CNRS Nantes University UFIP UFIP
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***  1nl2_dps  ***

elNémo ID: 22071022481586483

Job options:

ID        	=	 22071022481586483
JOBID     	=	 1nl2_dps
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 1nl2_dps

HEADER    HYDROLASE                               06-JAN-03   1NL2              
TITLE     BOVINE PROTHROMBIN FRAGMENT 1 IN COMPLEX WITH CALCIUM AND             
TITLE    2 LYSOPHOSPHOTIDYLSERINE                                               
CAVEAT     1NL2    LPS A 451 HAS WRONG CHIRALITY AT ATOM C31                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTHROMBIN;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: FRAGMENT 1 (RESIDUES 1-156);                               
COMPND   5 EC: 3.4.21.5                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913                                                 
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HUANG,G.HUANG,B.FURIE,B.SEATON,B.C.FURIE                            
REVDAT   4   29-JUL-20 1NL2    1       CAVEAT COMPND REMARK SEQADV              
REVDAT   4 2                   1       HETNAM LINK   SITE   ATOM                
REVDAT   3   13-JUL-11 1NL2    1       VERSN                                    
REVDAT   2   24-FEB-09 1NL2    1       VERSN                                    
REVDAT   1   16-SEP-03 1NL2    0                                                
JRNL        AUTH   M.HUANG,A.C.RIGBY,X.MORELLI,M.A.GRANT,G.HUANG,B.FURIE,       
JRNL        AUTH 2 B.SEATON,B.C.FURIE                                           
JRNL        TITL   STRUCTURAL BASIS OF MEMBRANE BINDING BY GLA DOMAINS OF       
JRNL        TITL 2 VITAMIN K-DEPENDENT PROTEINS.                                
JRNL        REF    NAT.STRUCT.BIOL.              V.  10   751 2003              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   12923575                                                     
JRNL        DOI    10.1038/NSB971                                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 11181                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 793                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1622                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 129                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1175                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 60                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.58000                                              
REMARK   3    B22 (A**2) : -0.71000                                             
REMARK   3    B33 (A**2) : -8.87000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.30                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.770                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 5.340 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.430 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 7.680 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 9.000 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 42.08                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PT.PAR                                         
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NL2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000017967.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.6                                
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          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11566                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY                : 9.700                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1NL1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.6                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       19.44700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.47950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.60850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.47950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.44700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.60850            
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, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CG   ASN A   101     C8   NAG A   303              1.66            
REMARK 500   OD1  ASN A   101     C8   NAG A   303              1.68            
REMARK 500   CB   ASN A   101     C8   NAG A   303              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   OE1  GLU A    56     O    HOH A   541     4567     1.01            
REMARK 500   ND2  ASN A     2     O    HOH A   558     4467     1.51            
REMARK 500   NE   ARG A    93     O    VAL A   141     3656     1.63            
REMARK 500   O    HOH A   502     O    HOH A   541     4567     1.71            
REMARK 500   CB   GLN A   146    CL     CL A   251     3646     1.92            
REMARK 500   ND2  ASN A     2     O    HOH A   509     4467     1.93            
REMARK 500   CA   PRO A    95     O    HOH A   549     3656     1.97            
REMARK 500   CD   ARG A    93     O    VAL A   141     3656     1.98            
REMARK 500   CE   LYS A    97     O    GLN A   146     3656     1.98            
REMARK 500   CB   PRO A    95     O    HOH A   549     3656     2.01            
REMARK 500   NZ   LYS A    97     O    GLN A   146     3656     2.05            
REMARK 500  OE12  CGU A    27     O    HOH A   509     4467     2.05            
REMARK 500   O    ARG A    93     CG2  VAL A   143     3656     2.08            
REMARK 500   O    GLY A    69     CB   TYR A    94     3646     2.13            
REMARK 500   OH   TYR A    94     CB   VAL A   141     3656     2.14            
REMARK 500   CD   GLU A    56     O    HOH A   541     4567     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A   5     -123.60    -52.73                                   
REMARK 500    ALA A  51       35.12   -142.33                                   
REMARK 500    GLU A 112     -125.10     43.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 205  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A   1   O                                                      
REMARK 620 2 CGU A   7  OE11  80.5                                              
REMARK 620 3 CGU A   7  OE12  64.0  53.0                                        
REMARK 620 4 CGU A  17  OE21  66.2  71.6 108.7                                  
REMARK 620 5 CGU A  17  OE22 120.8  78.8 131.1  54.7                            
REMARK 620 6 CGU A  21  OE11  78.0 146.8 133.3  76.6  90.8                      
REMARK 620 7 HOH A 527   O    78.1 122.4  69.6 139.2 155.4  77.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A   2   OD1                                                    
REMARK 620 2 CGU A   7  OE11  91.5                                              
REMARK 620 3 CGU A   8  OE22  65.3  81.0                                        
REMARK 620 4 CGU A  17  OE21 129.4  67.7 144.4                                  
REMARK 620 5 CGU A  17  OE11 143.8  94.1  80.4  85.3                            
REMARK 620 6 CGU A  27  OE22  86.5 128.3 141.0  74.3 116.6                      
REMARK 620 7 CGU A  27  OE11  87.5 149.1  70.6 133.5  69.9  82.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A   8  OE12                                                    
REMARK 620 2 CGU A   8  OE21  86.8                                              
REMARK 620 3 CGU A  27  OE12 104.6  96.7                                        
REMARK 620 4 CGU A  30  OE21 155.2  68.4  78.2                                  
REMARK 620 5 CGU A  30  OE22 150.5 112.7  95.1  50.1                            
REMARK 620 6 HOH A 504   O    83.4 169.5  82.2 121.2  77.8                      
REMARK 620 7 HOH A 507   O    91.1  82.4 164.2  86.9  71.0 101.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A   8  OE21                                                    
REMARK 620 2 CGU A   8  OE22  47.7                                              
REMARK 620 3 CGU A  17  OE11 115.1  69.6                                        
REMARK 620 4 CGU A  27  OE11  86.5  65.0  80.4                                  
REMARK 620 5 CGU A  30  OE21  72.7 108.5 156.4  77.8                            
REMARK 620 6 HOH A 514   O    76.4 117.2 131.7 147.6  70.9                      
REMARK 620 7 HOH A 519   O    93.4  86.1  63.9 140.5 139.5  68.9                
REMARK 620 8 HOH A 522   O   161.9 148.0  83.0  95.1  90.0  93.2  96.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 207  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  15  OE21                                                    
REMARK 620 2 CGU A  15  OE12  86.1                                              
REMARK 620 3 CGU A  20  OE21 158.1  78.6                                        
REMARK 620 4 CGU A  20  OE11  85.1  93.5  80.5                                  
REMARK 620 5 HOH A 537   O   109.8  88.3  85.4 165.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 206  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  21  OE12                                                    
REMARK 620 2 CGU A  21  OE22  77.8                                              
REMARK 620 3 LPS A 451   OT1  92.1 168.5                                        
REMARK 620 4 HOH A 557   O   150.8 129.7  61.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU A  26  OE12                                                    
REMARK 620 2 CGU A  26  OE21  75.5                                              
REMARK 620 3 CGU A  30  OE11  88.2 148.5                                        
REMARK 620 4 CGU A  30  OE22  81.1  71.8  79.3                                  
REMARK 620 N                    1     2     3                                   
DBREF  1NL2 A    1   146  UNP    P00735   THRB_BOVIN      44    189             
SEQADV 1NL2 CGU A    7  UNP  P00735    GLU    50 MODIFIED RESIDUE               
SEQADV 1NL2 CGU A    8  UNP  P00735    GLU    51 MODIFIED RESIDUE               
SEQADV 1NL2 CGU A   15  UNP  P00735    GLU    58 MODIFIED RESIDUE               
SEQADV 1NL2 CGU A   17  UNP  P00735    GLU    60 MODIFIED RESIDUE               
SEQADV 1NL2 CGU A   20  UNP  P00735    GLU    63 MODIFIED RESIDUE               
SEQADV 1NL2 CGU A   21  UNP  P00735    GLU    64 MODIFIED RESIDUE               
SEQADV 1NL2 CGU A   26  UNP  P00735    GLU    69 MODIFIED RESIDUE               
SEQADV 1NL2 CGU A   27  UNP  P00735    GLU    70 MODIFIED RESIDUE               
SEQADV 1NL2 CGU A   30  UNP  P00735    GLU    73 MODIFIED RESIDUE               
SEQADV 1NL2 CGU A   33  UNP  P00735    GLU    76 MODIFIED RESIDUE               
SEQRES   1 A  146  ALA ASN LYS GLY PHE LEU CGU CGU VAL ARG LYS GLY ASN          
SEQRES   2 A  146  LEU CGU ARG CGU CYS LEU CGU CGU PRO CYS SER ARG CGU          
SEQRES   3 A  146  CGU ALA PHE CGU ALA LEU CGU SER LEU SER ALA THR ASP          
SEQRES   4 A  146  ALA PHE TRP ALA LYS TYR THR ALA CYS GLU SER ALA ARG          
SEQRES   5 A  146  ASN PRO ARG GLU LYS LEU ASN GLU CYS LEU GLU GLY ASN          
SEQRES   6 A  146  CYS ALA GLU GLY VAL GLY MET ASN TYR ARG GLY ASN VAL          
SEQRES   7 A  146  SER VAL THR ARG SER GLY ILE GLU CYS GLN LEU TRP ARG          
SEQRES   8 A  146  SER ARG TYR PRO HIS LYS PRO GLU ILE ASN SER THR THR          
SEQRES   9 A  146  HIS PRO GLY ALA ASP LEU ARG GLU ASN PHE CYS ARG ASN          
SEQRES  10 A  146  PRO ASP GLY SER ILE THR GLY PRO TRP CYS TYR THR THR          
SEQRES  11 A  146  SER PRO THR LEU ARG ARG GLU GLU CYS SER VAL PRO VAL          
SEQRES  12 A  146  CYS GLY GLN                                                  
MODRES 1NL2 ASN A   77  ASN  GLYCOSYLATION SITE                                 
MODRES 1NL2 ASN A  101  ASN  GLYCOSYLATION SITE                                 
MODRES 1NL2 CGU A    7  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1NL2 CGU A    8  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1NL2 CGU A   15  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1NL2 CGU A   17  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1NL2 CGU A   20  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1NL2 CGU A   21  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1NL2 CGU A   26  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1NL2 CGU A   27  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1NL2 CGU A   30  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1NL2 CGU A   33  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
HET    CGU  A   7      12                                                       
HET    CGU  A   8      12                                                       
HET    CGU  A  15      12                                                       
HET    CGU  A  17      12                                                       
HET    CGU  A  20      12                                                       
HET    CGU  A  21      12                                                       
HET    CGU  A  26      12                                                       
HET    CGU  A  27      12                                                       
HET    CGU  A  30      12                                                       
HET    CGU  A  33      12                                                       
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    NAG  A 303      14                                                       
HET     CA  A 201       1                                                       
HET     CA  A 202       1                                                       
HET     CA  A 203       1                                                       
HET     CA  A 204       1                                                       
HET     CA  A 205       1                                                       
HET     CA  A 206       1                                                       
HET     CA  A 207       1                                                       
HET     CL  A 250       1                                                       
HET     CL  A 251       1                                                       
HET     CL  A 252       1                                                       
HET    LPS  A 451      32                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     LPS O-{HYDROXY[((2R)-2-HYDROXY-3-{[(1S)-1-                           
HETNAM   2 LPS  HYDROXYPENTADECYL]OXY}PROPYL)OXY]PHOSPHORYL}-L-SERINE           
HETSYN     LPS LYSOPHOSPHOTIDYLSERINE                                           
FORMUL   1  CGU    10(C6 H9 N O6)                                               
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   4   CA    7(CA 2+)                                                     
FORMUL  11   CL    3(CL 1-)                                                     
FORMUL  14  LPS    C21 H44 N O9 P                                               
FORMUL  15  HOH   *60(H2 O)                                                     
HELIX    1   1 LEU A    6  ARG A   10  5                                   5    
HELIX    2   2 ASN A   13  CYS A   18  1                                   6    
HELIX    3   3 SER A   24  LEU A   32  1                                   9    
HELIX    4   4 SER A   34  ALA A   47  1                                  14    
HELIX    5   5 CYS A   48  ARG A   52  5                                   5    
HELIX    6   6 PRO A   54  GLY A   64  1                                  11    
SHEET    1   A 2 TRP A 126  TYR A 128  0                                        
SHEET    2   A 2 ARG A 136  GLU A 138 -1  O  GLU A 137   N  CYS A 127           
SSBOND   1 CYS A   18    CYS A   23                          1555   1555  2.03  
SSBOND   2 CYS A   48    CYS A   61                          1555   1555  2.03  
SSBOND   3 CYS A   66    CYS A  144                          1555   1555  2.03  
SSBOND   4 CYS A   87    CYS A  127                          1555   1555  2.03  
SSBOND   5 CYS A  115    CYS A  139                          1555   1555  2.03  
LINK         C   LEU A   6                 N   CGU A   7     1555   1555  1.33  
LINK         C   CGU A   7                 N   CGU A   8     1555   1555  1.33  
LINK         C   CGU A   8                 N   VAL A   9     1555   1555  1.33  
LINK         C   LEU A  14                 N   CGU A  15     1555   1555  1.33  
LINK         C   CGU A  15                 N   ARG A  16     1555   1555  1.33  
LINK         C   ARG A  16                 N   CGU A  17     1555   1555  1.33  
LINK         C   CGU A  17                 N   CYS A  18     1555   1555  1.33  
LINK         C   LEU A  19                 N   CGU A  20     1555   1555  1.33  
LINK         C   CGU A  20                 N   CGU A  21     1555   1555  1.33  
LINK         C   CGU A  21                 N   PRO A  22     1555   1555  1.34  
LINK         C   ARG A  25                 N   CGU A  26     1555   1555  1.33  
LINK         C   CGU A  26                 N   CGU A  27     1555   1555  1.33  
LINK         C   CGU A  27                 N   ALA A  28     1555   1555  1.33  
LINK         C   PHE A  29                 N   CGU A  30     1555   1555  1.33  
LINK         C   CGU A  30                 N   ALA A  31     1555   1555  1.33  
LINK         C   LEU A  32                 N   CGU A  33     1555   1555  1.33  
LINK         C   CGU A  33                 N   SER A  34     1555   1555  1.33  
LINK         ND2 ASN A  77                 C1  NAG B   1     1555   1555  1.46  
LINK         ND2 ASN A 101                 C1  NAG A 303     1555   1555  1.48  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.38  
LINK         O   ALA A   1                CA    CA A 205     1555   1555  2.35  
LINK         OD1 ASN A   2                CA    CA A 204     1555   1555  2.41  
LINK        OE11 CGU A   7                CA    CA A 204     1555   1555  2.61  
LINK        OE11 CGU A   7                CA    CA A 205     1555   1555  2.49  
LINK        OE12 CGU A   7                CA    CA A 205     1555   1555  2.46  
LINK        OE12 CGU A   8                CA    CA A 202     1555   1555  2.45  
LINK        OE21 CGU A   8                CA    CA A 202     1555   1555  2.58  
LINK        OE21 CGU A   8                CA    CA A 203     1555   1555  2.27  
LINK        OE22 CGU A   8                CA    CA A 203     1555   1555  2.95  
LINK        OE22 CGU A   8                CA    CA A 204     1555   1555  2.26  
