CNRS Nantes University UFIP UFIP
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***  raj  ***

elNémo ID: 220914180552139259

Job options:

ID        	=	 220914180552139259
JOBID     	=	 raj
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 raj

HEADER    PROTEIN FIBRIL                          13-JUL-20   6ZRF              
TITLE     AMYLOID STRUCTURE OF AMYLIN (IAPP - ISLET AMYLOID POLYPEPTIDE)        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISLET AMYLOID POLYPEPTIDE;                                 
COMPND   3 CHAIN: A, C, E, G, I, K, B, D, F, H, J, L;                           
COMPND   4 SYNONYM: AMYLIN,DIABETES-ASSOCIATED PEPTIDE,DAP,INSULINOMA AMYLOID   
COMPND   5 PEPTIDE;                                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: TYC = C-TERMINAL AMIDATED TYR                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   4 ORGANISM_TAXID: 32630                                                
KEYWDS    AMYLOID FIBRIL TYPE-2-DIABETES HORMONE, PROTEIN FIBRIL                
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    R.U.GALLARDO,M.G.IADANZA,N.A.RANSON,S.E.RADFORD                       
REVDAT   3   18-NOV-20 6ZRF    1       JRNL                                     
REVDAT   2   14-OCT-20 6ZRF    1       SHEET                                    
REVDAT   1   30-SEP-20 6ZRF    0                                                
JRNL        AUTH   R.GALLARDO,M.G.IADANZA,Y.XU,G.R.HEATH,R.FOSTER,S.E.RADFORD,  
JRNL        AUTH 2 N.A.RANSON                                                   
JRNL        TITL   FIBRIL STRUCTURES OF DIABETES-RELATED AMYLIN VARIANTS REVEAL 
JRNL        TITL 2 A BASIS FOR SURFACE-TEMPLATED ASSEMBLY.                      
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  27  1048 2020              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   32929282                                                     
JRNL        DOI    10.1038/S41594-020-0496-3                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : RELION, EPU, GCTF, RELION, PHENIX         
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.600                          
REMARK   3   NUMBER OF PARTICLES               : 32846                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6ZRF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUL-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292110022.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : HELICAL                           
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : HELICAL ARRAY                     
REMARK 245   PARTICLE TYPE                  : HELICAL                           
REMARK 245   NAME OF SAMPLE                 : AMYLOID FIBRIL OF AMYLIN (ISLET   
REMARK 245                                    AMYLOID POLIPEPTIDE)              
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.18                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 6.80                              
REMARK 245   SAMPLE DETAILS                 : PRODUCED SYNTHETICALLY,           
REMARK 245  OXIDISED, C-TERMINALLY AMIDATED, FIBRILLATED IN VITRO               
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 50.07                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, G, I, K, B, D, F, H,         
REMARK 350                    AND CHAINS: J, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A     1                                                      
REMARK 465     CYS A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     LYS C     1                                                      
REMARK 465     CYS C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     CYS C     7                                                      
REMARK 465     ALA C     8                                                      
REMARK 465     THR C     9                                                      
REMARK 465     GLN C    10                                                      
REMARK 465     ARG C    11                                                      
REMARK 465     LEU C    12                                                      
REMARK 465     LYS E     1                                                      
REMARK 465     CYS E     2                                                      
REMARK 465     ASN E     3                                                      
REMARK 465     THR E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     THR E     6                                                      
REMARK 465     CYS E     7                                                      
REMARK 465     ALA E     8                                                      
REMARK 465     THR E     9                                                      
REMARK 465     GLN E    10                                                      
REMARK 465     ARG E    11                                                      
REMARK 465     LEU E    12                                                      
REMARK 465     LYS G     1                                                      
REMARK 465     CYS G     2                                                      
REMARK 465     ASN G     3                                                      
REMARK 465     THR G     4                                                      
REMARK 465     ALA G     5                                                      
REMARK 465     THR G     6                                                      
REMARK 465     CYS G     7                                                      
REMARK 465     ALA G     8                                                      
REMARK 465     THR G     9                                                      
REMARK 465     GLN G    10                                                      
REMARK 465     ARG G    11                                                      
REMARK 465     LEU G    12                                                      
REMARK 465     LYS I     1                                                      
REMARK 465     CYS I     2                                                      
REMARK 465     ASN I     3                                                      
REMARK 465     THR I     4                                                      
REMARK 465     ALA I     5                                                      
REMARK 465     THR I     6                                                      
REMARK 465     CYS I     7                                                      
REMARK 465     ALA I     8                                                      
REMARK 465     THR I     9                                                      
REMARK 465     GLN I    10                                                      
REMARK 465     ARG I    11                                                      
REMARK 465     LEU I    12                                                      
REMARK 465     LYS K     1                                                      
REMARK 465     CYS K     2                                                      
REMARK 465     ASN K     3                                                      
REMARK 465     THR K     4                                                      
REMARK 465     ALA K     5                                                      
REMARK 465     THR K     6                                                      
REMARK 465     CYS K     7                                                      
REMARK 465     ALA K     8                                                      
REMARK 465     THR K     9                                                      
REMARK 465     GLN K    10                                                      
REMARK 465     ARG K    11                                                      
REMARK 465     LEU K    12                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     CYS B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     CYS B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     LYS D     1                                                      
REMARK 465     CYS D     2                                                      
REMARK 465     ASN D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     CYS D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     THR D     9                                                      
REMARK 465     GLN D    10                                                      
REMARK 465     ARG D    11                                                      
REMARK 465     LEU D    12                                                      
REMARK 465     LYS F     1                                                      
REMARK 465     CYS F     2                                                      
REMARK 465     ASN F     3                                                      
REMARK 465     THR F     4                                                      
REMARK 465     ALA F     5                                                      
REMARK 465     THR F     6                                                      
REMARK 465     CYS F     7                                                      
REMARK 465     ALA F     8                                                      
REMARK 465     THR F     9                                                      
REMARK 465     GLN F    10                                                      
REMARK 465     ARG F    11                                                      
REMARK 465     LEU F    12                                                      
REMARK 465     LYS H     1                                                      
REMARK 465     CYS H     2                                                      
REMARK 465     ASN H     3                                                      
REMARK 465     THR H     4                                                      
REMARK 465     ALA H     5                                                      
REMARK 465     THR H     6                                                      
REMARK 465     CYS H     7                                                      
REMARK 465     ALA H     8                                                      
REMARK 465     THR H     9                                                      
REMARK 465     GLN H    10                                                      
REMARK 465     ARG H    11                                                      
REMARK 465     LEU H    12                                                      
REMARK 465     LYS J     1                                                      
REMARK 465     CYS J     2                                                      
REMARK 465     ASN J     3                                                      
REMARK 465     THR J     4                                                      
REMARK 465     ALA J     5                                                      
REMARK 465     THR J     6                                                      
REMARK 465     CYS J     7                                                      
REMARK 465     ALA J     8                                                      
REMARK 465     THR J     9                                                      
REMARK 465     GLN J    10                                                      
REMARK 465     ARG J    11                                                      
REMARK 465     LEU J    12                                                      
REMARK 465     LYS L     1                                                      
REMARK 465     CYS L     2                                                      
REMARK 465     ASN L     3                                                      
REMARK 465     THR L     4                                                      
REMARK 465     ALA L     5                                                      
REMARK 465     THR L     6                                                      
REMARK 465     CYS L     7                                                      
REMARK 465     ALA L     8                                                      
REMARK 465     THR L     9                                                      
REMARK 465     GLN L    10                                                      
REMARK 465     ARG L    11                                                      
REMARK 465     LEU L    12                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER H    20     OG   SER J    20              1.99            
REMARK 500   ND2  ASN C    31     OD1  ASN C    35              2.15            
REMARK 500   ND2  ASN B    31     OD1  ASN B    35              2.15            
REMARK 500   ND2  ASN E    31     OD1  ASN E    35              2.15            
REMARK 500   ND2  ASN G    31     OD1  ASN G    35              2.15            
REMARK 500   ND2  ASN D    31     OD1  ASN D    35              2.15            
REMARK 500   ND2  ASN K    31     OD1  ASN K    35              2.15            
REMARK 500   ND2  ASN A    31     OD1  ASN A    35              2.15            
REMARK 500   ND2  ASN F    31     OD1  ASN F    35              2.15            
REMARK 500   ND2  ASN J    31     OD1  ASN J    35              2.15            
REMARK 500   ND2  ASN L    31     OD1  ASN L    35              2.15            
REMARK 500   ND2  ASN I    31     OD1  ASN I    35              2.15            
REMARK 500   ND2  ASN H    31     OD1  ASN H    35              2.15            
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    PHE A  23       -0.45     69.44                                   
REMARK 500    THR A  36      136.98   -175.74                                   
REMARK 500    PHE C  23       -0.49     69.49                                   
REMARK 500    THR C  36      137.02   -175.76                                   
REMARK 500    PHE E  23       -0.43     69.41                                   
REMARK 500    THR E  36      137.05   -175.72                                   
REMARK 500    PHE G  23       -0.39     69.37                                   
REMARK 500    THR G  36      136.96   -175.75                                   
REMARK 500    PHE I  23       -0.40     69.40                                   
REMARK 500    THR I  36      137.01   -175.76                                   
REMARK 500    PHE K  23       -0.43     69.43                                   
REMARK 500    THR K  36      137.00   -175.74                                   
REMARK 500    PHE B  23       -0.38     69.39                                   
REMARK 500    THR B  36      136.99   -175.68                                   
REMARK 500    PHE D  23       -0.29     69.32                                   
REMARK 500    THR D  36      136.97   -175.78                                   
REMARK 500    PHE F  23       -0.40     69.44                                   
REMARK 500    THR F  36      136.95   -175.73                                   
REMARK 500    PHE H  23       -3.91     70.44                                   
REMARK 500    THR H  36      137.10   -175.70                                   
REMARK 500    THR J  36      136.98   -175.81                                   
REMARK 500    PHE L  23       -0.36     69.30                                   
REMARK 500    THR L  36      136.98   -175.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-11380   RELATED DB: EMDB                             
REMARK 900 AMYLOID STRUCTURE OF AMYLIN (IAPP - ISLET AMYLOID POLYPEPTIDE)       
DBREF  6ZRF A    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF C    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF E    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF G    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF I    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF K    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF B    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF D    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF F    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF H    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF J    1    37  UNP    P10997   IAPP_HUMAN      34     70             
DBREF  6ZRF L    1    37  UNP    P10997   IAPP_HUMAN      34     70             
SEQADV 6ZRF TYC A   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC C   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC E   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC G   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC I   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC K   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC B   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC D   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC F   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC H   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC J   37  UNP  P10997    TYR    70 CONFLICT                       
SEQADV 6ZRF TYC L   37  UNP  P10997    TYR    70 CONFLICT                       
SEQRES   1 A   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 A   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 A   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 C   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 C   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 C   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 E   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 E   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 E   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 G   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 G   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 G   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 I   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 I   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 I   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 K   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 K   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 K   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 B   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 B   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 B   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 D   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 D   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 D   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 F   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 F   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 F   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 H   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 H   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 H   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 J   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 J   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 J   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
SEQRES   1 L   37  LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA          
SEQRES   2 L   37  ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE          
SEQRES   3 L   37  LEU SER SER THR ASN VAL GLY SER ASN THR TYC                  
HET    TYC  A  37      13                                                       
HET    TYC  C  37      13                                                       
HET    TYC  E  37      13                                                       
HET    TYC  G  37      13                                                       
HET    TYC  I  37      13                                                       
HET    TYC  K  37      13                                                       
HET    TYC  B  37      13                                                       
HET    TYC  D  37      13                                                       
HET    TYC  F  37      13                                                       
HET    TYC  H  37      13                                                       
HET    TYC  J  37      13                                                       
HET    TYC  L  37      13                                                       
HETNAM     TYC L-TYROSINAMIDE                                                   
FORMUL   1  TYC    12(C9 H12 N2 O2)                                             
SHEET    1   1 1 ASN A  14  SER A  19  0                                        
SHEET    1   2 1 ILE A  26  ASN A  31  0                                        
SHEET    1   3 1 ASN A  35  THR A  36  0                                        
SHEET    1   4 1 ASN C  14  SER C  19  0                                        
SHEET    1   5 1 ILE C  26  ASN C  31  0                                        
SHEET    1   6 1 ASN C  35  THR C  36  0                                        
SHEET    1   7 1 ASN E  14  SER E  19  0                                        
SHEET    1   8 1 ILE E  26  ASN E  31  0                                        
SHEET    1   9 1 ASN E  35  THR E  36  0                                        
SHEET    1  10 1 ASN G  14  SER G  19  0                                        
SHEET    1  11 1 ILE G  26  ASN G  31  0                                        
SHEET    1  12 1 ASN G  35  THR G  36  0                                        
SHEET    1  13 1 ASN I  14  SER I  19  0                                        
SHEET    1  14 1 ILE I  26  ASN I  31  0                                        
SHEET    1  15 1 ASN I  35  THR I  36  0                                        
SHEET    1  16 1 ASN K  14  SER K  19  0                                        
SHEET    1  17 1 ILE K  26  ASN K  31  0                                        
SHEET    1  18 1 ASN K  35  THR K  36  0                                        
SHEET    1  19 1 ASN B  14  SER B  19  0                                        
SHEET    1  20 1 ILE B  26  ASN B  31  0                                        
SHEET    1  21 1 ASN B  35  THR B  36  0                                        
SHEET    1  22 1 ASN D  14  SER D  19  0                                        
SHEET    1  23 1 ILE D  26  ASN D  31  0                                        
SHEET    1  24 1 ASN D  35  THR D  36  0                                        
SHEET    1  25 1 ASN F  14  SER F  19  0                                        
SHEET    1  26 1 ILE F  26  ASN F  31  0                                        
SHEET    1  27 1 ASN F  35  THR F  36  0                                        
SHEET    1  28 1 ASN H  14  SER H  19  0                                        
SHEET    1  29 1 ILE H  26  ASN H  31  0                                        
SHEET    1  30 1 ASN H  35  THR H  36  0                                        
SHEET    1  31 1 ASN J  14  SER J  19  0                                        
SHEET    1  32 1 ILE J  26  ASN J  31  0                                        
SHEET    1  33 1 ASN J  35  THR J  36  0                                        
SHEET    1  34 1 ASN L  14  SER L  19  0                                        
SHEET    1  35 1 ILE L  26  ASN L  31  0                                        
SHEET    1  36 1 ASN L  35  THR L  36  0                                        
LINK         C   THR A  36                 N   TYC A  37     1555   1555  1.32  
LINK         C   THR C  36                 N   TYC C  37     1555   1555  1.32  
LINK         C   THR E  36                 N   TYC E  37     1555   1555  1.32  
LINK         C   THR G  36                 N   TYC G  37     1555   1555  1.32  
LINK         C   THR I  36                 N   TYC I  37     1555   1555  1.32  
LINK         C   THR K  36                 N   TYC K  37     1555   1555  1.32  
LINK         C   THR B  36                 N   TYC B  37     1555   1555  1.32  
LINK         C   THR D  36                 N   TYC D  37     1555   1555  1.32  
LINK         C   THR F  36                 N   TYC F  37     1555   1555  1.32  
LINK         C   THR H  36                 N   TYC H  37     1555   1555  1.32  
LINK         C   THR J  36                 N   TYC J  37     1555   1555  1.32  
LINK         C   THR L  36                 N   TYC L  37     1555   1555  1.32  
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   ALA A  13     130.522  98.086 119.920  1.00111.86           N  
ATOM      2  CA  ALA A  13     129.119  98.354 120.205  1.00111.86           C  
ATOM      3  C   ALA A  13     128.214  97.470 119.359  1.00111.86           C  
ATOM      4  O   ALA A  13     128.190  97.582 118.135  1.00111.86           O  
ATOM      5  CB  ALA A  13     128.807  99.813 119.968  1.00111.86           C  
ATOM      6  N   ASN A  14     127.471  96.587 120.017  1.00116.57           N  
ATOM      7  CA  ASN A  14     126.612  95.626 119.342  1.00116.57           C  
ATOM      8  C   ASN A  14     125.165  96.076 119.445  1.00116.57           C  
ATOM      9  O   ASN A  14     124.636  96.210 120.549  1.00116.57           O  
ATOM     10  CB  ASN A  14     126.772  94.237 119.956  1.00116.57           C  
ATOM     11  CG  ASN A  14     128.213  93.774 119.981  1.00116.57           C  
ATOM     12  OD1 ASN A  14     129.002  94.123 119.105  1.00116.57           O  
ATOM     13  ND2 ASN A  14     128.564  92.982 120.987  1.00116.57           N  
ATOM     14  N   PHE A  15     124.524  96.293 118.299  1.00104.53           N  
ATOM     15  CA  PHE A  15     123.148  96.783 118.255  1.00104.53           C  
ATOM     16  C   PHE A  15     122.342  95.868 117.351  1.00104.53           C  
ATOM     17  O   PHE A  15     122.608  95.793 116.150  1.00104.53           O  
ATOM     18  CB  PHE A  15     123.075  98.214 117.733  1.00104.53           C  
ATOM     19  CG  PHE A  15     123.571  99.241 118.687  1.00104.53           C  
ATOM     20  CD1 PHE A  15     124.880  99.247 119.105  1.00104.53           C  
ATOM     21  CD2 PHE A  15     122.736 100.227 119.133  1.00104.53           C  
ATOM     22  CE1 PHE A  15     125.329 100.201 119.970  1.00104.53           C  
ATOM     23  CE2 PHE A  15     123.179 101.181 119.989  1.00104.53           C  
ATOM     24  CZ  PHE A  15     124.477 101.165 120.414  1.00104.53           C  
ATOM     25  N   LEU A  16     121.354  95.189 117.914  1.00 95.20           N  
ATOM     26  CA  LEU A  16     120.396  94.437 117.122  1.00 95.20           C  
ATOM     27  C   LEU A  16     119.006  94.758 117.634  1.00 95.20           C  
ATOM     28  O   LEU A  16     118.765  94.721 118.844  1.00 95.20           O  
ATOM     29  CB  LEU A  16     120.656  92.934 117.195  1.00 95.20           C  
ATOM     30  CG  LEU A  16     119.932  92.104 116.132  1.00 95.20           C  
ATOM     31  CD1 LEU A  16     120.758  90.885 115.780  1.00 95.20           C  
ATOM     32  CD2 LEU A  16     118.534  91.682 116.568  1.00 95.20           C  
ATOM     33  N   VAL A  17     118.097  95.071 116.721  1.00 85.60           N  
ATOM     34  CA  VAL A  17     116.725  95.400 117.070  1.00 85.60           C  
ATOM     35  C   VAL A  17     115.811  94.560 116.204  1.00 85.60           C  
ATOM     36  O   VAL A  17     115.952  94.549 114.978  1.00 85.60           O  
