CNRS Nantes University US2B US2B
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***  galectin1  ***

elNémo ID: 2403301330071557285

Job options:

ID        	=	 2403301330071557285
JOBID     	=	 galectin1
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 galectin1

HEADER    SUGAR BINDING PROTEIN                   20-AUG-04   1W6O              
TITLE     X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 COMPLEXED WITH LACTOSE
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GALECTIN-1;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BETA-GALACTOSIDE-BINDING LECTIN L-14-I, HPL, LACTOSE-BINDING
COMPND   5 LECTIN 1, S-LAC LECTIN 1, GALAPTIN, HBL;                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: GALECTIN-1;                                                
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: BETA-GALACTOSIDE-BINDING LECTIN L-14-I, HPL, LACTOSE-BINDING
COMPND  12 LECTIN 1, S-LAC LECTIN 1, GALAPTIN, HBL;                             
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: SCS1;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PUC540;                                    
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PH14GAL;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: SCS1;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR: PUC540;                                    
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PH14GAL                                   
KEYWDS    LECTIN, CARBOHYDRATE-BINDING PROTEINS, GALACTOSIDES, GALECTIN, SUGAR  
KEYWDS   2 BINDING PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.I.F.LOPEZ-LUCENDO,H.J.GABIUS,A.ROMERO                               
REVDAT   7   13-DEC-23 1W6O    1       HETSYN                                   
REVDAT   6   29-JUL-20 1W6O    1       COMPND REMARK HET    HETNAM              
REVDAT   6 2                   1       FORMUL LINK   SITE   ATOM                
REVDAT   5   24-JUL-19 1W6O    1       REMARK                                   
REVDAT   4   08-MAY-19 1W6O    1       REMARK LINK                              
REVDAT   3   06-OCT-09 1W6O    1       HEADER KEYWDS REMARK HETNAM              
REVDAT   2   24-FEB-09 1W6O    1       VERSN                                    
REVDAT   1   20-OCT-04 1W6O    0                                                
JRNL        AUTH   M.I.F.LOPEZ-LUCENDO,D.SOLIS,S.ANDRE,J.HIRABAYASHI,K.KASAI,   
JRNL        AUTH 2 H.KALTNER,H.J.GABIUS,A.ROMERO                                
JRNL        TITL   GROWTH-REGULATORY HUMAN GALECTIN-1: CRYSTALLOGRAPHIC         
JRNL        TITL 2 CHARACTERISATION OF THE STRUCTURAL CHANGES INDUCED BY        
JRNL        TITL 3 SINGLE-SITE MUTATIONS AND THEIR IMPACT ON THE THERMODYNAMICS 
JRNL        TITL 4 OF LIGAND BINDING                                            
JRNL        REF    J.MOL.BIOL.                   V. 343   957 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15476813                                                     
JRNL        DOI    10.1016/J.JMB.2004.08.078                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1487364.510                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24611                          
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) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 968                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3864                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1950                       
REMARK   3   BIN FREE R VALUE                    : 0.2400                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 151                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2059                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 71                                      
REMARK   3   SOLVENT ATOMS            : 250                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 6.00                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.89000                                              
REMARK   3    B22 (A**2) : -1.68000                                             
REMARK   3    B33 (A**2) : -1.21000                                             
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) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.07                            
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) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.150                           
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) : 1.220 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.900 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.100 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.160 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 46.71                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : SULFATO.PARAM                                  
REMARK   3  PARAMETER FILE  4  : LAC.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.TOP                                
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : SULFATO.TOP                                    
REMARK   3  TOPOLOGY FILE  4   : LAC.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1W6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-AUG-04.                  
REMARK 100 THE DEPOSITION ID IS D_1290020832.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9035                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEACH                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28964                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.100                              
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: PDB ENTRY 1GZW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE OBTAINED IN SITTING        
REMARK 280  DROPS BY MIXING EQUAL VOLUMES OF THE PROTEIN SOLUTION (10 MG/ML)    
REMARK 280  AND THE PRECIPITATING BUFFER (2M AMMONIUM SULPHATE AND 1% REMARK    
REMARK 280  280 BETA-MERCAPTO ETHANOL,PH 5.6). THE GALACTOSE COMPLEX WAS        
REMARK 280  OBTAINED BY SOAKING C2S CRYSTALS FOR 72H IN THE MOTHER LIQUOR       
REMARK 280  SUPPLEMENTED WITH 10 MM OF LACTOSE, PH 5.60, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP                                                        
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       18.35600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.84150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.09950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.84150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.35600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.09950            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.3 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 MAY REGULATE CELL APOPTOSIS AND CELL DIFFERENTIATION.                
REMARK 400                                                                      
REMARK 400 ENGINEERED MUTATION CYS 2 SER AND GLY 65 ASP IN CHAINS               
REMARK 400 A AND B.                                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  5061     O    HOH B  5062              1.58            
REMARK 500   OXT  ASP A  1134     CE   LYS B  2129              2.09            
REMARK 500   OXT  ASP A  1134     NZ   LYS B  2129              2.17            
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   O    HOH A  2097     O    HOH B  5130     3655     2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ALA A1001   CA  -  C   -  N   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    SER A1002   C   -  N   -  CA  ANGL. DEV. =  25.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A1002      -87.09    -35.66                                   
REMARK 500    ASN A1050       89.20   -158.59                                   
REMARK 500    SER B2002     -171.62    -60.53                                   
REMARK 500    ASN B2050       85.85   -155.97                                   
REMARK 500    ASN B2056       59.98     37.19                                   
REMARK 500    PHE B2077       72.31   -150.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A 1001     SER A 1002                  -69.33                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ALA A1001        -23.84                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GZW   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HUMAN GALECTIN-1                          
REMARK 900 RELATED ID: 1W6M   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 COMPLEXED WITH       
REMARK 900 GALACTOSE                                                            
REMARK 900 RELATED ID: 1W6N   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1                      
REMARK 900 RELATED ID: 1W6P   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 COMPLEXED WITH N-    
REMARK 900 ACETYL- LACTOSAMINE                                                  
REMARK 900 RELATED ID: 1W6Q   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF R111H HUMAN GALECTIN-1                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CYS 2 ENGINEERED TO SER. GLY 65 ADDITIONAL MUTATION TO ASP           
DBREF  1W6O A 1001  1134  UNP    P09382   LEG1_HUMAN       1    134             
DBREF  1W6O B 2001  2134  UNP    P09382   LEG1_HUMAN       1    134             
SEQADV 1W6O SER A 1002  UNP  P09382    CYS     2 ENGINEERED MUTATION            
SEQADV 1W6O ASP A 1065  UNP  P09382    GLY    65 ENGINEERED MUTATION            
SEQADV 1W6O SER B 2002  UNP  P09382    CYS     2 ENGINEERED MUTATION            
SEQADV 1W6O ASP B 2065  UNP  P09382    GLY    65 ENGINEERED MUTATION            
SEQRES   1 A  134  ALA SER GLY LEU VAL ALA SER ASN LEU ASN LEU LYS PRO          
SEQRES   2 A  134  GLY GLU CSO LEU ARG VAL ARG GLY GLU VAL ALA PRO ASP          
SEQRES   3 A  134  ALA LYS SER PHE VAL LEU ASN LEU GLY LYS ASP SER ASN          
SEQRES   4 A  134  ASN LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN ALA HIS          
SEQRES   5 A  134  GLY ASP ALA ASN THR ILE VAL CYS ASN SER LYS ASP ASP          
SEQRES   6 A  134  GLY ALA TRP GLY THR GLU GLN ARG GLU ALA VAL PHE PRO          
SEQRES   7 A  134  PHE GLN PRO GLY SER VAL ALA GLU VAL CYS ILE THR PHE          
SEQRES   8 A  134  ASP GLN ALA ASN LEU THR VAL LYS LEU PRO ASP GLY TYR          
SEQRES   9 A  134  GLU PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU ALA ILE          
SEQRES  10 A  134  ASN TYR MET ALA ALA ASP GLY ASP PHE LYS ILE LYS CYS          
SEQRES  11 A  134  VAL ALA PHE ASP                                              
SEQRES   1 B  134  ALA SER GLY LEU VAL ALA SER ASN LEU ASN LEU LYS PRO          
SEQRES   2 B  134  GLY GLU CYS LEU ARG VAL ARG GLY GLU VAL ALA PRO ASP          
SEQRES   3 B  134  ALA LYS SER PHE VAL LEU ASN LEU GLY LYS ASP SER ASN          
SEQRES   4 B  134  ASN LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN ALA HIS          
SEQRES   5 B  134  GLY ASP ALA ASN THR ILE VAL CYS ASN SER LYS ASP ASP          
SEQRES   6 B  134  GLY ALA TRP GLY THR GLU GLN ARG GLU ALA VAL PHE PRO          
SEQRES   7 B  134  PHE GLN PRO GLY SER VAL ALA GLU VAL CYS ILE THR PHE          
SEQRES   8 B  134  ASP GLN ALA ASN LEU THR VAL LYS LEU PRO ASP GLY TYR          
SEQRES   9 B  134  GLU PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU ALA ILE          
SEQRES  10 B  134  ASN TYR MET ALA ALA ASP GLY ASP PHE LYS ILE LYS CYS          
SEQRES  11 B  134  VAL ALA PHE ASP                                              
MODRES 1W6O CSO A 1016  CYS  S-HYDROXYCYSTEINE                                  
HET    CSO  A1016       7                                                       
HET    BGC  C   1      12                                                       
HET    GAL  C   2      11                                                       
HET    BGC  D   1      12                                                       
HET    GAL  D   2      11                                                       
HET    BME  A2137       4                                                       
HET    BME  A2138       4                                                       
HET    SO4  B3135       5                                                       
HET    BME  B3138       4                                                       
HET    BME  B3139       4                                                       
HET    BME  B3140       4                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     BGC BETA-D-GLUCOPYRANOSE                                             
HETNAM     GAL BETA-D-GALACTOPYRANOSE                                           
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     SO4 SULFATE ION                                                      
HETSYN     BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE                               
HETSYN     GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE                         
FORMUL   1  CSO    C3 H7 N O3 S                                                 
FORMUL   3  BGC    2(C6 H12 O6)                                                 
FORMUL   3  GAL    2(C6 H12 O6)                                                 
FORMUL   5  BME    5(C2 H6 O S)                                                 
FORMUL   7  SO4    O4 S 2-                                                      
FORMUL  11  HOH   *250(H2 O)                                                    
SHEET    1  AA11 ALA A1067  TRP A1068  0                                        
SHEET    2  AA11 ASP A1054  ASP A1064 -1  O  ASP A1064   N  ALA A1067           
SHEET    3  AA11 ASN A1040  ALA A1051 -1  O  LEU A1041   N  LYS A1063           
SHEET    4  AA11 PHE A1030  ASP A1037 -1  N  PHE A1030   O  PRO A1047           
SHEET    5  AA11 ILE A1117  GLY A1124 -1  N  ASN A1118   O  GLY A1035           
SHEET    6  AA11 VAL A1005  LEU A1011 -1  O  ALA A1006   N  MET A1120           
SHEET    7  AA11 VAL B2005  SER B2007 -1  O  VAL B2005   N  SER A1007           
SHEET    8  AA11 TYR B2119  ALA B2122 -1  O  MET B2120   N  ALA B2006           
SHEET    9  AA11 LEU B2032  ASP B2037 -1  O  ASN B2033   N  ALA B2121           
SHEET   10  AA11 ASN B2040  ALA B2051 -1  O  ASN B2040   N  LYS B2036           
SHEET   11  AA11 ASP B2054  ASP B2064 -1  O  ASP B2054   N  ALA B2051           
SHEET    1  AB 3 ALA A1067  TRP A1068  0                                        
SHEET    2  AB 3 ASP A1054  ASP A1064 -1  O  ASP A1064   N  ALA A1067           
SHEET    3  AB 3 GLN A1072  ARG A1073 -1  O  GLN A1072   N  CYS A1060           
SHEET    1  AC10 GLU A1105  PRO A1109  0                                        
SHEET    2  AC10 ASN A1095  LYS A1099 -1  O  LEU A1096   N  PHE A1108           
SHEET    3  AC10 VAL A1084  PHE A1091 -1  O  CYS A1088   N  LYS A1099           
SHEET    4  AC10 CSO A1016  VAL A1023 -1  O  LEU A1017   N  ILE A1089           
SHEET    5  AC10 PHE A1126  PHE A1133 -1  O  LYS A1127   N  GLU A1022           
SHEET    6  AC10 PHE B2126  PHE B2133 -1  O  LYS B2129   N  PHE A1133           
SHEET    7  AC10 LEU B2017  VAL B2023 -1  O  ARG B2018   N  ALA B2132           
SHEET    8  AC10 VAL B2084  PHE B2091 -1  O  ALA B2085   N  GLY B2021           
SHEET    9  AC10 ASN B2095  LYS B2099 -1  O  THR B2097   N  THR B2090           
SHEET   10  AC10 GLU B2105  PRO B2109 -1  O  PHE B2106   N  VAL B2098           
LINK         C   GLU A1015                 N   CSO A1016     1555   1555  1.33  
LINK         C   CSO A1016                 N   LEU A1017     1555   1555  1.33  
LINK         SG  CYS A1088                 S2  BME A2137     1555   1555  1.92  
LINK         SG  CYS A1130                 S2  BME A2138     1555   1555  1.93  
LINK         SG  CYS B2016                 S2  BME B3138     1555   1555  1.92  
LINK         SG  CYS B2088                 S2  BME B3139     1555   1555  1.92  
LINK         SG  CYS B2130                 S2  BME B3140     1555   1555  1.93  
LINK         O4  BGC C   1                 C1  GAL C   2     1555   1555  1.41  
LINK         O4  BGC D   1                 C1  GAL D   2     1555   1555  1.41  
CRYST1   36.712   88.199   93.683  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      0.027239  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011338  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010674        0.00000                         
MTRIX1   1 -0.376390 -0.361370 -0.853070       66.42253    1                    
MTRIX2   1 -0.370680 -0.785140  0.496140       67.96960    1                    
MTRIX3   1 -0.849070  0.502960  0.161570       18.94398    1                    
ATOM      1  N   ALA A1001       1.314  41.735  29.951  1.00 44.07           N  
ATOM      2  CA  ALA A1001       2.170  40.686  30.579  1.00 43.70           C  
ATOM      3  C   ALA A1001       3.196  41.309  31.522  1.00 42.91           C  
ATOM      4  O   ALA A1001       3.377  40.845  32.649  1.00 43.72           O  
ATOM      5  CB  ALA A1001       2.877  39.874  29.491  1.00 43.69           C  
ATOM      6  N   SER A1002       2.902  42.602  31.472  1.00 40.89           N  
ATOM      7  CA  SER A1002       2.897  43.831  30.665  1.00 37.86           C  
ATOM      8  C   SER A1002       4.127  43.864  29.763  1.00 34.79           C  
ATOM      9  O   SER A1002       4.080  43.423  28.604  1.00 35.30           O  
ATOM     10  CB  SER A1002       2.923  45.057  31.581  1.00 38.22           C  
ATOM     11  OG  SER A1002       3.363  46.197  30.856  1.00 40.67           O  
ATOM     12  N   GLY A1003       5.180  44.391  30.344  1.00 30.01           N  
ATOM     13  CA  GLY A1003       6.483  44.530  29.692  1.00 23.13           C  
ATOM     14  C   GLY A1003       7.571  44.543  30.760  1.00 18.77           C  
ATOM     15  O   GLY A1003       7.330  44.938  31.910  1.00 16.97           O  
ATOM     16  N   LEU A1004       8.740  44.109  30.351  1.00 17.65           N  
ATOM     17  CA  LEU A1004       9.908  44.044  31.235  1.00 17.57           C  
ATOM     18  C   LEU A1004      10.176  45.419  31.855  1.00 17.44           C  
ATOM     19  O   LEU A1004      10.103  46.452  31.173  1.00 14.45           O  
ATOM     20  CB  LEU A1004      11.140  43.609  30.442  1.00 20.18           C  
ATOM     21  CG  LEU A1004      12.417  43.602  31.283  1.00 21.52           C  
ATOM     22  CD1 LEU A1004      12.372  42.590  32.430  1.00 23.61           C  
ATOM     23  CD2 LEU A1004      13.665  43.252  30.470  1.00 22.91           C  
ATOM     24  N   VAL A1005      10.477  45.377  33.141  1.00 15.57           N  
ATOM     25  CA  VAL A1005      10.780  46.577  33.938  1.00 15.57           C  
ATOM     26  C   VAL A1005      12.078  46.361  34.715  1.00 16.40           C  
ATOM     27  O   VAL A1005      12.176  45.453  35.555  1.00 16.72           O  
ATOM     28  CB  VAL A1005       9.647  46.856  34.930  1.00 15.82           C  
ATOM     29  CG1 VAL A1005       9.934  48.051  35.843  1.00 17.24           C  
ATOM     30  CG2 VAL A1005       8.315  47.168  34.246  1.00 16.21           C  
ATOM     31  N   ALA A1006      13.041  47.208  34.409  1.00 15.93           N  
ATOM     32  CA  ALA A1006      14.368  47.162  35.038  1.00 16.11           C  
ATOM     33  C   ALA A1006      14.678  48.487  35.735  1.00 17.19           C  
ATOM     34  O   ALA A1006      14.433  49.571  35.185  1.00 17.93           O  
ATOM     35  CB  ALA A1006      15.441  46.904  33.978  1.00 15.01           C  
ATOM     36  N   SER A1007      15.211  48.341  36.933  1.00 17.05           N  
ATOM     37  CA  SER A1007      15.601  49.472  37.786  1.00 19.20           C  
ATOM     38  C   SER A1007      17.040  49.274  38.269  1.00 19.59           C  
ATOM     39  O   SER A1007      17.602  48.174  38.164  1.00 17.66           O  
ATOM     40  CB  SER A1007      14.670  49.562  38.999  1.00 21.33           C  
ATOM     41  OG  SER A1007      14.704  48.346  39.732  1.00 28.68           O  
ATOM     42  N   ASN A1008      17.593  50.355  38.784  1.00 20.97           N  
ATOM     43  CA  ASN A1008      18.969  50.374  39.302  1.00 22.43           C  
ATOM     44  C   ASN A1008      19.964  50.200  38.152  1.00 22.63           C  
ATOM     45  O   ASN A1008      21.044  49.616  38.324  1.00 22.38           O  
ATOM     46  CB  ASN A1008      19.168  49.236  40.305  1.00 25.64           C  
ATOM     47  CG  ASN A1008      18.419  49.460  41.619  1.00 28.26           C  
ATOM     48  OD1 ASN A1008      18.437  48.594  42.493  1.00 31.33           O  
ATOM     49  ND2 ASN A1008      17.754  50.583  41.816  1.00 29.35           N  
ATOM     50  N   LEU A1009      19.585  50.684  36.988  1.00 21.84           N  
ATOM     51  CA  LEU A1009      20.431  50.565  35.803  1.00 23.08           C  
ATOM     52  C   LEU A1009      21.722  51.365  35.902  1.00 24.30           C  
ATOM     53  O   LEU A1009      22.770  50.928  35.427  1.00 25.08           O  
ATOM     54  CB  LEU A1009      19.670  51.011  34.553  1.00 22.70           C  
ATOM     55  CG  LEU A1009      18.631  50.045  33.983  1.00 24.00           C  
ATOM     56  CD1 LEU A1009      17.559  49.757  35.014  1.00 25.97           C  
ATOM     57  CD2 LEU A1009      18.020  50.650  32.729  1.00 24.25           C  
ATOM     58  N   ASN A1010      21.639  52.538  36.517  1.00 24.63           N  
ATOM     59  CA  ASN A1010      22.796  53.409  36.663  1.00 26.09           C  
ATOM     60  C   ASN A1010      23.539  53.567  35.335  1.00 25.32           C  
ATOM     61  O   ASN A1010      24.763  53.449  35.275  1.00 25.47           O  
ATOM     62  CB  ASN A1010      23.743  52.858  37.733  1.00 27.63           C  
ATOM     63  CG  ASN A1010      24.878  53.813  38.047  1.00 29.97           C  
ATOM     64  OD1 ASN A1010      24.650  54.987  38.338  1.00 30.45           O  
ATOM     65  ND2 ASN A1010      26.107  53.314  37.992  1.00 30.48           N  
ATOM     66  N   LEU A1011      22.786  53.822  34.270  1.00 24.75           N  
ATOM     67  CA  LEU A1011      23.368  54.016  32.946  1.00 24.14           C  
ATOM     68  C   LEU A1011      23.905  55.444  32.899  1.00 24.04           C  
ATOM     69  O   LEU A1011      23.143  56.407  32.994  1.00 23.58           O  
ATOM     70  CB  LEU A1011      22.303  53.822  31.866  1.00 25.42           C  
ATOM     71  CG  LEU A1011      22.786  53.847  30.415  1.00 26.92           C  
ATOM     72  CD1 LEU A1011      23.635  52.614  30.138  1.00 28.63           C  
ATOM     73  CD2 LEU A1011      21.587  53.880  29.482  1.00 27.59           C  
ATOM     74  N   LYS A1012      25.218  55.574  32.751  1.00 23.31           N  
ATOM     75  CA  LYS A1012      25.860  56.881  32.724  1.00 24.70           C  
ATOM     76  C   LYS A1012      25.982  57.500  31.335  1.00 23.69           C  
ATOM     77  O   LYS A1012      25.828  56.819  30.322  1.00 21.95           O  
ATOM     78  CB  LYS A1012      27.248  56.776  33.364  1.00 26.91           C  
ATOM     79  CG  LYS A1012      27.384  57.523  34.683  1.00 31.82           C  
ATOM     80  CD  LYS A1012      26.382  57.039  35.723  1.00 32.33           C  
ATOM     81  CE  LYS A1012      26.505  57.838  37.018  1.00 34.81           C  
ATOM     82  NZ  LYS A1012      25.513  57.419  38.049  1.00 33.13           N  
ATOM     83  N   PRO A1013      26.254  58.816  31.275  1.00 24.25           N  
ATOM     84  CA  PRO A1013      26.399  59.519  29.999  1.00 24.51           C  
ATOM     85  C   PRO A1013      27.454  58.856  29.124  1.00 24.19           C  
ATOM     86  O   PRO A1013      28.528  58.496  29.603  1.00 24.81           O  
ATOM     87  CB  PRO A1013      26.807  60.922  30.431  1.00 25.02           C  
ATOM     88  CG  PRO A1013      26.053  61.094  31.700  1.00 24.58           C  
ATOM     89  CD  PRO A1013      26.297  59.772  32.396  1.00 24.68           C  
ATOM     90  N   GLY A1014      27.143  58.693  27.842  1.00 23.56           N  
ATOM     91  CA  GLY A1014      28.080  58.067  26.930  1.00 23.34           C  
ATOM     92  C   GLY A1014      27.834  56.579  26.791  1.00 23.62           C  
ATOM     93  O   GLY A1014      28.386  55.934  25.902  1.00 23.60           O  
ATOM     94  N   GLU A1015      27.004  56.028  27.672  1.00 22.71           N  
ATOM     95  CA  GLU A1015      26.696  54.605  27.629  1.00 23.58           C  
ATOM     96  C   GLU A1015      25.483  54.327  26.746  1.00 22.91           C  
ATOM     97  O   GLU A1015      24.557  55.137  26.669  1.00 22.00           O  
ATOM     98  CB  GLU A1015      26.469  54.076  29.046  1.00 25.90           C  
ATOM     99  CG  GLU A1015      27.697  54.229  29.932  1.00 29.69           C  
ATOM    100  CD  GLU A1015      27.558  53.539  31.273  1.00 33.50           C  
ATOM    101  OE1 GLU A1015      28.535  53.564  32.049  1.00 35.14           O  
ATOM    102  OE2 GLU A1015      26.481  52.974  31.552  1.00 37.12           O  
HETATM  103  N   CSO A1016      25.498  53.176  26.084  1.00 23.00           N  
HETATM  104  CA  CSO A1016      24.423  52.804  25.173  1.00 22.50           C  
HETATM  105  CB  CSO A1016      25.008  52.464  23.802  1.00 24.89           C  
HETATM  106  SG  CSO A1016      23.789  52.199  22.489  1.00 30.68           S  
HETATM  107  C   CSO A1016      23.609  51.610  25.673  1.00 20.62           C  
HETATM  108  O   CSO A1016      24.144  50.662  26.248  1.00 19.61           O  
HETATM  109  OD  CSO A1016      23.957  50.593  22.273  1.00 23.93           O  
ATOM    110  N   LEU A1017      22.305  51.681  25.440  1.00 18.10           N  
ATOM    111  CA  LEU A1017      21.376  50.630  25.823  1.00 15.99           C  
ATOM    112  C   LEU A1017      20.841  50.024  24.533  1.00 15.39           C  
ATOM    113  O   LEU A1017      20.282  50.732  23.698  1.00 13.71           O  
ATOM    114  CB  LEU A1017      20.219  51.225  26.625  1.00 18.01           C  
ATOM    115  CG  LEU A1017      19.064  50.292  26.982  1.00 19.35           C  
ATOM    116  CD1 LEU A1017      19.550  49.210  27.933  1.00 21.78           C  
ATOM    117  CD2 LEU A1017      17.952  51.101  27.624  1.00 22.73           C  
ATOM    118  N   ARG A1018      21.025  48.719  24.366  1.00 13.82           N  
ATOM    119  CA  ARG A1018      20.551  48.034  23.170  1.00 13.99           C  
ATOM    120  C   ARG A1018      19.348  47.178  23.552  1.00 13.90           C  
ATOM    121  O   ARG A1018      19.422  46.362  24.473  1.00 12.49           O  
ATOM    122  CB  ARG A1018      21.667  47.157  22.597  1.00 17.15           C  
ATOM    123  CG  ARG A1018      21.358  46.531  21.247  1.00 22.93           C  
ATOM    124  CD  ARG A1018      22.489  45.608  20.816  1.00 26.46           C  
ATOM    125  NE  ARG A1018      23.753  46.320  20.652  1.00 30.40           N  
ATOM    126  CZ  ARG A1018      24.110  46.978  19.552  1.00 32.13           C  
ATOM    127  NH1 ARG A1018      25.281  47.599  19.500  1.00 33.50           N  
ATOM    128  NH2 ARG A1018      23.307  47.003  18.497  1.00 32.86           N  
