HEADER    LIGASE                                  31-AUG-98   1DAM              
TITLE     DETHIOBIOTIN SYNTHETASE COMPLEXED WITH DETHIOBIOTIN, ADP, INORGANIC   
TITLE    2 PHOSPHATE AND MAGNESIUM                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (DETHIOBIOTIN SYNTHETASE);                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DTBS;                                                       
COMPND   5 EC: 6.3.3.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_GENE: BIOD                                         
KEYWDS    LIGASE, BIOTIN BIOSYNTHESIS, MAGNESIUM, ATP-BINDING, PHOSPHORYL       
KEYWDS   2 TRANSFER                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.KAECK,J.SANDMARK,K.J.GIBSON,G.SCHNEIDER,Y.LINDQVIST                 
REVDAT   8   07-FEB-24 1DAM    1       REMARK LINK                              
REVDAT   7   04-OCT-17 1DAM    1       REMARK                                   
REVDAT   6   06-APR-16 1DAM    1       HETSYN                                   
REVDAT   5   13-JUL-11 1DAM    1       VERSN                                    
REVDAT   4   24-FEB-09 1DAM    1       VERSN                                    
REVDAT   3   01-APR-03 1DAM    1       JRNL                                     
REVDAT   2   29-DEC-99 1DAM    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   13-JAN-99 1DAM    0                                                
JRNL        AUTH   H.KACK,J.SANDMARK,K.J.GIBSON,G.SCHNEIDER,Y.LINDQVIST         
JRNL        TITL   CRYSTAL STRUCTURE OF TWO QUATERNARY COMPLEXES OF             
JRNL        TITL 2 DETHIOBIOTIN SYNTHETASE, ENZYME-MGADP-ALF3-DIAMINOPELARGONIC 
JRNL        TITL 3 ACID AND ENZYME-MGADP-DETHIOBIOTIN-PHOSPHATE; IMPLICATIONS   
JRNL        TITL 4 FOR CATALYSIS.                                               
JRNL        REF    PROTEIN SCI.                  V.   7  2560 1998              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   9865950                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.KAECK,K.J.GIBSON,G.SCHNEIDER,Y.LINDQVIST                   
REMARK   1  TITL   SNAPSHOT OF A PHOSPHORYLATED SUBSTRATE INTERMEDIATE BY       
REMARK   1  TITL 2 KINETIC CRYSTALLOGRAPHY                                      
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  95  5495 1998              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.HUANG,Y.LINDQVIST,G.SCHNEIDER,K.J.GIBSON,D.FLINT,G.LORIMER 
REMARK   1  TITL   CRYSTAL STRUCTURE OF AN ATP-DEPENDENT CARBOXYLASE,           
REMARK   1  TITL 2 DETHIOBIOTIN SYNTHETASE, AT 1.65 A RESOLUTION                
REMARK   1  REF    STRUCTURE                     V.   2   407 1994              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 18683                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 789                             
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1692                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 49                                      
REMARK   3   SOLVENT ATOMS            : 199                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.007 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.024 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.023 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.018 ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.085 ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.171 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.250 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : 0.167 ; 0.300               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : 15.000; NULL                
REMARK   3    PLANAR                    (DEGREES) : 3.300 ; 7.000               
REMARK   3    STAGGERED                 (DEGREES) : 18.800; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.068 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.658 ; 3.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.310 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.101 ; 3.000                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE DEPOSITION ID IS D_1000008250.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17046                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.1000                            
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) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       36.35000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.35000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.45000            
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: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 6610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
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    ARG A   3   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 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    ASP A  10      179.83    179.90                                   
REMARK 500    ASN A 209       69.33     33.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 901  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  16   OG1                                                    
REMARK 620 2 ASP A  54   OD2  83.4                                              
REMARK 620 3 GLU A 115   OE2  86.6  99.6                                        
REMARK 620 4 HOH A 444   O    83.9  68.8 165.7                                  
REMARK 620 5 ADP A 801   O2B  91.9 145.9 113.9  77.1                            
REMARK 620 6 PO4 A 802   O2  166.9  84.1  91.5  95.4 100.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 902  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 444   O                                                      
REMARK 620 2 HOH A 448   O    78.0                                              
REMARK 620 3 HOH A 749   O    78.4  79.9                                        
REMARK 620 4 HOH A 750   O   158.5  85.2  85.6                                  
REMARK 620 5 ADP A 801   O3B 103.1  98.8 177.8  92.6                            
REMARK 620 6 PO4 A 802   O3  105.0 161.6  83.0  87.0  98.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTB A 803                 
DBREF  1DAM A    1   224  UNP    P13000   BIOD_ECOLI       1    224             
SEQRES   1 A  224  SER LYS ARG TYR PHE VAL THR GLY THR ASP THR GLU VAL          
SEQRES   2 A  224  GLY LYS THR VAL ALA SER CYS ALA LEU LEU GLN ALA ALA          
SEQRES   3 A  224  LYS ALA ALA GLY TYR ARG THR ALA GLY TYR LYS PRO VAL          
SEQRES   4 A  224  ALA SER GLY SER GLU LYS THR PRO GLU GLY LEU ARG ASN          
SEQRES   5 A  224  SER ASP ALA LEU ALA LEU GLN ARG ASN SER SER LEU GLN          
SEQRES   6 A  224  LEU ASP TYR ALA THR VAL ASN PRO TYR THR PHE ALA GLU          
SEQRES   7 A  224  PRO THR SER PRO HIS ILE ILE SER ALA GLN GLU GLY ARG          
SEQRES   8 A  224  PRO ILE GLU SER LEU VAL MET SER ALA GLY LEU ARG ALA          
SEQRES   9 A  224  LEU GLU GLN GLN ALA ASP TRP VAL LEU VAL GLU GLY ALA          
SEQRES  10 A  224  GLY GLY TRP PHE THR PRO LEU SER ASP THR PHE THR PHE          
SEQRES  11 A  224  ALA ASP TRP VAL THR GLN GLU GLN LEU PRO VAL ILE LEU          
SEQRES  12 A  224  VAL VAL GLY VAL LYS LEU GLY CYS ILE ASN HIS ALA MET          
SEQRES  13 A  224  LEU THR ALA GLN VAL ILE GLN HIS ALA GLY LEU THR LEU          
SEQRES  14 A  224  ALA GLY TRP VAL ALA ASN ASP VAL THR PRO PRO GLY LYS          
SEQRES  15 A  224  ARG HIS ALA GLU TYR MET THR THR LEU THR ARG MET ILE          
SEQRES  16 A  224  PRO ALA PRO LEU LEU GLY GLU ILE PRO TRP LEU ALA GLU          
SEQRES  17 A  224  ASN PRO GLU ASN ALA ALA THR GLY LYS TYR ILE ASN LEU          
SEQRES  18 A  224  ALA LEU LEU                                                  
HET     MG  A 901       1                                                       
HET     MG  A 902       1                                                       
HET    PO4  A 802       5                                                       
HET    ADP  A 801      27                                                       
HET    DTB  A 803      15                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     DTB 6-(5-METHYL-2-OXO-IMIDAZOLIDIN-4-YL)-HEXANOIC ACID               
HETSYN     DTB D-DESTHIOBIOTIN                                                  
FORMUL   2   MG    2(MG 2+)                                                     
FORMUL   4  PO4    O4 P 3-                                                      
FORMUL   5  ADP    C10 H15 N5 O10 P2                                            
FORMUL   6  DTB    C10 H18 N2 O3                                                
FORMUL   7  HOH   *199(H2 O)                                                    
HELIX    1   1 LYS A   15  ALA A   29  1                                  15    
HELIX    2   2 SER A   53  ARG A   60  1                                   8    
HELIX    3   3 TYR A   68  VAL A   71  1                                   4    
HELIX    4   4 PRO A   82  GLU A   89  1                                   8    
HELIX    5   5 SER A   95  GLN A  107  1                                  13    
HELIX    6   6 PHE A  130  GLU A  137  1                                   8    
HELIX    7   7 CYS A  151  HIS A  164  1                                  14    
HELIX    8   8 HIS A  184  MET A  194  1                                  11    
HELIX    9   9 PRO A  210  ASN A  212  5                                   3    
HELIX   10  10 GLY A  216  TYR A  218  5                                   3    
SHEET    1   A 6 LEU A 199  ILE A 203  0                                        
SHEET    2   A 6 LEU A 169  ASN A 175  1  N  TRP A 172   O  LEU A 200           
SHEET    3   A 6 VAL A 141  GLY A 146  1  N  VAL A 141   O  ALA A 170           
SHEET    4   A 6 LYS A   2  GLY A   8  1  N  PHE A   5   O  ILE A 142           
SHEET    5   A 6 TRP A 111  GLU A 115  1  N  VAL A 112   O  LYS A   2           
SHEET    6   A 6 THR A  33  TYR A  36  1  N  ALA A  34   O  TRP A 111           
SHEET    1   B 2 VAL A  39  SER A  41  0                                        
SHEET    2   B 2 TYR A  74  PHE A  76  1  N  TYR A  74   O  ALA A  40           
SHEET    1   C 2 SER A  43  THR A  46  0                                        
SHEET    2   C 2 GLY A  49  ASN A  52 -1  N  ARG A  51   O  GLU A  44           
LINK         OG1 THR A  16                MG    MG A 901     1555   1555  2.24  
LINK         OD2 ASP A  54                MG    MG A 901     1555   1555  2.14  
LINK         OE2 GLU A 115                MG    MG A 901     1555   1555  2.00  
LINK         O   HOH A 444                MG    MG A 901     1555   1555  2.83  
LINK         O   HOH A 444                MG    MG A 902     1555   1555  2.11  
LINK         O   HOH A 448                MG    MG A 902     1555   1555  2.24  
LINK         O   HOH A 749                MG    MG A 902     1555   1555  2.07  
LINK         O   HOH A 750                MG    MG A 902     1555   1555  2.39  
LINK         O2B ADP A 801                MG    MG A 901     1555   1555  2.00  
LINK         O3B ADP A 801                MG    MG A 902     1555   1555  1.91  
LINK         O2  PO4 A 802                MG    MG A 901     1555   1555  2.00  
LINK         O3  PO4 A 802                MG    MG A 902     1555   1555  2.24  
SITE     1 AC1  7 THR A  16  ASP A  54  GLU A 115  HOH A 444                    
SITE     2 AC1  7 ADP A 801  PO4 A 802   MG A 902                               
SITE     1 AC2  7 HOH A 444  HOH A 448  HOH A 749  HOH A 750                    
SITE     2 AC2  7 ADP A 801  PO4 A 802   MG A 901                               
SITE     1 AC3 13 THR A  11  LYS A  15  LYS A  37  ASP A  54                    
SITE     2 AC3 13 GLU A 115  ALA A 117  GLY A 118  HOH A 719                    
SITE     3 AC3 13 HOH A 749  ADP A 801  DTB A 803   MG A 901                    
SITE     4 AC3 13  MG A 902                                                     
SITE     1 AC4 21 GLU A  12  VAL A  13  GLY A  14  LYS A  15                    
SITE     2 AC4 21 THR A  16  VAL A  17  GLU A 115  ASN A 175                    
SITE     3 AC4 21 ASP A 176  PRO A 204  TRP A 205  LEU A 206                    
SITE     4 AC4 21 PRO A 210  GLU A 211  HOH A 444  HOH A 448                    
SITE     5 AC4 21 HOH A 714  HOH A 759  PO4 A 802   MG A 901                    
SITE     6 AC4 21  MG A 902                                                     
SITE     1 AC5 13 THR A  11  SER A  41  SER A  81  LEU A 149                    
SITE     2 AC5 13 GLY A 150  CYS A 151  ILE A 152  ASN A 153                    
SITE     3 AC5 13 TYR A 187  HOH A 655  HOH A 717  HOH A 749                    
SITE     4 AC5 13 PO4 A 802                                                     
CRYST1   72.700   48.900   61.100  90.00 106.70  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013755  0.000000  0.004127        0.00000                         
SCALE2      0.000000  0.020450  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017087        0.00000                         
ATOM      1  N   SER A   1      14.103  42.560  26.050  1.00 31.03           N  
ATOM      2  CA  SER A   1      14.351  41.139  25.705  1.00 30.57           C  
ATOM      3  C   SER A   1      13.815  40.821  24.307  1.00 29.10           C  
ATOM      4  O   SER A   1      12.766  41.355  23.950  1.00 29.48           O  
ATOM      5  CB  SER A   1      13.636  40.209  26.675  1.00 31.07           C  
ATOM      6  OG  SER A   1      12.300  40.656  26.849  1.00 33.05           O  
ATOM      7  N   LYS A   2      14.504  39.926  23.622  1.00 26.18           N  
ATOM      8  CA  LYS A   2      14.158  39.549  22.262  1.00 23.31           C  
ATOM      9  C   LYS A   2      12.860  38.744  22.174  1.00 20.60           C  
ATOM     10  O   LYS A   2      12.587  37.870  23.004  1.00 18.04           O  
ATOM     11  CB  LYS A   2      15.285  38.718  21.643  1.00 24.93           C  
ATOM     12  CG  LYS A   2      16.661  39.347  21.812  1.00 27.06           C  
ATOM     13  CD  LYS A   2      17.268  39.773  20.482  1.00 28.00           C  
ATOM     14  CE  LYS A   2      18.552  40.578  20.644  1.00 29.53           C  
ATOM     15  NZ  LYS A   2      19.402  40.535  19.448  1.00 31.07           N  
ATOM     16  N   ARG A   3      12.093  39.085  21.147  1.00 17.73           N  
ATOM     17  CA  ARG A   3      10.849  38.377  20.816  1.00 16.34           C  
ATOM     18  C   ARG A   3      10.712  38.200  19.297  1.00 13.16           C  
ATOM     19  O   ARG A   3      11.120  39.104  18.579  1.00 11.43           O  
ATOM     20  CB  ARG A   3       9.561  39.115  21.236  1.00 18.93           C  
ATOM     21  CG  ARG A   3       9.729  40.186  22.304  1.00 22.34           C  
ATOM     22  CD  ARG A   3       9.177  41.547  21.862  1.00 23.37           C  
ATOM     23  NE  ARG A   3       7.747  41.748  22.168  1.00 25.82           N  
ATOM     24  CZ  ARG A   3       6.905  42.460  21.400  1.00 26.69           C  
ATOM     25  NH1 ARG A   3       7.327  43.039  20.267  1.00 27.21           N  
ATOM     26  NH2 ARG A   3       5.610  42.650  21.690  1.00 26.88           N  
ATOM     27  N   TYR A   4      10.298  37.031  18.832  1.00 11.46           N  
ATOM     28  CA  TYR A   4      10.122  36.787  17.397  1.00 10.57           C  
ATOM     29  C   TYR A   4       8.799  36.048  17.203  1.00 10.19           C  
ATOM     30  O   TYR A   4       8.426  35.259  18.063  1.00 10.51           O  
ATOM     31  CB  TYR A   4      11.230  35.929  16.746  1.00 11.34           C  
ATOM     32  CG  TYR A   4      12.593  36.563  16.990  1.00 13.45           C  
ATOM     33  CD1 TYR A   4      13.029  37.603  16.197  1.00 14.39           C  
ATOM     34  CD2 TYR A   4      13.337  36.187  18.107  1.00 14.47           C  
ATOM     35  CE1 TYR A   4      14.242  38.227  16.454  1.00 16.14           C  
ATOM     36  CE2 TYR A   4      14.536  36.832  18.381  1.00 15.75           C  
ATOM     37  CZ  TYR A   4      14.977  37.837  17.554  1.00 15.84           C  
ATOM     38  OH  TYR A   4      16.181  38.464  17.810  1.00 16.55           O  
ATOM     39  N   PHE A   5       8.108  36.285  16.097  1.00  9.38           N  
ATOM     40  CA  PHE A   5       6.909  35.504  15.794  1.00  9.20           C  
ATOM     41  C   PHE A   5       7.278  34.585  14.624  1.00  9.59           C  
ATOM     42  O   PHE A   5       7.733  35.129  13.619  1.00  9.90           O  
ATOM     43  CB  PHE A   5       5.756  36.407  15.353  1.00  8.51           C  
ATOM     44  CG  PHE A   5       4.482  35.665  15.053  1.00 10.14           C  
ATOM     45  CD1 PHE A   5       3.640  35.248  16.077  1.00  9.82           C  
ATOM     46  CD2 PHE A   5       4.141  35.369  13.744  1.00 10.41           C  
ATOM     47  CE1 PHE A   5       2.464  34.584  15.794  1.00 10.16           C  
ATOM     48  CE2 PHE A   5       2.953  34.709  13.456  1.00  9.66           C  
ATOM     49  CZ  PHE A   5       2.121  34.300  14.479  1.00 11.41           C  
ATOM     50  N   VAL A   6       7.036  33.293  14.736  1.00  9.24           N  
ATOM     51  CA  VAL A   6       7.369  32.397  13.627  1.00  9.41           C  
ATOM     52  C   VAL A   6       6.109  32.030  12.848  1.00  9.50           C  
ATOM     53  O   VAL A   6       5.149  31.525  13.423  1.00  7.63           O  
ATOM     54  CB  VAL A   6       8.070  31.129  14.147  1.00 11.05           C  
ATOM     55  CG1 VAL A   6       8.306  30.105  13.034  1.00 11.44           C  
ATOM     56  CG2 VAL A   6       9.388  31.494  14.819  1.00 11.81           C  
ATOM     57  N   THR A   7       6.125  32.363  11.556  1.00  8.36           N  
ATOM     58  CA  THR A   7       4.991  32.036  10.679  1.00  8.18           C  
ATOM     59  C   THR A   7       5.521  31.085   9.602  1.00  8.65           C  
ATOM     60  O   THR A   7       6.718  30.774   9.609  1.00  7.99           O  
ATOM     61  CB  THR A   7       4.299  33.276  10.118  1.00  7.75           C  
ATOM     62  OG1 THR A   7       3.093  32.850   9.450  1.00  8.60           O  
ATOM     63  CG2 THR A   7       5.186  34.028   9.124  1.00  8.46           C  
ATOM     64  N   GLY A   8       4.627  30.554   8.775  1.00  8.75           N  
ATOM     65  CA  GLY A   8       5.072  29.614   7.742  1.00 10.64           C  
ATOM     66  C   GLY A   8       4.283  29.894   6.460  1.00 11.86           C  
ATOM     67  O   GLY A   8       3.285  30.626   6.467  1.00 12.17           O  
ATOM     68  N   THR A   9       4.741  29.309   5.375  1.00 13.37           N  
ATOM     69  CA  THR A   9       4.097  29.487   4.066  1.00 15.83           C  
ATOM     70  C   THR A   9       2.734  28.759   4.033  1.00 16.83           C  
ATOM     71  O   THR A   9       1.934  28.939   3.108  1.00 16.61           O  
ATOM     72  CB  THR A   9       5.011  28.952   2.963  1.00 15.64           C  
ATOM     73  OG1 THR A   9       5.644  27.756   3.393  1.00 16.63           O  
ATOM     74  CG2 THR A   9       6.117  29.941   2.582  1.00 15.25           C  
ATOM     75  N   ASP A  10       2.495  27.956   5.060  1.00 16.97           N  
ATOM     76  CA  ASP A  10       1.246  27.165   5.210  1.00 18.19           C  
ATOM     77  C   ASP A  10       1.352  26.372   6.510  1.00 18.79           C  
ATOM     78  O   ASP A  10       2.345  26.468   7.242  1.00 19.86           O  
ATOM     79  CB  ASP A  10       1.140  26.169   4.039  1.00 18.34           C  
ATOM     80  CG  ASP A  10      -0.251  25.553   3.883  1.00 18.55           C  
ATOM     81  OD1 ASP A  10      -1.204  25.901   4.677  1.00 19.09           O  
ATOM     82  OD2 ASP A  10      -0.469  24.684   2.953  1.00 19.00           O  
ATOM     83  N   THR A  11       0.328  25.605   6.821  1.00 18.44           N  
ATOM     84  CA  THR A  11       0.439  24.678   7.949  1.00 18.60           C  
ATOM     85  C   THR A  11       1.226  23.490   7.388  1.00 18.74           C  
ATOM     86  O   THR A  11       1.301  23.315   6.164  1.00 18.01           O  
ATOM     87  CB  THR A  11      -0.943  24.257   8.477  1.00 19.02           C  
ATOM     88  OG1 THR A  11      -0.798  23.531   9.696  1.00 18.33           O  
ATOM     89  CG2 THR A  11      -1.704  23.353   7.506  1.00 18.86           C  
ATOM     90  N   GLU A  12       1.812  22.727   8.274  1.00 18.93           N  
ATOM     91  CA  GLU A  12       2.613  21.523   7.936  1.00 19.48           C  
ATOM     92  C   GLU A  12       3.823  21.813   7.014  1.00 18.39           C  
ATOM     93  O   GLU A  12       4.133  21.039   6.092  1.00 18.30           O  
ATOM     94  CB  GLU A  12       1.768  20.445   7.244  1.00 22.01           C  
ATOM     95  CG  GLU A  12       2.227  19.049   7.669  1.00 24.47           C  
ATOM     96  CD  GLU A  12       1.424  17.905   7.064  1.00 26.82           C  
ATOM     97  OE1 GLU A  12       0.166  18.049   6.843  1.00 27.50           O  
ATOM     98  OE2 GLU A  12       2.013  16.793   6.784  1.00 28.86           O  
ATOM     99  N   VAL A  13       4.526  22.912   7.282  1.00 17.09           N  
ATOM    100  CA  VAL A  13       5.737  23.256   6.501  1.00 16.33           C  
ATOM    101  C   VAL A  13       7.005  23.257   7.369  1.00 15.67           C  
ATOM    102  O   VAL A  13       8.128  23.340   6.851  1.00 14.65           O  
ATOM    103  CB  VAL A  13       5.639  24.622   5.823  1.00 16.19           C  
ATOM    104  CG1 VAL A  13       4.439  24.735   4.880  1.00 16.07           C  
ATOM    105  CG2 VAL A  13       5.498  25.775   6.817  1.00 15.75           C  
ATOM    106  N   GLY A  14       6.825  23.183   8.682  1.00 16.24           N  
ATOM    107  CA  GLY A  14       7.975  23.072   9.608  1.00 15.08           C  
ATOM    108  C   GLY A  14       8.096  24.224  10.629  1.00 14.89           C  
ATOM    109  O   GLY A  14       9.166  24.457  11.207  1.00 13.38           O  
