CNRS Nantes University US2B US2B
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***  3GY4_1  ***

elNémo ID: 240918104815855546

Job options:

ID        	=	 240918104815855546
JOBID     	=	 3GY4_1
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 3GY4_1

HEADER    HYDROLASE                               03-APR-09   3GY4              
TITLE     A COMPARATIVE STUDY ON THE INHIBITION OF BOVINE BETA-TRYPSIN BY BIS-  
TITLE    2 BENZAMIDINES DIMINAZENE AND PENTAMIDINE BY X-RAY CRYSTALLOGRAPHY AND 
TITLE    3 ITC                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATIONIC TRYPSIN;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BETA-TRYPSIN, ALPHA-TRYPSIN CHAIN 1, ALPHA-TRYPSIN CHAIN 2; 
COMPND   5 EC: 3.4.21.4                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: BOVINE,COW;                                         
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 OTHER_DETAILS: PANCREATIC                                            
KEYWDS    BOVINE BETA-TRYPSIN, P-AMINO BENZAMIDINE, PROTEIN-LIGAND COMPLEX,     
KEYWDS   2 PROTEIN-LIGAND INTERACTION, CALCIUM, DIGESTION, DISULFIDE BOND,      
KEYWDS   3 HYDROLASE, METAL-BINDING, PROTEASE, SECRETED, SERINE PROTEASE,       
KEYWDS   4 ZYMOGEN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.S.PERILO,M.T.PEREIRA,M.M.SANTORO,R.A.P.NAGEM                        
REVDAT   2   02-JUN-10 3GY4    1       JRNL                                     
REVDAT   1   23-MAR-10 3GY4    0                                                
JRNL        AUTH   C.S.PERILO,M.T.PEREIRA,M.M.SANTORO,R.A.NAGEM                 
JRNL        TITL   STRUCTURAL BINDING EVIDENCE OF THE TRYPANOCIDAL DRUGS        
JRNL        TITL 2 BERENIL AND PENTACARINATE ACTIVE PRINCIPLES TO A SERINE      
JRNL        TITL 3 PROTEASE MODEL.                                              
JRNL        REF    INT.J.BIOL.MACROMOL.          V.  46   502 2010              
JRNL        REFN                   ISSN 0141-8130                               
JRNL        PMID   20356563                                                     
JRNL        DOI    10.1016/J.IJBIOMAC.2010.03.006                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 29342                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.175                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1253                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2117                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.2380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1629                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 61                                      
REMARK   3   SOLVENT ATOMS            : 365                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : -0.22000                                             
REMARK   3    B33 (A**2) : 0.29000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.078         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.074         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.138         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1771 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2404 ; 1.160 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   235 ; 5.901 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    60 ;39.235 ;26.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   288 ;12.118 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ;14.621 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   265 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1285 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   910 ; 0.263 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1201 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   274 ; 0.110 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     5 ; 0.128 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    51 ; 0.214 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    43 ; 0.119 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1147 ; 0.626 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1818 ; 0.954 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   706 ; 1.645 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   577 ; 2.417 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3GY4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052451.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JAN-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU ULTRAX 18                   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30624                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03700                            
REMARK 200   FOR THE DATA SET  : 29.2100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.12200                            
REMARK 200   FOR SHELL         : 8.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG8000, 0.1M AMMONIUM SULFATE,      
REMARK 280  0.05M TRIS-HCL, 0.008M CACL2, PH 8.0, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 291K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.13250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.38300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.05300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       33.38300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.13250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.05300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A 130   C     ALA A 132   N       0.250                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  71      -81.87   -113.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 247  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 ASN A  72   O    92.5                                              
REMARK 620 3 VAL A  75   O   165.2  79.5                                        
REMARK 620 4 GLU A  80   OE2 102.6 159.8  88.2                                  
REMARK 620 5 HOH A 502   O    87.7  90.8 104.7  76.9                            
REMARK 620 6 HOH A 516   O    79.2 102.3  90.2  93.6 161.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 247                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PBZ A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 246                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 6                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GY2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GY3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GY5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GY6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GY7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GY8   RELATED DB: PDB                                   
DBREF  3GY4 A   16   245  UNP    P00760   TRY1_BOVIN      24    246             
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER          
SEQRES   7 A  223  ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS          
SEQRES   8 A  223  SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER          
SEQRES   9 A  223  LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER          
SEQRES  11 A  223  TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU          
SEQRES  12 A  223  SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA          
SEQRES  18 A  223  SER ASN                                                      
HET     CA  A 247       1                                                       
HET    PBZ  A   1      10                                                       
HET    EDO  A 246       4                                                       
HET    EDO  A   2       4                                                       
HET    EDO  A   3       4                                                       
HET    EDO  A   4       4                                                       
HET    EDO  A   5       4                                                       
HET    SO4  A 248       5                                                       
HET    SO4  A 249       5                                                       
HET    SO4  A 250       5                                                       
HET    SO4  A 251       5                                                       
HET    SO4  A 252       5                                                       
HET    SO4  A   6       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     PBZ P-AMINO BENZAMIDINE                                              
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     SO4 SULFATE ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  PBZ    C7 H10 N3 1+                                                 
FORMUL   4  EDO    5(C2 H6 O2)                                                  
FORMUL   9  SO4    6(O4 S 2-)                                                   
FORMUL  15  HOH   *365(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 SER A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  SER A  244  1                                  11    
SHEET    1   A 7 TYR A  20  THR A  21  0                                        
SHEET    2   A 7 LYS A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   A 7 GLN A 135  GLY A 140 -1  N  ILE A 138   O  LEU A 158           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   A 7 LYS A 204  TRP A 215 -1  O  LYS A 204   N  CYS A 201           
SHEET    6   A 7 GLY A 226  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7   A 7 MET A 180  ALA A 183 -1  N  PHE A 181   O  TYR A 228           
SHEET    1   B 7 GLN A  30  ASN A  34  0                                        
SHEET    2   B 7 HIS A  40  ASN A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   B 7 MET A 104  LEU A 108 -1  O  ILE A 106   N  VAL A  52           
SHEET    5   B 7 GLN A  81  VAL A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    6   B 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    7   B 7 GLN A  30  ASN A  34 -1  N  SER A  32   O  ARG A  66           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.05  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.05  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.03  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.03  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.05  
LINK         OE1 GLU A  70                CA    CA A 247     1555   1555  2.22  
LINK         O   ASN A  72                CA    CA A 247     1555   1555  2.32  
LINK         O   VAL A  75                CA    CA A 247     1555   1555  2.30  
LINK         OE2 GLU A  80                CA    CA A 247     1555   1555  2.29  
LINK        CA    CA A 247                 O   HOH A 502     1555   1555  2.43  
LINK        CA    CA A 247                 O   HOH A 516     1555   1555  2.40  
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  80                    
SITE     2 AC1  6 HOH A 502  HOH A 516                                          
SITE     1 AC2 11 SO4 A   6  ASP A 189  SER A 190  SER A 195                    
SITE     2 AC2 11 TRP A 215  GLY A 216  GLY A 219  CYS A 220                    
SITE     3 AC2 11 GLY A 226  HOH A 512  HOH A 515                               
SITE     1 AC3  4 GLU A  80  GLN A  81  PHE A  82  HOH A 281                    
SITE     1 AC4  6 ASN A  95  THR A  98  ASN A 100  HOH A 439                    
SITE     2 AC4  6 HOH A 572  HOH A 573                                          
SITE     1 AC5  5 ARG A 117  SER A 170  HOH A 346  HOH A 389                    
SITE     2 AC5  5 HOH A 438                                                     
SITE     1 AC6  6 SER A 164  ASP A 165  SER A 166  HOH A 322                    
SITE     2 AC6  6 HOH A 352  HOH A 424                                          
SITE     1 AC7 10 ARG A  66  ILE A  73  ASN A  74  VAL A  75                    
SITE     2 AC7 10 VAL A  90  HIS A  91  PRO A  92  HOH A 272                    
SITE     3 AC7 10 HOH A 387  HOH A 516                                          
SITE     1 AC8  8 LYS A  87  LYS A 107  THR A 149  HOH A 395                    
SITE     2 AC8  8 HOH A 413  HOH A 469  HOH A 535  HOH A 599                    
SITE     1 AC9  9 PRO A 124  THR A 125  SER A 127  SER A 147                    
SITE     2 AC9  9 GLY A 148  LYS A 204  HOH A 378  HOH A 450                    
SITE     3 AC9  9 HOH A 488                                                     
SITE     1 BC1  7 HOH A  11  LYS A 169  PRO A 173  GLY A 174                    
SITE     2 BC1  7 HOH A 438  HOH A 473  HOH A 481                               
SITE     1 BC2  4 LYS A 145  SER A 146  SER A 147  HOH A 595                    
SITE     1 BC3  5 THR A 177  SER A 178  HOH A 283  HOH A 482                    
SITE     2 BC3  5 HOH A 540                                                     
SITE     1 BC4 10 PBZ A   1  HIS A  57  GLN A 192  GLY A 193                    
SITE     2 BC4 10 SER A 195  HOH A 383  HOH A 394  HOH A 455                    
SITE     3 BC4 10 HOH A 483  HOH A 548                                          
CRYST1   54.265   58.106   66.766  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018428  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017210  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014978        0.00000                         
ATOM      1  N   ILE A  16      -8.048   9.475  20.073  1.00  4.91           N  
ATOM      2  CA  ILE A  16      -8.032   8.545  18.906  1.00  5.35           C  
ATOM      3  C   ILE A  16      -9.318   8.773  18.118  1.00  5.73           C  
ATOM      4  O   ILE A  16     -10.430   8.648  18.664  1.00  5.65           O  
ATOM      5  CB  ILE A  16      -7.962   7.064  19.362  1.00  4.78           C  
ATOM      6  CG1 ILE A  16      -6.735   6.798  20.257  1.00  4.49           C  
ATOM      7  CG2 ILE A  16      -7.955   6.108  18.165  1.00  5.75           C  
ATOM      8  CD1 ILE A  16      -5.377   6.723  19.513  1.00  5.57           C  
ATOM      9  N   VAL A  17      -9.144   9.113  16.843  1.00  5.96           N  
ATOM     10  CA  VAL A  17     -10.257   9.341  15.921  1.00  6.18           C  
ATOM     11  C   VAL A  17     -10.435   8.106  15.043  1.00  6.45           C  
ATOM     12  O   VAL A  17      -9.464   7.592  14.475  1.00  6.22           O  
ATOM     13  CB  VAL A  17     -10.021  10.595  15.031  1.00  5.99           C  
ATOM     14  CG1 VAL A  17     -11.185  10.800  14.055  1.00  6.88           C  
ATOM     15  CG2 VAL A  17      -9.837  11.831  15.897  1.00  7.33           C  
ATOM     16  N   GLY A  18     -11.677   7.624  14.951  1.00  6.82           N  
ATOM     17  CA  GLY A  18     -11.993   6.487  14.075  1.00  7.18           C  
ATOM     18  C   GLY A  18     -11.473   5.139  14.557  1.00  7.61           C  
ATOM     19  O   GLY A  18     -11.291   4.203  13.757  1.00  8.73           O  
ATOM     20  N   GLY A  19     -11.257   5.032  15.865  1.00  7.37           N  
ATOM     21  CA  GLY A  19     -10.798   3.783  16.469  1.00  7.03           C  
ATOM     22  C   GLY A  19     -11.923   3.008  17.123  1.00  7.33           C  
ATOM     23  O   GLY A  19     -13.096   3.116  16.726  1.00  7.95           O  
ATOM     24  N   TYR A  20     -11.555   2.213  18.119  1.00  6.30           N  
ATOM     25  CA  TYR A  20     -12.508   1.351  18.796  1.00  6.44           C  
ATOM     26  C   TYR A  20     -12.205   1.301  20.285  1.00  6.52           C  
ATOM     27  O   TYR A  20     -11.097   1.620  20.721  1.00  6.62           O  
ATOM     28  CB  TYR A  20     -12.491  -0.061  18.178  1.00  6.41           C  
ATOM     29  CG  TYR A  20     -11.159  -0.786  18.274  1.00  6.04           C  
ATOM     30  CD1 TYR A  20     -10.929  -1.731  19.281  1.00  5.43           C  
ATOM     31  CD2 TYR A  20     -10.130  -0.531  17.355  1.00  5.79           C  
ATOM     32  CE1 TYR A  20      -9.701  -2.406  19.379  1.00  6.32           C  
ATOM     33  CE2 TYR A  20      -8.901  -1.200  17.445  1.00  6.67           C  
ATOM     34  CZ  TYR A  20      -8.699  -2.127  18.448  1.00  6.13           C  
ATOM     35  OH  TYR A  20      -7.485  -2.774  18.526  1.00  8.10           O  
ATOM     36  N   THR A  21     -13.191   0.898  21.071  1.00  6.58           N  
ATOM     37  CA  THR A  21     -12.968   0.737  22.504  1.00  6.56           C  
ATOM     38  C   THR A  21     -12.062  -0.487  22.737  1.00  6.73           C  
ATOM     39  O   THR A  21     -12.410  -1.609  22.351  1.00  7.12           O  
ATOM     40  CB  THR A  21     -14.317   0.612  23.241  1.00  6.65           C  
ATOM     41  OG1 THR A  21     -15.063   1.827  23.065  1.00  7.95           O  
ATOM     42  CG2 THR A  21     -14.117   0.335  24.721  1.00  7.07           C  
ATOM     43  N   CYS A  22     -10.899  -0.266  23.353  1.00  6.55           N  
ATOM     44  CA  CYS A  22      -9.910  -1.338  23.528  1.00  6.47           C  
ATOM     45  C   CYS A  22     -10.486  -2.502  24.317  1.00  6.64           C  
ATOM     46  O   CYS A  22     -10.325  -3.664  23.933  1.00  7.44           O  
ATOM     47  CB  CYS A  22      -8.660  -0.836  24.262  1.00  6.24           C  
ATOM     48  SG  CYS A  22      -7.822   0.560  23.519  1.00  6.07           S  
ATOM     49  N   GLY A  23     -11.180  -2.168  25.403  1.00  6.71           N  
ATOM     50  CA  GLY A  23     -11.537  -3.142  26.427  1.00  6.38           C  
ATOM     51  C   GLY A  23     -10.666  -2.917  27.647  1.00  6.94           C  
ATOM     52  O   GLY A  23      -9.463  -2.663  27.527  1.00  7.05           O  
ATOM     53  N   ALA A  24     -11.268  -3.009  28.826  1.00  7.25           N  
ATOM     54  CA  ALA A  24     -10.566  -2.672  30.057  1.00  7.02           C  
ATOM     55  C   ALA A  24      -9.297  -3.499  30.256  1.00  7.43           C  
ATOM     56  O   ALA A  24      -9.336  -4.737  30.245  1.00  7.80           O  
ATOM     57  CB  ALA A  24     -11.486  -2.835  31.256  1.00  7.90           C  
ATOM     58  N   ASN A  25      -8.178  -2.796  30.416  1.00  7.37           N  
ATOM     59  CA  ASN A  25      -6.888  -3.396  30.758  1.00  7.54           C  
ATOM     60  C   ASN A  25      -6.340  -4.356  29.713  1.00  7.31           C  
ATOM     61  O   ASN A  25      -5.535  -5.229  30.030  1.00  7.99           O  
ATOM     62  CB  ASN A  25      -6.951  -4.072  32.131  1.00  7.60           C  
ATOM     63  CG  ASN A  25      -7.515  -3.165  33.191  1.00  8.29           C  
ATOM     64  OD1 ASN A  25      -8.575  -3.435  33.739  1.00 10.26           O  
ATOM     65  ND2 ASN A  25      -6.831  -2.058  33.457  1.00  7.58           N  
ATOM     66  N   THR A  26      -6.772  -4.174  28.466  1.00  6.81           N  
ATOM     67  CA  THR A  26      -6.275  -4.981  27.348  1.00  6.59           C  
ATOM     68  C   THR A  26      -4.987  -4.425  26.762  1.00  6.39           C  
ATOM     69  O   THR A  26      -4.367  -5.065  25.906  1.00  6.70           O  
ATOM     70  CB  THR A  26      -7.325  -5.104  26.223  1.00  6.31           C  
ATOM     71  OG1 THR A  26      -7.659  -3.794  25.740  1.00  7.32           O  
ATOM     72  CG2 THR A  26      -8.582  -5.808  26.752  1.00  8.02           C  
ATOM     73  N   VAL A  27      -4.611  -3.223  27.204  1.00  6.37           N  
ATOM     74  CA  VAL A  27      -3.367  -2.581  26.782  1.00  6.10           C  
ATOM     75  C   VAL A  27      -2.607  -2.254  28.073  1.00  5.69           C  
ATOM     76  O   VAL A  27      -2.606  -1.119  28.539  1.00  5.73           O  
ATOM     77  CB  VAL A  27      -3.631  -1.288  25.942  1.00  5.91           C  
ATOM     78  CG1 VAL A  27      -2.329  -0.756  25.373  1.00  5.97           C  
ATOM     79  CG2 VAL A  27      -4.629  -1.559  24.811  1.00  7.41           C  
ATOM     80  N   PRO A  28      -1.993  -3.277  28.687  1.00  5.30           N  
ATOM     81  CA  PRO A  28      -1.562  -3.186  30.086  1.00  5.79           C  
ATOM     82  C   PRO A  28      -0.363  -2.275  30.345  1.00  5.80           C  
ATOM     83  O   PRO A  28      -0.098  -1.923  31.505  1.00  5.08           O  
ATOM     84  CB  PRO A  28      -1.243  -4.645  30.444  1.00  5.81           C  
ATOM     85  CG  PRO A  28      -0.887  -5.286  29.128  1.00  5.40           C  
ATOM     86  CD  PRO A  28      -1.740  -4.609  28.097  1.00  6.19           C  
ATOM     87  N   TYR A  29       0.331  -1.895  29.274  1.00  5.29           N  
ATOM     88  CA  TYR A  29       1.469  -0.974  29.352  1.00  5.24           C  
ATOM     89  C   TYR A  29       1.056   0.485  29.182  1.00  5.28           C  
ATOM     90  O   TYR A  29       1.881   1.383  29.366  1.00  5.22           O  
ATOM     91  CB  TYR A  29       2.509  -1.328  28.287  1.00  5.50           C  
ATOM     92  CG  TYR A  29       1.879  -1.465  26.915  1.00  4.76           C  
ATOM     93  CD1 TYR A  29       1.681  -0.350  26.095  1.00  5.57           C  
ATOM     94  CD2 TYR A  29       1.438  -2.707  26.454  1.00  6.07           C  
ATOM     95  CE1 TYR A  29       1.098  -0.468  24.845  1.00  5.70           C  
ATOM     96  CE2 TYR A  29       0.842  -2.843  25.191  1.00  5.41           C  
ATOM     97  CZ  TYR A  29       0.662  -1.714  24.394  1.00  6.48           C  
ATOM     98  OH  TYR A  29       0.065  -1.823  23.152  1.00  5.97           O  
ATOM     99  N   GLN A  30      -0.210   0.724  28.826  1.00  4.73           N  
ATOM    100  CA  GLN A  30      -0.695   2.096  28.627  1.00  4.77           C  
ATOM    101  C   GLN A  30      -0.877   2.794  29.964  1.00  5.57           C  
ATOM    102  O   GLN A  30      -1.605   2.293  30.836  1.00  5.51           O  
ATOM    103  CB  GLN A  30      -2.034   2.093  27.889  1.00  5.01           C  
ATOM    104  CG  GLN A  30      -2.710   3.469  27.855  1.00  5.56           C  
ATOM    105  CD  GLN A  30      -2.209   4.387  26.739  1.00  4.84           C  
ATOM    106  OE1 GLN A  30      -1.823   5.548  26.976  1.00  7.89           O  
ATOM    107  NE2 GLN A  30      -2.226   3.885  25.524  1.00  3.62           N  
ATOM    108  N   VAL A  31      -0.215   3.938  30.132  1.00  5.45           N  
ATOM    109  CA  VAL A  31      -0.463   4.768  31.314  1.00  6.34           C  
ATOM    110  C   VAL A  31      -1.089   6.107  30.940  1.00  6.17           C  
ATOM    111  O   VAL A  31      -0.992   6.572  29.797  1.00  5.50           O  
ATOM    112  CB  VAL A  31       0.803   5.020  32.187  1.00  7.23           C  
ATOM    113  CG1 VAL A  31       1.527   3.713  32.552  1.00  9.03           C  
ATOM    114  CG2 VAL A  31       1.739   6.009  31.525  1.00  8.41           C  
ATOM    115  N   SER A  32      -1.726   6.716  31.933  1.00  5.48           N  
ATOM    116  CA  SER A  32      -2.190   8.086  31.841  1.00  5.52           C  
ATOM    117  C   SER A  32      -1.323   8.951  32.744  1.00  5.98           C  
ATOM    118  O   SER A  32      -1.094   8.595  33.907  1.00  6.64           O  
ATOM    119  CB  SER A  32      -3.643   8.156  32.303  1.00  5.78           C  
ATOM    120  OG  SER A  32      -4.056   9.497  32.504  1.00  6.40           O  
ATOM    121  N   LEU A  33      -0.829  10.066  32.204  1.00  5.65           N  
ATOM    122  CA  LEU A  33      -0.102  11.043  33.013  1.00  5.91           C  
ATOM    123  C   LEU A  33      -1.114  12.051  33.541  1.00  6.40           C  
ATOM    124  O   LEU A  33      -1.891  12.615  32.767  1.00  6.23           O  
ATOM    125  CB  LEU A  33       0.990  11.749  32.202  1.00  6.34           C  
ATOM    126  CG  LEU A  33       1.996  10.841  31.498  1.00  5.62           C  
ATOM    127  CD1 LEU A  33       3.072  11.708  30.849  1.00  8.34           C  
ATOM    128  CD2 LEU A  33       2.620   9.822  32.455  1.00  6.77           C  
ATOM    129  N   ASN A  34      -1.120  12.257  34.856  1.00  7.01           N  
ATOM    130  CA  ASN A  34      -2.121  13.067  35.506  1.00  7.70           C  
