CNRS Nantes University UFIP UFIP
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***  MEMBRANE PROTEIN 03-OCT-98 1BXW  ***

elNémo ID: 19111509481316238

Job options:

ID        	=	 19111509481316238
JOBID     	=	 MEMBRANE PROTEIN 03-OCT-98 1BXW
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    MEMBRANE PROTEIN                        03-OCT-98   1BXW              
TITLE     OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (OUTER MEMBRANE PROTEIN A);                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: TRANSMEMBRANE DOMAIN;                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI BL21(DE3);                     
SOURCE   3 ORGANISM_TAXID: 469008;                                              
SOURCE   4 STRAIN: BL21DE3;                                                     
SOURCE   5 GENE: OMPA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;                                   
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3B-171                                 
KEYWDS    OUTER MEMBRANE, TRANSMEMBRANE PROTEIN, MEMBRANE PROTEIN               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.E.SCHULZ,A.PAUTSCH                                                  
REVDAT   5   14-MAR-18 1BXW    1       SEQADV                                   
REVDAT   4   29-NOV-17 1BXW    1       REMARK                                   
REVDAT   3   24-FEB-09 1BXW    1       VERSN                                    
REVDAT   2   22-DEC-99 1BXW    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   14-OCT-98 1BXW    0                                                
JRNL        AUTH   A.PAUTSCH,G.E.SCHULZ                                         
JRNL        TITL   STRUCTURE OF THE OUTER MEMBRANE PROTEIN A TRANSMEMBRANE      
JRNL        TITL 2 DOMAIN.                                                      
JRNL        REF    NAT.STRUCT.BIOL.              V.   5  1013 1998              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   9808047                                                      
JRNL        DOI    10.1038/2983                                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 8328                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 404                             
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1330                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 39                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.640         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.015 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.030 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  DISORDERED REGIONS ARE FROM GLY22-GLY28, GLY65-GLU68 AND            
REMARK   3   ILE147-PRO147 WERE MODELED STEREOCHEMICALLY                        
REMARK   4                                                                      
REMARK   4 1BXW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE DEPOSITION ID IS D_1000008140.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8328                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.02800                            
REMARK 200   FOR THE DATA SET  : 16.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.11000                            
REMARK 200   FOR SHELL         : 6.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG-8000 10 % MPD 0.05 M            
REMARK 280  POTASSIUM PHOSPHATE PH 5.0                                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       34.59000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.97500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       34.59000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       38.97500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A  31    CG   ND1  CD2  CE1  NE2                             
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     GLY A    22                                                      
REMARK 475     LEU A    23                                                      
REMARK 475     ILE A    24                                                      
REMARK 475     ASN A    25                                                      
REMARK 475     ASN A    26                                                      
REMARK 475     ASN A    27                                                      
REMARK 475     GLY A    28                                                      
REMARK 475     GLY A    65                                                      
REMARK 475     SER A    66                                                      
REMARK 475     VAL A    67                                                      
REMARK 475     GLU A    68                                                      
REMARK 475     ILE A   147                                                      
REMARK 475     GLY A   148                                                      
REMARK 475     ASP A   149                                                      
REMARK 475     ALA A   150                                                      
REMARK 475     HIS A   151                                                      
REMARK 475     THR A   152                                                      
REMARK 475     ILE A   153                                                      
REMARK 475     GLY A   154                                                      
REMARK 475     THR A   155                                                      
REMARK 475     ARG A   156                                                      
REMARK 475     PRO A   157                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   64   CB   CG   CD   CE   NZ                              
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASN A    26     CA   PRO A    29     2556     1.44            
REMARK 500   OD1  ASN A    26     C    PRO A    29     2556     1.68            
REMARK 500   OD1  ASN A    26     N    PRO A    29     2556     1.72            
REMARK 500   OD1  ASN A     5     CD1  ILE A   147     2657     2.03            
REMARK 500   OD1  ASN A    26     O    PRO A    29     2556     2.08            
REMARK 500   CG   ASN A    26     N    PRO A    29     2556     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY A  28   C     PRO A  29   N       0.125                       
REMARK 500    GLY A 148   N     GLY A 148   CA      0.090                       
REMARK 500    ARG A 156   CA    ARG A 156   C       0.206                       
REMARK 500    PRO A 157   N     PRO A 157   CA     -0.251                       
REMARK 500    PRO A 157   CD    PRO A 157   N      -0.368                       
REMARK 500    PRO A 157   CA    PRO A 157   C      -0.164                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A   4   CA  -  C   -  N   ANGL. DEV. =  18.3 DEGREES          
REMARK 500    GLY A  22   O   -  C   -  N   ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ASN A  25   C   -  N   -  CA  ANGL. DEV. = -16.5 DEGREES          
REMARK 500    ASN A  25   CA  -  C   -  N   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ASN A  25   O   -  C   -  N   ANGL. DEV. =  14.8 DEGREES          
REMARK 500    GLY A  28   O   -  C   -  N   ANGL. DEV. = -11.6 DEGREES          
REMARK 500    PRO A  29   C   -  N   -  CA  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    PRO A  29   C   -  N   -  CD  ANGL. DEV. = -18.1 DEGREES          
REMARK 500    ARG A  60   CD  -  NE  -  CZ  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A  60   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A  60   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    GLU A  68   C   -  N   -  CA  ANGL. DEV. = -16.3 DEGREES          
REMARK 500    GLN A  75   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ASP A  90   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    SER A 120   N   -  CA  -  CB  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    VAL A 122   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ILE A 135   CA  -  CB  -  CG2 ANGL. DEV. =  15.6 DEGREES          
REMARK 500    ARG A 138   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ARG A 138   CD  -  NE  -  CZ  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ALA A 150   CA  -  C   -  N   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ALA A 150   O   -  C   -  N   ANGL. DEV. =  17.6 DEGREES          
REMARK 500    HIS A 151   CB  -  CA  -  C   ANGL. DEV. = -38.2 DEGREES          
REMARK 500    HIS A 151   CA  -  C   -  N   ANGL. DEV. = -38.2 DEGREES          
REMARK 500    HIS A 151   O   -  C   -  N   ANGL. DEV. =  43.4 DEGREES          
REMARK 500    THR A 152   C   -  N   -  CA  ANGL. DEV. =  30.0 DEGREES          
REMARK 500    THR A 155   O   -  C   -  N   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    ARG A 156   C   -  N   -  CA  ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ARG A 156   CB  -  CA  -  C   ANGL. DEV. =  12.4 DEGREES          
REMARK 500    ARG A 156   N   -  CA  -  CB  ANGL. DEV. = -15.9 DEGREES          
REMARK 500    ARG A 156   NH1 -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A 156   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    PRO A 157   C   -  N   -  CA  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    PRO A 157   C   -  N   -  CD  ANGL. DEV. = -16.7 DEGREES          
REMARK 500    PRO A 157   CA  -  N   -  CD  ANGL. DEV. = -25.9 DEGREES          
REMARK 500    PRO A 157   N   -  CA  -  CB  ANGL. DEV. = -26.1 DEGREES          
REMARK 500    PRO A 157   CB  -  CG  -  CD  ANGL. DEV. = -25.7 DEGREES          
REMARK 500    PRO A 157   N   -  CD  -  CG  ANGL. DEV. = -34.0 DEGREES          
REMARK 500    PRO A 157   N   -  CA  -  C   ANGL. DEV. =  19.1 DEGREES          
REMARK 500    PRO A 157   CA  -  C   -  O   ANGL. DEV. = -17.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   5       57.62   -113.00                                   
REMARK 500    TYR A  18      120.18    166.90                                   
REMARK 500    ASP A  20     -140.62   -156.38                                   
REMARK 500    LEU A  23      150.39     68.74                                   
REMARK 500    ASN A  25      -90.55     -9.26                                   
REMARK 500    ASN A  26      121.49    -29.94                                   
REMARK 500    HIS A  31      175.58    173.40                                   
REMARK 500    TYR A  63      102.76   -169.58                                   
REMARK 500    SER A  66       52.30    128.49                                   
REMARK 500    VAL A  67       90.53     49.93                                   
REMARK 500    VAL A 110      -72.06    -67.54                                   
REMARK 500    ALA A 150     -164.72    173.09                                   
REMARK 500    HIS A 151      -97.21     35.47                                   
REMARK 500    THR A 152     -139.61   -128.76                                   
REMARK 500    THR A 155     -137.22   -149.83                                   
REMARK 500    ARG A 156     -162.43   -178.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A  156     PRO A  157                 -147.47                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG A 156        -11.76                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 172                 
DBREF  1BXW A    0   171  UNP    P0A910   OMPA_ECOLI      21    192             
SEQADV 1BXW MET A    0  UNP  P0A910    ALA    21 SEE REMARK 999                 
SEQADV 1BXW LEU A   23  UNP  P0A910    PHE    44 ENGINEERED MUTATION            
SEQADV 1BXW LYS A   34  UNP  P0A910    GLN    55 ENGINEERED MUTATION            
SEQADV 1BXW TYR A  107  UNP  P0A910    LYS   128 ENGINEERED MUTATION            
SEQRES   1 A  172  MET ALA PRO LYS ASP ASN THR TRP TYR THR GLY ALA LYS          
SEQRES   2 A  172  LEU GLY TRP SER GLN TYR HIS ASP THR GLY LEU ILE ASN          
SEQRES   3 A  172  ASN ASN GLY PRO THR HIS GLU ASN LYS LEU GLY ALA GLY          
SEQRES   4 A  172  ALA PHE GLY GLY TYR GLN VAL ASN PRO TYR VAL GLY PHE          
SEQRES   5 A  172  GLU MET GLY TYR ASP TRP LEU GLY ARG MET PRO TYR LYS          
SEQRES   6 A  172  GLY SER VAL GLU ASN GLY ALA TYR LYS ALA GLN GLY VAL          
SEQRES   7 A  172  GLN LEU THR ALA LYS LEU GLY TYR PRO ILE THR ASP ASP          
SEQRES   8 A  172  LEU ASP ILE TYR THR ARG LEU GLY GLY MET VAL TRP ARG          
SEQRES   9 A  172  ALA ASP THR TYR SER ASN VAL TYR GLY LYS ASN HIS ASP          
SEQRES  10 A  172  THR GLY VAL SER PRO VAL PHE ALA GLY GLY VAL GLU TYR          
SEQRES  11 A  172  ALA ILE THR PRO GLU ILE ALA THR ARG LEU GLU TYR GLN          
SEQRES  12 A  172  TRP THR ASN ASN ILE GLY ASP ALA HIS THR ILE GLY THR          
SEQRES  13 A  172  ARG PRO ASP ASN GLY MET LEU SER LEU GLY VAL SER TYR          
SEQRES  14 A  172  ARG PHE GLY                                                  
HET    C8E  A 172      21                                                       
HETNAM     C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE                             
FORMUL   2  C8E    C16 H34 O5                                                   
FORMUL   3  HOH   *39(H2 O)                                                     
SHEET    1  S1 1 THR A   6  SER A  16  0                                        
SHEET    1  S2 1 LYS A  34  VAL A  45  0                                        
SHEET    1  S3 1 VAL A  49  ARG A  60  0                                        
SHEET    1  S4 1 TYR A  72  PRO A  86  0                                        
SHEET    1  S5 1 LEU A  91  THR A 106  0                                        
SHEET    1  S6 1 ASN A 114  ALA A 130  0                                        
SHEET    1  S7 1 ILE A 135  TRP A 143  0                                        
SHEET    1  S8 1 MET A 161  PHE A 170  0                                        
LINK         OD2 ASP A 149                 C17 C8E A 172     2657   1555  1.24  
LINK         CB  ASP A 149                 C17 C8E A 172     2657   1555  1.88  
LINK         OD1 ASP A 149                 C17 C8E A 172     2657   1555  1.59  
LINK         OD2 ASP A 149                 O18 C8E A 172     2657   1555  1.96  
LINK         CA  ASP A 149                 O18 C8E A 172     2657   1555  1.92  
LINK         CB  ASP A 149                 O18 C8E A 172     2657   1555  1.18  
LINK         OD1 ASP A 149                 O18 C8E A 172     2657   1555  1.38  
LINK         N   ASP A 149                 C19 C8E A 172     2657   1555  1.68  
LINK         C   ASP A 149                 C19 C8E A 172     2657   1555  1.87  
LINK         CA  ASP A 149                 C20 C8E A 172     2657   1555  1.45  
LINK         C   ASP A 149                 C20 C8E A 172     2657   1555  1.22  
LINK         CB  ASP A 149                 C20 C8E A 172     2657   1555  2.02  
LINK         N   ALA A 150                 O21 C8E A 172     2657   1555  1.70  
LINK         N   ALA A 150                 C20 C8E A 172     2657   1555  1.34  
SITE     1 AC1  4 TYR A  43  PHE A  51  LEU A  79  GLY A  99                    
CRYST1   69.180   77.950   50.930  90.00  91.52  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014455  0.000000  0.000383        0.00000                         
SCALE2      0.000000  0.012829  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019642        0.00000                         
ATOM      1  N   MET A   0      44.836   7.751  38.125  0.60 47.07           N  
ATOM      2  CA  MET A   0      45.979   8.712  38.058  0.60 53.70           C  
ATOM      3  C   MET A   0      45.533  10.128  38.396  0.60 51.48           C  
ATOM      4  O   MET A   0      45.577  11.014  37.548  0.60 51.38           O  
ATOM      5  CB  MET A   0      46.684   8.718  36.701  0.60 67.99           C  
ATOM      6  CG  MET A   0      48.180   8.952  36.789  1.00 82.64           C  
ATOM      7  SD  MET A   0      48.817  10.199  35.659  1.00 96.24           S  
ATOM      8  CE  MET A   0      50.504  10.376  36.322  1.00 96.86           C  
ATOM      9  N   ALA A   1      45.254  10.379  39.672  1.00 50.76           N  