ATOM    129  N   VAL A1019      18.235  47.376  22.854  1.00 12.25           N  
ATOM    130  CA  VAL A1019      17.024  46.622  23.139  1.00 12.51           C  
ATOM    131  C   VAL A1019      16.517  45.941  21.876  1.00 13.91           C  
ATOM    132  O   VAL A1019      16.238  46.598  20.878  1.00 11.92           O  
ATOM    133  CB  VAL A1019      15.918  47.550  23.699  1.00 12.24           C  
ATOM    134  CG1 VAL A1019      14.688  46.735  24.069  1.00 14.18           C  
ATOM    135  CG2 VAL A1019      16.439  48.306  24.913  1.00 13.15           C  
ATOM    136  N   ARG A1020      16.417  44.615  21.923  1.00 13.36           N  
ATOM    137  CA  ARG A1020      15.933  43.843  20.788  1.00 14.68           C  
ATOM    138  C   ARG A1020      14.653  43.144  21.209  1.00 15.39           C  
ATOM    139  O   ARG A1020      14.577  42.581  22.301  1.00 14.72           O  
ATOM    140  CB  ARG A1020      16.974  42.805  20.365  1.00 18.20           C  
ATOM    141  CG  ARG A1020      16.582  41.984  19.145  1.00 22.14           C  
ATOM    142  CD  ARG A1020      17.668  40.975  18.810  1.00 26.75           C  
ATOM    143  NE  ARG A1020      18.963  41.625  18.634  1.00 31.48           N  
ATOM    144  CZ  ARG A1020      20.104  40.977  18.420  1.00 33.16           C  
ATOM    145  NH1 ARG A1020      20.115  39.652  18.354  1.00 34.41           N  
ATOM    146  NH2 ARG A1020      21.235  41.655  18.273  1.00 34.55           N  
ATOM    147  N   GLY A1021      13.643  43.190  20.349  1.00 14.77           N  
ATOM    148  CA  GLY A1021      12.383  42.551  20.677  1.00 15.33           C  
ATOM    149  C   GLY A1021      11.572  42.194  19.449  1.00 16.78           C  
ATOM    150  O   GLY A1021      11.916  42.573  18.330  1.00 16.03           O  
ATOM    151  N   GLU A1022      10.487  41.460  19.666  1.00 17.24           N  
ATOM    152  CA  GLU A1022       9.617  41.042  18.578  1.00 19.06           C  
ATOM    153  C   GLU A1022       8.375  41.919  18.521  1.00 18.74           C  
ATOM    154  O   GLU A1022       7.664  42.066  19.516  1.00 18.05           O  
ATOM    155  CB  GLU A1022       9.206  39.576  18.770  1.00 21.74           C  
ATOM    156  CG  GLU A1022      10.360  38.593  18.647  1.00 26.03           C  
ATOM    157  CD  GLU A1022       9.967  37.167  19.000  1.00 29.68           C  
ATOM    158  OE1 GLU A1022      10.785  36.252  18.759  1.00 31.39           O  
ATOM    159  OE2 GLU A1022       8.849  36.963  19.524  1.00 31.81           O  
ATOM    160  N   VAL A1023       8.126  42.520  17.363  1.00 19.36           N  
ATOM    161  CA  VAL A1023       6.945  43.357  17.201  1.00 19.16           C  
ATOM    162  C   VAL A1023       5.789  42.413  16.893  1.00 19.25           C  
ATOM    163  O   VAL A1023       5.877  41.599  15.974  1.00 20.32           O  
ATOM    164  CB  VAL A1023       7.099  44.351  16.030  1.00 19.02           C  
ATOM    165  CG1 VAL A1023       5.865  45.231  15.939  1.00 19.57           C  
ATOM    166  CG2 VAL A1023       8.345  45.203  16.224  1.00 19.07           C  
ATOM    167  N   ALA A1024       4.717  42.513  17.670  1.00 20.77           N  
ATOM    168  CA  ALA A1024       3.551  41.659  17.475  1.00 22.02           C  
ATOM    169  C   ALA A1024       3.067  41.729  16.030  1.00 23.52           C  
ATOM    170  O   ALA A1024       3.135  42.777  15.389  1.00 21.40           O  
ATOM    171  CB  ALA A1024       2.434  42.074  18.427  1.00 21.48           C  
ATOM    172  N   PRO A1025       2.574  40.604  15.494  1.00 25.42           N  
ATOM    173  CA  PRO A1025       2.084  40.571  14.113  1.00 27.49           C  
ATOM    174  C   PRO A1025       0.883  41.491  13.894  1.00 28.24           C  
ATOM    175  O   PRO A1025       0.563  41.850  12.760  1.00 29.68           O  
ATOM    176  CB  PRO A1025       1.741  39.097  13.907  1.00 28.22           C  
ATOM    177  CG  PRO A1025       1.340  38.653  15.282  1.00 28.09           C  
ATOM    178  CD  PRO A1025       2.399  39.294  16.145  1.00 26.94           C  
ATOM    179  N   ASP A1026       0.229  41.870  14.987  1.00 28.55           N  
ATOM    180  CA  ASP A1026      -0.937  42.746  14.928  1.00 29.92           C  
ATOM    181  C   ASP A1026      -0.673  43.998  15.756  1.00 28.10           C  
ATOM    182  O   ASP A1026      -1.604  44.658  16.222  1.00 28.10           O  
ATOM    183  CB  ASP A1026      -2.158  42.022  15.491  1.00 33.79           C  
ATOM    184  CG  ASP A1026      -1.985  41.650  16.953  1.00 37.07           C  
ATOM    185  OD1 ASP A1026      -1.015  40.930  17.272  1.00 38.62           O  
ATOM    186  OD2 ASP A1026      -2.814  42.083  17.782  1.00 39.49           O  
ATOM    187  N   ALA A1027       0.604  44.317  15.934  1.00 26.22           N  
ATOM    188  CA  ALA A1027       1.010  45.473  16.723  1.00 23.76           C  
ATOM    189  C   ALA A1027       0.287  46.760  16.350  1.00 22.54           C  
ATOM    190  O   ALA A1027       0.082  47.057  15.174  1.00 22.55           O  
ATOM    191  CB  ALA A1027       2.514  45.677  16.600  1.00 22.34           C  
ATOM    192  N   LYS A1028      -0.096  47.517  17.371  1.00 20.36           N  
ATOM    193  CA  LYS A1028      -0.770  48.793  17.190  1.00 20.43           C  
ATOM    194  C   LYS A1028       0.149  49.882  17.726  1.00 18.59           C  
ATOM    195  O   LYS A1028       0.157  51.014  17.241  1.00 16.81           O  
ATOM    196  CB  LYS A1028      -2.088  48.810  17.966  1.00 23.06           C  
ATOM    197  CG  LYS A1028      -3.137  47.846  17.434  1.00 26.16           C  
ATOM    198  CD  LYS A1028      -3.557  48.223  16.018  1.00 30.26           C  
ATOM    199  CE  LYS A1028      -4.622  47.276  15.490  1.00 32.75           C  
ATOM    200  NZ  LYS A1028      -5.823  47.262  16.372  1.00 33.82           N  
ATOM    201  N   SER A1029       0.936  49.515  18.729  1.00 17.99           N  
ATOM    202  CA  SER A1029       1.854  50.445  19.364  1.00 17.55           C  
ATOM    203  C   SER A1029       2.648  49.744  20.455  1.00 17.05           C  
ATOM    204  O   SER A1029       2.176  48.780  21.050  1.00 17.37           O  
ATOM    205  CB  SER A1029       1.061  51.598  19.987  1.00 20.44           C  
ATOM    206  OG  SER A1029       1.793  52.249  21.005  1.00 22.25           O  
ATOM    207  N   PHE A1030       3.868  50.210  20.693  1.00 14.30           N  
ATOM    208  CA  PHE A1030       4.679  49.657  21.764  1.00 12.32           C  
ATOM    209  C   PHE A1030       5.503  50.798  22.322  1.00 12.42           C  
ATOM    210  O   PHE A1030       5.693  51.827  21.662  1.00 11.03           O  
ATOM    211  CB  PHE A1030       5.535  48.464  21.293  1.00 12.18           C  
ATOM    212  CG  PHE A1030       6.784  48.828  20.535  1.00 12.45           C  
ATOM    213  CD1 PHE A1030       7.943  49.204  21.207  1.00 13.20           C  
ATOM    214  CD2 PHE A1030       6.827  48.706  19.150  1.00 13.14           C  
ATOM    215  CE1 PHE A1030       9.129  49.443  20.510  1.00 13.43           C  
ATOM    216  CE2 PHE A1030       8.007  48.944  18.444  1.00 13.48           C  
ATOM    217  CZ  PHE A1030       9.160  49.311  19.127  1.00 12.66           C  
ATOM    218  N   VAL A1031       5.962  50.634  23.554  1.00 10.44           N  
ATOM    219  CA  VAL A1031       6.711  51.684  24.211  1.00 10.90           C  
ATOM    220  C   VAL A1031       7.939  51.181  24.943  1.00  9.76           C  
ATOM    221  O   VAL A1031       7.975  50.054  25.432  1.00 11.43           O  
ATOM    222  CB  VAL A1031       5.815  52.419  25.249  1.00 11.05           C  
ATOM    223  CG1 VAL A1031       6.643  53.407  26.063  1.00 11.14           C  
ATOM    224  CG2 VAL A1031       4.673  53.139  24.545  1.00 12.13           C  
ATOM    225  N   LEU A1032       8.947  52.040  24.985  1.00  9.87           N  
ATOM    226  CA  LEU A1032      10.178  51.786  25.715  1.00 10.41           C  
ATOM    227  C   LEU A1032      10.341  53.079  26.502  1.00 10.30           C  
ATOM    228  O   LEU A1032      10.486  54.150  25.914  1.00  8.70           O  
ATOM    229  CB  LEU A1032      11.373  51.591  24.774  1.00 12.04           C  
ATOM    230  CG  LEU A1032      11.418  50.308  23.936  1.00 13.82           C  
ATOM    231  CD1 LEU A1032      12.690  50.288  23.105  1.00 15.65           C  
ATOM    232  CD2 LEU A1032      11.366  49.090  24.850  1.00 14.86           C  
ATOM    233  N   ASN A1033      10.265  52.983  27.825  1.00 10.82           N  
ATOM    234  CA  ASN A1033      10.414  54.151  28.681  1.00 11.53           C  
ATOM    235  C   ASN A1033      11.742  54.093  29.417  1.00 11.55           C  
ATOM    236  O   ASN A1033      12.140  53.041  29.921  1.00 13.10           O  
ATOM    237  CB  ASN A1033       9.275  54.237  29.705  1.00 11.87           C  
ATOM    238  CG  ASN A1033       7.951  54.618  29.078  1.00 13.97           C  
ATOM    239  OD1 ASN A1033       7.901  55.450  28.170  1.00 14.30           O  
ATOM    240  ND2 ASN A1033       6.867  54.027  29.571  1.00 11.74           N  
ATOM    241  N   LEU A1034      12.422  55.232  29.469  1.00 10.50           N  
ATOM    242  CA  LEU A1034      13.706  55.342  30.146  1.00 11.60           C  
ATOM    243  C   LEU A1034      13.686  56.593  31.012  1.00 12.52           C  
ATOM    244  O   LEU A1034      13.131  57.617  30.615  1.00 11.38           O  
ATOM    245  CB  LEU A1034      14.839  55.458  29.124  1.00 12.25           C  
ATOM    246  CG  LEU A1034      15.048  54.291  28.159  1.00 13.38           C  
ATOM    247  CD1 LEU A1034      16.186  54.626  27.199  1.00 16.14           C  
ATOM    248  CD2 LEU A1034      15.370  53.031  28.947  1.00 16.15           C  
ATOM    249  N   GLY A1035      14.291  56.517  32.192  1.00 12.83           N  
ATOM    250  CA  GLY A1035      14.315  57.679  33.058  1.00 13.95           C  
ATOM    251  C   GLY A1035      14.807  57.383  34.458  1.00 15.67           C  
ATOM    252  O   GLY A1035      15.579  56.447  34.670  1.00 15.54           O  
ATOM    253  N   LYS A1036      14.367  58.197  35.410  1.00 17.82           N  
ATOM    254  CA  LYS A1036      14.744  58.034  36.810  1.00 19.60           C  
ATOM    255  C   LYS A1036      13.803  57.019  37.445  1.00 19.78           C  
ATOM    256  O   LYS A1036      14.218  56.179  38.246  1.00 20.31           O  
ATOM    257  CB  LYS A1036      14.642  59.373  37.548  1.00 21.53           C  
ATOM    258  CG  LYS A1036      14.895  59.267  39.046  1.00 24.79           C  
ATOM    259  CD  LYS A1036      14.791  60.617  39.745  1.00 28.55           C  
ATOM    260  CE  LYS A1036      15.915  61.554  39.332  1.00 30.73           C  
ATOM    261  NZ  LYS A1036      15.883  62.830  40.109  1.00 33.72           N  
ATOM    262  N   ASP A1037      12.530  57.117  37.082  1.00 19.40           N  
ATOM    263  CA  ASP A1037      11.498  56.212  37.569  1.00 20.78           C  
ATOM    264  C   ASP A1037      10.286  56.307  36.649  1.00 20.11           C  
ATOM    265  O   ASP A1037      10.317  57.024  35.650  1.00 20.61           O  
ATOM    266  CB  ASP A1037      11.105  56.545  39.016  1.00 21.70           C  
ATOM    267  CG  ASP A1037      10.684  57.991  39.197  1.00 24.02           C  
ATOM    268  OD1 ASP A1037       9.839  58.473  38.416  1.00 20.97           O  
ATOM    269  OD2 ASP A1037      11.195  58.643  40.134  1.00 25.89           O  
ATOM    270  N   SER A1038       9.221  55.592  36.989  1.00 20.39           N  
ATOM    271  CA  SER A1038       8.017  55.574  36.169  1.00 20.01           C  
ATOM    272  C   SER A1038       7.363  56.931  35.925  1.00 20.52           C  
ATOM    273  O   SER A1038       6.656  57.102  34.933  1.00 20.79           O  
ATOM    274  CB  SER A1038       6.980  54.631  36.783  1.00 21.59           C  
ATOM    275  OG  SER A1038       6.521  55.127  38.027  1.00 22.92           O  
ATOM    276  N   ASN A1039       7.588  57.894  36.814  1.00 19.63           N  
ATOM    277  CA  ASN A1039       6.974  59.211  36.650  1.00 20.66           C  
ATOM    278  C   ASN A1039       7.923  60.286  36.148  1.00 18.10           C  
ATOM    279  O   ASN A1039       7.518  61.428  35.943  1.00 18.38           O  
ATOM    280  CB  ASN A1039       6.348  59.670  37.968  1.00 23.17           C  
ATOM    281  CG  ASN A1039       5.226  58.764  38.423  1.00 26.37           C  
ATOM    282  OD1 ASN A1039       4.265  58.534  37.689  1.00 29.19           O  
ATOM    283  ND2 ASN A1039       5.339  58.246  39.640  1.00 29.39           N  
ATOM    284  N   ASN A1040       9.182  59.918  35.951  1.00 17.39           N  
ATOM    285  CA  ASN A1040      10.191  60.855  35.478  1.00 16.14           C  
ATOM    286  C   ASN A1040      10.996  60.189  34.370  1.00 15.13           C  
ATOM    287  O   ASN A1040      12.003  59.522  34.624  1.00 14.23           O  
ATOM    288  CB  ASN A1040      11.094  61.260  36.641  1.00 17.27           C  
ATOM    289  CG  ASN A1040      10.351  62.071  37.693  1.00 19.53           C  
ATOM    290  OD1 ASN A1040      10.086  63.259  37.504  1.00 18.57           O  
ATOM    291  ND2 ASN A1040       9.997  61.425  38.798  1.00 20.09           N  
ATOM    292  N   LEU A1041      10.541  60.384  33.137  1.00 12.93           N  
ATOM    293  CA  LEU A1041      11.173  59.771  31.975  1.00 12.96           C  
ATOM    294  C   LEU A1041      11.915  60.748  31.083  1.00 12.48           C  
ATOM    295  O   LEU A1041      11.354  61.766  30.667  1.00 12.23           O  
ATOM    296  CB  LEU A1041      10.110  59.062  31.134  1.00 12.89           C  
ATOM    297  CG  LEU A1041       9.158  58.117  31.866  1.00 13.31           C  
ATOM    298  CD1 LEU A1041       8.078  57.647  30.908  1.00 12.12           C  
ATOM    299  CD2 LEU A1041       9.934  56.930  32.425  1.00 13.45           C  
ATOM    300  N   CYS A1042      13.174  60.438  30.784  1.00 10.98           N  
ATOM    301  CA  CYS A1042      13.949  61.283  29.893  1.00 12.43           C  
ATOM    302  C   CYS A1042      13.579  60.871  28.471  1.00 13.14           C  
ATOM    303  O   CYS A1042      13.770  61.631  27.520  1.00 12.42           O  
ATOM    304  CB  CYS A1042      15.453  61.116  30.135  1.00 14.04           C  
ATOM    305  SG  CYS A1042      16.086  59.422  30.083  1.00 13.88           S  
ATOM    306  N   LEU A1043      13.033  59.665  28.330  1.00 11.04           N  
ATOM    307  CA  LEU A1043      12.623  59.192  27.014  1.00 10.56           C  
ATOM    308  C   LEU A1043      11.463  58.202  26.998  1.00 11.48           C  
ATOM    309  O   LEU A1043      11.554  57.092  27.523  1.00 10.79           O  
ATOM    310  CB  LEU A1043      13.807  58.572  26.265  1.00 11.79           C  
ATOM    311  CG  LEU A1043      13.466  58.089  24.847  1.00 11.20           C  
ATOM    312  CD1 LEU A1043      13.029  59.279  23.999  1.00 14.23           C  
ATOM    313  CD2 LEU A1043      14.664  57.395  24.221  1.00 11.47           C  
ATOM    314  N   HIS A1044      10.364  58.634  26.393  1.00  9.49           N  
ATOM    315  CA  HIS A1044       9.186  57.801  26.213  1.00 10.56           C  
ATOM    316  C   HIS A1044       9.261  57.571  24.705  1.00 10.26           C  
ATOM    317  O   HIS A1044       8.926  58.461  23.928  1.00 11.18           O  
ATOM    318  CB  HIS A1044       7.915  58.578  26.580  1.00 10.38           C  
ATOM    319  CG  HIS A1044       6.644  57.916  26.142  1.00 11.33           C  
ATOM    320  ND1 HIS A1044       6.177  56.746  26.703  1.00 12.35           N  
ATOM    321  CD2 HIS A1044       5.739  58.265  25.197  1.00 11.47           C  
ATOM    322  CE1 HIS A1044       5.040  56.404  26.123  1.00 13.45           C  
ATOM    323  NE2 HIS A1044       4.752  57.309  25.205  1.00 13.95           N  
ATOM    324  N   PHE A1045       9.751  56.398  24.312  1.00 10.01           N  
ATOM    325  CA  PHE A1045       9.915  56.022  22.905  1.00 10.50           C  
ATOM    326  C   PHE A1045       8.672  55.241  22.496  1.00 11.21           C  
ATOM    327  O   PHE A1045       8.498  54.087  22.887  1.00  9.15           O  
ATOM    328  CB  PHE A1045      11.175  55.163  22.759  1.00  9.73           C  
ATOM    329  CG  PHE A1045      11.436  54.698  21.359  1.00  8.08           C  
ATOM    330  CD1 PHE A1045      11.841  55.595  20.377  1.00  8.58           C  
ATOM    331  CD2 PHE A1045      11.279  53.360  21.022  1.00  6.99           C  
ATOM    332  CE1 PHE A1045      12.086  55.164  19.075  1.00  9.53           C  
ATOM    333  CE2 PHE A1045      11.518  52.917  19.725  1.00  8.73           C  
ATOM    334  CZ  PHE A1045      11.924  53.819  18.749  1.00  8.52           C  
ATOM    335  N   ASN A1046       7.826  55.861  21.680  1.00  9.89           N  
ATOM    336  CA  ASN A1046       6.554  55.253  21.309  1.00 10.13           C  
ATOM    337  C   ASN A1046       6.235  55.078  19.823  1.00  9.79           C  
ATOM    338  O   ASN A1046       5.616  55.948  19.210  1.00  9.57           O  
ATOM    339  CB  ASN A1046       5.451  56.084  21.980  1.00 10.53           C  
ATOM    340  CG  ASN A1046       4.054  55.521  21.781  1.00 11.18           C  
ATOM    341  OD1 ASN A1046       3.072  56.226  22.014  1.00 12.66           O  
ATOM    342  ND2 ASN A1046       3.954  54.260  21.372  1.00 11.42           N  
ATOM    343  N   PRO A1047       6.683  53.965  19.218  1.00 10.80           N  
ATOM    344  CA  PRO A1047       6.386  53.739  17.801  1.00 11.20           C  
ATOM    345  C   PRO A1047       4.900  53.391  17.707  1.00 13.08           C  
ATOM    346  O   PRO A1047       4.450  52.401  18.289  1.00 11.47           O  
ATOM    347  CB  PRO A1047       7.265  52.544  17.450  1.00 13.21           C  
ATOM    348  CG  PRO A1047       8.453  52.745  18.332  1.00 10.48           C  
ATOM    349  CD  PRO A1047       7.802  53.110  19.651  1.00  9.24           C  
ATOM    350  N   ARG A1048       4.140  54.210  16.989  1.00 11.58           N  
ATOM    351  CA  ARG A1048       2.714  53.971  16.844  1.00 12.62           C  
ATOM    352  C   ARG A1048       2.374  53.506  15.438  1.00 13.03           C  
ATOM    353  O   ARG A1048       2.512  54.260  14.475  1.00 12.39           O  
ATOM    354  CB  ARG A1048       1.934  55.248  17.155  1.00 11.88           C  
ATOM    355  CG  ARG A1048       2.093  55.735  18.578  1.00 11.64           C  
ATOM    356  CD  ARG A1048       1.417  57.080  18.775  1.00 12.19           C  
ATOM    357  NE  ARG A1048       1.567  57.561  20.144  1.00 11.54           N  
ATOM    358  CZ  ARG A1048       1.151  58.748  20.572  1.00 12.34           C  
ATOM    359  NH1 ARG A1048       0.557  59.586  19.733  1.00 12.23           N  
ATOM    360  NH2 ARG A1048       1.326  59.097  21.841  1.00 12.94           N  
ATOM    361  N   PHE A1049       1.940  52.256  15.322  1.00 13.07           N  
ATOM    362  CA  PHE A1049       1.560  51.714  14.027  1.00 14.03           C  
ATOM    363  C   PHE A1049       0.190  52.298  13.702  1.00 14.59           C  
ATOM    364  O   PHE A1049      -0.061  52.757  12.591  1.00 15.03           O  
ATOM    365  CB  PHE A1049       1.493  50.186  14.089  1.00 13.54           C  
ATOM    366  CG  PHE A1049       2.795  49.539  14.478  1.00 13.51           C  
ATOM    367  CD1 PHE A1049       3.194  49.496  15.810  1.00 15.22           C  
ATOM    368  CD2 PHE A1049       3.640  49.007  13.507  1.00 14.98           C  
ATOM    369  CE1 PHE A1049       4.417  48.936  16.172  1.00 14.88           C  
ATOM    370  CE2 PHE A1049       4.868  48.444  13.855  1.00 13.97           C  
ATOM    371  CZ  PHE A1049       5.257  48.409  15.191  1.00 15.72           C  
ATOM    372  N   ASN A1050      -0.688  52.285  14.699  1.00 17.33           N  
ATOM    373  CA  ASN A1050      -2.033  52.823  14.558  1.00 17.60           C  
ATOM    374  C   ASN A1050      -2.593  53.152  15.938  1.00 18.26           C  
ATOM    375  O   ASN A1050      -3.236  52.313  16.572  1.00 16.44           O  
ATOM    376  CB  ASN A1050      -2.938  51.813  13.850  1.00 20.29           C  
ATOM    377  CG  ASN A1050      -4.386  52.257  13.816  1.00 22.72           C  
ATOM    378  OD1 ASN A1050      -4.686  53.408  13.504  1.00 24.48           O  
ATOM    379  ND2 ASN A1050      -5.294  51.341  14.135  1.00 25.53           N  
ATOM    380  N   ALA A1051      -2.346  54.376  16.398  1.00 18.69           N  
ATOM    381  CA  ALA A1051      -2.817  54.800  17.710  1.00 20.20           C  
ATOM    382  C   ALA A1051      -2.810  56.313  17.885  1.00 21.29           C  
ATOM    383  O   ALA A1051      -1.906  57.004  17.410  1.00 20.80           O  
ATOM    384  CB  ALA A1051      -1.965  54.153  18.795  1.00 20.57           C  
ATOM    385  N   HIS A1052      -3.830  56.819  18.572  1.00 22.54           N  
ATOM    386  CA  HIS A1052      -3.956  58.246  18.851  1.00 23.76           C  
ATOM    387  C   HIS A1052      -3.945  59.137  17.618  1.00 23.94           C  
ATOM    388  O   HIS A1052      -3.554  60.302  17.693  1.00 25.75           O  
ATOM    389  CB  HIS A1052      -2.840  58.680  19.799  1.00 26.19           C  
ATOM    390  CG  HIS A1052      -2.838  57.937  21.097  1.00 27.49           C  
ATOM    391  ND1 HIS A1052      -3.874  58.021  22.002  1.00 29.23           N  
ATOM    392  CD2 HIS A1052      -1.943  57.070  21.627  1.00 28.08           C  
ATOM    393  CE1 HIS A1052      -3.618  57.236  23.034  1.00 29.16           C  
ATOM    394  NE2 HIS A1052      -2.453  56.648  22.831  1.00 29.78           N  
ATOM    395  N   GLY A1053      -4.378  58.598  16.485  1.00 22.68           N  
ATOM    396  CA  GLY A1053      -4.407  59.389  15.269  1.00 22.10           C  
ATOM    397  C   GLY A1053      -3.121  59.300  14.471  1.00 20.65           C  
ATOM    398  O   GLY A1053      -3.014  59.874  13.387  1.00 21.63           O  
ATOM    399  N   ASP A1054      -2.138  58.586  15.008  1.00 18.01           N  
ATOM    400  CA  ASP A1054      -0.864  58.417  14.321  1.00 16.54           C  
ATOM    401  C   ASP A1054      -0.827  57.091  13.573  1.00 15.84           C  
ATOM    402  O   ASP A1054      -1.240  56.058  14.102  1.00 16.05           O  
ATOM    403  CB  ASP A1054       0.300  58.453  15.319  1.00 17.11           C  
ATOM    404  CG  ASP A1054       0.544  59.835  15.887  1.00 18.56           C  
ATOM    405  OD1 ASP A1054       0.871  60.755  15.107  1.00 18.14           O  
ATOM    406  OD2 ASP A1054       0.411  60.000  17.116  1.00 19.63           O  
ATOM    407  N   ALA A1055      -0.329  57.127  12.341  1.00 14.06           N  
ATOM    408  CA  ALA A1055      -0.203  55.926  11.524  1.00 14.14           C  
ATOM    409  C   ALA A1055       1.274  55.785  11.182  1.00 12.58           C  
ATOM    410  O   ALA A1055       1.830  56.615  10.460  1.00 11.54           O  
ATOM    411  CB  ALA A1055      -1.031  56.059  10.247  1.00 14.08           C  
ATOM    412  N   ASN A1056       1.911  54.741  11.707  1.00 12.82           N  
ATOM    413  CA  ASN A1056       3.334  54.524  11.466  1.00 10.88           C  
ATOM    414  C   ASN A1056       4.101  55.799  11.768  1.00 11.68           C  
ATOM    415  O   ASN A1056       4.705  56.419  10.885  1.00  9.94           O  
ATOM    416  CB  ASN A1056       3.572  54.087  10.025  1.00 11.42           C  
ATOM    417  CG  ASN A1056       3.164  52.654   9.791  1.00 11.38           C  
ATOM    418  OD1 ASN A1056       2.485  52.051  10.625  1.00 11.95           O  
ATOM    419  ND2 ASN A1056       3.570  52.096   8.657  1.00 12.06           N  
ATOM    420  N   THR A1057       4.067  56.175  13.039  1.00 11.61           N  
ATOM    421  CA  THR A1057       4.735  57.371  13.512  1.00 10.50           C  
ATOM    422  C   THR A1057       5.446  57.092  14.825  1.00 10.72           C  
ATOM    423  O   THR A1057       4.850  56.549  15.759  1.00 10.05           O  
ATOM    424  CB  THR A1057       3.728  58.511  13.784  1.00 11.29           C  
ATOM    425  OG1 THR A1057       2.934  58.746  12.617  1.00 11.77           O  
ATOM    426  CG2 THR A1057       4.469  59.792  14.167  1.00 13.22           C  
ATOM    427  N   ILE A1058       6.720  57.460  14.892  1.00  9.36           N  
ATOM    428  CA  ILE A1058       7.480  57.296  16.121  1.00  8.27           C  
ATOM    429  C   ILE A1058       7.239  58.574  16.914  1.00  9.22           C  
ATOM    430  O   ILE A1058       7.577  59.665  16.455  1.00  9.06           O  
ATOM    431  CB  ILE A1058       8.994  57.170  15.854  1.00  9.70           C  
ATOM    432  CG1 ILE A1058       9.285  55.886  15.071  1.00  9.34           C  
ATOM    433  CG2 ILE A1058       9.756  57.180  17.179  1.00  9.88           C  
ATOM    434  CD1 ILE A1058      10.744  55.723  14.667  1.00  8.19           C  
ATOM    435  N   VAL A1059       6.636  58.441  18.088  1.00  8.68           N  
ATOM    436  CA  VAL A1059       6.371  59.591  18.940  1.00 10.34           C  
ATOM    437  C   VAL A1059       7.249  59.484  20.174  1.00  8.86           C  
ATOM    438  O   VAL A1059       7.282  58.442  20.828  1.00  9.65           O  
ATOM    439  CB  VAL A1059       4.899  59.640  19.399  1.00 10.34           C  
ATOM    440  CG1 VAL A1059       4.682  60.840  20.320  1.00 12.01           C  
ATOM    441  CG2 VAL A1059       3.977  59.725  18.193  1.00 10.76           C  
ATOM    442  N   CYS A1060       7.979  60.553  20.474  1.00 10.83           N  
ATOM    443  CA  CYS A1060       8.835  60.570  21.651  1.00 10.34           C  
ATOM    444  C   CYS A1060       8.431  61.714  22.550  1.00 11.68           C  
ATOM    445  O   CYS A1060       7.932  62.743  22.092  1.00 12.58           O  
ATOM    446  CB  CYS A1060      10.307  60.732  21.268  1.00 12.54           C  
ATOM    447  SG  CYS A1060      11.041  59.275  20.507  1.00 13.50           S  
ATOM    448  N   ASN A1061       8.632  61.530  23.844  1.00 11.62           N  
ATOM    449  CA  ASN A1061       8.298  62.580  24.778  1.00 11.03           C  
ATOM    450  C   ASN A1061       9.026  62.347  26.080  1.00 11.57           C  
ATOM    451  O   ASN A1061       9.648  61.303  26.290  1.00 11.26           O  
ATOM    452  CB  ASN A1061       6.788  62.623  25.031  1.00 12.06           C  
ATOM    453  CG  ASN A1061       6.314  63.995  25.482  1.00 11.56           C  
ATOM    454  OD1 ASN A1061       7.122  64.864  25.802  1.00 11.63           O  
ATOM    455  ND2 ASN A1061       5.001  64.195  25.509  1.00 12.46           N  
ATOM    456  N   SER A1062       8.959  63.348  26.944  1.00 12.07           N  
ATOM    457  CA  SER A1062       9.573  63.277  28.248  1.00 12.40           C  
ATOM    458  C   SER A1062       8.403  63.329  29.216  1.00 13.93           C  
ATOM    459  O   SER A1062       7.279  63.665  28.831  1.00 13.36           O  
ATOM    460  CB  SER A1062      10.491  64.478  28.472  1.00 13.47           C  
ATOM    461  OG  SER A1062       9.774  65.693  28.325  1.00 12.90           O  
ATOM    462  N   LYS A1063       8.662  62.979  30.465  1.00 14.14           N  
ATOM    463  CA  LYS A1063       7.627  63.008  31.479  1.00 16.91           C  