ATOM    131  C   ASN A  34      -1.498  14.182  36.358  1.00  9.16           C  
ATOM    132  O   ASN A  34      -0.594  13.937  37.054  1.00  8.71           O  
ATOM    133  CB  ASN A  34      -3.021  12.135  36.366  1.00  9.61           C  
ATOM    134  CG  ASN A  34      -4.190  12.885  37.054  1.00  7.93           C  
ATOM    135  OD1 ASN A  34      -3.989  13.596  37.954  1.00  8.28           O  
ATOM    136  ND2 ASN A  34      -5.398  12.632  36.590  1.00  9.41           N  
ATOM    137  N   SER A  37      -1.985  15.442  36.170  1.00 10.16           N  
ATOM    138  CA  SER A  37      -1.564  16.544  37.004  1.00  9.64           C  
ATOM    139  C   SER A  37      -2.826  17.264  37.531  1.00  9.08           C  
ATOM    140  O   SER A  37      -2.944  18.411  37.456  1.00  9.31           O  
ATOM    141  CB  SER A  37      -0.670  17.526  36.228  1.00 10.76           C  
ATOM    142  OG  SER A  37      -1.382  18.028  35.162  1.00 13.64           O  
ATOM    143  N   GLY A  38      -3.727  16.459  38.056  1.00  7.81           N  
ATOM    144  CA  GLY A  38      -5.070  16.909  38.444  1.00  7.50           C  
ATOM    145  C   GLY A  38      -6.134  16.508  37.434  1.00  7.19           C  
ATOM    146  O   GLY A  38      -7.341  16.631  37.686  1.00  7.31           O  
ATOM    147  N   TYR A  39      -5.667  16.015  36.285  1.00  6.64           N  
ATOM    148  CA  TYR A  39      -6.481  15.670  35.120  1.00  6.26           C  
ATOM    149  C   TYR A  39      -5.539  14.916  34.185  1.00  5.46           C  
ATOM    150  O   TYR A  39      -4.313  15.120  34.248  1.00  5.70           O  
ATOM    151  CB  TYR A  39      -6.989  16.939  34.416  1.00  6.88           C  
ATOM    152  CG  TYR A  39      -5.897  17.969  34.239  1.00  6.84           C  
ATOM    153  CD1 TYR A  39      -5.674  18.945  35.217  1.00  9.32           C  
ATOM    154  CD2 TYR A  39      -5.047  17.944  33.123  1.00  7.08           C  
ATOM    155  CE1 TYR A  39      -4.644  19.861  35.088  1.00  8.81           C  
ATOM    156  CE2 TYR A  39      -4.013  18.870  32.985  1.00  8.29           C  
ATOM    157  CZ  TYR A  39      -3.824  19.824  33.972  1.00 10.50           C  
ATOM    158  OH  TYR A  39      -2.805  20.743  33.851  1.00 14.06           O  
ATOM    159  N   HIS A  40      -6.102  14.054  33.337  1.00  5.08           N  
ATOM    160  CA  HIS A  40      -5.312  13.380  32.296  1.00  5.16           C  
ATOM    161  C   HIS A  40      -4.786  14.419  31.318  1.00  5.24           C  
ATOM    162  O   HIS A  40      -5.563  15.252  30.838  1.00  6.67           O  
ATOM    163  CB  HIS A  40      -6.185  12.396  31.525  1.00  4.68           C  
ATOM    164  CG  HIS A  40      -5.571  11.949  30.235  1.00  5.44           C  
ATOM    165  ND1 HIS A  40      -4.695  10.889  30.171  1.00  5.18           N  
ATOM    166  CD2 HIS A  40      -5.679  12.430  28.970  1.00  6.48           C  
ATOM    167  CE1 HIS A  40      -4.296  10.727  28.921  1.00  5.61           C  
ATOM    168  NE2 HIS A  40      -4.874  11.650  28.172  1.00  6.49           N  
ATOM    169  N   PHE A  41      -3.496  14.360  30.982  1.00  5.38           N  
ATOM    170  CA  PHE A  41      -2.983  15.289  29.972  1.00  4.78           C  
ATOM    171  C   PHE A  41      -2.119  14.651  28.872  1.00  5.27           C  
ATOM    172  O   PHE A  41      -1.838  15.288  27.856  1.00  6.15           O  
ATOM    173  CB  PHE A  41      -2.244  16.450  30.638  1.00  5.66           C  
ATOM    174  CG  PHE A  41      -0.949  16.054  31.260  1.00  4.64           C  
ATOM    175  CD1 PHE A  41       0.226  16.036  30.497  1.00  6.26           C  
ATOM    176  CD2 PHE A  41      -0.874  15.690  32.617  1.00  3.62           C  
ATOM    177  CE1 PHE A  41       1.444  15.653  31.071  1.00  5.87           C  
ATOM    178  CE2 PHE A  41       0.343  15.323  33.194  1.00  4.88           C  
ATOM    179  CZ  PHE A  41       1.513  15.297  32.412  1.00  5.44           C  
ATOM    180  N   CYS A  42      -1.692  13.409  29.086  1.00  4.96           N  
ATOM    181  CA  CYS A  42      -0.870  12.706  28.090  1.00  4.51           C  
ATOM    182  C   CYS A  42      -0.849  11.217  28.393  1.00  4.24           C  
ATOM    183  O   CYS A  42      -1.149  10.787  29.502  1.00  5.87           O  
ATOM    184  CB  CYS A  42       0.580  13.219  28.106  1.00  5.30           C  
ATOM    185  SG  CYS A  42       0.938  14.661  27.056  1.00  5.71           S  
ATOM    186  N   GLY A  43      -0.486  10.439  27.379  1.00  4.18           N  
ATOM    187  CA  GLY A  43      -0.265   9.019  27.555  1.00  4.91           C  
ATOM    188  C   GLY A  43       1.202   8.711  27.806  1.00  4.70           C  
ATOM    189  O   GLY A  43       2.068   9.592  27.735  1.00  4.95           O  
ATOM    190  N   GLY A  44       1.484   7.448  28.105  1.00  5.01           N  
ATOM    191  CA  GLY A  44       2.861   6.993  28.271  1.00  5.11           C  
ATOM    192  C   GLY A  44       2.858   5.482  28.197  1.00  5.21           C  
ATOM    193  O   GLY A  44       1.791   4.867  28.131  1.00  5.79           O  
ATOM    194  N   SER A  45       4.047   4.887  28.219  1.00  5.49           N  
ATOM    195  CA  SER A  45       4.197   3.426  28.123  1.00  5.53           C  
ATOM    196  C   SER A  45       5.118   2.944  29.217  1.00  5.81           C  
ATOM    197  O   SER A  45       6.235   3.454  29.341  1.00  6.42           O  
ATOM    198  CB  SER A  45       4.800   3.035  26.769  1.00  5.70           C  
ATOM    199  OG  SER A  45       3.979   3.461  25.698  1.00  6.10           O  
ATOM    200  N   LEU A  46       4.660   1.967  29.996  1.00  5.72           N  
ATOM    201  CA  LEU A  46       5.469   1.390  31.063  1.00  6.17           C  
ATOM    202  C   LEU A  46       6.477   0.457  30.424  1.00  6.54           C  
ATOM    203  O   LEU A  46       6.087  -0.469  29.731  1.00  6.93           O  
ATOM    204  CB  LEU A  46       4.582   0.615  32.039  1.00  6.14           C  
ATOM    205  CG  LEU A  46       5.242   0.140  33.337  1.00  7.20           C  
ATOM    206  CD1 LEU A  46       5.569   1.319  34.257  1.00  7.81           C  
ATOM    207  CD2 LEU A  46       4.329  -0.836  34.050  1.00  8.48           C  
ATOM    208  N   ILE A  47       7.770   0.713  30.639  1.00  6.89           N  
ATOM    209  CA  ILE A  47       8.809  -0.135  30.025  1.00  7.81           C  
ATOM    210  C   ILE A  47       9.567  -1.018  31.025  1.00  7.91           C  
ATOM    211  O   ILE A  47      10.276  -1.943  30.623  1.00  8.83           O  
ATOM    212  CB  ILE A  47       9.791   0.664  29.134  1.00  7.91           C  
ATOM    213  CG1 ILE A  47      10.507   1.747  29.949  1.00  8.82           C  
ATOM    214  CG2 ILE A  47       9.046   1.262  27.925  1.00  8.56           C  
ATOM    215  CD1 ILE A  47      11.748   2.280  29.272  1.00  9.90           C  
ATOM    216  N   ASN A  48       9.441  -0.710  32.314  1.00  8.52           N  
ATOM    217  CA  ASN A  48       9.787  -1.649  33.391  1.00  8.59           C  
ATOM    218  C   ASN A  48       9.001  -1.263  34.641  1.00  8.78           C  
ATOM    219  O   ASN A  48       8.155  -0.379  34.572  1.00  9.41           O  
ATOM    220  CB  ASN A  48      11.314  -1.807  33.632  1.00  8.96           C  
ATOM    221  CG  ASN A  48      12.022  -0.510  34.057  1.00 10.23           C  
ATOM    222  OD1 ASN A  48      13.200  -0.306  33.716  1.00 14.31           O  
ATOM    223  ND2 ASN A  48      11.361   0.317  34.827  1.00  8.05           N  
ATOM    224  N   SER A  49       9.255  -1.902  35.777  1.00  8.92           N  
ATOM    225  CA  SER A  49       8.442  -1.613  36.957  1.00  9.24           C  
ATOM    226  C   SER A  49       8.531  -0.172  37.473  1.00  8.81           C  
ATOM    227  O   SER A  49       7.662   0.257  38.235  1.00  9.85           O  
ATOM    228  CB  SER A  49       8.777  -2.578  38.104  1.00  9.30           C  
ATOM    229  OG  SER A  49      10.065  -2.313  38.635  1.00 10.93           O  
ATOM    230  N   GLN A  50       9.558   0.578  37.065  1.00  8.91           N  
ATOM    231  CA  GLN A  50       9.763   1.916  37.634  1.00  8.47           C  
ATOM    232  C   GLN A  50       9.905   3.055  36.613  1.00  7.70           C  
ATOM    233  O   GLN A  50      10.104   4.206  37.000  1.00  7.91           O  
ATOM    234  CB  GLN A  50      10.946   1.921  38.623  1.00  9.70           C  
ATOM    235  CG  GLN A  50      10.786   2.953  39.731  1.00 12.03           C  
ATOM    236  CD  GLN A  50      11.649   2.688  40.955  1.00 14.80           C  
ATOM    237  OE1 GLN A  50      12.434   1.725  41.000  1.00 15.95           O  
ATOM    238  NE2 GLN A  50      11.516   3.556  41.959  1.00 15.19           N  
ATOM    239  N   TRP A  51       9.776   2.739  35.329  1.00  6.93           N  
ATOM    240  CA  TRP A  51      10.039   3.739  34.284  1.00  6.13           C  
ATOM    241  C   TRP A  51       8.987   3.765  33.196  1.00  6.21           C  
ATOM    242  O   TRP A  51       8.535   2.713  32.723  1.00  6.20           O  
ATOM    243  CB  TRP A  51      11.392   3.493  33.610  1.00  6.30           C  
ATOM    244  CG  TRP A  51      12.569   3.871  34.465  1.00  6.85           C  
ATOM    245  CD1 TRP A  51      13.237   3.055  35.337  1.00  8.35           C  
ATOM    246  CD2 TRP A  51      13.225   5.148  34.528  1.00  6.75           C  
ATOM    247  NE1 TRP A  51      14.264   3.742  35.938  1.00  7.42           N  
ATOM    248  CE2 TRP A  51      14.287   5.023  35.453  1.00  7.47           C  
ATOM    249  CE3 TRP A  51      13.027   6.383  33.885  1.00  7.30           C  
ATOM    250  CZ2 TRP A  51      15.145   6.083  35.761  1.00  7.65           C  
ATOM    251  CZ3 TRP A  51      13.880   7.445  34.194  1.00  7.87           C  
ATOM    252  CH2 TRP A  51      14.931   7.284  35.125  1.00  7.35           C  
ATOM    253  N   VAL A  52       8.633   4.987  32.798  1.00  5.71           N  
ATOM    254  CA  VAL A  52       7.662   5.231  31.735  1.00  6.08           C  
ATOM    255  C   VAL A  52       8.304   6.049  30.601  1.00  6.20           C  
ATOM    256  O   VAL A  52       9.070   6.979  30.874  1.00  6.24           O  
ATOM    257  CB  VAL A  52       6.436   5.985  32.315  1.00  6.06           C  
ATOM    258  CG1 VAL A  52       5.556   6.596  31.207  1.00  6.92           C  
ATOM    259  CG2 VAL A  52       5.607   5.044  33.204  1.00  6.71           C  
ATOM    260  N   VAL A  53       8.014   5.670  29.350  1.00  5.80           N  
ATOM    261  CA  VAL A  53       8.393   6.451  28.167  1.00  6.41           C  
ATOM    262  C   VAL A  53       7.203   7.294  27.715  1.00  5.77           C  
ATOM    263  O   VAL A  53       6.083   6.790  27.585  1.00  5.90           O  
ATOM    264  CB  VAL A  53       8.838   5.540  26.979  1.00  6.93           C  
ATOM    265  CG1 VAL A  53       9.029   6.352  25.690  1.00  8.95           C  
ATOM    266  CG2 VAL A  53      10.125   4.830  27.306  1.00  8.92           C  
ATOM    267  N   SER A  54       7.459   8.574  27.469  1.00  5.17           N  
ATOM    268  CA  SER A  54       6.420   9.469  26.957  1.00  4.38           C  
ATOM    269  C   SER A  54       7.031  10.461  25.965  1.00  4.29           C  
ATOM    270  O   SER A  54       8.179  10.281  25.550  1.00  3.72           O  
ATOM    271  CB  SER A  54       5.699  10.176  28.121  1.00  4.49           C  
ATOM    272  OG  SER A  54       4.559  10.878  27.642  1.00  3.89           O  
ATOM    273  N   ALA A  55       6.255  11.472  25.561  1.00  4.36           N  
ATOM    274  CA  ALA A  55       6.738  12.502  24.647  1.00  4.22           C  
ATOM    275  C   ALA A  55       7.336  13.655  25.444  1.00  4.34           C  
ATOM    276  O   ALA A  55       6.798  14.045  26.488  1.00  4.83           O  
ATOM    277  CB  ALA A  55       5.597  13.031  23.788  1.00  4.81           C  
ATOM    278  N   ALA A  56       8.442  14.210  24.953  1.00  4.66           N  
ATOM    279  CA  ALA A  56       9.047  15.367  25.617  1.00  4.78           C  
ATOM    280  C   ALA A  56       8.089  16.546  25.692  1.00  4.85           C  
ATOM    281  O   ALA A  56       8.136  17.308  26.651  1.00  5.47           O  
ATOM    282  CB  ALA A  56      10.347  15.772  24.931  1.00  5.46           C  
ATOM    283  N   HIS A  57       7.224  16.688  24.689  1.00  5.22           N  
ATOM    284  CA  HIS A  57       6.294  17.814  24.684  1.00  5.25           C  
ATOM    285  C   HIS A  57       5.213  17.655  25.760  1.00  5.81           C  
ATOM    286  O   HIS A  57       4.444  18.596  26.005  1.00  6.53           O  
ATOM    287  CB  HIS A  57       5.728  18.113  23.280  1.00  5.49           C  
ATOM    288  CG  HIS A  57       4.525  17.308  22.890  1.00  5.74           C  
ATOM    289  ND1 HIS A  57       4.595  16.213  22.048  1.00  5.34           N  
ATOM    290  CD2 HIS A  57       3.212  17.480  23.175  1.00  6.27           C  
ATOM    291  CE1 HIS A  57       3.376  15.739  21.849  1.00  6.93           C  
ATOM    292  NE2 HIS A  57       2.520  16.491  22.521  1.00  7.35           N  
ATOM    293  N   CYS A  58       5.193  16.492  26.420  1.00  6.28           N  
ATOM    294  CA  CYS A  58       4.321  16.254  27.564  1.00  6.98           C  
ATOM    295  C   CYS A  58       4.957  16.661  28.885  1.00  7.67           C  
ATOM    296  O   CYS A  58       4.316  16.556  29.929  1.00  8.35           O  
ATOM    297  CB  CYS A  58       3.931  14.777  27.668  1.00  6.76           C  
ATOM    298  SG  CYS A  58       2.812  14.208  26.363  1.00  6.92           S  
ATOM    299  N   TYR A  59       6.216  17.094  28.856  1.00  7.42           N  
ATOM    300  CA  TYR A  59       6.896  17.454  30.089  1.00  7.94           C  
ATOM    301  C   TYR A  59       6.119  18.485  30.911  1.00  8.04           C  
ATOM    302  O   TYR A  59       5.622  19.470  30.376  1.00  8.10           O  
ATOM    303  CB  TYR A  59       8.326  17.985  29.833  1.00  8.02           C  
ATOM    304  CG  TYR A  59       8.847  18.638  31.087  1.00  8.60           C  
ATOM    305  CD1 TYR A  59       8.765  20.009  31.250  1.00  8.60           C  
ATOM    306  CD2 TYR A  59       9.306  17.865  32.161  1.00  8.82           C  
ATOM    307  CE1 TYR A  59       9.170  20.621  32.436  1.00  8.99           C  
ATOM    308  CE2 TYR A  59       9.728  18.471  33.351  1.00 10.09           C  
ATOM    309  CZ  TYR A  59       9.650  19.849  33.461  1.00 10.44           C  
ATOM    310  OH  TYR A  59      10.039  20.490  34.609  1.00 14.26           O  
ATOM    311  N   LYS A  60       6.036  18.222  32.213  1.00  8.37           N  
ATOM    312  CA  LYS A  60       5.659  19.219  33.214  1.00  8.84           C  
ATOM    313  C   LYS A  60       6.074  18.683  34.575  1.00  9.35           C  
ATOM    314  O   LYS A  60       6.398  17.502  34.704  1.00  9.72           O  
ATOM    315  CB  LYS A  60       4.157  19.507  33.184  1.00  9.73           C  
ATOM    316  CG  LYS A  60       3.296  18.298  33.439  1.00  9.21           C  
ATOM    317  CD  LYS A  60       1.872  18.692  33.802  1.00 10.30           C  
ATOM    318  CE  LYS A  60       1.101  19.194  32.588  1.00 10.21           C  
ATOM    319  NZ  LYS A  60      -0.300  19.583  32.967  1.00 11.60           N  
ATOM    320  N   SER A  61       6.097  19.550  35.586  1.00 10.04           N  
ATOM    321  CA  SER A  61       6.386  19.075  36.940  1.00 11.04           C  
ATOM    322  C   SER A  61       5.108  18.537  37.581  1.00 10.52           C  
ATOM    323  O   SER A  61       4.006  18.818  37.109  1.00 11.00           O  
ATOM    324  CB  SER A  61       7.002  20.186  37.792  1.00 11.91           C  
ATOM    325  OG  SER A  61       6.083  21.239  37.947  1.00 14.71           O  
ATOM    326  N   GLY A  62       5.260  17.732  38.628  1.00 10.53           N  
ATOM    327  CA  GLY A  62       4.114  17.285  39.432  1.00 10.92           C  
ATOM    328  C   GLY A  62       3.263  16.232  38.740  1.00 10.70           C  
ATOM    329  O   GLY A  62       2.028  16.273  38.787  1.00 12.24           O  
ATOM    330  N   ILE A  63       3.924  15.279  38.102  1.00  9.85           N  
ATOM    331  CA  ILE A  63       3.216  14.232  37.366  1.00  8.40           C  
ATOM    332  C   ILE A  63       2.902  13.071  38.300  1.00  8.40           C  
ATOM    333  O   ILE A  63       3.775  12.622  39.042  1.00  8.69           O  
ATOM    334  CB  ILE A  63       4.069  13.730  36.165  1.00  8.15           C  
ATOM    335  CG1 ILE A  63       4.270  14.873  35.154  1.00  7.51           C  
ATOM    336  CG2 ILE A  63       3.444  12.489  35.505  1.00  9.43           C  
ATOM    337  CD1 ILE A  63       5.119  14.505  33.921  1.00 10.37           C  
ATOM    338  N   GLN A  64       1.649  12.617  38.270  1.00  7.90           N  
ATOM    339  CA  GLN A  64       1.279  11.327  38.862  1.00  7.05           C  
ATOM    340  C   GLN A  64       0.998  10.351  37.725  1.00  6.77           C  
ATOM    341  O   GLN A  64       0.191  10.644  36.837  1.00  6.99           O  
ATOM    342  CB  GLN A  64       0.036  11.448  39.746  1.00  7.39           C  
ATOM    343  CG  GLN A  64      -0.301  10.179  40.535  1.00  7.47           C  
ATOM    344  CD  GLN A  64      -1.637  10.308  41.228  1.00  8.93           C  
ATOM    345  OE1 GLN A  64      -2.661  10.546  40.583  1.00  9.96           O  
ATOM    346  NE2 GLN A  64      -1.635  10.170  42.552  1.00 10.46           N  
ATOM    347  N   VAL A  65       1.666   9.200  37.755  1.00  6.22           N  
ATOM    348  CA  VAL A  65       1.471   8.178  36.736  1.00  6.32           C  
ATOM    349  C   VAL A  65       0.316   7.281  37.162  1.00  6.31           C  
ATOM    350  O   VAL A  65       0.276   6.801  38.294  1.00  6.64           O  
ATOM    351  CB  VAL A  65       2.750   7.360  36.520  1.00  6.65           C  
ATOM    352  CG1 VAL A  65       2.521   6.228  35.526  1.00  6.91           C  
ATOM    353  CG2 VAL A  65       3.872   8.267  36.021  1.00  7.30           C  
ATOM    354  N   ARG A  66      -0.626   7.073  36.251  1.00  5.37           N  
ATOM    355  CA  ARG A  66      -1.794   6.256  36.554  1.00  5.59           C  
ATOM    356  C   ARG A  66      -1.781   5.009  35.694  1.00  5.94           C  
ATOM    357  O   ARG A  66      -1.903   5.074  34.465  1.00  5.76           O  
ATOM    358  CB  ARG A  66      -3.078   7.074  36.388  1.00  5.58           C  
ATOM    359  CG  ARG A  66      -3.118   8.198  37.407  1.00  4.92           C  
ATOM    360  CD  ARG A  66      -4.474   8.844  37.495  1.00  5.22           C  
ATOM    361  NE  ARG A  66      -4.539   9.606  38.739  1.00  5.29           N  
ATOM    362  CZ  ARG A  66      -5.669  10.000  39.313  1.00  5.94           C  
ATOM    363  NH1 ARG A  66      -6.840   9.744  38.720  1.00  7.73           N  
ATOM    364  NH2 ARG A  66      -5.623  10.657  40.467  1.00  7.35           N  
ATOM    365  N   LEU A  67      -1.564   3.873  36.357  1.00  6.12           N  
ATOM    366  CA  LEU A  67      -1.515   2.569  35.690  1.00  6.35           C  
ATOM    367  C   LEU A  67      -2.812   1.765  35.892  1.00  7.10           C  
ATOM    368  O   LEU A  67      -3.502   2.035  36.791  1.00  6.35           O  
ATOM    369  CB  LEU A  67      -0.346   1.780  36.320  1.00  7.11           C  
ATOM    370  CG  LEU A  67       1.017   2.487  36.276  1.00  7.66           C  
ATOM    371  CD1 LEU A  67       1.475   3.050  37.554  1.00 11.09           C  
ATOM    372  CD2 LEU A  67       2.121   1.623  35.760  1.00 12.88           C  
ATOM    373  N   GLY A  69      -3.015   0.815  35.028  1.00 11.62           N  
ATOM    374  CA  GLY A  69      -4.131  -0.053  35.212  1.00 10.61           C  
ATOM    375  C   GLY A  69      -5.494   0.611  34.972  1.00  9.73           C  
ATOM    376  O   GLY A  69      -6.503   0.187  35.425  1.00  9.97           O  
ATOM    377  N   GLU A  70      -5.448   1.637  34.167  1.00  9.01           N  
ATOM    378  CA  GLU A  70      -6.631   2.475  33.945  1.00  8.66           C  
ATOM    379  C   GLU A  70      -7.440   2.038  32.733  1.00  8.47           C  
ATOM    380  O   GLU A  70      -6.871   1.754  31.664  1.00  9.39           O  
ATOM    381  CB  GLU A  70      -6.225   3.937  33.747  1.00  9.50           C  
ATOM    382  CG  GLU A  70      -5.808   4.624  35.037  1.00 10.54           C  
ATOM    383  CD  GLU A  70      -7.021   5.207  35.767  1.00  8.50           C  
ATOM    384  OE1 GLU A  70      -8.140   4.682  35.573  1.00  8.67           O  
ATOM    385  OE2 GLU A  70      -6.848   6.195  36.512  1.00  7.05           O  
ATOM    386  N   ASP A  71      -8.762   2.007  32.894  1.00  7.33           N  
ATOM    387  CA  ASP A  71      -9.643   2.027  31.737  1.00  7.43           C  
ATOM    388  C   ASP A  71     -10.430   3.338  31.738  1.00  7.10           C  
ATOM    389  O   ASP A  71     -10.031   4.286  31.058  1.00  7.27           O  
ATOM    390  CB  ASP A  71     -10.555   0.794  31.630  1.00  7.57           C  
ATOM    391  CG  ASP A  71     -11.238   0.716  30.276  1.00  8.67           C  
ATOM    392  OD1 ASP A  71     -10.549   0.960  29.259  1.00  8.44           O  
ATOM    393  OD2 ASP A  71     -12.462   0.452  30.234  1.00 10.22           O  
ATOM    394  N   ASN A  72     -11.514   3.413  32.510  1.00  6.48           N  
ATOM    395  CA  ASN A  72     -12.208   4.689  32.669  1.00  6.38           C  
ATOM    396  C   ASN A  72     -11.394   5.614  33.570  1.00  6.50           C  
ATOM    397  O   ASN A  72     -11.251   5.351  34.770  1.00  6.75           O  
ATOM    398  CB  ASN A  72     -13.622   4.494  33.219  1.00  6.57           C  
ATOM    399  CG  ASN A  72     -14.463   5.760  33.115  1.00  7.85           C  
ATOM    400  OD1 ASN A  72     -13.987   6.866  33.408  1.00  8.24           O  
ATOM    401  ND2 ASN A  72     -15.716   5.609  32.670  1.00  9.25           N  
ATOM    402  N   ILE A  73     -10.844   6.688  33.002  1.00  6.62           N  
ATOM    403  CA  ILE A  73      -9.963   7.569  33.783  1.00  6.93           C  
ATOM    404  C   ILE A  73     -10.718   8.467  34.767  1.00  6.90           C  
ATOM    405  O   ILE A  73     -10.090   9.176  35.559  1.00  7.22           O  
ATOM    406  CB  ILE A  73      -8.993   8.417  32.911  1.00  7.10           C  
ATOM    407  CG1 ILE A  73      -9.758   9.127  31.791  1.00  8.13           C  
ATOM    408  CG2 ILE A  73      -7.816   7.558  32.401  1.00  6.39           C  
ATOM    409  CD1 ILE A  73      -9.009  10.300  31.168  1.00  9.23           C  
ATOM    410  N   ASN A  74     -12.052   8.409  34.729  1.00  6.95           N  
ATOM    411  CA  ASN A  74     -12.874   9.204  35.635  1.00  7.02           C  
ATOM    412  C   ASN A  74     -13.570   8.389  36.726  1.00  7.09           C  
ATOM    413  O   ASN A  74     -14.297   8.956  37.546  1.00  7.77           O  
ATOM    414  CB  ASN A  74     -13.914  10.020  34.857  1.00  7.03           C  
ATOM    415  CG  ASN A  74     -13.371  11.356  34.383  1.00  9.68           C  
ATOM    416  OD1 ASN A  74     -12.629  12.038  35.105  1.00  9.14           O  
ATOM    417  ND2 ASN A  74     -13.761  11.755  33.180  1.00 12.15           N  
ATOM    418  N   VAL A  75     -13.370   7.069  36.716  1.00  6.72           N  
ATOM    419  CA  VAL A  75     -13.988   6.170  37.689  1.00  6.63           C  
ATOM    420  C   VAL A  75     -12.941   5.207  38.244  1.00  7.09           C  
ATOM    421  O   VAL A  75     -12.202   4.604  37.469  1.00  6.51           O  
ATOM    422  CB  VAL A  75     -15.137   5.337  37.049  1.00  6.88           C  
ATOM    423  CG1 VAL A  75     -15.763   4.366  38.076  1.00  7.03           C  
ATOM    424  CG2 VAL A  75     -16.202   6.256  36.440  1.00  7.68           C  