ATOM     10  CA  ALA A   1      44.838  11.712  40.084  1.00 53.13           C  
ATOM     11  C   ALA A   1      46.036  12.651  40.029  1.00 51.14           C  
ATOM     12  O   ALA A   1      47.195  12.259  40.003  1.00 53.33           O  
ATOM     13  CB  ALA A   1      44.229  11.697  41.473  1.00 53.91           C  
ATOM     14  N   PRO A   2      45.736  13.936  40.024  1.00 49.63           N  
ATOM     15  CA  PRO A   2      46.822  14.919  40.021  1.00 51.58           C  
ATOM     16  C   PRO A   2      47.754  14.618  41.197  1.00 56.34           C  
ATOM     17  O   PRO A   2      47.328  14.035  42.194  1.00 54.38           O  
ATOM     18  CB  PRO A   2      46.081  16.238  40.142  1.00 45.83           C  
ATOM     19  CG  PRO A   2      44.708  15.943  39.588  1.00 44.84           C  
ATOM     20  CD  PRO A   2      44.381  14.536  40.054  1.00 41.42           C  
ATOM     21  N   LYS A   3      49.028  14.969  41.121  1.00 59.06           N  
ATOM     22  CA  LYS A   3      50.040  14.820  42.121  1.00 57.46           C  
ATOM     23  C   LYS A   3      49.699  15.590  43.397  1.00 58.47           C  
ATOM     24  O   LYS A   3      49.028  16.621  43.351  1.00 56.51           O  
ATOM     25  CB  LYS A   3      51.427  15.295  41.615  1.00 61.97           C  
ATOM     26  CG  LYS A   3      52.164  14.085  41.004  1.00 73.82           C  
ATOM     27  CD  LYS A   3      53.504  14.483  40.423  1.00 84.53           C  
ATOM     28  CE  LYS A   3      53.912  13.607  39.255  1.00 89.35           C  
ATOM     29  NZ  LYS A   3      53.599  14.169  37.911  1.00 87.78           N  
ATOM     30  N   ASP A   4      50.217  15.122  44.529  1.00 56.14           N  
ATOM     31  CA  ASP A   4      49.945  15.676  45.802  1.00 54.53           C  
ATOM     32  C   ASP A   4      49.830  17.133  46.003  1.00 53.35           C  
ATOM     33  O   ASP A   4      48.638  17.428  46.449  1.00 66.58           O  
ATOM     34  CB  ASP A   4      50.678  15.018  46.976  1.00 57.39           C  
ATOM     35  CG  ASP A   4      50.130  13.656  47.321  1.00 53.28           C  
ATOM     36  OD1 ASP A   4      49.300  13.075  46.604  1.00 53.00           O  
ATOM     37  OD2 ASP A   4      50.573  13.132  48.365  1.00 61.41           O  
ATOM     38  N   ASN A   5      50.643  18.144  45.942  1.00 48.24           N  
ATOM     39  CA  ASN A   5      49.996  19.460  46.363  1.00 51.62           C  
ATOM     40  C   ASN A   5      49.901  20.365  45.178  1.00 55.33           C  
ATOM     41  O   ASN A   5      50.441  21.481  45.185  1.00 56.19           O  
ATOM     42  CB  ASN A   5      50.703  20.044  47.569  1.00 61.34           C  
ATOM     43  CG  ASN A   5      50.415  19.146  48.790  1.00 73.93           C  
ATOM     44  OD1 ASN A   5      51.132  18.154  49.011  1.00 71.46           O  
ATOM     45  ND2 ASN A   5      49.356  19.472  49.529  1.00 71.85           N  
ATOM     46  N   THR A   6      49.209  19.846  44.141  1.00 53.19           N  
ATOM     47  CA  THR A   6      49.085  20.561  42.879  1.00 48.54           C  
ATOM     48  C   THR A   6      47.691  20.983  42.467  1.00 44.32           C  
ATOM     49  O   THR A   6      46.643  20.564  42.940  1.00 42.08           O  
ATOM     50  CB  THR A   6      49.721  19.712  41.756  1.00 48.93           C  
ATOM     51  OG1 THR A   6      49.169  18.408  41.759  1.00 43.82           O  
ATOM     52  CG2 THR A   6      51.235  19.552  42.019  1.00 52.54           C  
ATOM     53  N   TRP A   7      47.677  21.898  41.517  1.00 44.80           N  
ATOM     54  CA  TRP A   7      46.536  22.502  40.923  1.00 44.13           C  
ATOM     55  C   TRP A   7      46.236  21.965  39.521  1.00 43.83           C  
ATOM     56  O   TRP A   7      47.146  21.481  38.865  1.00 37.53           O  
ATOM     57  CB  TRP A   7      46.742  24.022  40.752  1.00 46.15           C  
ATOM     58  CG  TRP A   7      47.049  24.660  42.073  1.00 60.76           C  
ATOM     59  CD1 TRP A   7      48.257  24.726  42.716  1.00 59.66           C  
ATOM     60  CD2 TRP A   7      46.090  25.311  42.917  1.00 59.96           C  
ATOM     61  NE1 TRP A   7      48.095  25.387  43.910  1.00 61.88           N  
ATOM     62  CE2 TRP A   7      46.786  25.755  44.059  1.00 63.80           C  
ATOM     63  CE3 TRP A   7      44.717  25.542  42.809  1.00 58.23           C  
ATOM     64  CZ2 TRP A   7      46.148  26.439  45.089  1.00 66.14           C  
ATOM     65  CZ3 TRP A   7      44.082  26.219  43.821  1.00 61.96           C  
ATOM     66  CH2 TRP A   7      44.798  26.667  44.950  1.00 68.79           C  
ATOM     67  N   TYR A   8      44.962  22.168  39.147  1.00 37.43           N  
ATOM     68  CA  TYR A   8      44.537  21.833  37.797  1.00 38.16           C  
ATOM     69  C   TYR A   8      43.414  22.796  37.383  1.00 39.41           C  
ATOM     70  O   TYR A   8      42.822  23.474  38.236  1.00 36.77           O  
ATOM     71  CB  TYR A   8      44.135  20.383  37.723  1.00 31.51           C  
ATOM     72  CG  TYR A   8      43.014  19.992  38.669  1.00 37.37           C  
ATOM     73  CD1 TYR A   8      43.337  19.602  39.977  1.00 36.75           C  
ATOM     74  CD2 TYR A   8      41.666  19.976  38.287  1.00 24.76           C  
ATOM     75  CE1 TYR A   8      42.343  19.198  40.845  1.00 34.22           C  
ATOM     76  CE2 TYR A   8      40.674  19.602  39.162  1.00 24.69           C  
ATOM     77  CZ  TYR A   8      41.026  19.209  40.450  1.00 32.23           C  
ATOM     78  OH  TYR A   8      40.074  18.817  41.362  1.00 35.82           O  
ATOM     79  N   THR A   9      43.123  22.866  36.099  1.00 34.79           N  
ATOM     80  CA  THR A   9      42.053  23.652  35.534  1.00 38.87           C  
ATOM     81  C   THR A   9      41.452  22.844  34.357  1.00 33.99           C  
ATOM     82  O   THR A   9      42.140  22.052  33.732  1.00 30.96           O  
ATOM     83  CB  THR A   9      42.392  25.034  34.908  1.00 38.16           C  
ATOM     84  OG1 THR A   9      43.443  24.870  33.937  1.00 41.10           O  
ATOM     85  CG2 THR A   9      42.803  26.033  35.937  1.00 50.29           C  
ATOM     86  N   GLY A  10      40.220  23.151  34.023  1.00 30.77           N  
ATOM     87  CA  GLY A  10      39.560  22.551  32.901  1.00 30.93           C  
ATOM     88  C   GLY A  10      38.312  23.283  32.434  1.00 29.68           C  
ATOM     89  O   GLY A  10      37.832  24.259  32.998  1.00 27.19           O  
ATOM     90  N   ALA A  11      37.719  22.693  31.388  1.00 25.71           N  
ATOM     91  CA  ALA A  11      36.511  23.253  30.787  1.00 27.22           C  
ATOM     92  C   ALA A  11      35.596  22.110  30.453  1.00 23.48           C  
ATOM     93  O   ALA A  11      36.020  20.949  30.373  1.00 24.03           O  
ATOM     94  CB  ALA A  11      36.977  24.099  29.558  1.00 25.19           C  
ATOM     95  N   LYS A  12      34.314  22.360  30.262  1.00 27.87           N  
ATOM     96  CA  LYS A  12      33.390  21.263  29.943  1.00 22.01           C  
ATOM     97  C   LYS A  12      32.283  21.800  29.046  1.00 23.82           C  
ATOM     98  O   LYS A  12      32.008  22.982  28.988  1.00 22.03           O  
ATOM     99  CB  LYS A  12      32.815  20.632  31.201  1.00 19.34           C  
ATOM    100  CG  LYS A  12      32.195  21.602  32.221  1.00 29.52           C  
ATOM    101  CD  LYS A  12      31.655  20.867  33.462  1.00 31.13           C  
ATOM    102  CE  LYS A  12      30.510  21.535  34.140  1.00 44.78           C  
ATOM    103  NZ  LYS A  12      29.921  20.929  35.380  1.00 38.92           N  
ATOM    104  N   LEU A  13      31.659  20.915  28.321  1.00 23.65           N  
ATOM    105  CA  LEU A  13      30.485  21.179  27.519  1.00 26.88           C  
ATOM    106  C   LEU A  13      29.375  20.342  28.183  1.00 33.38           C  
ATOM    107  O   LEU A  13      29.518  19.130  28.432  1.00 29.98           O  
ATOM    108  CB  LEU A  13      30.692  20.771  26.054  1.00 23.37           C  
ATOM    109  CG  LEU A  13      31.860  21.550  25.418  1.00 33.65           C  
ATOM    110  CD1 LEU A  13      32.159  21.125  24.014  1.00 29.89           C  
ATOM    111  CD2 LEU A  13      31.465  23.029  25.509  1.00 30.86           C  
ATOM    112  N   GLY A  14      28.249  20.980  28.476  1.00 39.07           N  
ATOM    113  CA  GLY A  14      27.190  20.202  29.115  1.00 44.22           C  
ATOM    114  C   GLY A  14      25.892  20.211  28.343  1.00 41.05           C  
ATOM    115  O   GLY A  14      25.684  21.057  27.495  1.00 44.91           O  
ATOM    116  N   TRP A  15      25.049  19.253  28.647  1.00 39.26           N  
ATOM    117  CA  TRP A  15      23.733  19.114  28.122  1.00 44.28           C  
ATOM    118  C   TRP A  15      22.790  18.701  29.269  1.00 47.21           C  
ATOM    119  O   TRP A  15      23.056  17.888  30.130  1.00 40.20           O  
ATOM    120  CB  TRP A  15      23.497  18.244  26.911  1.00 41.46           C  
ATOM    121  CG  TRP A  15      23.709  16.785  27.056  1.00 48.76           C  
ATOM    122  CD1 TRP A  15      22.788  15.830  27.379  1.00 50.14           C  
ATOM    123  CD2 TRP A  15      24.946  16.068  26.884  0.60 46.68           C  
ATOM    124  NE1 TRP A  15      23.344  14.581  27.417  0.60 43.68           N  
ATOM    125  CE2 TRP A  15      24.683  14.707  27.124  0.60 46.97           C  
ATOM    126  CE3 TRP A  15      26.251  16.458  26.558  1.00 46.47           C  
ATOM    127  CZ2 TRP A  15      25.681  13.728  27.055  0.60 48.81           C  
ATOM    128  CZ3 TRP A  15      27.239  15.505  26.485  1.00 43.26           C  
ATOM    129  CH2 TRP A  15      26.951  14.141  26.743  1.00 50.50           C  
ATOM    130  N   SER A  16      21.643  19.352  29.244  1.00 57.99           N  
ATOM    131  CA  SER A  16      20.601  19.027  30.206  1.00 72.19           C  
ATOM    132  C   SER A  16      19.288  18.869  29.443  1.00 83.93           C  
ATOM    133  O   SER A  16      18.904  19.794  28.731  1.00 83.42           O  
ATOM    134  CB  SER A  16      20.462  20.073  31.290  1.00 69.30           C  
ATOM    135  OG  SER A  16      19.642  19.519  32.293  1.00 72.37           O  
ATOM    136  N   GLN A  17      18.653  17.729  29.602  1.00100.79           N  
ATOM    137  CA  GLN A  17      17.416  17.387  28.937  1.00117.21           C  
ATOM    138  C   GLN A  17      16.150  18.101  29.333  1.00128.96           C  
ATOM    139  O   GLN A  17      15.099  17.967  28.670  1.00132.78           O  
ATOM    140  CB  GLN A  17      17.190  15.860  29.064  1.00116.92           C  
ATOM    141  CG  GLN A  17      16.122  15.346  28.125  1.00119.23           C  
ATOM    142  CD  GLN A  17      16.460  15.480  26.661  1.00120.49           C  
ATOM    143  OE1 GLN A  17      15.777  14.860  25.833  1.00120.93           O  
ATOM    144  NE2 GLN A  17      17.475  16.247  26.284  1.00120.79           N  
ATOM    145  N   TYR A  18      16.094  18.841  30.390  1.00140.37           N  
ATOM    146  CA  TYR A  18      15.020  19.627  30.950  1.00150.86           C  
ATOM    147  C   TYR A  18      15.554  19.950  32.356  1.00159.33           C  
ATOM    148  O   TYR A  18      15.963  19.036  33.085  1.00160.75           O  
ATOM    149  CB  TYR A  18      13.624  19.020  30.931  1.00149.17           C  
ATOM    150  CG  TYR A  18      13.509  17.675  31.617  1.00148.50           C  
ATOM    151  CD1 TYR A  18      13.567  17.583  33.001  1.00149.08           C  
ATOM    152  CD2 TYR A  18      13.368  16.497  30.896  1.00147.42           C  
ATOM    153  CE1 TYR A  18      13.504  16.371  33.652  1.00149.38           C  
ATOM    154  CE2 TYR A  18      13.294  15.271  31.532  1.00147.37           C  
ATOM    155  CZ  TYR A  18      13.361  15.216  32.909  1.00148.82           C  
ATOM    156  OH  TYR A  18      13.283  13.994  33.542  1.00149.16           O  
ATOM    157  N   HIS A  19      15.707  21.226  32.680  1.00167.97           N  
ATOM    158  CA  HIS A  19      16.259  21.554  34.011  1.00175.49           C  
ATOM    159  C   HIS A  19      15.115  22.101  34.865  1.00179.57           C  
ATOM    160  O   HIS A  19      15.264  22.450  36.025  1.00179.04           O  
ATOM    161  CB  HIS A  19      17.408  22.524  33.907  1.00177.91           C  
ATOM    162  CG  HIS A  19      18.698  22.125  34.539  1.00181.03           C  
ATOM    163  ND1 HIS A  19      19.328  20.924  34.316  1.00182.19           N  
ATOM    164  CD2 HIS A  19      19.499  22.797  35.408  1.00182.69           C  
ATOM    165  CE1 HIS A  19      20.454  20.875  35.005  1.00182.28           C  
ATOM    166  NE2 HIS A  19      20.580  21.995  35.685  1.00182.39           N  
ATOM    167  N   ASP A  20      13.952  22.151  34.226  1.00184.44           N  
ATOM    168  CA  ASP A  20      12.718  22.640  34.802  1.00188.28           C  
ATOM    169  C   ASP A  20      11.505  22.053  34.080  1.00188.84           C  
ATOM    170  O   ASP A  20      11.450  20.891  33.681  1.00188.82           O  
ATOM    171  CB  ASP A  20      12.689  24.171  34.729  1.00192.13           C  
ATOM    172  CG  ASP A  20      12.729  24.769  33.343  1.00194.77           C  
ATOM    173  OD1 ASP A  20      12.150  24.212  32.382  1.00196.26           O  
ATOM    174  OD2 ASP A  20      13.346  25.850  33.179  1.00195.32           O  
ATOM    175  N   THR A  21      10.498  22.864  33.882  1.00188.48           N  
ATOM    176  CA  THR A  21       9.237  22.786  33.255  1.00186.47           C  
ATOM    177  C   THR A  21       8.124  23.291  34.212  1.00185.82           C  
ATOM    178  O   THR A  21       7.957  24.506  34.331  1.00185.13           O  
ATOM    179  CB  THR A  21       8.746  21.485  32.628  1.00185.11           C  
ATOM    180  OG1 THR A  21       8.891  20.365  33.501  1.00184.33           O  
ATOM    181  CG2 THR A  21       9.422  21.193  31.293  1.00182.86           C  
ATOM    182  N   GLY A  22       7.201  24.188  32.684  0.00 20.00           N  
ATOM    183  CA  GLY A  22       6.162  25.309  32.758  0.00 20.00           C  
ATOM    184  C   GLY A  22       4.661  24.994  33.133  0.00 20.00           C  
ATOM    185  O   GLY A  22       4.414  24.937  34.369  0.00 20.00           O  
ATOM    186  N   LEU A  23       3.872  25.005  31.992  0.00 20.00           N  
ATOM    187  CA  LEU A  23       2.380  24.633  31.656  0.00 20.00           C  
ATOM    188  C   LEU A  23       1.128  25.497  32.201  0.00 20.00           C  
ATOM    189  O   LEU A  23       1.187  26.093  33.288  0.00 20.00           O  
ATOM    190  CB  LEU A  23       2.092  23.189  32.047  0.00 20.00           C  
ATOM    191  CG  LEU A  23       3.098  22.200  31.429  0.00 20.00           C  
ATOM    192  CD1 LEU A  23       2.791  20.737  31.762  0.00 20.00           C  
ATOM    193  CD2 LEU A  23       3.168  22.262  29.898  0.00 20.00           C  
ATOM    194  N   ILE A  24       0.008  25.452  31.315  0.00 20.00           N  
ATOM    195  CA  ILE A  24      -1.444  26.037  31.474  0.00 20.00           C  
ATOM    196  C   ILE A  24      -2.403  24.940  31.131  0.00 20.00           C  
ATOM    197  O   ILE A  24      -2.229  24.215  30.137  0.00 20.00           O  
ATOM    198  CB  ILE A  24      -1.634  27.292  30.623  0.00 20.00           C  
ATOM    199  CG1 ILE A  24      -0.672  28.418  31.021  0.00 20.00           C  
ATOM    200  CG2 ILE A  24      -3.041  27.890  30.756  0.00 20.00           C  
ATOM    201  CD1 ILE A  24      -0.900  29.710  30.237  0.00 20.00           C  
ATOM    202  N   ASN A  25      -3.523  24.693  31.859  0.00 20.00           N  
ATOM    203  CA  ASN A  25      -3.963  23.417  31.442  0.00 20.00           C  
ATOM    204  C   ASN A  25      -3.043  23.240  30.285  0.00 20.00           C  
ATOM    205  O   ASN A  25      -1.883  22.812  30.487  0.00 20.00           O  
ATOM    206  CB  ASN A  25      -5.311  23.322  30.746  0.00 20.00           C  
ATOM    207  CG  ASN A  25      -6.527  23.316  31.667  0.00 20.00           C  
ATOM    208  OD1 ASN A  25      -6.503  22.680  32.715  0.00 20.00           O  
ATOM    209  ND2 ASN A  25      -7.610  23.989  31.320  0.00 20.00           N  
ATOM    210  N   ASN A  26      -3.727  23.742  29.286  0.00 20.00           N  