ATOM    110  N   LYS A  15       7.023  24.943  10.889  1.00 12.41           N  
ATOM    111  CA  LYS A  15       7.079  26.037  11.882  1.00 12.23           C  
ATOM    112  C   LYS A  15       7.599  25.502  13.230  1.00 12.29           C  
ATOM    113  O   LYS A  15       8.456  26.112  13.880  1.00 13.98           O  
ATOM    114  CB  LYS A  15       5.696  26.646  12.112  1.00 10.46           C  
ATOM    115  CG  LYS A  15       5.238  27.548  10.965  1.00 10.36           C  
ATOM    116  CD  LYS A  15       3.987  28.364  11.303  1.00 10.54           C  
ATOM    117  CE  LYS A  15       2.836  27.505  11.831  1.00 12.00           C  
ATOM    118  NZ  LYS A  15       2.233  26.652  10.796  1.00 11.67           N  
ATOM    119  N   THR A  16       7.070  24.352  13.631  1.00 12.20           N  
ATOM    120  CA  THR A  16       7.429  23.743  14.927  1.00 12.21           C  
ATOM    121  C   THR A  16       8.844  23.206  14.901  1.00 12.31           C  
ATOM    122  O   THR A  16       9.619  23.545  15.794  1.00 12.41           O  
ATOM    123  CB  THR A  16       6.424  22.662  15.311  1.00 12.71           C  
ATOM    124  OG1 THR A  16       5.143  23.255  15.505  1.00 11.41           O  
ATOM    125  CG2 THR A  16       6.795  21.949  16.614  1.00 12.68           C  
ATOM    126  N   VAL A  17       9.203  22.440  13.863  1.00 11.85           N  
ATOM    127  CA  VAL A  17      10.581  21.941  13.796  1.00 11.80           C  
ATOM    128  C   VAL A  17      11.564  23.096  13.745  1.00 11.26           C  
ATOM    129  O   VAL A  17      12.552  23.103  14.487  1.00 11.29           O  
ATOM    130  CB  VAL A  17      10.735  20.980  12.605  1.00 12.08           C  
ATOM    131  CG1 VAL A  17      12.194  20.708  12.296  1.00 11.95           C  
ATOM    132  CG2 VAL A  17      10.000  19.675  12.914  1.00 12.46           C  
ATOM    133  N   ALA A  18      11.317  24.090  12.876  1.00 10.35           N  
ATOM    134  CA  ALA A  18      12.202  25.256  12.843  1.00  9.14           C  
ATOM    135  C   ALA A  18      12.196  26.028  14.157  1.00  8.97           C  
ATOM    136  O   ALA A  18      13.231  26.585  14.548  1.00  8.47           O  
ATOM    137  CB  ALA A  18      11.822  26.159  11.676  1.00  8.84           C  
ATOM    138  N   SER A  19      11.051  26.118  14.833  1.00  8.82           N  
ATOM    139  CA  SER A  19      10.972  26.864  16.094  1.00  9.55           C  
ATOM    140  C   SER A  19      11.855  26.190  17.144  1.00  9.74           C  
ATOM    141  O   SER A  19      12.557  26.872  17.888  1.00  9.52           O  
ATOM    142  CB  SER A  19       9.524  26.929  16.591  1.00 10.47           C  
ATOM    143  OG  SER A  19       8.780  27.849  15.787  1.00 10.73           O  
ATOM    144  N   CYS A  20      11.826  24.865  17.201  1.00 10.32           N  
ATOM    145  CA  CYS A  20      12.731  24.111  18.081  1.00 10.34           C  
ATOM    146  C   CYS A  20      14.191  24.358  17.757  1.00 10.90           C  
ATOM    147  O   CYS A  20      15.036  24.563  18.644  1.00 10.62           O  
ATOM    148  CB  CYS A  20      12.411  22.614  18.062  1.00 10.92           C  
ATOM    149  SG  CYS A  20      10.743  22.241  18.692  1.00 14.67           S  
ATOM    150  N   ALA A  21      14.548  24.442  16.461  1.00 10.25           N  
ATOM    151  CA  ALA A  21      15.929  24.742  16.097  1.00 10.51           C  
ATOM    152  C   ALA A  21      16.337  26.122  16.584  1.00  9.98           C  
ATOM    153  O   ALA A  21      17.446  26.343  17.072  1.00  9.18           O  
ATOM    154  CB  ALA A  21      16.114  24.652  14.577  1.00  9.54           C  
ATOM    155  N   LEU A  22      15.436  27.099  16.434  1.00  9.74           N  
ATOM    156  CA  LEU A  22      15.677  28.474  16.815  1.00 10.31           C  
ATOM    157  C   LEU A  22      15.889  28.563  18.323  1.00 10.17           C  
ATOM    158  O   LEU A  22      16.885  29.135  18.778  1.00 11.14           O  
ATOM    159  CB  LEU A  22      14.504  29.334  16.342  1.00  9.94           C  
ATOM    160  CG  LEU A  22      14.569  29.729  14.857  1.00 10.16           C  
ATOM    161  CD1 LEU A  22      13.209  30.212  14.386  1.00 10.58           C  
ATOM    162  CD2 LEU A  22      15.619  30.823  14.680  1.00  9.56           C  
ATOM    163  N   LEU A  23      14.997  27.906  19.062  1.00  9.59           N  
ATOM    164  CA  LEU A  23      15.120  27.853  20.518  1.00  9.72           C  
ATOM    165  C   LEU A  23      16.417  27.194  20.968  1.00 11.53           C  
ATOM    166  O   LEU A  23      17.091  27.696  21.882  1.00 11.71           O  
ATOM    167  CB  LEU A  23      13.910  27.118  21.083  1.00 10.34           C  
ATOM    168  CG  LEU A  23      12.642  27.964  21.266  1.00 11.01           C  
ATOM    169  CD1 LEU A  23      11.449  27.031  21.449  1.00 10.63           C  
ATOM    170  CD2 LEU A  23      12.805  28.920  22.443  1.00 12.05           C  
ATOM    171  N   GLN A  24      16.791  26.074  20.356  1.00 11.08           N  
ATOM    172  CA  GLN A  24      18.044  25.387  20.666  1.00 11.65           C  
ATOM    173  C   GLN A  24      19.240  26.288  20.396  1.00 11.15           C  
ATOM    174  O   GLN A  24      20.156  26.420  21.227  1.00 10.62           O  
ATOM    175  CB  GLN A  24      18.148  24.076  19.871  1.00 11.46           C  
ATOM    176  CG  GLN A  24      17.243  22.938  20.324  1.00 11.37           C  
ATOM    177  CD  GLN A  24      17.296  21.750  19.376  1.00 12.58           C  
ATOM    178  OE1 GLN A  24      18.347  21.510  18.768  1.00 12.60           O  
ATOM    179  NE2 GLN A  24      16.200  21.004  19.243  1.00 11.69           N  
ATOM    180  N   ALA A  25      19.243  27.017  19.285  1.00 11.85           N  
ATOM    181  CA  ALA A  25      20.322  27.943  18.976  1.00 12.91           C  
ATOM    182  C   ALA A  25      20.414  29.061  20.013  1.00 11.98           C  
ATOM    183  O   ALA A  25      21.500  29.489  20.394  1.00 12.64           O  
ATOM    184  CB  ALA A  25      20.126  28.565  17.592  1.00 12.09           C  
ATOM    185  N   ALA A  26      19.262  29.603  20.414  1.00 12.49           N  
ATOM    186  CA  ALA A  26      19.223  30.670  21.414  1.00 12.62           C  
ATOM    187  C   ALA A  26      19.733  30.178  22.768  1.00 11.89           C  
ATOM    188  O   ALA A  26      20.520  30.872  23.417  1.00 12.83           O  
ATOM    189  CB  ALA A  26      17.825  31.244  21.560  1.00 12.42           C  
ATOM    190  N   LYS A  27      19.369  28.975  23.171  1.00 14.50           N  
ATOM    191  CA  LYS A  27      19.926  28.381  24.390  1.00 16.56           C  
ATOM    192  C   LYS A  27      21.435  28.266  24.254  1.00 17.61           C  
ATOM    193  O   LYS A  27      22.186  28.676  25.155  1.00 18.08           O  
ATOM    194  CB  LYS A  27      19.281  27.037  24.714  1.00 17.63           C  
ATOM    195  CG  LYS A  27      19.965  26.242  25.821  1.00 19.15           C  
ATOM    196  CD  LYS A  27      19.304  24.884  26.019  1.00 20.85           C  
ATOM    197  CE  LYS A  27      19.602  24.311  27.399  1.00 22.37           C  
ATOM    198  NZ  LYS A  27      18.733  23.147  27.734  1.00 24.29           N  
ATOM    199  N   ALA A  28      21.930  27.787  23.110  1.00 17.42           N  
ATOM    200  CA  ALA A  28      23.356  27.692  22.839  1.00 18.60           C  
ATOM    201  C   ALA A  28      24.073  29.031  22.959  1.00 18.33           C  
ATOM    202  O   ALA A  28      25.222  29.118  23.434  1.00 16.76           O  
ATOM    203  CB  ALA A  28      23.595  27.128  21.431  1.00 17.50           C  
ATOM    204  N   ALA A  29      23.397  30.109  22.561  1.00 18.34           N  
ATOM    205  CA  ALA A  29      23.931  31.455  22.672  1.00 17.80           C  
ATOM    206  C   ALA A  29      23.903  31.974  24.110  1.00 18.59           C  
ATOM    207  O   ALA A  29      24.471  33.036  24.345  1.00 19.31           O  
ATOM    208  CB  ALA A  29      23.196  32.424  21.746  1.00 18.66           C  
ATOM    209  N   GLY A  30      23.248  31.295  25.034  1.00 18.86           N  
ATOM    210  CA  GLY A  30      23.222  31.665  26.439  1.00 17.78           C  
ATOM    211  C   GLY A  30      21.966  32.395  26.884  1.00 18.37           C  
ATOM    212  O   GLY A  30      21.939  32.994  27.964  1.00 16.17           O  
ATOM    213  N   TYR A  31      20.945  32.472  26.020  1.00 16.86           N  
ATOM    214  CA  TYR A  31      19.700  33.106  26.420  1.00 16.93           C  
ATOM    215  C   TYR A  31      18.847  32.199  27.306  1.00 16.67           C  
ATOM    216  O   TYR A  31      18.906  30.973  27.275  1.00 18.42           O  
ATOM    217  CB  TYR A  31      18.852  33.420  25.174  1.00 15.41           C  
ATOM    218  CG  TYR A  31      19.363  34.558  24.330  1.00 15.18           C  
ATOM    219  CD1 TYR A  31      19.093  35.880  24.694  1.00 15.41           C  
ATOM    220  CD2 TYR A  31      20.108  34.337  23.182  1.00 14.66           C  
ATOM    221  CE1 TYR A  31      19.551  36.933  23.925  1.00 15.40           C  
ATOM    222  CE2 TYR A  31      20.570  35.386  22.410  1.00 15.77           C  
ATOM    223  CZ  TYR A  31      20.288  36.678  22.790  1.00 16.11           C  
ATOM    224  OH  TYR A  31      20.762  37.721  22.026  1.00 16.95           O  
ATOM    225  N   ARG A  32      17.994  32.834  28.090  1.00 16.31           N  
ATOM    226  CA  ARG A  32      17.006  32.194  28.946  1.00 17.14           C  
ATOM    227  C   ARG A  32      15.739  32.162  28.070  1.00 15.89           C  
ATOM    228  O   ARG A  32      15.048  33.172  27.923  1.00 15.42           O  
ATOM    229  CB  ARG A  32      16.761  32.997  30.219  1.00 18.81           C  
ATOM    230  CG  ARG A  32      17.894  32.919  31.238  1.00 21.69           C  
ATOM    231  CD  ARG A  32      17.742  34.030  32.275  1.00 23.37           C  
ATOM    232  NE  ARG A  32      16.441  33.990  32.940  1.00 25.52           N  
ATOM    233  CZ  ARG A  32      16.084  33.133  33.891  1.00 25.82           C  
ATOM    234  NH1 ARG A  32      16.943  32.205  34.316  1.00 27.19           N  
ATOM    235  NH2 ARG A  32      14.869  33.193  34.424  1.00 25.16           N  
ATOM    236  N   THR A  33      15.504  31.027  27.427  1.00 15.13           N  
ATOM    237  CA  THR A  33      14.466  30.940  26.408  1.00 13.85           C  
ATOM    238  C   THR A  33      13.116  30.396  26.829  1.00 13.66           C  
ATOM    239  O   THR A  33      12.903  29.611  27.746  1.00 13.27           O  
ATOM    240  CB  THR A  33      14.952  30.077  25.218  1.00 14.57           C  
ATOM    241  OG1 THR A  33      14.994  28.709  25.615  1.00 13.13           O  
ATOM    242  CG2 THR A  33      16.323  30.489  24.723  1.00 14.47           C  
ATOM    243  N   ALA A  34      12.107  30.778  26.037  1.00 12.84           N  
ATOM    244  CA  ALA A  34      10.738  30.342  26.198  1.00 12.71           C  
ATOM    245  C   ALA A  34      10.074  30.317  24.812  1.00 12.41           C  
ATOM    246  O   ALA A  34      10.297  31.232  24.029  1.00 11.95           O  
ATOM    247  CB  ALA A  34       9.921  31.256  27.104  1.00 13.38           C  
ATOM    248  N   GLY A  35       9.289  29.270  24.594  1.00 12.11           N  
ATOM    249  CA  GLY A  35       8.485  29.174  23.380  1.00 11.46           C  
ATOM    250  C   GLY A  35       7.029  29.398  23.792  1.00 11.73           C  
ATOM    251  O   GLY A  35       6.590  29.028  24.888  1.00 11.41           O  
ATOM    252  N   TYR A  36       6.285  30.017  22.889  1.00  9.63           N  
ATOM    253  CA  TYR A  36       4.905  30.393  23.195  1.00  9.79           C  
ATOM    254  C   TYR A  36       4.052  30.020  21.994  1.00 10.01           C  
ATOM    255  O   TYR A  36       4.387  30.448  20.883  1.00  9.52           O  
ATOM    256  CB  TYR A  36       4.852  31.881  23.535  1.00  9.04           C  
ATOM    257  CG  TYR A  36       3.532  32.457  24.012  1.00  9.31           C  
ATOM    258  CD1 TYR A  36       2.798  31.834  25.010  1.00  9.43           C  
ATOM    259  CD2 TYR A  36       3.032  33.637  23.487  1.00 10.13           C  
ATOM    260  CE1 TYR A  36       1.597  32.356  25.465  1.00  9.61           C  
ATOM    261  CE2 TYR A  36       1.820  34.173  23.925  1.00  9.98           C  
ATOM    262  CZ  TYR A  36       1.114  33.523  24.913  1.00 10.28           C  
ATOM    263  OH  TYR A  36      -0.092  34.049  25.350  1.00  8.87           O  
ATOM    264  N   LYS A  37       3.036  29.223  22.248  1.00 10.11           N  
ATOM    265  CA  LYS A  37       2.043  28.827  21.224  1.00  9.62           C  
ATOM    266  C   LYS A  37       0.698  29.219  21.823  1.00  9.47           C  
ATOM    267  O   LYS A  37      -0.008  28.440  22.475  1.00 10.96           O  
ATOM    268  CB  LYS A  37       2.181  27.338  20.931  1.00 10.16           C  
ATOM    269  CG  LYS A  37       1.130  26.722  20.005  1.00 11.25           C  
ATOM    270  CD  LYS A  37       1.603  26.590  18.562  1.00 11.49           C  
ATOM    271  CE  LYS A  37       0.487  26.070  17.654  1.00 11.59           C  
ATOM    272  NZ  LYS A  37       0.901  26.035  16.213  1.00 13.85           N  
ATOM    273  N   PRO A  38       0.311  30.490  21.699  1.00 10.08           N  
ATOM    274  CA  PRO A  38      -0.887  31.008  22.331  1.00  9.96           C  
ATOM    275  C   PRO A  38      -2.155  30.286  21.931  1.00 10.76           C  
ATOM    276  O   PRO A  38      -3.022  30.052  22.774  1.00 10.77           O  
ATOM    277  CB  PRO A  38      -0.946  32.488  21.994  1.00  9.38           C  
ATOM    278  CG  PRO A  38      -0.013  32.649  20.836  1.00  9.47           C  
ATOM    279  CD  PRO A  38       1.016  31.565  20.965  1.00  9.86           C  
ATOM    280  N   VAL A  39      -2.252  29.978  20.640  1.00  9.92           N  
ATOM    281  CA  VAL A  39      -3.455  29.324  20.131  1.00 10.61           C  
ATOM    282  C   VAL A  39      -3.071  28.015  19.451  1.00 11.10           C  
ATOM    283  O   VAL A  39      -2.217  28.018  18.564  1.00 10.71           O  
ATOM    284  CB  VAL A  39      -4.184  30.261  19.125  1.00 10.40           C  
ATOM    285  CG1 VAL A  39      -5.294  29.481  18.423  1.00 11.40           C  
ATOM    286  CG2 VAL A  39      -4.763  31.488  19.813  1.00 10.79           C  
ATOM    287  N   ALA A  40      -3.709  26.926  19.856  1.00 11.63           N  
ATOM    288  CA  ALA A  40      -3.441  25.621  19.261  1.00 12.87           C  
ATOM    289  C   ALA A  40      -4.706  24.789  19.101  1.00 13.19           C  
ATOM    290  O   ALA A  40      -5.597  24.772  19.955  1.00 14.02           O  
ATOM    291  CB  ALA A  40      -2.435  24.888  20.165  1.00 13.22           C  
ATOM    292  N   SER A  41      -4.809  24.058  17.993  1.00 13.35           N  
ATOM    293  CA  SER A  41      -5.938  23.179  17.730  1.00 13.62           C  
ATOM    294  C   SER A  41      -5.372  21.853  17.215  1.00 13.98           C  
ATOM    295  O   SER A  41      -4.308  21.854  16.593  1.00 14.71           O  
ATOM    296  CB  SER A  41      -6.968  23.776  16.784  1.00 14.03           C  
ATOM    297  OG  SER A  41      -6.456  23.880  15.473  1.00 14.52           O  
ATOM    298  N   GLY A  42      -6.055  20.766  17.539  1.00 15.48           N  
ATOM    299  CA  GLY A  42      -5.562  19.433  17.127  1.00 16.51           C  
ATOM    300  C   GLY A  42      -4.743  18.975  18.352  1.00 17.74           C  
ATOM    301  O   GLY A  42      -3.519  19.083  18.354  1.00 17.36           O  
ATOM    302  N   SER A  43      -5.464  18.608  19.408  1.00 17.56           N  
ATOM    303  CA  SER A  43      -4.838  18.227  20.668  1.00 18.04           C  
ATOM    304  C   SER A  43      -5.374  16.939  21.278  1.00 18.99           C  
ATOM    305  O   SER A  43      -6.553  16.604  21.110  1.00 19.43           O  
ATOM    306  CB  SER A  43      -5.055  19.371  21.678  1.00 18.51           C  
ATOM    307  OG  SER A  43      -4.641  20.613  21.114  1.00 18.56           O  
ATOM    308  N   GLU A  44      -4.527  16.264  22.059  1.00 19.85           N  
ATOM    309  CA  GLU A  44      -4.918  15.013  22.699  1.00 21.00           C  
ATOM    310  C   GLU A  44      -5.321  15.135  24.161  1.00 19.50           C  
ATOM    311  O   GLU A  44      -4.899  16.004  24.913  1.00 16.57           O  
ATOM    312  CB  GLU A  44      -3.773  14.003  22.540  1.00 23.86           C  
ATOM    313  CG  GLU A  44      -3.937  13.179  21.265  1.00 27.56           C  
ATOM    314  CD  GLU A  44      -4.789  11.950  21.538  1.00 30.15           C  
ATOM    315  OE1 GLU A  44      -6.016  12.094  21.758  1.00 31.82           O  
ATOM    316  OE2 GLU A  44      -4.223  10.830  21.544  1.00 31.80           O  
ATOM    317  N   LYS A  45      -6.236  14.247  24.574  1.00 18.93           N  
ATOM    318  CA  LYS A  45      -6.726  14.268  25.946  1.00 19.28           C  
ATOM    319  C   LYS A  45      -5.690  13.636  26.870  1.00 18.93           C  
ATOM    320  O   LYS A  45      -5.001  12.695  26.478  1.00 18.62           O  
ATOM    321  CB  LYS A  45      -8.050  13.518  26.083  1.00 21.12           C  
ATOM    322  CG  LYS A  45      -7.956  12.071  25.650  1.00 22.24           C  
ATOM    323  CD  LYS A  45      -9.318  11.386  25.629  1.00 24.39           C  
ATOM    324  CE  LYS A  45      -9.111   9.939  25.194  1.00 25.51           C  
ATOM    325  NZ  LYS A  45      -8.687   9.103  26.360  1.00 26.20           N  
ATOM    326  N   THR A  46      -5.497  14.222  28.040  1.00 17.38           N  
ATOM    327  CA  THR A  46      -4.608  13.689  29.071  1.00 18.26           C  
ATOM    328  C   THR A  46      -5.351  13.898  30.389  1.00 18.80           C  
ATOM    329  O   THR A  46      -6.328  14.660  30.446  1.00 18.24           O  
ATOM    330  CB  THR A  46      -3.215  14.340  29.193  1.00 17.41           C  
ATOM    331  OG1 THR A  46      -3.300  15.592  29.878  1.00 16.00           O  
ATOM    332  CG2 THR A  46      -2.532  14.568  27.853  1.00 17.59           C  
ATOM    333  N   PRO A  47      -4.830  13.361  31.481  1.00 19.37           N  
ATOM    334  CA  PRO A  47      -5.415  13.545  32.799  1.00 19.99           C  
ATOM    335  C   PRO A  47      -5.460  14.987  33.266  1.00 20.42           C  
ATOM    336  O   PRO A  47      -6.258  15.397  34.117  1.00 20.01           O  
ATOM    337  CB  PRO A  47      -4.537  12.681  33.715  1.00 19.24           C  
ATOM    338  CG  PRO A  47      -3.949  11.660  32.796  1.00 19.22           C  
ATOM    339  CD  PRO A  47      -3.654  12.452  31.530  1.00 19.21           C  
ATOM    340  N   GLU A  48      -4.583  15.832  32.727  1.00 20.68           N  
ATOM    341  CA  GLU A  48      -4.516  17.234  33.068  1.00 20.67           C  
ATOM    342  C   GLU A  48      -5.322  18.130  32.125  1.00 19.10           C  
ATOM    343  O   GLU A  48      -5.449  19.318  32.398  1.00 17.03           O  
ATOM    344  CB  GLU A  48      -3.046  17.664  33.066  1.00 23.71           C  
ATOM    345  CG  GLU A  48      -2.223  16.868  34.088  1.00 27.13           C  
ATOM    346  CD  GLU A  48      -1.316  17.832  34.838  1.00 29.47           C  
ATOM    347  OE1 GLU A  48      -0.229  18.117  34.304  1.00 29.53           O  
ATOM    348  OE2 GLU A  48      -1.727  18.295  35.924  1.00 31.33           O  
ATOM    349  N   GLY A  49      -5.944  17.533  31.115  1.00 17.26           N  
ATOM    350  CA  GLY A  49      -6.688  18.313  30.123  1.00 18.22           C  
ATOM    351  C   GLY A  49      -6.034  18.121  28.755  1.00 17.27           C  
ATOM    352  O   GLY A  49      -5.129  17.303  28.590  1.00 18.60           O  
ATOM    353  N   LEU A  50      -6.519  18.870  27.765  1.00 16.80           N  
ATOM    354  CA  LEU A  50      -5.999  18.734  26.409  1.00 15.46           C  
ATOM    355  C   LEU A  50      -4.562  19.204  26.306  1.00 13.60           C  
ATOM    356  O   LEU A  50      -4.192  20.198  26.923  1.00 12.66           O  
ATOM    357  CB  LEU A  50      -6.920  19.556  25.480  1.00 16.33           C  
ATOM    358  CG  LEU A  50      -8.377  19.056  25.452  1.00 17.35           C  
ATOM    359  CD1 LEU A  50      -9.260  19.994  24.635  1.00 18.28           C  
ATOM    360  CD2 LEU A  50      -8.414  17.653  24.878  1.00 18.75           C  
ATOM    361  N   ARG A  51      -3.741  18.504  25.521  1.00 14.51           N  
ATOM    362  CA  ARG A  51      -2.346  18.915  25.342  1.00 13.76           C  
ATOM    363  C   ARG A  51      -2.014  18.908  23.848  1.00 13.68           C  
ATOM    364  O   ARG A  51      -2.281  17.890  23.203  1.00 13.02           O  
ATOM    365  CB  ARG A  51      -1.434  17.932  26.083  1.00 15.49           C  
ATOM    366  CG  ARG A  51      -1.425  18.019  27.592  1.00 16.67           C  
ATOM    367  CD  ARG A  51      -0.912  19.346  28.083  1.00 17.55           C  
ATOM    368  NE  ARG A  51      -0.891  19.515  29.535  1.00 19.19           N  
ATOM    369  CZ  ARG A  51      -1.765  20.196  30.249  1.00 19.42           C  
ATOM    370  NH1 ARG A  51      -2.832  20.743  29.681  1.00 20.34           N  
ATOM    371  NH2 ARG A  51      -1.592  20.296  31.564  1.00 20.80           N  
ATOM    372  N   ASN A  52      -1.489  19.996  23.300  1.00 12.16           N  
ATOM    373  CA  ASN A  52      -1.141  20.016  21.868  1.00 11.89           C  
ATOM    374  C   ASN A  52       0.330  19.706  21.660  1.00 12.26           C  
ATOM    375  O   ASN A  52       1.200  20.210  22.368  1.00 12.32           O  
ATOM    376  CB  ASN A  52      -1.480  21.408  21.321  1.00 12.49           C  
ATOM    377  CG  ASN A  52      -0.955  21.683  19.928  1.00 12.12           C  
ATOM    378  OD1 ASN A  52      -1.639  21.409  18.928  1.00 14.21           O  
ATOM    379  ND2 ASN A  52       0.222  22.267  19.852  1.00 10.27           N  