ATOM    425  N   VAL A  76     -12.888   5.054  39.571  1.00  7.39           N  
ATOM    426  CA  VAL A  76     -12.013   4.031  40.171  1.00  8.05           C  
ATOM    427  C   VAL A  76     -12.690   2.678  39.990  1.00  8.52           C  
ATOM    428  O   VAL A  76     -13.770   2.436  40.543  1.00  8.91           O  
ATOM    429  CB  VAL A  76     -11.691   4.314  41.657  1.00  8.31           C  
ATOM    430  CG1 VAL A  76     -10.785   3.206  42.241  1.00  9.48           C  
ATOM    431  CG2 VAL A  76     -11.030   5.684  41.813  1.00  8.34           C  
ATOM    432  N   GLU A  77     -12.064   1.817  39.185  1.00  8.23           N  
ATOM    433  CA  GLU A  77     -12.660   0.539  38.776  1.00  8.91           C  
ATOM    434  C   GLU A  77     -12.036  -0.695  39.425  1.00  9.14           C  
ATOM    435  O   GLU A  77     -12.610  -1.788  39.340  1.00 10.29           O  
ATOM    436  CB  GLU A  77     -12.659   0.408  37.247  1.00  8.71           C  
ATOM    437  CG  GLU A  77     -13.488   1.488  36.563  1.00  8.81           C  
ATOM    438  CD  GLU A  77     -13.498   1.383  35.047  1.00 10.90           C  
ATOM    439  OE1 GLU A  77     -14.605   1.261  34.472  1.00 14.14           O  
ATOM    440  OE2 GLU A  77     -12.416   1.438  34.425  1.00  8.43           O  
ATOM    441  N   GLY A  78     -10.875  -0.527  40.057  1.00  8.75           N  
ATOM    442  CA  GLY A  78     -10.307  -1.593  40.891  1.00  9.06           C  
ATOM    443  C   GLY A  78      -8.937  -2.125  40.511  1.00  9.59           C  
ATOM    444  O   GLY A  78      -8.362  -2.923  41.255  1.00 10.87           O  
ATOM    445  N   ASN A  79      -8.409  -1.706  39.361  1.00  9.03           N  
ATOM    446  CA  ASN A  79      -7.099  -2.199  38.929  1.00  8.60           C  
ATOM    447  C   ASN A  79      -6.032  -1.111  38.811  1.00  8.27           C  
ATOM    448  O   ASN A  79      -4.922  -1.373  38.347  1.00  8.32           O  
ATOM    449  CB  ASN A  79      -7.221  -2.972  37.614  1.00  9.12           C  
ATOM    450  CG  ASN A  79      -8.050  -4.226  37.766  1.00 10.21           C  
ATOM    451  OD1 ASN A  79      -9.191  -4.306  37.282  1.00 12.19           O  
ATOM    452  ND2 ASN A  79      -7.491  -5.210  38.454  1.00 11.62           N  
ATOM    453  N   GLU A  80      -6.370   0.094  39.257  1.00  8.08           N  
ATOM    454  CA  GLU A  80      -5.461   1.224  39.187  1.00  8.16           C  
ATOM    455  C   GLU A  80      -4.299   1.133  40.158  1.00  8.04           C  
ATOM    456  O   GLU A  80      -4.427   0.618  41.277  1.00  9.20           O  
ATOM    457  CB  GLU A  80      -6.196   2.536  39.477  1.00  7.80           C  
ATOM    458  CG  GLU A  80      -7.272   2.860  38.457  1.00  8.17           C  
ATOM    459  CD  GLU A  80      -8.668   2.403  38.861  1.00  7.72           C  
ATOM    460  OE1 GLU A  80      -8.831   1.564  39.782  1.00  7.72           O  
ATOM    461  OE2 GLU A  80      -9.619   2.878  38.205  1.00  6.79           O  
ATOM    462  N   GLN A  81      -3.163   1.660  39.719  1.00  7.58           N  
ATOM    463  CA  GLN A  81      -2.084   2.041  40.632  1.00  7.50           C  
ATOM    464  C   GLN A  81      -1.699   3.473  40.302  1.00  7.54           C  
ATOM    465  O   GLN A  81      -1.365   3.771  39.151  1.00  8.20           O  
ATOM    466  CB  GLN A  81      -0.870   1.121  40.489  1.00  7.63           C  
ATOM    467  CG  GLN A  81      -1.198  -0.351  40.757  1.00  7.83           C  
ATOM    468  CD  GLN A  81      -0.023  -1.288  40.513  1.00  8.60           C  
ATOM    469  OE1 GLN A  81       1.119  -1.008  40.915  1.00  9.90           O  
ATOM    470  NE2 GLN A  81      -0.300  -2.409  39.870  1.00  8.99           N  
ATOM    471  N   PHE A  82      -1.759   4.353  41.302  1.00  6.91           N  
ATOM    472  CA  PHE A  82      -1.382   5.749  41.127  1.00  7.11           C  
ATOM    473  C   PHE A  82      -0.049   5.947  41.834  1.00  7.19           C  
ATOM    474  O   PHE A  82       0.056   5.706  43.045  1.00  7.95           O  
ATOM    475  CB  PHE A  82      -2.398   6.679  41.790  1.00  6.52           C  
ATOM    476  CG  PHE A  82      -3.802   6.645  41.201  1.00  7.45           C  
ATOM    477  CD1 PHE A  82      -4.836   7.289  41.886  1.00  8.30           C  
ATOM    478  CD2 PHE A  82      -4.099   5.996  40.000  1.00  6.99           C  
ATOM    479  CE1 PHE A  82      -6.138   7.293  41.395  1.00  8.34           C  
ATOM    480  CE2 PHE A  82      -5.414   5.997  39.490  1.00  7.49           C  
ATOM    481  CZ  PHE A  82      -6.433   6.649  40.204  1.00  8.23           C  
ATOM    482  N   ILE A  83       0.971   6.367  41.090  1.00  7.04           N  
ATOM    483  CA  ILE A  83       2.315   6.506  41.650  1.00  7.27           C  
ATOM    484  C   ILE A  83       2.915   7.820  41.152  1.00  7.17           C  
ATOM    485  O   ILE A  83       2.994   8.047  39.945  1.00  7.40           O  
ATOM    486  CB  ILE A  83       3.232   5.324  41.235  1.00  6.74           C  
ATOM    487  CG1 ILE A  83       2.605   3.975  41.620  1.00  7.23           C  
ATOM    488  CG2 ILE A  83       4.637   5.470  41.875  1.00  7.43           C  
ATOM    489  CD1 ILE A  83       3.318   2.766  41.036  1.00  8.53           C  
ATOM    490  N   SER A  84       3.317   8.685  42.090  1.00  7.63           N  
ATOM    491  CA  SER A  84       3.944   9.955  41.730  1.00  8.41           C  
ATOM    492  C   SER A  84       5.297   9.727  41.057  1.00  7.80           C  
ATOM    493  O   SER A  84       6.016   8.780  41.400  1.00  8.45           O  
ATOM    494  CB  SER A  84       4.128  10.827  42.973  1.00  8.65           C  
ATOM    495  OG  SER A  84       2.869  11.199  43.509  1.00 12.42           O  
ATOM    496  N   ALA A  85       5.630  10.586  40.100  1.00  8.13           N  
ATOM    497  CA  ALA A  85       6.961  10.554  39.483  1.00  8.52           C  
ATOM    498  C   ALA A  85       7.987  11.164  40.428  1.00  8.66           C  
ATOM    499  O   ALA A  85       7.708  12.161  41.101  1.00  9.42           O  
ATOM    500  CB  ALA A  85       6.961  11.305  38.164  1.00  8.76           C  
ATOM    501  N   SER A  86       9.173  10.563  40.477  1.00  8.45           N  
ATOM    502  CA  SER A  86      10.278  11.118  41.260  1.00  8.40           C  
ATOM    503  C   SER A  86      11.186  12.008  40.422  1.00  8.54           C  
ATOM    504  O   SER A  86      11.857  12.898  40.952  1.00  8.76           O  
ATOM    505  CB  SER A  86      11.111   9.997  41.875  1.00  8.60           C  
ATOM    506  OG  SER A  86      11.581   9.124  40.865  1.00  8.75           O  
ATOM    507  N   LYS A  87      11.234  11.743  39.121  1.00  8.23           N  
ATOM    508  CA  LYS A  87      12.086  12.514  38.220  1.00  8.56           C  
ATOM    509  C   LYS A  87      11.628  12.338  36.787  1.00  8.53           C  
ATOM    510  O   LYS A  87      11.034  11.322  36.433  1.00  8.56           O  
ATOM    511  CB  LYS A  87      13.572  12.111  38.365  1.00  9.30           C  
ATOM    512  CG  LYS A  87      13.920  10.696  37.919  1.00 11.26           C  
ATOM    513  CD  LYS A  87      15.391  10.347  38.200  1.00 11.51           C  
ATOM    514  CE  LYS A  87      15.674  10.125  39.701  1.00 12.99           C  
ATOM    515  NZ  LYS A  87      17.022   9.490  39.952  1.00 12.48           N  
ATOM    516  N   SER A  88      11.882  13.349  35.967  1.00  8.36           N  
ATOM    517  CA ASER A  88      11.633  13.265  34.534  0.50  8.38           C  
ATOM    518  CA BSER A  88      11.658  13.218  34.537  0.50  8.60           C  
ATOM    519  C   SER A  88      12.917  13.650  33.813  1.00  7.99           C  
ATOM    520  O   SER A  88      13.682  14.488  34.310  1.00  8.63           O  
ATOM    521  CB ASER A  88      10.485  14.190  34.120  0.50  8.62           C  
ATOM    522  CB BSER A  88      10.454  14.032  34.072  0.50  8.92           C  
ATOM    523  OG ASER A  88       9.230  13.673  34.540  0.50  8.74           O  
ATOM    524  OG BSER A  88      10.693  15.412  34.227  0.50 10.37           O  
ATOM    525  N   ILE A  89      13.158  13.027  32.667  1.00  7.07           N  
ATOM    526  CA  ILE A  89      14.349  13.307  31.876  1.00  6.94           C  
ATOM    527  C   ILE A  89      13.910  13.465  30.436  1.00  6.51           C  
ATOM    528  O   ILE A  89      13.558  12.486  29.770  1.00  6.28           O  
ATOM    529  CB  ILE A  89      15.385  12.176  31.996  1.00  7.06           C  
ATOM    530  CG1 ILE A  89      15.741  11.960  33.480  1.00  8.10           C  
ATOM    531  CG2 ILE A  89      16.633  12.461  31.121  1.00  7.37           C  
ATOM    532  CD1 ILE A  89      16.543  10.746  33.772  1.00 11.29           C  
ATOM    533  N   VAL A  90      13.921  14.713  29.972  1.00  6.12           N  
ATOM    534  CA  VAL A  90      13.643  15.036  28.583  1.00  6.02           C  
ATOM    535  C   VAL A  90      14.901  14.719  27.760  1.00  5.67           C  
ATOM    536  O   VAL A  90      16.027  14.915  28.229  1.00  6.03           O  
ATOM    537  CB  VAL A  90      13.247  16.540  28.466  1.00  6.37           C  
ATOM    538  CG1 VAL A  90      13.303  17.031  27.029  1.00  6.49           C  
ATOM    539  CG2 VAL A  90      11.854  16.778  29.029  1.00  5.72           C  
ATOM    540  N   HIS A  91      14.711  14.212  26.541  1.00  5.47           N  
ATOM    541  CA  HIS A  91      15.845  13.881  25.692  1.00  5.69           C  
ATOM    542  C   HIS A  91      16.804  15.066  25.587  1.00  6.09           C  
ATOM    543  O   HIS A  91      16.354  16.213  25.463  1.00  5.96           O  
ATOM    544  CB  HIS A  91      15.387  13.436  24.303  1.00  5.90           C  
ATOM    545  CG  HIS A  91      16.481  12.791  23.518  1.00  6.56           C  
ATOM    546  ND1 HIS A  91      17.391  13.518  22.778  1.00  7.20           N  
ATOM    547  CD2 HIS A  91      16.858  11.494  23.416  1.00  6.49           C  
ATOM    548  CE1 HIS A  91      18.271  12.690  22.240  1.00  7.26           C  
ATOM    549  NE2 HIS A  91      17.974  11.459  22.617  1.00  8.51           N  
ATOM    550  N   PRO A  92      18.124  14.807  25.653  1.00  6.04           N  
ATOM    551  CA  PRO A  92      19.057  15.941  25.617  1.00  6.47           C  
ATOM    552  C   PRO A  92      18.981  16.821  24.363  1.00  6.82           C  
ATOM    553  O   PRO A  92      19.353  18.001  24.432  1.00  8.18           O  
ATOM    554  CB  PRO A  92      20.442  15.273  25.731  1.00  6.53           C  
ATOM    555  CG  PRO A  92      20.237  13.855  25.344  1.00  7.13           C  
ATOM    556  CD  PRO A  92      18.832  13.516  25.799  1.00  6.74           C  
ATOM    557  N   SER A  93      18.489  16.275  23.250  1.00  6.95           N  
ATOM    558  CA  SER A  93      18.430  17.017  21.983  1.00  6.66           C  
ATOM    559  C   SER A  93      17.005  17.385  21.558  1.00  6.30           C  
ATOM    560  O   SER A  93      16.763  17.723  20.386  1.00  6.45           O  
ATOM    561  CB  SER A  93      19.130  16.222  20.880  1.00  7.82           C  
ATOM    562  OG  SER A  93      20.485  16.001  21.244  1.00  9.04           O  
ATOM    563  N   TYR A  94      16.071  17.321  22.506  1.00  5.49           N  
ATOM    564  CA  TYR A  94      14.688  17.660  22.178  1.00  5.28           C  
ATOM    565  C   TYR A  94      14.611  19.107  21.702  1.00  5.63           C  
ATOM    566  O   TYR A  94      15.071  20.017  22.395  1.00  6.28           O  
ATOM    567  CB  TYR A  94      13.792  17.466  23.392  1.00  5.19           C  
ATOM    568  CG  TYR A  94      12.396  18.008  23.208  1.00  4.92           C  
ATOM    569  CD1 TYR A  94      11.867  18.945  24.094  1.00  5.27           C  
ATOM    570  CD2 TYR A  94      11.597  17.558  22.159  1.00  4.78           C  
ATOM    571  CE1 TYR A  94      10.578  19.423  23.937  1.00  5.72           C  
ATOM    572  CE2 TYR A  94      10.317  18.022  21.991  1.00  4.43           C  
ATOM    573  CZ  TYR A  94       9.811  18.963  22.879  1.00  5.11           C  
ATOM    574  OH  TYR A  94       8.527  19.440  22.712  1.00  7.09           O  
ATOM    575  N   ASN A  95      14.016  19.306  20.526  1.00  5.49           N  
ATOM    576  CA  ASN A  95      13.720  20.648  20.027  1.00  5.93           C  
ATOM    577  C   ASN A  95      12.210  20.831  19.975  1.00  5.77           C  
ATOM    578  O   ASN A  95      11.523  20.167  19.198  1.00  5.83           O  
ATOM    579  CB  ASN A  95      14.330  20.831  18.639  1.00  6.12           C  
ATOM    580  CG  ASN A  95      14.088  22.208  18.069  1.00  8.24           C  
ATOM    581  OD1 ASN A  95      12.975  22.712  18.101  1.00  9.21           O  
ATOM    582  ND2 ASN A  95      15.138  22.827  17.532  1.00 10.45           N  
ATOM    583  N   SER A  96      11.695  21.738  20.794  1.00  5.70           N  
ATOM    584  CA  SER A  96      10.239  21.893  20.915  1.00  6.32           C  
ATOM    585  C   SER A  96       9.608  22.586  19.703  1.00  6.56           C  
ATOM    586  O   SER A  96       8.383  22.518  19.498  1.00  7.29           O  
ATOM    587  CB  SER A  96       9.895  22.638  22.199  1.00  6.85           C  
ATOM    588  OG  SER A  96      10.457  23.935  22.185  1.00  8.52           O  
ATOM    589  N   ASN A  97      10.436  23.250  18.895  1.00  6.29           N  
ATOM    590  CA  ASN A  97       9.935  23.916  17.693  1.00  6.61           C  
ATOM    591  C   ASN A  97       9.682  22.907  16.574  1.00  6.77           C  
ATOM    592  O   ASN A  97       8.630  22.916  15.936  1.00  7.96           O  
ATOM    593  CB  ASN A  97      10.917  24.996  17.216  1.00  7.09           C  
ATOM    594  CG  ASN A  97      11.050  26.151  18.197  1.00  7.29           C  
ATOM    595  OD1 ASN A  97      12.147  26.698  18.373  1.00  9.88           O  
ATOM    596  ND2 ASN A  97       9.943  26.546  18.812  1.00  6.01           N  
ATOM    597  N   THR A  98      10.646  22.021  16.349  1.00  6.23           N  
ATOM    598  CA  THR A  98      10.548  21.032  15.270  1.00  6.54           C  
ATOM    599  C   THR A  98       9.973  19.702  15.751  1.00  6.77           C  
ATOM    600  O   THR A  98       9.596  18.839  14.944  1.00  7.69           O  
ATOM    601  CB  THR A  98      11.922  20.749  14.683  1.00  6.50           C  
ATOM    602  OG1 THR A  98      12.763  20.192  15.707  1.00  7.54           O  
ATOM    603  CG2 THR A  98      12.539  22.026  14.134  1.00  7.01           C  
ATOM    604  N   LEU A  99       9.922  19.545  17.072  1.00  6.71           N  
ATOM    605  CA  LEU A  99       9.548  18.290  17.726  1.00  6.76           C  
ATOM    606  C   LEU A  99      10.557  17.158  17.493  1.00  6.29           C  
ATOM    607  O   LEU A  99      10.267  15.987  17.764  1.00  5.97           O  
ATOM    608  CB  LEU A  99       8.098  17.868  17.402  1.00  7.48           C  
ATOM    609  CG  LEU A  99       7.027  18.808  17.983  1.00 10.39           C  
ATOM    610  CD1 LEU A  99       5.645  18.232  17.738  1.00 12.88           C  
ATOM    611  CD2 LEU A  99       7.230  19.040  19.472  1.00 11.24           C  
ATOM    612  N   ASN A 100      11.746  17.497  17.007  1.00  5.28           N  
ATOM    613  CA  ASN A 100      12.777  16.470  16.839  1.00  4.94           C  
ATOM    614  C   ASN A 100      13.183  15.917  18.201  1.00  5.22           C  
ATOM    615  O   ASN A 100      13.362  16.687  19.150  1.00  4.86           O  
ATOM    616  CB  ASN A 100      13.996  17.043  16.129  1.00  5.22           C  
ATOM    617  CG  ASN A 100      14.889  15.957  15.513  1.00  4.82           C  
ATOM    618  OD1 ASN A 100      14.433  14.856  15.185  1.00  6.19           O  
ATOM    619  ND2 ASN A 100      16.165  16.284  15.326  1.00  6.30           N  
ATOM    620  N   ASN A 101      13.294  14.591  18.298  1.00  5.12           N  
ATOM    621  CA  ASN A 101      13.634  13.919  19.562  1.00  5.17           C  
ATOM    622  C   ASN A 101      12.551  14.109  20.634  1.00  5.12           C  
ATOM    623  O   ASN A 101      12.849  14.449  21.787  1.00  5.46           O  
ATOM    624  CB  ASN A 101      15.008  14.370  20.106  1.00  5.03           C  
ATOM    625  CG  ASN A 101      16.128  14.227  19.079  1.00  5.76           C  
ATOM    626  OD1 ASN A 101      16.479  13.115  18.669  1.00  7.01           O  
ATOM    627  ND2 ASN A 101      16.693  15.353  18.664  1.00  6.43           N  
ATOM    628  N   ASP A 102      11.296  13.878  20.236  1.00  4.96           N  
ATOM    629  CA  ASP A 102      10.149  14.051  21.136  1.00  4.45           C  
ATOM    630  C   ASP A 102       9.960  12.831  22.013  1.00  4.25           C  
ATOM    631  O   ASP A 102       9.052  12.004  21.802  1.00  3.88           O  
ATOM    632  CB  ASP A 102       8.885  14.352  20.326  1.00  4.44           C  
ATOM    633  CG  ASP A 102       7.739  14.868  21.180  1.00  4.76           C  
ATOM    634  OD1 ASP A 102       7.945  15.156  22.387  1.00  5.44           O  
ATOM    635  OD2 ASP A 102       6.609  14.968  20.630  1.00  5.87           O  
ATOM    636  N   ILE A 103      10.860  12.717  22.984  1.00  4.16           N  
ATOM    637  CA  ILE A 103      10.869  11.574  23.885  1.00  4.14           C  
ATOM    638  C   ILE A 103      11.358  12.002  25.272  1.00  4.57           C  
ATOM    639  O   ILE A 103      12.269  12.849  25.397  1.00  4.75           O  
ATOM    640  CB  ILE A 103      11.698  10.377  23.310  1.00  4.34           C  
ATOM    641  CG1 ILE A 103      11.587   9.153  24.227  1.00  4.60           C  
ATOM    642  CG2 ILE A 103      13.168  10.763  23.058  1.00  5.08           C  
ATOM    643  CD1 ILE A 103      12.128   7.900  23.556  1.00  7.00           C  
ATOM    644  N  AMET A 104      10.723  11.459  26.304  0.50  4.17           N  
ATOM    645  N  BMET A 104      10.744  11.426  26.309  0.50  4.84           N  
ATOM    646  CA AMET A 104      11.192  11.663  27.664  0.50  4.52           C  
ATOM    647  CA BMET A 104      11.074  11.739  27.704  0.50  5.82           C  
ATOM    648  C  AMET A 104      10.992  10.397  28.469  0.50  4.60           C  
ATOM    649  C  BMET A 104      10.833  10.521  28.600  0.50  5.59           C  
ATOM    650  O  AMET A 104      10.219   9.512  28.083  0.50  3.85           O  
ATOM    651  O  BMET A 104       9.862   9.786  28.403  0.50  6.25           O  
ATOM    652  CB AMET A 104      10.486  12.848  28.334  0.50  4.94           C  
ATOM    653  CB BMET A 104      10.232  12.925  28.187  0.50  6.54           C  
ATOM    654  CG AMET A 104       9.008  12.637  28.618  0.50  4.37           C  
ATOM    655  CG BMET A 104      10.342  13.250  29.672  0.50  8.45           C  
ATOM    656  SD AMET A 104       8.236  14.052  29.435  0.50  5.57           S  
ATOM    657  SD BMET A 104       9.090  14.435  30.227  0.50 11.69           S  
ATOM    658  CE AMET A 104       9.020  14.028  31.044  0.50  6.49           C  
ATOM    659  CE BMET A 104       7.583  13.656  29.660  0.50 10.03           C  
ATOM    660  N   LEU A 105      11.723  10.313  29.573  1.00  4.91           N  
ATOM    661  CA  LEU A 105      11.578   9.227  30.536  1.00  5.00           C  
ATOM    662  C   LEU A 105      11.054   9.788  31.846  1.00  5.26           C  
ATOM    663  O   LEU A 105      11.437  10.882  32.257  1.00  6.26           O  
ATOM    664  CB  LEU A 105      12.931   8.534  30.763  1.00  4.82           C  
ATOM    665  CG  LEU A 105      13.396   7.640  29.606  1.00  5.36           C  
ATOM    666  CD1 LEU A 105      14.892   7.331  29.728  1.00  6.74           C  
ATOM    667  CD2 LEU A 105      12.593   6.342  29.557  1.00  7.32           C  
ATOM    668  N   ILE A 106      10.169   9.029  32.491  1.00  5.12           N  
ATOM    669  CA  ILE A 106       9.618   9.414  33.787  1.00  5.38           C  
ATOM    670  C   ILE A 106       9.863   8.247  34.741  1.00  5.50           C  
ATOM    671  O   ILE A 106       9.501   7.108  34.440  1.00  6.07           O  
ATOM    672  CB  ILE A 106       8.115   9.672  33.667  1.00  5.46           C  
ATOM    673  CG1 ILE A 106       7.868  10.815  32.681  1.00  5.70           C  
ATOM    674  CG2 ILE A 106       7.498  10.022  35.029  1.00  6.21           C  
ATOM    675  CD1 ILE A 106       6.433  10.874  32.176  1.00  8.58           C  
ATOM    676  N   LYS A 107      10.499   8.530  35.873  1.00  5.77           N  
ATOM    677  CA  LYS A 107      10.698   7.497  36.888  1.00  6.38           C  
ATOM    678  C   LYS A 107       9.628   7.601  37.970  1.00  6.54           C  
ATOM    679  O   LYS A 107       9.305   8.700  38.450  1.00  7.45           O  
ATOM    680  CB  LYS A 107      12.096   7.595  37.501  1.00  6.82           C  
ATOM    681  CG  LYS A 107      12.487   6.373  38.319  1.00  7.74           C  
ATOM    682  CD  LYS A 107      13.807   6.571  39.014  1.00  8.55           C  
ATOM    683  CE  LYS A 107      14.213   5.324  39.762  1.00  7.89           C  
ATOM    684  NZ  LYS A 107      15.578   5.456  40.357  1.00  9.16           N  
ATOM    685  N   LEU A 108       9.093   6.440  38.341  1.00  7.29           N  
ATOM    686  CA  LEU A 108       8.138   6.312  39.443  1.00  7.79           C  
ATOM    687  C   LEU A 108       8.835   6.331  40.803  1.00  8.16           C  
ATOM    688  O   LEU A 108       9.923   5.770  40.952  1.00  8.02           O  
ATOM    689  CB  LEU A 108       7.338   5.009  39.300  1.00  8.54           C  
ATOM    690  CG  LEU A 108       6.650   4.768  37.954  1.00  9.22           C  
ATOM    691  CD1 LEU A 108       5.869   3.451  37.909  1.00  9.73           C  
ATOM    692  CD2 LEU A 108       5.761   5.938  37.595  1.00 12.12           C  
ATOM    693  N   LYS A 109       8.205   6.960  41.795  1.00  8.30           N  
ATOM    694  CA  LYS A 109       8.754   6.992  43.165  1.00  9.63           C  
ATOM    695  C   LYS A 109       8.870   5.600  43.770  1.00 10.00           C  
ATOM    696  O   LYS A 109       9.745   5.346  44.602  1.00 10.36           O  
ATOM    697  CB  LYS A 109       7.891   7.857  44.085  1.00 10.43           C  
ATOM    698  CG  LYS A 109       8.132   9.333  43.970  1.00 12.05           C  
ATOM    699  CD  LYS A 109       7.154  10.096  44.858  1.00 15.38           C  
ATOM    700  CE  LYS A 109       7.627  11.518  45.143  1.00 19.05           C  
ATOM    701  NZ  LYS A 109       8.721  11.531  46.170  1.00 20.88           N  
ATOM    702  N   SER A 110       7.967   4.713  43.372  1.00  9.95           N  
ATOM    703  CA  SER A 110       8.013   3.318  43.788  1.00  9.97           C  
ATOM    704  C   SER A 110       7.702   2.428  42.596  1.00  9.83           C  
ATOM    705  O   SER A 110       7.023   2.848  41.665  1.00  9.12           O  
ATOM    706  CB  SER A 110       7.013   3.056  44.909  1.00 10.55           C  
ATOM    707  OG  SER A 110       5.687   3.321  44.482  1.00 12.21           O  
ATOM    708  N   ALA A 111       8.205   1.197  42.620  1.00  9.61           N  
ATOM    709  CA  ALA A 111       7.974   0.266  41.527  1.00  9.30           C  
ATOM    710  C   ALA A 111       6.507  -0.123  41.492  1.00  9.63           C  
ATOM    711  O   ALA A 111       5.904  -0.381  42.540  1.00  9.75           O  
ATOM    712  CB  ALA A 111       8.835  -0.983  41.702  1.00  9.22           C  
ATOM    713  N   ALA A 112       5.926  -0.150  40.298  1.00  9.61           N  
ATOM    714  CA  ALA A 112       4.569  -0.655  40.160  1.00  9.95           C  
ATOM    715  C   ALA A 112       4.559  -2.150  40.424  1.00 10.17           C  
ATOM    716  O   ALA A 112       5.588  -2.829  40.261  1.00 10.51           O  
ATOM    717  CB  ALA A 112       4.029  -0.364  38.771  1.00 10.37           C  
ATOM    718  N   SER A 113       3.398  -2.647  40.852  1.00 10.16           N  