ATOM    211  CA  ASN A  26      -3.371  23.928  27.892  0.00 20.00           C  
ATOM    212  C   ASN A  26      -1.870  24.158  27.725  0.00 20.00           C  
ATOM    213  O   ASN A  26      -1.305  25.114  28.274  0.00 20.00           O  
ATOM    214  CB  ASN A  26      -4.191  25.134  27.393  0.00 20.00           C  
ATOM    215  CG  ASN A  26      -5.692  25.026  27.755  0.00 20.00           C  
ATOM    216  OD1 ASN A  26      -6.379  24.132  27.254  0.00 20.00           O  
ATOM    217  ND2 ASN A  26      -6.256  25.881  28.594  0.00 20.00           N  
ATOM    218  N   ASN A  27      -1.309  23.254  26.937  0.00 20.00           N  
ATOM    219  CA  ASN A  27       0.136  23.175  26.628  0.00 20.00           C  
ATOM    220  C   ASN A  27       0.633  24.446  25.901  0.00 20.00           C  
ATOM    221  O   ASN A  27      -0.119  25.090  25.157  0.00 20.00           O  
ATOM    222  CB  ASN A  27       0.372  21.924  25.782  0.00 20.00           C  
ATOM    223  CG  ASN A  27      -0.186  20.668  26.463  0.00 20.00           C  
ATOM    224  OD1 ASN A  27       0.213  20.351  27.584  0.00 20.00           O  
ATOM    225  ND2 ASN A  27      -1.096  19.930  25.856  0.00 20.00           N  
ATOM    226  N   GLY A  28       1.918  24.758  26.151  0.00 20.00           N  
ATOM    227  CA  GLY A  28       2.607  25.975  25.612  0.00 20.00           C  
ATOM    228  C   GLY A  28       3.823  25.596  24.739  0.00 20.00           C  
ATOM    229  O   GLY A  28       3.765  25.711  23.509  0.00 20.00           O  
ATOM    230  N   PRO A  29       5.119  25.031  25.116  1.00168.39           N  
ATOM    231  CA  PRO A  29       6.222  24.359  24.438  1.00168.30           C  
ATOM    232  C   PRO A  29       5.987  22.876  24.235  1.00167.61           C  
ATOM    233  O   PRO A  29       4.978  22.339  24.714  1.00168.90           O  
ATOM    234  CB  PRO A  29       7.401  24.629  25.356  1.00168.20           C  
ATOM    235  CG  PRO A  29       6.815  24.798  26.717  1.00167.42           C  
ATOM    236  CD  PRO A  29       5.466  25.420  26.514  1.00167.27           C  
ATOM    237  N   THR A  30       6.885  22.175  23.529  1.00164.54           N  
ATOM    238  CA  THR A  30       6.708  20.746  23.281  1.00160.14           C  
ATOM    239  C   THR A  30       7.621  19.825  24.077  1.00154.19           C  
ATOM    240  O   THR A  30       7.265  18.660  24.338  1.00153.24           O  
ATOM    241  CB  THR A  30       6.750  20.393  21.781  1.00162.00           C  
ATOM    242  OG1 THR A  30       8.088  20.425  21.271  1.00161.78           O  
ATOM    243  CG2 THR A  30       5.885  21.338  20.951  1.00161.34           C  
ATOM    244  N   HIS A  31       8.789  20.252  24.498  1.00146.35           N  
ATOM    245  CA  HIS A  31       9.770  19.501  25.281  1.00136.95           C  
ATOM    246  C   HIS A  31      11.026  20.366  25.378  1.00131.11           C  
ATOM    247  O   HIS A  31      10.968  21.449  24.746  1.00133.58           O  
ATOM    248  CB  HIS A  31      10.065  18.140  24.709  1.00135.94           C  
ATOM    249  N   GLU A  32      12.101  20.023  26.101  1.00119.59           N  
ATOM    250  CA  GLU A  32      13.186  21.030  26.101  1.00108.61           C  
ATOM    251  C   GLU A  32      14.602  20.536  26.220  1.00 96.69           C  
ATOM    252  O   GLU A  32      14.944  19.467  26.679  1.00 95.18           O  
ATOM    253  CB  GLU A  32      12.874  22.148  27.070  1.00112.82           C  
ATOM    254  CG  GLU A  32      13.322  22.067  28.509  1.00116.49           C  
ATOM    255  CD  GLU A  32      12.928  23.336  29.264  1.00118.97           C  
ATOM    256  OE1 GLU A  32      11.785  23.818  29.081  1.00119.51           O  
ATOM    257  OE2 GLU A  32      13.742  23.877  30.032  1.00119.83           O  
ATOM    258  N   ASN A  33      15.526  21.366  25.713  1.00 81.12           N  
ATOM    259  CA  ASN A  33      16.934  21.051  25.707  1.00 65.43           C  
ATOM    260  C   ASN A  33      17.758  22.281  26.098  1.00 56.53           C  
ATOM    261  O   ASN A  33      17.503  23.360  25.573  1.00 52.64           O  
ATOM    262  CB  ASN A  33      17.426  20.635  24.314  1.00 62.08           C  
ATOM    263  CG  ASN A  33      17.032  19.228  23.924  1.00 65.31           C  
ATOM    264  OD1 ASN A  33      17.503  18.264  24.547  1.00 64.43           O  
ATOM    265  ND2 ASN A  33      16.177  19.136  22.905  1.00 56.88           N  
ATOM    266  N   LYS A  34      18.716  22.048  26.982  1.00 50.02           N  
ATOM    267  CA  LYS A  34      19.659  23.049  27.404  1.00 50.60           C  
ATOM    268  C   LYS A  34      21.085  22.512  27.122  1.00 44.33           C  
ATOM    269  O   LYS A  34      21.374  21.360  27.391  1.00 40.69           O  
ATOM    270  CB  LYS A  34      19.628  23.415  28.872  1.00 60.75           C  
ATOM    271  CG  LYS A  34      18.387  24.060  29.416  1.00 67.41           C  
ATOM    272  CD  LYS A  34      17.588  23.019  30.205  1.00 75.20           C  
ATOM    273  CE  LYS A  34      16.455  23.663  30.974  1.00 82.99           C  
ATOM    274  NZ  LYS A  34      16.695  25.101  31.272  1.00 89.10           N  
ATOM    275  N   LEU A  35      21.919  23.385  26.631  1.00 39.25           N  
ATOM    276  CA  LEU A  35      23.290  23.146  26.324  1.00 36.79           C  
ATOM    277  C   LEU A  35      24.115  24.259  26.962  1.00 44.90           C  
ATOM    278  O   LEU A  35      23.624  25.376  27.003  1.00 44.53           O  
ATOM    279  CB  LEU A  35      23.589  23.265  24.797  1.00 30.28           C  
ATOM    280  CG  LEU A  35      23.020  22.047  24.041  1.00 35.40           C  
ATOM    281  CD1 LEU A  35      23.290  22.186  22.581  1.00 43.92           C  
ATOM    282  CD2 LEU A  35      23.716  20.792  24.576  1.00 46.79           C  
ATOM    283  N   GLY A  36      25.329  23.923  27.389  1.00 47.07           N  
ATOM    284  CA  GLY A  36      26.170  24.957  27.932  1.00 44.81           C  
ATOM    285  C   GLY A  36      27.610  24.491  28.092  1.00 44.21           C  
ATOM    286  O   GLY A  36      28.072  23.464  27.637  1.00 40.70           O  
ATOM    287  N   ALA A  37      28.299  25.318  28.857  1.00 37.61           N  
ATOM    288  CA  ALA A  37      29.700  25.137  29.101  1.00 28.94           C  
ATOM    289  C   ALA A  37      30.043  25.564  30.504  1.00 35.55           C  
ATOM    290  O   ALA A  37      29.153  26.023  31.231  1.00 41.03           O  
ATOM    291  CB  ALA A  37      30.363  26.036  28.043  1.00 17.37           C  
ATOM    292  N   GLY A  38      31.301  25.394  30.893  1.00 33.69           N  
ATOM    293  CA  GLY A  38      31.698  25.735  32.264  1.00 26.33           C  
ATOM    294  C   GLY A  38      33.203  25.620  32.370  1.00 27.47           C  
ATOM    295  O   GLY A  38      33.818  25.095  31.453  1.00 29.40           O  
ATOM    296  N   ALA A  39      33.772  26.151  33.438  1.00 28.33           N  
ATOM    297  CA  ALA A  39      35.214  26.108  33.636  1.00 25.50           C  
ATOM    298  C   ALA A  39      35.414  25.702  35.093  1.00 26.60           C  
ATOM    299  O   ALA A  39      34.518  26.013  35.899  1.00 27.65           O  
ATOM    300  CB  ALA A  39      35.890  27.454  33.361  1.00 22.33           C  
ATOM    301  N   PHE A  40      36.508  25.018  35.402  1.00 24.06           N  
ATOM    302  CA  PHE A  40      36.654  24.641  36.810  1.00 31.99           C  
ATOM    303  C   PHE A  40      38.143  24.628  37.130  1.00 31.89           C  
ATOM    304  O   PHE A  40      38.946  24.447  36.215  1.00 27.01           O  
ATOM    305  CB  PHE A  40      35.998  23.260  37.145  1.00 27.03           C  
ATOM    306  CG  PHE A  40      36.510  22.137  36.287  1.00 26.16           C  
ATOM    307  CD1 PHE A  40      35.914  21.845  35.057  1.00 20.45           C  
ATOM    308  CD2 PHE A  40      37.620  21.405  36.710  1.00 30.01           C  
ATOM    309  CE1 PHE A  40      36.448  20.810  34.282  1.00 28.40           C  
ATOM    310  CE2 PHE A  40      38.148  20.363  35.927  1.00 29.16           C  
ATOM    311  CZ  PHE A  40      37.551  20.082  34.703  1.00 28.70           C  
ATOM    312  N   GLY A  41      38.448  24.793  38.405  1.00 31.00           N  
ATOM    313  CA  GLY A  41      39.890  24.733  38.795  1.00 37.89           C  
ATOM    314  C   GLY A  41      39.875  24.038  40.172  1.00 39.28           C  
ATOM    315  O   GLY A  41      38.855  24.093  40.878  1.00 33.84           O  
ATOM    316  N   GLY A  42      40.983  23.377  40.501  1.00 37.71           N  
ATOM    317  CA  GLY A  42      41.016  22.685  41.783  1.00 32.15           C  
ATOM    318  C   GLY A  42      42.409  22.515  42.326  1.00 38.93           C  
ATOM    319  O   GLY A  42      43.449  22.827  41.751  1.00 44.12           O  
ATOM    320  N   TYR A  43      42.453  21.982  43.529  1.00 43.20           N  
ATOM    321  CA  TYR A  43      43.679  21.684  44.248  1.00 40.66           C  
ATOM    322  C   TYR A  43      43.571  20.243  44.740  1.00 34.58           C  
ATOM    323  O   TYR A  43      42.567  19.867  45.327  1.00 34.44           O  
ATOM    324  CB  TYR A  43      43.897  22.677  45.368  1.00 41.48           C  
ATOM    325  CG  TYR A  43      45.078  22.413  46.248  1.00 52.85           C  
ATOM    326  CD1 TYR A  43      46.381  22.684  45.813  1.00 56.05           C  
ATOM    327  CD2 TYR A  43      44.911  21.904  47.534  1.00 58.89           C  
ATOM    328  CE1 TYR A  43      47.460  22.457  46.637  1.00 55.32           C  
ATOM    329  CE2 TYR A  43      46.000  21.671  48.363  1.00 59.52           C  
ATOM    330  CZ  TYR A  43      47.267  21.947  47.904  1.00 60.35           C  
ATOM    331  OH  TYR A  43      48.349  21.709  48.726  1.00 64.89           O  
ATOM    332  N   GLN A  44      44.583  19.449  44.422  1.00 35.86           N  
ATOM    333  CA  GLN A  44      44.597  18.054  44.881  1.00 43.23           C  
ATOM    334  C   GLN A  44      45.306  17.972  46.228  1.00 42.13           C  
ATOM    335  O   GLN A  44      46.349  18.608  46.418  1.00 43.97           O  
ATOM    336  CB  GLN A  44      45.253  17.178  43.819  1.00 45.87           C  
ATOM    337  CG  GLN A  44      44.872  15.721  43.854  1.00 35.86           C  
ATOM    338  CD  GLN A  44      43.460  15.374  43.535  1.00 34.70           C  
ATOM    339  OE1 GLN A  44      42.816  15.926  42.652  1.00 38.82           O  
ATOM    340  NE2 GLN A  44      42.919  14.395  44.266  1.00 33.78           N  
ATOM    341  N   VAL A  45      44.766  17.260  47.196  1.00 43.96           N  
ATOM    342  CA  VAL A  45      45.442  17.173  48.511  1.00 45.94           C  
ATOM    343  C   VAL A  45      46.268  15.886  48.581  1.00 44.59           C  
ATOM    344  O   VAL A  45      47.408  15.884  49.026  1.00 46.38           O  
ATOM    345  CB  VAL A  45      44.456  17.251  49.692  1.00 48.66           C  
ATOM    346  CG1 VAL A  45      45.169  17.029  51.017  1.00 41.34           C  
ATOM    347  CG2 VAL A  45      43.772  18.631  49.692  1.00 41.13           C  
ATOM    348  N   ASN A  46      45.702  14.801  48.125  1.00 41.56           N  
ATOM    349  CA  ASN A  46      46.307  13.476  48.056  1.00 43.46           C  
ATOM    350  C   ASN A  46      45.524  12.730  46.987  1.00 41.63           C  
ATOM    351  O   ASN A  46      44.559  13.267  46.447  1.00 47.60           O  
ATOM    352  CB  ASN A  46      46.331  12.837  49.414  1.00 39.51           C  
ATOM    353  CG  ASN A  46      44.923  12.597  49.966  1.00 46.51           C  
ATOM    354  OD1 ASN A  46      44.068  11.999  49.318  1.00 44.69           O  
ATOM    355  ND2 ASN A  46      44.638  13.065  51.175  1.00 42.31           N  
ATOM    356  N   PRO A  47      45.839  11.509  46.636  1.00 45.19           N  
ATOM    357  CA  PRO A  47      45.195  10.810  45.546  1.00 44.07           C  
ATOM    358  C   PRO A  47      43.729  10.594  45.681  1.00 38.49           C  
ATOM    359  O   PRO A  47      43.066  10.178  44.712  1.00 44.15           O  
ATOM    360  CB  PRO A  47      45.963   9.491  45.367  1.00 44.31           C  
ATOM    361  CG  PRO A  47      46.856   9.377  46.545  1.00 48.06           C  
ATOM    362  CD  PRO A  47      47.021  10.753  47.155  1.00 50.70           C  
ATOM    363  N   TYR A  48      43.146  10.770  46.828  1.00 35.37           N  
ATOM    364  CA  TYR A  48      41.734  10.497  47.033  1.00 34.90           C  
ATOM    365  C   TYR A  48      40.904  11.758  47.154  1.00 34.80           C  
ATOM    366  O   TYR A  48      39.698  11.640  46.930  1.00 32.41           O  
ATOM    367  CB  TYR A  48      41.633   9.693  48.362  1.00 44.76           C  
ATOM    368  CG  TYR A  48      42.453   8.428  48.244  1.00 54.21           C  
ATOM    369  CD1 TYR A  48      41.938   7.360  47.522  1.00 56.07           C  
ATOM    370  CD2 TYR A  48      43.721   8.325  48.800  1.00 58.55           C  
ATOM    371  CE1 TYR A  48      42.652   6.191  47.376  1.00 65.42           C  
ATOM    372  CE2 TYR A  48      44.450   7.147  48.656  1.00 64.13           C  
ATOM    373  CZ  TYR A  48      43.917   6.091  47.956  1.00 69.42           C  
ATOM    374  OH  TYR A  48      44.612   4.903  47.772  1.00 72.89           O  
ATOM    375  N   VAL A  49      41.508  12.896  47.563  1.00 28.37           N  
ATOM    376  CA  VAL A  49      40.778  14.089  47.814  1.00 29.55           C  
ATOM    377  C   VAL A  49      41.372  15.369  47.226  1.00 34.27           C  
ATOM    378  O   VAL A  49      42.554  15.704  47.301  1.00 29.98           O  
ATOM    379  CB  VAL A  49      40.388  14.278  49.303  1.00 36.30           C  
ATOM    380  CG1 VAL A  49      40.719  13.146  50.247  1.00 29.34           C  
ATOM    381  CG2 VAL A  49      40.905  15.551  49.925  1.00 32.91           C  
ATOM    382  N   GLY A  50      40.450  16.141  46.626  1.00 29.72           N  
ATOM    383  CA  GLY A  50      40.720  17.437  46.004  1.00 30.13           C  
ATOM    384  C   GLY A  50      39.534  18.367  46.281  1.00 33.09           C  
ATOM    385  O   GLY A  50      38.452  17.980  46.766  1.00 29.48           O  
ATOM    386  N   PHE A  51      39.735  19.644  46.052  1.00 32.14           N  
ATOM    387  CA  PHE A  51      38.668  20.635  46.223  1.00 32.43           C  
ATOM    388  C   PHE A  51      38.571  21.439  44.929  1.00 32.62           C  
ATOM    389  O   PHE A  51      39.629  21.800  44.402  1.00 31.79           O  
ATOM    390  CB  PHE A  51      38.998  21.605  47.357  1.00 29.69           C  
ATOM    391  CG  PHE A  51      38.997  20.849  48.658  1.00 29.91           C  
ATOM    392  CD1 PHE A  51      37.820  20.389  49.184  1.00 29.00           C  
ATOM    393  CD2 PHE A  51      40.197  20.596  49.298  1.00 30.11           C  
ATOM    394  CE1 PHE A  51      37.792  19.693  50.382  1.00 29.10           C  
ATOM    395  CE2 PHE A  51      40.186  19.907  50.493  1.00 29.83           C  
ATOM    396  CZ  PHE A  51      38.998  19.460  51.028  1.00 37.55           C  
ATOM    397  N   GLU A  52      37.387  21.703  44.404  1.00 31.94           N  
ATOM    398  CA  GLU A  52      37.332  22.492  43.188  1.00 32.31           C  
ATOM    399  C   GLU A  52      36.202  23.526  43.235  1.00 32.05           C  
ATOM    400  O   GLU A  52      35.159  23.513  43.858  1.00 28.00           O  
ATOM    401  CB  GLU A  52      37.134  21.745  41.866  1.00 30.98           C  
ATOM    402  CG  GLU A  52      36.766  20.323  41.913  1.00 25.08           C  
ATOM    403  CD  GLU A  52      36.791  19.652  40.546  1.00 37.28           C  
ATOM    404  OE1 GLU A  52      35.848  19.971  39.777  1.00 29.93           O  
ATOM    405  OE2 GLU A  52      37.681  18.817  40.240  1.00 34.49           O  
ATOM    406  N   MET A  53      36.490  24.449  42.363  1.00 31.48           N  
ATOM    407  CA  MET A  53      35.663  25.586  42.086  1.00 34.69           C  
ATOM    408  C   MET A  53      35.292  25.557  40.616  1.00 35.87           C  
ATOM    409  O   MET A  53      36.152  25.390  39.752  1.00 39.16           O  
ATOM    410  CB  MET A  53      36.599  26.793  42.392  1.00 43.45           C  
ATOM    411  CG  MET A  53      35.803  28.080  42.354  1.00 62.85           C  
