PHE A 181      34.622  13.184  -5.962  1.00 46.18           C  
ATOM   1421  CE2 PHE A 181      37.030  13.228  -6.156  1.00 46.18           C  
ATOM   1422  CZ  PHE A 181      35.857  13.678  -5.548  1.00 46.18           C  
ATOM   1423  N   GLY A 182      33.373  11.285 -10.762  1.00 52.58           N  
ATOM   1424  CA  GLY A 182      32.056  11.767 -11.085  1.00 52.58           C  
ATOM   1425  C   GLY A 182      31.121  10.612 -10.909  1.00 52.58           C  
ATOM   1426  O   GLY A 182      31.535   9.509 -10.532  1.00 52.58           O  
ATOM   1427  N   MET A 183      29.854  10.847 -11.197  1.00 64.44           N  
ATOM   1428  CA  MET A 183      28.879   9.797 -11.046  1.00 64.44           C  
ATOM   1429  C   MET A 183      27.705  10.054 -11.969  1.00 64.44           C  
ATOM   1430  O   MET A 183      26.966  11.020 -11.806  1.00 64.44           O  
ATOM   1431  CB  MET A 183      28.459   9.745  -9.579  1.00 74.33           C  
ATOM   1432  CG  MET A 183      27.277   8.877  -9.258  1.00 74.33           C  
ATOM   1433  SD  MET A 183      25.742   9.823  -9.228  1.00 74.33           S  
ATOM   1434  CE  MET A 183      24.818   8.832 -10.324  1.00 74.33           C  
ATOM   1435  N   LYS A 184      27.572   9.207 -12.978  1.00 73.15           N  
ATOM   1436  CA  LYS A 184      26.470   9.330 -13.911  1.00 73.15           C  
ATOM   1437  C   LYS A 184      25.392   8.436 -13.320  1.00 73.15           C  
ATOM   1438  O   LYS A 184      25.692   7.366 -12.777  1.00 73.15           O  
ATOM   1439  CB  LYS A 184      26.878   8.846 -15.320  1.00 97.78           C  
ATOM   1440  CG  LYS A 184      27.904   9.761 -16.052  1.00 97.78           C  
ATOM   1441  CD  LYS A 184      28.406   9.199 -17.417  1.00 97.78           C  
ATOM   1442  CE  LYS A 184      29.413  10.146 -18.096  1.00 97.78           C  
ATOM   1443  NZ  LYS A 184      30.043   9.568 -19.310  1.00 97.78           N  
ATOM   1444  N   GLU A 185      24.145   8.892 -13.380  1.00 97.78           N  
ATOM   1445  CA  GLU A 185      23.039   8.109 -12.852  1.00 97.78           C  
ATOM   1446  C   GLU A 185      22.314   7.473 -14.015  1.00 97.78           C  
ATOM   1447  O   GLU A 185      21.604   8.144 -14.761  1.00 97.78           O  
ATOM   1448  CB  GLU A 185      22.088   8.999 -12.056  1.00100.49           C  
ATOM   1449  CG  GLU A 185      20.944   8.249 -11.380  1.00100.49           C  
ATOM   1450  CD  GLU A 185      20.682   8.739  -9.957  1.00100.49           C  
ATOM   1451  OE1 GLU A 185      20.772   9.965  -9.714  1.00100.49           O  
ATOM   1452  OE2 GLU A 185      20.377   7.898  -9.081  1.00100.49           O  
ATOM   1453  N   ILE A 186      22.511   6.172 -14.170  1.00123.68           N  
ATOM   1454  CA  ILE A 186      21.892   5.433 -15.256  1.00123.68           C  
ATOM   1455  C   ILE A 186      20.522   4.919 -14.848  1.00123.68           C  
ATOM   1456  O   ILE A 186      20.051   5.179 -13.740  1.00123.68           O  
ATOM   1457  CB  ILE A 186      22.759   4.221 -15.662  1.00151.18           C  
ATOM   1458  CG1 ILE A 186      22.644   3.108 -14.611  1.00151.18           C  
ATOM   1459  CG2 ILE A 186      24.210   4.652 -15.812  1.00151.18           C  
ATOM   1460  CD1 ILE A 186      23.138   3.490 -13.230  1.00151.18           C  
ATOM   1461  N   VAL A 187      19.889   4.193 -15.761  1.00182.18           N  
ATOM   1462  CA  VAL A 187      18.587   3.599 -15.510  1.00182.18           C  
ATOM   1463  C   VAL A 187      18.853   2.140 -15.129  1.00182.18           C  
ATOM   1464  O   VAL A 187      19.402   1.889 -14.055  1.00182.18           O  
ATOM   1465  CB  VAL A 187      17.689   3.713 -16.756  1.00111.58           C  
ATOM   1466  CG1 VAL A 187      17.285   5.168 -16.958  1.00111.58           C  
ATOM   1467  CG2 VAL A 187      18.440   3.225 -17.988  1.00111.58           C  
ATOM   1468  N   ASN A 188      18.498   1.179 -15.980  1.00173.47           N  
ATOM   1469  CA  ASN A 188      18.757  -0.217 -15.633  1.00173.47           C  
ATOM   1470  C   ASN A 188      18.525  -1.257 -16.734  1.00173.47           C  
ATOM   1471  O   ASN A 188      17.410  -1.749 -16.911  1.00173.47           O  
ATOM   1472  CB  ASN A 188      17.931  -0.607 -14.404  1.00102.16           C  
ATOM   1473  CG  ASN A 188      18.538  -1.764 -13.642  1.00102.16           C  
ATOM   1474  OD1 ASN A 188      18.886  -2.796 -14.222  1.00102.16           O  
ATOM   1475  ND2 ASN A 188      18.669  -1.599 -12.331  1.00102.16           N  
ATOM   1476  N   PRO A 189      19.582  -1.609 -17.482  0.00199.79           N  
ATOM   1477  CA  PRO A 189      19.460  -2.601 -18.551  0.00199.79           C  
ATOM   1478  C   PRO A 189      18.969  -3.924 -17.953  0.00199.79           C  
ATOM   1479  O   PRO A 189      18.688  -4.876 -18.682  0.00199.79           O  
ATOM   1480  CB  PRO A 189      20.884  -2.693 -19.091  0.00154.01           C  
ATOM   1481  CG  PRO A 189      21.391  -1.297 -18.898  0.00154.01           C  