ATOM    719  CA ASER A 113       3.178  -4.078  41.013  0.50 10.39           C  
ATOM    720  CA BSER A 113       3.179  -4.080  41.005  0.50 10.51           C  
ATOM    721  C   SER A 113       2.727  -4.649  39.673  1.00 10.56           C  
ATOM    722  O   SER A 113       1.628  -4.356  39.199  1.00 10.76           O  
ATOM    723  CB ASER A 113       2.122  -4.334  42.092  0.50 10.61           C  
ATOM    724  CB BSER A 113       2.121  -4.349  42.071  0.50 10.76           C  
ATOM    725  OG ASER A 113       1.913  -5.721  42.285  0.50 10.82           O  
ATOM    726  OG BSER A 113       2.567  -3.896  43.329  0.50 11.70           O  
ATOM    727  N   LEU A 114       3.585  -5.453  39.061  1.00 10.73           N  
ATOM    728  CA  LEU A 114       3.279  -5.987  37.751  1.00 11.00           C  
ATOM    729  C   LEU A 114       2.397  -7.220  37.842  1.00 11.67           C  
ATOM    730  O   LEU A 114       2.614  -8.095  38.681  1.00 12.32           O  
ATOM    731  CB  LEU A 114       4.557  -6.258  36.946  1.00 11.05           C  
ATOM    732  CG  LEU A 114       5.461  -5.028  36.800  1.00 11.40           C  
ATOM    733  CD1 LEU A 114       6.740  -5.361  36.030  1.00 12.84           C  
ATOM    734  CD2 LEU A 114       4.732  -3.849  36.146  1.00 12.47           C  
ATOM    735  N   ASN A 115       1.392  -7.250  36.975  1.00 11.96           N  
ATOM    736  CA  ASN A 115       0.417  -8.333  36.893  1.00 11.77           C  
ATOM    737  C   ASN A 115      -0.128  -8.377  35.453  1.00 11.52           C  
ATOM    738  O   ASN A 115       0.422  -7.718  34.566  1.00 11.29           O  
ATOM    739  CB  ASN A 115      -0.688  -8.117  37.937  1.00 11.86           C  
ATOM    740  CG  ASN A 115      -1.328  -6.743  37.824  1.00 12.59           C  
ATOM    741  OD1 ASN A 115      -1.799  -6.369  36.752  1.00 12.69           O  
ATOM    742  ND2 ASN A 115      -1.326  -5.979  38.917  1.00 13.68           N  
ATOM    743  N   SER A 116      -1.191  -9.141  35.209  1.00 10.88           N  
ATOM    744  CA  SER A 116      -1.718  -9.263  33.847  1.00 10.85           C  
ATOM    745  C   SER A 116      -2.296  -7.963  33.279  1.00 10.42           C  
ATOM    746  O   SER A 116      -2.375  -7.792  32.055  1.00 10.69           O  
ATOM    747  CB  SER A 116      -2.785 -10.353  33.795  1.00 11.40           C  
ATOM    748  OG  SER A 116      -3.905  -9.969  34.577  1.00 12.27           O  
ATOM    749  N   ARG A 117      -2.709  -7.064  34.165  1.00  9.84           N  
ATOM    750  CA  ARG A 117      -3.382  -5.822  33.754  1.00  9.40           C  
ATOM    751  C   ARG A 117      -2.476  -4.604  33.795  1.00  9.60           C  
ATOM    752  O   ARG A 117      -2.810  -3.561  33.224  1.00  9.65           O  
ATOM    753  CB  ARG A 117      -4.646  -5.594  34.585  1.00  9.78           C  
ATOM    754  CG  ARG A 117      -5.662  -6.716  34.389  1.00  9.63           C  
ATOM    755  CD  ARG A 117      -6.909  -6.517  35.215  1.00 12.65           C  
ATOM    756  NE  ARG A 117      -7.940  -7.480  34.819  1.00 15.80           N  
ATOM    757  CZ  ARG A 117      -8.003  -8.744  35.232  1.00 18.21           C  
ATOM    758  NH1 ARG A 117      -7.095  -9.233  36.071  1.00 18.86           N  
ATOM    759  NH2 ARG A 117      -8.989  -9.525  34.803  1.00 18.78           N  
ATOM    760  N   VAL A 118      -1.345  -4.742  34.485  1.00  9.18           N  
ATOM    761  CA  VAL A 118      -0.315  -3.712  34.560  1.00  8.63           C  
ATOM    762  C   VAL A 118       1.014  -4.390  34.229  1.00  8.83           C  
ATOM    763  O   VAL A 118       1.576  -5.141  35.040  1.00  9.25           O  
ATOM    764  CB  VAL A 118      -0.270  -3.023  35.944  1.00  8.56           C  
ATOM    765  CG1 VAL A 118       0.840  -1.984  35.998  1.00  8.66           C  
ATOM    766  CG2 VAL A 118      -1.618  -2.374  36.268  1.00  9.15           C  
ATOM    767  N   ALA A 119       1.506  -4.129  33.028  1.00  7.73           N  
ATOM    768  CA  ALA A 119       2.639  -4.867  32.497  1.00  7.62           C  
ATOM    769  C   ALA A 119       3.494  -3.948  31.657  1.00  7.43           C  
ATOM    770  O   ALA A 119       2.979  -3.049  31.000  1.00  7.85           O  
ATOM    771  CB  ALA A 119       2.142  -6.023  31.660  1.00  7.75           C  
ATOM    772  N   SER A 120       4.801  -4.181  31.676  1.00  7.31           N  
ATOM    773  CA  SER A 120       5.717  -3.409  30.838  1.00  7.84           C  
ATOM    774  C   SER A 120       5.670  -3.899  29.386  1.00  8.12           C  
ATOM    775  O   SER A 120       5.310  -5.047  29.113  1.00  8.86           O  
ATOM    776  CB  SER A 120       7.135  -3.506  31.390  1.00  8.48           C  
ATOM    777  OG  SER A 120       7.515  -4.870  31.501  1.00  9.66           O  
ATOM    778  N   ILE A 121       6.008  -3.005  28.460  1.00  7.67           N  
ATOM    779  CA  ILE A 121       6.185  -3.350  27.049  1.00  7.92           C  
ATOM    780  C   ILE A 121       7.679  -3.346  26.703  1.00  8.08           C  
ATOM    781  O   ILE A 121       8.424  -2.474  27.148  1.00  8.19           O  
ATOM    782  CB  ILE A 121       5.376  -2.386  26.099  1.00  8.02           C  
ATOM    783  CG1 ILE A 121       5.373  -2.885  24.641  1.00  8.21           C  
ATOM    784  CG2 ILE A 121       5.880  -0.932  26.196  1.00  8.82           C  
ATOM    785  CD1 ILE A 121       4.547  -4.132  24.396  1.00 11.70           C  
ATOM    786  N   SER A 122       8.111  -4.328  25.914  1.00  8.53           N  
ATOM    787  CA  SER A 122       9.510  -4.415  25.504  1.00  9.18           C  
ATOM    788  C   SER A 122       9.907  -3.301  24.546  1.00  8.95           C  
ATOM    789  O   SER A 122       9.110  -2.859  23.726  1.00  8.79           O  
ATOM    790  CB  SER A 122       9.777  -5.761  24.835  1.00 10.09           C  
ATOM    791  OG  SER A 122       9.465  -6.826  25.715  1.00 13.66           O  
ATOM    792  N   LEU A 123      11.156  -2.864  24.674  1.00  9.05           N  
ATOM    793  CA  LEU A 123      11.777  -1.976  23.695  1.00  9.57           C  
ATOM    794  C   LEU A 123      12.115  -2.768  22.423  1.00 10.31           C  
ATOM    795  O   LEU A 123      12.288  -3.987  22.485  1.00 11.08           O  
ATOM    796  CB  LEU A 123      13.037  -1.334  24.294  1.00  9.30           C  
ATOM    797  CG  LEU A 123      12.786  -0.395  25.485  1.00  9.81           C  
ATOM    798  CD1 LEU A 123      14.105   0.118  26.049  1.00 10.94           C  
ATOM    799  CD2 LEU A 123      11.873   0.763  25.107  1.00 11.07           C  
ATOM    800  N   PRO A 124      12.184  -2.090  21.262  1.00 10.75           N  
ATOM    801  CA  PRO A 124      12.506  -2.826  20.033  1.00 11.55           C  
ATOM    802  C   PRO A 124      13.942  -3.314  20.061  1.00 12.57           C  
ATOM    803  O   PRO A 124      14.800  -2.651  20.637  1.00 11.85           O  
ATOM    804  CB  PRO A 124      12.354  -1.793  18.918  1.00 11.88           C  
ATOM    805  CG  PRO A 124      12.120  -0.481  19.562  1.00 11.84           C  
ATOM    806  CD  PRO A 124      11.966  -0.649  21.038  1.00 10.83           C  
ATOM    807  N   THR A 125      14.169  -4.426  19.378  1.00 13.92           N  
ATOM    808  CA  THR A 125      15.541  -4.859  19.141  1.00 16.42           C  
ATOM    809  C   THR A 125      15.995  -4.410  17.757  1.00 17.12           C  
ATOM    810  O   THR A 125      17.068  -4.243  17.449  1.00 17.23           O  
ATOM    811  CB  THR A 125      15.834  -6.361  19.505  1.00 16.92           C  
ATOM    812  OG1 THR A 125      16.251  -7.172  18.418  1.00 20.30           O  
ATOM    813  CG2 THR A 125      14.914  -6.925  20.282  1.00 18.87           C  
ATOM    814  N   SER A 127      15.010  -4.152  16.977  1.00 12.78           N  
ATOM    815  CA  SER A 127      15.075  -3.642  15.556  1.00 12.91           C  
ATOM    816  C   SER A 127      13.983  -2.600  15.137  1.00 12.05           C  
ATOM    817  O   SER A 127      12.957  -2.682  15.628  1.00 12.25           O  
ATOM    818  CB  SER A 127      15.084  -4.747  14.482  1.00 13.28           C  
ATOM    819  OG  SER A 127      13.867  -5.361  14.358  1.00 16.56           O  
ATOM    820  N   CYS A 128      14.310  -1.650  14.257  1.00 11.65           N  
ATOM    821  CA  CYS A 128      13.332  -0.669  13.794  1.00 11.54           C  
ATOM    822  C   CYS A 128      12.284  -1.344  12.938  1.00 12.01           C  
ATOM    823  O   CYS A 128      12.608  -2.191  12.104  1.00 13.29           O  
ATOM    824  CB  CYS A 128      14.018   0.422  12.989  1.00 10.97           C  
ATOM    825  SG  CYS A 128      15.198   1.338  13.945  1.00  9.97           S  
ATOM    826  N   ALA A 129      11.023  -0.988  13.160  1.00 12.12           N  
ATOM    827  CA  ALA A 129       9.930  -1.523  12.355  1.00 12.15           C  
ATOM    828  C   ALA A 129       9.947  -0.908  10.959  1.00 12.08           C  
ATOM    829  O   ALA A 129      10.470   0.198  10.759  1.00 14.03           O  
ATOM    830  CB  ALA A 129       8.596  -1.291  13.035  1.00 12.38           C  
ATOM    831  N   SER A 130       9.398  -1.640   9.999  1.00 11.25           N  
ATOM    832  CA  SER A 130       9.359  -1.202   8.622  1.00 10.96           C  
ATOM    833  C   SER A 130       7.978  -0.619   8.317  1.00 10.70           C  
ATOM    834  O   SER A 130       6.937  -1.132   8.739  1.00  9.59           O  
ATOM    835  CB  SER A 130       9.670  -2.374   7.682  1.00 10.93           C  
ATOM    836  OG  SER A 130      10.984  -2.860   7.893  1.00 12.21           O  
ATOM    837  N   ALA A 132       7.973   0.392   7.095  1.00 10.07           N  
ATOM    838  CA  ALA A 132       6.711   0.677   6.426  1.00  9.76           C  
ATOM    839  C   ALA A 132       5.941  -0.609   6.111  1.00  9.57           C  
ATOM    840  O   ALA A 132       6.517  -1.601   5.640  1.00 10.08           O  
ATOM    841  CB  ALA A 132       6.965   1.466   5.180  1.00 10.00           C  
ATOM    842  N   GLY A 133       4.646  -0.586   6.400  1.00  9.62           N  
ATOM    843  CA  GLY A 133       3.775  -1.713   6.125  1.00  9.65           C  
ATOM    844  C   GLY A 133       3.419  -2.520   7.350  1.00  9.97           C  
ATOM    845  O   GLY A 133       2.412  -3.222   7.352  1.00 10.82           O  
ATOM    846  N   THR A 134       4.250  -2.442   8.386  1.00 10.07           N  
ATOM    847  CA  THR A 134       3.975  -3.183   9.618  1.00 10.50           C  
ATOM    848  C   THR A 134       2.756  -2.576  10.292  1.00 10.00           C  
ATOM    849  O   THR A 134       2.638  -1.355  10.385  1.00  9.66           O  
ATOM    850  CB  THR A 134       5.197  -3.169  10.561  1.00 11.37           C  
ATOM    851  OG1 THR A 134       6.278  -3.837   9.904  1.00 14.62           O  
ATOM    852  CG2 THR A 134       4.923  -3.909  11.878  1.00 11.04           C  
ATOM    853  N   GLN A 135       1.851  -3.442  10.740  1.00  9.79           N  
ATOM    854  CA  GLN A 135       0.665  -3.026  11.485  1.00 10.15           C  
ATOM    855  C   GLN A 135       1.026  -2.793  12.949  1.00  9.59           C  
ATOM    856  O   GLN A 135       1.756  -3.590  13.561  1.00 10.01           O  
ATOM    857  CB  GLN A 135      -0.440  -4.083  11.390  1.00 11.11           C  
ATOM    858  CG  GLN A 135      -1.804  -3.588  11.897  1.00 14.26           C  
ATOM    859  CD  GLN A 135      -2.741  -4.715  12.333  1.00 18.93           C  
ATOM    860  OE1 GLN A 135      -3.691  -5.054  11.624  1.00 22.64           O  
ATOM    861  NE2 GLN A 135      -2.485  -5.286  13.511  1.00 20.38           N  
ATOM    862  N   CYS A 136       0.501  -1.704  13.510  1.00  7.87           N  
ATOM    863  CA  CYS A 136       0.733  -1.353  14.908  1.00  8.04           C  
ATOM    864  C   CYS A 136      -0.575  -1.034  15.625  1.00  7.33           C  
ATOM    865  O   CYS A 136      -1.594  -0.793  14.985  1.00  7.97           O  
ATOM    866  CB  CYS A 136       1.684  -0.159  15.013  1.00  7.90           C  
ATOM    867  SG  CYS A 136       3.207  -0.375  14.050  1.00  8.51           S  
ATOM    868  N   LEU A 137      -0.518  -1.039  16.953  1.00  6.58           N  
ATOM    869  CA  LEU A 137      -1.641  -0.650  17.793  1.00  5.96           C  
ATOM    870  C   LEU A 137      -1.312   0.671  18.482  1.00  5.57           C  
ATOM    871  O   LEU A 137      -0.307   0.782  19.198  1.00  5.33           O  
ATOM    872  CB  LEU A 137      -1.930  -1.729  18.837  1.00  6.49           C  
ATOM    873  CG  LEU A 137      -3.138  -1.454  19.738  1.00  5.99           C  
ATOM    874  CD1 LEU A 137      -4.434  -1.580  18.953  1.00  8.48           C  
ATOM    875  CD2 LEU A 137      -3.146  -2.345  20.979  1.00  6.71           C  
ATOM    876  N   ILE A 138      -2.182   1.657  18.255  1.00  4.70           N  
ATOM    877  CA  ILE A 138      -2.034   2.996  18.824  1.00  4.95           C  
ATOM    878  C   ILE A 138      -3.203   3.192  19.782  1.00  5.04           C  
ATOM    879  O   ILE A 138      -4.325   2.801  19.482  1.00  6.03           O  
ATOM    880  CB  ILE A 138      -2.041   4.077  17.715  1.00  5.05           C  
ATOM    881  CG1 ILE A 138      -0.977   3.737  16.652  1.00  5.01           C  
ATOM    882  CG2 ILE A 138      -1.751   5.456  18.323  1.00  5.89           C  
ATOM    883  CD1 ILE A 138      -1.043   4.613  15.412  1.00  8.85           C  
ATOM    884  N   SER A 139      -2.955   3.795  20.941  1.00  4.43           N  
ATOM    885  CA  SER A 139      -4.002   3.853  21.962  1.00  4.51           C  
ATOM    886  C   SER A 139      -3.910   5.127  22.783  1.00  4.68           C  
ATOM    887  O   SER A 139      -2.849   5.743  22.874  1.00  5.02           O  
ATOM    888  CB  SER A 139      -3.946   2.605  22.861  1.00  4.62           C  
ATOM    889  OG  SER A 139      -2.621   2.353  23.315  1.00  4.74           O  
ATOM    890  N   GLY A 140      -5.037   5.530  23.372  1.00  4.60           N  
ATOM    891  CA  GLY A 140      -5.053   6.735  24.195  1.00  4.66           C  
ATOM    892  C   GLY A 140      -6.443   7.209  24.564  1.00  5.16           C  
ATOM    893  O   GLY A 140      -7.446   6.674  24.083  1.00  5.82           O  
ATOM    894  N   TRP A 141      -6.477   8.236  25.409  1.00  5.05           N  
ATOM    895  CA  TRP A 141      -7.708   8.832  25.913  1.00  5.26           C  
ATOM    896  C   TRP A 141      -7.930  10.215  25.284  1.00  5.40           C  
ATOM    897  O   TRP A 141      -8.641  11.056  25.842  1.00  6.56           O  
ATOM    898  CB  TRP A 141      -7.621   8.985  27.437  1.00  5.09           C  
ATOM    899  CG  TRP A 141      -7.746   7.693  28.214  1.00  4.93           C  
ATOM    900  CD1 TRP A 141      -8.912   7.056  28.550  1.00  5.63           C  
ATOM    901  CD2 TRP A 141      -6.684   6.903  28.770  1.00  5.42           C  
ATOM    902  NE1 TRP A 141      -8.642   5.925  29.288  1.00  6.19           N  
ATOM    903  CE2 TRP A 141      -7.284   5.807  29.440  1.00  4.91           C  
ATOM    904  CE3 TRP A 141      -5.287   7.027  28.796  1.00  5.39           C  
ATOM    905  CZ2 TRP A 141      -6.531   4.819  30.086  1.00  4.72           C  
ATOM    906  CZ3 TRP A 141      -4.539   6.053  29.449  1.00  6.20           C  
ATOM    907  CH2 TRP A 141      -5.165   4.967  30.095  1.00  5.73           C  
ATOM    908  N   GLY A 142      -7.316  10.458  24.129  1.00  5.52           N  
ATOM    909  CA  GLY A 142      -7.423  11.757  23.482  1.00  5.95           C  
ATOM    910  C   GLY A 142      -8.726  11.974  22.731  1.00  5.93           C  
ATOM    911  O   GLY A 142      -9.602  11.109  22.696  1.00  6.37           O  
ATOM    912  N   ASN A 143      -8.839  13.155  22.139  1.00  5.88           N  
ATOM    913  CA  ASN A 143     -10.017  13.565  21.384  1.00  6.27           C  
ATOM    914  C   ASN A 143     -10.392  12.526  20.321  1.00  6.46           C  
ATOM    915  O   ASN A 143      -9.507  11.976  19.646  1.00  5.75           O  
ATOM    916  CB  ASN A 143      -9.692  14.913  20.734  1.00  6.06           C  
ATOM    917  CG  ASN A 143     -10.897  15.592  20.091  1.00  6.20           C  
ATOM    918  OD1 ASN A 143     -12.043  15.129  20.176  1.00  7.39           O  
ATOM    919  ND2 ASN A 143     -10.627  16.723  19.435  1.00  9.35           N  
ATOM    920  N   THR A 144     -11.694  12.250  20.193  1.00  6.91           N  
ATOM    921  CA  THR A 144     -12.177  11.272  19.218  1.00  7.42           C  
ATOM    922  C   THR A 144     -12.802  11.924  17.978  1.00  8.69           C  
ATOM    923  O   THR A 144     -13.317  11.224  17.096  1.00  8.81           O  
ATOM    924  CB  THR A 144     -13.217  10.309  19.839  1.00  7.41           C  
ATOM    925  OG1 THR A 144     -14.323  11.072  20.329  1.00  7.87           O  
ATOM    926  CG2 THR A 144     -12.606   9.493  20.989  1.00  7.49           C  
ATOM    927  N   LYS A 145     -12.723  13.254  17.901  1.00  9.91           N  
ATOM    928  CA ALYS A 145     -13.293  14.020  16.789  0.50 10.75           C  
ATOM    929  CA BLYS A 145     -13.277  13.977  16.758  0.50 10.89           C  
ATOM    930  C   LYS A 145     -12.224  14.750  15.973  1.00 11.26           C  
ATOM    931  O   LYS A 145     -11.311  15.356  16.544  1.00 11.10           O  
ATOM    932  CB ALYS A 145     -14.297  15.048  17.321  0.50 11.09           C  
ATOM    933  CB BLYS A 145     -14.428  14.901  17.185  0.50 11.37           C  
ATOM    934  CG ALYS A 145     -15.452  14.447  18.101  0.50 11.61           C  
ATOM    935  CG BLYS A 145     -15.750  14.185  17.495  0.50 12.59           C  
ATOM    936  CD ALYS A 145     -16.622  15.405  18.205  0.50 13.67           C  
ATOM    937  CD BLYS A 145     -16.091  13.127  16.452  0.50 14.66           C  
ATOM    938  CE ALYS A 145     -17.919  14.661  18.519  0.50 14.51           C  
ATOM    939  CE BLYS A 145     -17.431  12.460  16.739  0.50 15.72           C  
ATOM    940  NZ ALYS A 145     -18.456  13.890  17.356  0.50 17.08           N  
ATOM    941  NZ BLYS A 145     -17.495  11.075  16.179  0.50 15.83           N  
ATOM    942  N   SER A 146     -12.361  14.718  14.649  1.00 11.95           N  
ATOM    943  CA ASER A 146     -11.491  15.476  13.750  0.30 12.32           C  
ATOM    944  CA BSER A 146     -11.477  15.479  13.771  0.70 12.76           C  
ATOM    945  C   SER A 146     -11.927  16.939  13.725  1.00 12.94           C  
ATOM    946  O   SER A 146     -11.098  17.859  13.612  1.00 13.84           O  
ATOM    947  CB ASER A 146     -11.543  14.879  12.343  0.30 12.38           C  
ATOM    948  CB BSER A 146     -11.439  14.852  12.374  0.70 13.05           C  
ATOM    949  OG ASER A 146     -10.805  15.666  11.426  0.30 11.26           O  
ATOM    950  OG BSER A 146     -12.742  14.578  11.892  0.70 14.71           O  
ATOM    951  N   SER A 147     -13.237  17.141  13.834  1.00 12.85           N  
ATOM    952  CA  SER A 147     -13.849  18.461  13.880  1.00 13.60           C  
ATOM    953  C   SER A 147     -14.532  18.618  15.232  1.00 13.24           C  
ATOM    954  O   SER A 147     -15.480  17.894  15.545  1.00 14.22           O  
ATOM    955  CB  SER A 147     -14.875  18.607  12.754  1.00 13.91           C  
ATOM    956  OG  SER A 147     -14.238  18.660  11.489  1.00 16.45           O  
ATOM    957  N   GLY A 148     -14.042  19.549  16.041  1.00 13.04           N  
ATOM    958  CA  GLY A 148     -14.613  19.757  17.364  1.00 12.96           C  
ATOM    959  C   GLY A 148     -13.927  18.870  18.386  1.00 12.48           C  
ATOM    960  O   GLY A 148     -12.812  18.377  18.145  1.00 12.73           O  
ATOM    961  N   THR A 149     -14.582  18.668  19.528  1.00 12.00           N  
ATOM    962  CA  THR A 149     -13.938  17.980  20.646  1.00 11.25           C  
ATOM    963  C   THR A 149     -14.886  17.057  21.408  1.00 10.42           C  
ATOM    964  O   THR A 149     -15.995  17.453  21.788  1.00 11.05           O  
ATOM    965  CB  THR A 149     -13.286  18.995  21.633  1.00 11.46           C  
ATOM    966  OG1 THR A 149     -12.265  19.738  20.953  1.00 13.26           O  
ATOM    967  CG2 THR A 149     -12.651  18.289  22.824  1.00 12.01           C  
ATOM    968  N   SER A 150     -14.433  15.821  21.618  1.00  9.42           N  
ATOM    969  CA  SER A 150     -15.087  14.898  22.534  1.00  8.96           C  
ATOM    970  C   SER A 150     -14.030  13.973  23.112  1.00  9.00           C  
ATOM    971  O   SER A 150     -13.325  13.290  22.366  1.00  8.79           O  
ATOM    972  CB  SER A 150     -16.140  14.061  21.819  1.00  9.18           C  
ATOM    973  OG  SER A 150     -16.797  13.195  22.739  1.00  9.71           O  
ATOM    974  N   TYR A 151     -13.911  13.973  24.437  1.00  8.95           N  
ATOM    975  CA  TYR A 151     -12.957  13.100  25.108  1.00  9.46           C  
ATOM    976  C   TYR A 151     -13.674  11.888  25.672  1.00  9.87           C  
ATOM    977  O   TYR A 151     -14.696  12.032  26.362  1.00 10.46           O  
ATOM    978  CB  TYR A 151     -12.222  13.859  26.205  1.00  9.94           C  
ATOM    979  CG  TYR A 151     -11.045  14.645  25.690  1.00 10.54           C  
ATOM    980  CD1 TYR A 151      -9.743  14.234  25.978  1.00 12.53           C  
ATOM    981  CD2 TYR A 151     -11.223  15.787  24.905  1.00 12.24           C  
ATOM    982  CE1 TYR A 151      -8.642  14.943  25.512  1.00 13.58           C  
ATOM    983  CE2 TYR A 151     -10.116  16.503  24.418  1.00 13.99           C  
ATOM    984  CZ  TYR A 151      -8.834  16.068  24.729  1.00 13.44           C  
ATOM    985  OH  TYR A 151      -7.732  16.760  24.269  1.00 15.96           O  
ATOM    986  N   PRO A 152     -13.149  10.687  25.382  1.00  9.53           N  
ATOM    987  CA  PRO A 152     -13.752   9.453  25.842  1.00 10.49           C  
ATOM    988  C   PRO A 152     -13.291   9.248  27.273  1.00 11.42           C  
ATOM    989  O   PRO A 152     -12.284   9.805  27.686  1.00 13.47           O  
ATOM    990  CB  PRO A 152     -13.128   8.404  24.917  1.00  9.97           C  
ATOM    991  CG  PRO A 152     -11.734   8.929  24.666  1.00  9.26           C  
ATOM    992  CD  PRO A 152     -11.897  10.452  24.628  1.00  9.16           C  
ATOM    993  N  AASP A 153     -14.002   8.452  28.040  0.50 11.75           N  
ATOM    994  N  BASP A 153     -14.043   8.470  28.032  0.50 12.21           N  
ATOM    995  CA AASP A 153     -13.502   8.201  29.382  0.50 10.91           C  
ATOM    996  CA BASP A 153     -13.626   8.163  29.394  0.50 11.84           C  
ATOM    997  C  AASP A 153     -12.727   6.890  29.439  0.50 10.26           C  
ATOM    998  C  BASP A 153     -12.731   6.922  29.407  0.50 10.85           C  
ATOM    999  O  AASP A 153     -11.818   6.730  30.266  0.50  9.85           O  
ATOM   1000  O  BASP A 153     -11.763   6.839  30.178  0.50 10.60           O  
ATOM   1001  CB AASP A 153     -14.623   8.301  30.410  0.50 11.37           C  
ATOM   1002  CB BASP A 153     -14.839   8.014  30.318  0.50 12.87           C  
ATOM   1003  CG AASP A 153     -15.225   9.699  30.471  0.50 11.13           C  
ATOM   1004  CG BASP A 153     -15.822   6.953  29.839  0.50 14.54           C  
ATOM   1005  OD1AASP A 153     -14.474  10.670  30.691  0.50 12.46           O  
ATOM   1006  OD1BASP A 153     -15.404   5.792  29.662  0.50 18.06           O  
ATOM   1007  OD2AASP A 153     -16.453   9.827  30.278  0.50 12.56           O  
ATOM   1008  OD2BASP A 153     -17.024   7.265  29.675  0.50 18.93           O  
ATOM   1009  N   VAL A 154     -13.055   5.979  28.523  1.00  9.51           N  
ATOM   1010  CA  VAL A 154     -12.357   4.701  28.422  1.00  8.04           C  
ATOM   1011  C   VAL A 154     -11.302   4.723  27.317  1.00  6.66           C  
ATOM   1012  O   VAL A 154     -11.326   5.585  26.434  1.00  6.01           O  