LINK        OE21 CGU A  15                CA    CA A 207     1555   1555  2.05  
LINK        OE12 CGU A  15                CA    CA A 207     1555   1555  2.37  
LINK        OE11 CGU A  17                CA    CA A 203     1555   1555  2.41  
LINK        OE21 CGU A  17                CA    CA A 204     1555   1555  2.37  
LINK        OE11 CGU A  17                CA    CA A 204     1555   1555  2.53  
LINK        OE21 CGU A  17                CA    CA A 205     1555   1555  2.26  
LINK        OE22 CGU A  17                CA    CA A 205     1555   1555  2.51  
LINK        OE21 CGU A  20                CA    CA A 207     1555   1555  2.39  
LINK        OE11 CGU A  20                CA    CA A 207     1555   1555  2.27  
LINK        OE11 CGU A  21                CA    CA A 205     1555   1555  2.50  
LINK        OE12 CGU A  21                CA    CA A 206     1555   1555  2.42  
LINK        OE22 CGU A  21                CA    CA A 206     1555   1555  2.42  
LINK        OE12 CGU A  26                CA    CA A 201     1555   1555  2.42  
LINK        OE21 CGU A  26                CA    CA A 201     1555   1555  2.39  
LINK        OE12 CGU A  27                CA    CA A 202     1555   1555  2.45  
LINK        OE11 CGU A  27                CA    CA A 203     1555   1555  2.11  
LINK        OE22 CGU A  27                CA    CA A 204     1555   1555  2.34  
LINK        OE11 CGU A  27                CA    CA A 204     1555   1555  2.59  
LINK        OE11 CGU A  30                CA    CA A 201     1555   1555  2.17  
LINK        OE22 CGU A  30                CA    CA A 201     1555   1555  2.50  
LINK        OE21 CGU A  30                CA    CA A 202     1555   1555  2.45  
LINK        OE22 CGU A  30                CA    CA A 202     1555   1555  2.71  
LINK        OE21 CGU A  30                CA    CA A 203     1555   1555  2.50  
LINK        CA    CA A 202                 O   HOH A 504     1555   1555  2.48  
LINK        CA    CA A 202                 O   HOH A 507     1555   1555  2.05  
LINK        CA    CA A 203                 O   HOH A 514     1555   1555  2.14  
LINK        CA    CA A 203                 O   HOH A 519     1555   1555  2.45  
LINK        CA    CA A 203                 O   HOH A 522     1555   1555  2.58  
LINK        CA    CA A 205                 O   HOH A 527     1555   1555  2.43  
LINK        CA    CA A 206                 OT1 LPS A 451     1555   1555  2.20  
LINK        CA    CA A 206                 O   HOH A 557     1555   1555  2.72  
LINK        CA    CA A 207                 O   HOH A 537     1555   1555  2.76  
CISPEP   1 ASN A   53    PRO A   54          0        -0.17                     
CISPEP   2 TYR A   94    PRO A   95          0         0.01                     
CRYST1   38.894   53.217  128.959  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.025711  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018791  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007754        0.00000                         
ATOM      1  N   ALA A   1       2.680  33.023 124.458  1.00 32.16           N  
ATOM      2  CA  ALA A   1       1.468  32.155 124.511  1.00 40.61           C  
ATOM      3  C   ALA A   1       0.539  32.561 125.656  1.00 40.86           C  
ATOM      4  O   ALA A   1       0.991  33.070 126.680  1.00 47.28           O  
ATOM      5  CB  ALA A   1       1.882  30.695 124.669  1.00 33.31           C  
ATOM      6  N   ASN A   2      -0.760  32.347 125.467  1.00 51.00           N  
ATOM      7  CA  ASN A   2      -1.757  32.669 126.487  1.00 51.62           C  
ATOM      8  C   ASN A   2      -2.398  31.376 126.951  1.00 55.13           C  
ATOM      9  O   ASN A   2      -3.279  30.851 126.269  1.00 57.25           O  
ATOM     10  CB  ASN A   2      -2.855  33.571 125.921  1.00 46.64           C  
ATOM     11  CG  ASN A   2      -2.366  34.963 125.612  1.00 42.46           C  
ATOM     12  OD1 ASN A   2      -1.582  35.537 126.366  1.00 54.57           O  
ATOM     13  ND2 ASN A   2      -2.844  35.526 124.512  1.00 38.08           N  
ATOM     14  N   LYS A   3      -1.974  30.850 128.097  1.00 49.94           N  
ATOM     15  CA  LYS A   3      -2.570  29.606 128.561  1.00 68.31           C  
ATOM     16  C   LYS A   3      -4.019  29.833 129.019  1.00 77.93           C  
ATOM     17  O   LYS A   3      -4.655  28.943 129.591  1.00 76.27           O  
ATOM     18  CB  LYS A   3      -1.724  28.962 129.670  1.00 62.80           C  
ATOM     19  CG  LYS A   3      -2.022  29.420 131.069  1.00 59.60           C  
ATOM     20  CD  LYS A   3      -1.351  30.730 131.385  1.00 80.87           C  
ATOM     21  CE  LYS A   3      -1.618  31.104 132.824  1.00 76.01           C  
ATOM     22  NZ  LYS A   3      -0.833  32.279 133.253  1.00 79.44           N  
ATOM     23  N   GLY A   4      -4.527  31.038 128.759  1.00 77.40           N  
ATOM     24  CA  GLY A   4      -5.905  31.359 129.086  1.00 76.16           C  
ATOM     25  C   GLY A   4      -6.252  32.170 130.321  1.00 81.50           C  
ATOM     26  O   GLY A   4      -6.805  33.268 130.215  1.00 85.80           O  
ATOM     27  N   PHE A   5      -5.931  31.630 131.490  1.00 74.13           N  
ATOM     28  CA  PHE A   5      -6.255  32.265 132.762  1.00 69.07           C  
ATOM     29  C   PHE A   5      -5.853  33.717 133.037  1.00 60.81           C  
ATOM     30  O   PHE A   5      -6.228  34.606 132.281  1.00 62.05           O  
ATOM     31  CB  PHE A   5      -5.796  31.345 133.888  1.00 77.48           C  
ATOM     32  CG  PHE A   5      -6.669  30.127 134.050  1.00 92.85           C  
ATOM     33  CD1 PHE A   5      -6.113  28.870 134.269  1.00 90.23           C  
ATOM     34  CD2 PHE A   5      -8.062  30.246 133.998  1.00 91.63           C  
ATOM     35  CE1 PHE A   5      -6.930  27.750 134.437  1.00 90.23           C  
ATOM     36  CE2 PHE A   5      -8.885  29.136 134.165  1.00 81.73           C  
ATOM     37  CZ  PHE A   5      -8.320  27.886 134.385  1.00 88.72           C  
ATOM     38  N   LEU A   6      -5.105  33.971 134.110  1.00 51.27           N  
ATOM     39  CA  LEU A   6      -4.750  35.349 134.460  1.00 42.94           C  
ATOM     40  C   LEU A   6      -3.409  35.927 134.008  1.00 40.71           C  
ATOM     41  O   LEU A   6      -3.096  37.070 134.343  1.00 38.69           O  
ATOM     42  CB  LEU A   6      -4.874  35.557 135.982  1.00 38.71           C  
ATOM     43  CG  LEU A   6      -6.220  35.280 136.673  1.00 43.76           C  
ATOM     44  CD1 LEU A   6      -6.193  35.844 138.088  1.00 30.46           C  
ATOM     45  CD2 LEU A   6      -7.358  35.915 135.897  1.00 36.87           C  
HETATM   46  N   CGU A   7      -2.624  35.179 133.243  1.00 35.17           N  
HETATM   47  CA  CGU A   7      -1.325  35.699 132.820  1.00 38.86           C  
HETATM   48  C   CGU A   7      -1.398  37.037 132.118  1.00 39.82           C  
HETATM   49  O   CGU A   7      -0.476  37.844 132.214  1.00 37.12           O  
HETATM   50  CB  CGU A   7      -0.599  34.710 131.910  1.00 46.34           C  
HETATM   51  CG  CGU A   7      -1.162  34.298 130.550  1.00 51.74           C  
HETATM   52  CD1 CGU A   7      -0.129  34.037 129.470  1.00 33.90           C  
HETATM   53  CD2 CGU A   7      -2.580  33.738 130.492  1.00 52.46           C  
HETATM   54 OE11 CGU A   7       0.643  34.964 129.141  1.00 45.97           O  
HETATM   55 OE12 CGU A   7      -0.107  32.896 128.974  1.00 50.96           O  
HETATM   56 OE21 CGU A   7      -3.138  33.457 131.573  1.00 46.23           O  
HETATM   57 OE22 CGU A   7      -3.110  33.577 129.368  1.00 55.18           O  
HETATM   58  N   CGU A   8      -2.502  37.284 131.422  1.00 47.41           N  
HETATM   59  CA  CGU A   8      -2.650  38.538 130.699  1.00 52.97           C  
HETATM   60  C   CGU A   8      -2.843  39.770 131.567  1.00 49.87           C  
HETATM   61  O   CGU A   8      -3.012  40.877 131.047  1.00 46.00           O  
HETATM   62  CB  CGU A   8      -3.770  38.431 129.661  1.00 51.22           C  
HETATM   63  CG  CGU A   8      -3.237  37.883 128.336  1.00 50.88           C  
HETATM   64  CD1 CGU A   8      -4.261  37.357 127.343  1.00 60.14           C  
HETATM   65  CD2 CGU A   8      -1.825  38.295 127.922  1.00 44.88           C  
HETATM   66 OE11 CGU A   8      -4.752  36.223 127.532  1.00 65.95           O  
HETATM   67 OE12 CGU A   8      -4.550  38.098 126.382  1.00 57.21           O  
HETATM   68 OE21 CGU A   8      -1.638  39.492 127.620  1.00 42.02           O  
HETATM   69 OE22 CGU A   8      -0.930  37.427 127.905  1.00 33.07           O  
ATOM     70  N   VAL A   9      -2.814  39.580 132.883  1.00 44.92           N  
ATOM     71  CA  VAL A   9      -2.937  40.695 133.819  1.00 42.89           C  
ATOM     72  C   VAL A   9      -1.541  41.295 134.020  1.00 47.06           C  
ATOM     73  O   VAL A   9      -1.397  42.444 134.437  1.00 46.38           O  
ATOM     74  CB  VAL A   9      -3.470  40.230 135.197  1.00 50.26           C  
ATOM     75  CG1 VAL A   9      -3.448  41.384 136.173  1.00 40.30           C  
ATOM     76  CG2 VAL A   9      -4.883  39.689 135.062  1.00 37.69           C  
ATOM     77  N   ARG A  10      -0.517  40.500 133.711  1.00 43.36           N  
ATOM     78  CA  ARG A  10       0.877  40.921 133.857  1.00 53.82           C  
ATOM     79  C   ARG A  10       1.343  41.765 132.673  1.00 55.31           C  
ATOM     80  O   ARG A  10       0.881  41.584 131.545  1.00 51.94           O  
ATOM     81  CB  ARG A  10       1.802  39.704 133.962  1.00 51.97           C  
ATOM     82  CG  ARG A  10       1.335  38.603 134.903  1.00 53.34           C  
ATOM     83  CD  ARG A  10       2.380  37.500 134.972  1.00 41.66           C  
ATOM     84  NE  ARG A  10       3.604  37.956 135.633  1.00 51.29           N  
ATOM     85  CZ  ARG A  10       4.744  37.267 135.678  1.00 57.94           C  
ATOM     86  NH1 ARG A  10       4.835  36.078 135.095  1.00 43.43           N  
ATOM     87  NH2 ARG A  10       5.796  37.767 136.316  1.00 44.91           N  
ATOM     88  N   LYS A  11       2.266  42.682 132.932  1.00 56.57           N  
ATOM     89  CA  LYS A  11       2.786  43.514 131.864  1.00 56.37           C  
ATOM     90  C   LYS A  11       3.553  42.621 130.897  1.00 58.58           C  
ATOM     91  O   LYS A  11       4.282  41.709 131.309  1.00 56.52           O  
ATOM     92  CB  LYS A  11       3.707  44.608 132.418  1.00 61.84           C  
ATOM     93  CG  LYS A  11       4.941  44.105 133.147  1.00 67.40           C  
ATOM     94  CD  LYS A  11       5.828  45.263 133.590  1.00 59.44           C  
ATOM     95  CE  LYS A  11       7.024  44.764 134.385  0.30 65.09           C  
ATOM     96  NZ  LYS A  11       7.882  45.880 134.869  0.30 63.89           N  
ATOM     97  N   GLY A  12       3.365  42.881 129.608  1.00 53.95           N  
ATOM     98  CA  GLY A  12       4.035  42.107 128.581  1.00 47.44           C  
ATOM     99  C   GLY A  12       5.533  41.970 128.792  1.00 41.12           C  
ATOM    100  O   GLY A  12       6.212  42.893 129.250  1.00 35.77           O  
ATOM    101  N   ASN A  13       6.043  40.789 128.474  1.00 37.09           N  
ATOM    102  CA  ASN A  13       7.460  40.504 128.597  1.00 39.03           C  
ATOM    103  C   ASN A  13       7.842  39.618 127.422  1.00 39.52           C  
ATOM    104  O   ASN A  13       7.404  38.467 127.311  1.00 29.43           O  
ATOM    105  CB  ASN A  13       7.762  39.800 129.918  1.00 46.72           C  
ATOM    106  CG  ASN A  13       9.245  39.498 130.092  1.00 39.46           C  
ATOM    107  OD1 ASN A  13       9.755  38.493 129.590  1.00 40.13           O  
ATOM    108  ND2 ASN A  13       9.944  40.377 130.797  1.00 42.32           N  
ATOM    109  N   LEU A  14       8.656  40.185 126.542  1.00 34.00           N  
ATOM    110  CA  LEU A  14       9.107  39.519 125.330  1.00 36.86           C  
ATOM    111  C   LEU A  14       9.784  38.185 125.593  1.00 29.27           C  
ATOM    112  O   LEU A  14       9.534  37.210 124.892  1.00 40.77           O  
ATOM    113  CB  LEU A  14      10.061  40.448 124.568  1.00 44.86           C  
ATOM    114  CG  LEU A  14      10.195  40.232 123.062  1.00 41.41           C  
ATOM    115  CD1 LEU A  14       8.840  40.456 122.396  1.00 39.46           C  
ATOM    116  CD2 LEU A  14      11.234  41.191 122.503  1.00 48.25           C  
HETATM  117  N   CGU A  15      10.642  38.144 126.604  1.00 33.60           N  
HETATM  118  CA  CGU A  15      11.361  36.917 126.937  1.00 32.76           C  
HETATM  119  C   CGU A  15      10.421  35.781 127.342  1.00 37.97           C  
HETATM  120  O   CGU A  15      10.523  34.661 126.837  1.00 35.49           O  
HETATM  121  CB  CGU A  15      12.343  37.194 128.079  1.00 31.77           C  
HETATM  122  CG  CGU A  15      13.278  36.058 128.505  1.00 32.58           C  
HETATM  123  CD1 CGU A  15      13.927  35.270 127.397  1.00 28.54           C  
HETATM  124  CD2 CGU A  15      13.902  36.120 129.881  1.00 30.40           C  
HETATM  125 OE11 CGU A  15      14.343  35.909 126.403  1.00 38.84           O  
HETATM  126 OE12 CGU A  15      14.016  34.035 127.551  1.00 42.36           O  
HETATM  127 OE21 CGU A  15      14.288  35.048 130.391  1.00 34.36           O  
HETATM  128 OE22 CGU A  15      14.008  37.240 130.413  1.00 34.78           O  
ATOM    129  N   ARG A  16       9.507  36.083 128.259  1.00 34.07           N  
ATOM    130  CA  ARG A  16       8.557  35.102 128.766  1.00 37.89           C  
ATOM    131  C   ARG A  16       7.527  34.699 127.723  1.00 35.65           C  
ATOM    132  O   ARG A  16       7.321  33.516 127.458  1.00 35.21           O  
ATOM    133  CB  ARG A  16       7.831  35.676 129.987  1.00 37.79           C  
ATOM    134  CG  ARG A  16       6.889  34.703 130.690  1.00 38.74           C  
ATOM    135  CD  ARG A  16       5.666  35.437 131.231  1.00 44.90           C  
ATOM    136  NE  ARG A  16       6.029  36.618 132.006  1.00 48.21           N  
ATOM    137  CZ  ARG A  16       5.324  37.746 132.027  1.00 51.87           C  
ATOM    138  NH1 ARG A  16       4.215  37.849 131.312  1.00 32.98           N  
ATOM    139  NH2 ARG A  16       5.732  38.777 132.754  1.00 45.64           N  
HETATM  140  N   CGU A  17       6.898  35.703 127.124  1.00 35.96           N  
HETATM  141  CA  CGU A  17       5.846  35.498 126.140  1.00 32.48           C  
HETATM  142  C   CGU A  17       6.204  35.133 124.701  1.00 44.67           C  
HETATM  143  O   CGU A  17       5.445  34.410 124.052  1.00 33.63           O  
HETATM  144  CB  CGU A  17       4.936  36.726 126.128  1.00 36.92           C  
HETATM  145  CG  CGU A  17       3.990  36.835 127.327  1.00 27.98           C  
HETATM  146  CD1 CGU A  17       3.302  38.169 127.514  1.00 33.99           C  
HETATM  147  CD2 CGU A  17       3.432  35.544 127.892  1.00 31.51           C  
HETATM  148 OE11 CGU A  17       2.074  38.145 127.737  1.00 43.45           O  
HETATM  149 OE12 CGU A  17       3.990  39.210 127.430  1.00 34.80           O  
HETATM  150 OE21 CGU A  17       2.621  34.916 127.186  1.00 43.00           O  
HETATM  151 OE22 CGU A  17       3.807  35.177 129.024  1.00 43.64           O  
ATOM    152  N   CYS A  18       7.340  35.611 124.196  1.00 44.00           N  
ATOM    153  CA  CYS A  18       7.715  35.321 122.811  1.00 36.65           C  
ATOM    154  C   CYS A  18       8.954  34.468 122.569  1.00 39.61           C  
ATOM    155  O   CYS A  18       9.042  33.775 121.558  1.00 41.16           O  
ATOM    156  CB  CYS A  18       7.877  36.623 122.040  1.00 33.88           C  
ATOM    157  SG  CYS A  18       6.344  37.569 121.777  1.00 36.95           S  
ATOM    158  N   LEU A  19       9.919  34.515 123.479  1.00 41.02           N  
ATOM    159  CA  LEU A  19      11.138  33.743 123.299  1.00 35.31           C  
ATOM    160  C   LEU A  19      11.120  32.424 124.058  1.00 36.41           C  
ATOM    161  O   LEU A  19      11.705  31.438 123.603  1.00 42.43           O  
ATOM    162  CB  LEU A  19      12.353  34.590 123.696  1.00 24.19           C  
ATOM    163  CG  LEU A  19      12.366  35.902 122.909  1.00 37.59           C  
ATOM    164  CD1 LEU A  19      13.515  36.802 123.357  1.00 39.79           C  
ATOM    165  CD2 LEU A  19      12.473  35.583 121.432  1.00 41.00           C  
HETATM  166  N   CGU A  20      10.450  32.403 125.207  1.00 40.10           N  
HETATM  167  CA  CGU A  20      10.342  31.178 126.003  1.00 37.05           C  
HETATM  168  C   CGU A  20       9.115  30.387 125.569  1.00 39.81           C  
HETATM  169  O   CGU A  20       8.994  29.200 125.860  1.00 42.68           O  
HETATM  170  CB  CGU A  20      10.216  31.503 127.490  1.00 46.00           C  
HETATM  171  CG  CGU A  20      11.445  31.707 128.380  1.00 40.55           C  
HETATM  172  CD1 CGU A  20      11.194  32.459 129.670  1.00 50.24           C  
HETATM  173  CD2 CGU A  20      12.603  30.743 128.239  1.00 52.63           C  
HETATM  174 OE11 CGU A  20      12.160  33.047 130.204  1.00 48.22           O  
HETATM  175 OE12 CGU A  20      10.029  32.440 130.122  1.00 50.60           O  
HETATM  176 OE21 CGU A  20      13.756  31.175 128.466  1.00 50.97           O  
HETATM  177 OE22 CGU A  20      12.336  29.566 127.918  1.00 37.53           O  
HETATM  178  N   CGU A  21       8.205  31.071 124.881  1.00 42.72           N  
HETATM  179  CA  CGU A  21       6.962  30.487 124.380  1.00 40.02           C  
HETATM  180  C   CGU A  21       6.663  31.151 123.049  1.00 39.33           C  
HETATM  181  O   CGU A  21       7.130  32.262 122.783  1.00 35.72           O  
HETATM  182  CB  CGU A  21       5.767  30.830 125.284  1.00 37.97           C  
HETATM  183  CG  CGU A  21       5.446  30.435 126.728  1.00 45.34           C  
HETATM  184  CD1 CGU A  21       4.659  31.463 127.549  1.00 38.80           C  
HETATM  185  CD2 CGU A  21       5.482  28.961 127.092  1.00 55.94           C  
HETATM  186 OE11 CGU A  21       3.923  32.277 126.949  1.00 41.13           O  
HETATM  187 OE12 CGU A  21       4.786  31.434 128.789  1.00 56.99           O  
HETATM  188 OE21 CGU A  21       5.117  28.139 126.223  1.00 62.82           O  
HETATM  189 OE22 CGU A  21       5.866  28.648 128.242  1.00 62.02           O  
ATOM    190  N   PRO A  22       5.877  30.482 122.195  1.00 37.64           N  
ATOM    191  CA  PRO A  22       5.526  31.076 120.904  1.00 32.93           C  
ATOM    192  C   PRO A  22       4.506  32.162 121.255  1.00 34.77           C  