ATOM    380  N   SER A  53       0.652  18.925  20.629  1.00 12.74           N  
ATOM    381  CA  SER A  53       2.011  18.514  20.342  1.00 13.36           C  
ATOM    382  C   SER A  53       2.969  19.642  19.996  1.00 13.88           C  
ATOM    383  O   SER A  53       4.141  19.504  20.379  1.00 12.91           O  
ATOM    384  CB  SER A  53       2.032  17.415  19.278  1.00 14.95           C  
ATOM    385  OG  SER A  53       1.768  17.910  17.985  1.00 16.56           O  
ATOM    386  N   ASP A  54       2.563  20.699  19.291  1.00 12.43           N  
ATOM    387  CA  ASP A  54       3.461  21.815  19.031  1.00 12.46           C  
ATOM    388  C   ASP A  54       3.832  22.476  20.360  1.00 11.77           C  
ATOM    389  O   ASP A  54       5.002  22.735  20.610  1.00 11.95           O  
ATOM    390  CB  ASP A  54       2.859  22.935  18.169  1.00 12.72           C  
ATOM    391  CG  ASP A  54       2.582  22.553  16.741  1.00 12.72           C  
ATOM    392  OD1 ASP A  54       2.704  21.358  16.435  1.00 12.66           O  
ATOM    393  OD2 ASP A  54       2.263  23.452  15.923  1.00 14.34           O  
ATOM    394  N   ALA A  55       2.826  22.692  21.213  1.00 12.41           N  
ATOM    395  CA  ALA A  55       3.093  23.325  22.508  1.00 12.50           C  
ATOM    396  C   ALA A  55       4.054  22.488  23.339  1.00 12.74           C  
ATOM    397  O   ALA A  55       4.950  23.022  23.997  1.00 12.59           O  
ATOM    398  CB  ALA A  55       1.805  23.563  23.289  1.00 12.39           C  
ATOM    399  N   LEU A  56       3.884  21.165  23.311  1.00 13.56           N  
ATOM    400  CA  LEU A  56       4.801  20.279  24.046  1.00 13.67           C  
ATOM    401  C   LEU A  56       6.219  20.378  23.501  1.00 13.70           C  
ATOM    402  O   LEU A  56       7.187  20.410  24.272  1.00 13.59           O  
ATOM    403  CB  LEU A  56       4.279  18.848  24.018  1.00 14.12           C  
ATOM    404  CG  LEU A  56       2.987  18.541  24.785  1.00 15.25           C  
ATOM    405  CD1 LEU A  56       2.612  17.066  24.620  1.00 14.88           C  
ATOM    406  CD2 LEU A  56       3.133  18.856  26.261  1.00 15.79           C  
ATOM    407  N   ALA A  57       6.384  20.472  22.174  1.00 13.02           N  
ATOM    408  CA  ALA A  57       7.707  20.599  21.566  1.00 13.36           C  
ATOM    409  C   ALA A  57       8.393  21.899  21.972  1.00 13.00           C  
ATOM    410  O   ALA A  57       9.570  21.946  22.328  1.00 12.77           O  
ATOM    411  CB  ALA A  57       7.622  20.561  20.044  1.00 12.92           C  
ATOM    412  N   LEU A  58       7.613  22.989  21.975  1.00 13.02           N  
ATOM    413  CA  LEU A  58       8.120  24.296  22.382  1.00 13.18           C  
ATOM    414  C   LEU A  58       8.483  24.268  23.871  1.00 14.82           C  
ATOM    415  O   LEU A  58       9.501  24.836  24.287  1.00 15.22           O  
ATOM    416  CB  LEU A  58       7.103  25.399  22.098  1.00 12.47           C  
ATOM    417  CG  LEU A  58       6.708  25.685  20.657  1.00 12.74           C  
ATOM    418  CD1 LEU A  58       5.844  26.945  20.559  1.00 12.83           C  
ATOM    419  CD2 LEU A  58       7.876  25.890  19.699  1.00 12.39           C  
ATOM    420  N   GLN A  59       7.621  23.654  24.670  1.00 14.39           N  
ATOM    421  CA  GLN A  59       7.880  23.523  26.107  1.00 15.67           C  
ATOM    422  C   GLN A  59       9.168  22.753  26.378  1.00 15.86           C  
ATOM    423  O   GLN A  59      10.025  23.215  27.137  1.00 16.66           O  
ATOM    424  CB  GLN A  59       6.707  22.804  26.783  1.00 15.80           C  
ATOM    425  CG  GLN A  59       6.831  22.705  28.298  1.00 17.27           C  
ATOM    426  CD  GLN A  59       5.685  21.901  28.892  1.00 17.20           C  
ATOM    427  OE1 GLN A  59       5.157  20.991  28.265  1.00 16.53           O  
ATOM    428  NE2 GLN A  59       5.271  22.242  30.107  1.00 17.03           N  
ATOM    429  N   ARG A  60       9.375  21.603  25.732  1.00 16.24           N  
ATOM    430  CA  ARG A  60      10.574  20.800  25.982  1.00 17.54           C  
ATOM    431  C   ARG A  60      11.830  21.416  25.393  1.00 16.85           C  
ATOM    432  O   ARG A  60      12.941  21.145  25.855  1.00 16.57           O  
ATOM    433  CB  ARG A  60      10.394  19.361  25.514  1.00 20.23           C  
ATOM    434  CG  ARG A  60      10.259  19.152  24.024  1.00 22.71           C  
ATOM    435  CD  ARG A  60       9.967  17.684  23.713  1.00 25.63           C  
ATOM    436  NE  ARG A  60       8.919  17.142  24.571  1.00 27.57           N  
ATOM    437  CZ  ARG A  60       7.688  16.834  24.172  1.00 28.64           C  
ATOM    438  NH1 ARG A  60       7.316  17.013  22.907  1.00 29.05           N  
ATOM    439  NH2 ARG A  60       6.794  16.345  25.017  1.00 29.24           N  
ATOM    440  N   ASN A  61      11.693  22.295  24.392  1.00 16.31           N  
ATOM    441  CA  ASN A  61      12.852  22.955  23.827  1.00 15.73           C  
ATOM    442  C   ASN A  61      13.151  24.300  24.479  1.00 16.05           C  
ATOM    443  O   ASN A  61      14.105  24.958  24.062  1.00 16.05           O  
ATOM    444  CB  ASN A  61      12.735  23.097  22.305  1.00 15.24           C  
ATOM    445  CG  ASN A  61      13.167  21.804  21.635  1.00 15.52           C  
ATOM    446  OD1 ASN A  61      14.371  21.615  21.420  1.00 17.28           O  
ATOM    447  ND2 ASN A  61      12.225  20.936  21.312  1.00 14.85           N  
ATOM    448  N   SER A  62      12.401  24.704  25.494  1.00 15.29           N  
ATOM    449  CA  SER A  62      12.672  25.944  26.211  1.00 16.34           C  
ATOM    450  C   SER A  62      13.774  25.677  27.247  1.00 16.90           C  
ATOM    451  O   SER A  62      13.843  24.541  27.718  1.00 16.08           O  
ATOM    452  CB  SER A  62      11.414  26.452  26.915  1.00 16.10           C  
ATOM    453  OG  SER A  62      10.362  26.688  25.983  1.00 17.13           O  
ATOM    454  N   SER A  63      14.634  26.645  27.551  1.00 18.20           N  
ATOM    455  CA  SER A  63      15.715  26.381  28.513  1.00 19.01           C  
ATOM    456  C   SER A  63      15.105  26.381  29.916  1.00 20.60           C  
ATOM    457  O   SER A  63      15.548  25.659  30.801  1.00 20.54           O  
ATOM    458  CB  SER A  63      16.885  27.341  28.427  1.00 18.77           C  
ATOM    459  OG  SER A  63      16.549  28.696  28.659  1.00 17.71           O  
ATOM    460  N   LEU A  64      14.077  27.205  30.094  1.00 21.23           N  
ATOM    461  CA  LEU A  64      13.363  27.257  31.361  1.00 22.47           C  
ATOM    462  C   LEU A  64      12.351  26.121  31.446  1.00 23.52           C  
ATOM    463  O   LEU A  64      11.857  25.635  30.424  1.00 23.32           O  
ATOM    464  CB  LEU A  64      12.639  28.599  31.481  1.00 23.20           C  
ATOM    465  CG  LEU A  64      13.541  29.839  31.456  1.00 23.63           C  
ATOM    466  CD1 LEU A  64      12.738  31.072  31.086  1.00 24.71           C  
ATOM    467  CD2 LEU A  64      14.269  30.000  32.785  1.00 24.39           C  
ATOM    468  N   GLN A  65      12.041  25.713  32.671  1.00 24.03           N  
ATOM    469  CA  GLN A  65      10.985  24.720  32.876  1.00 24.98           C  
ATOM    470  C   GLN A  65       9.690  25.532  32.953  1.00 23.71           C  
ATOM    471  O   GLN A  65       9.573  26.440  33.781  1.00 23.44           O  
ATOM    472  CB  GLN A  65      11.230  23.859  34.104  1.00 27.88           C  
ATOM    473  CG  GLN A  65      12.544  23.101  34.082  1.00 30.69           C  
ATOM    474  CD  GLN A  65      12.390  21.593  34.042  1.00 32.78           C  
ATOM    475  OE1 GLN A  65      12.835  20.944  33.087  1.00 34.09           O  
ATOM    476  NE2 GLN A  65      11.769  21.010  35.060  1.00 32.70           N  
ATOM    477  N   LEU A  66       8.813  25.355  31.964  1.00 21.07           N  
ATOM    478  CA  LEU A  66       7.595  26.154  31.900  1.00 19.91           C  
ATOM    479  C   LEU A  66       6.342  25.319  32.091  1.00 18.39           C  
ATOM    480  O   LEU A  66       6.271  24.211  31.557  1.00 17.63           O  
ATOM    481  CB  LEU A  66       7.499  26.860  30.534  1.00 19.93           C  
ATOM    482  CG  LEU A  66       8.613  27.851  30.206  1.00 20.72           C  
ATOM    483  CD1 LEU A  66       8.668  28.149  28.710  1.00 20.81           C  
ATOM    484  CD2 LEU A  66       8.434  29.126  31.018  1.00 20.84           C  
ATOM    485  N   ASP A  67       5.349  25.846  32.809  1.00 17.39           N  
ATOM    486  CA  ASP A  67       4.088  25.114  32.973  1.00 16.82           C  
ATOM    487  C   ASP A  67       3.402  25.071  31.609  1.00 15.10           C  
ATOM    488  O   ASP A  67       3.453  26.068  30.881  1.00 15.11           O  
ATOM    489  CB  ASP A  67       3.171  25.777  34.009  1.00 18.36           C  
ATOM    490  CG  ASP A  67       3.898  26.020  35.327  1.00 19.33           C  
ATOM    491  OD1 ASP A  67       4.511  25.055  35.811  1.00 20.70           O  
ATOM    492  OD2 ASP A  67       3.915  27.145  35.864  1.00 21.62           O  
ATOM    493  N   TYR A  68       2.682  24.005  31.298  1.00 14.19           N  
ATOM    494  CA  TYR A  68       2.028  23.894  29.997  1.00 14.56           C  
ATOM    495  C   TYR A  68       1.139  25.079  29.679  1.00 14.08           C  
ATOM    496  O   TYR A  68       1.242  25.680  28.599  1.00 13.66           O  
ATOM    497  CB  TYR A  68       1.222  22.576  29.884  1.00 14.02           C  
ATOM    498  CG  TYR A  68       0.588  22.502  28.499  1.00 13.33           C  
ATOM    499  CD1 TYR A  68       1.339  22.021  27.432  1.00 12.56           C  
ATOM    500  CD2 TYR A  68      -0.704  22.942  28.266  1.00 12.25           C  
ATOM    501  CE1 TYR A  68       0.798  21.962  26.165  1.00 12.92           C  
ATOM    502  CE2 TYR A  68      -1.252  22.881  26.998  1.00 11.58           C  
ATOM    503  CZ  TYR A  68      -0.498  22.403  25.951  1.00 12.73           C  
ATOM    504  OH  TYR A  68      -1.033  22.354  24.686  1.00 12.11           O  
ATOM    505  N   ALA A  69       0.245  25.484  30.591  1.00 13.28           N  
ATOM    506  CA  ALA A  69      -0.666  26.592  30.286  1.00 12.75           C  
ATOM    507  C   ALA A  69       0.037  27.894  29.959  1.00 12.95           C  
ATOM    508  O   ALA A  69      -0.495  28.757  29.250  1.00 13.04           O  
ATOM    509  CB  ALA A  69      -1.675  26.772  31.412  1.00 13.59           C  
ATOM    510  N   THR A  70       1.249  28.089  30.463  1.00 12.40           N  
ATOM    511  CA  THR A  70       2.032  29.282  30.201  1.00 12.93           C  
ATOM    512  C   THR A  70       2.538  29.266  28.757  1.00 12.33           C  
ATOM    513  O   THR A  70       2.698  30.318  28.146  1.00 11.89           O  
ATOM    514  CB  THR A  70       3.200  29.356  31.200  1.00 14.96           C  
ATOM    515  OG1 THR A  70       2.680  29.218  32.546  1.00 16.47           O  
ATOM    516  CG2 THR A  70       3.889  30.696  31.052  1.00 17.64           C  
ATOM    517  N   VAL A  71       2.775  28.070  28.244  1.00 11.46           N  
ATOM    518  CA  VAL A  71       3.235  27.941  26.848  1.00 12.49           C  
ATOM    519  C   VAL A  71       2.023  28.033  25.929  1.00 11.87           C  
ATOM    520  O   VAL A  71       2.120  28.648  24.869  1.00 12.89           O  
ATOM    521  CB  VAL A  71       3.976  26.623  26.608  1.00 12.40           C  
ATOM    522  CG1 VAL A  71       4.279  26.352  25.136  1.00 14.17           C  
ATOM    523  CG2 VAL A  71       5.276  26.605  27.421  1.00 13.97           C  
ATOM    524  N   ASN A  72       0.911  27.439  26.352  1.00 10.96           N  
ATOM    525  CA  ASN A  72      -0.278  27.413  25.507  1.00 10.69           C  
ATOM    526  C   ASN A  72      -1.601  27.587  26.240  1.00 11.53           C  
ATOM    527  O   ASN A  72      -2.310  26.646  26.617  1.00 10.89           O  
ATOM    528  CB  ASN A  72      -0.276  26.102  24.697  1.00 10.77           C  
ATOM    529  CG  ASN A  72      -1.562  25.905  23.913  1.00 11.00           C  
ATOM    530  OD1 ASN A  72      -2.046  26.802  23.209  1.00 11.27           O  
ATOM    531  ND2 ASN A  72      -2.146  24.731  24.065  1.00  9.61           N  
ATOM    532  N   PRO A  73      -2.009  28.851  26.416  1.00 11.78           N  
ATOM    533  CA  PRO A  73      -3.251  29.190  27.073  1.00 12.43           C  
ATOM    534  C   PRO A  73      -4.517  28.682  26.394  1.00 13.19           C  
ATOM    535  O   PRO A  73      -5.500  28.340  27.071  1.00 14.09           O  
ATOM    536  CB  PRO A  73      -3.247  30.715  27.116  1.00 12.93           C  
ATOM    537  CG  PRO A  73      -1.878  31.170  26.758  1.00 12.61           C  
ATOM    538  CD  PRO A  73      -1.224  30.044  26.021  1.00 12.51           C  
ATOM    539  N   TYR A  74      -4.568  28.647  25.068  1.00 12.30           N  
ATOM    540  CA  TYR A  74      -5.764  28.229  24.336  1.00 11.47           C  
ATOM    541  C   TYR A  74      -5.553  26.932  23.560  1.00 12.22           C  
ATOM    542  O   TYR A  74      -4.888  26.895  22.532  1.00 11.96           O  
ATOM    543  CB  TYR A  74      -6.178  29.324  23.344  1.00 11.86           C  
ATOM    544  CG  TYR A  74      -6.817  30.562  23.896  1.00  9.79           C  
ATOM    545  CD1 TYR A  74      -8.083  30.553  24.482  1.00  9.41           C  
ATOM    546  CD2 TYR A  74      -6.140  31.766  23.832  1.00  9.93           C  
ATOM    547  CE1 TYR A  74      -8.647  31.716  24.982  1.00 10.72           C  
ATOM    548  CE2 TYR A  74      -6.691  32.939  24.322  1.00 10.59           C  
ATOM    549  CZ  TYR A  74      -7.941  32.902  24.892  1.00 11.03           C  
ATOM    550  OH  TYR A  74      -8.467  34.072  25.374  1.00 11.15           O  
ATOM    551  N   THR A  75      -6.123  25.842  24.047  1.00 13.43           N  
ATOM    552  CA  THR A  75      -5.995  24.520  23.472  1.00 14.02           C  
ATOM    553  C   THR A  75      -7.322  23.922  23.032  1.00 14.68           C  
ATOM    554  O   THR A  75      -8.227  23.721  23.838  1.00 15.01           O  
ATOM    555  CB  THR A  75      -5.358  23.560  24.518  1.00 14.74           C  
ATOM    556  OG1 THR A  75      -4.407  24.293  25.303  1.00 14.84           O  
ATOM    557  CG2 THR A  75      -4.671  22.409  23.806  1.00 14.69           C  
ATOM    558  N   PHE A  76      -7.428  23.615  21.741  1.00 14.48           N  
ATOM    559  CA  PHE A  76      -8.647  23.027  21.181  1.00 14.34           C  
ATOM    560  C   PHE A  76      -8.364  21.605  20.701  1.00 13.53           C  
ATOM    561  O   PHE A  76      -7.295  21.338  20.174  1.00 12.28           O  
ATOM    562  CB  PHE A  76      -9.189  23.896  20.038  1.00 14.53           C  
ATOM    563  CG  PHE A  76      -9.548  25.286  20.508  1.00 14.38           C  
ATOM    564  CD1 PHE A  76     -10.732  25.516  21.192  1.00 14.78           C  
ATOM    565  CD2 PHE A  76      -8.692  26.345  20.263  1.00 13.80           C  
ATOM    566  CE1 PHE A  76     -11.046  26.798  21.613  1.00 15.96           C  
ATOM    567  CE2 PHE A  76      -9.007  27.625  20.684  1.00 15.27           C  
ATOM    568  CZ  PHE A  76     -10.191  27.853  21.368  1.00 15.05           C  
ATOM    569  N   ALA A  77      -9.328  20.700  20.865  1.00 15.01           N  
ATOM    570  CA  ALA A  77      -9.131  19.314  20.454  1.00 16.79           C  
ATOM    571  C   ALA A  77      -9.093  19.131  18.944  1.00 17.95           C  
ATOM    572  O   ALA A  77      -8.249  18.409  18.405  1.00 17.82           O  
ATOM    573  CB  ALA A  77     -10.265  18.439  21.016  1.00 17.66           C  
ATOM    574  N   GLU A  78     -10.079  19.743  18.263  1.00 17.61           N  
ATOM    575  CA  GLU A  78     -10.163  19.515  16.819  1.00 17.98           C  
ATOM    576  C   GLU A  78      -9.189  20.376  16.035  1.00 18.00           C  
ATOM    577  O   GLU A  78      -9.129  21.594  16.187  1.00 17.98           O  
ATOM    578  CB  GLU A  78     -11.598  19.757  16.340  1.00 17.64           C  
ATOM    579  CG  GLU A  78     -11.839  19.403  14.874  1.00 17.94           C  
ATOM    580  CD  GLU A  78     -13.205  19.898  14.422  1.00 18.13           C  
ATOM    581  OE1 GLU A  78     -14.118  19.935  15.274  1.00 18.02           O  
ATOM    582  OE2 GLU A  78     -13.362  20.253  13.237  1.00 17.56           O  
ATOM    583  N   PRO A  79      -8.427  19.751  15.139  1.00 18.77           N  
ATOM    584  CA  PRO A  79      -7.462  20.425  14.296  1.00 18.90           C  
ATOM    585  C   PRO A  79      -8.078  21.193  13.136  1.00 18.74           C  
ATOM    586  O   PRO A  79      -7.742  20.938  11.969  1.00 19.12           O  
ATOM    587  CB  PRO A  79      -6.588  19.283  13.772  1.00 19.90           C  
ATOM    588  CG  PRO A  79      -7.520  18.126  13.702  1.00 20.17           C  
ATOM    589  CD  PRO A  79      -8.439  18.283  14.891  1.00 19.47           C  
ATOM    590  N   THR A  80      -8.951  22.149  13.421  1.00 15.51           N  
ATOM    591  CA  THR A  80      -9.561  22.978  12.388  1.00 14.91           C  
ATOM    592  C   THR A  80      -9.191  24.435  12.648  1.00 13.36           C  
ATOM    593  O   THR A  80      -8.388  24.674  13.555  1.00 12.77           O  
ATOM    594  CB  THR A  80     -11.078  22.802  12.298  1.00 14.95           C  
ATOM    595  OG1 THR A  80     -11.554  23.572  11.182  1.00 15.27           O  
ATOM    596  CG2 THR A  80     -11.783  23.295  13.555  1.00 13.99           C  
ATOM    597  N   SER A  81      -9.656  25.378  11.830  1.00 12.30           N  
ATOM    598  CA  SER A  81      -9.273  26.771  12.087  1.00 11.50           C  
ATOM    599  C   SER A  81      -9.728  27.193  13.480  1.00 10.44           C  
ATOM    600  O   SER A  81     -10.856  26.904  13.872  1.00 10.26           O  
ATOM    601  CB  SER A  81      -9.970  27.660  11.050  1.00 11.48           C  
ATOM    602  OG  SER A  81      -9.504  28.985  11.137  1.00 12.71           O  
ATOM    603  N   PRO A  82      -8.882  27.903  14.219  1.00 10.57           N  
ATOM    604  CA  PRO A  82      -9.200  28.379  15.556  1.00 10.52           C  
ATOM    605  C   PRO A  82     -10.541  29.069  15.679  1.00 11.73           C  
ATOM    606  O   PRO A  82     -11.313  28.760  16.605  1.00 10.65           O  
ATOM    607  CB  PRO A  82      -8.052  29.346  15.876  1.00 10.80           C  
ATOM    608  CG  PRO A  82      -6.893  28.738  15.152  1.00 11.14           C  
ATOM    609  CD  PRO A  82      -7.495  28.257  13.835  1.00 10.76           C  
ATOM    610  N   HIS A  83     -10.878  29.991  14.770  1.00 10.35           N  
ATOM    611  CA  HIS A  83     -12.185  30.648  14.864  1.00 12.28           C  
ATOM    612  C   HIS A  83     -13.365  29.680  14.820  1.00 12.18           C  
ATOM    613  O   HIS A  83     -14.368  29.913  15.514  1.00 12.04           O  
ATOM    614  CB  HIS A  83     -12.319  31.737  13.803  1.00 11.35           C  
ATOM    615  CG  HIS A  83     -12.594  31.267  12.414  1.00 12.49           C  
ATOM    616  ND1 HIS A  83     -11.779  30.421  11.701  1.00 12.93           N  
ATOM    617  CD2 HIS A  83     -13.656  31.569  11.615  1.00 12.28           C  
ATOM    618  CE1 HIS A  83     -12.324  30.224  10.507  1.00 12.30           C  
ATOM    619  NE2 HIS A  83     -13.453  30.904  10.429  1.00 11.80           N  
ATOM    620  N   ILE A  84     -13.318  28.609  14.048  1.00 12.24           N  
ATOM    621  CA  ILE A  84     -14.414  27.654  13.938  1.00 13.38           C  
ATOM    622  C   ILE A  84     -14.675  26.892  15.225  1.00 13.96           C  
ATOM    623  O   ILE A  84     -15.785  26.886  15.768  1.00 14.44           O  
ATOM    624  CB  ILE A  84     -14.127  26.663  12.787  1.00 12.31           C  
ATOM    625  CG1 ILE A  84     -14.255  27.443  11.473  1.00 12.00           C  
ATOM    626  CG2 ILE A  84     -15.077  25.479  12.777  1.00 13.43           C  
ATOM    627  CD1 ILE A  84     -13.649  26.719  10.293  1.00 12.54           C  
ATOM    628  N   ILE A  85     -13.615  26.275  15.745  1.00 14.06           N  
ATOM    629  CA  ILE A  85     -13.721  25.479  16.973  1.00 15.13           C  
ATOM    630  C   ILE A  85     -13.924  26.363  18.198  1.00 15.11           C  
ATOM    631  O   ILE A  85     -14.645  25.999  19.140  1.00 15.55           O  
ATOM    632  CB  ILE A  85     -12.526  24.527  17.083  1.00 14.54           C  
ATOM    633  CG1 ILE A  85     -12.683  23.537  18.250  1.00 14.76           C  
ATOM    634  CG2 ILE A  85     -11.219  25.298  17.257  1.00 14.04           C  
ATOM    635  CD1 ILE A  85     -13.961  22.727  18.213  1.00 15.26           C  
ATOM    636  N   SER A  86     -13.393  27.578  18.198  1.00 15.17           N  
ATOM    637  CA  SER A  86     -13.643  28.515  19.300  1.00 17.04           C  
ATOM    638  C   SER A  86     -15.128  28.856  19.365  1.00 17.57           C  
ATOM    639  O   SER A  86     -15.760  28.839  20.432  1.00 18.63           O  
ATOM    640  CB  SER A  86     -12.807  29.786  19.094  1.00 18.30           C  
ATOM    641  OG  SER A  86     -13.321  30.855  19.865  1.00 19.33           O  
ATOM    642  N   ALA A  87     -15.731  29.142  18.207  1.00 17.28           N  
ATOM    643  CA  ALA A  87     -17.144  29.491  18.127  1.00 18.36           C  
ATOM    644  C   ALA A  87     -18.044  28.317  18.487  1.00 18.69           C  
ATOM    645  O   ALA A  87     -19.042  28.484  19.186  1.00 18.41           O  
ATOM    646  CB  ALA A  87     -17.534  29.995  16.739  1.00 16.85           C  
ATOM    647  N   GLN A  88     -17.700  27.122  18.008  1.00 20.21           N  
ATOM    648  CA  GLN A  88     -18.513  25.942  18.293  1.00 22.13           C  
ATOM    649  C   GLN A  88     -18.441  25.575  19.771  1.00 22.13           C  
