HEADER    SIGNALING PROTEIN                       17-NOV-19   6TGS              
TITLE     ATNBR1-PB1 DOMAIN                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN NBR1 HOMOLOG;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ATNBR1,AT4G24690;                                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: NBR1, AT4G24690, F22K18.110;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    AUTOPHAGY, SIGNALING PROTEIN                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.JAKOBI,C.SACHSE                                                   
REVDAT   1   12-FEB-20 6TGS    0                                                
JRNL        AUTH   A.J.JAKOBI,S.T.HUBER,S.A.MORTENSEN,S.W.SCHULTZ,A.PALARA,     
JRNL        AUTH 2 T.KUHM,B.K.SHRESTHA,T.LAMARK,W.J.H.HAGEN,M.WILMANNS,         
JRNL        AUTH 3 T.JOHANSEN,A.BRECH,C.SACHSE                                  
JRNL        TITL   STRUCTURAL BASIS OF P62/SQSTM1 HELICAL FILAMENTS AND THEIR   
JRNL        TITL 2 ROLE IN CELLULAR CARGO UPTAKE.                               
JRNL        REF    NAT COMMUN                    V.  11   440 2020              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31974402                                                     
JRNL        DOI    10.1038/S41467-020-14343-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_3500: ???)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.220                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12367                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.160                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1227                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.7324 -  3.1821    0.98     2509   140  0.1931 0.2329        
REMARK   3     2  3.1821 -  2.5258    0.99     2536   121  0.2078 0.2250        
REMARK   3     3  2.5258 -  2.2066    0.99     2480   157  0.2049 0.2293        
REMARK   3     4  2.2066 -  2.0048    0.97     2447   150  0.2113 0.2833        
REMARK   3     5  2.0048 -  1.8611    0.99     2541   126  0.2258 0.2472        
REMARK   3     6  1.8611 -  1.7514    0.99     2552   127  0.2844 0.2791        
REMARK   3     7  1.7514 -  1.6637    0.98     2479   151  0.3179 0.3576        
REMARK   3     8  1.6637 -  1.5913    0.99     2501   151  0.3310 0.3807        
REMARK   3     9  1.5913 -  1.5300    0.97     2497   104  0.3668 0.4122        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.000           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007            783                                  
REMARK   3   ANGLE     :  0.900           1054                                  
REMARK   3   CHIRALITY :  0.057            120                                  
REMARK   3   PLANARITY :  0.005            138                                  
REMARK   3   DIHEDRAL  :  5.793            601                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6TGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-NOV-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102752.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12367                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.02799                            
REMARK 200  R SYM                      (I) : 0.03958                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41320                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.420                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: EMD-10499                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES (PH 6.5), 18-20% (W/V)         
REMARK 280  PEG20000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       21.56400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.71900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.56400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.71900            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 5880 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 S    SO4 A 108  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 225  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     VAL A    93                                                      
REMARK 465     SER A    94                                                      
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   O2   GOL A   105     O    HOH A   201              1.95            
REMARK 500   O1   SIN A   110     O    HOH A   201              2.03            
REMARK 500   O    HOH A   204     O    HOH A   223              2.05            
REMARK 500   O1   SIN A   110     O    HOH A   201              2.07            
REMARK 500   O3   SIN A   110     O    HOH A   202              2.13            
REMARK 500   O1   GOL A   103     O    HOH A   203              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A  11   C     VAL A  12   N      -0.164                       
REMARK 500    LYS A  83   C     PHE A  84   N      -0.145                       
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    ASN A  28   CB  -  CA  -  C   ANGL. DEV. = -17.3 DEGREES          
REMARK 500    PHE A  84   C   -  N   -  CA  ANGL. DEV. =  18.8 DEGREES          
REMARK 500    PHE A  84   O   -  C   -  N   ANGL. DEV. =  11.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 106                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 107                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 108                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 109                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SIN A 110                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-10500   RELATED DB: EMDB                             
REMARK 900 RELATED ID: 6TGP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: EMD-10499   RELATED DB: EMDB                             
