HEADER    HYDROLASE(O-GLYCOSYL)                   27-MAR-92   1LHJ              
TITLE     ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING      
TITLE    2 CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE 
TITLE    3 MUTANTS                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMAN LYSOZYME;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.17;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    HYDROLASE(O-GLYCOSYL)                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.INAKA,M.MATSUSHIMA,T.HERNING,R.KUROKI,K.YUTANI,M.KIKUCHI            
REVDAT   3   29-NOV-17 1LHJ    1       HELIX                                    
REVDAT   2   24-FEB-09 1LHJ    1       VERSN                                    
REVDAT   1   31-JAN-94 1LHJ    0                                                
JRNL        AUTH   T.HERNING,K.YUTANI,K.INAKA,R.KUROKI,M.MATSUSHIMA,M.KIKUCHI   
JRNL        TITL   ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A      
JRNL        TITL 2 SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE    
JRNL        TITL 3 ANALYSIS OF PROLINE MUTANTS.                                 
JRNL        REF    BIOCHEMISTRY                  V.  31  7077 1992              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   1643041                                                      
JRNL        DOI    10.1021/BI00146A008                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.INAKA,R.KUROKI,M.KIKUCHI,M.MATSUSHIMA                      
REMARK   1  TITL   CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES 
REMARK   1  TITL 2 WITH AN INTRODUCED CA BINDING SITE                           
REMARK   1  REF    J.BIOL.CHEM.                  V. 266 20666 1991              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   T.HERNING,K.YUTANI,Y.TANIYAMA,M.KIKUCHI                      
REMARK   1  TITL   EFFECTS OF PROLINE MUTATIONS ON THE UNFOLDING AND REFOLDING  
REMARK   1  TITL 2 OF HUMAN LYSOZYME: THE SLOW REFOLDING KINITICS PHASE DOES    
REMARK   1  TITL 3 NOT RESULT FROM PROLINE CIS-TRANS ISOMERIZATION              
REMARK   1  REF    BIOCHEMISTRY                  V.  30  9882 1991              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   T.HERNING,K.YUTANI,K.INAKA,R.KUROKI,M.MATSUSHIMA,M.KIKUCHI   
REMARK   1  TITL   ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A      
REMARK   1  TITL 2 SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE    
REMARK   1  TITL 3 ANALYSIS OF PROLINE MUTANTS                                  
REMARK   1  REF    BIOCHEMISTRY                  V.  31  7077 1992              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 9358                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.152                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1026                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.017 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000174722.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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   (%): 38.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.23000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       16.92000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.60500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       16.92000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.23000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.60500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG A   115     O    HOH A   200              1.82            
REMARK 500   O    VAL A    74     O    HOH A   233              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   203     O    HOH A   215     4457     1.57            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A   7   CG  -  CD  -  OE2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG A  14   CD  -  NE  -  CZ  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ARG A  14   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A  14   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ASP A  18   CB  -  CG  -  OD1 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG A  41   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A  50   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A  53   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG A  98   CD  -  NE  -  CZ  ANGL. DEV. =  35.4 DEGREES          
REMARK 500    ARG A 101   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 101   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    GLY A 103   C   -  N   -  CA  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG A 115   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 115   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ASP A 120   CB  -  CG  -  OD2 ANGL. DEV. =  -7.1 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    ARG A 101        9.41    -63.13                                   
REMARK 500    GLN A 104      -39.69   -140.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1LHJ A    1   130  UNP    P61626   LYSC_HUMAN      19    148             
SEQADV 1LHJ GLY A  103  UNP  P61626    PRO   121 CONFLICT                       
SEQRES   1 A  130  LYS VAL PHE GLU ARG CYS GLU LEU ALA ARG THR LEU LYS          
SEQRES   2 A  130  ARG LEU GLY MET ASP GLY TYR ARG GLY ILE SER LEU ALA          
SEQRES   3 A  130  ASN TRP MET CYS LEU ALA LYS TRP GLU SER GLY TYR ASN          
SEQRES   4 A  130  THR ARG ALA THR ASN TYR ASN ALA GLY ASP ARG SER THR          
SEQRES   5 A  130  ASP TYR GLY ILE PHE GLN ILE ASN SER ARG TYR TRP CYS          
SEQRES   6 A  130  ASN ASP GLY LYS THR PRO GLY ALA VAL ASN ALA CYS HIS          
SEQRES   7 A  130  LEU SER CYS SER ALA LEU LEU GLN ASP ASN ILE ALA ASP          
SEQRES   8 A  130  ALA VAL ALA CYS ALA LYS ARG VAL VAL ARG ASP GLY GLN          
SEQRES   9 A  130  GLY ILE ARG ALA TRP VAL ALA TRP ARG ASN ARG CYS GLN          
SEQRES  10 A  130  ASN ARG ASP VAL ARG GLN TYR VAL GLN GLY CYS GLY VAL          
FORMUL   2  HOH   *128(H2 O)                                                    
HELIX    1   A ARG A    5  ARG A   14  1                                  10    
HELIX    2   B LEU A   25  GLU A   35  1                                  11    
HELIX    3   E SER A   80  LEU A   85  5                                   6    
HELIX    4   C ALA A   90  VAL A   99  1                                  10    
HELIX    5   D VAL A  110  CYS A  116  1                                   7    
SHEET    1   A 2 LYS A   1  PHE A   3  0                                        
SHEET    2   A 2 TYR A  38  THR A  40 -1  N  THR A  40   O  LYS A   1           
SHEET    1   B 3 ALA A  42  ASN A  46  0                                        
SHEET    2   B 3 SER A  51  GLY A  55 -1  N  GLY A  55   O  ALA A  42           
SHEET    3   B 3 ILE A  59  SER A  61 -1  N  SER A  61   O  THR A  52           
SSBOND   1 CYS A    6    CYS A  128                          1555   1555  2.03  
SSBOND   2 CYS A   30    CYS A  116                          1555   1555  2.06  
SSBOND   3 CYS A   65    CYS A   81                          1555   1555  2.01  
SSBOND   4 CYS A   77    CYS A   95                          1555   1555  2.03  
CRYST1   56.460   61.210   33.840  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017712  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016337  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029551        0.00000                         
ATOM      1  N   LYS A   1       0.818  19.582  23.338  1.00 11.97           N  
ATOM      2  CA  LYS A   1       1.403  20.465  22.267  1.00 11.11           C  
ATOM      3  C   LYS A   1       2.676  19.863  21.671  1.00 11.19           C  
ATOM      4  O   LYS A   1       3.474  19.214  22.397  1.00 10.41           O  
ATOM      5  CB  LYS A   1       1.693  21.816  22.869  1.00 12.39           C  
ATOM      6  CG  LYS A   1       2.762  22.666  22.250  1.00 14.64           C  
ATOM      7  CD  LYS A   1       2.939  23.961  23.056  1.00 15.11           C  
ATOM      8  CE  LYS A   1       4.053  24.776  22.380  1.00 17.75           C  
ATOM      9  NZ  LYS A   1       3.876  26.180  22.782  1.00 21.18           N  
ATOM     10  N   VAL A   2       2.793  20.075  20.348  1.00  9.79           N  
ATOM     11  CA  VAL A   2       3.992  19.617  19.639  1.00 10.31           C  
ATOM     12  C   VAL A   2       4.833  20.890  19.397  1.00 10.71           C  
ATOM     13  O   VAL A   2       4.331  21.712  18.602  1.00 10.80           O  
ATOM     14  CB  VAL A   2       3.669  18.833  18.340  1.00 10.43           C  
ATOM     15  CG1 VAL A   2       4.917  18.567  17.522  1.00 11.77           C  
ATOM     16  CG2 VAL A   2       2.956  17.526  18.607  1.00 11.72           C  
ATOM     17  N   PHE A   3       5.966  21.056  20.058  1.00  9.52           N  
ATOM     18  CA  PHE A   3       6.795  22.253  19.796  1.00 10.41           C  
ATOM     19  C   PHE A   3       7.559  22.135  18.477  1.00 10.47           C  
ATOM     20  O   PHE A   3       7.900  21.084  17.968  1.00  9.02           O  
ATOM     21  CB  PHE A   3       7.873  22.398  20.900  1.00 10.64           C  
ATOM     22  CG  PHE A   3       7.434  22.943  22.225  1.00  9.89           C  
ATOM     23  CD1 PHE A   3       7.672  24.302  22.507  1.00 11.82           C  
ATOM     24  CD2 PHE A   3       6.819  22.149  23.185  1.00  9.97           C  
ATOM     25  CE1 PHE A   3       7.307  24.847  23.729  1.00  9.97           C  
ATOM     26  CE2 PHE A   3       6.425  22.682  24.413  1.00 11.51           C  
ATOM     27  CZ  PHE A   3       6.677  24.044  24.671  1.00 13.20           C  
ATOM     28  N   GLU A   4       7.845  23.321  17.881  1.00 10.81           N  
ATOM     29  CA  GLU A   4       8.701  23.434  16.700  1.00 11.23           C  
ATOM     30  C   GLU A   4      10.088  23.512  17.377  1.00 10.18           C  
ATOM     31  O   GLU A   4      10.147  23.976  18.543  1.00  9.35           O  
ATOM     32  CB  GLU A   4       8.523  24.683  15.865  1.00 17.94           C  
ATOM     33  CG  GLU A   4       7.052  25.063  15.708  1.00 26.14           C  
ATOM     34  CD  GLU A   4       6.508  25.016  14.311  1.00 30.85           C  
ATOM     35  OE1 GLU A   4       6.108  26.070  13.806  1.00 33.88           O  
ATOM     36  OE2 GLU A   4       6.506  23.856  13.822  1.00 34.22           O  
ATOM     37  N   ARG A   5      11.063  23.048  16.665  1.00  9.24           N  
ATOM     38  CA  ARG A   5      12.439  22.990  17.172  1.00  9.66           C  
ATOM     39  C   ARG A   5      12.922  24.302  17.822  1.00 10.30           C  
ATOM     40  O   ARG A   5      13.272  24.328  19.009  1.00  8.13           O  
ATOM     41  CB  ARG A   5      13.355  22.627  15.980  1.00  9.85           C  
ATOM     42  CG  ARG A   5      14.802  22.352  16.375  1.00 10.70           C  
ATOM     43  CD  ARG A   5      15.604  21.890  15.194  1.00 12.26           C  
ATOM     44  NE  ARG A   5      15.596  22.838  14.092  1.00 12.46           N  
ATOM     45  CZ  ARG A   5      16.534  23.757  13.884  1.00 15.59           C  
ATOM     46  NH1 ARG A   5      16.484  24.573  12.838  1.00 16.45           N  
ATOM     47  NH2 ARG A   5      17.579  23.941  14.710  1.00 16.26           N  
ATOM     48  N   CYS A   6      12.997  25.387  17.023  1.00  8.66           N  
ATOM     49  CA  CYS A   6      13.514  26.650  17.621  1.00  9.01           C  
ATOM     50  C   CYS A   6      12.710  27.228  18.747  1.00  9.59           C  
ATOM     51  O   CYS A   6      13.310  27.825  19.698  1.00  7.54           O  
ATOM     52  CB  CYS A   6      13.890  27.649  16.514  1.00  9.61           C  
ATOM     53  SG  CYS A   6      15.300  27.039  15.533  1.00 11.24           S  
ATOM     54  N   GLU A   7      11.392  27.056  18.666  1.00  9.17           N  
ATOM     55  CA  GLU A   7      10.517  27.557  19.763  1.00  9.70           C  
ATOM     56  C   GLU A   7      10.902  26.873  21.069  1.00  9.18           C  
ATOM     57  O   GLU A   7      11.033  27.458  22.138  1.00  9.08           O  
ATOM     58  CB  GLU A   7       9.080  27.255  19.428  1.00 11.52           C  
ATOM     59  CG  GLU A   7       7.926  27.645  20.316  1.00 16.96           C  
ATOM     60  CD  GLU A   7       6.647  26.850  20.120  1.00 19.96           C  
ATOM     61  OE1 GLU A   7       6.495  25.853  19.376  1.00 19.56           O  
ATOM     62  OE2 GLU A   7       5.798  27.348  20.918  1.00 20.31           O  
ATOM     63  N   LEU A   8      11.076  25.534  21.003  1.00  7.81           N  
ATOM     64  CA  LEU A   8      11.431  24.785  22.221  1.00  7.48           C  
ATOM     65  C   LEU A   8      12.808  25.188  22.713  1.00  5.00           C  