ATOM    412  SD  MET A  53      35.856  28.963  43.914  1.00 71.63           S  
ATOM    413  CE  MET A  53      34.671  30.288  43.536  1.00 72.05           C  
ATOM    414  N   GLY A  54      34.013  25.752  40.310  1.00 35.77           N  
ATOM    415  CA  GLY A  54      33.604  25.853  38.938  1.00 32.40           C  
ATOM    416  C   GLY A  54      32.521  26.897  38.699  1.00 32.02           C  
ATOM    417  O   GLY A  54      31.751  27.280  39.561  1.00 28.88           O  
ATOM    418  N   TYR A  55      32.441  27.279  37.428  1.00 32.48           N  
ATOM    419  CA  TYR A  55      31.410  28.197  36.952  1.00 34.15           C  
ATOM    420  C   TYR A  55      30.720  27.487  35.800  1.00 28.37           C  
ATOM    421  O   TYR A  55      31.431  26.939  34.933  1.00 28.68           O  
ATOM    422  CB  TYR A  55      32.097  29.521  36.525  1.00 43.65           C  
ATOM    423  CG  TYR A  55      31.115  30.379  35.744  1.00 52.31           C  
ATOM    424  CD1 TYR A  55      30.023  30.966  36.367  1.00 53.92           C  
ATOM    425  CD2 TYR A  55      31.287  30.544  34.374  1.00 57.20           C  
ATOM    426  CE1 TYR A  55      29.127  31.712  35.623  1.00 58.32           C  
ATOM    427  CE2 TYR A  55      30.395  31.292  33.618  1.00 60.26           C  
ATOM    428  CZ  TYR A  55      29.323  31.873  34.264  1.00 61.32           C  
ATOM    429  OH  TYR A  55      28.427  32.616  33.536  1.00 66.33           O  
ATOM    430  N   ASP A  56      29.419  27.409  35.738  1.00 23.90           N  
ATOM    431  CA  ASP A  56      28.746  26.749  34.630  1.00 28.41           C  
ATOM    432  C   ASP A  56      27.659  27.692  34.070  1.00 34.41           C  
ATOM    433  O   ASP A  56      27.103  28.537  34.768  1.00 32.35           O  
ATOM    434  CB  ASP A  56      28.016  25.489  35.016  1.00 38.70           C  
ATOM    435  CG  ASP A  56      28.699  24.352  35.673  1.00 46.40           C  
ATOM    436  OD1 ASP A  56      29.902  24.103  35.501  1.00 54.62           O  
ATOM    437  OD2 ASP A  56      27.984  23.621  36.404  1.00 59.31           O  
ATOM    438  N   TRP A  57      27.299  27.443  32.826  1.00 37.27           N  
ATOM    439  CA  TRP A  57      26.244  28.212  32.170  1.00 36.22           C  
ATOM    440  C   TRP A  57      25.454  27.282  31.264  1.00 39.89           C  
ATOM    441  O   TRP A  57      26.052  26.397  30.633  1.00 41.64           O  
ATOM    442  CB  TRP A  57      26.746  29.455  31.503  1.00 32.04           C  
ATOM    443  CG  TRP A  57      27.308  29.420  30.150  1.00 43.39           C  
ATOM    444  CD1 TRP A  57      26.576  29.273  29.001  0.50 41.37           C  
ATOM    445  CD2 TRP A  57      28.683  29.520  29.740  0.50 39.24           C  
ATOM    446  NE1 TRP A  57      27.415  29.265  27.909  0.50 45.93           N  
ATOM    447  CE2 TRP A  57      28.710  29.425  28.345  0.50 41.62           C  
ATOM    448  CE3 TRP A  57      29.883  29.663  30.425  0.50 47.40           C  
ATOM    449  CZ2 TRP A  57      29.900  29.491  27.625  0.50 52.50           C  
ATOM    450  CZ3 TRP A  57      31.081  29.721  29.717  0.50 48.97           C  
ATOM    451  CH2 TRP A  57      31.081  29.638  28.315  0.50 49.79           C  
ATOM    452  N   LEU A  58      24.140  27.461  31.265  1.00 36.95           N  
ATOM    453  CA  LEU A  58      23.243  26.680  30.447  1.00 43.35           C  
ATOM    454  C   LEU A  58      22.260  27.628  29.736  1.00 48.25           C  
ATOM    455  O   LEU A  58      21.757  28.572  30.338  1.00 51.39           O  
ATOM    456  CB  LEU A  58      22.425  25.687  31.263  1.00 41.11           C  
ATOM    457  CG  LEU A  58      23.077  24.410  31.725  1.00 56.39           C  
ATOM    458  CD1 LEU A  58      22.138  23.684  32.689  1.00 53.68           C  
ATOM    459  CD2 LEU A  58      23.456  23.474  30.556  1.00 58.29           C  
ATOM    460  N   GLY A  59      21.976  27.376  28.487  1.00 50.72           N  
ATOM    461  CA  GLY A  59      21.048  28.177  27.700  1.00 51.14           C  
ATOM    462  C   GLY A  59      19.979  27.268  27.106  1.00 53.17           C  
ATOM    463  O   GLY A  59      20.312  26.167  26.691  1.00 50.67           O  
ATOM    464  N   ARG A  60      18.726  27.701  27.099  1.00 63.59           N  
ATOM    465  CA  ARG A  60      17.667  26.851  26.491  1.00 69.46           C  
ATOM    466  C   ARG A  60      17.879  26.898  24.982  1.00 66.18           C  
ATOM    467  O   ARG A  60      18.255  27.955  24.478  1.00 63.41           O  
ATOM    468  CB  ARG A  60      16.296  27.327  26.889  1.00 78.97           C  
ATOM    469  CG  ARG A  60      15.173  27.238  25.887  1.00 89.57           C  
ATOM    470  CD  ARG A  60      14.124  26.201  26.234  1.00 93.65           C  
ATOM    471  NE  ARG A  60      13.341  26.464  27.404  1.00 99.08           N  
ATOM    472  CZ  ARG A  60      12.738  27.545  27.869  1.00 99.08           C  
ATOM    473  NH1 ARG A  60      12.759  28.726  27.261  1.00 93.48           N  
ATOM    474  NH2 ARG A  60      12.075  27.421  29.029  1.00 97.35           N  
ATOM    475  N   MET A  61      17.715  25.781  24.305  1.00 73.89           N  
ATOM    476  CA  MET A  61      17.912  25.747  22.843  1.00 84.74           C  
ATOM    477  C   MET A  61      16.571  25.924  22.130  1.00 91.32           C  
ATOM    478  O   MET A  61      15.579  25.285  22.490  1.00 87.89           O  
ATOM    479  CB  MET A  61      18.617  24.476  22.400  1.00 79.38           C  
ATOM    480  CG  MET A  61      19.766  24.688  21.450  1.00 77.53           C  
ATOM    481  SD  MET A  61      21.109  25.716  22.085  1.00 70.85           S  
ATOM    482  CE  MET A  61      21.385  26.772  20.645  1.00 78.51           C  
ATOM    483  N   PRO A  62      16.549  26.814  21.145  1.00101.20           N  
ATOM    484  CA  PRO A  62      15.354  27.147  20.412  1.00110.21           C  
ATOM    485  C   PRO A  62      14.763  26.039  19.565  1.00118.89           C  
ATOM    486  O   PRO A  62      15.413  25.639  18.599  1.00119.05           O  
ATOM    487  CB  PRO A  62      15.765  28.330  19.525  1.00107.90           C  
ATOM    488  CG  PRO A  62      17.245  28.251  19.419  1.00105.63           C  
ATOM    489  CD  PRO A  62      17.725  27.613  20.698  1.00103.85           C  
ATOM    490  N   TYR A  63      13.569  25.554  19.912  1.00128.05           N  
ATOM    491  CA  TYR A  63      12.828  24.573  19.191  1.00134.58           C  
ATOM    492  C   TYR A  63      11.382  24.323  19.611  1.00131.94           C  
ATOM    493  O   TYR A  63      11.128  23.608  20.580  1.00133.54           O  
ATOM    494  CB  TYR A  63      13.497  23.182  19.006  1.00143.07           C  
ATOM    495  CG  TYR A  63      13.678  23.090  17.480  1.00151.22           C  
ATOM    496  CD1 TYR A  63      12.611  22.807  16.643  1.00152.85           C  
ATOM    497  CD2 TYR A  63      14.918  23.368  16.935  1.00153.98           C  
ATOM    498  CE1 TYR A  63      12.796  22.766  15.271  1.00155.91           C  
ATOM    499  CE2 TYR A  63      15.093  23.342  15.577  1.00156.52           C  
ATOM    500  CZ  TYR A  63      14.045  23.030  14.744  1.00157.67           C  
ATOM    501  OH  TYR A  63      14.242  22.993  13.382  1.00159.13           O  
ATOM    502  N   LYS A  64      10.453  24.869  18.829  1.00123.41           N  
ATOM    503  CA  LYS A  64       9.022  24.757  19.029  1.00114.53           C  
ATOM    504  C   LYS A  64       8.615  24.329  20.432  1.00117.06           C  
ATOM    505  O   LYS A  64       8.097  25.105  21.240  1.00118.88           O  
ATOM    506  CB  LYS A  64       8.388  23.804  17.988  0.00 97.58           C  
ATOM    507  CG  LYS A  64       8.621  24.257  16.548  0.00 83.04           C  
ATOM    508  CD  LYS A  64       7.890  23.367  15.543  0.00 75.73           C  
ATOM    509  CE  LYS A  64       8.821  23.101  14.329  0.00 78.02           C  
ATOM    510  NZ  LYS A  64       8.126  22.314  13.251  0.00 73.74           N  
ATOM    511  N   GLY A  65       7.295  25.874  18.037  0.00 20.00           N  
ATOM    512  CA  GLY A  65       6.254  26.841  17.725  0.00 20.00           C  
ATOM    513  C   GLY A  65       4.887  26.264  18.138  0.00 20.00           C  
ATOM    514  O   GLY A  65       4.751  25.057  18.421  0.00 20.00           O  
ATOM    515  N   SER A  66       3.975  27.186  18.130  0.00 20.00           N  
ATOM    516  CA  SER A  66       2.606  27.056  18.603  0.00 20.00           C  
ATOM    517  C   SER A  66       2.439  28.224  19.535  0.00 20.00           C  
ATOM    518  O   SER A  66       2.074  28.069  20.707  0.00 20.00           O  
ATOM    519  CB  SER A  66       2.390  25.731  19.319  0.00 20.00           C  
ATOM    520  OG  SER A  66       3.229  25.652  20.457  0.00 20.00           O  
ATOM    521  N   VAL A  67       2.784  29.321  18.943  0.00 20.00           N  
ATOM    522  CA  VAL A  67       2.726  30.600  19.566  0.00 20.00           C  
ATOM    523  C   VAL A  67       3.383  30.642  20.920  0.00 20.00           C  
ATOM    524  O   VAL A  67       2.793  30.337  21.961  0.00 20.00           O  
ATOM    525  CB  VAL A  67       1.280  31.013  19.866  0.00 20.00           C  
ATOM    526  CG1 VAL A  67       1.187  32.337  20.637  0.00 20.00           C  
ATOM    527  CG2 VAL A  67       0.426  31.198  18.618  0.00 20.00           C  
ATOM    528  N   GLU A  68       4.653  30.948  21.073  0.00 20.00           N  
ATOM    529  CA  GLU A  68       4.754  31.496  22.386  0.00 20.00           C  
ATOM    530  C   GLU A  68       5.789  31.131  23.452  0.00 20.00           C  
ATOM    531  O   GLU A  68       5.457  31.253  24.637  0.00 20.00           O  
ATOM    532  CB  GLU A  68       3.359  31.260  23.004  0.00 20.00           C  
ATOM    533  CG  GLU A  68       2.220  31.535  21.981  0.00 20.00           C  
ATOM    534  CD  GLU A  68       0.807  31.219  22.498  0.00 20.00           C  
ATOM    535  OE1 GLU A  68       0.649  30.688  23.661  0.00 20.00           O  
ATOM    536  OE2 GLU A  68      -0.230  31.486  21.769  0.00 20.00           O  
ATOM    537  N   ASN A  69       8.453  29.370  23.442  1.00110.80           N  
ATOM    538  CA  ASN A  69       8.159  30.622  24.118  1.00112.92           C  
ATOM    539  C   ASN A  69       9.316  31.618  24.034  1.00110.90           C  
ATOM    540  O   ASN A  69       9.474  32.283  22.993  1.00109.37           O  
ATOM    541  CB  ASN A  69       7.660  30.458  25.545  1.00115.42           C  
ATOM    542  CG  ASN A  69       7.848  29.136  26.230  1.00117.61           C  
ATOM    543  OD1 ASN A  69       7.356  28.091  25.775  1.00118.91           O  
ATOM    544  ND2 ASN A  69       8.552  29.100  27.367  1.00114.55           N  
ATOM    545  N   GLY A  70      10.103  31.765  25.103  1.00106.96           N  
ATOM    546  CA  GLY A  70      11.206  32.718  25.089  1.00104.38           C  
ATOM    547  C   GLY A  70      12.513  32.206  25.677  1.00101.36           C  
ATOM    548  O   GLY A  70      12.709  31.017  25.929  1.00103.00           O  
ATOM    549  N   ALA A  71      13.457  33.111  25.920  1.00 95.23           N  
ATOM    550  CA  ALA A  71      14.774  32.883  26.458  1.00 88.31           C  
ATOM    551  C   ALA A  71      14.900  32.415  27.910  1.00 82.21           C  
ATOM    552  O   ALA A  71      14.178  32.787  28.828  1.00 76.81           O  
ATOM    553  CB  ALA A  71      15.620  34.163  26.278  1.00 79.58           C  
ATOM    554  N   TYR A  72      15.881  31.535  28.145  1.00 74.90           N  
ATOM    555  CA  TYR A  72      16.203  30.961  29.425  1.00 68.78           C  
ATOM    556  C   TYR A  72      17.717  30.735  29.517  1.00 65.09           C  
ATOM    557  O   TYR A  72      18.324  30.032  28.720  1.00 62.14           O  
ATOM    558  CB  TYR A  72      15.466  29.672  29.762  1.00 68.61           C  
ATOM    559  CG  TYR A  72      15.814  29.114  31.120  1.00 80.08           C  
ATOM    560  CD1 TYR A  72      17.026  28.429  31.324  1.00 83.36           C  
ATOM    561  CD2 TYR A  72      14.965  29.242  32.212  1.00 84.11           C  
ATOM    562  CE1 TYR A  72      17.382  27.907  32.546  1.00 82.70           C  
ATOM    563  CE2 TYR A  72      15.309  28.715  33.458  1.00 87.07           C  
ATOM    564  CZ  TYR A  72      16.516  28.048  33.619  1.00 87.63           C  
ATOM    565  OH  TYR A  72      16.842  27.534  34.859  1.00 84.53           O  
ATOM    566  N   LYS A  73      18.293  31.307  30.554  1.00 61.67           N  
ATOM    567  CA  LYS A  73      19.736  31.210  30.798  1.00 57.44           C  
ATOM    568  C   LYS A  73      19.968  30.929  32.273  1.00 56.15           C  
ATOM    569  O   LYS A  73      19.350  31.539  33.146  1.00 57.23           O  
ATOM    570  CB  LYS A  73      20.355  32.491  30.291  1.00 53.29           C  
ATOM    571  CG  LYS A  73      21.681  32.963  30.760  1.00 66.14           C  
ATOM    572  CD  LYS A  73      22.487  33.651  29.649  1.00 74.93           C  
ATOM    573  CE  LYS A  73      23.976  33.606  29.923  1.00 79.93           C  
ATOM    574  NZ  LYS A  73      24.659  32.322  29.577  1.00 73.24           N  
ATOM    575  N   ALA A  74      20.821  29.951  32.615  1.00 49.14           N  
ATOM    576  CA  ALA A  74      21.123  29.687  34.013  1.00 38.93           C  
ATOM    577  C   ALA A  74      22.632  29.762  34.185  1.00 36.49           C  
ATOM    578  O   ALA A  74      23.392  29.488  33.282  1.00 40.18           O  
ATOM    579  CB  ALA A  74      20.503  28.473  34.625  1.00 35.98           C  
ATOM    580  N   GLN A  75      23.051  30.183  35.356  1.00 33.42           N  
ATOM    581  CA  GLN A  75      24.494  30.278  35.580  1.00 38.38           C  
ATOM    582  C   GLN A  75      24.774  29.975  37.031  1.00 42.59           C  
ATOM    583  O   GLN A  75      23.834  30.030  37.846  1.00 39.02           O  
ATOM    584  CB  GLN A  75      25.012  31.450  34.890  1.00 40.96           C  
ATOM    585  CG  GLN A  75      25.070  32.817  35.503  1.00 58.95           C  
ATOM    586  CD  GLN A  75      25.739  33.792  34.543  1.00 63.68           C  
ATOM    587  OE1 GLN A  75      26.050  34.927  34.835  1.00 72.83           O  
ATOM    588  NE2 GLN A  75      25.988  33.333  33.317  1.00 73.77           N  
ATOM    589  N   GLY A  76      25.996  29.508  37.357  1.00 39.76           N  
ATOM    590  CA  GLY A  76      26.237  29.115  38.758  1.00 34.73           C  
ATOM    591  C   GLY A  76      27.714  28.924  39.056  1.00 38.53           C  
ATOM    592  O   GLY A  76      28.526  28.519  38.219  1.00 34.59           O  
ATOM    593  N   VAL A  77      28.074  29.291  40.296  1.00 36.51           N  
ATOM    594  CA  VAL A  77      29.405  29.071  40.808  1.00 38.31           C  
ATOM    595  C   VAL A  77      29.285  28.024  41.917  1.00 36.22           C  
ATOM    596  O   VAL A  77      28.347  28.043  42.724  1.00 28.79           O  
ATOM    597  CB  VAL A  77      30.204  30.293  41.264  1.00 45.83           C  
ATOM    598  CG1 VAL A  77      29.904  31.426  40.283  1.00 47.63           C  
ATOM    599  CG2 VAL A  77      29.879  30.714  42.664  1.00 43.79           C  
ATOM    600  N   GLN A  78      30.186  27.029  41.842  1.00 38.07           N  
ATOM    601  CA  GLN A  78      30.137  25.917  42.818  1.00 29.59           C  
ATOM    602  C   GLN A  78      31.464  25.723  43.485  1.00 24.14           C  
ATOM    603  O   GLN A  78      32.528  26.136  42.979  1.00 29.43           O  
ATOM    604  CB  GLN A  78      29.555  24.687  42.131  1.00 25.00           C  
ATOM    605  CG  GLN A  78      30.432  24.202  40.932  1.00 31.90           C  
ATOM    606  CD  GLN A  78      29.928  22.865  40.434  1.00 24.68           C  
ATOM    607  OE1 GLN A  78      30.220  21.854  41.068  1.00 34.36           O  
ATOM    608  NE2 GLN A  78      29.129  22.766  39.390  1.00 29.24           N  
ATOM    609  N   LEU A  79      31.459  25.150  44.662  1.00 27.95           N  
ATOM    610  CA  LEU A  79      32.634  24.877  45.518  1.00 27.95           C  
ATOM    611  C   LEU A  79      32.399  23.456  46.068  1.00 30.72           C  