ATOM    464  C   LYS A1063       8.300  63.528  32.730  1.00 17.01           C  
ATOM    465  O   LYS A1063       9.211  62.898  33.262  1.00 16.23           O  
ATOM    466  CB  LYS A1063       7.066  61.607  31.713  1.00 16.51           C  
ATOM    467  CG  LYS A1063       5.735  61.596  32.439  1.00 18.84           C  
ATOM    468  CD  LYS A1063       5.110  60.216  32.376  1.00 20.68           C  
ATOM    469  CE  LYS A1063       3.639  60.256  32.726  1.00 20.10           C  
ATOM    470  NZ  LYS A1063       3.018  58.918  32.547  1.00 23.68           N  
ATOM    471  N   ASP A1064       7.859  64.696  33.180  1.00 20.17           N  
ATOM    472  CA  ASP A1064       8.429  65.325  34.357  1.00 21.53           C  
ATOM    473  C   ASP A1064       7.418  65.297  35.494  1.00 22.07           C  
ATOM    474  O   ASP A1064       6.368  65.934  35.417  1.00 20.69           O  
ATOM    475  CB  ASP A1064       8.801  66.775  34.037  1.00 24.25           C  
ATOM    476  CG  ASP A1064       9.694  67.391  35.089  1.00 26.29           C  
ATOM    477  OD1 ASP A1064       9.511  67.076  36.282  1.00 26.93           O  
ATOM    478  OD2 ASP A1064      10.573  68.202  34.725  1.00 27.91           O  
ATOM    479  N   ASP A1065       7.736  64.553  36.545  1.00 22.65           N  
ATOM    480  CA  ASP A1065       6.853  64.452  37.699  1.00 24.13           C  
ATOM    481  C   ASP A1065       5.439  64.069  37.268  1.00 23.87           C  
ATOM    482  O   ASP A1065       4.458  64.596  37.795  1.00 24.68           O  
ATOM    483  CB  ASP A1065       6.811  65.788  38.445  1.00 27.28           C  
ATOM    484  CG  ASP A1065       6.365  65.637  39.890  1.00 30.35           C  
ATOM    485  OD1 ASP A1065       5.466  64.814  40.160  1.00 30.78           O  
ATOM    486  OD2 ASP A1065       6.912  66.354  40.754  1.00 32.95           O  
ATOM    487  N   GLY A1066       5.343  63.167  36.295  1.00 21.11           N  
ATOM    488  CA  GLY A1066       4.047  62.717  35.817  1.00 20.27           C  
ATOM    489  C   GLY A1066       3.430  63.516  34.680  1.00 19.05           C  
ATOM    490  O   GLY A1066       2.430  63.096  34.096  1.00 18.88           O  
ATOM    491  N   ALA A1067       4.020  64.661  34.353  1.00 19.36           N  
ATOM    492  CA  ALA A1067       3.490  65.504  33.286  1.00 19.56           C  
ATOM    493  C   ALA A1067       4.195  65.281  31.953  1.00 18.57           C  
ATOM    494  O   ALA A1067       5.417  65.387  31.864  1.00 19.01           O  
ATOM    495  CB  ALA A1067       3.596  66.971  33.684  1.00 20.11           C  
ATOM    496  N   TRP A1068       3.418  64.975  30.918  1.00 17.67           N  
ATOM    497  CA  TRP A1068       3.977  64.755  29.587  1.00 17.25           C  
ATOM    498  C   TRP A1068       4.540  66.061  29.044  1.00 17.18           C  
ATOM    499  O   TRP A1068       3.958  67.129  29.242  1.00 18.40           O  
ATOM    500  CB  TRP A1068       2.903  64.236  28.625  1.00 16.76           C  
ATOM    501  CG  TRP A1068       2.520  62.802  28.834  1.00 16.73           C  
ATOM    502  CD1 TRP A1068       1.276  62.319  29.122  1.00 17.48           C  
ATOM    503  CD2 TRP A1068       3.384  61.662  28.750  1.00 15.41           C  
ATOM    504  NE1 TRP A1068       1.311  60.949  29.223  1.00 17.47           N  
ATOM    505  CE2 TRP A1068       2.593  60.519  29.001  1.00 17.08           C  
ATOM    506  CE3 TRP A1068       4.751  61.496  28.489  1.00 15.91           C  
ATOM    507  CZ2 TRP A1068       3.123  59.222  28.997  1.00 16.52           C  
ATOM    508  CZ3 TRP A1068       5.279  60.205  28.485  1.00 15.80           C  
ATOM    509  CH2 TRP A1068       4.464  59.087  28.739  1.00 14.82           C  
ATOM    510  N   GLY A1069       5.676  65.975  28.361  1.00 16.40           N  
ATOM    511  CA  GLY A1069       6.278  67.165  27.791  1.00 16.45           C  
ATOM    512  C   GLY A1069       5.763  67.385  26.381  1.00 14.38           C  
ATOM    513  O   GLY A1069       4.683  66.909  26.028  1.00 15.32           O  
ATOM    514  N   THR A1070       6.536  68.106  25.576  1.00 15.91           N  
ATOM    515  CA  THR A1070       6.163  68.379  24.194  1.00 15.00           C  
ATOM    516  C   THR A1070       6.602  67.208  23.321  1.00 13.80           C  
ATOM    517  O   THR A1070       7.784  66.862  23.280  1.00 14.15           O  
ATOM    518  CB  THR A1070       6.838  69.663  23.688  1.00 14.99           C  
ATOM    519  OG1 THR A1070       6.494  70.752  24.557  1.00 18.16           O  
ATOM    520  CG2 THR A1070       6.382  69.983  22.268  1.00 15.21           C  
ATOM    521  N   GLU A1071       5.648  66.601  22.624  1.00 13.00           N  
ATOM    522  CA  GLU A1071       5.944  65.458  21.768  1.00 12.33           C  
ATOM    523  C   GLU A1071       6.835  65.792  20.577  1.00 12.85           C  
ATOM    524  O   GLU A1071       6.798  66.902  20.041  1.00 11.73           O  
ATOM    525  CB  GLU A1071       4.650  64.831  21.243  1.00 12.06           C  
ATOM    526  CG  GLU A1071       3.669  64.397  22.323  1.00 14.75           C  
ATOM    527  CD  GLU A1071       2.456  63.685  21.751  1.00 13.75           C  
ATOM    528  OE1 GLU A1071       1.942  64.122  20.700  1.00 13.13           O  
ATOM    529  OE2 GLU A1071       2.007  62.692  22.356  1.00 17.21           O  
ATOM    530  N   GLN A1072       7.641  64.814  20.181  1.00 10.68           N  
ATOM    531  CA  GLN A1072       8.521  64.934  19.030  1.00 10.90           C  
ATOM    532  C   GLN A1072       8.174  63.742  18.147  1.00  9.98           C  
ATOM    533  O   GLN A1072       7.982  62.633  18.647  1.00 11.63           O  
ATOM    534  CB  GLN A1072       9.997  64.871  19.445  1.00 10.53           C  
ATOM    535  CG  GLN A1072      10.965  64.968  18.260  1.00 10.25           C  
ATOM    536  CD  GLN A1072      12.423  65.031  18.681  1.00 11.24           C  
ATOM    537  OE1 GLN A1072      12.849  65.979  19.343  1.00 12.24           O  
ATOM    538  NE2 GLN A1072      13.197  64.017  18.298  1.00 11.20           N  
ATOM    539  N   ARG A1073       8.071  63.971  16.843  1.00  8.93           N  
ATOM    540  CA  ARG A1073       7.742  62.904  15.905  1.00  9.10           C  
ATOM    541  C   ARG A1073       8.825  62.787  14.841  1.00  9.98           C  
ATOM    542  O   ARG A1073       9.368  63.795  14.391  1.00  9.48           O  
ATOM    543  CB  ARG A1073       6.383  63.177  15.251  1.00 10.51           C  
ATOM    544  CG  ARG A1073       5.198  62.952  16.194  1.00 12.31           C  
ATOM    545  CD  ARG A1073       3.858  63.218  15.511  1.00 13.89           C  
ATOM    546  NE  ARG A1073       2.730  62.719  16.302  1.00 13.41           N  
ATOM    547  CZ  ARG A1073       2.396  63.174  17.506  1.00 14.87           C  
ATOM    548  NH1 ARG A1073       3.097  64.149  18.072  1.00 15.40           N  
ATOM    549  NH2 ARG A1073       1.363  62.648  18.152  1.00 16.05           N  
ATOM    550  N   GLU A1074       9.134  61.554  14.445  1.00  8.83           N  
ATOM    551  CA  GLU A1074      10.170  61.308  13.448  1.00  8.48           C  
ATOM    552  C   GLU A1074       9.627  61.155  12.037  1.00  9.32           C  
ATOM    553  O   GLU A1074       8.427  60.960  11.835  1.00  9.93           O  
ATOM    554  CB  GLU A1074      10.985  60.071  13.826  1.00  8.87           C  
ATOM    555  CG  GLU A1074      11.607  60.150  15.209  1.00  9.41           C  
ATOM    556  CD  GLU A1074      12.272  61.490  15.471  1.00 10.83           C  
ATOM    557  OE1 GLU A1074      13.080  61.928  14.628  1.00 14.37           O  
ATOM    558  OE2 GLU A1074      11.986  62.104  16.522  1.00 10.56           O  
ATOM    559  N   ALA A1075      10.532  61.231  11.066  1.00  9.00           N  
ATOM    560  CA  ALA A1075      10.179  61.144   9.654  1.00  9.18           C  
ATOM    561  C   ALA A1075      10.245  59.743   9.065  1.00  9.77           C  
ATOM    562  O   ALA A1075       9.933  59.551   7.891  1.00 10.58           O  
ATOM    563  CB  ALA A1075      11.076  62.074   8.853  1.00 10.09           C  
ATOM    564  N   VAL A1076      10.646  58.765   9.869  1.00  9.85           N  
ATOM    565  CA  VAL A1076      10.747  57.392   9.387  1.00  8.84           C  
ATOM    566  C   VAL A1076      10.082  56.424  10.359  1.00  7.57           C  
ATOM    567  O   VAL A1076       9.841  56.762  11.519  1.00  8.59           O  
ATOM    568  CB  VAL A1076      12.226  56.972   9.202  1.00  9.48           C  
ATOM    569  CG1 VAL A1076      12.924  57.921   8.238  1.00 11.66           C  
ATOM    570  CG2 VAL A1076      12.935  56.968  10.551  1.00  9.66           C  
ATOM    571  N   PHE A1077       9.777  55.223   9.880  1.00  8.24           N  
ATOM    572  CA  PHE A1077       9.148  54.212  10.719  1.00  8.61           C  
ATOM    573  C   PHE A1077       9.643  52.829  10.304  1.00  9.38           C  
ATOM    574  O   PHE A1077       8.915  52.045   9.695  1.00  9.14           O  
ATOM    575  CB  PHE A1077       7.621  54.307  10.594  1.00  8.91           C  
ATOM    576  CG  PHE A1077       6.876  53.586  11.684  1.00  8.97           C  
ATOM    577  CD1 PHE A1077       6.413  52.286  11.491  1.00  9.59           C  
ATOM    578  CD2 PHE A1077       6.652  54.204  12.913  1.00  8.70           C  
ATOM    579  CE1 PHE A1077       5.736  51.613  12.506  1.00 11.49           C  
ATOM    580  CE2 PHE A1077       5.978  53.542  13.935  1.00  9.67           C  
ATOM    581  CZ  PHE A1077       5.519  52.242  13.730  1.00  9.90           C  
ATOM    582  N   PRO A1078      10.909  52.516  10.626  1.00 11.27           N  
ATOM    583  CA  PRO A1078      11.494  51.222  10.277  1.00 11.80           C  
ATOM    584  C   PRO A1078      11.079  50.078  11.198  1.00 13.39           C  
ATOM    585  O   PRO A1078      11.926  49.359  11.724  1.00 13.12           O  
ATOM    586  CB  PRO A1078      12.992  51.503  10.328  1.00 10.73           C  
ATOM    587  CG  PRO A1078      13.096  52.471  11.446  1.00 12.06           C  
ATOM    588  CD  PRO A1078      11.930  53.414  11.198  1.00 12.17           C  
ATOM    589  N   PHE A1079       9.773  49.931  11.397  1.00 13.54           N  
ATOM    590  CA  PHE A1079       9.226  48.862  12.224  1.00 15.01           C  
ATOM    591  C   PHE A1079       8.119  48.172  11.445  1.00 17.06           C  
ATOM    592  O   PHE A1079       7.311  48.829  10.788  1.00 16.73           O  
ATOM    593  CB  PHE A1079       8.649  49.406  13.535  1.00 14.14           C  
ATOM    594  CG  PHE A1079       9.676  50.015  14.444  1.00 11.98           C  
ATOM    595  CD1 PHE A1079       9.828  51.394  14.519  1.00 11.65           C  
ATOM    596  CD2 PHE A1079      10.495  49.206  15.223  1.00 12.42           C  
ATOM    597  CE1 PHE A1079      10.784  51.961  15.357  1.00 13.33           C  
ATOM    598  CE2 PHE A1079      11.453  49.762  16.063  1.00 11.78           C  
ATOM    599  CZ  PHE A1079      11.597  51.143  16.131  1.00 11.97           C  
ATOM    600  N   GLN A1080       8.088  46.847  11.520  1.00 19.18           N  
ATOM    601  CA  GLN A1080       7.077  46.070  10.819  1.00 22.03           C  
ATOM    602  C   GLN A1080       6.493  45.013  11.747  1.00 22.54           C  
ATOM    603  O   GLN A1080       7.229  44.284  12.411  1.00 21.85           O  
ATOM    604  CB  GLN A1080       7.686  45.393   9.585  1.00 23.29           C  
ATOM    605  CG  GLN A1080       8.323  46.359   8.585  1.00 26.69           C  
ATOM    606  CD  GLN A1080       9.731  46.783   8.974  1.00 28.46           C  
ATOM    607  OE1 GLN A1080      10.240  47.798   8.494  1.00 29.34           O  
ATOM    608  NE2 GLN A1080      10.374  45.998   9.833  1.00 29.31           N  
ATOM    609  N   PRO A1081       5.155  44.930  11.820  1.00 23.61           N  
ATOM    610  CA  PRO A1081       4.513  43.935  12.685  1.00 23.27           C  
ATOM    611  C   PRO A1081       5.004  42.529  12.343  1.00 23.34           C  
ATOM    612  O   PRO A1081       5.249  42.216  11.177  1.00 22.86           O  
ATOM    613  CB  PRO A1081       3.031  44.123  12.377  1.00 24.72           C  
ATOM    614  CG  PRO A1081       2.943  45.595  12.079  1.00 25.00           C  
ATOM    615  CD  PRO A1081       4.152  45.814  11.199  1.00 24.58           C  
ATOM    616  N   GLY A1082       5.165  41.695  13.364  1.00 23.72           N  
ATOM    617  CA  GLY A1082       5.618  40.333  13.144  1.00 23.77           C  
ATOM    618  C   GLY A1082       7.081  40.188  12.765  1.00 24.60           C  
ATOM    619  O   GLY A1082       7.457  39.225  12.097  1.00 25.76           O  
ATOM    620  N   SER A1083       7.912  41.139  13.179  1.00 23.58           N  
ATOM    621  CA  SER A1083       9.335  41.072  12.869  1.00 23.09           C  
ATOM    622  C   SER A1083      10.166  41.581  14.039  1.00 21.67           C  
ATOM    623  O   SER A1083       9.701  42.398  14.833  1.00 20.64           O  
ATOM    624  CB  SER A1083       9.655  41.900  11.623  1.00 25.10           C  
ATOM    625  OG  SER A1083       9.546  43.285  11.894  1.00 29.60           O  
ATOM    626  N   VAL A1084      11.395  41.088  14.141  1.00 20.34           N  
ATOM    627  CA  VAL A1084      12.292  41.506  15.209  1.00 19.72           C  
ATOM    628  C   VAL A1084      12.829  42.893  14.881  1.00 18.58           C  
ATOM    629  O   VAL A1084      13.088  43.211  13.720  1.00 18.82           O  
ATOM    630  CB  VAL A1084      13.482  40.531  15.355  1.00 20.30           C  
ATOM    631  CG1 VAL A1084      14.418  41.004  16.462  1.00 20.30           C  
ATOM    632  CG2 VAL A1084      12.969  39.132  15.656  1.00 21.81           C  
ATOM    633  N   ALA A1085      12.987  43.717  15.909  1.00 17.40           N  
ATOM    634  CA  ALA A1085      13.495  45.067  15.733  1.00 16.69           C  
ATOM    635  C   ALA A1085      14.421  45.397  16.889  1.00 16.29           C  
ATOM    636  O   ALA A1085      14.137  45.062  18.039  1.00 16.25           O  
ATOM    637  CB  ALA A1085      12.342  46.061  15.692  1.00 16.05           C  
ATOM    638  N   GLU A1086      15.532  46.049  16.579  1.00 15.89           N  
ATOM    639  CA  GLU A1086      16.485  46.428  17.604  1.00 14.35           C  
ATOM    640  C   GLU A1086      16.641  47.939  17.632  1.00 14.65           C  
ATOM    641  O   GLU A1086      16.709  48.584  16.588  1.00 13.27           O  
ATOM    642  CB  GLU A1086      17.835  45.771  17.335  1.00 15.54           C  
ATOM    643  CG  GLU A1086      18.904  46.107  18.356  1.00 18.41           C  
ATOM    644  CD  GLU A1086      20.160  45.290  18.150  1.00 21.35           C  
ATOM    645  OE1 GLU A1086      20.120  44.068  18.402  1.00 22.73           O  
ATOM    646  OE2 GLU A1086      21.180  45.868  17.725  1.00 23.51           O  
ATOM    647  N   VAL A1087      16.678  48.498  18.834  1.00 14.31           N  
ATOM    648  CA  VAL A1087      16.848  49.932  19.006  1.00 15.16           C  
ATOM    649  C   VAL A1087      18.041  50.148  19.929  1.00 15.05           C  
ATOM    650  O   VAL A1087      18.226  49.408  20.893  1.00 14.63           O  
ATOM    651  CB  VAL A1087      15.593  50.571  19.632  1.00 15.84           C  
ATOM    652  CG1 VAL A1087      15.797  52.064  19.810  1.00 19.60           C  
ATOM    653  CG2 VAL A1087      14.382  50.307  18.744  1.00 17.53           C  
ATOM    654  N   CYS A1088      18.860  51.145  19.611  1.00 14.20           N  
ATOM    655  CA  CYS A1088      20.030  51.466  20.417  1.00 14.71           C  
ATOM    656  C   CYS A1088      19.890  52.892  20.911  1.00 15.16           C  
ATOM    657  O   CYS A1088      19.759  53.823  20.116  1.00 15.18           O  
ATOM    658  CB  CYS A1088      21.312  51.303  19.603  1.00 18.15           C  
ATOM    659  SG  CYS A1088      21.578  49.617  19.026  1.00 22.95           S  
ATOM    660  N   ILE A1089      19.910  53.057  22.228  1.00 14.17           N  
ATOM    661  CA  ILE A1089      19.761  54.372  22.827  1.00 13.72           C  
ATOM    662  C   ILE A1089      20.993  54.757  23.628  1.00 14.45           C  
ATOM    663  O   ILE A1089      21.414  54.044  24.540  1.00 13.02           O  
ATOM    664  CB  ILE A1089      18.518  54.409  23.735  1.00 14.32           C  
ATOM    665  CG1 ILE A1089      17.290  53.998  22.915  1.00 15.75           C  
ATOM    666  CG2 ILE A1089      18.326  55.807  24.320  1.00 14.57           C  
ATOM    667  CD1 ILE A1089      16.028  53.827  23.723  1.00 18.54           C  
ATOM    668  N   THR A1090      21.581  55.888  23.265  1.00 15.19           N  
ATOM    669  CA  THR A1090      22.758  56.368  23.961  1.00 17.39           C  
ATOM    670  C   THR A1090      22.362  57.564  24.801  1.00 17.94           C  
ATOM    671  O   THR A1090      21.653  58.463  24.341  1.00 17.75           O  
ATOM    672  CB  THR A1090      23.866  56.766  22.980  1.00 18.28           C  
ATOM    673  OG1 THR A1090      24.177  55.646  22.143  1.00 18.64           O  
ATOM    674  CG2 THR A1090      25.121  57.186  23.739  1.00 20.20           C  
ATOM    675  N   PHE A1091      22.814  57.556  26.046  1.00 19.97           N  
ATOM    676  CA  PHE A1091      22.504  58.620  26.978  1.00 22.11           C  
ATOM    677  C   PHE A1091      23.636  59.631  27.092  1.00 23.30           C  
ATOM    678  O   PHE A1091      24.797  59.263  27.254  1.00 23.18           O  
ATOM    679  CB  PHE A1091      22.212  58.025  28.357  1.00 21.29           C  
ATOM    680  CG  PHE A1091      21.966  59.053  29.418  1.00 23.59           C  
ATOM    681  CD1 PHE A1091      22.643  58.990  30.630  1.00 24.69           C  
ATOM    682  CD2 PHE A1091      21.056  60.082  29.210  1.00 24.72           C  
ATOM    683  CE1 PHE A1091      22.417  59.938  31.621  1.00 24.83           C  
ATOM    684  CE2 PHE A1091      20.822  61.037  30.196  1.00 25.80           C  
ATOM    685  CZ  PHE A1091      21.505  60.964  31.404  1.00 25.37           C  
ATOM    686  N   ASP A1092      23.281  60.906  27.000  1.00 25.27           N  
ATOM    687  CA  ASP A1092      24.240  61.993  27.128  1.00 27.70           C  
ATOM    688  C   ASP A1092      23.567  63.099  27.929  1.00 27.46           C  
ATOM    689  O   ASP A1092      22.341  63.150  28.009  1.00 27.71           O  
ATOM    690  CB  ASP A1092      24.672  62.500  25.750  1.00 31.20           C  
ATOM    691  CG  ASP A1092      25.707  61.597  25.099  1.00 35.03           C  
ATOM    692  OD1 ASP A1092      26.768  61.367  25.720  1.00 37.61           O  
ATOM    693  OD2 ASP A1092      25.465  61.120  23.969  1.00 37.74           O  
ATOM    694  N   GLN A1093      24.359  63.979  28.528  1.00 27.80           N  
ATOM    695  CA  GLN A1093      23.799  65.051  29.343  1.00 28.21           C  
ATOM    696  C   GLN A1093      22.869  65.995  28.585  1.00 26.94           C  
ATOM    697  O   GLN A1093      21.834  66.407  29.109  1.00 27.03           O  
ATOM    698  CB  GLN A1093      24.919  65.859  30.002  1.00 30.75           C  
ATOM    699  CG  GLN A1093      24.415  66.912  30.979  1.00 34.69           C  
ATOM    700  CD  GLN A1093      23.662  66.313  32.159  1.00 36.33           C  
ATOM    701  OE1 GLN A1093      23.058  67.035  32.954  1.00 39.12           O  
ATOM    702  NE2 GLN A1093      23.700  64.989  32.279  1.00 37.39           N  
ATOM    703  N   ALA A1094      23.234  66.334  27.355  1.00 25.38           N  
ATOM    704  CA  ALA A1094      22.426  67.244  26.551  1.00 23.51           C  
ATOM    705  C   ALA A1094      21.277  66.549  25.824  1.00 22.44           C  
ATOM    706  O   ALA A1094      20.155  67.056  25.792  1.00 21.33           O  
ATOM    707  CB  ALA A1094      23.311  67.963  25.546  1.00 24.59           C  
ATOM    708  N   ASN A1095      21.555  65.388  25.243  1.00 20.81           N  
ATOM    709  CA  ASN A1095      20.536  64.656  24.498  1.00 20.49           C  
ATOM    710  C   ASN A1095      20.725  63.151  24.561  1.00 18.25           C  
ATOM    711  O   ASN A1095      21.779  62.649  24.952  1.00 20.17           O  
ATOM    712  CB  ASN A1095      20.580  65.040  23.014  1.00 21.73           C  
ATOM    713  CG  ASN A1095      20.259  66.495  22.767  1.00 24.25           C  
ATOM    714  OD1 ASN A1095      19.102  66.906  22.825  1.00 27.18           O  
ATOM    715  ND2 ASN A1095      21.287  67.285  22.484  1.00 26.05           N  
ATOM    716  N   LEU A1096      19.680  62.438  24.168  1.00 16.68           N  
ATOM    717  CA  LEU A1096      19.744  60.994  24.077  1.00 14.11           C  
ATOM    718  C   LEU A1096      19.775  60.786  22.575  1.00 13.21           C  
ATOM    719  O   LEU A1096      19.145  61.542  21.833  1.00 13.47           O  
ATOM    720  CB  LEU A1096      18.493  60.327  24.651  1.00 15.72           C  
ATOM    721  CG  LEU A1096      18.305  60.303  26.167  1.00 15.55           C  
ATOM    722  CD1 LEU A1096      17.475  61.491  26.604  1.00 17.35           C  
ATOM    723  CD2 LEU A1096      17.613  59.008  26.560  1.00 16.12           C  
ATOM    724  N   THR A1097      20.525  59.794  22.118  1.00 11.23           N  
ATOM    725  CA  THR A1097      20.586  59.509  20.696  1.00 12.02           C  
ATOM    726  C   THR A1097      19.936  58.152  20.481  1.00 12.39           C  
ATOM    727  O   THR A1097      20.273  57.181  21.157  1.00 14.36           O  
ATOM    728  CB  THR A1097      22.037  59.461  20.183  1.00 13.49           C  
ATOM    729  OG1 THR A1097      22.655  60.740  20.376  1.00 14.84           O  
ATOM    730  CG2 THR A1097      22.061  59.111  18.701  1.00 14.44           C  
ATOM    731  N   VAL A1098      18.986  58.093  19.558  1.00 10.59           N  
ATOM    732  CA  VAL A1098      18.303  56.844  19.268  1.00 10.86           C  
ATOM    733  C   VAL A1098      18.669  56.362  17.874  1.00 11.11           C  
ATOM    734  O   VAL A1098      18.580  57.120  16.903  1.00 10.85           O  
ATOM    735  CB  VAL A1098      16.767  57.017  19.340  1.00 10.05           C  
ATOM    736  CG1 VAL A1098      16.075  55.694  19.025  1.00 10.16           C  
ATOM    737  CG2 VAL A1098      16.365  57.517  20.718  1.00 11.61           C  
ATOM    738  N   LYS A1099      19.105  55.110  17.777  1.00  9.87           N  
ATOM    739  CA  LYS A1099      19.442  54.537  16.482  1.00 10.57           C  
ATOM    740  C   LYS A1099      18.399  53.468  16.205  1.00 11.47           C  
ATOM    741  O   LYS A1099      18.242  52.519  16.978  1.00 10.63           O  
ATOM    742  CB  LYS A1099      20.845  53.916  16.477  1.00 12.98           C  
ATOM    743  CG  LYS A1099      21.214  53.323  15.119  1.00 14.54           C  
ATOM    744  CD  LYS A1099      22.603  52.698  15.099  1.00 20.09           C  
ATOM    745  CE  LYS A1099      23.695  53.754  15.124  1.00 22.73           C  
ATOM    746  NZ  LYS A1099      25.048  53.150  14.943  1.00 25.83           N  
ATOM    747  N   LEU A1100      17.673  53.644  15.108  1.00 10.21           N  
ATOM    748  CA  LEU A1100      16.612  52.727  14.717  1.00 10.72           C  
ATOM    749  C   LEU A1100      17.135  51.494  13.985  1.00 11.27           C  
ATOM    750  O   LEU A1100      18.308  51.432  13.614  1.00 11.52           O  
ATOM    751  CB  LEU A1100      15.597  53.479  13.849  1.00  8.98           C  
ATOM    752  CG  LEU A1100      14.942  54.667  14.565  1.00 10.84           C  
ATOM    753  CD1 LEU A1100      13.935  55.339  13.640  1.00 10.37           C  
ATOM    754  CD2 LEU A1100      14.255  54.186  15.837  1.00 10.37           C  
ATOM    755  N   PRO A1101      16.266  50.489  13.776  1.00 13.74           N  
ATOM    756  CA  PRO A1101      16.626  49.244  13.091  1.00 13.32           C  
ATOM    757  C   PRO A1101      17.363  49.421  11.768  1.00 14.00           C  
ATOM    758  O   PRO A1101      18.255  48.639  11.451  1.00 14.85           O  
ATOM    759  CB  PRO A1101      15.279  48.553  12.907  1.00 13.70           C  
ATOM    760  CG  PRO A1101      14.539  48.957  14.128  1.00 16.49           C  
ATOM    761  CD  PRO A1101      14.865  50.434  14.239  1.00 13.27           C  
ATOM    762  N   ASP A1102      17.002  50.443  10.998  1.00 12.89           N  
ATOM    763  CA  ASP A1102      17.649  50.655   9.707  1.00 12.30           C  
ATOM    764  C   ASP A1102      18.840  51.607   9.726  1.00 12.90           C  
ATOM    765  O   ASP A1102      19.352  51.983   8.671  1.00 12.88           O  
ATOM    766  CB  ASP A1102      16.624  51.133   8.676  1.00 13.13           C  
ATOM    767  CG  ASP A1102      16.076  52.507   8.986  1.00 14.58           C  
ATOM    768  OD1 ASP A1102      16.297  53.012  10.107  1.00 12.16           O  
ATOM    769  OD2 ASP A1102      15.410  53.081   8.101  1.00 17.06           O  
ATOM    770  N   GLY A1103      19.279  51.996  10.920  1.00 12.89           N  
ATOM    771  CA  GLY A1103      20.426  52.881  11.030  1.00 12.35           C  
ATOM    772  C   GLY A1103      20.094  54.353  11.172  1.00 10.95           C  
ATOM    773  O   GLY A1103      20.971  55.171  11.457  1.00  9.83           O  
ATOM    774  N   TYR A1104      18.833  54.706  10.955  1.00 11.01           N  
ATOM    775  CA  TYR A1104      18.425  56.095  11.085  1.00 10.86           C  
ATOM    776  C   TYR A1104      18.616  56.505  12.538  1.00 11.08           C  
ATOM    777  O   TYR A1104      18.223  55.779  13.450  1.00 12.35           O  
ATOM    778  CB  TYR A1104      16.954  56.265  10.707  1.00 11.18           C  
ATOM    779  CG  TYR A1104      16.513  57.711  10.644  1.00 12.06           C  
ATOM    780  CD1 TYR A1104      16.743  58.478   9.504  1.00 13.93           C  
ATOM    781  CD2 TYR A1104      15.851  58.308  11.719  1.00 11.86           C  
ATOM    782  CE1 TYR A1104      16.320  59.805   9.428  1.00 13.66           C  
ATOM    783  CE2 TYR A1104      15.424  59.634  11.656  1.00 13.14           C  
ATOM    784  CZ  TYR A1104      15.659  60.374  10.505  1.00 13.77           C  
ATOM    785  OH  TYR A1104      15.217  61.675  10.425  1.00 13.88           O  
ATOM    786  N   GLU A1105      19.224  57.666  12.749  1.00 11.29           N  
ATOM    787  CA  GLU A1105      19.458  58.168  14.099  1.00 13.18           C  
ATOM    788  C   GLU A1105      18.786  59.518  14.306  1.00 12.56           C  
ATOM    789  O   GLU A1105      18.660  60.306  13.373  1.00 13.78           O  
ATOM    790  CB  GLU A1105      20.955  58.346  14.359  1.00 17.17           C  
ATOM    791  CG  GLU A1105      21.750  57.067  14.515  1.00 22.79           C  
ATOM    792  CD  GLU A1105      23.232  57.341  14.688  1.00 26.36           C  
ATOM    793  OE1 GLU A1105      23.865  57.811  13.719  1.00 29.55           O  
ATOM    794  OE2 GLU A1105      23.760  57.097  15.793  1.00 29.19           O  
ATOM    795  N   PHE A1106      18.343  59.771  15.531  1.00 11.09           N  
ATOM    796  CA  PHE A1106      17.746  61.052  15.868  1.00 10.00           C  
ATOM    797  C   PHE A1106      18.031  61.303  17.337  1.00 11.74           C  