ATOM     66  O   LEU A   8      13.001  25.296  23.920  1.00  6.83           O  
ATOM     67  CB  LEU A   8      11.341  23.251  21.896  1.00  7.81           C  
ATOM     68  CG  LEU A   8      11.840  22.359  23.013  1.00  8.82           C  
ATOM     69  CD1 LEU A   8      10.999  22.460  24.291  1.00  8.74           C  
ATOM     70  CD2 LEU A   8      11.915  20.885  22.571  1.00  8.68           C  
ATOM     71  N   ALA A   9      13.744  25.399  21.823  1.00  6.47           N  
ATOM     72  CA  ALA A   9      15.141  25.737  22.179  1.00  7.51           C  
ATOM     73  C   ALA A   9      15.170  27.045  23.000  1.00  8.50           C  
ATOM     74  O   ALA A   9      15.881  27.118  24.026  1.00  8.21           O  
ATOM     75  CB  ALA A   9      16.012  25.821  20.941  1.00  9.27           C  
ATOM     76  N   ARG A  10      14.395  27.985  22.505  1.00  8.27           N  
ATOM     77  CA  ARG A  10      14.307  29.301  23.204  1.00  8.44           C  
ATOM     78  C   ARG A  10      13.606  29.131  24.525  1.00  7.76           C  
ATOM     79  O   ARG A  10      14.016  29.817  25.493  1.00  7.68           O  
ATOM     80  CB  ARG A  10      13.637  30.369  22.322  1.00  6.25           C  
ATOM     81  CG  ARG A  10      14.561  30.743  21.156  1.00  8.22           C  
ATOM     82  CD  ARG A  10      14.016  31.874  20.332  1.00 10.81           C  
ATOM     83  NE  ARG A  10      12.701  31.529  19.740  1.00 10.69           N  
ATOM     84  CZ  ARG A  10      12.633  31.126  18.448  1.00  8.93           C  
ATOM     85  NH1 ARG A  10      11.470  30.914  17.888  1.00 10.59           N  
ATOM     86  NH2 ARG A  10      13.737  31.011  17.719  1.00  9.68           N  
ATOM     87  N   THR A  11      12.607  28.282  24.567  1.00  8.12           N  
ATOM     88  CA  THR A  11      11.866  28.015  25.834  1.00  7.96           C  
ATOM     89  C   THR A  11      12.790  27.409  26.863  1.00  8.61           C  
ATOM     90  O   THR A  11      12.750  27.862  28.028  1.00  8.23           O  
ATOM     91  CB  THR A  11      10.574  27.143  25.592  1.00  9.47           C  
ATOM     92  OG1 THR A  11       9.768  27.880  24.653  1.00 10.06           O  
ATOM     93  CG2 THR A  11       9.757  26.853  26.872  1.00  9.14           C  
ATOM     94  N   LEU A  12      13.586  26.418  26.427  1.00  8.28           N  
ATOM     95  CA  LEU A  12      14.552  25.770  27.325  1.00  8.59           C  
ATOM     96  C   LEU A  12      15.611  26.727  27.834  1.00  9.61           C  
ATOM     97  O   LEU A  12      16.026  26.616  29.011  1.00  9.56           O  
ATOM     98  CB  LEU A  12      15.196  24.508  26.664  1.00  7.46           C  
ATOM     99  CG  LEU A  12      14.180  23.374  26.403  1.00  9.91           C  
ATOM    100  CD1 LEU A  12      14.873  22.159  25.751  1.00 11.06           C  
ATOM    101  CD2 LEU A  12      13.474  22.883  27.677  1.00 11.39           C  
ATOM    102  N   LYS A  13      16.083  27.583  26.924  1.00  9.25           N  
ATOM    103  CA  LYS A  13      17.134  28.532  27.383  1.00  9.81           C  
ATOM    104  C   LYS A  13      16.538  29.429  28.480  1.00  8.77           C  
ATOM    105  O   LYS A  13      17.217  29.653  29.488  1.00  9.58           O  
ATOM    106  CB  LYS A  13      17.616  29.417  26.223  1.00 12.36           C  
ATOM    107  CG  LYS A  13      18.878  30.203  26.670  1.00 14.38           C  
ATOM    108  CD  LYS A  13      19.513  30.866  25.459  1.00 19.10           C  
ATOM    109  CE  LYS A  13      20.694  31.780  25.839  1.00 20.22           C  
ATOM    110  NZ  LYS A  13      21.654  30.870  26.560  1.00 24.30           N  
ATOM    111  N   ARG A  14      15.320  29.907  28.325  1.00  7.64           N  
ATOM    112  CA  ARG A  14      14.738  30.786  29.380  1.00 11.42           C  
ATOM    113  C   ARG A  14      14.549  30.090  30.711  1.00 10.69           C  
ATOM    114  O   ARG A  14      14.588  30.741  31.757  1.00  9.62           O  
ATOM    115  CB  ARG A  14      13.415  31.409  28.950  1.00 14.30           C  
ATOM    116  CG  ARG A  14      13.567  32.456  27.843  1.00 20.29           C  
ATOM    117  CD  ARG A  14      12.255  33.124  27.566  1.00 22.92           C  
ATOM    118  NE  ARG A  14      11.115  32.242  27.465  1.00 26.50           N  
ATOM    119  CZ  ARG A  14      10.434  31.712  26.457  1.00 27.28           C  
ATOM    120  NH1 ARG A  14      10.710  31.918  25.149  1.00 28.03           N  
ATOM    121  NH2 ARG A  14       9.399  30.917  26.814  1.00 25.76           N  
ATOM    122  N   LEU A  15      14.375  28.750  30.629  1.00 10.38           N  
ATOM    123  CA  LEU A  15      14.154  27.940  31.823  1.00 10.17           C  
ATOM    124  C   LEU A  15      15.450  27.530  32.494  1.00 10.82           C  
ATOM    125  O   LEU A  15      15.334  26.755  33.473  1.00 11.47           O  
ATOM    126  CB  LEU A  15      13.184  26.762  31.497  1.00  9.67           C  
ATOM    127  CG  LEU A  15      11.744  27.197  31.232  1.00 10.48           C  
ATOM    128  CD1 LEU A  15      10.901  26.051  30.704  1.00 11.94           C  
ATOM    129  CD2 LEU A  15      11.057  27.720  32.512  1.00 10.83           C  
ATOM    130  N   GLY A  16      16.572  27.994  31.983  1.00  8.87           N  
ATOM    131  CA  GLY A  16      17.862  27.742  32.609  1.00  8.90           C  
ATOM    132  C   GLY A  16      18.498  26.390  32.322  1.00  8.97           C  
ATOM    133  O   GLY A  16      19.340  25.971  33.148  1.00  9.20           O  
ATOM    134  N   MET A  17      18.154  25.818  31.189  1.00  8.87           N  
ATOM    135  CA  MET A  17      18.697  24.444  30.886  1.00 10.13           C  
ATOM    136  C   MET A  17      20.042  24.469  30.221  1.00  9.84           C  
ATOM    137  O   MET A  17      20.710  23.400  30.173  1.00 10.54           O  
ATOM    138  CB  MET A  17      17.682  23.673  30.024  1.00  9.50           C  
ATOM    139  CG  MET A  17      16.400  23.439  30.810  1.00 14.45           C  
ATOM    140  SD  MET A  17      16.802  22.032  31.910  1.00 17.25           S  
ATOM    141  CE  MET A  17      16.183  20.673  30.874  1.00 18.79           C  
ATOM    142  N   ASP A  18      20.422  25.595  29.663  1.00 10.11           N  
ATOM    143  CA  ASP A  18      21.727  25.626  28.972  1.00 11.21           C  
ATOM    144  C   ASP A  18      22.903  25.558  29.936  1.00 11.18           C  
ATOM    145  O   ASP A  18      23.281  26.475  30.710  1.00 10.64           O  
ATOM    146  CB  ASP A  18      21.800  26.778  27.949  1.00 13.24           C  
ATOM    147  CG  ASP A  18      22.986  26.625  26.999  1.00 15.25           C  
ATOM    148  OD1 ASP A  18      23.513  25.560  26.616  1.00 13.94           O  
ATOM    149  OD2 ASP A  18      23.457  27.705  26.572  1.00 17.34           O  
ATOM    150  N   GLY A  19      23.565  24.383  29.870  1.00  9.96           N  
ATOM    151  CA  GLY A  19      24.730  24.083  30.715  1.00 10.31           C  
ATOM    152  C   GLY A  19      24.364  23.656  32.148  1.00 10.88           C  
ATOM    153  O   GLY A  19      25.254  23.637  33.015  1.00 10.82           O  
ATOM    154  N   TYR A  20      23.116  23.315  32.397  1.00 10.06           N  
ATOM    155  CA  TYR A  20      22.624  22.873  33.718  1.00  9.97           C  
ATOM    156  C   TYR A  20      23.397  21.583  34.033  1.00  9.57           C  
ATOM    157  O   TYR A  20      23.337  20.632  33.240  1.00  7.88           O  
ATOM    158  CB  TYR A  20      21.094  22.625  33.698  1.00 10.27           C  
ATOM    159  CG  TYR A  20      20.649  22.256  35.104  1.00 10.64           C  
ATOM    160  CD1 TYR A  20      20.460  23.267  36.048  1.00 11.96           C  
ATOM    161  CD2 TYR A  20      20.488  20.941  35.515  1.00 12.28           C  
ATOM    162  CE1 TYR A  20      20.104  22.956  37.363  1.00 13.94           C  
ATOM    163  CE2 TYR A  20      20.097  20.629  36.816  1.00 12.90           C  
ATOM    164  CZ  TYR A  20      19.915  21.633  37.732  1.00 13.49           C  
ATOM    165  OH  TYR A  20      19.576  21.330  39.018  1.00 15.91           O  
ATOM    166  N   ARG A  21      24.128  21.593  35.126  1.00 10.17           N  
ATOM    167  CA  ARG A  21      24.964  20.426  35.528  1.00 10.76           C  
ATOM    168  C   ARG A  21      25.815  19.893  34.384  1.00  9.60           C  
ATOM    169  O   ARG A  21      25.967  18.680  34.184  1.00  9.60           O  
ATOM    170  CB  ARG A  21      24.163  19.301  36.161  1.00 14.20           C  
ATOM    171  CG  ARG A  21      23.320  19.719  37.369  1.00 19.33           C  
ATOM    172  CD  ARG A  21      24.230  19.629  38.574  1.00 26.09           C  
ATOM    173  NE  ARG A  21      24.423  18.193  38.876  1.00 28.93           N  
ATOM    174  CZ  ARG A  21      25.292  17.636  39.713  1.00 29.14           C  
ATOM    175  NH1 ARG A  21      25.201  16.319  39.840  1.00 27.84           N  
ATOM    176  NH2 ARG A  21      26.219  18.345  40.384  1.00 29.59           N  
ATOM    177  N   GLY A  22      26.368  20.782  33.574  1.00  6.90           N  
ATOM    178  CA  GLY A  22      27.234  20.524  32.472  1.00  7.58           C  
ATOM    179  C   GLY A  22      26.649  20.068  31.189  1.00  6.99           C  
ATOM    180  O   GLY A  22      27.324  19.644  30.238  1.00  8.23           O  
ATOM    181  N   ILE A  23      25.323  20.175  31.135  1.00  8.35           N  
ATOM    182  CA  ILE A  23      24.605  19.707  29.914  1.00  8.53           C  
ATOM    183  C   ILE A  23      24.242  20.851  28.979  1.00  9.18           C  
ATOM    184  O   ILE A  23      23.419  21.664  29.381  1.00  9.12           O  
ATOM    185  CB  ILE A  23      23.307  18.896  30.317  1.00  7.61           C  
ATOM    186  CG1 ILE A  23      23.689  17.750  31.288  1.00  6.39           C  
ATOM    187  CG2 ILE A  23      22.564  18.429  29.033  1.00  7.95           C  
ATOM    188  CD1 ILE A  23      22.455  17.306  32.146  1.00  5.59           C  
ATOM    189  N   SER A  24      24.844  20.819  27.785  1.00  9.62           N  
ATOM    190  CA  SER A  24      24.514  21.896  26.818  1.00  7.90           C  
ATOM    191  C   SER A  24      23.081  21.733  26.319  1.00  8.89           C  
ATOM    192  O   SER A  24      22.395  20.657  26.288  1.00  7.83           O  
ATOM    193  CB  SER A  24      25.482  21.805  25.657  1.00  8.19           C  
ATOM    194  OG  SER A  24      25.125  20.769  24.762  1.00  9.43           O  
ATOM    195  N   LEU A  25      22.558  22.923  25.903  1.00  8.00           N  
ATOM    196  CA  LEU A  25      21.230  22.966  25.332  1.00  8.43           C  
ATOM    197  C   LEU A  25      20.974  21.954  24.199  1.00  9.13           C  
ATOM    198  O   LEU A  25      19.869  21.351  24.172  1.00  7.49           O  
ATOM    199  CB  LEU A  25      21.028  24.435  24.829  1.00  9.72           C  
ATOM    200  CG  LEU A  25      19.574  24.659  24.477  1.00 12.83           C  
ATOM    201  CD1 LEU A  25      18.626  24.459  25.653  1.00 12.85           C  
ATOM    202  CD2 LEU A  25      19.425  26.119  23.978  1.00 14.04           C  
ATOM    203  N   ALA A  26      21.942  21.803  23.284  1.00  9.02           N  
ATOM    204  CA  ALA A  26      21.807  20.897  22.131  1.00  7.23           C  
ATOM    205  C   ALA A  26      21.601  19.480  22.642  1.00  6.91           C  
ATOM    206  O   ALA A  26      20.874  18.752  21.934  1.00  7.18           O  
ATOM    207  CB  ALA A  26      22.993  21.010  21.189  1.00  9.15           C  
ATOM    208  N   ASN A  27      22.148  19.150  23.800  1.00  7.62           N  
ATOM    209  CA  ASN A  27      21.958  17.757  24.316  1.00  6.37           C  
ATOM    210  C   ASN A  27      20.525  17.566  24.767  1.00  6.81           C  
ATOM    211  O   ASN A  27      19.928  16.496  24.540  1.00  8.20           O  
ATOM    212  CB  ASN A  27      22.979  17.449  25.419  1.00  8.39           C  
ATOM    213  CG  ASN A  27      24.286  16.945  24.834  1.00 11.40           C  
ATOM    214  OD1 ASN A  27      24.337  15.845  24.215  1.00 10.80           O  
ATOM    215  ND2 ASN A  27      25.379  17.712  24.954  1.00 10.09           N  
ATOM    216  N   TRP A  28      19.965  18.543  25.422  1.00  7.02           N  
ATOM    217  CA  TRP A  28      18.567  18.477  25.902  1.00  7.36           C  
ATOM    218  C   TRP A  28      17.629  18.395  24.689  1.00  6.93           C  
ATOM    219  O   TRP A  28      16.633  17.689  24.769  1.00  5.72           O  
ATOM    220  CB  TRP A  28      18.255  19.733  26.742  1.00  7.32           C  
ATOM    221  CG  TRP A  28      18.885  19.811  28.084  1.00  8.14           C  
ATOM    222  CD1 TRP A  28      19.846  20.700  28.518  1.00  7.71           C  