ATOM    612  O   LEU A  79      31.390  23.209  46.726  1.00 26.93           O  
ATOM    613  CB  LEU A  79      32.669  25.776  46.707  1.00 29.93           C  
ATOM    614  CG  LEU A  79      33.943  26.143  47.427  1.00 46.00           C  
ATOM    615  CD1 LEU A  79      33.673  26.049  48.931  1.00 43.58           C  
ATOM    616  CD2 LEU A  79      35.183  25.372  47.026  1.00 36.38           C  
ATOM    617  N   THR A  80      33.229  22.487  45.692  1.00 27.76           N  
ATOM    618  CA  THR A  80      33.003  21.131  46.085  1.00 27.76           C  
ATOM    619  C   THR A  80      34.265  20.403  46.517  1.00 30.28           C  
ATOM    620  O   THR A  80      35.426  20.711  46.306  1.00 34.17           O  
ATOM    621  CB  THR A  80      32.351  20.285  44.951  1.00 26.86           C  
ATOM    622  OG1 THR A  80      33.192  20.314  43.807  1.00 27.19           O  
ATOM    623  CG2 THR A  80      31.005  20.790  44.510  1.00 23.10           C  
ATOM    624  N   ALA A  81      33.966  19.326  47.243  1.00 31.81           N  
ATOM    625  CA  ALA A  81      35.049  18.432  47.678  1.00 33.16           C  
ATOM    626  C   ALA A  81      34.912  17.274  46.657  1.00 37.44           C  
ATOM    627  O   ALA A  81      33.788  16.902  46.251  1.00 30.56           O  
ATOM    628  CB  ALA A  81      34.958  18.006  49.097  1.00 26.83           C  
ATOM    629  N   LYS A  82      36.086  16.869  46.175  1.00 34.60           N  
ATOM    630  CA  LYS A  82      36.101  15.792  45.190  1.00 34.84           C  
ATOM    631  C   LYS A  82      36.754  14.562  45.836  1.00 35.90           C  
ATOM    632  O   LYS A  82      37.895  14.594  46.310  1.00 31.45           O  
ATOM    633  CB  LYS A  82      36.735  16.200  43.875  1.00 32.02           C  
ATOM    634  CG  LYS A  82      37.305  15.077  43.025  1.00 31.28           C  
ATOM    635  CD  LYS A  82      37.467  15.443  41.554  1.00 31.00           C  
ATOM    636  CE  LYS A  82      38.703  14.756  40.959  1.00 44.83           C  
ATOM    637  NZ  LYS A  82      39.997  15.317  41.475  1.00 34.53           N  
ATOM    638  N   LEU A  83      35.960  13.510  45.914  1.00 36.11           N  
ATOM    639  CA  LEU A  83      36.399  12.230  46.441  1.00 40.61           C  
ATOM    640  C   LEU A  83      36.503  11.169  45.366  1.00 36.38           C  
ATOM    641  O   LEU A  83      35.563  10.804  44.644  1.00 38.58           O  
ATOM    642  CB  LEU A  83      35.408  11.787  47.535  1.00 49.69           C  
ATOM    643  CG  LEU A  83      35.575  12.707  48.774  1.00 55.01           C  
ATOM    644  CD1 LEU A  83      34.382  12.566  49.685  1.00 64.59           C  
ATOM    645  CD2 LEU A  83      36.868  12.301  49.468  1.00 63.45           C  
ATOM    646  N   GLY A  84      37.699  10.617  45.196  1.00 39.19           N  
ATOM    647  CA  GLY A  84      37.876   9.600  44.168  1.00 43.50           C  
ATOM    648  C   GLY A  84      38.708   8.401  44.598  1.00 44.65           C  
ATOM    649  O   GLY A  84      39.497   8.381  45.536  1.00 37.69           O  
ATOM    650  N   TYR A  85      38.523   7.367  43.800  1.00 47.21           N  
ATOM    651  CA  TYR A  85      39.249   6.126  43.965  1.00 52.51           C  
ATOM    652  C   TYR A  85      39.833   5.697  42.629  1.00 44.68           C  
ATOM    653  O   TYR A  85      39.161   5.655  41.592  1.00 35.85           O  
ATOM    654  CB  TYR A  85      38.269   5.107  44.563  1.00 62.44           C  
ATOM    655  CG  TYR A  85      38.962   3.781  44.800  1.00 77.62           C  
ATOM    656  CD1 TYR A  85      39.829   3.632  45.885  1.00 84.22           C  
ATOM    657  CD2 TYR A  85      38.750   2.716  43.937  1.00 81.20           C  
ATOM    658  CE1 TYR A  85      40.474   2.425  46.105  1.00 90.45           C  
ATOM    659  CE2 TYR A  85      39.389   1.510  44.156  1.00 90.16           C  
ATOM    660  CZ  TYR A  85      40.244   1.373  45.235  1.00 93.94           C  
ATOM    661  OH  TYR A  85      40.876   0.164  45.442  1.00 96.76           O  
ATOM    662  N   PRO A  86      41.108   5.367  42.596  1.00 46.56           N  
ATOM    663  CA  PRO A  86      41.753   4.916  41.374  1.00 50.29           C  
ATOM    664  C   PRO A  86      41.413   3.497  40.971  1.00 47.25           C  
ATOM    665  O   PRO A  86      42.007   2.602  41.549  1.00 54.89           O  
ATOM    666  CB  PRO A  86      43.263   4.988  41.675  1.00 48.17           C  
ATOM    667  CG  PRO A  86      43.365   4.964  43.156  1.00 54.87           C  
ATOM    668  CD  PRO A  86      42.033   5.376  43.749  1.00 51.18           C  
ATOM    669  N   ILE A  87      40.537   3.231  40.047  1.00 51.11           N  
ATOM    670  CA  ILE A  87      40.214   1.941  39.490  1.00 55.63           C  
ATOM    671  C   ILE A  87      41.428   1.305  38.768  1.00 54.33           C  
ATOM    672  O   ILE A  87      41.596   0.093  38.878  1.00 54.13           O  
ATOM    673  CB  ILE A  87      39.095   2.010  38.417  1.00 55.37           C  
ATOM    674  CG1 ILE A  87      37.836   2.623  38.990  1.00 60.23           C  
ATOM    675  CG2 ILE A  87      38.814   0.615  37.870  1.00 62.36           C  
ATOM    676  CD1 ILE A  87      37.527   2.174  40.406  1.00 66.13           C  
ATOM    677  N   THR A  88      42.191   2.071  38.009  1.00 46.79           N  
ATOM    678  CA  THR A  88      43.379   1.679  37.299  1.00 44.97           C  
ATOM    679  C   THR A  88      44.439   2.773  37.514  1.00 48.11           C  
ATOM    680  O   THR A  88      44.203   3.609  38.385  1.00 52.61           O  
ATOM    681  CB  THR A  88      43.239   1.438  35.798  1.00 47.23           C  
ATOM    682  OG1 THR A  88      43.036   2.703  35.111  1.00 45.29           O  
ATOM    683  CG2 THR A  88      42.110   0.466  35.476  1.00 40.88           C  
ATOM    684  N   ASP A  89      45.535   2.824  36.768  1.00 47.10           N  
ATOM    685  CA  ASP A  89      46.538   3.860  36.983  1.00 50.64           C  
ATOM    686  C   ASP A  89      46.180   5.127  36.185  1.00 48.21           C  
ATOM    687  O   ASP A  89      46.746   6.202  36.422  1.00 44.36           O  
ATOM    688  CB  ASP A  89      47.956   3.464  36.529  1.00 59.90           C  
ATOM    689  CG  ASP A  89      48.554   2.268  37.240  1.00 66.96           C  
ATOM    690  OD1 ASP A  89      48.622   2.239  38.495  1.00 60.83           O  
ATOM    691  OD2 ASP A  89      48.959   1.337  36.489  1.00 65.84           O  
ATOM    692  N   ASP A  90      45.283   4.916  35.240  1.00 39.31           N  
ATOM    693  CA  ASP A  90      44.764   5.898  34.341  1.00 43.09           C  
ATOM    694  C   ASP A  90      43.302   6.309  34.598  1.00 46.12           C  
ATOM    695  O   ASP A  90      42.905   7.412  34.203  1.00 45.24           O  
ATOM    696  CB  ASP A  90      44.843   5.272  32.923  1.00 41.67           C  
ATOM    697  CG  ASP A  90      46.231   5.198  32.326  1.00 46.94           C  
ATOM    698  OD1 ASP A  90      47.239   5.798  32.801  1.00 40.21           O  
ATOM    699  OD2 ASP A  90      46.312   4.478  31.299  1.00 43.61           O  
ATOM    700  N   LEU A  91      42.468   5.476  35.188  1.00 39.31           N  
ATOM    701  CA  LEU A  91      41.089   5.728  35.416  1.00 37.51           C  
ATOM    702  C   LEU A  91      40.638   5.917  36.853  1.00 43.05           C  
ATOM    703  O   LEU A  91      40.806   5.031  37.711  1.00 43.01           O  
ATOM    704  CB  LEU A  91      40.257   4.556  34.857  1.00 45.35           C  
ATOM    705  CG  LEU A  91      39.169   4.857  33.849  1.00 54.23           C  
ATOM    706  CD1 LEU A  91      37.958   3.948  34.104  1.00 63.21           C  
ATOM    707  CD2 LEU A  91      38.691   6.303  33.892  1.00 58.24           C  
ATOM    708  N   ASP A  92      40.047   7.100  37.118  1.00 38.56           N  
ATOM    709  CA  ASP A  92      39.478   7.361  38.430  1.00 37.73           C  
ATOM    710  C   ASP A  92      37.933   7.456  38.345  1.00 32.05           C  
ATOM    711  O   ASP A  92      37.376   7.842  37.304  1.00 33.63           O  
ATOM    712  CB  ASP A  92      39.885   8.627  39.110  1.00 41.63           C  
ATOM    713  CG  ASP A  92      41.259   8.776  39.651  1.00 42.87           C  
ATOM    714  OD1 ASP A  92      41.889   7.835  40.122  1.00 53.51           O  
ATOM    715  OD2 ASP A  92      41.776   9.920  39.614  1.00 58.90           O  
ATOM    716  N   ILE A  93      37.321   7.064  39.443  1.00 28.32           N  
ATOM    717  CA  ILE A  93      35.854   7.247  39.561  1.00 40.85           C  
ATOM    718  C   ILE A  93      35.734   8.249  40.739  1.00 33.18           C  
ATOM    719  O   ILE A  93      36.562   8.221  41.650  1.00 32.00           O  
ATOM    720  CB  ILE A  93      34.930   6.058  39.726  1.00 48.39           C  
ATOM    721  CG1 ILE A  93      35.171   5.325  41.049  1.00 53.58           C  
ATOM    722  CG2 ILE A  93      35.109   5.090  38.564  1.00 55.60           C  
ATOM    723  CD1 ILE A  93      34.292   4.124  41.258  1.00 63.82           C  
ATOM    724  N   TYR A  94      34.816   9.175  40.708  1.00 31.06           N  
ATOM    725  CA  TYR A  94      34.749  10.186  41.757  1.00 31.94           C  
ATOM    726  C   TYR A  94      33.328  10.701  41.884  1.00 28.31           C  
ATOM    727  O   TYR A  94      32.428  10.423  41.073  1.00 27.85           O  
ATOM    728  CB  TYR A  94      35.710  11.392  41.468  1.00 30.22           C  
ATOM    729  CG  TYR A  94      35.264  12.197  40.259  1.00 27.72           C  
ATOM    730  CD1 TYR A  94      34.302  13.204  40.373  1.00 21.92           C  
ATOM    731  CD2 TYR A  94      35.770  11.896  38.979  1.00 22.80           C  
ATOM    732  CE1 TYR A  94      33.897  13.920  39.275  1.00 29.93           C  
ATOM    733  CE2 TYR A  94      35.362  12.599  37.863  1.00 23.92           C  
ATOM    734  CZ  TYR A  94      34.411  13.620  38.016  1.00 32.44           C  
ATOM    735  OH  TYR A  94      33.974  14.345  36.925  1.00 27.37           O  
ATOM    736  N   THR A  95      33.182  11.421  42.982  1.00 25.21           N  
ATOM    737  CA  THR A  95      31.963  12.124  43.309  1.00 33.88           C  
ATOM    738  C   THR A  95      32.457  13.501  43.790  1.00 29.30           C  
ATOM    739  O   THR A  95      33.574  13.589  44.309  1.00 22.78           O  
ATOM    740  CB  THR A  95      30.996  11.550  44.373  1.00 36.35           C  
ATOM    741  OG1 THR A  95      31.695  11.379  45.619  1.00 39.34           O  
ATOM    742  CG2 THR A  95      30.480  10.189  43.922  1.00 44.22           C  
ATOM    743  N   ARG A  96      31.583  14.455  43.592  1.00 30.80           N  
ATOM    744  CA  ARG A  96      31.838  15.813  44.081  1.00 29.37           C  
ATOM    745  C   ARG A  96      30.635  16.154  44.965  1.00 24.89           C  
ATOM    746  O   ARG A  96      29.510  15.805  44.597  1.00 18.38           O  
ATOM    747  CB  ARG A  96      31.973  16.820  42.935  1.00 19.12           C  
ATOM    748  CG  ARG A  96      33.199  16.596  42.100  1.00 18.38           C  
ATOM    749  CD  ARG A  96      33.539  17.631  41.062  1.00 26.92           C  
ATOM    750  NE  ARG A  96      32.527  17.798  39.985  1.00 26.47           N  
ATOM    751  CZ  ARG A  96      31.593  18.759  40.049  1.00 24.94           C  
ATOM    752  NH1 ARG A  96      31.562  19.581  41.121  1.00 15.97           N  
ATOM    753  NH2 ARG A  96      30.673  18.901  39.096  1.00 26.45           N  
ATOM    754  N   LEU A  97      30.886  16.798  46.089  1.00 24.48           N  
ATOM    755  CA  LEU A  97      29.780  17.233  46.924  1.00 26.00           C  
ATOM    756  C   LEU A  97      30.093  18.609  47.492  1.00 28.42           C  
ATOM    757  O   LEU A  97      31.220  18.885  47.892  1.00 24.96           O  
ATOM    758  CB  LEU A  97      29.339  16.251  47.972  1.00 38.87           C  
ATOM    759  CG  LEU A  97      30.275  15.873  49.089  1.00 41.30           C  
ATOM    760  CD1 LEU A  97      29.489  15.179  50.192  1.00 50.68           C  
ATOM    761  CD2 LEU A  97      31.384  14.946  48.585  1.00 51.88           C  
ATOM    762  N   GLY A  98      29.059  19.472  47.441  1.00 27.63           N  
ATOM    763  CA  GLY A  98      29.228  20.829  47.936  1.00 20.20           C  
ATOM    764  C   GLY A  98      28.045  21.720  47.641  1.00 25.37           C  
ATOM    765  O   GLY A  98      26.862  21.335  47.632  1.00 23.85           O  
ATOM    766  N   GLY A  99      28.383  23.006  47.405  1.00 27.34           N  
ATOM    767  CA  GLY A  99      27.287  23.954  47.190  1.00 26.38           C  
ATOM    768  C   GLY A  99      27.502  24.847  46.006  1.00 28.22           C  
ATOM    769  O   GLY A  99      28.609  25.049  45.513  1.00 35.66           O  
ATOM    770  N   MET A 100      26.392  25.350  45.505  1.00 33.13           N  
ATOM    771  CA  MET A 100      26.276  26.237  44.385  1.00 35.05           C  
ATOM    772  C   MET A 100      25.283  27.405  44.569  1.00 37.43           C  
ATOM    773  O   MET A 100      24.142  27.341  45.021  1.00 31.38           O  
ATOM    774  CB  MET A 100      25.756  25.427  43.195  1.00 34.61           C  
ATOM    775  CG  MET A 100      25.819  26.261  41.910  1.00 44.29           C  
ATOM    776  SD  MET A 100      24.971  25.311  40.599  1.00 47.61           S  
ATOM    777  CE  MET A 100      26.423  25.250  39.471  1.00 54.87           C  
ATOM    778  N   VAL A 101      25.796  28.540  44.169  1.00 38.13           N  
ATOM    779  CA  VAL A 101      25.133  29.806  44.113  1.00 42.14           C  
ATOM    780  C   VAL A 101      24.708  29.990  42.644  1.00 41.16           C  
ATOM    781  O   VAL A 101      25.568  30.130  41.752  1.00 38.16           O  
ATOM    782  CB  VAL A 101      26.049  30.978  44.549  1.00 44.38           C  
ATOM    783  CG1 VAL A 101      25.291  32.297  44.461  1.00 47.57           C  
ATOM    784  CG2 VAL A 101      26.508  30.763  45.982  1.00 51.58           C  
ATOM    785  N   TRP A 102      23.417  30.006  42.390  1.00 37.79           N  
ATOM    786  CA  TRP A 102      22.968  30.222  41.034  1.00 40.44           C  
ATOM    787  C   TRP A 102      21.952  31.339  40.810  1.00 47.45           C  
ATOM    788  O   TRP A 102      21.247  31.920  41.630  1.00 44.00           O  
ATOM    789  CB  TRP A 102      22.348  28.896  40.587  1.00 37.50           C  
ATOM    790  CG  TRP A 102      21.219  28.477  41.479  1.00 53.62           C  
ATOM    791  CD1 TRP A 102      21.270  27.636  42.543  1.00 55.33           C  
ATOM    792  CD2 TRP A 102      19.844  28.877  41.356  1.00 57.58           C  
ATOM    793  NE1 TRP A 102      20.028  27.451  43.088  1.00 57.13           N  
ATOM    794  CE2 TRP A 102      19.129  28.207  42.382  1.00 61.20           C  
ATOM    795  CE3 TRP A 102      19.169  29.724  40.478  1.00 50.53           C  
ATOM    796  CZ2 TRP A 102      17.757  28.369  42.576  1.00 61.59           C  
ATOM    797  CZ3 TRP A 102      17.802  29.868  40.666  1.00 60.79           C  
ATOM    798  CH2 TRP A 102      17.114  29.206  41.692  1.00 63.70           C  
ATOM    799  N   ARG A 103      21.781  31.601  39.510  1.00 50.62           N  
ATOM    800  CA  ARG A 103      20.893  32.586  38.984  1.00 52.18           C  
ATOM    801  C   ARG A 103      20.275  32.189  37.653  1.00 53.47           C  
ATOM    802  O   ARG A 103      21.011  31.993  36.692  1.00 52.72           O  
ATOM    803  CB  ARG A 103      21.673  33.899  38.734  1.00 55.36           C  
ATOM    804  CG  ARG A 103      20.717  35.006  38.224  1.00 59.01           C  
ATOM    805  CD  ARG A 103      21.522  36.270  37.959  1.00 63.46           C  
ATOM    806  NE  ARG A 103      20.886  37.173  37.030  1.00 68.77           N  
ATOM    807  CZ  ARG A 103      20.080  38.184  37.352  1.00 69.20           C  
ATOM    808  NH1 ARG A 103      19.805  38.427  38.614  1.00 67.55           N  
ATOM    809  NH2 ARG A 103      19.541  38.948  36.411  1.00 62.02           N  
ATOM    810  N   ALA A 104      18.951  32.139  37.588  1.00 54.79           N  
ATOM    811  CA  ALA A 104      18.266  31.883  36.313  1.00 54.08           C  
ATOM    812  C   ALA A 104      17.642  33.216  35.855  1.00 58.28           C  