ATOM   1482  CD  PRO A 189      20.921  -0.998 -17.493  0.00154.01           C  
ATOM   1483  N   LEU A 190      18.868  -3.971 -16.623  0.00199.79           N  
ATOM   1484  CA  LEU A 190      18.406  -5.167 -15.925  0.00199.79           C  
ATOM   1485  C   LEU A 190      17.085  -4.977 -15.147  0.00199.79           C  
ATOM   1486  O   LEU A 190      17.058  -5.102 -13.916  0.00199.79           O  
ATOM   1487  CB  LEU A 190      19.527  -5.700 -14.995  0.00154.90           C  
ATOM   1488  CG  LEU A 190      19.324  -7.017 -14.223  0.00154.90           C  
ATOM   1489  CD1 LEU A 190      19.240  -8.200 -15.181  0.00154.90           C  
ATOM   1490  CD2 LEU A 190      20.487  -7.222 -13.256  0.00154.90           C  
ATOM   1491  N   THR A 191      16.029  -4.629 -15.890  1.00200.00           N  
ATOM   1492  CA  THR A 191      14.654  -4.472 -15.403  1.00200.00           C  
ATOM   1493  C   THR A 191      14.086  -3.374 -14.474  1.00200.00           C  
ATOM   1494  O   THR A 191      12.875  -3.184 -14.473  1.00200.00           O  
ATOM   1495  CB  THR A 191      14.145  -5.800 -14.794  1.00153.92           C  
ATOM   1496  OG1 THR A 191      15.123  -6.321 -13.891  1.00153.92           O  
ATOM   1497  CG2 THR A 191      13.824  -6.839 -15.886  1.00153.92           C  
ATOM   1498  N   LYS A 192      14.866  -2.627 -13.705  1.00141.78           N  
ATOM   1499  CA  LYS A 192      14.171  -1.667 -12.834  1.00141.78           C  
ATOM   1500  C   LYS A 192      14.024  -0.204 -13.272  1.00141.78           C  
ATOM   1501  O   LYS A 192      13.321   0.125 -14.237  1.00141.78           O  
ATOM   1502  CB  LYS A 192      14.777  -1.697 -11.430  1.00134.25           C  
ATOM   1503  CG  LYS A 192      14.503  -2.988 -10.653  1.00134.25           C  
ATOM   1504  CD  LYS A 192      13.205  -2.933  -9.831  1.00134.25           C  
ATOM   1505  CE  LYS A 192      11.953  -3.106 -10.674  1.00134.25           C  
ATOM   1506  NZ  LYS A 192      11.777  -4.525 -11.080  1.00134.25           N  
ATOM   1507  N   LYS A 193      14.682   0.674 -12.525  1.00193.27           N  
ATOM   1508  CA  LYS A 193      14.647   2.099 -12.786  1.00193.27           C  
ATOM   1509  C   LYS A 193      16.017   2.718 -12.508  1.00193.27           C  
ATOM   1510  O   LYS A 193      17.003   2.325 -13.121  1.00193.27           O  
ATOM   1511  CB  LYS A 193      13.579   2.768 -11.918  1.00143.14           C  
ATOM   1512  CG  LYS A 193      12.183   2.167 -12.022  1.00143.14           C  
ATOM   1513  CD  LYS A 193      12.032   0.989 -11.075  1.00143.14           C  
ATOM   1514  CE  LYS A 193      10.594   0.508 -11.006  1.00143.14           C  
ATOM   1515  NZ  LYS A 193      10.409  -0.523  -9.944  1.00143.14           N  
ATOM   1516  N   GLY A 194      16.076   3.658 -11.565  1.00143.10           N  
ATOM   1517  CA  GLY A 194      17.326   4.338 -11.235  1.00143.10           C  
ATOM   1518  C   GLY A 194      18.481   3.529 -10.657  1.00143.10           C  
ATOM   1519  O   GLY A 194      18.326   2.355 -10.320  1.00143.10           O  
ATOM   1520  N   GLU A 195      19.644   4.172 -10.539  1.00 92.08           N  
ATOM   1521  CA  GLU A 195      20.850   3.530 -10.006  1.00 92.08           C  
ATOM   1522  C   GLU A 195      22.045   4.476 -10.167  1.00 92.08           C  
ATOM   1523  O   GLU A 195      22.081   5.272 -11.107  1.00 92.08           O  
ATOM   1524  CB  GLU A 195      21.118   2.227 -10.758  1.00106.66           C  
ATOM   1525  CG  GLU A 195      21.777   1.146  -9.930  1.00106.66           C  
ATOM   1526  CD  GLU A 195      21.852  -0.178 -10.672  1.00106.66           C  
ATOM   1527  OE1 GLU A 195      22.581  -0.257 -11.686  1.00106.66           O  
ATOM   1528  OE2 GLU A 195      21.174  -1.138 -10.244  1.00106.66           O  
ATOM   1529  N   LYS A 196      23.022   4.391  -9.265  1.00 92.05           N  
ATOM   1530  CA  LYS A 196      24.193   5.274  -9.334  1.00 92.05           C  
ATOM   1531  C   LYS A 196      25.521   4.591  -9.666  1.00 92.05           C  
ATOM   1532  O   LYS A 196      25.974   3.710  -8.929  1.00 92.05           O  
ATOM   1533  CB  LYS A 196      24.376   6.034  -8.016  1.00 86.62           C  
ATOM   1534  CG  LYS A 196      23.270   7.017  -7.679  1.00 86.62           C  
ATOM   1535  CD  LYS A 196      23.639   7.869  -6.462  1.00 86.62           C  
ATOM   1536  CE  LYS A 196      22.480   8.744  -6.010  1.00 86.62           C  
ATOM   1537  NZ  LYS A 196      21.274   7.917  -5.685  1.00 86.62           N  
ATOM   1538  N   HIS A 197      26.148   5.017 -10.765  1.00 70.34           N  
ATOM   1539  CA  HIS A 197      27.436   4.471 -11.178  1.00 70.34           C  
ATOM   1540  C   HIS A 197      28.501   5.527 -10.935  1.00 70.34           C  
ATOM   1541  O   HIS A 197      28.507   6.573 -11.579  1.00 70.34           O  
ATOM   1542  CB  HIS A 197      27.392   4.074 -12.651  1.00 99.97           C  