ATOM    223  CD2 TRP A  28      18.584  18.990  29.203  1.00  7.87           C  
ATOM    224  NE1 TRP A  28      20.094  20.527  29.849  1.00  8.43           N  
ATOM    225  CE2 TRP A  28      19.343  19.476  30.307  1.00  8.61           C  
ATOM    226  CE3 TRP A  28      17.706  17.936  29.395  1.00  8.86           C  
ATOM    227  CZ2 TRP A  28      19.292  18.920  31.564  1.00  9.35           C  
ATOM    228  CZ3 TRP A  28      17.644  17.375  30.674  1.00  8.33           C  
ATOM    229  CH2 TRP A  28      18.414  17.830  31.733  1.00  9.51           C  
ATOM    230  N   MET A  29      17.944  19.110  23.636  1.00  7.16           N  
ATOM    231  CA  MET A  29      17.130  19.150  22.386  1.00  5.90           C  
ATOM    232  C   MET A  29      17.152  17.733  21.772  1.00  5.61           C  
ATOM    233  O   MET A  29      16.111  17.186  21.400  1.00  6.23           O  
ATOM    234  CB  MET A  29      17.614  20.224  21.434  1.00  6.63           C  
ATOM    235  CG  MET A  29      17.335  21.662  21.864  1.00  5.87           C  
ATOM    236  SD  MET A  29      15.539  21.951  21.886  1.00 10.10           S  
ATOM    237  CE  MET A  29      15.072  21.587  20.206  1.00  8.70           C  
ATOM    238  N   CYS A  30      18.372  17.217  21.743  1.00  5.79           N  
ATOM    239  CA  CYS A  30      18.570  15.843  21.179  1.00  7.68           C  
ATOM    240  C   CYS A  30      17.720  14.833  21.941  1.00  6.97           C  
ATOM    241  O   CYS A  30      17.004  13.989  21.387  1.00  6.63           O  
ATOM    242  CB  CYS A  30      20.070  15.482  21.195  1.00  7.60           C  
ATOM    243  SG  CYS A  30      20.353  13.892  20.271  1.00  8.95           S  
ATOM    244  N   LEU A  31      17.778  14.938  23.257  1.00  8.23           N  
ATOM    245  CA  LEU A  31      16.985  14.044  24.121  1.00  7.69           C  
ATOM    246  C   LEU A  31      15.511  14.242  23.848  1.00  8.88           C  
ATOM    247  O   LEU A  31      14.837  13.211  23.654  1.00  7.83           O  
ATOM    248  CB  LEU A  31      17.328  14.296  25.599  1.00  6.81           C  
ATOM    249  CG  LEU A  31      16.456  13.518  26.596  1.00  6.30           C  
ATOM    250  CD1 LEU A  31      16.771  12.034  26.553  1.00  9.40           C  
ATOM    251  CD2 LEU A  31      16.712  14.093  27.982  1.00  7.24           C  
ATOM    252  N   ALA A  32      15.021  15.496  23.853  1.00  6.34           N  
ATOM    253  CA  ALA A  32      13.547  15.645  23.633  1.00  7.41           C  
ATOM    254  C   ALA A  32      13.096  15.122  22.281  1.00  7.96           C  
ATOM    255  O   ALA A  32      11.965  14.613  22.169  1.00  6.54           O  
ATOM    256  CB  ALA A  32      13.219  17.144  23.834  1.00  8.74           C  
ATOM    257  N   LYS A  33      13.954  15.354  21.288  1.00  7.52           N  
ATOM    258  CA  LYS A  33      13.609  14.922  19.910  1.00  9.50           C  
ATOM    259  C   LYS A  33      13.377  13.391  19.857  1.00 10.05           C  
ATOM    260  O   LYS A  33      12.337  12.925  19.359  1.00  9.02           O  
ATOM    261  CB  LYS A  33      14.699  15.337  18.935  1.00 10.49           C  
ATOM    262  CG  LYS A  33      14.285  15.150  17.454  1.00 17.00           C  
ATOM    263  CD  LYS A  33      14.562  13.722  16.996  1.00 22.20           C  
ATOM    264  CE  LYS A  33      14.201  13.536  15.518  1.00 23.67           C  
ATOM    265  NZ  LYS A  33      14.612  12.137  15.161  1.00 28.19           N  
ATOM    266  N   TRP A  34      14.342  12.633  20.353  1.00 10.07           N  
ATOM    267  CA  TRP A  34      14.225  11.144  20.301  1.00 11.36           C  
ATOM    268  C   TRP A  34      13.254  10.597  21.329  1.00 11.67           C  
ATOM    269  O   TRP A  34      12.620   9.545  21.017  1.00 11.85           O  
ATOM    270  CB  TRP A  34      15.653  10.602  20.386  1.00 11.64           C  
ATOM    271  CG  TRP A  34      16.434  11.007  19.166  1.00 15.90           C  
ATOM    272  CD1 TRP A  34      17.413  11.961  19.059  1.00 16.14           C  
ATOM    273  CD2 TRP A  34      16.306  10.432  17.853  1.00 18.85           C  
ATOM    274  NE1 TRP A  34      17.884  12.024  17.770  1.00 16.92           N  
ATOM    275  CE2 TRP A  34      17.229  11.096  17.009  1.00 19.05           C  
ATOM    276  CE3 TRP A  34      15.495   9.404  17.329  1.00 21.08           C  
ATOM    277  CZ2 TRP A  34      17.346  10.783  15.668  1.00 19.82           C  
ATOM    278  CZ3 TRP A  34      15.626   9.084  15.975  1.00 21.76           C  
ATOM    279  CH2 TRP A  34      16.526   9.769  15.168  1.00 22.08           C  
ATOM    280  N   GLU A  35      13.063  11.272  22.462  1.00  9.60           N  
ATOM    281  CA  GLU A  35      12.132  10.699  23.448  1.00 10.84           C  
ATOM    282  C   GLU A  35      10.647  10.820  23.093  1.00 11.19           C  
ATOM    283  O   GLU A  35       9.869   9.861  23.228  1.00  8.78           O  
ATOM    284  CB  GLU A  35      12.369  11.212  24.867  1.00 11.54           C  
ATOM    285  CG  GLU A  35      13.670  10.716  25.540  1.00 14.15           C  
ATOM    286  CD  GLU A  35      13.558   9.311  26.096  1.00 17.05           C  
ATOM    287  OE1 GLU A  35      12.591   8.591  25.905  1.00 17.30           O  
ATOM    288  OE2 GLU A  35      14.564   8.993  26.754  1.00 17.95           O  
ATOM    289  N   SER A  36      10.230  12.004  22.651  1.00 10.40           N  
ATOM    290  CA  SER A  36       8.866  12.322  22.328  1.00  9.57           C  
ATOM    291  C   SER A  36       8.585  13.080  21.047  1.00 10.43           C  
ATOM    292  O   SER A  36       7.368  13.404  20.837  1.00 10.71           O  
ATOM    293  CB  SER A  36       8.366  13.270  23.477  1.00  9.87           C  
ATOM    294  OG  SER A  36       9.112  14.484  23.402  1.00  8.02           O  
ATOM    295  N   GLY A  37       9.567  13.390  20.248  1.00  9.88           N  
ATOM    296  CA  GLY A  37       9.296  14.208  19.035  1.00 10.23           C  
ATOM    297  C   GLY A  37       8.813  15.609  19.490  1.00 10.44           C  
ATOM    298  O   GLY A  37       8.026  16.227  18.751  1.00 10.83           O  
ATOM    299  N   TYR A  38       9.261  16.086  20.630  1.00  8.49           N  
ATOM    300  CA  TYR A  38       8.897  17.410  21.158  1.00  9.71           C  
ATOM    301  C   TYR A  38       7.412  17.526  21.482  1.00 10.31           C  
ATOM    302  O   TYR A  38       6.801  18.623  21.472  1.00  9.32           O  
ATOM    303  CB  TYR A  38       9.252  18.539  20.118  1.00  8.47           C  
ATOM    304  CG  TYR A  38      10.613  18.582  19.487  1.00  7.57           C  
ATOM    305  CD1 TYR A  38      10.775  18.837  18.133  1.00  8.54           C  
ATOM    306  CD2 TYR A  38      11.763  18.376  20.260  1.00  8.05           C  
ATOM    307  CE1 TYR A  38      12.028  18.915  17.533  1.00 11.28           C  
ATOM    308  CE2 TYR A  38      13.024  18.443  19.684  1.00  9.52           C  
ATOM    309  CZ  TYR A  38      13.165  18.717  18.325  1.00  9.55           C  
ATOM    310  OH  TYR A  38      14.434  18.757  17.805  1.00 10.81           O  
ATOM    311  N   ASN A  39       6.840  16.374  21.842  1.00  9.14           N  
ATOM    312  CA  ASN A  39       5.392  16.290  22.165  1.00  9.91           C  
ATOM    313  C   ASN A  39       5.132  16.207  23.675  1.00  9.35           C  
ATOM    314  O   ASN A  39       5.513  15.157  24.247  1.00  7.72           O  
ATOM    315  CB  ASN A  39       4.787  15.045  21.453  1.00 10.28           C  
ATOM    316  CG  ASN A  39       3.286  14.972  21.661  1.00 10.55           C  
ATOM    317  OD1 ASN A  39       2.627  15.774  22.337  1.00 10.06           O  
ATOM    318  ND2 ASN A  39       2.723  13.913  21.028  1.00 13.81           N  
ATOM    319  N   THR A  40       4.481  17.224  24.224  1.00  8.32           N  
ATOM    320  CA  THR A  40       4.263  17.213  25.686  1.00  9.76           C  
ATOM    321  C   THR A  40       3.209  16.192  26.152  1.00 10.55           C  
ATOM    322  O   THR A  40       3.152  15.962  27.372  1.00 12.12           O  
ATOM    323  CB  THR A  40       3.844  18.655  26.210  1.00  9.48           C  
ATOM    324  OG1 THR A  40       2.547  18.857  25.555  1.00 10.21           O  
ATOM    325  CG2 THR A  40       4.830  19.783  25.883  1.00 10.38           C  
ATOM    326  N   ARG A  41       2.432  15.641  25.241  1.00 10.70           N  
ATOM    327  CA  ARG A  41       1.378  14.689  25.596  1.00 13.55           C  
ATOM    328  C   ARG A  41       1.809  13.229  25.359  1.00 11.61           C  
ATOM    329  O   ARG A  41       0.972  12.333  25.528  1.00 12.66           O  
ATOM    330  CB  ARG A  41       0.037  14.951  24.854  1.00 17.50           C  
ATOM    331  CG  ARG A  41      -0.585  16.288  25.262  1.00 26.44           C  
ATOM    332  CD  ARG A  41      -1.934  16.544  24.674  1.00 33.70           C  
ATOM    333  NE  ARG A  41      -1.955  16.805  23.250  1.00 39.56           N  
ATOM    334  CZ  ARG A  41      -2.854  16.378  22.356  1.00 42.25           C  
ATOM    335  NH1 ARG A  41      -3.932  15.649  22.667  1.00 44.13           N  
ATOM    336  NH2 ARG A  41      -2.664  16.629  21.053  1.00 43.31           N  
ATOM    337  N   ALA A  42       3.033  13.024  24.978  1.00 11.42           N  
ATOM    338  CA  ALA A  42       3.466  11.636  24.705  1.00 12.20           C  
ATOM    339  C   ALA A  42       3.514  10.823  25.996  1.00 11.82           C  
ATOM    340  O   ALA A  42       3.923  11.273  27.067  1.00  9.98           O  
ATOM    341  CB  ALA A  42       4.811  11.627  24.001  1.00 12.29           C  
ATOM    342  N   THR A  43       3.093   9.562  25.808  1.00 12.56           N  
ATOM    343  CA  THR A  43       3.144   8.620  26.954  1.00 13.60           C  
ATOM    344  C   THR A  43       3.551   7.247  26.363  1.00 14.50           C  
ATOM    345  O   THR A  43       3.188   6.972  25.203  1.00 14.86           O  
ATOM    346  CB  THR A  43       1.880   8.473  27.828  1.00 15.68           C  
ATOM    347  OG1 THR A  43       0.917   7.831  26.925  1.00 19.39           O  
ATOM    348  CG2 THR A  43       1.292   9.752  28.422  1.00 18.42           C  
ATOM    349  N   ASN A  44       4.295   6.512  27.172  1.00 13.78           N  
ATOM    350  CA  ASN A  44       4.731   5.177  26.761  1.00 14.12           C  
ATOM    351  C   ASN A  44       4.487   4.250  27.959  1.00 13.01           C  
ATOM    352  O   ASN A  44       5.117   4.442  28.983  1.00 11.44           O  
ATOM    353  CB  ASN A  44       6.207   5.180  26.351  1.00 17.06           C  
ATOM    354  CG  ASN A  44       6.708   3.730  26.180  1.00 20.96           C  
ATOM    355  OD1 ASN A  44       6.670   3.202  25.072  1.00 21.54           O  
ATOM    356  ND2 ASN A  44       7.102   3.110  27.291  1.00 21.49           N  
ATOM    357  N   TYR A  45       3.632   3.260  27.796  1.00 14.12           N  
ATOM    358  CA  TYR A  45       3.443   2.288  28.921  1.00 14.10           C  
ATOM    359  C   TYR A  45       4.449   1.151  28.737  1.00 14.33           C  
ATOM    360  O   TYR A  45       4.615   0.583  27.636  1.00 14.38           O  
ATOM    361  CB  TYR A  45       1.990   1.819  28.939  1.00 14.50           C  
ATOM    362  CG  TYR A  45       1.748   0.716  29.929  1.00 14.48           C  
ATOM    363  CD1 TYR A  45       1.517  -0.620  29.446  1.00 15.66           C  
ATOM    364  CD2 TYR A  45       1.756   0.985  31.274  1.00 14.36           C  
ATOM    365  CE1 TYR A  45       1.259  -1.658  30.364  1.00 15.77           C  
ATOM    366  CE2 TYR A  45       1.526  -0.050  32.208  1.00 16.04           C  
ATOM    367  CZ  TYR A  45       1.283  -1.359  31.725  1.00 14.76           C  
ATOM    368  OH  TYR A  45       1.061  -2.275  32.706  1.00 15.87           O  
ATOM    369  N   ASN A  46       5.170   0.806  29.780  1.00 13.78           N  
ATOM    370  CA  ASN A  46       6.172  -0.290  29.768  1.00 15.29           C  
ATOM    371  C   ASN A  46       5.437  -1.516  30.365  1.00 14.47           C  
ATOM    372  O   ASN A  46       5.381  -1.636  31.584  1.00 14.17           O  
ATOM    373  CB  ASN A  46       7.450   0.067  30.526  1.00 16.41           C  
ATOM    374  CG  ASN A  46       8.048   1.393  30.057  1.00 19.30           C  
ATOM    375  OD1 ASN A  46       8.514   1.384  28.897  1.00 19.09           O  
ATOM    376  ND2 ASN A  46       8.001   2.466  30.827  1.00 17.73           N  
ATOM    377  N   ALA A  47       4.911  -2.311  29.466  1.00 15.84           N  
ATOM    378  CA  ALA A  47       4.157  -3.533  29.865  1.00 17.29           C  
ATOM    379  C   ALA A  47       4.966  -4.452  30.785  1.00 14.85           C  