ATOM    798  O   PHE A1106      18.336  60.373  18.086  1.00 12.59           O  
ATOM    799  CB  PHE A1106      16.235  61.084  15.581  1.00 10.29           C  
ATOM    800  CG  PHE A1106      15.413  60.177  16.455  1.00 10.33           C  
ATOM    801  CD1 PHE A1106      15.178  58.857  16.087  1.00  8.54           C  
ATOM    802  CD2 PHE A1106      14.852  60.655  17.635  1.00  9.37           C  
ATOM    803  CE1 PHE A1106      14.392  58.023  16.882  1.00 11.31           C  
ATOM    804  CE2 PHE A1106      14.067  59.830  18.436  1.00 10.21           C  
ATOM    805  CZ  PHE A1106      13.837  58.510  18.055  1.00 10.34           C  
ATOM    806  N   LYS A1107      17.965  62.561  17.747  1.00 11.77           N  
ATOM    807  CA  LYS A1107      18.234  62.894  19.133  1.00 11.41           C  
ATOM    808  C   LYS A1107      16.998  63.445  19.820  1.00 12.01           C  
ATOM    809  O   LYS A1107      16.094  63.971  19.172  1.00 10.93           O  
ATOM    810  CB  LYS A1107      19.370  63.917  19.213  1.00 15.13           C  
ATOM    811  CG  LYS A1107      20.695  63.407  18.670  1.00 16.20           C  
ATOM    812  CD  LYS A1107      21.760  64.496  18.698  1.00 20.76           C  
ATOM    813  CE  LYS A1107      23.071  64.000  18.113  1.00 21.71           C  
ATOM    814  NZ  LYS A1107      23.667  62.885  18.904  1.00 24.27           N  
ATOM    815  N   PHE A1108      16.963  63.303  21.138  1.00 11.98           N  
ATOM    816  CA  PHE A1108      15.861  63.813  21.935  1.00 12.14           C  
ATOM    817  C   PHE A1108      16.524  64.517  23.107  1.00 12.43           C  
ATOM    818  O   PHE A1108      17.377  63.942  23.783  1.00 13.72           O  
ATOM    819  CB  PHE A1108      14.965  62.680  22.440  1.00 12.49           C  
ATOM    820  CG  PHE A1108      13.681  63.160  23.061  1.00 11.51           C  
ATOM    821  CD1 PHE A1108      12.685  63.735  22.273  1.00 12.78           C  
ATOM    822  CD2 PHE A1108      13.475  63.060  24.432  1.00 12.28           C  
ATOM    823  CE1 PHE A1108      11.500  64.203  22.845  1.00 12.73           C  
ATOM    824  CE2 PHE A1108      12.293  63.525  25.016  1.00 12.83           C  
ATOM    825  CZ  PHE A1108      11.305  64.099  24.221  1.00 12.96           C  
ATOM    826  N   PRO A1109      16.143  65.774  23.362  1.00 13.71           N  
ATOM    827  CA  PRO A1109      16.725  66.547  24.461  1.00 15.24           C  
ATOM    828  C   PRO A1109      16.517  65.949  25.847  1.00 14.61           C  
ATOM    829  O   PRO A1109      15.446  65.427  26.156  1.00 14.91           O  
ATOM    830  CB  PRO A1109      16.052  67.907  24.310  1.00 16.52           C  
ATOM    831  CG  PRO A1109      14.687  67.530  23.820  1.00 17.43           C  
ATOM    832  CD  PRO A1109      15.017  66.505  22.752  1.00 15.79           C  
ATOM    833  N   ASN A1110      17.560  66.024  26.669  1.00 15.32           N  
ATOM    834  CA  ASN A1110      17.509  65.528  28.038  1.00 15.95           C  
ATOM    835  C   ASN A1110      16.899  66.644  28.887  1.00 16.83           C  
ATOM    836  O   ASN A1110      17.579  67.274  29.699  1.00 17.79           O  
ATOM    837  CB  ASN A1110      18.924  65.184  28.520  1.00 16.76           C  
ATOM    838  CG  ASN A1110      18.946  64.642  29.935  1.00 18.31           C  
ATOM    839  OD1 ASN A1110      17.913  64.265  30.487  1.00 19.26           O  
ATOM    840  ND2 ASN A1110      20.134  64.587  30.527  1.00 20.17           N  
ATOM    841  N   ARG A1111      15.606  66.877  28.676  1.00 16.39           N  
ATOM    842  CA  ARG A1111      14.853  67.925  29.365  1.00 17.96           C  
ATOM    843  C   ARG A1111      14.893  67.871  30.888  1.00 18.70           C  
ATOM    844  O   ARG A1111      14.927  68.913  31.545  1.00 19.66           O  
ATOM    845  CB  ARG A1111      13.396  67.895  28.901  1.00 16.99           C  
ATOM    846  CG  ARG A1111      13.214  68.157  27.413  1.00 17.05           C  
ATOM    847  CD  ARG A1111      11.784  67.873  27.000  1.00 16.89           C  
ATOM    848  NE  ARG A1111      11.523  68.211  25.605  1.00 16.13           N  
ATOM    849  CZ  ARG A1111      10.467  67.771  24.927  1.00 16.05           C  
ATOM    850  NH1 ARG A1111       9.587  66.977  25.517  1.00 14.90           N  
ATOM    851  NH2 ARG A1111      10.287  68.126  23.665  1.00 15.14           N  
ATOM    852  N   LEU A1112      14.873  66.665  31.445  1.00 19.42           N  
ATOM    853  CA  LEU A1112      14.904  66.490  32.895  1.00 20.28           C  
ATOM    854  C   LEU A1112      16.311  66.651  33.467  1.00 20.34           C  
ATOM    855  O   LEU A1112      16.497  66.643  34.685  1.00 19.46           O  
ATOM    856  CB  LEU A1112      14.350  65.113  33.273  1.00 20.58           C  
ATOM    857  CG  LEU A1112      12.833  64.907  33.259  1.00 21.55           C  
ATOM    858  CD1 LEU A1112      12.243  65.339  31.928  1.00 23.33           C  
ATOM    859  CD2 LEU A1112      12.531  63.440  33.535  1.00 21.43           C  
ATOM    860  N   ASN A1113      17.296  66.794  32.585  1.00 19.79           N  
ATOM    861  CA  ASN A1113      18.686  66.960  32.993  1.00 21.46           C  
ATOM    862  C   ASN A1113      19.190  65.810  33.856  1.00 22.04           C  
ATOM    863  O   ASN A1113      19.946  66.018  34.803  1.00 20.88           O  
ATOM    864  CB  ASN A1113      18.862  68.278  33.749  1.00 23.59           C  
ATOM    865  CG  ASN A1113      18.500  69.480  32.904  1.00 26.31           C  
ATOM    866  OD1 ASN A1113      19.061  69.685  31.828  1.00 26.91           O  
ATOM    867  ND2 ASN A1113      17.558  70.282  33.387  1.00 27.52           N  
ATOM    868  N   LEU A1114      18.762  64.595  33.527  1.00 21.23           N  
ATOM    869  CA  LEU A1114      19.191  63.415  34.263  1.00 21.68           C  
ATOM    870  C   LEU A1114      20.686  63.219  34.065  1.00 21.89           C  
ATOM    871  O   LEU A1114      21.216  63.494  32.989  1.00 20.62           O  
ATOM    872  CB  LEU A1114      18.442  62.178  33.761  1.00 22.34           C  
ATOM    873  CG  LEU A1114      17.154  61.768  34.480  1.00 24.31           C  
ATOM    874  CD1 LEU A1114      16.296  62.979  34.784  1.00 23.87           C  
ATOM    875  CD2 LEU A1114      16.405  60.762  33.619  1.00 24.65           C  
ATOM    876  N   GLU A1115      21.365  62.750  35.106  1.00 22.27           N  
ATOM    877  CA  GLU A1115      22.798  62.507  35.028  1.00 23.52           C  
ATOM    878  C   GLU A1115      23.038  61.014  34.860  1.00 21.76           C  
ATOM    879  O   GLU A1115      24.169  60.565  34.688  1.00 22.24           O  
ATOM    880  CB  GLU A1115      23.492  63.017  36.293  1.00 26.54           C  
ATOM    881  CG  GLU A1115      23.423  64.528  36.453  1.00 30.68           C  
ATOM    882  CD  GLU A1115      24.100  65.017  37.716  1.00 32.90           C  
ATOM    883  OE1 GLU A1115      24.169  66.250  37.914  1.00 35.91           O  
ATOM    884  OE2 GLU A1115      24.561  64.172  38.513  1.00 34.82           O  
ATOM    885  N   ALA A1116      21.954  60.250  34.910  1.00 20.59           N  
ATOM    886  CA  ALA A1116      22.031  58.807  34.756  1.00 19.31           C  
ATOM    887  C   ALA A1116      20.636  58.244  34.556  1.00 18.29           C  
ATOM    888  O   ALA A1116      19.648  58.831  34.996  1.00 17.96           O  
ATOM    889  CB  ALA A1116      22.674  58.181  35.987  1.00 20.40           C  
ATOM    890  N   ILE A1117      20.560  57.112  33.869  1.00 18.09           N  
ATOM    891  CA  ILE A1117      19.286  56.451  33.631  1.00 18.26           C  
ATOM    892  C   ILE A1117      19.257  55.211  34.516  1.00 18.03           C  
ATOM    893  O   ILE A1117      20.121  54.344  34.402  1.00 19.48           O  
ATOM    894  CB  ILE A1117      19.136  56.042  32.147  1.00 17.15           C  
ATOM    895  CG1 ILE A1117      19.045  57.300  31.275  1.00 18.48           C  
ATOM    896  CG2 ILE A1117      17.899  55.171  31.966  1.00 18.25           C  
ATOM    897  CD1 ILE A1117      18.963  57.021  29.783  1.00 18.88           C  
ATOM    898  N   ASN A1118      18.277  55.138  35.410  1.00 17.96           N  
ATOM    899  CA  ASN A1118      18.171  53.998  36.316  1.00 19.00           C  
ATOM    900  C   ASN A1118      16.919  53.168  36.100  1.00 17.81           C  
ATOM    901  O   ASN A1118      16.777  52.092  36.677  1.00 17.95           O  
ATOM    902  CB  ASN A1118      18.189  54.465  37.771  1.00 21.97           C  
ATOM    903  CG  ASN A1118      19.534  55.005  38.193  1.00 25.67           C  
ATOM    904  OD1 ASN A1118      19.829  56.186  38.017  1.00 28.04           O  
ATOM    905  ND2 ASN A1118      20.369  54.132  38.744  1.00 27.37           N  
ATOM    906  N   TYR A1119      16.018  53.664  35.263  1.00 16.56           N  
ATOM    907  CA  TYR A1119      14.760  52.978  35.018  1.00 15.09           C  
ATOM    908  C   TYR A1119      14.470  52.721  33.544  1.00 15.02           C  
ATOM    909  O   TYR A1119      14.667  53.592  32.699  1.00 12.99           O  
ATOM    910  CB  TYR A1119      13.630  53.810  35.625  1.00 14.77           C  
ATOM    911  CG  TYR A1119      12.239  53.300  35.346  1.00 14.28           C  
ATOM    912  CD1 TYR A1119      11.648  52.336  36.162  1.00 14.62           C  
ATOM    913  CD2 TYR A1119      11.497  53.808  34.280  1.00 14.18           C  
ATOM    914  CE1 TYR A1119      10.346  51.894  35.922  1.00 15.08           C  
ATOM    915  CE2 TYR A1119      10.204  53.373  34.033  1.00 14.30           C  
ATOM    916  CZ  TYR A1119       9.633  52.421  34.856  1.00 14.71           C  
ATOM    917  OH  TYR A1119       8.346  52.011  34.615  1.00 14.94           O  
ATOM    918  N   MET A1120      14.000  51.514  33.248  1.00 14.72           N  
ATOM    919  CA  MET A1120      13.640  51.135  31.889  1.00 15.81           C  
ATOM    920  C   MET A1120      12.417  50.237  31.958  1.00 16.28           C  
ATOM    921  O   MET A1120      12.356  49.323  32.779  1.00 17.33           O  
ATOM    922  CB  MET A1120      14.768  50.369  31.198  1.00 18.20           C  
ATOM    923  CG  MET A1120      14.378  49.897  29.800  1.00 23.40           C  
ATOM    924  SD  MET A1120      15.388  48.549  29.166  1.00 29.76           S  
ATOM    925  CE  MET A1120      14.440  47.148  29.703  1.00 30.23           C  
ATOM    926  N   ALA A1121      11.445  50.497  31.093  1.00 15.61           N  
ATOM    927  CA  ALA A1121      10.232  49.697  31.068  1.00 14.36           C  
ATOM    928  C   ALA A1121       9.754  49.539  29.638  1.00 15.09           C  
ATOM    929  O   ALA A1121       9.834  50.474  28.839  1.00 14.81           O  
ATOM    930  CB  ALA A1121       9.151  50.355  31.908  1.00 15.97           C  
ATOM    931  N   ALA A1122       9.277  48.343  29.317  1.00 12.84           N  
ATOM    932  CA  ALA A1122       8.765  48.053  27.989  1.00 13.95           C  
ATOM    933  C   ALA A1122       7.275  47.798  28.132  1.00 14.02           C  
ATOM    934  O   ALA A1122       6.825  47.268  29.144  1.00 14.05           O  
ATOM    935  CB  ALA A1122       9.455  46.826  27.410  1.00 14.66           C  
ATOM    936  N   ASP A1123       6.506  48.186  27.125  1.00 15.60           N  
ATOM    937  CA  ASP A1123       5.070  47.979  27.166  1.00 17.94           C  
ATOM    938  C   ASP A1123       4.535  47.977  25.742  1.00 18.84           C  
ATOM    939  O   ASP A1123       5.224  48.393  24.814  1.00 18.91           O  
ATOM    940  CB  ASP A1123       4.410  49.082  27.996  1.00 21.28           C  
ATOM    941  CG  ASP A1123       2.945  48.807  28.278  1.00 25.74           C  
ATOM    942  OD1 ASP A1123       2.599  47.641  28.567  1.00 27.86           O  
ATOM    943  OD2 ASP A1123       2.142  49.763  28.227  1.00 28.79           O  
ATOM    944  N   GLY A1124       3.315  47.490  25.566  1.00 20.04           N  
ATOM    945  CA  GLY A1124       2.748  47.454  24.235  1.00 20.04           C  
ATOM    946  C   GLY A1124       3.032  46.155  23.510  1.00 20.22           C  
ATOM    947  O   GLY A1124       3.390  45.150  24.121  1.00 19.57           O  
ATOM    948  N   ASP A1125       2.896  46.189  22.190  1.00 20.57           N  
ATOM    949  CA  ASP A1125       3.095  45.009  21.362  1.00 21.95           C  
ATOM    950  C   ASP A1125       4.543  44.772  20.943  1.00 21.73           C  
ATOM    951  O   ASP A1125       4.852  44.668  19.754  1.00 20.88           O  
ATOM    952  CB  ASP A1125       2.191  45.121  20.137  1.00 23.78           C  
ATOM    953  CG  ASP A1125       0.793  45.583  20.502  1.00 26.99           C  
ATOM    954  OD1 ASP A1125       0.217  45.016  21.454  1.00 26.92           O  
ATOM    955  OD2 ASP A1125       0.272  46.511  19.846  1.00 28.68           O  
ATOM    956  N   PHE A1126       5.421  44.666  21.935  1.00 21.27           N  
ATOM    957  CA  PHE A1126       6.845  44.444  21.700  1.00 22.05           C  
ATOM    958  C   PHE A1126       7.370  43.472  22.757  1.00 22.29           C  
ATOM    959  O   PHE A1126       7.433  43.806  23.940  1.00 24.13           O  
ATOM    960  CB  PHE A1126       7.590  45.780  21.796  1.00 20.65           C  
ATOM    961  CG  PHE A1126       9.024  45.724  21.346  1.00 20.18           C  
ATOM    962  CD1 PHE A1126       9.345  45.395  20.032  1.00 19.87           C  
ATOM    963  CD2 PHE A1126      10.053  46.058  22.222  1.00 20.36           C  
ATOM    964  CE1 PHE A1126      10.668  45.403  19.596  1.00 19.80           C  
ATOM    965  CE2 PHE A1126      11.379  46.070  21.796  1.00 20.44           C  
ATOM    966  CZ  PHE A1126      11.687  45.743  20.480  1.00 19.17           C  
ATOM    967  N   LYS A1127       7.737  42.268  22.330  1.00 22.30           N  
ATOM    968  CA  LYS A1127       8.250  41.257  23.254  1.00 23.51           C  
ATOM    969  C   LYS A1127       9.773  41.318  23.292  1.00 21.34           C  
ATOM    970  O   LYS A1127      10.438  40.902  22.345  1.00 21.47           O  
ATOM    971  CB  LYS A1127       7.797  39.862  22.809  1.00 24.55           C  
ATOM    972  CG  LYS A1127       8.253  38.722  23.717  1.00 28.10           C  
ATOM    973  CD  LYS A1127       7.595  38.790  25.085  1.00 32.00           C  
ATOM    974  CE  LYS A1127       8.017  37.618  25.963  1.00 33.78           C  
ATOM    975  NZ  LYS A1127       7.703  36.304  25.331  1.00 36.36           N  
ATOM    976  N   ILE A1128      10.320  41.838  24.386  1.00 20.72           N  
ATOM    977  CA  ILE A1128      11.768  41.958  24.527  1.00 19.79           C  
ATOM    978  C   ILE A1128      12.469  40.606  24.490  1.00 19.47           C  
ATOM    979  O   ILE A1128      12.103  39.677  25.214  1.00 19.63           O  
ATOM    980  CB  ILE A1128      12.144  42.693  25.838  1.00 20.89           C  
ATOM    981  CG1 ILE A1128      11.718  44.163  25.745  1.00 21.74           C  
ATOM    982  CG2 ILE A1128      13.646  42.590  26.092  1.00 18.95           C  
ATOM    983  CD1 ILE A1128      12.176  45.019  26.909  1.00 24.16           C  
ATOM    984  N   LYS A1129      13.479  40.500  23.634  1.00 17.55           N  
ATOM    985  CA  LYS A1129      14.237  39.265  23.506  1.00 18.21           C  
ATOM    986  C   LYS A1129      15.606  39.407  24.159  1.00 16.47           C  
ATOM    987  O   LYS A1129      16.188  38.425  24.614  1.00 15.01           O  
ATOM    988  CB  LYS A1129      14.395  38.883  22.033  1.00 21.19           C  
ATOM    989  CG  LYS A1129      13.074  38.610  21.313  1.00 25.69           C  
ATOM    990  CD  LYS A1129      12.181  37.644  22.093  1.00 30.09           C  
ATOM    991  CE  LYS A1129      12.880  36.327  22.403  1.00 32.33           C  
ATOM    992  NZ  LYS A1129      13.301  35.595  21.178  1.00 35.29           N  
ATOM    993  N   CYS A1130      16.122  40.631  24.196  1.00 15.23           N  
ATOM    994  CA  CYS A1130      17.411  40.869  24.831  1.00 17.09           C  
ATOM    995  C   CYS A1130      17.639  42.346  25.076  1.00 15.51           C  
ATOM    996  O   CYS A1130      17.150  43.201  24.337  1.00 13.82           O  
ATOM    997  CB  CYS A1130      18.579  40.308  24.013  1.00 21.15           C  
ATOM    998  SG  CYS A1130      18.905  41.102  22.421  1.00 27.52           S  
ATOM    999  N   VAL A1131      18.382  42.632  26.136  1.00 14.09           N  
ATOM   1000  CA  VAL A1131      18.721  43.998  26.488  1.00 13.77           C  
ATOM   1001  C   VAL A1131      20.188  43.980  26.885  1.00 13.78           C  
ATOM   1002  O   VAL A1131      20.617  43.124  27.658  1.00 13.40           O  
ATOM   1003  CB  VAL A1131      17.889  44.514  27.682  1.00 14.66           C  
ATOM   1004  CG1 VAL A1131      18.316  45.932  28.027  1.00 15.24           C  
ATOM   1005  CG2 VAL A1131      16.403  44.485  27.343  1.00 13.62           C  
ATOM   1006  N   ALA A1132      20.954  44.915  26.338  1.00 14.82           N  
ATOM   1007  CA  ALA A1132      22.369  45.016  26.644  1.00 15.33           C  
ATOM   1008  C   ALA A1132      22.624  46.393  27.234  1.00 19.11           C  
ATOM   1009  O   ALA A1132      22.122  47.395  26.721  1.00 16.73           O  
ATOM   1010  CB  ALA A1132      23.193  44.821  25.381  1.00 15.87           C  
ATOM   1011  N   PHE A1133      23.385  46.437  28.323  1.00 22.42           N  
ATOM   1012  CA  PHE A1133      23.709  47.696  28.987  1.00 27.44           C  
ATOM   1013  C   PHE A1133      25.220  47.884  28.937  1.00 30.68           C  
ATOM   1014  O   PHE A1133      25.947  47.237  29.687  1.00 30.98           O  
ATOM   1015  CB  PHE A1133      23.270  47.674  30.460  1.00 27.04           C  
ATOM   1016  CG  PHE A1133      21.905  47.085  30.693  1.00 27.95           C  
ATOM   1017  CD1 PHE A1133      21.710  45.709  30.663  1.00 27.84           C  
ATOM   1018  CD2 PHE A1133      20.817  47.909  30.966  1.00 27.68           C  
ATOM   1019  CE1 PHE A1133      20.450  45.158  30.901  1.00 28.88           C  
ATOM   1020  CE2 PHE A1133      19.555  47.370  31.205  1.00 28.37           C  
ATOM   1021  CZ  PHE A1133      19.371  45.993  31.174  1.00 28.87           C  
ATOM   1022  N   ASP A1134      25.692  48.764  28.061  1.00 34.91           N  
ATOM   1023  CA  ASP A1134      27.125  49.010  27.944  1.00 38.68           C  
ATOM   1024  C   ASP A1134      27.938  47.726  27.837  1.00 40.12           C  
ATOM   1025  O   ASP A1134      28.500  47.473  26.752  1.00 40.74           O  
ATOM   1026  CB  ASP A1134      27.623  49.825  29.137  1.00 41.23           C  
ATOM   1027  CG  ASP A1134      28.355  51.080  28.720  1.00 43.86           C  
ATOM   1028  OD1 ASP A1134      29.046  51.672  29.572  1.00 46.31           O  
ATOM   1029  OD2 ASP A1134      28.238  51.472  27.542  1.00 46.25           O  
ATOM   1030  OXT ASP A1134      28.003  46.988  28.842  1.00 41.42           O  
TER    1031      ASP A1134                                                      
ATOM   1032  N   ALA B2001      23.360  50.342  46.887  1.00 37.39           N  
ATOM   1033  CA  ALA B2001      24.148  50.308  45.621  1.00 36.65           C  
ATOM   1034  C   ALA B2001      24.126  48.911  45.009  1.00 35.63           C  
ATOM   1035  O   ALA B2001      25.076  48.501  44.340  1.00 35.88           O  
ATOM   1036  CB  ALA B2001      25.586  50.736  45.894  1.00 36.93           C  
ATOM   1037  N   SER B2002      23.037  48.184  45.240  1.00 34.31           N  
ATOM   1038  CA  SER B2002      22.899  46.832  44.713  1.00 31.63           C  
ATOM   1039  C   SER B2002      22.957  46.824  43.189  1.00 28.50           C  
ATOM   1040  O   SER B2002      23.254  47.842  42.561  1.00 29.22           O  
ATOM   1041  CB  SER B2002      21.583  46.206  45.192  1.00 33.30           C  
ATOM   1042  OG  SER B2002      20.465  46.993  44.814  1.00 36.32           O  
ATOM   1043  N   GLY B2003      22.670  45.671  42.598  1.00 24.72           N  
ATOM   1044  CA  GLY B2003      22.709  45.561  41.155  1.00 18.17           C  
ATOM   1045  C   GLY B2003      21.374  45.780  40.471  1.00 15.99           C  
ATOM   1046  O   GLY B2003      20.415  46.283  41.062  1.00 12.99           O  
ATOM   1047  N   LEU B2004      21.326  45.394  39.203  1.00 13.54           N  
ATOM   1048  CA  LEU B2004      20.131  45.531  38.388  1.00 13.35           C  
ATOM   1049  C   LEU B2004      18.979  44.713  38.952  1.00 12.90           C  
ATOM   1050  O   LEU B2004      19.172  43.602  39.441  1.00 11.13           O  
ATOM   1051  CB  LEU B2004      20.442  45.079  36.956  1.00 14.55           C  
ATOM   1052  CG  LEU B2004      19.354  45.121  35.880  1.00 17.07           C  
ATOM   1053  CD1 LEU B2004      19.995  44.929  34.519  1.00 20.12           C  
ATOM   1054  CD2 LEU B2004      18.318  44.042  36.124  1.00 17.72           C  
ATOM   1055  N   VAL B2005      17.778  45.277  38.890  1.00 12.60           N  
ATOM   1056  CA  VAL B2005      16.586  44.586  39.355  1.00 11.64           C  
ATOM   1057  C   VAL B2005      15.611  44.598  38.189  1.00 13.40           C  
ATOM   1058  O   VAL B2005      15.363  45.645  37.588  1.00 13.98           O  
ATOM   1059  CB  VAL B2005      15.941  45.295  40.565  1.00 12.90           C  
ATOM   1060  CG1 VAL B2005      14.663  44.575  40.969  1.00 13.45           C  
ATOM   1061  CG2 VAL B2005      16.916  45.312  41.734  1.00 12.43           C  
ATOM   1062  N   ALA B2006      15.082  43.428  37.856  1.00 11.93           N  
ATOM   1063  CA  ALA B2006      14.135  43.315  36.757  1.00 12.76           C  
ATOM   1064  C   ALA B2006      12.867  42.634  37.239  1.00 13.70           C  
ATOM   1065  O   ALA B2006      12.922  41.662  37.991  1.00 14.10           O  
ATOM   1066  CB  ALA B2006      14.753  42.519  35.617  1.00 12.61           C  
ATOM   1067  N   SER B2007      11.726  43.161  36.814  1.00 13.68           N  
ATOM   1068  CA  SER B2007      10.439  42.597  37.187  1.00 14.39           C  
ATOM   1069  C   SER B2007       9.623  42.377  35.920  1.00 15.38           C  
ATOM   1070  O   SER B2007       9.989  42.866  34.849  1.00 11.73           O  
ATOM   1071  CB  SER B2007       9.700  43.535  38.148  1.00 16.89           C  
ATOM   1072  OG  SER B2007       9.542  44.825  37.586  1.00 18.54           O  
ATOM   1073  N   ASN B2008       8.524  41.639  36.045  1.00 15.54           N  
ATOM   1074  CA  ASN B2008       7.666  41.339  34.906  1.00 19.06           C  
ATOM   1075  C   ASN B2008       8.486  40.606  33.845  1.00 19.33           C  
ATOM   1076  O   ASN B2008       8.290  40.791  32.643  1.00 19.55           O  
ATOM   1077  CB  ASN B2008       7.090  42.636  34.328  1.00 23.14           C  
ATOM   1078  CG  ASN B2008       5.929  43.166  35.139  1.00 27.62           C  
ATOM   1079  OD1 ASN B2008       5.570  42.595  36.167  1.00 31.32           O  
ATOM   1080  ND2 ASN B2008       5.334  44.264  34.685  1.00 28.79           N  
ATOM   1081  N   LEU B2009       9.404  39.763  34.308  1.00 18.85           N  
ATOM   1082  CA  LEU B2009      10.281  38.998  33.428  1.00 18.83           C  
ATOM   1083  C   LEU B2009       9.493  38.020  32.561  1.00 18.68           C  
ATOM   1084  O   LEU B2009       9.826  37.796  31.396  1.00 17.93           O  
ATOM   1085  CB  LEU B2009      11.307  38.240  34.272  1.00 21.77           C  
ATOM   1086  CG  LEU B2009      12.714  38.072  33.701  1.00 22.94           C  
ATOM   1087  CD1 LEU B2009      13.295  39.435  33.362  1.00 24.93           C  
ATOM   1088  CD2 LEU B2009      13.588  37.357  34.717  1.00 24.49           C  
ATOM   1089  N   ASN B2010       8.453  37.438  33.150  1.00 16.20           N  
ATOM   1090  CA  ASN B2010       7.581  36.483  32.478  1.00 16.85           C  
ATOM   1091  C   ASN B2010       8.307  35.323  31.796  1.00 15.78           C  
ATOM   1092  O   ASN B2010       7.932  34.902  30.699  1.00 15.16           O  
ATOM   1093  CB  ASN B2010       6.697  37.212  31.463  1.00 18.26           C  
ATOM   1094  CG  ASN B2010       5.590  36.331  30.919  1.00 19.68           C  
ATOM   1095  OD1 ASN B2010       4.885  35.660  31.677  1.00 21.51           O  
ATOM   1096  ND2 ASN B2010       5.424  36.335  29.603  1.00 23.70           N  
ATOM   1097  N   LEU B2011       9.343  34.805  32.446  1.00 13.06           N  
ATOM   1098  CA  LEU B2011      10.088  33.682  31.892  1.00 11.90           C  
ATOM   1099  C   LEU B2011       9.250  32.430  32.113  1.00 12.47           C  
ATOM   1100  O   LEU B2011       8.874  32.119  33.244  1.00 12.45           O  
ATOM   1101  CB  LEU B2011      11.438  33.521  32.595  1.00 12.17           C  
ATOM   1102  CG  LEU B2011      12.352  32.451  31.984  1.00 12.94           C  
ATOM   1103  CD1 LEU B2011      12.907  32.954  30.655  1.00 13.28           C  
ATOM   1104  CD2 LEU B2011      13.496  32.133  32.938  1.00 12.21           C  
ATOM   1105  N   LYS B2012       8.967  31.710  31.037  1.00 12.40           N  
ATOM   1106  CA  LYS B2012       8.149  30.506  31.119  1.00 14.06           C  
ATOM   1107  C   LYS B2012       8.984  29.232  31.068  1.00 13.70           C  
ATOM   1108  O   LYS B2012      10.135  29.251  30.640  1.00 13.25           O  
ATOM   1109  CB  LYS B2012       7.135  30.510  29.972  1.00 16.45           C  
ATOM   1110  CG  LYS B2012       6.284  31.767  29.930  1.00 19.53           C  
ATOM   1111  CD  LYS B2012       5.378  31.793  28.714  1.00 23.55           C  
ATOM   1112  CE  LYS B2012       4.516  33.046  28.721  1.00 26.57           C  
ATOM   1113  NZ  LYS B2012       3.733  33.151  29.986  1.00 29.81           N  
ATOM   1114  N   PRO B2013       8.407  28.102  31.511  1.00 15.14           N  
ATOM   1115  CA  PRO B2013       9.109  26.816  31.508  1.00 15.95           C  
ATOM   1116  C   PRO B2013       9.693  26.513  30.136  1.00 17.01           C  
ATOM   1117  O   PRO B2013       9.010  26.650  29.120  1.00 17.79           O  
ATOM   1118  CB  PRO B2013       8.014  25.825  31.891  1.00 15.05           C  
ATOM   1119  CG  PRO B2013       7.139  26.634  32.791  1.00 16.40           C  
ATOM   1120  CD  PRO B2013       7.050  27.954  32.066  1.00 15.57           C  
ATOM   1121  N   GLY B2014      10.960  26.111  30.108  1.00 17.93           N  
ATOM   1122  CA  GLY B2014      11.600  25.787  28.848  1.00 18.05           C  
ATOM   1123  C   GLY B2014      12.339  26.944  28.205  1.00 18.60           C  
ATOM   1124  O   GLY B2014      13.243  26.729  27.395  1.00 19.03           O  
ATOM   1125  N   GLU B2015      11.958  28.171  28.546  1.00 17.35           N  
ATOM   1126  CA  GLU B2015      12.622  29.341  27.979  1.00 16.12           C  
ATOM   1127  C   GLU B2015      13.984  29.491  28.635  1.00 16.03           C  
ATOM   1128  O   GLU B2015      14.138  29.237  29.827  1.00 14.97           O  
ATOM   1129  CB  GLU B2015      11.794  30.604  28.216  1.00 16.13           C  
ATOM   1130  CG  GLU B2015      10.368  30.512  27.711  0.80 19.54           C  
ATOM   1131  CD  GLU B2015       9.664  31.856  27.694  1.00 21.97           C  
ATOM   1132  OE1 GLU B2015       9.911  32.674  28.603  1.00 21.36           O  