ATOM   1543  CG  HIS A 197      26.558   2.860 -12.921  1.00 99.97           C  
ATOM   1544  ND1 HIS A 197      26.175   2.486 -14.190  1.00 99.97           N  
ATOM   1545  CD2 HIS A 197      26.051   1.924 -12.085  1.00 99.97           C  
ATOM   1546  CE1 HIS A 197      25.468   1.372 -14.126  1.00 99.97           C  
ATOM   1547  NE2 HIS A 197      25.378   1.010 -12.859  1.00 99.97           N  
ATOM   1548  N   TYR A 198      29.387   5.261  -9.981  1.00 60.94           N  
ATOM   1549  CA  TYR A 198      30.447   6.206  -9.641  1.00 60.94           C  
ATOM   1550  C   TYR A 198      31.676   5.867 -10.430  1.00 60.94           C  
ATOM   1551  O   TYR A 198      31.877   4.710 -10.788  1.00 60.94           O  
ATOM   1552  CB  TYR A 198      30.801   6.130  -8.154  1.00 59.81           C  
ATOM   1553  CG  TYR A 198      29.705   6.582  -7.216  1.00 59.81           C  
ATOM   1554  CD1 TYR A 198      28.542   5.828  -7.047  1.00 59.81           C  
ATOM   1555  CD2 TYR A 198      29.831   7.770  -6.499  1.00 59.81           C  
ATOM   1556  CE1 TYR A 198      27.538   6.241  -6.194  1.00 59.81           C  
ATOM   1557  CE2 TYR A 198      28.830   8.192  -5.641  1.00 59.81           C  
ATOM   1558  CZ  TYR A 198      27.688   7.422  -5.494  1.00 59.81           C  
ATOM   1559  OH  TYR A 198      26.700   7.838  -4.632  1.00 59.81           O  
ATOM   1560  N   TYR A 199      32.518   6.861 -10.684  1.00 41.51           N  
ATOM   1561  CA  TYR A 199      33.736   6.594 -11.436  1.00 41.51           C  
ATOM   1562  C   TYR A 199      34.864   7.584 -11.194  1.00 41.51           C  
ATOM   1563  O   TYR A 199      34.651   8.705 -10.738  1.00 41.51           O  
ATOM   1564  CB  TYR A 199      33.416   6.583 -12.915  1.00 36.09           C  
ATOM   1565  CG  TYR A 199      32.857   7.891 -13.383  1.00 36.09           C  
ATOM   1566  CD1 TYR A 199      33.666   9.029 -13.475  1.00 36.09           C  
ATOM   1567  CD2 TYR A 199      31.526   8.000 -13.746  1.00 36.09           C  
ATOM   1568  CE1 TYR A 199      33.163  10.241 -13.920  1.00 36.09           C  
ATOM   1569  CE2 TYR A 199      31.010   9.206 -14.198  1.00 36.09           C  
ATOM   1570  CZ  TYR A 199      31.835  10.322 -14.286  1.00 36.09           C  
ATOM   1571  OH  TYR A 199      31.323  11.503 -14.776  1.00 36.09           O  
ATOM   1572  N   TYR A 200      36.074   7.153 -11.501  1.00 43.55           N  
ATOM   1573  CA  TYR A 200      37.227   8.007 -11.375  1.00 43.55           C  
ATOM   1574  C   TYR A 200      37.468   8.552 -12.773  1.00 43.55           C  
ATOM   1575  O   TYR A 200      37.032   7.962 -13.757  1.00 43.55           O  
ATOM   1576  CB  TYR A 200      38.426   7.193 -10.954  1.00 58.34           C  
ATOM   1577  CG  TYR A 200      38.577   7.049  -9.473  1.00 58.34           C  
ATOM   1578  CD1 TYR A 200      38.291   5.844  -8.827  1.00 58.34           C  
ATOM   1579  CD2 TYR A 200      39.056   8.107  -8.715  1.00 58.34           C  
ATOM   1580  CE1 TYR A 200      38.488   5.698  -7.462  1.00 58.34           C  
ATOM   1581  CE2 TYR A 200      39.256   7.971  -7.358  1.00 58.34           C  
ATOM   1582  CZ  TYR A 200      38.974   6.771  -6.741  1.00 58.34           C  
ATOM   1583  OH  TYR A 200      39.216   6.671  -5.402  1.00 58.34           O  
ATOM   1584  N   ILE A 201      38.166   9.670 -12.870  1.00 44.20           N  
ATOM   1585  CA  ILE A 201      38.464  10.271 -14.162  1.00 44.20           C  
ATOM   1586  C   ILE A 201      39.968  10.268 -14.394  1.00 44.20           C  
ATOM   1587  O   ILE A 201      40.717  10.999 -13.708  1.00 44.20           O  
ATOM   1588  CB  ILE A 201      37.987  11.696 -14.189  1.00 44.05           C  
ATOM   1589  CG1 ILE A 201      36.472  11.713 -14.061  1.00 44.05           C  
ATOM   1590  CG2 ILE A 201      38.458  12.379 -15.445  1.00 44.05           C  
ATOM   1591  CD1 ILE A 201      35.960  13.037 -13.570  1.00 44.05           C  
ATOM   1592  N   ILE A 202      40.401   9.452 -15.360  1.00 37.06           N  
ATOM   1593  CA  ILE A 202      41.814   9.338 -15.677  1.00 37.06           C  
ATOM   1594  C   ILE A 202      42.194  10.192 -16.860  1.00 37.06           C  
ATOM   1595  O   ILE A 202      41.408  10.363 -17.779  1.00 37.06           O  
ATOM   1596  CB  ILE A 202      42.215   7.925 -16.066  1.00 44.70           C  
ATOM   1597  CG1 ILE A 202      41.713   6.913 -15.051  1.00 44.70           C  
ATOM   1598  CG2 ILE A 202      43.721   7.843 -16.120  1.00 44.70           C  
ATOM   1599  CD1 ILE A 202      42.382   7.026 -13.712  1.00 44.70           C  
ATOM   1600  N   LYS A 203      43.413  10.725 -16.818  1.00 38.35           N  
ATOM   1601  CA  LYS A 203      43.975  11.519 -17.904  1.00 38.35           C  
ATOM   1602  C   LYS A 203      45.113  10.644 -18.441  1.00 38.35           C  
ATOM   1603  O   LYS A 203      46.140  10.456 -17.781  1.00 38.35           O  