ATOM    193  O   PRO A  22       3.790  32.034 122.251  1.00 37.30           O  
ATOM    194  CB  PRO A  22       4.896  29.910 120.147  1.00 37.80           C  
ATOM    195  CG  PRO A  22       4.272  29.088 121.251  1.00 36.35           C  
ATOM    196  CD  PRO A  22       5.358  29.106 122.303  1.00 42.60           C  
ATOM    197  N   CYS A  23       4.438  33.228 120.466  1.00 37.16           N  
ATOM    198  CA  CYS A  23       3.494  34.296 120.766  1.00 34.23           C  
ATOM    199  C   CYS A  23       2.829  34.825 119.507  1.00 40.43           C  
ATOM    200  O   CYS A  23       3.296  34.566 118.404  1.00 42.51           O  
ATOM    201  CB  CYS A  23       4.208  35.440 121.486  1.00 35.55           C  
ATOM    202  SG  CYS A  23       5.322  36.435 120.437  1.00 37.22           S  
ATOM    203  N   SER A  24       1.735  35.562 119.686  1.00 39.78           N  
ATOM    204  CA  SER A  24       0.994  36.148 118.570  1.00 38.47           C  
ATOM    205  C   SER A  24       1.501  37.568 118.363  1.00 37.75           C  
ATOM    206  O   SER A  24       2.102  38.144 119.269  1.00 39.16           O  
ATOM    207  CB  SER A  24      -0.497  36.204 118.895  1.00 28.38           C  
ATOM    208  OG  SER A  24      -0.731  37.137 119.937  1.00 36.62           O  
ATOM    209  N   ARG A  25       1.246  38.146 117.192  1.00 32.74           N  
ATOM    210  CA  ARG A  25       1.713  39.503 116.941  1.00 41.24           C  
ATOM    211  C   ARG A  25       1.204  40.474 118.002  1.00 37.04           C  
ATOM    212  O   ARG A  25       1.941  41.367 118.433  1.00 47.79           O  
ATOM    213  CB  ARG A  25       1.301  39.999 115.546  1.00 38.15           C  
ATOM    214  CG  ARG A  25       1.978  41.328 115.168  1.00 40.26           C  
ATOM    215  CD  ARG A  25       1.785  41.692 113.701  1.00 53.74           C  
ATOM    216  NE  ARG A  25       2.582  42.853 113.303  1.00 55.91           N  
ATOM    217  CZ  ARG A  25       2.413  44.083 113.783  1.00 67.76           C  
ATOM    218  NH1 ARG A  25       1.469  44.324 114.683  1.00 67.18           N  
ATOM    219  NH2 ARG A  25       3.190  45.076 113.366  1.00 51.30           N  
HETATM  220  N   CGU A  26      -0.045  40.305 118.430  1.00 34.97           N  
HETATM  221  CA  CGU A  26      -0.607  41.188 119.446  1.00 31.03           C  
HETATM  222  C   CGU A  26       0.152  41.035 120.768  1.00 33.71           C  
HETATM  223  O   CGU A  26       0.372  42.013 121.481  1.00 33.05           O  
HETATM  224  CB  CGU A  26      -2.097  40.906 119.653  1.00 31.92           C  
HETATM  225  CG  CGU A  26      -2.830  41.904 120.570  1.00 44.73           C  
HETATM  226  CD1 CGU A  26      -2.413  43.364 120.510  1.00 43.44           C  
HETATM  227  CD2 CGU A  26      -4.150  41.486 121.187  1.00 46.31           C  
HETATM  228 OE11 CGU A  26      -2.177  43.857 119.388  1.00 53.64           O  
HETATM  229 OE12 CGU A  26      -2.340  43.998 121.587  1.00 48.31           O  
HETATM  230 OE21 CGU A  26      -4.558  42.148 122.163  1.00 39.76           O  
HETATM  231 OE22 CGU A  26      -4.755  40.515 120.685  1.00 56.27           O  
HETATM  232  N   CGU A  27       0.554  39.810 121.098  1.00 39.03           N  
HETATM  233  CA  CGU A  27       1.312  39.600 122.327  1.00 43.12           C  
HETATM  234  C   CGU A  27       2.642  40.355 122.213  1.00 46.00           C  
HETATM  235  O   CGU A  27       3.047  41.066 123.135  1.00 41.59           O  
HETATM  236  CB  CGU A  27       1.576  38.108 122.568  1.00 39.64           C  
HETATM  237  CG  CGU A  27       0.609  37.289 123.439  1.00 35.18           C  
HETATM  238  CD1 CGU A  27      -0.288  38.060 124.404  1.00 40.79           C  
HETATM  239  CD2 CGU A  27       0.902  35.800 123.607  1.00 51.76           C  
HETATM  240 OE11 CGU A  27       0.188  38.383 125.509  1.00 32.60           O  
HETATM  241 OE12 CGU A  27      -1.455  38.325 124.053  1.00 31.39           O  
HETATM  242 OE21 CGU A  27       0.797  35.048 122.613  1.00 38.75           O  
HETATM  243 OE22 CGU A  27       1.242  35.403 124.742  1.00 48.32           O  
ATOM    244  N   ALA A  28       3.316  40.206 121.075  1.00 34.28           N  
ATOM    245  CA  ALA A  28       4.583  40.896 120.855  1.00 28.36           C  
ATOM    246  C   ALA A  28       4.360  42.397 120.990  1.00 34.45           C  
ATOM    247  O   ALA A  28       5.151  43.104 121.618  1.00 36.33           O  
ATOM    248  CB  ALA A  28       5.131  40.570 119.468  1.00 19.77           C  
ATOM    249  N   PHE A  29       3.272  42.881 120.398  1.00 35.96           N  
ATOM    250  CA  PHE A  29       2.951  44.302 120.459  1.00 31.13           C  
ATOM    251  C   PHE A  29       2.787  44.746 121.914  1.00 35.02           C  
ATOM    252  O   PHE A  29       3.268  45.810 122.305  1.00 35.06           O  
ATOM    253  CB  PHE A  29       1.666  44.590 119.680  1.00 39.94           C  
ATOM    254  CG  PHE A  29       1.228  46.021 119.751  1.00 46.70           C  
ATOM    255  CD1 PHE A  29       1.947  47.015 119.091  1.00 41.92           C  
ATOM    256  CD2 PHE A  29       0.124  46.386 120.519  1.00 55.51           C  
ATOM    257  CE1 PHE A  29       1.575  48.351 119.196  1.00 56.02           C  
ATOM    258  CE2 PHE A  29      -0.258  47.723 120.632  1.00 56.95           C  
ATOM    259  CZ  PHE A  29       0.469  48.707 119.971  1.00 56.98           C  
HETATM  260  N   CGU A  30       2.108  43.926 122.712  1.00 38.57           N  
HETATM  261  CA  CGU A  30       1.893  44.235 124.123  1.00 38.99           C  
HETATM  262  C   CGU A  30       3.229  44.264 124.873  1.00 48.61           C  
HETATM  263  O   CGU A  30       3.435  45.097 125.752  1.00 48.15           O  
HETATM  264  CB  CGU A  30       0.973  43.188 124.764  1.00 38.86           C  
HETATM  265  CG  CGU A  30      -0.557  43.302 124.697  1.00 36.39           C  
HETATM  266  CD1 CGU A  30      -1.161  44.617 125.133  1.00 43.19           C  
HETATM  267  CD2 CGU A  30      -1.370  42.027 124.725  1.00 33.49           C  
HETATM  268 OE11 CGU A  30      -2.266  44.945 124.642  1.00 42.68           O  
HETATM  269 OE12 CGU A  30      -0.523  45.287 125.969  1.00 39.73           O  
HETATM  270 OE21 CGU A  30      -0.927  41.068 125.380  1.00 37.71           O  
HETATM  271 OE22 CGU A  30      -2.444  42.009 124.097  1.00 39.63           O  
ATOM    272  N   ALA A  31       4.136  43.359 124.509  1.00 39.98           N  
ATOM    273  CA  ALA A  31       5.435  43.265 125.164  1.00 42.40           C  
ATOM    274  C   ALA A  31       6.427  44.345 124.735  1.00 45.38           C  
ATOM    275  O   ALA A  31       7.391  44.617 125.448  1.00 56.65           O  
ATOM    276  CB  ALA A  31       6.038  41.875 124.923  1.00 35.37           C  
ATOM    277  N   LEU A  32       6.189  44.960 123.578  1.00 49.29           N  
ATOM    278  CA  LEU A  32       7.083  45.999 123.065  1.00 45.59           C  
ATOM    279  C   LEU A  32       6.491  47.386 123.247  1.00 49.99           C  
ATOM    280  O   LEU A  32       5.306  47.521 123.548  1.00 68.16           O  
ATOM    281  CB  LEU A  32       7.397  45.727 121.591  1.00 34.72           C  
ATOM    282  CG  LEU A  32       8.100  44.377 121.416  1.00 31.43           C  
ATOM    283  CD1 LEU A  32       8.157  43.988 119.951  1.00 34.41           C  
ATOM    284  CD2 LEU A  32       9.497  44.458 122.033  1.00 33.84           C  
HETATM  285  N   CGU A  33       7.309  48.420 123.063  1.00 58.87           N  
HETATM  286  CA  CGU A  33       6.835  49.790 123.255  1.00 72.92           C  
HETATM  287  C   CGU A  33       6.528  50.628 122.013  1.00 71.28           C  
HETATM  288  O   CGU A  33       6.466  51.854 122.108  1.00 78.80           O  
HETATM  289  CB  CGU A  33       7.820  50.565 124.141  1.00 82.53           C  
HETATM  290  CG  CGU A  33       7.937  50.205 125.630  1.00 92.51           C  
HETATM  291  CD1 CGU A  33       8.923  51.000 126.474  1.00 91.64           C  
HETATM  292  CD2 CGU A  33       6.984  49.165 126.216  1.00 96.86           C  
HETATM  293 OE11 CGU A  33      10.135  50.936 126.177  1.00 87.21           O  
HETATM  294 OE12 CGU A  33       8.465  51.674 127.423  1.00 95.76           O  
HETATM  295 OE21 CGU A  33       7.409  47.999 126.371  1.00 94.92           O  
HETATM  296 OE22 CGU A  33       5.827  49.532 126.520  1.00101.76           O  
ATOM    297  N   SER A  34       6.330  49.991 120.860  1.00 65.92           N  
ATOM    298  CA  SER A  34       6.020  50.738 119.639  1.00 59.25           C  
ATOM    299  C   SER A  34       5.738  49.855 118.430  1.00 55.33           C  
ATOM    300  O   SER A  34       6.135  48.690 118.390  1.00 49.40           O  
ATOM    301  CB  SER A  34       7.164  51.696 119.289  1.00 54.56           C  
ATOM    302  OG  SER A  34       8.335  50.986 118.930  1.00 56.77           O  
ATOM    303  N   LEU A  35       5.055  50.430 117.441  1.00 48.84           N  
ATOM    304  CA  LEU A  35       4.722  49.714 116.218  1.00 50.30           C  
ATOM    305  C   LEU A  35       6.003  49.402 115.455  1.00 44.16           C  
ATOM    306  O   LEU A  35       6.156  48.316 114.890  1.00 42.39           O  
ATOM    307  CB  LEU A  35       3.791  50.556 115.339  1.00 47.93           C  
ATOM    308  CG  LEU A  35       3.357  49.889 114.025  1.00 53.75           C  
ATOM    309  CD1 LEU A  35       2.667  48.571 114.327  1.00 63.59           C  
ATOM    310  CD2 LEU A  35       2.423  50.803 113.250  1.00 58.44           C  
ATOM    311  N   SER A  36       6.920  50.362 115.443  1.00 34.57           N  
ATOM    312  CA  SER A  36       8.192  50.182 114.754  1.00 46.17           C  
ATOM    313  C   SER A  36       8.882  48.939 115.280  1.00 36.23           C  
ATOM    314  O   SER A  36       9.247  48.051 114.515  1.00 49.04           O  
ATOM    315  CB  SER A  36       9.105  51.394 114.968  1.00 34.19           C  
ATOM    316  OG  SER A  36       8.682  52.497 114.186  1.00 66.00           O  
ATOM    317  N   ALA A  37       9.048  48.882 116.596  1.00 38.62           N  
ATOM    318  CA  ALA A  37       9.705  47.747 117.225  1.00 36.02           C  
ATOM    319  C   ALA A  37       8.932  46.460 116.975  1.00 34.69           C  
ATOM    320  O   ALA A  37       9.533  45.400 116.811  1.00 35.29           O  
ATOM    321  CB  ALA A  37       9.854  47.993 118.710  1.00 36.14           C  
ATOM    322  N   THR A  38       7.604  46.554 116.936  1.00 30.09           N  
ATOM    323  CA  THR A  38       6.780  45.376 116.688  1.00 34.93           C  
ATOM    324  C   THR A  38       6.938  44.859 115.251  1.00 30.29           C  
ATOM    325  O   THR A  38       7.022  43.653 115.034  1.00 36.59           O  
ATOM    326  CB  THR A  38       5.279  45.651 116.939  1.00 34.11           C  
ATOM    327  OG1 THR A  38       5.096  46.177 118.260  1.00 29.66           O  
ATOM    328  CG2 THR A  38       4.484  44.350 116.805  1.00 30.44           C  
ATOM    329  N   ASP A  39       6.965  45.764 114.275  1.00 32.82           N  
ATOM    330  CA  ASP A  39       7.129  45.362 112.881  1.00 30.26           C  
ATOM    331  C   ASP A  39       8.479  44.680 112.701  1.00 35.52           C  
ATOM    332  O   ASP A  39       8.571  43.617 112.086  1.00 36.85           O  
ATOM    333  CB  ASP A  39       7.056  46.572 111.932  1.00 39.05           C  
ATOM    334  CG  ASP A  39       5.643  47.101 111.756  1.00 42.35           C  
ATOM    335  OD1 ASP A  39       4.699  46.284 111.715  1.00 40.45           O  
ATOM    336  OD2 ASP A  39       5.478  48.333 111.641  1.00 42.75           O  
ATOM    337  N   ALA A  40       9.525  45.299 113.241  1.00 30.22           N  
ATOM    338  CA  ALA A  40      10.875  44.752 113.146  1.00 27.41           C  
ATOM    339  C   ALA A  40      10.948  43.374 113.795  1.00 28.84           C  
ATOM    340  O   ALA A  40      11.368  42.411 113.158  1.00 41.52           O  
ATOM    341  CB  ALA A  40      11.874  45.699 113.813  1.00 25.63           C  
ATOM    342  N   PHE A  41      10.530  43.275 115.056  1.00 32.08           N  
ATOM    343  CA  PHE A  41      10.567  41.994 115.758  1.00 31.52           C  
ATOM    344  C   PHE A  41       9.753  40.902 115.075  1.00 42.09           C  
ATOM    345  O   PHE A  41      10.228  39.776 114.918  1.00 39.34           O  
ATOM    346  CB  PHE A  41      10.061  42.127 117.193  1.00 36.67           C  
ATOM    347  CG  PHE A  41      10.019  40.814 117.933  1.00 36.52           C  
ATOM    348  CD1 PHE A  41      11.192  40.230 118.409  1.00 31.19           C  
ATOM    349  CD2 PHE A  41       8.817  40.129 118.099  1.00 37.33           C  
ATOM    350  CE1 PHE A  41      11.172  38.974 119.036  1.00 33.49           C  
ATOM    351  CE2 PHE A  41       8.787  38.877 118.723  1.00 39.81           C  
ATOM    352  CZ  PHE A  41       9.969  38.300 119.190  1.00 26.53           C  
ATOM    353  N   TRP A  42       8.527  41.224 114.673  1.00 37.93           N  
ATOM    354  CA  TRP A  42       7.679  40.221 114.037  1.00 40.77           C  
ATOM    355  C   TRP A  42       8.257  39.663 112.738  1.00 40.09           C  
ATOM    356  O   TRP A  42       8.086  38.480 112.434  1.00 36.26           O  
ATOM    357  CB  TRP A  42       6.277  40.777 113.783  1.00 29.34           C  
ATOM    358  CG  TRP A  42       5.307  39.683 113.493  1.00 41.47           C  
ATOM    359  CD1 TRP A  42       4.733  39.391 112.293  1.00 41.94           C  
ATOM    360  CD2 TRP A  42       4.845  38.685 114.414  1.00 40.30           C  
ATOM    361  NE1 TRP A  42       3.945  38.268 112.405  1.00 41.89           N  
ATOM    362  CE2 TRP A  42       3.997  37.815 113.696  1.00 38.26           C  
ATOM    363  CE3 TRP A  42       5.069  38.439 115.775  1.00 36.02           C  
ATOM    364  CZ2 TRP A  42       3.368  36.718 114.294  1.00 45.61           C  
ATOM    365  CZ3 TRP A  42       4.444  37.349 116.369  1.00 35.39           C  
ATOM    366  CH2 TRP A  42       3.604  36.502 115.627  1.00 36.45           C  
ATOM    367  N   ALA A  43       8.941  40.515 111.978  1.00 34.71           N  
ATOM    368  CA  ALA A  43       9.554  40.091 110.724  1.00 38.83           C  
ATOM    369  C   ALA A  43      10.721  39.148 110.999  1.00 24.08           C  
ATOM    370  O   ALA A  43      10.939  38.198 110.259  1.00 41.33           O  
ATOM    371  CB  ALA A  43      10.035  41.306 109.932  1.00 36.72           C  
ATOM    372  N   LYS A  44      11.462  39.414 112.070  1.00 30.98           N  
ATOM    373  CA  LYS A  44      12.607  38.581 112.438  1.00 36.94           C  
ATOM    374  C   LYS A  44      12.108  37.281 113.063  1.00 35.52           C  
ATOM    375  O   LYS A  44      12.640  36.197 112.815  1.00 33.74           O  
ATOM    376  CB  LYS A  44      13.495  39.319 113.452  1.00 28.48           C  
ATOM    377  CG  LYS A  44      13.880  40.727 113.032  1.00 38.72           C  
ATOM    378  CD  LYS A  44      14.649  41.465 114.122  1.00 40.06           C  
ATOM    379  CE  LYS A  44      16.011  40.838 114.362  1.00 47.65           C  
ATOM    380  NZ  LYS A  44      16.823  41.629 115.321  1.00 59.58           N  
ATOM    381  N   TYR A  45      11.071  37.417 113.876  1.00 39.00           N  
ATOM    382  CA  TYR A  45      10.466  36.300 114.585  1.00 31.73           C  
ATOM    383  C   TYR A  45       9.888  35.251 113.631  1.00 36.58           C  
ATOM    384  O   TYR A  45      10.186  34.062 113.760  1.00 42.86           O  
ATOM    385  CB  TYR A  45       9.382  36.851 115.526  1.00 33.52           C  
ATOM    386  CG  TYR A  45       8.811  35.865 116.513  1.00 36.19           C  
ATOM    387  CD1 TYR A  45       9.646  35.074 117.299  1.00 41.63           C  
ATOM    388  CD2 TYR A  45       7.434  35.751 116.693  1.00 36.21           C  
ATOM    389  CE1 TYR A  45       9.126  34.196 118.240  1.00 38.05           C  
ATOM    390  CE2 TYR A  45       6.901  34.874 117.633  1.00 43.96           C  
ATOM    391  CZ  TYR A  45       7.753  34.102 118.403  1.00 41.62           C  
ATOM    392  OH  TYR A  45       7.246  33.233 119.337  1.00 41.39           O  
ATOM    393  N   THR A  46       9.077  35.689 112.668  1.00 37.09           N  
ATOM    394  CA  THR A  46       8.466  34.765 111.713  1.00 34.78           C  
ATOM    395  C   THR A  46       9.490  34.176 110.747  1.00 37.09           C  
ATOM    396  O   THR A  46       9.315  33.069 110.240  1.00 37.29           O  
ATOM    397  CB  THR A  46       7.366  35.456 110.891  1.00 29.70           C  
ATOM    398  OG1 THR A  46       7.932  36.559 110.171  1.00 38.75           O  
ATOM    399  CG2 THR A  46       6.259  35.973 111.803  1.00 29.71           C  
ATOM    400  N   ALA A  47      10.562  34.917 110.493  1.00 34.82           N  
ATOM    401  CA  ALA A  47      11.600  34.447 109.581  1.00 32.22           C  
ATOM    402  C   ALA A  47      12.493  33.414 110.257  1.00 27.48           C  
ATOM    403  O   ALA A  47      13.396  32.874 109.629  1.00 42.29           O  
ATOM    404  CB  ALA A  47      12.440  35.624 109.094  1.00 24.14           C  
ATOM    405  N   CYS A  48      12.235  33.140 111.535  1.00 39.78           N  
ATOM    406  CA  CYS A  48      13.032  32.182 112.294  1.00 30.80           C  
ATOM    407  C   CYS A  48      12.280  30.975 112.843  1.00 45.10           C  
ATOM    408  O   CYS A  48      12.799  30.266 113.710  1.00 45.65           O  
ATOM    409  CB  CYS A  48      13.733  32.890 113.456  1.00 40.26           C  
ATOM    410  SG  CYS A  48      15.072  33.996 112.925  1.00 34.17           S  
ATOM    411  N   GLU A  49      11.076  30.721 112.344  1.00 46.57           N  
ATOM    412  CA  GLU A  49      10.307  29.583 112.838  1.00 63.13           C  
ATOM    413  C   GLU A  49      11.026  28.245 112.680  1.00 55.77           C  
ATOM    414  O   GLU A  49      10.908  27.369 113.536  1.00 56.98           O  
ATOM    415  CB  GLU A  49       8.931  29.528 112.163  1.00 71.75           C  
ATOM    416  CG  GLU A  49       7.978  30.625 112.637  1.00 88.42           C  
ATOM    417  CD  GLU A  49       7.811  30.645 114.154  1.00 96.13           C  
ATOM    418  OE1 GLU A  49       7.318  29.640 114.712  1.00102.74           O  
ATOM    419  OE2 GLU A  49       8.175  31.662 114.788  1.00 87.86           O  
ATOM    420  N   SER A  50      11.784  28.089 111.601  1.00 57.35           N  
ATOM    421  CA  SER A  50      12.507  26.842 111.377  1.00 51.35           C  
ATOM    422  C   SER A  50      13.717  26.715 112.301  1.00 51.26           C  