ATOM   1133  OE2 GLU B2015       8.856  32.089  26.770  1.00 25.89           O  
ATOM   1134  N   CYS B2016      14.973  29.910  27.857  1.00 15.28           N  
ATOM   1135  CA  CYS B2016      16.318  30.061  28.386  1.00 15.55           C  
ATOM   1136  C   CYS B2016      16.636  31.517  28.711  1.00 14.24           C  
ATOM   1137  O   CYS B2016      16.556  32.394  27.847  1.00 14.88           O  
ATOM   1138  CB  CYS B2016      17.339  29.527  27.381  1.00 19.40           C  
ATOM   1139  SG  CYS B2016      19.058  29.657  27.915  1.00 21.98           S  
ATOM   1140  N   LEU B2017      16.984  31.766  29.969  1.00 12.15           N  
ATOM   1141  CA  LEU B2017      17.353  33.100  30.417  1.00 10.97           C  
ATOM   1142  C   LEU B2017      18.871  33.144  30.473  1.00 10.44           C  
ATOM   1143  O   LEU B2017      19.487  32.397  31.233  1.00 10.87           O  
ATOM   1144  CB  LEU B2017      16.790  33.383  31.813  1.00 11.15           C  
ATOM   1145  CG  LEU B2017      17.240  34.699  32.459  1.00 12.52           C  
ATOM   1146  CD1 LEU B2017      16.669  35.879  31.676  1.00 13.54           C  
ATOM   1147  CD2 LEU B2017      16.775  34.746  33.907  1.00 14.03           C  
ATOM   1148  N   ARG B2018      19.473  34.005  29.662  1.00 10.18           N  
ATOM   1149  CA  ARG B2018      20.926  34.136  29.647  1.00 10.45           C  
ATOM   1150  C   ARG B2018      21.288  35.469  30.273  1.00 10.79           C  
ATOM   1151  O   ARG B2018      20.807  36.518  29.845  1.00 10.20           O  
ATOM   1152  CB  ARG B2018      21.460  34.079  28.215  1.00 12.92           C  
ATOM   1153  CG  ARG B2018      21.148  32.781  27.494  1.00 16.12           C  
ATOM   1154  CD  ARG B2018      21.610  32.820  26.048  1.00 16.44           C  
ATOM   1155  NE  ARG B2018      21.044  31.712  25.287  1.00 22.64           N  
ATOM   1156  CZ  ARG B2018      21.570  30.494  25.223  1.00 23.09           C  
ATOM   1157  NH1 ARG B2018      22.694  30.214  25.869  1.00 26.09           N  
ATOM   1158  NH2 ARG B2018      20.957  29.548  24.523  1.00 23.71           N  
ATOM   1159  N   VAL B2019      22.132  35.425  31.295  1.00 10.31           N  
ATOM   1160  CA  VAL B2019      22.543  36.636  31.978  1.00 11.26           C  
ATOM   1161  C   VAL B2019      24.056  36.730  31.982  1.00 12.05           C  
ATOM   1162  O   VAL B2019      24.739  35.834  32.470  1.00 12.36           O  
ATOM   1163  CB  VAL B2019      22.046  36.651  33.433  1.00 11.98           C  
ATOM   1164  CG1 VAL B2019      22.463  37.951  34.110  1.00 12.44           C  
ATOM   1165  CG2 VAL B2019      20.536  36.480  33.465  1.00 13.08           C  
ATOM   1166  N   ARG B2020      24.573  37.816  31.424  1.00 11.10           N  
ATOM   1167  CA  ARG B2020      26.009  38.026  31.372  1.00 11.98           C  
ATOM   1168  C   ARG B2020      26.316  39.257  32.201  1.00 11.45           C  
ATOM   1169  O   ARG B2020      25.642  40.281  32.076  1.00 10.06           O  
ATOM   1170  CB  ARG B2020      26.456  38.235  29.926  1.00 15.08           C  
ATOM   1171  CG  ARG B2020      27.942  38.493  29.753  1.00 19.61           C  
ATOM   1172  CD  ARG B2020      28.252  38.755  28.291  1.00 24.40           C  
ATOM   1173  NE  ARG B2020      27.937  37.596  27.462  1.00 28.21           N  
ATOM   1174  CZ  ARG B2020      27.766  37.644  26.146  1.00 31.21           C  
ATOM   1175  NH1 ARG B2020      27.875  38.801  25.505  1.00 33.02           N  
ATOM   1176  NH2 ARG B2020      27.490  36.536  25.469  1.00 32.64           N  
ATOM   1177  N   GLY B2021      27.325  39.155  33.058  1.00 11.61           N  
ATOM   1178  CA  GLY B2021      27.675  40.286  33.894  1.00 12.26           C  
ATOM   1179  C   GLY B2021      29.130  40.292  34.305  1.00 13.08           C  
ATOM   1180  O   GLY B2021      29.824  39.281  34.191  1.00 13.97           O  
ATOM   1181  N   GLU B2022      29.589  41.440  34.785  1.00 13.20           N  
ATOM   1182  CA  GLU B2022      30.968  41.592  35.223  1.00 14.36           C  
ATOM   1183  C   GLU B2022      31.071  41.382  36.729  1.00 12.82           C  
ATOM   1184  O   GLU B2022      30.385  42.045  37.506  1.00 12.65           O  
ATOM   1185  CB  GLU B2022      31.481  42.990  34.865  1.00 16.64           C  
ATOM   1186  CG  GLU B2022      31.481  43.288  33.375  1.00 20.13           C  
ATOM   1187  CD  GLU B2022      31.844  44.731  33.064  1.00 22.91           C  
ATOM   1188  OE1 GLU B2022      31.903  45.081  31.868  1.00 25.25           O  
ATOM   1189  OE2 GLU B2022      32.069  45.514  34.012  1.00 26.03           O  
ATOM   1190  N   VAL B2023      31.918  40.444  37.137  1.00 13.19           N  
ATOM   1191  CA  VAL B2023      32.119  40.182  38.554  1.00 13.25           C  
ATOM   1192  C   VAL B2023      33.096  41.245  39.059  1.00 13.63           C  
ATOM   1193  O   VAL B2023      34.183  41.407  38.501  1.00 14.52           O  
ATOM   1194  CB  VAL B2023      32.716  38.772  38.778  1.00 12.58           C  
ATOM   1195  CG1 VAL B2023      32.891  38.504  40.266  1.00 12.68           C  
ATOM   1196  CG2 VAL B2023      31.806  37.722  38.153  1.00 13.63           C  
ATOM   1197  N   ALA B2024      32.702  41.981  40.095  1.00 14.32           N  
ATOM   1198  CA  ALA B2024      33.551  43.032  40.653  1.00 16.06           C  
ATOM   1199  C   ALA B2024      34.961  42.510  40.924  1.00 17.09           C  
ATOM   1200  O   ALA B2024      35.140  41.390  41.402  1.00 16.81           O  
ATOM   1201  CB  ALA B2024      32.937  43.577  41.941  1.00 15.28           C  
ATOM   1202  N   PRO B2025      35.984  43.323  40.622  1.00 18.05           N  
ATOM   1203  CA  PRO B2025      37.374  42.913  40.844  1.00 19.11           C  
ATOM   1204  C   PRO B2025      37.699  42.561  42.297  1.00 19.90           C  
ATOM   1205  O   PRO B2025      38.557  41.721  42.558  1.00 21.42           O  
ATOM   1206  CB  PRO B2025      38.172  44.117  40.341  1.00 19.13           C  
ATOM   1207  CG  PRO B2025      37.251  45.267  40.612  1.00 20.67           C  
ATOM   1208  CD  PRO B2025      35.919  44.716  40.148  1.00 19.82           C  
ATOM   1209  N   ASP B2026      37.011  43.198  43.238  1.00 19.81           N  
ATOM   1210  CA  ASP B2026      37.254  42.943  44.656  1.00 22.16           C  
ATOM   1211  C   ASP B2026      36.123  42.134  45.282  1.00 20.96           C  
ATOM   1212  O   ASP B2026      35.963  42.114  46.502  1.00 21.17           O  
ATOM   1213  CB  ASP B2026      37.399  44.272  45.398  1.00 25.96           C  
ATOM   1214  CG  ASP B2026      36.112  45.072  45.408  1.00 29.25           C  
ATOM   1215  OD1 ASP B2026      35.458  45.168  44.345  1.00 31.90           O  
ATOM   1216  OD2 ASP B2026      35.755  45.609  46.477  1.00 32.44           O  
ATOM   1217  N   ALA B2027      35.340  41.467  44.444  1.00 19.29           N  
ATOM   1218  CA  ALA B2027      34.214  40.679  44.927  1.00 18.13           C  
ATOM   1219  C   ALA B2027      34.628  39.484  45.778  1.00 16.70           C  
ATOM   1220  O   ALA B2027      35.529  38.726  45.413  1.00 16.55           O  
ATOM   1221  CB  ALA B2027      33.375  40.203  43.746  1.00 17.56           C  
ATOM   1222  N   LYS B2028      33.974  39.329  46.924  1.00 14.75           N  
ATOM   1223  CA  LYS B2028      34.250  38.198  47.799  1.00 14.87           C  
ATOM   1224  C   LYS B2028      33.203  37.151  47.437  1.00 13.00           C  
ATOM   1225  O   LYS B2028      33.319  35.980  47.786  1.00  9.79           O  
ATOM   1226  CB  LYS B2028      34.112  38.596  49.270  1.00 16.95           C  
ATOM   1227  CG  LYS B2028      34.990  39.771  49.686  1.00 21.47           C  
ATOM   1228  CD  LYS B2028      36.437  39.593  49.243  1.00 24.52           C  
ATOM   1229  CE  LYS B2028      37.087  38.378  49.885  1.00 28.07           C  
ATOM   1230  NZ  LYS B2028      38.509  38.223  49.453  1.00 30.57           N  
ATOM   1231  N   SER B2029      32.188  37.602  46.708  1.00 12.42           N  
ATOM   1232  CA  SER B2029      31.094  36.750  46.260  1.00 11.86           C  
ATOM   1233  C   SER B2029      30.152  37.616  45.436  1.00 11.35           C  
ATOM   1234  O   SER B2029      30.328  38.829  45.358  1.00 12.62           O  
ATOM   1235  CB  SER B2029      30.325  36.200  47.462  1.00 12.39           C  
ATOM   1236  OG  SER B2029      29.603  37.236  48.113  1.00 12.65           O  
ATOM   1237  N   PHE B2030      29.171  36.995  44.797  1.00 10.65           N  
ATOM   1238  CA  PHE B2030      28.184  37.761  44.055  1.00  9.95           C  
ATOM   1239  C   PHE B2030      26.890  36.970  44.063  1.00  9.98           C  
ATOM   1240  O   PHE B2030      26.888  35.773  44.347  1.00  7.09           O  
ATOM   1241  CB  PHE B2030      28.677  38.119  42.637  1.00 10.16           C  
ATOM   1242  CG  PHE B2030      28.578  37.010  41.622  1.00  9.96           C  
ATOM   1243  CD1 PHE B2030      27.388  36.773  40.940  1.00  9.71           C  
ATOM   1244  CD2 PHE B2030      29.701  36.264  41.281  1.00 10.64           C  
ATOM   1245  CE1 PHE B2030      27.322  35.812  39.928  1.00 10.52           C  
ATOM   1246  CE2 PHE B2030      29.646  35.304  40.273  1.00 11.88           C  
ATOM   1247  CZ  PHE B2030      28.452  35.080  39.593  1.00 10.33           C  
ATOM   1248  N   VAL B2031      25.786  37.647  43.790  1.00  9.10           N  
ATOM   1249  CA  VAL B2031      24.487  36.999  43.830  1.00  9.35           C  
ATOM   1250  C   VAL B2031      23.600  37.365  42.662  1.00  9.05           C  
ATOM   1251  O   VAL B2031      23.605  38.500  42.196  1.00 10.11           O  
ATOM   1252  CB  VAL B2031      23.731  37.384  45.125  1.00  9.50           C  
ATOM   1253  CG1 VAL B2031      22.282  36.895  45.065  1.00 12.54           C  
ATOM   1254  CG2 VAL B2031      24.446  36.808  46.338  1.00 10.54           C  
ATOM   1255  N   LEU B2032      22.844  36.378  42.198  1.00  9.15           N  
ATOM   1256  CA  LEU B2032      21.880  36.564  41.128  1.00 10.08           C  
ATOM   1257  C   LEU B2032      20.642  35.883  41.699  1.00  9.09           C  
ATOM   1258  O   LEU B2032      20.651  34.677  41.928  1.00  8.66           O  
ATOM   1259  CB  LEU B2032      22.316  35.843  39.851  1.00 11.37           C  
ATOM   1260  CG  LEU B2032      21.913  36.459  38.503  1.00 15.71           C  
ATOM   1261  CD1 LEU B2032      21.551  35.343  37.536  1.00 13.22           C  
ATOM   1262  CD2 LEU B2032      20.748  37.424  38.661  1.00 16.29           C  
ATOM   1263  N   ASN B2033      19.598  36.658  41.969  1.00  8.09           N  
ATOM   1264  CA  ASN B2033      18.373  36.095  42.515  1.00  8.16           C  
ATOM   1265  C   ASN B2033      17.287  36.026  41.460  1.00  9.12           C  
ATOM   1266  O   ASN B2033      17.133  36.947  40.657  1.00  8.95           O  
ATOM   1267  CB  ASN B2033      17.856  36.929  43.689  1.00  8.55           C  
ATOM   1268  CG  ASN B2033      18.722  36.804  44.924  1.00  9.34           C  
ATOM   1269  OD1 ASN B2033      19.287  35.746  45.196  1.00  9.72           O  
ATOM   1270  ND2 ASN B2033      18.808  37.881  45.694  1.00  8.86           N  
ATOM   1271  N   LEU B2034      16.541  34.925  41.477  1.00  7.95           N  
ATOM   1272  CA  LEU B2034      15.438  34.706  40.550  1.00  8.65           C  
ATOM   1273  C   LEU B2034      14.230  34.251  41.348  1.00  9.17           C  
ATOM   1274  O   LEU B2034      14.361  33.490  42.307  1.00  8.29           O  
ATOM   1275  CB  LEU B2034      15.783  33.621  39.525  1.00 11.08           C  
ATOM   1276  CG  LEU B2034      16.894  33.891  38.506  1.00 11.31           C  
ATOM   1277  CD1 LEU B2034      17.138  32.626  37.697  1.00 13.80           C  
ATOM   1278  CD2 LEU B2034      16.506  35.036  37.587  1.00 14.78           C  
ATOM   1279  N   GLY B2035      13.053  34.712  40.946  1.00  8.73           N  
ATOM   1280  CA  GLY B2035      11.854  34.307  41.645  1.00  9.10           C  
ATOM   1281  C   GLY B2035      10.626  35.115  41.287  1.00 11.09           C  
ATOM   1282  O   GLY B2035      10.493  35.624  40.171  1.00 10.18           O  
ATOM   1283  N   LYS B2036       9.721  35.211  42.253  1.00 10.51           N  
ATOM   1284  CA  LYS B2036       8.472  35.950  42.102  1.00 13.32           C  
ATOM   1285  C   LYS B2036       8.711  37.391  42.544  1.00 13.48           C  
ATOM   1286  O   LYS B2036       8.209  38.333  41.934  1.00 15.08           O  
ATOM   1287  CB  LYS B2036       7.394  35.309  42.977  1.00 15.99           C  
ATOM   1288  CG  LYS B2036       6.013  35.930  42.845  1.00 20.70           C  
ATOM   1289  CD  LYS B2036       5.176  35.677  44.097  1.00 25.63           C  
ATOM   1290  CE  LYS B2036       5.101  34.201  44.457  1.00 27.50           C  
ATOM   1291  NZ  LYS B2036       4.366  33.993  45.743  1.00 31.29           N  
ATOM   1292  N   ASP B2037       9.469  37.545  43.623  1.00 12.47           N  
ATOM   1293  CA  ASP B2037       9.814  38.854  44.163  1.00 13.46           C  
ATOM   1294  C   ASP B2037      10.953  38.688  45.167  1.00 13.58           C  
ATOM   1295  O   ASP B2037      11.429  37.577  45.391  1.00 12.20           O  
ATOM   1296  CB  ASP B2037       8.602  39.520  44.832  1.00 14.38           C  
ATOM   1297  CG  ASP B2037       8.016  38.687  45.953  1.00 16.41           C  
ATOM   1298  OD1 ASP B2037       8.794  38.114  46.744  1.00 12.58           O  
ATOM   1299  OD2 ASP B2037       6.772  38.620  46.050  1.00 17.33           O  
ATOM   1300  N   SER B2038      11.383  39.784  45.779  1.00 14.15           N  
ATOM   1301  CA  SER B2038      12.493  39.737  46.722  1.00 14.45           C  
ATOM   1302  C   SER B2038      12.330  38.775  47.901  1.00 13.41           C  
ATOM   1303  O   SER B2038      13.323  38.365  48.500  1.00 14.22           O  
ATOM   1304  CB  SER B2038      12.783  41.143  47.255  1.00 15.67           C  
ATOM   1305  OG  SER B2038      11.668  41.657  47.960  1.00 18.75           O  
ATOM   1306  N   ASN B2039      11.095  38.411  48.236  1.00 13.56           N  
ATOM   1307  CA  ASN B2039      10.860  37.508  49.368  1.00 12.44           C  
ATOM   1308  C   ASN B2039      10.517  36.083  48.963  1.00 10.08           C  
ATOM   1309  O   ASN B2039      10.321  35.217  49.813  1.00 10.30           O  
ATOM   1310  CB  ASN B2039       9.741  38.055  50.253  1.00 14.16           C  
ATOM   1311  CG  ASN B2039      10.084  39.398  50.855  1.00 16.20           C  
ATOM   1312  OD1 ASN B2039      11.140  39.563  51.458  1.00 18.38           O  
ATOM   1313  ND2 ASN B2039       9.186  40.365  50.702  1.00 20.39           N  
ATOM   1314  N   ASN B2040      10.443  35.844  47.661  1.00  9.74           N  
ATOM   1315  CA  ASN B2040      10.112  34.523  47.152  1.00  8.61           C  
ATOM   1316  C   ASN B2040      11.039  34.215  45.987  1.00  9.10           C  
ATOM   1317  O   ASN B2040      10.755  34.561  44.843  1.00  8.64           O  
ATOM   1318  CB  ASN B2040       8.648  34.509  46.711  1.00  8.54           C  
ATOM   1319  CG  ASN B2040       7.693  34.704  47.875  1.00  9.87           C  
ATOM   1320  OD1 ASN B2040       7.382  33.760  48.598  1.00 11.09           O  
ATOM   1321  ND2 ASN B2040       7.241  35.941  48.076  1.00 11.83           N  
ATOM   1322  N   LEU B2041      12.155  33.561  46.295  1.00  7.50           N  
ATOM   1323  CA  LEU B2041      13.150  33.234  45.288  1.00  7.74           C  
ATOM   1324  C   LEU B2041      13.209  31.749  44.966  1.00  7.50           C  
ATOM   1325  O   LEU B2041      13.378  30.920  45.861  1.00  6.01           O  
ATOM   1326  CB  LEU B2041      14.528  33.695  45.771  1.00  7.87           C  
ATOM   1327  CG  LEU B2041      14.672  35.152  46.222  1.00  9.87           C  
ATOM   1328  CD1 LEU B2041      16.058  35.362  46.824  1.00 10.07           C  
ATOM   1329  CD2 LEU B2041      14.439  36.090  45.039  1.00  7.65           C  
ATOM   1330  N   CYS B2042      13.064  31.408  43.689  1.00  8.54           N  
ATOM   1331  CA  CYS B2042      13.151  30.008  43.298  1.00  8.77           C  
ATOM   1332  C   CYS B2042      14.638  29.685  43.206  1.00  8.98           C  
ATOM   1333  O   CYS B2042      15.045  28.523  43.289  1.00  7.54           O  
ATOM   1334  CB  CYS B2042      12.455  29.759  41.952  1.00 11.94           C  
ATOM   1335  SG  CYS B2042      12.996  30.794  40.578  1.00 14.06           S  
ATOM   1336  N   LEU B2043      15.452  30.726  43.060  1.00  8.30           N  
ATOM   1337  CA  LEU B2043      16.891  30.533  42.970  1.00  8.62           C  
ATOM   1338  C   LEU B2043      17.731  31.705  43.463  1.00  8.28           C  
ATOM   1339  O   LEU B2043      17.672  32.811  42.923  1.00  8.66           O  
ATOM   1340  CB  LEU B2043      17.304  30.203  41.533  1.00  7.71           C  
ATOM   1341  CG  LEU B2043      18.818  29.996  41.368  1.00  8.78           C  
ATOM   1342  CD1 LEU B2043      19.236  28.718  42.090  1.00 11.39           C  
ATOM   1343  CD2 LEU B2043      19.183  29.916  39.898  1.00  9.29           C  
ATOM   1344  N   HIS B2044      18.500  31.440  44.512  1.00  7.35           N  
ATOM   1345  CA  HIS B2044      19.433  32.402  45.087  1.00  7.96           C  
ATOM   1346  C   HIS B2044      20.761  31.783  44.647  1.00  9.06           C  
ATOM   1347  O   HIS B2044      21.221  30.804  45.238  1.00 10.37           O  
ATOM   1348  CB  HIS B2044      19.320  32.411  46.619  1.00  8.30           C  
ATOM   1349  CG  HIS B2044      20.403  33.183  47.313  1.00  9.37           C  
ATOM   1350  ND1 HIS B2044      20.546  34.550  47.195  1.00  7.97           N  
ATOM   1351  CD2 HIS B2044      21.383  32.776  48.155  1.00  9.89           C  
ATOM   1352  CE1 HIS B2044      21.564  34.951  47.936  1.00 10.24           C  
ATOM   1353  NE2 HIS B2044      22.090  33.894  48.529  1.00  9.44           N  
ATOM   1354  N   PHE B2045      21.333  32.331  43.578  1.00  7.52           N  
ATOM   1355  CA  PHE B2045      22.588  31.845  43.001  1.00  7.65           C  
ATOM   1356  C   PHE B2045      23.698  32.673  43.629  1.00  6.96           C  
ATOM   1357  O   PHE B2045      23.827  33.862  43.344  1.00  8.47           O  
ATOM   1358  CB  PHE B2045      22.552  32.043  41.484  1.00  7.80           C  
ATOM   1359  CG  PHE B2045      23.741  31.476  40.771  1.00  7.68           C  
ATOM   1360  CD1 PHE B2045      23.928  30.098  40.686  1.00  7.22           C  
ATOM   1361  CD2 PHE B2045      24.678  32.320  40.186  1.00  7.87           C  
ATOM   1362  CE1 PHE B2045      25.038  29.567  40.023  1.00  8.60           C  
ATOM   1363  CE2 PHE B2045      25.792  31.800  39.522  1.00  8.09           C  
ATOM   1364  CZ  PHE B2045      25.970  30.422  39.441  1.00  9.33           C  
ATOM   1365  N   ASN B2046      24.516  32.028  44.456  1.00  6.38           N  
ATOM   1366  CA  ASN B2046      25.544  32.731  45.215  1.00  6.76           C  
ATOM   1367  C   ASN B2046      26.969  32.171  45.150  1.00  6.48           C  
ATOM   1368  O   ASN B2046      27.389  31.428  46.039  1.00  6.80           O  
ATOM   1369  CB  ASN B2046      25.055  32.772  46.675  1.00  6.84           C  
ATOM   1370  CG  ASN B2046      25.982  33.517  47.618  1.00  7.99           C  
ATOM   1371  OD1 ASN B2046      25.918  33.309  48.834  1.00  8.47           O  
ATOM   1372  ND2 ASN B2046      26.820  34.399  47.087  1.00  7.66           N  
ATOM   1373  N   PRO B2047      27.721  32.500  44.085  1.00  6.82           N  
ATOM   1374  CA  PRO B2047      29.092  31.997  44.000  1.00  8.18           C  
ATOM   1375  C   PRO B2047      29.916  32.743  45.047  1.00  8.26           C  
ATOM   1376  O   PRO B2047      29.952  33.978  45.061  1.00  8.94           O  
ATOM   1377  CB  PRO B2047      29.506  32.356  42.575  1.00  8.38           C  
ATOM   1378  CG  PRO B2047      28.214  32.289  41.830  1.00  8.02           C  
ATOM   1379  CD  PRO B2047      27.275  33.004  42.773  1.00  6.61           C  
ATOM   1380  N   ARG B2048      30.564  31.995  45.929  1.00  8.41           N  
ATOM   1381  CA  ARG B2048      31.371  32.599  46.977  1.00  8.05           C  
ATOM   1382  C   ARG B2048      32.856  32.355  46.766  1.00  7.86           C  
ATOM   1383  O   ARG B2048      33.304  31.210  46.757  1.00  8.62           O  
ATOM   1384  CB  ARG B2048      30.952  32.043  48.340  1.00  8.43           C  
ATOM   1385  CG  ARG B2048      29.506  32.342  48.690  1.00  7.79           C  
ATOM   1386  CD  ARG B2048      29.113  31.748  50.031  1.00  9.53           C  
ATOM   1387  NE  ARG B2048      27.738  32.105  50.367  1.00  9.27           N  
ATOM   1388  CZ  ARG B2048      27.068  31.627  51.409  1.00 12.29           C  
ATOM   1389  NH1 ARG B2048      27.645  30.760  52.231  1.00 11.09           N  
ATOM   1390  NH2 ARG B2048      25.816  32.015  51.624  1.00 11.42           N  
ATOM   1391  N   PHE B2049      33.613  33.434  46.589  1.00  8.25           N  
ATOM   1392  CA  PHE B2049      35.055  33.327  46.407  1.00  8.28           C  
ATOM   1393  C   PHE B2049      35.659  33.115  47.790  1.00  8.77           C  
ATOM   1394  O   PHE B2049      36.396  32.154  48.027  1.00  7.82           O  
ATOM   1395  CB  PHE B2049      35.596  34.605  45.761  1.00  7.46           C  
ATOM   1396  CG  PHE B2049      35.020  34.874  44.403  1.00  9.07           C  
ATOM   1397  CD1 PHE B2049      33.996  35.796  44.238  1.00 10.20           C  
ATOM   1398  CD2 PHE B2049      35.474  34.168  43.291  1.00  8.16           C  
ATOM   1399  CE1 PHE B2049      33.425  36.010  42.985  1.00 10.37           C  
ATOM   1400  CE2 PHE B2049      34.908  34.373  42.036  1.00 11.22           C  
ATOM   1401  CZ  PHE B2049      33.882  35.297  41.883  1.00 11.06           C  
ATOM   1402  N   ASN B2050      35.321  34.023  48.698  1.00  9.16           N  
ATOM   1403  CA  ASN B2050      35.753  33.960  50.088  1.00 11.18           C  
ATOM   1404  C   ASN B2050      34.722  34.755  50.869  1.00 11.72           C  
ATOM   1405  O   ASN B2050      34.896  35.948  51.103  1.00 12.04           O  
ATOM   1406  CB  ASN B2050      37.137  34.586  50.284  1.00 11.95           C  
ATOM   1407  CG  ASN B2050      37.608  34.516  51.733  1.00 15.29           C  
ATOM   1408  OD1 ASN B2050      38.653  35.066  52.089  1.00 16.64           O  
ATOM   1409  ND2 ASN B2050      36.835  33.834  52.575  1.00 14.63           N  
ATOM   1410  N   ALA B2051      33.636  34.096  51.255  1.00 11.10           N  
ATOM   1411  CA  ALA B2051      32.581  34.771  51.998  1.00 10.68           C  
ATOM   1412  C   ALA B2051      31.792  33.802  52.864  1.00 11.26           C  
ATOM   1413  O   ALA B2051      31.625  32.634  52.512  1.00 10.59           O  
ATOM   1414  CB  ALA B2051      31.643  35.481  51.028  1.00 11.21           C  
ATOM   1415  N   HIS B2052      31.320  34.303  54.001  1.00 10.65           N  
ATOM   1416  CA  HIS B2052      30.528  33.517  54.936  1.00 11.23           C  
ATOM   1417  C   HIS B2052      31.203  32.215  55.348  1.00 10.09           C  
ATOM   1418  O   HIS B2052      30.533  31.226  55.638  1.00 12.09           O  
ATOM   1419  CB  HIS B2052      29.157  33.218  54.324  1.00 15.06           C  
ATOM   1420  CG  HIS B2052      28.415  34.442  53.893  1.00 20.42           C  
ATOM   1421  ND1 HIS B2052      27.941  35.378  54.787  1.00 24.19           N  
ATOM   1422  CD2 HIS B2052      28.091  34.900  52.661  1.00 21.90           C  
ATOM   1423  CE1 HIS B2052      27.359  36.361  54.124  1.00 24.73           C  
ATOM   1424  NE2 HIS B2052      27.437  36.095  52.833  1.00 25.11           N  
ATOM   1425  N   GLY B2053      32.530  32.221  55.369  1.00  9.57           N  
ATOM   1426  CA  GLY B2053      33.268  31.034  55.758  1.00 11.05           C  
ATOM   1427  C   GLY B2053      33.510  30.023  54.652  1.00 11.66           C  
ATOM   1428  O   GLY B2053      34.135  28.988  54.889  1.00 12.93           O  
ATOM   1429  N   ASP B2054      33.016  30.309  53.450  1.00  9.97           N  
ATOM   1430  CA  ASP B2054      33.196  29.404  52.320  1.00  9.85           C  
ATOM   1431  C   ASP B2054      34.222  29.955  51.344  1.00 10.73           C  
ATOM   1432  O   ASP B2054      34.425  31.168  51.263  1.00 10.69           O  
ATOM   1433  CB  ASP B2054      31.879  29.197  51.565  1.00 10.68           C  
ATOM   1434  CG  ASP B2054      30.811  28.541  52.411  1.00 11.18           C  
ATOM   1435  OD1 ASP B2054      31.164  27.774  53.333  1.00  9.99           O  
ATOM   1436  OD2 ASP B2054      29.615  28.783  52.138  1.00  8.49           O  
ATOM   1437  N   ALA B2055      34.865  29.059  50.603  1.00  8.88           N  
ATOM   1438  CA  ALA B2055      35.853  29.459  49.611  1.00  8.58           C  
ATOM   1439  C   ALA B2055      35.541  28.769  48.287  1.00  8.07           C  
ATOM   1440  O   ALA B2055      35.301  27.560  48.254  1.00  9.05           O  
ATOM   1441  CB  ALA B2055      37.253  29.086  50.080  1.00  9.39           C  
ATOM   1442  N   ASN B2056      35.532  29.548  47.209  1.00  7.99           N  
ATOM   1443  CA  ASN B2056      35.263  29.044  45.866  1.00  8.98           C  
ATOM   1444  C   ASN B2056      34.205  27.955  45.833  1.00  8.83           C  
ATOM   1445  O   ASN B2056      34.452  26.828  45.398  1.00  9.82           O  
ATOM   1446  CB  ASN B2056      36.560  28.541  45.234  1.00 11.47           C  
ATOM   1447  CG  ASN B2056      37.635  29.601  45.230  1.00 14.12           C  
ATOM   1448  OD1 ASN B2056      37.360  30.763  44.945  1.00 13.16           O  
ATOM   1449  ND2 ASN B2056      38.866  29.211  45.547  1.00 21.09           N  
ATOM   1450  N   THR B2057      33.014  28.311  46.294  1.00  8.50           N  
ATOM   1451  CA  THR B2057      31.901  27.383  46.325  1.00  7.64           C  
ATOM   1452  C   THR B2057      30.638  28.102  45.880  1.00  7.68           C  
ATOM   1453  O   THR B2057      30.361  29.218  46.317  1.00  7.13           O  
ATOM   1454  CB  THR B2057      31.663  26.838  47.750  1.00  9.74           C  
ATOM   1455  OG1 THR B2057      32.839  26.163  48.207  1.00  9.71           O  
ATOM   1456  CG2 THR B2057      30.486  25.861  47.763  1.00  8.72           C  
ATOM   1457  N   ILE B2058      29.880  27.465  44.998  1.00  6.75           N  
ATOM   1458  CA  ILE B2058      28.630  28.049  44.549  1.00  6.09           C  
ATOM   1459  C   ILE B2058      27.580  27.558  45.527  1.00  6.08           C  
ATOM   1460  O   ILE B2058      27.409  26.352  45.701  1.00  5.85           O  
ATOM   1461  CB  ILE B2058      28.228  27.567  43.146  1.00  6.27           C  
ATOM   1462  CG1 ILE B2058      29.277  27.992  42.116  1.00  6.47           C  
ATOM   1463  CG2 ILE B2058      26.865  28.144  42.783  1.00  6.19           C  
ATOM   1464  CD1 ILE B2058      28.995  27.471  40.713  1.00 10.37           C  
ATOM   1465  N   VAL B2059      26.896  28.489  46.178  1.00  5.78           N  
ATOM   1466  CA  VAL B2059      25.842  28.138  47.120  1.00  5.85           C  