ATOM   1013  CB  VAL A 154     -13.328   3.527  28.180  1.00  7.46           C  
ATOM   1014  CG1 VAL A 154     -14.297   3.382  29.351  1.00  8.63           C  
ATOM   1015  CG2 VAL A 154     -14.094   3.713  26.861  1.00  8.82           C  
ATOM   1016  N   LEU A 155     -10.375   3.771  27.379  1.00  6.20           N  
ATOM   1017  CA  LEU A 155      -9.246   3.765  26.459  1.00  5.40           C  
ATOM   1018  C   LEU A 155      -9.683   3.381  25.058  1.00  5.36           C  
ATOM   1019  O   LEU A 155     -10.448   2.418  24.878  1.00  5.18           O  
ATOM   1020  CB  LEU A 155      -8.150   2.817  26.963  1.00  5.32           C  
ATOM   1021  CG  LEU A 155      -6.813   2.790  26.220  1.00  5.15           C  
ATOM   1022  CD1 LEU A 155      -6.124   4.143  26.343  1.00  5.92           C  
ATOM   1023  CD2 LEU A 155      -5.898   1.690  26.735  1.00  5.98           C  
ATOM   1024  N   LYS A 156      -9.202   4.154  24.083  1.00  5.21           N  
ATOM   1025  CA  LYS A 156      -9.492   3.900  22.670  1.00  5.19           C  
ATOM   1026  C   LYS A 156      -8.253   3.379  21.966  1.00  5.32           C  
ATOM   1027  O   LYS A 156      -7.123   3.692  22.347  1.00  5.48           O  
ATOM   1028  CB  LYS A 156     -10.006   5.162  21.960  1.00  5.18           C  
ATOM   1029  CG  LYS A 156     -11.317   5.712  22.533  1.00  7.01           C  
ATOM   1030  CD  LYS A 156     -12.450   4.800  22.115  1.00  9.99           C  
ATOM   1031  CE  LYS A 156     -13.772   5.183  22.719  1.00 12.65           C  
ATOM   1032  NZ  LYS A 156     -14.816   4.393  21.992  1.00 14.46           N  
ATOM   1033  N   CYS A 157      -8.504   2.588  20.926  1.00  5.32           N  
ATOM   1034  CA  CYS A 157      -7.484   1.844  20.193  1.00  5.34           C  
ATOM   1035  C   CYS A 157      -7.637   2.041  18.690  1.00  5.67           C  
ATOM   1036  O   CYS A 157      -8.742   2.250  18.196  1.00  6.34           O  
ATOM   1037  CB  CYS A 157      -7.625   0.356  20.501  1.00  6.13           C  
ATOM   1038  SG  CYS A 157      -6.760  -0.244  21.959  1.00  6.24           S  
ATOM   1039  N   LEU A 158      -6.516   1.963  17.974  1.00  5.66           N  
ATOM   1040  CA  LEU A 158      -6.515   2.052  16.522  1.00  6.35           C  
ATOM   1041  C   LEU A 158      -5.412   1.182  15.963  1.00  6.22           C  
ATOM   1042  O   LEU A 158      -4.252   1.314  16.368  1.00  7.33           O  
ATOM   1043  CB  LEU A 158      -6.278   3.500  16.070  1.00  7.05           C  
ATOM   1044  CG  LEU A 158      -6.097   3.707  14.564  1.00  8.11           C  
ATOM   1045  CD1 LEU A 158      -7.438   3.508  13.864  1.00  7.09           C  
ATOM   1046  CD2 LEU A 158      -5.549   5.110  14.296  1.00  8.62           C  
ATOM   1047  N   LYS A 159      -5.773   0.288  15.044  1.00  6.08           N  
ATOM   1048  CA  LYS A 159      -4.770  -0.451  14.293  1.00  6.03           C  
ATOM   1049  C   LYS A 159      -4.426   0.338  13.040  1.00  6.22           C  
ATOM   1050  O   LYS A 159      -5.308   0.790  12.318  1.00  7.09           O  
ATOM   1051  CB  LYS A 159      -5.269  -1.856  13.954  1.00  5.72           C  
ATOM   1052  CG  LYS A 159      -5.400  -2.724  15.172  1.00  5.88           C  
ATOM   1053  CD  LYS A 159      -5.786  -4.141  14.802  1.00  6.17           C  
ATOM   1054  CE  LYS A 159      -5.846  -5.005  16.059  1.00  8.09           C  
ATOM   1055  NZ  LYS A 159      -6.196  -6.421  15.711  1.00  8.49           N  
ATOM   1056  N   ALA A 160      -3.130   0.522  12.806  1.00  6.68           N  
ATOM   1057  CA  ALA A 160      -2.669   1.376  11.714  1.00  6.91           C  
ATOM   1058  C   ALA A 160      -1.305   0.924  11.216  1.00  7.02           C  
ATOM   1059  O   ALA A 160      -0.470   0.494  12.012  1.00  7.39           O  
ATOM   1060  CB  ALA A 160      -2.590   2.820  12.177  1.00  7.49           C  
ATOM   1061  N   PRO A 161      -1.077   1.018   9.896  1.00  6.80           N  
ATOM   1062  CA  PRO A 161       0.241   0.681   9.360  1.00  7.19           C  
ATOM   1063  C   PRO A 161       1.243   1.833   9.403  1.00  6.94           C  
ATOM   1064  O   PRO A 161       0.879   3.007   9.279  1.00  6.82           O  
ATOM   1065  CB  PRO A 161      -0.067   0.332   7.901  1.00  7.39           C  
ATOM   1066  CG  PRO A 161      -1.210   1.251   7.546  1.00  7.58           C  
ATOM   1067  CD  PRO A 161      -2.032   1.382   8.828  1.00  7.27           C  
ATOM   1068  N   ILE A 162       2.511   1.480   9.561  1.00  6.84           N  
ATOM   1069  CA  ILE A 162       3.569   2.445   9.371  1.00  6.88           C  
ATOM   1070  C   ILE A 162       3.599   2.800   7.880  1.00  7.40           C  
ATOM   1071  O   ILE A 162       3.487   1.921   7.022  1.00  7.37           O  
ATOM   1072  CB  ILE A 162       4.914   1.873   9.849  1.00  6.82           C  
ATOM   1073  CG1 ILE A 162       4.867   1.609  11.364  1.00  7.00           C  
ATOM   1074  CG2 ILE A 162       6.080   2.812   9.473  1.00  6.52           C  
ATOM   1075  CD1 ILE A 162       6.123   0.977  11.925  1.00  9.24           C  
ATOM   1076  N   LEU A 163       3.707   4.091   7.585  1.00  7.40           N  
ATOM   1077  CA  LEU A 163       3.787   4.547   6.193  1.00  7.48           C  
ATOM   1078  C   LEU A 163       5.238   4.692   5.751  1.00  8.34           C  
ATOM   1079  O   LEU A 163       6.141   4.836   6.583  1.00  8.72           O  
ATOM   1080  CB  LEU A 163       3.054   5.884   6.027  1.00  8.13           C  
ATOM   1081  CG  LEU A 163       1.571   5.865   6.412  1.00  8.24           C  
ATOM   1082  CD1 LEU A 163       0.985   7.249   6.324  1.00 10.19           C  
ATOM   1083  CD2 LEU A 163       0.774   4.903   5.535  1.00 10.95           C  
ATOM   1084  N   SER A 164       5.458   4.665   4.437  1.00  8.57           N  
ATOM   1085  CA  SER A 164       6.807   4.834   3.897  1.00  9.67           C  
ATOM   1086  C   SER A 164       7.365   6.202   4.251  1.00  9.71           C  
ATOM   1087  O   SER A 164       6.619   7.178   4.389  1.00 10.06           O  
ATOM   1088  CB  SER A 164       6.805   4.664   2.381  1.00  9.88           C  
ATOM   1089  OG  SER A 164       6.063   5.698   1.759  1.00 10.70           O  
ATOM   1090  N   ASP A 165       8.683   6.282   4.388  1.00 10.56           N  
ATOM   1091  CA AASP A 165       9.299   7.571   4.656  0.30 10.53           C  
ATOM   1092  CA BASP A 165       9.359   7.556   4.628  0.70 11.18           C  
ATOM   1093  C   ASP A 165       9.046   8.556   3.515  1.00 11.12           C  
ATOM   1094  O   ASP A 165       8.849   9.745   3.767  1.00 10.40           O  
ATOM   1095  CB AASP A 165      10.787   7.426   4.984  0.30 10.73           C  
ATOM   1096  CB BASP A 165      10.872   7.342   4.738  0.70 12.23           C  
ATOM   1097  CG AASP A 165      11.023   6.910   6.397  0.30 10.17           C  
ATOM   1098  CG BASP A 165      11.618   8.606   5.131  0.70 14.35           C  
ATOM   1099  OD1AASP A 165      10.179   7.168   7.290  0.30 10.30           O  
ATOM   1100  OD1BASP A 165      11.241   9.241   6.141  0.70 17.38           O  
ATOM   1101  OD2AASP A 165      12.059   6.251   6.621  0.30 10.41           O  
ATOM   1102  OD2BASP A 165      12.596   8.961   4.435  0.70 18.15           O  
ATOM   1103  N   SER A 166       9.007   8.061   2.274  1.00 11.13           N  
ATOM   1104  CA ASER A 166       8.717   8.931   1.135  0.50 11.19           C  
ATOM   1105  CA BSER A 166       8.696   8.893   1.108  0.50 11.34           C  
ATOM   1106  C   SER A 166       7.309   9.538   1.226  1.00 11.10           C  
ATOM   1107  O   SER A 166       7.138  10.740   0.986  1.00 11.54           O  
ATOM   1108  CB ASER A 166       8.942   8.220  -0.207  0.50 11.35           C  
ATOM   1109  CB BSER A 166       8.793   8.065  -0.181  0.50 11.53           C  
ATOM   1110  OG ASER A 166       8.171   7.039  -0.307  0.50 11.79           O  
ATOM   1111  OG BSER A 166       8.557   8.863  -1.327  0.50 12.77           O  
ATOM   1112  N   SER A 167       6.309   8.736   1.602  1.00 10.29           N  
ATOM   1113  CA ASER A 167       4.955   9.272   1.722  0.50 10.09           C  
ATOM   1114  CA BSER A 167       4.936   9.231   1.762  0.50 10.23           C  
ATOM   1115  C   SER A 167       4.855  10.214   2.920  1.00  9.96           C  
ATOM   1116  O   SER A 167       4.151  11.227   2.856  1.00 10.01           O  
ATOM   1117  CB ASER A 167       3.904   8.159   1.801  0.50 10.23           C  
ATOM   1118  CB BSER A 167       3.960   8.074   2.013  0.50 10.30           C  
ATOM   1119  OG ASER A 167       4.041   7.402   2.984  0.50 10.54           O  
ATOM   1120  OG BSER A 167       3.681   7.360   0.822  0.50 11.54           O  
ATOM   1121  N   CYS A 168       5.574   9.888   3.995  1.00  9.45           N  
ATOM   1122  CA  CYS A 168       5.615  10.729   5.186  1.00  8.74           C  
ATOM   1123  C   CYS A 168       6.181  12.113   4.851  1.00  9.38           C  
ATOM   1124  O   CYS A 168       5.555  13.143   5.148  1.00  9.32           O  
ATOM   1125  CB  CYS A 168       6.433  10.023   6.273  1.00  8.40           C  
ATOM   1126  SG  CYS A 168       6.312  10.764   7.902  1.00  7.87           S  
ATOM   1127  N   LYS A 169       7.338  12.123   4.193  1.00  9.23           N  
ATOM   1128  CA ALYS A 169       7.994  13.369   3.800  0.50  9.71           C  
ATOM   1129  CA BLYS A 169       7.996  13.368   3.800  0.50  9.86           C  
ATOM   1130  C   LYS A 169       7.167  14.163   2.790  1.00 10.01           C  
ATOM   1131  O   LYS A 169       7.113  15.397   2.857  1.00 10.36           O  
ATOM   1132  CB ALYS A 169       9.399  13.090   3.262  0.50  9.56           C  
ATOM   1133  CB BLYS A 169       9.399  13.085   3.256  0.50  9.80           C  
ATOM   1134  CG ALYS A 169      10.338  12.551   4.321  0.50  9.79           C  
ATOM   1135  CG BLYS A 169      10.400  12.687   4.335  0.50 10.70           C  
ATOM   1136  CD ALYS A 169      11.750  12.399   3.801  0.50 10.66           C  
ATOM   1137  CD BLYS A 169      11.576  11.904   3.760  0.50 12.49           C  
ATOM   1138  CE ALYS A 169      12.687  12.209   4.968  0.50 11.84           C  
ATOM   1139  CE BLYS A 169      12.558  12.769   2.986  0.50 13.56           C  
ATOM   1140  NZ ALYS A 169      14.022  11.683   4.575  0.50 12.69           N  
ATOM   1141  NZ BLYS A 169      13.369  13.664   3.859  0.50 14.70           N  
ATOM   1142  N   SER A 170       6.514  13.460   1.863  1.00 10.32           N  
ATOM   1143  CA  SER A 170       5.629  14.114   0.887  1.00 10.89           C  
ATOM   1144  C   SER A 170       4.425  14.779   1.557  1.00 10.50           C  
ATOM   1145  O   SER A 170       3.945  15.829   1.097  1.00 11.52           O  
ATOM   1146  CB  SER A 170       5.145  13.116  -0.161  1.00 11.44           C  
ATOM   1147  OG  SER A 170       6.210  12.728  -0.997  1.00 14.46           O  
ATOM   1148  N   ALA A 171       3.935  14.157   2.631  1.00  9.38           N  
ATOM   1149  CA  ALA A 171       2.785  14.668   3.376  1.00  9.05           C  
ATOM   1150  C   ALA A 171       3.144  15.907   4.191  1.00  8.72           C  
ATOM   1151  O   ALA A 171       2.317  16.801   4.355  1.00  8.86           O  
ATOM   1152  CB  ALA A 171       2.211  13.586   4.282  1.00  9.29           C  
ATOM   1153  N   TYR A 172       4.384  15.944   4.684  1.00  8.28           N  
ATOM   1154  CA  TYR A 172       4.858  17.031   5.530  1.00  7.76           C  
ATOM   1155  C   TYR A 172       6.220  17.530   5.055  1.00  8.11           C  
ATOM   1156  O   TYR A 172       7.240  17.264   5.708  1.00  7.75           O  
ATOM   1157  CB  TYR A 172       4.978  16.554   6.975  1.00  7.75           C  
ATOM   1158  CG  TYR A 172       3.679  16.186   7.660  1.00  6.65           C  
ATOM   1159  CD1 TYR A 172       3.323  14.845   7.852  1.00  6.62           C  
ATOM   1160  CD2 TYR A 172       2.841  17.176   8.183  1.00  7.22           C  
ATOM   1161  CE1 TYR A 172       2.143  14.505   8.512  1.00  6.54           C  
ATOM   1162  CE2 TYR A 172       1.666  16.850   8.835  1.00  8.22           C  
ATOM   1163  CZ  TYR A 172       1.323  15.516   9.006  1.00  6.29           C  
ATOM   1164  OH  TYR A 172       0.147  15.218   9.660  1.00  7.44           O  
ATOM   1165  N   PRO A 173       6.248  18.260   3.923  1.00  8.53           N  
ATOM   1166  CA  PRO A 173       7.507  18.748   3.342  1.00  9.23           C  
ATOM   1167  C   PRO A 173       8.357  19.493   4.364  1.00  9.10           C  
ATOM   1168  O   PRO A 173       7.839  20.339   5.093  1.00  9.58           O  
ATOM   1169  CB  PRO A 173       7.043  19.737   2.263  1.00  9.92           C  
ATOM   1170  CG  PRO A 173       5.665  19.292   1.903  1.00  9.18           C  
ATOM   1171  CD  PRO A 173       5.069  18.648   3.124  1.00  8.84           C  
ATOM   1172  N   GLY A 174       9.641  19.143   4.442  1.00  9.16           N  
ATOM   1173  CA  GLY A 174      10.590  19.895   5.263  1.00  9.55           C  
ATOM   1174  C   GLY A 174      10.477  19.682   6.764  1.00  9.71           C  
ATOM   1175  O   GLY A 174      11.111  20.406   7.539  1.00 11.17           O  
ATOM   1176  N   GLN A 175       9.683  18.694   7.182  1.00  9.21           N  
ATOM   1177  CA  GLN A 175       9.371  18.529   8.608  1.00  8.53           C  
ATOM   1178  C   GLN A 175       9.724  17.177   9.212  1.00  8.07           C  
ATOM   1179  O   GLN A 175       9.763  17.054  10.435  1.00  8.48           O  
ATOM   1180  CB  GLN A 175       7.891  18.808   8.868  1.00  8.38           C  
ATOM   1181  CG  GLN A 175       7.444  20.208   8.417  1.00  8.62           C  
ATOM   1182  CD  GLN A 175       5.963  20.265   8.106  1.00 11.32           C  
ATOM   1183  OE1 GLN A 175       5.551  20.389   6.941  1.00 13.78           O  
ATOM   1184  NE2 GLN A 175       5.154  20.155   9.139  1.00  9.46           N  
ATOM   1185  N   ILE A 176       9.948  16.165   8.375  1.00  7.35           N  
ATOM   1186  CA  ILE A 176      10.169  14.811   8.885  1.00  7.60           C  
ATOM   1187  C   ILE A 176      11.662  14.515   9.022  1.00  8.16           C  
ATOM   1188  O   ILE A 176      12.402  14.527   8.035  1.00  9.10           O  
ATOM   1189  CB  ILE A 176       9.484  13.758   7.978  1.00  7.49           C  
ATOM   1190  CG1 ILE A 176       7.991  14.079   7.812  1.00  7.80           C  
ATOM   1191  CG2 ILE A 176       9.714  12.342   8.523  1.00  7.62           C  
ATOM   1192  CD1 ILE A 176       7.188  14.105   9.126  1.00  7.36           C  
ATOM   1193  N   THR A 177      12.102  14.280  10.258  1.00  7.65           N  
ATOM   1194  CA  THR A 177      13.500  13.944  10.517  1.00  7.47           C  
ATOM   1195  C   THR A 177      13.669  12.426  10.590  1.00  7.34           C  
ATOM   1196  O   THR A 177      12.691  11.678  10.566  1.00  7.91           O  
ATOM   1197  CB  THR A 177      13.990  14.546  11.843  1.00  7.51           C  
ATOM   1198  OG1 THR A 177      13.376  13.840  12.929  1.00  7.22           O  
ATOM   1199  CG2 THR A 177      13.652  16.039  11.926  1.00  7.64           C  
ATOM   1200  N   SER A 178      14.917  11.983  10.719  1.00  6.90           N  
ATOM   1201  CA  SER A 178      15.220  10.566  10.857  1.00  7.63           C  
ATOM   1202  C   SER A 178      14.700   9.977  12.168  1.00  7.17           C  
ATOM   1203  O   SER A 178      14.735   8.760  12.350  1.00  7.62           O  
ATOM   1204  CB  SER A 178      16.731  10.331  10.735  1.00  7.84           C  
ATOM   1205  OG  SER A 178      17.409  10.946  11.808  1.00 11.54           O  
ATOM   1206  N   ASN A 179      14.216  10.839  13.066  1.00  6.81           N  
ATOM   1207  CA  ASN A 179      13.702  10.404  14.365  1.00  6.49           C  
ATOM   1208  C   ASN A 179      12.179  10.355  14.423  1.00  6.33           C  
ATOM   1209  O   ASN A 179      11.591  10.286  15.508  1.00  6.21           O  
ATOM   1210  CB  ASN A 179      14.241  11.335  15.444  1.00  6.47           C  
ATOM   1211  CG  ASN A 179      15.745  11.333  15.481  1.00  6.98           C  
ATOM   1212  OD1 ASN A 179      16.369  10.272  15.537  1.00  7.75           O  
ATOM   1213  ND2 ASN A 179      16.342  12.512  15.422  1.00  8.23           N  
ATOM   1214  N   MET A 180      11.550  10.378  13.244  1.00  6.42           N  
ATOM   1215  CA  MET A 180      10.094  10.396  13.133  1.00  6.61           C  
ATOM   1216  C   MET A 180       9.650   9.408  12.072  1.00  6.81           C  
ATOM   1217  O   MET A 180      10.371   9.155  11.097  1.00  7.38           O  
ATOM   1218  CB  MET A 180       9.616  11.779  12.691  1.00  6.89           C  
ATOM   1219  CG  MET A 180      10.072  12.918  13.585  1.00  7.19           C  
ATOM   1220  SD  MET A 180       9.624  14.484  12.819  1.00  7.34           S  
ATOM   1221  CE  MET A 180      10.400  15.632  13.972  1.00  7.14           C  
ATOM   1222  N   PHE A 181       8.468   8.836  12.264  1.00  6.58           N  
ATOM   1223  CA  PHE A 181       7.815   8.114  11.178  1.00  7.00           C  
ATOM   1224  C   PHE A 181       6.333   8.440  11.151  1.00  6.90           C  
ATOM   1225  O   PHE A 181       5.762   8.888  12.151  1.00  7.02           O  
ATOM   1226  CB  PHE A 181       8.059   6.597  11.258  1.00  7.31           C  
ATOM   1227  CG  PHE A 181       7.424   5.914  12.449  1.00  7.18           C  
ATOM   1228  CD1 PHE A 181       6.115   5.428  12.392  1.00  5.84           C  
ATOM   1229  CD2 PHE A 181       8.154   5.729  13.623  1.00  8.21           C  
ATOM   1230  CE1 PHE A 181       5.536   4.787  13.482  1.00  7.07           C  
ATOM   1231  CE2 PHE A 181       7.588   5.086  14.733  1.00  8.72           C  
ATOM   1232  CZ  PHE A 181       6.277   4.608  14.659  1.00  7.18           C  
ATOM   1233  N   CYS A 182       5.717   8.229   9.994  1.00  6.78           N  
ATOM   1234  CA  CYS A 182       4.270   8.397   9.871  1.00  6.72           C  
ATOM   1235  C   CYS A 182       3.572   7.054   9.986  1.00  6.89           C  
ATOM   1236  O   CYS A 182       4.084   6.039   9.533  1.00  6.63           O  
ATOM   1237  CB  CYS A 182       3.918   9.016   8.520  1.00  7.07           C  
ATOM   1238  SG  CYS A 182       4.336  10.768   8.361  1.00  8.13           S  
ATOM   1239  N   ALA A 183       2.387   7.060  10.579  1.00  6.39           N  
ATOM   1240  CA  ALA A 183       1.540   5.882  10.560  1.00  6.09           C  
ATOM   1241  C   ALA A 183       0.101   6.325  10.477  1.00  6.25           C  
ATOM   1242  O   ALA A 183      -0.250   7.414  10.937  1.00  6.38           O  
ATOM   1243  CB  ALA A 183       1.767   5.011  11.790  1.00  5.95           C  
ATOM   1244  N   GLY A 184      -0.723   5.481   9.871  1.00  6.27           N  
ATOM   1245  CA  GLY A 184      -2.130   5.792   9.721  1.00  6.67           C  
ATOM   1246  C   GLY A 184      -2.612   5.592   8.305  1.00  7.36           C  
ATOM   1247  O   GLY A 184      -2.245   4.611   7.650  1.00  7.75           O  
ATOM   1248  N   TYR A 184A     -3.434   6.534   7.843  1.00  7.93           N  
ATOM   1249  CA  TYR A 184A     -4.199   6.362   6.606  1.00  8.98           C  
ATOM   1250  C   TYR A 184A     -4.267   7.682   5.865  1.00  9.72           C  
ATOM   1251  O   TYR A 184A     -4.800   8.658   6.390  1.00 10.37           O  
ATOM   1252  CB  TYR A 184A     -5.612   5.874   6.939  1.00  9.19           C  
ATOM   1253  CG  TYR A 184A     -5.606   4.525   7.610  1.00  9.24           C  
ATOM   1254  CD1 TYR A 184A     -5.530   4.417   9.001  1.00  9.13           C  
ATOM   1255  CD2 TYR A 184A     -5.623   3.355   6.854  1.00  8.63           C  
ATOM   1256  CE1 TYR A 184A     -5.500   3.170   9.623  1.00  9.24           C  
ATOM   1257  CE2 TYR A 184A     -5.601   2.101   7.471  1.00  9.23           C  
ATOM   1258  CZ  TYR A 184A     -5.542   2.019   8.848  1.00  9.50           C  
ATOM   1259  OH  TYR A 184A     -5.505   0.782   9.461  1.00 10.83           O  
ATOM   1260  N   LEU A 185      -3.725   7.720   4.651  1.00 10.09           N  
ATOM   1261  CA  LEU A 185      -3.712   8.968   3.881  1.00 10.96           C  
ATOM   1262  C   LEU A 185      -5.113   9.480   3.529  1.00 11.27           C  
ATOM   1263  O   LEU A 185      -5.311  10.689   3.369  1.00 11.48           O  
ATOM   1264  CB  LEU A 185      -2.842   8.837   2.630  1.00 10.77           C  
ATOM   1265  CG  LEU A 185      -1.334   8.679   2.871  1.00 11.77           C  
ATOM   1266  CD1 LEU A 185      -0.582   8.565   1.551  1.00 12.80           C  
ATOM   1267  CD2 LEU A 185      -0.766   9.826   3.715  1.00 11.58           C  
ATOM   1268  N   GLU A 186      -6.083   8.568   3.455  1.00 11.64           N  
ATOM   1269  CA  GLU A 186      -7.467   8.937   3.160  1.00 12.67           C  
ATOM   1270  C   GLU A 186      -8.117   9.742   4.287  1.00 12.42           C  
ATOM   1271  O   GLU A 186      -9.150  10.384   4.077  1.00 13.27           O  
ATOM   1272  CB  GLU A 186      -8.315   7.696   2.847  1.00 13.10           C  
ATOM   1273  CG  GLU A 186      -8.388   6.664   3.977  1.00 16.63           C  
ATOM   1274  CD  GLU A 186      -7.412   5.505   3.800  1.00 19.79           C  
ATOM   1275  OE1 GLU A 186      -7.866   4.348   3.963  1.00 22.22           O  
ATOM   1276  OE2 GLU A 186      -6.208   5.736   3.500  1.00 20.07           O  
ATOM   1277  N   GLY A 187      -7.514   9.702   5.474  1.00 12.11           N  
ATOM   1278  CA  GLY A 187      -8.084  10.364   6.645  1.00 11.77           C  
ATOM   1279  C   GLY A 187      -9.131   9.511   7.353  1.00 11.28           C  
ATOM   1280  O   GLY A 187      -9.463   8.398   6.907  1.00 12.66           O  
ATOM   1281  N   GLY A 188      -9.636  10.037   8.467  1.00  9.94           N  
ATOM   1282  CA  GLY A 188     -10.682   9.371   9.246  1.00  9.13           C  
ATOM   1283  C   GLY A 188     -10.204   8.542  10.426  1.00  8.70           C  
ATOM   1284  O   GLY A 188     -10.985   8.237  11.325  1.00  8.96           O  
ATOM   1285  N   LYS A 188A     -8.930   8.157  10.418  1.00  8.07           N  
ATOM   1286  CA  LYS A 188A     -8.395   7.264  11.449  1.00  7.75           C  
ATOM   1287  C   LYS A 188A     -7.017   7.778  11.864  1.00  7.34           C  
ATOM   1288  O   LYS A 188A     -6.101   7.804  11.048  1.00  7.59           O  
ATOM   1289  CB  LYS A 188A     -8.264   5.845  10.897  1.00  8.09           C  
ATOM   1290  CG  LYS A 188A     -9.588   5.114  10.749  1.00 10.32           C  
ATOM   1291  CD  LYS A 188A     -9.422   3.768  10.044  1.00 13.89           C  
ATOM   1292  CE  LYS A 188A     -8.973   3.898   8.583  1.00 18.54           C  
ATOM   1293  NZ  LYS A 188A     -9.581   5.032   7.791  1.00 22.31           N  
ATOM   1294  N   ASP A 189      -6.870   8.183  13.125  1.00  6.61           N  
ATOM   1295  CA  ASP A 189      -5.628   8.846  13.564  1.00  6.21           C  
ATOM   1296  C   ASP A 189      -5.596   8.935  15.088  1.00  6.07           C  
ATOM   1297  O   ASP A 189      -6.622   8.763  15.740  1.00  6.42           O  
ATOM   1298  CB  ASP A 189      -5.596  10.275  12.974  1.00  6.01           C  
ATOM   1299  CG  ASP A 189      -4.197  10.904  12.921  1.00  7.43           C  
ATOM   1300  OD1 ASP A 189      -4.124  12.061  12.450  1.00  6.91           O  
ATOM   1301  OD2 ASP A 189      -3.187  10.280  13.328  1.00  6.63           O  
ATOM   1302  N   SER A 190      -4.425   9.209  15.652  1.00  5.85           N  
ATOM   1303  CA  SER A 190      -4.348   9.731  17.018  1.00  6.20           C  
ATOM   1304  C   SER A 190      -4.646  11.238  16.999  1.00  6.33           C  
ATOM   1305  O   SER A 190      -4.818  11.835  15.920  1.00  6.60           O  
ATOM   1306  CB  SER A 190      -2.987   9.427  17.664  1.00  6.66           C  