ATOM   1604  CB  LYS A 203      44.547  12.842 -17.393  1.00 25.78           C  
ATOM   1605  CG  LYS A 203      45.369  13.589 -18.455  1.00 25.78           C  
ATOM   1606  CD  LYS A 203      46.137  14.774 -17.887  1.00 25.78           C  
ATOM   1607  CE  LYS A 203      46.955  15.484 -18.966  1.00 25.78           C  
ATOM   1608  NZ  LYS A 203      47.819  16.585 -18.413  1.00 25.78           N  
ATOM   1609  N   ASN A 204      44.925  10.092 -19.629  1.00 50.62           N  
ATOM   1610  CA  ASN A 204      45.945   9.236 -20.202  1.00 50.62           C  
ATOM   1611  C   ASN A 204      46.991  10.045 -20.960  1.00 50.62           C  
ATOM   1612  O   ASN A 204      46.950  11.274 -20.969  1.00 50.62           O  
ATOM   1613  CB  ASN A 204      45.307   8.239 -21.148  1.00 51.62           C  
ATOM   1614  CG  ASN A 204      46.078   6.953 -21.229  1.00 51.62           C  
ATOM   1615  OD1 ASN A 204      47.273   6.904 -20.918  1.00 51.62           O  
ATOM   1616  ND2 ASN A 204      45.402   5.894 -21.656  1.00 51.62           N  
ATOM   1617  N   SER A 205      47.933   9.352 -21.590  1.00 48.03           N  
ATOM   1618  CA  SER A 205      48.970  10.020 -22.366  1.00 48.03           C  
ATOM   1619  C   SER A 205      49.073   9.374 -23.733  1.00 48.03           C  
ATOM   1620  O   SER A 205      50.161   9.058 -24.217  1.00 48.03           O  
ATOM   1621  CB  SER A 205      50.327   9.973 -21.653  1.00 44.33           C  
ATOM   1622  OG  SER A 205      50.524   8.751 -20.962  1.00 44.33           O  
ATOM   1623  N   TRP A 206      47.918   9.169 -24.351  1.00 34.08           N  
ATOM   1624  CA  TRP A 206      47.870   8.584 -25.668  1.00 34.08           C  
ATOM   1625  C   TRP A 206      47.176   9.557 -26.585  1.00 34.08           C  
ATOM   1626  O   TRP A 206      46.443   9.155 -27.485  1.00 34.08           O  
ATOM   1627  CB  TRP A 206      47.122   7.257 -25.624  1.00 45.30           C  
ATOM   1628  CG  TRP A 206      47.809   6.241 -24.768  1.00 45.30           C  
ATOM   1629  CD1 TRP A 206      49.087   6.307 -24.271  1.00 45.30           C  
ATOM   1630  CD2 TRP A 206      47.277   4.984 -24.333  1.00 45.30           C  
ATOM   1631  NE1 TRP A 206      49.380   5.172 -23.558  1.00 45.30           N  
ATOM   1632  CE2 TRP A 206      48.292   4.341 -23.576  1.00 45.30           C  
ATOM   1633  CE3 TRP A 206      46.040   4.339 -24.504  1.00 45.30           C  
ATOM   1634  CZ2 TRP A 206      48.111   3.083 -22.993  1.00 45.30           C  
ATOM   1635  CZ3 TRP A 206      45.857   3.084 -23.923  1.00 45.30           C  
ATOM   1636  CH2 TRP A 206      46.896   2.471 -23.175  1.00 45.30           C  
ATOM   1637  N   GLY A 207      47.407  10.846 -26.349  1.00 46.76           N  
ATOM   1638  CA  GLY A 207      46.798  11.886 -27.167  1.00 46.76           C  
ATOM   1639  C   GLY A 207      45.278  12.002 -27.083  1.00 46.76           C  
ATOM   1640  O   GLY A 207      44.585  11.101 -26.571  1.00 46.76           O  
ATOM   1641  N   GLN A 208      44.757  13.118 -27.597  1.00 63.56           N  
ATOM   1642  CA  GLN A 208      43.323  13.380 -27.583  1.00 63.56           C  
ATOM   1643  C   GLN A 208      42.520  12.358 -28.349  1.00 63.56           C  
ATOM   1644  O   GLN A 208      41.466  11.936 -27.906  1.00 63.56           O  
ATOM   1645  CB  GLN A 208      43.036  14.767 -28.129  1.00 91.66           C  
ATOM   1646  CG  GLN A 208      43.339  15.852 -27.128  1.00 91.66           C  
ATOM   1647  CD  GLN A 208      43.361  17.233 -27.755  1.00 91.66           C  
ATOM   1648  OE1 GLN A 208      42.597  17.521 -28.696  1.00 91.66           O  
ATOM   1649  NE2 GLN A 208      44.231  18.107 -27.233  1.00 91.66           N  
ATOM   1650  N   GLN A 209      43.012  11.938 -29.499  1.00 69.71           N  
ATOM   1651  CA  GLN A 209      42.272  10.964 -30.274  1.00 69.71           C  
ATOM   1652  C   GLN A 209      42.004   9.651 -29.534  1.00 69.71           C  
ATOM   1653  O   GLN A 209      41.581   8.673 -30.145  1.00 69.71           O  
ATOM   1654  CB  GLN A 209      42.994  10.694 -31.590  1.00 95.96           C  
ATOM   1655  CG  GLN A 209      44.424  11.217 -31.652  1.00 95.96           C  
ATOM   1656  CD  GLN A 209      45.306  10.700 -30.528  1.00 95.96           C  
ATOM   1657  OE1 GLN A 209      45.218   9.530 -30.127  1.00 95.96           O  
ATOM   1658  NE2 GLN A 209      46.180  11.569 -30.026  1.00 95.96           N  
ATOM   1659  N   TRP A 210      42.250   9.616 -28.227  1.00 61.45           N  
ATOM   1660  CA  TRP A 210      41.978   8.397 -27.469  1.00 61.45           C  
ATOM   1661  C   TRP A 210      40.948   8.579 -26.369  1.00 61.45           C  
ATOM   1662  O   TRP A 210      40.953   9.585 -25.642  1.00 61.45           O  
ATOM   1663  CB  TRP A 210      43.220   7.843 -26.827  1.00 60.22           C  
ATOM   1664  CG  TRP A 210      42.910   6.621 -26.078  1.00 60.22           C  