ATOM    380  O   ALA A  47       4.371  -5.088  31.662  1.00 16.16           O  
ATOM    381  CB  ALA A  47       3.764  -4.351  28.627  1.00 17.58           C  
ATOM    382  N   GLY A  48       6.239  -4.489  30.502  1.00 15.51           N  
ATOM    383  CA  GLY A  48       7.229  -5.292  31.234  1.00 15.37           C  
ATOM    384  C   GLY A  48       7.405  -5.003  32.701  1.00 15.46           C  
ATOM    385  O   GLY A  48       7.624  -5.948  33.514  1.00 14.68           O  
ATOM    386  N   ASP A  49       7.310  -3.705  33.086  1.00 13.58           N  
ATOM    387  CA  ASP A  49       7.497  -3.384  34.513  1.00 12.82           C  
ATOM    388  C   ASP A  49       6.338  -2.585  35.117  1.00 11.50           C  
ATOM    389  O   ASP A  49       6.442  -2.260  36.329  1.00 12.12           O  
ATOM    390  CB  ASP A  49       8.888  -2.845  34.803  1.00 13.43           C  
ATOM    391  CG  ASP A  49       8.972  -1.346  34.580  1.00 18.01           C  
ATOM    392  OD1 ASP A  49       8.172  -0.861  33.778  1.00 16.48           O  
ATOM    393  OD2 ASP A  49       9.741  -0.675  35.312  1.00 21.28           O  
ATOM    394  N   ARG A  50       5.296  -2.318  34.377  1.00 10.49           N  
ATOM    395  CA  ARG A  50       4.100  -1.636  34.853  1.00 12.19           C  
ATOM    396  C   ARG A  50       4.322  -0.144  35.139  1.00 12.42           C  
ATOM    397  O   ARG A  50       3.506   0.507  35.808  1.00 14.28           O  
ATOM    398  CB  ARG A  50       3.491  -2.363  36.076  1.00 12.98           C  
ATOM    399  CG  ARG A  50       2.956  -3.765  35.674  1.00 17.64           C  
ATOM    400  CD  ARG A  50       2.198  -4.379  36.825  1.00 21.78           C  
ATOM    401  NE  ARG A  50       1.790  -5.751  36.530  1.00 26.45           N  
ATOM    402  CZ  ARG A  50       0.719  -6.152  35.831  1.00 27.14           C  
ATOM    403  NH1 ARG A  50      -0.142  -5.303  35.227  1.00 28.80           N  
ATOM    404  NH2 ARG A  50       0.447  -7.449  35.812  1.00 25.54           N  
ATOM    405  N   SER A  51       5.409   0.393  34.615  1.00 12.13           N  
ATOM    406  CA  SER A  51       5.663   1.860  34.809  1.00 10.41           C  
ATOM    407  C   SER A  51       5.254   2.551  33.511  1.00 10.26           C  
ATOM    408  O   SER A  51       5.056   1.901  32.457  1.00  9.35           O  
ATOM    409  CB  SER A  51       7.147   2.019  35.130  1.00  9.04           C  
ATOM    410  OG  SER A  51       7.998   1.840  34.010  1.00  7.94           O  
ATOM    411  N   THR A  52       5.157   3.889  33.536  1.00  9.06           N  
ATOM    412  CA  THR A  52       4.819   4.654  32.309  1.00  7.69           C  
ATOM    413  C   THR A  52       5.755   5.889  32.235  1.00  8.58           C  
ATOM    414  O   THR A  52       6.113   6.402  33.313  1.00  8.68           O  
ATOM    415  CB  THR A  52       3.355   5.222  32.358  1.00  9.71           C  
ATOM    416  OG1 THR A  52       2.498   4.029  32.514  1.00 10.59           O  
ATOM    417  CG2 THR A  52       2.897   6.001  31.116  1.00  6.45           C  
ATOM    418  N   ASP A  53       6.094   6.252  31.035  1.00  8.09           N  
ATOM    419  CA  ASP A  53       6.980   7.389  30.711  1.00  7.25           C  
ATOM    420  C   ASP A  53       6.074   8.529  30.226  1.00  6.74           C  
ATOM    421  O   ASP A  53       5.241   8.245  29.383  1.00  7.11           O  
ATOM    422  CB  ASP A  53       8.038   7.032  29.684  1.00 10.49           C  
ATOM    423  CG  ASP A  53       8.907   5.856  30.128  1.00 10.54           C  
ATOM    424  OD1 ASP A  53       9.316   5.804  31.265  1.00 11.81           O  
ATOM    425  OD2 ASP A  53       9.113   5.075  29.202  1.00 14.57           O  
ATOM    426  N   TYR A  54       6.314   9.698  30.819  1.00  6.00           N  
ATOM    427  CA  TYR A  54       5.435  10.836  30.548  1.00  7.11           C  
ATOM    428  C   TYR A  54       6.116  12.105  30.030  1.00  7.51           C  
ATOM    429  O   TYR A  54       7.194  12.489  30.530  1.00  8.92           O  
ATOM    430  CB  TYR A  54       4.871  11.240  31.969  1.00  7.28           C  
ATOM    431  CG  TYR A  54       3.859  10.258  32.534  1.00  8.21           C  
ATOM    432  CD1 TYR A  54       2.518  10.310  32.156  1.00  7.97           C  
ATOM    433  CD2 TYR A  54       4.270   9.228  33.404  1.00  8.83           C  
ATOM    434  CE1 TYR A  54       1.587   9.415  32.695  1.00  8.39           C  
ATOM    435  CE2 TYR A  54       3.346   8.312  33.929  1.00  8.57           C  
ATOM    436  CZ  TYR A  54       2.008   8.397  33.551  1.00  9.01           C  
ATOM    437  OH  TYR A  54       1.084   7.520  34.073  1.00  9.94           O  
ATOM    438  N   GLY A  55       5.425  12.691  29.048  1.00  8.82           N  
ATOM    439  CA  GLY A  55       5.869  14.022  28.566  1.00  8.65           C  
ATOM    440  C   GLY A  55       6.990  14.092  27.601  1.00  7.89           C  
ATOM    441  O   GLY A  55       7.534  13.084  27.070  1.00  6.64           O  
ATOM    442  N   ILE A  56       7.402  15.373  27.409  1.00  6.38           N  
ATOM    443  CA  ILE A  56       8.472  15.679  26.438  1.00  5.91           C  
ATOM    444  C   ILE A  56       9.805  14.998  26.725  1.00  5.59           C  
ATOM    445  O   ILE A  56      10.530  14.721  25.719  1.00  7.19           O  
ATOM    446  CB  ILE A  56       8.517  17.264  26.383  1.00  6.07           C  
ATOM    447  CG1 ILE A  56       9.187  17.727  25.087  1.00 10.10           C  
ATOM    448  CG2 ILE A  56       9.038  17.847  27.696  1.00  7.46           C  
ATOM    449  CD1 ILE A  56       8.775  19.216  24.719  1.00  9.46           C  
ATOM    450  N   PHE A  57      10.095  14.753  27.997  1.00  7.32           N  
ATOM    451  CA  PHE A  57      11.382  14.090  28.346  1.00  8.19           C  
ATOM    452  C   PHE A  57      11.144  12.601  28.701  1.00  9.58           C  
ATOM    453  O   PHE A  57      12.146  11.962  29.143  1.00  9.53           O  
ATOM    454  CB  PHE A  57      12.075  14.799  29.516  1.00  8.95           C  
ATOM    455  CG  PHE A  57      12.492  16.217  29.160  1.00 11.80           C  
ATOM    456  CD1 PHE A  57      11.868  17.294  29.864  1.00 13.64           C  
ATOM    457  CD2 PHE A  57      13.457  16.453  28.208  1.00 13.24           C  
ATOM    458  CE1 PHE A  57      12.173  18.593  29.509  1.00 14.41           C  
ATOM    459  CE2 PHE A  57      13.828  17.761  27.860  1.00 12.96           C  
ATOM    460  CZ  PHE A  57      13.162  18.815  28.561  1.00 13.95           C  
ATOM    461  N   GLN A  58       9.905  12.178  28.588  1.00  9.12           N  
ATOM    462  CA  GLN A  58       9.518  10.764  28.908  1.00  8.92           C  
ATOM    463  C   GLN A  58      10.079  10.358  30.260  1.00  8.02           C  
ATOM    464  O   GLN A  58      10.935   9.420  30.386  1.00  9.62           O  
ATOM    465  CB  GLN A  58       9.973   9.849  27.748  1.00  7.29           C  
ATOM    466  CG  GLN A  58       9.145   9.950  26.490  1.00  7.40           C  
ATOM    467  CD  GLN A  58       7.756   9.431  26.684  1.00  8.47           C  
ATOM    468  OE1 GLN A  58       7.550   8.208  26.538  1.00 11.39           O  
ATOM    469  NE2 GLN A  58       6.783  10.261  27.003  1.00  8.37           N  
ATOM    470  N   ILE A  59       9.641  11.023  31.300  1.00  7.00           N  
ATOM    471  CA  ILE A  59      10.099  10.799  32.699  1.00  7.83           C  
ATOM    472  C   ILE A  59       9.335   9.613  33.265  1.00  8.33           C  
ATOM    473  O   ILE A  59       8.104   9.567  33.075  1.00  8.08           O  
ATOM    474  CB  ILE A  59       9.933  12.140  33.470  1.00  8.73           C  
ATOM    475  CG1 ILE A  59      11.153  13.045  33.025  1.00 10.36           C  
ATOM    476  CG2 ILE A  59       9.916  11.969  35.012  1.00  9.60           C  
ATOM    477  CD1 ILE A  59      11.066  14.498  33.510  1.00  8.95           C  
ATOM    478  N   ASN A  60      10.040   8.680  33.900  1.00  7.73           N  
ATOM    479  CA  ASN A  60       9.360   7.431  34.375  1.00  8.71           C  
ATOM    480  C   ASN A  60       8.678   7.536  35.704  1.00  8.32           C  
ATOM    481  O   ASN A  60       9.155   8.195  36.655  1.00  9.08           O  
ATOM    482  CB  ASN A  60      10.420   6.313  34.268  1.00  9.48           C  
ATOM    483  CG  ASN A  60       9.868   4.908  34.553  1.00 10.60           C  
ATOM    484  OD1 ASN A  60       9.918   4.416  35.681  1.00 11.78           O  
ATOM    485  ND2 ASN A  60       9.335   4.299  33.507  1.00 11.30           N  
ATOM    486  N   SER A  61       7.532   6.817  35.788  1.00  8.02           N  
ATOM    487  CA  SER A  61       6.707   6.812  36.981  1.00  7.89           C  
ATOM    488  C   SER A  61       7.200   5.980  38.159  1.00  9.15           C  
ATOM    489  O   SER A  61       6.612   6.112  39.242  1.00  8.03           O  
ATOM    490  CB  SER A  61       5.265   6.389  36.620  1.00  8.98           C  
ATOM    491  OG  SER A  61       5.214   5.012  36.300  1.00  9.07           O  
ATOM    492  N   ARG A  62       8.227   5.170  37.988  1.00  9.79           N  
ATOM    493  CA  ARG A  62       8.692   4.354  39.124  1.00 12.05           C  
ATOM    494  C   ARG A  62       9.495   5.181  40.119  1.00 13.12           C  
ATOM    495  O   ARG A  62       9.412   4.994  41.351  1.00 12.55           O  
ATOM    496  CB  ARG A  62       9.526   3.160  38.633  1.00 13.64           C  
ATOM    497  CG  ARG A  62      10.298   2.422  39.710  1.00 17.05           C  
ATOM    498  CD  ARG A  62      10.640   1.015  39.394  1.00 18.93           C  
ATOM    499  NE  ARG A  62       9.651   0.299  38.584  1.00 20.99           N  
ATOM    500  CZ  ARG A  62       8.580  -0.276  39.181  1.00 22.35           C  
ATOM    501  NH1 ARG A  62       8.524  -0.313  40.522  1.00 22.27           N  
ATOM    502  NH2 ARG A  62       7.524  -0.665  38.461  1.00 20.91           N  
ATOM    503  N   TYR A  63      10.235   6.139  39.535  1.00 13.85           N  
ATOM    504  CA  TYR A  63      11.122   6.985  40.314  1.00 13.76           C  
ATOM    505  C   TYR A  63      10.847   8.443  40.511  1.00 13.86           C  
ATOM    506  O   TYR A  63      11.169   9.002  41.594  1.00 13.55           O  
ATOM    507  CB  TYR A  63      12.493   6.937  39.525  1.00 18.98           C  
ATOM    508  CG  TYR A  63      13.035   5.528  39.390  1.00 24.80           C  
ATOM    509  CD1 TYR A  63      13.073   4.824  38.188  1.00 26.49           C  
ATOM    510  CD2 TYR A  63      13.480   4.878  40.547  1.00 26.39           C  
ATOM    511  CE1 TYR A  63      13.595   3.524  38.133  1.00 29.01           C  
ATOM    512  CE2 TYR A  63      13.989   3.587  40.505  1.00 28.50           C  
ATOM    513  CZ  TYR A  63      14.040   2.914  39.299  1.00 29.72           C  
ATOM    514  OH  TYR A  63      14.568   1.636  39.356  1.00 32.84           O  
ATOM    515  N   TRP A  64      10.276   9.029  39.465  1.00 12.03           N  
ATOM    516  CA  TRP A  64      10.127  10.513  39.454  1.00 11.46           C  
ATOM    517  C   TRP A  64       8.807  11.152  39.706  1.00 11.24           C  
ATOM    518  O   TRP A  64       8.766  12.231  40.346  1.00 11.70           O  
ATOM    519  CB  TRP A  64      10.721  10.967  38.084  1.00 11.45           C  
ATOM    520  CG  TRP A  64      12.049  10.325  37.811  1.00 11.20           C  
ATOM    521  CD1 TRP A  64      12.321   9.367  36.894  1.00 11.86           C  
ATOM    522  CD2 TRP A  64      13.264  10.579  38.536  1.00 11.82           C  
ATOM    523  NE1 TRP A  64      13.655   8.986  37.019  1.00 14.34           N  
ATOM    524  CE2 TRP A  64      14.248   9.738  37.990  1.00 13.38           C  
ATOM    525  CE3 TRP A  64      13.585  11.476  39.565  1.00 12.77           C  
ATOM    526  CZ2 TRP A  64      15.560   9.722  38.456  1.00 14.11           C  
ATOM    527  CZ3 TRP A  64      14.902  11.443  40.037  1.00 15.61           C  
ATOM    528  CH2 TRP A  64      15.873  10.587  39.486  1.00 13.61           C  
ATOM    529  N   CYS A  65       7.729  10.570  39.191  1.00 10.76           N  
ATOM    530  CA  CYS A  65       6.399  11.224  39.411  1.00 10.06           C  
ATOM    531  C   CYS A  65       5.396  10.191  39.911  1.00 10.12           C  
ATOM    532  O   CYS A  65       5.630   8.990  39.674  1.00 11.18           O  
ATOM    533  CB  CYS A  65       5.962  11.908  38.118  1.00  8.16           C  
ATOM    534  SG  CYS A  65       5.647  10.830  36.691  1.00  9.13           S  
ATOM    535  N   ASN A  66       4.307  10.672  40.504  1.00  9.85           N  
ATOM    536  CA  ASN A  66       3.284   9.706  40.973  1.00 10.03           C  