ATOM     37  CB  VAL A  17     116.423  96.889 116.880  1.00 85.60           C  
ATOM     38  CG1 VAL A  17     114.950  97.131 117.050  1.00 85.60           C  
ATOM     39  CG2 VAL A  17     117.216  97.712 117.865  1.00 85.60           C  
ATOM     40  N   HIS A  18     114.877  93.860 116.833  1.00 87.42           N  
ATOM     41  CA  HIS A  18     113.950  92.975 116.139  1.00 87.42           C  
ATOM     42  C   HIS A  18     112.558  93.326 116.648  1.00 87.42           C  
ATOM     43  O   HIS A  18     112.061  92.713 117.593  1.00 87.42           O  
ATOM     44  CB  HIS A  18     114.325  91.523 116.390  1.00 87.42           C  
ATOM     45  CG  HIS A  18     113.271  90.540 115.993  1.00 87.42           C  
ATOM     46  ND1 HIS A  18     113.271  89.238 116.439  1.00 87.42           N  
ATOM     47  CD2 HIS A  18     112.188  90.664 115.190  1.00 87.42           C  
ATOM     48  CE1 HIS A  18     112.229  88.603 115.935  1.00 87.42           C  
ATOM     49  NE2 HIS A  18     111.556  89.445 115.174  1.00 87.42           N  
ATOM     50  N   SER A  19     111.932  94.313 116.022  1.00 77.57           N  
ATOM     51  CA  SER A  19     110.626  94.782 116.449  1.00 77.57           C  
ATOM     52  C   SER A  19     109.520  94.076 115.686  1.00 77.57           C  
ATOM     53  O   SER A  19     109.752  93.435 114.663  1.00 77.57           O  
ATOM     54  CB  SER A  19     110.498  96.284 116.244  1.00 77.57           C  
ATOM     55  OG  SER A  19     109.135  96.658 116.254  1.00 77.57           O  
ATOM     56  N   SER A  20     108.300  94.193 116.204  1.00 81.54           N  
ATOM     57  CA  SER A  20     107.134  93.647 115.521  1.00 81.54           C  
ATOM     58  C   SER A  20     106.138  94.728 115.129  1.00 81.54           C  
ATOM     59  O   SER A  20     105.821  94.860 113.945  1.00 81.54           O  
ATOM     60  CB  SER A  20     106.451  92.599 116.399  1.00 81.54           C  
ATOM     61  OG  SER A  20     105.527  93.221 117.267  1.00 81.54           O  
ATOM     62  N   ASN A  21     105.635  95.506 116.085  1.00 80.20           N  
ATOM     63  CA  ASN A  21     104.707  96.604 115.819  1.00 80.20           C  
ATOM     64  C   ASN A  21     105.235  97.790 116.601  1.00 80.20           C  
ATOM     65  O   ASN A  21     104.837  98.010 117.745  1.00 80.20           O  
ATOM     66  CB  ASN A  21     103.297  96.269 116.232  1.00 80.20           C  
ATOM     67  CG  ASN A  21     102.833  94.956 115.688  1.00 80.20           C  
ATOM     68  OD1 ASN A  21     103.139  94.598 114.554  1.00 80.20           O  
ATOM     69  ND2 ASN A  21     102.078  94.222 116.492  1.00 80.20           N  
ATOM     70  N   ASN A  22     106.115  98.565 115.984  1.00 81.05           N  
ATOM     71  CA  ASN A  22     106.896  99.515 116.759  1.00 81.05           C  
ATOM     72  C   ASN A  22     106.043 100.675 117.256  1.00 81.05           C  
ATOM     73  O   ASN A  22     106.026 100.970 118.454  1.00 81.05           O  
ATOM     74  CB  ASN A  22     108.065 100.017 115.934  1.00 81.05           C  
ATOM     75  CG  ASN A  22     108.920 100.962 116.697  1.00 81.05           C  
ATOM     76  OD1 ASN A  22     108.917 100.962 117.919  1.00 81.05           O  
ATOM     77  ND2 ASN A  22     109.658 101.791 115.989  1.00 81.05           N  
ATOM     78  N   PHE A  23     105.366 101.372 116.343  1.00 80.62           N  
ATOM     79  CA  PHE A  23     104.520 102.524 116.655  1.00 80.62           C  
ATOM     80  C   PHE A  23     105.286 103.755 117.107  1.00 80.62           C  
ATOM     81  O   PHE A  23     104.674 104.786 117.388  1.00 80.62           O  
ATOM     82  CB  PHE A  23     103.563 102.244 117.811  1.00 80.62           C  
ATOM     83  CG  PHE A  23     102.281 101.633 117.409  1.00 80.62           C  
ATOM     84  CD1 PHE A  23     101.452 102.275 116.533  1.00 80.62           C  
ATOM     85  CD2 PHE A  23     101.865 100.452 117.975  1.00 80.62           C  
ATOM     86  CE1 PHE A  23     100.259 101.723 116.186  1.00 80.62           C  
ATOM     87  CE2 PHE A  23     100.669  99.902 117.635  1.00 80.62           C  
ATOM     88  CZ  PHE A  23      99.865 100.536 116.740  1.00 80.62           C  
ATOM     89  N   GLY A  24     106.605 103.680 117.186  1.00 84.71           N  
ATOM     90  CA  GLY A  24     107.311 104.746 117.853  1.00 84.71           C  
ATOM     91  C   GLY A  24     108.805 104.646 117.676  1.00 84.71           C  
ATOM     92  O   GLY A  24     109.313 103.758 116.995  1.00 84.71           O  
ATOM     93  N   ALA A  25     109.504 105.572 118.310  1.00 87.21           N  
ATOM     94  CA  ALA A  25     110.930 105.715 118.078  1.00 87.21           C  
ATOM     95  C   ALA A  25     111.685 104.550 118.688  1.00 87.21           C  
ATOM     96  O   ALA A  25     111.626 104.334 119.899  1.00 87.21           O  
ATOM     97  CB  ALA A  25     111.425 107.030 118.665  1.00 87.21           C  
ATOM     98  N   ILE A  26     112.381 103.791 117.856  1.00 80.81           N  
ATOM     99  CA  ILE A  26     113.435 102.902 118.320  1.00 80.81           C  
ATOM    100  C   ILE A  26     114.723 103.658 118.041  1.00 80.81           C  
ATOM    101  O   ILE A  26     115.367 103.478 117.013  1.00 80.81           O  
ATOM    102  CB  ILE A  26     113.397 101.552 117.621  1.00 80.81           C  
ATOM    103  CG1 ILE A  26     112.072 100.864 117.889  1.00 80.81           C  
ATOM    104  CG2 ILE A  26     114.518 100.679 118.110  1.00 80.81           C  
ATOM    105  CD1 ILE A  26     111.968  99.509 117.257  1.00 80.81           C  
ATOM    106  N   LEU A  27     115.116 104.507 118.975  1.00 88.21           N  
ATOM    107  CA  LEU A  27     116.192 105.446 118.693  1.00 88.21           C  
ATOM    108  C   LEU A  27     117.540 104.824 119.011  1.00 88.21           C  
ATOM    109  O   LEU A  27     118.316 105.324 119.812  1.00 88.21           O  
ATOM    110  CB  LEU A  27     115.969 106.729 119.479  1.00 88.21           C  
ATOM    111  CG  LEU A  27     116.625 108.017 118.986  1.00 88.21           C  
ATOM    112  CD1 LEU A  27     115.758 109.165 119.429  1.00 88.21           C  
ATOM    113  CD2 LEU A  27     118.047 108.223 119.471  1.00 88.21           C  
ATOM    114  N   SER A  28     117.821 103.693 118.393  1.00 86.61           N  
ATOM    115  CA  SER A  28     119.067 102.996 118.666  1.00 86.61           C  
ATOM    116  C   SER A  28     120.215 103.790 118.058  1.00 86.61           C  
ATOM    117  O   SER A  28     120.318 103.894 116.835  1.00 86.61           O  
ATOM    118  CB  SER A  28     118.993 101.587 118.096  1.00 86.61           C  
ATOM    119  OG  SER A  28     120.013 100.776 118.625  1.00 86.61           O  
ATOM    120  N   SER A  29     121.079 104.359 118.894  1.00 93.32           N  
ATOM    121  CA  SER A  29     122.078 105.292 118.393  1.00 93.32           C  
ATOM    122  C   SER A  29     123.354 105.189 119.209  1.00 93.32           C  
ATOM    123  O   SER A  29     123.450 104.409 120.156  1.00 93.32           O  
ATOM    124  CB  SER A  29     121.563 106.726 118.431  1.00 93.32           C  
ATOM    125  OG  SER A  29     121.325 107.134 119.763  1.00 93.32           O  
ATOM    126  N   THR A  30     124.344 105.995 118.821  1.00104.01           N  
ATOM    127  CA  THR A  30     125.624 106.085 119.517  1.00104.01           C  
ATOM    128  C   THR A  30     126.362 107.312 119.009  1.00104.01           C  
ATOM    129  O   THR A  30     126.286 107.627 117.820  1.00104.01           O  
ATOM    130  CB  THR A  30     126.486 104.840 119.299  1.00104.01           C  
ATOM    131  OG1 THR A  30     125.739 103.671 119.637  1.00104.01           O  
ATOM    132  CG2 THR A  30     127.727 104.890 120.174  1.00104.01           C  
ATOM    133  N   ASN A  31     127.089 107.985 119.899  1.00109.92           N  
ATOM    134  CA  ASN A  31     127.717 109.250 119.544  1.00109.92           C  
ATOM    135  C   ASN A  31     128.747 109.704 120.561  1.00109.92           C  
ATOM    136  O   ASN A  31     128.654 109.368 121.740  1.00109.92           O  
ATOM    137  CB  ASN A  31     126.656 110.326 119.400  1.00109.92           C  
ATOM    138  CG  ASN A  31     125.670 110.286 120.511  1.00109.92           C  
ATOM    139  OD1 ASN A  31     125.856 109.563 121.476  1.00109.92           O  
ATOM    140  ND2 ASN A  31     124.593 111.032 120.378  1.00109.92           N  
ATOM    141  N   VAL A  32     129.745 110.456 120.108  1.00114.15           N  
ATOM    142  CA  VAL A  32     130.654 111.101 121.046  1.00114.15           C  
ATOM    143  C   VAL A  32     130.167 112.499 121.400  1.00114.15           C  
ATOM    144  O   VAL A  32     129.935 112.808 122.571  1.00114.15           O  
ATOM    145  CB  VAL A  32     132.088 111.104 120.489  1.00114.15           C  
ATOM    146  CG1 VAL A  32     132.996 111.868 121.390  1.00114.15           C  
ATOM    147  CG2 VAL A  32     132.602 109.684 120.386  1.00114.15           C  
ATOM    148  N   GLY A  33     129.984 113.353 120.408  1.00116.32           N  
ATOM    149  CA  GLY A  33     129.710 114.744 120.685  1.00116.32           C  
ATOM    150  C   GLY A  33     128.289 115.002 121.126  1.00116.32           C  
ATOM    151  O   GLY A  33     127.580 114.126 121.616  1.00116.32           O  
ATOM    152  N   SER A  34     127.876 116.251 120.942  1.00118.94           N  
ATOM    153  CA  SER A  34     126.568 116.686 121.404  1.00118.94           C  
ATOM    154  C   SER A  34     125.483 116.262 120.430  1.00118.94           C  
ATOM    155  O   SER A  34     125.756 115.937 119.274  1.00118.94           O  
ATOM    156  CB  SER A  34     126.543 118.200 121.559  1.00118.94           C  
ATOM    157  OG  SER A  34     126.229 118.806 120.319  1.00118.94           O  
ATOM    158  N   ASN A  35     124.246 116.286 120.904  1.00114.38           N  
ATOM    159  CA  ASN A  35     123.068 115.979 120.111  1.00114.38           C  
ATOM    160  C   ASN A  35     121.887 116.778 120.635  1.00114.38           C  
ATOM    161  O   ASN A  35     122.044 117.723 121.409  1.00114.38           O  
ATOM    162  CB  ASN A  35     122.773 114.486 120.146  1.00114.38           C  
ATOM    163  CG  ASN A  35     123.859 113.684 119.516  1.00114.38           C  
ATOM    164  OD1 ASN A  35     124.737 113.168 120.202  1.00114.38           O  
ATOM    165  ND2 ASN A  35     123.819 113.570 118.199  1.00114.38           N  
ATOM    166  N   THR A  36     120.698 116.377 120.211  1.00101.56           N  
ATOM    167  CA  THR A  36     119.469 117.005 120.648  1.00101.56           C  
ATOM    168  C   THR A  36     118.301 116.250 120.067  1.00101.56           C  
ATOM    169  O   THR A  36     118.322 115.870 118.908  1.00101.56           O  
ATOM    170  CB  THR A  36     119.394 118.465 120.217  1.00101.56           C  
ATOM    171  OG1 THR A  36     120.281 119.237 121.033  1.00101.56           O  
ATOM    172  CG2 THR A  36     117.988 119.001 120.370  1.00101.56           C  
HETATM  173  N   TYC A  37     117.283 116.019 120.875  1.00 95.08           N  
HETATM  174  CA  TYC A  37     116.099 115.319 120.388  1.00 95.08           C  
HETATM  175  C   TYC A  37     114.906 116.156 120.686  1.00 95.08           C  
HETATM  176  O   TYC A  37     113.911 115.627 121.137  1.00 95.08           O  
HETATM  177  CB  TYC A  37     115.992 113.957 121.040  1.00 95.08           C  
HETATM  178  CG  TYC A  37     117.189 113.141 120.633  1.00 95.08           C  
HETATM  179  CD1 TYC A  37     118.344 113.167 121.390  1.00 95.08           C  
HETATM  180  CD2 TYC A  37     117.135 112.353 119.504  1.00 95.08           C  
HETATM  181  CE1 TYC A  37     119.443 112.413 121.018  1.00 95.08           C  
HETATM  182  CE2 TYC A  37     118.233 111.601 119.132  1.00 95.08           C  
HETATM  183  OH  TYC A  37     120.462 110.886 119.522  1.00 95.08           O  
HETATM  184  CZ  TYC A  37     119.386 111.627 119.888  1.00 95.08           C  
HETATM  185  NXT TYC A  37     114.976 117.460 120.444  1.00 95.08           N  
TER     186      TYC A  37                                                      
ATOM    187  N   ALA C  13     130.960  99.521 115.057  1.00110.51           N  
ATOM    188  CA  ALA C  13     129.543  99.706 115.343  1.00110.51           C  
ATOM    189  C   ALA C  13     128.692  98.768 114.498  1.00110.51           C  
ATOM    190  O   ALA C  13     128.660  98.877 113.275  1.00110.51           O  
ATOM    191  CB  ALA C  13     129.144 101.143 115.104  1.00110.51           C  
ATOM    192  N   ASN C  14     128.004  97.844 115.158  1.00114.05           N  
ATOM    193  CA  ASN C  14     127.203  96.832 114.485  1.00114.05           C  
ATOM    194  C   ASN C  14     125.732  97.195 114.589  1.00114.05           C  
ATOM    195  O   ASN C  14     125.197  97.298 115.694  1.00114.05           O  
ATOM    196  CB  ASN C  14     127.446  95.455 115.102  1.00114.05           C  
ATOM    197  CG  ASN C  14     128.912  95.080 115.126  1.00114.05           C  
ATOM    198  OD1 ASN C  14     129.678  95.474 114.249  1.00114.05           O  
ATOM    199  ND2 ASN C  14     129.310  94.312 116.132  1.00114.05           N  
ATOM    200  N   PHE C  15     125.078  97.372 113.443  1.00103.25           N  
ATOM    201  CA  PHE C  15     123.676  97.779 113.400  1.00103.25           C  
ATOM    202  C   PHE C  15     122.924  96.816 112.498  1.00103.25           C  
ATOM    203  O   PHE C  15     123.194  96.756 111.296  1.00103.25           O  
ATOM    204  CB  PHE C  15     123.517  99.202 112.876  1.00103.25           C  
ATOM    205  CG  PHE C  15     123.952 100.258 113.829  1.00103.25           C  
ATOM    206  CD1 PHE C  15     125.258 100.343 114.245  1.00103.25           C  
ATOM    207  CD2 PHE C  15     123.059 101.194 114.274  1.00103.25           C  
ATOM    208  CE1 PHE C  15     125.650 101.323 115.108  1.00103.25           C  
ATOM    209  CE2 PHE C  15     123.446 102.173 115.128  1.00103.25           C  
ATOM    210  CZ  PHE C  15     124.742 102.236 115.552  1.00103.25           C  
ATOM    211  N   LEU C  16     121.979  96.080 113.063  1.00 91.45           N  
ATOM    212  CA  LEU C  16     121.067  95.271 112.272  1.00 91.45           C  
ATOM    213  C   LEU C  16     119.660  95.510 112.785  1.00 91.45           C  
ATOM    214  O   LEU C  16     119.423  95.460 113.995  1.00 91.45           O  
ATOM    215  CB  LEU C  16     121.416  93.786 112.347  1.00 91.45           C  
ATOM    216  CG  LEU C  16     120.742  92.913 111.286  1.00 91.45           C  
ATOM    217  CD1 LEU C  16     121.639  91.746 110.935  1.00 91.45           C  
ATOM    218  CD2 LEU C  16     119.372  92.410 111.724  1.00 91.45           C  
ATOM    219  N   VAL C  17     118.734  95.767 111.872  1.00 82.62           N  
ATOM    220  CA  VAL C  17     117.346  96.014 112.222  1.00 82.62           C  
ATOM    221  C   VAL C  17     116.482  95.120 111.358  1.00 82.62           C  
ATOM    222  O   VAL C  17     116.622  95.115 110.132  1.00 82.62           O  
ATOM    223  CB  VAL C  17     116.955  97.482 112.030  1.00 82.62           C  
ATOM    224  CG1 VAL C  17     115.471  97.637 112.201  1.00 82.62           C  
ATOM    225  CG2 VAL C  17     117.698  98.352 113.013  1.00 82.62           C  
ATOM    226  N   HIS C  18     115.592  94.366 111.989  1.00 82.95           N  
ATOM    227  CA  HIS C  18     114.719  93.427 111.297  1.00 82.95           C  
ATOM    228  C   HIS C  18     113.308  93.695 111.806  1.00 82.95           C  
ATOM    229  O   HIS C  18     112.850  93.054 112.752  1.00 82.95           O  
ATOM    230  CB  HIS C  18     115.179  92.000 111.549  1.00 82.95           C  
ATOM    231  CG  HIS C  18     114.186  90.956 111.154  1.00 82.95           C  
ATOM    232  ND1 HIS C  18     114.264  89.657 111.602  1.00 82.95           N  
ATOM    233  CD2 HIS C  18     113.097  91.013 110.352  1.00 82.95           C  
ATOM    234  CE1 HIS C  18     113.261  88.960 111.099  1.00 82.95           C  
ATOM    235  NE2 HIS C  18     112.539  89.760 110.338  1.00 82.95           N  
ATOM    236  N   SER C  19     112.625  94.642 111.179  1.00 76.74           N  
ATOM    237  CA  SER C  19     111.293  95.033 111.607  1.00 76.74           C  
ATOM    238  C   SER C  19     110.231  94.261 110.846  1.00 76.74           C  
ATOM    239  O   SER C  19     110.500  93.634 109.824  1.00 76.74           O  
ATOM    240  CB  SER C  19     111.076  96.525 111.400  1.00 76.74           C  
ATOM    241  OG  SER C  19     109.693  96.816 111.410  1.00 76.74           O  
ATOM    242  N   SER C  20     109.006  94.306 111.365  1.00 82.22           N  
ATOM    243  CA  SER C  20     107.874  93.690 110.684  1.00 82.22           C  
ATOM    244  C   SER C  20     106.816  94.710 110.291  1.00 82.22           C  
ATOM    245  O   SER C  20     106.490  94.821 109.107  1.00 82.22           O  
ATOM    246  CB  SER C  20     107.256  92.605 111.563  1.00 82.22           C  
ATOM    247  OG  SER C  20     106.297  93.173 112.431  1.00 82.22           O  
ATOM    248  N   ASN C  21     106.268  95.458 111.246  1.00 82.76           N  
ATOM    249  CA  ASN C  21     105.276  96.499 110.979  1.00 82.76           C  
ATOM    250  C   ASN C  21     105.733  97.715 111.760  1.00 82.76           C  
ATOM    251  O   ASN C  21     105.323  97.913 112.903  1.00 82.76           O  
ATOM    252  CB  ASN C  21     103.889  96.080 111.394  1.00 82.76           C  
ATOM    253  CG  ASN C  21     103.504  94.742 110.852  1.00 82.76           C  
ATOM    254  OD1 ASN C  21     103.829  94.401 109.718  1.00 82.76           O  
ATOM    255  ND2 ASN C  21     102.794  93.965 111.658  1.00 82.76           N  
ATOM    256  N   ASN C  22     106.565  98.540 111.141  1.00 79.53           N  
ATOM    257  CA  ASN C  22     107.288  99.536 111.914  1.00 79.53           C  
ATOM    258  C   ASN C  22     106.368 100.644 112.410  1.00 79.53           C  
ATOM    259  O   ASN C  22     106.334 100.939 113.608  1.00 79.53           O  
ATOM    260  CB  ASN C  22     108.424 100.106 111.087  1.00 79.53           C  
ATOM    261  CG  ASN C  22     109.222 101.101 111.849  1.00 79.53           C  
ATOM    262  OD1 ASN C  22     109.220 101.102 113.071  1.00 79.53           O  
ATOM    263  ND2 ASN C  22     109.909 101.971 111.139  1.00 79.53           N  
ATOM    264  N   PHE C  23     105.650 101.298 111.496  1.00 79.21           N  
ATOM    265  CA  PHE C  23     104.737 102.398 111.808  1.00 79.21           C  
ATOM    266  C   PHE C  23     105.429 103.673 112.257  1.00 79.21           C  
ATOM    267  O   PHE C  23     104.756 104.666 112.538  1.00 79.21           O  
ATOM    268  CB  PHE C  23     103.799 102.063 112.965  1.00 79.21           C  
ATOM    269  CG  PHE C  23     102.556 101.376 112.565  1.00 79.21           C  
ATOM    270  CD1 PHE C  23     101.689 101.966 111.689  1.00 79.21           C  
ATOM    271  CD2 PHE C  23     102.211 100.174 113.133  1.00 79.21           C  
ATOM    272  CE1 PHE C  23     100.531 101.344 111.344  1.00 79.21           C  
ATOM    273  CE2 PHE C  23     101.050  99.553 112.795  1.00 79.21           C  
ATOM    274  CZ  PHE C  23     100.208 100.136 111.900  1.00 79.21           C  
ATOM    275  N   GLY C  24     106.750 103.678 112.335  1.00 79.68           N  
ATOM    276  CA  GLY C  24     107.392 104.784 113.001  1.00 79.68           C  
ATOM    277  C   GLY C  24     108.888 104.772 112.822  1.00 79.68           C  
ATOM    278  O   GLY C  24     109.448 103.916 112.142  1.00 79.68           O  
ATOM    279  N   ALA C  25     109.532 105.739 113.455  1.00 80.56           N  
ATOM    280  CA  ALA C  25     110.947 105.967 113.221  1.00 80.56           C  
ATOM    281  C   ALA C  25     111.770 104.850 113.832  1.00 80.56           C  
ATOM    282  O   ALA C  25     111.726 104.632 115.043  1.00 80.56           O  
ATOM    283  CB  ALA C  25     111.363 107.310 113.806  1.00 80.56           C  
ATOM    284  N   ILE C  26     112.510 104.133 113.000  1.00 73.69           N  
ATOM    285  CA  ILE C  26     113.615 103.308 113.465  1.00 73.69           C  
ATOM    286  C   ILE C  26     114.855 104.140 113.184  1.00 73.69           C  
ATOM    287  O   ILE C  26     115.508 103.997 112.156  1.00 73.69           O  
ATOM    288  CB  ILE C  26     113.657 101.958 112.768  1.00 73.69           C  
ATOM    289  CG1 ILE C  26     112.375 101.193 113.038  1.00 73.69           C  
ATOM    290  CG2 ILE C  26     114.828 101.154 113.257  1.00 73.69           C  
ATOM    291  CD1 ILE C  26     112.352  99.833 112.407  1.00 73.69           C  
ATOM    292  N   LEU C  27     115.198 105.012 114.116  1.00 79.24           N  
ATOM    293  CA  LEU C  27     116.216 106.013 113.833  1.00 79.24           C  
ATOM    294  C   LEU C  27     117.599 105.473 114.150  1.00 79.24           C  
ATOM    295  O   LEU C  27     118.344 106.019 114.950  1.00 79.24           O  
ATOM    296  CB  LEU C  27     115.917 107.281 114.617  1.00 79.24           C  
ATOM    297  CG  LEU C  27     116.748 108.532 114.336  1.00 79.24           C  
ATOM    298  CD1 LEU C  27     115.849 109.724 114.535  1.00 79.24           C  
ATOM    299  CD2 LEU C  27     117.990 108.667 115.195  1.00 79.24           C  
ATOM    300  N   SER C  28     117.946 104.359 113.533  1.00 81.87           N  
ATOM    301  CA  SER C  28     119.232 103.739 113.806  1.00 81.87           C  
ATOM    302  C   SER C  28     120.329 104.598 113.196  1.00 81.87           C  
ATOM    303  O   SER C  28     120.426 104.707 111.973  1.00 81.87           O  
ATOM    304  CB  SER C  28     119.241 102.327 113.238  1.00 81.87           C  
ATOM    305  OG  SER C  28     120.308 101.579 113.768  1.00 81.87           O  
ATOM    306  N   SER C  29     121.159 105.219 114.031  1.00 93.17           N  
ATOM    307  CA  SER C  29     122.100 106.209 113.527  1.00 93.17           C  
ATOM    308  C   SER C  29     123.381 106.183 114.342  1.00 93.17           C  
ATOM    309  O   SER C  29     123.524 105.412 115.291  1.00 93.17           O  
ATOM    310  CB  SER C  29     121.501 107.610 113.564  1.00 93.17           C  
ATOM    311  OG  SER C  29     121.242 108.005 114.896  1.00 93.17           O  
ATOM    312  N   THR C  30     124.320 107.047 113.952  1.00106.59           N  
ATOM    313  CA  THR C  30     125.593 107.214 114.648  1.00106.59           C  
ATOM    314  C   THR C  30     126.257 108.482 114.138  1.00106.59           C  
ATOM    315  O   THR C  30     126.161 108.790 112.948  1.00106.59           O  
ATOM    316  CB  THR C  30     126.528 106.022 114.431  1.00106.59           C  
ATOM    317  OG1 THR C  30     125.852 104.811 114.771  1.00106.59           O  
ATOM    318  CG2 THR C  30     127.764 106.147 115.305  1.00106.59           C  
ATOM    319  N   ASN C  31     126.943 109.198 115.026  1.00107.91           N  
ATOM    320  CA  ASN C  31     127.494 110.497 114.668  1.00107.91           C  
ATOM    321  C   ASN C  31     128.496 111.013 115.684  1.00107.91           C  
ATOM    322  O   ASN C  31     128.424 110.675 116.864  1.00107.91           O  
ATOM    323  CB  ASN C  31     126.371 111.508 114.524  1.00107.91           C  
ATOM    324  CG  ASN C  31     125.390 111.412 115.636  1.00107.91           C  
ATOM    325  OD1 ASN C  31     125.620 110.702 116.601  1.00107.91           O  
ATOM    326  ND2 ASN C  31     124.271 112.092 115.503  1.00107.91           N  
ATOM    327  N   VAL C  32     129.448 111.823 115.230  1.00109.88           N  
ATOM    328  CA  VAL C  32     130.317 112.522 116.166  1.00109.88           C  
ATOM    329  C   VAL C  32     129.748 113.889 116.518  1.00109.88           C  
ATOM    330  O   VAL C  32     129.499 114.186 117.689  1.00109.88           O  
ATOM    331  CB  VAL C  32     131.748 112.611 115.607  1.00109.88           C  
ATOM    332  CG1 VAL C  32     132.610 113.429 116.506  1.00109.88           C  
ATOM    333  CG2 VAL C  32     132.346 111.225 115.502  1.00109.88           C  
ATOM    334  N   GLY C  33     129.514 114.729 115.526  1.00109.97           N  
ATOM    335  CA  GLY C  33     129.158 116.102 115.800  1.00109.97           C  
ATOM    336  C   GLY C  33     127.724 116.276 116.242  1.00109.97           C  
ATOM    337  O   GLY C  33     127.069 115.360 116.734  1.00109.97           O  
ATOM    338  N   SER C  34     127.237 117.498 116.057  1.00112.71           N  
ATOM    339  CA  SER C  34     125.906 117.854 116.520  1.00112.71           C  
ATOM    340  C   SER C  34     124.848 117.366 115.547  1.00112.71           C  
ATOM    341  O   SER C  34     125.139 117.056 114.391  1.00112.71           O  
ATOM    342  CB  SER C  34     125.791 119.364 116.672  1.00112.71           C  
ATOM    343  OG  SER C  34     125.440 119.950 115.432  1.00112.71           O  
ATOM    344  N   ASN C  35     123.611 117.316 116.022  1.00106.83           N  
ATOM    345  CA  ASN C  35     122.453 116.938 115.231  1.00106.83           C  
ATOM    346  C   ASN C  35     121.227 117.667 115.754  1.00106.83           C  
ATOM    347  O   ASN C  35     121.328 118.620 116.527  1.00106.83           O  
ATOM    348  CB  ASN C  35     122.248 115.431 115.267  1.00106.83           C  
ATOM    349  CG  ASN C  35     123.379 114.694 114.638  1.00106.83           C  
ATOM    350  OD1 ASN C  35     124.287 114.232 115.324  1.00106.83           O  
ATOM    351  ND2 ASN C  35     123.345 114.577 113.321  1.00106.83           N  
ATOM    352  N   THR C  36     120.064 117.195 115.332  1.00 96.23           N  
ATOM    353  CA  THR C  36     118.800 117.749 115.769  1.00 96.23           C  
ATOM    354  C   THR C  36     117.679 116.925 115.190  1.00 96.23           C  
ATOM    355  O   THR C  36     117.721 116.546 114.031  1.00 96.23           O  
ATOM    356  CB  THR C  36     118.638 119.202 115.336  1.00 96.23           C  
ATOM    357  OG1 THR C  36     119.478 120.026 116.150  1.00 96.23           O  
ATOM    358  CG2 THR C  36     117.202 119.653 115.490  1.00 96.23           C  
HETATM  359  N   TYC C  37     116.676 116.635 115.999  1.00 88.81           N  
HETATM  360  CA  TYC C  37     115.536 115.865 115.514  1.00 88.81           C  
HETATM  361  C   TYC C  37     114.296 116.630 115.812  1.00 88.81           C  
HETATM  362  O   TYC C  37     113.334 116.043 116.265  1.00 88.81           O  
HETATM  363  CB  TYC C  37     115.511 114.500 116.168  1.00 88.81           C  
HETATM  364  CG  TYC C  37     116.754 113.756 115.761  1.00 88.81           C  
HETATM  365  CD1 TYC C  37     117.906 113.852 116.517  1.00 88.81           C  
HETATM  366  CD2 TYC C  37     116.746 112.965 114.633  1.00 88.81           C  
HETATM  367  CE1 TYC C  37     119.048 113.165 116.145  1.00 88.81           C  
HETATM  368  CE2 TYC C  37     117.887 112.279 114.261  1.00 88.81           C  
HETATM  369  OH  TYC C  37     120.155 111.699 114.650  1.00 88.81           O  
HETATM  370  CZ  TYC C  37     119.037 112.375 115.016  1.00 88.81           C  
HETATM  371  NXT TYC C  37     114.288 117.935 115.568  1.00 88.81           N  
TER     372      TYC C  37                                                      
ATOM    373  N   ALA E  13     131.326 101.060 110.230  1.00106.19           N  
ATOM    374  CA  ALA E  13     129.900 101.156 110.515  1.00106.19           C  