ATOM   1665  CD1 TRP A 210      42.773   5.388 -26.587  1.00 60.22           C  
ATOM   1666  CD2 TRP A 210      42.782   6.494 -24.663  1.00 60.22           C  
ATOM   1667  NE1 TRP A 210      42.586   4.476 -25.586  1.00 60.22           N  
ATOM   1668  CE2 TRP A 210      42.590   5.131 -24.387  1.00 60.22           C  
ATOM   1669  CE3 TRP A 210      42.817   7.402 -23.598  1.00 60.22           C  
ATOM   1670  CZ2 TRP A 210      42.438   4.639 -23.088  1.00 60.22           C  
ATOM   1671  CZ3 TRP A 210      42.662   6.918 -22.307  1.00 60.22           C  
ATOM   1672  CH2 TRP A 210      42.477   5.546 -22.064  1.00 60.22           C  
ATOM   1673  N   GLY A 211      40.086   7.577 -26.221  1.00 75.93           N  
ATOM   1674  CA  GLY A 211      39.044   7.677 -25.223  1.00 75.93           C  
ATOM   1675  C   GLY A 211      38.404   9.054 -25.300  1.00 75.93           C  
ATOM   1676  O   GLY A 211      38.490   9.749 -26.315  1.00 75.93           O  
ATOM   1677  N   GLU A 212      37.764   9.465 -24.219  1.00 68.14           N  
ATOM   1678  CA  GLU A 212      37.114  10.759 -24.217  1.00 68.14           C  
ATOM   1679  C   GLU A 212      38.172  11.836 -24.152  1.00 68.14           C  
ATOM   1680  O   GLU A 212      38.704  12.138 -23.094  1.00 68.14           O  
ATOM   1681  CB  GLU A 212      36.148  10.886 -23.029  1.00103.43           C  
ATOM   1682  CG  GLU A 212      35.090   9.782 -22.961  1.00103.43           C  
ATOM   1683  CD  GLU A 212      34.059  10.006 -21.867  1.00103.43           C  
ATOM   1684  OE1 GLU A 212      33.209   9.108 -21.659  1.00103.43           O  
ATOM   1685  OE2 GLU A 212      34.099  11.079 -21.224  1.00103.43           O  
ATOM   1686  N   ARG A 213      38.490  12.401 -25.306  1.00 43.14           N  
ATOM   1687  CA  ARG A 213      39.468  13.473 -25.386  1.00 43.14           C  
ATOM   1688  C   ARG A 213      40.779  13.182 -24.674  1.00 43.14           C  
ATOM   1689  O   ARG A 213      41.450  14.104 -24.225  1.00 43.14           O  
ATOM   1690  CB  ARG A 213      38.857  14.764 -24.836  1.00 78.45           C  
ATOM   1691  CG  ARG A 213      39.749  15.978 -24.997  1.00 78.45           C  
ATOM   1692  CD  ARG A 213      38.972  17.188 -25.477  1.00 78.45           C  
ATOM   1693  NE  ARG A 213      39.859  18.333 -25.621  1.00 78.45           N  
ATOM   1694  CZ  ARG A 213      39.478  19.538 -26.023  1.00 78.45           C  
ATOM   1695  NH1 ARG A 213      38.204  19.767 -26.334  1.00 78.45           N  
ATOM   1696  NH2 ARG A 213      40.379  20.513 -26.101  1.00 78.45           N  
ATOM   1697  N   GLY A 214      41.152  11.908 -24.583  1.00 51.68           N  
ATOM   1698  CA  GLY A 214      42.396  11.553 -23.917  1.00 51.68           C  
ATOM   1699  C   GLY A 214      42.174  11.045 -22.499  1.00 51.68           C  
ATOM   1700  O   GLY A 214      43.062  10.429 -21.895  1.00 51.68           O  
ATOM   1701  N   PHE A 215      40.979  11.310 -21.968  1.00 39.64           N  
ATOM   1702  CA  PHE A 215      40.593  10.882 -20.629  1.00 39.64           C  
ATOM   1703  C   PHE A 215      39.771   9.623 -20.657  1.00 39.64           C  
ATOM   1704  O   PHE A 215      39.103   9.335 -21.634  1.00 39.64           O  
ATOM   1705  CB  PHE A 215      39.746  11.937 -19.946  1.00 46.23           C  
ATOM   1706  CG  PHE A 215      40.442  13.207 -19.746  1.00 46.23           C  
ATOM   1707  CD1 PHE A 215      40.346  14.211 -20.682  1.00 46.23           C  
ATOM   1708  CD2 PHE A 215      41.249  13.391 -18.640  1.00 46.23           C  
ATOM   1709  CE1 PHE A 215      41.050  15.394 -20.530  1.00 46.23           C  
ATOM   1710  CE2 PHE A 215      41.964  14.581 -18.477  1.00 46.23           C  
ATOM   1711  CZ  PHE A 215      41.862  15.583 -19.428  1.00 46.23           C  
ATOM   1712  N   ILE A 216      39.806   8.884 -19.563  1.00 47.16           N  
ATOM   1713  CA  ILE A 216      39.005   7.685 -19.452  1.00 47.16           C  
ATOM   1714  C   ILE A 216      38.394   7.635 -18.045  1.00 47.16           C  
ATOM   1715  O   ILE A 216      38.982   8.145 -17.079  1.00 47.16           O  
ATOM   1716  CB  ILE A 216      39.841   6.471 -19.650  1.00 38.01           C  
ATOM   1717  CG1 ILE A 216      38.969   5.228 -19.541  1.00 38.01           C  
ATOM   1718  CG2 ILE A 216      40.929   6.470 -18.612  1.00 38.01           C  
ATOM   1719  CD1 ILE A 216      39.748   3.958 -19.580  1.00 38.01           C  
ATOM   1720  N   ASN A 217      37.211   7.035 -17.941  1.00 48.07           N  
ATOM   1721  CA  ASN A 217      36.517   6.914 -16.674  1.00 48.07           C  
ATOM   1722  C   ASN A 217      36.612   5.472 -16.209  1.00 48.07           C  
ATOM   1723  O   ASN A 217      36.310   4.560 -16.966  1.00 48.07           O  
ATOM   1724  CB  ASN A 217      35.051   7.312 -16.838  1.00 54.28           C  
ATOM   1725  CG  ASN A 217      34.881   8.778 -17.191  1.00 54.28           C  
ATOM   1726  OD1 ASN A 217      34.491   9.122 -18.299  1.00 54.28           O  