ATOM    813  O   ALA A 104      17.080  34.013  36.619  1.00 57.59           O  
ATOM    814  CB  ALA A 104      17.294  30.752  36.415  1.00 41.87           C  
ATOM    815  N   ASP A 105      17.834  33.539  34.597  1.00 58.89           N  
ATOM    816  CA  ASP A 105      17.296  34.718  33.945  1.00 56.02           C  
ATOM    817  C   ASP A 105      16.292  34.248  32.880  1.00 61.77           C  
ATOM    818  O   ASP A 105      16.678  33.539  31.956  1.00 62.41           O  
ATOM    819  CB  ASP A 105      18.328  35.613  33.318  1.00 42.18           C  
ATOM    820  CG  ASP A 105      19.039  36.490  34.311  1.00 56.82           C  
ATOM    821  OD1 ASP A 105      18.491  37.531  34.726  1.00 67.03           O  
ATOM    822  OD2 ASP A 105      20.178  36.171  34.711  1.00 69.89           O  
ATOM    823  N   THR A 106      15.020  34.605  33.033  1.00 68.61           N  
ATOM    824  CA  THR A 106      14.012  34.251  32.058  1.00 74.42           C  
ATOM    825  C   THR A 106      13.588  35.508  31.266  1.00 77.29           C  
ATOM    826  O   THR A 106      14.074  36.624  31.434  1.00 66.18           O  
ATOM    827  CB  THR A 106      12.776  33.537  32.585  1.00 78.35           C  
ATOM    828  OG1 THR A 106      12.219  34.250  33.700  1.00 82.54           O  
ATOM    829  CG2 THR A 106      13.097  32.117  33.038  1.00 78.82           C  
ATOM    830  N   TYR A 107      12.695  35.231  30.332  1.00 85.80           N  
ATOM    831  CA  TYR A 107      12.111  36.181  29.422  1.00 93.31           C  
ATOM    832  C   TYR A 107      10.727  35.690  28.961  1.00 95.28           C  
ATOM    833  O   TYR A 107      10.467  34.502  28.822  1.00 92.58           O  
ATOM    834  CB  TYR A 107      12.962  36.504  28.206  1.00 97.20           C  
ATOM    835  CG  TYR A 107      12.503  37.780  27.522  1.00105.51           C  
ATOM    836  CD1 TYR A 107      12.829  39.016  28.068  1.00107.43           C  
ATOM    837  CD2 TYR A 107      11.751  37.760  26.355  1.00108.37           C  
ATOM    838  CE1 TYR A 107      12.419  40.194  27.476  1.00108.68           C  
ATOM    839  CE2 TYR A 107      11.338  38.938  25.745  1.00110.13           C  
ATOM    840  CZ  TYR A 107      11.672  40.153  26.312  1.00109.94           C  
ATOM    841  OH  TYR A 107      11.283  41.346  25.737  1.00105.25           O  
ATOM    842  N   SER A 108       9.847  36.660  28.805  1.00 99.31           N  
ATOM    843  CA  SER A 108       8.455  36.464  28.409  1.00102.94           C  
ATOM    844  C   SER A 108       8.067  37.636  27.512  1.00105.85           C  
ATOM    845  O   SER A 108       8.696  38.696  27.637  1.00106.69           O  
ATOM    846  CB  SER A 108       7.535  36.394  29.628  1.00 97.68           C  
ATOM    847  OG  SER A 108       6.226  35.993  29.289  1.00 91.28           O  
ATOM    848  N   ASN A 109       7.106  37.443  26.622  1.00110.07           N  
ATOM    849  CA  ASN A 109       6.713  38.554  25.725  1.00112.55           C  
ATOM    850  C   ASN A 109       5.685  39.421  26.463  1.00108.61           C  
ATOM    851  O   ASN A 109       5.688  40.647  26.379  1.00104.03           O  
ATOM    852  CB  ASN A 109       6.222  38.081  24.378  1.00118.66           C  
ATOM    853  CG  ASN A 109       5.859  36.613  24.289  1.00123.13           C  
ATOM    854  OD1 ASN A 109       6.599  35.815  23.701  1.00124.40           O  
ATOM    855  ND2 ASN A 109       4.719  36.248  24.874  1.00122.79           N  
ATOM    856  N   VAL A 110       4.845  38.719  27.223  1.00105.49           N  
ATOM    857  CA  VAL A 110       3.827  39.344  28.045  1.00103.77           C  
ATOM    858  C   VAL A 110       4.522  40.129  29.178  1.00101.22           C  
ATOM    859  O   VAL A 110       4.595  41.350  29.173  1.00100.46           O  
ATOM    860  CB  VAL A 110       2.891  38.310  28.714  1.00102.79           C  
ATOM    861  CG1 VAL A 110       1.765  38.997  29.489  1.00100.57           C  
ATOM    862  CG2 VAL A 110       2.310  37.331  27.717  1.00102.85           C  
ATOM    863  N   TYR A 111       5.059  39.366  30.105  1.00 97.26           N  
ATOM    864  CA  TYR A 111       5.711  39.725  31.319  1.00 92.52           C  
ATOM    865  C   TYR A 111       7.106  40.298  31.296  1.00 83.30           C  
ATOM    866  O   TYR A 111       7.520  40.892  32.309  1.00 71.23           O  
ATOM    867  CB  TYR A 111       5.716  38.461  32.238  1.00101.22           C  
ATOM    868  CG  TYR A 111       4.309  37.973  32.531  1.00109.69           C  
ATOM    869  CD1 TYR A 111       3.413  38.788  33.221  1.00111.85           C  
ATOM    870  CD2 TYR A 111       3.876  36.714  32.121  1.00111.58           C  
ATOM    871  CE1 TYR A 111       2.127  38.364  33.503  1.00111.77           C  
ATOM    872  CE2 TYR A 111       2.585  36.289  32.396  1.00112.28           C  
ATOM    873  CZ  TYR A 111       1.723  37.117  33.086  1.00112.38           C  
ATOM    874  OH  TYR A 111       0.443  36.708  33.370  1.00113.71           O  
ATOM    875  N   GLY A 112       7.857  40.182  30.209  1.00 80.35           N  
ATOM    876  CA  GLY A 112       9.221  40.736  30.170  1.00 77.58           C  
ATOM    877  C   GLY A 112      10.221  39.864  30.958  1.00 73.60           C  
ATOM    878  O   GLY A 112      10.000  38.677  31.267  1.00 66.36           O  
ATOM    879  N   LYS A 113      11.343  40.487  31.316  1.00 66.66           N  
ATOM    880  CA  LYS A 113      12.405  39.873  32.071  1.00 65.89           C  
ATOM    881  C   LYS A 113      12.097  39.581  33.556  1.00 65.87           C  
ATOM    882  O   LYS A 113      11.546  40.413  34.279  1.00 62.64           O  
ATOM    883  CB  LYS A 113      13.654  40.790  32.090  1.00 57.94           C  
ATOM    884  CG  LYS A 113      14.300  41.055  30.759  1.00 60.30           C  
ATOM    885  CD  LYS A 113      15.525  41.944  30.903  1.00 67.00           C  
ATOM    886  CE  LYS A 113      15.222  43.412  30.656  1.00 73.03           C  
ATOM    887  NZ  LYS A 113      15.748  44.253  31.790  1.00 71.88           N  
ATOM    888  N   ASN A 114      12.510  38.400  34.017  1.00 61.19           N  
ATOM    889  CA  ASN A 114      12.508  37.932  35.348  1.00 60.92           C  
ATOM    890  C   ASN A 114      13.806  37.171  35.676  1.00 64.85           C  
ATOM    891  O   ASN A 114      14.510  36.628  34.846  1.00 65.51           O  
ATOM    892  CB  ASN A 114      11.320  37.121  35.854  1.00 60.51           C  
ATOM    893  CG  ASN A 114      11.076  37.437  37.338  1.00 58.42           C  
ATOM    894  OD1 ASN A 114      11.630  38.403  37.904  1.00 53.52           O  
ATOM    895  ND2 ASN A 114      10.246  36.634  37.984  1.00 62.56           N  
ATOM    896  N   HIS A 115      14.164  37.178  36.954  1.00 67.94           N  
ATOM    897  CA  HIS A 115      15.342  36.498  37.443  1.00 67.42           C  
ATOM    898  C   HIS A 115      14.970  35.747  38.729  1.00 67.79           C  
ATOM    899  O   HIS A 115      13.937  35.985  39.355  1.00 65.91           O  
ATOM    900  CB  HIS A 115      16.535  37.387  37.664  1.00 68.32           C  
ATOM    901  CG  HIS A 115      16.480  38.308  38.830  1.00 76.63           C  
ATOM    902  ND1 HIS A 115      17.007  39.588  38.762  1.00 77.48           N  
ATOM    903  CD2 HIS A 115      15.987  38.166  40.089  1.00 79.58           C  
ATOM    904  CE1 HIS A 115      16.839  40.184  39.923  1.00 83.14           C  
ATOM    905  NE2 HIS A 115      16.220  39.343  40.749  1.00 83.95           N  
ATOM    906  N   ASP A 116      15.879  34.858  39.072  1.00 66.18           N  
ATOM    907  CA  ASP A 116      15.707  34.054  40.285  1.00 65.80           C  
ATOM    908  C   ASP A 116      17.086  33.749  40.848  1.00 61.57           C  
ATOM    909  O   ASP A 116      18.092  33.774  40.148  1.00 61.20           O  
ATOM    910  CB  ASP A 116      14.867  32.841  40.029  1.00 69.59           C  
ATOM    911  CG  ASP A 116      14.201  32.269  41.257  1.00 75.72           C  
ATOM    912  OD1 ASP A 116      14.254  32.863  42.355  1.00 72.71           O  
ATOM    913  OD2 ASP A 116      13.602  31.172  41.077  1.00 80.38           O  
ATOM    914  N   THR A 117      17.147  33.561  42.141  1.00 59.27           N  
ATOM    915  CA  THR A 117      18.437  33.310  42.805  1.00 57.90           C  
ATOM    916  C   THR A 117      18.289  32.175  43.775  1.00 59.18           C  
ATOM    917  O   THR A 117      17.199  31.752  44.217  1.00 58.57           O  
ATOM    918  CB  THR A 117      18.951  34.648  43.297  1.00 62.68           C  
ATOM    919  OG1 THR A 117      19.635  35.235  42.170  1.00 58.80           O  
ATOM    920  CG2 THR A 117      19.873  34.605  44.496  1.00 69.68           C  
ATOM    921  N   GLY A 118      19.430  31.536  44.071  1.00 54.94           N  
ATOM    922  CA  GLY A 118      19.371  30.378  44.957  1.00 45.09           C  
ATOM    923  C   GLY A 118      20.742  29.960  45.407  1.00 45.90           C  
ATOM    924  O   GLY A 118      21.813  30.347  44.956  1.00 44.53           O  
ATOM    925  N   VAL A 119      20.699  29.126  46.424  1.00 47.54           N  
ATOM    926  CA  VAL A 119      21.856  28.491  47.026  1.00 41.35           C  
ATOM    927  C   VAL A 119      21.434  27.020  47.082  1.00 47.22           C  
ATOM    928  O   VAL A 119      20.308  26.666  47.424  1.00 44.65           O  
ATOM    929  CB  VAL A 119      22.317  29.041  48.329  1.00 41.41           C  
ATOM    930  CG1 VAL A 119      23.635  28.349  48.746  1.00 46.67           C  
ATOM    931  CG2 VAL A 119      22.597  30.548  48.240  1.00 41.79           C  
ATOM    932  N   SER A 120      22.323  26.141  46.575  1.00 48.44           N  
ATOM    933  CA  SER A 120      21.816  24.735  46.581  1.00 44.50           C  
ATOM    934  C   SER A 120      22.913  23.741  46.729  1.00 44.09           C  
ATOM    935  O   SER A 120      24.065  23.918  46.311  1.00 44.88           O  
ATOM    936  CB  SER A 120      21.028  24.693  45.260  1.00 46.81           C  
ATOM    937  OG  SER A 120      20.338  23.518  45.014  1.00 55.21           O  
ATOM    938  N   PRO A 121      22.639  22.608  47.362  1.00 44.67           N  
ATOM    939  CA  PRO A 121      23.625  21.538  47.458  1.00 43.27           C  
ATOM    940  C   PRO A 121      23.880  21.017  46.033  1.00 41.46           C  
ATOM    941  O   PRO A 121      22.932  20.914  45.226  1.00 29.97           O  
ATOM    942  CB  PRO A 121      22.932  20.456  48.293  1.00 38.86           C  
ATOM    943  CG  PRO A 121      21.789  21.169  48.941  1.00 44.30           C  
ATOM    944  CD  PRO A 121      21.336  22.206  47.942  1.00 43.14           C  
ATOM    945  N   VAL A 122      25.145  20.667  45.720  1.00 39.03           N  
ATOM    946  CA  VAL A 122      25.416  20.076  44.417  1.00 38.73           C  
ATOM    947  C   VAL A 122      26.103  18.697  44.587  1.00 35.91           C  
ATOM    948  O   VAL A 122      26.953  18.480  45.450  1.00 40.62           O  
ATOM    949  CB  VAL A 122      26.449  20.755  43.483  1.00 34.04           C  
ATOM    950  CG1 VAL A 122      25.881  20.841  42.102  1.00 33.38           C  
ATOM    951  CG2 VAL A 122      27.086  21.955  44.055  1.00 22.15           C  
ATOM    952  N   PHE A 123      25.770  17.806  43.695  1.00 34.23           N  
ATOM    953  CA  PHE A 123      26.337  16.477  43.672  1.00 31.45           C  
ATOM    954  C   PHE A 123      26.753  16.079  42.274  1.00 29.36           C  
ATOM    955  O   PHE A 123      26.101  16.423  41.289  1.00 34.57           O  
ATOM    956  CB  PHE A 123      25.329  15.457  44.212  1.00 38.05           C  
ATOM    957  CG  PHE A 123      24.832  15.766  45.610  1.00 44.14           C  
ATOM    958  CD1 PHE A 123      25.687  15.689  46.690  1.00 45.06           C  
ATOM    959  CD2 PHE A 123      23.519  16.172  45.838  1.00 43.17           C  
ATOM    960  CE1 PHE A 123      25.240  15.981  47.971  1.00 47.88           C  
ATOM    961  CE2 PHE A 123      23.074  16.440  47.097  1.00 46.16           C  
ATOM    962  CZ  PHE A 123      23.933  16.346  48.179  1.00 44.13           C  
ATOM    963  N   ALA A 124      27.837  15.298  42.180  1.00 27.94           N  
ATOM    964  CA  ALA A 124      28.242  14.797  40.862  1.00 25.83           C  
ATOM    965  C   ALA A 124      28.882  13.412  41.007  1.00 28.07           C  
ATOM    966  O   ALA A 124      29.470  13.090  42.041  1.00 25.49           O  
ATOM    967  CB  ALA A 124      29.196  15.697  40.115  1.00 23.88           C  
ATOM    968  N   GLY A 125      28.732  12.659  39.939  1.00 26.38           N  
ATOM    969  CA  GLY A 125      29.432  11.334  39.910  1.00 33.92           C  
ATOM    970  C   GLY A 125      30.094  11.303  38.515  1.00 32.98           C  
ATOM    971  O   GLY A 125      29.526  11.753  37.510  1.00 31.41           O  
ATOM    972  N   GLY A 126      31.323  10.831  38.429  1.00 30.16           N  
ATOM    973  CA  GLY A 126      31.946  10.858  37.086  1.00 26.04           C  
ATOM    974  C   GLY A 126      33.153   9.950  37.010  1.00 27.50           C  
ATOM    975  O   GLY A 126      33.531   9.224  37.931  1.00 26.85           O  
ATOM    976  N   VAL A 127      33.761   9.991  35.834  1.00 29.55           N  
ATOM    977  CA  VAL A 127      34.991   9.221  35.575  1.00 30.43           C  
ATOM    978  C   VAL A 127      35.993  10.213  35.016  1.00 28.63           C  
ATOM    979  O   VAL A 127      35.613  11.128  34.250  1.00 24.49           O  
ATOM    980  CB  VAL A 127      34.681   8.020  34.687  1.00 33.85           C  
ATOM    981  CG1 VAL A 127      35.648   7.809  33.563  1.00 44.33           C  
ATOM    982  CG2 VAL A 127      34.653   6.745  35.560  1.00 42.52           C  
ATOM    983  N   GLU A 128      37.228  10.085  35.419  1.00 28.45           N  
ATOM    984  CA  GLU A 128      38.309  10.942  34.948  1.00 30.67           C  
ATOM    985  C   GLU A 128      39.402  10.046  34.318  1.00 36.55           C  
ATOM    986  O   GLU A 128      39.859   9.113  34.983  1.00 28.27           O  
ATOM    987  CB  GLU A 128      38.911  11.779  36.064  1.00 28.26           C  
ATOM    988  CG  GLU A 128      39.775  12.888  35.495  1.00 38.83           C  
ATOM    989  CD  GLU A 128      39.948  14.087  36.386  1.00 36.94           C  
ATOM    990  OE1 GLU A 128      40.831  14.066  37.250  1.00 35.39           O  
ATOM    991  OE2 GLU A 128      39.213  15.082  36.207  1.00 50.52           O  
ATOM    992  N   TYR A 129      39.755  10.265  33.055  1.00 35.44           N  
ATOM    993  CA  TYR A 129      40.764   9.415  32.403  1.00 39.37           C  
ATOM    994  C   TYR A 129      42.006  10.207  32.047  1.00 36.25           C  
ATOM    995  O   TYR A 129      41.973  11.157  31.263  1.00 35.93           O  
ATOM    996  CB  TYR A 129      40.138   8.675  31.240  1.00 46.89           C  
ATOM    997  CG  TYR A 129      41.016   7.752  30.448  1.00 64.58           C  
ATOM    998  CD1 TYR A 129      41.942   8.281  29.562  1.00 72.80           C  
ATOM    999  CD2 TYR A 129      40.952   6.366  30.552  1.00 71.30           C  
ATOM   1000  CE1 TYR A 129      42.779   7.478  28.814  1.00 80.17           C  
ATOM   1001  CE2 TYR A 129      41.779   5.551  29.792  1.00 76.50           C  
ATOM   1002  CZ  TYR A 129      42.690   6.105  28.926  1.00 81.20           C  
ATOM   1003  OH  TYR A 129      43.543   5.336  28.150  1.00 82.94           O  
ATOM   1004  N   ALA A 130      43.145   9.838  32.628  1.00 38.38           N  
ATOM   1005  CA  ALA A 130      44.405  10.538  32.364  1.00 43.20           C  
ATOM   1006  C   ALA A 130      44.997  10.035  31.043  1.00 45.10           C  
ATOM   1007  O   ALA A 130      45.471   8.919  31.033  1.00 49.67           O  
ATOM   1008  CB  ALA A 130      45.463  10.346  33.418  1.00 35.00           C  
ATOM   1009  N   ILE A 131      44.898  10.863  30.025  1.00 48.95           N  
ATOM   1010  CA  ILE A 131      45.417  10.534  28.715  1.00 50.97           C  
ATOM   1011  C   ILE A 131      46.960  10.460  28.864  1.00 49.39           C  
ATOM   1012  O   ILE A 131      47.595   9.490  28.492  1.00 51.54           O  