ATOM   1467  C   VAL B2059      24.512  28.549  46.505  1.00  6.63           C  
ATOM   1468  O   VAL B2059      24.356  29.685  46.061  1.00  6.24           O  
ATOM   1469  CB  VAL B2059      26.005  28.885  48.464  1.00  7.51           C  
ATOM   1470  CG1 VAL B2059      24.900  28.463  49.435  1.00  9.17           C  
ATOM   1471  CG2 VAL B2059      27.373  28.595  49.062  1.00  7.98           C  
ATOM   1472  N   CYS B2060      23.564  27.620  46.457  1.00  5.23           N  
ATOM   1473  CA  CYS B2060      22.245  27.917  45.918  1.00  6.66           C  
ATOM   1474  C   CYS B2060      21.225  27.667  47.007  1.00  5.50           C  
ATOM   1475  O   CYS B2060      21.409  26.786  47.843  1.00  6.94           O  
ATOM   1476  CB  CYS B2060      21.911  27.014  44.727  1.00  6.53           C  
ATOM   1477  SG  CYS B2060      22.894  27.303  43.249  1.00  8.05           S  
ATOM   1478  N   ASN B2061      20.156  28.449  47.006  1.00  5.93           N  
ATOM   1479  CA  ASN B2061      19.100  28.250  47.983  1.00  6.20           C  
ATOM   1480  C   ASN B2061      17.816  28.860  47.461  1.00  7.09           C  
ATOM   1481  O   ASN B2061      17.812  29.573  46.458  1.00  6.76           O  
ATOM   1482  CB  ASN B2061      19.457  28.883  49.335  1.00  8.40           C  
ATOM   1483  CG  ASN B2061      18.712  28.233  50.496  1.00  7.76           C  
ATOM   1484  OD1 ASN B2061      17.889  27.340  50.296  1.00  6.35           O  
ATOM   1485  ND2 ASN B2061      19.003  28.675  51.715  1.00  5.35           N  
ATOM   1486  N   SER B2062      16.723  28.549  48.141  1.00  7.16           N  
ATOM   1487  CA  SER B2062      15.421  29.075  47.778  1.00  6.70           C  
ATOM   1488  C   SER B2062      14.957  29.903  48.964  1.00  8.57           C  
ATOM   1489  O   SER B2062      15.454  29.732  50.080  1.00  6.70           O  
ATOM   1490  CB  SER B2062      14.441  27.930  47.532  1.00  6.35           C  
ATOM   1491  OG  SER B2062      14.391  27.085  48.665  1.00  6.99           O  
ATOM   1492  N   LYS B2063      14.014  30.803  48.712  1.00  7.47           N  
ATOM   1493  CA  LYS B2063      13.459  31.662  49.750  1.00  8.23           C  
ATOM   1494  C   LYS B2063      11.952  31.613  49.543  1.00  8.24           C  
ATOM   1495  O   LYS B2063      11.456  32.034  48.504  1.00  8.45           O  
ATOM   1496  CB  LYS B2063      13.978  33.089  49.572  1.00  9.21           C  
ATOM   1497  CG  LYS B2063      13.741  34.000  50.758  1.00 12.23           C  
ATOM   1498  CD  LYS B2063      14.321  35.378  50.476  1.00 14.68           C  
ATOM   1499  CE  LYS B2063      14.283  36.265  51.701  1.00 20.27           C  
ATOM   1500  NZ  LYS B2063      14.785  37.630  51.378  1.00 18.64           N  
ATOM   1501  N   ASP B2064      11.229  31.093  50.528  1.00  8.84           N  
ATOM   1502  CA  ASP B2064       9.782  30.956  50.411  1.00  9.49           C  
ATOM   1503  C   ASP B2064       9.066  31.801  51.454  1.00  9.28           C  
ATOM   1504  O   ASP B2064       9.201  31.562  52.652  1.00  8.65           O  
ATOM   1505  CB  ASP B2064       9.409  29.478  50.561  1.00 12.40           C  
ATOM   1506  CG  ASP B2064       8.008  29.170  50.071  1.00 15.57           C  
ATOM   1507  OD1 ASP B2064       7.672  27.971  49.970  1.00 18.18           O  
ATOM   1508  OD2 ASP B2064       7.246  30.119  49.795  1.00 16.05           O  
ATOM   1509  N   ASP B2065       8.298  32.783  50.988  1.00  9.10           N  
ATOM   1510  CA  ASP B2065       7.581  33.695  51.878  1.00 11.17           C  
ATOM   1511  C   ASP B2065       8.558  34.193  52.939  1.00 10.64           C  
ATOM   1512  O   ASP B2065       8.224  34.293  54.121  1.00 10.96           O  
ATOM   1513  CB  ASP B2065       6.382  32.992  52.529  1.00 13.54           C  
ATOM   1514  CG  ASP B2065       5.490  33.951  53.315  1.00 19.94           C  
ATOM   1515  OD1 ASP B2065       5.545  35.175  53.064  1.00 18.91           O  
ATOM   1516  OD2 ASP B2065       4.719  33.478  54.175  1.00 19.10           O  
ATOM   1517  N   GLY B2066       9.780  34.476  52.494  1.00  8.29           N  
ATOM   1518  CA  GLY B2066      10.813  34.981  53.379  1.00  8.41           C  
ATOM   1519  C   GLY B2066      11.757  33.969  54.005  1.00  7.10           C  
ATOM   1520  O   GLY B2066      12.869  34.323  54.383  1.00  9.03           O  
ATOM   1521  N   ALA B2067      11.335  32.715  54.111  1.00  7.09           N  
ATOM   1522  CA  ALA B2067      12.170  31.693  54.741  1.00  6.98           C  
ATOM   1523  C   ALA B2067      13.191  31.028  53.823  1.00  6.17           C  
ATOM   1524  O   ALA B2067      12.848  30.524  52.754  1.00  6.08           O  
ATOM   1525  CB  ALA B2067      11.285  30.627  55.376  1.00  5.78           C  
ATOM   1526  N   TRP B2068      14.449  31.014  54.255  1.00  7.44           N  
ATOM   1527  CA  TRP B2068      15.502  30.382  53.472  1.00  7.10           C  
ATOM   1528  C   TRP B2068      15.391  28.870  53.633  1.00  6.79           C  
ATOM   1529  O   TRP B2068      15.154  28.369  54.737  1.00  8.64           O  
ATOM   1530  CB  TRP B2068      16.887  30.851  53.941  1.00  8.90           C  
ATOM   1531  CG  TRP B2068      17.237  32.248  53.507  1.00  9.36           C  
ATOM   1532  CD1 TRP B2068      17.350  33.359  54.301  1.00 10.43           C  
ATOM   1533  CD2 TRP B2068      17.519  32.679  52.173  1.00 10.41           C  
ATOM   1534  NE1 TRP B2068      17.685  34.455  53.539  1.00 11.97           N  
ATOM   1535  CE2 TRP B2068      17.795  34.065  52.229  1.00 10.81           C  
ATOM   1536  CE3 TRP B2068      17.562  32.029  50.932  1.00  9.17           C  
ATOM   1537  CZ2 TRP B2068      18.114  34.810  51.090  1.00 12.00           C  
ATOM   1538  CZ3 TRP B2068      17.880  32.773  49.799  1.00  9.86           C  
ATOM   1539  CH2 TRP B2068      18.150  34.147  49.887  1.00 10.15           C  
ATOM   1540  N   GLY B2069      15.553  28.147  52.531  1.00  7.55           N  
ATOM   1541  CA  GLY B2069      15.470  26.700  52.576  1.00  6.86           C  
ATOM   1542  C   GLY B2069      16.821  26.080  52.869  1.00  7.78           C  
ATOM   1543  O   GLY B2069      17.705  26.731  53.429  1.00  8.19           O  
ATOM   1544  N   THR B2070      16.983  24.818  52.495  1.00  8.46           N  
ATOM   1545  CA  THR B2070      18.244  24.123  52.710  1.00  8.71           C  
ATOM   1546  C   THR B2070      19.163  24.400  51.531  1.00  7.18           C  
ATOM   1547  O   THR B2070      18.816  24.123  50.383  1.00  7.70           O  
ATOM   1548  CB  THR B2070      18.025  22.606  52.837  1.00  8.72           C  
ATOM   1549  OG1 THR B2070      17.201  22.344  53.977  1.00  7.36           O  
ATOM   1550  CG2 THR B2070      19.358  21.877  52.999  1.00  9.75           C  
ATOM   1551  N   GLU B2071      20.333  24.952  51.820  1.00  7.99           N  
ATOM   1552  CA  GLU B2071      21.296  25.271  50.778  1.00  7.21           C  
ATOM   1553  C   GLU B2071      21.816  24.016  50.089  1.00  8.30           C  
ATOM   1554  O   GLU B2071      21.811  22.926  50.658  1.00  8.28           O  
ATOM   1555  CB  GLU B2071      22.493  26.029  51.370  1.00  8.50           C  
ATOM   1556  CG  GLU B2071      22.133  27.306  52.116  1.00  9.11           C  
ATOM   1557  CD  GLU B2071      23.329  27.924  52.825  1.00 11.31           C  
ATOM   1558  OE1 GLU B2071      24.275  27.181  53.165  1.00  9.99           O  
ATOM   1559  OE2 GLU B2071      23.315  29.149  53.060  1.00 11.81           O  
ATOM   1560  N   GLN B2072      22.254  24.188  48.848  1.00  8.56           N  
ATOM   1561  CA  GLN B2072      22.850  23.110  48.074  1.00  8.35           C  
ATOM   1562  C   GLN B2072      24.116  23.725  47.497  1.00  8.01           C  
ATOM   1563  O   GLN B2072      24.088  24.843  46.979  1.00  8.15           O  
ATOM   1564  CB  GLN B2072      21.922  22.637  46.948  1.00  9.98           C  
ATOM   1565  CG  GLN B2072      20.730  21.812  47.436  1.00 11.08           C  
ATOM   1566  CD  GLN B2072      19.988  21.112  46.309  1.00 11.81           C  
ATOM   1567  OE1 GLN B2072      18.999  20.411  46.543  1.00 17.69           O  
ATOM   1568  NE2 GLN B2072      20.462  21.292  45.084  1.00 10.78           N  
ATOM   1569  N   ARG B2073      25.232  23.017  47.623  1.00  7.14           N  
ATOM   1570  CA  ARG B2073      26.499  23.518  47.105  1.00  6.82           C  
ATOM   1571  C   ARG B2073      26.882  22.748  45.853  1.00  7.69           C  
ATOM   1572  O   ARG B2073      26.681  21.537  45.772  1.00  8.50           O  
ATOM   1573  CB  ARG B2073      27.582  23.413  48.187  1.00  6.27           C  
ATOM   1574  CG  ARG B2073      27.410  24.477  49.265  1.00  6.20           C  
ATOM   1575  CD  ARG B2073      28.338  24.305  50.456  1.00  5.89           C  
ATOM   1576  NE  ARG B2073      28.367  25.530  51.252  1.00  6.52           N  
ATOM   1577  CZ  ARG B2073      27.333  26.013  51.932  1.00  8.01           C  
ATOM   1578  NH1 ARG B2073      27.463  27.143  52.612  1.00  9.24           N  
ATOM   1579  NH2 ARG B2073      26.178  25.358  51.957  1.00 10.84           N  
ATOM   1580  N   GLU B2074      27.434  23.456  44.873  1.00  7.11           N  
ATOM   1581  CA  GLU B2074      27.796  22.828  43.615  1.00  7.24           C  
ATOM   1582  C   GLU B2074      29.201  22.237  43.606  1.00  8.84           C  
ATOM   1583  O   GLU B2074      30.043  22.593  44.422  1.00  8.31           O  
ATOM   1584  CB  GLU B2074      27.612  23.829  42.482  1.00  7.78           C  
ATOM   1585  CG  GLU B2074      26.236  24.515  42.502  1.00  9.21           C  
ATOM   1586  CD  GLU B2074      25.077  23.531  42.646  1.00 11.69           C  
ATOM   1587  OE1 GLU B2074      25.142  22.444  42.038  1.00 10.41           O  
ATOM   1588  OE2 GLU B2074      24.091  23.848  43.355  1.00  9.92           O  
ATOM   1589  N   ALA B2075      29.441  21.337  42.659  1.00  8.97           N  
ATOM   1590  CA  ALA B2075      30.717  20.634  42.549  1.00  9.18           C  
ATOM   1591  C   ALA B2075      31.851  21.367  41.841  1.00  8.67           C  
ATOM   1592  O   ALA B2075      33.002  20.938  41.917  1.00 10.18           O  
ATOM   1593  CB  ALA B2075      30.485  19.285  41.877  1.00  9.32           C  
ATOM   1594  N   VAL B2076      31.537  22.460  41.155  1.00  8.50           N  
ATOM   1595  CA  VAL B2076      32.553  23.212  40.420  1.00  9.00           C  
ATOM   1596  C   VAL B2076      32.508  24.697  40.752  1.00  9.25           C  
ATOM   1597  O   VAL B2076      31.586  25.163  41.422  1.00  9.34           O  
ATOM   1598  CB  VAL B2076      32.363  23.047  38.888  1.00  8.71           C  
ATOM   1599  CG1 VAL B2076      32.395  21.568  38.509  1.00 10.17           C  
ATOM   1600  CG2 VAL B2076      31.044  23.676  38.455  1.00  9.40           C  
ATOM   1601  N   PHE B2077      33.510  25.437  40.287  1.00 10.30           N  
ATOM   1602  CA  PHE B2077      33.556  26.870  40.530  1.00  9.32           C  
ATOM   1603  C   PHE B2077      34.285  27.602  39.409  1.00 11.29           C  
ATOM   1604  O   PHE B2077      35.413  28.071  39.583  1.00 11.11           O  
ATOM   1605  CB  PHE B2077      34.229  27.167  41.871  1.00  9.96           C  
ATOM   1606  CG  PHE B2077      33.984  28.560  42.368  1.00  8.42           C  
ATOM   1607  CD1 PHE B2077      34.907  29.572  42.138  1.00  9.38           C  
ATOM   1608  CD2 PHE B2077      32.806  28.865  43.048  1.00  9.92           C  
ATOM   1609  CE1 PHE B2077      34.666  30.874  42.578  1.00 10.87           C  
ATOM   1610  CE2 PHE B2077      32.550  30.160  43.491  1.00 10.65           C  
ATOM   1611  CZ  PHE B2077      33.485  31.169  43.256  1.00 10.36           C  
ATOM   1612  N   PRO B2078      33.644  27.702  38.236  1.00 12.37           N  
ATOM   1613  CA  PRO B2078      34.213  28.376  37.066  1.00 13.65           C  
ATOM   1614  C   PRO B2078      33.969  29.883  37.094  1.00 13.46           C  
ATOM   1615  O   PRO B2078      33.389  30.441  36.164  1.00 15.59           O  
ATOM   1616  CB  PRO B2078      33.495  27.699  35.906  1.00 13.31           C  
ATOM   1617  CG  PRO B2078      32.127  27.498  36.465  1.00 14.09           C  
ATOM   1618  CD  PRO B2078      32.407  26.985  37.871  1.00 13.38           C  
ATOM   1619  N   PHE B2079      34.397  30.530  38.173  1.00 12.43           N  
ATOM   1620  CA  PHE B2079      34.234  31.971  38.317  1.00 13.00           C  
ATOM   1621  C   PHE B2079      35.497  32.604  38.865  1.00 14.20           C  
ATOM   1622  O   PHE B2079      36.268  31.959  39.568  1.00 14.00           O  
ATOM   1623  CB  PHE B2079      33.072  32.304  39.258  1.00 12.52           C  
ATOM   1624  CG  PHE B2079      31.737  31.880  38.740  1.00 10.60           C  
ATOM   1625  CD1 PHE B2079      31.157  30.689  39.162  1.00 12.32           C  
ATOM   1626  CD2 PHE B2079      31.068  32.660  37.803  1.00 10.01           C  
ATOM   1627  CE1 PHE B2079      29.926  30.277  38.651  1.00 12.45           C  
ATOM   1628  CE2 PHE B2079      29.842  32.259  37.287  1.00 12.19           C  
ATOM   1629  CZ  PHE B2079      29.268  31.064  37.713  1.00 10.44           C  
ATOM   1630  N   GLN B2080      35.695  33.873  38.533  1.00 16.10           N  
ATOM   1631  CA  GLN B2080      36.858  34.616  38.998  1.00 19.57           C  
ATOM   1632  C   GLN B2080      36.490  36.081  39.171  1.00 18.49           C  
ATOM   1633  O   GLN B2080      35.780  36.651  38.346  1.00 18.27           O  
ATOM   1634  CB  GLN B2080      37.999  34.511  37.996  1.00 24.36           C  
ATOM   1635  CG  GLN B2080      37.760  35.254  36.709  1.00 32.10           C  
ATOM   1636  CD  GLN B2080      38.297  34.511  35.516  1.00 35.40           C  
ATOM   1637  OE1 GLN B2080      37.569  33.795  34.836  1.00 40.51           O  
ATOM   1638  NE2 GLN B2080      39.589  34.675  35.253  1.00 38.06           N  
ATOM   1639  N   PRO B2081      36.955  36.709  40.268  1.00 18.31           N  
ATOM   1640  CA  PRO B2081      36.643  38.123  40.494  1.00 17.37           C  
ATOM   1641  C   PRO B2081      37.223  38.938  39.339  1.00 17.74           C  
ATOM   1642  O   PRO B2081      38.215  38.534  38.736  1.00 16.91           O  
ATOM   1643  CB  PRO B2081      37.349  38.425  41.815  1.00 17.97           C  
ATOM   1644  CG  PRO B2081      37.356  37.090  42.515  1.00 18.24           C  
ATOM   1645  CD  PRO B2081      37.717  36.150  41.397  1.00 17.65           C  
ATOM   1646  N   GLY B2082      36.593  40.064  39.022  1.00 17.04           N  
ATOM   1647  CA  GLY B2082      37.082  40.910  37.947  1.00 20.09           C  
ATOM   1648  C   GLY B2082      37.078  40.296  36.559  1.00 20.71           C  
ATOM   1649  O   GLY B2082      38.034  40.454  35.800  1.00 22.41           O  
ATOM   1650  N   SER B2083      36.004  39.593  36.219  1.00 20.30           N  
ATOM   1651  CA  SER B2083      35.890  38.976  34.904  1.00 20.46           C  
ATOM   1652  C   SER B2083      34.424  38.893  34.515  1.00 20.16           C  
ATOM   1653  O   SER B2083      33.540  39.022  35.363  1.00 20.36           O  
ATOM   1654  CB  SER B2083      36.496  37.571  34.911  1.00 22.59           C  
ATOM   1655  OG  SER B2083      35.774  36.712  35.776  1.00 25.88           O  
ATOM   1656  N   VAL B2084      34.174  38.684  33.228  1.00 17.56           N  
ATOM   1657  CA  VAL B2084      32.816  38.572  32.727  1.00 18.36           C  
ATOM   1658  C   VAL B2084      32.375  37.121  32.833  1.00 17.65           C  
ATOM   1659  O   VAL B2084      33.113  36.204  32.464  1.00 18.16           O  
ATOM   1660  CB  VAL B2084      32.720  39.024  31.257  1.00 18.64           C  
ATOM   1661  CG1 VAL B2084      31.310  38.800  30.732  1.00 20.33           C  
ATOM   1662  CG2 VAL B2084      33.099  40.494  31.145  1.00 21.48           C  
ATOM   1663  N   ALA B2085      31.170  36.920  33.349  1.00 16.02           N  
ATOM   1664  CA  ALA B2085      30.633  35.581  33.514  1.00 14.71           C  
ATOM   1665  C   ALA B2085      29.200  35.546  33.021  1.00 13.16           C  
ATOM   1666  O   ALA B2085      28.433  36.478  33.252  1.00 12.78           O  
ATOM   1667  CB  ALA B2085      30.685  35.176  34.977  1.00 15.31           C  
ATOM   1668  N   GLU B2086      28.848  34.468  32.334  1.00 12.71           N  
ATOM   1669  CA  GLU B2086      27.494  34.317  31.835  1.00 12.95           C  
ATOM   1670  C   GLU B2086      26.912  33.019  32.355  1.00 12.68           C  
ATOM   1671  O   GLU B2086      27.600  32.000  32.425  1.00 12.89           O  
ATOM   1672  CB  GLU B2086      27.477  34.316  30.304  1.00 12.45           C  
ATOM   1673  CG  GLU B2086      26.084  34.125  29.709  1.00 15.06           C  
ATOM   1674  CD  GLU B2086      26.055  34.309  28.203  1.00 17.97           C  
ATOM   1675  OE1 GLU B2086      25.059  33.899  27.573  1.00 18.66           O  
ATOM   1676  OE2 GLU B2086      27.024  34.871  27.650  1.00 19.85           O  
ATOM   1677  N   VAL B2087      25.648  33.070  32.755  1.00 11.64           N  
ATOM   1678  CA  VAL B2087      24.970  31.884  33.244  1.00 11.37           C  
ATOM   1679  C   VAL B2087      23.673  31.774  32.463  1.00 12.07           C  
ATOM   1680  O   VAL B2087      23.090  32.780  32.057  1.00 11.84           O  
ATOM   1681  CB  VAL B2087      24.671  31.966  34.762  1.00 13.68           C  
ATOM   1682  CG1 VAL B2087      25.981  32.053  35.537  1.00 12.64           C  
ATOM   1683  CG2 VAL B2087      23.789  33.163  35.068  1.00 13.29           C  
ATOM   1684  N   CYS B2088      23.239  30.545  32.231  1.00 11.08           N  
ATOM   1685  CA  CYS B2088      22.021  30.308  31.486  1.00 11.85           C  
ATOM   1686  C   CYS B2088      21.088  29.495  32.369  1.00 11.97           C  
ATOM   1687  O   CYS B2088      21.460  28.434  32.873  1.00 13.32           O  
ATOM   1688  CB  CYS B2088      22.358  29.584  30.181  1.00 14.01           C  
ATOM   1689  SG  CYS B2088      23.493  30.555  29.142  1.00 15.68           S  
ATOM   1690  N   ILE B2089      19.883  30.009  32.577  1.00 11.59           N  
ATOM   1691  CA  ILE B2089      18.919  29.330  33.428  1.00 11.01           C  
ATOM   1692  C   ILE B2089      17.624  28.988  32.708  1.00 11.37           C  
ATOM   1693  O   ILE B2089      17.110  29.772  31.913  1.00  9.87           O  
ATOM   1694  CB  ILE B2089      18.556  30.189  34.673  1.00 12.64           C  
ATOM   1695  CG1 ILE B2089      19.811  30.506  35.489  1.00 13.73           C  
ATOM   1696  CG2 ILE B2089      17.553  29.451  35.544  1.00 12.27           C  
ATOM   1697  CD1 ILE B2089      20.551  31.736  35.020  1.00 18.51           C  
ATOM   1698  N   THR B2090      17.108  27.801  32.997  1.00 10.85           N  
ATOM   1699  CA  THR B2090      15.849  27.350  32.426  1.00 11.57           C  
ATOM   1700  C   THR B2090      15.174  26.578  33.552  1.00 11.59           C  
ATOM   1701  O   THR B2090      15.818  26.237  34.549  1.00  9.84           O  
ATOM   1702  CB  THR B2090      16.066  26.424  31.212  1.00 13.18           C  
ATOM   1703  OG1 THR B2090      14.801  26.127  30.608  1.00 19.66           O  
ATOM   1704  CG2 THR B2090      16.739  25.127  31.637  1.00 12.68           C  
ATOM   1705  N   PHE B2091      13.884  26.307  33.418  1.00 10.13           N  
ATOM   1706  CA  PHE B2091      13.208  25.577  34.476  1.00 10.03           C  
ATOM   1707  C   PHE B2091      11.949  24.872  34.013  1.00 11.17           C  
ATOM   1708  O   PHE B2091      11.410  25.155  32.942  1.00 11.36           O  
ATOM   1709  CB  PHE B2091      12.837  26.526  35.622  1.00  8.97           C  
ATOM   1710  CG  PHE B2091      11.670  27.433  35.309  1.00 11.37           C  
ATOM   1711  CD1 PHE B2091      11.833  28.546  34.492  1.00 11.97           C  
ATOM   1712  CD2 PHE B2091      10.400  27.152  35.813  1.00 11.28           C  
ATOM   1713  CE1 PHE B2091      10.748  29.372  34.174  1.00 13.26           C  
ATOM   1714  CE2 PHE B2091       9.305  27.971  35.502  1.00 12.13           C  
ATOM   1715  CZ  PHE B2091       9.482  29.081  34.682  1.00 12.08           C  
ATOM   1716  N   ASP B2092      11.513  23.926  34.833  1.00 11.00           N  
ATOM   1717  CA  ASP B2092      10.276  23.197  34.606  1.00 13.14           C  
ATOM   1718  C   ASP B2092       9.688  23.141  36.008  1.00 14.16           C  
ATOM   1719  O   ASP B2092      10.282  23.684  36.941  1.00 12.27           O  
ATOM   1720  CB  ASP B2092      10.518  21.789  34.029  1.00 15.02           C  
ATOM   1721  CG  ASP B2092      11.459  20.948  34.869  1.00 15.71           C  
ATOM   1722  OD1 ASP B2092      11.262  20.855  36.097  1.00 15.27           O  
ATOM   1723  OD2 ASP B2092      12.393  20.360  34.288  1.00 19.93           O  
ATOM   1724  N   GLN B2093       8.537  22.504  36.170  1.00 14.77           N  
ATOM   1725  CA  GLN B2093       7.900  22.442  37.479  1.00 16.18           C  
ATOM   1726  C   GLN B2093       8.731  21.805  38.590  1.00 14.02           C  
ATOM   1727  O   GLN B2093       8.594  22.176  39.757  1.00 13.45           O  
ATOM   1728  CB  GLN B2093       6.546  21.725  37.371  1.00 20.17           C  
ATOM   1729  CG  GLN B2093       6.526  20.514  36.442  1.00 26.64           C  
ATOM   1730  CD  GLN B2093       7.328  19.335  36.962  1.00 30.18           C  
ATOM   1731  OE1 GLN B2093       7.024  18.776  38.019  1.00 31.22           O  
ATOM   1732  NE2 GLN B2093       8.357  18.945  36.214  1.00 31.74           N  
ATOM   1733  N   ALA B2094       9.603  20.869  38.230  1.00 11.98           N  
ATOM   1734  CA  ALA B2094      10.412  20.169  39.220  1.00 10.95           C  
ATOM   1735  C   ALA B2094      11.764  20.787  39.553  1.00 10.24           C  
ATOM   1736  O   ALA B2094      12.134  20.882  40.726  1.00 10.19           O  
ATOM   1737  CB  ALA B2094      10.615  18.724  38.783  1.00 11.90           C  
ATOM   1738  N   ASN B2095      12.502  21.201  38.530  1.00 10.38           N  
ATOM   1739  CA  ASN B2095      13.833  21.757  38.750  1.00  9.85           C  
ATOM   1740  C   ASN B2095      14.203  22.920  37.857  1.00 10.04           C  
ATOM   1741  O   ASN B2095      13.640  23.109  36.776  1.00  9.52           O  
ATOM   1742  CB  ASN B2095      14.903  20.686  38.506  1.00  9.82           C  
ATOM   1743  CG  ASN B2095      14.773  19.494  39.421  1.00 11.47           C  
ATOM   1744  OD1 ASN B2095      15.168  19.544  40.586  1.00 11.28           O  
ATOM   1745  ND2 ASN B2095      14.222  18.405  38.894  1.00  9.21           N  
ATOM   1746  N   LEU B2096      15.175  23.691  38.331  1.00  8.33           N  
ATOM   1747  CA  LEU B2096      15.733  24.773  37.551  1.00  7.75           C  
ATOM   1748  C   LEU B2096      17.041  24.156  37.084  1.00  8.28           C  
ATOM   1749  O   LEU B2096      17.635  23.340  37.792  1.00  8.70           O  
ATOM   1750  CB  LEU B2096      16.035  26.009  38.402  1.00  8.75           C  
ATOM   1751  CG  LEU B2096      14.850  26.917  38.728  1.00 10.55           C  
ATOM   1752  CD1 LEU B2096      14.198  26.442  40.008  1.00 13.28           C  
ATOM   1753  CD2 LEU B2096      15.322  28.358  38.877  1.00 12.56           C  
ATOM   1754  N   THR B2097      17.473  24.513  35.887  1.00  7.81           N  
ATOM   1755  CA  THR B2097      18.727  24.002  35.362  1.00  7.33           C  
ATOM   1756  C   THR B2097      19.595  25.226  35.137  1.00  8.86           C  
ATOM   1757  O   THR B2097      19.187  26.168  34.457  1.00  8.79           O  
ATOM   1758  CB  THR B2097      18.523  23.260  34.029  1.00 10.12           C  
ATOM   1759  OG1 THR B2097      17.683  22.117  34.243  1.00  8.61           O  
ATOM   1760  CG2 THR B2097      19.866  22.802  33.461  1.00  9.12           C  
ATOM   1761  N   VAL B2098      20.783  25.216  35.728  1.00  8.65           N  
ATOM   1762  CA  VAL B2098      21.709  26.331  35.611  1.00  7.59           C  
ATOM   1763  C   VAL B2098      22.961  25.883  34.872  1.00  7.98           C  
ATOM   1764  O   VAL B2098      23.618  24.927  35.277  1.00  7.63           O  
ATOM   1765  CB  VAL B2098      22.122  26.856  37.006  1.00  8.57           C  
ATOM   1766  CG1 VAL B2098      23.113  27.994  36.864  1.00  7.62           C  
ATOM   1767  CG2 VAL B2098      20.883  27.310  37.781  1.00  9.58           C  
ATOM   1768  N   LYS B2099      23.279  26.570  33.781  1.00  7.29           N  
ATOM   1769  CA  LYS B2099      24.461  26.242  33.004  1.00  8.14           C  
ATOM   1770  C   LYS B2099      25.483  27.337  33.269  1.00  8.39           C  
ATOM   1771  O   LYS B2099      25.173  28.525  33.176  1.00 10.20           O  
ATOM   1772  CB  LYS B2099      24.107  26.168  31.523  1.00  9.87           C  
ATOM   1773  CG  LYS B2099      25.198  25.582  30.656  1.00 13.44           C  
ATOM   1774  CD  LYS B2099      24.636  25.269  29.279  1.00 15.52           C  
ATOM   1775  CE  LYS B2099      25.670  24.635  28.388  1.00 18.56           C  
ATOM   1776  NZ  LYS B2099      25.081  24.327  27.060  1.00 16.44           N  
ATOM   1777  N   LEU B2100      26.702  26.931  33.595  1.00  7.19           N  
ATOM   1778  CA  LEU B2100      27.762  27.873  33.934  1.00  9.29           C  
ATOM   1779  C   LEU B2100      28.674  28.253  32.774  1.00 10.18           C  
ATOM   1780  O   LEU B2100      28.557  27.712  31.674  1.00 10.66           O  
ATOM   1781  CB  LEU B2100      28.590  27.286  35.081  1.00  6.69           C  
ATOM   1782  CG  LEU B2100      27.729  26.889  36.280  1.00  8.53           C  
ATOM   1783  CD1 LEU B2100      28.586  26.201  37.333  1.00  8.05           C  
ATOM   1784  CD2 LEU B2100      27.051  28.132  36.849  1.00  8.40           C  
ATOM   1785  N   PRO B2101      29.591  29.207  33.007  1.00 11.01           N  
ATOM   1786  CA  PRO B2101      30.524  29.654  31.968  1.00 13.13           C  
ATOM   1787  C   PRO B2101      31.332  28.512  31.349  1.00 14.62           C  
ATOM   1788  O   PRO B2101      31.692  28.567  30.175  1.00 17.54           O  
ATOM   1789  CB  PRO B2101      31.416  30.642  32.714  1.00 12.58           C  
ATOM   1790  CG  PRO B2101      30.469  31.253  33.703  1.00 12.15           C  
ATOM   1791  CD  PRO B2101      29.721  30.043  34.217  1.00 12.05           C  
ATOM   1792  N   ASP B2102      31.612  27.483  32.141  1.00 14.91           N  
ATOM   1793  CA  ASP B2102      32.391  26.341  31.670  1.00 16.17           C  
ATOM   1794  C   ASP B2102      31.558  25.281  30.953  1.00 16.75           C  
ATOM   1795  O   ASP B2102      32.064  24.203  30.637  1.00 17.53           O  
ATOM   1796  CB  ASP B2102      33.139  25.695  32.845  1.00 17.58           C  
ATOM   1797  CG  ASP B2102      32.200  25.112  33.883  1.00 18.98           C  
ATOM   1798  OD1 ASP B2102      30.988  25.404  33.817  1.00 18.11           O  
ATOM   1799  OD2 ASP B2102      32.672  24.368  34.772  1.00 21.78           O  
ATOM   1800  N   GLY B2103      30.288  25.584  30.692  1.00 14.71           N  
ATOM   1801  CA  GLY B2103      29.425  24.627  30.017  1.00 12.88           C  