ATOM   1727  ND2 ASN A 217      35.182   9.651 -16.244  1.00 54.28           N  
ATOM   1728  N   ILE A 218      37.044   5.262 -14.971  1.00 61.50           N  
ATOM   1729  CA  ILE A 218      37.160   3.920 -14.430  1.00 61.50           C  
ATOM   1730  C   ILE A 218      36.136   3.758 -13.330  1.00 61.50           C  
ATOM   1731  O   ILE A 218      35.964   4.660 -12.505  1.00 61.50           O  
ATOM   1732  CB  ILE A 218      38.538   3.685 -13.836  1.00 79.77           C  
ATOM   1733  CG1 ILE A 218      39.592   3.875 -14.917  1.00 79.77           C  
ATOM   1734  CG2 ILE A 218      38.624   2.293 -13.263  1.00 79.77           C  
ATOM   1735  CD1 ILE A 218      39.279   3.118 -16.191  1.00 79.77           C  
ATOM   1736  N   GLU A 219      35.460   2.611 -13.308  1.00 61.37           N  
ATOM   1737  CA  GLU A 219      34.445   2.354 -12.294  1.00 61.37           C  
ATOM   1738  C   GLU A 219      35.001   2.496 -10.886  1.00 61.37           C  
ATOM   1739  O   GLU A 219      36.207   2.407 -10.664  1.00 61.37           O  
ATOM   1740  CB  GLU A 219      33.843   0.951 -12.471  1.00132.04           C  
ATOM   1741  CG  GLU A 219      32.740   0.615 -11.459  1.00132.04           C  
ATOM   1742  CD  GLU A 219      32.073  -0.727 -11.719  1.00132.04           C  
ATOM   1743  OE1 GLU A 219      31.374  -0.864 -12.746  1.00132.04           O  
ATOM   1744  OE2 GLU A 219      32.249  -1.646 -10.893  1.00132.04           O  
ATOM   1745  N   THR A 220      34.106   2.732  -9.939  1.00 66.67           N  
ATOM   1746  CA  THR A 220      34.484   2.860  -8.543  1.00 66.67           C  
ATOM   1747  C   THR A 220      33.226   3.056  -7.718  1.00 66.67           C  
ATOM   1748  O   THR A 220      32.121   3.137  -8.264  1.00 66.67           O  
ATOM   1749  CB  THR A 220      35.409   4.049  -8.326  1.00 38.71           C  
ATOM   1750  OG1 THR A 220      35.785   4.134  -6.942  1.00 38.71           O  
ATOM   1751  CG2 THR A 220      34.720   5.312  -8.743  1.00 38.71           C  
ATOM   1752  N   ASP A 221      33.388   3.128  -6.402  1.00 61.70           N  
ATOM   1753  CA  ASP A 221      32.248   3.308  -5.520  1.00 61.70           C  
ATOM   1754  C   ASP A 221      32.254   4.672  -4.847  1.00 61.70           C  
ATOM   1755  O   ASP A 221      33.272   5.360  -4.792  1.00 61.70           O  
ATOM   1756  CB  ASP A 221      32.217   2.201  -4.460  1.00107.52           C  
ATOM   1757  CG  ASP A 221      33.448   2.196  -3.579  1.00107.52           C  
ATOM   1758  OD1 ASP A 221      33.528   1.327  -2.688  1.00107.52           O  
ATOM   1759  OD2 ASP A 221      34.331   3.055  -3.768  1.00107.52           O  
ATOM   1760  N   GLU A 222      31.094   5.056  -4.338  1.00 59.28           N  
ATOM   1761  CA  GLU A 222      30.965   6.332  -3.668  1.00 59.28           C  
ATOM   1762  C   GLU A 222      32.183   6.627  -2.809  1.00 59.28           C  
ATOM   1763  O   GLU A 222      32.705   7.739  -2.795  1.00 59.28           O  
ATOM   1764  CB  GLU A 222      29.707   6.329  -2.802  1.00100.29           C  
ATOM   1765  CG  GLU A 222      29.584   7.520  -1.873  1.00100.29           C  
ATOM   1766  CD  GLU A 222      28.152   7.757  -1.465  1.00100.29           C  
ATOM   1767  OE1 GLU A 222      27.477   6.768  -1.107  1.00100.29           O  
ATOM   1768  OE2 GLU A 222      27.703   8.927  -1.507  1.00100.29           O  
ATOM   1769  N   SER A 223      32.642   5.601  -2.114  1.00 51.23           N  
ATOM   1770  CA  SER A 223      33.769   5.728  -1.208  1.00 51.23           C  
ATOM   1771  C   SER A 223      35.101   6.008  -1.875  1.00 51.23           C  
ATOM   1772  O   SER A 223      35.962   6.657  -1.292  1.00 51.23           O  
ATOM   1773  CB  SER A 223      33.878   4.456  -0.378  1.00 79.77           C  
ATOM   1774  OG  SER A 223      33.897   3.324  -1.232  1.00 79.77           O  
ATOM   1775  N   GLY A 224      35.273   5.520  -3.094  1.00 78.18           N  
ATOM   1776  CA  GLY A 224      36.540   5.719  -3.771  1.00 78.18           C  
ATOM   1777  C   GLY A 224      37.570   4.773  -3.169  1.00 78.18           C  
ATOM   1778  O   GLY A 224      38.680   5.182  -2.795  1.00 78.18           O  
ATOM   1779  N   LEU A 225      37.176   3.504  -3.059  1.00 57.91           N  
ATOM   1780  CA  LEU A 225      38.015   2.448  -2.501  1.00 57.91           C  
ATOM   1781  C   LEU A 225      38.070   1.372  -3.542  1.00 57.91           C  
ATOM   1782  O   LEU A 225      38.974   0.547  -3.561  1.00 57.91           O  
ATOM   1783  CB  LEU A 225      37.407   1.874  -1.217  1.00 86.61           C  
ATOM   1784  CG  LEU A 225      37.598   2.632   0.106  1.00 86.61           C  
ATOM   1785  CD1 LEU A 225      39.078   2.771   0.382  1.00 86.61           C  
ATOM   1786  CD2 LEU A 225      36.958   4.010   0.065  1.00 86.61           C  
ATOM   1787  N   MET A 226      37.082   1.379  -4.415  1.00 87.37           N  