ATOM    423  O   SER A  50      14.528  25.799 112.151  1.00 47.13           O  
ATOM    424  CB  SER A  50      12.962  26.737 109.911  1.00 59.33           C  
ATOM    425  OG  SER A  50      13.879  27.763 109.552  1.00 55.06           O  
ATOM    426  N   ALA A  51      13.836  27.623 113.266  1.00 44.47           N  
ATOM    427  CA  ALA A  51      14.970  27.583 114.177  1.00 36.19           C  
ATOM    428  C   ALA A  51      14.641  27.950 115.616  1.00 38.47           C  
ATOM    429  O   ALA A  51      15.467  28.550 116.301  1.00 48.76           O  
ATOM    430  CB  ALA A  51      16.070  28.495 113.654  1.00 39.60           C  
ATOM    431  N   ARG A  52      13.455  27.586 116.094  1.00 47.27           N  
ATOM    432  CA  ARG A  52      13.091  27.929 117.466  1.00 50.35           C  
ATOM    433  C   ARG A  52      13.675  27.000 118.520  1.00 45.67           C  
ATOM    434  O   ARG A  52      13.592  27.286 119.713  1.00 57.93           O  
ATOM    435  CB  ARG A  52      11.565  28.011 117.618  1.00 61.90           C  
ATOM    436  CG  ARG A  52      10.954  29.182 116.845  1.00 72.41           C  
ATOM    437  CD  ARG A  52       9.503  29.471 117.213  1.00 73.22           C  
ATOM    438  NE  ARG A  52       9.360  30.423 118.316  1.00 75.98           N  
ATOM    439  CZ  ARG A  52       9.504  30.127 119.607  1.00 76.97           C  
ATOM    440  NH1 ARG A  52       9.803  28.892 119.989  1.00 80.94           N  
ATOM    441  NH2 ARG A  52       9.334  31.071 120.524  1.00 67.81           N  
ATOM    442  N   ASN A  53      14.276  25.897 118.085  1.00 45.89           N  
ATOM    443  CA  ASN A  53      14.881  24.945 119.013  1.00 48.03           C  
ATOM    444  C   ASN A  53      16.239  24.461 118.511  1.00 51.62           C  
ATOM    445  O   ASN A  53      16.365  24.026 117.365  1.00 58.40           O  
ATOM    446  CB  ASN A  53      13.968  23.734 119.207  1.00 58.81           C  
ATOM    447  CG  ASN A  53      12.581  24.115 119.683  1.00 72.48           C  
ATOM    448  OD1 ASN A  53      12.418  24.757 120.724  1.00 68.44           O  
ATOM    449  ND2 ASN A  53      11.567  23.712 118.921  1.00 74.32           N  
ATOM    450  N   PRO A  54      17.278  24.538 119.360  1.00 47.45           N  
ATOM    451  CA  PRO A  54      17.220  25.052 120.731  1.00 47.22           C  
ATOM    452  C   PRO A  54      17.320  26.576 120.756  1.00 44.81           C  
ATOM    453  O   PRO A  54      17.357  27.217 119.712  1.00 43.50           O  
ATOM    454  CB  PRO A  54      18.415  24.379 121.397  1.00 47.48           C  
ATOM    455  CG  PRO A  54      19.421  24.365 120.297  1.00 53.32           C  
ATOM    456  CD  PRO A  54      18.593  23.926 119.092  1.00 54.05           C  
ATOM    457  N   ARG A  55      17.376  27.145 121.953  1.00 43.69           N  
ATOM    458  CA  ARG A  55      17.456  28.591 122.115  1.00 46.18           C  
ATOM    459  C   ARG A  55      18.690  29.196 121.437  1.00 50.69           C  
ATOM    460  O   ARG A  55      18.635  30.304 120.900  1.00 45.29           O  
ATOM    461  CB  ARG A  55      17.451  28.940 123.609  1.00 41.58           C  
ATOM    462  CG  ARG A  55      17.390  30.430 123.921  1.00 41.07           C  
ATOM    463  CD  ARG A  55      16.093  31.064 123.425  1.00 47.14           C  
ATOM    464  NE  ARG A  55      16.094  32.515 123.599  1.00 37.84           N  
ATOM    465  CZ  ARG A  55      15.559  33.152 124.636  1.00 42.19           C  
ATOM    466  NH1 ARG A  55      14.961  32.472 125.606  1.00 31.57           N  
ATOM    467  NH2 ARG A  55      15.635  34.475 124.710  1.00 30.01           N  
ATOM    468  N   GLU A  56      19.799  28.464 121.459  1.00 51.17           N  
ATOM    469  CA  GLU A  56      21.042  28.940 120.862  1.00 46.37           C  
ATOM    470  C   GLU A  56      20.843  29.166 119.366  1.00 45.93           C  
ATOM    471  O   GLU A  56      21.403  30.088 118.777  1.00 38.82           O  
ATOM    472  CB  GLU A  56      22.160  27.909 121.071  1.00 52.27           C  
ATOM    473  CG AGLU A  56      22.391  27.476 122.519  0.50 55.13           C  
ATOM    474  CG BGLU A  56      23.550  28.367 120.641  0.50 53.02           C  
ATOM    475  CD AGLU A  56      21.372  26.467 123.012  0.50 54.76           C  
ATOM    476  CD BGLU A  56      24.148  29.404 121.581  0.50 68.61           C  
ATOM    477  OE1AGLU A  56      20.198  26.839 123.209  0.50 62.86           O  
ATOM    478  OE1BGLU A  56      23.585  30.514 121.683  0.50 68.59           O  
ATOM    479  OE2AGLU A  56      21.750  25.292 123.198  0.50 60.39           O  
ATOM    480  OE2BGLU A  56      25.179  29.104 122.224  0.50 67.88           O  
ATOM    481  N   LYS A  57      20.037  28.304 118.763  1.00 43.67           N  
ATOM    482  CA  LYS A  57      19.749  28.356 117.338  1.00 42.76           C  
ATOM    483  C   LYS A  57      18.814  29.522 117.054  1.00 43.81           C  
ATOM    484  O   LYS A  57      19.005  30.266 116.091  1.00 44.72           O  
ATOM    485  CB  LYS A  57      19.116  27.022 116.921  1.00 34.10           C  
ATOM    486  CG  LYS A  57      18.796  26.840 115.458  1.00 40.52           C  
ATOM    487  CD  LYS A  57      18.294  25.416 115.245  1.00 49.43           C  
ATOM    488  CE  LYS A  57      17.663  25.202 113.875  1.00 48.07           C  
ATOM    489  NZ  LYS A  57      18.635  25.324 112.765  1.00 54.48           N  
ATOM    490  N   LEU A  58      17.808  29.683 117.906  1.00 43.45           N  
ATOM    491  CA  LEU A  58      16.842  30.761 117.757  1.00 40.64           C  
ATOM    492  C   LEU A  58      17.530  32.109 117.930  1.00 37.23           C  
ATOM    493  O   LEU A  58      17.333  33.011 117.123  1.00 41.06           O  
ATOM    494  CB  LEU A  58      15.715  30.614 118.786  1.00 37.68           C  
ATOM    495  CG  LEU A  58      14.696  31.754 118.864  1.00 38.68           C  
ATOM    496  CD1 LEU A  58      13.971  31.891 117.542  1.00 36.68           C  
ATOM    497  CD2 LEU A  58      13.708  31.479 119.976  1.00 41.73           C  
ATOM    498  N   ASN A  59      18.342  32.241 118.975  1.00 39.19           N  
ATOM    499  CA  ASN A  59      19.044  33.497 119.222  1.00 41.01           C  
ATOM    500  C   ASN A  59      19.969  33.864 118.065  1.00 41.49           C  
ATOM    501  O   ASN A  59      20.109  35.038 117.719  1.00 40.18           O  
ATOM    502  CB  ASN A  59      19.859  33.428 120.514  1.00 44.58           C  
ATOM    503  CG  ASN A  59      18.992  33.323 121.750  1.00 52.35           C  
ATOM    504  OD1 ASN A  59      17.888  33.867 121.802  1.00 44.04           O  
ATOM    505  ND2 ASN A  59      19.499  32.634 122.765  1.00 52.86           N  
ATOM    506  N   GLU A  60      20.610  32.864 117.472  1.00 31.03           N  
ATOM    507  CA  GLU A  60      21.497  33.137 116.355  1.00 38.53           C  
ATOM    508  C   GLU A  60      20.682  33.637 115.165  1.00 41.06           C  
ATOM    509  O   GLU A  60      21.047  34.620 114.513  1.00 39.16           O  
ATOM    510  CB  GLU A  60      22.266  31.883 115.949  1.00 28.79           C  
ATOM    511  CG  GLU A  60      23.139  32.128 114.741  1.00 43.87           C  
ATOM    512  CD  GLU A  60      23.750  30.870 114.195  1.00 44.54           C  
ATOM    513  OE1 GLU A  60      23.001  29.896 113.974  1.00 44.40           O  
ATOM    514  OE2 GLU A  60      24.978  30.861 113.972  1.00 53.95           O  
ATOM    515  N   CYS A  61      19.577  32.953 114.886  1.00 39.51           N  
ATOM    516  CA  CYS A  61      18.710  33.337 113.777  1.00 41.28           C  
ATOM    517  C   CYS A  61      18.185  34.761 113.950  1.00 39.22           C  
ATOM    518  O   CYS A  61      18.193  35.551 113.006  1.00 35.70           O  
ATOM    519  CB  CYS A  61      17.525  32.371 113.660  1.00 40.82           C  
ATOM    520  SG  CYS A  61      16.464  32.700 112.217  1.00 38.66           S  
ATOM    521  N   LEU A  62      17.741  35.086 115.161  1.00 38.82           N  
ATOM    522  CA  LEU A  62      17.202  36.410 115.448  1.00 41.17           C  
ATOM    523  C   LEU A  62      18.262  37.502 115.367  1.00 36.36           C  
ATOM    524  O   LEU A  62      17.967  38.624 114.961  1.00 34.37           O  
ATOM    525  CB  LEU A  62      16.529  36.423 116.826  1.00 35.20           C  
ATOM    526  CG  LEU A  62      15.245  35.599 116.957  1.00 26.81           C  
ATOM    527  CD1 LEU A  62      14.780  35.616 118.400  1.00 44.08           C  
ATOM    528  CD2 LEU A  62      14.156  36.162 116.047  1.00 38.07           C  
ATOM    529  N   GLU A  63      19.492  37.180 115.754  1.00 37.44           N  
ATOM    530  CA  GLU A  63      20.580  38.151 115.680  1.00 38.56           C  
ATOM    531  C   GLU A  63      20.739  38.490 114.194  1.00 44.15           C  
ATOM    532  O   GLU A  63      21.021  39.630 113.825  1.00 43.45           O  
ATOM    533  CB  GLU A  63      21.876  37.550 116.232  1.00 35.55           C  
ATOM    534  CG  GLU A  63      23.090  38.483 116.185  1.00 60.59           C  
ATOM    535  CD  GLU A  63      23.030  39.607 117.216  1.00 67.88           C  
ATOM    536  OE1 GLU A  63      22.991  39.306 118.429  1.00 72.19           O  
ATOM    537  OE2 GLU A  63      23.027  40.790 116.814  1.00 72.75           O  
ATOM    538  N   GLY A  64      20.562  37.475 113.352  1.00 38.24           N  
ATOM    539  CA  GLY A  64      20.639  37.663 111.916  1.00 35.27           C  
ATOM    540  C   GLY A  64      21.962  37.943 111.231  1.00 36.63           C  
ATOM    541  O   GLY A  64      21.979  38.593 110.184  1.00 39.52           O  
ATOM    542  N   ASN A  65      23.070  37.472 111.786  1.00 40.86           N  
ATOM    543  CA  ASN A  65      24.355  37.696 111.137  1.00 38.16           C  
ATOM    544  C   ASN A  65      24.534  36.653 110.045  1.00 47.66           C  
ATOM    545  O   ASN A  65      25.423  36.760 109.194  1.00 52.08           O  
ATOM    546  CB  ASN A  65      25.494  37.599 112.145  1.00 52.56           C  
ATOM    547  CG  ASN A  65      25.810  38.928 112.785  1.00 60.30           C  
ATOM    548  OD1 ASN A  65      26.237  39.867 112.110  1.00 70.25           O  
ATOM    549  ND2 ASN A  65      25.602  39.021 114.092  1.00 63.12           N  
ATOM    550  N   CYS A  66      23.674  35.641 110.085  1.00 38.60           N  
ATOM    551  CA  CYS A  66      23.683  34.559 109.111  1.00 35.89           C  
ATOM    552  C   CYS A  66      22.254  34.442 108.619  1.00 43.14           C  
ATOM    553  O   CYS A  66      21.327  34.943 109.264  1.00 38.77           O  
ATOM    554  CB  CYS A  66      24.111  33.241 109.766  1.00 34.80           C  
ATOM    555  SG  CYS A  66      23.080  32.781 111.197  1.00 39.36           S  
ATOM    556  N   ALA A  67      22.077  33.780 107.483  1.00 35.39           N  
ATOM    557  CA  ALA A  67      20.752  33.603 106.911  1.00 40.03           C  
ATOM    558  C   ALA A  67      20.172  32.223 107.200  1.00 40.31           C  
ATOM    559  O   ALA A  67      20.803  31.203 106.925  1.00 37.47           O  
ATOM    560  CB  ALA A  67      20.803  33.836 105.404  1.00 34.04           C  
ATOM    561  N   GLU A  68      18.969  32.204 107.767  1.00 39.70           N  
ATOM    562  CA  GLU A  68      18.269  30.960 108.063  1.00 40.33           C  
ATOM    563  C   GLU A  68      17.249  30.779 106.949  1.00 41.00           C  
ATOM    564  O   GLU A  68      16.535  31.716 106.592  1.00 46.41           O  
ATOM    565  CB  GLU A  68      17.556  31.049 109.413  1.00 44.29           C  
ATOM    566  CG  GLU A  68      16.558  29.920 109.694  1.00 42.46           C  
ATOM    567  CD  GLU A  68      17.198  28.539 109.779  1.00 38.70           C  
ATOM    568  OE1 GLU A  68      18.420  28.456 110.021  1.00 41.95           O  
ATOM    569  OE2 GLU A  68      16.471  27.533 109.623  1.00 42.81           O  
ATOM    570  N   GLY A  69      17.187  29.579 106.392  1.00 42.53           N  
ATOM    571  CA  GLY A  69      16.255  29.343 105.310  1.00 39.32           C  
ATOM    572  C   GLY A  69      16.617  30.207 104.111  1.00 52.79           C  
ATOM    573  O   GLY A  69      17.753  30.183 103.631  1.00 49.87           O  
ATOM    574  N   VAL A  70      15.658  30.989 103.632  1.00 47.18           N  
ATOM    575  CA  VAL A  70      15.896  31.844 102.482  1.00 45.47           C  
ATOM    576  C   VAL A  70      16.548  33.176 102.890  1.00 47.67           C  
ATOM    577  O   VAL A  70      16.865  34.015 102.045  1.00 34.18           O  
ATOM    578  CB  VAL A  70      14.564  32.035 101.699  1.00 39.68           C  
ATOM    579  CG1 VAL A  70      14.145  33.482 101.652  1.00 55.93           C  
ATOM    580  CG2 VAL A  70      14.710  31.453 100.319  1.00 43.92           C  
ATOM    581  N   GLY A  71      16.757  33.358 104.193  1.00 41.58           N  
ATOM    582  CA  GLY A  71      17.404  34.568 104.674  1.00 45.81           C  
ATOM    583  C   GLY A  71      16.581  35.801 105.025  1.00 41.67           C  
ATOM    584  O   GLY A  71      17.150  36.866 105.266  1.00 40.73           O  
ATOM    585  N   MET A  72      15.259  35.686 105.058  1.00 36.75           N  
ATOM    586  CA  MET A  72      14.426  36.835 105.409  1.00 41.93           C  
ATOM    587  C   MET A  72      14.808  37.402 106.778  1.00 36.63           C  
ATOM    588  O   MET A  72      14.482  38.540 107.110  1.00 39.71           O  
ATOM    589  CB  MET A  72      12.949  36.436 105.412  1.00 37.65           C  
ATOM    590  CG  MET A  72      12.383  36.190 104.028  1.00 34.98           C  
ATOM    591  SD  MET A  72      10.601  35.985 104.048  1.00 37.29           S  
ATOM    592  CE  MET A  72      10.075  37.680 104.435  1.00 29.78           C  
ATOM    593  N   ASN A  73      15.519  36.593 107.554  1.00 39.89           N  
ATOM    594  CA  ASN A  73      15.964  36.949 108.895  1.00 37.93           C  
ATOM    595  C   ASN A  73      17.302  37.689 108.883  1.00 46.52           C  
ATOM    596  O   ASN A  73      17.718  38.251 109.904  1.00 34.57           O  
ATOM    597  CB  ASN A  73      16.154  35.678 109.707  1.00 45.23           C  
ATOM    598  CG  ASN A  73      17.386  34.902 109.269  1.00 30.24           C  
ATOM    599  OD1 ASN A  73      17.484  34.464 108.119  1.00 36.01           O  
ATOM    600  ND2 ASN A  73      18.339  34.744 110.178  1.00 31.75           N  
ATOM    601  N   TYR A  74      17.986  37.670 107.740  1.00 34.87           N  
ATOM    602  CA  TYR A  74      19.294  38.305 107.645  1.00 41.71           C  
ATOM    603  C   TYR A  74      19.275  39.808 107.926  1.00 35.44           C  
ATOM    604  O   TYR A  74      18.475  40.548 107.357  1.00 32.26           O  
ATOM    605  CB  TYR A  74      19.916  38.035 106.273  1.00 38.30           C  
ATOM    606  CG  TYR A  74      21.321  38.573 106.155  1.00 45.80           C  
ATOM    607  CD1 TYR A  74      22.375  37.968 106.829  1.00 29.06           C  
ATOM    608  CD2 TYR A  74      21.589  39.719 105.406  1.00 36.22           C  
ATOM    609  CE1 TYR A  74      23.663  38.494 106.765  1.00 44.50           C  
ATOM    610  CE2 TYR A  74      22.867  40.249 105.334  1.00 38.18           C  
ATOM    611  CZ  TYR A  74      23.898  39.633 106.015  1.00 37.59           C  
ATOM    612  OH  TYR A  74      25.163  40.160 105.943  1.00 39.64           O  
ATOM    613  N   ARG A  75      20.167  40.243 108.812  1.00 38.35           N  
ATOM    614  CA  ARG A  75      20.281  41.653 109.192  1.00 41.21           C  
ATOM    615  C   ARG A  75      21.752  42.081 109.216  1.00 41.93           C  
ATOM    616  O   ARG A  75      22.111  43.058 109.875  1.00 39.26           O  
ATOM    617  CB  ARG A  75      19.659  41.884 110.583  1.00 35.78           C  
ATOM    618  CG  ARG A  75      18.144  41.701 110.651  1.00 26.34           C  
ATOM    619  CD  ARG A  75      17.452  42.747 109.825  1.00 39.97           C  
ATOM    620  NE  ARG A  75      15.996  42.657 109.833  1.00 28.68           N  
ATOM    621  CZ  ARG A  75      15.293  41.723 109.202  1.00 33.68           C  
ATOM    622  NH1 ARG A  75      15.907  40.773 108.514  1.00 31.00           N  
ATOM    623  NH2 ARG A  75      13.968  41.769 109.223  1.00 25.14           N  
ATOM    624  N   GLY A  76      22.595  41.345 108.496  1.00 47.06           N  
ATOM    625  CA  GLY A  76      24.018  41.647 108.461  1.00 39.05           C  
ATOM    626  C   GLY A  76      24.397  42.901 107.693  1.00 41.09           C  
ATOM    627  O   GLY A  76      23.533  43.694 107.324  1.00 45.95           O  
ATOM    628  N   ASN A  77      25.829  43.158 107.570  1.00 40.76           N  
ATOM    629  CA  ASN A  77      26.323  44.289 106.802  1.00 43.23           C  
ATOM    630  C   ASN A  77      26.988  44.027 105.442  1.00 46.42           C  
ATOM    631  O   ASN A  77      27.546  44.939 104.887  1.00 43.16           O  
ATOM    632  CB  ASN A  77      27.329  45.042 107.694  1.00 49.74           C  
ATOM    633  CG  ASN A  77      26.662  45.732 108.854  1.00 53.72           C  
ATOM    634  OD1 ASN A  77      25.452  45.582 109.109  1.00 51.69           O  
ATOM    635  ND2 ASN A  77      27.475  46.492 109.590  1.00 65.62           N  
ATOM    636  N   VAL A  78      26.643  42.883 104.754  1.00 35.19           N  
ATOM    637  CA  VAL A  78      27.198  42.689 103.422  1.00 34.08           C  
ATOM    638  C   VAL A  78      26.424  43.645 102.516  1.00 44.49           C  
ATOM    639  O   VAL A  78      25.193  43.705 102.575  1.00 37.11           O  
ATOM    640  CB  VAL A  78      27.038  41.234 102.943  1.00 31.92           C  
ATOM    641  CG1 VAL A  78      27.397  41.116 101.474  1.00 26.34           C  
ATOM    642  CG2 VAL A  78      27.954  40.326 103.766  1.00 37.42           C  
ATOM    643  N   SER A  79      27.151  44.417 101.710  1.00 41.04           N  
ATOM    644  CA  SER A  79      26.530  45.390 100.819  1.00 42.52           C  
ATOM    645  C   SER A  79      26.985  45.244  99.371  1.00 43.81           C  
ATOM    646  O   SER A  79      26.851  46.164  98.564  1.00 46.74           O  
ATOM    647  CB  SER A  79      26.807  46.811 101.328  1.00 40.48           C  
ATOM    648  OG  SER A  79      28.182  47.003 101.595  1.00 37.17           O  
ATOM    649  N   VAL A  80      27.517  44.075  99.045  1.00 45.72           N  
ATOM    650  CA  VAL A  80      27.967  43.797  97.691  1.00 42.50           C  
ATOM    651  C   VAL A  80      27.226  42.563  97.192  1.00 38.78           C  