ATOM   1307  OG  SER A 190      -1.900   9.935  16.900  1.00  6.37           O  
ATOM   1308  N   CYS A 191      -4.718  11.852  18.179  1.00  6.07           N  
ATOM   1309  CA  CYS A 191      -5.176  13.233  18.280  1.00  6.48           C  
ATOM   1310  C   CYS A 191      -4.736  13.865  19.607  1.00  6.63           C  
ATOM   1311  O   CYS A 191      -4.067  13.210  20.408  1.00  6.91           O  
ATOM   1312  CB  CYS A 191      -6.698  13.252  18.117  1.00  6.49           C  
ATOM   1313  SG  CYS A 191      -7.413  14.845  17.671  1.00  7.03           S  
ATOM   1314  N   GLN A 192      -5.117  15.128  19.832  1.00  6.98           N  
ATOM   1315  CA  GLN A 192      -4.839  15.824  21.098  1.00  7.58           C  
ATOM   1316  C   GLN A 192      -5.221  14.939  22.274  1.00  6.87           C  
ATOM   1317  O   GLN A 192      -6.309  14.361  22.297  1.00  6.83           O  
ATOM   1318  CB  GLN A 192      -5.649  17.121  21.223  1.00  8.38           C  
ATOM   1319  CG  GLN A 192      -5.560  18.067  20.046  1.00 11.97           C  
ATOM   1320  CD  GLN A 192      -6.844  18.096  19.217  1.00 15.47           C  
ATOM   1321  OE1 GLN A 192      -7.966  18.086  19.756  1.00 17.02           O  
ATOM   1322  NE2 GLN A 192      -6.685  18.152  17.897  1.00 15.88           N  
ATOM   1323  N   GLY A 193      -4.341  14.861  23.261  1.00  6.22           N  
ATOM   1324  CA  GLY A 193      -4.621  14.068  24.446  1.00  6.04           C  
ATOM   1325  C   GLY A 193      -4.057  12.662  24.339  1.00  5.75           C  
ATOM   1326  O   GLY A 193      -3.935  11.966  25.357  1.00  5.47           O  
ATOM   1327  N   ASP A 194      -3.737  12.236  23.112  1.00  5.39           N  
ATOM   1328  CA  ASP A 194      -3.074  10.940  22.911  1.00  5.15           C  
ATOM   1329  C   ASP A 194      -1.559  11.053  23.004  1.00  4.78           C  
ATOM   1330  O   ASP A 194      -0.864  10.027  23.061  1.00  5.30           O  
ATOM   1331  CB  ASP A 194      -3.437  10.314  21.564  1.00  5.09           C  
ATOM   1332  CG  ASP A 194      -4.885   9.910  21.469  1.00  5.33           C  
ATOM   1333  OD1 ASP A 194      -5.460  10.101  20.376  1.00  6.29           O  
ATOM   1334  OD2 ASP A 194      -5.424   9.375  22.460  1.00  5.22           O  
ATOM   1335  N   SER A 195      -1.053  12.287  23.005  1.00  4.93           N  
ATOM   1336  CA  SER A 195       0.389  12.538  22.985  1.00  5.05           C  
ATOM   1337  C   SER A 195       1.117  11.767  24.057  1.00  4.23           C  
ATOM   1338  O   SER A 195       0.639  11.652  25.190  1.00  4.66           O  
ATOM   1339  CB  SER A 195       0.692  14.017  23.186  1.00  5.25           C  
ATOM   1340  OG  SER A 195       0.195  14.779  22.109  1.00  6.98           O  
ATOM   1341  N   GLY A 196       2.281  11.239  23.686  1.00  3.82           N  
ATOM   1342  CA  GLY A 196       3.115  10.496  24.627  1.00  4.39           C  
ATOM   1343  C   GLY A 196       2.789   9.020  24.687  1.00  4.40           C  
ATOM   1344  O   GLY A 196       3.557   8.233  25.245  1.00  4.73           O  
ATOM   1345  N   GLY A 197       1.639   8.643  24.131  1.00  4.51           N  
ATOM   1346  CA  GLY A 197       1.177   7.256  24.209  1.00  4.63           C  
ATOM   1347  C   GLY A 197       1.849   6.341  23.207  1.00  5.16           C  
ATOM   1348  O   GLY A 197       2.626   6.788  22.362  1.00  4.81           O  
ATOM   1349  N   PRO A 198       1.570   5.040  23.323  1.00  4.62           N  
ATOM   1350  CA  PRO A 198       2.293   4.007  22.565  1.00  5.08           C  
ATOM   1351  C   PRO A 198       1.841   3.770  21.133  1.00  5.29           C  
ATOM   1352  O   PRO A 198       0.648   3.865  20.807  1.00  5.17           O  
ATOM   1353  CB  PRO A 198       1.971   2.735  23.347  1.00  5.31           C  
ATOM   1354  CG  PRO A 198       0.596   2.999  23.900  1.00  5.26           C  
ATOM   1355  CD  PRO A 198       0.594   4.456  24.261  1.00  5.07           C  
ATOM   1356  N   VAL A 199       2.819   3.382  20.313  1.00  4.85           N  
ATOM   1357  CA  VAL A 199       2.580   2.706  19.047  1.00  5.29           C  
ATOM   1358  C   VAL A 199       3.330   1.383  19.181  1.00  5.26           C  
ATOM   1359  O   VAL A 199       4.567   1.372  19.262  1.00  5.08           O  
ATOM   1360  CB  VAL A 199       3.150   3.517  17.860  1.00  5.64           C  
ATOM   1361  CG1 VAL A 199       2.920   2.792  16.538  1.00  6.57           C  
ATOM   1362  CG2 VAL A 199       2.571   4.940  17.827  1.00  6.48           C  
ATOM   1363  N   VAL A 200       2.581   0.283  19.254  1.00  5.28           N  
ATOM   1364  CA  VAL A 200       3.178  -1.026  19.509  1.00  6.06           C  
ATOM   1365  C   VAL A 200       3.006  -1.903  18.275  1.00  6.10           C  
ATOM   1366  O   VAL A 200       1.909  -2.020  17.739  1.00  6.00           O  
ATOM   1367  CB  VAL A 200       2.574  -1.671  20.776  1.00  5.89           C  
ATOM   1368  CG1 VAL A 200       2.895  -3.164  20.864  1.00  7.04           C  
ATOM   1369  CG2 VAL A 200       3.103  -0.941  22.008  1.00  6.67           C  
ATOM   1370  N   CYS A 201       4.103  -2.502  17.821  1.00  6.35           N  
ATOM   1371  CA  CYS A 201       4.093  -3.326  16.615  1.00  7.23           C  
ATOM   1372  C   CYS A 201       4.798  -4.629  16.952  1.00  8.06           C  
ATOM   1373  O   CYS A 201       5.918  -4.612  17.450  1.00  7.74           O  
ATOM   1374  CB  CYS A 201       4.780  -2.615  15.437  1.00  7.94           C  
ATOM   1375  SG  CYS A 201       4.624  -0.807  15.434  1.00  8.15           S  
ATOM   1376  N   SER A 202       4.110  -5.747  16.722  1.00  8.70           N  
ATOM   1377  CA  SER A 202       4.643  -7.073  17.049  1.00  9.75           C  
ATOM   1378  C   SER A 202       5.172  -7.157  18.490  1.00  9.68           C  
ATOM   1379  O   SER A 202       6.226  -7.738  18.748  1.00 10.19           O  
ATOM   1380  CB  SER A 202       5.711  -7.468  16.024  1.00  9.85           C  
ATOM   1381  OG  SER A 202       5.141  -7.424  14.726  1.00 14.41           O  
ATOM   1382  N   GLY A 203       4.429  -6.554  19.418  1.00  9.89           N  
ATOM   1383  CA  GLY A 203       4.748  -6.616  20.844  1.00 10.05           C  
ATOM   1384  C   GLY A 203       5.909  -5.743  21.277  1.00 10.49           C  
ATOM   1385  O   GLY A 203       6.434  -5.909  22.382  1.00 10.69           O  
ATOM   1386  N   LYS A 204       6.302  -4.834  20.424  1.00 10.70           N  
ATOM   1387  CA  LYS A 204       7.382  -3.928  20.799  1.00 12.01           C  
ATOM   1388  C   LYS A 204       6.944  -2.457  20.620  1.00 12.17           C  
ATOM   1389  O   LYS A 204       6.254  -2.101  19.764  1.00  9.98           O  
ATOM   1390  CB  LYS A 204       8.696  -4.217  20.051  1.00 13.18           C  
ATOM   1391  CG  LYS A 204       9.166  -5.678  20.039  1.00 15.60           C  
ATOM   1392  CD  LYS A 204       9.598  -6.171  21.343  1.00 17.57           C  
ATOM   1393  CE  LYS A 204       9.820  -7.703  21.344  1.00 19.40           C  
ATOM   1394  NZ  LYS A 204      11.074  -8.193  21.138  1.00 19.77           N  
ATOM   1395  N   LEU A 209       7.463  -1.617  21.547  1.00  9.27           N  
ATOM   1396  CA  LEU A 209       7.175  -0.175  21.495  1.00  8.46           C  
ATOM   1397  C   LEU A 209       8.017   0.482  20.429  1.00  8.68           C  
ATOM   1398  O   LEU A 209       9.106   0.729  20.626  1.00  9.58           O  
ATOM   1399  CB  LEU A 209       7.471   0.479  22.849  1.00  9.11           C  
ATOM   1400  CG  LEU A 209       7.104   1.969  22.909  1.00  8.87           C  
ATOM   1401  CD1 LEU A 209       5.630   2.210  22.810  1.00  9.05           C  
ATOM   1402  CD2 LEU A 209       7.628   2.539  24.222  1.00 10.85           C  
ATOM   1403  N   GLN A 210       7.395   0.771  19.310  1.00  7.47           N  
ATOM   1404  CA  GLN A 210       8.127   1.347  18.177  1.00  6.94           C  
ATOM   1405  C   GLN A 210       7.928   2.854  18.004  1.00  6.49           C  
ATOM   1406  O   GLN A 210       8.740   3.523  17.356  1.00  6.65           O  
ATOM   1407  CB  GLN A 210       7.771   0.620  16.869  1.00  6.99           C  
ATOM   1408  CG  GLN A 210       8.186  -0.865  16.826  1.00  7.49           C  
ATOM   1409  CD  GLN A 210       9.665  -1.098  16.487  1.00  9.90           C  
ATOM   1410  OE1 GLN A 210      10.131  -2.244  16.420  1.00 10.98           O  
ATOM   1411  NE2 GLN A 210      10.395  -0.029  16.256  1.00  8.59           N  
ATOM   1412  N   GLY A 211       6.851   3.388  18.586  1.00  5.74           N  
ATOM   1413  CA  GLY A 211       6.529   4.792  18.396  1.00  5.26           C  
ATOM   1414  C   GLY A 211       5.926   5.443  19.622  1.00  5.23           C  
ATOM   1415  O   GLY A 211       5.461   4.766  20.545  1.00  5.70           O  
ATOM   1416  N   ILE A 212       5.956   6.769  19.614  1.00  4.22           N  
ATOM   1417  CA  ILE A 212       5.324   7.585  20.632  1.00  4.40           C  
ATOM   1418  C   ILE A 212       4.477   8.606  19.900  1.00  4.09           C  
ATOM   1419  O   ILE A 212       4.957   9.240  18.956  1.00  4.96           O  
ATOM   1420  CB  ILE A 212       6.381   8.339  21.450  1.00  3.75           C  
ATOM   1421  CG1 ILE A 212       7.314   7.361  22.162  1.00  5.96           C  
ATOM   1422  CG2 ILE A 212       5.725   9.253  22.462  1.00  4.34           C  
ATOM   1423  CD1 ILE A 212       8.555   8.027  22.686  1.00  7.89           C  
ATOM   1424  N   VAL A 213       3.222   8.770  20.328  1.00  4.37           N  
ATOM   1425  CA  VAL A 213       2.334   9.769  19.708  1.00  4.62           C  
ATOM   1426  C   VAL A 213       2.973  11.156  19.843  1.00  4.76           C  
ATOM   1427  O   VAL A 213       3.205  11.632  20.968  1.00  5.29           O  
ATOM   1428  CB  VAL A 213       0.944   9.781  20.359  1.00  4.59           C  
ATOM   1429  CG1 VAL A 213       0.052  10.831  19.706  1.00  5.85           C  
ATOM   1430  CG2 VAL A 213       0.294   8.397  20.259  1.00  4.98           C  
ATOM   1431  N   SER A 214       3.269  11.790  18.704  1.00  4.96           N  
ATOM   1432  CA  SER A 214       4.038  13.047  18.716  1.00  5.23           C  
ATOM   1433  C   SER A 214       3.276  14.253  18.148  1.00  5.43           C  
ATOM   1434  O   SER A 214       3.011  15.221  18.866  1.00  5.62           O  
ATOM   1435  CB  SER A 214       5.404  12.864  18.023  1.00  5.75           C  
ATOM   1436  OG  SER A 214       6.219  14.021  18.154  1.00  5.15           O  
ATOM   1437  N   TRP A 215       2.939  14.218  16.865  1.00  5.77           N  
ATOM   1438  CA  TRP A 215       2.291  15.378  16.248  1.00  5.42           C  
ATOM   1439  C   TRP A 215       1.590  15.047  14.947  1.00  6.34           C  
ATOM   1440  O   TRP A 215       1.597  13.911  14.505  1.00  5.92           O  
ATOM   1441  CB  TRP A 215       3.289  16.539  16.056  1.00  5.56           C  
ATOM   1442  CG  TRP A 215       4.438  16.277  15.109  1.00  6.59           C  
ATOM   1443  CD1 TRP A 215       5.612  15.623  15.385  1.00  5.63           C  
ATOM   1444  CD2 TRP A 215       4.524  16.699  13.744  1.00  5.70           C  
ATOM   1445  NE1 TRP A 215       6.423  15.602  14.260  1.00  6.58           N  
ATOM   1446  CE2 TRP A 215       5.779  16.257  13.242  1.00  6.14           C  
ATOM   1447  CE3 TRP A 215       3.662  17.396  12.890  1.00  7.01           C  
ATOM   1448  CZ2 TRP A 215       6.188  16.501  11.921  1.00  6.50           C  
ATOM   1449  CZ3 TRP A 215       4.072  17.635  11.577  1.00  6.97           C  
ATOM   1450  CH2 TRP A 215       5.328  17.197  11.113  1.00  5.54           C  
ATOM   1451  N   GLY A 216       0.960  16.062  14.363  1.00  6.71           N  
ATOM   1452  CA  GLY A 216       0.254  15.932  13.094  1.00  7.43           C  
ATOM   1453  C   GLY A 216      -0.525  17.203  12.836  1.00  8.29           C  
ATOM   1454  O   GLY A 216      -0.697  18.023  13.744  1.00  9.43           O  
ATOM   1455  N   SER A 217      -1.014  17.366  11.611  1.00  8.33           N  
ATOM   1456  CA  SER A 217      -1.866  18.501  11.275  1.00  9.15           C  
ATOM   1457  C   SER A 217      -3.316  18.159  11.598  1.00  8.65           C  
ATOM   1458  O   SER A 217      -3.937  17.347  10.912  1.00  7.82           O  
ATOM   1459  CB  SER A 217      -1.724  18.861   9.795  1.00  9.79           C  
ATOM   1460  OG  SER A 217      -2.365  20.091   9.506  1.00 13.50           O  
ATOM   1461  N   GLY A 219      -3.850  18.772  12.650  1.00  9.21           N  
ATOM   1462  CA  GLY A 219      -5.185  18.443  13.116  1.00  8.54           C  
ATOM   1463  C   GLY A 219      -5.220  16.980  13.507  1.00  8.48           C  
ATOM   1464  O   GLY A 219      -4.280  16.480  14.124  1.00  9.21           O  
ATOM   1465  N   CYS A 220      -6.292  16.282  13.144  1.00  8.02           N  
ATOM   1466  CA  CYS A 220      -6.347  14.838  13.374  1.00  7.64           C  
ATOM   1467  C   CYS A 220      -7.212  14.197  12.316  1.00  7.91           C  
ATOM   1468  O   CYS A 220      -8.311  14.684  12.034  1.00  7.88           O  
ATOM   1469  CB  CYS A 220      -6.955  14.532  14.737  1.00  8.36           C  
ATOM   1470  SG  CYS A 220      -6.278  15.499  16.092  1.00  8.38           S  
ATOM   1471  N   ALA A 221      -6.721  13.096  11.753  1.00  8.14           N  
ATOM   1472  CA  ALA A 221      -7.484  12.287  10.804  1.00  8.44           C  
ATOM   1473  C   ALA A 221      -7.833  13.062   9.530  1.00  9.31           C  
ATOM   1474  O   ALA A 221      -8.813  12.753   8.853  1.00  9.25           O  
ATOM   1475  CB  ALA A 221      -8.736  11.713  11.481  1.00  8.48           C  
ATOM   1476  N   GLN A 221A     -7.016  14.059   9.205  1.00  9.33           N  
ATOM   1477  CA  GLN A 221A     -7.225  14.842   7.987  1.00 10.00           C  
ATOM   1478  C   GLN A 221A     -6.614  14.119   6.804  1.00  9.93           C  
ATOM   1479  O   GLN A 221A     -5.580  13.467   6.935  1.00  9.78           O  
ATOM   1480  CB  GLN A 221A     -6.570  16.218   8.116  1.00 10.53           C  
ATOM   1481  CG  GLN A 221A     -7.130  17.082   9.226  1.00 12.47           C  
ATOM   1482  CD  GLN A 221A     -8.609  17.328   9.073  1.00 16.10           C  
ATOM   1483  OE1 GLN A 221A     -9.067  17.814   8.038  1.00 17.50           O  
ATOM   1484  NE2 GLN A 221A     -9.374  16.978  10.100  1.00 18.93           N  
ATOM   1485  N   LYS A 222      -7.240  14.265   5.639  1.00 10.09           N  
ATOM   1486  CA  LYS A 222      -6.721  13.661   4.413  1.00 10.89           C  
ATOM   1487  C   LYS A 222      -5.291  14.136   4.159  1.00 10.88           C  
ATOM   1488  O   LYS A 222      -4.996  15.328   4.267  1.00 10.80           O  
ATOM   1489  CB  LYS A 222      -7.619  14.018   3.220  1.00 11.19           C  
ATOM   1490  CG  LYS A 222      -7.272  13.285   1.942  1.00 13.84           C  
ATOM   1491  CD  LYS A 222      -8.218  13.651   0.800  1.00 16.19           C  
ATOM   1492  CE  LYS A 222      -7.646  13.179  -0.536  1.00 20.06           C  
ATOM   1493  NZ  LYS A 222      -8.474  13.609  -1.704  1.00 22.96           N  
ATOM   1494  N   ASN A 223      -4.412  13.191   3.833  1.00 10.85           N  
ATOM   1495  CA  ASN A 223      -3.011  13.488   3.512  1.00 11.63           C  
ATOM   1496  C   ASN A 223      -2.188  14.075   4.660  1.00 11.37           C  
ATOM   1497  O   ASN A 223      -1.104  14.640   4.441  1.00 12.32           O  
ATOM   1498  CB  ASN A 223      -2.918  14.360   2.251  1.00 12.09           C  
ATOM   1499  CG  ASN A 223      -3.334  13.603   1.001  1.00 14.60           C  
ATOM   1500  OD1 ASN A 223      -3.007  12.423   0.846  1.00 18.86           O  
ATOM   1501  ND2 ASN A 223      -4.079  14.266   0.118  1.00 17.08           N  
ATOM   1502  N   LYS A 224      -2.700  13.934   5.882  1.00 10.51           N  
ATOM   1503  CA  LYS A 224      -2.000  14.413   7.072  1.00  9.77           C  
ATOM   1504  C   LYS A 224      -1.974  13.325   8.137  1.00  9.03           C  
ATOM   1505  O   LYS A 224      -2.665  13.410   9.155  1.00  8.80           O  
ATOM   1506  CB  LYS A 224      -2.622  15.708   7.600  1.00  9.93           C  
ATOM   1507  CG  LYS A 224      -2.472  16.894   6.633  1.00 10.81           C  
ATOM   1508  CD  LYS A 224      -0.997  17.274   6.473  1.00 12.88           C  
ATOM   1509  CE  LYS A 224      -0.810  18.383   5.464  1.00 12.22           C  
ATOM   1510  NZ  LYS A 224       0.611  18.833   5.376  1.00 11.49           N  
ATOM   1511  N   PRO A 225      -1.165  12.283   7.899  1.00  8.76           N  
ATOM   1512  CA  PRO A 225      -1.146  11.176   8.852  1.00  8.05           C  
ATOM   1513  C   PRO A 225      -0.467  11.553  10.168  1.00  7.57           C  
ATOM   1514  O   PRO A 225       0.153  12.613  10.276  1.00  7.01           O  
ATOM   1515  CB  PRO A 225      -0.355  10.098   8.107  1.00  7.92           C  
ATOM   1516  CG  PRO A 225       0.592  10.881   7.231  1.00  8.77           C  
ATOM   1517  CD  PRO A 225      -0.234  12.060   6.775  1.00  8.61           C  
ATOM   1518  N   GLY A 226      -0.627  10.702  11.178  1.00  7.16           N  
ATOM   1519  CA  GLY A 226       0.060  10.918  12.442  1.00  6.24           C  
ATOM   1520  C   GLY A 226       1.563  10.763  12.302  1.00  6.08           C  
ATOM   1521  O   GLY A 226       2.040   9.918  11.535  1.00  6.23           O  
ATOM   1522  N   VAL A 227       2.292  11.597  13.047  1.00  5.56           N  
ATOM   1523  CA  VAL A 227       3.747  11.538  13.126  1.00  5.49           C  
ATOM   1524  C   VAL A 227       4.149  11.085  14.530  1.00  5.70           C  
ATOM   1525  O   VAL A 227       3.614  11.568  15.547  1.00  5.54           O  
ATOM   1526  CB  VAL A 227       4.404  12.888  12.756  1.00  5.21           C  
ATOM   1527  CG1 VAL A 227       5.910  12.693  12.533  1.00  6.66           C  
ATOM   1528  CG2 VAL A 227       3.777  13.442  11.508  1.00  5.81           C  
ATOM   1529  N   TYR A 228       5.072  10.127  14.561  1.00  5.04           N  
ATOM   1530  CA  TYR A 228       5.446   9.412  15.768  1.00  4.86           C  
ATOM   1531  C   TYR A 228       6.952   9.432  15.988  1.00  4.81           C  
ATOM   1532  O   TYR A 228       7.724   9.342  15.036  1.00  4.74           O  
ATOM   1533  CB  TYR A 228       4.934   7.966  15.666  1.00  4.97           C  
ATOM   1534  CG  TYR A 228       3.433   7.954  15.524  1.00  4.55           C  
ATOM   1535  CD1 TYR A 228       2.622   8.006  16.648  1.00  5.54           C  
ATOM   1536  CD2 TYR A 228       2.822   7.927  14.263  1.00  4.65           C  
ATOM   1537  CE1 TYR A 228       1.249   8.022  16.542  1.00  4.73           C  
ATOM   1538  CE2 TYR A 228       1.432   7.954  14.138  1.00  4.42           C  
ATOM   1539  CZ  TYR A 228       0.651   7.994  15.289  1.00  5.16           C  
ATOM   1540  OH  TYR A 228      -0.725   8.013  15.211  1.00  5.81           O  
ATOM   1541  N   THR A 229       7.364   9.544  17.248  1.00  4.26           N  
ATOM   1542  CA  THR A 229       8.772   9.428  17.592  1.00  4.36           C  
ATOM   1543  C   THR A 229       9.254   8.015  17.332  1.00  4.84           C  
ATOM   1544  O   THR A 229       8.609   7.050  17.749  1.00  4.84           O  
ATOM   1545  CB  THR A 229       9.012   9.796  19.065  1.00  4.36           C  
ATOM   1546  OG1 THR A 229       8.347  11.030  19.336  1.00  4.52           O  
ATOM   1547  CG2 THR A 229      10.517   9.924  19.364  1.00  5.46           C  
ATOM   1548  N   LYS A 230      10.399   7.912  16.657  1.00  4.89           N  
ATOM   1549  CA  LYS A 230      10.960   6.625  16.244  1.00  4.97           C  
ATOM   1550  C   LYS A 230      11.793   5.993  17.373  1.00  5.10           C  
ATOM   1551  O   LYS A 230      13.002   6.214  17.475  1.00  4.86           O  
ATOM   1552  CB  LYS A 230      11.775   6.801  14.959  1.00  5.53           C  
ATOM   1553  CG  LYS A 230      12.187   5.502  14.296  1.00  6.94           C  
ATOM   1554  CD  LYS A 230      12.779   5.786  12.928  1.00  7.26           C  
ATOM   1555  CE  LYS A 230      13.356   4.514  12.340  1.00  9.38           C  
ATOM   1556  NZ  LYS A 230      13.588   4.638  10.874  1.00 12.00           N  
ATOM   1557  N   VAL A 231      11.128   5.196  18.206  1.00  5.11           N  
ATOM   1558  CA  VAL A 231      11.700   4.719  19.473  1.00  5.32           C  
ATOM   1559  C   VAL A 231      12.984   3.911  19.286  1.00  5.60           C  
ATOM   1560  O   VAL A 231      13.881   3.961  20.131  1.00  5.82           O  
ATOM   1561  CB  VAL A 231      10.639   3.913  20.297  1.00  5.20           C  
ATOM   1562  CG1 VAL A 231      11.258   3.223  21.504  1.00  5.72           C  
ATOM   1563  CG2 VAL A 231       9.486   4.821  20.746  1.00  5.87           C  
ATOM   1564  N   CYS A 232      13.082   3.164  18.183  1.00  5.66           N  
ATOM   1565  CA  CYS A 232      14.259   2.315  17.986  1.00  6.29           C  
ATOM   1566  C   CYS A 232      15.563   3.117  17.985  1.00  6.53           C  
ATOM   1567  O   CYS A 232      16.625   2.589  18.338  1.00  7.74           O  
ATOM   1568  CB  CYS A 232      14.123   1.459  16.734  1.00  6.73           C  
ATOM   1569  SG  CYS A 232      14.041   2.407  15.230  1.00  7.77           S  
ATOM   1570  N   ASN A 233      15.487   4.395  17.616  1.00  6.08           N  
ATOM   1571  CA  ASN A 233      16.666   5.266  17.614  1.00  5.97           C  
ATOM   1572  C   ASN A 233      17.189   5.580  19.016  1.00  6.46           C  
ATOM   1573  O   ASN A 233      18.326   6.056  19.168  1.00  7.54           O  
ATOM   1574  CB  ASN A 233      16.348   6.609  16.944  1.00  5.92           C  
ATOM   1575  CG  ASN A 233      16.151   6.512  15.432  1.00  6.44           C  
ATOM   1576  OD1 ASN A 233      15.924   7.542  14.772  1.00  9.09           O  
ATOM   1577  ND2 ASN A 233      16.231   5.316  14.875  1.00  5.42           N  
ATOM   1578  N   TYR A 234      16.357   5.319  20.021  1.00  6.30           N  
ATOM   1579  CA  TYR A 234      16.586   5.792  21.386  1.00  5.93           C  
ATOM   1580  C   TYR A 234      16.872   4.701  22.397  1.00  6.46           C  
ATOM   1581  O   TYR A 234      16.996   4.985  23.584  1.00  7.49           O  
ATOM   1582  CB  TYR A 234      15.390   6.637  21.868  1.00  5.83           C  
ATOM   1583  CG  TYR A 234      15.195   7.843  20.991  1.00  5.15           C  
ATOM   1584  CD1 TYR A 234      15.970   8.989  21.169  1.00  4.23           C  
ATOM   1585  CD2 TYR A 234      14.270   7.823  19.948  1.00  5.37           C  
ATOM   1586  CE1 TYR A 234      15.814  10.093  20.329  1.00  4.97           C  
ATOM   1587  CE2 TYR A 234      14.112   8.909  19.106  1.00  5.09           C  
ATOM   1588  CZ  TYR A 234      14.889  10.044  19.313  1.00  5.89           C  
ATOM   1589  OH  TYR A 234      14.733  11.127  18.495  1.00  6.85           O  
ATOM   1590  N   VAL A 235      16.938   3.454  21.944  1.00  6.99           N  
ATOM   1591  CA  VAL A 235      17.098   2.333  22.880  1.00  7.42           C  
ATOM   1592  C   VAL A 235      18.365   2.457  23.723  1.00  7.47           C  
ATOM   1593  O   VAL A 235      18.312   2.234  24.937  1.00  7.77           O  
ATOM   1594  CB  VAL A 235      17.016   0.961  22.166  1.00  7.62           C  
ATOM   1595  CG1 VAL A 235      17.280  -0.186  23.138  1.00  8.61           C  
ATOM   1596  CG2 VAL A 235      15.639   0.786  21.552  1.00  9.05           C  
ATOM   1597  N   SER A 236      19.479   2.843  23.100  1.00  7.55           N  
ATOM   1598  CA ASER A 236      20.733   2.997  23.835  0.30  7.45           C  
ATOM   1599  CA BSER A 236      20.741   3.009  23.826  0.70  8.08           C  
ATOM   1600  C   SER A 236      20.617   4.089  24.895  1.00  7.39           C  