ATOM   1788  CA  MET A 226      37.048   0.396  -5.464  1.00 87.37           C  
ATOM   1789  C   MET A 226      37.990   0.883  -6.571  1.00 87.37           C  
ATOM   1790  O   MET A 226      37.611   1.675  -7.449  1.00 87.37           O  
ATOM   1791  CB  MET A 226      35.633   0.252  -5.981  1.00 91.20           C  
ATOM   1792  CG  MET A 226      35.420  -1.019  -6.719  1.00 91.20           C  
ATOM   1793  SD  MET A 226      34.186  -0.756  -7.953  1.00 91.20           S  
ATOM   1794  CE  MET A 226      34.922  -1.579  -9.389  1.00 91.20           C  
ATOM   1795  N   ARG A 227      39.230   0.405  -6.514  1.00 49.76           N  
ATOM   1796  CA  ARG A 227      40.247   0.789  -7.476  1.00 49.76           C  
ATOM   1797  C   ARG A 227      40.454  -0.246  -8.560  1.00 49.76           C  
ATOM   1798  O   ARG A 227      41.390  -1.039  -8.477  1.00 49.76           O  
ATOM   1799  CB  ARG A 227      41.557   1.017  -6.739  1.00 74.06           C  
ATOM   1800  CG  ARG A 227      41.474   2.109  -5.704  1.00 74.06           C  
ATOM   1801  CD  ARG A 227      42.397   1.814  -4.567  1.00 74.06           C  
ATOM   1802  NE  ARG A 227      43.377   0.820  -4.966  1.00 74.06           N  
ATOM   1803  CZ  ARG A 227      44.313   0.330  -4.163  1.00 74.06           C  
ATOM   1804  NH1 ARG A 227      44.404   0.749  -2.902  1.00 74.06           N  
ATOM   1805  NH2 ARG A 227      45.148  -0.595  -4.622  1.00 74.06           N  
ATOM   1806  N   LYS A 228      39.596  -0.259  -9.575  1.00 63.82           N  
ATOM   1807  CA  LYS A 228      39.785  -1.228 -10.648  1.00 63.82           C  
ATOM   1808  C   LYS A 228      41.209  -1.139 -11.188  1.00 63.82           C  
ATOM   1809  O   LYS A 228      41.901  -0.136 -11.014  1.00 63.82           O  
ATOM   1810  CB  LYS A 228      38.809  -0.998 -11.798  1.00 97.88           C  
ATOM   1811  CG  LYS A 228      37.416  -1.512 -11.526  1.00 97.88           C  
ATOM   1812  CD  LYS A 228      36.744  -2.064 -12.790  1.00 97.88           C  
ATOM   1813  CE  LYS A 228      37.440  -3.336 -13.272  1.00 97.88           C  
ATOM   1814  NZ  LYS A 228      36.699  -4.037 -14.352  1.00 97.88           N  
ATOM   1815  N   CYS A 229      41.657  -2.215 -11.813  1.00 53.23           N  
ATOM   1816  CA  CYS A 229      42.972  -2.256 -12.409  1.00 53.23           C  
ATOM   1817  C   CYS A 229      44.115  -1.735 -11.553  1.00 53.23           C  
ATOM   1818  O   CYS A 229      45.114  -1.255 -12.080  1.00 53.23           O  
ATOM   1819  CB  CYS A 229      42.913  -1.507 -13.729  1.00 85.99           C  
ATOM   1820  SG  CYS A 229      41.663  -2.226 -14.844  1.00 85.99           S  
ATOM   1821  N   GLY A 230      43.982  -1.816 -10.237  1.00 42.75           N  
ATOM   1822  CA  GLY A 230      45.073  -1.372  -9.387  1.00 42.75           C  
ATOM   1823  C   GLY A 230      45.217   0.121  -9.154  1.00 42.75           C  
ATOM   1824  O   GLY A 230      46.164   0.547  -8.465  1.00 42.75           O  
ATOM   1825  N   LEU A 231      44.298   0.914  -9.720  1.00 46.56           N  
ATOM   1826  CA  LEU A 231      44.297   2.370  -9.546  1.00 46.56           C  
ATOM   1827  C   LEU A 231      45.081   2.894  -8.337  1.00 46.56           C  
ATOM   1828  O   LEU A 231      44.974   2.380  -7.222  1.00 46.56           O  
ATOM   1829  CB  LEU A 231      42.871   2.879  -9.397  1.00 54.74           C  
ATOM   1830  CG  LEU A 231      42.044   3.020 -10.657  1.00 54.74           C  
ATOM   1831  CD1 LEU A 231      40.609   3.363 -10.283  1.00 54.74           C  
ATOM   1832  CD2 LEU A 231      42.648   4.105 -11.527  1.00 54.74           C  
ATOM   1833  N   GLY A 232      45.859   3.936  -8.564  1.00 82.21           N  
ATOM   1834  CA  GLY A 232      46.601   4.533  -7.477  1.00 82.21           C  
ATOM   1835  C   GLY A 232      47.289   3.611  -6.491  1.00 82.21           C  
ATOM   1836  O   GLY A 232      47.575   4.035  -5.366  1.00 82.21           O  
ATOM   1837  N   THR A 233      47.534   2.358  -6.874  1.00 53.13           N  
ATOM   1838  CA  THR A 233      48.264   1.443  -5.989  1.00 53.13           C  
ATOM   1839  C   THR A 233      49.480   2.247  -5.550  1.00 53.13           C  
ATOM   1840  O   THR A 233      49.839   2.303  -4.374  1.00 53.13           O  
ATOM   1841  CB  THR A 233      48.781   0.243  -6.743  1.00 50.06           C  
ATOM   1842  OG1 THR A 233      47.685  -0.603  -7.117  1.00 50.06           O  
ATOM   1843  CG2 THR A 233      49.783  -0.490  -5.892  1.00 50.06           C  
ATOM   1844  N   ASP A 234      50.104   2.853  -6.556  1.00 98.68           N  
ATOM   1845  CA  ASP A 234      51.245   3.740  -6.407  1.00 98.68           C  
ATOM   1846  C   ASP A 234      50.592   5.069  -6.687  1.00 98.68           C  
ATOM   1847  O   ASP A 234      50.072   5.279  -7.782  1.00 98.68           O  
ATOM   1848  CB  ASP A 234      52.273   3.491  -7.495  1.00 84.32           C  