ATOM    375  C   ALA E  13     129.110 100.167 109.668  1.00106.19           C  
ATOM    376  O   ALA E  13     129.073 100.274 108.445  1.00106.19           O  
ATOM    377  CB  ALA E  13     129.413 102.565 110.276  1.00106.19           C  
ATOM    378  N   ASN E  14     128.481  99.201 110.327  1.00109.53           N  
ATOM    379  CA  ASN E  14     127.745  98.142 109.653  1.00109.53           C  
ATOM    380  C   ASN E  14     126.254  98.412 109.755  1.00109.53           C  
ATOM    381  O   ASN E  14     125.712  98.481 110.859  1.00109.53           O  
ATOM    382  CB  ASN E  14     128.073  96.783 110.269  1.00109.53           C  
ATOM    383  CG  ASN E  14     129.559  96.500 110.295  1.00109.53           C  
ATOM    384  OD1 ASN E  14     130.300  96.941 109.419  1.00109.53           O  
ATOM    385  ND2 ASN E  14     130.004  95.757 111.301  1.00109.53           N  
ATOM    386  N   PHE E  15     125.592  98.548 108.608  1.00101.38           N  
ATOM    387  CA  PHE E  15     124.167  98.867 108.564  1.00101.38           C  
ATOM    388  C   PHE E  15     123.478  97.860 107.660  1.00101.38           C  
ATOM    389  O   PHE E  15     123.752  97.816 106.459  1.00101.38           O  
ATOM    390  CB  PHE E  15     123.920 100.278 108.040  1.00101.38           C  
ATOM    391  CG  PHE E  15     124.287 101.358 108.994  1.00101.38           C  
ATOM    392  CD1 PHE E  15     125.585 101.524 109.412  1.00101.38           C  
ATOM    393  CD2 PHE E  15     123.337 102.236 109.438  1.00101.38           C  
ATOM    394  CE1 PHE E  15     125.914 102.526 110.275  1.00101.38           C  
ATOM    395  CE2 PHE E  15     123.660 103.238 110.293  1.00101.38           C  
ATOM    396  CZ  PHE E  15     124.950 103.381 110.718  1.00101.38           C  
ATOM    397  N   LEU E  16     122.580  97.065 108.224  1.00 92.57           N  
ATOM    398  CA  LEU E  16     121.721  96.202 107.432  1.00 92.57           C  
ATOM    399  C   LEU E  16     120.302  96.352 107.944  1.00 92.57           C  
ATOM    400  O   LEU E  16     120.067  96.286 109.153  1.00 92.57           O  
ATOM    401  CB  LEU E  16     122.163  94.741 107.507  1.00 92.57           C  
ATOM    402  CG  LEU E  16     121.546  93.828 106.444  1.00 92.57           C  
ATOM    403  CD1 LEU E  16     122.514  92.719 106.094  1.00 92.57           C  
ATOM    404  CD2 LEU E  16     120.209  93.240 106.881  1.00 92.57           C  
ATOM    405  N   VAL E  17     119.362  96.550 107.029  1.00 84.90           N  
ATOM    406  CA  VAL E  17     117.961  96.710 107.378  1.00 84.90           C  
ATOM    407  C   VAL E  17     117.156  95.764 106.512  1.00 84.90           C  
ATOM    408  O   VAL E  17     117.297  95.769 105.286  1.00 84.90           O  
ATOM    409  CB  VAL E  17     117.480  98.151 107.186  1.00 84.90           C  
ATOM    410  CG1 VAL E  17     115.988  98.212 107.355  1.00 84.90           C  
ATOM    411  CG2 VAL E  17     118.165  99.065 108.170  1.00 84.90           C  
ATOM    412  N   HIS E  18     116.314  94.956 107.142  1.00 83.02           N  
ATOM    413  CA  HIS E  18     115.502  93.965 106.449  1.00 83.02           C  
ATOM    414  C   HIS E  18     114.077  94.143 106.956  1.00 83.02           C  
ATOM    415  O   HIS E  18     113.659  93.475 107.902  1.00 83.02           O  
ATOM    416  CB  HIS E  18     116.051  92.568 106.701  1.00 83.02           C  
ATOM    417  CG  HIS E  18     115.125  91.465 106.304  1.00 83.02           C  
ATOM    418  ND1 HIS E  18     115.283  90.173 106.752  1.00 83.02           N  
ATOM    419  CD2 HIS E  18     114.036  91.454 105.501  1.00 83.02           C  
ATOM    420  CE1 HIS E  18     114.326  89.415 106.248  1.00 83.02           C  
ATOM    421  NE2 HIS E  18     113.556  90.168 105.486  1.00 83.02           N  
ATOM    422  N   SER E  19     113.336  95.046 106.329  1.00 79.83           N  
ATOM    423  CA  SER E  19     111.982  95.353 106.755  1.00 79.83           C  
ATOM    424  C   SER E  19     110.971  94.517 105.992  1.00 79.83           C  
ATOM    425  O   SER E  19     111.280  93.907 104.970  1.00 79.83           O  
ATOM    426  CB  SER E  19     111.673  96.828 106.548  1.00 79.83           C  
ATOM    427  OG  SER E  19     110.274  97.033 106.557  1.00 79.83           O  
ATOM    428  N   SER E  20     109.745  94.484 106.510  1.00 85.00           N  
ATOM    429  CA  SER E  20     108.655  93.799 105.827  1.00 85.00           C  
ATOM    430  C   SER E  20     107.535  94.751 105.434  1.00 85.00           C  
ATOM    431  O   SER E  20     107.205  94.842 104.250  1.00 85.00           O  
ATOM    432  CB  SER E  20     108.105  92.677 106.706  1.00 85.00           C  
ATOM    433  OG  SER E  20     107.111  93.183 107.573  1.00 85.00           O  
ATOM    434  N   ASN E  21     106.940  95.463 106.388  1.00 86.38           N  
ATOM    435  CA  ASN E  21     105.886  96.440 106.121  1.00 86.38           C  
ATOM    436  C   ASN E  21     106.265  97.682 106.902  1.00 86.38           C  
ATOM    437  O   ASN E  21     105.842  97.853 108.045  1.00 86.38           O  
ATOM    438  CB  ASN E  21     104.527  95.935 106.534  1.00 86.38           C  
ATOM    439  CG  ASN E  21     104.227  94.575 105.991  1.00 86.38           C  
ATOM    440  OD1 ASN E  21     104.575  94.256 104.858  1.00 86.38           O  
ATOM    441  ND2 ASN E  21     103.567  93.755 106.796  1.00 86.38           N  
ATOM    442  N   ASN E  22     107.044  98.558 106.285  1.00 83.11           N  
ATOM    443  CA  ASN E  22     107.703  99.597 107.059  1.00 83.11           C  
ATOM    444  C   ASN E  22     106.715 100.645 107.554  1.00 83.11           C  
ATOM    445  O   ASN E  22     106.662 100.936 108.752  1.00 83.11           O  
ATOM    446  CB  ASN E  22     108.803 100.237 106.234  1.00 83.11           C  
ATOM    447  CG  ASN E  22     109.536 101.279 106.996  1.00 83.11           C  
ATOM    448  OD1 ASN E  22     109.533 101.280 108.218  1.00 83.11           O  
ATOM    449  ND2 ASN E  22     110.168 102.191 106.288  1.00 83.11           N  
ATOM    450  N   PHE E  23     105.958 101.253 106.640  1.00 82.47           N  
ATOM    451  CA  PHE E  23     104.979 102.293 106.951  1.00 82.47           C  
ATOM    452  C   PHE E  23     105.589 103.609 107.402  1.00 82.47           C  
ATOM    453  O   PHE E  23     104.855 104.557 107.682  1.00 82.47           O  
ATOM    454  CB  PHE E  23     104.062 101.899 108.106  1.00 82.47           C  
ATOM    455  CG  PHE E  23     102.865 101.137 107.705  1.00 82.47           C  
ATOM    456  CD1 PHE E  23     101.963 101.672 106.828  1.00 82.47           C  
ATOM    457  CD2 PHE E  23     102.595  99.915 108.272  1.00 82.47           C  
ATOM    458  CE1 PHE E  23     100.847 100.978 106.482  1.00 82.47           C  
ATOM    459  CE2 PHE E  23     101.475  99.223 107.932  1.00 82.47           C  
ATOM    460  CZ  PHE E  23     100.600  99.753 107.037  1.00 82.47           C  
ATOM    461  N   GLY E  24     106.907 103.697 107.481  1.00 81.21           N  
ATOM    462  CA  GLY E  24     107.477 104.840 108.148  1.00 81.21           C  
ATOM    463  C   GLY E  24     108.972 104.922 107.971  1.00 81.21           C  
ATOM    464  O   GLY E  24     109.585 104.103 107.291  1.00 81.21           O  
ATOM    465  N   ALA E  25     109.553 105.927 108.605  1.00 80.46           N  
ATOM    466  CA  ALA E  25     110.951 106.243 108.373  1.00 80.46           C  
ATOM    467  C   ALA E  25     111.842 105.179 108.984  1.00 80.46           C  
ATOM    468  O   ALA E  25     111.810 104.959 110.195  1.00 80.46           O  
ATOM    469  CB  ALA E  25     111.282 107.609 108.958  1.00 80.46           C  
ATOM    470  N   ILE E  26     112.626 104.510 108.153  1.00 76.50           N  
ATOM    471  CA  ILE E  26     113.780 103.756 108.619  1.00 76.50           C  
ATOM    472  C   ILE E  26     114.966 104.664 108.339  1.00 76.50           C  
ATOM    473  O   ILE E  26     115.628 104.562 107.312  1.00 76.50           O  
ATOM    474  CB  ILE E  26     113.907 102.411 107.921  1.00 76.50           C  
ATOM    475  CG1 ILE E  26     112.676 101.568 108.189  1.00 76.50           C  
ATOM    476  CG2 ILE E  26     115.126 101.682 108.412  1.00 76.50           C  
ATOM    477  CD1 ILE E  26     112.738 100.209 107.559  1.00 76.50           C  
ATOM    478  N   LEU E  27     115.253 105.556 109.272  1.00 80.07           N  
ATOM    479  CA  LEU E  27     116.207 106.618 108.990  1.00 80.07           C  
ATOM    480  C   LEU E  27     117.620 106.165 109.310  1.00 80.07           C  
ATOM    481  O   LEU E  27     118.329 106.757 110.110  1.00 80.07           O  
ATOM    482  CB  LEU E  27     115.828 107.865 109.774  1.00 80.07           C  
ATOM    483  CG  LEU E  27     116.323 109.222 109.281  1.00 80.07           C  
ATOM    484  CD1 LEU E  27     115.322 110.257 109.722  1.00 80.07           C  
ATOM    485  CD2 LEU E  27     117.709 109.601 109.766  1.00 80.07           C  
ATOM    486  N   SER E  28     118.037 105.076 108.692  1.00 81.76           N  
ATOM    487  CA  SER E  28     119.359 104.537 108.966  1.00 81.76           C  
ATOM    488  C   SER E  28     120.401 105.464 108.358  1.00 81.76           C  
ATOM    489  O   SER E  28     120.492 105.578 107.135  1.00 81.76           O  
ATOM    490  CB  SER E  28     119.457 103.129 108.398  1.00 81.76           C  
ATOM    491  OG  SER E  28     120.568 102.449 108.929  1.00 81.76           O  
ATOM    492  N   SER E  29     121.189 106.135 109.194  1.00 92.62           N  
ATOM    493  CA  SER E  29     122.067 107.182 108.692  1.00 92.62           C  
ATOM    494  C   SER E  29     123.347 107.236 109.509  1.00 92.62           C  
ATOM    495  O   SER E  29     123.536 106.475 110.457  1.00 92.62           O  
ATOM    496  CB  SER E  29     121.382 108.543 108.729  1.00 92.62           C  
ATOM    497  OG  SER E  29     121.097 108.921 110.060  1.00 92.62           O  
ATOM    498  N   THR E  30     124.230 108.157 109.120  1.00105.01           N  
ATOM    499  CA  THR E  30     125.489 108.402 109.817  1.00105.01           C  
ATOM    500  C   THR E  30     126.073 109.709 109.308  1.00105.01           C  
ATOM    501  O   THR E  30     125.959 110.012 108.118  1.00105.01           O  
ATOM    502  CB  THR E  30     126.497 107.272 109.601  1.00105.01           C  
ATOM    503  OG1 THR E  30     125.898 106.021 109.940  1.00105.01           O  
ATOM    504  CG2 THR E  30     127.722 107.474 110.476  1.00105.01           C  
ATOM    505  N   ASN E  31     126.712 110.468 110.197  1.00107.39           N  
ATOM    506  CA  ASN E  31     127.181 111.799 109.841  1.00107.39           C  
ATOM    507  C   ASN E  31     128.148 112.376 110.858  1.00107.39           C  
ATOM    508  O   ASN E  31     128.096 112.033 112.037  1.00107.39           O  
ATOM    509  CB  ASN E  31     125.997 112.737 109.695  1.00107.39           C  
ATOM    510  CG  ASN E  31     125.023 112.579 110.806  1.00107.39           C  
ATOM    511  OD1 ASN E  31     125.296 111.885 111.772  1.00107.39           O  
ATOM    512  ND2 ASN E  31     123.864 113.188 110.672  1.00107.39           N  
ATOM    513  N   VAL E  32     129.048 113.243 110.405  1.00114.06           N  
ATOM    514  CA  VAL E  32     129.870 113.995 111.343  1.00114.06           C  
ATOM    515  C   VAL E  32     129.216 115.324 111.694  1.00114.06           C  
ATOM    516  O   VAL E  32     128.948 115.604 112.865  1.00114.06           O  
ATOM    517  CB  VAL E  32     131.294 114.173 110.785  1.00114.06           C  
ATOM    518  CG1 VAL E  32     132.102 115.043 111.684  1.00114.06           C  
ATOM    519  CG2 VAL E  32     131.977 112.825 110.683  1.00114.06           C  
ATOM    520  N   GLY E  33     128.931 116.148 110.702  1.00114.13           N  
ATOM    521  CA  GLY E  33     128.490 117.496 110.977  1.00114.13           C  
ATOM    522  C   GLY E  33     127.047 117.580 111.417  1.00114.13           C  
ATOM    523  O   GLY E  33     126.451 116.624 111.908  1.00114.13           O  
ATOM    524  N   SER E  34     126.485 118.769 111.232  1.00114.27           N  
ATOM    525  CA  SER E  34     125.134 119.041 111.693  1.00114.27           C  
ATOM    526  C   SER E  34     124.109 118.487 110.719  1.00114.27           C  
ATOM    527  O   SER E  34     124.421 118.197 109.563  1.00114.27           O  
ATOM    528  CB  SER E  34     124.925 120.541 111.846  1.00114.27           C  
ATOM    529  OG  SER E  34     124.539 121.104 110.605  1.00114.27           O  
ATOM    530  N   ASN E  35     122.878 118.361 111.192  1.00105.31           N  
ATOM    531  CA  ASN E  35     121.746 117.911 110.399  1.00105.31           C  
ATOM    532  C   ASN E  35     120.477 118.561 110.922  1.00105.31           C  
ATOM    533  O   ASN E  35     120.517 119.519 111.695  1.00105.31           O  
ATOM    534  CB  ASN E  35     121.636 116.394 110.435  1.00105.31           C  
ATOM    535  CG  ASN E  35     122.811 115.730 109.807  1.00105.31           C  
ATOM    536  OD1 ASN E  35     123.746 115.325 110.494  1.00105.31           O  
ATOM    537  ND2 ASN E  35     122.786 115.611 108.490  1.00105.31           N  
ATOM    538  N   THR E  36     119.346 118.018 110.498  1.00 94.60           N  
ATOM    539  CA  THR E  36     118.049 118.492 110.934  1.00 94.60           C  
ATOM    540  C   THR E  36     116.983 117.599 110.353  1.00 94.60           C  
ATOM    541  O   THR E  36     117.050 117.224 109.195  1.00 94.60           O  
ATOM    542  CB  THR E  36     117.798 119.932 110.501  1.00 94.60           C  
ATOM    543  OG1 THR E  36     118.583 120.807 111.316  1.00 94.60           O  
ATOM    544  CG2 THR E  36     116.336 120.292 110.654  1.00 94.60           C  
HETATM  545  N   TYC E  37     115.999 117.247 111.161  1.00 86.67           N  
HETATM  546  CA  TYC E  37     114.910 116.407 110.675  1.00 86.67           C  
HETATM  547  C   TYC E  37     113.624 117.094 110.971  1.00 86.67           C  
HETATM  548  O   TYC E  37     112.701 116.447 111.422  1.00 86.67           O  
HETATM  549  CB  TYC E  37     114.969 115.044 111.328  1.00 86.67           C  
HETATM  550  CG  TYC E  37     116.258 114.379 110.922  1.00 86.67           C  
HETATM  551  CD1 TYC E  37     117.400 114.547 111.679  1.00 86.67           C  
HETATM  552  CD2 TYC E  37     116.300 113.589 109.794  1.00 86.67           C  
HETATM  553  CE1 TYC E  37     118.583 113.932 111.309  1.00 86.67           C  
HETATM  554  CE2 TYC E  37     117.482 112.976 109.423  1.00 86.67           C  
HETATM  555  OH  TYC E  37     119.781 112.539 109.815  1.00 86.67           O  
HETATM  556  CZ  TYC E  37     118.623 113.143 110.179  1.00 86.67           C  
HETATM  557  NXT TYC E  37     113.535 118.396 110.727  1.00 86.67           N  
TER     558      TYC E  37                                                      
ATOM    559  N   ALA G  13     131.630 102.574 105.333  1.00108.22           N  
ATOM    560  CA  ALA G  13     130.201 102.582 105.620  1.00108.22           C  
ATOM    561  C   ALA G  13     129.472 101.546 104.774  1.00108.22           C  
ATOM    562  O   ALA G  13     129.427 101.652 103.551  1.00108.22           O  
ATOM    563  CB  ALA G  13     129.628 103.959 105.382  1.00108.22           C  
ATOM    564  N   ASN G  14     128.904 100.544 105.433  1.00109.56           N  
ATOM    565  CA  ASN G  14     128.234  99.442 104.759  1.00109.56           C  
ATOM    566  C   ASN G  14     126.729  99.620 104.863  1.00109.56           C  
ATOM    567  O   ASN G  14     126.186  99.655 105.968  1.00109.56           O  
ATOM    568  CB  ASN G  14     128.644  98.105 105.374  1.00109.56           C  
ATOM    569  CG  ASN G  14     130.146  97.913 105.397  1.00109.56           C  
ATOM    570  OD1 ASN G  14     130.857  98.400 104.520  1.00109.56           O  
ATOM    571  ND2 ASN G  14     130.636  97.199 106.402  1.00109.56           N  
ATOM    572  N   PHE G  15     126.058  99.716 103.718  1.00104.56           N  
ATOM    573  CA  PHE G  15     124.616  99.947 103.676  1.00104.56           C  
ATOM    574  C   PHE G  15     123.989  98.900 102.773  1.00104.56           C  
ATOM    575  O   PHE G  15     124.263  98.874 101.571  1.00104.56           O  
ATOM    576  CB  PHE G  15     124.283 101.341 103.153  1.00104.56           C  
ATOM    577  CG  PHE G  15     124.584 102.441 104.107  1.00104.56           C  
ATOM    578  CD1 PHE G  15     125.870 102.686 104.524  1.00104.56           C  
ATOM    579  CD2 PHE G  15     123.583 103.258 104.553  1.00104.56           C  
ATOM    580  CE1 PHE G  15     126.138 103.706 105.387  1.00104.56           C  
ATOM    581  CE2 PHE G  15     123.845 104.277 105.409  1.00104.56           C  
ATOM    582  CZ  PHE G  15     125.125 104.499 105.832  1.00104.56           C  
ATOM    583  N   LEU G  16     123.142  98.052 103.336  1.00 98.26           N  
ATOM    584  CA  LEU G  16     122.336  97.138 102.546  1.00 98.26           C  
ATOM    585  C   LEU G  16     120.911  97.200 103.059  1.00 98.26           C  
ATOM    586  O   LEU G  16     120.682  97.120 104.269  1.00 98.26           O  
ATOM    587  CB  LEU G  16     122.867  95.707 102.619  1.00 98.26           C  
ATOM    588  CG  LEU G  16     122.305  94.759 101.556  1.00 98.26           C  
ATOM    589  CD1 LEU G  16     123.339  93.711 101.204  1.00 98.26           C  
ATOM    590  CD2 LEU G  16     121.008  94.090 101.994  1.00 98.26           C  
ATOM    591  N   VAL G  17     119.960  97.342 102.146  1.00 90.33           N  
ATOM    592  CA  VAL G  17     118.552  97.415 102.497  1.00 90.33           C  
ATOM    593  C   VAL G  17     117.805  96.422 101.632  1.00 90.33           C  
ATOM    594  O   VAL G  17     117.944  96.436 100.406  1.00 90.33           O  
ATOM    595  CB  VAL G  17     117.983  98.824 102.307  1.00 90.33           C  
ATOM    596  CG1 VAL G  17     116.491  98.794 102.478  1.00 90.33           C  
ATOM    597  CG2 VAL G  17     118.613  99.778 103.291  1.00 90.33           C  
ATOM    598  N   HIS G  18     117.015  95.564 102.263  1.00 88.12           N  
ATOM    599  CA  HIS G  18     116.264  94.525 101.569  1.00 88.12           C  
ATOM    600  C   HIS G  18     114.832  94.616 102.079  1.00 88.12           C  
ATOM    601  O   HIS G  18     114.457  93.922 103.025  1.00 88.12           O  
ATOM    602  CB  HIS G  18     116.898  93.165 101.820  1.00 88.12           C  
ATOM    603  CG  HIS G  18     116.041  92.006 101.424  1.00 88.12           C  
ATOM    604  ND1 HIS G  18     116.279  90.727 101.870  1.00 88.12           N  
ATOM    605  CD2 HIS G  18     114.953  91.930 100.622  1.00 88.12           C  
ATOM    606  CE1 HIS G  18     115.369  89.912 101.367  1.00 88.12           C  
ATOM    607  NE2 HIS G  18     114.553  90.617 100.607  1.00 88.12           N  
ATOM    608  N   SER G  19     114.036  95.472 101.454  1.00 85.62           N  
ATOM    609  CA  SER G  19     112.667  95.695 101.882  1.00 85.62           C  
ATOM    610  C   SER G  19     111.707  94.799 101.120  1.00 85.62           C  
ATOM    611  O   SER G  19     112.052  94.210 100.097  1.00 85.62           O  
ATOM    612  CB  SER G  19     112.267  97.149 101.677  1.00 85.62           C  
ATOM    613  OG  SER G  19     110.859  97.267 101.688  1.00 85.62           O  
ATOM    614  N   SER G  20     110.487  94.691 101.639  1.00 89.88           N  
ATOM    615  CA  SER G  20     109.439  93.941 100.958  1.00 89.88           C  
ATOM    616  C   SER G  20     108.263  94.822 100.567  1.00 89.88           C  
ATOM    617  O   SER G  20     107.926  94.894  99.383  1.00 89.88           O  
ATOM    618  CB  SER G  20     108.960  92.787 101.836  1.00 89.88           C  
ATOM    619  OG  SER G  20     107.938  93.230 102.705  1.00 89.88           O  
ATOM    620  N   ASN G  21     107.627  95.496 101.523  1.00 91.58           N  
ATOM    621  CA  ASN G  21     106.514  96.407 101.257  1.00 91.58           C  
ATOM    622  C   ASN G  21     106.818  97.669 102.039  1.00 91.58           C  
ATOM    623  O   ASN G  21     106.387  97.814 103.183  1.00 91.58           O  
ATOM    624  CB  ASN G  21     105.190  95.820 101.672  1.00 91.58           C  
ATOM    625  CG  ASN G  21     104.972  94.444 101.128  1.00 91.58           C  
ATOM    626  OD1 ASN G  21     105.337  94.147  99.995  1.00 91.58           O  
ATOM    627  ND2 ASN G  21     104.365  93.585 101.934  1.00 91.58           N  
ATOM    628  N   ASN G  22     107.541  98.592 101.421  1.00 85.92           N  
ATOM    629  CA  ASN G  22     108.136  99.669 102.195  1.00 85.92           C  
ATOM    630  C   ASN G  22     107.087 100.654 102.692  1.00 85.92           C  
ATOM    631  O   ASN G  22     107.017 100.941 103.891  1.00 85.92           O  
ATOM    632  CB  ASN G  22     109.193 100.375 101.369  1.00 85.92           C  
ATOM    633  CG  ASN G  22     109.863 101.460 102.131  1.00 85.92           C  
ATOM    634  OD1 ASN G  22     109.861 101.460 103.353  1.00 85.92           O  
ATOM    635  ND2 ASN G  22     110.436 102.409 101.422  1.00 85.92           N  
ATOM    636  N   PHE G  23     106.293 101.215 101.780  1.00 85.16           N  
ATOM    637  CA  PHE G  23     105.252 102.194 102.093  1.00 85.16           C  
ATOM    638  C   PHE G  23     105.780 103.543 102.544  1.00 85.16           C  
ATOM    639  O   PHE G  23     104.991 104.446 102.826  1.00 85.16           O  
ATOM    640  CB  PHE G  23     104.362 101.743 103.249  1.00 85.16           C  
ATOM    641  CG  PHE G  23     103.213 100.909 102.850  1.00 85.16           C  
ATOM    642  CD1 PHE G  23     102.280 101.388 101.974  1.00 85.16           C  
ATOM    643  CD2 PHE G  23     103.020  99.673 103.416  1.00 85.16           C  
ATOM    644  CE1 PHE G  23     101.207 100.628 101.629  1.00 85.16           C  
ATOM    645  CE2 PHE G  23     101.944  98.913 103.077  1.00 85.16           C  
ATOM    646  CZ  PHE G  23     101.037  99.390 102.183  1.00 85.16           C  
ATOM    647  N   GLY G  24     107.091 103.711 102.621  1.00 81.16           N  
ATOM    648  CA  GLY G  24     107.591 104.888 103.288  1.00 81.16           C  
ATOM    649  C   GLY G  24     109.078 105.061 103.109  1.00 81.16           C  
ATOM    650  O   GLY G  24     109.739 104.281 102.428  1.00 81.16           O  
ATOM    651  N   ALA G  25     109.598 106.100 103.743  1.00 82.67           N  
ATOM    652  CA  ALA G  25     110.973 106.500 103.509  1.00 82.67           C  
ATOM    653  C   ALA G  25     111.929 105.493 104.118  1.00 82.67           C  
ATOM    654  O   ALA G  25     111.911 105.270 105.329  1.00 82.67           O  
ATOM    655  CB  ALA G  25     111.221 107.884 104.095  1.00 82.67           C  
ATOM    656  N   ILE G  26     112.750 104.874 103.285  1.00 78.26           N  
ATOM    657  CA  ILE G  26     113.949 104.191 103.749  1.00 78.26           C  
ATOM    658  C   ILE G  26     115.078 105.170 103.469  1.00 78.26           C  
ATOM    659  O   ILE G  26     115.743 105.110 102.440  1.00 78.26           O  
ATOM    660  CB  ILE G  26     114.157 102.857 103.050  1.00 78.26           C  
ATOM    661  CG1 ILE G  26     112.980 101.939 103.320  1.00 78.26           C  
ATOM    662  CG2 ILE G  26     115.419 102.204 103.539  1.00 78.26           C  
ATOM    663  CD1 ILE G  26     113.125 100.588 102.688  1.00 78.26           C  
ATOM    664  N   LEU G  27     115.310 106.077 104.402  1.00 81.24           N  
ATOM    665  CA  LEU G  27     116.197 107.197 104.119  1.00 81.24           C  
ATOM    666  C   LEU G  27     117.636 106.830 104.436  1.00 81.24           C  
ATOM    667  O   LEU G  27     118.308 107.464 105.236  1.00 81.24           O  
ATOM    668  CB  LEU G  27     115.744 108.417 104.905  1.00 81.24           C  
ATOM    669  CG  LEU G  27     116.154 109.803 104.411  1.00 81.24           C  
ATOM    670  CD1 LEU G  27     115.092 110.774 104.855  1.00 81.24           C  
ATOM    671  CD2 LEU G  27     117.515 110.265 104.895  1.00 81.24           C  
ATOM    672  N   SER G  28     118.118 105.769 103.817  1.00 83.74           N  
ATOM    673  CA  SER G  28     119.470 105.312 104.089  1.00 83.74           C  
ATOM    674  C   SER G  28     120.453 106.301 103.480  1.00 83.74           C  
ATOM    675  O   SER G  28     120.535 106.422 102.257  1.00 83.74           O  
ATOM    676  CB  SER G  28     119.654 103.913 103.520  1.00 83.74           C  
ATOM    677  OG  SER G  28     120.805 103.302 104.048  1.00 83.74           O  
ATOM    678  N   SER G  29     121.200 107.019 104.315  1.00 94.07           N  
ATOM    679  CA  SER G  29     122.011 108.118 103.813  1.00 94.07           C  
ATOM    680  C   SER G  29     123.286 108.250 104.628  1.00 94.07           C  
ATOM    681  O   SER G  29     123.523 107.501 105.575  1.00 94.07           O  
ATOM    682  CB  SER G  29     121.244 109.435 103.851  1.00 94.07           C  
ATOM    683  OG  SER G  29     120.938 109.793 105.183  1.00 94.07           O  
ATOM    684  N   THR G  30     124.111 109.223 104.238  1.00106.50           N  
ATOM    685  CA  THR G  30     125.354 109.545 104.934  1.00106.50           C  
ATOM    686  C   THR G  30     125.856 110.886 104.425  1.00106.50           C  
ATOM    687  O   THR G  30     125.722 111.181 103.236  1.00106.50           O  
ATOM    688  CB  THR G  30     126.429 108.478 104.715  1.00106.50           C  
ATOM    689  OG1 THR G  30     125.908 107.193 105.054  1.00106.50           O  
ATOM    690  CG2 THR G  30     127.641 108.754 105.589  1.00106.50           C  
ATOM    691  N   ASN G  31     126.449 111.681 105.314  1.00107.70           N  
ATOM    692  CA  ASN G  31     126.835 113.038 104.958  1.00107.70           C  
ATOM    693  C   ASN G  31     127.766 113.673 105.973  1.00107.70           C  
ATOM    694  O   ASN G  31     127.737 113.327 107.153  1.00107.70           O  
ATOM    695  CB  ASN G  31     125.595 113.903 104.815  1.00107.70           C  
ATOM    696  CG  ASN G  31     124.634 113.684 105.926  1.00107.70           C  
ATOM    697  OD1 ASN G  31     124.950 113.007 106.891  1.00107.70           O  
ATOM    698  ND2 ASN G  31     123.439 114.222 105.795  1.00107.70           N  
ATOM    699  N   VAL G  32     128.610 114.594 105.520  1.00112.98           N  
ATOM    700  CA  VAL G  32     129.387 115.395 106.457  1.00112.98           C  
ATOM    701  C   VAL G  32     128.653 116.680 106.810  1.00112.98           C  
ATOM    702  O   VAL G  32     128.369 116.943 107.982  1.00112.98           O  
ATOM    703  CB  VAL G  32     130.795 115.660 105.898  1.00112.98           C  
ATOM    704  CG1 VAL G  32     131.550 116.578 106.796  1.00112.98           C  
ATOM    705  CG2 VAL G  32     131.559 114.358 105.793  1.00112.98           C  
ATOM    706  N   GLY G  33     128.317 117.486 105.819  1.00112.30           N  
ATOM    707  CA  GLY G  33     127.794 118.804 106.095  1.00112.30           C  
ATOM    708  C   GLY G  33     126.349 118.799 106.538  1.00112.30           C  
ATOM    709  O   GLY G  33     125.813 117.809 107.029  1.00112.30           O  
ATOM    710  N   SER G  34     125.715 119.952 106.355  1.00111.86           N  
ATOM    711  CA  SER G  34     124.351 120.141 106.818  1.00111.86           C  
ATOM    712  C   SER G  34     123.361 119.526 105.845  1.00111.86           C  