ATOM    652  O   VAL A  80      26.971  41.634  97.955  1.00 49.53           O  
ATOM    653  CB  VAL A  80      29.482  43.526  97.652  1.00 49.10           C  
ATOM    654  CG1 VAL A  80      29.922  43.245  96.237  1.00 47.11           C  
ATOM    655  CG2 VAL A  80      30.234  44.720  98.210  1.00 60.78           C  
ATOM    656  N   THR A  81      26.873  42.552  95.914  1.00 38.89           N  
ATOM    657  CA  THR A  81      26.168  41.411  95.359  1.00 41.42           C  
ATOM    658  C   THR A  81      27.113  40.252  95.058  1.00 46.14           C  
ATOM    659  O   THR A  81      28.336  40.354  95.192  1.00 42.67           O  
ATOM    660  CB  THR A  81      25.439  41.758  94.054  1.00 49.71           C  
ATOM    661  OG1 THR A  81      26.398  41.899  93.000  1.00 41.47           O  
ATOM    662  CG2 THR A  81      24.648  43.046  94.205  1.00 42.44           C  
ATOM    663  N   ARG A  82      26.507  39.147  94.652  1.00 42.09           N  
ATOM    664  CA  ARG A  82      27.204  37.921  94.305  1.00 49.36           C  
ATOM    665  C   ARG A  82      28.318  38.195  93.294  1.00 50.68           C  
ATOM    666  O   ARG A  82      29.466  37.802  93.503  1.00 44.92           O  
ATOM    667  CB  ARG A  82      26.177  36.942  93.728  1.00 51.10           C  
ATOM    668  CG  ARG A  82      26.682  35.574  93.360  1.00 66.67           C  
ATOM    669  CD  ARG A  82      25.500  34.708  92.972  1.00 72.36           C  
ATOM    670  NE  ARG A  82      25.883  33.325  92.719  1.00 88.78           N  
ATOM    671  CZ  ARG A  82      25.030  32.306  92.717  1.00 86.46           C  
ATOM    672  NH1 ARG A  82      23.742  32.519  92.961  1.00 83.87           N  
ATOM    673  NH2 ARG A  82      25.463  31.077  92.466  1.00 85.40           N  
ATOM    674  N   SER A  83      27.978  38.883  92.207  1.00 48.27           N  
ATOM    675  CA  SER A  83      28.953  39.193  91.167  1.00 52.94           C  
ATOM    676  C   SER A  83      29.912  40.329  91.539  1.00 52.69           C  
ATOM    677  O   SER A  83      30.787  40.683  90.754  1.00 55.95           O  
ATOM    678  CB  SER A  83      28.236  39.528  89.854  1.00 49.30           C  
ATOM    679  OG  SER A  83      27.582  40.780  89.924  1.00 52.76           O  
ATOM    680  N   GLY A  84      29.742  40.905  92.726  1.00 54.59           N  
ATOM    681  CA  GLY A  84      30.626  41.975  93.159  1.00 43.22           C  
ATOM    682  C   GLY A  84      30.153  43.400  92.927  1.00 45.90           C  
ATOM    683  O   GLY A  84      30.918  44.347  93.098  1.00 45.94           O  
ATOM    684  N   ILE A  85      28.900  43.573  92.532  1.00 43.49           N  
ATOM    685  CA  ILE A  85      28.381  44.918  92.310  1.00 44.39           C  
ATOM    686  C   ILE A  85      28.002  45.574  93.645  1.00 41.39           C  
ATOM    687  O   ILE A  85      27.294  44.983  94.461  1.00 41.01           O  
ATOM    688  CB  ILE A  85      27.137  44.886  91.404  1.00 42.17           C  
ATOM    689  CG1 ILE A  85      27.466  44.157  90.103  1.00 29.37           C  
ATOM    690  CG2 ILE A  85      26.666  46.306  91.115  1.00 38.87           C  
ATOM    691  CD1 ILE A  85      26.266  43.906  89.217  1.00 34.15           C  
ATOM    692  N   GLU A  86      28.496  46.787  93.864  1.00 42.87           N  
ATOM    693  CA  GLU A  86      28.203  47.548  95.073  1.00 35.83           C  
ATOM    694  C   GLU A  86      26.688  47.793  95.129  1.00 43.54           C  
ATOM    695  O   GLU A  86      26.080  48.244  94.151  1.00 41.78           O  
ATOM    696  CB  GLU A  86      28.948  48.887  95.030  1.00 36.16           C  
ATOM    697  CG  GLU A  86      28.618  49.853  96.164  1.00 46.50           C  
ATOM    698  CD  GLU A  86      29.257  49.466  97.485  1.00 66.86           C  
ATOM    699  OE1 GLU A  86      29.144  48.288  97.883  1.00 73.47           O  
ATOM    700  OE2 GLU A  86      29.867  50.347  98.130  1.00 78.64           O  
ATOM    701  N   CYS A  87      26.078  47.494  96.271  1.00 38.24           N  
ATOM    702  CA  CYS A  87      24.637  47.672  96.425  1.00 41.31           C  
ATOM    703  C   CYS A  87      24.166  49.123  96.417  1.00 35.62           C  
ATOM    704  O   CYS A  87      24.864  50.021  96.887  1.00 40.94           O  
ATOM    705  CB  CYS A  87      24.159  47.029  97.727  1.00 40.40           C  
ATOM    706  SG  CYS A  87      24.149  45.215  97.764  1.00 38.15           S  
ATOM    707  N   GLN A  88      22.966  49.336  95.885  1.00 36.52           N  
ATOM    708  CA  GLN A  88      22.349  50.660  95.851  1.00 34.16           C  
ATOM    709  C   GLN A  88      21.672  50.912  97.206  1.00 35.06           C  
ATOM    710  O   GLN A  88      21.180  49.977  97.835  1.00 29.24           O  
ATOM    711  CB  GLN A  88      21.278  50.727  94.755  1.00 34.26           C  
ATOM    712  CG  GLN A  88      20.504  52.055  94.715  1.00 29.57           C  
ATOM    713  CD  GLN A  88      19.297  52.022  93.784  1.00 25.40           C  
ATOM    714  OE1 GLN A  88      19.405  51.656  92.611  1.00 41.12           O  
ATOM    715  NE2 GLN A  88      18.143  52.418  94.302  1.00 36.02           N  
ATOM    716  N   LEU A  89      21.655  52.167  97.650  1.00 35.61           N  
ATOM    717  CA  LEU A  89      21.010  52.534  98.910  1.00 40.45           C  
ATOM    718  C   LEU A  89      19.514  52.281  98.749  1.00 39.80           C  
ATOM    719  O   LEU A  89      18.915  52.733  97.774  1.00 38.20           O  
ATOM    720  CB  LEU A  89      21.228  54.019  99.217  1.00 32.90           C  
ATOM    721  CG  LEU A  89      22.623  54.517  99.590  1.00 44.22           C  
ATOM    722  CD1 LEU A  89      22.623  56.029  99.557  1.00 46.00           C  
ATOM    723  CD2 LEU A  89      23.015  54.014 100.977  1.00 43.51           C  
ATOM    724  N   TRP A  90      18.915  51.561  99.695  1.00 35.60           N  
ATOM    725  CA  TRP A  90      17.483  51.268  99.635  1.00 40.02           C  
ATOM    726  C   TRP A  90      16.640  52.531  99.478  1.00 38.08           C  
ATOM    727  O   TRP A  90      15.618  52.522  98.787  1.00 30.72           O  
ATOM    728  CB  TRP A  90      17.032  50.515 100.893  1.00 32.24           C  
ATOM    729  CG  TRP A  90      17.602  49.135 100.993  1.00 44.25           C  
ATOM    730  CD1 TRP A  90      18.686  48.741 101.727  1.00 42.84           C  
ATOM    731  CD2 TRP A  90      17.125  47.961 100.320  1.00 38.32           C  
ATOM    732  NE1 TRP A  90      18.911  47.394 101.553  1.00 39.27           N  
ATOM    733  CE2 TRP A  90      17.967  46.892 100.694  1.00 38.86           C  
ATOM    734  CE3 TRP A  90      16.065  47.710  99.436  1.00 35.33           C  
ATOM    735  CZ2 TRP A  90      17.784  45.590 100.215  1.00 33.98           C  
ATOM    736  CZ3 TRP A  90      15.883  46.414  98.959  1.00 34.95           C  
ATOM    737  CH2 TRP A  90      16.740  45.372  99.352  1.00 33.91           C  
ATOM    738  N   ARG A  91      17.078  53.615 100.115  1.00 40.81           N  
ATOM    739  CA  ARG A  91      16.356  54.883 100.057  1.00 39.32           C  
ATOM    740  C   ARG A  91      16.598  55.656  98.767  1.00 40.14           C  
ATOM    741  O   ARG A  91      15.836  56.556  98.436  1.00 47.27           O  
ATOM    742  CB  ARG A  91      16.722  55.772 101.252  1.00 36.56           C  
ATOM    743  CG  ARG A  91      18.171  56.249 101.282  1.00 37.23           C  
ATOM    744  CD  ARG A  91      18.343  57.318 102.341  1.00 46.06           C  
ATOM    745  NE  ARG A  91      19.668  57.929 102.320  1.00 53.30           N  
ATOM    746  CZ  ARG A  91      20.758  57.389 102.858  1.00 64.84           C  
ATOM    747  NH1 ARG A  91      20.697  56.211 103.473  1.00 54.35           N  
ATOM    748  NH2 ARG A  91      21.915  58.035 102.786  1.00 62.12           N  
ATOM    749  N   SER A  92      17.654  55.315  98.034  1.00 42.94           N  
ATOM    750  CA  SER A  92      17.933  56.019  96.787  1.00 30.55           C  
ATOM    751  C   SER A  92      16.942  55.611  95.710  1.00 42.63           C  
ATOM    752  O   SER A  92      16.385  54.509  95.737  1.00 32.81           O  
ATOM    753  CB  SER A  92      19.355  55.733  96.306  1.00 36.21           C  
ATOM    754  OG  SER A  92      19.640  56.475  95.131  1.00 38.26           O  
ATOM    755  N   ARG A  93      16.725  56.509  94.756  1.00 43.38           N  
ATOM    756  CA  ARG A  93      15.802  56.254  93.660  1.00 38.48           C  
ATOM    757  C   ARG A  93      16.583  56.109  92.349  1.00 39.73           C  
ATOM    758  O   ARG A  93      16.005  56.133  91.263  1.00 34.61           O  
ATOM    759  CB  ARG A  93      14.793  57.408  93.576  1.00 36.30           C  
ATOM    760  CG  ARG A  93      13.739  57.278  92.491  1.00 57.05           C  
ATOM    761  CD  ARG A  93      13.752  58.502  91.579  1.00 58.50           C  
ATOM    762  NE  ARG A  93      12.626  58.539  90.648  1.00 56.53           N  
ATOM    763  CZ  ARG A  93      11.352  58.676  91.012  1.00 66.44           C  
ATOM    764  NH1 ARG A  93      11.032  58.787  92.296  1.00 43.11           N  
ATOM    765  NH2 ARG A  93      10.396  58.713  90.091  1.00 66.63           N  
ATOM    766  N   TYR A  94      17.902  55.950  92.464  1.00 41.99           N  
ATOM    767  CA  TYR A  94      18.781  55.810  91.301  1.00 36.26           C  
ATOM    768  C   TYR A  94      19.949  54.865  91.604  1.00 37.03           C  
ATOM    769  O   TYR A  94      20.503  54.880  92.703  1.00 31.24           O  
ATOM    770  CB  TYR A  94      19.346  57.175  90.885  1.00 31.95           C  
ATOM    771  CG  TYR A  94      18.334  58.304  90.870  1.00 36.24           C  
ATOM    772  CD1 TYR A  94      18.132  59.103  91.998  1.00 31.19           C  
ATOM    773  CD2 TYR A  94      17.571  58.568  89.738  1.00 31.77           C  
ATOM    774  CE1 TYR A  94      17.197  60.136  91.993  1.00 27.22           C  
ATOM    775  CE2 TYR A  94      16.629  59.598  89.727  1.00 37.67           C  
ATOM    776  CZ  TYR A  94      16.447  60.378  90.856  1.00 29.18           C  
ATOM    777  OH  TYR A  94      15.507  61.391  90.847  1.00 28.89           O  
ATOM    778  N   PRO A  95      20.362  54.050  90.616  1.00 32.39           N  
ATOM    779  CA  PRO A  95      19.815  53.958  89.256  1.00 28.15           C  
ATOM    780  C   PRO A  95      18.479  53.230  89.092  1.00 35.29           C  
ATOM    781  O   PRO A  95      17.931  53.186  87.994  1.00 42.86           O  
ATOM    782  CB  PRO A  95      20.935  53.267  88.487  1.00 30.58           C  
ATOM    783  CG  PRO A  95      21.531  52.353  89.522  1.00 33.69           C  
ATOM    784  CD  PRO A  95      21.605  53.263  90.733  1.00 30.00           C  
ATOM    785  N   HIS A  96      17.950  52.658  90.169  1.00 47.88           N  
ATOM    786  CA  HIS A  96      16.679  51.935  90.082  1.00 44.76           C  
ATOM    787  C   HIS A  96      15.665  52.450  91.093  1.00 44.52           C  
ATOM    788  O   HIS A  96      16.010  52.714  92.247  1.00 44.93           O  
ATOM    789  CB  HIS A  96      16.909  50.440  90.322  1.00 41.10           C  
ATOM    790  CG  HIS A  96      17.997  49.855  89.478  1.00 37.71           C  
ATOM    791  ND1 HIS A  96      17.824  49.550  88.145  1.00 35.86           N  
ATOM    792  CD2 HIS A  96      19.290  49.576  89.765  1.00 37.71           C  
ATOM    793  CE1 HIS A  96      18.967  49.112  87.647  1.00 38.46           C  
ATOM    794  NE2 HIS A  96      19.872  49.118  88.609  1.00 37.76           N  
ATOM    795  N   LYS A  97      14.422  52.605  90.644  1.00 37.80           N  
ATOM    796  CA  LYS A  97      13.335  53.058  91.506  1.00 47.76           C  
ATOM    797  C   LYS A  97      12.787  51.835  92.243  1.00 42.81           C  
ATOM    798  O   LYS A  97      12.039  51.037  91.679  1.00 43.19           O  
ATOM    799  CB  LYS A  97      12.226  53.720  90.673  1.00 46.73           C  
ATOM    800  CG  LYS A  97      12.541  55.152  90.254  1.00 67.10           C  
ATOM    801  CD  LYS A  97      11.490  55.755  89.310  1.00 71.18           C  
ATOM    802  CE  LYS A  97      11.617  55.221  87.879  1.00 74.97           C  
ATOM    803  NZ  LYS A  97      10.844  56.028  86.875  1.00 56.57           N  
ATOM    804  N   PRO A  98      13.160  51.676  93.519  1.00 38.05           N  
ATOM    805  CA  PRO A  98      12.727  50.555  94.358  1.00 37.55           C  
ATOM    806  C   PRO A  98      11.221  50.344  94.454  1.00 43.40           C  
ATOM    807  O   PRO A  98      10.469  51.262  94.783  1.00 44.97           O  
ATOM    808  CB  PRO A  98      13.328  50.893  95.720  1.00 27.92           C  
ATOM    809  CG  PRO A  98      14.536  51.698  95.369  1.00 39.00           C  
ATOM    810  CD  PRO A  98      14.006  52.598  94.292  1.00 28.01           C  
ATOM    811  N   GLU A  99      10.788  49.125  94.158  1.00 44.40           N  
ATOM    812  CA  GLU A  99       9.379  48.769  94.261  1.00 39.13           C  
ATOM    813  C   GLU A  99       9.191  48.373  95.728  1.00 38.21           C  
ATOM    814  O   GLU A  99       8.090  48.430  96.271  1.00 41.51           O  
ATOM    815  CB  GLU A  99       9.060  47.570  93.357  1.00 43.44           C  
ATOM    816  CG  GLU A  99      10.295  46.891  92.750  1.00 59.08           C  
ATOM    817  CD  GLU A  99      10.218  45.367  92.755  1.00 73.20           C  
ATOM    818  OE1 GLU A  99       9.102  44.825  92.599  1.00 85.52           O  
ATOM    819  OE2 GLU A  99      11.276  44.709  92.899  1.00 48.98           O  
ATOM    820  N   ILE A 100      10.297  47.983  96.358  1.00 32.67           N  
ATOM    821  CA  ILE A 100      10.313  47.552  97.753  1.00 40.55           C  
ATOM    822  C   ILE A 100      11.122  48.502  98.633  1.00 38.87           C  
ATOM    823  O   ILE A 100      12.280  48.782  98.341  1.00 45.34           O  
ATOM    824  CB  ILE A 100      10.909  46.128  97.852  1.00 33.76           C  
ATOM    825  CG1 ILE A 100       9.947  45.131  97.200  1.00 34.17           C  
ATOM    826  CG2 ILE A 100      11.186  45.764  99.293  1.00 29.02           C  
ATOM    827  CD1 ILE A 100      10.463  43.706  97.142  1.00 48.24           C  
ATOM    828  N   ASN A 101      10.506  48.995  99.736  1.00 51.71           N  
ATOM    829  CA  ASN A 101      11.207  49.915 100.622  1.00 53.38           C  
ATOM    830  C   ASN A 101      10.577  49.934 102.008  1.00 50.42           C  
ATOM    831  O   ASN A 101       9.707  49.152 102.358  1.00 46.19           O  
ATOM    832  CB  ASN A 101      11.226  51.322 100.024  1.00 62.01           C  
ATOM    833  CG  ASN A 101       9.862  51.980 100.041  1.00 70.31           C  
ATOM    834  OD1 ASN A 101       9.237  52.108 101.094  1.00 78.26           O  
ATOM    835  ND2 ASN A 101       9.394  52.403  98.872  1.00 79.13           N  
ATOM    836  N   SER A 102      11.107  50.849 102.857  1.00 44.19           N  
ATOM    837  CA  SER A 102      10.652  51.032 104.235  1.00 48.34           C  
ATOM    838  C   SER A 102       9.134  51.071 104.379  1.00 51.75           C  
ATOM    839  O   SER A 102       8.579  50.568 105.360  1.00 60.56           O  
ATOM    840  CB  SER A 102      11.215  52.335 104.814  1.00 46.36           C  
ATOM    841  OG  SER A 102      12.626  52.388 104.729  1.00 58.47           O  
ATOM    842  N   THR A 103       8.463  51.676 103.407  1.00 53.38           N  
ATOM    843  CA  THR A 103       7.011  51.804 103.452  1.00 52.13           C  
ATOM    844  C   THR A 103       6.258  50.526 103.109  1.00 53.44           C  
ATOM    845  O   THR A 103       5.333  50.130 103.819  1.00 51.55           O  
ATOM    846  CB  THR A 103       6.541  52.924 102.515  1.00 56.43           C  
ATOM    847  OG1 THR A 103       7.109  54.167 102.947  1.00 48.14           O  
ATOM    848  CG2 THR A 103       5.019  53.024 102.517  1.00 56.90           C  
ATOM    849  N   THR A 104       6.649  49.884 102.017  1.00 55.75           N  
ATOM    850  CA  THR A 104       5.995  48.653 101.601  1.00 52.99           C  
ATOM    851  C   THR A 104       6.376  47.492 102.508  1.00 56.04           C  
ATOM    852  O   THR A 104       5.639  46.507 102.601  1.00 51.81           O  
ATOM    853  CB  THR A 104       6.376  48.265 100.152  1.00 55.54           C  
ATOM    854  OG1 THR A 104       7.804  48.178 100.041  1.00 48.44           O  
ATOM    855  CG2 THR A 104       5.841  49.286  99.161  1.00 40.76           C  
ATOM    856  N   HIS A 105       7.523  47.607 103.174  1.00 51.32           N  
ATOM    857  CA  HIS A 105       7.998  46.535 104.044  1.00 48.83           C  
ATOM    858  C   HIS A 105       8.642  47.002 105.343  1.00 53.27           C  
ATOM    859  O   HIS A 105       9.859  46.885 105.524  1.00 43.49           O  
ATOM    860  CB  HIS A 105       8.988  45.662 103.281  1.00 40.22           C  
ATOM    861  CG  HIS A 105       8.400  45.007 102.075  1.00 34.51           C  
ATOM    862  ND1 HIS A 105       8.031  43.680 102.054  1.00 49.15           N  
ATOM    863  CD2 HIS A 105       8.094  45.502 100.852  1.00 34.30           C  
ATOM    864  CE1 HIS A 105       7.525  43.384 100.869  1.00 47.84           C  
ATOM    865  NE2 HIS A 105       7.553  44.472 100.121  1.00 41.16           N  
ATOM    866  N   PRO A 106       7.831  47.536 106.271  1.00 57.23           N  
ATOM    867  CA  PRO A 106       8.381  47.999 107.548  1.00 52.73           C  
ATOM    868  C   PRO A 106       8.820  46.769 108.343  1.00 54.19           C  
ATOM    869  O   PRO A 106       8.177  45.714 108.277  1.00 54.19           O  
ATOM    870  CB  PRO A 106       7.200  48.725 108.181  1.00 55.54           C  
ATOM    871  CG  PRO A 106       6.022  47.911 107.695  1.00 48.84           C  
ATOM    872  CD  PRO A 106       6.361  47.676 106.239  1.00 48.00           C  
ATOM    873  N   GLY A 107       9.919  46.893 109.077  1.00 47.88           N  
ATOM    874  CA  GLY A 107      10.406  45.759 109.842  1.00 46.79           C  
ATOM    875  C   GLY A 107      11.390  44.891 109.069  1.00 38.37           C  
ATOM    876  O   GLY A 107      11.934  43.931 109.610  1.00 42.37           O  
ATOM    877  N   ALA A 108      11.620  45.224 107.802  1.00 37.55           N  
ATOM    878  CA  ALA A 108      12.555  44.469 106.971  1.00 34.74           C  
ATOM    879  C   ALA A 108      13.981  44.977 107.172  1.00 43.24           C  
ATOM    880  O   ALA A 108      14.945  44.357 106.713  1.00 43.77           O  