ATOM   1601  O   SER A 236      21.029   3.893  26.040  1.00  8.00           O  
ATOM   1602  CB ASER A 236      21.899   3.277  22.887  0.30  7.72           C  
ATOM   1603  CB BSER A 236      21.887   3.360  22.876  0.70  8.77           C  
ATOM   1604  OG ASER A 236      22.198   2.124  22.122  0.30  7.68           O  
ATOM   1605  OG BSER A 236      23.116   3.387  23.578  0.70 12.80           O  
ATOM   1606  N   TRP A 237      20.045   5.227  24.511  1.00  7.05           N  
ATOM   1607  CA  TRP A 237      19.844   6.327  25.449  1.00  6.55           C  
ATOM   1608  C   TRP A 237      18.917   5.896  26.588  1.00  7.00           C  
ATOM   1609  O   TRP A 237      19.180   6.184  27.761  1.00  6.98           O  
ATOM   1610  CB  TRP A 237      19.293   7.580  24.745  1.00  7.32           C  
ATOM   1611  CG  TRP A 237      18.874   8.664  25.698  1.00  5.99           C  
ATOM   1612  CD1 TRP A 237      19.688   9.513  26.397  1.00  5.61           C  
ATOM   1613  CD2 TRP A 237      17.529   9.011  26.054  1.00  5.45           C  
ATOM   1614  NE1 TRP A 237      18.930  10.371  27.164  1.00  6.65           N  
ATOM   1615  CE2 TRP A 237      17.602  10.077  26.984  1.00  5.71           C  
ATOM   1616  CE3 TRP A 237      16.268   8.522  25.680  1.00  4.99           C  
ATOM   1617  CZ2 TRP A 237      16.456  10.675  27.529  1.00  6.08           C  
ATOM   1618  CZ3 TRP A 237      15.130   9.107  26.230  1.00  6.12           C  
ATOM   1619  CH2 TRP A 237      15.234  10.172  27.149  1.00  6.24           C  
ATOM   1620  N   ILE A 238      17.837   5.195  26.251  1.00  6.74           N  
ATOM   1621  CA  ILE A 238      16.913   4.742  27.279  1.00  6.76           C  
ATOM   1622  C   ILE A 238      17.620   3.822  28.271  1.00  7.19           C  
ATOM   1623  O   ILE A 238      17.534   4.020  29.477  1.00  7.20           O  
ATOM   1624  CB  ILE A 238      15.679   4.051  26.673  1.00  7.07           C  
ATOM   1625  CG1 ILE A 238      14.848   5.084  25.910  1.00  5.89           C  
ATOM   1626  CG2 ILE A 238      14.840   3.389  27.759  1.00  7.28           C  
ATOM   1627  CD1 ILE A 238      13.721   4.486  25.068  1.00  5.52           C  
ATOM   1628  N   LYS A 239      18.330   2.824  27.760  1.00  7.33           N  
ATOM   1629  CA  LYS A 239      18.967   1.851  28.651  1.00  7.84           C  
ATOM   1630  C   LYS A 239      20.036   2.494  29.540  1.00  7.99           C  
ATOM   1631  O   LYS A 239      20.120   2.204  30.739  1.00  8.34           O  
ATOM   1632  CB  LYS A 239      19.555   0.697  27.836  1.00  8.42           C  
ATOM   1633  CG  LYS A 239      18.496  -0.137  27.166  1.00 11.44           C  
ATOM   1634  CD  LYS A 239      19.120  -1.262  26.367  1.00 16.17           C  
ATOM   1635  CE  LYS A 239      18.103  -2.348  26.080  1.00 20.11           C  
ATOM   1636  NZ  LYS A 239      18.727  -3.474  25.324  1.00 23.53           N  
ATOM   1637  N   GLN A 240      20.835   3.383  28.955  1.00  8.14           N  
ATOM   1638  CA  GLN A 240      21.914   4.031  29.700  1.00  9.19           C  
ATOM   1639  C   GLN A 240      21.339   4.973  30.744  1.00  8.55           C  
ATOM   1640  O   GLN A 240      21.846   5.069  31.872  1.00  8.64           O  
ATOM   1641  CB  GLN A 240      22.831   4.792  28.749  1.00 10.28           C  
ATOM   1642  CG  GLN A 240      23.746   3.906  27.931  1.00 14.68           C  
ATOM   1643  CD  GLN A 240      24.438   4.657  26.803  1.00 19.56           C  
ATOM   1644  OE1 GLN A 240      24.329   5.884  26.694  1.00 23.35           O  
ATOM   1645  NE2 GLN A 240      25.143   3.921  25.948  1.00 22.86           N  
ATOM   1646  N   THR A 241      20.266   5.666  30.374  1.00  7.64           N  
ATOM   1647  CA  THR A 241      19.641   6.599  31.296  1.00  7.37           C  
ATOM   1648  C   THR A 241      19.067   5.854  32.494  1.00  7.63           C  
ATOM   1649  O   THR A 241      19.284   6.246  33.652  1.00  7.81           O  
ATOM   1650  CB  THR A 241      18.581   7.465  30.587  1.00  7.20           C  
ATOM   1651  OG1 THR A 241      19.226   8.223  29.557  1.00  7.00           O  
ATOM   1652  CG2 THR A 241      17.903   8.405  31.585  1.00  7.81           C  
ATOM   1653  N   ILE A 242      18.341   4.773  32.221  1.00  7.35           N  
ATOM   1654  CA  ILE A 242      17.786   3.953  33.298  1.00  7.75           C  
ATOM   1655  C   ILE A 242      18.885   3.366  34.189  1.00  8.01           C  
ATOM   1656  O   ILE A 242      18.720   3.307  35.414  1.00  9.05           O  
ATOM   1657  CB  ILE A 242      16.871   2.845  32.738  1.00  7.97           C  
ATOM   1658  CG1 ILE A 242      15.589   3.473  32.191  1.00  9.16           C  
ATOM   1659  CG2 ILE A 242      16.568   1.796  33.815  1.00  7.83           C  
ATOM   1660  CD1 ILE A 242      14.670   2.485  31.491  1.00 10.31           C  
ATOM   1661  N   ALA A 243      20.003   2.967  33.582  1.00  7.95           N  
ATOM   1662  CA  ALA A 243      21.100   2.333  34.331  1.00  8.33           C  
ATOM   1663  C   ALA A 243      21.752   3.252  35.361  1.00  8.66           C  
ATOM   1664  O   ALA A 243      22.380   2.762  36.306  1.00  9.54           O  
ATOM   1665  CB  ALA A 243      22.159   1.811  33.377  1.00  8.24           C  
ATOM   1666  N   SER A 244      21.621   4.568  35.171  1.00  9.05           N  
ATOM   1667  CA  SER A 244      22.300   5.551  36.029  1.00  9.08           C  
ATOM   1668  C   SER A 244      21.372   6.519  36.766  1.00  9.17           C  
ATOM   1669  O   SER A 244      21.828   7.499  37.353  1.00  9.41           O  
ATOM   1670  CB  SER A 244      23.341   6.345  35.229  1.00  9.70           C  
ATOM   1671  OG  SER A 244      24.450   5.521  34.883  1.00 12.29           O  
ATOM   1672  N   ASN A 245      20.075   6.233  36.752  1.00  8.47           N  
ATOM   1673  CA  ASN A 245      19.110   7.107  37.405  1.00  8.54           C  
ATOM   1674  C   ASN A 245      18.074   6.332  38.183  1.00  8.77           C  
ATOM   1675  O   ASN A 245      17.131   6.930  38.705  1.00  8.66           O  
ATOM   1676  CB  ASN A 245      18.434   7.993  36.371  1.00  8.61           C  
ATOM   1677  CG  ASN A 245      19.365   9.053  35.829  1.00  9.34           C  
ATOM   1678  OD1 ASN A 245      19.532  10.125  36.427  1.00  9.48           O  
ATOM   1679  ND2 ASN A 245      19.982   8.761  34.688  1.00  8.70           N  
ATOM   1680  OXT ASN A 245      18.170   5.108  38.284  1.00  8.84           O  
TER    1681      ASN A 245                                                      
HETATM 1682 CA    CA A 247     -10.114   4.355  36.532  1.00  6.77          CA  
HETATM 1683  N2  PBZ A   1      -2.852  13.941  14.088  1.00  7.64           N  
HETATM 1684  N3  PBZ A   1      -1.717  12.159  14.958  1.00  7.44           N  
HETATM 1685  C7  PBZ A   1      -2.118  13.428  15.066  1.00  9.54           C  
HETATM 1686  C4  PBZ A   1      -1.775  14.268  16.268  1.00  9.86           C  
HETATM 1687  C2  PBZ A   1      -1.046  14.404  18.571  1.00 10.88           C  
HETATM 1688  C3  PBZ A   1      -1.348  13.648  17.443  1.00  9.80           C  
HETATM 1689  C5  PBZ A   1      -1.887  15.660  16.224  1.00 11.58           C  
HETATM 1690  C6  PBZ A   1      -1.576  16.415  17.361  1.00 11.21           C  
HETATM 1691  C1  PBZ A   1      -1.165  15.787  18.532  1.00 11.14           C  
HETATM 1692  N1  PBZ A   1      -0.860  16.518  19.637  1.00 12.15           N  
HETATM 1693  C1  EDO A 246      -5.580   4.216  43.954  1.00 19.26           C  
HETATM 1694  O1  EDO A 246      -5.641   3.557  45.221  1.00 20.21           O  
HETATM 1695  C2  EDO A 246      -4.584   3.478  43.076  1.00 17.48           C  
HETATM 1696  O2  EDO A 246      -3.260   3.690  43.588  1.00 16.05           O  
HETATM 1697  C1  EDO A   2      16.600  20.216  14.674  1.00 20.66           C  
HETATM 1698  O1  EDO A   2      15.242  20.405  15.081  1.00 17.58           O  
HETATM 1699  C2  EDO A   2      17.418  19.988  15.919  1.00 21.43           C  
HETATM 1700  O2  EDO A   2      17.019  18.732  16.446  1.00 17.99           O  
HETATM 1701  C1  EDO A   3       7.633  14.803  -2.878  1.00 39.43           C  
HETATM 1702  O1  EDO A   3       6.218  15.023  -2.767  1.00 39.44           O  
HETATM 1703  C2  EDO A   3       8.397  16.119  -2.758  1.00 38.93           C  
HETATM 1704  O2  EDO A   3       7.912  16.873  -1.639  1.00 38.55           O  
HETATM 1705  C1  EDO A   4      11.143   4.822   0.838  1.00 24.35           C  
HETATM 1706  O1  EDO A   4      10.101   5.477   1.566  1.00 21.91           O  
HETATM 1707  C2  EDO A   4      11.886   5.849  -0.005  1.00 25.31           C  
HETATM 1708  O2  EDO A   4      12.625   6.705   0.871  1.00 25.81           O  
HETATM 1709  C1  EDO A   5      -9.616   9.919  40.030  1.00 20.30           C  
HETATM 1710  O1  EDO A   5      -9.966  10.876  39.021  1.00 21.28           O  
HETATM 1711  C2  EDO A   5      -9.995   8.498  39.610  1.00 20.81           C  
HETATM 1712  O2  EDO A   5     -10.692   8.516  38.358  1.00 22.16           O  
HETATM 1713  S   SO4 A 248      10.284  -7.543   9.551  0.75 10.00           S  
HETATM 1714  O1  SO4 A 248       9.536  -6.330   9.213  0.75 10.20           O  
HETATM 1715  O2  SO4 A 248       9.466  -8.710   9.214  0.75 11.61           O  
HETATM 1716  O3  SO4 A 248      11.533  -7.569   8.787  0.75 10.54           O  
HETATM 1717  O4  SO4 A 248      10.618  -7.546  10.975  0.75 11.69           O  
HETATM 1718  S   SO4 A 249     -11.602  22.352  16.018  0.75 12.32           S  
HETATM 1719  O1  SO4 A 249     -12.270  21.971  17.258  0.75 11.48           O  
HETATM 1720  O2  SO4 A 249     -10.147  22.289  16.201  0.75 12.21           O  
HETATM 1721  O3  SO4 A 249     -12.011  23.705  15.657  0.75 11.26           O  
HETATM 1722  O4  SO4 A 249     -11.957  21.402  14.970  0.75 12.56           O  
HETATM 1723  S   SO4 A 250      11.926  16.934   2.991  0.75 27.59           S  
HETATM 1724  O1  SO4 A 250      12.520  17.936   3.875  0.75 28.90           O  
HETATM 1725  O2  SO4 A 250      12.871  16.660   1.918  0.75 28.97           O  
HETATM 1726  O3  SO4 A 250      11.687  15.736   3.780  0.75 28.10           O  
HETATM 1727  O4  SO4 A 250      10.665  17.417   2.432  0.75 28.08           O  
HETATM 1728  S   SO4 A 251     -15.531  13.886  13.201  0.50 15.00           S  
HETATM 1729  O1  SO4 A 251     -15.657  13.969  11.747  0.50 16.44           O  
HETATM 1730  O2  SO4 A 251     -14.415  12.999  13.533  0.50 11.83           O  
HETATM 1731  O3  SO4 A 251     -16.777  13.338  13.733  0.50 15.80           O  
HETATM 1732  O4  SO4 A 251     -15.330  15.223  13.742  0.50 14.19           O  
HETATM 1733  S   SO4 A 252      17.323  14.315   9.615  0.65 29.28           S  
HETATM 1734  O1  SO4 A 252      16.540  13.658   8.574  0.65 29.51           O  
HETATM 1735  O2  SO4 A 252      17.214  13.581  10.870  0.65 28.73           O  
HETATM 1736  O3  SO4 A 252      16.829  15.680   9.798  0.65 30.34           O  
HETATM 1737  O4  SO4 A 252      18.725  14.357   9.206  0.65 29.84           O  
HETATM 1738  S   SO4 A   6      -1.423  17.576  23.078  0.75 11.25           S  
HETATM 1739  O1  SO4 A   6      -1.849  16.204  22.870  0.75 11.68           O  
HETATM 1740  O2  SO4 A   6      -1.564  17.902  24.496  0.75 16.04           O  
HETATM 1741  O3  SO4 A   6      -2.282  18.467  22.300  0.75 13.04           O  
HETATM 1742  O4  SO4 A   6      -0.031  17.745  22.666  0.75 12.24           O  
HETATM 1743  O   HOH A   7      10.947   2.600  16.268  1.00  7.35           O  
HETATM 1744  O   HOH A   8      10.030  19.067  12.204  1.00 11.78           O  
HETATM 1745  O   HOH A   9      -8.402   0.722  42.468  1.00 15.14           O  
HETATM 1746  O   HOH A  10      -6.581   8.865   8.656  1.00 16.63           O  
HETATM 1747  O   HOH A  11       9.720  16.019   5.498  1.00  9.73           O  
HETATM 1748  O   HOH A  12      19.614   9.325  21.745  1.00 11.10           O  
HETATM 1749  O   HOH A  13       9.393  -5.507  33.356  1.00 15.11           O  
HETATM 1750  O   HOH A  14     -15.858   0.537  19.775  1.00 18.56           O  
HETATM 1751  O   HOH A  15     -15.250  10.892  22.953  1.00 12.16           O  
HETATM 1752  O   HOH A  35      11.940   6.864  44.821  1.00 15.78           O  
HETATM 1753  O   HOH A  36       3.395   7.773  44.788  1.00 16.84           O  
HETATM 1754  O   HOH A  68      16.531   5.600  12.204  1.00 18.27           O  
HETATM 1755  O   HOH A 126      11.481  -4.885  14.024  1.00 29.03           O  
HETATM 1756  O   HOH A 131       5.604   4.880  -0.741  1.00 23.51           O  
HETATM 1757  O   HOH A 205     -15.073   4.163  19.082  1.00 31.30           O  
HETATM 1758  O   HOH A 206      19.468  -4.844  18.467  1.00 34.29           O  
HETATM 1759  O   HOH A 207       5.610  -2.354  44.277  1.00 39.33           O  
HETATM 1760  O   HOH A 208      10.919  -3.577  40.815  1.00 29.11           O  
HETATM 1761  O   HOH A 253      15.345  -4.130  25.472  1.00 43.61           O  
HETATM 1762  O   HOH A 254       6.298  20.853  11.497  1.00 29.49           O  
HETATM 1763  O   HOH A 255       3.497 -10.094  36.018  1.00 31.27           O  
HETATM 1764  O   HOH A 256       9.767   3.539   9.887  1.00 31.90           O  
HETATM 1765  O   HOH A 257      -0.003  -3.083   6.249  1.00 35.51           O  
HETATM 1766  O   HOH A 258       6.788  14.966  38.001  1.00 15.41           O  
HETATM 1767  O   HOH A 259     -18.866  14.932  23.730  1.00 30.17           O  
HETATM 1768  O   HOH A 260     -13.010  -5.071  33.634  1.00 38.00           O  
HETATM 1769  O   HOH A 261      -2.393   3.303   5.158  1.00  9.53           O  
HETATM 1770  O   HOH A 262      -0.417   1.534   4.253  1.00 13.95           O  
HETATM 1771  O   HOH A 263      -3.890  19.644   3.764  1.00 13.37           O  
HETATM 1772  O   HOH A 264       8.818  25.799  21.218  1.00 15.73           O  
HETATM 1773  O   HOH A 265     -13.580   9.076  11.456  1.00 16.06           O  
HETATM 1774  O   HOH A 266     -16.467   0.550  27.875  1.00 18.27           O  
HETATM 1775  O   HOH A 267     -14.214  -3.854  19.593  1.00 15.95           O  
HETATM 1776  O   HOH A 268      12.693  19.559  11.273  1.00 16.68           O  
HETATM 1777  O   HOH A 269       5.148   1.609   1.406  1.00 18.46           O  
HETATM 1778  O   HOH A 270      14.335  24.537  21.615  1.00 23.44           O  
HETATM 1779  O   HOH A 271      -4.172   1.496   4.160  1.00 20.28           O  
HETATM 1780  O   HOH A 272      -9.976  12.115  36.531  1.00 19.69           O  
HETATM 1781  O   HOH A 273      12.993  -6.527  22.193  1.00 21.30           O  
HETATM 1782  O   HOH A 274       1.331  20.564  12.032  1.00 18.08           O  
HETATM 1783  O   HOH A 275      12.464  22.688   6.576  1.00 17.72           O  
HETATM 1784  O   HOH A 276       3.103  19.759  20.413  1.00 19.09           O  
HETATM 1785  O   HOH A 277      10.451  24.549  24.977  1.00 16.43           O  
HETATM 1786  O   HOH A 278       7.739  -7.942  33.887  1.00 20.73           O  
HETATM 1787  O   HOH A 279      -0.739   4.867   1.624  1.00 18.58           O  
HETATM 1788  O   HOH A 280     -16.395   8.449  23.052  1.00 24.67           O  
HETATM 1789  O   HOH A 281      -8.216   4.670  44.314  1.00 24.48           O  
HETATM 1790  O   HOH A 282     -14.710   6.874  18.474  1.00 20.44           O  
HETATM 1791  O   HOH A 283      17.268  17.800  11.996  1.00 23.67           O  
HETATM 1792  O   HOH A 284     -12.831  -2.440  34.751  1.00 23.27           O  
HETATM 1793  O   HOH A 285      16.569  15.546  37.268  1.00 25.72           O  
HETATM 1794  O   HOH A 286      19.365  -1.278  34.059  1.00 23.95           O  
HETATM 1795  O   HOH A 287      10.056  -6.284  37.726  1.00 20.89           O  
HETATM 1796  O   HOH A 288       8.734  -4.900  13.562  1.00 25.98           O  
HETATM 1797  O   HOH A 289      -0.683   2.164   1.559  1.00 21.98           O  
HETATM 1798  O   HOH A 290      -1.772  -4.753  16.221  1.00 30.26           O  
HETATM 1799  O   HOH A 291      23.607   9.435  37.662  1.00 19.73           O  
HETATM 1800  O   HOH A 292       9.078  21.369  11.207  1.00 23.48           O  
HETATM 1801  O   HOH A 293      18.569   7.485  12.456  1.00 26.16           O  
HETATM 1802  O   HOH A 294      17.193  -0.674  36.371  1.00 28.48           O  
HETATM 1803  O   HOH A 295      18.776  21.564  22.307  1.00 24.41           O  
HETATM 1804  O   HOH A 296     -16.937  12.328  29.999  1.00 25.72           O  
HETATM 1805  O   HOH A 297      18.365   1.702  12.533  1.00 28.84           O  
HETATM 1806  O   HOH A 298      23.145   0.606  29.109  1.00 30.45           O  
HETATM 1807  O   HOH A 299       2.075  -9.634  31.658  1.00 20.98           O  
HETATM 1808  O   HOH A 300      20.781  19.270  19.235  1.00 29.92           O  
HETATM 1809  O   HOH A 301      -3.484  13.289  42.977  1.00 24.96           O  
HETATM 1810  O   HOH A 302     -14.825   1.385  15.479  1.00 21.46           O  
HETATM 1811  O   HOH A 303      11.746  11.127   0.107  1.00 24.39           O  
HETATM 1812  O   HOH A 304      25.119   2.066  31.110  1.00 27.78           O  
HETATM 1813  O   HOH A 305      -4.336  18.417  41.418  1.00 29.24           O  
HETATM 1814  O   HOH A 306      -1.033  -1.118   4.685  1.00 26.44           O  
HETATM 1815  O   HOH A 307      -4.595  11.229   9.651  1.00  8.58           O  
HETATM 1816  O   HOH A 308      17.632   3.510  10.818  1.00 27.95           O  
HETATM 1817  O   HOH A 309      -3.273  -3.244  42.184  1.00 27.58           O  
HETATM 1818  O   HOH A 310      -1.459  22.725  10.970  1.00 25.57           O  
HETATM 1819  O   HOH A 311      18.074  24.162  15.914  1.00 31.14           O  
HETATM 1820  O   HOH A 312      16.032  28.472  16.292  1.00 29.96           O  
HETATM 1821  O   HOH A 313     -14.124  13.253  29.359  1.00 19.42           O  
HETATM 1822  O   HOH A 314       8.140  -8.594  30.846  1.00 28.79           O  
HETATM 1823  O   HOH A 315     -16.674  10.415  19.151  1.00 18.40           O  
HETATM 1824  O   HOH A 316      19.955   6.263  21.647  1.00 11.65           O  
HETATM 1825  O   HOH A 317      -9.696  -5.396  21.114  0.50 16.17           O  
HETATM 1826  O   HOH A 318      12.259   0.066  43.234  0.50 12.78           O  
HETATM 1827  O   HOH A 319      22.569   6.575  21.423  0.50 19.63           O  
HETATM 1828  O   HOH A 320       9.719  14.600  -0.135  0.50 18.15           O  
HETATM 1829  O   HOH A 321      -3.949  -1.079   5.363  0.50 15.34           O  
HETATM 1830  O   HOH A 322      12.271   9.046   1.752  0.50 15.46           O  
HETATM 1831  O   HOH A 323      21.667  -1.242  30.419  0.50 12.79           O  
HETATM 1832  O   HOH A 324      -4.299  -7.971  11.084  0.50 19.79           O  
HETATM 1833  O   HOH A 325      -3.605  -8.070  17.231  0.50 25.08           O  
HETATM 1834  O   HOH A 326      -9.889   0.896   9.933  0.50 18.99           O  
HETATM 1835  O   HOH A 327      -8.831  13.533  33.858  1.00 13.04           O  
HETATM 1836  O   HOH A 328      14.397  25.829  16.669  1.00 13.91           O  
HETATM 1837  O   HOH A 329      -7.994  13.654  37.583  1.00 12.14           O  
HETATM 1838  O   HOH A 330     -17.802   2.375  26.522  0.50 18.40           O  
HETATM 1839  O   HOH A 331     -16.219  -2.196  20.698  0.50 17.05           O  
HETATM 1840  O   HOH A 332     -11.000  -6.457  24.005  0.50 15.00           O  
HETATM 1841  O   HOH A 333      -0.253  -8.732  30.438  1.00 12.29           O  
HETATM 1842  O   HOH A 334      21.032  20.163  21.692  0.50 22.86           O  
HETATM 1843  O   HOH A 335     -17.215   4.398  24.999  0.50 24.69           O  
HETATM 1844  O   HOH A 336       0.682  15.567   0.440  0.50 17.92           O  
HETATM 1845  O   HOH A 337       5.548  23.591  11.309  0.50 15.94           O  
HETATM 1846  O   HOH A 338       2.320   9.511  -0.863  0.50 23.76           O  
HETATM 1847  O   HOH A 339     -16.910   0.883  38.531  0.50 21.84           O  
HETATM 1848  O   HOH A 340     -16.887  -2.376  23.080  0.50 19.39           O  
HETATM 1849  O   HOH A 341      -9.994   0.696  44.540  0.50 19.74           O  
HETATM 1850  O   HOH A 342      -1.126  19.920  30.260  1.00 15.83           O  
HETATM 1851  O   HOH A 343       3.094  -8.225  34.087  1.00 13.22           O  
HETATM 1852  O   HOH A 344       1.075  18.883  28.458  0.50 21.84           O  
HETATM 1853  O   HOH A 345      -4.685   4.908   1.513  0.50 20.35           O  
HETATM 1854  O   HOH A 346      -6.588 -11.320  38.026  0.50 30.65           O  
HETATM 1855  O   HOH A 347       3.809   9.804  46.768  0.50 22.02           O  
HETATM 1856  O   HOH A 348     -17.485  -2.150  26.892  0.50 25.10           O  
HETATM 1857  O   HOH A 349      -2.795  16.420  41.384  0.50 18.79           O  
HETATM 1858  O   HOH A 350      12.319   2.106   7.541  0.50 16.87           O  
HETATM 1859  O   HOH A 351      -1.398  -4.835  43.265  0.50 31.42           O  
HETATM 1860  O   HOH A 352      13.166  -4.679  35.936  0.50 24.55           O  
HETATM 1861  O   HOH A 353       1.527   0.348  43.310  1.00 16.23           O  
HETATM 1862  O   HOH A 354     -16.816   1.028  30.515  0.50 16.39           O  
HETATM 1863  O   HOH A 355       5.331  -6.934  33.036  1.00  9.03           O  
HETATM 1864  O   HOH A 356     -12.510  -0.158  44.228  0.50 25.58           O  
HETATM 1865  O   HOH A 357     -15.210   8.563  13.852  0.50 19.41           O  
HETATM 1866  O   HOH A 358      -1.024  13.361  44.305  0.50 20.13           O  
HETATM 1867  O   HOH A 359     -15.669  -2.062  31.395  0.50 18.79           O  
HETATM 1868  O   HOH A 360      -3.214   1.232   1.304  0.50 23.18           O  
HETATM 1869  O   HOH A 361       0.962 -12.468  35.397  0.50 25.50           O  
HETATM 1870  O   HOH A 362      -7.598   0.103   5.564  0.50 16.62           O  
HETATM 1871  O   HOH A 363       7.484  23.734  29.712  0.50 25.28           O  
HETATM 1872  O   HOH A 364      18.422   0.601  15.931  0.50 20.57           O  
HETATM 1873  O   HOH A 365      21.917  10.020  22.913  0.50 22.46           O  
HETATM 1874  O   HOH A 366      16.710  25.256  20.476  0.50 26.27           O  
HETATM 1875  O   HOH A 367      -4.971  16.843   0.521  0.50 20.33           O  
HETATM 1876  O   HOH A 368      19.686   5.263  14.815  0.50 28.98           O  
HETATM 1877  O   HOH A 369      16.611  -1.297  30.477  0.50 21.31           O  
HETATM 1878  O   HOH A 370       4.827  -6.991  43.119  0.50 27.17           O  
HETATM 1879  O   HOH A 371      26.628   6.268  36.333  0.50 21.69           O  
HETATM 1880  O   HOH A 372       2.911  20.591   5.906  1.00 11.70           O  
HETATM 1881  O   HOH A 373     -17.966   2.734  29.495  0.50 20.67           O  
HETATM 1882  O   HOH A 374      -8.418  -0.161  46.860  0.50 21.62           O  
HETATM 1883  O   HOH A 375     -18.602   3.460  34.420  0.50 25.81           O  
HETATM 1884  O   HOH A 376       3.405   3.507   2.777  1.00 12.01           O  
HETATM 1885  O   HOH A 377      -8.161   0.575   1.694  0.50 25.32           O  
HETATM 1886  O   HOH A 378       8.362  -4.530  16.226  1.00 14.28           O  
HETATM 1887  O   HOH A 379       3.415   1.930  -1.191  0.50 19.23           O  
HETATM 1888  O   HOH A 380      -7.458  17.821   1.867  0.50 23.58           O  
HETATM 1889  O   HOH A 381      19.613   3.068  20.175  1.00 20.37           O  
HETATM 1890  O   HOH A 382      16.277  22.343  11.819  0.50 28.43           O  
HETATM 1891  O   HOH A 383       0.847  20.467  22.021  0.50 15.50           O  
HETATM 1892  O   HOH A 384      19.319  -0.296  31.555  1.00 13.78           O  
HETATM 1893  O   HOH A 385      18.507   1.420  37.308  1.00 11.72           O  
HETATM 1894  O   HOH A 386     -11.587  -6.325  29.759  1.00 18.77           O  
HETATM 1895  O   HOH A 387      17.357  20.177  24.155  1.00 11.07           O  