ATOM    713  O   SER G  34     123.687 119.256 104.688  1.00111.86           O  
ATOM    714  CB  SER G  34     124.051 121.625 106.972  1.00111.86           C  
ATOM    715  OG  SER G  34     123.629 122.164 105.732  1.00111.86           O  
ATOM    716  N   ASN G  35     122.140 119.324 106.320  1.00105.45           N  
ATOM    717  CA  ASN G  35     121.037 118.807 105.528  1.00105.45           C  
ATOM    718  C   ASN G  35     119.730 119.377 106.053  1.00105.45           C  
ATOM    719  O   ASN G  35     119.713 120.335 106.827  1.00105.45           O  
ATOM    720  CB  ASN G  35     121.019 117.285 105.563  1.00105.45           C  
ATOM    721  CG  ASN G  35     122.232 116.695 104.933  1.00105.45           C  
ATOM    722  OD1 ASN G  35     123.191 116.348 105.618  1.00105.45           O  
ATOM    723  ND2 ASN G  35     122.213 116.575 103.616  1.00105.45           N  
ATOM    724  N   THR G  36     118.634 118.766 105.631  1.00 96.53           N  
ATOM    725  CA  THR G  36     117.312 119.159 106.068  1.00 96.53           C  
ATOM    726  C   THR G  36     116.301 118.204 105.489  1.00 96.53           C  
ATOM    727  O   THR G  36     116.389 117.834 104.330  1.00 96.53           O  
ATOM    728  CB  THR G  36     116.972 120.582 105.638  1.00 96.53           C  
ATOM    729  OG1 THR G  36     117.704 121.502 106.452  1.00 96.53           O  
ATOM    730  CG2 THR G  36     115.491 120.852 105.792  1.00 96.53           C  
HETATM  731  N   TYC G  37     115.342 117.791 106.298  1.00 86.67           N  
HETATM  732  CA  TYC G  37     114.306 116.887 105.812  1.00 86.67           C  
HETATM  733  C   TYC G  37     112.981 117.493 106.111  1.00 86.67           C  
HETATM  734  O   TYC G  37     112.099 116.791 106.563  1.00 86.67           O  
HETATM  735  CB  TYC G  37     114.449 115.529 106.465  1.00 86.67           C  
HETATM  736  CG  TYC G  37     115.775 114.944 106.057  1.00 86.67           C  
HETATM  737  CD1 TYC G  37     116.906 115.181 106.812  1.00 86.67           C  
HETATM  738  CD2 TYC G  37     115.865 114.160 104.927  1.00 86.67           C  
HETATM  739  CE1 TYC G  37     118.124 114.640 106.440  1.00 86.67           C  
HETATM  740  CE2 TYC G  37     117.081 113.620 104.555  1.00 86.67           C  
HETATM  741  OH  TYC G  37     119.403 113.324 104.942  1.00 86.67           O  
HETATM  742  CZ  TYC G  37     118.211 113.856 105.309  1.00 86.67           C  
HETATM  743  NXT TYC G  37     112.811 118.787 105.869  1.00 86.67           N  
TER     744      TYC G  37                                                      
ATOM    745  N   ALA I  13     131.815 104.141 100.493  1.00112.69           N  
ATOM    746  CA  ALA I  13     130.388 104.060 100.778  1.00112.69           C  
ATOM    747  C   ALA I  13     129.726 102.981  99.932  1.00112.69           C  
ATOM    748  O   ALA I  13     129.675 103.083  98.709  1.00112.69           O  
ATOM    749  CB  ALA I  13     129.731 105.399 100.539  1.00112.69           C  
ATOM    750  N   ASN I  14     129.220 101.946 100.591  1.00114.17           N  
ATOM    751  CA  ASN I  14     128.620 100.804  99.917  1.00114.17           C  
ATOM    752  C   ASN I  14     127.107 100.888 100.020  1.00114.17           C  
ATOM    753  O   ASN I  14     126.561 100.891 101.124  1.00114.17           O  
ATOM    754  CB  ASN I  14     129.112  99.496 100.533  1.00114.17           C  
ATOM    755  CG  ASN I  14     130.623  99.397 100.558  1.00114.17           C  
ATOM    756  OD1 ASN I  14     131.303  99.927  99.682  1.00114.17           O  
ATOM    757  ND2 ASN I  14     131.156  98.715 101.564  1.00114.17           N  
ATOM    758  N   PHE I  15     126.433 100.942  98.873  1.00107.63           N  
ATOM    759  CA  PHE I  15     124.979 101.083  98.830  1.00107.63           C  
ATOM    760  C   PHE I  15     124.419  99.999  97.926  1.00107.63           C  
ATOM    761  O   PHE I  15     124.696  99.990  96.725  1.00107.63           O  
ATOM    762  CB  PHE I  15     124.561 102.453  98.306  1.00107.63           C  
ATOM    763  CG  PHE I  15     124.792 103.571  99.259  1.00107.63           C  
ATOM    764  CD1 PHE I  15     126.060 103.895  99.677  1.00107.63           C  
ATOM    765  CD2 PHE I  15     123.742 104.325  99.704  1.00107.63           C  
ATOM    766  CE1 PHE I  15     126.263 104.930 100.541  1.00107.63           C  
ATOM    767  CE2 PHE I  15     123.940 105.358 100.560  1.00107.63           C  
ATOM    768  CZ  PHE I  15     125.202 105.659 100.984  1.00107.63           C  
ATOM    769  N   LEU I  16     123.626  99.100  98.490  1.00101.02           N  
ATOM    770  CA  LEU I  16     122.879  98.137  97.699  1.00101.02           C  
ATOM    771  C   LEU I  16     121.453  98.112  98.211  1.00101.02           C  
ATOM    772  O   LEU I  16     121.228  98.018  99.420  1.00101.02           O  
ATOM    773  CB  LEU I  16     123.497  96.743  97.773  1.00101.02           C  
ATOM    774  CG  LEU I  16     122.997  95.761  96.711  1.00101.02           C  
ATOM    775  CD1 LEU I  16     124.094  94.779  96.360  1.00101.02           C  
ATOM    776  CD2 LEU I  16     121.743  95.013  97.147  1.00101.02           C  
ATOM    777  N   VAL I  17     120.495  98.193  97.297  1.00 91.87           N  
ATOM    778  CA  VAL I  17     119.085  98.180  97.646  1.00 91.87           C  
ATOM    779  C   VAL I  17     118.402  97.142  96.780  1.00 91.87           C  
ATOM    780  O   VAL I  17     118.542  97.164  95.554  1.00 91.87           O  
ATOM    781  CB  VAL I  17     118.430  99.550  97.454  1.00 91.87           C  
ATOM    782  CG1 VAL I  17     116.943  99.428  97.624  1.00 91.87           C  
ATOM    783  CG2 VAL I  17     118.999 100.542  98.439  1.00 91.87           C  
ATOM    784  N   HIS I  18     117.666  96.236  97.411  1.00 91.31           N  
ATOM    785  CA  HIS I  18     116.982  95.152  96.717  1.00 91.31           C  
ATOM    786  C   HIS I  18     115.546  95.154  97.225  1.00 91.31           C  
ATOM    787  O   HIS I  18     115.214  94.440  98.171  1.00 91.31           O  
ATOM    788  CB  HIS I  18     117.699  93.834  96.969  1.00 91.31           C  
ATOM    789  CG  HIS I  18     116.916  92.625  96.573  1.00 91.31           C  
ATOM    790  ND1 HIS I  18     117.232  91.363  97.020  1.00 91.31           N  
ATOM    791  CD2 HIS I  18     115.836  92.481  95.770  1.00 91.31           C  
ATOM    792  CE1 HIS I  18     116.375  90.492  96.517  1.00 91.31           C  
ATOM    793  NE2 HIS I  18     115.518  91.145  95.755  1.00 91.31           N  
ATOM    794  N   SER I  19     114.700  95.959  96.599  1.00 89.51           N  
ATOM    795  CA  SER I  19     113.319  96.098  97.026  1.00 89.51           C  
ATOM    796  C   SER I  19     112.418  95.143  96.263  1.00 89.51           C  
ATOM    797  O   SER I  19     112.799  94.576  95.241  1.00 89.51           O  
ATOM    798  CB  SER I  19     112.830  97.523  96.819  1.00 89.51           C  
ATOM    799  OG  SER I  19     111.417  97.554  96.829  1.00 89.51           O  
ATOM    800  N   SER I  20     111.206  94.960  96.781  1.00 93.30           N  
ATOM    801  CA  SER I  20     110.207  94.146  96.099  1.00 93.30           C  
ATOM    802  C   SER I  20     108.979  94.953  95.706  1.00 93.30           C  
ATOM    803  O   SER I  20     108.639  95.003  94.522  1.00 93.30           O  
ATOM    804  CB  SER I  20     109.800  92.965  96.977  1.00 93.30           C  
ATOM    805  OG  SER I  20     108.752  93.345  97.845  1.00 93.30           O  
ATOM    806  N   ASN I  21     108.301  95.586  96.661  1.00 95.87           N  
ATOM    807  CA  ASN I  21     107.135  96.426  96.394  1.00 95.87           C  
ATOM    808  C   ASN I  21     107.358  97.705  97.175  1.00 95.87           C  
ATOM    809  O   ASN I  21     106.918  97.823  98.319  1.00 95.87           O  
ATOM    810  CB  ASN I  21     105.848  95.758  96.807  1.00 95.87           C  
ATOM    811  CG  ASN I  21     105.718  94.371  96.264  1.00 95.87           C  
ATOM    812  OD1 ASN I  21     106.101  94.097  95.131  1.00 95.87           O  
ATOM    813  ND2 ASN I  21     105.164  93.476  97.070  1.00 95.87           N  
ATOM    814  N   ASN I  22     108.024  98.670  96.558  1.00 90.49           N  
ATOM    815  CA  ASN I  22     108.550  99.782  97.332  1.00 90.49           C  
ATOM    816  C   ASN I  22     107.441 100.701  97.827  1.00 90.49           C  
ATOM    817  O   ASN I  22     107.352 100.983  99.026  1.00 90.49           O  
ATOM    818  CB  ASN I  22     109.562 100.553  96.506  1.00 90.49           C  
ATOM    819  CG  ASN I  22     110.162 101.677  97.269  1.00 90.49           C  
ATOM    820  OD1 ASN I  22     110.159 101.678  98.491  1.00 90.49           O  
ATOM    821  ND2 ASN I  22     110.676 102.660  96.560  1.00 90.49           N  
ATOM    822  N   PHE I  23     106.615 101.211  96.914  1.00 92.80           N  
ATOM    823  CA  PHE I  23     105.515 102.123  97.225  1.00 92.80           C  
ATOM    824  C   PHE I  23     105.958 103.504  97.676  1.00 92.80           C  
ATOM    825  O   PHE I  23     105.114 104.355  97.956  1.00 92.80           O  
ATOM    826  CB  PHE I  23     104.654 101.620  98.381  1.00 92.80           C  
ATOM    827  CG  PHE I  23     103.559 100.715  97.980  1.00 92.80           C  
ATOM    828  CD1 PHE I  23     102.598 101.135  97.104  1.00 92.80           C  
ATOM    829  CD2 PHE I  23     103.442  99.469  98.547  1.00 92.80           C  
ATOM    830  CE1 PHE I  23     101.576 100.310  96.757  1.00 92.80           C  
ATOM    831  CE2 PHE I  23     102.416  98.645  98.208  1.00 92.80           C  
ATOM    832  CZ  PHE I  23     101.482  99.064  97.312  1.00 92.80           C  
ATOM    833  N   GLY I  24     107.256 103.752  97.754  1.00 87.01           N  
ATOM    834  CA  GLY I  24     107.681 104.958  98.421  1.00 87.01           C  
ATOM    835  C   GLY I  24     109.154 105.223  98.244  1.00 87.01           C  
ATOM    836  O   GLY I  24     109.863 104.485  97.564  1.00 87.01           O  
ATOM    837  N   ALA I  25     109.608 106.292  98.877  1.00 86.84           N  
ATOM    838  CA  ALA I  25     110.956 106.777  98.645  1.00 86.84           C  
ATOM    839  C   ALA I  25     111.972 105.832  99.256  1.00 86.84           C  
ATOM    840  O   ALA I  25     111.967 105.609 100.467  1.00 86.84           O  
ATOM    841  CB  ALA I  25     111.117 108.174  99.230  1.00 86.84           C  
ATOM    842  N   ILE I  26     112.831 105.264  98.424  1.00 82.04           N  
ATOM    843  CA  ILE I  26     114.070 104.658  98.889  1.00 82.04           C  
ATOM    844  C   ILE I  26     115.135 105.705  98.610  1.00 82.04           C  
ATOM    845  O   ILE I  26     115.804 105.685  97.582  1.00 82.04           O  
ATOM    846  CB  ILE I  26     114.361 103.338  98.192  1.00 82.04           C  
ATOM    847  CG1 ILE I  26     113.243 102.350  98.460  1.00 82.04           C  
ATOM    848  CG2 ILE I  26     115.660 102.765  98.682  1.00 82.04           C  
ATOM    849  CD1 ILE I  26     113.472 101.009  97.829  1.00 82.04           C  
ATOM    850  N   LEU I  27     115.310 106.625  99.543  1.00 84.36           N  
ATOM    851  CA  LEU I  27     116.126 107.797  99.260  1.00 84.36           C  
ATOM    852  C   LEU I  27     117.585 107.521  99.579  1.00 84.36           C  
ATOM    853  O   LEU I  27     118.216 108.195 100.379  1.00 84.36           O  
ATOM    854  CB  LEU I  27     115.597 108.987 100.045  1.00 84.36           C  
ATOM    855  CG  LEU I  27     115.921 110.395  99.551  1.00 84.36           C  
ATOM    856  CD1 LEU I  27     114.800 111.299  99.992  1.00 84.36           C  
ATOM    857  CD2 LEU I  27     117.250 110.941 100.036  1.00 84.36           C  
ATOM    858  N   SER I  28     118.132 106.491  98.961  1.00 88.90           N  
ATOM    859  CA  SER I  28     119.510 106.119  99.235  1.00 88.90           C  
ATOM    860  C   SER I  28     120.430 107.167  98.626  1.00 88.90           C  
ATOM    861  O   SER I  28     120.506 107.292  97.403  1.00 88.90           O  
ATOM    862  CB  SER I  28     119.781 104.734  98.666  1.00 88.90           C  
ATOM    863  OG  SER I  28     120.967 104.195  99.196  1.00 88.90           O  
ATOM    864  N   SER I  29     121.130 107.930  99.462  1.00 97.49           N  
ATOM    865  CA  SER I  29     121.872 109.077  98.959  1.00 97.49           C  
ATOM    866  C   SER I  29     123.136 109.288  99.776  1.00 97.49           C  
ATOM    867  O   SER I  29     123.418 108.556 100.724  1.00 97.49           O  
ATOM    868  CB  SER I  29     121.025 110.343  98.997  1.00 97.49           C  
ATOM    869  OG  SER I  29     120.697 110.683 100.328  1.00 97.49           O  
ATOM    870  N   THR I  30     123.899 110.310  99.387  1.00109.74           N  
ATOM    871  CA  THR I  30     125.119 110.709 100.083  1.00109.74           C  
ATOM    872  C   THR I  30     125.537 112.078  99.574  1.00109.74           C  
ATOM    873  O   THR I  30     125.387 112.364  98.385  1.00109.74           O  
ATOM    874  CB  THR I  30     126.258 109.711  99.866  1.00109.74           C  
ATOM    875  OG1 THR I  30     125.817 108.396 100.205  1.00109.74           O  
ATOM    876  CG2 THR I  30     127.450 110.062 100.741  1.00109.74           C  
ATOM    877  N   ASN I  31     126.079 112.909 100.463  1.00112.44           N  
ATOM    878  CA  ASN I  31     126.380 114.288 100.107  1.00112.44           C  
ATOM    879  C   ASN I  31     127.269 114.979 101.123  1.00112.44           C  
ATOM    880  O   ASN I  31     127.260 114.632 102.303  1.00112.44           O  
ATOM    881  CB  ASN I  31     125.089 115.073  99.962  1.00112.44           C  
ATOM    882  CG  ASN I  31     124.143 114.796 101.073  1.00112.44           C  
ATOM    883  OD1 ASN I  31     124.499 114.141 102.038  1.00112.44           O  
ATOM    884  ND2 ASN I  31     122.917 115.258 100.940  1.00112.44           N  
ATOM    885  N   VAL I  32     128.055 115.951 100.670  1.00117.40           N  
ATOM    886  CA  VAL I  32     128.779 116.798 101.608  1.00117.40           C  
ATOM    887  C   VAL I  32     127.967 118.036 101.960  1.00117.40           C  
ATOM    888  O   VAL I  32     127.666 118.281 103.131  1.00117.40           O  
ATOM    889  CB  VAL I  32     130.170 117.150 101.050  1.00117.40           C  
ATOM    890  CG1 VAL I  32     130.866 118.113 101.950  1.00117.40           C  
ATOM    891  CG2 VAL I  32     131.014 115.897 100.947  1.00117.40           C  
ATOM    892  N   GLY I  33     127.582 118.820 100.967  1.00116.67           N  
ATOM    893  CA  GLY I  33     126.979 120.102 101.242  1.00116.67           C  
ATOM    894  C   GLY I  33     125.537 120.008 101.684  1.00116.67           C  
ATOM    895  O   GLY I  33     125.062 118.987 102.174  1.00116.67           O  
ATOM    896  N   SER I  34     124.832 121.119 101.499  1.00118.49           N  
ATOM    897  CA  SER I  34     123.459 121.223 101.960  1.00118.49           C  
ATOM    898  C   SER I  34     122.509 120.548 100.987  1.00118.49           C  
ATOM    899  O   SER I  34     122.853 120.298  99.831  1.00118.49           O  
ATOM    900  CB  SER I  34     123.067 122.686 102.114  1.00118.49           C  
ATOM    901  OG  SER I  34     122.614 123.197 100.873  1.00118.49           O  
ATOM    902  N   ASN I  35     121.303 120.270 101.461  1.00112.07           N  
ATOM    903  CA  ASN I  35     120.235 119.685 100.668  1.00112.07           C  
ATOM    904  C   ASN I  35     118.895 120.174 101.191  1.00112.07           C  
ATOM    905  O   ASN I  35     118.818 121.129 101.965  1.00112.07           O  
ATOM    906  CB  ASN I  35     120.312 118.166 100.704  1.00112.07           C  
ATOM    907  CG  ASN I  35     121.560 117.652 100.075  1.00112.07           C  
ATOM    908  OD1 ASN I  35     122.537 117.365 100.761  1.00112.07           O  
ATOM    909  ND2 ASN I  35     121.549 117.530  98.758  1.00112.07           N  
ATOM    910  N   THR I  36     117.840 119.496 100.768  1.00101.36           N  
ATOM    911  CA  THR I  36     116.495 119.806 101.204  1.00101.36           C  
ATOM    912  C   THR I  36     115.546 118.790 100.624  1.00101.36           C  
ATOM    913  O   THR I  36     115.658 118.426  99.465  1.00101.36           O  
ATOM    914  CB  THR I  36     116.067 121.205 100.772  1.00101.36           C  
ATOM    915  OG1 THR I  36     116.740 122.169 101.587  1.00101.36           O  
ATOM    916  CG2 THR I  36     114.573 121.382 100.925  1.00101.36           C  
HETATM  917  N   TYC I  37     114.613 118.319 101.433  1.00 91.51           N  
HETATM  918  CA  TYC I  37     113.635 117.352 100.946  1.00 91.51           C  
HETATM  919  C   TYC I  37     112.275 117.875 101.243  1.00 91.51           C  
HETATM  920  O   TYC I  37     111.438 117.120 101.695  1.00 91.51           O  
HETATM  921  CB  TYC I  37     113.862 116.006 101.600  1.00 91.51           C  
HETATM  922  CG  TYC I  37     115.223 115.504 101.193  1.00 91.51           C  
HETATM  923  CD1 TYC I  37     116.336 115.811 101.950  1.00 91.51           C  
HETATM  924  CD2 TYC I  37     115.362 114.726 100.064  1.00 91.51           C  
HETATM  925  CE1 TYC I  37     117.586 115.347 101.579  1.00 91.51           C  
HETATM  926  CE2 TYC I  37     116.610 114.263  99.693  1.00 91.51           C  
HETATM  927  OH  TYC I  37     118.945 114.112 100.084  1.00 91.51           O  
HETATM  928  CZ  TYC I  37     117.722 114.569 100.449  1.00 91.51           C  
HETATM  929  NXT TYC I  37     112.026 119.156 101.000  1.00 91.51           N  
TER     930      TYC I  37                                                      
ATOM    931  N   ALA K  13     131.919 105.769  95.630  1.00117.90           N  
ATOM    932  CA  ALA K  13     130.501 105.595  95.917  1.00117.90           C  
ATOM    933  C   ALA K  13     129.909 104.478  95.068  1.00117.90           C  
ATOM    934  O   ALA K  13     129.849 104.582  93.845  1.00117.90           O  
ATOM    935  CB  ALA K  13     129.758 106.889  95.685  1.00117.90           C  
ATOM    936  N   ASN K  14     129.473 103.409  95.724  1.00117.17           N  
ATOM    937  CA  ASN K  14     128.948 102.234  95.046  1.00117.17           C  
ATOM    938  C   ASN K  14     127.432 102.219  95.152  1.00117.17           C  
ATOM    939  O   ASN K  14     126.890 102.182  96.257  1.00117.17           O  
ATOM    940  CB  ASN K  14     129.525 100.958  95.656  1.00117.17           C  
ATOM    941  CG  ASN K  14     131.038 100.958  95.678  1.00117.17           C  
ATOM    942  OD1 ASN K  14     131.681 101.534  94.803  1.00117.17           O  
ATOM    943  ND2 ASN K  14     131.617 100.308  96.680  1.00117.17           N  
ATOM    944  N   PHE K  15     126.754 102.233  94.007  1.00111.10           N  
ATOM    945  CA  PHE K  15     125.294 102.280  93.966  1.00111.10           C  
ATOM    946  C   PHE K  15     124.804 101.165  93.059  1.00111.10           C  
ATOM    947  O   PHE K  15     125.078 101.179  91.857  1.00111.10           O  
ATOM    948  CB  PHE K  15     124.786 103.622  93.449  1.00111.10           C  
ATOM    949  CG  PHE K  15     124.946 104.748  94.406  1.00111.10           C  
ATOM    950  CD1 PHE K  15     126.191 105.153  94.823  1.00111.10           C  
ATOM    951  CD2 PHE K  15     123.850 105.430  94.856  1.00111.10           C  
ATOM    952  CE1 PHE K  15     126.328 106.195  95.690  1.00111.10           C  
ATOM    953  CE2 PHE K  15     123.982 106.471  95.715  1.00111.10           C  
ATOM    954  CZ  PHE K  15     125.223 106.852  96.139  1.00111.10           C  
ATOM    955  N   LEU K  16     124.072 100.214  93.620  1.00106.97           N  
ATOM    956  CA  LEU K  16     123.388  99.208  92.827  1.00106.97           C  
ATOM    957  C   LEU K  16     121.967  99.088  93.341  1.00106.97           C  
ATOM    958  O   LEU K  16     121.751  98.974  94.550  1.00106.97           O  
ATOM    959  CB  LEU K  16     124.096  97.856  92.894  1.00106.97           C  
ATOM    960  CG  LEU K  16     123.658  96.848  91.829  1.00106.97           C  
ATOM    961  CD1 LEU K  16     124.816  95.941  91.472  1.00106.97           C  
ATOM    962  CD2 LEU K  16     122.457  96.018  92.265  1.00106.97           C  
ATOM    963  N   VAL K  17     121.005  99.110  92.429  1.00 97.65           N  
ATOM    964  CA  VAL K  17     119.599  99.003  92.781  1.00 97.65           C  
ATOM    965  C   VAL K  17     118.983  97.927  91.912  1.00 97.65           C  
ATOM    966  O   VAL K  17     119.119  97.963  90.686  1.00 97.65           O  
ATOM    967  CB  VAL K  17     118.856 100.329  92.595  1.00 97.65           C  
ATOM    968  CG1 VAL K  17     117.380 100.109  92.767  1.00 97.65           C  
ATOM    969  CG2 VAL K  17     119.361 101.352  93.583  1.00 97.65           C  
ATOM    970  N   HIS K  18     118.309  96.972  92.540  1.00 99.09           N  
ATOM    971  CA  HIS K  18     117.696  95.849  91.843  1.00 99.09           C  
ATOM    972  C   HIS K  18     116.264  95.756  92.354  1.00 99.09           C  
ATOM    973  O   HIS K  18     115.981  95.017  93.297  1.00 99.09           O  
ATOM    974  CB  HIS K  18     118.497  94.580  92.088  1.00 99.09           C  
ATOM    975  CG  HIS K  18     117.794  93.323  91.688  1.00 99.09           C  
ATOM    976  ND1 HIS K  18     118.192  92.083  92.130  1.00 99.09           N  
ATOM    977  CD2 HIS K  18     116.724  93.113  90.887  1.00 99.09           C  
ATOM    978  CE1 HIS K  18     117.393  91.160  91.625  1.00 99.09           C  
ATOM    979  NE2 HIS K  18     116.494  91.759  90.867  1.00 99.09           N  
ATOM    980  N   SER K  19     115.366  96.506  91.731  1.00 95.77           N  
ATOM    981  CA  SER K  19     113.979  96.553  92.161  1.00 95.77           C  
ATOM    982  C   SER K  19     113.141  95.544  91.396  1.00 95.77           C  
ATOM    983  O   SER K  19     113.556  95.008  90.371  1.00 95.77           O  
ATOM    984  CB  SER K  19     113.398  97.944  91.961  1.00 95.77           C  
ATOM    985  OG  SER K  19     111.986  97.883  91.973  1.00 95.77           O  
ATOM    986  N   SER K  20     111.944  95.281  91.916  1.00 98.19           N  
ATOM    987  CA  SER K  20     111.000  94.407  91.232  1.00 98.19           C  
ATOM    988  C   SER K  20     109.721  95.133  90.845  1.00 98.19           C  
ATOM    989  O   SER K  20     109.376  95.165  89.661  1.00 98.19           O  
ATOM    990  CB  SER K  20     110.671  93.198  92.106  1.00 98.19           C  
ATOM    991  OG  SER K  20     109.602  93.505  92.977  1.00 98.19           O  
ATOM    992  N   ASN K  21     109.005  95.717  91.803  1.00 99.47           N  
ATOM    993  CA  ASN K  21     107.786  96.480  91.541  1.00 99.47           C  
ATOM    994  C   ASN K  21     107.927  97.768  92.327  1.00 99.47           C  
ATOM    995  O   ASN K  21     107.483  97.853  93.472  1.00 99.47           O  
ATOM    996  CB  ASN K  21     106.546  95.728  91.954  1.00 99.47           C  
ATOM    997  CG  ASN K  21     106.505  94.338  91.406  1.00 99.47           C  
ATOM    998  OD1 ASN K  21     106.904  94.094  90.271  1.00 99.47           O  
ATOM    999  ND2 ASN K  21     106.012  93.406  92.208  1.00 99.47           N  
ATOM   1000  N   ASN K  22     108.527  98.777  91.713  1.00 94.35           N  
ATOM   1001  CA  ASN K  22     108.981  99.918  92.490  1.00 94.35           C  
ATOM   1002  C   ASN K  22     107.816 100.760  92.991  1.00 94.35           C  
ATOM   1003  O   ASN K  22     107.711 101.032  94.191  1.00 94.35           O  
ATOM   1004  CB  ASN K  22     109.940 100.756  91.666  1.00 94.35           C  
ATOM   1005  CG  ASN K  22     110.467 101.914  92.432  1.00 94.35           C  
ATOM   1006  OD1 ASN K  22     110.466 101.910  93.654  1.00 94.35           O  
ATOM   1007  ND2 ASN K  22     110.915 102.931  91.726  1.00 94.35           N  
ATOM   1008  N   PHE K  23     106.956 101.220  92.081  1.00 98.41           N  
ATOM   1009  CA  PHE K  23     105.800 102.057  92.398  1.00 98.41           C  
ATOM   1010  C   PHE K  23     106.153 103.462  92.854  1.00 98.41           C  
ATOM   1011  O   PHE K  23     105.256 104.255  93.138  1.00 98.41           O  
ATOM   1012  CB  PHE K  23     104.976 101.494  93.553  1.00 98.41           C  
ATOM   1013  CG  PHE K  23     103.942 100.521  93.151  1.00 98.41           C  
ATOM   1014  CD1 PHE K  23     102.954 100.882  92.277  1.00 98.41           C  
ATOM   1015  CD2 PHE K  23     103.907  99.269  93.713  1.00 98.41           C  
ATOM   1016  CE1 PHE K  23     101.986  99.993  91.929  1.00 98.41           C  
ATOM   1017  CE2 PHE K  23     102.936  98.380  93.372  1.00 98.41           C  
ATOM   1018  CZ  PHE K  23     101.975  98.741  92.480  1.00 98.41           C  
ATOM   1019  N   GLY K  24     107.432 103.793  92.931  1.00 92.01           N  
ATOM   1020  CA  GLY K  24     107.780 105.022  93.602  1.00 92.01           C  
ATOM   1021  C   GLY K  24     109.232 105.383  93.423  1.00 92.01           C  
ATOM   1022  O   GLY K  24     109.986 104.696  92.739  1.00 92.01           O  
ATOM   1023  N   ALA K  25     109.616 106.477  94.060  1.00 90.04           N  
ATOM   1024  CA  ALA K  25     110.930 107.050  93.827  1.00 90.04           C  
ATOM   1025  C   ALA K  25     112.006 106.170  94.433  1.00 90.04           C  
ATOM   1026  O   ALA K  25     112.018 105.942  95.643  1.00 90.04           O  
ATOM   1027  CB  ALA K  25     111.000 108.452  94.418  1.00 90.04           C  
ATOM   1028  N   ILE K  26     112.899 105.663  93.598  1.00 85.89           N  
ATOM   1029  CA  ILE K  26     114.175 105.136  94.058  1.00 85.89           C  
ATOM   1030  C   ILE K  26     115.170 106.251  93.781  1.00 85.89           C  
ATOM   1031  O   ILE K  26     115.836 106.279  92.752  1.00 85.89           O  
ATOM   1032  CB  ILE K  26     114.550 103.841  93.355  1.00 85.89           C  
ATOM   1033  CG1 ILE K  26     113.499 102.781  93.621  1.00 85.89           C  
ATOM   1034  CG2 ILE K  26     115.885 103.352  93.840  1.00 85.89           C  
ATOM   1035  CD1 ILE K  26     113.814 101.461  92.984  1.00 85.89           C  
ATOM   1036  N   LEU K  27     115.286 107.177  94.717  1.00 87.88           N  
ATOM   1037  CA  LEU K  27     116.023 108.401  94.438  1.00 87.88           C  
ATOM   1038  C   LEU K  27     117.498 108.219  94.754  1.00 87.88           C  
ATOM   1039  O   LEU K  27     118.085 108.930  95.555  1.00 87.88           O  
ATOM   1040  CB  LEU K  27     115.420 109.551  95.228  1.00 87.88           C  
ATOM   1041  CG  LEU K  27     115.650 110.979  94.740  1.00 87.88           C  
ATOM   1042  CD1 LEU K  27     114.474 111.806  95.187  1.00 87.88           C  
ATOM   1043  CD2 LEU K  27     116.942 111.609  95.225  1.00 87.88           C  
ATOM   1044  N   SER K  28     118.110 107.230  94.131  1.00 93.94           N  
ATOM   1045  CA  SER K  28     119.509 106.947  94.400  1.00 93.94           C  
ATOM   1046  C   SER K  28     120.358 108.055  93.795  1.00 93.94           C  
ATOM   1047  O   SER K  28     120.423 108.190  92.572  1.00 93.94           O  
ATOM   1048  CB  SER K  28     119.869 105.585  93.826  1.00 93.94           C  
ATOM   1049  OG  SER K  28     121.089 105.123  94.352  1.00 93.94           O  
ATOM   1050  N   SER K  29     121.009 108.859  94.632  1.00102.54           N  