ATOM    881  CB  ALA A 108      12.166  44.583 105.513  1.00 27.63           C  
ATOM    882  N   ASP A 109      14.101  46.102 107.872  1.00 36.60           N  
ATOM    883  CA  ASP A 109      15.390  46.725 108.150  1.00 32.24           C  
ATOM    884  C   ASP A 109      16.164  47.023 106.880  1.00 35.19           C  
ATOM    885  O   ASP A 109      17.331  46.645 106.741  1.00 34.50           O  
ATOM    886  CB  ASP A 109      16.238  45.845 109.065  1.00 38.00           C  
ATOM    887  CG  ASP A 109      17.481  46.562 109.567  1.00 42.76           C  
ATOM    888  OD1 ASP A 109      17.369  47.763 109.882  1.00 41.50           O  
ATOM    889  OD2 ASP A 109      18.560  45.935 109.659  1.00 46.43           O  
ATOM    890  N   LEU A 110      15.498  47.702 105.951  1.00 33.50           N  
ATOM    891  CA  LEU A 110      16.109  48.083 104.688  1.00 41.29           C  
ATOM    892  C   LEU A 110      16.924  49.358 104.902  1.00 44.19           C  
ATOM    893  O   LEU A 110      16.548  50.438 104.437  1.00 44.30           O  
ATOM    894  CB  LEU A 110      15.021  48.316 103.643  1.00 39.07           C  
ATOM    895  CG  LEU A 110      14.080  47.127 103.430  1.00 38.11           C  
ATOM    896  CD1 LEU A 110      12.996  47.522 102.432  1.00 30.83           C  
ATOM    897  CD2 LEU A 110      14.870  45.908 102.930  1.00 29.60           C  
ATOM    898  N   ARG A 111      18.037  49.225 105.623  1.00 45.16           N  
ATOM    899  CA  ARG A 111      18.914  50.358 105.916  1.00 41.82           C  
ATOM    900  C   ARG A 111      20.097  50.432 104.965  1.00 37.65           C  
ATOM    901  O   ARG A 111      20.595  49.406 104.498  1.00 32.90           O  
ATOM    902  CB  ARG A 111      19.445  50.279 107.356  1.00 47.13           C  
ATOM    903  CG  ARG A 111      18.439  50.665 108.430  1.00 68.61           C  
ATOM    904  CD  ARG A 111      19.083  50.763 109.818  1.00 61.03           C  
ATOM    905  NE  ARG A 111      19.571  49.478 110.318  1.00 48.31           N  
ATOM    906  CZ  ARG A 111      20.713  48.905 109.952  1.00 50.84           C  
ATOM    907  NH1 ARG A 111      21.508  49.497 109.073  1.00 76.03           N  
ATOM    908  NH2 ARG A 111      21.065  47.737 110.469  1.00 61.24           N  
ATOM    909  N   GLU A 112      20.549  51.656 104.701  1.00 35.21           N  
ATOM    910  CA  GLU A 112      21.672  51.895 103.807  1.00 30.62           C  
ATOM    911  C   GLU A 112      21.563  51.035 102.544  1.00 37.52           C  
ATOM    912  O   GLU A 112      20.554  51.082 101.834  1.00 39.78           O  
ATOM    913  CB  GLU A 112      22.980  51.589 104.533  1.00 42.44           C  
ATOM    914  CG  GLU A 112      23.111  52.296 105.866  1.00 58.64           C  
ATOM    915  CD  GLU A 112      24.493  52.159 106.456  1.00 63.76           C  
ATOM    916  OE1 GLU A 112      24.639  52.401 107.672  1.00 70.05           O  
ATOM    917  OE2 GLU A 112      25.432  51.816 105.702  1.00 70.98           O  
ATOM    918  N   ASN A 113      22.609  50.262 102.265  1.00 33.58           N  
ATOM    919  CA  ASN A 113      22.621  49.385 101.102  1.00 33.01           C  
ATOM    920  C   ASN A 113      22.986  47.960 101.502  1.00 38.86           C  
ATOM    921  O   ASN A 113      23.639  47.244 100.742  1.00 37.19           O  
ATOM    922  CB  ASN A 113      23.605  49.892 100.029  1.00 38.03           C  
ATOM    923  CG  ASN A 113      25.070  49.853 100.475  1.00 36.26           C  
ATOM    924  OD1 ASN A 113      25.973  49.981  99.648  1.00 37.43           O  
ATOM    925  ND2 ASN A 113      25.307  49.694 101.771  1.00 31.36           N  
ATOM    926  N   PHE A 114      22.574  47.555 102.701  1.00 37.15           N  
ATOM    927  CA  PHE A 114      22.856  46.203 103.176  1.00 39.20           C  
ATOM    928  C   PHE A 114      21.906  45.215 102.508  1.00 38.63           C  
ATOM    929  O   PHE A 114      20.744  45.532 102.257  1.00 38.07           O  
ATOM    930  CB  PHE A 114      22.700  46.116 104.697  1.00 30.67           C  
ATOM    931  CG  PHE A 114      23.605  47.045 105.457  1.00 36.37           C  
ATOM    932  CD1 PHE A 114      24.957  47.135 105.140  1.00 36.76           C  
ATOM    933  CD2 PHE A 114      23.111  47.814 106.505  1.00 44.80           C  
ATOM    934  CE1 PHE A 114      25.801  47.976 105.854  1.00 38.07           C  
ATOM    935  CE2 PHE A 114      23.949  48.658 107.227  1.00 44.04           C  
ATOM    936  CZ  PHE A 114      25.298  48.738 106.900  1.00 42.67           C  
ATOM    937  N   CYS A 115      22.407  44.020 102.216  1.00 38.79           N  
ATOM    938  CA  CYS A 115      21.596  42.994 101.577  1.00 38.73           C  
ATOM    939  C   CYS A 115      20.481  42.520 102.494  1.00 33.58           C  
ATOM    940  O   CYS A 115      20.682  42.333 103.689  1.00 35.64           O  
ATOM    941  CB  CYS A 115      22.472  41.814 101.181  1.00 36.81           C  
ATOM    942  SG  CYS A 115      23.750  42.273  99.983  1.00 36.93           S  
ATOM    943  N   ARG A 116      19.302  42.334 101.921  1.00 33.73           N  
ATOM    944  CA  ARG A 116      18.140  41.895 102.680  1.00 27.33           C  
ATOM    945  C   ARG A 116      17.244  41.085 101.764  1.00 34.22           C  
ATOM    946  O   ARG A 116      17.336  41.193 100.541  1.00 34.95           O  
ATOM    947  CB  ARG A 116      17.352  43.107 103.194  1.00 25.17           C  
ATOM    948  CG  ARG A 116      18.085  43.984 104.200  1.00 32.70           C  
ATOM    949  CD  ARG A 116      18.020  43.391 105.598  1.00 28.36           C  
ATOM    950  NE  ARG A 116      18.619  44.269 106.604  1.00 29.81           N  
ATOM    951  CZ  ARG A 116      19.918  44.312 106.881  1.00 31.91           C  
ATOM    952  NH1 ARG A 116      20.763  43.526 106.228  1.00 29.62           N  
ATOM    953  NH2 ARG A 116      20.370  45.127 107.822  1.00 26.64           N  
ATOM    954  N   ASN A 117      16.388  40.260 102.356  1.00 33.70           N  
ATOM    955  CA  ASN A 117      15.450  39.472 101.576  1.00 37.93           C  
ATOM    956  C   ASN A 117      14.058  39.767 102.116  1.00 40.24           C  
ATOM    957  O   ASN A 117      13.443  38.924 102.767  1.00 40.12           O  
ATOM    958  CB  ASN A 117      15.745  37.980 101.691  1.00 31.41           C  
ATOM    959  CG  ASN A 117      15.040  37.177 100.617  1.00 34.19           C  
ATOM    960  OD1 ASN A 117      14.281  37.726  99.828  1.00 30.32           O  
ATOM    961  ND2 ASN A 117      15.289  35.883 100.579  1.00 31.19           N  
ATOM    962  N   PRO A 118      13.548  40.981 101.850  1.00 41.27           N  
ATOM    963  CA  PRO A 118      12.226  41.415 102.308  1.00 35.02           C  
ATOM    964  C   PRO A 118      11.035  40.709 101.663  1.00 38.32           C  
ATOM    965  O   PRO A 118       9.954  40.658 102.248  1.00 32.88           O  
ATOM    966  CB  PRO A 118      12.243  42.914 102.015  1.00 37.11           C  
ATOM    967  CG  PRO A 118      13.071  42.993 100.770  1.00 33.86           C  
ATOM    968  CD  PRO A 118      14.215  42.055 101.086  1.00 41.14           C  
ATOM    969  N   ASP A 119      11.225  40.155 100.470  1.00 34.17           N  
ATOM    970  CA  ASP A 119      10.122  39.489  99.786  1.00 30.76           C  
ATOM    971  C   ASP A 119      10.291  37.980  99.660  1.00 36.00           C  
ATOM    972  O   ASP A 119       9.660  37.345  98.819  1.00 39.00           O  
ATOM    973  CB  ASP A 119       9.910  40.124  98.400  1.00 34.62           C  
ATOM    974  CG  ASP A 119      11.128  39.997  97.500  1.00 39.80           C  
ATOM    975  OD1 ASP A 119      12.244  39.776  98.020  1.00 41.46           O  
ATOM    976  OD2 ASP A 119      10.969  40.134  96.269  1.00 40.19           O  
ATOM    977  N   GLY A 120      11.136  37.407 100.510  1.00 30.92           N  
ATOM    978  CA  GLY A 120      11.355  35.974 100.475  1.00 31.93           C  
ATOM    979  C   GLY A 120      11.853  35.443  99.144  1.00 41.67           C  
ATOM    980  O   GLY A 120      11.472  34.350  98.732  1.00 37.97           O  
ATOM    981  N   SER A 121      12.698  36.217  98.468  1.00 46.40           N  
ATOM    982  CA  SER A 121      13.254  35.804  97.189  1.00 41.16           C  
ATOM    983  C   SER A 121      13.921  34.444  97.359  1.00 39.98           C  
ATOM    984  O   SER A 121      14.655  34.208  98.317  1.00 44.11           O  
ATOM    985  CB  SER A 121      14.273  36.832  96.693  1.00 46.36           C  
ATOM    986  OG  SER A 121      15.115  36.271  95.701  1.00 53.87           O  
ATOM    987  N   ILE A 122      13.662  33.552  96.416  1.00 42.18           N  
ATOM    988  CA  ILE A 122      14.208  32.211  96.476  1.00 39.09           C  
ATOM    989  C   ILE A 122      15.735  32.136  96.459  1.00 37.51           C  
ATOM    990  O   ILE A 122      16.318  31.225  97.047  1.00 40.44           O  
ATOM    991  CB  ILE A 122      13.623  31.342  95.342  1.00 45.73           C  
ATOM    992  CG1 ILE A 122      13.509  29.913  95.838  1.00 39.12           C  
ATOM    993  CG2 ILE A 122      14.478  31.429  94.087  1.00 40.31           C  
ATOM    994  CD1 ILE A 122      12.709  29.818  97.113  1.00 43.56           C  
ATOM    995  N   THR A 123      16.385  33.090  95.804  1.00 34.71           N  
ATOM    996  CA  THR A 123      17.843  33.087  95.746  1.00 31.81           C  
ATOM    997  C   THR A 123      18.529  33.777  96.933  1.00 33.09           C  
ATOM    998  O   THR A 123      19.721  34.073  96.879  1.00 38.13           O  
ATOM    999  CB  THR A 123      18.352  33.695  94.408  1.00 36.18           C  
ATOM   1000  OG1 THR A 123      17.614  34.883  94.087  1.00 29.60           O  
ATOM   1001  CG2 THR A 123      18.191  32.678  93.276  1.00 35.31           C  
ATOM   1002  N   GLY A 124      17.769  34.029  98.000  1.00 36.18           N  
ATOM   1003  CA  GLY A 124      18.335  34.629  99.202  1.00 29.96           C  
ATOM   1004  C   GLY A 124      18.415  36.143  99.312  1.00 32.15           C  
ATOM   1005  O   GLY A 124      17.877  36.863  98.471  1.00 29.71           O  
ATOM   1006  N   PRO A 125      19.082  36.656 100.362  1.00 27.75           N  
ATOM   1007  CA  PRO A 125      19.235  38.100 100.585  1.00 36.18           C  
ATOM   1008  C   PRO A 125      19.798  38.755  99.334  1.00 37.97           C  
ATOM   1009  O   PRO A 125      20.721  38.229  98.714  1.00 39.93           O  
ATOM   1010  CB  PRO A 125      20.209  38.168 101.755  1.00 33.69           C  
ATOM   1011  CG  PRO A 125      19.887  36.914 102.524  1.00 29.85           C  
ATOM   1012  CD  PRO A 125      19.747  35.887 101.430  1.00 27.42           C  
ATOM   1013  N   TRP A 126      19.242  39.905  98.974  1.00 41.68           N  
ATOM   1014  CA  TRP A 126      19.657  40.624  97.774  1.00 34.98           C  
ATOM   1015  C   TRP A 126      19.715  42.132  97.992  1.00 32.71           C  
ATOM   1016  O   TRP A 126      19.663  42.622  99.118  1.00 33.30           O  
ATOM   1017  CB  TRP A 126      18.669  40.338  96.638  1.00 29.43           C  
ATOM   1018  CG  TRP A 126      17.247  40.618  97.027  1.00 31.35           C  
ATOM   1019  CD1 TRP A 126      16.413  39.799  97.739  1.00 36.53           C  
ATOM   1020  CD2 TRP A 126      16.502  41.815  96.767  1.00 37.76           C  
ATOM   1021  NE1 TRP A 126      15.196  40.411  97.936  1.00 34.71           N  
ATOM   1022  CE2 TRP A 126      15.224  41.650  97.352  1.00 39.25           C  
ATOM   1023  CE3 TRP A 126      16.789  43.012  96.099  1.00 31.84           C  
ATOM   1024  CZ2 TRP A 126      14.237  42.638  97.287  1.00 34.59           C  
ATOM   1025  CZ3 TRP A 126      15.807  43.994  96.035  1.00 30.33           C  
ATOM   1026  CH2 TRP A 126      14.545  43.800  96.625  1.00 31.35           C  
ATOM   1027  N   CYS A 127      19.820  42.864  96.892  1.00 31.68           N  
ATOM   1028  CA  CYS A 127      19.851  44.311  96.956  1.00 34.04           C  
ATOM   1029  C   CYS A 127      19.764  44.876  95.554  1.00 33.70           C  
ATOM   1030  O   CYS A 127      20.156  44.216  94.595  1.00 42.42           O  
ATOM   1031  CB  CYS A 127      21.149  44.783  97.616  1.00 41.68           C  
ATOM   1032  SG  CYS A 127      22.609  44.751  96.529  1.00 35.67           S  
ATOM   1033  N   TYR A 128      19.217  46.083  95.428  1.00 44.81           N  
ATOM   1034  CA  TYR A 128      19.157  46.739  94.128  1.00 33.65           C  
ATOM   1035  C   TYR A 128      20.624  47.089  93.869  1.00 34.96           C  
ATOM   1036  O   TYR A 128      21.316  47.515  94.795  1.00 34.21           O  
ATOM   1037  CB  TYR A 128      18.292  48.006  94.194  1.00 33.56           C  
ATOM   1038  CG  TYR A 128      16.814  47.720  94.374  1.00 33.41           C  
ATOM   1039  CD1 TYR A 128      16.203  47.840  95.621  1.00 33.83           C  
ATOM   1040  CD2 TYR A 128      16.032  47.301  93.298  1.00 32.09           C  
ATOM   1041  CE1 TYR A 128      14.851  47.553  95.795  1.00 37.12           C  
ATOM   1042  CE2 TYR A 128      14.677  47.007  93.461  1.00 33.94           C  
ATOM   1043  CZ  TYR A 128      14.092  47.136  94.712  1.00 44.02           C  
ATOM   1044  OH  TYR A 128      12.752  46.854  94.877  1.00 42.97           O  
ATOM   1045  N   THR A 129      21.108  46.896  92.641  1.00 29.37           N  
ATOM   1046  CA  THR A 129      22.518  47.167  92.349  1.00 29.71           C  
ATOM   1047  C   THR A 129      22.768  48.530  91.731  1.00 36.27           C  
ATOM   1048  O   THR A 129      21.889  49.101  91.090  1.00 39.17           O  
ATOM   1049  CB  THR A 129      23.141  46.096  91.399  1.00 35.39           C  
ATOM   1050  OG1 THR A 129      23.010  46.519  90.034  1.00 27.10           O  
ATOM   1051  CG2 THR A 129      22.442  44.757  91.570  1.00 26.12           C  
ATOM   1052  N   THR A 130      23.986  49.035  91.928  1.00 42.67           N  
ATOM   1053  CA  THR A 130      24.388  50.328  91.395  1.00 42.60           C  
ATOM   1054  C   THR A 130      24.684  50.273  89.901  1.00 46.95           C  
ATOM   1055  O   THR A 130      25.065  51.277  89.299  1.00 52.76           O  
ATOM   1056  CB  THR A 130      25.620  50.880  92.127  1.00 38.43           C  
ATOM   1057  OG1 THR A 130      26.636  49.871  92.177  1.00 46.52           O  
ATOM   1058  CG2 THR A 130      25.240  51.331  93.544  1.00 35.70           C  
ATOM   1059  N   SER A 131      24.527  49.096  89.306  1.00 39.98           N  
ATOM   1060  CA  SER A 131      24.731  48.955  87.873  1.00 37.49           C  
ATOM   1061  C   SER A 131      23.404  49.308  87.214  1.00 39.54           C  
ATOM   1062  O   SER A 131      22.358  48.775  87.582  1.00 42.23           O  
ATOM   1063  CB  SER A 131      25.107  47.525  87.500  1.00 41.33           C  
ATOM   1064  OG  SER A 131      24.866  47.302  86.120  1.00 35.41           O  
ATOM   1065  N   PRO A 132      23.431  50.218  86.235  1.00 41.49           N  
ATOM   1066  CA  PRO A 132      22.223  50.644  85.525  1.00 46.55           C  
ATOM   1067  C   PRO A 132      21.522  49.518  84.770  1.00 52.10           C  
ATOM   1068  O   PRO A 132      20.306  49.556  84.579  1.00 49.48           O  
ATOM   1069  CB  PRO A 132      22.747  51.722  84.576  1.00 45.58           C  
ATOM   1070  CG  PRO A 132      23.938  52.267  85.306  1.00 42.70           C  
ATOM   1071  CD  PRO A 132      24.592  51.028  85.828  1.00 35.99           C  
ATOM   1072  N   THR A 133      22.291  48.519  84.346  1.00 46.15           N  
ATOM   1073  CA  THR A 133      21.738  47.405  83.582  1.00 53.15           C  
ATOM   1074  C   THR A 133      21.170  46.256  84.413  1.00 55.33           C  
ATOM   1075  O   THR A 133      20.394  45.451  83.901  1.00 68.00           O  
ATOM   1076  CB  THR A 133      22.791  46.828  82.612  1.00 50.30           C  
ATOM   1077  OG1 THR A 133      23.945  46.409  83.351  1.00 58.58           O  
ATOM   1078  CG2 THR A 133      23.208  47.877  81.597  1.00 53.99           C  
ATOM   1079  N   LEU A 134      21.546  46.170  85.684  1.00 49.00           N  
ATOM   1080  CA  LEU A 134      21.047  45.095  86.542  1.00 44.50           C  
ATOM   1081  C   LEU A 134      20.268  45.667  87.725  1.00 38.12           C  
ATOM   1082  O   LEU A 134      20.858  46.187  88.670  1.00 43.61           O  
ATOM   1083  CB  LEU A 134      22.215  44.255  87.066  1.00 36.29           C  
ATOM   1084  CG  LEU A 134      22.022  42.748  87.241  1.00 38.12           C  
ATOM   1085  CD1 LEU A 134      22.916  42.294  88.372  1.00 33.31           C  
ATOM   1086  CD2 LEU A 134      20.577  42.397  87.533  1.00 45.68           C  
ATOM   1087  N   ARG A 135      18.946  45.563  87.671  1.00 35.45           N  
ATOM   1088  CA  ARG A 135      18.083  46.075  88.734  1.00 42.72           C  
ATOM   1089  C   ARG A 135      18.398  45.518  90.133  1.00 41.12           C  
ATOM   1090  O   ARG A 135      18.609  46.280  91.077  1.00 38.42           O  
ATOM   1091  CB  ARG A 135      16.617  45.801  88.377  1.00 35.40           C  
ATOM   1092  CG  ARG A 135      15.610  46.471  89.301  1.00 43.64           C  
ATOM   1093  CD  ARG A 135      14.190  46.282  88.781  1.00 39.25           C  
ATOM   1094  NE  ARG A 135      13.186  46.714  89.749  1.00 40.10           N  
ATOM   1095  CZ  ARG A 135      12.944  47.980  90.077  1.00 32.07           C  
ATOM   1096  NH1 ARG A 135      13.632  48.964  89.513  1.00 46.88           N  
ATOM   1097  NH2 ARG A 135      12.016  48.264  90.978  1.00 39.64           N  
ATOM   1098  N   ARG A 136      18.432  44.195  90.271  1.00 35.81           N  
ATOM   1099  CA  ARG A 136      18.722  43.580  91.562  1.00 37.57           C  
ATOM   1100  C   ARG A 136      19.440  42.245  91.411  1.00 36.27           C  
ATOM   1101  O   ARG A 136      19.317  41.578  90.388  1.00 47.45           O  
ATOM   1102  CB  ARG A 136      17.425  43.366  92.349  1.00 38.22           C  
ATOM   1103  CG  ARG A 136      16.407  42.507  91.621  1.00 36.86           C  
ATOM   1104  CD  ARG A 136      15.113  42.345  92.419  1.00 35.27           C  
ATOM   1105  NE  ARG A 136      15.184  41.259  93.387  1.00 39.23           N  
ATOM   1106  CZ  ARG A 136      14.187  40.911  94.195  1.00 48.75           C  
ATOM   1107  NH1 ARG A 136      13.034  41.570  94.155  1.00 45.53           N  
ATOM   1108  NH2 ARG A 136      14.342  39.895  95.035  1.00 36.85           N  
ATOM   1109  N   GLU A 137      20.192  41.865  92.439  1.00 37.12           N  
ATOM   1110  CA  GLU A 137      20.922  40.604  92.432  1.00 34.99           C  