ATOM    650  O   GLN A  88     -19.436  25.103  20.330  1.00 22.13           O  
ATOM    651  CB  GLN A  88     -18.083  24.758  17.425  1.00 24.73           C  
ATOM    652  CG  GLN A  88     -19.104  23.641  17.345  1.00 28.10           C  
ATOM    653  CD  GLN A  88     -19.930  23.588  16.080  1.00 30.11           C  
ATOM    654  OE1 GLN A  88     -20.253  22.502  15.579  1.00 31.62           O  
ATOM    655  NE2 GLN A  88     -20.332  24.730  15.529  1.00 31.49           N  
ATOM    656  N   GLU A  89     -17.280  25.788  20.392  1.00 20.17           N  
ATOM    657  CA  GLU A  89     -17.144  25.451  21.806  1.00 20.74           C  
ATOM    658  C   GLU A  89     -17.517  26.569  22.754  1.00 19.61           C  
ATOM    659  O   GLU A  89     -17.539  26.331  23.964  1.00 18.50           O  
ATOM    660  CB  GLU A  89     -15.705  24.956  22.056  1.00 22.09           C  
ATOM    661  CG  GLU A  89     -15.577  23.608  21.354  1.00 23.99           C  
ATOM    662  CD  GLU A  89     -14.341  22.815  21.683  1.00 25.33           C  
ATOM    663  OE1 GLU A  89     -13.353  23.404  22.146  1.00 25.01           O  
ATOM    664  OE2 GLU A  89     -14.398  21.580  21.437  1.00 26.44           O  
ATOM    665  N   GLY A  90     -17.784  27.766  22.250  1.00 18.22           N  
ATOM    666  CA  GLY A  90     -18.132  28.904  23.074  1.00 19.24           C  
ATOM    667  C   GLY A  90     -16.946  29.332  23.937  1.00 19.40           C  
ATOM    668  O   GLY A  90     -17.127  29.715  25.086  1.00 19.20           O  
ATOM    669  N   ARG A  91     -15.743  29.318  23.379  1.00 17.79           N  
ATOM    670  CA  ARG A  91     -14.534  29.720  24.084  1.00 17.19           C  
ATOM    671  C   ARG A  91     -13.807  30.765  23.239  1.00 16.67           C  
ATOM    672  O   ARG A  91     -12.952  30.407  22.437  1.00 15.49           O  
ATOM    673  CB  ARG A  91     -13.601  28.529  24.336  1.00 17.96           C  
ATOM    674  CG  ARG A  91     -12.466  28.831  25.302  1.00 20.34           C  
ATOM    675  CD  ARG A  91     -11.482  27.698  25.513  1.00 20.09           C  
ATOM    676  NE  ARG A  91     -12.049  26.515  26.152  1.00 21.16           N  
ATOM    677  CZ  ARG A  91     -12.342  26.476  27.459  1.00 21.54           C  
ATOM    678  NH1 ARG A  91     -12.115  27.505  28.273  1.00 20.97           N  
ATOM    679  NH2 ARG A  91     -12.855  25.378  27.989  1.00 20.90           N  
ATOM    680  N   PRO A  92     -14.182  32.023  23.413  1.00 16.34           N  
ATOM    681  CA  PRO A  92     -13.602  33.115  22.664  1.00 15.95           C  
ATOM    682  C   PRO A  92     -12.097  33.230  22.853  1.00 15.41           C  
ATOM    683  O   PRO A  92     -11.565  32.983  23.937  1.00 14.58           O  
ATOM    684  CB  PRO A  92     -14.321  34.364  23.127  1.00 16.62           C  
ATOM    685  CG  PRO A  92     -15.223  33.974  24.238  1.00 16.79           C  
ATOM    686  CD  PRO A  92     -15.227  32.481  24.356  1.00 17.21           C  
ATOM    687  N   ILE A  93     -11.427  33.558  21.754  1.00 15.69           N  
ATOM    688  CA  ILE A  93      -9.991  33.819  21.776  1.00 15.64           C  
ATOM    689  C   ILE A  93      -9.794  35.322  21.938  1.00 16.85           C  
ATOM    690  O   ILE A  93     -10.272  36.093  21.103  1.00 17.56           O  
ATOM    691  CB  ILE A  93      -9.271  33.271  20.527  1.00 14.28           C  
ATOM    692  CG1 ILE A  93      -9.399  31.748  20.532  1.00 12.97           C  
ATOM    693  CG2 ILE A  93      -7.814  33.723  20.500  1.00 14.18           C  
ATOM    694  CD1 ILE A  93      -9.024  31.052  19.233  1.00 12.95           C  
ATOM    695  N   GLU A  94      -9.183  35.741  23.047  1.00 16.46           N  
ATOM    696  CA  GLU A  94      -9.011  37.159  23.314  1.00 18.34           C  
ATOM    697  C   GLU A  94      -7.591  37.669  23.118  1.00 17.00           C  
ATOM    698  O   GLU A  94      -6.660  37.141  23.724  1.00 15.43           O  
ATOM    699  CB  GLU A  94      -9.393  37.470  24.770  1.00 21.26           C  
ATOM    700  CG  GLU A  94     -10.557  38.396  24.970  1.00 25.55           C  
ATOM    701  CD  GLU A  94     -10.397  39.825  24.516  1.00 25.91           C  
ATOM    702  OE1 GLU A  94      -9.302  40.385  24.298  1.00 27.16           O  
ATOM    703  OE2 GLU A  94     -11.473  40.441  24.337  1.00 27.69           O  
ATOM    704  N   SER A  95      -7.451  38.758  22.356  1.00 15.95           N  
ATOM    705  CA  SER A  95      -6.153  39.392  22.169  1.00 14.95           C  
ATOM    706  C   SER A  95      -5.467  39.707  23.490  1.00 14.65           C  
ATOM    707  O   SER A  95      -4.282  39.428  23.702  1.00 14.15           O  
ATOM    708  CB  SER A  95      -6.303  40.712  21.402  1.00 13.31           C  
ATOM    709  OG  SER A  95      -5.039  41.280  21.131  1.00 12.79           O  
ATOM    710  N   LEU A  96      -6.213  40.304  24.413  1.00 14.55           N  
ATOM    711  CA  LEU A  96      -5.697  40.644  25.735  1.00 15.74           C  
ATOM    712  C   LEU A  96      -5.102  39.430  26.444  1.00 14.25           C  
ATOM    713  O   LEU A  96      -4.052  39.551  27.073  1.00 14.29           O  
ATOM    714  CB  LEU A  96      -6.845  41.196  26.588  1.00 18.15           C  
ATOM    715  CG  LEU A  96      -7.021  42.691  26.802  1.00 20.73           C  
ATOM    716  CD1 LEU A  96      -6.167  43.572  25.915  1.00 21.13           C  
ATOM    717  CD2 LEU A  96      -8.497  43.077  26.706  1.00 20.51           C  
ATOM    718  N   VAL A  97      -5.765  38.272  26.360  1.00 12.66           N  
ATOM    719  CA  VAL A  97      -5.266  37.066  27.022  1.00 12.49           C  
ATOM    720  C   VAL A  97      -3.990  36.576  26.344  1.00 11.57           C  
ATOM    721  O   VAL A  97      -3.032  36.199  27.027  1.00 10.76           O  
ATOM    722  CB  VAL A  97      -6.321  35.948  27.102  1.00 13.22           C  
ATOM    723  CG1 VAL A  97      -5.744  34.608  27.544  1.00 13.19           C  
ATOM    724  CG2 VAL A  97      -7.415  36.352  28.094  1.00 14.79           C  
ATOM    725  N   MET A  98      -3.950  36.642  25.008  1.00 11.19           N  
ATOM    726  CA  MET A  98      -2.750  36.205  24.284  1.00 11.54           C  
ATOM    727  C   MET A  98      -1.567  37.102  24.625  1.00 11.87           C  
ATOM    728  O   MET A  98      -0.466  36.632  24.938  1.00 12.67           O  
ATOM    729  CB  MET A  98      -2.989  36.188  22.769  1.00 12.37           C  
ATOM    730  CG  MET A  98      -4.197  35.332  22.370  1.00 11.60           C  
ATOM    731  SD  MET A  98      -4.609  35.567  20.623  1.00 12.08           S  
ATOM    732  CE  MET A  98      -3.106  35.109  19.778  1.00 12.67           C  
ATOM    733  N   SER A  99      -1.831  38.414  24.714  1.00 12.36           N  
ATOM    734  CA  SER A  99      -0.795  39.379  25.056  1.00 12.61           C  
ATOM    735  C   SER A  99      -0.324  39.237  26.494  1.00 13.03           C  
ATOM    736  O   SER A  99       0.877  39.287  26.752  1.00 12.30           O  
ATOM    737  CB  SER A  99      -1.299  40.804  24.797  1.00 13.88           C  
ATOM    738  OG  SER A  99      -1.399  41.046  23.401  1.00 13.11           O  
ATOM    739  N   ALA A 100      -1.259  38.997  27.421  1.00 12.96           N  
ATOM    740  CA  ALA A 100      -0.893  38.799  28.822  1.00 13.15           C  
ATOM    741  C   ALA A 100       0.037  37.599  28.971  1.00 13.26           C  
ATOM    742  O   ALA A 100       1.046  37.658  29.688  1.00 13.33           O  
ATOM    743  CB  ALA A 100      -2.134  38.589  29.681  1.00 13.37           C  
ATOM    744  N   GLY A 101      -0.244  36.512  28.237  1.00 12.10           N  
ATOM    745  CA  GLY A 101       0.608  35.325  28.312  1.00 12.66           C  
ATOM    746  C   GLY A 101       2.027  35.591  27.840  1.00 12.54           C  
ATOM    747  O   GLY A 101       2.996  35.025  28.373  1.00 11.65           O  
ATOM    748  N   LEU A 102       2.163  36.414  26.793  1.00 12.60           N  
ATOM    749  CA  LEU A 102       3.466  36.783  26.273  1.00 13.43           C  
ATOM    750  C   LEU A 102       4.235  37.576  27.326  1.00 14.22           C  
ATOM    751  O   LEU A 102       5.426  37.350  27.559  1.00 15.04           O  
ATOM    752  CB  LEU A 102       3.351  37.600  24.984  1.00 13.29           C  
ATOM    753  CG  LEU A 102       4.660  38.097  24.364  1.00 14.12           C  
ATOM    754  CD1 LEU A 102       5.687  36.982  24.255  1.00 12.90           C  
ATOM    755  CD2 LEU A 102       4.391  38.697  22.983  1.00 14.49           C  
ATOM    756  N   ARG A 103       3.548  38.515  27.973  1.00 15.11           N  
ATOM    757  CA  ARG A 103       4.155  39.286  29.062  1.00 16.37           C  
ATOM    758  C   ARG A 103       4.602  38.381  30.201  1.00 15.27           C  
ATOM    759  O   ARG A 103       5.684  38.589  30.769  1.00 15.36           O  
ATOM    760  CB  ARG A 103       3.147  40.308  29.598  1.00 17.72           C  
ATOM    761  CG  ARG A 103       2.643  41.301  28.558  1.00 20.82           C  
ATOM    762  CD  ARG A 103       3.723  42.302  28.194  1.00 23.59           C  
ATOM    763  NE  ARG A 103       4.449  41.934  26.982  1.00 24.85           N  
ATOM    764  CZ  ARG A 103       3.983  41.948  25.740  1.00 25.17           C  
ATOM    765  NH1 ARG A 103       2.731  42.298  25.471  1.00 24.99           N  
ATOM    766  NH2 ARG A 103       4.788  41.589  24.749  1.00 24.80           N  
ATOM    767  N   ALA A 104       3.793  37.386  30.566  1.00 14.92           N  
ATOM    768  CA  ALA A 104       4.104  36.475  31.658  1.00 14.47           C  
ATOM    769  C   ALA A 104       5.388  35.702  31.381  1.00 15.55           C  
ATOM    770  O   ALA A 104       6.224  35.506  32.259  1.00 14.83           O  
ATOM    771  CB  ALA A 104       2.964  35.495  31.917  1.00 14.33           C  
ATOM    772  N   LEU A 105       5.579  35.249  30.140  1.00 15.60           N  
ATOM    773  CA  LEU A 105       6.796  34.566  29.743  1.00 17.19           C  
ATOM    774  C   LEU A 105       8.007  35.491  29.806  1.00 18.59           C  
ATOM    775  O   LEU A 105       9.083  35.072  30.241  1.00 20.03           O  
ATOM    776  CB  LEU A 105       6.692  34.007  28.317  1.00 15.34           C  
ATOM    777  CG  LEU A 105       5.899  32.695  28.247  1.00 15.31           C  
ATOM    778  CD1 LEU A 105       5.918  32.164  26.816  1.00 14.29           C  
ATOM    779  CD2 LEU A 105       6.469  31.664  29.214  1.00 15.09           C  
ATOM    780  N   GLU A 106       7.809  36.760  29.462  1.00 19.85           N  
ATOM    781  CA  GLU A 106       8.876  37.749  29.550  1.00 21.82           C  
ATOM    782  C   GLU A 106       9.306  38.006  30.993  1.00 22.50           C  
ATOM    783  O   GLU A 106      10.431  38.472  31.193  1.00 22.21           O  
ATOM    784  CB  GLU A 106       8.505  39.052  28.847  1.00 23.22           C  
ATOM    785  CG  GLU A 106       8.399  38.991  27.332  1.00 24.52           C  
ATOM    786  CD  GLU A 106       7.654  40.140  26.697  1.00 25.03           C  
ATOM    787  OE1 GLU A 106       7.069  41.000  27.378  1.00 25.27           O  
ATOM    788  OE2 GLU A 106       7.592  40.220  25.449  1.00 26.87           O  
ATOM    789  N   GLN A 107       8.531  37.628  32.000  1.00 22.22           N  
ATOM    790  CA  GLN A 107       8.911  37.711  33.396  1.00 24.23           C  
ATOM    791  C   GLN A 107      10.167  36.879  33.683  1.00 24.60           C  
ATOM    792  O   GLN A 107      10.983  37.254  34.534  1.00 24.36           O  
ATOM    793  CB  GLN A 107       7.814  37.139  34.304  1.00 24.69           C  
ATOM    794  CG  GLN A 107       6.540  37.925  34.454  1.00 25.29           C  
ATOM    795  CD  GLN A 107       5.538  37.237  35.372  1.00 26.21           C  
ATOM    796  OE1 GLN A 107       5.912  36.505  36.293  1.00 26.82           O  
ATOM    797  NE2 GLN A 107       4.252  37.468  35.136  1.00 25.94           N  
ATOM    798  N   GLN A 108      10.289  35.712  33.042  1.00 24.90           N  
ATOM    799  CA  GLN A 108      11.451  34.872  33.280  1.00 25.06           C  
ATOM    800  C   GLN A 108      12.346  34.634  32.076  1.00 23.91           C  
ATOM    801  O   GLN A 108      13.521  34.310  32.299  1.00 24.59           O  
ATOM    802  CB  GLN A 108      11.028  33.539  33.901  1.00 28.12           C  
ATOM    803  CG  GLN A 108      10.076  32.705  33.077  1.00 30.71           C  
ATOM    804  CD  GLN A 108       8.748  32.461  33.764  1.00 32.33           C  
ATOM    805  OE1 GLN A 108       8.001  33.419  33.993  1.00 34.04           O  
ATOM    806  NE2 GLN A 108       8.454  31.203  34.081  1.00 32.12           N  
ATOM    807  N   ALA A 109      11.875  34.783  30.848  1.00 21.13           N  
ATOM    808  CA  ALA A 109      12.735  34.540  29.689  1.00 19.52           C  
ATOM    809  C   ALA A 109      13.236  35.830  29.063  1.00 17.96           C  
ATOM    810  O   ALA A 109      12.541  36.850  29.089  1.00 17.46           O  
ATOM    811  CB  ALA A 109      11.977  33.701  28.657  1.00 18.72           C  
ATOM    812  N   ASP A 110      14.447  35.808  28.506  1.00 16.79           N  
ATOM    813  CA  ASP A 110      14.975  36.998  27.848  1.00 16.48           C  
ATOM    814  C   ASP A 110      15.015  36.810  26.329  1.00 15.17           C  
ATOM    815  O   ASP A 110      15.475  37.674  25.591  1.00 14.93           O  
ATOM    816  CB  ASP A 110      16.322  37.430  28.407  1.00 18.20           C  
ATOM    817  CG  ASP A 110      17.436  36.414  28.291  1.00 19.46           C  
ATOM    818  OD1 ASP A 110      17.222  35.334  27.717  1.00 18.86           O  
ATOM    819  OD2 ASP A 110      18.557  36.688  28.794  1.00 19.77           O  
ATOM    820  N   TRP A 111      14.454  35.700  25.865  1.00 15.12           N  
ATOM    821  CA  TRP A 111      14.408  35.387  24.425  1.00 14.32           C  
ATOM    822  C   TRP A 111      13.150  34.540  24.228  1.00 13.42           C  
ATOM    823  O   TRP A 111      13.005  33.480  24.829  1.00 13.80           O  
ATOM    824  CB  TRP A 111      15.653  34.638  23.998  1.00 14.03           C  
ATOM    825  CG  TRP A 111      15.951  34.639  22.528  1.00 13.47           C  
ATOM    826  CD1 TRP A 111      16.786  35.489  21.866  1.00 13.05           C  
ATOM    827  CD2 TRP A 111      15.406  33.749  21.544  1.00 13.27           C  
ATOM    828  NE1 TRP A 111      16.801  35.186  20.518  1.00 13.51           N  
ATOM    829  CE2 TRP A 111      15.956  34.129  20.301  1.00 13.62           C  
ATOM    830  CE3 TRP A 111      14.507  32.682  21.587  1.00 13.40           C  
ATOM    831  CZ2 TRP A 111      15.633  33.469  19.114  1.00 13.46           C  
ATOM    832  CZ3 TRP A 111      14.190  32.016  20.411  1.00 13.69           C  
ATOM    833  CH2 TRP A 111      14.764  32.419  19.196  1.00 14.02           C  
ATOM    834  N   VAL A 112      12.150  35.117  23.563  1.00 12.34           N  
ATOM    835  CA  VAL A 112      10.854  34.446  23.479  1.00 11.35           C  
ATOM    836  C   VAL A 112      10.493  34.246  22.007  1.00 11.27           C  
ATOM    837  O   VAL A 112      10.508  35.204  21.250  1.00 12.62           O  
ATOM    838  CB  VAL A 112       9.727  35.235  24.174  1.00 11.18           C  
ATOM    839  CG1 VAL A 112       8.370  34.535  24.021  1.00  8.66           C  
ATOM    840  CG2 VAL A 112       9.996  35.424  25.669  1.00 11.80           C  
ATOM    841  N   LEU A 113      10.130  33.012  21.694  1.00 12.37           N  
ATOM    842  CA  LEU A 113       9.713  32.680  20.333  1.00 12.40           C  
ATOM    843  C   LEU A 113       8.237  32.313  20.410  1.00 11.64           C  
ATOM    844  O   LEU A 113       7.842  31.483  21.215  1.00 12.45           O  
ATOM    845  CB  LEU A 113      10.536  31.517  19.798  1.00 13.41           C  
ATOM    846  CG  LEU A 113      10.195  30.972  18.403  1.00 14.43           C  
ATOM    847  CD1 LEU A 113      11.420  30.280  17.841  1.00 14.88           C  
ATOM    848  CD2 LEU A 113       8.998  30.026  18.476  1.00 13.95           C  
ATOM    849  N   VAL A 114       7.450  32.927  19.549  1.00 11.80           N  
ATOM    850  CA  VAL A 114       6.014  32.745  19.505  1.00 11.25           C  
ATOM    851  C   VAL A 114       5.668  32.031  18.191  1.00 11.39           C  
ATOM    852  O   VAL A 114       6.049  32.555  17.154  1.00 12.33           O  
ATOM    853  CB  VAL A 114       5.285  34.098  19.542  1.00 11.10           C  
ATOM    854  CG1 VAL A 114       3.774  33.902  19.567  1.00 10.70           C  
ATOM    855  CG2 VAL A 114       5.734  34.936  20.742  1.00  9.57           C  
ATOM    856  N   GLU A 115       5.079  30.856  18.288  1.00 12.06           N  
ATOM    857  CA  GLU A 115       4.696  30.147  17.068  1.00 13.55           C  
ATOM    858  C   GLU A 115       3.239  30.467  16.732  1.00 12.85           C  
ATOM    859  O   GLU A 115       2.378  30.412  17.612  1.00 12.45           O  
ATOM    860  CB  GLU A 115       4.872  28.630  17.176  1.00 13.42           C  
ATOM    861  CG  GLU A 115       4.605  27.957  15.832  1.00 14.87           C  
ATOM    862  CD  GLU A 115       4.600  26.452  15.818  1.00 16.30           C  
ATOM    863  OE1 GLU A 115       5.215  25.834  16.719  1.00 16.97           O  
ATOM    864  OE2 GLU A 115       4.014  25.866  14.863  1.00 14.71           O  
ATOM    865  N   GLY A 116       2.995  30.760  15.461  1.00 11.89           N  
ATOM    866  CA  GLY A 116       1.600  31.027  15.062  1.00 12.36           C  
ATOM    867  C   GLY A 116       0.923  29.678  14.820  1.00 11.91           C  
ATOM    868  O   GLY A 116       1.391  28.653  15.303  1.00 12.69           O  
ATOM    869  N   ALA A 117      -0.229  29.735  14.179  1.00 11.90           N  
ATOM    870  CA  ALA A 117      -0.998  28.524  13.869  1.00 12.81           C  
ATOM    871  C   ALA A 117      -1.384  28.651  12.398  1.00 12.43           C  
ATOM    872  O   ALA A 117      -1.745  29.747  11.965  1.00 12.18           O  
ATOM    873  CB  ALA A 117      -2.203  28.408  14.776  1.00 12.88           C  
ATOM    874  N   GLY A 118      -1.146  27.593  11.623  1.00 13.76           N  
ATOM    875  CA  GLY A 118      -1.463  27.710  10.191  1.00 13.28           C  
ATOM    876  C   GLY A 118      -0.504  28.720   9.564  1.00 13.14           C  
ATOM    877  O   GLY A 118       0.668  28.850   9.939  1.00 13.76           O  
ATOM    878  N   GLY A 119      -1.033  29.447   8.590  1.00 12.98           N  
ATOM    879  CA  GLY A 119      -0.267  30.472   7.891  1.00 10.58           C  
ATOM    880  C   GLY A 119      -0.554  31.849   8.494  1.00 11.12           C  
ATOM    881  O   GLY A 119      -1.214  31.977   9.527  1.00 11.62           O  
ATOM    882  N   TRP A 120      -0.085  32.895   7.829  1.00  9.48           N  
ATOM    883  CA  TRP A 120      -0.189  34.263   8.283  1.00  9.50           C  
ATOM    884  C   TRP A 120      -1.572  34.708   8.703  1.00  8.97           C  
ATOM    885  O   TRP A 120      -1.756  35.316   9.773  1.00  8.98           O  
ATOM    886  CB  TRP A 120       0.364  35.224   7.199  1.00  9.42           C  
ATOM    887  CG  TRP A 120       0.421  36.650   7.640  1.00 10.57           C  
ATOM    888  CD1 TRP A 120      -0.291  37.688   7.126  1.00 11.33           C  
ATOM    889  CD2 TRP A 120       1.212  37.190   8.705  1.00 10.46           C  
ATOM    890  NE1 TRP A 120       0.001  38.844   7.810  1.00 11.46           N  
ATOM    891  CE2 TRP A 120       0.931  38.568   8.775  1.00 11.89           C  
ATOM    892  CE3 TRP A 120       2.128  36.632   9.604  1.00 10.79           C  
ATOM    893  CZ2 TRP A 120       1.524  39.422   9.707  1.00 10.93           C  
ATOM    894  CZ3 TRP A 120       2.730  37.492  10.512  1.00 10.45           C  
ATOM    895  CH2 TRP A 120       2.421  38.852  10.581  1.00 11.30           C  
ATOM    896  N   PHE A 121      -2.571  34.427   7.878  1.00  8.94           N  
ATOM    897  CA  PHE A 121      -3.889  35.008   8.131  1.00 10.86           C  
ATOM    898  C   PHE A 121      -4.878  34.123   8.840  1.00 11.82           C  
ATOM    899  O   PHE A 121      -6.102  34.367   8.808  1.00 13.36           O  
ATOM    900  CB  PHE A 121      -4.287  35.513   6.768  1.00 12.53           C  
ATOM    901  CG  PHE A 121      -4.008  36.872   6.263  1.00 13.57           C  
ATOM    902  CD1 PHE A 121      -4.168  38.004   7.032  1.00 13.70           C  
ATOM    903  CD2 PHE A 121      -3.576  36.994   4.939  1.00 14.26           C  
ATOM    904  CE1 PHE A 121      -3.902  39.261   6.500  1.00 14.73           C  
ATOM    905  CE2 PHE A 121      -3.303  38.244   4.416  1.00 13.94           C  
ATOM    906  CZ  PHE A 121      -3.468  39.372   5.198  1.00 14.25           C  
ATOM    907  N   THR A 122      -4.447  33.159   9.632  1.00 10.97           N  
ATOM    908  CA  THR A 122      -5.409  32.312  10.349  1.00 10.96           C  
ATOM    909  C   THR A 122      -6.367  33.079  11.228  1.00 10.82           C  
ATOM    910  O   THR A 122      -5.968  33.789  12.152  1.00 11.38           O  
ATOM    911  CB  THR A 122      -4.557  31.330  11.190  1.00 11.97           C  
ATOM    912  OG1 THR A 122      -3.712  30.634  10.265  1.00 12.77           O  
ATOM    913  CG2 THR A 122      -5.439  30.346  11.923  1.00 11.14           C  
ATOM    914  N   PRO A 123      -7.674  32.926  11.006  1.00 11.34           N  
ATOM    915  CA  PRO A 123      -8.686  33.617  11.776  1.00 10.71           C  
ATOM    916  C   PRO A 123      -8.789  33.053  13.192  1.00 11.18           C  
ATOM    917  O   PRO A 123      -8.716  31.836  13.390  1.00 10.55           O  
ATOM    918  CB  PRO A 123      -9.994  33.386  11.026  1.00 12.09           C  
ATOM    919  CG  PRO A 123      -9.540  33.012   9.647  1.00 11.51           C  
ATOM    920  CD  PRO A 123      -8.278  32.187   9.872  1.00 11.19           C  