HETATM 1896  O   HOH A 388      -3.103  -3.200  39.431  1.00 11.56           O  
HETATM 1897  O   HOH A 389      -5.313 -12.103  34.410  1.00 22.35           O  
HETATM 1898  O   HOH A 390     -13.938   8.767  16.285  1.00 12.98           O  
HETATM 1899  O   HOH A 391       8.611  20.025  26.869  1.00 10.27           O  
HETATM 1900  O   HOH A 392     -16.579  20.612  20.113  1.00 19.22           O  
HETATM 1901  O   HOH A 393      -2.706  13.898  40.421  1.00 14.18           O  
HETATM 1902  O   HOH A 394       0.660  18.975  25.791  1.00 27.19           O  
HETATM 1903  O   HOH A 395      -8.441  18.575  22.481  1.00 23.50           O  
HETATM 1904  O   HOH A 396     -10.831   1.523  13.842  1.00 15.17           O  
HETATM 1905  O   HOH A 397      -7.288  -4.980  20.020  1.00 18.15           O  
HETATM 1906  O   HOH A 398      22.961   0.125  36.486  1.00 16.15           O  
HETATM 1907  O   HOH A 399     -10.215  -2.172  35.502  1.00 12.08           O  
HETATM 1908  O   HOH A 400      -2.779   5.323   3.394  1.00 12.96           O  
HETATM 1909  O   HOH A 401       4.151   1.042  44.122  1.00 16.13           O  
HETATM 1910  O   HOH A 402       9.184  12.057  -0.507  1.00 18.48           O  
HETATM 1911  O   HOH A 403       1.639  -6.249  19.039  1.00 17.23           O  
HETATM 1912  O   HOH A 404       2.321  -6.325  10.457  1.00 20.54           O  
HETATM 1913  O   HOH A 405      10.695   2.120  13.469  1.00 13.17           O  
HETATM 1914  O   HOH A 406       0.694   9.726  44.150  1.00 16.91           O  
HETATM 1915  O   HOH A 407      -0.431  -6.700  41.440  1.00 21.11           O  
HETATM 1916  O   HOH A 408      24.457   4.560  32.361  1.00 16.23           O  
HETATM 1917  O   HOH A 409       8.084  15.776  35.857  1.00 14.90           O  
HETATM 1918  O   HOH A 410      -0.022  16.521   2.726  1.00 24.76           O  
HETATM 1919  O   HOH A 411       2.129  11.319   1.038  1.00 18.78           O  
HETATM 1920  O   HOH A 412      -0.757  -4.529  22.619  1.00 13.95           O  
HETATM 1921  O   HOH A 413       8.685  -4.289  10.796  1.00 17.99           O  
HETATM 1922  O   HOH A 414       6.671  -6.715  25.130  1.00 15.91           O  
HETATM 1923  O   HOH A 415       8.944   4.085  47.539  1.00 23.77           O  
HETATM 1924  O   HOH A 416     -12.222  -4.286  21.445  1.00 15.56           O  
HETATM 1925  O   HOH A 417      13.035  29.158  19.807  1.00 16.92           O  
HETATM 1926  O   HOH A 418      18.720  11.222  38.686  1.00 17.86           O  
HETATM 1927  O   HOH A 419      19.083  15.320  16.984  1.00 15.14           O  
HETATM 1928  O   HOH A 420      14.526   7.231  10.155  1.00 16.83           O  
HETATM 1929  O   HOH A 421       6.555  -4.308   6.005  1.00 19.37           O  
HETATM 1930  O   HOH A 422      -6.850   1.916   3.803  1.00 24.00           O  
HETATM 1931  O   HOH A 423     -14.501   0.435  32.010  1.00 16.37           O  
HETATM 1932  O   HOH A 424      10.162   3.752   4.045  1.00 21.96           O  
HETATM 1933  O   HOH A 425      12.271   8.504   9.188  1.00 17.59           O  
HETATM 1934  O   HOH A 426     -14.663   5.117  15.664  1.00 21.55           O  
HETATM 1935  O   HOH A 427      -7.709  -4.423  22.911  1.00 21.71           O  
HETATM 1936  O   HOH A 428      18.017   3.100  14.827  1.00 16.83           O  
HETATM 1937  O   HOH A 429       5.722  22.299  34.750  1.00 18.78           O  
HETATM 1938  O   HOH A 430      22.914   1.600  26.191  1.00 28.08           O  
HETATM 1939  O   HOH A 431     -13.130   4.214  11.644  1.00 17.00           O  
HETATM 1940  O   HOH A 432      12.779  -3.926  26.817  1.00 17.82           O  
HETATM 1941  O   HOH A 433      -7.758   0.061  11.340  1.00 17.90           O  
HETATM 1942  O   HOH A 434       5.895  -6.663  40.347  1.00 21.32           O  
HETATM 1943  O   HOH A 435      19.299  13.126  15.346  1.00 23.00           O  
HETATM 1944  O   HOH A 436      -6.242  -0.824  42.637  1.00 16.21           O  
HETATM 1945  O   HOH A 437      -4.073  11.247   6.878  1.00 13.36           O  
HETATM 1946  O   HOH A 438       8.569  16.711   0.810  1.00 29.77           O  
HETATM 1947  O   HOH A 439      18.127  19.380  18.755  1.00 15.05           O  
HETATM 1948  O   HOH A 440       5.815  10.326  -2.098  1.00 29.32           O  
HETATM 1949  O   HOH A 441      -9.836  15.472   5.537  1.00 24.94           O  
HETATM 1950  O   HOH A 442      17.322  -0.494  18.076  1.00 37.85           O  
HETATM 1951  O   HOH A 443      15.282   2.606   9.747  1.00 18.54           O  
HETATM 1952  O   HOH A 444       1.398  -5.662  15.661  1.00 22.40           O  
HETATM 1953  O   HOH A 445       9.939   0.341  44.720  1.00 18.72           O  
HETATM 1954  O   HOH A 446     -17.811  18.269  17.314  1.00 34.54           O  
HETATM 1955  O   HOH A 447       2.747  -5.863  27.665  1.00 20.15           O  
HETATM 1956  O   HOH A 448      16.196  -3.642  22.946  1.00 24.73           O  
HETATM 1957  O   HOH A 449       6.737  21.117  28.437  1.00 22.06           O  
HETATM 1958  O   HOH A 450       8.708  -9.026  18.268  1.00 18.20           O  
HETATM 1959  O   HOH A 451      14.210  -2.537  32.049  1.00 28.43           O  
HETATM 1960  O   HOH A 452      -1.796 -11.233  37.039  1.00 28.94           O  
HETATM 1961  O   HOH A 453      -4.522  -8.256  37.205  1.00 24.26           O  
HETATM 1962  O   HOH A 454      12.619  -1.807  37.427  1.00 22.28           O  
HETATM 1963  O   HOH A 455      -1.828  14.659  25.086  1.00 24.79           O  
HETATM 1964  O   HOH A 456       0.803  20.768   7.657  1.00 18.73           O  
HETATM 1965  O   HOH A 457      21.782  11.280  37.256  1.00 16.16           O  
HETATM 1966  O   HOH A 458      10.895  -2.615  28.166  1.00 20.18           O  
HETATM 1967  O   HOH A 459       5.688  -8.643  23.674  1.00 25.53           O  
HETATM 1968  O   HOH A 460     -14.168  -2.897  28.818  1.00 23.36           O  
HETATM 1969  O   HOH A 461      -4.692  10.913  43.450  1.00 21.07           O  
HETATM 1970  O   HOH A 462      23.648   6.245  24.066  1.00 30.09           O  
HETATM 1971  O   HOH A 463       4.619   5.654  45.712  1.00 25.91           O  
HETATM 1972  O   HOH A 464       0.101  17.886  39.850  1.00 26.62           O  
HETATM 1973  O   HOH A 465      -9.740  17.958  16.598  1.00 17.38           O  
HETATM 1974  O   HOH A 466      16.182  15.497  34.703  1.00 21.60           O  
HETATM 1975  O   HOH A 467       8.480  -5.751  29.186  1.00 19.49           O  
HETATM 1976  O   HOH A 468      13.375  10.113   7.572  1.00 20.49           O  
HETATM 1977  O   HOH A 469      -8.689  21.253  20.276  1.00 24.83           O  
HETATM 1978  O   HOH A 470       8.135  16.828  39.558  1.00 21.54           O  
HETATM 1979  O   HOH A 471       2.597  20.853   9.649  1.00 17.05           O  
HETATM 1980  O   HOH A 472       1.954   5.478   1.817  1.00 23.05           O  
HETATM 1981  O   HOH A 473     -10.681  -8.847  32.295  1.00 29.92           O  
HETATM 1982  O   HOH A 474       0.721  18.601  16.570  1.00 22.23           O  
HETATM 1983  O   HOH A 475      17.674  22.058  19.496  1.00 23.89           O  
HETATM 1984  O   HOH A 476      13.519  18.608   8.814  1.00 23.20           O  
HETATM 1985  O   HOH A 477      -6.253  -6.409  11.923  1.00 19.04           O  
HETATM 1986  O   HOH A 478      -6.041  -7.683  18.242  1.00 24.64           O  
HETATM 1987  O   HOH A 479      -0.050  14.987  40.339  1.00 21.74           O  
HETATM 1988  O   HOH A 480       2.106  20.894  36.971  1.00 30.59           O  
HETATM 1989  O   HOH A 481      13.265  16.891   6.659  1.00 30.35           O  
HETATM 1990  O   HOH A 482      17.878  15.098  13.193  1.00 20.27           O  
HETATM 1991  O   HOH A 483      -3.225  17.273  26.586  1.00 23.44           O  
HETATM 1992  O   HOH A 484     -16.573   1.915  41.022  1.00 24.66           O  
HETATM 1993  O   HOH A 485      14.356   0.214  36.783  1.00 20.04           O  
HETATM 1994  O   HOH A 486      20.296   6.355  17.149  1.00 34.04           O  
HETATM 1995  O   HOH A 487      -1.560  22.189   8.139  1.00 24.48           O  
HETATM 1996  O   HOH A 488     -10.488  20.064  18.622  1.00 18.00           O  
HETATM 1997  O   HOH A 489      21.973  13.869  22.073  1.00 26.26           O  
HETATM 1998  O   HOH A 490     -17.765   1.226  23.523  1.00 30.16           O  
HETATM 1999  O   HOH A 491      -4.702  -1.913  10.399  1.00 26.67           O  
HETATM 2000  O   HOH A 492      -3.144  -5.360  23.567  1.00 18.75           O  
HETATM 2001  O   HOH A 493       6.741  19.368  13.759  1.00 26.04           O  
HETATM 2002  O   HOH A 494      -2.064  20.083  14.782  1.00 16.53           O  
HETATM 2003  O   HOH A 495      -4.385  20.749  38.367  1.00 29.46           O  
HETATM 2004  O   HOH A 496     -11.454  13.244   9.239  1.00 30.48           O  
HETATM 2005  O   HOH A 497      -8.038  18.580   5.655  1.00 26.44           O  
HETATM 2006  O   HOH A 498       5.520   7.701  -1.742  1.00 33.47           O  
HETATM 2007  O   HOH A 499      -9.029   0.009  36.698  1.00  7.58           O  
HETATM 2008  O   HOH A 500      -1.968   7.826  24.536  1.00  5.66           O  
HETATM 2009  O   HOH A 501     -14.824   6.392  41.233  1.00  9.51           O  
HETATM 2010  O   HOH A 502     -10.194   2.199  35.408  1.00  7.40           O  
HETATM 2011  O   HOH A 503      -7.941   0.028  29.719  1.00  6.51           O  
HETATM 2012  O   HOH A 504       5.032   5.841  24.994  1.00  7.93           O  
HETATM 2013  O   HOH A 505      -5.679  10.524  34.536  1.00  5.81           O  
HETATM 2014  O   HOH A 506      -1.149   0.356  32.833  1.00  7.74           O  
HETATM 2015  O   HOH A 507      11.264  12.779  17.167  1.00  6.55           O  
HETATM 2016  O   HOH A 508       7.268   7.118   7.899  1.00  8.95           O  
HETATM 2017  O   HOH A 509     -13.725  -0.091  28.014  1.00  8.14           O  
HETATM 2018  O   HOH A 510      -9.161   8.371  22.454  1.00  5.49           O  
HETATM 2019  O   HOH A 511     -11.910   6.364  18.338  1.00  9.17           O  
HETATM 2020  O   HOH A 512       0.860  11.320  16.196  1.00  8.20           O  
HETATM 2021  O   HOH A 513      -4.412  -1.637  32.262  1.00  6.48           O  
HETATM 2022  O   HOH A 514      -7.435   8.862  35.973  1.00  7.81           O  
HETATM 2023  O   HOH A 515       1.820  17.696  18.985  1.00 10.93           O  
HETATM 2024  O   HOH A 516      -9.322   6.256  37.770  1.00  7.19           O  
HETATM 2025  O   HOH A 517       8.718  13.914  16.712  1.00  8.10           O  
HETATM 2026  O   HOH A 518      -3.258   3.227  32.895  1.00  5.70           O  
HETATM 2027  O   HOH A 519      -2.032   7.808  12.981  1.00  6.68           O  
HETATM 2028  O   HOH A 520      -8.508  18.192  12.907  1.00  8.95           O  
HETATM 2029  O   HOH A 521       5.630  -7.460  30.403  1.00 11.18           O  
HETATM 2030  O   HOH A 522      -4.577  14.828  10.528  1.00  9.61           O  
HETATM 2031  O   HOH A 523      -0.725   0.494  22.088  1.00  5.66           O  
HETATM 2032  O   HOH A 524     -11.315   0.488  26.649  1.00  6.96           O  
HETATM 2033  O   HOH A 525      -4.254   0.771  30.775  1.00  7.64           O  
HETATM 2034  O   HOH A 526      -3.803   9.191  26.162  1.00  4.64           O  
HETATM 2035  O   HOH A 527       8.629  28.937  19.139  1.00  7.50           O  
HETATM 2036  O   HOH A 528      -3.697  -7.141  29.663  1.00  9.61           O  
HETATM 2037  O   HOH A 529      10.547  -4.501  35.715  1.00 14.20           O  
HETATM 2038  O   HOH A 530      -3.715   8.640   9.976  1.00  8.23           O  
HETATM 2039  O   HOH A 531      13.477  22.239  23.119  1.00  6.79           O  
HETATM 2040  O   HOH A 532     -15.826   8.449  39.752  1.00  8.10           O  
HETATM 2041  O   HOH A 533       2.359   1.460   4.501  1.00 10.49           O  
HETATM 2042  O   HOH A 534      -5.584  -1.154  28.895  1.00  6.50           O  
HETATM 2043  O   HOH A 535      12.909   7.251  42.251  1.00 13.26           O  
HETATM 2044  O   HOH A 536     -10.461  11.142  27.943  1.00 17.91           O  
HETATM 2045  O   HOH A 537      -4.327  18.301  16.507  1.00 18.40           O  
HETATM 2046  O   HOH A 538       7.517  21.266  24.426  1.00 11.12           O  
HETATM 2047  O   HOH A 539      14.177   1.130  39.380  1.00 28.47           O  
HETATM 2048  O   HOH A 540      14.417  12.680   7.288  1.00 22.55           O  
HETATM 2049  O   HOH A 541      -5.658  17.800   4.677  1.00 20.18           O  
HETATM 2050  O   HOH A 542      -1.820  21.107   4.449  1.00 23.28           O  
HETATM 2051  O   HOH A 543     -16.625   2.882  32.183  1.00 25.60           O  
HETATM 2052  O   HOH A 544       5.414  13.824  41.085  1.00 21.19           O  
HETATM 2053  O   HOH A 545       0.168  22.039  34.579  1.00 34.89           O  
HETATM 2054  O   HOH A 546       1.528  13.820  42.439  1.00 29.74           O  
HETATM 2055  O   HOH A 547       4.501  21.025  24.974  1.00 34.51           O  
HETATM 2056  O   HOH A 548      -4.597  19.527  23.766  1.00 33.42           O  
HETATM 2057  O   HOH A 549      10.528   1.148   6.029  1.00 22.68           O  
HETATM 2058  O   HOH A 550      16.555  -2.497  12.620  1.00 33.80           O  
HETATM 2059  O   HOH A 551       0.343  -4.441  17.812  1.00 24.55           O  
HETATM 2060  O   HOH A 552      18.669   9.750  13.998  1.00 21.43           O  
HETATM 2061  O   HOH A 553      22.914   8.030  25.681  1.00 29.47           O  
HETATM 2062  O   HOH A 554      -0.071  12.933   1.431  1.00 31.47           O  
HETATM 2063  O   HOH A 555       9.064   3.934   7.207  1.00 32.24           O  
HETATM 2064  O   HOH A 556      -4.529  -5.496  38.280  1.00 35.67           O  
HETATM 2065  O   HOH A 557      14.760  -3.448  11.147  1.00 30.66           O  
HETATM 2066  O   HOH A 558       5.039  -6.798   9.659  1.00 34.95           O  
HETATM 2067  O   HOH A 559      -6.256  -3.946  11.163  1.00 27.31           O  
HETATM 2068  O   HOH A 560      -3.219  -0.037  44.174  1.00 38.00           O  
HETATM 2069  O   HOH A 561      -8.138  15.860  31.208  1.00 23.61           O  
HETATM 2070  O   HOH A 562      -5.928  -3.500  42.844  1.00 28.91           O  
HETATM 2071  O   HOH A 563       2.673  -6.130  13.581  1.00 24.27           O  
HETATM 2072  O   HOH A 564      -0.055   2.660  43.921  1.00 33.08           O  
HETATM 2073  O   HOH A 565       0.369   7.474  45.357  1.00 37.95           O  
HETATM 2074  O   HOH A 566      17.772  -1.075  14.199  1.00 38.11           O  
HETATM 2075  O   HOH A 567      18.920  12.202  18.040  1.00 26.70           O  
HETATM 2076  O   HOH A 568      -7.978  15.251  28.679  1.00 33.46           O  
HETATM 2077  O   HOH A 569      12.353  -3.694   9.956  1.00 26.54           O  
HETATM 2078  O   HOH A 570     -10.990  -6.685  37.475  1.00 29.77           O  
HETATM 2079  O   HOH A 571       7.348  -4.577  41.250  1.00 30.45           O  
HETATM 2080  O   HOH A 572      16.049  23.233  14.366  1.00 18.64           O  
HETATM 2081  O   HOH A 573      14.867  19.020  12.858  1.00 16.05           O  
HETATM 2082  O   HOH A 574      -9.879  -5.993  33.600  1.00 19.60           O  
HETATM 2083  O   HOH A 575      -4.330  -7.273  13.907  1.00 25.69           O  
HETATM 2084  O   HOH A 576       7.367  -7.709  27.598  1.00 20.11           O  
HETATM 2085  O   HOH A 577      -9.519  -3.424  43.783  1.00 29.27           O  
HETATM 2086  O   HOH A 578       5.674  22.265  31.531  1.00 39.99           O  
HETATM 2087  O   HOH A 579      12.684   1.414  10.113  1.00 34.68           O  
HETATM 2088  O   HOH A 580      11.568  -4.961  31.427  1.00 32.87           O  
HETATM 2089  O   HOH A 581      -2.089  -2.882   8.621  1.00 33.86           O  
HETATM 2090  O   HOH A 582      16.307   3.062  37.879  1.00 11.95           O  
HETATM 2091  O   HOH A 583       1.620  19.964  14.672  1.00 21.70           O  
HETATM 2092  O   HOH A 584      24.098   6.972  30.360  1.00 36.15           O  
HETATM 2093  O   HOH A 585      19.521  18.330  14.345  1.00 37.85           O  
HETATM 2094  O   HOH A 586       3.967  -5.515   6.024  1.00 31.62           O  
HETATM 2095  O   HOH A 587     -16.922   1.164  35.786  1.00 34.93           O  
HETATM 2096  O   HOH A 588      20.705  13.449  19.834  1.00 40.23           O  
HETATM 2097  O   HOH A 589      -6.031  17.399  26.421  1.00 32.95           O  
HETATM 2098  O   HOH A 590     -17.396  13.884  26.227  1.00 36.23           O  
HETATM 2099  O   HOH A 591       8.365   4.123  -0.888  1.00 36.04           O  
HETATM 2100  O   HOH A 592       1.198  -6.029  45.539  1.00 48.59           O  
HETATM 2101  O   HOH A 593     -11.712  18.733  10.642  1.00 36.17           O  
HETATM 2102  O   HOH A 594     -15.638  -1.488  38.715  1.00 34.46           O  
HETATM 2103  O   HOH A 595     -13.065  12.070  10.974  1.00 31.61           O  
HETATM 2104  O   HOH A 596     -10.212  10.992   1.530  1.00 37.24           O  
HETATM 2105  O   HOH A 597       3.068  20.053  29.585  1.00 35.79           O  
HETATM 2106  O   HOH A 598      21.157  -0.550  23.012  1.00 37.87           O  
HETATM 2107  O   HOH A 599      12.580  -5.823  11.710  1.00 21.71           O  
CONECT   48 1038                                                                
CONECT  185  298                                                                
CONECT  298  185                                                                
CONECT  384 1682                                                                
CONECT  397 1682                                                                
CONECT  421 1682                                                                
CONECT  461 1682                                                                
CONECT  825 1569                                                                
CONECT  867 1375                                                                
CONECT 1038   48                                                                
CONECT 1126 1238                                                                
CONECT 1238 1126                                                                
CONECT 1313 1470                                                                
CONECT 1375  867                                                                
CONECT 1470 1313                                                                
CONECT 1569  825                                                                
CONECT 1682  384  397  421  461                                                 
CONECT 1682 2010 2024                                                           
CONECT 1683 1685                                                                
CONECT 1684 1685                                                                
CONECT 1685 1683 1684 1686                                                      
CONECT 1686 1685 1688 1689                                                      
CONECT 1687 1688 1691                                                           
CONECT 1688 1686 1687                                                           
CONECT 1689 1686 1690                                                           
CONECT 1690 1689 1691                                                           
CONECT 1691 1687 1690 1692                                                      
CONECT 1692 1691                                                                
CONECT 1693 1694 1695                                                           
CONECT 1694 1693                                                                
CONECT 1695 1693 1696                                                           
CONECT 1696 1695                                                                
CONECT 1697 1698 1699                                                           
CONECT 1698 1697                                                                
CONECT 1699 1697 1700                                                           
CONECT 1700 1699                                                                
CONECT 1701 1702 1703                                                           
CONECT 1702 1701                                                                
CONECT 1703 1701 1704                                                           
CONECT 1704 1703                                                                
CONECT 1705 1706 1707                                                           
CONECT 1706 1705                                                                
CONECT 1707 1705 1708                                                           
CONECT 1708 1707                                                                
CONECT 1709 1710 1711                                                           
CONECT 1710 1709                                                                
CONECT 1711 1709 1712                                                           
CONECT 1712 1711                                                                
CONECT 1713 1714 1715 1716 1717                                                 
CONECT 1714 1713                                                                
CONECT 1715 1713                                                                
CONECT 1716 1713                                                                
CONECT 1717 1713                                                                
CONECT 1718 1719 1720 1721 1722                                                 
CONECT 1719 1718                                                                
CONECT 1720 1718                                                                
CONECT 1721 1718                                                                
CONECT 1722 1718                                                                
CONECT 1723 1724 1725 1726 1727                                                 
CONECT 1724 1723                                                                
CONECT 1725 1723                                                                
CONECT 1726 1723                                                                
CONECT 1727 1723                                                                
CONECT 1728 1729 1730 1731 1732                                                 
CONECT 1729 1728                                                                
CONECT 1730 1728                                                                
CONECT 1731 1728                                                                
CONECT 1732 1728                                                                
CONECT 1733 1734 1735 1736 1737                                                 
CONECT 1734 1733                                                                
CONECT 1735 1733                                                                
CONECT 1736 1733                                                                
CONECT 1737 1733                                                                
CONECT 1738 1739 1740 1741 1742                                                 
CONECT 1739 1738                                                                
CONECT 1740 1738                                                                
CONECT 1741 1738                                                                
CONECT 1742 1738                                                                
CONECT 2010 1682                                                                
CONECT 2024 1682                                                                
MASTER      343    0   13    3   14    0   28    6 2055    1   80   18          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.