ATOM   1111  C   GLU A 137      21.175  40.121  93.855  1.00 37.81           C  
ATOM   1112  O   GLU A 137      21.375  40.928  94.765  1.00 40.84           O  
ATOM   1113  CB  GLU A 137      22.258  40.763  91.705  1.00 43.20           C  
ATOM   1114  CG  GLU A 137      23.061  39.481  91.639  1.00 46.47           C  
ATOM   1115  CD  GLU A 137      24.371  39.647  90.905  1.00 44.40           C  
ATOM   1116  OE1 GLU A 137      25.199  40.464  91.349  1.00 52.27           O  
ATOM   1117  OE2 GLU A 137      24.574  38.958  89.884  1.00 56.69           O  
ATOM   1118  N   GLU A 138      21.167  38.802  94.040  1.00 42.27           N  
ATOM   1119  CA  GLU A 138      21.396  38.214  95.351  1.00 32.65           C  
ATOM   1120  C   GLU A 138      22.836  38.417  95.804  1.00 37.62           C  
ATOM   1121  O   GLU A 138      23.732  38.659  94.990  1.00 32.95           O  
ATOM   1122  CB  GLU A 138      21.042  36.718  95.351  1.00 37.44           C  
ATOM   1123  CG  GLU A 138      21.905  35.809  94.484  1.00 40.77           C  
ATOM   1124  CD  GLU A 138      21.747  36.055  92.993  1.00 52.04           C  
ATOM   1125  OE1 GLU A 138      20.598  36.195  92.515  1.00 47.00           O  
ATOM   1126  OE2 GLU A 138      22.781  36.091  92.295  1.00 65.18           O  
ATOM   1127  N   CYS A 139      23.045  38.328  97.113  1.00 33.88           N  
ATOM   1128  CA  CYS A 139      24.363  38.515  97.700  1.00 35.56           C  
ATOM   1129  C   CYS A 139      24.851  37.233  98.343  1.00 36.43           C  
ATOM   1130  O   CYS A 139      24.079  36.306  98.563  1.00 36.75           O  
ATOM   1131  CB  CYS A 139      24.314  39.589  98.782  1.00 31.16           C  
ATOM   1132  SG  CYS A 139      23.344  41.080  98.390  1.00 35.67           S  
ATOM   1133  N   SER A 140      26.136  37.205  98.672  1.00 36.10           N  
ATOM   1134  CA  SER A 140      26.735  36.045  99.308  1.00 44.32           C  
ATOM   1135  C   SER A 140      26.852  36.299 100.806  1.00 42.90           C  
ATOM   1136  O   SER A 140      27.703  37.058 101.269  1.00 43.47           O  
ATOM   1137  CB  SER A 140      28.112  35.753  98.702  1.00 46.74           C  
ATOM   1138  OG  SER A 140      28.719  34.645  99.341  1.00 63.24           O  
ATOM   1139  N   VAL A 141      25.976  35.645 101.553  1.00 51.17           N  
ATOM   1140  CA  VAL A 141      25.916  35.766 103.000  1.00 45.71           C  
ATOM   1141  C   VAL A 141      26.062  34.383 103.634  1.00 41.34           C  
ATOM   1142  O   VAL A 141      25.602  33.388 103.071  1.00 55.84           O  
ATOM   1143  CB  VAL A 141      24.554  36.379 103.413  1.00 51.19           C  
ATOM   1144  CG1 VAL A 141      24.261  36.088 104.857  1.00 41.12           C  
ATOM   1145  CG2 VAL A 141      24.561  37.878 103.155  1.00 44.24           C  
ATOM   1146  N   PRO A 142      26.701  34.302 104.812  1.00 37.56           N  
ATOM   1147  CA  PRO A 142      26.882  33.012 105.491  1.00 40.83           C  
ATOM   1148  C   PRO A 142      25.565  32.376 105.944  1.00 39.93           C  
ATOM   1149  O   PRO A 142      24.662  33.058 106.420  1.00 47.33           O  
ATOM   1150  CB  PRO A 142      27.799  33.362 106.663  1.00 39.17           C  
ATOM   1151  CG  PRO A 142      27.445  34.789 106.959  1.00 36.91           C  
ATOM   1152  CD  PRO A 142      27.329  35.394 105.579  1.00 37.53           C  
ATOM   1153  N   VAL A 143      25.458  31.064 105.774  1.00 39.83           N  
ATOM   1154  CA  VAL A 143      24.256  30.338 106.163  1.00 46.09           C  
ATOM   1155  C   VAL A 143      24.370  29.925 107.625  1.00 45.98           C  
ATOM   1156  O   VAL A 143      25.440  29.517 108.079  1.00 48.49           O  
ATOM   1157  CB  VAL A 143      24.067  29.074 105.298  1.00 49.87           C  
ATOM   1158  CG1 VAL A 143      22.731  28.421 105.606  1.00 55.81           C  
ATOM   1159  CG2 VAL A 143      24.150  29.438 103.831  1.00 41.20           C  
ATOM   1160  N   CYS A 144      23.265  30.035 108.357  1.00 48.00           N  
ATOM   1161  CA  CYS A 144      23.242  29.688 109.773  1.00 42.70           C  
ATOM   1162  C   CYS A 144      23.470  28.201 110.021  1.00 48.76           C  
ATOM   1163  O   CYS A 144      22.835  27.352 109.392  1.00 45.40           O  
ATOM   1164  CB  CYS A 144      21.903  30.089 110.398  1.00 43.44           C  
ATOM   1165  SG  CYS A 144      21.476  31.863 110.359  1.00 38.20           S  
ATOM   1166  N   GLY A 145      24.376  27.893 110.944  1.00 57.09           N  
ATOM   1167  CA  GLY A 145      24.658  26.507 111.279  1.00 57.38           C  
ATOM   1168  C   GLY A 145      25.584  25.761 110.336  1.00 65.94           C  
ATOM   1169  O   GLY A 145      25.650  24.532 110.373  1.00 65.61           O  
ATOM   1170  N   GLN A 146      26.305  26.490 109.492  1.00 73.61           N  
ATOM   1171  CA  GLN A 146      27.227  25.858 108.555  1.00 82.20           C  
ATOM   1172  C   GLN A 146      28.246  26.873 108.046  1.00 81.30           C  
ATOM   1173  O   GLN A 146      28.049  27.406 106.932  1.00 75.11           O  
ATOM   1174  CB  GLN A 146      26.456  25.249 107.378  1.00 92.68           C  
ATOM   1175  CG  GLN A 146      27.109  24.004 106.761  1.00102.25           C  
ATOM   1176  CD  GLN A 146      28.500  24.263 106.191  1.00107.43           C  
ATOM   1177  OE1 GLN A 146      29.432  24.614 106.920  1.00106.20           O  
ATOM   1178  NE2 GLN A 146      28.644  24.083 104.879  1.00 96.99           N  
ATOM   1179  OXT GLN A 146      29.223  27.135 108.782  1.00 81.57           O  
TER    1180      GLN A 146                                                      
HETATM 1181  C1  NAG B   1      26.950  47.235 110.729  1.00 75.23           C  
HETATM 1182  C2  NAG B   1      28.117  47.682 111.632  1.00 78.72           C  
HETATM 1183  C3  NAG B   1      27.640  48.624 112.729  1.00 85.58           C  
HETATM 1184  C4  NAG B   1      26.797  49.763 112.153  1.00 87.25           C  
HETATM 1185  C5  NAG B   1      25.688  49.162 111.294  1.00 81.91           C  
HETATM 1186  C6  NAG B   1      24.791  50.216 110.657  1.00 78.79           C  
HETATM 1187  C7  NAG B   1      29.586  45.792 111.513  1.00 73.68           C  
HETATM 1188  C8  NAG B   1      29.324  44.285 111.559  1.00 72.92           C  
HETATM 1189  N2  NAG B   1      28.802  46.553 112.257  1.00 77.28           N  
HETATM 1190  O3  NAG B   1      28.767  49.142 113.417  1.00 85.79           O  
HETATM 1191  O4  NAG B   1      26.200  50.471 113.243  1.00 98.43           O  
HETATM 1192  O5  NAG B   1      26.267  48.378 110.240  1.00 79.05           O  
HETATM 1193  O6  NAG B   1      25.566  51.147 109.915  1.00 73.47           O  
HETATM 1194  O7  NAG B   1      30.453  46.261 110.769  1.00 71.63           O  
HETATM 1195  C1  NAG B   2      26.218  51.849 113.202  1.00103.87           C  
HETATM 1196  C2  NAG B   2      25.091  52.375 114.101  1.00105.90           C  
HETATM 1197  C3  NAG B   2      25.202  53.889 114.365  1.00109.24           C  
HETATM 1198  C4  NAG B   2      26.620  54.362 114.675  1.00109.68           C  
HETATM 1199  C5  NAG B   2      27.605  53.743 113.665  1.00106.35           C  
HETATM 1200  C6  NAG B   2      29.069  54.071 113.911  1.00103.55           C  
HETATM 1201  C7  NAG B   2      22.803  51.610 114.152  1.00108.24           C  
HETATM 1202  C8  NAG B   2      21.946  52.577 114.984  1.00108.54           C  
HETATM 1203  N2  NAG B   2      23.816  52.126 113.460  1.00107.65           N  
HETATM 1204  O3  NAG B   2      24.355  54.229 115.462  1.00112.83           O  
HETATM 1205  O4  NAG B   2      26.638  55.789 114.587  1.00111.69           O  
HETATM 1206  O5  NAG B   2      27.497  52.292 113.680  1.00104.46           O  
HETATM 1207  O6  NAG B   2      29.870  53.605 112.823  1.00100.42           O  
HETATM 1208  O7  NAG B   2      22.528  50.399 114.139  1.00106.63           O  
HETATM 1209  C1  NAG A 303       8.138  53.120  98.577  1.00 85.98           C  
HETATM 1210  C2  NAG A 303       8.609  54.572  98.582  1.00 92.22           C  
HETATM 1211  C3  NAG A 303       7.378  55.476  98.431  1.00 92.68           C  
HETATM 1212  C4  NAG A 303       6.621  55.108  97.146  1.00 91.06           C  
HETATM 1213  C5  NAG A 303       6.320  53.596  97.097  1.00 89.74           C  
HETATM 1214  C6  NAG A 303       5.762  53.156  95.756  1.00 89.62           C  
HETATM 1215  C7  NAG A 303      10.523  54.321 100.033  1.00105.95           C  
HETATM 1216  C8  NAG A 303      10.564  53.140 100.995  1.00110.06           C  
HETATM 1217  N2  NAG A 303       9.331  54.872  99.805  1.00 99.77           N  
HETATM 1218  O3  NAG A 303       7.773  56.841  98.385  1.00 94.62           O  
HETATM 1219  O4  NAG A 303       5.403  55.839  97.088  1.00 92.97           O  
HETATM 1220  O5  NAG A 303       7.525  52.826  97.317  1.00 84.53           O  
HETATM 1221  O6  NAG A 303       6.450  52.012  95.266  1.00 91.40           O  
HETATM 1222  O7  NAG A 303      11.565  54.725  99.504  1.00105.63           O  
HETATM 1223 CA    CA A 201      -3.838  43.998 123.492  1.00 33.90          CA  
HETATM 1224 CA    CA A 202      -2.960  39.697 125.417  1.00 44.33          CA  
HETATM 1225 CA    CA A 203       0.517  39.837 127.003  1.00 38.51          CA  
HETATM 1226 CA    CA A 204       0.676  36.233 126.859  1.00 41.60          CA  
HETATM 1227 CA    CA A 205       2.311  33.198 128.616  1.00 42.51          CA  
HETATM 1228 CA    CA A 206       5.962  29.935 130.283  1.00 68.72          CA  
HETATM 1229 CA    CA A 207      14.377  33.117 129.709  1.00 42.84          CA  
HETATM 1230 CL    CL A 250      17.306  39.097  93.527  1.00 48.58          CL  
HETATM 1231 CL    CL A 251      13.609  52.015  87.578  1.00 48.99          CL  
HETATM 1232 CL    CL A 252      19.012  54.280 105.669  1.00 42.72          CL  
HETATM 1233  OT2 LPS A 451       4.204  32.577 130.930  0.67 57.18           O  
HETATM 1234  C   LPS A 451       4.504  31.572 131.622  0.67 66.94           C  
HETATM 1235  OT1 LPS A 451       5.676  31.287 131.997  0.67 65.84           O  
HETATM 1236  C12 LPS A 451       3.297  30.690 132.010  0.67 72.18           C  
HETATM 1237  N   LPS A 451       3.727  29.387 132.606  0.67 67.26           N  
HETATM 1238  C11 LPS A 451       2.219  31.384 132.905  0.67 69.75           C  
HETATM 1239  O12 LPS A 451       2.072  32.826 132.722  0.67 75.55           O  
HETATM 1240  P   LPS A 451       2.650  34.071 133.621  0.67 52.53           P  
HETATM 1241  O13 LPS A 451       3.781  33.604 134.462  0.67 75.70           O  
HETATM 1242  O14 LPS A 451       2.897  35.229 132.745  0.67 69.69           O  
HETATM 1243  O11 LPS A 451       1.380  34.424 134.544  0.67 65.36           O  
HETATM 1244  C1  LPS A 451       0.893  33.903 135.781  0.67 54.63           C  
HETATM 1245  C2  LPS A 451      -0.566  34.345 135.983  0.67 58.48           C  
HETATM 1246  O21 LPS A 451      -0.628  35.600 136.651  0.67 74.58           O  
HETATM 1247  C3  LPS A 451      -1.445  33.338 136.723  0.67 65.58           C  
HETATM 1248  O31 LPS A 451      -1.890  32.339 135.803  0.67 82.45           O  
HETATM 1249  C31 LPS A 451      -3.120  31.840 135.987  0.67 93.26           C  
HETATM 1250  O32 LPS A 451      -4.118  32.504 136.204  0.67 92.13           O  
HETATM 1251  C32 LPS A 451      -3.071  30.274 135.816  0.67 89.19           C  
HETATM 1252  C33 LPS A 451      -2.606  29.354 136.981  0.67 79.64           C  
HETATM 1253  C34 LPS A 451      -3.089  27.885 136.799  0.67 70.28           C  
HETATM 1254  C35 LPS A 451      -2.714  26.874 137.903  0.67 68.45           C  
HETATM 1255  C36 LPS A 451      -3.491  26.999 139.227  0.67 69.96           C  
HETATM 1256  C37 LPS A 451      -4.601  25.956 139.411  0.67 66.57           C  
HETATM 1257  C38 LPS A 451      -5.838  26.509 140.147  0.67 69.97           C  
HETATM 1258  C39 LPS A 451      -7.205  26.369 139.419  0.67 67.93           C  
HETATM 1259  C40 LPS A 451      -7.465  27.221 138.141  0.67 64.03           C  
HETATM 1260  C41 LPS A 451      -7.683  28.743 138.316  0.67 55.36           C  
HETATM 1261  C42 LPS A 451      -6.607  29.610 137.659  0.67 40.02           C  
HETATM 1262  C43 LPS A 451      -6.515  31.050 138.123  0.67 35.65           C  
HETATM 1263  C44 LPS A 451      -5.507  31.272 139.194  0.67 39.71           C  
HETATM 1264  C45 LPS A 451      -5.173  32.732 139.413  0.67 51.76           C  
HETATM 1265  O   HOH A 501       8.338  43.695 106.544  1.00 23.65           O  
HETATM 1266  O   HOH A 502      22.422  31.929 123.181  1.00 26.40           O  
HETATM 1267  O   HOH A 503      23.016  55.209  93.628  1.00 27.69           O  
HETATM 1268  O   HOH A 504      -4.411  39.493 123.415  1.00 27.42           O  
HETATM 1269  O   HOH A 505      -0.519  36.283 115.070  1.00 27.41           O  
HETATM 1270  O   HOH A 506      14.683  41.936 105.486  1.00 32.41           O  
HETATM 1271  O   HOH A 507      -3.851  41.244 126.414  1.00 33.76           O  
HETATM 1272  O   HOH A 508      23.352  35.573 113.882  1.00 35.82           O  
HETATM 1273  O   HOH A 509      16.252  42.549 134.129  1.00 33.34           O  
HETATM 1274  O   HOH A 510      24.367  34.272  96.604  1.00 37.21           O  
HETATM 1275  O   HOH A 511       1.709  37.255 130.505  1.00 33.24           O  
HETATM 1276  O   HOH A 512      13.881  52.973 102.169  1.00 38.13           O  
HETATM 1277  O   HOH A 513      17.728  36.876  95.628  1.00 36.55           O  
HETATM 1278  O   HOH A 514      -0.065  41.707 127.864  1.00 33.69           O  
HETATM 1279  O   HOH A 515      30.132  43.757 101.999  1.00 34.25           O  
HETATM 1280  O   HOH A 516      -5.608  36.713 131.675  1.00 27.25           O  
HETATM 1281  O   HOH A 517      14.712  33.644 107.530  1.00 31.08           O  
HETATM 1282  O   HOH A 518      14.243  42.741  88.626  1.00 35.83           O  
HETATM 1283  O   HOH A 519       1.299  40.026 129.314  1.00 38.19           O  
HETATM 1284  O   HOH A 520      19.771  27.493 112.052  1.00 37.82           O  
HETATM 1285  O   HOH A 521      23.295  53.942  96.195  1.00 37.91           O  
HETATM 1286  O   HOH A 522       2.616  40.838 125.893  1.00 35.05           O  
HETATM 1287  O   HOH A 523       9.588  42.982 127.065  1.00 35.97           O  
HETATM 1288  O   HOH A 524       6.867  42.533 110.538  1.00 36.01           O  
HETATM 1289  O   HOH A 525      27.923  39.057  98.333  1.00 35.50           O  
HETATM 1290  O   HOH A 526      13.636  32.913 104.996  1.00 37.93           O  
HETATM 1291  O   HOH A 527       1.735  30.838 128.557  1.00 34.53           O  
HETATM 1292  O   HOH A 528      14.205  44.262 111.534  1.00 37.53           O  
HETATM 1293  O   HOH A 529      12.868  47.709 110.334  1.00 37.46           O  
HETATM 1294  O   HOH A 530      11.549  34.578 132.215  1.00 39.80           O  
HETATM 1295  O   HOH A 531      14.839  29.418 126.237  1.00 42.23           O  
HETATM 1296  O   HOH A 532      19.092  47.978  97.986  1.00 41.76           O  
HETATM 1297  O   HOH A 533       6.524  53.328 116.230  1.00 43.73           O  
HETATM 1298  O   HOH A 534      25.542  52.613  96.947  1.00 46.36           O  
HETATM 1299  O   HOH A 535       3.007  31.545 137.399  1.00 50.90           O  
HETATM 1300  O   HOH A 536      12.849  29.847 107.337  1.00 40.92           O  
HETATM 1301  O   HOH A 537      16.960  32.517 128.934  1.00 42.30           O  
HETATM 1302  O   HOH A 538       4.289  45.701 136.718  1.00 45.90           O  
HETATM 1303  O   HOH A 539      11.146  37.275 131.831  1.00 40.98           O  
HETATM 1304  O   HOH A 540      22.923  45.779 109.282  1.00 43.90           O  
HETATM 1305  O   HOH A 541       4.128  48.350 135.917  1.00 44.50           O  
HETATM 1306  O   HOH A 542      26.790  38.800 107.331  1.00 45.75           O  
HETATM 1307  O   HOH A 543      -1.160  33.728 121.256  1.00 48.36           O  
HETATM 1308  O   HOH A 544      26.595  29.924 111.470  1.00 46.12           O  
HETATM 1309  O   HOH A 545      -1.404  37.555 138.295  1.00 45.91           O  
HETATM 1310  O   HOH A 546      17.607  51.598  85.363  1.00 47.69           O  
HETATM 1311  O   HOH A 547      -0.122  45.921 115.630  1.00 53.47           O  
HETATM 1312  O   HOH A 548      20.394  29.897 113.867  1.00 49.05           O  
HETATM 1313  O   HOH A 549      19.087  27.881 106.075  1.00 46.71           O  
HETATM 1314  O   HOH A 550       3.440  27.858 130.442  1.00 50.88           O  
HETATM 1315  O   HOH A 551      12.951  49.917 108.353  1.00 57.02           O  
HETATM 1316  O   HOH A 552      19.078  53.587 102.379  1.00 43.83           O  
HETATM 1317  O   HOH A 553       4.668  55.246  93.643  1.00 54.49           O  
HETATM 1318  O   HOH A 554      27.393  41.394 109.718  1.00 58.70           O  
HETATM 1319  O   HOH A 555       4.310  48.661 121.492  1.00 60.41           O  
HETATM 1320  O   HOH A 556       7.584  43.347  95.121  1.00 55.58           O  
HETATM 1321  O   HOH A 557       7.383  29.481 132.560  1.00 57.85           O  
HETATM 1322  O   HOH A 558      16.231  44.967 134.705  1.00 68.96           O  
HETATM 1323  O   HOH A 559      12.618  49.949 113.373  1.00 68.51           O  
HETATM 1324  O   HOH A 560      17.739  37.904  91.123  1.00 52.39           O  
CONECT    4 1227                                                                
CONECT   12 1226                                                                
CONECT   40   46                                                                
CONECT   46   40   47                                                           
CONECT   47   46   48   50                                                      
CONECT   48   47   49   58                                                      
CONECT   49   48                                                                
CONECT   50   47   51                                                           
CONECT   51   50   52   53                                                      
CONECT   52   51   54   55                                                      
CONECT   53   51   56   57                                                      
CONECT   54   52 1226 1227                                                      
CONECT   55   52 1227                                                           
CONECT   56   53                                                                
CONECT   57   53                                                                