ATOM   1849  CG  ASP A 234      53.172   2.344  -7.187  1.00 84.32           C  
ATOM   1850  OD1 ASP A 234      53.973   2.482  -6.234  1.00 84.32           O  
ATOM   1851  OD2 ASP A 234      53.074   1.317  -7.896  1.00 84.32           O  
ATOM   1852  N   ALA A 235      50.595   5.965  -5.718  1.00 42.67           N  
ATOM   1853  CA  ALA A 235      49.964   7.253  -5.944  1.00 42.67           C  
ATOM   1854  C   ALA A 235      50.748   8.406  -5.348  1.00 42.67           C  
ATOM   1855  O   ALA A 235      51.087   8.397  -4.166  1.00 42.67           O  
ATOM   1856  CB  ALA A 235      48.580   7.239  -5.388  1.00 23.76           C  
ATOM   1857  N   PHE A 236      51.048   9.399  -6.171  1.00 55.25           N  
ATOM   1858  CA  PHE A 236      51.788  10.541  -5.686  1.00 55.25           C  
ATOM   1859  C   PHE A 236      51.255  11.806  -6.308  1.00 55.25           C  
ATOM   1860  O   PHE A 236      50.682  11.787  -7.403  1.00 55.25           O  
ATOM   1861  CB  PHE A 236      53.265  10.421  -6.030  1.00 53.50           C  
ATOM   1862  CG  PHE A 236      53.872   9.123  -5.632  1.00 53.50           C  
ATOM   1863  CD1 PHE A 236      53.582   7.958  -6.337  1.00 53.50           C  
ATOM   1864  CD2 PHE A 236      54.748   9.062  -4.561  1.00 53.50           C  
ATOM   1865  CE1 PHE A 236      54.161   6.743  -5.979  1.00 53.50           C  
ATOM   1866  CE2 PHE A 236      55.332   7.859  -4.195  1.00 53.50           C  
ATOM   1867  CZ  PHE A 236      55.039   6.692  -4.906  1.00 53.50           C  
ATOM   1868  N   ILE A 237      51.455  12.903  -5.588  1.00 39.67           N  
ATOM   1869  CA  ILE A 237      51.040  14.223  -6.025  1.00 39.67           C  
ATOM   1870  C   ILE A 237      52.162  15.146  -5.564  1.00 39.67           C  
ATOM   1871  O   ILE A 237      52.466  15.233  -4.380  1.00 39.67           O  
ATOM   1872  CB  ILE A 237      49.629  14.607  -5.438  1.00 59.92           C  
ATOM   1873  CG1 ILE A 237      49.600  16.067  -5.017  1.00 59.92           C  
ATOM   1874  CG2 ILE A 237      49.253  13.697  -4.310  1.00 59.92           C  
ATOM   1875  CD1 ILE A 237      49.700  17.019  -6.179  1.00 59.92           C  
ATOM   1876  N   PRO A 238      52.809  15.836  -6.512  1.00 46.05           N  
ATOM   1877  CA  PRO A 238      53.907  16.739  -6.180  1.00 46.05           C  
ATOM   1878  C   PRO A 238      53.384  18.008  -5.547  1.00 46.05           C  
ATOM   1879  O   PRO A 238      52.234  18.386  -5.756  1.00 46.05           O  
ATOM   1880  CB  PRO A 238      54.524  17.014  -7.538  1.00 25.71           C  
ATOM   1881  CG  PRO A 238      53.272  17.201  -8.375  1.00 25.71           C  
ATOM   1882  CD  PRO A 238      52.368  16.064  -7.901  1.00 25.71           C  
ATOM   1883  N   LEU A 239      54.241  18.664  -4.779  1.00 65.02           N  
ATOM   1884  CA  LEU A 239      53.883  19.918  -4.140  1.00 65.02           C  
ATOM   1885  C   LEU A 239      54.874  20.972  -4.572  1.00 65.02           C  
ATOM   1886  O   LEU A 239      56.085  20.742  -4.568  1.00 65.02           O  
ATOM   1887  CB  LEU A 239      53.913  19.790  -2.618  1.00 77.04           C  
ATOM   1888  CG  LEU A 239      52.706  19.094  -1.996  1.00 77.04           C  
ATOM   1889  CD1 LEU A 239      51.450  19.821  -2.452  1.00 77.04           C  
ATOM   1890  CD2 LEU A 239      52.661  17.622  -2.401  1.00 77.04           C  
ATOM   1891  N   ILE A 240      54.358  22.127  -4.961  1.00 69.47           N  
ATOM   1892  CA  ILE A 240      55.224  23.209  -5.373  1.00 69.47           C  
ATOM   1893  C   ILE A 240      55.152  24.350  -4.366  1.00 69.47           C  
ATOM   1894  O   ILE A 240      55.728  25.419  -4.575  1.00 69.47           O  
ATOM   1895  CB  ILE A 240      54.836  23.697  -6.745  1.00 62.59           C  
ATOM   1896  CG1 ILE A 240      53.322  23.882  -6.816  1.00 62.59           C  
ATOM   1897  CG2 ILE A 240      55.308  22.702  -7.779  1.00 62.59           C  
ATOM   1898  CD1 ILE A 240      52.866  24.612  -8.071  1.00 62.59           C  
ATOM   1899  N   GLU A 241      54.428  24.107  -3.276  1.00118.68           N  
ATOM   1900  CA  GLU A 241      54.287  25.071  -2.193  1.00118.68           C  
ATOM   1901  C   GLU A 241      54.655  24.368  -0.894  1.00118.68           C  
ATOM   1902  O   GLU A 241      55.687  24.741  -0.294  1.00118.68           O  
ATOM   1903  CB  GLU A 241      52.853  25.581  -2.089  1.00 98.38           C  
ATOM   1904  CG  GLU A 241      52.386  26.386  -3.273  1.00 98.38           C  
ATOM   1905  CD  GLU A 241      51.030  27.039  -3.034  1.00 98.38           C  
ATOM   1906  OE1 GLU A 241      50.155  26.385  -2.416  1.00 98.38           O  
ATOM   1907  OE2 GLU A 241      50.838  28.200  -3.476  1.00 98.38           O  
ATOM   1908  OXT GLU A 241      53.907  23.442  -0.502  1.00 98.38           O  
TER    1909      GLU A 241                                                      



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