ATOM    537  C   ASN A  66       2.109   9.568  40.048  1.00  9.44           C  
ATOM    538  O   ASN A  66       1.478  10.586  39.778  1.00  8.73           O  
ATOM    539  CB  ASN A  66       2.788  10.125  42.384  1.00 10.28           C  
ATOM    540  CG  ASN A  66       1.838   9.070  42.956  1.00 11.49           C  
ATOM    541  OD1 ASN A  66       2.066   7.855  42.883  1.00 12.01           O  
ATOM    542  ND2 ASN A  66       0.724   9.577  43.469  1.00 12.08           N  
ATOM    543  N   ASP A  67       1.798   8.327  39.653  1.00  9.27           N  
ATOM    544  CA  ASP A  67       0.628   8.059  38.810  1.00  9.88           C  
ATOM    545  C   ASP A  67      -0.302   7.061  39.547  1.00 10.36           C  
ATOM    546  O   ASP A  67      -1.331   6.622  39.042  1.00  9.97           O  
ATOM    547  CB  ASP A  67       0.987   7.676  37.374  1.00 10.56           C  
ATOM    548  CG  ASP A  67       1.614   6.294  37.230  1.00 10.27           C  
ATOM    549  OD1 ASP A  67       1.856   5.577  38.255  1.00 10.59           O  
ATOM    550  OD2 ASP A  67       1.842   5.938  36.044  1.00 10.50           O  
ATOM    551  N   GLY A  68       0.017   6.741  40.778  1.00 10.80           N  
ATOM    552  CA  GLY A  68      -0.698   5.872  41.673  1.00 12.46           C  
ATOM    553  C   GLY A  68      -0.729   4.400  41.294  1.00 12.75           C  
ATOM    554  O   GLY A  68      -0.937   3.628  42.235  1.00 13.44           O  
ATOM    555  N   LYS A  69      -0.543   4.058  40.045  1.00 13.37           N  
ATOM    556  CA  LYS A  69      -0.645   2.667  39.589  1.00 13.84           C  
ATOM    557  C   LYS A  69       0.674   1.974  39.365  1.00 13.58           C  
ATOM    558  O   LYS A  69       0.592   0.837  38.823  1.00 15.81           O  
ATOM    559  CB  LYS A  69      -1.488   2.604  38.308  1.00 14.05           C  
ATOM    560  CG  LYS A  69      -0.921   3.298  37.073  1.00 14.42           C  
ATOM    561  CD  LYS A  69      -1.833   3.092  35.887  1.00 16.17           C  
ATOM    562  CE  LYS A  69      -1.271   3.673  34.599  1.00 20.74           C  
ATOM    563  NZ  LYS A  69      -2.442   4.156  33.747  1.00 25.86           N  
ATOM    564  N   THR A  70       1.788   2.550  39.711  1.00 13.15           N  
ATOM    565  CA  THR A  70       3.120   1.899  39.503  1.00 13.24           C  
ATOM    566  C   THR A  70       3.582   1.312  40.816  1.00 13.31           C  
ATOM    567  O   THR A  70       3.761   1.962  41.848  1.00 12.50           O  
ATOM    568  CB  THR A  70       4.199   2.943  38.953  1.00 13.80           C  
ATOM    569  OG1 THR A  70       3.661   3.613  37.773  1.00 11.15           O  
ATOM    570  CG2 THR A  70       5.567   2.301  38.654  1.00 12.83           C  
ATOM    571  N   PRO A  71       3.821   0.010  40.818  1.00 14.12           N  
ATOM    572  CA  PRO A  71       4.242  -0.621  42.093  1.00 15.15           C  
ATOM    573  C   PRO A  71       5.633  -0.214  42.487  1.00 15.49           C  
ATOM    574  O   PRO A  71       6.486  -0.076  41.622  1.00 15.59           O  
ATOM    575  CB  PRO A  71       4.061  -2.116  41.800  1.00 14.78           C  
ATOM    576  CG  PRO A  71       3.452  -2.289  40.459  1.00 14.86           C  
ATOM    577  CD  PRO A  71       3.661  -0.943  39.716  1.00 14.21           C  
ATOM    578  N   GLY A  72       5.894  -0.051  43.784  1.00 16.08           N  
ATOM    579  CA  GLY A  72       7.187   0.288  44.346  1.00 19.09           C  
ATOM    580  C   GLY A  72       7.712   1.633  43.901  1.00 20.24           C  
ATOM    581  O   GLY A  72       8.939   1.900  43.864  1.00 22.74           O  
ATOM    582  N   ALA A  73       6.787   2.522  43.542  1.00 19.48           N  
ATOM    583  CA  ALA A  73       7.188   3.829  43.039  1.00 19.16           C  
ATOM    584  C   ALA A  73       7.563   4.822  44.122  1.00 19.21           C  
ATOM    585  O   ALA A  73       7.072   4.821  45.249  1.00 20.43           O  
ATOM    586  CB  ALA A  73       6.018   4.390  42.202  1.00 19.84           C  
ATOM    587  N   VAL A  74       8.475   5.672  43.753  1.00 17.90           N  
ATOM    588  CA  VAL A  74       8.928   6.796  44.582  1.00 19.92           C  
ATOM    589  C   VAL A  74       8.524   8.001  43.682  1.00 19.98           C  
ATOM    590  O   VAL A  74       8.249   7.827  42.462  1.00 21.49           O  
ATOM    591  CB  VAL A  74      10.356   6.654  45.032  1.00 20.60           C  
ATOM    592  CG1 VAL A  74      10.434   5.380  45.954  1.00 24.00           C  
ATOM    593  CG2 VAL A  74      11.384   6.537  43.931  1.00 22.62           C  
ATOM    594  N   ASN A  75       8.416   9.118  44.292  1.00 18.38           N  
ATOM    595  CA  ASN A  75       7.985  10.340  43.595  1.00 15.99           C  
ATOM    596  C   ASN A  75       9.061  11.375  43.957  1.00 15.61           C  
ATOM    597  O   ASN A  75       8.813  12.293  44.761  1.00 15.84           O  
ATOM    598  CB  ASN A  75       6.558  10.590  44.098  1.00 15.18           C  
ATOM    599  CG  ASN A  75       6.000  11.905  43.585  1.00 14.74           C  
ATOM    600  OD1 ASN A  75       6.594  12.486  42.680  1.00 14.46           O  
ATOM    601  ND2 ASN A  75       4.894  12.352  44.167  1.00 14.55           N  
ATOM    602  N   ALA A  76      10.235  11.126  43.366  1.00 15.24           N  
ATOM    603  CA  ALA A  76      11.387  11.996  43.659  1.00 15.31           C  
ATOM    604  C   ALA A  76      11.087  13.425  43.243  1.00 16.44           C  
ATOM    605  O   ALA A  76      11.568  14.277  44.049  1.00 16.90           O  
ATOM    606  CB  ALA A  76      12.720  11.507  43.180  1.00 14.98           C  
ATOM    607  N   CYS A  77      10.316  13.647  42.166  1.00 14.55           N  
ATOM    608  CA  CYS A  77      10.041  15.071  41.847  1.00 14.00           C  
ATOM    609  C   CYS A  77       8.909  15.696  42.637  1.00 13.60           C  
ATOM    610  O   CYS A  77       8.631  16.911  42.466  1.00 12.66           O  
ATOM    611  CB  CYS A  77       9.825  15.302  40.348  1.00 11.76           C  
ATOM    612  SG  CYS A  77      11.239  14.865  39.333  1.00 10.27           S  
ATOM    613  N   HIS A  78       8.229  14.934  43.455  1.00 13.49           N  
ATOM    614  CA  HIS A  78       7.089  15.379  44.246  1.00 14.00           C  
ATOM    615  C   HIS A  78       6.051  16.032  43.343  1.00 14.35           C  
ATOM    616  O   HIS A  78       5.555  17.170  43.569  1.00 13.93           O  
ATOM    617  CB  HIS A  78       7.457  16.312  45.424  1.00 19.71           C  
ATOM    618  CG  HIS A  78       8.876  16.209  45.880  1.00 26.99           C  
ATOM    619  ND1 HIS A  78       9.727  17.311  45.989  1.00 30.22           N  
ATOM    620  CD2 HIS A  78       9.615  15.122  46.265  1.00 29.19           C  
ATOM    621  CE1 HIS A  78      10.912  16.889  46.396  1.00 30.79           C  
ATOM    622  NE2 HIS A  78      10.885  15.575  46.558  1.00 30.27           N  
ATOM    623  N   LEU A  79       5.633  15.322  42.286  1.00 11.82           N  
ATOM    624  CA  LEU A  79       4.635  15.780  41.354  1.00 12.35           C  
ATOM    625  C   LEU A  79       3.736  14.614  40.892  1.00 11.24           C  
ATOM    626  O   LEU A  79       4.279  13.523  40.772  1.00 10.79           O  
ATOM    627  CB  LEU A  79       5.312  16.162  39.990  1.00 14.52           C  
ATOM    628  CG  LEU A  79       6.144  17.403  39.871  1.00 15.98           C  
ATOM    629  CD1 LEU A  79       6.918  17.412  38.552  1.00 15.63           C  
ATOM    630  CD2 LEU A  79       5.227  18.611  39.977  1.00 17.39           C  
ATOM    631  N   SER A  80       2.530  14.990  40.550  1.00  9.84           N  
ATOM    632  CA  SER A  80       1.606  14.018  39.922  1.00  9.05           C  
ATOM    633  C   SER A  80       2.144  13.838  38.493  1.00  9.20           C  
ATOM    634  O   SER A  80       2.625  14.851  37.896  1.00  8.22           O  
ATOM    635  CB  SER A  80       0.224  14.665  39.856  1.00  9.78           C  
ATOM    636  OG  SER A  80      -0.498  14.033  38.809  1.00 12.76           O  
ATOM    637  N   CYS A  81       2.138  12.641  37.906  1.00  8.26           N  
ATOM    638  CA  CYS A  81       2.597  12.441  36.553  1.00  7.74           C  
ATOM    639  C   CYS A  81       1.742  13.317  35.621  1.00  7.31           C  
ATOM    640  O   CYS A  81       2.203  13.614  34.519  1.00  8.97           O  
ATOM    641  CB  CYS A  81       2.593  10.981  36.067  1.00  7.13           C  
ATOM    642  SG  CYS A  81       3.827  10.052  37.063  1.00  9.03           S  
ATOM    643  N   SER A  82       0.561  13.702  36.001  1.00  7.17           N  
ATOM    644  CA  SER A  82      -0.271  14.597  35.155  1.00  8.73           C  
ATOM    645  C   SER A  82       0.500  15.898  34.829  1.00  8.79           C  
ATOM    646  O   SER A  82       0.380  16.474  33.722  1.00 10.42           O  
ATOM    647  CB  SER A  82      -1.521  15.004  35.945  1.00  8.96           C  
ATOM    648  OG  SER A  82      -2.450  15.639  35.072  1.00  9.41           O  
ATOM    649  N   ALA A  83       1.231  16.385  35.772  1.00  8.39           N  
ATOM    650  CA  ALA A  83       2.004  17.624  35.631  1.00  9.00           C  
ATOM    651  C   ALA A  83       2.968  17.599  34.437  1.00  9.89           C  
ATOM    652  O   ALA A  83       3.365  18.672  33.934  1.00  9.16           O  
ATOM    653  CB  ALA A  83       2.776  17.896  36.930  1.00  8.73           C  
ATOM    654  N   LEU A  84       3.373  16.406  34.059  1.00  8.90           N  
ATOM    655  CA  LEU A  84       4.293  16.190  32.975  1.00  9.91           C  
ATOM    656  C   LEU A  84       3.598  16.064  31.626  1.00  9.59           C  
ATOM    657  O   LEU A  84       4.295  15.708  30.650  1.00 12.27           O  
ATOM    658  CB  LEU A  84       5.154  14.950  33.295  1.00  9.75           C  
ATOM    659  CG  LEU A  84       5.918  14.960  34.610  1.00 11.03           C  
ATOM    660  CD1 LEU A  84       6.752  13.666  34.686  1.00 12.79           C  
ATOM    661  CD2 LEU A  84       6.850  16.154  34.766  1.00 13.21           C  
ATOM    662  N   LEU A  85       2.313  16.289  31.565  1.00  9.61           N  
ATOM    663  CA  LEU A  85       1.553  16.202  30.321  1.00 10.65           C  
ATOM    664  C   LEU A  85       1.000  17.605  29.974  1.00 12.27           C  
ATOM    665  O   LEU A  85       0.272  17.694  28.999  1.00 14.04           O  
ATOM    666  CB  LEU A  85       0.482  15.111  30.391  1.00 10.37           C  
ATOM    667  CG  LEU A  85       0.930  13.652  30.536  1.00 10.62           C  
ATOM    668  CD1 LEU A  85      -0.289  12.744  30.500  1.00 12.54           C  
ATOM    669  CD2 LEU A  85       1.861  13.240  29.397  1.00 10.48           C  
ATOM    670  N   GLN A  86       1.429  18.631  30.649  1.00 13.39           N  
ATOM    671  CA  GLN A  86       0.917  20.020  30.376  1.00 13.93           C  
ATOM    672  C   GLN A  86       1.582  20.677  29.188  1.00 12.90           C  
ATOM    673  O   GLN A  86       2.716  20.284  28.866  1.00 13.31           O  
ATOM    674  CB  GLN A  86       1.205  20.921  31.575  1.00 15.47           C  
ATOM    675  CG  GLN A  86       0.749  20.451  32.938  1.00 18.99           C  
ATOM    676  CD  GLN A  86       1.159  21.501  33.981  1.00 20.27           C  
ATOM    677  OE1 GLN A  86       0.621  22.623  33.881  1.00 23.38           O  
ATOM    678  NE2 GLN A  86       2.063  21.187  34.881  1.00 18.47           N  
ATOM    679  N   ASP A  87       0.932  21.696  28.600  1.00 12.88           N  
ATOM    680  CA  ASP A  87       1.535  22.398  27.455  1.00 13.47           C  
ATOM    681  C   ASP A  87       2.709  23.263  27.962  1.00 12.61           C  
ATOM    682  O   ASP A  87       3.631  23.497  27.164  1.00 14.48           O  
ATOM    683  CB  ASP A  87       0.503  23.179  26.643  1.00 16.00           C  
ATOM    684  CG  ASP A  87      -0.515  22.294  25.931  1.00 19.96           C  
ATOM    685  OD1 ASP A  87      -0.277  21.106  25.714  1.00 19.81           O  
ATOM    686  OD2 ASP A  87      -1.566  22.886  25.562  1.00 24.64           O  
ATOM    687  N   ASN A  88       2.596  23.718  29.187  1.00 11.65           N  
ATOM    688  CA  ASN A  88       3.623  24.549  29.830  1.00 13.24           C  
ATOM    689  C   ASN A  88       4.679  23.545  30.356  1.00 11.71           C  
ATOM    690  O   ASN A  88       4.190  22.808  31.251  1.00 12.68           O  
ATOM    691  CB  ASN A  88       3.037  25.329  31.025  1.00 14.86           C  
ATOM    692  CG  ASN A  88       4.058  26.299  31.595  1.00 17.91           C  
ATOM    693  OD1 ASN A  88       5.140  25.892  32.024  1.00 17.51           O  