CONECT   58   48   59                                                           
CONECT   59   58   60   62                                                      
CONECT   60   59   61   70                                                      
CONECT   61   60                                                                
CONECT   62   59   63                                                           
CONECT   63   62   64   65                                                      
CONECT   64   63   66   67                                                      
CONECT   65   63   68   69                                                      
CONECT   66   64                                                                
CONECT   67   64 1224                                                           
CONECT   68   65 1224 1225                                                      
CONECT   69   65 1225 1226                                                      
CONECT   70   60                                                                
CONECT  111  117                                                                
CONECT  117  111  118                                                           
CONECT  118  117  119  121                                                      
CONECT  119  118  120  129                                                      
CONECT  120  119                                                                
CONECT  121  118  122                                                           
CONECT  122  121  123  124                                                      
CONECT  123  122  125  126                                                      
CONECT  124  122  127  128                                                      
CONECT  125  123                                                                
CONECT  126  123 1229                                                           
CONECT  127  124 1229                                                           
CONECT  128  124                                                                
CONECT  129  119                                                                
CONECT  131  140                                                                
CONECT  140  131  141                                                           
CONECT  141  140  142  144                                                      
CONECT  142  141  143  152                                                      
CONECT  143  142                                                                
CONECT  144  141  145                                                           
CONECT  145  144  146  147                                                      
CONECT  146  145  148  149                                                      
CONECT  147  145  150  151                                                      
CONECT  148  146 1225 1226                                                      
CONECT  149  146                                                                
CONECT  150  147 1226 1227                                                      
CONECT  151  147 1227                                                           
CONECT  152  142                                                                
CONECT  157  202                                                                
CONECT  160  166                                                                
CONECT  166  160  167                                                           
CONECT  167  166  168  170                                                      
CONECT  168  167  169  178                                                      
CONECT  169  168                                                                
CONECT  170  167  171                                                           
CONECT  171  170  172  173                                                      
CONECT  172  171  174  175                                                      
CONECT  173  171  176  177                                                      
CONECT  174  172 1229                                                           
CONECT  175  172                                                                
CONECT  176  173 1229                                                           
CONECT  177  173                                                                
CONECT  178  168  179                                                           
CONECT  179  178  180  182                                                      
CONECT  180  179  181  190                                                      
CONECT  181  180                                                                
CONECT  182  179  183                                                           
CONECT  183  182  184  185                                                      
CONECT  184  183  186  187                                                      
CONECT  185  183  188  189                                                      
CONECT  186  184 1227                                                           
CONECT  187  184 1228                                                           
CONECT  188  185                                                                
CONECT  189  185 1228                                                           
CONECT  190  180                                                                
CONECT  202  157                                                                
CONECT  211  220                                                                
CONECT  220  211  221                                                           
CONECT  221  220  222  224                                                      
CONECT  222  221  223  232                                                      
CONECT  223  222                                                                
CONECT  224  221  225                                                           
CONECT  225  224  226  227                                                      
CONECT  226  225  228  229                                                      
CONECT  227  225  230  231                                                      
CONECT  228  226                                                                
CONECT  229  226 1223                                                           
CONECT  230  227 1223                                                           
CONECT  231  227                                                                
CONECT  232  222  233                                                           
CONECT  233  232  234  236                                                      
CONECT  234  233  235  244                                                      
CONECT  235  234                                                                
CONECT  236  233  237                                                           
CONECT  237  236  238  239                                                      
CONECT  238  237  240  241                                                      
CONECT  239  237  242  243                                                      
CONECT  240  238 1225 1226                                                      
CONECT  241  238 1224                                                           
CONECT  242  239                                                                
CONECT  243  239 1226                                                           
CONECT  244  234                                                                
CONECT  251  260                                                                
CONECT  260  251  261                                                           
CONECT  261  260  262  264                                                      
CONECT  262  261  263  272                                                      
CONECT  263  262                                                                
CONECT  264  261  265                                                           
CONECT  265  264  266  267                                                      
CONECT  266  265  268  269                                                      
CONECT  267  265  270  271                                                      
CONECT  268  266 1223                                                           
CONECT  269  266                                                                
CONECT  270  267 1224 1225                                                      
CONECT  271  267 1223 1224                                                      
CONECT  272  262                                                                
CONECT  279  285                                                                
CONECT  285  279  286                                                           
CONECT  286  285  287  289                                                      
CONECT  287  286  288  297                                                      
CONECT  288  287                                                                
CONECT  289  286  290                                                           
CONECT  290  289  291  292                                                      
CONECT  291  290  293  294                                                      
CONECT  292  290  295  296                                                      
CONECT  293  291                                                                
CONECT  294  291                                                                
CONECT  295  292                                                                
CONECT  296  292                                                                
CONECT  297  287                                                                
CONECT  410  520                                                                
CONECT  520  410                                                                
CONECT  555 1165                                                                
CONECT  635 1181                                                                
CONECT  706 1032                                                                
CONECT  835 1209                                                                
CONECT  942 1132                                                                
CONECT 1032  706                                                                
CONECT 1132  942                                                                
CONECT 1165  555                                                                
CONECT 1181  635 1182 1192                                                      
CONECT 1182 1181 1183 1189                                                      
CONECT 1183 1182 1184 1190                                                      
CONECT 1184 1183 1185 1191                                                      
CONECT 1185 1184 1186 1192                                                      
CONECT 1186 1185 1193                                                           
CONECT 1187 1188 1189 1194                                                      
CONECT 1188 1187                                                                
CONECT 1189 1182 1187                                                           
CONECT 1190 1183                                                                
CONECT 1191 1184 1195                                                           
CONECT 1192 1181 1185                                                           
CONECT 1193 1186                                                                
CONECT 1194 1187                                                                
CONECT 1195 1191 1196 1206                                                      
CONECT 1196 1195 1197 1203                                                      
CONECT 1197 1196 1198 1204                                                      
CONECT 1198 1197 1199 1205                                                      
CONECT 1199 1198 1200 1206                                                      
CONECT 1200 1199 1207                                                           
CONECT 1201 1202 1203 1208                                                      
CONECT 1202 1201                                                                
CONECT 1203 1196 1201                                                           
CONECT 1204 1197                                                                
CONECT 1205 1198                                                                
CONECT 1206 1195 1199                                                           
CONECT 1207 1200                                                                
CONECT 1208 1201                                                                
CONECT 1209  835 1210 1220                                                      
CONECT 1210 1209 1211 1217                                                      
CONECT 1211 1210 1212 1218                                                      
CONECT 1212 1211 1213 1219                                                      
CONECT 1213 1212 1214 1220                                                      
CONECT 1214 1213 1221                                                           
CONECT 1215 1216 1217 1222                                                      
CONECT 1216 1215                                                                
CONECT 1217 1210 1215                                                           
CONECT 1218 1211                                                                
CONECT 1219 1212                                                                
CONECT 1220 1209 1213                                                           
CONECT 1221 1214                                                                
CONECT 1222 1215                                                                
CONECT 1223  229  230  268  271                                                 
CONECT 1224   67   68  241  270                                                 
CONECT 1224  271 1268 1271                                                      
CONECT 1225   68   69  148  240                                                 
CONECT 1225  270 1278 1283 1286                                                 
CONECT 1226   12   54   69  148                                                 
CONECT 1226  150  240  243                                                      
CONECT 1227    4   54   55  150                                                 
CONECT 1227  151  186 1291                                                      
CONECT 1228  187  189 1235 1321                                                 
CONECT 1229  126  127  174  176                                                 
CONECT 1229 1301                                                                
CONECT 1233 1234                                                                
CONECT 1234 1233 1235 1236                                                      
CONECT 1235 1228 1234                                                           
CONECT 1236 1234 1237 1238                                                      
CONECT 1237 1236                                                                
CONECT 1238 1236 1239                                                           
CONECT 1239 1238 1240                                                           
CONECT 1240 1239 1241 1242 1243                                                 
CONECT 1241 1240                                                                
CONECT 1242 1240                                                                
CONECT 1243 1240 1244                                                           
CONECT 1244 1243 1245                                                           
CONECT 1245 1244 1246 1247                                                      
CONECT 1246 1245                                                                
CONECT 1247 1245 1248                                                           
CONECT 1248 1247 1249                                                           
CONECT 1249 1248 1250 1251                                                      
CONECT 1250 1249                                                                
CONECT 1251 1249 1252                                                           
CONECT 1252 1251 1253                                                           
CONECT 1253 1252 1254                                                           
CONECT 1254 1253 1255                                                           
CONECT 1255 1254 1256                                                           
CONECT 1256 1255 1257                                                           
CONECT 1257 1256 1258                                                           
CONECT 1258 1257 1259                                                           
CONECT 1259 1258 1260                                                           
CONECT 1260 1259 1261                                                           
CONECT 1261 1260 1262                                                           
CONECT 1262 1261 1263                                                           
CONECT 1263 1262 1264                                                           
CONECT 1264 1263                                                                
CONECT 1268 1224                                                                
CONECT 1271 1224                                                                
CONECT 1278 1225                                                                
CONECT 1283 1225                                                                
CONECT 1286 1225                                                                
CONECT 1291 1227                                                                
CONECT 1301 1229                                                                
CONECT 1321 1228                                                                
MASTER      364    0   24    6    2    0    0    6 1319    1  242   12          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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.