ATOM    921  N   LEU A 124      -8.948  33.964  14.138  1.00 10.44           N  
ATOM    922  CA  LEU A 124      -9.111  33.671  15.559  1.00  9.80           C  
ATOM    923  C   LEU A 124     -10.552  33.867  16.002  1.00  9.98           C  
ATOM    924  O   LEU A 124     -11.100  33.264  16.940  1.00 10.06           O  
ATOM    925  CB  LEU A 124      -8.130  34.538  16.360  1.00  9.92           C  
ATOM    926  CG  LEU A 124      -6.644  34.233  16.181  1.00 11.24           C  
ATOM    927  CD1 LEU A 124      -5.773  35.026  17.152  1.00 11.81           C  
ATOM    928  CD2 LEU A 124      -6.327  32.751  16.342  1.00 11.36           C  
ATOM    929  N   SER A 125     -11.252  34.787  15.333  1.00  8.57           N  
ATOM    930  CA  SER A 125     -12.678  35.015  15.461  1.00 10.25           C  
ATOM    931  C   SER A 125     -13.176  35.376  14.055  1.00 11.17           C  
ATOM    932  O   SER A 125     -12.339  35.494  13.150  1.00  9.67           O  
ATOM    933  CB  SER A 125     -13.086  36.105  16.444  1.00 11.18           C  
ATOM    934  OG  SER A 125     -12.911  37.401  15.889  1.00 12.06           O  
ATOM    935  N   ASP A 126     -14.454  35.696  13.907  1.00 13.00           N  
ATOM    936  CA  ASP A 126     -14.975  36.142  12.620  1.00 13.98           C  
ATOM    937  C   ASP A 126     -14.522  37.542  12.229  1.00 12.75           C  
ATOM    938  O   ASP A 126     -14.737  37.992  11.090  1.00 12.35           O  
ATOM    939  CB  ASP A 126     -16.514  36.137  12.625  1.00 16.75           C  
ATOM    940  CG  ASP A 126     -17.074  34.740  12.485  1.00 21.01           C  
ATOM    941  OD1 ASP A 126     -16.266  33.809  12.258  1.00 22.46           O  
ATOM    942  OD2 ASP A 126     -18.313  34.585  12.599  1.00 22.89           O  
ATOM    943  N   THR A 127     -13.945  38.300  13.159  1.00 10.95           N  
ATOM    944  CA  THR A 127     -13.461  39.634  12.861  1.00 11.08           C  
ATOM    945  C   THR A 127     -12.008  39.852  13.227  1.00 12.21           C  
ATOM    946  O   THR A 127     -11.559  40.994  13.109  1.00 12.69           O  
ATOM    947  CB  THR A 127     -14.325  40.705  13.579  1.00 11.17           C  
ATOM    948  OG1 THR A 127     -14.221  40.541  15.003  1.00 10.81           O  
ATOM    949  CG2 THR A 127     -15.785  40.624  13.171  1.00 11.37           C  
ATOM    950  N   PHE A 128     -11.256  38.835  13.636  1.00 12.42           N  
ATOM    951  CA  PHE A 128      -9.881  39.067  14.114  1.00 14.03           C  
ATOM    952  C   PHE A 128      -8.991  37.903  13.703  1.00 13.61           C  
ATOM    953  O   PHE A 128      -9.344  36.751  13.954  1.00 12.80           O  
ATOM    954  CB  PHE A 128      -9.928  39.281  15.618  1.00 16.57           C  
ATOM    955  CG  PHE A 128      -8.692  39.197  16.462  1.00 18.84           C  
ATOM    956  CD1 PHE A 128      -7.684  40.131  16.353  1.00 19.99           C  
ATOM    957  CD2 PHE A 128      -8.568  38.192  17.413  1.00 20.40           C  
ATOM    958  CE1 PHE A 128      -6.551  40.059  17.160  1.00 21.07           C  
ATOM    959  CE2 PHE A 128      -7.440  38.098  18.209  1.00 21.77           C  
ATOM    960  CZ  PHE A 128      -6.434  39.038  18.072  1.00 20.57           C  
ATOM    961  N   THR A 129      -7.861  38.217  13.066  1.00 13.18           N  
ATOM    962  CA  THR A 129      -6.943  37.173  12.625  1.00 12.55           C  
ATOM    963  C   THR A 129      -5.665  37.161  13.468  1.00 11.55           C  
ATOM    964  O   THR A 129      -5.337  38.121  14.177  1.00 11.81           O  
ATOM    965  CB  THR A 129      -6.514  37.277  11.152  1.00 13.11           C  
ATOM    966  OG1 THR A 129      -5.688  38.438  10.972  1.00 14.61           O  
ATOM    967  CG2 THR A 129      -7.696  37.352  10.192  1.00 13.66           C  
ATOM    968  N   PHE A 130      -4.868  36.115  13.239  1.00 10.07           N  
ATOM    969  CA  PHE A 130      -3.589  36.011  13.966  1.00 10.91           C  
ATOM    970  C   PHE A 130      -2.710  37.172  13.525  1.00 10.96           C  
ATOM    971  O   PHE A 130      -2.073  37.797  14.355  1.00  9.60           O  
ATOM    972  CB  PHE A 130      -2.849  34.694  13.734  1.00 10.94           C  
ATOM    973  CG  PHE A 130      -2.235  34.064  14.955  1.00 12.10           C  
ATOM    974  CD1 PHE A 130      -1.409  34.767  15.803  1.00 11.66           C  
ATOM    975  CD2 PHE A 130      -2.463  32.723  15.226  1.00 13.46           C  
ATOM    976  CE1 PHE A 130      -0.853  34.157  16.911  1.00 12.77           C  
ATOM    977  CE2 PHE A 130      -1.920  32.097  16.331  1.00 14.35           C  
ATOM    978  CZ  PHE A 130      -1.129  32.839  17.200  1.00 12.77           C  
ATOM    979  N   ALA A 131      -2.738  37.488  12.213  1.00 11.70           N  
ATOM    980  CA  ALA A 131      -2.040  38.661  11.711  1.00 11.88           C  
ATOM    981  C   ALA A 131      -2.418  39.935  12.454  1.00 12.61           C  
ATOM    982  O   ALA A 131      -1.538  40.790  12.664  1.00 13.23           O  
ATOM    983  CB  ALA A 131      -2.325  38.850  10.217  1.00 11.48           C  
ATOM    984  N   ASP A 132      -3.672  40.126  12.871  1.00 12.02           N  
ATOM    985  CA  ASP A 132      -4.045  41.309  13.629  1.00 13.13           C  
ATOM    986  C   ASP A 132      -3.264  41.392  14.942  1.00 12.85           C  
ATOM    987  O   ASP A 132      -2.800  42.484  15.316  1.00 13.56           O  
ATOM    988  CB  ASP A 132      -5.546  41.350  13.952  1.00 14.10           C  
ATOM    989  CG  ASP A 132      -6.414  41.490  12.713  1.00 14.38           C  
ATOM    990  OD1 ASP A 132      -5.983  42.190  11.778  1.00 13.06           O  
ATOM    991  OD2 ASP A 132      -7.515  40.900  12.660  1.00 15.02           O  
ATOM    992  N   TRP A 133      -3.136  40.252  15.630  1.00 11.26           N  
ATOM    993  CA  TRP A 133      -2.466  40.245  16.933  1.00 11.49           C  
ATOM    994  C   TRP A 133      -0.972  40.493  16.793  1.00 11.56           C  
ATOM    995  O   TRP A 133      -0.403  41.245  17.573  1.00 11.20           O  
ATOM    996  CB  TRP A 133      -2.661  38.902  17.645  1.00 11.34           C  
ATOM    997  CG  TRP A 133      -2.010  38.836  18.991  1.00 11.48           C  
ATOM    998  CD1 TRP A 133      -2.467  39.394  20.138  1.00 11.15           C  
ATOM    999  CD2 TRP A 133      -0.807  38.131  19.334  1.00 11.53           C  
ATOM   1000  NE1 TRP A 133      -1.619  39.114  21.173  1.00 12.21           N  
ATOM   1001  CE2 TRP A 133      -0.583  38.337  20.711  1.00 12.23           C  
ATOM   1002  CE3 TRP A 133       0.108  37.365  18.607  1.00 11.94           C  
ATOM   1003  CZ2 TRP A 133       0.512  37.794  21.379  1.00 11.88           C  
ATOM   1004  CZ3 TRP A 133       1.200  36.837  19.268  1.00 11.41           C  
ATOM   1005  CH2 TRP A 133       1.390  37.041  20.649  1.00 12.02           C  
ATOM   1006  N   VAL A 134      -0.357  39.862  15.786  1.00 10.54           N  
ATOM   1007  CA  VAL A 134       1.078  40.068  15.562  1.00 11.54           C  
ATOM   1008  C   VAL A 134       1.362  41.541  15.282  1.00 12.03           C  
ATOM   1009  O   VAL A 134       2.307  42.156  15.794  1.00 12.29           O  
ATOM   1010  CB  VAL A 134       1.592  39.173  14.425  1.00 10.88           C  
ATOM   1011  CG1 VAL A 134       3.081  39.394  14.175  1.00 11.18           C  
ATOM   1012  CG2 VAL A 134       1.346  37.707  14.779  1.00 10.72           C  
ATOM   1013  N   THR A 135       0.484  42.154  14.494  1.00 12.80           N  
ATOM   1014  CA  THR A 135       0.562  43.580  14.180  1.00 13.79           C  
ATOM   1015  C   THR A 135       0.402  44.432  15.433  1.00 16.01           C  
ATOM   1016  O   THR A 135       1.170  45.382  15.611  1.00 14.94           O  
ATOM   1017  CB  THR A 135      -0.460  43.986  13.108  1.00 13.61           C  
ATOM   1018  OG1 THR A 135      -0.241  43.200  11.917  1.00 13.07           O  
ATOM   1019  CG2 THR A 135      -0.315  45.459  12.747  1.00 14.62           C  
ATOM   1020  N   GLN A 136      -0.536  44.100  16.324  1.00 18.08           N  
ATOM   1021  CA  GLN A 136      -0.700  44.858  17.562  1.00 19.33           C  
ATOM   1022  C   GLN A 136       0.541  44.814  18.439  1.00 19.11           C  
ATOM   1023  O   GLN A 136       0.988  45.826  18.986  1.00 18.43           O  
ATOM   1024  CB  GLN A 136      -1.862  44.311  18.400  1.00 22.89           C  
ATOM   1025  CG  GLN A 136      -3.210  44.841  17.924  1.00 26.61           C  
ATOM   1026  CD  GLN A 136      -4.342  44.257  18.752  1.00 29.01           C  
ATOM   1027  OE1 GLN A 136      -4.375  44.454  19.976  1.00 30.30           O  
ATOM   1028  NE2 GLN A 136      -5.226  43.543  18.073  1.00 30.07           N  
ATOM   1029  N   GLU A 137       1.117  43.617  18.562  1.00 17.97           N  
ATOM   1030  CA  GLU A 137       2.315  43.381  19.341  1.00 17.75           C  
ATOM   1031  C   GLU A 137       3.583  43.866  18.648  1.00 17.24           C  
ATOM   1032  O   GLU A 137       4.638  43.921  19.286  1.00 17.96           O  
ATOM   1033  CB  GLU A 137       2.457  41.881  19.642  1.00 18.04           C  
ATOM   1034  CG  GLU A 137       1.428  41.374  20.644  1.00 19.94           C  
ATOM   1035  CD  GLU A 137       1.678  41.914  22.039  1.00 21.47           C  
ATOM   1036  OE1 GLU A 137       2.827  42.243  22.374  1.00 22.44           O  
ATOM   1037  OE2 GLU A 137       0.719  42.019  22.822  1.00 23.07           O  
ATOM   1038  N   GLN A 138       3.529  44.173  17.363  1.00 15.46           N  
ATOM   1039  CA  GLN A 138       4.678  44.631  16.598  1.00 15.46           C  
ATOM   1040  C   GLN A 138       5.864  43.686  16.717  1.00 15.59           C  
ATOM   1041  O   GLN A 138       7.032  44.078  16.884  1.00 15.57           O  
ATOM   1042  CB  GLN A 138       5.077  46.054  17.039  1.00 17.25           C  
ATOM   1043  CG  GLN A 138       4.009  47.087  16.699  1.00 18.31           C  
ATOM   1044  CD  GLN A 138       4.051  47.489  15.240  1.00 19.46           C  
ATOM   1045  OE1 GLN A 138       5.026  48.074  14.756  1.00 20.20           O  
ATOM   1046  NE2 GLN A 138       2.968  47.180  14.537  1.00 20.17           N  
ATOM   1047  N   LEU A 139       5.569  42.387  16.623  1.00 13.51           N  
ATOM   1048  CA  LEU A 139       6.603  41.373  16.726  1.00 13.19           C  
ATOM   1049  C   LEU A 139       7.345  41.252  15.401  1.00 12.42           C  
ATOM   1050  O   LEU A 139       6.701  41.192  14.364  1.00 11.46           O  
ATOM   1051  CB  LEU A 139       5.966  40.016  17.035  1.00 14.35           C  
ATOM   1052  CG  LEU A 139       5.356  39.777  18.405  1.00 15.47           C  
ATOM   1053  CD1 LEU A 139       4.514  38.506  18.445  1.00 16.02           C  
ATOM   1054  CD2 LEU A 139       6.464  39.691  19.450  1.00 16.81           C  
ATOM   1055  N   PRO A 140       8.666  41.188  15.445  1.00 13.71           N  
ATOM   1056  CA  PRO A 140       9.459  40.915  14.247  1.00 12.90           C  
ATOM   1057  C   PRO A 140       9.142  39.475  13.852  1.00 12.71           C  
ATOM   1058  O   PRO A 140       8.883  38.632  14.729  1.00 12.45           O  
ATOM   1059  CB  PRO A 140      10.893  41.083  14.676  1.00 14.65           C  
ATOM   1060  CG  PRO A 140      10.860  41.588  16.071  1.00 14.42           C  
ATOM   1061  CD  PRO A 140       9.512  41.241  16.654  1.00 13.62           C  
ATOM   1062  N   VAL A 141       9.069  39.215  12.552  1.00 11.06           N  
ATOM   1063  CA  VAL A 141       8.567  37.954  12.058  1.00  9.73           C  
ATOM   1064  C   VAL A 141       9.640  37.101  11.392  1.00  8.59           C  
ATOM   1065  O   VAL A 141      10.439  37.655  10.645  1.00  9.18           O  
ATOM   1066  CB  VAL A 141       7.431  38.191  11.021  1.00  9.69           C  
ATOM   1067  CG1 VAL A 141       6.939  36.866  10.440  1.00  9.68           C  
ATOM   1068  CG2 VAL A 141       6.272  38.943  11.657  1.00  9.41           C  
ATOM   1069  N   ILE A 142       9.610  35.810  11.689  1.00  7.83           N  
ATOM   1070  CA  ILE A 142      10.528  34.869  11.041  1.00  8.55           C  
ATOM   1071  C   ILE A 142       9.683  33.967  10.133  1.00  8.93           C  
ATOM   1072  O   ILE A 142       8.681  33.412  10.595  1.00  8.81           O  
ATOM   1073  CB  ILE A 142      11.347  34.005  12.006  1.00  9.25           C  
ATOM   1074  CG1 ILE A 142      12.313  34.883  12.820  1.00 10.71           C  
ATOM   1075  CG2 ILE A 142      12.151  32.951  11.241  1.00  9.48           C  
ATOM   1076  CD1 ILE A 142      13.020  34.067  13.913  1.00 10.08           C  
ATOM   1077  N   LEU A 143      10.015  33.874   8.854  1.00  9.93           N  
ATOM   1078  CA  LEU A 143       9.232  33.073   7.925  1.00 10.44           C  
ATOM   1079  C   LEU A 143       9.834  31.689   7.701  1.00  9.45           C  
ATOM   1080  O   LEU A 143      10.981  31.588   7.259  1.00 11.10           O  
ATOM   1081  CB  LEU A 143       9.153  33.791   6.567  1.00 10.84           C  
ATOM   1082  CG  LEU A 143       8.483  33.042   5.408  1.00 13.35           C  
ATOM   1083  CD1 LEU A 143       7.040  32.713   5.744  1.00 13.51           C  
ATOM   1084  CD2 LEU A 143       8.591  33.919   4.162  1.00 12.52           C  
ATOM   1085  N   VAL A 144       9.064  30.638   7.962  1.00  8.83           N  
ATOM   1086  CA  VAL A 144       9.568  29.287   7.706  1.00  8.07           C  
ATOM   1087  C   VAL A 144       9.041  28.870   6.331  1.00  8.83           C  
ATOM   1088  O   VAL A 144       7.830  28.903   6.096  1.00  9.68           O  
ATOM   1089  CB  VAL A 144       9.188  28.269   8.782  1.00  8.66           C  
ATOM   1090  CG1 VAL A 144       9.730  26.884   8.435  1.00  8.18           C  
ATOM   1091  CG2 VAL A 144       9.786  28.741  10.112  1.00  9.66           C  
ATOM   1092  N   VAL A 145       9.984  28.534   5.467  1.00  8.85           N  
ATOM   1093  CA  VAL A 145       9.660  28.139   4.102  1.00 10.27           C  
ATOM   1094  C   VAL A 145       9.959  26.660   3.910  1.00 11.72           C  
ATOM   1095  O   VAL A 145      11.108  26.222   3.929  1.00 11.21           O  
ATOM   1096  CB  VAL A 145      10.470  28.969   3.080  1.00 10.68           C  
ATOM   1097  CG1 VAL A 145      10.089  28.570   1.658  1.00 12.48           C  
ATOM   1098  CG2 VAL A 145      10.266  30.471   3.301  1.00 10.46           C  
ATOM   1099  N   GLY A 146       8.892  25.903   3.642  1.00 13.96           N  
ATOM   1100  CA  GLY A 146       9.048  24.466   3.380  1.00 16.52           C  
ATOM   1101  C   GLY A 146       9.542  24.406   1.929  1.00 17.93           C  
ATOM   1102  O   GLY A 146       8.838  24.908   1.037  1.00 19.43           O  
ATOM   1103  N   VAL A 147      10.726  23.861   1.725  1.00 18.15           N  
ATOM   1104  CA  VAL A 147      11.275  23.824   0.376  1.00 19.15           C  
ATOM   1105  C   VAL A 147      10.541  22.767  -0.447  1.00 20.71           C  
ATOM   1106  O   VAL A 147      10.767  21.564  -0.330  1.00 21.10           O  
ATOM   1107  CB  VAL A 147      12.799  23.672   0.387  1.00 19.43           C  
ATOM   1108  CG1 VAL A 147      13.366  23.671  -1.027  1.00 20.29           C  
ATOM   1109  CG2 VAL A 147      13.432  24.823   1.176  1.00 19.89           C  
ATOM   1110  N   LYS A 148       9.580  23.230  -1.243  1.00 20.40           N  
ATOM   1111  CA  LYS A 148       8.783  22.361  -2.100  1.00 21.10           C  
ATOM   1112  C   LYS A 148       8.142  23.176  -3.220  1.00 21.16           C  
ATOM   1113  O   LYS A 148       8.132  24.404  -3.146  1.00 20.30           O  
ATOM   1114  CB  LYS A 148       7.726  21.616  -1.287  1.00 21.89           C  
ATOM   1115  CG  LYS A 148       6.705  22.517  -0.606  1.00 22.64           C  
ATOM   1116  CD  LYS A 148       5.745  21.665   0.224  1.00 23.49           C  
ATOM   1117  CE  LYS A 148       4.796  22.541   1.028  1.00 23.76           C  
ATOM   1118  NZ  LYS A 148       3.640  21.744   1.551  1.00 22.53           N  
ATOM   1119  N   LEU A 149       7.709  22.505  -4.286  1.00 21.15           N  
ATOM   1120  CA  LEU A 149       7.030  23.223  -5.372  1.00 21.70           C  
ATOM   1121  C   LEU A 149       5.878  24.033  -4.794  1.00 19.86           C  
ATOM   1122  O   LEU A 149       5.106  23.505  -3.987  1.00 19.25           O  
ATOM   1123  CB  LEU A 149       6.510  22.217  -6.398  1.00 24.31           C  
ATOM   1124  CG  LEU A 149       6.585  22.620  -7.872  1.00 26.85           C  
ATOM   1125  CD1 LEU A 149       7.844  22.071  -8.525  1.00 26.97           C  
ATOM   1126  CD2 LEU A 149       5.335  22.139  -8.601  1.00 27.97           C  
ATOM   1127  N   GLY A 150       5.755  25.294  -5.185  1.00 17.05           N  
ATOM   1128  CA  GLY A 150       4.702  26.152  -4.671  1.00 15.44           C  
ATOM   1129  C   GLY A 150       5.180  27.051  -3.535  1.00 14.56           C  
ATOM   1130  O   GLY A 150       4.511  28.049  -3.243  1.00 13.38           O  
ATOM   1131  N   CYS A 151       6.370  26.795  -2.994  1.00 13.52           N  
ATOM   1132  CA  CYS A 151       6.862  27.617  -1.896  1.00 13.82           C  
ATOM   1133  C   CYS A 151       7.357  28.978  -2.333  1.00 12.15           C  
ATOM   1134  O   CYS A 151       7.338  29.897  -1.503  1.00 12.32           O  
ATOM   1135  CB  CYS A 151       7.940  26.850  -1.117  1.00 13.58           C  
ATOM   1136  SG  CYS A 151       9.566  26.861  -1.893  1.00 16.77           S  
ATOM   1137  N   ILE A 152       7.798  29.161  -3.582  1.00 11.21           N  
ATOM   1138  CA  ILE A 152       8.251  30.518  -3.960  1.00 11.00           C  
ATOM   1139  C   ILE A 152       7.053  31.461  -3.863  1.00 10.77           C  
ATOM   1140  O   ILE A 152       7.114  32.509  -3.225  1.00  9.93           O  
ATOM   1141  CB  ILE A 152       8.864  30.553  -5.363  1.00 11.26           C  
ATOM   1142  CG1 ILE A 152      10.179  29.760  -5.358  1.00 12.45           C  
ATOM   1143  CG2 ILE A 152       9.142  31.975  -5.829  1.00 10.50           C  
ATOM   1144  CD1 ILE A 152      10.578  29.323  -6.757  1.00 13.42           C  
ATOM   1145  N   ASN A 153       5.926  31.065  -4.474  1.00 10.81           N  
ATOM   1146  CA  ASN A 153       4.711  31.877  -4.464  1.00  9.72           C  
ATOM   1147  C   ASN A 153       4.253  32.146  -3.029  1.00  9.99           C  
ATOM   1148  O   ASN A 153       4.058  33.293  -2.639  1.00  8.68           O  
ATOM   1149  CB  ASN A 153       3.567  31.185  -5.230  1.00  9.83           C  
ATOM   1150  CG  ASN A 153       2.235  31.904  -5.128  1.00  7.90           C  
ATOM   1151  OD1 ASN A 153       2.094  33.107  -5.345  1.00  8.28           O  
ATOM   1152  ND2 ASN A 153       1.183  31.167  -4.759  1.00  9.26           N  
ATOM   1153  N   HIS A 154       4.143  31.089  -2.217  1.00 10.38           N  
ATOM   1154  CA  HIS A 154       3.681  31.317  -0.838  1.00 11.55           C  
ATOM   1155  C   HIS A 154       4.655  32.183  -0.055  1.00 11.56           C  
ATOM   1156  O   HIS A 154       4.234  33.034   0.733  1.00 11.06           O  
ATOM   1157  CB  HIS A 154       3.407  29.985  -0.131  1.00 11.85           C  
ATOM   1158  CG  HIS A 154       2.243  29.258  -0.746  1.00 13.20           C  
ATOM   1159  ND1 HIS A 154       2.139  27.886  -0.743  1.00 13.28           N  
ATOM   1160  CD2 HIS A 154       1.159  29.713  -1.411  1.00 14.00           C  
ATOM   1161  CE1 HIS A 154       1.018  27.531  -1.344  1.00 14.12           C  
ATOM   1162  NE2 HIS A 154       0.411  28.626  -1.778  1.00 13.99           N  
ATOM   1163  N   ALA A 155       5.950  31.996  -0.260  1.00 11.59           N  
ATOM   1164  CA  ALA A 155       6.933  32.812   0.459  1.00 11.35           C  
ATOM   1165  C   ALA A 155       6.803  34.265   0.026  1.00 11.65           C  
ATOM   1166  O   ALA A 155       6.760  35.164   0.868  1.00 11.19           O  
ATOM   1167  CB  ALA A 155       8.347  32.286   0.279  1.00 10.19           C  
ATOM   1168  N   MET A 156       6.662  34.520  -1.276  1.00 12.53           N  
ATOM   1169  CA  MET A 156       6.520  35.897  -1.751  1.00 14.12           C  
ATOM   1170  C   MET A 156       5.251  36.573  -1.257  1.00 12.77           C  
ATOM   1171  O   MET A 156       5.270  37.738  -0.886  1.00 10.87           O  
ATOM   1172  CB  MET A 156       6.571  35.936  -3.287  1.00 17.26           C  
ATOM   1173  CG  MET A 156       7.992  35.667  -3.763  1.00 22.40           C  
ATOM   1174  SD  MET A 156       8.219  35.652  -5.550  1.00 27.19           S  
ATOM   1175  CE  MET A 156       6.858  34.631  -6.107  1.00 27.29           C  
ATOM   1176  N   LEU A 157       4.135  35.847  -1.261  1.00 11.61           N  
ATOM   1177  CA  LEU A 157       2.858  36.363  -0.805  1.00 10.69           C  
ATOM   1178  C   LEU A 157       2.963  36.748   0.674  1.00  9.04           C  
ATOM   1179  O   LEU A 157       2.634  37.871   1.025  1.00  9.02           O  
ATOM   1180  CB  LEU A 157       1.754  35.308  -0.949  1.00 11.15           C  
ATOM   1181  CG  LEU A 157       1.264  34.979  -2.368  1.00 12.63           C  
ATOM   1182  CD1 LEU A 157       0.321  33.797  -2.311  1.00 13.35           C  
ATOM   1183  CD2 LEU A 157       0.602  36.204  -2.984  1.00 13.10           C  
ATOM   1184  N   THR A 158       3.513  35.822   1.467  1.00  9.38           N  
ATOM   1185  CA  THR A 158       3.583  36.073   2.914  1.00  9.57           C  
ATOM   1186  C   THR A 158       4.500  37.239   3.216  1.00  9.64           C  
ATOM   1187  O   THR A 158       4.186  38.158   3.998  1.00  9.38           O  
ATOM   1188  CB  THR A 158       3.986  34.779   3.650  1.00  9.72           C  
ATOM   1189  OG1 THR A 158       3.060  33.734   3.298  1.00  9.59           O  
ATOM   1190  CG2 THR A 158       3.925  34.973   5.162  1.00 10.14           C  