ATOM   1013  CB  ILE A 131      45.121  11.629  27.674  1.00 53.22           C  
ATOM   1014  CG1 ILE A 131      43.678  12.081  27.659  1.00 52.20           C  
ATOM   1015  CG2 ILE A 131      45.519  11.088  26.285  1.00 63.46           C  
ATOM   1016  CD1 ILE A 131      42.679  10.952  27.372  1.00 50.81           C  
ATOM   1017  N   THR A 132      47.498  11.541  29.394  1.00 36.66           N  
ATOM   1018  CA  THR A 132      48.877  11.754  29.675  1.00 41.51           C  
ATOM   1019  C   THR A 132      48.901  12.280  31.110  1.00 44.04           C  
ATOM   1020  O   THR A 132      47.850  12.455  31.703  1.00 47.31           O  
ATOM   1021  CB  THR A 132      49.555  12.799  28.773  1.00 44.22           C  
ATOM   1022  OG1 THR A 132      49.282  14.093  29.335  1.00 40.70           O  
ATOM   1023  CG2 THR A 132      49.091  12.726  27.348  1.00 39.84           C  
ATOM   1024  N   PRO A 133      50.053  12.528  31.661  1.00 50.42           N  
ATOM   1025  CA  PRO A 133      50.128  12.987  33.046  1.00 53.53           C  
ATOM   1026  C   PRO A 133      49.629  14.402  33.193  1.00 49.09           C  
ATOM   1027  O   PRO A 133      49.246  14.766  34.322  1.00 47.28           O  
ATOM   1028  CB  PRO A 133      51.577  12.754  33.438  1.00 54.03           C  
ATOM   1029  CG  PRO A 133      52.111  11.836  32.370  1.00 54.57           C  
ATOM   1030  CD  PRO A 133      51.417  12.330  31.101  1.00 51.52           C  
ATOM   1031  N   GLU A 134      49.557  15.206  32.134  1.00 41.57           N  
ATOM   1032  CA  GLU A 134      49.024  16.556  32.302  1.00 45.19           C  
ATOM   1033  C   GLU A 134      47.628  16.749  31.714  1.00 41.41           C  
ATOM   1034  O   GLU A 134      47.013  17.809  31.932  1.00 40.60           O  
ATOM   1035  CB  GLU A 134      49.922  17.633  31.702  1.00 47.48           C  
ATOM   1036  CG  GLU A 134      50.673  17.135  30.470  1.00 70.41           C  
ATOM   1037  CD  GLU A 134      52.080  16.685  30.907  1.00 73.25           C  
ATOM   1038  OE1 GLU A 134      52.572  17.353  31.842  1.00 72.65           O  
ATOM   1039  OE2 GLU A 134      52.596  15.717  30.328  1.00 73.52           O  
ATOM   1040  N   ILE A 135      47.106  15.783  30.948  1.00 34.21           N  
ATOM   1041  CA  ILE A 135      45.801  16.052  30.380  1.00 35.07           C  
ATOM   1042  C   ILE A 135      44.845  14.919  30.699  1.00 36.32           C  
ATOM   1043  O   ILE A 135      45.046  13.721  30.469  1.00 30.16           O  
ATOM   1044  CB  ILE A 135      45.746  16.654  28.993  1.00 42.22           C  
ATOM   1045  CG1 ILE A 135      45.060  15.657  28.030  1.00 28.91           C  
ATOM   1046  CG2 ILE A 135      46.907  17.286  28.232  1.00 26.61           C  
ATOM   1047  CD1 ILE A 135      43.635  16.162  27.894  1.00 37.93           C  
ATOM   1048  N   ALA A 136      43.684  15.350  31.277  1.00 30.01           N  
ATOM   1049  CA  ALA A 136      42.707  14.308  31.630  1.00 32.28           C  
ATOM   1050  C   ALA A 136      41.336  14.627  31.067  1.00 29.22           C  
ATOM   1051  O   ALA A 136      40.981  15.787  30.917  1.00 29.07           O  
ATOM   1052  CB  ALA A 136      42.645  14.202  33.176  1.00 27.96           C  
ATOM   1053  N   THR A 137      40.529  13.626  30.752  1.00 32.23           N  
ATOM   1054  CA  THR A 137      39.167  13.921  30.280  1.00 33.78           C  
ATOM   1055  C   THR A 137      38.219  13.440  31.397  1.00 34.62           C  
ATOM   1056  O   THR A 137      38.611  12.532  32.134  1.00 25.03           O  
ATOM   1057  CB  THR A 137      38.851  13.159  28.983  1.00 38.04           C  
ATOM   1058  OG1 THR A 137      39.279  11.788  29.201  1.00 34.97           O  
ATOM   1059  CG2 THR A 137      39.541  13.725  27.760  1.00 32.41           C  
ATOM   1060  N   ARG A 138      37.037  14.045  31.513  1.00 31.68           N  
ATOM   1061  CA  ARG A 138      36.044  13.655  32.451  1.00 26.52           C  
ATOM   1062  C   ARG A 138      34.660  13.493  31.781  1.00 27.59           C  
ATOM   1063  O   ARG A 138      34.289  14.144  30.839  1.00 24.55           O  
ATOM   1064  CB  ARG A 138      35.924  14.390  33.727  1.00 28.00           C  
ATOM   1065  CG  ARG A 138      35.766  15.857  33.934  1.00 31.12           C  
ATOM   1066  CD  ARG A 138      36.792  16.196  35.057  1.00 37.01           C  
ATOM   1067  NE  ARG A 138      36.238  16.894  36.128  1.00 25.55           N  
ATOM   1068  CZ  ARG A 138      36.701  17.337  37.261  1.00 33.28           C  
ATOM   1069  NH1 ARG A 138      37.950  17.117  37.656  1.00 21.94           N  
ATOM   1070  NH2 ARG A 138      35.847  18.037  38.041  1.00 30.05           N  
ATOM   1071  N   LEU A 139      33.937  12.521  32.310  1.00 25.25           N  
ATOM   1072  CA  LEU A 139      32.561  12.202  31.908  1.00 23.50           C  
ATOM   1073  C   LEU A 139      31.847  12.295  33.267  1.00 23.39           C  
ATOM   1074  O   LEU A 139      32.199  11.666  34.251  1.00 27.44           O  
ATOM   1075  CB  LEU A 139      32.466  10.925  31.175  1.00 36.55           C  
ATOM   1076  CG  LEU A 139      31.234  10.437  30.432  1.00 52.22           C  
ATOM   1077  CD1 LEU A 139      30.441   9.445  31.280  1.00 52.43           C  
ATOM   1078  CD2 LEU A 139      30.325  11.572  29.954  1.00 50.49           C  
ATOM   1079  N   GLU A 140      30.928  13.220  33.398  1.00 22.28           N  
ATOM   1080  CA  GLU A 140      30.302  13.487  34.679  1.00 26.81           C  
ATOM   1081  C   GLU A 140      28.823  13.804  34.529  1.00 26.91           C  
ATOM   1082  O   GLU A 140      28.373  14.395  33.544  1.00 21.76           O  
ATOM   1083  CB  GLU A 140      31.052  14.706  35.291  1.00 19.73           C  
ATOM   1084  CG  GLU A 140      30.479  15.205  36.595  1.00 35.79           C  
ATOM   1085  CD  GLU A 140      31.133  16.490  37.080  1.00 32.99           C  
ATOM   1086  OE1 GLU A 140      32.213  16.378  37.664  1.00 30.85           O  
ATOM   1087  OE2 GLU A 140      30.597  17.600  36.904  1.00 30.08           O  
ATOM   1088  N   TYR A 141      28.108  13.427  35.556  1.00 22.08           N  
ATOM   1089  CA  TYR A 141      26.691  13.683  35.710  1.00 28.90           C  
ATOM   1090  C   TYR A 141      26.547  14.508  37.016  1.00 27.27           C  
ATOM   1091  O   TYR A 141      26.926  14.088  38.119  1.00 32.14           O  
ATOM   1092  CB  TYR A 141      25.894  12.371  35.808  1.00 33.53           C  
ATOM   1093  CG  TYR A 141      24.439  12.666  36.118  1.00 42.09           C  
ATOM   1094  CD1 TYR A 141      23.668  13.264  35.103  1.00 47.81           C  
ATOM   1095  CD2 TYR A 141      23.864  12.418  37.355  1.00 44.04           C  
ATOM   1096  CE1 TYR A 141      22.351  13.578  35.312  1.00 46.25           C  
ATOM   1097  CE2 TYR A 141      22.520  12.721  37.585  1.00 45.18           C  
ATOM   1098  CZ  TYR A 141      21.794  13.295  36.556  1.00 52.56           C  
ATOM   1099  OH  TYR A 141      20.466  13.626  36.722  1.00 61.65           O  
ATOM   1100  N   GLN A 142      26.052  15.721  36.894  1.00 27.33           N  
ATOM   1101  CA  GLN A 142      25.877  16.606  38.061  1.00 30.45           C  
ATOM   1102  C   GLN A 142      24.403  16.828  38.369  1.00 33.45           C  
ATOM   1103  O   GLN A 142      23.555  17.076  37.481  1.00 36.09           O  
ATOM   1104  CB  GLN A 142      26.537  17.940  37.735  1.00 24.23           C  
ATOM   1105  CG  GLN A 142      26.608  18.980  38.801  1.00 35.85           C  
ATOM   1106  CD  GLN A 142      27.281  20.254  38.295  1.00 42.04           C  
ATOM   1107  OE1 GLN A 142      28.521  20.335  38.140  1.00 39.89           O  
ATOM   1108  NE2 GLN A 142      26.421  21.234  38.047  1.00 33.15           N  
ATOM   1109  N   TRP A 143      24.049  16.813  39.640  1.00 34.10           N  
ATOM   1110  CA  TRP A 143      22.648  17.108  39.967  1.00 42.45           C  
ATOM   1111  C   TRP A 143      22.615  17.946  41.228  1.00 45.74           C  
ATOM   1112  O   TRP A 143      23.541  18.029  42.010  1.00 42.04           O  
ATOM   1113  CB  TRP A 143      21.743  15.894  40.069  1.00 40.76           C  
ATOM   1114  CG  TRP A 143      21.975  15.022  41.265  1.00 44.69           C  
ATOM   1115  CD1 TRP A 143      21.247  15.014  42.421  1.00 48.82           C  
ATOM   1116  CD2 TRP A 143      23.017  14.049  41.435  1.00 48.05           C  
ATOM   1117  NE1 TRP A 143      21.767  14.085  43.297  1.00 47.31           N  
ATOM   1118  CE2 TRP A 143      22.848  13.480  42.725  1.00 48.31           C  
ATOM   1119  CE3 TRP A 143      24.092  13.613  40.630  1.00 44.90           C  
ATOM   1120  CZ2 TRP A 143      23.706  12.492  43.215  1.00 47.47           C  
ATOM   1121  CZ3 TRP A 143      24.949  12.632  41.109  1.00 46.96           C  
ATOM   1122  CH2 TRP A 143      24.749  12.086  42.391  1.00 52.32           C  
ATOM   1123  N   THR A 144      21.492  18.627  41.375  1.00 63.67           N  
ATOM   1124  CA  THR A 144      21.222  19.425  42.586  1.00 69.89           C  
ATOM   1125  C   THR A 144      19.879  18.879  43.091  1.00 75.75           C  
ATOM   1126  O   THR A 144      19.023  18.582  42.245  1.00 73.03           O  
ATOM   1127  CB  THR A 144      21.108  20.922  42.356  1.00 62.89           C  
ATOM   1128  OG1 THR A 144      19.779  21.141  41.885  1.00 63.17           O  
ATOM   1129  CG2 THR A 144      22.130  21.448  41.354  1.00 51.70           C  
ATOM   1130  N   ASN A 145      19.748  18.680  44.398  1.00 87.28           N  
ATOM   1131  CA  ASN A 145      18.402  18.166  44.817  1.00 98.95           C  
ATOM   1132  C   ASN A 145      17.608  19.404  45.222  1.00105.90           C  
ATOM   1133  O   ASN A 145      18.212  20.356  45.763  1.00105.00           O  
ATOM   1134  CB  ASN A 145      18.493  17.056  45.797  1.00 97.07           C  
ATOM   1135  CG  ASN A 145      19.173  17.361  47.104  1.00 98.90           C  
ATOM   1136  OD1 ASN A 145      19.523  16.443  47.853  1.00100.45           O  
ATOM   1137  ND2 ASN A 145      19.374  18.636  47.405  1.00 99.47           N  
ATOM   1138  N   ASN A 146      16.328  19.480  44.864  1.00113.09           N  
ATOM   1139  CA  ASN A 146      15.539  20.681  45.187  1.00120.88           C  
ATOM   1140  C   ASN A 146      14.090  20.347  45.514  1.00121.28           C  
ATOM   1141  O   ASN A 146      13.254  20.020  44.673  1.00120.73           O  
ATOM   1142  CB  ASN A 146      15.638  21.724  44.071  1.00123.34           C  
ATOM   1143  CG  ASN A 146      16.836  22.647  44.120  1.00124.35           C  
ATOM   1144  OD1 ASN A 146      17.243  23.254  43.116  1.00122.08           O  
ATOM   1145  ND2 ASN A 146      17.465  22.793  45.287  1.00123.35           N  
ATOM   1146  N   ILE A 147      14.813  21.445  47.151  0.00 20.00           N  
ATOM   1147  CA  ILE A 147      13.925  21.788  48.320  0.00 20.00           C  
ATOM   1148  C   ILE A 147      13.656  23.364  48.348  0.00 20.00           C  
ATOM   1149  O   ILE A 147      12.569  23.840  48.117  0.00 20.00           O  
ATOM   1150  CB  ILE A 147      14.487  21.231  49.667  0.00 20.00           C  
ATOM   1151  CG1 ILE A 147      14.371  19.690  49.768  0.00 20.00           C  
ATOM   1152  CG2 ILE A 147      13.712  21.754  50.888  0.00 20.00           C  
ATOM   1153  CD1 ILE A 147      14.676  19.138  51.167  0.00 20.00           C  
ATOM   1154  N   GLY A 148      14.579  24.285  48.660  0.00 20.00           N  
ATOM   1155  CA  GLY A 148      14.345  25.802  48.475  0.00 20.00           C  
ATOM   1156  C   GLY A 148      13.279  26.513  49.376  0.00 20.00           C  
ATOM   1157  O   GLY A 148      12.196  25.998  49.668  0.00 20.00           O  
ATOM   1158  N   ASP A 149      13.642  27.741  49.781  0.00 20.00           N  
ATOM   1159  CA  ASP A 149      12.778  28.613  50.604  0.00 20.00           C  
ATOM   1160  C   ASP A 149      12.083  29.610  49.679  0.00 20.00           C  
ATOM   1161  O   ASP A 149      12.672  30.090  48.693  0.00 20.00           O  
ATOM   1162  CB  ASP A 149      13.615  29.339  51.658  0.00 20.00           C  
ATOM   1163  CG  ASP A 149      14.277  28.379  52.652  0.00 20.00           C  
ATOM   1164  OD1 ASP A 149      14.159  27.103  52.493  0.00 20.00           O  
ATOM   1165  OD2 ASP A 149      14.956  28.844  53.645  0.00 20.00           O  
ATOM   1166  N   ALA A 150      10.821  29.915  49.969  0.00 20.00           N  
ATOM   1167  CA  ALA A 150      10.125  30.896  49.137  0.00 20.00           C  
ATOM   1168  C   ALA A 150       8.618  31.121  49.381  0.00 20.00           C  
ATOM   1169  O   ALA A 150       8.104  30.699  50.467  0.00 20.00           O  
ATOM   1170  CB  ALA A 150      10.170  30.491  47.663  0.00 20.00           C  
ATOM   1171  N   HIS A 151       8.268  31.788  48.245  0.00 20.00           N  
ATOM   1172  CA  HIS A 151       7.003  32.372  47.684  0.00 20.00           C  
ATOM   1173  C   HIS A 151       5.991  32.986  48.462  0.00 20.00           C  
ATOM   1174  O   HIS A 151       6.175  34.286  48.619  0.00 20.00           O  
ATOM   1175  CB  HIS A 151       5.718  31.520  47.546  0.00 20.00           C  
ATOM   1176  CG  HIS A 151       5.736  30.065  47.282  0.00 20.00           C  
ATOM   1177  ND1 HIS A 151       6.362  29.067  48.071  0.00 20.00           N  
ATOM   1178  CD2 HIS A 151       5.138  29.488  46.276  0.00 20.00           C  
ATOM   1179  CE1 HIS A 151       6.191  27.919  47.403  0.00 20.00           C  
ATOM   1180  NE2 HIS A 151       5.482  28.175  46.316  0.00 20.00           N  
ATOM   1181  N   THR A 152       5.468  31.690  48.316  0.00 20.00           N  
ATOM   1182  CA  THR A 152       4.358  30.636  48.542  0.00 20.00           C  
ATOM   1183  C   THR A 152       5.063  29.309  49.180  0.00 20.00           C  
ATOM   1184  O   THR A 152       5.976  29.408  49.998  0.00 20.00           O  
ATOM   1185  CB  THR A 152       4.073  30.155  47.092  0.00 20.00           C  
ATOM   1186  OG1 THR A 152       5.340  30.104  46.387  0.00 20.00           O  
ATOM   1187  CG2 THR A 152       3.195  31.108  46.296  0.00 20.00           C  
ATOM   1188  N   ILE A 153       4.688  28.028  48.779  0.00 20.00           N  
ATOM   1189  CA  ILE A 153       5.370  26.748  49.311  0.00 20.00           C  
ATOM   1190  C   ILE A 153       6.116  25.982  48.167  0.00 20.00           C  
ATOM   1191  O   ILE A 153       5.631  25.899  47.033  0.00 20.00           O  
ATOM   1192  CB  ILE A 153       4.362  25.777  49.965  0.00 20.00           C  
ATOM   1193  CG1 ILE A 153       3.566  26.423  51.104  0.00 20.00           C  
ATOM   1194  CG2 ILE A 153       5.028  24.538  50.589  0.00 20.00           C  
ATOM   1195  CD1 ILE A 153       2.591  25.460  51.785  0.00 20.00           C  
ATOM   1196  N   GLY A 154       7.289  25.424  48.512  0.00 20.00           N  
ATOM   1197  CA  GLY A 154       8.220  24.749  47.545  0.00 20.00           C  
ATOM   1198  C   GLY A 154       7.769  23.310  47.104  0.00 20.00           C  
ATOM   1199  O   GLY A 154       7.146  22.582  47.913  0.00 20.00           O  
ATOM   1200  N   THR A 155       8.160  23.010  45.789  0.00 20.00           N  
ATOM   1201  CA  THR A 155       7.941  21.686  45.010  0.00 20.00           C  
ATOM   1202  C   THR A 155       9.090  21.420  43.950  0.00 20.00           C  
ATOM   1203  O   THR A 155      10.282  21.589  44.221  0.00 20.00           O  
ATOM   1204  CB  THR A 155       6.542  21.593  44.460  0.00 20.00           C  
ATOM   1205  OG1 THR A 155       6.284  22.691  43.599  0.00 20.00           O  
ATOM   1206  CG2 THR A 155       5.472  21.604  45.554  0.00 20.00           C  
ATOM   1207  N   ARG A 156       9.003  20.953  42.618  0.00 20.00           N  
ATOM   1208  CA  ARG A 156      10.402  20.818  42.159  0.00 20.00           C  
ATOM   1209  C   ARG A 156      10.926  20.313  40.588  0.00 20.00           C  
ATOM   1210  O   ARG A 156      10.074  19.911  39.726  0.00 20.00           O  
ATOM   1211  CB  ARG A 156      10.914  20.133  43.499  0.00 20.00           C  
ATOM   1212  CG  ARG A 156      11.062  21.235  44.722  0.00 20.00           C  
ATOM   1213  CD  ARG A 156      10.042  22.486  44.924  0.00 20.00           C  