ATOM    694  ND2 ASN A  88       3.767  27.628  31.559  1.00 19.59           N  
ATOM    695  N   ILE A  89       5.881  23.606  29.832  1.00 10.32           N  
ATOM    696  CA  ILE A  89       6.869  22.579  30.362  1.00 11.22           C  
ATOM    697  C   ILE A  89       7.614  22.941  31.629  1.00 10.20           C  
ATOM    698  O   ILE A  89       8.572  22.184  31.989  1.00  8.86           O  
ATOM    699  CB  ILE A  89       7.778  22.167  29.174  1.00 12.01           C  
ATOM    700  CG1 ILE A  89       8.659  23.389  28.792  1.00 13.44           C  
ATOM    701  CG2 ILE A  89       6.955  21.558  27.993  1.00 11.18           C  
ATOM    702  CD1 ILE A  89       9.733  23.096  27.713  1.00 16.92           C  
ATOM    703  N   ALA A  90       7.208  23.978  32.370  1.00  8.15           N  
ATOM    704  CA  ALA A  90       8.008  24.303  33.584  1.00  8.69           C  
ATOM    705  C   ALA A  90       8.228  23.151  34.569  1.00  8.08           C  
ATOM    706  O   ALA A  90       9.373  22.955  35.053  1.00  8.42           O  
ATOM    707  CB  ALA A  90       7.437  25.526  34.285  1.00  8.95           C  
ATOM    708  N   ASP A  91       7.168  22.452  34.888  1.00  8.70           N  
ATOM    709  CA  ASP A  91       7.197  21.293  35.831  1.00  9.34           C  
ATOM    710  C   ASP A  91       8.091  20.183  35.284  1.00  9.57           C  
ATOM    711  O   ASP A  91       8.861  19.592  36.058  1.00  9.24           O  
ATOM    712  CB  ASP A  91       5.816  20.773  36.191  1.00 12.79           C  
ATOM    713  CG  ASP A  91       4.969  21.786  36.959  1.00 17.74           C  
ATOM    714  OD1 ASP A  91       3.792  21.978  36.625  1.00 20.92           O  
ATOM    715  OD2 ASP A  91       5.518  22.434  37.878  1.00 18.47           O  
ATOM    716  N   ALA A  92       7.944  19.881  34.008  1.00  8.93           N  
ATOM    717  CA  ALA A  92       8.766  18.831  33.379  1.00  7.65           C  
ATOM    718  C   ALA A  92      10.228  19.218  33.422  1.00  9.29           C  
ATOM    719  O   ALA A  92      11.124  18.358  33.643  1.00  9.06           O  
ATOM    720  CB  ALA A  92       8.242  18.529  31.978  1.00  7.08           C  
ATOM    721  N   VAL A  93      10.555  20.498  33.202  1.00  8.44           N  
ATOM    722  CA  VAL A  93      11.968  20.945  33.255  1.00  7.98           C  
ATOM    723  C   VAL A  93      12.502  20.834  34.682  1.00  7.94           C  
ATOM    724  O   VAL A  93      13.643  20.411  34.926  1.00  8.12           O  
ATOM    725  CB  VAL A  93      12.108  22.398  32.704  1.00  8.33           C  
ATOM    726  CG1 VAL A  93      13.430  23.012  33.191  1.00 10.25           C  
ATOM    727  CG2 VAL A  93      12.015  22.385  31.176  1.00  9.76           C  
ATOM    728  N   ALA A  94      11.684  21.279  35.642  1.00  8.25           N  
ATOM    729  CA  ALA A  94      12.171  21.212  37.042  1.00  9.46           C  
ATOM    730  C   ALA A  94      12.351  19.700  37.362  1.00  8.65           C  
ATOM    731  O   ALA A  94      13.297  19.414  38.135  1.00 10.33           O  
ATOM    732  CB  ALA A  94      11.247  21.975  37.956  1.00  9.75           C  
ATOM    733  N   CYS A  95      11.522  18.848  36.815  1.00  6.56           N  
ATOM    734  CA  CYS A  95      11.714  17.398  37.127  1.00  8.25           C  
ATOM    735  C   CYS A  95      12.978  16.860  36.427  1.00  8.56           C  
ATOM    736  O   CYS A  95      13.772  16.102  37.055  1.00  8.77           O  
ATOM    737  CB  CYS A  95      10.469  16.587  36.862  1.00  9.28           C  
ATOM    738  SG  CYS A  95      10.562  14.837  37.425  1.00 10.40           S  
ATOM    739  N   ALA A  96      13.151  17.217  35.165  1.00  7.12           N  
ATOM    740  CA  ALA A  96      14.334  16.776  34.414  1.00  7.75           C  
ATOM    741  C   ALA A  96      15.597  17.211  35.119  1.00  8.06           C  
ATOM    742  O   ALA A  96      16.629  16.498  35.100  1.00  8.18           O  
ATOM    743  CB  ALA A  96      14.231  17.189  32.960  1.00  9.01           C  
ATOM    744  N   LYS A  97      15.588  18.420  35.720  1.00  8.76           N  
ATOM    745  CA  LYS A  97      16.774  18.921  36.442  1.00  8.49           C  
ATOM    746  C   LYS A  97      17.093  18.002  37.640  1.00  9.62           C  
ATOM    747  O   LYS A  97      18.279  17.724  37.906  1.00  9.24           O  
ATOM    748  CB  LYS A  97      16.540  20.339  36.947  1.00  8.22           C  
ATOM    749  CG  LYS A  97      16.698  21.350  35.777  1.00 10.75           C  
ATOM    750  CD  LYS A  97      16.422  22.788  36.302  1.00  9.43           C  
ATOM    751  CE  LYS A  97      16.497  23.786  35.115  1.00 10.80           C  
ATOM    752  NZ  LYS A  97      16.143  25.124  35.661  1.00 11.24           N  
ATOM    753  N   ARG A  98      16.028  17.538  38.278  1.00 10.11           N  
ATOM    754  CA  ARG A  98      16.127  16.629  39.443  1.00 11.87           C  
ATOM    755  C   ARG A  98      16.716  15.309  38.961  1.00 10.66           C  
ATOM    756  O   ARG A  98      17.634  14.760  39.604  1.00 11.29           O  
ATOM    757  CB  ARG A  98      14.792  16.396  40.104  1.00 14.76           C  
ATOM    758  CG  ARG A  98      14.751  15.616  41.392  1.00 19.86           C  
ATOM    759  CD  ARG A  98      15.878  15.782  42.335  1.00 22.15           C  
ATOM    760  NE  ARG A  98      16.288  14.535  42.861  1.00 28.25           N  
ATOM    761  CZ  ARG A  98      17.090  13.577  43.247  1.00 26.67           C  
ATOM    762  NH1 ARG A  98      16.578  12.474  43.784  1.00 26.82           N  
ATOM    763  NH2 ARG A  98      18.411  13.710  43.188  1.00 26.42           N  
ATOM    764  N   VAL A  99      16.230  14.836  37.825  1.00  9.83           N  
ATOM    765  CA  VAL A  99      16.801  13.551  37.326  1.00  9.38           C  
ATOM    766  C   VAL A  99      18.313  13.578  37.178  1.00 11.30           C  
ATOM    767  O   VAL A  99      18.992  12.613  37.587  1.00  9.19           O  
ATOM    768  CB  VAL A  99      16.190  13.239  35.959  1.00  9.14           C  
ATOM    769  CG1 VAL A  99      16.863  12.058  35.287  1.00 12.60           C  
ATOM    770  CG2 VAL A  99      14.689  13.025  36.122  1.00 10.12           C  
ATOM    771  N   VAL A 100      18.786  14.653  36.531  1.00 10.82           N  
ATOM    772  CA  VAL A 100      20.228  14.751  36.257  1.00 15.04           C  
ATOM    773  C   VAL A 100      21.035  14.992  37.518  1.00 16.75           C  
ATOM    774  O   VAL A 100      22.217  14.580  37.516  1.00 16.08           O  
ATOM    775  CB  VAL A 100      20.539  15.687  35.069  1.00 14.07           C  
ATOM    776  CG1 VAL A 100      19.862  15.172  33.772  1.00 14.71           C  
ATOM    777  CG2 VAL A 100      20.107  17.131  35.294  1.00 14.76           C  
ATOM    778  N   ARG A 101      20.446  15.595  38.525  1.00 18.12           N  
ATOM    779  CA  ARG A 101      21.230  15.808  39.752  1.00 23.26           C  
ATOM    780  C   ARG A 101      21.653  14.503  40.401  1.00 26.44           C  
ATOM    781  O   ARG A 101      22.235  14.471  41.481  1.00 27.92           O  
ATOM    782  CB  ARG A 101      20.476  16.710  40.733  1.00 24.95           C  
ATOM    783  CG  ARG A 101      20.362  18.144  40.274  1.00 25.51           C  
ATOM    784  CD  ARG A 101      20.184  19.096  41.414  1.00 25.28           C  
ATOM    785  NE  ARG A 101      18.906  18.863  42.066  1.00 25.28           N  
ATOM    786  CZ  ARG A 101      17.727  19.381  41.745  1.00 23.55           C  
ATOM    787  NH1 ARG A 101      17.502  20.199  40.731  1.00 22.56           N  
ATOM    788  NH2 ARG A 101      16.711  19.054  42.548  1.00 24.36           N  
ATOM    789  N   ASP A 102      21.475  13.374  39.769  1.00 30.17           N  
ATOM    790  CA  ASP A 102      21.801  12.009  40.139  1.00 31.89           C  
ATOM    791  C   ASP A 102      22.904  11.317  39.355  1.00 32.03           C  
ATOM    792  O   ASP A 102      22.676  10.889  38.220  1.00 33.49           O  
ATOM    793  CB  ASP A 102      20.468  11.207  40.039  1.00 32.30           C  
ATOM    794  CG  ASP A 102      19.803  11.596  41.363  1.00 36.69           C  
ATOM    795  OD1 ASP A 102      19.628  10.745  42.234  1.00 38.31           O  
ATOM    796  OD2 ASP A 102      19.534  12.825  41.465  1.00 37.30           O  
ATOM    797  N   GLY A 103      24.029  11.099  39.988  1.00 33.39           N  
ATOM    798  CA  GLY A 103      25.279  10.490  39.657  1.00 32.41           C  
ATOM    799  C   GLY A 103      25.352   9.553  38.447  1.00 32.74           C  
ATOM    800  O   GLY A 103      26.040   8.497  38.386  1.00 31.36           O  
ATOM    801  N   GLN A 104      24.594   9.985  37.457  1.00 30.43           N  
ATOM    802  CA  GLN A 104      24.330   9.517  36.147  1.00 28.25           C  
ATOM    803  C   GLN A 104      24.248  10.725  35.183  1.00 24.68           C  
ATOM    804  O   GLN A 104      24.708  10.538  34.030  1.00 24.78           O  
ATOM    805  CB  GLN A 104      23.075   8.660  35.987  1.00 31.75           C  
ATOM    806  CG  GLN A 104      23.373   7.198  35.737  1.00 33.38           C  
ATOM    807  CD  GLN A 104      22.116   6.350  35.671  1.00 35.77           C  
ATOM    808  OE1 GLN A 104      21.046   6.712  36.174  1.00 36.07           O  
ATOM    809  NE2 GLN A 104      22.270   5.187  35.043  1.00 35.43           N  
ATOM    810  N   GLY A 105      23.639  11.833  35.609  1.00 21.38           N  
ATOM    811  CA  GLY A 105      23.573  12.982  34.668  1.00 17.43           C  
ATOM    812  C   GLY A 105      22.653  12.697  33.482  1.00 16.25           C  
ATOM    813  O   GLY A 105      21.610  12.050  33.639  1.00 15.41           O  
ATOM    814  N   ILE A 106      23.012  13.182  32.298  1.00 14.67           N  
ATOM    815  CA  ILE A 106      22.187  13.039  31.083  1.00 14.72           C  
ATOM    816  C   ILE A 106      22.093  11.556  30.632  1.00 14.57           C  
ATOM    817  O   ILE A 106      21.112  11.114  30.010  1.00 13.06           O  
ATOM    818  CB  ILE A 106      22.740  14.024  29.997  1.00 14.42           C  
ATOM    819  CG1 ILE A 106      21.829  14.106  28.751  1.00 15.93           C  
ATOM    820  CG2 ILE A 106      24.198  13.682  29.574  1.00 14.06           C  
ATOM    821  CD1 ILE A 106      20.412  14.713  28.987  1.00 16.41           C  
ATOM    822  N   ARG A 107      23.130  10.822  31.054  1.00 13.93           N  
ATOM    823  CA  ARG A 107      23.190   9.386  30.740  1.00 15.68           C  
ATOM    824  C   ARG A 107      22.058   8.620  31.394  1.00 14.96           C  
ATOM    825  O   ARG A 107      21.835   7.461  31.016  1.00 13.10           O  
ATOM    826  CB  ARG A 107      24.535   8.757  31.188  1.00 19.91           C  
ATOM    827  CG  ARG A 107      25.733   9.187  30.334  1.00 23.16           C  
ATOM    828  CD  ARG A 107      27.011   8.695  30.967  1.00 25.64           C  
ATOM    829  NE  ARG A 107      28.167   8.768  30.108  1.00 25.73           N  
ATOM    830  CZ  ARG A 107      28.681   9.892  29.599  1.00 28.94           C  
ATOM    831  NH1 ARG A 107      29.747   9.774  28.780  1.00 28.52           N  
ATOM    832  NH2 ARG A 107      28.144  11.090  29.889  1.00 26.64           N  
ATOM    833  N   ALA A 108      21.360   9.233  32.323  1.00 14.84           N  
ATOM    834  CA  ALA A 108      20.182   8.596  32.965  1.00 15.22           C  
ATOM    835  C   ALA A 108      19.209   8.060  31.927  1.00 15.74           C  
ATOM    836  O   ALA A 108      18.534   7.032  32.191  1.00 16.42           O  
ATOM    837  CB  ALA A 108      19.470   9.574  33.889  1.00 16.22           C  
ATOM    838  N   TRP A 109      19.115   8.712  30.760  1.00 14.40           N  
ATOM    839  CA  TRP A 109      18.213   8.309  29.677  1.00 12.84           C  
ATOM    840  C   TRP A 109      18.966   7.454  28.654  1.00 11.77           C  
ATOM    841  O   TRP A 109      19.944   7.966  28.063  1.00 10.43           O  
ATOM    842  CB  TRP A 109      17.624   9.527  28.968  1.00 11.22           C  
ATOM    843  CG  TRP A 109      16.541  10.295  29.642  1.00 10.83           C  
ATOM    844  CD1 TRP A 109      15.183  10.121  29.523  1.00 11.47           C  
ATOM    845  CD2 TRP A 109      16.706  11.411  30.539  1.00 10.51           C  
ATOM    846  NE1 TRP A 109      14.507  11.014  30.300  1.00 11.62           N  
ATOM    847  CE2 TRP A 109      15.406  11.850  30.897  1.00 10.69           C  
ATOM    848  CE3 TRP A 109      17.825  12.088  30.995  1.00 11.81           C  
ATOM    849  CZ2 TRP A 109      15.198  12.921  31.754  1.00 10.99           C  
ATOM    850  CZ3 TRP A 109      17.628  13.169  31.837  1.00 11.98           C  
ATOM    851  CH2 TRP A 109      16.337  13.591  32.203  1.00 11.30           C  