ATOM   1191  N   ALA A 159       5.683  37.253   2.602  1.00 10.99           N  
ATOM   1192  CA  ALA A 159       6.605  38.364   2.793  1.00 10.68           C  
ATOM   1193  C   ALA A 159       5.969  39.692   2.406  1.00 11.30           C  
ATOM   1194  O   ALA A 159       6.159  40.709   3.084  1.00 10.43           O  
ATOM   1195  CB  ALA A 159       7.914  38.136   2.070  1.00 10.92           C  
ATOM   1196  N   GLN A 160       5.273  39.770   1.263  1.00 11.88           N  
ATOM   1197  CA  GLN A 160       4.699  41.045   0.864  1.00 12.11           C  
ATOM   1198  C   GLN A 160       3.665  41.541   1.870  1.00 11.16           C  
ATOM   1199  O   GLN A 160       3.667  42.715   2.229  1.00 10.42           O  
ATOM   1200  CB  GLN A 160       4.084  41.012  -0.538  1.00 13.15           C  
ATOM   1201  CG  GLN A 160       3.627  42.401  -0.985  1.00 15.44           C  
ATOM   1202  CD  GLN A 160       3.123  42.420  -2.416  1.00 16.96           C  
ATOM   1203  OE1 GLN A 160       1.998  42.860  -2.666  1.00 18.92           O  
ATOM   1204  NE2 GLN A 160       3.980  41.968  -3.320  1.00 17.49           N  
ATOM   1205  N   VAL A 161       2.787  40.648   2.310  1.00 12.06           N  
ATOM   1206  CA  VAL A 161       1.728  41.056   3.250  1.00 13.01           C  
ATOM   1207  C   VAL A 161       2.316  41.478   4.586  1.00 12.93           C  
ATOM   1208  O   VAL A 161       1.854  42.441   5.198  1.00 14.48           O  
ATOM   1209  CB  VAL A 161       0.735  39.897   3.338  1.00 14.09           C  
ATOM   1210  CG1 VAL A 161      -0.194  39.995   4.528  1.00 16.08           C  
ATOM   1211  CG2 VAL A 161      -0.065  39.812   2.033  1.00 12.86           C  
ATOM   1212  N   ILE A 162       3.355  40.795   5.049  1.00 12.71           N  
ATOM   1213  CA  ILE A 162       4.020  41.162   6.296  1.00 12.95           C  
ATOM   1214  C   ILE A 162       4.582  42.572   6.198  1.00 14.19           C  
ATOM   1215  O   ILE A 162       4.376  43.389   7.097  1.00 14.68           O  
ATOM   1216  CB  ILE A 162       5.145  40.172   6.646  1.00 13.63           C  
ATOM   1217  CG1 ILE A 162       4.531  38.829   7.042  1.00 13.33           C  
ATOM   1218  CG2 ILE A 162       6.048  40.746   7.734  1.00 14.66           C  
ATOM   1219  CD1 ILE A 162       5.540  37.709   7.199  1.00 13.43           C  
ATOM   1220  N   GLN A 163       5.281  42.859   5.100  1.00 15.41           N  
ATOM   1221  CA  GLN A 163       5.875  44.179   4.917  1.00 18.13           C  
ATOM   1222  C   GLN A 163       4.827  45.271   4.797  1.00 19.09           C  
ATOM   1223  O   GLN A 163       4.961  46.362   5.366  1.00 18.00           O  
ATOM   1224  CB  GLN A 163       6.826  44.186   3.720  1.00 19.11           C  
ATOM   1225  CG  GLN A 163       8.090  43.385   4.018  1.00 21.41           C  
ATOM   1226  CD  GLN A 163       9.190  43.580   2.995  1.00 22.77           C  
ATOM   1227  OE1 GLN A 163      10.356  43.739   3.375  1.00 25.24           O  
ATOM   1228  NE2 GLN A 163       8.853  43.573   1.718  1.00 24.17           N  
ATOM   1229  N   HIS A 164       3.692  44.932   4.183  1.00 20.43           N  
ATOM   1230  CA  HIS A 164       2.609  45.904   4.019  1.00 21.70           C  
ATOM   1231  C   HIS A 164       1.892  46.222   5.312  1.00 20.97           C  
ATOM   1232  O   HIS A 164       1.334  47.319   5.465  1.00 20.53           O  
ATOM   1233  CB  HIS A 164       1.703  45.413   2.884  1.00 24.88           C  
ATOM   1234  CG  HIS A 164       2.362  45.595   1.542  1.00 27.24           C  
ATOM   1235  ND1 HIS A 164       1.658  45.620   0.359  1.00 28.59           N  
ATOM   1236  CD2 HIS A 164       3.665  45.776   1.194  1.00 28.60           C  
ATOM   1237  CE1 HIS A 164       2.483  45.803  -0.656  1.00 28.16           C  
ATOM   1238  NE2 HIS A 164       3.704  45.901  -0.179  1.00 29.02           N  
ATOM   1239  N   ALA A 165       1.978  45.354   6.320  1.00 19.16           N  
ATOM   1240  CA  ALA A 165       1.408  45.608   7.628  1.00 18.07           C  
ATOM   1241  C   ALA A 165       2.311  46.482   8.492  1.00 17.67           C  
ATOM   1242  O   ALA A 165       1.981  46.729   9.663  1.00 16.36           O  
ATOM   1243  CB  ALA A 165       1.179  44.275   8.342  1.00 17.94           C  
ATOM   1244  N   GLY A 166       3.464  46.883   7.982  1.00 16.61           N  
ATOM   1245  CA  GLY A 166       4.428  47.712   8.667  1.00 17.19           C  
ATOM   1246  C   GLY A 166       5.382  46.945   9.569  1.00 16.75           C  
ATOM   1247  O   GLY A 166       6.101  47.550  10.360  1.00 15.93           O  
ATOM   1248  N   LEU A 167       5.387  45.618   9.482  1.00 15.26           N  
ATOM   1249  CA  LEU A 167       6.174  44.759  10.338  1.00 14.87           C  
ATOM   1250  C   LEU A 167       7.541  44.426   9.760  1.00 15.58           C  
ATOM   1251  O   LEU A 167       7.758  44.465   8.548  1.00 16.35           O  
ATOM   1252  CB  LEU A 167       5.412  43.453  10.610  1.00 13.92           C  
ATOM   1253  CG  LEU A 167       4.094  43.522  11.386  1.00 13.66           C  
ATOM   1254  CD1 LEU A 167       3.453  42.138  11.460  1.00 12.92           C  
ATOM   1255  CD2 LEU A 167       4.280  44.062  12.797  1.00 14.19           C  
ATOM   1256  N   THR A 168       8.465  44.066  10.639  1.00 15.60           N  
ATOM   1257  CA  THR A 168       9.803  43.671  10.215  1.00 16.17           C  
ATOM   1258  C   THR A 168       9.843  42.170   9.947  1.00 14.87           C  
ATOM   1259  O   THR A 168       9.435  41.367  10.785  1.00 14.31           O  
ATOM   1260  CB  THR A 168      10.862  44.002  11.287  1.00 17.85           C  
ATOM   1261  OG1 THR A 168      10.850  45.420  11.517  1.00 20.59           O  
ATOM   1262  CG2 THR A 168      12.253  43.576  10.865  1.00 18.32           C  
ATOM   1263  N   LEU A 169      10.318  41.813   8.764  1.00 14.71           N  
ATOM   1264  CA  LEU A 169      10.545  40.416   8.409  1.00 13.15           C  
ATOM   1265  C   LEU A 169      12.015  40.193   8.798  1.00 13.23           C  
ATOM   1266  O   LEU A 169      12.914  40.589   8.051  1.00 11.67           O  
ATOM   1267  CB  LEU A 169      10.307  40.150   6.926  1.00 15.25           C  
ATOM   1268  CG  LEU A 169      10.470  38.690   6.466  1.00 15.48           C  
ATOM   1269  CD1 LEU A 169       9.393  37.827   7.106  1.00 15.85           C  
ATOM   1270  CD2 LEU A 169      10.380  38.615   4.944  1.00 16.26           C  
ATOM   1271  N   ALA A 170      12.225  39.677   9.996  1.00 11.10           N  
ATOM   1272  CA  ALA A 170      13.555  39.516  10.575  1.00 12.89           C  
ATOM   1273  C   ALA A 170      14.443  38.474   9.918  1.00 12.86           C  
ATOM   1274  O   ALA A 170      15.670  38.571   9.951  1.00 12.37           O  
ATOM   1275  CB  ALA A 170      13.416  39.162  12.051  1.00 13.02           C  
ATOM   1276  N   GLY A 171      13.836  37.459   9.314  1.00 12.51           N  
ATOM   1277  CA  GLY A 171      14.623  36.434   8.631  1.00 12.14           C  
ATOM   1278  C   GLY A 171      13.725  35.301   8.149  1.00 11.38           C  
ATOM   1279  O   GLY A 171      12.528  35.308   8.403  1.00 11.51           O  
ATOM   1280  N   TRP A 172      14.330  34.355   7.437  1.00 11.01           N  
ATOM   1281  CA  TRP A 172      13.609  33.177   6.974  1.00 10.89           C  
ATOM   1282  C   TRP A 172      14.477  31.940   7.216  1.00 10.10           C  
ATOM   1283  O   TRP A 172      15.701  32.005   7.358  1.00 10.44           O  
ATOM   1284  CB  TRP A 172      13.131  33.289   5.537  1.00 10.10           C  
ATOM   1285  CG  TRP A 172      14.126  33.232   4.431  1.00 10.26           C  
ATOM   1286  CD1 TRP A 172      14.949  34.255   4.040  1.00 10.77           C  
ATOM   1287  CD2 TRP A 172      14.422  32.130   3.565  1.00 10.61           C  
ATOM   1288  NE1 TRP A 172      15.731  33.851   2.980  1.00 11.20           N  
ATOM   1289  CE2 TRP A 172      15.433  32.550   2.679  1.00 10.49           C  
ATOM   1290  CE3 TRP A 172      13.914  30.823   3.468  1.00  9.38           C  
ATOM   1291  CZ2 TRP A 172      15.955  31.715   1.696  1.00 11.88           C  
ATOM   1292  CZ3 TRP A 172      14.444  29.990   2.498  1.00 10.72           C  
ATOM   1293  CH2 TRP A 172      15.443  30.444   1.625  1.00 10.87           C  
ATOM   1294  N   VAL A 173      13.788  30.816   7.389  1.00  8.71           N  
ATOM   1295  CA  VAL A 173      14.411  29.536   7.599  1.00  8.56           C  
ATOM   1296  C   VAL A 173      13.932  28.586   6.494  1.00  8.67           C  
ATOM   1297  O   VAL A 173      12.743  28.500   6.207  1.00 10.35           O  
ATOM   1298  CB  VAL A 173      14.096  28.907   8.965  1.00  8.87           C  
ATOM   1299  CG1 VAL A 173      14.764  27.545   9.069  1.00 10.04           C  
ATOM   1300  CG2 VAL A 173      14.538  29.836  10.102  1.00  9.29           C  
ATOM   1301  N   ALA A 174      14.911  27.968   5.853  1.00  9.58           N  
ATOM   1302  CA  ALA A 174      14.628  26.977   4.822  1.00  9.63           C  
ATOM   1303  C   ALA A 174      14.518  25.610   5.494  1.00 11.28           C  
ATOM   1304  O   ALA A 174      15.432  25.167   6.186  1.00 12.00           O  
ATOM   1305  CB  ALA A 174      15.752  26.992   3.795  1.00 10.57           C  
ATOM   1306  N   ASN A 175      13.373  24.966   5.332  1.00 10.31           N  
ATOM   1307  CA  ASN A 175      13.137  23.657   5.929  1.00  9.96           C  
ATOM   1308  C   ASN A 175      12.996  22.607   4.837  1.00 10.54           C  
ATOM   1309  O   ASN A 175      12.096  22.678   3.998  1.00 10.62           O  
ATOM   1310  CB  ASN A 175      11.891  23.710   6.807  1.00 10.12           C  
ATOM   1311  CG  ASN A 175      11.725  22.440   7.622  1.00 10.28           C  
ATOM   1312  OD1 ASN A 175      12.694  21.929   8.174  1.00 10.12           O  
ATOM   1313  ND2 ASN A 175      10.495  21.943   7.665  1.00 10.97           N  
ATOM   1314  N   ASP A 176      13.874  21.606   4.887  1.00 11.38           N  
ATOM   1315  CA  ASP A 176      13.798  20.507   3.923  1.00 12.07           C  
ATOM   1316  C   ASP A 176      12.773  19.480   4.377  1.00 13.44           C  
ATOM   1317  O   ASP A 176      13.096  18.479   5.011  1.00 14.21           O  
ATOM   1318  CB  ASP A 176      15.202  19.896   3.742  1.00 12.42           C  
ATOM   1319  CG  ASP A 176      16.194  20.948   3.265  1.00 13.59           C  
ATOM   1320  OD1 ASP A 176      15.779  22.032   2.829  1.00 14.87           O  
ATOM   1321  OD2 ASP A 176      17.422  20.742   3.299  1.00 15.09           O  
ATOM   1322  N   VAL A 177      11.509  19.666   4.012  1.00 15.09           N  
ATOM   1323  CA  VAL A 177      10.404  18.802   4.348  1.00 17.23           C  
ATOM   1324  C   VAL A 177      10.412  17.455   3.607  1.00 18.07           C  
ATOM   1325  O   VAL A 177       9.786  16.481   4.052  1.00 18.98           O  
ATOM   1326  CB  VAL A 177       9.014  19.450   4.117  1.00 18.34           C  
ATOM   1327  CG1 VAL A 177       8.603  20.383   5.257  1.00 19.19           C  
ATOM   1328  CG2 VAL A 177       8.950  20.284   2.837  1.00 18.19           C  
ATOM   1329  N   THR A 178      11.103  17.397   2.491  1.00 17.22           N  
ATOM   1330  CA  THR A 178      11.221  16.144   1.719  1.00 17.60           C  
ATOM   1331  C   THR A 178      12.669  15.864   1.388  1.00 15.91           C  
ATOM   1332  O   THR A 178      13.520  16.761   1.476  1.00 14.84           O  
ATOM   1333  CB  THR A 178      10.519  16.225   0.366  1.00 18.04           C  
ATOM   1334  OG1 THR A 178      11.151  17.207  -0.442  1.00 19.17           O  
ATOM   1335  CG2 THR A 178       9.041  16.576   0.464  1.00 19.81           C  
ATOM   1336  N   PRO A 179      13.008  14.632   1.007  1.00 16.22           N  
ATOM   1337  CA  PRO A 179      14.360  14.321   0.612  1.00 15.58           C  
ATOM   1338  C   PRO A 179      14.780  15.194  -0.545  1.00 16.60           C  
ATOM   1339  O   PRO A 179      13.887  15.770  -1.249  1.00 17.04           O  
ATOM   1340  CB  PRO A 179      14.319  12.851   0.284  1.00 16.53           C  
ATOM   1341  CG  PRO A 179      12.907  12.358   0.538  1.00 16.86           C  
ATOM   1342  CD  PRO A 179      12.061  13.519   0.963  1.00 16.62           C  
ATOM   1343  N   PRO A 180      16.095  15.324  -0.776  1.00 16.80           N  
ATOM   1344  CA  PRO A 180      16.624  16.174  -1.826  1.00 16.79           C  
ATOM   1345  C   PRO A 180      15.997  15.905  -3.183  1.00 15.78           C  
ATOM   1346  O   PRO A 180      15.961  14.752  -3.610  1.00 13.58           O  
ATOM   1347  CB  PRO A 180      18.118  15.965  -1.754  1.00 16.62           C  
ATOM   1348  CG  PRO A 180      18.402  15.043  -0.584  1.00 17.30           C  
ATOM   1349  CD  PRO A 180      17.102  14.629   0.029  1.00 16.88           C  
ATOM   1350  N   GLY A 181      15.598  16.954  -3.889  1.00 16.78           N  
ATOM   1351  CA  GLY A 181      15.069  16.810  -5.246  1.00 17.20           C  
ATOM   1352  C   GLY A 181      15.967  17.536  -6.242  1.00 17.25           C  
ATOM   1353  O   GLY A 181      16.869  18.282  -5.869  1.00 17.44           O  
ATOM   1354  N   LYS A 182      15.715  17.374  -7.526  1.00 18.86           N  
ATOM   1355  CA  LYS A 182      16.461  17.954  -8.611  1.00 19.74           C  
ATOM   1356  C   LYS A 182      16.728  19.449  -8.605  1.00 20.03           C  
ATOM   1357  O   LYS A 182      17.841  19.896  -8.934  1.00 21.48           O  
ATOM   1358  CB  LYS A 182      15.673  17.655  -9.923  1.00 21.04           C  
ATOM   1359  CG  LYS A 182      16.471  18.030 -11.148  1.00 22.26           C  
ATOM   1360  CD  LYS A 182      15.702  17.935 -12.453  1.00 22.11           C  
ATOM   1361  CE  LYS A 182      16.391  18.773 -13.522  1.00 22.80           C  
ATOM   1362  NZ  LYS A 182      16.560  18.050 -14.807  1.00 22.60           N  
ATOM   1363  N   ARG A 183      15.724  20.275  -8.310  1.00 18.48           N  
ATOM   1364  CA  ARG A 183      15.988  21.729  -8.380  1.00 16.95           C  
ATOM   1365  C   ARG A 183      16.208  22.384  -7.021  1.00 16.41           C  
ATOM   1366  O   ARG A 183      15.933  23.574  -6.838  1.00 14.06           O  
ATOM   1367  CB  ARG A 183      14.837  22.382  -9.136  1.00 17.01           C  
ATOM   1368  CG  ARG A 183      14.719  21.999 -10.606  1.00 18.40           C  
ATOM   1369  CD  ARG A 183      15.942  22.351 -11.425  1.00 18.95           C  
ATOM   1370  NE  ARG A 183      15.761  21.977 -12.836  1.00 19.71           N  
ATOM   1371  CZ  ARG A 183      16.665  22.220 -13.777  1.00 19.72           C  
ATOM   1372  NH1 ARG A 183      17.808  22.832 -13.497  1.00 19.88           N  
ATOM   1373  NH2 ARG A 183      16.406  21.841 -15.030  1.00 20.93           N  
ATOM   1374  N   HIS A 184      16.787  21.635  -6.082  1.00 16.20           N  
ATOM   1375  CA  HIS A 184      17.002  22.145  -4.732  1.00 16.67           C  
ATOM   1376  C   HIS A 184      17.830  23.416  -4.672  1.00 15.28           C  
ATOM   1377  O   HIS A 184      17.426  24.395  -4.037  1.00 15.04           O  
ATOM   1378  CB  HIS A 184      17.630  21.035  -3.859  1.00 17.94           C  
ATOM   1379  CG  HIS A 184      17.664  21.501  -2.431  1.00 18.88           C  
ATOM   1380  ND1 HIS A 184      18.823  21.986  -1.883  1.00 19.53           N  
ATOM   1381  CD2 HIS A 184      16.703  21.593  -1.489  1.00 19.58           C  
ATOM   1382  CE1 HIS A 184      18.567  22.343  -0.634  1.00 19.52           C  
ATOM   1383  NE2 HIS A 184      17.302  22.125  -0.365  1.00 19.95           N  
ATOM   1384  N   ALA A 185      18.997  23.440  -5.316  1.00 15.45           N  
ATOM   1385  CA  ALA A 185      19.882  24.588  -5.310  1.00 15.34           C  
ATOM   1386  C   ALA A 185      19.272  25.805  -6.000  1.00 14.52           C  
ATOM   1387  O   ALA A 185      19.372  26.919  -5.496  1.00 13.53           O  
ATOM   1388  CB  ALA A 185      21.213  24.233  -5.979  1.00 15.36           C  
ATOM   1389  N   GLU A 186      18.572  25.584  -7.118  1.00 14.05           N  
ATOM   1390  CA  GLU A 186      17.889  26.665  -7.815  1.00 14.16           C  
ATOM   1391  C   GLU A 186      16.752  27.241  -6.983  1.00 12.12           C  
ATOM   1392  O   GLU A 186      16.488  28.440  -7.055  1.00 10.55           O  
ATOM   1393  CB  GLU A 186      17.294  26.166  -9.142  1.00 15.56           C  
ATOM   1394  CG  GLU A 186      18.367  25.781 -10.146  1.00 17.61           C  
ATOM   1395  CD  GLU A 186      18.789  24.330 -10.111  1.00 19.53           C  
ATOM   1396  OE1 GLU A 186      18.734  23.623  -9.077  1.00 17.95           O  
ATOM   1397  OE2 GLU A 186      19.222  23.874 -11.206  1.00 20.63           O  
ATOM   1398  N   TYR A 187      16.040  26.399  -6.244  1.00 12.11           N  
ATOM   1399  CA  TYR A 187      14.960  26.905  -5.394  1.00 12.35           C  
ATOM   1400  C   TYR A 187      15.527  27.750  -4.262  1.00 11.31           C  
ATOM   1401  O   TYR A 187      15.056  28.854  -3.941  1.00  9.86           O  
ATOM   1402  CB  TYR A 187      14.138  25.728  -4.833  1.00 14.10           C  
ATOM   1403  CG  TYR A 187      12.807  25.679  -5.571  1.00 17.37           C  
ATOM   1404  CD1 TYR A 187      12.747  25.264  -6.890  1.00 17.44           C  
ATOM   1405  CD2 TYR A 187      11.635  26.091  -4.946  1.00 18.09           C  
ATOM   1406  CE1 TYR A 187      11.543  25.238  -7.567  1.00 18.64           C  
ATOM   1407  CE2 TYR A 187      10.428  26.073  -5.615  1.00 18.25           C  
ATOM   1408  CZ  TYR A 187      10.392  25.653  -6.935  1.00 19.11           C  
ATOM   1409  OH  TYR A 187       9.190  25.641  -7.606  1.00 19.58           O  
ATOM   1410  N   MET A 188      16.627  27.272  -3.680  1.00 11.96           N  
ATOM   1411  CA  MET A 188      17.286  28.017  -2.598  1.00 11.80           C  
ATOM   1412  C   MET A 188      17.766  29.362  -3.114  1.00 12.57           C  
ATOM   1413  O   MET A 188      17.604  30.413  -2.487  1.00 12.94           O  
ATOM   1414  CB  MET A 188      18.421  27.172  -1.990  1.00 10.80           C  
ATOM   1415  CG  MET A 188      17.933  26.076  -1.037  1.00 11.95           C  
ATOM   1416  SD  MET A 188      16.989  26.764   0.339  1.00 14.58           S  
ATOM   1417  CE  MET A 188      18.290  27.596   1.269  1.00 13.27           C  
ATOM   1418  N   THR A 189      18.371  29.409  -4.303  1.00 12.70           N  
ATOM   1419  CA  THR A 189      18.827  30.652  -4.896  1.00 13.17           C  
ATOM   1420  C   THR A 189      17.659  31.611  -5.144  1.00 12.12           C  
ATOM   1421  O   THR A 189      17.765  32.798  -4.846  1.00 11.94           O  
ATOM   1422  CB  THR A 189      19.577  30.441  -6.228  1.00 14.79           C  
ATOM   1423  OG1 THR A 189      20.720  29.613  -5.991  1.00 16.65           O  
ATOM   1424  CG2 THR A 189      20.027  31.781  -6.781  1.00 16.25           C  
ATOM   1425  N   THR A 190      16.562  31.097  -5.694  1.00 12.55           N  
ATOM   1426  CA  THR A 190      15.395  31.918  -5.994  1.00 11.63           C  
ATOM   1427  C   THR A 190      14.777  32.463  -4.711  1.00 11.11           C  
ATOM   1428  O   THR A 190      14.466  33.647  -4.625  1.00 10.37           O  
ATOM   1429  CB  THR A 190      14.319  31.131  -6.768  1.00 12.17           C  
ATOM   1430  OG1 THR A 190      14.905  30.676  -7.993  1.00 12.15           O  
ATOM   1431  CG2 THR A 190      13.102  31.996  -7.082  1.00 12.18           C  
ATOM   1432  N   LEU A 191      14.631  31.599  -3.702  1.00 11.06           N  
ATOM   1433  CA  LEU A 191      14.056  32.083  -2.449  1.00 11.10           C  
ATOM   1434  C   LEU A 191      14.941  33.145  -1.796  1.00 10.89           C  
ATOM   1435  O   LEU A 191      14.468  34.129  -1.221  1.00 12.27           O  
ATOM   1436  CB  LEU A 191      13.912  30.914  -1.463  1.00 11.23           C  
ATOM   1437  CG  LEU A 191      12.778  29.937  -1.774  1.00 11.01           C  
ATOM   1438  CD1 LEU A 191      12.963  28.649  -1.015  1.00 10.37           C  
ATOM   1439  CD2 LEU A 191      11.426  30.557  -1.405  1.00 10.72           C  
ATOM   1440  N   THR A 192      16.249  32.921  -1.850  1.00 10.99           N  
ATOM   1441  CA  THR A 192      17.225  33.816  -1.240  1.00 11.09           C  
ATOM   1442  C   THR A 192      17.157  35.201  -1.864  1.00 12.22           C  
ATOM   1443  O   THR A 192      17.121  36.217  -1.172  1.00 12.57           O  
ATOM   1444  CB  THR A 192      18.653  33.249  -1.345  1.00 11.66           C  
ATOM   1445  OG1 THR A 192      18.723  31.972  -0.689  1.00 11.44           O  
ATOM   1446  CG2 THR A 192      19.637  34.226  -0.711  1.00 11.25           C  
ATOM   1447  N   ARG A 193      17.048  35.260  -3.192  1.00 13.54           N  
ATOM   1448  CA  ARG A 193      16.957  36.534  -3.881  1.00 14.37           C  
ATOM   1449  C   ARG A 193      15.642  37.245  -3.577  1.00 14.76           C  
ATOM   1450  O   ARG A 193      15.612  38.462  -3.377  1.00 14.86           O  
ATOM   1451  CB  ARG A 193      17.062  36.323  -5.408  1.00 16.95           C  
ATOM   1452  CG  ARG A 193      16.629  37.565  -6.179  1.00 18.31           C  
ATOM   1453  CD  ARG A 193      16.727  37.438  -7.681  1.00 19.36           C  
ATOM   1454  NE  ARG A 193      15.705  36.578  -8.298  1.00 20.16           N  
ATOM   1455  CZ  ARG A 193      16.056  35.376  -8.765  1.00 19.35           C  
ATOM   1456  NH1 ARG A 193      17.311  34.968  -8.618  1.00 19.03           N  
ATOM   1457  NH2 ARG A 193      15.167  34.579  -9.337  1.00 21.41           N  
ATOM   1458  N   MET A 194      14.547  36.487  -3.580  1.00 13.44           N  
ATOM   1459  CA  MET A 194      13.227  37.084  -3.468  1.00 14.83           C  
ATOM   1460  C   MET A 194      12.745  37.459  -2.077  1.00 14.16           C  