ATOM   1802  C   GLY B2103      28.831  23.590  30.957  1.00 12.82           C  
ATOM   1803  O   GLY B2103      27.997  22.778  30.555  1.00 11.03           O  
ATOM   1804  N   TYR B2104      29.272  23.610  32.210  1.00 10.22           N  
ATOM   1805  CA  TYR B2104      28.775  22.679  33.218  1.00  9.46           C  
ATOM   1806  C   TYR B2104      27.376  23.110  33.629  1.00  8.60           C  
ATOM   1807  O   TYR B2104      27.123  24.296  33.814  1.00  9.00           O  
ATOM   1808  CB  TYR B2104      29.682  22.706  34.447  1.00 10.18           C  
ATOM   1809  CG  TYR B2104      29.216  21.838  35.599  1.00 10.29           C  
ATOM   1810  CD1 TYR B2104      29.601  20.498  35.692  1.00 10.60           C  
ATOM   1811  CD2 TYR B2104      28.420  22.364  36.616  1.00 10.63           C  
ATOM   1812  CE1 TYR B2104      29.213  19.709  36.773  1.00 10.81           C  
ATOM   1813  CE2 TYR B2104      28.024  21.585  37.699  1.00  9.97           C  
ATOM   1814  CZ  TYR B2104      28.427  20.261  37.775  1.00 12.09           C  
ATOM   1815  OH  TYR B2104      28.068  19.504  38.865  1.00 12.82           O  
ATOM   1816  N   GLU B2105      26.462  22.156  33.768  1.00  8.50           N  
ATOM   1817  CA  GLU B2105      25.107  22.504  34.176  1.00  8.98           C  
ATOM   1818  C   GLU B2105      24.626  21.602  35.301  1.00  9.17           C  
ATOM   1819  O   GLU B2105      24.931  20.409  35.333  1.00 10.23           O  
ATOM   1820  CB  GLU B2105      24.138  22.411  32.996  1.00  9.38           C  
ATOM   1821  CG  GLU B2105      23.849  20.995  32.541  1.00  8.91           C  
ATOM   1822  CD  GLU B2105      22.693  20.922  31.558  1.00  9.76           C  
ATOM   1823  OE1 GLU B2105      22.248  19.796  31.255  1.00 10.84           O  
ATOM   1824  OE2 GLU B2105      22.232  21.986  31.091  1.00 11.66           O  
ATOM   1825  N   PHE B2106      23.882  22.185  36.232  1.00  8.77           N  
ATOM   1826  CA  PHE B2106      23.351  21.429  37.356  1.00  8.45           C  
ATOM   1827  C   PHE B2106      21.902  21.819  37.574  1.00  8.03           C  
ATOM   1828  O   PHE B2106      21.420  22.800  37.004  1.00  7.92           O  
ATOM   1829  CB  PHE B2106      24.147  21.713  38.634  1.00  7.62           C  
ATOM   1830  CG  PHE B2106      24.062  23.142  39.101  1.00  8.48           C  
ATOM   1831  CD1 PHE B2106      24.940  24.103  38.608  1.00  8.24           C  
ATOM   1832  CD2 PHE B2106      23.088  23.530  40.019  1.00  7.56           C  
ATOM   1833  CE1 PHE B2106      24.850  25.434  39.023  1.00  9.64           C  
ATOM   1834  CE2 PHE B2106      22.990  24.854  40.438  1.00  8.77           C  
ATOM   1835  CZ  PHE B2106      23.874  25.809  39.939  1.00  8.78           C  
ATOM   1836  N   LYS B2107      21.206  21.046  38.399  1.00  7.33           N  
ATOM   1837  CA  LYS B2107      19.817  21.340  38.691  1.00  7.89           C  
ATOM   1838  C   LYS B2107      19.607  21.705  40.148  1.00  8.07           C  
ATOM   1839  O   LYS B2107      20.326  21.242  41.032  1.00  9.46           O  
ATOM   1840  CB  LYS B2107      18.922  20.147  38.346  1.00  9.87           C  
ATOM   1841  CG  LYS B2107      18.816  19.862  36.861  1.00 10.68           C  
ATOM   1842  CD  LYS B2107      17.694  18.871  36.592  1.00 13.13           C  
ATOM   1843  CE  LYS B2107      17.506  18.639  35.101  1.00 14.36           C  
ATOM   1844  NZ  LYS B2107      16.368  17.715  34.843  1.00 13.72           N  
ATOM   1845  N   PHE B2108      18.619  22.559  40.378  1.00  6.90           N  
ATOM   1846  CA  PHE B2108      18.248  22.985  41.719  1.00  7.01           C  
ATOM   1847  C   PHE B2108      16.741  22.795  41.750  1.00  7.63           C  
ATOM   1848  O   PHE B2108      16.037  23.226  40.827  1.00  7.15           O  
ATOM   1849  CB  PHE B2108      18.591  24.458  41.951  1.00  6.52           C  
ATOM   1850  CG  PHE B2108      18.319  24.921  43.355  1.00  7.34           C  
ATOM   1851  CD1 PHE B2108      19.113  24.478  44.411  1.00  8.40           C  
ATOM   1852  CD2 PHE B2108      17.253  25.772  43.628  1.00  8.32           C  
ATOM   1853  CE1 PHE B2108      18.845  24.876  45.728  1.00  8.66           C  
ATOM   1854  CE2 PHE B2108      16.974  26.178  44.937  1.00  7.54           C  
ATOM   1855  CZ  PHE B2108      17.772  25.727  45.990  1.00  7.88           C  
ATOM   1856  N   PRO B2109      16.219  22.139  42.798  1.00  7.55           N  
ATOM   1857  CA  PRO B2109      14.773  21.913  42.884  1.00  6.95           C  
ATOM   1858  C   PRO B2109      13.953  23.197  42.856  1.00  7.67           C  
ATOM   1859  O   PRO B2109      14.348  24.211  43.435  1.00  8.59           O  
ATOM   1860  CB  PRO B2109      14.610  21.164  44.209  1.00  8.39           C  
ATOM   1861  CG  PRO B2109      15.945  20.502  44.410  1.00 11.56           C  
ATOM   1862  CD  PRO B2109      16.906  21.588  43.978  1.00  7.69           C  
ATOM   1863  N   ASN B2110      12.812  23.136  42.176  1.00  7.41           N  
ATOM   1864  CA  ASN B2110      11.902  24.273  42.072  1.00  7.49           C  
ATOM   1865  C   ASN B2110      10.980  24.145  43.278  1.00  8.91           C  
ATOM   1866  O   ASN B2110       9.870  23.621  43.169  1.00  8.18           O  
ATOM   1867  CB  ASN B2110      11.094  24.172  40.776  1.00  8.25           C  
ATOM   1868  CG  ASN B2110      10.260  25.407  40.511  1.00  8.45           C  
ATOM   1869  OD1 ASN B2110      10.042  26.227  41.401  1.00  9.51           O  
ATOM   1870  ND2 ASN B2110       9.775  25.537  39.282  1.00 11.58           N  
ATOM   1871  N   ARG B2111      11.455  24.626  44.424  1.00  7.51           N  
ATOM   1872  CA  ARG B2111      10.720  24.534  45.681  1.00  8.12           C  
ATOM   1873  C   ARG B2111       9.536  25.476  45.828  1.00  8.66           C  
ATOM   1874  O   ARG B2111       8.745  25.338  46.757  1.00  8.89           O  
ATOM   1875  CB  ARG B2111      11.680  24.754  46.839  1.00  6.86           C  
ATOM   1876  CG  ARG B2111      12.797  23.729  46.891  1.00  8.26           C  
ATOM   1877  CD  ARG B2111      13.935  24.260  47.723  1.00  7.57           C  
ATOM   1878  NE  ARG B2111      14.920  23.235  48.046  1.00  7.30           N  
ATOM   1879  CZ  ARG B2111      16.048  23.488  48.697  1.00  6.06           C  
ATOM   1880  NH1 ARG B2111      16.318  24.731  49.079  1.00  6.16           N  
ATOM   1881  NH2 ARG B2111      16.894  22.506  48.975  1.00  7.85           N  
ATOM   1882  N   LEU B2112       9.425  26.449  44.935  1.00  8.10           N  
ATOM   1883  CA  LEU B2112       8.306  27.376  44.997  1.00  9.19           C  
ATOM   1884  C   LEU B2112       7.255  26.963  43.976  1.00 10.34           C  
ATOM   1885  O   LEU B2112       6.202  27.588  43.862  1.00 10.03           O  
ATOM   1886  CB  LEU B2112       8.783  28.807  44.737  1.00 11.05           C  
ATOM   1887  CG  LEU B2112       9.345  29.568  45.946  1.00 11.65           C  
ATOM   1888  CD1 LEU B2112      10.533  28.831  46.546  1.00 15.01           C  
ATOM   1889  CD2 LEU B2112       9.747  30.966  45.504  1.00 11.79           C  
ATOM   1890  N   ASN B2113       7.554  25.895  43.242  1.00 11.97           N  
ATOM   1891  CA  ASN B2113       6.650  25.361  42.232  1.00 13.56           C  
ATOM   1892  C   ASN B2113       6.256  26.445  41.238  1.00 14.08           C  
ATOM   1893  O   ASN B2113       5.128  26.476  40.750  1.00 14.20           O  
ATOM   1894  CB  ASN B2113       5.398  24.796  42.910  1.00 13.47           C  
ATOM   1895  CG  ASN B2113       5.711  24.126  44.232  1.00 15.18           C  
ATOM   1896  OD1 ASN B2113       5.252  24.566  45.289  1.00 16.76           O  
ATOM   1897  ND2 ASN B2113       6.508  23.063  44.183  1.00 11.96           N  
ATOM   1898  N   LEU B2114       7.194  27.336  40.941  1.00 15.19           N  
ATOM   1899  CA  LEU B2114       6.935  28.423  40.008  1.00 16.38           C  
ATOM   1900  C   LEU B2114       6.648  27.923  38.601  1.00 16.09           C  
ATOM   1901  O   LEU B2114       7.314  27.014  38.098  1.00 13.71           O  
ATOM   1902  CB  LEU B2114       8.123  29.387  39.976  1.00 17.52           C  
ATOM   1903  CG  LEU B2114       8.027  30.653  40.834  1.00 21.57           C  
ATOM   1904  CD1 LEU B2114       7.447  30.329  42.193  1.00 22.65           C  
ATOM   1905  CD2 LEU B2114       9.406  31.284  40.962  1.00 19.26           C  
ATOM   1906  N   GLU B2115       5.639  28.521  37.978  1.00 16.24           N  
ATOM   1907  CA  GLU B2115       5.253  28.177  36.618  1.00 17.51           C  
ATOM   1908  C   GLU B2115       5.682  29.342  35.725  1.00 16.85           C  
ATOM   1909  O   GLU B2115       5.425  29.362  34.522  1.00 16.16           O  
ATOM   1910  CB  GLU B2115       3.739  27.945  36.550  1.00 20.39           C  
ATOM   1911  CG  GLU B2115       3.263  26.859  37.527  1.00 23.68           C  
ATOM   1912  CD  GLU B2115       1.769  26.579  37.447  1.00 25.89           C  
ATOM   1913  OE1 GLU B2115       1.283  25.728  38.228  1.00 26.82           O  
ATOM   1914  OE2 GLU B2115       1.085  27.204  36.609  1.00 27.77           O  
ATOM   1915  N   ALA B2116       6.353  30.309  36.344  1.00 16.46           N  
ATOM   1916  CA  ALA B2116       6.870  31.489  35.659  1.00 14.66           C  
ATOM   1917  C   ALA B2116       7.817  32.229  36.595  1.00 13.82           C  
ATOM   1918  O   ALA B2116       7.602  32.263  37.806  1.00 12.82           O  
ATOM   1919  CB  ALA B2116       5.731  32.405  35.243  1.00 17.70           C  
ATOM   1920  N   ILE B2117       8.875  32.800  36.032  1.00 11.10           N  
ATOM   1921  CA  ILE B2117       9.847  33.560  36.809  1.00 11.30           C  
ATOM   1922  C   ILE B2117       9.715  35.008  36.361  1.00 12.06           C  
ATOM   1923  O   ILE B2117       9.992  35.331  35.204  1.00 12.00           O  
ATOM   1924  CB  ILE B2117      11.286  33.072  36.542  1.00 11.50           C  
ATOM   1925  CG1 ILE B2117      11.431  31.620  37.009  1.00 12.41           C  
ATOM   1926  CG2 ILE B2117      12.282  33.980  37.258  1.00 12.74           C  
ATOM   1927  CD1 ILE B2117      12.821  31.032  36.811  1.00 15.17           C  
ATOM   1928  N   ASN B2118       9.291  35.878  37.271  1.00 11.90           N  
ATOM   1929  CA  ASN B2118       9.095  37.283  36.932  1.00 12.82           C  
ATOM   1930  C   ASN B2118      10.070  38.267  37.557  1.00 11.63           C  
ATOM   1931  O   ASN B2118      10.096  39.437  37.182  1.00 13.89           O  
ATOM   1932  CB  ASN B2118       7.672  37.705  37.306  1.00 15.87           C  
ATOM   1933  CG  ASN B2118       6.634  37.130  36.372  1.00 18.87           C  
ATOM   1934  OD1 ASN B2118       5.861  36.243  36.744  1.00 22.71           O  
ATOM   1935  ND2 ASN B2118       6.614  37.629  35.142  1.00 15.55           N  
ATOM   1936  N   TYR B2119      10.878  37.795  38.496  1.00 10.30           N  
ATOM   1937  CA  TYR B2119      11.811  38.665  39.195  1.00  9.88           C  
ATOM   1938  C   TYR B2119      13.260  38.193  39.138  1.00  9.60           C  
ATOM   1939  O   TYR B2119      13.544  37.003  39.249  1.00  8.50           O  
ATOM   1940  CB  TYR B2119      11.360  38.775  40.657  1.00 10.05           C  
ATOM   1941  CG  TYR B2119      12.305  39.502  41.589  1.00 10.27           C  
ATOM   1942  CD1 TYR B2119      12.248  40.890  41.738  1.00  9.93           C  
ATOM   1943  CD2 TYR B2119      13.233  38.794  42.354  1.00  9.11           C  
ATOM   1944  CE1 TYR B2119      13.089  41.553  42.632  1.00  9.61           C  
ATOM   1945  CE2 TYR B2119      14.076  39.443  43.247  1.00  9.38           C  
ATOM   1946  CZ  TYR B2119      13.998  40.820  43.385  1.00 10.46           C  
ATOM   1947  OH  TYR B2119      14.820  41.456  44.288  1.00 12.65           O  
ATOM   1948  N   MET B2120      14.166  39.146  38.947  1.00  9.80           N  
ATOM   1949  CA  MET B2120      15.593  38.871  38.924  1.00 10.65           C  
ATOM   1950  C   MET B2120      16.302  40.080  39.505  1.00 11.79           C  
ATOM   1951  O   MET B2120      15.921  41.225  39.241  1.00 12.38           O  
ATOM   1952  CB  MET B2120      16.104  38.625  37.506  1.00 12.32           C  
ATOM   1953  CG  MET B2120      17.622  38.486  37.448  1.00 14.66           C  
ATOM   1954  SD  MET B2120      18.256  38.231  35.785  1.00 20.85           S  
ATOM   1955  CE  MET B2120      18.111  39.873  35.124  1.00 18.25           C  
ATOM   1956  N   ALA B2121      17.336  39.825  40.294  1.00 11.10           N  
ATOM   1957  CA  ALA B2121      18.096  40.899  40.909  1.00 10.77           C  
ATOM   1958  C   ALA B2121      19.518  40.441  41.181  1.00 11.70           C  
ATOM   1959  O   ALA B2121      19.743  39.337  41.678  1.00 11.29           O  
ATOM   1960  CB  ALA B2121      17.431  41.332  42.210  1.00 11.00           C  
ATOM   1961  N   ALA B2122      20.474  41.296  40.838  1.00 11.53           N  
ATOM   1962  CA  ALA B2122      21.884  41.010  41.059  1.00 12.14           C  
ATOM   1963  C   ALA B2122      22.339  41.919  42.191  1.00 13.58           C  
ATOM   1964  O   ALA B2122      21.742  42.974  42.410  1.00 14.07           O  
ATOM   1965  CB  ALA B2122      22.683  41.309  39.791  1.00 11.81           C  
ATOM   1966  N   ASP B2123      23.374  41.522  42.924  1.00 13.24           N  
ATOM   1967  CA  ASP B2123      23.849  42.380  44.000  1.00 15.19           C  
ATOM   1968  C   ASP B2123      24.948  43.301  43.478  1.00 16.57           C  
ATOM   1969  O   ASP B2123      25.222  43.327  42.276  1.00 17.02           O  
ATOM   1970  CB  ASP B2123      24.338  41.560  45.205  1.00 15.21           C  
ATOM   1971  CG  ASP B2123      25.585  40.745  44.911  1.00 16.51           C  
ATOM   1972  OD1 ASP B2123      26.076  40.081  45.849  1.00 17.32           O  
ATOM   1973  OD2 ASP B2123      26.073  40.761  43.764  1.00 16.27           O  
ATOM   1974  N   GLY B2124      25.572  44.053  44.378  1.00 17.04           N  
ATOM   1975  CA  GLY B2124      26.604  44.989  43.972  1.00 17.06           C  
ATOM   1976  C   GLY B2124      27.891  44.423  43.399  1.00 16.89           C  
ATOM   1977  O   GLY B2124      28.734  45.185  42.931  1.00 17.42           O  
ATOM   1978  N   ASP B2125      28.051  43.103  43.416  1.00 14.40           N  
ATOM   1979  CA  ASP B2125      29.271  42.491  42.898  1.00 14.37           C  
ATOM   1980  C   ASP B2125      29.109  41.851  41.525  1.00 13.64           C  
ATOM   1981  O   ASP B2125      30.065  41.321  40.959  1.00 13.85           O  
ATOM   1982  CB  ASP B2125      29.801  41.461  43.899  1.00 14.74           C  
ATOM   1983  CG  ASP B2125      30.448  42.113  45.111  1.00 17.38           C  
ATOM   1984  OD1 ASP B2125      30.127  41.722  46.250  1.00 16.91           O  
ATOM   1985  OD2 ASP B2125      31.284  43.020  44.917  1.00 17.83           O  
ATOM   1986  N   PHE B2126      27.897  41.909  40.989  1.00 13.23           N  
ATOM   1987  CA  PHE B2126      27.630  41.341  39.677  1.00 14.31           C  
ATOM   1988  C   PHE B2126      26.910  42.381  38.832  1.00 13.41           C  
ATOM   1989  O   PHE B2126      25.696  42.566  38.955  1.00 13.49           O  
ATOM   1990  CB  PHE B2126      26.775  40.077  39.812  1.00 13.14           C  
ATOM   1991  CG  PHE B2126      26.638  39.293  38.535  1.00 14.11           C  
ATOM   1992  CD1 PHE B2126      27.765  38.872  37.837  1.00 14.53           C  
ATOM   1993  CD2 PHE B2126      25.381  38.948  38.047  1.00 14.08           C  
ATOM   1994  CE1 PHE B2126      27.645  38.117  36.671  1.00 14.84           C  
ATOM   1995  CE2 PHE B2126      25.247  38.195  36.886  1.00 14.05           C  
ATOM   1996  CZ  PHE B2126      26.383  37.777  36.196  1.00 14.18           C  
ATOM   1997  N   LYS B2127      27.670  43.068  37.986  1.00 13.33           N  
ATOM   1998  CA  LYS B2127      27.115  44.100  37.118  1.00 14.09           C  
ATOM   1999  C   LYS B2127      26.613  43.468  35.826  1.00 12.31           C  
ATOM   2000  O   LYS B2127      27.399  43.092  34.954  1.00 11.93           O  
ATOM   2001  CB  LYS B2127      28.178  45.156  36.802  1.00 15.77           C  
ATOM   2002  CG  LYS B2127      27.649  46.355  36.030  1.00 17.82           C  
ATOM   2003  CD  LYS B2127      28.763  47.349  35.742  1.00 22.06           C  
ATOM   2004  CE  LYS B2127      28.231  48.585  35.036  1.00 25.51           C  
ATOM   2005  NZ  LYS B2127      29.314  49.579  34.786  1.00 29.23           N  
ATOM   2006  N   ILE B2128      25.297  43.341  35.715  1.00 12.69           N  
ATOM   2007  CA  ILE B2128      24.694  42.743  34.535  1.00 12.10           C  
ATOM   2008  C   ILE B2128      24.956  43.596  33.296  1.00 12.93           C  
ATOM   2009  O   ILE B2128      24.709  44.805  33.293  1.00 13.40           O  
ATOM   2010  CB  ILE B2128      23.173  42.541  34.745  1.00 12.36           C  
ATOM   2011  CG1 ILE B2128      22.954  41.511  35.862  1.00 12.85           C  
ATOM   2012  CG2 ILE B2128      22.510  42.091  33.447  1.00 10.87           C  
ATOM   2013  CD1 ILE B2128      21.492  41.175  36.141  1.00 15.79           C  
ATOM   2014  N   LYS B2129      25.471  42.954  32.250  1.00 13.20           N  
ATOM   2015  CA  LYS B2129      25.781  43.637  30.998  1.00 13.36           C  
ATOM   2016  C   LYS B2129      24.759  43.313  29.912  1.00 13.67           C  
ATOM   2017  O   LYS B2129      24.562  44.093  28.981  1.00 11.78           O  
ATOM   2018  CB  LYS B2129      27.180  43.247  30.517  1.00 15.78           C  
ATOM   2019  CG  LYS B2129      28.297  43.616  31.489  1.00 17.10           C  
ATOM   2020  CD  LYS B2129      28.301  45.108  31.811  1.00 20.28           C  
ATOM   2021  CE  LYS B2129      28.552  45.957  30.574  1.00 22.99           C  
ATOM   2022  NZ  LYS B2129      28.546  47.415  30.896  1.00 25.27           N  
ATOM   2023  N   CYS B2130      24.117  42.156  30.021  1.00 13.79           N  
ATOM   2024  CA  CYS B2130      23.110  41.786  29.039  1.00 15.99           C  
ATOM   2025  C   CYS B2130      22.229  40.663  29.556  1.00 14.58           C  
ATOM   2026  O   CYS B2130      22.662  39.815  30.338  1.00 13.38           O  
ATOM   2027  CB  CYS B2130      23.732  41.377  27.699  1.00 22.36           C  
ATOM   2028  SG  CYS B2130      24.606  39.797  27.679  1.00 31.21           S  
ATOM   2029  N   VAL B2131      20.980  40.683  29.112  1.00 12.24           N  
ATOM   2030  CA  VAL B2131      20.009  39.672  29.487  1.00 12.49           C  
ATOM   2031  C   VAL B2131      19.280  39.289  28.211  1.00 12.68           C  
ATOM   2032  O   VAL B2131      18.823  40.157  27.466  1.00 13.16           O  
ATOM   2033  CB  VAL B2131      18.990  40.212  30.505  1.00 13.52           C  
ATOM   2034  CG1 VAL B2131      17.924  39.160  30.777  1.00 13.81           C  
ATOM   2035  CG2 VAL B2131      19.701  40.595  31.797  1.00 14.98           C  
ATOM   2036  N   ALA B2132      19.189  37.991  27.950  1.00 13.28           N  
ATOM   2037  CA  ALA B2132      18.513  37.511  26.755  1.00 13.10           C  
ATOM   2038  C   ALA B2132      17.472  36.471  27.130  1.00 14.98           C  
ATOM   2039  O   ALA B2132      17.621  35.758  28.124  1.00 12.68           O  
ATOM   2040  CB  ALA B2132      19.527  36.913  25.783  1.00 13.16           C  
ATOM   2041  N   PHE B2133      16.411  36.401  26.336  1.00 16.04           N  
ATOM   2042  CA  PHE B2133      15.342  35.442  26.569  1.00 19.85           C  
ATOM   2043  C   PHE B2133      15.178  34.620  25.297  1.00 22.88           C  
ATOM   2044  O   PHE B2133      14.846  35.157  24.242  1.00 23.06           O  
ATOM   2045  CB  PHE B2133      14.031  36.167  26.892  1.00 19.36           C  
ATOM   2046  CG  PHE B2133      14.168  37.229  27.948  1.00 21.73           C  
ATOM   2047  CD1 PHE B2133      14.660  38.490  27.625  1.00 22.79           C  
ATOM   2048  CD2 PHE B2133      13.818  36.965  29.268  1.00 23.49           C  
ATOM   2049  CE1 PHE B2133      14.802  39.474  28.602  1.00 24.02           C  
ATOM   2050  CE2 PHE B2133      13.956  37.940  30.252  1.00 23.40           C  
ATOM   2051  CZ  PHE B2133      14.450  39.199  29.919  1.00 24.80           C  
ATOM   2052  N   ASP B2134      15.420  33.318  25.395  1.00 26.09           N  
ATOM   2053  CA  ASP B2134      15.303  32.439  24.240  1.00 30.08           C  
ATOM   2054  C   ASP B2134      15.036  30.998  24.661  1.00 31.13           C  
ATOM   2055  O   ASP B2134      15.797  30.107  24.230  1.00 33.34           O  
ATOM   2056  CB  ASP B2134      16.584  32.509  23.408  1.00 32.87           C  
ATOM   2057  CG  ASP B2134      17.828  32.206  24.226  1.00 35.49           C  
ATOM   2058  OD1 ASP B2134      18.942  32.272  23.666  1.00 37.47           O  
ATOM   2059  OD2 ASP B2134      17.693  31.903  25.430  1.00 39.01           O  
ATOM   2060  OXT ASP B2134      14.064  30.778  25.412  1.00 32.31           O  
TER    2061      ASP B2134                                                      
HETATM 2062  C2  BGC C   1      -1.604  63.635  21.382  1.00 29.25           C  
HETATM 2063  C3  BGC C   1      -1.462  62.127  21.735  1.00 28.48           C  
HETATM 2064  C4  BGC C   1      -1.584  62.002  23.283  1.00 28.22           C  
HETATM 2065  C5  BGC C   1      -3.008  62.530  23.737  1.00 30.31           C  
HETATM 2066  C6  BGC C   1      -3.243  62.481  25.255  1.00 31.21           C  
HETATM 2067  C1  BGC C   1      -3.001  64.120  21.854  1.00 31.16           C  
HETATM 2068  O1  BGC C   1      -3.163  65.473  21.556  1.00 33.78           O  
HETATM 2069  O2  BGC C   1      -1.495  63.820  19.962  1.00 29.64           O  
HETATM 2070  O3  BGC C   1      -0.170  61.680  21.310  1.00 25.59           O  
HETATM 2071  O4  BGC C   1      -1.429  60.600  23.678  1.00 26.46           O  
HETATM 2072  O5  BGC C   1      -3.170  63.935  23.305  1.00 31.45           O  
HETATM 2073  O6  BGC C   1      -2.158  63.065  25.999  1.00 32.95           O  
HETATM 2074  C1  GAL C   2      -0.530  60.229  24.700  1.00 23.90           C  
HETATM 2075  C2  GAL C   2      -0.592  58.685  24.887  1.00 23.84           C  
HETATM 2076  C3  GAL C   2       0.406  58.299  26.024  1.00 22.50           C  
HETATM 2077  C4  GAL C   2       1.845  58.715  25.593  1.00 20.56           C  
HETATM 2078  C5  GAL C   2       1.836  60.270  25.379  1.00 20.26           C  
HETATM 2079  C6  GAL C   2       3.196  60.779  24.921  1.00 18.91           C  
HETATM 2080  O2  GAL C   2      -1.921  58.323  25.252  1.00 25.45           O  
HETATM 2081  O3  GAL C   2       0.366  56.878  26.218  1.00 22.65           O  
HETATM 2082  O4  GAL C   2       2.196  58.033  24.376  1.00 18.78           O  
HETATM 2083  O5  GAL C   2       0.831  60.637  24.349  1.00 21.89           O  
HETATM 2084  O6  GAL C   2       3.103  62.191  24.749  1.00 15.81           O  
HETATM 2085  C2  BGC D   1      25.802  29.121  55.838  0.70 23.61           C  
HETATM 2086  C3  BGC D   1      25.795  30.442  55.035  0.70 22.23           C  
HETATM 2087  C4  BGC D   1      24.704  31.360  55.665  0.70 22.53           C  
HETATM 2088  C5  BGC D   1      25.086  31.657  57.169  0.70 23.62           C  
HETATM 2089  C6  BGC D   1      24.073  32.538  57.908  0.70 24.74           C  
HETATM 2090  C1  BGC D   1      26.169  29.445  57.318  0.70 24.12           C  
HETATM 2091  O1  BGC D   1      26.181  28.275  58.075  0.70 26.74           O  
HETATM 2092  O2  BGC D   1      26.791  28.227  55.296  0.70 21.65           O  
HETATM 2093  O3  BGC D   1      25.451  30.156  53.680  0.70 20.81           O  
HETATM 2094  O4  BGC D   1      24.637  32.617  54.919  0.70 21.44           O  
HETATM 2095  O5  BGC D   1      25.194  30.378  57.912  0.70 25.20           O  
HETATM 2096  O6  BGC D   1      22.897  31.810  58.297  0.70 24.81           O  
HETATM 2097  C1  GAL D   2      23.464  33.065  54.278  0.70 21.12           C  
HETATM 2098  C2  GAL D   2      23.783  34.429  53.605  0.70 21.08           C  
HETATM 2099  C3  GAL D   2      22.487  34.944  52.900  0.70 20.47           C  
HETATM 2100  C4  GAL D   2      22.069  33.913  51.809  0.70 19.51           C  
HETATM 2101  C5  GAL D   2      21.783  32.548  52.533  0.70 17.47           C  
HETATM 2102  C6  GAL D   2      21.385  31.477  51.525  0.70 14.51           C  
HETATM 2103  O2  GAL D   2      24.195  35.353  54.613  0.70 22.42           O  
HETATM 2104  O3  GAL D   2      22.761  36.204  52.274  0.70 22.22           O  
HETATM 2105  O4  GAL D   2      23.144  33.773  50.852  0.70 19.67           O  
HETATM 2106  O5  GAL D   2      23.015  32.106  53.257  0.70 18.22           O  
HETATM 2107  O6  GAL D   2      21.130  30.263  52.221  0.70  6.32           O  
HETATM 2108  C1  BME A2137      19.744  48.757  16.014  1.00 32.03           C  
HETATM 2109  C2  BME A2137      20.282  50.090  16.517  1.00 30.76           C  
HETATM 2110  O1  BME A2137      20.663  48.113  15.156  1.00 34.71           O  
HETATM 2111  S2  BME A2137      21.969  49.978  17.184  1.00 31.19           S  
HETATM 2112  C1  BME A2138      22.506  42.053  22.023  1.00 37.42           C  
HETATM 2113  C2  BME A2138      21.575  41.808  23.202  1.00 35.13           C  
HETATM 2114  O1  BME A2138      22.850  40.844  21.377  1.00 40.82           O  
HETATM 2115  S2  BME A2138      19.960  42.611  22.997  1.00 33.58           S  
HETATM 2116  S   SO4 B3135      23.656  26.757  24.019  1.00 45.80           S  
HETATM 2117  O1  SO4 B3135      22.288  27.081  24.227  1.00 45.59           O  
HETATM 2118  O2  SO4 B3135      24.018  25.611  24.769  1.00 46.73           O  
HETATM 2119  O3  SO4 B3135      24.438  27.863  24.389  1.00 45.81           O  
HETATM 2120  O4  SO4 B3135      23.795  26.470  22.648  1.00 45.62           O  
HETATM 2121  C1  BME B3138      21.273  26.876  27.941  1.00 27.21           C  
HETATM 2122  C2  BME B3138      19.753  26.890  28.028  1.00 26.96           C  
HETATM 2123  O1  BME B3138      21.737  25.809  27.140  1.00 29.12           O  
HETATM 2124  S2  BME B3138      19.123  28.179  29.141  1.00 28.47           S  
HETATM 2125  C1  BME B3139      26.784  30.484  29.894  1.00 27.02           C  
HETATM 2126  C2  BME B3139      25.916  29.239  29.929  1.00 24.87           C  
HETATM 2127  O1  BME B3139      27.799  30.373  28.919  1.00 30.03           O  
HETATM 2128  S2  BME B3139      24.714  29.183  28.571  1.00 25.85           S  
HETATM 2129  C1  BME B3140      23.768  36.773  25.317  1.00 41.42           C  
HETATM 2130  C2  BME B3140      24.024  37.142  26.771  1.00 39.26           C  
HETATM 2131  O1  BME B3140      24.632  35.738  24.893  1.00 44.65           O  
HETATM 2132  S2  BME B3140      23.122  38.629  27.290  1.00 36.69           S  
HETATM 2133  O   HOH A2001       4.052  41.233  21.987  1.00 41.99           O  
HETATM 2134  O   HOH A2002      -0.685  48.677  11.424  1.00 36.50           O  
HETATM 2135  O   HOH A2003       1.085  52.516  25.326  1.00 40.72           O  