ATOM    852  N   VAL A 110      18.586   6.198  28.487  1.00 11.57           N  
ATOM    853  CA  VAL A 110      19.291   5.375  27.501  1.00 12.09           C  
ATOM    854  C   VAL A 110      19.141   5.930  26.103  1.00 11.61           C  
ATOM    855  O   VAL A 110      20.060   5.690  25.297  1.00 12.67           O  
ATOM    856  CB  VAL A 110      18.976   3.842  27.552  1.00 16.79           C  
ATOM    857  CG1 VAL A 110      19.093   3.249  28.945  1.00 16.23           C  
ATOM    858  CG2 VAL A 110      17.646   3.572  26.866  1.00 16.64           C  
ATOM    859  N   ALA A 111      18.072   6.580  25.711  1.00 12.36           N  
ATOM    860  CA  ALA A 111      17.896   7.184  24.389  1.00 11.04           C  
ATOM    861  C   ALA A 111      19.047   8.176  24.136  1.00 10.61           C  
ATOM    862  O   ALA A 111      19.576   8.289  23.023  1.00 10.48           O  
ATOM    863  CB  ALA A 111      16.542   7.931  24.298  1.00 11.88           C  
ATOM    864  N   TRP A 112      19.441   8.924  25.163  1.00 10.56           N  
ATOM    865  CA  TRP A 112      20.541   9.896  24.987  1.00  9.99           C  
ATOM    866  C   TRP A 112      21.808   9.139  24.604  1.00  9.70           C  
ATOM    867  O   TRP A 112      22.508   9.508  23.656  1.00  7.27           O  
ATOM    868  CB  TRP A 112      20.689  10.845  26.193  1.00  9.45           C  
ATOM    869  CG  TRP A 112      21.808  11.804  25.947  1.00 10.53           C  
ATOM    870  CD1 TRP A 112      21.705  13.041  25.339  1.00  8.81           C  
ATOM    871  CD2 TRP A 112      23.198  11.615  26.294  1.00 11.22           C  
ATOM    872  NE1 TRP A 112      22.965  13.601  25.280  1.00 10.28           N  
ATOM    873  CE2 TRP A 112      23.885  12.802  25.865  1.00 10.13           C  
ATOM    874  CE3 TRP A 112      23.909  10.598  26.914  1.00 10.43           C  
ATOM    875  CZ2 TRP A 112      25.256  12.924  26.019  1.00 10.28           C  
ATOM    876  CZ3 TRP A 112      25.277  10.734  27.107  1.00 10.91           C  
ATOM    877  CH2 TRP A 112      25.953  11.889  26.658  1.00 11.78           C  
ATOM    878  N   ARG A 113      22.107   8.042  25.309  1.00  9.79           N  
ATOM    879  CA  ARG A 113      23.286   7.241  24.951  1.00 11.39           C  
ATOM    880  C   ARG A 113      23.223   6.701  23.509  1.00 11.39           C  
ATOM    881  O   ARG A 113      24.258   6.694  22.781  1.00 11.83           O  
ATOM    882  CB  ARG A 113      23.416   6.059  25.904  1.00 12.36           C  
ATOM    883  CG  ARG A 113      23.724   6.418  27.360  1.00 14.23           C  
ATOM    884  CD  ARG A 113      23.508   5.102  28.083  1.00 19.82           C  
ATOM    885  NE  ARG A 113      22.980   5.268  29.416  1.00 22.83           N  
ATOM    886  CZ  ARG A 113      22.744   4.200  30.187  1.00 25.63           C  
ATOM    887  NH1 ARG A 113      22.955   2.963  29.713  1.00 25.08           N  
ATOM    888  NH2 ARG A 113      22.330   4.447  31.427  1.00 26.09           N  
ATOM    889  N   ASN A 114      22.029   6.249  23.090  1.00 11.82           N  
ATOM    890  CA  ASN A 114      21.855   5.660  21.754  1.00 11.98           C  
ATOM    891  C   ASN A 114      21.928   6.612  20.565  1.00 13.29           C  
ATOM    892  O   ASN A 114      22.450   6.290  19.464  1.00 11.90           O  
ATOM    893  CB  ASN A 114      20.478   4.978  21.641  1.00 11.54           C  
ATOM    894  CG  ASN A 114      20.292   3.784  22.552  1.00 13.60           C  
ATOM    895  OD1 ASN A 114      21.253   3.255  23.100  1.00 16.34           O  
ATOM    896  ND2 ASN A 114      19.035   3.377  22.692  1.00 16.24           N  
ATOM    897  N   ARG A 115      21.277   7.788  20.783  1.00 12.38           N  
ATOM    898  CA  ARG A 115      21.137   8.760  19.732  1.00 11.87           C  
ATOM    899  C   ARG A 115      21.894  10.063  19.803  1.00 10.96           C  
ATOM    900  O   ARG A 115      21.902  10.712  18.725  1.00 12.16           O  
ATOM    901  CB  ARG A 115      19.621   9.209  19.654  1.00 15.04           C  
ATOM    902  CG  ARG A 115      18.657   7.987  19.682  1.00 18.15           C  
ATOM    903  CD  ARG A 115      18.441   7.498  18.292  1.00 18.68           C  
ATOM    904  NE  ARG A 115      17.400   6.491  18.218  1.00 22.64           N  
ATOM    905  CZ  ARG A 115      17.040   5.869  17.081  1.00 22.75           C  
ATOM    906  NH1 ARG A 115      17.620   6.089  15.903  1.00 22.60           N  
ATOM    907  NH2 ARG A 115      16.031   5.004  17.196  1.00 23.02           N  
ATOM    908  N   CYS A 116      22.403  10.395  20.949  1.00  9.23           N  
ATOM    909  CA  CYS A 116      23.051  11.716  21.106  1.00 10.43           C  
ATOM    910  C   CYS A 116      24.516  11.715  21.483  1.00  9.98           C  
ATOM    911  O   CYS A 116      25.278  12.532  20.925  1.00  8.76           O  
ATOM    912  CB  CYS A 116      22.262  12.505  22.195  1.00  7.58           C  
ATOM    913  SG  CYS A 116      20.483  12.608  21.873  1.00  8.92           S  
ATOM    914  N   GLN A 117      24.876  10.825  22.379  1.00  9.44           N  
ATOM    915  CA  GLN A 117      26.239  10.670  22.906  1.00 10.89           C  
ATOM    916  C   GLN A 117      27.250  10.472  21.787  1.00 11.89           C  
ATOM    917  O   GLN A 117      27.079   9.711  20.842  1.00 10.43           O  
ATOM    918  CB  GLN A 117      26.306   9.607  24.000  1.00 11.75           C  
ATOM    919  CG  GLN A 117      27.724   9.227  24.409  1.00 14.92           C  
ATOM    920  CD  GLN A 117      27.741   8.239  25.557  1.00 16.81           C  
ATOM    921  OE1 GLN A 117      28.557   8.375  26.486  1.00 20.19           O  
ATOM    922  NE2 GLN A 117      26.834   7.280  25.561  1.00 14.56           N  
ATOM    923  N   ASN A 118      28.316  11.272  21.917  1.00 12.46           N  
ATOM    924  CA  ASN A 118      29.409  11.270  20.940  1.00 16.81           C  
ATOM    925  C   ASN A 118      28.956  11.664  19.548  1.00 16.04           C  
ATOM    926  O   ASN A 118      29.759  11.367  18.610  1.00 19.95           O  
ATOM    927  CB  ASN A 118      30.187   9.945  20.911  1.00 19.32           C  
ATOM    928  CG  ASN A 118      30.817   9.607  22.247  1.00 21.84           C  
ATOM    929  OD1 ASN A 118      31.011   8.404  22.500  1.00 25.92           O  
ATOM    930  ND2 ASN A 118      31.141  10.584  23.069  1.00 22.98           N  
ATOM    931  N   ARG A 119      27.817  12.228  19.336  1.00 14.08           N  
ATOM    932  CA  ARG A 119      27.382  12.624  18.008  1.00 13.70           C  
ATOM    933  C   ARG A 119      27.468  14.169  17.904  1.00 12.98           C  
ATOM    934  O   ARG A 119      27.618  14.823  18.925  1.00 12.96           O  
ATOM    935  CB  ARG A 119      25.946  12.207  17.667  1.00 13.18           C  
ATOM    936  CG  ARG A 119      25.895  10.639  17.769  1.00 13.90           C  
ATOM    937  CD  ARG A 119      24.627  10.208  17.125  1.00 15.09           C  
ATOM    938  NE  ARG A 119      24.345   8.820  17.509  1.00 13.81           N  
ATOM    939  CZ  ARG A 119      24.110   7.842  16.662  1.00 14.55           C  
ATOM    940  NH1 ARG A 119      23.766   6.671  17.160  1.00 15.11           N  
ATOM    941  NH2 ARG A 119      24.309   8.004  15.369  1.00 16.19           N  
ATOM    942  N   ASP A 120      27.327  14.620  16.675  1.00 13.81           N  
ATOM    943  CA  ASP A 120      27.380  16.078  16.402  1.00 13.66           C  
ATOM    944  C   ASP A 120      25.939  16.536  16.665  1.00 13.98           C  
ATOM    945  O   ASP A 120      25.089  16.221  15.810  1.00 16.39           O  
ATOM    946  CB  ASP A 120      27.896  16.328  14.984  1.00 15.47           C  
ATOM    947  CG  ASP A 120      27.886  17.841  14.704  1.00 17.88           C  
ATOM    948  OD1 ASP A 120      27.559  18.661  15.577  1.00 17.63           O  
ATOM    949  OD2 ASP A 120      28.216  18.084  13.527  1.00 19.85           O  
ATOM    950  N   VAL A 121      25.707  17.154  17.805  1.00 13.14           N  
ATOM    951  CA  VAL A 121      24.375  17.607  18.178  1.00 13.58           C  
ATOM    952  C   VAL A 121      24.091  19.068  17.845  1.00 13.86           C  
ATOM    953  O   VAL A 121      22.979  19.554  18.173  1.00 12.09           O  
ATOM    954  CB  VAL A 121      24.052  17.293  19.672  1.00 13.35           C  
ATOM    955  CG1 VAL A 121      23.804  15.801  19.848  1.00 15.66           C  
ATOM    956  CG2 VAL A 121      25.069  17.802  20.658  1.00 13.49           C  
ATOM    957  N   ARG A 122      25.014  19.714  17.153  1.00 15.21           N  
ATOM    958  CA  ARG A 122      24.757  21.160  16.796  1.00 15.67           C  
ATOM    959  C   ARG A 122      23.516  21.365  15.984  1.00 15.55           C  
ATOM    960  O   ARG A 122      22.878  22.425  16.166  1.00 16.04           O  
ATOM    961  CB  ARG A 122      25.958  21.703  15.998  1.00 18.33           C  
ATOM    962  CG  ARG A 122      27.270  21.543  16.703  1.00 21.40           C  
ATOM    963  CD  ARG A 122      28.486  21.920  15.926  1.00 25.40           C  
ATOM    964  NE  ARG A 122      28.840  20.982  14.869  1.00 28.60           N  
ATOM    965  CZ  ARG A 122      29.959  21.129  14.131  1.00 30.61           C  
ATOM    966  NH1 ARG A 122      30.745  22.189  14.377  1.00 32.16           N  
ATOM    967  NH2 ARG A 122      30.281  20.250  13.183  1.00 30.03           N  
ATOM    968  N   GLN A 123      23.120  20.500  15.084  1.00 14.49           N  
ATOM    969  CA  GLN A 123      21.934  20.646  14.247  1.00 15.70           C  
ATOM    970  C   GLN A 123      20.676  20.982  15.048  1.00 15.01           C  
ATOM    971  O   GLN A 123      19.781  21.684  14.554  1.00 14.88           O  
ATOM    972  CB  GLN A 123      21.630  19.375  13.404  1.00 19.69           C  
ATOM    973  CG  GLN A 123      21.149  18.245  14.285  1.00 23.90           C  
ATOM    974  CD  GLN A 123      20.349  17.083  13.822  1.00 26.52           C  
ATOM    975  OE1 GLN A 123      19.117  17.026  13.704  1.00 27.23           O  
ATOM    976  NE2 GLN A 123      21.063  15.983  13.580  1.00 27.70           N  
ATOM    977  N   TYR A 124      20.566  20.463  16.283  1.00 14.21           N  
ATOM    978  CA  TYR A 124      19.372  20.696  17.061  1.00 13.57           C  
ATOM    979  C   TYR A 124      19.169  22.164  17.443  1.00 14.09           C  
ATOM    980  O   TYR A 124      17.964  22.473  17.582  1.00 16.15           O  
ATOM    981  CB  TYR A 124      19.235  19.797  18.282  1.00 12.10           C  
ATOM    982  CG  TYR A 124      19.226  18.335  17.837  1.00 14.14           C  
ATOM    983  CD1 TYR A 124      18.059  17.708  17.432  1.00 15.09           C  
ATOM    984  CD2 TYR A 124      20.407  17.596  17.844  1.00 14.87           C  
ATOM    985  CE1 TYR A 124      18.077  16.360  17.040  1.00 15.04           C  
ATOM    986  CE2 TYR A 124      20.430  16.233  17.444  1.00 14.04           C  
ATOM    987  CZ  TYR A 124      19.256  15.643  17.052  1.00 14.50           C  
ATOM    988  OH  TYR A 124      19.289  14.333  16.666  1.00 14.93           O  
ATOM    989  N   VAL A 125      20.207  22.948  17.552  1.00 12.92           N  
ATOM    990  CA  VAL A 125      19.992  24.363  17.916  1.00 14.47           C  
ATOM    991  C   VAL A 125      20.338  25.336  16.781  1.00 15.44           C  
ATOM    992  O   VAL A 125      20.150  26.526  17.068  1.00 13.80           O  
ATOM    993  CB  VAL A 125      20.844  24.726  19.167  1.00 14.21           C  
ATOM    994  CG1 VAL A 125      20.383  23.925  20.378  1.00 14.73           C  
ATOM    995  CG2 VAL A 125      22.332  24.511  18.878  1.00 13.76           C  
ATOM    996  N   GLN A 126      20.767  24.874  15.665  1.00 15.29           N  
ATOM    997  CA  GLN A 126      21.187  25.714  14.546  1.00 18.51           C  
ATOM    998  C   GLN A 126      20.129  26.664  14.093  1.00 17.87           C  
ATOM    999  O   GLN A 126      19.004  26.225  13.823  1.00 18.88           O  
ATOM   1000  CB  GLN A 126      21.693  24.860  13.393  1.00 24.07           C  
ATOM   1001  CG  GLN A 126      20.799  24.658  12.192  1.00 31.00           C  
ATOM   1002  CD  GLN A 126      21.326  23.532  11.317  1.00 36.81           C  
ATOM   1003  OE1 GLN A 126      20.609  22.568  10.954  1.00 40.06           O  
ATOM   1004  NE2 GLN A 126      22.632  23.634  11.015  1.00 38.23           N  
ATOM   1005  N   GLY A 127      20.467  27.966  14.034  1.00 17.71           N  
ATOM   1006  CA  GLY A 127      19.542  28.998  13.566  1.00 15.54           C  
ATOM   1007  C   GLY A 127      18.487  29.449  14.543  1.00 14.80           C  
ATOM   1008  O   GLY A 127      17.658  30.341  14.212  1.00 14.24           O  