ATOM   1461  O   MET A 194      11.986  38.429  -1.963  1.00 14.25           O  
ATOM   1462  CB  MET A 194      12.211  36.149  -4.137  1.00 16.25           C  
ATOM   1463  CG  MET A 194      12.485  35.969  -5.625  1.00 19.99           C  
ATOM   1464  SD  MET A 194      11.238  34.926  -6.399  1.00 22.02           S  
ATOM   1465  CE  MET A 194      10.647  36.050  -7.671  1.00 23.29           C  
ATOM   1466  N   ILE A 195      13.176  36.733  -1.055  1.00 12.18           N  
ATOM   1467  CA  ILE A 195      12.741  37.050   0.302  1.00 11.56           C  
ATOM   1468  C   ILE A 195      13.634  38.157   0.850  1.00 12.27           C  
ATOM   1469  O   ILE A 195      14.849  37.985   0.958  1.00 11.21           O  
ATOM   1470  CB  ILE A 195      12.799  35.797   1.204  1.00 10.21           C  
ATOM   1471  CG1 ILE A 195      11.925  34.693   0.632  1.00  9.46           C  
ATOM   1472  CG2 ILE A 195      12.362  36.189   2.632  1.00 10.41           C  
ATOM   1473  CD1 ILE A 195      12.020  33.340   1.304  1.00 10.20           C  
ATOM   1474  N   PRO A 196      13.048  39.289   1.204  1.00 13.01           N  
ATOM   1475  CA  PRO A 196      13.797  40.437   1.696  1.00 13.24           C  
ATOM   1476  C   PRO A 196      14.115  40.364   3.176  1.00 12.91           C  
ATOM   1477  O   PRO A 196      13.717  41.194   3.986  1.00 13.53           O  
ATOM   1478  CB  PRO A 196      12.882  41.618   1.353  1.00 13.77           C  
ATOM   1479  CG  PRO A 196      11.508  41.045   1.551  1.00 13.40           C  
ATOM   1480  CD  PRO A 196      11.608  39.613   1.071  1.00 13.20           C  
ATOM   1481  N   ALA A 197      14.890  39.368   3.561  1.00 12.55           N  
ATOM   1482  CA  ALA A 197      15.353  39.118   4.903  1.00 11.45           C  
ATOM   1483  C   ALA A 197      16.460  38.070   4.814  1.00 10.38           C  
ATOM   1484  O   ALA A 197      16.501  37.266   3.884  1.00  9.43           O  
ATOM   1485  CB  ALA A 197      14.225  38.615   5.801  1.00 11.85           C  
ATOM   1486  N   PRO A 198      17.319  38.033   5.828  1.00  8.98           N  
ATOM   1487  CA  PRO A 198      18.395  37.085   5.862  1.00  8.61           C  
ATOM   1488  C   PRO A 198      17.943  35.638   6.001  1.00  8.84           C  
ATOM   1489  O   PRO A 198      17.062  35.276   6.798  1.00  8.14           O  
ATOM   1490  CB  PRO A 198      19.218  37.475   7.101  1.00  9.33           C  
ATOM   1491  CG  PRO A 198      18.279  38.260   7.939  1.00  9.42           C  
ATOM   1492  CD  PRO A 198      17.346  38.975   6.972  1.00  9.11           C  
ATOM   1493  N   LEU A 199      18.593  34.788   5.214  1.00  8.64           N  
ATOM   1494  CA  LEU A 199      18.356  33.348   5.373  1.00  9.00           C  
ATOM   1495  C   LEU A 199      19.098  32.961   6.660  1.00  9.47           C  
ATOM   1496  O   LEU A 199      20.334  33.070   6.715  1.00  9.31           O  
ATOM   1497  CB  LEU A 199      18.946  32.588   4.198  1.00  9.71           C  
ATOM   1498  CG  LEU A 199      19.126  31.081   4.323  1.00  9.79           C  
ATOM   1499  CD1 LEU A 199      17.819  30.357   4.599  1.00 10.53           C  
ATOM   1500  CD2 LEU A 199      19.759  30.528   3.039  1.00  9.94           C  
ATOM   1501  N   LEU A 200      18.407  32.509   7.686  1.00 10.12           N  
ATOM   1502  CA  LEU A 200      19.036  32.170   8.963  1.00 10.93           C  
ATOM   1503  C   LEU A 200      19.695  30.802   8.968  1.00 13.31           C  
ATOM   1504  O   LEU A 200      20.614  30.520   9.747  1.00 13.56           O  
ATOM   1505  CB  LEU A 200      17.958  32.246  10.064  1.00 11.24           C  
ATOM   1506  CG  LEU A 200      17.198  33.583  10.160  1.00 10.90           C  
ATOM   1507  CD1 LEU A 200      16.177  33.497  11.286  1.00 12.33           C  
ATOM   1508  CD2 LEU A 200      18.145  34.745  10.381  1.00 11.73           C  
ATOM   1509  N   GLY A 201      19.253  29.934   8.041  1.00 12.35           N  
ATOM   1510  CA  GLY A 201      19.774  28.579   7.996  1.00 11.81           C  
ATOM   1511  C   GLY A 201      18.806  27.634   7.274  1.00 12.46           C  
ATOM   1512  O   GLY A 201      17.661  27.965   7.002  1.00 11.09           O  
ATOM   1513  N   GLU A 202      19.323  26.435   7.041  1.00 11.22           N  
ATOM   1514  CA  GLU A 202      18.579  25.399   6.339  1.00 11.74           C  
ATOM   1515  C   GLU A 202      18.571  24.117   7.173  1.00 11.62           C  
ATOM   1516  O   GLU A 202      19.635  23.601   7.520  1.00 12.07           O  
ATOM   1517  CB  GLU A 202      19.154  25.133   4.950  1.00 10.38           C  
ATOM   1518  CG  GLU A 202      18.355  24.051   4.212  1.00 13.06           C  
ATOM   1519  CD  GLU A 202      18.851  23.848   2.790  1.00 15.78           C  
ATOM   1520  OE1 GLU A 202      19.820  24.521   2.380  1.00 15.13           O  
ATOM   1521  OE2 GLU A 202      18.219  22.986   2.132  1.00 17.34           O  
ATOM   1522  N   ILE A 203      17.377  23.641   7.501  1.00 10.53           N  
ATOM   1523  CA  ILE A 203      17.257  22.423   8.291  1.00 10.76           C  
ATOM   1524  C   ILE A 203      17.082  21.243   7.331  1.00 11.19           C  
ATOM   1525  O   ILE A 203      16.222  21.300   6.449  1.00 10.13           O  
ATOM   1526  CB  ILE A 203      16.046  22.467   9.232  1.00 11.30           C  
ATOM   1527  CG1 ILE A 203      16.205  23.632  10.223  1.00 11.81           C  
ATOM   1528  CG2 ILE A 203      15.875  21.144   9.964  1.00 10.72           C  
ATOM   1529  CD1 ILE A 203      14.871  24.012  10.839  1.00 12.64           C  
ATOM   1530  N   PRO A 204      17.994  20.284   7.419  1.00 12.34           N  
ATOM   1531  CA  PRO A 204      17.976  19.143   6.534  1.00 12.60           C  
ATOM   1532  C   PRO A 204      16.779  18.234   6.759  1.00 12.47           C  
ATOM   1533  O   PRO A 204      16.066  18.313   7.764  1.00 11.60           O  
ATOM   1534  CB  PRO A 204      19.299  18.428   6.810  1.00 13.93           C  
ATOM   1535  CG  PRO A 204      19.894  19.023   8.027  1.00 13.35           C  
ATOM   1536  CD  PRO A 204      19.086  20.227   8.424  1.00 12.65           C  
ATOM   1537  N   TRP A 205      16.560  17.332   5.806  1.00 13.00           N  
ATOM   1538  CA  TRP A 205      15.482  16.351   5.915  1.00 15.09           C  
ATOM   1539  C   TRP A 205      15.870  15.302   6.967  1.00 16.45           C  
ATOM   1540  O   TRP A 205      16.818  14.525   6.778  1.00 16.89           O  
ATOM   1541  CB  TRP A 205      15.184  15.676   4.580  1.00 15.26           C  
ATOM   1542  CG  TRP A 205      14.091  14.607   4.669  1.00 16.03           C  
ATOM   1543  CD1 TRP A 205      12.792  14.801   4.932  1.00 16.61           C  
ATOM   1544  CD2 TRP A 205      14.295  13.213   4.478  1.00 16.90           C  
ATOM   1545  NE1 TRP A 205      12.160  13.518   4.910  1.00 16.62           N  
ATOM   1546  CE2 TRP A 205      13.059  12.600   4.643  1.00 17.30           C  
ATOM   1547  CE3 TRP A 205      15.414  12.425   4.184  1.00 17.64           C  
ATOM   1548  CZ2 TRP A 205      12.871  11.216   4.529  1.00 18.74           C  
ATOM   1549  CZ3 TRP A 205      15.215  11.034   4.072  1.00 19.21           C  
ATOM   1550  CH2 TRP A 205      14.002  10.459   4.236  1.00 19.64           C  
ATOM   1551  N   LEU A 206      15.114  15.335   8.050  1.00 17.72           N  
ATOM   1552  CA  LEU A 206      15.304  14.448   9.209  1.00 20.71           C  
ATOM   1553  C   LEU A 206      14.016  13.648   9.445  1.00 22.96           C  
ATOM   1554  O   LEU A 206      13.096  14.106  10.136  1.00 23.97           O  
ATOM   1555  CB  LEU A 206      15.615  15.303  10.435  1.00 19.31           C  
ATOM   1556  CG  LEU A 206      16.968  16.008  10.330  1.00 19.82           C  
ATOM   1557  CD1 LEU A 206      17.035  17.300  11.144  1.00 19.70           C  
ATOM   1558  CD2 LEU A 206      18.130  15.142  10.821  1.00 20.48           C  
ATOM   1559  N   ALA A 207      14.010  12.470   8.857  1.00 25.44           N  
ATOM   1560  CA  ALA A 207      12.860  11.548   8.869  1.00 28.29           C  
ATOM   1561  C   ALA A 207      12.292  11.283  10.278  1.00 30.31           C  
ATOM   1562  O   ALA A 207      11.090  11.445  10.526  1.00 32.05           O  
ATOM   1563  CB  ALA A 207      13.267  10.195   8.285  1.00 27.77           C  
ATOM   1564  N   GLU A 208      13.150  10.868  11.194  1.00 31.84           N  
ATOM   1565  CA  GLU A 208      12.704  10.482  12.551  1.00 32.95           C  
ATOM   1566  C   GLU A 208      12.819  11.629  13.573  1.00 31.95           C  
ATOM   1567  O   GLU A 208      13.889  12.230  13.742  1.00 31.90           O  
ATOM   1568  CB  GLU A 208      13.542   9.316  13.072  1.00 35.12           C  
ATOM   1569  CG  GLU A 208      12.926   8.639  14.297  1.00 38.05           C  
ATOM   1570  CD  GLU A 208      13.850   8.660  15.516  1.00 40.04           C  
ATOM   1571  OE1 GLU A 208      14.830   7.825  15.596  1.00 41.37           O  
ATOM   1572  OE2 GLU A 208      13.649   9.513  16.462  1.00 40.67           O  
ATOM   1573  N   ASN A 209      11.680  11.861  14.215  1.00 31.20           N  
ATOM   1574  CA  ASN A 209      11.500  12.855  15.298  1.00 31.07           C  
ATOM   1575  C   ASN A 209      12.387  14.094  15.114  1.00 28.64           C  
ATOM   1576  O   ASN A 209      13.339  14.314  15.878  1.00 29.11           O  
ATOM   1577  CB  ASN A 209      11.870  12.221  16.637  1.00 33.24           C  
ATOM   1578  CG  ASN A 209      10.737  12.279  17.657  1.00 35.32           C  
ATOM   1579  OD1 ASN A 209       9.892  11.387  17.689  1.00 36.55           O  
ATOM   1580  ND2 ASN A 209      10.670  13.288  18.504  1.00 35.35           N  
ATOM   1581  N   PRO A 210      12.128  14.946  14.115  1.00 26.95           N  
ATOM   1582  CA  PRO A 210      12.926  16.149  13.897  1.00 24.97           C  
ATOM   1583  C   PRO A 210      12.805  17.158  15.027  1.00 23.89           C  
ATOM   1584  O   PRO A 210      13.743  17.989  15.221  1.00 22.90           O  
ATOM   1585  CB  PRO A 210      12.334  16.757  12.647  1.00 24.67           C  
ATOM   1586  CG  PRO A 210      11.171  15.881  12.205  1.00 25.59           C  
ATOM   1587  CD  PRO A 210      11.040  14.733  13.157  1.00 26.04           C  
ATOM   1588  N   GLU A 211      11.681  17.104  15.738  1.00 22.70           N  
ATOM   1589  CA  GLU A 211      11.362  18.063  16.835  1.00 22.80           C  
ATOM   1590  C   GLU A 211      12.323  17.940  18.017  1.00 23.31           C  
ATOM   1591  O   GLU A 211      12.535  18.906  18.765  1.00 23.93           O  
ATOM   1592  CB  GLU A 211       9.949  17.819  17.370  1.00 22.33           C  
ATOM   1593  CG  GLU A 211       8.855  18.168  16.360  1.00 21.98           C  
ATOM   1594  CD  GLU A 211       8.585  17.034  15.375  1.00 21.24           C  
ATOM   1595  OE1 GLU A 211       9.198  15.908  15.508  1.00 19.95           O  
ATOM   1596  OE2 GLU A 211       7.748  17.204  14.412  1.00 21.61           O  
ATOM   1597  N   ASN A 212      12.886  16.759  18.210  1.00 23.24           N  
ATOM   1598  CA  ASN A 212      13.838  16.491  19.280  1.00 23.27           C  
ATOM   1599  C   ASN A 212      15.260  16.315  18.770  1.00 22.06           C  
ATOM   1600  O   ASN A 212      16.199  16.046  19.528  1.00 22.38           O  
ATOM   1601  CB  ASN A 212      13.345  15.262  20.058  1.00 24.64           C  
ATOM   1602  CG  ASN A 212      12.052  15.580  20.802  1.00 25.22           C  
ATOM   1603  OD1 ASN A 212      11.046  14.886  20.658  1.00 26.39           O  
ATOM   1604  ND2 ASN A 212      12.092  16.646  21.595  1.00 25.55           N  
ATOM   1605  N   ALA A 213      15.472  16.460  17.464  1.00 20.19           N  
ATOM   1606  CA  ALA A 213      16.802  16.355  16.870  1.00 17.08           C  
ATOM   1607  C   ALA A 213      17.616  17.585  17.238  1.00 16.10           C  
ATOM   1608  O   ALA A 213      17.028  18.636  17.516  1.00 16.63           O  
ATOM   1609  CB  ALA A 213      16.697  16.212  15.355  1.00 17.82           C  
ATOM   1610  N   ALA A 214      18.935  17.473  17.278  1.00 14.52           N  
ATOM   1611  CA  ALA A 214      19.788  18.614  17.604  1.00 13.98           C  
ATOM   1612  C   ALA A 214      19.943  19.445  16.331  1.00 12.86           C  
ATOM   1613  O   ALA A 214      20.827  19.170  15.520  1.00 13.89           O  
ATOM   1614  CB  ALA A 214      21.124  18.156  18.152  1.00 13.05           C  
ATOM   1615  N   THR A 215      19.059  20.419  16.163  1.00 11.47           N  
ATOM   1616  CA  THR A 215      19.044  21.236  14.953  1.00 11.16           C  
ATOM   1617  C   THR A 215      19.427  22.688  15.175  1.00 11.42           C  
ATOM   1618  O   THR A 215      19.468  23.479  14.224  1.00 11.46           O  
ATOM   1619  CB  THR A 215      17.593  21.226  14.414  1.00 11.67           C  
ATOM   1620  OG1 THR A 215      16.730  21.572  15.507  1.00 11.08           O  
ATOM   1621  CG2 THR A 215      17.190  19.851  13.897  1.00 12.01           C  
ATOM   1622  N   GLY A 216      19.788  23.048  16.407  1.00 10.41           N  
ATOM   1623  CA  GLY A 216      20.251  24.403  16.697  1.00 10.69           C  
ATOM   1624  C   GLY A 216      21.449  24.822  15.848  1.00 11.55           C  
ATOM   1625  O   GLY A 216      21.601  25.995  15.463  1.00  9.17           O  
ATOM   1626  N   LYS A 217      22.341  23.886  15.549  1.00 11.66           N  
ATOM   1627  CA  LYS A 217      23.518  24.100  14.731  1.00 13.69           C  
ATOM   1628  C   LYS A 217      23.196  24.599  13.327  1.00 12.68           C  
ATOM   1629  O   LYS A 217      24.046  25.282  12.745  1.00 13.45           O  
ATOM   1630  CB  LYS A 217      24.361  22.821  14.605  1.00 16.05           C  
ATOM   1631  CG  LYS A 217      23.624  21.632  14.010  1.00 19.16           C  
ATOM   1632  CD  LYS A 217      24.524  20.765  13.148  1.00 22.12           C  
ATOM   1633  CE  LYS A 217      25.271  19.699  13.911  1.00 24.23           C  
ATOM   1634  NZ  LYS A 217      26.256  18.979  13.030  1.00 25.92           N  
ATOM   1635  N   TYR A 218      22.010  24.332  12.787  1.00 10.70           N  
ATOM   1636  CA  TYR A 218      21.626  24.808  11.461  1.00 11.85           C  
ATOM   1637  C   TYR A 218      21.221  26.265  11.388  1.00 12.18           C  
ATOM   1638  O   TYR A 218      21.090  26.839  10.296  1.00 12.37           O  
ATOM   1639  CB  TYR A 218      20.481  23.912  10.934  1.00 11.04           C  
ATOM   1640  CG  TYR A 218      20.966  22.469  10.858  1.00 12.86           C  
ATOM   1641  CD1 TYR A 218      22.038  22.128  10.035  1.00 13.65           C  
ATOM   1642  CD2 TYR A 218      20.358  21.481  11.615  1.00 13.37           C  
ATOM   1643  CE1 TYR A 218      22.484  20.813   9.957  1.00 13.61           C  
ATOM   1644  CE2 TYR A 218      20.806  20.173  11.546  1.00 13.54           C  
ATOM   1645  CZ  TYR A 218      21.858  19.853  10.722  1.00 13.83           C  
ATOM   1646  OH  TYR A 218      22.282  18.544  10.677  1.00 14.46           O  
ATOM   1647  N   ILE A 219      21.093  26.940  12.521  1.00 12.45           N  
ATOM   1648  CA  ILE A 219      20.686  28.328  12.597  1.00 12.56           C  
ATOM   1649  C   ILE A 219      21.855  29.231  12.967  1.00 14.34           C  
ATOM   1650  O   ILE A 219      22.533  28.949  13.959  1.00 13.49           O  
ATOM   1651  CB  ILE A 219      19.597  28.496  13.677  1.00 12.78           C  
ATOM   1652  CG1 ILE A 219      18.370  27.634  13.366  1.00 13.76           C  
ATOM   1653  CG2 ILE A 219      19.234  29.958  13.876  1.00 13.05           C  
ATOM   1654  CD1 ILE A 219      17.608  27.985  12.110  1.00 13.81           C  
ATOM   1655  N   ASN A 220      22.036  30.308  12.228  1.00 14.21           N  
ATOM   1656  CA  ASN A 220      23.036  31.312  12.561  1.00 15.83           C  
ATOM   1657  C   ASN A 220      22.303  32.478  13.209  1.00 15.64           C  
ATOM   1658  O   ASN A 220      21.802  33.402  12.559  1.00 12.21           O  
ATOM   1659  CB  ASN A 220      23.854  31.794  11.362  1.00 17.62           C  
ATOM   1660  CG  ASN A 220      24.993  32.712  11.768  1.00 19.85           C  
ATOM   1661  OD1 ASN A 220      25.145  33.103  12.930  1.00 19.89           O  
ATOM   1662  ND2 ASN A 220      25.813  33.093  10.787  1.00 20.64           N  
ATOM   1663  N   LEU A 221      22.247  32.434  14.550  1.00 15.72           N  
ATOM   1664  CA  LEU A 221      21.551  33.495  15.276  1.00 17.76           C  
ATOM   1665  C   LEU A 221      22.176  34.871  15.113  1.00 18.70           C  
ATOM   1666  O   LEU A 221      21.466  35.862  15.310  1.00 19.24           O  
ATOM   1667  CB  LEU A 221      21.423  33.088  16.739  1.00 18.34           C  
ATOM   1668  CG  LEU A 221      20.057  33.204  17.407  1.00 19.72           C  
ATOM   1669  CD1 LEU A 221      18.903  32.750  16.519  1.00 19.48           C  
ATOM   1670  CD2 LEU A 221      20.088  32.393  18.687  1.00 20.30           C  
ATOM   1671  N   ALA A 222      23.432  35.017  14.697  1.00 18.79           N  
ATOM   1672  CA  ALA A 222      24.054  36.317  14.499  1.00 20.78           C  
ATOM   1673  C   ALA A 222      23.496  37.054  13.284  1.00 21.97           C  
ATOM   1674  O   ALA A 222      23.621  38.282  13.219  1.00 22.60           O  
ATOM   1675  CB  ALA A 222      25.568  36.226  14.381  1.00 20.06           C  
ATOM   1676  N   LEU A 223      22.811  36.354  12.378  1.00 22.25           N  
ATOM   1677  CA  LEU A 223      22.128  36.979  11.252  1.00 23.20           C  
ATOM   1678  C   LEU A 223      20.752  37.471  11.681  1.00 23.49           C  
ATOM   1679  O   LEU A 223      20.093  38.256  10.989  1.00 24.35           O  
ATOM   1680  CB  LEU A 223      22.019  36.019  10.061  1.00 22.82           C  
ATOM   1681  CG  LEU A 223      23.252  35.172   9.764  1.00 23.64           C  
ATOM   1682  CD1 LEU A 223      23.028  34.247   8.574  1.00 23.63           C  
ATOM   1683  CD2 LEU A 223      24.479  36.036   9.496  1.00 24.31           C  
ATOM   1684  N   LEU A 224      20.294  37.009  12.850  1.00 23.53           N  
ATOM   1685  CA  LEU A 224      18.988  37.467  13.311  1.00 22.83           C  
ATOM   1686  C   LEU A 224      19.223  38.915  13.743  1.00 24.58           C  
ATOM   1687  O   LEU A 224      19.775  39.094  14.877  1.00 23.73           O  
ATOM   1688  CB  LEU A 224      18.333  36.662  14.410  1.00 23.39           C  
ATOM   1689  CG  LEU A 224      16.953  36.070  14.166  1.00 22.40           C  
ATOM   1690  CD1 LEU A 224      16.368  35.512  15.451  1.00 22.10           C  
ATOM   1691  CD2 LEU A 224      15.978  37.051  13.527  1.00 21.74           C  
ATOM   1692  OXT LEU A 224      18.148  39.593  13.588  1.00 25.73           O  
TER    1693      LEU A 224                                                      
HETATM 1694 MG    MG A 901       3.459  24.042  14.250  1.00 18.72          MG  
HETATM 1695 MG    MG A 902       1.479  21.539  12.381  1.00 15.55          MG  
HETATM 1696  P   PO4 A 802       0.207  24.583  13.067  1.00 18.45           P  
HETATM 1697  O1  PO4 A 802      -0.663  25.230  14.078  1.00 16.95           O  
HETATM 1698  O2  PO4 A 802       1.731  24.753  13.527  1.00 15.69           O  
HETATM 1699  O3  PO4 A 802      -0.039  23.079  12.979  1.00 17.28           O  
HETATM 1700  O4  PO4 A 802       0.043  25.201  11.509  1.00 17.12           O  
HETATM 1701  PB  ADP A 801       3.880  23.194  11.076  1.00 14.59           P  
HETATM 1702  O1B ADP A 801       4.099  24.264  10.092  1.00 14.00           O  
HETATM 1703  O2B ADP A 801       4.352  23.449  12.564  1.00 13.56           O  
HETATM 1704  O3B ADP A 801       2.529  22.632  11.213  1.00 14.66           O  
HETATM 1705  PA  ADP A 801       5.835  20.961  11.743  1.00 14.57           P  
HETATM 1706  O1A ADP A 801       4.894  20.349  12.744  1.00 13.74           O  
HETATM 1707  O2A ADP A 801       7.099  21.542  12.257  1.00 12.72           O  
HETATM 1708  O3A ADP A 801       4.940  21.981  10.709  1.00 14.53           O  
HETATM 1709  O5' ADP A 801       6.265  19.846  10.553  1.00 14.03           O  
HETATM 1710  C5' ADP A 801       5.202  19.193   9.775  1.00 14.53           C  
HETATM 1711  C4' ADP A 801       5.453  17.695   9.626  1.00 16.00           C  
HETATM 1712  O4' ADP A 801       6.643  17.498   8.843  1.00 15.51           O  
HETATM 1713  C3' ADP A 801       5.710  17.001  10.965  1.00 15.95           C  
HETATM 1714  O3' ADP A 801       5.310  15.607  10.946  1.00 17.82           O  
HETATM 1715  C2' ADP A 801       7.229  17.111  11.164  1.00 16.12           C  
HETATM 1716  O2' ADP A 801       7.696  16.073  12.080  1.00 16.15           O  
HETATM 1717  C1' ADP A 801       7.692  16.920   9.712  1.00 15.29           C  
HETATM 1718  N9  ADP A 801       8.999  17.689   9.543  1.00 14.43           N  
HETATM 1719  C8  ADP A 801       9.087  19.022   9.484  1.00 13.74           C  
HETATM 1720  N7  ADP A 801      10.346  19.362   9.240  1.00 14.80           N  
HETATM 1721  C5  ADP A 801      11.038  18.261   8.976  1.00 13.62           C  
HETATM 1722  C6  ADP A 801      12.377  18.034   8.658  1.00 13.62           C  
HETATM 1723  N6  ADP A 801      13.165  19.046   8.298  1.00 11.79           N  
HETATM 1724  N1  ADP A 801      12.677  16.788   8.229  1.00 12.68           N  
HETATM 1725  C2  ADP A 801      11.736  15.851   8.132  1.00 13.66           C  
HETATM 1726  N3  ADP A 801      10.472  15.988   8.543  1.00 12.99           N  
HETATM 1727  C4  ADP A 801      10.095  17.246   8.870  1.00 14.72           C  
HETATM 1728  CN  DTB A 803      -3.145  22.488  13.006  1.00 24.58           C  
HETATM 1729  O   DTB A 803      -2.272  21.759  13.494  1.00 24.83           O  
HETATM 1730  N2  DTB A 803      -3.129  23.053  11.759  1.00 23.52           N  
HETATM 1731  CR  DTB A 803      -4.380  23.743  11.510  1.00 23.46           C  