ATOM   1214  NE  ARG A 156      10.617  23.524  45.912  0.00 20.00           N  
ATOM   1215  CZ  ARG A 156       9.998  24.590  46.569  0.00 20.00           C  
ATOM   1216  NH1 ARG A 156       8.696  24.882  46.430  0.00 20.00           N  
ATOM   1217  NH2 ARG A 156      10.644  25.443  47.418  0.00 20.00           N  
ATOM   1218  N   PRO A 157      12.246  19.936  40.656  0.00 20.00           N  
ATOM   1219  CA  PRO A 157      12.664  20.249  39.557  0.00 20.00           C  
ATOM   1220  C   PRO A 157      13.322  21.361  39.133  0.00 20.00           C  
ATOM   1221  O   PRO A 157      12.346  22.102  38.599  0.00 20.00           O  
ATOM   1222  CB  PRO A 157      11.215  19.987  39.298  0.00 20.00           C  
ATOM   1223  CG  PRO A 157      11.024  19.155  40.562  0.00 20.00           C  
ATOM   1224  CD  PRO A 157      12.391  18.891  40.323  0.00 20.00           C  
ATOM   1225  N   ASP A 158      14.998  21.075  39.843  1.00134.81           N  
ATOM   1226  CA  ASP A 158      16.216  21.056  39.021  1.00134.90           C  
ATOM   1227  C   ASP A 158      16.635  19.641  38.642  1.00127.06           C  
ATOM   1228  O   ASP A 158      16.717  18.774  39.527  1.00127.63           O  
ATOM   1229  CB  ASP A 158      17.343  21.725  39.828  1.00144.42           C  
ATOM   1230  CG  ASP A 158      18.726  21.299  39.375  1.00150.81           C  
ATOM   1231  OD1 ASP A 158      19.193  20.182  39.716  1.00154.45           O  
ATOM   1232  OD2 ASP A 158      19.398  22.085  38.679  1.00153.31           O  
ATOM   1233  N   ASN A 159      16.986  19.370  37.391  1.00114.81           N  
ATOM   1234  CA  ASN A 159      17.402  18.021  36.977  1.00101.41           C  
ATOM   1235  C   ASN A 159      18.889  17.913  36.669  1.00 90.36           C  
ATOM   1236  O   ASN A 159      19.640  18.871  36.841  1.00 85.75           O  
ATOM   1237  CB  ASN A 159      16.538  17.595  35.794  1.00 99.78           C  
ATOM   1238  CG  ASN A 159      16.567  16.133  35.429  1.00 96.91           C  
ATOM   1239  OD1 ASN A 159      16.405  15.243  36.271  1.00 95.67           O  
ATOM   1240  ND2 ASN A 159      16.774  15.846  34.137  1.00 90.12           N  
ATOM   1241  N   GLY A 160      19.394  16.750  36.247  1.00 77.46           N  
ATOM   1242  CA  GLY A 160      20.793  16.599  36.033  1.00 68.26           C  
ATOM   1243  C   GLY A 160      21.395  17.185  34.785  1.00 61.24           C  
ATOM   1244  O   GLY A 160      20.768  17.367  33.753  1.00 63.00           O  
ATOM   1245  N   MET A 161      22.696  17.438  34.876  1.00 51.13           N  
ATOM   1246  CA  MET A 161      23.490  17.891  33.764  1.00 43.98           C  
ATOM   1247  C   MET A 161      24.584  16.835  33.481  1.00 41.15           C  
ATOM   1248  O   MET A 161      25.331  16.405  34.376  1.00 39.60           O  
ATOM   1249  CB  MET A 161      24.119  19.245  34.020  1.00 38.23           C  
ATOM   1250  CG  MET A 161      24.880  19.804  32.842  1.00 47.73           C  
ATOM   1251  SD  MET A 161      25.653  21.391  33.147  1.00 60.62           S  
ATOM   1252  CE  MET A 161      27.071  20.970  34.108  1.00 46.94           C  
ATOM   1253  N   LEU A 162      24.657  16.420  32.232  1.00 30.92           N  
ATOM   1254  CA  LEU A 162      25.692  15.503  31.774  1.00 32.64           C  
ATOM   1255  C   LEU A 162      26.812  16.316  31.122  1.00 28.89           C  
ATOM   1256  O   LEU A 162      26.530  17.239  30.351  1.00 30.06           O  
ATOM   1257  CB  LEU A 162      25.235  14.542  30.673  1.00 31.23           C  
ATOM   1258  CG  LEU A 162      24.922  13.130  31.155  1.00 52.06           C  
ATOM   1259  CD1 LEU A 162      24.743  12.209  29.937  1.00 60.86           C  
ATOM   1260  CD2 LEU A 162      26.021  12.592  32.071  1.00 44.51           C  
ATOM   1261  N   SER A 163      28.055  15.966  31.402  1.00 29.07           N  
ATOM   1262  CA  SER A 163      29.107  16.736  30.721  1.00 27.70           C  
ATOM   1263  C   SER A 163      30.376  15.992  30.409  1.00 31.87           C  
ATOM   1264  O   SER A 163      30.706  14.956  30.993  1.00 32.53           O  
ATOM   1265  CB  SER A 163      29.313  18.028  31.496  1.00 20.98           C  
ATOM   1266  OG  SER A 163      29.954  17.738  32.703  1.00 25.46           O  
ATOM   1267  N   LEU A 164      31.100  16.506  29.417  1.00 29.04           N  
ATOM   1268  CA  LEU A 164      32.378  15.979  28.979  1.00 27.60           C  
ATOM   1269  C   LEU A 164      33.373  17.113  29.267  1.00 25.03           C  
ATOM   1270  O   LEU A 164      33.034  18.214  28.846  1.00 25.48           O  
ATOM   1271  CB  LEU A 164      32.380  15.856  27.439  1.00 37.33           C  
ATOM   1272  CG  LEU A 164      31.483  14.792  26.838  1.00 40.57           C  
ATOM   1273  CD1 LEU A 164      31.622  14.885  25.323  1.00 41.86           C  
ATOM   1274  CD2 LEU A 164      31.863  13.410  27.364  1.00 47.99           C  
ATOM   1275  N   GLY A 165      34.532  16.875  29.817  1.00 29.57           N  
ATOM   1276  CA  GLY A 165      35.468  17.963  30.139  1.00 23.13           C  
ATOM   1277  C   GLY A 165      36.889  17.437  29.850  1.00 31.66           C  
ATOM   1278  O   GLY A 165      37.128  16.249  29.663  1.00 28.43           O  
ATOM   1279  N   VAL A 166      37.799  18.386  29.777  1.00 25.49           N  
ATOM   1280  CA  VAL A 166      39.196  18.277  29.596  1.00 25.33           C  
ATOM   1281  C   VAL A 166      39.864  19.127  30.695  1.00 30.36           C  
ATOM   1282  O   VAL A 166      39.388  20.206  31.071  1.00 23.95           O  
ATOM   1283  CB  VAL A 166      39.654  18.817  28.238  1.00 26.51           C  
ATOM   1284  CG1 VAL A 166      41.134  18.510  28.045  1.00 26.50           C  
ATOM   1285  CG2 VAL A 166      38.907  18.092  27.121  1.00 31.09           C  
ATOM   1286  N   SER A 167      40.946  18.616  31.262  1.00 29.92           N  
ATOM   1287  CA  SER A 167      41.672  19.398  32.231  1.00 37.40           C  
ATOM   1288  C   SER A 167      43.189  19.211  32.075  1.00 33.88           C  
ATOM   1289  O   SER A 167      43.740  18.182  31.711  1.00 32.79           O  
ATOM   1290  CB  SER A 167      41.244  19.284  33.672  1.00 39.20           C  
ATOM   1291  OG  SER A 167      41.570  18.139  34.330  1.00 35.90           O  
ATOM   1292  N   TYR A 168      43.823  20.309  32.408  1.00 33.35           N  
ATOM   1293  CA  TYR A 168      45.260  20.419  32.409  1.00 37.84           C  
ATOM   1294  C   TYR A 168      45.793  20.438  33.840  1.00 35.33           C  
ATOM   1295  O   TYR A 168      45.336  21.162  34.715  1.00 34.32           O  
ATOM   1296  CB  TYR A 168      45.634  21.693  31.653  1.00 38.49           C  
ATOM   1297  CG  TYR A 168      47.133  21.831  31.532  1.00 44.95           C  
ATOM   1298  CD1 TYR A 168      47.826  21.063  30.607  1.00 44.62           C  
ATOM   1299  CD2 TYR A 168      47.831  22.718  32.361  1.00 45.53           C  
ATOM   1300  CE1 TYR A 168      49.196  21.177  30.477  1.00 45.48           C  
ATOM   1301  CE2 TYR A 168      49.203  22.828  32.230  1.00 51.33           C  
ATOM   1302  CZ  TYR A 168      49.868  22.065  31.291  1.00 52.37           C  
ATOM   1303  OH  TYR A 168      51.245  22.189  31.170  1.00 65.24           O  
ATOM   1304  N   ARG A 169      46.796  19.588  34.083  1.00 41.04           N  
ATOM   1305  CA  ARG A 169      47.405  19.534  35.412  1.00 40.60           C  
ATOM   1306  C   ARG A 169      48.761  20.213  35.405  1.00 40.89           C  
ATOM   1307  O   ARG A 169      49.600  19.819  34.579  1.00 40.83           O  
ATOM   1308  CB  ARG A 169      47.567  18.079  35.894  1.00 37.73           C  
ATOM   1309  CG  ARG A 169      46.236  17.364  36.089  1.00 32.58           C  
ATOM   1310  CD  ARG A 169      46.344  15.915  35.807  1.00 37.44           C  
ATOM   1311  NE  ARG A 169      45.082  15.203  36.020  1.00 45.08           N  
ATOM   1312  CZ  ARG A 169      45.092  13.902  36.311  1.00 43.95           C  
ATOM   1313  NH1 ARG A 169      46.268  13.293  36.398  1.00 48.90           N  
ATOM   1314  NH2 ARG A 169      43.980  13.227  36.514  1.00 41.08           N  
ATOM   1315  N   PHE A 170      48.928  21.210  36.250  1.00 43.28           N  
ATOM   1316  CA  PHE A 170      50.213  21.894  36.425  1.00 49.62           C  
ATOM   1317  C   PHE A 170      50.989  21.091  37.470  1.00 60.19           C  
ATOM   1318  O   PHE A 170      51.046  21.572  38.620  1.00 71.71           O  
ATOM   1319  CB  PHE A 170      49.952  23.294  37.018  1.00 48.04           C  
ATOM   1320  CG  PHE A 170      49.002  24.144  36.267  1.00 56.59           C  
ATOM   1321  CD1 PHE A 170      49.426  24.955  35.225  1.00 58.76           C  
ATOM   1322  CD2 PHE A 170      47.643  24.137  36.570  1.00 61.43           C  
ATOM   1323  CE1 PHE A 170      48.534  25.747  34.510  1.00 58.78           C  
ATOM   1324  CE2 PHE A 170      46.740  24.920  35.868  1.00 59.23           C  
ATOM   1325  CZ  PHE A 170      47.192  25.733  34.831  1.00 63.96           C  
ATOM   1326  N   GLY A 171      51.478  19.893  37.258  1.00 67.18           N  
ATOM   1327  CA  GLY A 171      52.145  19.118  38.297  1.00 67.05           C  
ATOM   1328  C   GLY A 171      53.230  19.851  39.064  1.00 70.25           C  
ATOM   1329  O   GLY A 171      53.090  20.902  39.716  1.00 58.96           O  
ATOM   1330  OXT GLY A 171      54.373  19.294  39.057  1.00 84.57           O  
TER    1331      GLY A 171                                                      
HETATM 1332  C1  C8E A 172      34.442  22.227  50.830  0.40 36.83           C  
HETATM 1333  C2  C8E A 172      34.838  23.633  50.974  0.40 42.36           C  
HETATM 1334  C3  C8E A 172      36.076  23.971  50.310  0.40 42.58           C  
HETATM 1335  C4  C8E A 172      37.100  23.909  51.364  0.40 48.94           C  
HETATM 1336  C5  C8E A 172      38.375  23.687  50.638  0.40 56.37           C  
HETATM 1337  C6  C8E A 172      39.260  24.810  50.849  0.40 61.84           C  
HETATM 1338  C7  C8E A 172      40.560  24.153  50.781  0.40 66.79           C  
HETATM 1339  C8  C8E A 172      41.584  25.194  51.005  0.40 73.76           C  
HETATM 1340  O9  C8E A 172      42.985  24.959  50.961  0.40 80.58           O  
HETATM 1341  C10 C8E A 172      43.550  24.542  49.744  0.40 89.58           C  
HETATM 1342  C11 C8E A 172      45.039  24.539  49.834  0.40 94.66           C  
HETATM 1343  O12 C8E A 172      45.559  25.850  49.505  0.40100.76           O  
HETATM 1344  C13 C8E A 172      46.851  26.191  50.060  0.40106.19           C  
HETATM 1345  C14 C8E A 172      48.186  26.703  49.408  0.40110.38           C  
HETATM 1346  O15 C8E A 172      49.000  27.877  49.679  0.40114.49           O  
HETATM 1347  C16 C8E A 172      50.369  27.591  50.007  0.10117.19           C  
HETATM 1348  C17 C8E A 172      51.443  28.433  49.341  0.10120.10           C  
HETATM 1349  O18 C8E A 172      52.879  28.355  49.509  0.10122.37           O  
HETATM 1350  C19 C8E A 172      53.395  28.750  50.816  0.10124.16           C  
HETATM 1351  C20 C8E A 172      54.690  29.645  50.966  0.10125.36           C  
HETATM 1352  O21 C8E A 172      55.904  29.161  50.357  0.10126.42           O  
HETATM 1353  O   HOH A 173      43.014   9.535  36.813  1.00 60.50           O  
HETATM 1354  O   HOH A 174      21.154  13.958  26.226  1.00 92.58           O  
HETATM 1355  O   HOH A 175      23.195  20.819  37.721  1.00 68.92           O  
HETATM 1356  O   HOH A 176      50.061  15.955  27.809  1.00 98.79           O  
HETATM 1357  O   HOH A 177      42.726  16.498  36.405  1.00 53.94           O  
HETATM 1358  O   HOH A 178      43.543   8.634  42.554  1.00 63.19           O  
HETATM 1359  O   HOH A 179      33.783  18.707  36.437  1.00 50.45           O  
HETATM 1360  O   HOH A 180      33.801  21.262  39.686  1.00 54.23           O  
HETATM 1361  O   HOH A 181      54.065  16.807  38.848  1.00 93.48           O  
HETATM 1362  O   HOH A 182      40.870  10.291  42.683  1.00 54.86           O  
HETATM 1363  O   HOH A 183      14.351  39.493  42.187  1.00 88.26           O  
HETATM 1364  O   HOH A 184      39.475  16.480  33.474  1.00 75.51           O  
HETATM 1365  O   HOH A 185      49.286  16.342  38.692  1.00 71.30           O  
HETATM 1366  O   HOH A 186       9.918  24.264  26.584  1.00 98.87           O  
HETATM 1367  O   HOH A 187      39.903  13.349  44.107  1.00 43.87           O  
HETATM 1368  O   HOH A 188      32.683  16.894  32.918  1.00 66.00           O  
HETATM 1369  O   HOH A 189      48.438  19.256  38.865  1.00 50.72           O  
HETATM 1370  O   HOH A 190      19.666  14.823  31.047  1.00 71.14           O  
HETATM 1371  O   HOH A 191      18.030  25.272  34.718  1.00 95.84           O  
HETATM 1372  O   HOH A 192      19.377  13.865  48.554  1.00 98.60           O  
HETATM 1373  O   HOH A 193      17.197  14.398  46.003  1.00105.15           O  
HETATM 1374  O   HOH A 194      20.961  25.272  37.309  1.00 71.75           O  
HETATM 1375  O   HOH A 195      32.883  22.454  42.221  1.00 33.95           O  
HETATM 1376  O   HOH A 196      23.501  25.603  36.308  1.00 72.31           O  
HETATM 1377  O   HOH A 197      40.832  15.974  39.073  1.00 34.45           O  
HETATM 1378  O   HOH A 198      14.967  34.462  43.795  1.00 72.51           O  
HETATM 1379  O   HOH A 199      20.779  17.469  26.595  1.00 80.47           O  
HETATM 1380  O   HOH A 200      32.054  21.622  36.861  1.00 61.33           O  
HETATM 1381  O   HOH A 201      50.449  22.905  40.363  1.00 53.89           O  
HETATM 1382  O   HOH A 202      24.765  29.090  27.131  1.00 97.54           O  
HETATM 1383  O   HOH A 203      17.798  15.923  39.338  1.00124.60           O  
HETATM 1384  O   HOH A 204      50.283  14.749  36.998  1.00122.66           O  
HETATM 1385  O   HOH A 205      47.921  12.438  44.645  1.00 42.66           O  
HETATM 1386  O   HOH A 206      32.411  24.315  35.932  1.00 43.86           O  
HETATM 1387  O   HOH A 207      29.409  22.409  31.613  1.00101.70           O  
HETATM 1388  O   HOH A 208      28.933  18.439  35.053  1.00 38.81           O  
HETATM 1389  O   HOH A 209      26.586  34.875  30.740  1.00101.12           O  
HETATM 1390  O   HOH A 210      19.806  38.867  43.008  1.00 76.05           O  
HETATM 1391  O   HOH A 211      42.104  12.018  38.084  1.00 65.98           O  
CONECT 1332 1333                                                                
CONECT 1333 1332 1334                                                           
CONECT 1334 1333 1335                                                           
CONECT 1335 1334 1336                                                           
CONECT 1336 1335 1337                                                           
CONECT 1337 1336 1338                                                           
CONECT 1338 1337 1339                                                           
CONECT 1339 1338 1340                                                           
CONECT 1340 1339 1341                                                           
CONECT 1341 1340 1342                                                           
CONECT 1342 1341 1343                                                           
CONECT 1343 1342 1344                                                           
CONECT 1344 1343 1345                                                           
CONECT 1345 1344 1346                                                           
CONECT 1346 1345 1347                                                           
CONECT 1347 1346 1348                                                           
CONECT 1348 1347 1349                                                           
CONECT 1349 1348 1350                                                           
CONECT 1350 1349 1351                                                           
CONECT 1351 1350 1352                                                           
CONECT 1352 1351                                                                
MASTER      404    0    1    0    8    0    1    6 1390    1   21   14          
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.