ATOM   1051  CA  SER K  29     121.674 110.054  94.133  1.00102.54           C  
ATOM   1052  C   SER K  29     122.922 110.343  94.948  1.00102.54           C  
ATOM   1053  O   SER K  29     123.253 109.627  95.893  1.00102.54           O  
ATOM   1054  CB  SER K  29     120.746 111.262  94.177  1.00102.54           C  
ATOM   1055  OG  SER K  29     120.398 111.574  95.510  1.00102.54           O  
ATOM   1056  N   THR K  30     123.617 111.415  94.562  1.00113.63           N  
ATOM   1057  CA  THR K  30     124.809 111.889  95.258  1.00113.63           C  
ATOM   1058  C   THR K  30     125.136 113.285  94.754  1.00113.63           C  
ATOM   1059  O   THR K  30     124.965 113.565  93.566  1.00113.63           O  
ATOM   1060  CB  THR K  30     126.011 110.968  95.036  1.00113.63           C  
ATOM   1061  OG1 THR K  30     125.657 109.626  95.370  1.00113.63           O  
ATOM   1062  CG2 THR K  30     127.178 111.393  95.910  1.00113.63           C  
ATOM   1063  N   ASN K  31     125.624 114.145  95.646  1.00112.74           N  
ATOM   1064  CA  ASN K  31     125.835 115.542  95.294  1.00112.74           C  
ATOM   1065  C   ASN K  31     126.679 116.286  96.312  1.00112.74           C  
ATOM   1066  O   ASN K  31     126.695 115.935  97.490  1.00112.74           O  
ATOM   1067  CB  ASN K  31     124.495 116.243  95.155  1.00112.74           C  
ATOM   1068  CG  ASN K  31     123.571 115.900  96.266  1.00112.74           C  
ATOM   1069  OD1 ASN K  31     123.971 115.266  97.228  1.00112.74           O  
ATOM   1070  ND2 ASN K  31     122.318 116.282  96.137  1.00112.74           N  
ATOM   1071  N   VAL K  32     127.399 117.309  95.861  1.00114.84           N  
ATOM   1072  CA  VAL K  32     128.068 118.198  96.801  1.00114.84           C  
ATOM   1073  C   VAL K  32     127.178 119.379  97.160  1.00114.84           C  
ATOM   1074  O   VAL K  32     126.864 119.599  98.332  1.00114.84           O  
ATOM   1075  CB  VAL K  32     129.432 118.642  96.242  1.00114.84           C  
ATOM   1076  CG1 VAL K  32     130.064 119.644  97.144  1.00114.84           C  
ATOM   1077  CG2 VAL K  32     130.355 117.448  96.132  1.00114.84           C  
ATOM   1078  N   GLY K  33     126.741 120.139  96.171  1.00117.06           N  
ATOM   1079  CA  GLY K  33     126.056 121.379  96.452  1.00117.06           C  
ATOM   1080  C   GLY K  33     124.624 121.189  96.896  1.00117.06           C  
ATOM   1081  O   GLY K  33     124.218 120.137  97.383  1.00117.06           O  
ATOM   1082  N   SER K  34     123.848 122.253  96.717  1.00121.82           N  
ATOM   1083  CA  SER K  34     122.472 122.266  97.181  1.00121.82           C  
ATOM   1084  C   SER K  34     121.566 121.533  96.206  1.00121.82           C  
ATOM   1085  O   SER K  34     121.924 121.311  95.048  1.00121.82           O  
ATOM   1086  CB  SER K  34     121.985 123.699  97.340  1.00121.82           C  
ATOM   1087  OG  SER K  34     121.498 124.184  96.103  1.00121.82           O  
ATOM   1088  N   ASN K  35     120.382 121.176  96.681  1.00114.47           N  
ATOM   1089  CA  ASN K  35     119.352 120.526  95.888  1.00114.47           C  
ATOM   1090  C   ASN K  35     117.985 120.925  96.415  1.00114.47           C  
ATOM   1091  O   ASN K  35     117.847 121.870  97.192  1.00114.47           O  
ATOM   1092  CB  ASN K  35     119.528 119.015  95.917  1.00114.47           C  
ATOM   1093  CG  ASN K  35     120.806 118.585  95.285  1.00114.47           C  
ATOM   1094  OD1 ASN K  35     121.801 118.360  95.968  1.00114.47           O  
ATOM   1095  ND2 ASN K  35     120.800 118.469  93.967  1.00114.47           N  
ATOM   1096  N   THR K  36     116.975 120.181  95.991  1.00102.64           N  
ATOM   1097  CA  THR K  36     115.613 120.401  96.430  1.00102.64           C  
ATOM   1098  C   THR K  36     114.731 119.327  95.848  1.00102.64           C  
ATOM   1099  O   THR K  36     114.865 118.976  94.687  1.00102.64           O  
ATOM   1100  CB  THR K  36     115.095 121.771  96.005  1.00102.64           C  
ATOM   1101  OG1 THR K  36     115.705 122.774  96.822  1.00102.64           O  
ATOM   1102  CG2 THR K  36     113.592 121.850  96.161  1.00102.64           C  
HETATM 1103  N   TYC K  37     113.833 118.794  96.656  1.00 96.06           N  
HETATM 1104  CA  TYC K  37     112.919 117.767  96.167  1.00 96.06           C  
HETATM 1105  C   TYC K  37     111.528 118.199  96.469  1.00 96.06           C  
HETATM 1106  O   TYC K  37     110.744 117.389  96.919  1.00 96.06           O  
HETATM 1107  CB  TYC K  37     113.235 116.436  96.815  1.00 96.06           C  
HETATM 1108  CG  TYC K  37     114.624 116.025  96.404  1.00 96.06           C  
HETATM 1109  CD1 TYC K  37     115.716 116.401  97.160  1.00 96.06           C  
HETATM 1110  CD2 TYC K  37     114.811 115.263  95.272  1.00 96.06           C  
HETATM 1111  CE1 TYC K  37     116.993 116.021  96.785  1.00 96.06           C  
HETATM 1112  CE2 TYC K  37     116.086 114.883  94.897  1.00 96.06           C  
HETATM 1113  OH  TYC K  37     118.427 114.883  95.283  1.00 96.06           O  
HETATM 1114  CZ  TYC K  37     117.177 115.258  95.652  1.00 96.06           C  
HETATM 1115  NXT TYC K  37     111.196 119.462  96.231  1.00 96.06           N  
TER    1116      TYC K  37                                                      
ATOM   1117  N   ALA B  13      82.823 115.649 122.379  1.00101.36           N  
ATOM   1118  CA  ALA B  13      84.219 115.339 122.661  1.00101.36           C  
ATOM   1119  C   ALA B  13      85.147 116.201 121.816  1.00101.36           C  
ATOM   1120  O   ALA B  13      85.166 116.093 120.591  1.00101.36           O  
ATOM   1121  CB  ALA B  13      84.489 113.873 122.419  1.00101.36           C  
ATOM   1122  N   ASN B  14      85.915 117.060 122.475  1.00106.70           N  
ATOM   1123  CA  ASN B  14      86.800 117.999 121.802  1.00106.70           C  
ATOM   1124  C   ASN B  14      88.235 117.508 121.902  1.00106.70           C  
ATOM   1125  O   ASN B  14      88.760 117.355 123.005  1.00106.70           O  
ATOM   1126  CB  ASN B  14      86.681 119.390 122.421  1.00106.70           C  
ATOM   1127  CG  ASN B  14      85.254 119.893 122.451  1.00106.70           C  
ATOM   1128  OD1 ASN B  14      84.454 119.570 121.575  1.00106.70           O  
ATOM   1129  ND2 ASN B  14      84.927 120.691 123.459  1.00106.70           N  
ATOM   1130  N   PHE B  15      88.867 117.277 120.754  1.00 99.69           N  
ATOM   1131  CA  PHE B  15      90.228 116.748 120.707  1.00 99.69           C  
ATOM   1132  C   PHE B  15      91.059 117.643 119.804  1.00 99.69           C  
ATOM   1133  O   PHE B  15      90.793 117.729 118.603  1.00 99.69           O  
ATOM   1134  CB  PHE B  15      90.259 115.317 120.179  1.00 99.69           C  
ATOM   1135  CG  PHE B  15      89.737 114.301 121.131  1.00 99.69           C  
ATOM   1136  CD1 PHE B  15      88.429 114.331 121.551  1.00 99.69           C  
ATOM   1137  CD2 PHE B  15      90.544 113.290 121.572  1.00 99.69           C  
ATOM   1138  CE1 PHE B  15      87.954 113.388 122.413  1.00 99.69           C  
ATOM   1139  CE2 PHE B  15      90.075 112.347 122.426  1.00 99.69           C  
ATOM   1140  CZ  PHE B  15      88.779 112.398 122.853  1.00 99.69           C  
ATOM   1141  N   LEU B  16      92.067 118.292 120.368  1.00 90.71           N  
ATOM   1142  CA  LEU B  16      93.044 119.019 119.576  1.00 90.71           C  
ATOM   1143  C   LEU B  16      94.426 118.657 120.085  1.00 90.71           C  
ATOM   1144  O   LEU B  16      94.670 118.683 121.295  1.00 90.71           O  
ATOM   1145  CB  LEU B  16      92.827 120.528 119.655  1.00 90.71           C  
ATOM   1146  CG  LEU B  16      93.572 121.342 118.593  1.00 90.71           C  
ATOM   1147  CD1 LEU B  16      92.781 122.584 118.247  1.00 90.71           C  
ATOM   1148  CD2 LEU B  16      94.983 121.721 119.029  1.00 90.71           C  
ATOM   1149  N   VAL B  17      95.324 118.321 119.169  1.00 80.55           N  
ATOM   1150  CA  VAL B  17      96.686 117.952 119.515  1.00 80.55           C  
ATOM   1151  C   VAL B  17      97.623 118.769 118.651  1.00 80.55           C  
ATOM   1152  O   VAL B  17      97.481 118.788 117.425  1.00 80.55           O  
ATOM   1153  CB  VAL B  17      96.946 116.456 119.320  1.00 80.55           C  
ATOM   1154  CG1 VAL B  17      98.412 116.171 119.487  1.00 80.55           C  
ATOM   1155  CG2 VAL B  17      96.131 115.652 120.303  1.00 80.55           C  
ATOM   1156  N   HIS B  18      98.577 119.440 119.281  1.00 84.94           N  
ATOM   1157  CA  HIS B  18      99.528 120.300 118.588  1.00 84.94           C  
ATOM   1158  C   HIS B  18     100.910 119.909 119.093  1.00 84.94           C  
ATOM   1159  O   HIS B  18     101.425 120.504 120.039  1.00 84.94           O  
ATOM   1160  CB  HIS B  18      99.195 121.762 118.844  1.00 84.94           C  
ATOM   1161  CG  HIS B  18     100.275 122.716 118.448  1.00 84.94           C  
ATOM   1162  ND1 HIS B  18     100.312 124.015 118.899  1.00 84.94           N  
ATOM   1163  CD2 HIS B  18     101.353 122.564 117.644  1.00 84.94           C  
ATOM   1164  CE1 HIS B  18     101.372 124.623 118.395  1.00 84.94           C  
ATOM   1165  NE2 HIS B  18     102.019 123.764 117.631  1.00 84.94           N  
ATOM   1166  N   SER B  19     101.506 118.906 118.463  1.00 80.92           N  
ATOM   1167  CA  SER B  19     102.800 118.399 118.886  1.00 80.92           C  
ATOM   1168  C   SER B  19     103.924 119.076 118.124  1.00 80.92           C  
ATOM   1169  O   SER B  19     103.709 119.727 117.104  1.00 80.92           O  
ATOM   1170  CB  SER B  19     102.885 116.895 118.676  1.00 80.92           C  
ATOM   1171  OG  SER B  19     104.236 116.483 118.683  1.00 80.92           O  
ATOM   1172  N   SER B  20     105.142 118.923 118.640  1.00 88.60           N  
ATOM   1173  CA  SER B  20     106.321 119.438 117.957  1.00 88.60           C  
ATOM   1174  C   SER B  20     107.285 118.330 117.560  1.00 88.60           C  
ATOM   1175  O   SER B  20     107.597 118.194 116.375  1.00 88.60           O  
ATOM   1176  CB  SER B  20     107.035 120.464 118.836  1.00 88.60           C  
ATOM   1177  OG  SER B  20     107.942 119.812 119.701  1.00 88.60           O  
ATOM   1178  N   ASN B  21     107.768 117.535 118.512  1.00 90.06           N  
ATOM   1179  CA  ASN B  21     108.664 116.412 118.241  1.00 90.06           C  
ATOM   1180  C   ASN B  21     108.103 115.239 119.021  1.00 90.06           C  
ATOM   1181  O   ASN B  21     108.496 115.003 120.162  1.00 90.06           O  
ATOM   1182  CB  ASN B  21     110.083 116.706 118.653  1.00 90.06           C  
ATOM   1183  CG  ASN B  21     110.583 118.007 118.112  1.00 90.06           C  
ATOM   1184  OD1 ASN B  21     110.286 118.378 116.980  1.00 90.06           O  
ATOM   1185  ND2 ASN B  21     111.360 118.716 118.918  1.00 90.06           N  
ATOM   1186  N   ASN B  22     107.201 114.491 118.402  1.00 87.13           N  
ATOM   1187  CA  ASN B  22     106.395 113.561 119.175  1.00 87.13           C  
ATOM   1188  C   ASN B  22     107.214 112.376 119.667  1.00 87.13           C  
ATOM   1189  O   ASN B  22     107.226 112.077 120.864  1.00 87.13           O  
ATOM   1190  CB  ASN B  22     105.211 113.095 118.351  1.00 87.13           C  
ATOM   1191  CG  ASN B  22     104.330 112.173 119.112  1.00 87.13           C  
ATOM   1192  OD1 ASN B  22     104.335 112.168 120.334  1.00 87.13           O  
ATOM   1193  ND2 ASN B  22     103.568 111.368 118.402  1.00 87.13           N  
ATOM   1194  N   PHE B  23     107.871 111.663 118.751  1.00 87.81           N  
ATOM   1195  CA  PHE B  23     108.684 110.487 119.058  1.00 87.81           C  
ATOM   1196  C   PHE B  23     107.884 109.277 119.507  1.00 87.81           C  
ATOM   1197  O   PHE B  23     108.468 108.227 119.783  1.00 87.81           O  
ATOM   1198  CB  PHE B  23     109.650 110.735 120.213  1.00 87.81           C  
ATOM   1199  CG  PHE B  23     110.948 111.311 119.811  1.00 87.81           C  
ATOM   1200  CD1 PHE B  23     111.758 110.649 118.932  1.00 87.81           C  
ATOM   1201  CD2 PHE B  23     111.398 112.478 120.380  1.00 87.81           C  
ATOM   1202  CE1 PHE B  23     112.965 111.169 118.585  1.00 87.81           C  
ATOM   1203  CE2 PHE B  23     112.610 112.995 120.040  1.00 87.81           C  
ATOM   1204  CZ  PHE B  23     113.394 112.342 119.142  1.00 87.81           C  
ATOM   1205  N   GLY B  24     106.568 109.388 119.587  1.00 87.00           N  
ATOM   1206  CA  GLY B  24     105.833 108.340 120.253  1.00 87.00           C  
ATOM   1207  C   GLY B  24     104.343 108.484 120.078  1.00 87.00           C  
ATOM   1208  O   GLY B  24     103.859 109.388 119.401  1.00 87.00           O  
ATOM   1209  N   ALA B  25     103.618 107.575 120.710  1.00 84.51           N  
ATOM   1210  CA  ALA B  25     102.189 107.474 120.481  1.00 84.51           C  
ATOM   1211  C   ALA B  25     101.467 108.658 121.095  1.00 84.51           C  
ATOM   1212  O   ALA B  25     101.534 108.868 122.307  1.00 84.51           O  
ATOM   1213  CB  ALA B  25     101.657 106.171 121.063  1.00 84.51           C  
ATOM   1214  N   ILE B  26     100.792 109.439 120.266  1.00 79.61           N  
ATOM   1215  CA  ILE B  26      99.764 110.356 120.735  1.00 79.61           C  
ATOM   1216  C   ILE B  26      98.455 109.637 120.456  1.00 79.61           C  
ATOM   1217  O   ILE B  26      97.815 109.839 119.431  1.00 79.61           O  
ATOM   1218  CB  ILE B  26      99.840 111.707 120.041  1.00 79.61           C  
ATOM   1219  CG1 ILE B  26     101.184 112.356 120.309  1.00 79.61           C  
ATOM   1220  CG2 ILE B  26      98.744 112.609 120.534  1.00 79.61           C  
ATOM   1221  CD1 ILE B  26     101.325 113.710 119.681  1.00 79.61           C  
ATOM   1222  N   LEU B  27      98.040 108.796 121.388  1.00 90.33           N  
ATOM   1223  CA  LEU B  27      96.937 107.890 121.105  1.00 90.33           C  
ATOM   1224  C   LEU B  27      95.607 108.549 121.428  1.00 90.33           C  
ATOM   1225  O   LEU B  27      94.819 108.068 122.227  1.00 90.33           O  
ATOM   1226  CB  LEU B  27      97.124 106.598 121.886  1.00 90.33           C  
ATOM   1227  CG  LEU B  27      96.431 105.331 121.390  1.00 90.33           C  
ATOM   1228  CD1 LEU B  27      97.267 104.158 121.827  1.00 90.33           C  
ATOM   1229  CD2 LEU B  27      95.006 105.165 121.877  1.00 90.33           C  
ATOM   1230  N   SER B  28      95.357 109.690 120.812  1.00 87.32           N  
ATOM   1231  CA  SER B  28      94.132 110.420 121.090  1.00 87.32           C  
ATOM   1232  C   SER B  28      92.962 109.661 120.481  1.00 87.32           C  
ATOM   1233  O   SER B  28      92.853 109.565 119.258  1.00 87.32           O  
ATOM   1234  CB  SER B  28      94.245 111.828 120.525  1.00 87.32           C  
ATOM   1235  OG  SER B  28      93.249 112.666 121.058  1.00 87.32           O  
ATOM   1236  N   SER B  29      92.083 109.113 121.317  1.00102.22           N  
ATOM   1237  CA  SER B  29      91.058 108.212 120.814  1.00102.22           C  
ATOM   1238  C   SER B  29      89.785 108.348 121.633  1.00102.22           C  
ATOM   1239  O   SER B  29      89.713 109.127 122.583  1.00102.22           O  
ATOM   1240  CB  SER B  29      91.531 106.763 120.847  1.00102.22           C  
ATOM   1241  OG  SER B  29      91.757 106.343 122.176  1.00102.22           O  
ATOM   1242  N   THR B  30      88.773 107.571 121.243  1.00116.75           N  
ATOM   1243  CA  THR B  30      87.492 107.516 121.942  1.00116.75           C  
ATOM   1244  C   THR B  30      86.719 106.312 121.431  1.00116.75           C  
ATOM   1245  O   THR B  30      86.785 105.998 120.241  1.00116.75           O  
ATOM   1246  CB  THR B  30      86.665 108.784 121.729  1.00116.75           C  
ATOM   1247  OG1 THR B  30      87.446 109.931 122.070  1.00116.75           O  
ATOM   1248  CG2 THR B  30      85.425 108.767 122.606  1.00116.75           C  
ATOM   1249  N   ASN B  31      85.974 105.657 122.320  1.00122.88           N  
ATOM   1250  CA  ASN B  31      85.310 104.411 121.962  1.00122.88           C  
ATOM   1251  C   ASN B  31      84.270 103.983 122.979  1.00122.88           C  
ATOM   1252  O   ASN B  31      84.374 104.312 124.159  1.00122.88           O  
ATOM   1253  CB  ASN B  31      86.341 103.306 121.812  1.00122.88           C  
ATOM   1254  CG  ASN B  31      87.329 103.314 122.922  1.00122.88           C  
ATOM   1255  OD1 ASN B  31      87.164 104.040 123.889  1.00122.88           O  
ATOM   1256  ND2 ASN B  31      88.383 102.538 122.785  1.00122.88           N  
ATOM   1257  N   VAL B  32      83.249 103.262 122.525  1.00124.47           N  
ATOM   1258  CA  VAL B  32      82.324 102.639 123.463  1.00124.47           C  
ATOM   1259  C   VAL B  32      82.771 101.227 123.810  1.00124.47           C  
ATOM   1260  O   VAL B  32      82.997 100.906 124.980  1.00124.47           O  
ATOM   1261  CB  VAL B  32      80.889 102.678 122.907  1.00124.47           C  
ATOM   1262  CG1 VAL B  32      79.961 101.937 123.806  1.00124.47           C  
ATOM   1263  CG2 VAL B  32      80.416 104.113 122.809  1.00124.47           C  
ATOM   1264  N   GLY B  33      82.929 100.371 122.816  1.00125.27           N  
ATOM   1265  CA  GLY B  33      83.163  98.972 123.087  1.00125.27           C  
ATOM   1266  C   GLY B  33      84.578  98.671 123.525  1.00125.27           C  
ATOM   1267  O   GLY B  33      85.312  99.526 124.017  1.00125.27           O  
ATOM   1268  N   SER B  34      84.955  97.412 123.337  1.00121.43           N  
ATOM   1269  CA  SER B  34      86.250  96.939 123.795  1.00121.43           C  
ATOM   1270  C   SER B  34      87.346  97.335 122.821  1.00121.43           C  
ATOM   1271  O   SER B  34      87.080  97.672 121.666  1.00121.43           O  
ATOM   1272  CB  SER B  34      86.233  95.425 123.945  1.00121.43           C  
ATOM   1273  OG  SER B  34      86.528  94.814 122.703  1.00121.43           O  
ATOM   1274  N   ASN B  35      88.583  97.275 123.292  1.00110.71           N  
ATOM   1275  CA  ASN B  35      89.768  97.551 122.499  1.00110.71           C  
ATOM   1276  C   ASN B  35      90.927  96.717 123.019  1.00110.71           C  
ATOM   1277  O   ASN B  35      90.744  95.775 123.790  1.00110.71           O  
ATOM   1278  CB  ASN B  35      90.105  99.035 122.538  1.00110.71           C  
ATOM   1279  CG  ASN B  35      89.041  99.869 121.913  1.00110.71           C  
ATOM   1280  OD1 ASN B  35      88.179 100.408 122.601  1.00110.71           O  
ATOM   1281  ND2 ASN B  35      89.083  99.987 120.596  1.00110.71           N  
ATOM   1282  N   THR B  36      92.125  97.086 122.594  1.00 89.26           N  
ATOM   1283  CA  THR B  36      93.336  96.422 123.026  1.00 89.26           C  
ATOM   1284  C   THR B  36      94.524  97.146 122.447  1.00 89.26           C  
ATOM   1285  O   THR B  36      94.513  97.529 121.288  1.00 89.26           O  
ATOM   1286  CB  THR B  36      93.369  94.962 122.591  1.00 89.26           C  
ATOM   1287  OG1 THR B  36      92.462  94.212 123.405  1.00 89.26           O  
ATOM   1288  CG2 THR B  36      94.761  94.386 122.740  1.00 89.26           C  
HETATM 1289  N   TYC B  37      95.550  97.345 123.253  1.00 79.54           N  
HETATM 1290  CA  TYC B  37      96.753  98.013 122.767  1.00 79.54           C  
HETATM 1291  C   TYC B  37      97.921  97.141 123.060  1.00 79.54           C  
HETATM 1292  O   TYC B  37      98.932  97.640 123.511  1.00 79.54           O  
HETATM 1293  CB  TYC B  37      96.900  99.368 123.423  1.00 79.54           C  
HETATM 1294  CG  TYC B  37      95.725 100.220 123.021  1.00 79.54           C  
HETATM 1295  CD1 TYC B  37      94.571 100.224 123.780  1.00 79.54           C  
HETATM 1296  CD2 TYC B  37      95.800 101.009 121.893  1.00 79.54           C  
HETATM 1297  CE1 TYC B  37      93.493 101.010 123.412  1.00 79.54           C  
HETATM 1298  CE2 TYC B  37      94.723 101.794 121.526  1.00 79.54           C  
HETATM 1299  OH  TYC B  37      92.515 102.570 121.923  1.00 79.54           O  
HETATM 1300  CZ  TYC B  37      93.571 101.797 122.284  1.00 79.54           C  
HETATM 1301  NXT TYC B  37      97.814  95.841 122.814  1.00 79.54           N  
TER    1302      TYC B  37                                                      
ATOM   1303  N   ALA D  13      82.299 114.216 117.532  1.00100.80           N  
ATOM   1304  CA  ALA D  13      83.710 113.992 117.813  1.00100.80           C  
ATOM   1305  C   ALA D  13      84.586 114.906 116.966  1.00100.80           C  
ATOM   1306  O   ALA D  13      84.610 114.796 115.743  1.00100.80           O  
ATOM   1307  CB  ALA D  13      84.067 112.544 117.573  1.00100.80           C  
ATOM   1308  N   ASN D  14      85.302 115.809 117.624  1.00104.74           N  
ATOM   1309  CA  ASN D  14      86.128 116.798 116.949  1.00104.74           C  
ATOM   1310  C   ASN D  14      87.589 116.394 117.048  1.00104.74           C  
ATOM   1311  O   ASN D  14      88.125 116.275 118.151  1.00104.74           O  
ATOM   1312  CB  ASN D  14      85.928 118.181 117.567  1.00104.74           C  
ATOM   1313  CG  ASN D  14      84.472 118.597 117.596  1.00104.74           C  
ATOM   1314  OD1 ASN D  14      83.693 118.226 116.721  1.00104.74           O  
ATOM   1315  ND2 ASN D  14      84.099 119.377 118.604  1.00104.74           N  
ATOM   1316  N   PHE D  15      88.234 116.199 115.900  1.00 98.08           N  
ATOM   1317  CA  PHE D  15      89.624 115.753 115.853  1.00 98.08           C  
ATOM   1318  C   PHE D  15      90.400 116.693 114.949  1.00 98.08           C  
ATOM   1319  O   PHE D  15      90.128 116.762 113.748  1.00 98.08           O  
ATOM   1320  CB  PHE D  15      89.741 114.325 115.327  1.00 98.08           C  
ATOM   1321  CG  PHE D  15      89.280 113.281 116.281  1.00 98.08           C  
ATOM   1322  CD1 PHE D  15      87.973 113.234 116.702  1.00 98.08           C  
ATOM   1323  CD2 PHE D  15      90.146 112.321 116.722  1.00 98.08           C  
ATOM   1324  CE1 PHE D  15      87.556 112.265 117.565  1.00 98.08           C  
ATOM   1325  CE2 PHE D  15      89.735 111.352 117.578  1.00 98.08           C  
ATOM   1326  CZ  PHE D  15      88.438 111.326 118.005  1.00 98.08           C  
ATOM   1327  N   LEU D  16      91.367 117.402 115.510  1.00 84.59           N  
ATOM   1328  CA  LEU D  16      92.300 118.185 114.717  1.00 84.59           C  
ATOM   1329  C   LEU D  16      93.700 117.907 115.226  1.00 84.59           C  
ATOM   1330  O   LEU D  16      93.942 117.950 116.434  1.00 84.59           O  
ATOM   1331  CB  LEU D  16      91.993 119.680 114.794  1.00 84.59           C  
ATOM   1332  CG  LEU D  16      92.687 120.534 113.731  1.00 84.59           C  
ATOM   1333  CD1 LEU D  16      91.824 121.726 113.383  1.00 84.59           C  
ATOM   1334  CD2 LEU D  16      94.073 120.998 114.164  1.00 84.59           C  
ATOM   1335  N   VAL D  17      94.616 117.624 114.309  1.00 76.60           N  
ATOM   1336  CA  VAL D  17      95.997 117.337 114.655  1.00 76.60           C  
ATOM   1337  C   VAL D  17      96.884 118.207 113.788  1.00 76.60           C  
ATOM   1338  O   VAL D  17      96.740 118.217 112.563  1.00 76.60           O  
ATOM   1339  CB  VAL D  17      96.345 115.860 114.461  1.00 76.60           C  
ATOM   1340  CG1 VAL D  17      97.826 115.662 114.627  1.00 76.60           C  
ATOM   1341  CG2 VAL D  17      95.582 115.010 115.446  1.00 76.60           C  
ATOM   1342  N   HIS D  18      97.797 118.935 114.416  1.00 79.09           N  
ATOM   1343  CA  HIS D  18      98.694 119.849 113.722  1.00 79.09           C  
ATOM   1344  C   HIS D  18     100.098 119.542 114.226  1.00 79.09           C  
ATOM   1345  O   HIS D  18     100.577 120.168 115.171  1.00 79.09           O  
ATOM   1346  CB  HIS D  18      98.275 121.290 113.976  1.00 79.09           C  
ATOM   1347  CG  HIS D  18      99.296 122.305 113.578  1.00 79.09           C  
ATOM   1348  ND1 HIS D  18      99.256 123.605 114.027  1.00 79.09           N  
ATOM   1349  CD2 HIS D  18     100.380 122.217 112.773  1.00 79.09           C  
ATOM   1350  CE1 HIS D  18     100.277 124.274 113.522  1.00 79.09           C  
ATOM   1351  NE2 HIS D  18     100.974 123.455 112.758  1.00 79.09           N  
ATOM   1352  N   SER D  19     100.752 118.576 113.597  1.00 77.60           N  
ATOM   1353  CA  SER D  19     102.073 118.147 114.020  1.00 77.60           C  
ATOM   1354  C   SER D  19     103.155 118.889 113.255  1.00 77.60           C  
ATOM   1355  O   SER D  19     102.900 119.525 112.235  1.00 77.60           O  
ATOM   1356  CB  SER D  19     102.248 116.650 113.811  1.00 77.60           C  
ATOM   1357  OG  SER D  19     103.621 116.320 113.817  1.00 77.60           O  
ATOM   1358  N   SER D  20     104.379 118.809 113.771  1.00 84.07           N  
ATOM   1359  CA  SER D  20     105.527 119.392 113.086  1.00 84.07           C  
ATOM   1360  C   SER D  20     106.554 118.344 112.690  1.00 84.07           C  
ATOM   1361  O   SER D  20     106.873 118.224 111.505  1.00 84.07           O  
ATOM   1362  CB  SER D  20     106.178 120.460 113.964  1.00 84.07           C  
ATOM   1363  OG  SER D  20     107.123 119.865 114.829  1.00 84.07           O  
ATOM   1364  N   ASN D  21     107.084 117.580 113.643  1.00 86.11           N  
ATOM   1365  CA  ASN D  21     108.045 116.512 113.373  1.00 86.11           C  
ATOM   1366  C   ASN D  21     107.557 115.309 114.153  1.00 86.11           C  
ATOM   1367  O   ASN D  21     107.964 115.099 115.295  1.00 86.11           O  
ATOM   1368  CB  ASN D  21     109.445 116.891 113.783  1.00 86.11           C  
ATOM   1369  CG  ASN D  21     109.866 118.218 113.240  1.00 86.11           C  
ATOM   1370  OD1 ASN D  21     109.547 118.569 112.107  1.00 86.11           O  
ATOM   1371  ND2 ASN D  21     110.599 118.974 114.045  1.00 86.11           N  
ATOM   1372  N   ASN D  22     106.699 114.508 113.538  1.00 85.43           N  
ATOM   1373  CA  ASN D  22     105.951 113.533 114.312  1.00 85.43           C  
ATOM   1374  C   ASN D  22     106.840 112.399 114.804  1.00 85.43           C  
ATOM   1375  O   ASN D  22     106.869 112.103 116.002  1.00 85.43           O  
ATOM   1376  CB  ASN D  22     104.796 112.996 113.489  1.00 85.43           C  
ATOM   1377  CG  ASN D  22     103.972 112.023 114.253  1.00 85.43           C  
ATOM   1378  OD1 ASN D  22     103.978 112.020 115.475  1.00 85.43           O  
ATOM   1379  ND2 ASN D  22     103.259 111.173 113.545  1.00 85.43           N  
ATOM   1380  N   PHE D  23     107.537 111.725 113.889  1.00 87.29           N  
ATOM   1381  CA  PHE D  23     108.418 110.599 114.196  1.00 87.29           C  
ATOM   1382  C   PHE D  23     107.692 109.345 114.648  1.00 87.29           C  
ATOM   1383  O   PHE D  23     108.338 108.332 114.924  1.00 87.29           O  
ATOM   1384  CB  PHE D  23     109.370 110.907 115.350  1.00 87.29           C  
ATOM   1385  CG  PHE D  23     110.631 111.559 114.947  1.00 87.29           C  
ATOM   1386  CD1 PHE D  23     111.478 110.945 114.068  1.00 87.29           C  
ATOM   1387  CD2 PHE D  23     111.011 112.751 115.514  1.00 87.29           C  
ATOM   1388  CE1 PHE D  23     112.651 111.535 113.719  1.00 87.29           C  