ATOM   1009  N   CYS A 128      18.495  28.881  15.749  1.00 13.26           N  
ATOM   1010  CA  CYS A 128      17.481  29.213  16.727  1.00 12.80           C  
ATOM   1011  C   CYS A 128      17.707  30.511  17.521  1.00 12.65           C  
ATOM   1012  O   CYS A 128      16.731  30.870  18.211  1.00 12.00           O  
ATOM   1013  CB  CYS A 128      17.207  28.050  17.706  1.00 11.89           C  
ATOM   1014  SG  CYS A 128      16.757  26.521  16.845  1.00 11.21           S  
ATOM   1015  N   GLY A 129      18.875  31.091  17.481  1.00 13.41           N  
ATOM   1016  CA  GLY A 129      19.052  32.342  18.271  1.00 15.20           C  
ATOM   1017  C   GLY A 129      19.333  32.044  19.735  1.00 17.82           C  
ATOM   1018  O   GLY A 129      19.100  32.937  20.587  1.00 18.99           O  
ATOM   1019  N   VAL A 130      19.800  30.832  20.035  1.00 17.79           N  
ATOM   1020  CA  VAL A 130      20.131  30.496  21.445  1.00 19.69           C  
ATOM   1021  C   VAL A 130      21.652  30.434  21.678  1.00 20.54           C  
ATOM   1022  O   VAL A 130      22.412  30.368  20.694  1.00 22.06           O  
ATOM   1023  CB  VAL A 130      19.407  29.231  21.909  1.00 19.42           C  
ATOM   1024  CG1 VAL A 130      17.902  29.422  21.830  1.00 17.32           C  
ATOM   1025  CG2 VAL A 130      19.893  28.013  21.138  1.00 19.01           C  
ATOM   1026  OXT VAL A 130      22.044  30.474  22.846  1.00 20.58           O  
TER    1027      VAL A 130                                                      
HETATM 1028  O   HOH A 131       4.397  17.674  13.328  1.00 48.62           O  
HETATM 1029  O   HOH A 132      12.207  19.112  13.790  1.00 24.80           O  
HETATM 1030  O   HOH A 133      17.556  14.241  14.268  1.00 31.34           O  
HETATM 1031  O   HOH A 134      27.242  12.511  14.276  1.00 20.57           O  
HETATM 1032  O   HOH A 135      10.428  21.186  14.442  1.00 19.68           O  
HETATM 1033  O   HOH A 136      11.593  25.628  14.463  1.00 16.69           O  
HETATM 1034  O   HOH A 137      14.579  18.302  14.972  1.00 15.41           O  
HETATM 1035  O   HOH A 138      28.479   9.309  14.976  1.00 25.94           O  
HETATM 1036  O   HOH A 139       8.959  17.555  14.979  1.00 28.77           O  
HETATM 1037  O   HOH A 140      10.037  15.535  15.372  1.00 52.04           O  
HETATM 1038  O   HOH A 141      10.779  29.806  15.455  1.00 19.10           O  
HETATM 1039  O   HOH A 142       8.283  19.875  15.537  1.00 22.23           O  
HETATM 1040  O   HOH A 143      10.232  26.912  15.847  1.00 19.94           O  
HETATM 1041  O   HOH A 144       4.162  22.163  16.072  1.00 39.99           O  
HETATM 1042  O   HOH A 145      21.638  13.002  17.018  1.00 19.60           O  
HETATM 1043  O   HOH A 146       6.178  14.576  17.135  1.00 29.41           O  
HETATM 1044  O   HOH A 147      21.033  29.149  17.981  1.00 24.39           O  
HETATM 1045  O   HOH A 148      19.466  25.674  35.856  1.00 34.20           O  
HETATM 1046  O   HOH A 149       9.031  31.271  19.104  1.00 27.73           O  
HETATM 1047  O   HOH A 150      28.024  18.452  19.157  1.00 23.11           O  
HETATM 1048  O   HOH A 151       5.150  11.964  20.009  1.00 24.46           O  
HETATM 1049  O   HOH A 152      24.977   7.855  20.263  1.00 15.17           O  
HETATM 1050  O   HOH A 153      14.787   6.665  20.443  1.00 32.15           O  
HETATM 1051  O   HOH A 154      16.663   5.113  21.044  1.00 22.79           O  
HETATM 1052  O   HOH A 155       4.909   9.432  21.612  1.00 29.26           O  
HETATM 1053  O   HOH A 156       0.561  17.409  21.857  1.00 15.57           O  
HETATM 1054  O   HOH A 157      -2.169  23.069  22.034  1.00 34.73           O  
HETATM 1055  O   HOH A 158      26.464  20.952  22.229  1.00 29.45           O  
HETATM 1056  O   HOH A 159       2.765   8.984  22.724  1.00 41.16           O  
HETATM 1057  O   HOH A 160      24.096  23.789  22.932  1.00 11.89           O  
HETATM 1058  O   HOH A 161      26.359  14.640  22.942  1.00 15.91           O  
HETATM 1059  O   HOH A 162      26.552   5.694  23.112  1.00 24.52           O  
HETATM 1060  O   HOH A 163      -1.660  20.415  23.312  1.00 37.05           O  
HETATM 1061  O   HOH A 164       4.276   5.173  23.376  1.00 33.86           O  
HETATM 1062  O   HOH A 165      10.852   6.941  23.762  1.00 38.68           O  
HETATM 1063  O   HOH A 166       6.516   7.490  24.256  1.00 41.30           O  
HETATM 1064  O   HOH A 167      15.521  32.206  24.999  1.00 21.93           O  
HETATM 1065  O   HOH A 168       1.930   3.105  25.519  1.00 31.68           O  
HETATM 1066  O   HOH A 169       4.085  26.000  26.208  1.00 25.70           O  
HETATM 1067  O   HOH A 170       9.296   6.131  26.348  1.00 23.61           O  
HETATM 1068  O   HOH A 171       5.382  -2.215  26.720  1.00 31.26           O  
HETATM 1069  O   HOH A 172      -3.742  26.965  26.727  1.00 77.15           O  
HETATM 1070  O   HOH A 173       0.065  19.089  26.808  1.00 25.35           O  
HETATM 1071  O   HOH A 174      10.305  35.274  27.129  1.00 38.43           O  
HETATM 1072  O   HOH A 175      15.501   6.467  27.178  1.00 14.94           O  
HETATM 1073  O   HOH A 176      27.228  19.075  27.238  1.00  8.22           O  
HETATM 1074  O   HOH A 177      17.147  33.333  27.268  1.00 42.73           O  
HETATM 1075  O   HOH A 178       0.173   5.349  27.582  1.00 34.27           O  
HETATM 1076  O   HOH A 179      27.869   6.355  29.006  1.00 42.70           O  
HETATM 1077  O   HOH A 180       6.578  26.098  28.529  1.00 17.50           O  
HETATM 1078  O   HOH A 181      10.452  29.587  28.873  1.00 23.34           O  
HETATM 1079  O   HOH A 182       6.148  17.344  29.250  1.00 13.34           O  
HETATM 1080  O   HOH A 183      -2.536  17.406  29.219  1.00 41.89           O  
HETATM 1081  O   HOH A 184      12.529   7.603  29.353  1.00 25.86           O  
HETATM 1082  O   HOH A 185       8.685  -2.714  29.530  1.00 38.32           O  
HETATM 1083  O   HOH A 186       7.702  28.659  29.535  1.00 24.70           O  
HETATM 1084  O   HOH A 187      11.442   3.207  29.975  1.00 57.55           O  
HETATM 1085  O   HOH A 188      19.771  28.390  29.991  1.00 13.17           O  
HETATM 1086  O   HOH A 189      16.143   5.202  30.079  1.00 26.01           O  
HETATM 1087  O   HOH A 190       4.954  19.337  30.235  1.00 16.70           O  
HETATM 1088  O   HOH A 191       8.579  14.993  30.575  1.00  8.52           O  
HETATM 1089  O   HOH A 192      14.637   6.830  30.797  1.00 35.13           O  
HETATM 1090  O   HOH A 193      25.714   4.981  30.895  1.00 43.73           O  
HETATM 1091  O   HOH A 194      22.964  29.178  31.092  1.00 30.20           O  
HETATM 1092  O   HOH A 195      -0.218  23.788  31.186  1.00 30.89           O  
HETATM 1093  O   HOH A 196      -0.143   4.265  31.393  1.00 19.13           O  
HETATM 1094  O   HOH A 197      23.336  27.830  14.600  1.00 30.03           O  
HETATM 1095  O   HOH A 198      -1.563  17.977  31.601  1.00 43.80           O  
HETATM 1096  O   HOH A 199       1.658  -4.848  32.313  1.00 25.61           O  
HETATM 1097  O   HOH A 200      18.612   7.611  15.975  1.00 57.62           O  
HETATM 1098  O   HOH A 201       5.205  20.468  32.730  1.00 11.08           O  
HETATM 1099  O   HOH A 202       7.103  29.625  32.796  1.00 23.78           O  
HETATM 1100  O   HOH A 203      -0.864   6.548  32.850  1.00 25.06           O  
HETATM 1101  O   HOH A 204      15.676   8.683  32.943  1.00 22.94           O  
HETATM 1102  O   HOH A 205      12.644   8.674  33.264  1.00 25.47           O  
HETATM 1103  O   HOH A 206      23.444  26.770  33.152  1.00 33.55           O  
HETATM 1104  O   HOH A 207       4.331  23.341  34.075  1.00 15.55           O  
HETATM 1105  O   HOH A 208      25.046  16.153  34.823  1.00 14.05           O  
HETATM 1106  O   HOH A 209       1.979   3.283  35.051  1.00 10.91           O  
HETATM 1107  O   HOH A 210       5.338  28.583  35.086  1.00 35.78           O  
HETATM 1108  O   HOH A 211      -1.974  18.608  35.300  1.00 19.97           O  
HETATM 1109  O   HOH A 212      10.911   1.824  35.578  1.00 19.25           O  
HETATM 1110  O   HOH A 213      10.913  25.126  35.696  1.00 27.60           O  
HETATM 1111  O   HOH A 214       1.017   0.300  36.162  1.00 26.39           O  
HETATM 1112  O   HOH A 215      27.359  23.895  36.396  1.00 38.90           O  
HETATM 1113  O   HOH A 216      17.733   7.930  36.516  1.00 41.81           O  
HETATM 1114  O   HOH A 217      13.645  24.800  36.886  1.00 23.53           O  
HETATM 1115  O   HOH A 218      24.011  23.598  37.000  1.00 30.68           O  
HETATM 1116  O   HOH A 219      17.896  26.235  37.463  1.00 31.58           O  
HETATM 1117  O   HOH A 220      24.812  15.506  37.523  1.00 21.69           O  
HETATM 1118  O   HOH A 221       7.625  24.610  38.207  1.00 39.99           O  
HETATM 1119  O   HOH A 222      -0.938  -1.193  38.272  1.00 35.09           O  
HETATM 1120  O   HOH A 223      14.051  23.630  39.014  1.00 52.98           O  
HETATM 1121  O   HOH A 224      25.801   1.987  27.993  1.00 32.57           O  
HETATM 1122  O   HOH A 225      22.459   7.349  39.341  1.00 54.71           O  
HETATM 1123  O   HOH A 226      14.676  20.734  40.262  1.00 22.38           O  
HETATM 1124  O   HOH A 227       3.810   6.254  40.354  1.00 13.45           O  
HETATM 1125  O   HOH A 228      10.181  18.691  40.472  1.00 35.22           O  
HETATM 1126  O   HOH A 229      16.767   6.516  40.726  1.00 57.67           O  
HETATM 1127  O   HOH A 230       1.361  17.941  40.865  1.00  8.93           O  
HETATM 1128  O   HOH A 231      19.155  23.015  40.968  1.00 42.41           O  
HETATM 1129  O   HOH A 232      -1.047  -0.840  40.995  1.00 54.63           O  
HETATM 1130  O   HOH A 233       6.694   7.342  41.232  1.00 25.18           O  
HETATM 1131  O   HOH A 234       2.547   4.487  41.939  1.00 15.67           O  
HETATM 1132  O   HOH A 235       3.018  20.597  42.031  1.00 38.20           O  
HETATM 1133  O   HOH A 236      15.007   8.722  42.233  1.00 40.82           O  
HETATM 1134  O   HOH A 237      10.906   0.371  42.596  1.00 51.78           O  
HETATM 1135  O   HOH A 238       0.279  12.827  43.089  1.00  5.00           O  
HETATM 1136  O   HOH A 239       4.718   7.288  43.337  1.00 43.68           O  
HETATM 1137  O   HOH A 240      24.954  25.327  24.431  1.00 29.52           O  
HETATM 1138  O   HOH A 241       7.382  19.186  43.695  1.00 52.23           O  
HETATM 1139  O   HOH A 242      11.280   3.160  43.437  1.00 45.72           O  
HETATM 1140  O   HOH A 243       0.874   1.476  43.526  1.00 38.00           O  
HETATM 1141  O   HOH A 244       0.352  17.440  43.982  1.00 22.58           O  
HETATM 1142  O   HOH A 245       3.058  14.283  44.153  1.00 26.05           O  
HETATM 1143  O   HOH A 246       2.409   5.763  44.347  1.00 41.32           O  
HETATM 1144  O   HOH A 247      14.311  17.158  44.359  1.00 32.49           O  
HETATM 1145  O   HOH A 248      -0.928   4.331  44.781  1.00 40.28           O  
HETATM 1146  O   HOH A 249       2.664  16.630  44.786  1.00 28.98           O  
HETATM 1147  O   HOH A 250       4.394   3.060  45.018  1.00 48.86           O  
HETATM 1148  O   HOH A 251      22.971  25.936  21.989  1.00 50.79           O  
HETATM 1149  O   HOH A 252       4.853   8.070  45.826  1.00 35.83           O  
HETATM 1150  O   HOH A 253       3.659  10.425  46.134  1.00 51.64           O  
HETATM 1151  O   HOH A 254      12.842  14.329  46.245  1.00 28.19           O  
HETATM 1152  O   HOH A 255       9.685   0.501  46.505  1.00 37.60           O  
HETATM 1153  O   HOH A 256       1.667   7.850  46.624  1.00 40.55           O  
HETATM 1154  O   HOH A 257      13.712  11.105  46.743  1.00 34.79           O  
HETATM 1155  O   HOH A 258       7.168   2.651  47.536  1.00 45.74           O  
CONECT   53 1014                                                                
CONECT  243  913                                                                
CONECT  534  642                                                                
CONECT  612  738                                                                
CONECT  642  534                                                                
CONECT  738  612                                                                
CONECT  913  243                                                                
CONECT 1014   53                                                                
MASTER      298    0    0    5    5    0    0    6 1154    1    8   10          
END                                                                             