HETATM 2136  O   HOH A2004      11.806  52.463  39.710  1.00 44.24           O  
HETATM 2137  O   HOH A2005       3.763  54.440  35.025  1.00 45.80           O  
HETATM 2138  O   HOH A2006       3.737  62.809  11.763  1.00 15.97           O  
HETATM 2139  O   HOH A2007       2.311  69.687  24.481  1.00 42.47           O  
HETATM 2140  O   HOH A2008       2.095  67.815  19.143  1.00 50.86           O  
HETATM 2141  O   HOH A2009      25.155  60.731  11.225  1.00 28.63           O  
HETATM 2142  O   HOH A2010      25.705  58.058  19.278  1.00 41.42           O  
HETATM 2143  O   HOH A2011       4.824  51.461  32.195  1.00 39.28           O  
HETATM 2144  O   HOH A2012       4.503  39.020  34.073  1.00 40.83           O  
HETATM 2145  O   HOH A2013       4.385  44.913  26.722  1.00 37.91           O  
HETATM 2146  O   HOH A2014       6.566  47.438  31.873  1.00 35.75           O  
HETATM 2147  O   HOH A2015       8.891  42.765  27.331  1.00 37.37           O  
HETATM 2148  O   HOH A2016      12.549  46.665  38.431  1.00 23.73           O  
HETATM 2149  O   HOH A2017      23.292  49.067  39.588  1.00 33.73           O  
HETATM 2150  O   HOH A2018      15.437  51.316  42.733  1.00 30.77           O  
HETATM 2151  O   HOH A2019      16.167  52.528  40.251  1.00 20.52           O  
HETATM 2152  O   HOH A2020      25.802  51.162  39.894  1.00 52.55           O  
HETATM 2153  O   HOH A2021      22.476  56.640  39.493  1.00 36.26           O  
HETATM 2154  O   HOH A2022      29.776  58.976  32.026  1.00 38.10           O  
HETATM 2155  O   HOH A2023      24.700  48.276  24.887  1.00 38.13           O  
HETATM 2156  O   HOH A2024      25.295  46.319  22.935  1.00 40.97           O  
HETATM 2157  O   HOH A2025       5.434  40.394  19.823  1.00 30.63           O  
HETATM 2158  O   HOH A2026      -0.513  44.320  10.671  1.00 39.87           O  
HETATM 2159  O   HOH A2027      -0.438  39.994  19.815  1.00 42.51           O  
HETATM 2160  O   HOH A2028      -2.556  44.954  18.707  1.00 58.55           O  
HETATM 2161  O   HOH A2029      -0.538  46.387  12.761  1.00 34.82           O  
HETATM 2162  O   HOH A2030      -0.148  54.431  21.859  1.00 32.77           O  
HETATM 2163  O   HOH A2031       2.000  50.717  23.579  1.00 24.15           O  
HETATM 2164  O   HOH A2032      -0.054  49.084  23.688  1.00 36.77           O  
HETATM 2165  O   HOH A2033       3.978  54.856  28.833  1.00 27.82           O  
HETATM 2166  O   HOH A2034      14.074  53.597  39.207  1.00 33.91           O  
HETATM 2167  O   HOH A2035       9.239  53.662  39.160  1.00 22.51           O  
HETATM 2168  O   HOH A2036       5.557  55.346  33.311  1.00 28.22           O  
HETATM 2169  O   HOH A2037       3.788  55.723  37.562  1.00 38.06           O  
HETATM 2170  O   HOH A2038       3.443  58.556  35.227  1.00 48.25           O  
HETATM 2171  O   HOH A2039       7.835  62.376  40.835  1.00 34.14           O  
HETATM 2172  O   HOH A2040      11.872  65.369  37.203  1.00 49.06           O  
HETATM 2173  O   HOH A2041      13.949  64.135  28.067  1.00 17.53           O  
HETATM 2174  O   HOH A2042       1.449  55.357  24.074  1.00 24.39           O  
HETATM 2175  O   HOH A2043      -0.263  52.276   9.965  1.00 30.14           O  
HETATM 2176  O   HOH A2044      -5.285  61.068  21.076  1.00 37.00           O  
HETATM 2177  O   HOH A2045      -1.910  62.101  17.917  1.00 32.81           O  
HETATM 2178  O   HOH A2046      -4.289  59.181  10.994  1.00 41.84           O  
HETATM 2179  O   HOH A2047      -1.075  62.581  11.955  1.00 47.35           O  
HETATM 2180  O   HOH A2048      -0.728  62.913  15.602  1.00 27.37           O  
HETATM 2181  O   HOH A2049       1.398  61.519  12.355  1.00 20.52           O  
HETATM 2182  O   HOH A2050       0.917  59.361  10.583  1.00 18.12           O  
HETATM 2183  O   HOH A2051       2.763  49.216  10.557  1.00 26.61           O  
HETATM 2184  O   HOH A2052       4.329  59.081  10.394  1.00 12.02           O  
HETATM 2185  O   HOH A2053       9.254  67.287  30.286  1.00 29.44           O  
HETATM 2186  O   HOH A2054       4.058  56.412  31.475  1.00 25.02           O  
HETATM 2187  O   HOH A2055      -0.345  58.595  31.492  1.00  5.34           O  
HETATM 2188  O   HOH A2056      11.454  70.198  36.246  1.00 44.64           O  
HETATM 2189  O   HOH A2057       6.752  67.737  31.033  1.00 21.87           O  
HETATM 2190  O   HOH A2058       1.687  68.017  30.399  1.00 30.13           O  
HETATM 2191  O   HOH A2059       0.595  65.002  31.369  1.00 25.34           O  
HETATM 2192  O   HOH A2060       4.041  69.852  28.217  1.00 39.25           O  
HETATM 2193  O   HOH A2061       2.083  67.472  26.462  1.00 41.35           O  
HETATM 2194  O   HOH A2062       6.504  71.018  28.038  1.00 42.17           O  
HETATM 2195  O   HOH A2063       8.616  72.727  24.234  1.00 45.27           O  
HETATM 2196  O   HOH A2064       8.526  69.746  26.784  1.00 21.35           O  
HETATM 2197  O   HOH A2065       4.676  68.553  19.523  1.00 28.27           O  
HETATM 2198  O   HOH A2066       2.990  67.696  22.420  1.00 22.19           O  
HETATM 2199  O   HOH A2067      15.282  67.008  19.052  1.00 31.22           O  
HETATM 2200  O   HOH A2068      10.206  61.241  18.166  1.00 26.51           O  
HETATM 2201  O   HOH A2069      13.084  62.186  11.995  1.00 11.72           O  
HETATM 2202  O   HOH A2070       5.825  61.111  10.896  1.00 18.73           O  
HETATM 2203  O   HOH A2071       7.756  58.366  12.475  1.00 11.09           O  
HETATM 2204  O   HOH A2072      11.699  60.006   5.797  1.00 31.52           O  
HETATM 2205  O   HOH A2073       8.357  61.105   6.651  1.00 25.08           O  
HETATM 2206  O   HOH A2074       5.107  48.804   9.163  1.00 22.44           O  
HETATM 2207  O   HOH A2075      12.296  46.565  11.768  1.00 20.60           O  
HETATM 2208  O   HOH A2076       8.840  49.981   7.676  1.00 16.92           O  
HETATM 2209  O   HOH A2077       6.878  41.419   9.382  1.00 45.69           O  
HETATM 2210  O   HOH A2078       6.313  38.125   9.912  1.00 45.41           O  
HETATM 2211  O   HOH A2079      10.182  45.591  13.113  1.00 19.84           O  
HETATM 2212  O   HOH A2080      12.376  39.343  12.025  1.00 28.89           O  
HETATM 2213  O   HOH A2081      13.522  42.116  11.272  1.00 38.42           O  
HETATM 2214  O   HOH A2082      22.885  44.553  16.160  1.00 50.44           O  
HETATM 2215  O   HOH A2083      16.532  45.477  13.900  1.00 16.01           O  
HETATM 2216  O   HOH A2084      22.307  55.146  20.099  1.00 21.88           O  
HETATM 2217  O   HOH A2085      23.208  61.316  22.972  1.00 24.43           O  
HETATM 2218  O   HOH A2086      19.553  69.668  26.000  1.00 38.35           O  
HETATM 2219  O   HOH A2087      20.277  69.825  21.334  1.00 47.08           O  
HETATM 2220  O   HOH A2088      17.728  67.364  20.630  1.00 32.69           O  
HETATM 2221  O   HOH A2089      18.863  46.526  13.276  1.00 25.45           O  
HETATM 2222  O   HOH A2090      20.461  54.240   7.685  1.00 15.01           O  
HETATM 2223  O   HOH A2091      23.605  54.672  11.539  1.00 26.66           O  
HETATM 2224  O   HOH A2092      14.628  62.515   7.867  1.00  9.63           O  
HETATM 2225  O   HOH A2093      24.011  55.875  18.089  1.00 24.14           O  
HETATM 2226  O   HOH A2094      23.154  59.150  11.366  1.00 35.53           O  
HETATM 2227  O   HOH A2095      17.093  64.960  16.359  1.00 17.35           O  
HETATM 2228  O   HOH A2096      15.180  71.420  30.402  1.00 38.05           O  
HETATM 2229  O   HOH A2097      16.613  69.607  27.269  1.00  5.23           O  
HETATM 2230  O   HOH A2098      14.209  70.415  33.636  1.00 41.02           O  
HETATM 2231  O   HOH A2099      15.268  64.291  30.362  1.00 20.37           O  
HETATM 2232  O   HOH A2100      21.309  67.922  36.608  1.00 45.48           O  
HETATM 2233  O   HOH A2101      19.569  61.345  37.949  1.00  5.33           O  
HETATM 2234  O   HOH A2102      17.794  58.505  36.851  1.00 35.68           O  
HETATM 2235  O   HOH A2103      21.924  52.943  40.509  1.00 38.24           O  
HETATM 2236  O   HOH A2104       6.930  53.016  32.477  1.00 18.22           O  
HETATM 2237  O   HOH A2105       6.963  50.732  36.524  1.00 27.39           O  
HETATM 2238  O   HOH A2106      -1.637  47.950  21.565  1.00 30.94           O  
HETATM 2239  O   HOH A2107       1.262  42.403  21.498  1.00 44.01           O  
HETATM 2240  O   HOH A2108       6.908  44.500  26.363  1.00 25.61           O  
HETATM 2241  O   HOH A2109      10.114  36.256  27.977  1.00 37.38           O  
HETATM 2242  O   HOH A2110      11.104  35.167  24.670  1.00 47.91           O  
HETATM 2243  O   HOH A2111      10.478  38.738  27.071  1.00 43.09           O  
HETATM 2244  O   HOH A2112      17.006  36.407  22.540  1.00 36.73           O  
HETATM 2245  O   HOH A2113      29.800  50.378  31.607  1.00 47.48           O  
HETATM 2246  O   HOH A2114       1.123  56.195  28.778  1.00 45.21           O  
HETATM 2247  O   HOH A2115       0.731  63.874  25.525  1.00 32.56           O  
HETATM 2248  O   HOH B5001      24.364  47.131  38.121  1.00 30.46           O  
HETATM 2249  O   HOH B5002      35.082  42.383  33.893  1.00 28.54           O  
HETATM 2250  O   HOH B5003      21.805  39.929  47.694  1.00 43.85           O  
HETATM 2251  O   HOH B5004       9.366  42.921  42.256  1.00 43.73           O  
HETATM 2252  O   HOH B5005      12.322  44.832  44.079  1.00 39.08           O  
HETATM 2253  O   HOH B5006      29.992  36.409  58.346  1.00 39.39           O  
HETATM 2254  O   HOH B5007      38.686  26.941  52.833  1.00 20.06           O  
HETATM 2255  O   HOH B5008      23.982  18.325  41.001  1.00 43.65           O  
HETATM 2256  O   HOH B5009      17.992  22.789  30.044  1.00 40.45           O  
HETATM 2257  O   HOH B5010      35.788  21.596  35.555  1.00 39.72           O  
HETATM 2258  O   HOH B5011      13.785  16.965  31.170  1.00 33.86           O  
HETATM 2259  O   HOH B5012       1.293  25.721  43.085  1.00 28.57           O  
HETATM 2260  O   HOH B5013      17.729  44.531  44.976  1.00 33.77           O  
HETATM 2261  O   HOH B5014       4.033  41.624  51.595  1.00 52.20           O  
HETATM 2262  O   HOH B5015      25.966  48.021  41.915  1.00 29.94           O  
HETATM 2263  O   HOH B5016      23.758  44.594  37.999  1.00 15.13           O  
HETATM 2264  O   HOH B5017       4.598  40.323  36.575  1.00 42.96           O  
HETATM 2265  O   HOH B5018       7.147  41.292  38.650  1.00 20.43           O  
HETATM 2266  O   HOH B5019       7.012  40.709  30.208  1.00 28.00           O  
HETATM 2267  O   HOH B5020      10.570  39.662  29.428  1.00 35.20           O  
HETATM 2268  O   HOH B5021       7.686  34.600  27.921  1.00 21.52           O  
HETATM 2269  O   HOH B5022       6.297  26.750  28.629  1.00 32.76           O  
HETATM 2270  O   HOH B5023      12.679  28.370  31.647  1.00 20.74           O  
HETATM 2271  O   HOH B5024       7.515  29.399  25.833  1.00 34.18           O  
HETATM 2272  O   HOH B5025      30.207  35.607  28.526  1.00 41.69           O  
HETATM 2273  O   HOH B5026      31.693  43.524  29.826  1.00 40.74           O  
HETATM 2274  O   HOH B5027      31.010  44.306  38.836  1.00 19.50           O  
HETATM 2275  O   HOH B5028      35.036  43.190  36.441  1.00 23.62           O  
HETATM 2276  O   HOH B5029      35.193  43.586  48.682  1.00 42.95           O  
HETATM 2277  O   HOH B5030      38.448  39.576  45.144  1.00 33.40           O  
HETATM 2278  O   HOH B5031      30.907  39.212  49.596  1.00 31.05           O  
HETATM 2279  O   HOH B5032      27.798  35.877  49.590  1.00 16.81           O  
HETATM 2280  O   HOH B5033      20.030  37.800  48.372  1.00 23.73           O  
HETATM 2281  O   HOH B5034       8.321  40.783  40.945  1.00 34.36           O  
HETATM 2282  O   HOH B5035       4.636  37.203  46.710  1.00 45.78           O  
HETATM 2283  O   HOH B5036       6.135  39.427  48.926  1.00 32.45           O  
HETATM 2284  O   HOH B5037       8.800  42.001  47.590  1.00 42.75           O  
HETATM 2285  O   HOH B5038      10.513  42.419  45.082  1.00 22.49           O  
HETATM 2286  O   HOH B5039      15.884  39.290  47.991  1.00 20.77           O  
HETATM 2287  O   HOH B5040      11.816  44.539  47.759  1.00 45.62           O  
HETATM 2288  O   HOH B5041      12.345  38.071  53.694  1.00 30.00           O  
HETATM 2289  O   HOH B5042       5.982  36.959  50.635  1.00 18.60           O  
HETATM 2290  O   HOH B5043      39.232  31.843  47.423  1.00 34.79           O  
HETATM 2291  O   HOH B5044      35.553  37.572  53.120  1.00 18.59           O  
HETATM 2292  O   HOH B5045      29.837  28.758  55.334  1.00 16.12           O  
HETATM 2293  O   HOH B5046      25.617  35.687  50.998  1.00 38.37           O  
HETATM 2294  O   HOH B5047      27.219  39.047  51.270  1.00 38.91           O  
HETATM 2295  O   HOH B5048      27.614  34.808  57.659  1.00 30.93           O  
HETATM 2296  O   HOH B5049      31.881  36.722  55.035  1.00 21.40           O  
HETATM 2297  O   HOH B5050      36.551  28.235  53.688  1.00 19.99           O  
HETATM 2298  O   HOH B5051      36.799  25.529  49.318  1.00 13.63           O  
HETATM 2299  O   HOH B5052      39.025  26.704  47.499  1.00 22.92           O  
HETATM 2300  O   HOH B5053      36.093  24.626  44.624  1.00 14.22           O  
HETATM 2301  O   HOH B5054      12.047  27.220  49.569  1.00 13.57           O  
HETATM 2302  O   HOH B5055      17.397  37.887  49.754  1.00 31.14           O  
HETATM 2303  O   HOH B5056      15.717  38.536  54.023  1.00 28.06           O  
HETATM 2304  O   HOH B5057       7.971  25.756  51.576  1.00 47.29           O  
HETATM 2305  O   HOH B5058       4.447  29.164  51.516  1.00 35.19           O  
HETATM 2306  O   HOH B5059       5.981  27.065  48.034  1.00 20.05           O  
HETATM 2307  O   HOH B5060       7.579  37.622  52.918  1.00 31.08           O  
HETATM 2308  O   HOH B5061       3.659  37.424  52.848  1.00 38.18           O  
HETATM 2309  O   HOH B5062       4.789  37.689  53.913  1.00  5.15           O  
HETATM 2310  O   HOH B5063      12.303  27.829  52.220  1.00 12.51           O  
HETATM 2311  O   HOH B5064      15.623  25.894  56.037  1.00 16.81           O  
HETATM 2312  O   HOH B5065      18.022  37.324  54.072  1.00 26.08           O  
HETATM 2313  O   HOH B5066      18.893  27.905  55.527  1.00 23.69           O  
HETATM 2314  O   HOH B5067      17.489  24.071  56.003  1.00 18.51           O  
HETATM 2315  O   HOH B5068      21.269  28.953  55.463  1.00 33.90           O  
HETATM 2316  O   HOH B5069      21.110  25.328  54.613  1.00 21.62           O  
HETATM 2317  O   HOH B5070      22.939  22.415  52.991  1.00 20.89           O  
HETATM 2318  O   HOH B5071      21.914  22.385  43.253  1.00 13.01           O  
HETATM 2319  O   HOH B5072      24.517  19.762  45.643  1.00 16.84           O  
HETATM 2320  O   HOH B5073      31.135  25.608  51.305  1.00 10.90           O  
HETATM 2321  O   HOH B5074      31.027  25.054  44.071  1.00 10.43           O  
HETATM 2322  O   HOH B5075      23.775  19.889  43.156  1.00 21.88           O  
HETATM 2323  O   HOH B5076      33.988  32.497  34.292  1.00 38.02           O  
HETATM 2324  O   HOH B5077      38.264  32.124  41.261  1.00 32.08           O  
HETATM 2325  O   HOH B5078      37.800  29.749  38.967  1.00 46.11           O  
HETATM 2326  O   HOH B5079      33.774  34.830  36.783  1.00 18.76           O  
HETATM 2327  O   HOH B5080      40.880  37.453  39.921  1.00 39.02           O  
HETATM 2328  O   HOH B5081      39.737  38.150  36.680  1.00 31.67           O  
HETATM 2329  O   HOH B5082      36.474  38.800  31.259  1.00  5.74           O  
HETATM 2330  O   HOH B5083      31.088  33.463  30.633  1.00 19.28           O  
HETATM 2331  O   HOH B5084      13.695  18.460  35.951  1.00 16.41           O  
HETATM 2332  O   HOH B5085      14.989  22.375  34.564  1.00 16.84           O  
HETATM 2333  O   HOH B5086      15.872  17.677  42.333  1.00 25.78           O  
HETATM 2334  O   HOH B5087      20.009  26.022  31.722  1.00 18.66           O  
HETATM 2335  O   HOH B5088      17.362  20.609  31.967  1.00 24.53           O  
HETATM 2336  O   HOH B5089      27.531  24.378  26.098  1.00 19.26           O  
HETATM 2337  O   HOH B5090      30.983  27.553  27.807  1.00 27.63           O  
HETATM 2338  O   HOH B5091      31.405  21.967  29.411  1.00 16.48           O  
HETATM 2339  O   HOH B5092      35.144  24.134  35.944  1.00 23.85           O  
HETATM 2340  O   HOH B5093      33.825  22.682  31.834  1.00 31.24           O  
HETATM 2341  O   HOH B5094      33.244  21.379  34.553  1.00 21.06           O  
HETATM 2342  O   HOH B5095      27.007  20.615  41.073  1.00 13.44           O  
HETATM 2343  O   HOH B5096      30.557  17.835  39.061  1.00 42.93           O  
HETATM 2344  O   HOH B5097      21.243  24.248  30.190  1.00 19.70           O  
HETATM 2345  O   HOH B5098      16.567  15.375  36.172  1.00 19.34           O  
HETATM 2346  O   HOH B5099      15.734  18.530  31.951  1.00 19.09           O  
HETATM 2347  O   HOH B5100      21.183  19.124  42.823  1.00 40.74           O  
HETATM 2348  O   HOH B5101      13.669  26.554  44.294  1.00 12.48           O  
HETATM 2349  O   HOH B5102      11.334  27.342  43.192  1.00 20.94           O  
HETATM 2350  O   HOH B5103       9.572  25.957  49.304  1.00 16.93           O  
HETATM 2351  O   HOH B5104      14.784  20.264  47.815  1.00 11.42           O  
HETATM 2352  O   HOH B5105       5.304  28.986  46.113  1.00 31.43           O  
HETATM 2353  O   HOH B5106       7.030  21.619  41.968  1.00  9.11           O  
HETATM 2354  O   HOH B5107       2.762  25.225  40.747  1.00 27.89           O  
HETATM 2355  O   HOH B5108       3.035  26.246  45.020  1.00 21.79           O  
HETATM 2356  O   HOH B5109       5.741  24.695  37.123  1.00 28.50           O  
HETATM 2357  O   HOH B5110       0.517  29.631  35.611  1.00 45.68           O  
HETATM 2358  O   HOH B5111       3.577  27.789  33.101  1.00 45.62           O  
HETATM 2359  O   HOH B5112       3.901  30.124  39.509  1.00 36.43           O  
HETATM 2360  O   HOH B5113      -0.962  24.369  38.791  1.00 12.32           O  
HETATM 2361  O   HOH B5114       3.997  23.763  38.939  1.00 34.13           O  
HETATM 2362  O   HOH B5115       7.269  34.515  39.325  1.00 17.03           O  
HETATM 2363  O   HOH B5116      16.918  40.100  45.690  1.00 16.58           O  
HETATM 2364  O   HOH B5117      14.729  43.992  44.947  1.00 18.36           O  
HETATM 2365  O   HOH B5118      19.728  44.579  43.254  1.00 41.95           O  
HETATM 2366  O   HOH B5119      26.069  45.446  40.347  1.00 24.86           O  
HETATM 2367  O   HOH B5120      24.488  40.103  48.036  1.00 22.38           O  
HETATM 2368  O   HOH B5121      28.325  40.019  47.205  1.00 21.96           O  
HETATM 2369  O   HOH B5122      24.785  44.347  47.160  1.00 39.55           O  
HETATM 2370  O   HOH B5123      29.126  45.586  40.352  1.00 25.64           O  
HETATM 2371  O   HOH B5124      33.005  44.425  46.438  1.00 41.55           O  
HETATM 2372  O   HOH B5125      32.084  41.147  47.942  1.00 16.80           O  
HETATM 2373  O   HOH B5126      31.728  45.741  44.288  1.00 38.82           O  
HETATM 2374  O   HOH B5127      23.550  47.401  34.656  1.00 38.66           O  
HETATM 2375  O   HOH B5128      26.177  48.137  32.807  1.00 45.56           O  
HETATM 2376  O   HOH B5129      26.741  44.656  27.100  1.00 28.30           O  
HETATM 2377  O   HOH B5130      21.231  26.823  20.667  1.00 34.27           O  
HETATM 2378  O   HOH B5131      26.099  27.168  20.957  1.00 30.12           O  
HETATM 2379  O   HOH B5132      28.523  27.100  27.494  1.00 25.43           O  
HETATM 2380  O   HOH B5133      30.557  31.546  28.910  1.00 27.55           O  
HETATM 2381  O   HOH B5134      24.827  37.979  50.147  1.00 45.31           O  
HETATM 2382  O   HOH B5135      20.312  37.857  52.731  1.00 50.94           O  
CONECT   96  103                                                                
CONECT  103   96  104                                                           
CONECT  104  103  105  107                                                      
CONECT  105  104  106                                                           
CONECT  106  105  109                                                           
CONECT  107  104  108  110                                                      
CONECT  108  107                                                                
CONECT  109  106                                                                
CONECT  110  107                                                                
CONECT  659 2111                                                                
CONECT  998 2115                                                                
CONECT 1139 2124                                                                
CONECT 1689 2128                                                                
CONECT 2028 2132                                                                
CONECT 2062 2063 2067 2069                                                      
CONECT 2063 2062 2064 2070                                                      
CONECT 2064 2063 2065 2071                                                      
CONECT 2065 2064 2066 2072                                                      
CONECT 2066 2065 2073                                                           
CONECT 2067 2062 2068 2072                                                      
CONECT 2068 2067                                                                
CONECT 2069 2062                                                                
CONECT 2070 2063                                                                
CONECT 2071 2064 2074                                                           
CONECT 2072 2065 2067                                                           
CONECT 2073 2066                                                                
CONECT 2074 2071 2075 2083                                                      
CONECT 2075 2074 2076 2080                                                      
CONECT 2076 2075 2077 2081                                                      
CONECT 2077 2076 2078 2082                                                      
CONECT 2078 2077 2079 2083                                                      
CONECT 2079 2078 2084                                                           
CONECT 2080 2075                                                                
CONECT 2081 2076                                                                
CONECT 2082 2077                                                                
CONECT 2083 2074 2078                                                           
CONECT 2084 2079                                                                
CONECT 2085 2086 2090 2092                                                      
CONECT 2086 2085 2087 2093                                                      
CONECT 2087 2086 2088 2094                                                      
CONECT 2088 2087 2089 2095                                                      
CONECT 2089 2088 2096                                                           
CONECT 2090 2085 2091 2095                                                      
CONECT 2091 2090                                                                
CONECT 2092 2085                                                                
CONECT 2093 2086                                                                
CONECT 2094 2087 2097                                                           
CONECT 2095 2088 2090                                                           
CONECT 2096 2089                                                                
CONECT 2097 2094 2098 2106                                                      
CONECT 2098 2097 2099 2103                                                      
CONECT 2099 2098 2100 2104                                                      
CONECT 2100 2099 2101 2105                                                      
CONECT 2101 2100 2102 2106                                                      
CONECT 2102 2101 2107                                                           
CONECT 2103 2098                                                                
CONECT 2104 2099                                                                
CONECT 2105 2100                                                                
CONECT 2106 2097 2101                                                           
CONECT 2107 2102                                                                
CONECT 2108 2109 2110                                                           
CONECT 2109 2108 2111                                                           
CONECT 2110 2108                                                                
CONECT 2111  659 2109                                                           
CONECT 2112 2113 2114                                                           
CONECT 2113 2112 2115                                                           
CONECT 2114 2112                                                                
CONECT 2115  998 2113                                                           
CONECT 2116 2117 2118 2119 2120                                                 
CONECT 2117 2116                                                                
CONECT 2118 2116                                                                
CONECT 2119 2116                                                                
CONECT 2120 2116                                                                
CONECT 2121 2122 2123                                                           
CONECT 2122 2121 2124                                                           
CONECT 2123 2121                                                                
CONECT 2124 1139 2122                                                           
CONECT 2125 2126 2127                                                           
CONECT 2126 2125 2128                                                           
CONECT 2127 2125                                                                
CONECT 2128 1689 2126                                                           
CONECT 2129 2130 2131                                                           
CONECT 2130 2129 2132                                                           
CONECT 2131 2129                                                                
CONECT 2132 2028 2130                                                           
MASTER      354    0   11    0   24    0    0    9 2380    2   85   22          
END                                                                             



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