ATOM   1389  CE2 PHE D  23     112.189 113.339 115.172  1.00 87.29           C  
ATOM   1390  CZ  PHE D  23     113.010 112.732 114.274  1.00 87.29           C  
ATOM   1391  N   GLY D  24     106.373 109.377 114.729  1.00 85.08           N  
ATOM   1392  CA  GLY D  24     105.702 108.288 115.397  1.00 85.08           C  
ATOM   1393  C   GLY D  24     104.206 108.343 115.223  1.00 85.08           C  
ATOM   1394  O   GLY D  24     103.668 109.215 114.545  1.00 85.08           O  
ATOM   1395  N   ALA D  25     103.537 107.394 115.858  1.00 80.95           N  
ATOM   1396  CA  ALA D  25     102.115 107.207 115.628  1.00 80.95           C  
ATOM   1397  C   ALA D  25     101.326 108.346 116.242  1.00 80.95           C  
ATOM   1398  O   ALA D  25     101.381 108.562 117.454  1.00 80.95           O  
ATOM   1399  CB  ALA D  25     101.662 105.875 116.214  1.00 80.95           C  
ATOM   1400  N   ILE D  26     100.604 109.085 115.413  1.00 75.89           N  
ATOM   1401  CA  ILE D  26      99.524 109.940 115.882  1.00 75.89           C  
ATOM   1402  C   ILE D  26      98.260 109.144 115.605  1.00 75.89           C  
ATOM   1403  O   ILE D  26      97.608 109.306 114.579  1.00 75.89           O  
ATOM   1404  CB  ILE D  26      99.518 111.292 115.186  1.00 75.89           C  
ATOM   1405  CG1 ILE D  26     100.822 112.019 115.451  1.00 75.89           C  
ATOM   1406  CG2 ILE D  26      98.372 112.128 115.679  1.00 75.89           C  
ATOM   1407  CD1 ILE D  26     100.882 113.379 114.822  1.00 75.89           C  
ATOM   1408  N   LEU D  27      97.896 108.282 116.537  1.00 80.60           N  
ATOM   1409  CA  LEU D  27      96.849 107.310 116.257  1.00 80.60           C  
ATOM   1410  C   LEU D  27      95.483 107.889 116.579  1.00 80.60           C  
ATOM   1411  O   LEU D  27      94.724 107.363 117.381  1.00 80.60           O  
ATOM   1412  CB  LEU D  27      97.114 106.034 117.039  1.00 80.60           C  
ATOM   1413  CG  LEU D  27      96.497 104.726 116.546  1.00 80.60           C  
ATOM   1414  CD1 LEU D  27      97.401 103.606 116.984  1.00 80.60           C  
ATOM   1415  CD2 LEU D  27      95.083 104.476 117.034  1.00 80.60           C  
ATOM   1416  N   SER D  28      95.165 109.013 115.963  1.00 80.82           N  
ATOM   1417  CA  SER D  28      93.898 109.668 116.241  1.00 80.82           C  
ATOM   1418  C   SER D  28      92.775 108.841 115.634  1.00 80.82           C  
ATOM   1419  O   SER D  28      92.672 108.736 114.411  1.00 80.82           O  
ATOM   1420  CB  SER D  28      93.927 111.080 115.674  1.00 80.82           C  
ATOM   1421  OG  SER D  28      92.884 111.858 116.207  1.00 80.82           O  
ATOM   1422  N   SER D  29      91.930 108.243 116.472  1.00 95.24           N  
ATOM   1423  CA  SER D  29      90.960 107.281 115.971  1.00 95.24           C  
ATOM   1424  C   SER D  29      89.684 107.342 116.790  1.00 95.24           C  
ATOM   1425  O   SER D  29      89.565 108.117 117.739  1.00 95.24           O  
ATOM   1426  CB  SER D  29      91.519 105.863 116.005  1.00 95.24           C  
ATOM   1427  OG  SER D  29      91.772 105.459 117.335  1.00 95.24           O  
ATOM   1428  N   THR D  30      88.719 106.506 116.402  1.00111.75           N  
ATOM   1429  CA  THR D  30      87.444 106.375 117.102  1.00111.75           C  
ATOM   1430  C   THR D  30      86.743 105.127 116.593  1.00111.75           C  
ATOM   1431  O   THR D  30      86.826 104.817 115.403  1.00111.75           O  
ATOM   1432  CB  THR D  30      86.543 107.593 116.888  1.00111.75           C  
ATOM   1433  OG1 THR D  30      87.254 108.783 117.227  1.00111.75           O  
ATOM   1434  CG2 THR D  30      85.306 107.502 117.767  1.00111.75           C  
ATOM   1435  N   ASN D  31      86.040 104.430 117.484  1.00116.35           N  
ATOM   1436  CA  ASN D  31      85.451 103.146 117.128  1.00116.35           C  
ATOM   1437  C   ASN D  31      84.438 102.658 118.145  1.00116.35           C  
ATOM   1438  O   ASN D  31      84.523 102.995 119.325  1.00116.35           O  
ATOM   1439  CB  ASN D  31      86.544 102.105 116.978  1.00116.35           C  
ATOM   1440  CG  ASN D  31      87.532 102.172 118.087  1.00116.35           C  
ATOM   1441  OD1 ASN D  31      87.325 102.888 119.054  1.00116.35           O  
ATOM   1442  ND2 ASN D  31      88.630 101.461 117.950  1.00116.35           N  
ATOM   1443  N   VAL D  32      83.463 101.877 117.694  1.00119.79           N  
ATOM   1444  CA  VAL D  32      82.576 101.202 118.633  1.00119.79           C  
ATOM   1445  C   VAL D  32      83.108  99.819 118.982  1.00119.79           C  
ATOM   1446  O   VAL D  32      83.352  99.514 120.153  1.00119.79           O  
ATOM   1447  CB  VAL D  32      81.142 101.154 118.079  1.00119.79           C  
ATOM   1448  CG1 VAL D  32      80.259 100.361 118.978  1.00119.79           C  
ATOM   1449  CG2 VAL D  32      80.583 102.557 117.976  1.00119.79           C  
ATOM   1450  N   GLY D  33      83.315  98.973 117.989  1.00119.76           N  
ATOM   1451  CA  GLY D  33      83.633  97.590 118.262  1.00119.76           C  
ATOM   1452  C   GLY D  33      85.062  97.376 118.699  1.00119.76           C  
ATOM   1453  O   GLY D  33      85.745  98.272 119.189  1.00119.76           O  
ATOM   1454  N   SER D  34      85.514  96.140 118.512  1.00117.00           N  
ATOM   1455  CA  SER D  34      86.836  95.747 118.970  1.00117.00           C  
ATOM   1456  C   SER D  34      87.904  96.205 117.994  1.00117.00           C  
ATOM   1457  O   SER D  34      87.619  96.525 116.839  1.00117.00           O  
ATOM   1458  CB  SER D  34      86.909  94.234 119.122  1.00117.00           C  
ATOM   1459  OG  SER D  34      87.239  93.639 117.879  1.00117.00           O  
ATOM   1460  N   ASN D  35      89.144  96.220 118.465  1.00106.04           N  
ATOM   1461  CA  ASN D  35      90.309  96.565 117.670  1.00106.04           C  
ATOM   1462  C   ASN D  35      91.516  95.802 118.189  1.00106.04           C  
ATOM   1463  O   ASN D  35      91.390  94.851 118.962  1.00106.04           O  
ATOM   1464  CB  ASN D  35      90.558  98.067 117.707  1.00106.04           C  
ATOM   1465  CG  ASN D  35      89.446  98.834 117.081  1.00106.04           C  
ATOM   1466  OD1 ASN D  35      88.554  99.322 117.771  1.00106.04           O  
ATOM   1467  ND2 ASN D  35      89.478  98.953 115.765  1.00106.04           N  
ATOM   1468  N   THR D  36      92.690  96.241 117.764  1.00 89.17           N  
ATOM   1469  CA  THR D  36      93.940  95.651 118.196  1.00 89.17           C  
ATOM   1470  C   THR D  36      95.081  96.443 117.614  1.00 89.17           C  
ATOM   1471  O   THR D  36      95.047  96.824 116.455  1.00 89.17           O  
ATOM   1472  CB  THR D  36      94.059  94.194 117.763  1.00 89.17           C  
ATOM   1473  OG1 THR D  36      93.198  93.394 118.578  1.00 89.17           O  
ATOM   1474  CG2 THR D  36      95.482  93.703 117.912  1.00 89.17           C  
HETATM 1475  N   TYC D  37      96.094  96.704 118.421  1.00 78.05           N  
HETATM 1476  CA  TYC D  37      97.255  97.442 117.931  1.00 78.05           C  
HETATM 1477  C   TYC D  37      98.474  96.642 118.226  1.00 78.05           C  
HETATM 1478  O   TYC D  37      99.453  97.201 118.675  1.00 78.05           O  
HETATM 1479  CB  TYC D  37      97.321  98.805 118.587  1.00 78.05           C  
HETATM 1480  CG  TYC D  37      96.097  99.584 118.183  1.00 78.05           C  
HETATM 1481  CD1 TYC D  37      94.946  99.520 118.943  1.00 78.05           C  
HETATM 1482  CD2 TYC D  37      96.125 100.375 117.056  1.00 78.05           C  
HETATM 1483  CE1 TYC D  37      93.822 100.240 118.575  1.00 78.05           C  
HETATM 1484  CE2 TYC D  37      95.002 101.093 116.688  1.00 78.05           C  
HETATM 1485  OH  TYC D  37      92.753 101.738 117.084  1.00 78.05           O  
HETATM 1486  CZ  TYC D  37      93.853 101.030 117.447  1.00 78.05           C  
HETATM 1487  NXT TYC D  37      98.444  95.337 117.980  1.00 78.05           N  
TER    1488      TYC D  37                                                      
ATOM   1489  N   ALA F  13      81.847 112.693 112.650  1.00102.39           N  
ATOM   1490  CA  ALA F  13      83.269 112.557 112.933  1.00102.39           C  
ATOM   1491  C   ALA F  13      84.086 113.524 112.087  1.00102.39           C  
ATOM   1492  O   ALA F  13      84.119 113.417 110.863  1.00102.39           O  
ATOM   1493  CB  ALA F  13      83.717 111.135 112.692  1.00102.39           C  
ATOM   1494  N   ASN F  14      84.744 114.471 112.746  1.00104.60           N  
ATOM   1495  CA  ASN F  14      85.508 115.510 112.072  1.00104.60           C  
ATOM   1496  C   ASN F  14      86.991 115.198 112.173  1.00104.60           C  
ATOM   1497  O   ASN F  14      87.532 115.111 113.276  1.00104.60           O  
ATOM   1498  CB  ASN F  14      85.220 116.877 112.690  1.00104.60           C  
ATOM   1499  CG  ASN F  14      83.742 117.202 112.718  1.00104.60           C  
ATOM   1500  OD1 ASN F  14      82.988 116.783 111.842  1.00104.60           O  
ATOM   1501  ND2 ASN F  14      83.319 117.956 113.725  1.00104.60           N  
ATOM   1502  N   PHE F  15      87.648 115.044 111.025  1.00 99.37           N  
ATOM   1503  CA  PHE F  15      89.063 114.685 110.980  1.00 99.37           C  
ATOM   1504  C   PHE F  15      89.780 115.673 110.077  1.00 99.37           C  
ATOM   1505  O   PHE F  15      89.506 115.725 108.876  1.00 99.37           O  
ATOM   1506  CB  PHE F  15      89.270 113.268 110.454  1.00 99.37           C  
ATOM   1507  CG  PHE F  15      88.873 112.197 111.407  1.00 99.37           C  
ATOM   1508  CD1 PHE F  15      87.571 112.067 111.826  1.00 99.37           C  
ATOM   1509  CD2 PHE F  15      89.798 111.293 111.850  1.00 99.37           C  
ATOM   1510  CE1 PHE F  15      87.215 111.075 112.688  1.00 99.37           C  
ATOM   1511  CE2 PHE F  15      89.448 110.300 112.704  1.00 99.37           C  
ATOM   1512  CZ  PHE F  15      88.154 110.193 113.130  1.00 99.37           C  
ATOM   1513  N   LEU F  16      90.701 116.440 110.639  1.00 87.47           N  
ATOM   1514  CA  LEU F  16      91.583 117.281 109.848  1.00 87.47           C  
ATOM   1515  C   LEU F  16      92.998 117.090 110.358  1.00 87.47           C  
ATOM   1516  O   LEU F  16      93.235 117.148 111.567  1.00 87.47           O  
ATOM   1517  CB  LEU F  16      91.183 118.753 109.925  1.00 87.47           C  
ATOM   1518  CG  LEU F  16      91.824 119.649 108.863  1.00 87.47           C  
ATOM   1519  CD1 LEU F  16      90.888 120.785 108.514  1.00 87.47           C  
ATOM   1520  CD2 LEU F  16      93.178 120.199 109.298  1.00 87.47           C  
ATOM   1521  N   VAL F  17      93.931 116.866 109.443  1.00 79.17           N  
ATOM   1522  CA  VAL F  17      95.327 116.666 109.791  1.00 79.17           C  
ATOM   1523  C   VAL F  17      96.158 117.590 108.924  1.00 79.17           C  
ATOM   1524  O   VAL F  17      96.015 117.590 107.699  1.00 79.17           O  
ATOM   1525  CB  VAL F  17      95.767 115.212 109.596  1.00 79.17           C  
ATOM   1526  CG1 VAL F  17      97.257 115.109 109.764  1.00 79.17           C  
ATOM   1527  CG2 VAL F  17      95.056 114.317 110.581  1.00 79.17           C  
ATOM   1528  N   HIS F  18      97.023 118.373 109.555  1.00 78.64           N  
ATOM   1529  CA  HIS F  18      97.862 119.342 108.862  1.00 78.64           C  
ATOM   1530  C   HIS F  18      99.282 119.123 109.367  1.00 78.64           C  
ATOM   1531  O   HIS F  18      99.720 119.778 110.313  1.00 78.64           O  
ATOM   1532  CB  HIS F  18      97.353 120.753 109.116  1.00 78.64           C  
ATOM   1533  CG  HIS F  18      98.309 121.830 108.719  1.00 78.64           C  
ATOM   1534  ND1 HIS F  18      98.189 123.125 109.168  1.00 78.64           N  
ATOM   1535  CD2 HIS F  18      99.398 121.811 107.915  1.00 78.64           C  
ATOM   1536  CE1 HIS F  18      99.166 123.857 108.665  1.00 78.64           C  
ATOM   1537  NE2 HIS F  18      99.914 123.083 107.901  1.00 78.64           N  
ATOM   1538  N   SER F  19      99.997 118.199 108.739  1.00 80.07           N  
ATOM   1539  CA  SER F  19     101.341 117.853 109.164  1.00 80.07           C  
ATOM   1540  C   SER F  19     102.375 118.662 108.401  1.00 80.07           C  
ATOM   1541  O   SER F  19     102.083 119.281 107.380  1.00 80.07           O  
ATOM   1542  CB  SER F  19     101.609 116.370 108.955  1.00 80.07           C  
ATOM   1543  OG  SER F  19     103.000 116.126 108.963  1.00 80.07           O  
ATOM   1544  N   SER F  20     103.602 118.659 108.917  1.00 86.53           N  
ATOM   1545  CA  SER F  20     104.711 119.313 108.235  1.00 86.53           C  
ATOM   1546  C   SER F  20     105.803 118.331 107.840  1.00 86.53           C  
ATOM   1547  O   SER F  20     106.130 118.232 106.655  1.00 86.53           O  
ATOM   1548  CB  SER F  20     105.293 120.418 109.114  1.00 86.53           C  
ATOM   1549  OG  SER F  20     106.273 119.884 109.979  1.00 86.53           O  
ATOM   1550  N   ASN F  21     106.377 117.602 108.793  1.00 88.46           N  
ATOM   1551  CA  ASN F  21     107.403 116.595 108.523  1.00 88.46           C  
ATOM   1552  C   ASN F  21     106.990 115.364 109.303  1.00 88.46           C  
ATOM   1553  O   ASN F  21     107.409 115.179 110.446  1.00 88.46           O  
ATOM   1554  CB  ASN F  21     108.777 117.061 108.935  1.00 88.46           C  
ATOM   1555  CG  ASN F  21     109.115 118.412 108.393  1.00 88.46           C  
ATOM   1556  OD1 ASN F  21     108.776 118.743 107.261  1.00 88.46           O  
ATOM   1557  ND2 ASN F  21     109.799 119.212 109.199  1.00 88.46           N  
ATOM   1558  N   ASN F  22     106.186 114.511 108.686  1.00 86.86           N  
ATOM   1559  CA  ASN F  22     105.499 113.490 109.460  1.00 86.86           C  
ATOM   1560  C   ASN F  22     106.457 112.414 109.952  1.00 86.86           C  
ATOM   1561  O   ASN F  22     106.503 112.120 111.151  1.00 86.86           O  
ATOM   1562  CB  ASN F  22     104.381 112.883 108.635  1.00 86.86           C  
ATOM   1563  CG  ASN F  22     103.618 111.861 109.397  1.00 86.86           C  
ATOM   1564  OD1 ASN F  22     103.623 111.858 110.619  1.00 86.86           O  
ATOM   1565  ND2 ASN F  22     102.961 110.967 108.687  1.00 86.86           N  
ATOM   1566  N   PHE F  23     107.195 111.785 109.038  1.00 87.95           N  
ATOM   1567  CA  PHE F  23     108.145 110.717 109.346  1.00 87.95           C  
ATOM   1568  C   PHE F  23     107.499 109.419 109.796  1.00 87.95           C  
ATOM   1569  O   PHE F  23     108.206 108.450 110.075  1.00 87.95           O  
ATOM   1570  CB  PHE F  23     109.074 111.084 110.501  1.00 87.95           C  
ATOM   1571  CG  PHE F  23     110.292 111.813 110.100  1.00 87.95           C  
ATOM   1572  CD1 PHE F  23     111.177 111.254 109.221  1.00 87.95           C  
ATOM   1573  CD2 PHE F  23     110.597 113.027 110.668  1.00 87.95           C  
ATOM   1574  CE1 PHE F  23     112.313 111.915 108.875  1.00 87.95           C  
ATOM   1575  CE2 PHE F  23     111.736 113.687 110.328  1.00 87.95           C  
ATOM   1576  CZ  PHE F  23     112.594 113.133 109.431  1.00 87.95           C  
ATOM   1577  N   GLY F  24     106.179 109.370 109.876  1.00 85.72           N  
ATOM   1578  CA  GLY F  24     105.576 108.241 110.543  1.00 85.72           C  
ATOM   1579  C   GLY F  24     104.081 108.201 110.367  1.00 85.72           C  
ATOM   1580  O   GLY F  24     103.490 109.039 109.689  1.00 85.72           O  
ATOM   1581  N   ALA F  25     103.472 107.213 111.001  1.00 82.72           N  
ATOM   1582  CA  ALA F  25     102.065 106.937 110.770  1.00 82.72           C  
ATOM   1583  C   ALA F  25     101.205 108.025 111.382  1.00 82.72           C  
ATOM   1584  O   ALA F  25     101.245 108.244 112.594  1.00 82.72           O  
ATOM   1585  CB  ALA F  25     101.696 105.580 111.353  1.00 82.72           C  
ATOM   1586  N   ILE F  26     100.440 108.717 110.553  1.00 78.39           N  
ATOM   1587  CA  ILE F  26      99.307 109.503 111.021  1.00 78.39           C  
ATOM   1588  C   ILE F  26      98.095 108.630 110.741  1.00 78.39           C  
ATOM   1589  O   ILE F  26      97.437 108.751 109.715  1.00 78.39           O  
ATOM   1590  CB  ILE F  26      99.218 110.852 110.325  1.00 78.39           C  
ATOM   1591  CG1 ILE F  26     100.474 111.660 110.593  1.00 78.39           C  
ATOM   1592  CG2 ILE F  26      98.021 111.614 110.816  1.00 78.39           C  
ATOM   1593  CD1 ILE F  26     100.449 113.020 109.963  1.00 78.39           C  
ATOM   1594  N   LEU F  27      97.785 107.745 111.673  1.00 81.84           N  
ATOM   1595  CA  LEU F  27      96.802 106.710 111.391  1.00 81.84           C  
ATOM   1596  C   LEU F  27      95.401 107.204 111.712  1.00 81.84           C  
ATOM   1597  O   LEU F  27      94.677 106.631 112.512  1.00 81.84           O  
ATOM   1598  CB  LEU F  27      97.144 105.453 112.173  1.00 81.84           C  
ATOM   1599  CG  LEU F  27      96.611 104.111 111.679  1.00 81.84           C  
ATOM   1600  CD1 LEU F  27      97.583 103.047 112.118  1.00 81.84           C  
ATOM   1601  CD2 LEU F  27      95.215 103.771 112.165  1.00 81.84           C  
ATOM   1602  N   SER F  28      95.015 108.304 111.096  1.00 80.90           N  
ATOM   1603  CA  SER F  28      93.709 108.880 111.371  1.00 80.90           C  
ATOM   1604  C   SER F  28      92.641 107.984 110.763  1.00 80.90           C  
ATOM   1605  O   SER F  28      92.546 107.873 109.540  1.00 80.90           O  
ATOM   1606  CB  SER F  28      93.650 110.291 110.806  1.00 80.90           C  
ATOM   1607  OG  SER F  28      92.560 111.002 111.337  1.00 80.90           O  
ATOM   1608  N   SER F  29      91.834 107.335 111.599  1.00 94.97           N  
ATOM   1609  CA  SER F  29      90.927 106.313 111.097  1.00 94.97           C  
ATOM   1610  C   SER F  29      89.647 106.295 111.914  1.00 94.97           C  
ATOM   1611  O   SER F  29      89.480 107.060 112.865  1.00 94.97           O  
ATOM   1612  CB  SER F  29      91.574 104.934 111.132  1.00 94.97           C  
ATOM   1613  OG  SER F  29      91.850 104.547 112.463  1.00 94.97           O  
ATOM   1614  N   THR F  30      88.737 105.400 111.526  1.00109.85           N  
ATOM   1615  CA  THR F  30      87.472 105.190 112.224  1.00109.85           C  
ATOM   1616  C   THR F  30      86.852 103.900 111.714  1.00109.85           C  
ATOM   1617  O   THR F  30      86.956 103.596 110.524  1.00109.85           O  
ATOM   1618  CB  THR F  30      86.496 106.348 112.009  1.00109.85           C  
ATOM   1619  OG1 THR F  30      87.132 107.581 112.349  1.00109.85           O  
ATOM   1620  CG2 THR F  30      85.267 106.180 112.885  1.00109.85           C  
ATOM   1621  N   ASN F  31      86.192 103.159 112.603  1.00114.58           N  
ATOM   1622  CA  ASN F  31      85.685 101.842 112.246  1.00114.58           C  
ATOM   1623  C   ASN F  31      84.703 101.291 113.262  1.00114.58           C  
ATOM   1624  O   ASN F  31      84.766 101.632 114.443  1.00114.58           O  
ATOM   1625  CB  ASN F  31      86.842 100.871 112.099  1.00114.58           C  
ATOM   1626  CG  ASN F  31      87.821 101.000 113.208  1.00114.58           C  
ATOM   1627  OD1 ASN F  31      87.568 101.701 114.174  1.00114.58           O  
ATOM   1628  ND2 ASN F  31      88.963 100.359 113.073  1.00114.58           N  
ATOM   1629  N   VAL F  32      83.779 100.451 112.810  1.00120.11           N  
ATOM   1630  CA  VAL F  32      82.936  99.721 113.747  1.00120.11           C  
ATOM   1631  C   VAL F  32      83.552  98.374 114.097  1.00120.11           C  
ATOM   1632  O   VAL F  32      83.814  98.086 115.268  1.00120.11           O  
ATOM   1633  CB  VAL F  32      81.507  99.585 113.191  1.00120.11           C  
ATOM   1634  CG1 VAL F  32      80.677  98.736 114.092  1.00120.11           C  
ATOM   1635  CG2 VAL F  32      80.862 100.951 113.092  1.00120.11           C  
ATOM   1636  N   GLY F  33      83.813  97.543 113.104  1.00119.58           N  
ATOM   1637  CA  GLY F  33      84.216  96.184 113.377  1.00119.58           C  
ATOM   1638  C   GLY F  33      85.657  96.059 113.816  1.00119.58           C  
ATOM   1639  O   GLY F  33      86.281  96.996 114.307  1.00119.58           O  
ATOM   1640  N   SER F  34      86.184  94.854 113.629  1.00115.88           N  
ATOM   1641  CA  SER F  34      87.527  94.543 114.089  1.00115.88           C  
ATOM   1642  C   SER F  34      88.566  95.069 113.114  1.00115.88           C  
ATOM   1643  O   SER F  34      88.263  95.369 111.959  1.00115.88           O  
ATOM   1644  CB  SER F  34      87.694  93.037 114.239  1.00115.88           C  
ATOM   1645  OG  SER F  34      88.063  92.466 112.998  1.00115.88           O  
ATOM   1646  N   ASN F  35      89.801  95.160 113.587  1.00106.73           N  
ATOM   1647  CA  ASN F  35      90.945  95.578 112.794  1.00106.73           C  
ATOM   1648  C   ASN F  35      92.196  94.892 113.314  1.00106.73           C  
ATOM   1649  O   ASN F  35      92.130  93.935 114.087  1.00106.73           O  
ATOM   1650  CB  ASN F  35      91.098  97.091 112.830  1.00106.73           C  
ATOM   1651  CG  ASN F  35      89.941  97.788 112.205  1.00106.73           C  
ATOM   1652  OD1 ASN F  35      89.019  98.219 112.892  1.00106.73           O  
ATOM   1653  ND2 ASN F  35      89.969  97.908 110.887  1.00106.73           N  
ATOM   1654  N   THR F  36      93.341  95.403 112.890  1.00 89.91           N  
ATOM   1655  CA  THR F  36      94.624  94.892 113.324  1.00 89.91           C  
ATOM   1656  C   THR F  36      95.716  95.754 112.744  1.00 89.91           C  
ATOM   1657  O   THR F  36      95.658  96.133 111.586  1.00 89.91           O  
ATOM   1658  CB  THR F  36      94.835  93.445 112.890  1.00 89.91           C  
ATOM   1659  OG1 THR F  36      94.025  92.593 113.705  1.00 89.91           O  
ATOM   1660  CG2 THR F  36      96.286  93.044 113.041  1.00 89.91           C  
HETATM 1661  N   TYC F  37      96.709  96.078 113.551  1.00 81.05           N  
HETATM 1662  CA  TYC F  37      97.822  96.887 113.065  1.00 81.05           C  
HETATM 1663  C   TYC F  37      99.087  96.164 113.359  1.00 81.05           C  
HETATM 1664  O   TYC F  37     100.029  96.783 113.810  1.00 81.05           O  
HETATM 1665  CB  TYC F  37      97.801  98.250 113.719  1.00 81.05           C  
HETATM 1666  CG  TYC F  37      96.532  98.953 113.315  1.00 81.05           C  
HETATM 1667  CD1 TYC F  37      95.386  98.816 114.073  1.00 81.05           C  
HETATM 1668  CD2 TYC F  37      96.511  99.744 112.187  1.00 81.05           C  
HETATM 1669  CE1 TYC F  37      94.220  99.465 113.704  1.00 81.05           C  
HETATM 1670  CE2 TYC F  37      95.346 100.391 111.818  1.00 81.05           C  
HETATM 1671  OH  TYC F  37      93.061 100.893 112.212  1.00 81.05           O  
HETATM 1672  CZ  TYC F  37      94.202 100.255 112.576  1.00 81.05           C  
HETATM 1673  NXT TYC F  37      99.140  94.860 113.114  1.00 81.05           N  
TER    1674      TYC F  37                                                      
ATOM   1675  N   ALA H  13      81.529 111.163 107.829  1.00102.28           N  
ATOM   1676  CA  ALA H  13      82.959 111.114 108.110  1.00102.28           C  
ATOM   1677  C   ALA H  13      83.714 112.130 107.264  1.00102.28           C  
ATOM   1678  O   ALA H  13      83.751 112.026 106.040  1.00102.28           O  
ATOM   1679  CB  ALA H  13      83.491 109.722 107.867  1.00102.28           C  
ATOM   1680  N   ASN H  14      84.312 113.114 107.923  1.00105.48           N  
ATOM   1681  CA  ASN H  14      85.011 114.198 107.249  1.00105.48           C  
ATOM   1682  C   ASN H  14      86.511 113.978 107.348  1.00105.48           C  
ATOM   1683  O   ASN H  14      87.056 113.924 108.451  1.00105.48           O  
ATOM   1684  CB  ASN H  14      84.640 115.545 107.868  1.00105.48           C  
ATOM   1685  CG  ASN H  14      83.145 115.779 107.898  1.00105.48           C  
ATOM   1686  OD1 ASN H  14      82.417 115.314 107.023  1.00105.48           O  
ATOM   1687  ND2 ASN H  14      82.679 116.505 108.907  1.00105.48           N  
ATOM   1688  N   PHE H  15      87.174 113.866 106.200  1.00101.59           N  
ATOM   1689  CA  PHE H  15      88.609 113.593 106.152  1.00101.59           C  
ATOM   1690  C   PHE H  15      89.262 114.624 105.248  1.00101.59           C  
ATOM   1691  O   PHE H  15      88.984 114.661 104.048  1.00101.59           O  
ATOM   1692  CB  PHE H  15      88.901 112.193 105.625  1.00101.59           C  
ATOM   1693  CG  PHE H  15      88.572 111.099 106.577  1.00101.59           C  
ATOM   1694  CD1 PHE H  15      87.281 110.889 106.998  1.00101.59           C  
ATOM   1695  CD2 PHE H  15      89.551 110.252 107.018  1.00101.59           C  
ATOM   1696  CE1 PHE H  15      86.987 109.876 107.860  1.00101.59           C  
ATOM   1697  CE2 PHE H  15      89.263 109.239 107.872  1.00101.59           C  
ATOM   1698  CZ  PHE H  15      87.980 109.053 108.299  1.00101.59           C  
ATOM   1699  N   LEU H  16      90.134 115.447 105.810  1.00 91.67           N  
ATOM   1700  CA  LEU H  16      90.963 116.340 105.019  1.00 91.67           C  
ATOM   1701  C   LEU H  16      92.388 116.236 105.527  1.00 91.67           C  
ATOM   1702  O   LEU H  16      92.623 116.307 106.736  1.00 91.67           O  
ATOM   1703  CB  LEU H  16      90.473 117.785 105.097  1.00 91.67           C  
ATOM   1704  CG  LEU H  16      91.057 118.719 104.035  1.00 91.67           C  
ATOM   1705  CD1 LEU H  16      90.053 119.797 103.688  1.00 91.67           C  
ATOM   1706  CD2 LEU H  16      92.375 119.350 104.470  1.00 91.67           C  
ATOM   1707  N   VAL H  17      93.332 116.070 104.611  1.00 81.54           N  
ATOM   1708  CA  VAL H  17      94.737 115.956 104.955  1.00 81.54           C  
ATOM   1709  C   VAL H  17      95.510 116.929 104.090  1.00 81.54           C  
ATOM   1710  O   VAL H  17      95.365 116.922 102.864  1.00 81.54           O  
ATOM   1711  CB  VAL H  17      95.266 114.531 104.760  1.00 81.54           C  
ATOM   1712  CG1 VAL H  17      96.759 114.519 104.926  1.00 81.54           C  
ATOM   1713  CG2 VAL H  17      94.613 113.593 105.744  1.00 81.54           C  
ATOM   1714  N   HIS H  18      96.326 117.763 104.720  1.00 81.66           N  
ATOM   1715  CA  HIS H  18      97.103 118.782 104.026  1.00 81.66           C  
ATOM   1716  C   HIS H  18      98.534 118.650 104.530  1.00 81.66           C  
ATOM   1717  O   HIS H  18      98.932 119.330 105.475  1.00 81.66           O  
ATOM   1718  CB  HIS H  18      96.509 120.159 104.282  1.00 81.66           C  
ATOM   1719  CG  HIS H  18      97.397 121.294 103.885  1.00 81.66           C  
ATOM   1720  ND1 HIS H  18      97.198 122.578 104.335  1.00 81.66           N  
ATOM   1721  CD2 HIS H  18      98.484 121.340 103.079  1.00 81.66           C  
ATOM   1722  CE1 HIS H  18      98.128 123.369 103.830  1.00 81.66           C  
ATOM   1723  NE2 HIS H  18      98.921 122.642 103.066  1.00 81.66           N  
ATOM   1724  N   SER H  19      99.303 117.773 103.899  1.00 83.27           N  
ATOM   1725  CA  SER H  19     100.667 117.510 104.322  1.00 83.27           C  
ATOM   1726  C   SER H  19     101.649 118.380 103.559  1.00 83.27           C  