HETATM 1732  CS  DTB A 803      -4.777  24.040  13.008  1.00 23.47           C  
HETATM 1733  N1  DTB A 803      -4.275  22.845  13.639  1.00 23.94           N  
HETATM 1734  CT  DTB A 803      -4.315  25.355  13.696  1.00 23.72           C  
HETATM 1735  CE  DTB A 803      -4.217  25.070  10.679  1.00 21.81           C  
HETATM 1736  CD  DTB A 803      -5.578  25.692  10.317  1.00 21.30           C  
HETATM 1737  CG  DTB A 803      -5.641  26.784   9.267  1.00 19.93           C  
HETATM 1738  CB  DTB A 803      -6.902  27.604   9.422  1.00 19.64           C  
HETATM 1739  CA  DTB A 803      -6.964  28.689   8.318  1.00 17.35           C  
HETATM 1740  C   DTB A 803      -6.712  28.188   6.829  1.00 16.49           C  
HETATM 1741  OI1 DTB A 803      -7.365  27.219   6.380  1.00 15.56           O  
HETATM 1742  OI2 DTB A 803      -5.799  28.743   6.205  1.00 14.58           O  
HETATM 1743  O   HOH A 301       2.054  28.220  -4.445  1.00 11.19           O  
HETATM 1744  O   HOH A 302      14.931  19.498  -2.733  1.00 29.71           O  
HETATM 1745  O   HOH A 304      12.450  19.973   0.734  1.00 20.75           O  
HETATM 1746  O   HOH A 306      13.939  13.332  -5.493  1.00 20.82           O  
HETATM 1747  O   HOH A 307      20.001  18.604   0.071  1.00 31.01           O  
HETATM 1748  O   HOH A 308      18.725  16.420   3.684  1.00 24.75           O  
HETATM 1749  O   HOH A 309      21.338  22.144   5.995  1.00 20.96           O  
HETATM 1750  O   HOH A 310      22.099  26.125   7.784  1.00 18.18           O  
HETATM 1751  O   HOH A 311      21.788  28.067   5.237  1.00 19.21           O  
HETATM 1752  O   HOH A 314      22.692  32.204   1.139  1.00 15.22           O  
HETATM 1753  O   HOH A 315      17.154  36.043   1.534  1.00 10.04           O  
HETATM 1754  O   HOH A 316      22.112  34.607   5.368  1.00 15.13           O  
HETATM 1755  O   HOH A 317      23.149  28.955   9.071  1.00 22.00           O  
HETATM 1756  O   HOH A 321      23.930  30.826  16.273  1.00 19.49           O  
HETATM 1757  O   HOH A 322      25.814  30.015  20.051  1.00 36.73           O  
HETATM 1758  O   HOH A 323      23.715  27.472  16.052  1.00 24.90           O  
HETATM 1759  O   HOH A 325      21.058  21.593  19.336  1.00 22.18           O  
HETATM 1760  O   HOH A 326      20.940  24.107  22.605  1.00 21.55           O  
HETATM 1761  O   HOH A 327      16.056  26.717  24.268  1.00 16.35           O  
HETATM 1762  O   HOH A 329       9.724  24.257  29.548  1.00 23.36           O  
HETATM 1763  O   HOH A 330      -0.599  15.750  30.847  1.00 25.23           O  
HETATM 1764  O   HOH A 331       3.173  21.384  32.614  1.00 23.56           O  
HETATM 1765  O   HOH A 332      -0.324  24.157  33.019  1.00 16.54           O  
HETATM 1766  O   HOH A 338     -12.623  33.588  19.081  1.00 14.75           O  
HETATM 1767  O   HOH A 339     -15.178  32.569  15.765  1.00 21.69           O  
HETATM 1768  O   HOH A 343     -10.847  23.663  24.745  1.00 29.32           O  
HETATM 1769  O   HOH A 344     -10.065  26.059  31.842  1.00 19.89           O  
HETATM 1770  O   HOH A 345     -16.098  30.769  27.628  1.00 19.19           O  
HETATM 1771  O   HOH A 348     -11.092  36.582  10.766  1.00 20.30           O  
HETATM 1772  O   HOH A 349     -11.303  39.105   9.987  1.00 24.57           O  
HETATM 1773  O   HOH A 350      -9.440  41.367  11.171  1.00 39.38           O  
HETATM 1774  O   HOH A 353       1.481  32.371   5.230  1.00  9.73           O  
HETATM 1775  O   HOH A 356      -1.251  41.463   7.493  1.00 11.78           O  
HETATM 1776  O   HOH A 357      -0.676  43.268   5.123  1.00 19.08           O  
HETATM 1777  O   HOH A 358       2.517  48.069  11.771  1.00 24.16           O  
HETATM 1778  O   HOH A 359       0.957  43.688  26.964  1.00 26.77           O  
HETATM 1779  O   HOH A 360      -3.450  41.960  28.141  1.00 20.29           O  
HETATM 1780  O   HOH A 361      -5.125  36.016  31.297  1.00 20.23           O  
HETATM 1781  O   HOH A 362       1.843  15.892  28.429  1.00 25.00           O  
HETATM 1782  O   HOH A 363      20.590  35.191  29.374  1.00 13.77           O  
HETATM 1783  O   HOH A 366       0.504  32.816  31.458  1.00 14.99           O  
HETATM 1784  O   HOH A 367      -0.903  35.249  31.311  1.00 13.40           O  
HETATM 1785  O   HOH A 368      -3.871  37.531  33.406  1.00 31.01           O  
HETATM 1786  O   HOH A 369      -3.178  35.013  29.675  1.00 13.56           O  
HETATM 1787  O   HOH A 370       2.160  32.664  29.426  1.00 13.76           O  
HETATM 1788  O   HOH A 371      -0.220  29.936  18.493  1.00  8.06           O  
HETATM 1789  O   HOH A 372      -1.354  17.626  19.192  1.00 16.44           O  
HETATM 1790  O   HOH A 373       5.810  17.230  20.907  1.00 32.64           O  
HETATM 1791  O   HOH A 376     -12.108  19.077  11.260  1.00 37.18           O  
HETATM 1792  O   HOH A 379      20.824  18.040  -7.705  1.00 20.33           O  
HETATM 1793  O   HOH A 380      21.555  27.449  -3.872  1.00 20.44           O  
HETATM 1794  O   HOH A 381      11.036  43.766   6.905  1.00 23.38           O  
HETATM 1795  O   HOH A 383      17.123  40.253  11.323  1.00 16.47           O  
HETATM 1796  O   HOH A 385      18.381  36.578  18.515  1.00 20.25           O  
HETATM 1797  O   HOH A 386      13.177  40.793  18.795  1.00 25.14           O  
HETATM 1798  O   HOH A 388      -4.070  42.777  23.042  1.00 17.99           O  
HETATM 1799  O   HOH A 390      27.032  30.928  25.147  1.00 32.29           O  
HETATM 1800  O   HOH A 393      14.230  20.800  15.388  1.00 14.10           O  
HETATM 1801  O   HOH A 396      21.996  34.374   2.553  1.00 12.40           O  
HETATM 1802  O   HOH A 398     -16.754  32.436  10.069  1.00 25.35           O  
HETATM 1803  O   HOH A 400      -8.440  28.285  27.365  1.00 33.29           O  
HETATM 1804  O   HOH A 402      17.768  28.956  31.288  1.00 28.34           O  
HETATM 1805  O   HOH A 404      -0.245  16.076  22.595  1.00 24.75           O  
HETATM 1806  O   HOH A 406      10.370  42.701  28.648  1.00 51.38           O  
HETATM 1807  O   HOH A 407      26.341  34.182  28.488  1.00 63.10           O  
HETATM 1808  O   HOH A 412      -0.238  35.376  11.816  1.00 15.16           O  
HETATM 1809  O   HOH A 416      19.762  29.245  -9.785  1.00 42.92           O  
HETATM 1810  O   HOH A 421       6.232  25.929   1.562  1.00 18.41           O  
HETATM 1811  O   HOH A 423       8.594  47.121  11.902  1.00 30.18           O  
HETATM 1812  O   HOH A 425      16.607  22.573  23.899  1.00 45.21           O  
HETATM 1813  O   HOH A 426      -0.356  32.538  12.434  1.00 13.49           O  
HETATM 1814  O   HOH A 427      16.329   7.224  19.931  1.00 33.18           O  
HETATM 1815  O   HOH A 430      19.636  36.051   2.720  1.00 13.78           O  
HETATM 1816  O   HOH A 432      26.892  25.555   6.999  1.00 80.27           O  
HETATM 1817  O   HOH A 433      -2.831  23.493  32.557  1.00 31.55           O  
HETATM 1818  O   HOH A 434      -0.736  42.883  28.984  1.00 25.70           O  
HETATM 1819  O   HOH A 436      27.134  32.887  14.651  1.00 31.27           O  
HETATM 1820  O   HOH A 438      26.513  19.072  22.521  1.00 36.25           O  
HETATM 1821  O   HOH A 440      23.674  29.679  18.700  1.00 16.12           O  
HETATM 1822  O   HOH A 441       3.231  24.393  -1.962  1.00 23.71           O  
HETATM 1823  O   HOH A 444       2.719  21.314  14.069  1.00 22.15           O  
HETATM 1824  O   HOH A 446     -14.815  40.166   9.438  1.00 26.32           O  
HETATM 1825  O   HOH A 447       4.059  16.717  29.241  1.00 35.40           O  
HETATM 1826  O   HOH A 448       2.461  19.567  11.978  1.00 14.89           O  
HETATM 1827  O   HOH A 449      27.047  28.802  -6.856  1.00 66.68           O  
HETATM 1828  O   HOH A 457     -13.523  45.366  17.216  1.00 22.66           O  
HETATM 1829  O   HOH A 460       7.762  42.120  29.387  1.00 27.71           O  
HETATM 1830  O   HOH A 463     -11.887  39.741  21.880  1.00 31.62           O  
HETATM 1831  O   HOH A 466      21.006  23.910  -0.005  1.00 24.73           O  
HETATM 1832  O   HOH A 470      12.559  20.878  -5.705  1.00 60.95           O  
HETATM 1833  O   HOH A 474      18.016  27.367 -14.221  1.00 27.10           O  
HETATM 1834  O   HOH A 477       1.983  23.994   1.515  1.00 41.73           O  
HETATM 1835  O   HOH A 481      23.005  24.491  24.220  1.00 18.79           O  
HETATM 1836  O   HOH A 486      -9.438  13.437  23.060  1.00 39.35           O  
HETATM 1837  O   HOH A 492       1.258  33.157  34.098  0.50 11.74           O  
HETATM 1838  O   HOH A 493      -4.955  30.393  29.718  1.00 62.16           O  
HETATM 1839  O   HOH A 498     -12.147  37.527  20.238  1.00 40.82           O  
HETATM 1840  O   HOH A 499       0.805  38.907  32.104  1.00 15.25           O  
HETATM 1841  O   HOH A 500      -3.678  32.382  30.374  1.00 15.72           O  
HETATM 1842  O   HOH A 504       6.643  40.855  31.629  1.00 22.42           O  
HETATM 1843  O   HOH A 505       3.204  39.474  33.415  1.00 28.50           O  
HETATM 1844  O   HOH A 506       3.964  32.316  34.762  1.00 21.78           O  
HETATM 1845  O   HOH A 507      -0.720  36.920  33.465  1.00 16.12           O  
HETATM 1846  O   HOH A 512      -7.313  46.035  14.959  1.00 58.13           O  
HETATM 1847  O   HOH A 513      -2.003  43.675   9.789  1.00 25.03           O  
HETATM 1848  O   HOH A 514       7.125  46.427  14.015  1.00 28.87           O  
HETATM 1849  O   HOH A 516      -9.646  39.656  20.672  1.00 12.71           O  
HETATM 1850  O   HOH A 518      -5.939  38.588  30.307  1.00 25.17           O  
HETATM 1851  O   HOH A 521      -2.001  46.059   8.663  1.00 23.69           O  
HETATM 1852  O   HOH A 522      -0.412  48.134   9.962  1.00 39.73           O  
HETATM 1853  O   HOH A 523       7.641  43.883  13.184  1.00 13.48           O  
HETATM 1854  O   HOH A 524      10.968  44.704  14.414  1.00 51.17           O  
HETATM 1855  O   HOH A 526       7.387  47.044   6.361  1.00 27.17           O  
HETATM 1856  O   HOH A 530      20.089  20.921   3.741  1.00 23.14           O  
HETATM 1857  O   HOH A 531      17.710  18.112   2.141  1.00 28.14           O  
HETATM 1858  O   HOH A 532      15.507  18.456   0.453  1.00 21.25           O  
HETATM 1859  O   HOH A 533      21.189  21.021   1.240  1.00 32.36           O  
HETATM 1860  O   HOH A 535      16.977  42.412   5.190  1.00 37.04           O  
HETATM 1861  O   HOH A 536      12.365  14.796  -3.262  1.00 30.41           O  
HETATM 1862  O   HOH A 538      14.329  15.169  -8.301  1.00 24.33           O  
HETATM 1863  O   HOH A 543      17.605  29.387 -12.573  1.00 23.21           O  
HETATM 1864  O   HOH A 544      17.428  30.094  -9.820  1.00 36.42           O  
HETATM 1865  O   HOH A 546      21.031  30.669  -0.427  1.00 16.41           O  
HETATM 1866  O   HOH A 547      21.899  30.613  -2.755  1.00 29.24           O  
HETATM 1867  O   HOH A 548      14.727  40.342  -1.656  1.00 36.55           O  
HETATM 1868  O   HOH A 551      21.476  26.699   2.899  1.00 24.00           O  
HETATM 1869  O   HOH A 560      19.237  22.622  23.646  1.00 34.02           O  
HETATM 1870  O   HOH A 561      20.865  37.434  17.274  1.00 32.77           O  
HETATM 1871  O   HOH A 569      24.004  39.507  19.826  1.00 41.68           O  
HETATM 1872  O   HOH A 571      24.312  36.321  20.469  1.00 32.58           O  
HETATM 1873  O   HOH A 574      -2.690  10.870  26.419  1.00 45.73           O  
HETATM 1874  O   HOH A 580      -9.646  20.950  30.059  1.00 29.07           O  
HETATM 1875  O   HOH A 586       4.061  18.977  16.930  1.00 17.94           O  
HETATM 1876  O   HOH A 587       3.447  19.366  29.680  1.00 24.29           O  
HETATM 1877  O   HOH A 589      11.223  19.619  31.832  1.00 39.59           O  
HETATM 1878  O   HOH A 590      13.612  26.875  34.935  1.00 26.02           O  
HETATM 1879  O   HOH A 595      -4.391  25.268  27.802  1.00 23.56           O  
HETATM 1880  O   HOH A 596     -11.988  32.048  26.456  1.00 13.05           O  
HETATM 1881  O   HOH A 597     -10.457  29.781  27.833  1.00 19.46           O  
HETATM 1882  O   HOH A 598     -10.294  33.975  27.177  1.00 20.74           O  
HETATM 1883  O   HOH A 600     -14.883  18.739  17.822  1.00 33.78           O  
HETATM 1884  O   HOH A 602     -19.980  22.775  22.011  1.00 33.64           O  
HETATM 1885  O   HOH A 607      -9.315  41.732  19.272  1.00 26.90           O  
HETATM 1886  O   HOH A 610      15.787  36.503  32.606  1.00 39.87           O  
HETATM 1887  O   HOH A 611      -6.010  40.395   9.185  1.00 23.36           O  
HETATM 1888  O   HOH A 612     -12.704  39.048  17.977  1.00 15.55           O  
HETATM 1889  O   HOH A 614     -13.021  41.910  20.762  0.70 21.69           O  
HETATM 1890  O   HOH A 615       7.593  19.566  -4.327  1.00 29.89           O  
HETATM 1891  O   HOH A 616       5.103  20.715   3.686  1.00 37.55           O  
HETATM 1892  O   HOH A 622      11.984  16.322  -8.147  1.00 34.07           O  
HETATM 1893  O   HOH A 624      21.159  28.083  -8.065  1.00 40.11           O  
HETATM 1894  O   HOH A 626      19.830  35.748  -7.372  1.00 22.29           O  
HETATM 1895  O   HOH A 652       1.794  31.247  11.243  1.00 10.30           O  
HETATM 1896  O   HOH A 653      20.142  18.903  -2.666  1.00 20.16           O  
HETATM 1897  O   HOH A 655       3.294  28.547  -7.171  1.00 22.88           O  
HETATM 1898  O   HOH A 656      18.883  16.130 -15.638  1.00 30.08           O  
HETATM 1899  O   HOH A 661       3.330  49.329  -0.713  1.00 78.95           O  
HETATM 1900  O   HOH A 663      12.788  35.424  -9.491  1.00 27.26           O  
HETATM 1901  O   HOH A 664     -14.967  38.535  18.713  1.00 27.63           O  
HETATM 1902  O   HOH A 671      28.749  19.741  18.889  1.00 48.57           O  
HETATM 1903  O   HOH A 675      25.147  34.407   5.659  1.00 44.08           O  
HETATM 1904  O   HOH A 676     -14.574  35.652  19.791  1.00 26.32           O  
HETATM 1905  O   HOH A 679      27.836  17.429   0.148  1.00 38.42           O  
HETATM 1906  O   HOH A 684       7.477  21.246  33.452  1.00 48.42           O  
HETATM 1907  O   HOH A 685       5.487  14.528  27.202  1.00 26.63           O  
HETATM 1908  O   HOH A 688       0.215  43.805  -1.145  1.00 48.45           O  
HETATM 1909  O   HOH A 689     -10.664  31.003  30.307  1.00 27.61           O  
HETATM 1910  O   HOH A 691      24.929  33.449  -0.617  1.00 43.67           O  
HETATM 1911  O   HOH A 693       4.579  42.206  33.326  1.00 21.28           O  
HETATM 1912  O   HOH A 694       8.611  14.205  21.499  1.00 29.03           O  
HETATM 1913  O   HOH A 700      -8.514  14.828  20.602  1.00 24.76           O  
HETATM 1914  O   HOH A 703     -11.755  41.523  18.452  1.00 20.81           O  
HETATM 1915  O   HOH A 704      -2.496  47.266  14.984  1.00 35.19           O  
HETATM 1916  O   HOH A 706      -8.207  40.928   7.634  1.00 41.32           O  
HETATM 1917  O   HOH A 707      -7.556  45.370  29.557  1.00 31.62           O  
HETATM 1918  O   HOH A 708      11.511  38.912  28.196  1.00 32.99           O  
HETATM 1919  O   HOH A 709       3.815  16.739  14.747  1.00 36.79           O  
HETATM 1920  O   HOH A 714       5.474  18.584  14.466  1.00 17.78           O  
HETATM 1921  O   HOH A 717      -0.782  22.051  16.121  1.00 22.13           O  
HETATM 1922  O   HOH A 718       2.227  16.993  11.225  1.00 47.70           O  
HETATM 1923  O   HOH A 719      -2.231  24.447  16.268  1.00 14.90           O  
HETATM 1924  O   HOH A 749       0.331  20.310  13.581  1.00 19.38           O  
HETATM 1925  O   HOH A 750      -0.022  20.923  10.630  1.00 19.26           O  
HETATM 1926  O   HOH A 751     -15.829  39.077  16.614  1.00 20.86           O  
HETATM 1927  O   HOH A 752     -12.401  20.515  19.755  1.00 28.85           O  
HETATM 1928  O   HOH A 753      26.401  34.717  22.377  1.00 23.87           O  
HETATM 1929  O   HOH A 754       4.073  25.929   0.055  1.00 29.08           O  
HETATM 1930  O   HOH A 755      -3.836  44.918  14.674  1.00 27.26           O  
HETATM 1931  O   HOH A 756      -5.518  22.521  28.075  1.00 32.51           O  
HETATM 1932  O   HOH A 757       5.674  28.593  33.776  1.00 28.91           O  
HETATM 1933  O   HOH A 758       4.368  29.727  35.857  1.00 34.72           O  
HETATM 1934  O   HOH A 759       8.909  13.427   8.751  1.00 31.73           O  
HETATM 1935  O   HOH A 760      -4.486  22.860  30.688  1.00 48.55           O  
HETATM 1936  O   HOH A 762      26.371  26.391  13.353  1.00 52.65           O  
HETATM 1937  O   HOH A 763     -15.943  40.200  21.430  1.00 35.78           O  
HETATM 1938  O   HOH A 764       2.690  49.670   4.927  1.00 42.35           O  
HETATM 1939  O   HOH A 765     -16.791  31.841  13.616  1.00 32.85           O  
HETATM 1940  O   HOH A 766      11.498  11.725  -2.433  1.00 30.67           O  
HETATM 1941  O   HOH A 767     -11.521  21.502  22.409  1.00 28.16           O  
CONECT  124 1694                                                                
CONECT  393 1694                                                                
CONECT  864 1694                                                                
CONECT 1694  124  393  864 1698                                                 
CONECT 1694 1703 1823                                                           
CONECT 1695 1699 1704 1823 1826                                                 
CONECT 1695 1924 1925                                                           
CONECT 1696 1697 1698 1699 1700                                                 
CONECT 1697 1696                                                                
CONECT 1698 1694 1696                                                           
CONECT 1699 1695 1696                                                           
CONECT 1700 1696                                                                
CONECT 1701 1702 1703 1704 1708                                                 
CONECT 1702 1701                                                                
CONECT 1703 1694 1701                                                           
CONECT 1704 1695 1701                                                           
CONECT 1705 1706 1707 1708 1709                                                 
CONECT 1706 1705                                                                
CONECT 1707 1705                                                                
CONECT 1708 1701 1705                                                           
CONECT 1709 1705 1710                                                           
CONECT 1710 1709 1711                                                           
CONECT 1711 1710 1712 1713                                                      
CONECT 1712 1711 1717                                                           
CONECT 1713 1711 1714 1715                                                      
CONECT 1714 1713                                                                
CONECT 1715 1713 1716 1717                                                      
CONECT 1716 1715                                                                
CONECT 1717 1712 1715 1718                                                      
CONECT 1718 1717 1719 1727                                                      
CONECT 1719 1718 1720                                                           
CONECT 1720 1719 1721                                                           
CONECT 1721 1720 1722 1727                                                      
CONECT 1722 1721 1723 1724                                                      
CONECT 1723 1722                                                                
CONECT 1724 1722 1725                                                           
CONECT 1725 1724 1726                                                           
CONECT 1726 1725 1727                                                           
CONECT 1727 1718 1721 1726                                                      
CONECT 1728 1729 1730 1733                                                      
CONECT 1729 1728                                                                
CONECT 1730 1728 1731                                                           
CONECT 1731 1730 1732 1735                                                      
CONECT 1732 1731 1733 1734                                                      
CONECT 1733 1728 1732                                                           
CONECT 1734 1732                                                                
CONECT 1735 1731 1736                                                           
CONECT 1736 1735 1737                                                           
CONECT 1737 1736 1738                                                           
CONECT 1738 1737 1739                                                           
CONECT 1739 1738 1740                                                           
CONECT 1740 1739 1741 1742                                                      
CONECT 1741 1740                                                                
CONECT 1742 1740                                                                
CONECT 1823 1694 1695                                                           
CONECT 1826 1695                                                                
CONECT 1924 1695                                                                
CONECT 1925 1695                                                                
MASTER      293    0    5   10   10    0   18    6 1940    1   58   18          
END                                                                             