ATOM   1727  O   SER H  19     101.318 118.980 102.539  1.00 83.27           O  
ATOM   1728  CB  SER H  19     101.025 116.046 104.112  1.00 83.27           C  
ATOM   1729  OG  SER H  19     102.429 115.887 104.117  1.00 83.27           O  
ATOM   1730  N   SER H  20     102.874 118.452 104.074  1.00 89.99           N  
ATOM   1731  CA  SER H  20     103.939 119.174 103.390  1.00 89.99           C  
ATOM   1732  C   SER H  20     105.089 118.261 102.992  1.00 89.99           C  
ATOM   1733  O   SER H  20     105.420 118.182 101.807  1.00 89.99           O  
ATOM   1734  CB  SER H  20     104.454 120.312 104.269  1.00 89.99           C  
ATOM   1735  OG  SER H  20     105.466 119.838 105.133  1.00 89.99           O  
ATOM   1736  N   ASN H  21     105.709 117.567 103.944  1.00 91.78           N  
ATOM   1737  CA  ASN H  21     106.795 116.626 103.672  1.00 91.78           C  
ATOM   1738  C   ASN H  21     106.458 115.370 104.453  1.00 91.78           C  
ATOM   1739  O   ASN H  21     106.888 115.211 105.594  1.00 91.78           O  
ATOM   1740  CB  ASN H  21     108.137 117.173 104.084  1.00 91.78           C  
ATOM   1741  CG  ASN H  21     108.391 118.544 103.542  1.00 91.78           C  
ATOM   1742  OD1 ASN H  21     108.031 118.853 102.410  1.00 91.78           O  
ATOM   1743  ND2 ASN H  21     109.026 119.384 104.348  1.00 91.78           N  
ATOM   1744  N   ASN H  22     105.707 114.470 103.835  1.00 88.27           N  
ATOM   1745  CA  ASN H  22     105.084 113.409 104.609  1.00 88.27           C  
ATOM   1746  C   ASN H  22     106.107 112.393 105.100  1.00 88.27           C  
ATOM   1747  O   ASN H  22     106.173 112.101 106.298  1.00 88.27           O  
ATOM   1748  CB  ASN H  22     104.005 112.734 103.786  1.00 88.27           C  
ATOM   1749  CG  ASN H  22     103.307 111.667 104.548  1.00 88.27           C  
ATOM   1750  OD1 ASN H  22     103.314 111.665 105.770  1.00 88.27           O  
ATOM   1751  ND2 ASN H  22     102.705 110.736 103.839  1.00 88.27           N  
ATOM   1752  N   PHE H  23     106.882 111.812 104.183  1.00 90.17           N  
ATOM   1753  CA  PHE H  23     107.895 110.803 104.490  1.00 90.17           C  
ATOM   1754  C   PHE H  23     107.324 109.462 104.914  1.00 90.17           C  
ATOM   1755  O   PHE H  23     108.082 108.515 105.129  1.00 90.17           O  
ATOM   1756  CB  PHE H  23     108.801 111.226 105.644  1.00 90.17           C  
ATOM   1757  CG  PHE H  23     109.972 112.028 105.242  1.00 90.17           C  
ATOM   1758  CD1 PHE H  23     110.889 111.524 104.362  1.00 90.17           C  
ATOM   1759  CD2 PHE H  23     110.203 113.257 105.810  1.00 90.17           C  
ATOM   1760  CE1 PHE H  23     111.981 112.255 104.014  1.00 90.17           C  
ATOM   1761  CE2 PHE H  23     111.298 113.987 105.470  1.00 90.17           C  
ATOM   1762  CZ  PHE H  23     112.189 113.486 104.571  1.00 90.17           C  
ATOM   1763  N   GLY H  24     106.011 109.351 105.043  1.00 85.96           N  
ATOM   1764  CA  GLY H  24     105.485 108.174 105.688  1.00 85.96           C  
ATOM   1765  C   GLY H  24     103.994 108.043 105.514  1.00 85.96           C  
ATOM   1766  O   GLY H  24     103.353 108.843 104.837  1.00 85.96           O  
ATOM   1767  N   ALA H  25     103.447 107.018 106.148  1.00 85.11           N  
ATOM   1768  CA  ALA H  25     102.060 106.657 105.918  1.00 85.11           C  
ATOM   1769  C   ALA H  25     101.136 107.690 106.533  1.00 85.11           C  
ATOM   1770  O   ALA H  25     101.163 107.909 107.745  1.00 85.11           O  
ATOM   1771  CB  ALA H  25     101.776 105.280 106.502  1.00 85.11           C  
ATOM   1772  N   ILE H  26     100.328 108.334 105.705  1.00 80.06           N  
ATOM   1773  CA  ILE H  26      99.151 109.049 106.175  1.00 80.06           C  
ATOM   1774  C   ILE H  26      97.995 108.103 105.897  1.00 80.06           C  
ATOM   1775  O   ILE H  26      97.328 108.185 104.871  1.00 80.06           O  
ATOM   1776  CB  ILE H  26      98.979 110.391 105.480  1.00 80.06           C  
ATOM   1777  CG1 ILE H  26     100.182 111.273 105.747  1.00 80.06           C  
ATOM   1778  CG2 ILE H  26      97.738 111.078 105.974  1.00 80.06           C  
ATOM   1779  CD1 ILE H  26     100.073 112.630 105.119  1.00 80.06           C  
ATOM   1780  N   LEU H  27      97.740 107.201 106.828  1.00 83.95           N  
ATOM   1781  CA  LEU H  27      96.821 106.108 106.546  1.00 83.95           C  
ATOM   1782  C   LEU H  27      95.394 106.514 106.870  1.00 83.95           C  
ATOM   1783  O   LEU H  27      94.707 105.898 107.671  1.00 83.95           O  
ATOM   1784  CB  LEU H  27      97.242 104.873 107.327  1.00 83.95           C  
ATOM   1785  CG  LEU H  27      96.791 103.501 106.833  1.00 83.95           C  
ATOM   1786  CD1 LEU H  27      97.827 102.499 107.270  1.00 83.95           C  
ATOM   1787  CD2 LEU H  27      95.420 103.077 107.321  1.00 83.95           C  
ATOM   1788  N   SER H  28      94.939 107.589 106.256  1.00 85.31           N  
ATOM   1789  CA  SER H  28      93.602 108.084 106.533  1.00 85.31           C  
ATOM   1790  C   SER H  28      92.589 107.125 105.926  1.00 85.31           C  
ATOM   1791  O   SER H  28      92.500 107.010 104.703  1.00 85.31           O  
ATOM   1792  CB  SER H  28      93.456 109.489 105.968  1.00 85.31           C  
ATOM   1793  OG  SER H  28      92.325 110.131 106.502  1.00 85.31           O  
ATOM   1794  N   SER H  29      91.826 106.427 106.762  1.00 98.06           N  
ATOM   1795  CA  SER H  29      90.982 105.352 106.259  1.00 98.06           C  
ATOM   1796  C   SER H  29      89.706 105.254 107.080  1.00 98.06           C  
ATOM   1797  O   SER H  29      89.494 106.007 108.030  1.00 98.06           O  
ATOM   1798  CB  SER H  29      91.712 104.014 106.293  1.00 98.06           C  
ATOM   1799  OG  SER H  29      92.012 103.644 107.623  1.00 98.06           O  
ATOM   1800  N   THR H  30      88.853 104.306 106.691  1.00112.01           N  
ATOM   1801  CA  THR H  30      87.603 104.018 107.391  1.00112.01           C  
ATOM   1802  C   THR H  30      87.062 102.693 106.881  1.00112.01           C  
ATOM   1803  O   THR H  30      87.183 102.396 105.690  1.00112.01           O  
ATOM   1804  CB  THR H  30      86.559 105.115 107.178  1.00112.01           C  
ATOM   1805  OG1 THR H  30      87.117 106.384 107.519  1.00112.01           O  
ATOM   1806  CG2 THR H  30      85.343 104.871 108.056  1.00112.01           C  
ATOM   1807  N   ASN H  31      86.450 101.913 107.770  1.00115.14           N  
ATOM   1808  CA  ASN H  31      86.025 100.567 107.412  1.00115.14           C  
ATOM   1809  C   ASN H  31      85.080  99.957 108.429  1.00115.14           C  
ATOM   1810  O   ASN H  31      85.123 100.300 109.610  1.00115.14           O  
ATOM   1811  CB  ASN H  31      87.239  99.669 107.263  1.00115.14           C  
ATOM   1812  CG  ASN H  31      88.209  99.858 108.371  1.00115.14           C  
ATOM   1813  OD1 ASN H  31      87.917 100.540 109.338  1.00115.14           O  
ATOM   1814  ND2 ASN H  31      89.388  99.287 108.234  1.00115.14           N  
ATOM   1815  N   VAL H  32      84.208  99.061 107.978  1.00120.44           N  
ATOM   1816  CA  VAL H  32      83.413  98.281 108.916  1.00120.44           C  
ATOM   1817  C   VAL H  32      84.110  96.974 109.263  1.00120.44           C  
ATOM   1818  O   VAL H  32      84.391  96.700 110.434  1.00120.44           O  
ATOM   1819  CB  VAL H  32      81.994  98.057 108.361  1.00120.44           C  
ATOM   1820  CG1 VAL H  32      81.217  97.160 109.261  1.00120.44           C  
ATOM   1821  CG2 VAL H  32      81.267  99.381 108.263  1.00120.44           C  
ATOM   1822  N   GLY H  33      84.421  96.161 108.269  1.00118.09           N  
ATOM   1823  CA  GLY H  33      84.906  94.829 108.541  1.00118.09           C  
ATOM   1824  C   GLY H  33      86.352  94.792 108.978  1.00118.09           C  
ATOM   1825  O   GLY H  33      86.918  95.765 109.469  1.00118.09           O  
ATOM   1826  N   SER H  34      86.953  93.622 108.789  1.00115.66           N  
ATOM   1827  CA  SER H  34      88.313  93.393 109.247  1.00115.66           C  
ATOM   1828  C   SER H  34      89.317  93.982 108.271  1.00115.66           C  
ATOM   1829  O   SER H  34      88.994  94.264 107.117  1.00115.66           O  
ATOM   1830  CB  SER H  34      88.572  91.901 109.397  1.00115.66           C  
ATOM   1831  OG  SER H  34      88.973  91.354 108.154  1.00115.66           O  
ATOM   1832  N   ASN H  35      90.545  94.148 108.742  1.00106.08           N  
ATOM   1833  CA  ASN H  35      91.659  94.636 107.947  1.00106.08           C  
ATOM   1834  C   ASN H  35      92.950  94.028 108.466  1.00106.08           C  
ATOM   1835  O   ASN H  35      92.944  93.067 109.238  1.00106.08           O  
ATOM   1836  CB  ASN H  35      91.720  96.156 107.986  1.00106.08           C  
ATOM   1837  CG  ASN H  35      90.522  96.783 107.362  1.00106.08           C  
ATOM   1838  OD1 ASN H  35      89.576  97.154 108.051  1.00106.08           O  
ATOM   1839  ND2 ASN H  35      90.539  96.905 106.045  1.00106.08           N  
ATOM   1840  N   THR H  36      94.062  94.608 108.041  1.00 91.65           N  
ATOM   1841  CA  THR H  36      95.374  94.177 108.473  1.00 91.65           C  
ATOM   1842  C   THR H  36      96.409  95.105 107.892  1.00 91.65           C  
ATOM   1843  O   THR H  36      96.328  95.479 106.734  1.00 91.65           O  
ATOM   1844  CB  THR H  36      95.672  92.747 108.038  1.00 91.65           C  
ATOM   1845  OG1 THR H  36      94.918  91.845 108.853  1.00 91.65           O  
ATOM   1846  CG2 THR H  36      97.145  92.434 108.186  1.00 91.65           C  
HETATM 1847  N   TYC H  37      97.383  95.487 108.698  1.00 84.06           N  
HETATM 1848  CA  TYC H  37      98.443  96.364 108.211  1.00 84.06           C  
HETATM 1849  C   TYC H  37      99.751  95.719 108.504  1.00 84.06           C  
HETATM 1850  O   TYC H  37     100.654  96.395 108.954  1.00 84.06           O  
HETATM 1851  CB  TYC H  37      98.341  97.724 108.867  1.00 84.06           C  
HETATM 1852  CG  TYC H  37      97.030  98.346 108.465  1.00 84.06           C  
HETATM 1853  CD1 TYC H  37      95.896  98.140 109.225  1.00 84.06           C  
HETATM 1854  CD2 TYC H  37      96.959  99.136 107.338  1.00 84.06           C  
HETATM 1855  CE1 TYC H  37      94.692  98.716 108.857  1.00 84.06           C  
HETATM 1856  CE2 TYC H  37      95.756  99.711 106.971  1.00 84.06           C  
HETATM 1857  OH  TYC H  37      93.445 100.072 107.368  1.00 84.06           O  
HETATM 1858  CZ  TYC H  37      94.623  99.504 107.730  1.00 84.06           C  
HETATM 1859  NXT TYC H  37      99.883  94.422 108.258  1.00 84.06           N  
TER    1860      TYC H  37                                                      
ATOM   1861  N   ALA J  13      81.470 109.763 103.331  1.00109.86           N  
ATOM   1862  CA  ALA J  13      82.899 109.789 103.610  1.00109.86           C  
ATOM   1863  C   ALA J  13      83.597 110.854 102.773  1.00109.86           C  
ATOM   1864  O   ALA J  13      83.638 110.764 101.549  1.00109.86           O  
ATOM   1865  CB  ALA J  13      83.507 108.431 103.352  1.00109.86           C  
ATOM   1866  N   ASN J  14      84.143 111.862 103.442  1.00111.08           N  
ATOM   1867  CA  ASN J  14      84.780 112.990 102.778  1.00111.08           C  
ATOM   1868  C   ASN J  14      86.290 112.849 102.874  1.00111.08           C  
ATOM   1869  O   ASN J  14      86.840 112.814 103.975  1.00111.08           O  
ATOM   1870  CB  ASN J  14      84.338 114.307 103.412  1.00111.08           C  
ATOM   1871  CG  ASN J  14      82.833 114.459 103.447  1.00111.08           C  
ATOM   1872  OD1 ASN J  14      82.130 113.965 102.567  1.00111.08           O  
ATOM   1873  ND2 ASN J  14      82.329 115.149 104.463  1.00111.08           N  
ATOM   1874  N   PHE J  15      86.956 112.785 101.723  1.00106.63           N  
ATOM   1875  CA  PHE J  15      88.405 112.592 101.670  1.00106.63           C  
ATOM   1876  C   PHE J  15      88.999 113.666 100.777  1.00106.63           C  
ATOM   1877  O   PHE J  15      88.717 113.700  99.577  1.00106.63           O  
ATOM   1878  CB  PHE J  15      88.771 111.214 101.128  1.00106.63           C  
ATOM   1879  CG  PHE J  15      88.503 110.095 102.070  1.00106.63           C  
ATOM   1880  CD1 PHE J  15      87.226 109.811 102.490  1.00106.63           C  
ATOM   1881  CD2 PHE J  15      89.527 109.298 102.500  1.00106.63           C  
ATOM   1882  CE1 PHE J  15      86.989 108.775 103.342  1.00106.63           C  
ATOM   1883  CE2 PHE J  15      89.296 108.262 103.344  1.00106.63           C  
ATOM   1884  CZ  PHE J  15      88.026 108.002 103.772  1.00106.63           C  
ATOM   1885  N   LEU J  16      89.827 114.530 101.348  1.00 97.08           N  
ATOM   1886  CA  LEU J  16      90.603 115.474 100.564  1.00 97.08           C  
ATOM   1887  C   LEU J  16      92.033 115.442 101.069  1.00 97.08           C  
ATOM   1888  O   LEU J  16      92.266 115.513 102.278  1.00 97.08           O  
ATOM   1889  CB  LEU J  16      90.036 116.889 100.658  1.00 97.08           C  
ATOM   1890  CG  LEU J  16      90.568 117.865  99.604  1.00 97.08           C  
ATOM   1891  CD1 LEU J  16      89.505 118.889  99.271  1.00 97.08           C  
ATOM   1892  CD2 LEU J  16      91.850 118.562 100.044  1.00 97.08           C  
ATOM   1893  N   VAL J  17      92.983 115.337 100.150  1.00 84.59           N  
ATOM   1894  CA  VAL J  17      94.394 115.296 100.492  1.00 84.59           C  
ATOM   1895  C   VAL J  17      95.110 116.318  99.636  1.00 84.59           C  
ATOM   1896  O   VAL J  17      94.964 116.317  98.411  1.00 84.59           O  
ATOM   1897  CB  VAL J  17      94.998 113.904 100.281  1.00 84.59           C  
ATOM   1898  CG1 VAL J  17      96.490 113.972 100.446  1.00 84.59           C  
ATOM   1899  CG2 VAL J  17      94.398 112.922 101.256  1.00 84.59           C  
ATOM   1900  N   HIS J  18      95.881 117.189 100.274  1.00 89.10           N  
ATOM   1901  CA  HIS J  18      96.600 118.256  99.590  1.00 89.10           C  
ATOM   1902  C   HIS J  18      98.038 118.196 100.090  1.00 89.10           C  
ATOM   1903  O   HIS J  18      98.400 118.887 101.043  1.00 89.10           O  
ATOM   1904  CB  HIS J  18      95.933 119.596  99.860  1.00 89.10           C  
ATOM   1905  CG  HIS J  18      96.757 120.781  99.475  1.00 89.10           C  
ATOM   1906  ND1 HIS J  18      96.489 122.049  99.939  1.00 89.10           N  
ATOM   1907  CD2 HIS J  18      97.838 120.896  98.668  1.00 89.10           C  
ATOM   1908  CE1 HIS J  18      97.374 122.893  99.441  1.00 89.10           C  
ATOM   1909  NE2 HIS J  18      98.204 122.219  98.668  1.00 89.10           N  
ATOM   1910  N   SER J  19      98.852 117.369  99.450  1.00 87.99           N  
ATOM   1911  CA  SER J  19     100.229 117.175  99.868  1.00 87.99           C  
ATOM   1912  C   SER J  19     101.160 118.107  99.113  1.00 87.99           C  
ATOM   1913  O   SER J  19     100.795 118.699  98.099  1.00 87.99           O  
ATOM   1914  CB  SER J  19     100.665 115.736  99.642  1.00 87.99           C  
ATOM   1915  OG  SER J  19     102.076 115.654  99.645  1.00 87.99           O  
ATOM   1916  N   SER J  20     102.380 118.240  99.627  1.00 96.33           N  
ATOM   1917  CA  SER J  20     103.404 119.025  98.950  1.00 96.33           C  
ATOM   1918  C   SER J  20     104.601 118.179  98.542  1.00 96.33           C  
ATOM   1919  O   SER J  20     104.934 118.132  97.355  1.00 96.33           O  
ATOM   1920  CB  SER J  20     103.858 120.180  99.840  1.00 96.33           C  
ATOM   1921  OG  SER J  20     104.895 119.752 100.697  1.00 96.33           O  
ATOM   1922  N   ASN J  21     105.259 117.510  99.485  1.00 98.05           N  
ATOM   1923  CA  ASN J  21     106.394 116.633  99.203  1.00 98.05           C  
ATOM   1924  C   ASN J  21     106.127 115.353  99.970  1.00 98.05           C  
ATOM   1925  O   ASN J  21     106.568 115.206 101.110  1.00 98.05           O  
ATOM   1926  CB  ASN J  21     107.705 117.248  99.618  1.00 98.05           C  
ATOM   1927  CG  ASN J  21     107.884 118.636  99.091  1.00 98.05           C  
ATOM   1928  OD1 ASN J  21     107.505 118.937  97.962  1.00 98.05           O  
ATOM   1929  ND2 ASN J  21     108.473 119.501  99.904  1.00 98.05           N  
ATOM   1930  N   ASN J  22     105.425 114.419  99.344  1.00 93.19           N  
ATOM   1931  CA  ASN J  22     104.863 113.318 100.108  1.00 93.19           C  
ATOM   1932  C   ASN J  22     105.940 112.355 100.587  1.00 93.19           C  
ATOM   1933  O   ASN J  22     106.023 112.054 101.781  1.00 93.19           O  
ATOM   1934  CB  ASN J  22     103.820 112.595  99.277  1.00 93.19           C  
ATOM   1935  CG  ASN J  22     103.183 111.483 100.029  1.00 93.19           C  
ATOM   1936  OD1 ASN J  22     103.191 111.468 101.251  1.00 93.19           O  
ATOM   1937  ND2 ASN J  22     102.630 110.528  99.312  1.00 93.19           N  
ATOM   1938  N   PHE J  23     106.743 111.825  99.663  1.00 96.03           N  
ATOM   1939  CA  PHE J  23     107.811 110.870  99.958  1.00 96.03           C  
ATOM   1940  C   PHE J  23     107.325 109.508 100.421  1.00 96.03           C  
ATOM   1941  O   PHE J  23     108.143 108.649 100.750  1.00 96.03           O  
ATOM   1942  CB  PHE J  23     108.695 111.330 101.115  1.00 96.03           C  
ATOM   1943  CG  PHE J  23     109.820 112.198 100.720  1.00 96.03           C  
ATOM   1944  CD1 PHE J  23     110.761 111.754  99.834  1.00 96.03           C  
ATOM   1945  CD2 PHE J  23     109.984 113.432 101.301  1.00 96.03           C  
ATOM   1946  CE1 PHE J  23     111.811 112.547  99.493  1.00 96.03           C  
ATOM   1947  CE2 PHE J  23     111.038 114.224 100.967  1.00 96.03           C  
ATOM   1948  CZ  PHE J  23     111.952 113.782 100.062  1.00 96.03           C  
ATOM   1949  N   GLY J  24     106.022 109.285 100.456  1.00 91.67           N  
ATOM   1950  CA  GLY J  24     105.549 108.101 101.131  1.00 91.67           C  
ATOM   1951  C   GLY J  24     104.066 107.892 100.958  1.00 91.67           C  
ATOM   1952  O   GLY J  24     103.382 108.662 100.290  1.00 91.67           O  
ATOM   1953  N   ALA J  25     103.577 106.833 101.581  1.00 90.23           N  
ATOM   1954  CA  ALA J  25     102.211 106.399 101.350  1.00 90.23           C  
ATOM   1955  C   ALA J  25     101.233 107.373 101.976  1.00 90.23           C  
ATOM   1956  O   ALA J  25     101.252 107.582 103.190  1.00 90.23           O  
ATOM   1957  CB  ALA J  25     102.003 105.002 101.919  1.00 90.23           C  
ATOM   1958  N   ILE J  26     100.391 107.981 101.156  1.00 86.44           N  
ATOM   1959  CA  ILE J  26      99.178 108.626 101.634  1.00 86.44           C  
ATOM   1960  C   ILE J  26      98.073 107.622 101.347  1.00 86.44           C  
ATOM   1961  O   ILE J  26      97.402 107.678 100.324  1.00 86.44           O  
ATOM   1962  CB  ILE J  26      98.931 109.964 100.954  1.00 86.44           C  
ATOM   1963  CG1 ILE J  26     100.085 110.908 101.228  1.00 86.44           C  
ATOM   1964  CG2 ILE J  26      97.656 110.577 101.457  1.00 86.44           C  
ATOM   1965  CD1 ILE J  26      99.902 112.264 100.614  1.00 86.44           C  
ATOM   1966  N   LEU J  27      97.870 106.698 102.270  1.00 90.14           N  
ATOM   1967  CA  LEU J  27      97.011 105.559 101.978  1.00 90.14           C  
ATOM   1968  C   LEU J  27      95.565 105.884 102.307  1.00 90.14           C  
ATOM   1969  O   LEU J  27      94.914 105.223 103.102  1.00 90.14           O  
ATOM   1970  CB  LEU J  27      97.500 104.341 102.746  1.00 90.14           C  
ATOM   1971  CG  LEU J  27      97.123 102.952 102.237  1.00 90.14           C  
ATOM   1972  CD1 LEU J  27      98.212 102.004 102.662  1.00 90.14           C  
ATOM   1973  CD2 LEU J  27      95.777 102.448 102.722  1.00 90.14           C  
ATOM   1974  N   SER J  28      95.052 106.940 101.705  1.00 94.07           N  
ATOM   1975  CA  SER J  28      93.689 107.358 101.989  1.00 94.07           C  
ATOM   1976  C   SER J  28      92.730 106.351 101.373  1.00 94.07           C  
ATOM   1977  O   SER J  28      92.644 106.244 100.149  1.00 94.07           O  
ATOM   1978  CB  SER J  28      93.466 108.759 101.438  1.00 94.07           C  
ATOM   1979  OG  SER J  28      92.302 109.334 101.980  1.00 94.07           O  
ATOM   1980  N   SER J  29      92.005 105.604 102.202  1.00105.86           N  
ATOM   1981  CA  SER J  29      91.221 104.491 101.690  1.00105.86           C  
ATOM   1982  C   SER J  29      89.954 104.316 102.510  1.00105.86           C  
ATOM   1983  O   SER J  29      89.703 105.046 103.468  1.00105.86           O  
ATOM   1984  CB  SER J  29      92.022 103.194 101.708  1.00105.86           C  
ATOM   1985  OG  SER J  29      92.344 102.827 103.034  1.00105.86           O  
ATOM   1986  N   THR J  30      89.152 103.327 102.112  1.00118.56           N  
ATOM   1987  CA  THR J  30      87.923 102.964 102.810  1.00118.56           C  
ATOM   1988  C   THR J  30      87.453 101.617 102.287  1.00118.56           C  
ATOM   1989  O   THR J  30      87.587 101.339 101.094  1.00118.56           O  
ATOM   1990  CB  THR J  30      86.819 104.005 102.612  1.00118.56           C  
ATOM   1991  OG1 THR J  30      87.308 105.298 102.964  1.00118.56           O  
ATOM   1992  CG2 THR J  30      85.620 103.686 103.488  1.00118.56           C  
ATOM   1993  N   ASN J  31      86.886 100.795 103.169  1.00118.56           N  
ATOM   1994  CA  ASN J  31      86.533  99.433 102.798  1.00118.56           C  
ATOM   1995  C   ASN J  31      85.624  98.761 103.811  1.00118.56           C  
ATOM   1996  O   ASN J  31      85.651  99.094 104.994  1.00118.56           O  
ATOM   1997  CB  ASN J  31      87.794  98.603 102.637  1.00118.56           C  
ATOM   1998  CG  ASN J  31      88.755  98.832 103.747  1.00118.56           C  
ATOM   1999  OD1 ASN J  31      88.426  99.488 104.722  1.00118.56           O  
ATOM   2000  ND2 ASN J  31      89.962  98.328 103.602  1.00118.56           N  
ATOM   2001  N   VAL J  32      84.802  97.824 103.350  1.00120.03           N  
ATOM   2002  CA  VAL J  32      84.052  96.992 104.280  1.00120.03           C  
ATOM   2003  C   VAL J  32      84.820  95.721 104.614  1.00120.03           C  
ATOM   2004  O   VAL J  32      85.117  95.451 105.781  1.00120.03           O  
ATOM   2005  CB  VAL J  32      82.647  96.697 103.725  1.00120.03           C  
ATOM   2006  CG1 VAL J  32      81.921  95.750 104.616  1.00120.03           C  
ATOM   2007  CG2 VAL J  32      81.848  97.982 103.641  1.00120.03           C  
ATOM   2008  N   GLY J  33      85.172  94.937 103.611  1.00119.02           N  
ATOM   2009  CA  GLY J  33      85.730  93.630 103.867  1.00119.02           C  
ATOM   2010  C   GLY J  33      87.177  93.667 104.303  1.00119.02           C  
ATOM   2011  O   GLY J  33      87.690  94.665 104.803  1.00119.02           O  
ATOM   2012  N   SER J  34      87.839  92.534 104.101  1.00120.00           N  
ATOM   2013  CA  SER J  34      89.210  92.374 104.555  1.00120.00           C  
ATOM   2014  C   SER J  34      90.179  93.027 103.585  1.00120.00           C  
ATOM   2015  O   SER J  34      89.839  93.304 102.434  1.00120.00           O  
ATOM   2016  CB  SER J  34      89.550  90.897 104.689  1.00120.00           C  
ATOM   2017  OG  SER J  34      89.978  90.385 103.440  1.00120.00           O  
ATOM   2018  N   ASN J  35      91.397  93.255 104.056  1.00111.49           N  
ATOM   2019  CA  ASN J  35      92.481  93.810 103.265  1.00111.49           C  
ATOM   2020  C   ASN J  35      93.806  93.267 103.776  1.00111.49           C  
ATOM   2021  O   ASN J  35      93.852  92.300 104.538  1.00111.49           O  
ATOM   2022  CB  ASN J  35      92.460  95.331 103.319  1.00111.49           C  
ATOM   2023  CG  ASN J  35      91.229  95.898 102.703  1.00111.49           C  
ATOM   2024  OD1 ASN J  35      90.265  96.211 103.397  1.00111.49           O  
ATOM   2025  ND2 ASN J  35      91.238  96.034 101.388  1.00111.49           N  
ATOM   2026  N   THR J  36      94.882  93.913 103.356  1.00 98.22           N  
ATOM   2027  CA  THR J  36      96.217  93.548 103.782  1.00 98.22           C  
ATOM   2028  C   THR J  36      97.200  94.537 103.209  1.00 98.22           C  
ATOM   2029  O   THR J  36      97.096  94.919 102.055  1.00 98.22           O  
ATOM   2030  CB  THR J  36      96.593  92.141 103.330  1.00 98.22           C  
ATOM   2031  OG1 THR J  36      95.889  91.191 104.138  1.00 98.22           O  
ATOM   2032  CG2 THR J  36      98.080  91.908 103.474  1.00 98.22           C  
HETATM 2033  N   TYC J  37      98.152  94.964 104.018  1.00 91.67           N  
HETATM 2034  CA  TYC J  37      99.162  95.901 103.539  1.00 91.67           C  
HETATM 2035  C   TYC J  37     100.505  95.326 103.822  1.00 91.67           C  
HETATM 2036  O   TYC J  37     101.370  96.045 104.279  1.00 91.67           O  
HETATM 2037  CB  TYC J  37      98.987  97.247 104.209  1.00 91.67           C  
HETATM 2038  CG  TYC J  37      97.644  97.802 103.815  1.00 91.67           C  
HETATM 2039  CD1 TYC J  37      96.524  97.526 104.573  1.00 91.67           C  
HETATM 2040  CD2 TYC J  37      97.529  98.598 102.696  1.00 91.67           C  
HETATM 2041  CE1 TYC J  37      95.290  98.040 104.213  1.00 91.67           C  
HETATM 2042  CE2 TYC J  37      96.295  99.110 102.337  1.00 91.67           C  
HETATM 2043  OH  TYC J  37      93.969  99.341 102.740  1.00 91.67           O  
HETATM 2044  CZ  TYC J  37      95.177  98.835 103.094  1.00 91.67           C  
HETATM 2045  NXT TYC J  37     100.706  94.040 103.562  1.00 91.67           N  
TER    2046      TYC J  37                                                      
ATOM   2047  N   ALA L  13      81.119 107.886  97.424  1.00135.77           N  
ATOM   2048  CA  ALA L  13      82.536 108.020  97.734  1.00135.77           C  
ATOM   2049  C   ALA L  13      83.173 109.121  96.897  1.00135.77           C  
ATOM   2050  O   ALA L  13      83.248 109.019  95.675  1.00135.77           O  
ATOM   2051  CB  ALA L  13      83.247 106.707  97.510  1.00135.77           C  
ATOM   2052  N   ASN L  14      83.629 110.176  97.562  1.00136.16           N  
ATOM   2053  CA  ASN L  14      84.197 111.338  96.895  1.00136.16           C  
ATOM   2054  C   ASN L  14      85.710 111.310  97.025  1.00136.16           C  
ATOM   2055  O   ASN L  14      86.236 111.331  98.138  1.00136.16           O  
ATOM   2056  CB  ASN L  14      83.646 112.628  97.499  1.00136.16           C  
ATOM   2057  CG  ASN L  14      82.133 112.670  97.499  1.00136.16           C  
ATOM   2058  OD1 ASN L  14      81.488 112.114  96.611  1.00136.16           O  
ATOM   2059  ND2 ASN L  14      81.557 113.334  98.492  1.00136.16           N  
ATOM   2060  N   PHE L  15      86.406 111.279  95.890  1.00134.40           N  
ATOM   2061  CA  PHE L  15      87.865 111.193  95.873  1.00134.40           C  
ATOM   2062  C   PHE L  15      88.399 112.295  94.976  1.00134.40           C  
ATOM   2063  O   PHE L  15      88.143 112.292  93.769  1.00134.40           O  
ATOM   2064  CB  PHE L  15      88.342 109.838  95.360  1.00134.40           C  
ATOM   2065  CG  PHE L  15      88.137 108.715  96.312  1.00134.40           C  
ATOM   2066  CD1 PHE L  15      86.875 108.343  96.709  1.00134.40           C  
ATOM   2067  CD2 PHE L  15      89.206 108.001  96.777  1.00134.40           C  
ATOM   2068  CE1 PHE L  15      86.694 107.304  97.571  1.00134.40           C  
ATOM   2069  CE2 PHE L  15      89.031 106.962  97.631  1.00134.40           C  
ATOM   2070  CZ  PHE L  15      87.774 106.616  98.034  1.00134.40           C  
ATOM   2071  N   LEU L  16      89.149 113.223  95.550  1.00129.38           N  
ATOM   2072  CA  LEU L  16      89.873 114.212  94.770  1.00129.38           C  
ATOM   2073  C   LEU L  16      91.288 114.291  95.307  1.00129.38           C  
ATOM   2074  O   LEU L  16      91.488 114.396  96.519  1.00129.38           O  
ATOM   2075  CB  LEU L  16      89.202 115.583  94.830  1.00129.38           C  
ATOM   2076  CG  LEU L  16      89.684 116.581  93.774  1.00129.38           C  
ATOM   2077  CD1 LEU L  16      88.558 117.520  93.402  1.00129.38           C  
ATOM   2078  CD2 LEU L  16      90.901 117.376  94.231  1.00129.38           C  
ATOM   2079  N   VAL L  17      92.264 114.244  94.410  1.00125.48           N  
ATOM   2080  CA  VAL L  17      93.666 114.311  94.784  1.00125.48           C  
ATOM   2081  C   VAL L  17      94.326 115.372  93.927  1.00125.48           C  
ATOM   2082  O   VAL L  17      94.208 115.342  92.699  1.00125.48           O  
ATOM   2083  CB  VAL L  17      94.375 112.965  94.606  1.00125.48           C  
ATOM   2084  CG1 VAL L  17      95.854 113.143  94.802  1.00125.48           C  
ATOM   2085  CG2 VAL L  17      93.827 111.955  95.583  1.00125.48           C  
ATOM   2086  N   HIS L  18      95.016 116.305  94.568  1.00123.75           N  
ATOM   2087  CA  HIS L  18      95.671 117.412  93.884  1.00123.75           C  
ATOM   2088  C   HIS L  18      97.097 117.464  94.417  1.00123.75           C  
ATOM   2089  O   HIS L  18      97.386 118.193  95.366  1.00123.75           O  
ATOM   2090  CB  HIS L  18      94.902 118.703  94.120  1.00123.75           C  
ATOM   2091  CG  HIS L  18      95.647 119.940  93.734  1.00123.75           C  
ATOM   2092  ND1 HIS L  18      95.275 121.191  94.173  1.00123.75           N  
ATOM   2093  CD2 HIS L  18      96.735 120.122  92.950  1.00123.75           C  
ATOM   2094  CE1 HIS L  18      96.108 122.091  93.682  1.00123.75           C  
ATOM   2095  NE2 HIS L  18      97.002 121.469  92.937  1.00123.75           N  
ATOM   2096  N   SER L  19      97.984 116.691  93.807  1.00120.42           N  
ATOM   2097  CA  SER L  19      99.362 116.604  94.258  1.00120.42           C  
ATOM   2098  C   SER L  19     100.239 117.591  93.509  1.00120.42           C  
ATOM   2099  O   SER L  19      99.855 118.141  92.479  1.00120.42           O  
ATOM   2100  CB  SER L  19      99.906 115.197  94.063  1.00120.42           C  
ATOM   2101  OG  SER L  19     101.319 115.220  94.098  1.00120.42           O  
ATOM   2102  N   SER L  20     101.434 117.819  94.047  1.00116.47           N  
ATOM   2103  CA  SER L  20     102.414 118.669  93.381  1.00116.47           C  
ATOM   2104  C   SER L  20     103.678 117.908  93.011  1.00116.47           C  
ATOM   2105  O   SER L  20     104.040 117.868  91.833  1.00116.47           O  
ATOM   2106  CB  SER L  20     102.762 119.866  94.263  1.00116.47           C  
ATOM   2107  OG  SER L  20     103.808 119.528  95.150  1.00116.47           O  
ATOM   2108  N   ASN L  21     104.362 117.301  93.979  1.00112.35           N  
ATOM   2109  CA  ASN L  21     105.564 116.505  93.734  1.00112.35           C  
ATOM   2110  C   ASN L  21     105.374 115.220  94.515  1.00112.35           C  
ATOM   2111  O   ASN L  21     105.797 115.121  95.666  1.00112.35           O  
ATOM   2112  CB  ASN L  21     106.817 117.221  94.168  1.00112.35           C  
ATOM   2113  CG  ASN L  21     106.905 118.611  93.624  1.00112.35           C  
ATOM   2114  OD1 ASN L  21     106.531 118.868  92.484  1.00112.35           O  
ATOM   2115  ND2 ASN L  21     107.412 119.527  94.437  1.00112.35           N  
ATOM   2116  N   ASN L  22     104.755 114.229  93.888  1.00110.12           N  
ATOM   2117  CA  ASN L  22     104.258 113.100  94.656  1.00110.12           C  
ATOM   2118  C   ASN L  22     105.391 112.224  95.173  1.00110.12           C  
ATOM   2119  O   ASN L  22     105.469 111.948  96.374  1.00110.12           O  
ATOM   2120  CB  ASN L  22     103.289 112.292  93.815  1.00110.12           C  
ATOM   2121  CG  ASN L  22     102.719 111.147  94.570  1.00110.12           C  
ATOM   2122  OD1 ASN L  22     102.701 111.149  95.792  1.00110.12           O  
ATOM   2123  ND2 ASN L  22     102.253 110.144  93.855  1.00110.12           N  
ATOM   2124  N   PHE L  23     106.252 111.744  94.275  1.00109.96           N  
ATOM   2125  CA  PHE L  23     107.380 110.873  94.608  1.00109.96           C  
ATOM   2126  C   PHE L  23     106.979 109.479  95.055  1.00109.96           C  
ATOM   2127  O   PHE L  23     107.851 108.659  95.352  1.00109.96           O  
ATOM   2128  CB  PHE L  23     108.200 111.411  95.777  1.00109.96           C  
ATOM   2129  CG  PHE L  23     109.268 112.355  95.393  1.00109.96           C  
ATOM   2130  CD1 PHE L  23     110.258 111.969  94.535  1.00109.96           C  
ATOM   2131  CD2 PHE L  23     109.329 113.605  95.959  1.00109.96           C  
ATOM   2132  CE1 PHE L  23     111.255 112.832  94.204  1.00109.96           C  
ATOM   2133  CE2 PHE L  23     110.329 114.467  95.635  1.00109.96           C  
ATOM   2134  CZ  PHE L  23     111.293 114.082  94.758  1.00109.96           C  
ATOM   2135  N   GLY L  24     105.691 109.182  95.111  1.00106.61           N  
ATOM   2136  CA  GLY L  24     105.299 107.962  95.774  1.00106.61           C  
ATOM   2137  C   GLY L  24     103.840 107.643  95.571  1.00106.61           C  
ATOM   2138  O   GLY L  24     103.116 108.352  94.877  1.00106.61           O  
ATOM   2139  N   ALA L  25     103.415 106.559  96.200  1.00106.38           N  
ATOM   2140  CA  ALA L  25     102.090 106.023  95.945  1.00106.38           C  
ATOM   2141  C   ALA L  25     101.029 106.931  96.536  1.00106.38           C  
ATOM   2142  O   ALA L  25     101.005 107.157  97.747  1.00106.38           O  
ATOM   2143  CB  ALA L  25     101.972 104.622  96.532  1.00106.38           C  
ATOM   2144  N   ILE L  26     100.164 107.465  95.688  1.00108.54           N  
ATOM   2145  CA  ILE L  26      98.896 108.026  96.130  1.00108.54           C  
ATOM   2146  C   ILE L  26      97.876 106.939  95.835  1.00108.54           C  
ATOM   2147  O   ILE L  26      97.225 106.932  94.796  1.00108.54           O  
ATOM   2148  CB  ILE L  26      98.568 109.332  95.424  1.00108.54           C  
ATOM   2149  CG1 ILE L  26      99.644 110.362  95.710  1.00108.54           C  
ATOM   2150  CG2 ILE L  26      97.240 109.857  95.890  1.00108.54           C  
ATOM   2151  CD1 ILE L  26      99.377 111.692  95.071  1.00108.54           C  
ATOM   2152  N   LEU L  27      97.719 106.015  96.767  1.00109.68           N  
ATOM   2153  CA  LEU L  27      96.952 104.814  96.473  1.00109.68           C  
ATOM   2154  C   LEU L  27      95.479 105.036  96.766  1.00109.68           C  
ATOM   2155  O   LEU L  27      94.860 104.340  97.557  1.00109.68           O  
ATOM   2156  CB  LEU L  27      97.511 103.645  97.270  1.00109.68           C  
ATOM   2157  CG  LEU L  27      97.248 102.225  96.774  1.00109.68           C  
ATOM   2158  CD1 LEU L  27      98.394 101.365  97.238  1.00109.68           C  
ATOM   2159  CD2 LEU L  27      95.932 101.631  97.238  1.00109.68           C  
ATOM   2160  N   SER L  28      94.904 106.043  96.136  1.00115.90           N  
ATOM   2161  CA  SER L  28      93.509 106.364  96.385  1.00115.90           C  
ATOM   2162  C   SER L  28      92.639 105.282  95.763  1.00115.90           C  
ATOM   2163  O   SER L  28      92.589 105.152  94.539  1.00115.90           O  
ATOM   2164  CB  SER L  28      93.196 107.738  95.808  1.00115.90           C  
ATOM   2165  OG  SER L  28      91.982 108.233  96.317  1.00115.90           O  
ATOM   2166  N   SER L  29      91.953 104.495  96.588  1.00128.46           N  
ATOM   2167  CA  SER L  29      91.263 103.320  96.076  1.00128.46           C  
ATOM   2168  C   SER L  29      89.995 103.063  96.871  1.00128.46           C  
ATOM   2169  O   SER L  29      89.669 103.787  97.812  1.00128.46           O  
ATOM   2170  CB  SER L  29      92.157 102.086  96.132  1.00128.46           C  
ATOM   2171  OG  SER L  29      92.475 101.762  97.469  1.00128.46           O  
ATOM   2172  N   THR L  30      89.276 102.013  96.471  1.00136.92           N  
ATOM   2173  CA  THR L  30      88.060 101.571  97.148  1.00136.92           C  
ATOM   2174  C   THR L  30      87.703 100.186  96.635  1.00136.92           C  
ATOM   2175  O   THR L  30      87.884  99.903  95.449  1.00136.92           O  
ATOM   2176  CB  THR L  30      86.889 102.525  96.909  1.00136.92           C  
ATOM   2177  OG1 THR L  30      87.275 103.856  97.252  1.00136.92           O  
ATOM   2178  CG2 THR L  30      85.697 102.132  97.763  1.00136.92           C  
ATOM   2179  N   ASN L  31      87.177  99.337  97.517  1.00129.95           N  
ATOM   2180  CA  ASN L  31      86.932  97.947  97.159  1.00129.95           C  
ATOM   2181  C   ASN L  31      86.053  97.225  98.161  1.00129.95           C  
ATOM   2182  O   ASN L  31      86.028  97.574  99.340  1.00129.95           O  
ATOM   2183  CB  ASN L  31      88.254  97.210  97.038  1.00129.95           C  
ATOM   2184  CG  ASN L  31      89.171  97.524  98.165  1.00129.95           C  
ATOM   2185  OD1 ASN L  31      88.772  98.168  99.122  1.00129.95           O  
ATOM   2186  ND2 ASN L  31      90.415  97.108  98.054  1.00129.95           N  
ATOM   2187  N   VAL L  32      85.311  96.224  97.697  1.00134.95           N  
ATOM   2188  CA  VAL L  32      84.603  95.352  98.624  1.00134.95           C  
ATOM   2189  C   VAL L  32      85.454  94.145  98.993  1.00134.95           C  
ATOM   2190  O   VAL L  32      85.743  93.914 100.170  1.00134.95           O  
ATOM   2191  CB  VAL L  32      83.237  94.948  98.043  1.00134.95           C  
ATOM   2192  CG1 VAL L  32      82.563  93.961  98.934  1.00134.95           C  
ATOM   2193  CG2 VAL L  32      82.348  96.168  97.924  1.00134.95           C  
ATOM   2194  N   GLY L  33      85.885  93.375  98.010  1.00135.88           N  
ATOM   2195  CA  GLY L  33      86.532  92.117  98.299  1.00135.88           C  
ATOM   2196  C   GLY L  33      87.961  92.265  98.765  1.00135.88           C  
ATOM   2197  O   GLY L  33      88.388  93.305  99.261  1.00135.88           O  
ATOM   2198  N   SER L  34      88.708  91.181  98.595  1.00135.14           N  
ATOM   2199  CA  SER L  34      90.078  91.129  99.080  1.00135.14           C  
ATOM   2200  C   SER L  34      91.018  91.837  98.122  1.00135.14           C  
ATOM   2201  O   SER L  34      90.684  92.072  96.960  1.00135.14           O  
ATOM   2202  CB  SER L  34      90.521  89.683  99.244  1.00135.14           C  
ATOM   2203  OG  SER L  34      91.014  89.186  98.013  1.00135.14           O  
ATOM   2204  N   ASN L  35      92.205  92.160  98.616  1.00124.19           N  
ATOM   2205  CA  ASN L  35      93.263  92.783  97.840  1.00124.19           C  
ATOM   2206  C   ASN L  35      94.612  92.345  98.388  1.00124.19           C  
ATOM   2207  O   ASN L  35      94.711  91.395  99.166  1.00124.19           O  
ATOM   2208  CB  ASN L  35      93.130  94.299  97.872  1.00124.19           C  
ATOM   2209  CG  ASN L  35      91.874  94.765  97.220  1.00124.19           C  
ATOM   2210  OD1 ASN L  35      90.875  95.016  97.888  1.00124.19           O  
ATOM   2211  ND2 ASN L  35      91.904  94.884  95.903  1.00124.19           N  
ATOM   2212  N   THR L  36      95.648  93.062  97.982  1.00110.76           N  
ATOM   2213  CA  THR L  36      96.996  92.802  98.442  1.00110.76           C  
ATOM   2214  C   THR L  36      97.916  93.852  97.876  1.00110.76           C  
ATOM   2215  O   THR L  36      97.811  94.210  96.714  1.00110.76           O  
ATOM   2216  CB  THR L  36      97.482  91.420  98.021  1.00110.76           C  
ATOM   2217  OG1 THR L  36      96.831  90.432  98.826  1.00110.76           O  
ATOM   2218  CG2 THR L  36      98.979  91.298  98.200  1.00110.76           C  
HETATM 2219  N   TYC L  37      98.816  94.359  98.699  1.00100.81           N  
HETATM 2220  CA  TYC L  37      99.766  95.361  98.227  1.00100.81           C  
HETATM 2221  C   TYC L  37     101.140  94.890  98.549  1.00100.81           C  
HETATM 2222  O   TYC L  37     101.939  95.676  99.013  1.00100.81           O  
HETATM 2223  CB  TYC L  37      99.478  96.699  98.873  1.00100.81           C  
HETATM 2224  CG  TYC L  37      98.107  97.149  98.441  1.00100.81           C  
HETATM 2225  CD1 TYC L  37      96.994  96.802  99.179  1.00100.81           C  
HETATM 2226  CD2 TYC L  37      97.959  97.918  97.308  1.00100.81           C  
HETATM 2227  CE1 TYC L  37      95.734  97.219  98.785  1.00100.81           C  
HETATM 2228  CE2 TYC L  37      96.702  98.334  96.915  1.00100.81           C  
HETATM 2229  OH  TYC L  37      94.355  98.399  97.264  1.00100.81           O  
HETATM 2230  CZ  TYC L  37      95.588  97.989  97.651  1.00100.81           C  
HETATM 2231  NXT TYC L  37     101.440  93.618  98.313  1.00100.81           N  
TER    2232      TYC L  37                                                      
CONECT  168  173                                                                
CONECT  173  168  174                                                           
CONECT  174  173  175  177                                                      
CONECT  175  174  176  185                                                      
CONECT  176  175                                                                
CONECT  177  174  178                                                           
CONECT  178  177  179  180                                                      
CONECT  179  178  181                                                           
CONECT  180  178  182                                                           
CONECT  181  179  184                                                           
CONECT  182  180  184                                                           
CONECT  183  184                                                                
CONECT  184  181  182  183                                                      
CONECT  185  175                                                                
CONECT  354  359                                                                
CONECT  359  354  360                                                           
CONECT  360  359  361  363                                                      
CONECT  361  360  362  371                                                      
CONECT  362  361                                                                
CONECT  363  360  364                                                           
CONECT  364  363  365  366                                                      
CONECT  365  364  367                                                           
CONECT  366  364  368                                                           
CONECT  367  365  370                                                           
CONECT  368  366  370                                                           
CONECT  369  370                                                                
CONECT  370  367  368  369                                                      
CONECT  371  361                                                                
CONECT  540  545                                                                
CONECT  545  540  546                                                           
CONECT  546  545  547  549                                                      
CONECT  547  546  548  557                                                      
CONECT  548  547                                                                
CONECT  549  546  550                                                           
CONECT  550  549  551  552                                                      
CONECT  551  550  553                                                           
CONECT  552  550  554                                                           
CONECT  553  551  556                                                           
CONECT  554  552  556                                                           
CONECT  555  556                                                                
CONECT  556  553  554  555                                                      
CONECT  557  547                                                                
CONECT  726  731                                                                
CONECT  731  726  732                                                           
CONECT  732  731  733  735                                                      
CONECT  733  732  734  743                                                      
CONECT  734  733                                                                
CONECT  735  732  736                                                           
CONECT  736  735  737  738                                                      
CONECT  737  736  739                                                           
CONECT  738  736  740                                                           
CONECT  739  737  742                                                           
CONECT  740  738  742                                                           
CONECT  741  742                                                                
CONECT  742  739  740  741                                                      
CONECT  743  733                                                                
CONECT  912  917                                                                
CONECT  917  912  918                                                           
CONECT  918  917  919  921                                                      
CONECT  919  918  920  929                                                      
CONECT  920  919                                                                
CONECT  921  918  922                                                           
CONECT  922  921  923  924                                                      
CONECT  923  922  925                                                           
CONECT  924  922  926                                                           
CONECT  925  923  928                                                           
CONECT  926  924  928                                                           
CONECT  927  928                                                                
CONECT  928  925  926  927                                                      
CONECT  929  919                                                                
CONECT 1098 1103                                                                
CONECT 1103 1098 1104                                                           
CONECT 1104 1103 1105 1107                                                      
CONECT 1105 1104 1106 1115                                                      
CONECT 1106 1105                                                                
CONECT 1107 1104 1108                                                           
CONECT 1108 1107 1109 1110                                                      
CONECT 1109 1108 1111                                                           
CONECT 1110 1108 1112                                                           
CONECT 1111 1109 1114                                                           
CONECT 1112 1110 1114                                                           
CONECT 1113 1114                                                                
CONECT 1114 1111 1112 1113                                                      
CONECT 1115 1105                                                                
CONECT 1284 1289                                                                
CONECT 1289 1284 1290                                                           
CONECT 1290 1289 1291 1293                                                      
CONECT 1291 1290 1292 1301                                                      
CONECT 1292 1291                                                                
CONECT 1293 1290 1294                                                           
CONECT 1294 1293 1295 1296                                                      
CONECT 1295 1294 1297                                                           
CONECT 1296 1294 1298                                                           
CONECT 1297 1295 1300                                                           
CONECT 1298 1296 1300                                                           
CONECT 1299 1300                                                                
CONECT 1300 1297 1298 1299                                                      
CONECT 1301 1291                                                                
CONECT 1470 1475                                                                
CONECT 1475 1470 1476                                                           
CONECT 1476 1475 1477 1479                                                      
CONECT 1477 1476 1478 1487                                                      
CONECT 1478 1477                                                                
CONECT 1479 1476 1480                                                           
CONECT 1480 1479 1481 1482                                                      
CONECT 1481 1480 1483                                                           
CONECT 1482 1480 1484                                                           
CONECT 1483 1481 1486                                                           
CONECT 1484 1482 1486                                                           
CONECT 1485 1486                                                                
CONECT 1486 1483 1484 1485                                                      
CONECT 1487 1477                                                                
CONECT 1656 1661                                                                
CONECT 1661 1656 1662                                                           
CONECT 1662 1661 1663 1665                                                      
CONECT 1663 1662 1664 1673                                                      
CONECT 1664 1663                                                                
CONECT 1665 1662 1666                                                           
CONECT 1666 1665 1667 1668                                                      
CONECT 1667 1666 1669                                                           
CONECT 1668 1666 1670                                                           
CONECT 1669 1667 1672                                                           
CONECT 1670 1668 1672                                                           
CONECT 1671 1672                                                                
CONECT 1672 1669 1670 1671                                                      
CONECT 1673 1663                                                                
CONECT 1842 1847                                                                
CONECT 1847 1842 1848                                                           
CONECT 1848 1847 1849 1851                                                      
CONECT 1849 1848 1850 1859                                                      
CONECT 1850 1849                                                                
CONECT 1851 1848 1852                                                           
CONECT 1852 1851 1853 1854                                                      
CONECT 1853 1852 1855                                                           
CONECT 1854 1852 1856                                                           
CONECT 1855 1853 1858                                                           
CONECT 1856 1854 1858                                                           
CONECT 1857 1858                                                                
CONECT 1858 1855 1856 1857                                                      
CONECT 1859 1849                                                                
CONECT 2028 2033                                                                
CONECT 2033 2028 2034                                                           
CONECT 2034 2033 2035 2037                                                      
CONECT 2035 2034 2036 2045                                                      
CONECT 2036 2035                                                                
CONECT 2037 2034 2038                                                           
CONECT 2038 2037 2039 2040                                                      
CONECT 2039 2038 2041                                                           
CONECT 2040 2038 2042                                                           
CONECT 2041 2039 2044                                                           
CONECT 2042 2040 2044                                                           
CONECT 2043 2044                                                                
CONECT 2044 2041 2042 2043                                                      
CONECT 2045 2035                                                                
CONECT 2214 2219                                                                
CONECT 2219 2214 2220                                                           
CONECT 2220 2219 2221 2223                                                      
CONECT 2221 2220 2222 2231                                                      
CONECT 2222 2221                                                                
CONECT 2223 2220 2224                                                           
CONECT 2224 2223 2225 2226                                                      
CONECT 2225 2224 2227                                                           
CONECT 2226 2224 2228                                                           
CONECT 2227 2225 2230                                                           
CONECT 2228 2226 2230                                                           
CONECT 2229 2230                                                                
CONECT 2230 2227 2228 2229                                                      
CONECT 2231 2221                                                                
MASTER      313    0   12    0   36    0    0    6 2220   12  168   36          
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: October 18th, 2018.