REMARK 900 RELATED ID: 6TGN   RELATED DB: PDB                                   
DBREF  6TGS A    1    94  UNP    Q9SB64   NBR1_ARATH       1     94             
SEQADV 6TGS ALA A   60  UNP  Q9SB64    ASP    60 ENGINEERED MUTATION            
SEQADV 6TGS ALA A   61  UNP  Q9SB64    GLU    61 ENGINEERED MUTATION            
SEQADV 6TGS ALA A   64  UNP  Q9SB64    ASP    64 ENGINEERED MUTATION            
SEQRES   1 A   94  MET GLU SER THR ALA ASN ALA LEU VAL VAL LYS VAL SER          
SEQRES   2 A   94  TYR GLY GLY VAL LEU ARG ARG PHE ARG VAL PRO VAL LYS          
SEQRES   3 A   94  ALA ASN GLY GLN LEU ASP LEU GLU MET ALA GLY LEU LYS          
SEQRES   4 A   94  GLU LYS ILE ALA ALA LEU PHE ASN LEU SER ALA ASP ALA          
SEQRES   5 A   94  GLU LEU SER LEU THR TYR SER ALA ALA ASP GLY ALA VAL          
SEQRES   6 A   94  VAL ALA LEU VAL ASP ASP ASN ASP LEU PHE ASP VAL THR          
SEQRES   7 A   94  ASN GLN ARG LEU LYS PHE LEU LYS ILE ASN VAL ASN ALA          
SEQRES   8 A   94  GLY VAL SER                                                  
HET    GOL  A 101       6                                                       
HET    GOL  A 102       6                                                       
HET    GOL  A 103       6                                                       
HET    GOL  A 104       6                                                       
HET    GOL  A 105       6                                                       
HET    PEG  A 106       7                                                       
HET    SO4  A 107       5                                                       
HET    SO4  A 108       5                                                       
HET     CL  A 109       1                                                       
HET    SIN  A 110      16                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SIN SUCCINIC ACID                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    5(C3 H8 O3)                                                  
FORMUL   7  PEG    C4 H10 O3                                                    
FORMUL   8  SO4    2(O4 S 2-)                                                   
FORMUL  10   CL    CL 1-                                                        
FORMUL  11  SIN    C4 H6 O4                                                     
FORMUL  12  HOH   *35(H2 O)                                                     
HELIX    1 AA1 GLU A   34  ASN A   47  1                                  14    
HELIX    2 AA2 ASP A   70  GLN A   80  1                                  11    
SHEET    1 AA1 5 VAL A  17  VAL A  23  0                                        
SHEET    2 AA1 5 LEU A   8  TYR A  14 -1  N  VAL A  12   O  ARG A  19           
SHEET    3 AA1 5 PHE A  84  ASN A  90  1  O  LEU A  85   N  LYS A  11           
SHEET    4 AA1 5 SER A  55  SER A  59 -1  N  SER A  55   O  ASN A  90           
SHEET    5 AA1 5 VAL A  65  ALA A  67 -1  O  VAL A  66   N  TYR A  58           
SITE     1 AC1  5 SER A  13  TYR A  14  GLY A  15  GLY A  16                    
SITE     2 AC1  5 VAL A  89                                                     
SITE     1 AC2  5 LYS A  39  GLU A  53  LEU A  54  VAL A  69                    
SITE     2 AC2  5 HOH A 206                                                     
SITE     1 AC3  9 PHE A  21  ARG A  22  TYR A  58  VAL A  66                    
SITE     2 AC3  9 ASP A  73  ASP A  76  GLN A  80  HOH A 203                    
SITE     3 AC3  9 HOH A 208                                                     
SITE     1 AC4  4 ARG A  19  LEU A  45  SER A  55  ALA A  67                    
SITE     1 AC5 12 VAL A  17  ALA A  27  ASP A  51  SO4 A 107                    
SITE     2 AC5 12 SIN A 110  HOH A 201  HOH A 202  HOH A 205                    
SITE     3 AC5 12 HOH A 207  HOH A 210  HOH A 211  HOH A 214                    
SITE     1 AC6  9 SER A  13  GLY A  16  VAL A  17  LEU A  18                    
SITE     2 AC6  9 ALA A  43  LEU A  48  SER A  49  ALA A  50                    
SITE     3 AC6  9 LYS A  86                                                     
SITE     1 AC7  6 LYS A  26  ALA A  27  ASN A  28  GLU A  40                    
SITE     2 AC7  6 GOL A 105  SIN A 110                                          
SITE     1 AC8  1 GLU A  34                                                     
SITE     1 AC9  4 LYS A  11  ASN A  47  ASP A  62  ALA A  64                    
SITE     1 AD1 11 GLY A  16  ALA A  36  LYS A  39  GLU A  40                    
SITE     2 AD1 11 ALA A  50  ASP A  51  GOL A 105  SO4 A 107                    
SITE     3 AD1 11 HOH A 201  HOH A 202  HOH A 216                               
CRYST1   43.128   79.438   24.135  90.00  90.00  90.00 P 21 21 2     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      0.023187  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012588  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.041434        0.00000                         
ATOM      1  N   ALA A   5      14.978  -6.084  10.633  1.00 77.68           N  
ATOM      2  CA  ALA A   5      14.943  -5.724  12.047  1.00 79.41           C  
ATOM      3  C   ALA A   5      15.826  -4.508  12.331  1.00 76.43           C  
ATOM      4  O   ALA A   5      16.196  -4.252  13.478  1.00 77.43           O  
ATOM      5  CB  ALA A   5      15.369  -6.910  12.909  1.00 69.18           C  
ATOM      6  N   ASN A   6      16.163  -3.766  11.276  1.00 72.55           N  
ATOM      7  CA  ASN A   6      16.914  -2.519  11.379  1.00 75.21           C  
ATOM      8  C   ASN A   6      16.064  -1.403  10.785  1.00 67.94           C  
ATOM      9  O   ASN A   6      15.621  -1.498   9.638  1.00 71.02           O  
ATOM     10  CB  ASN A   6      18.269  -2.627  10.671  1.00 66.13           C  
ATOM     11  CG  ASN A   6      18.144  -2.619   9.160  1.00 68.80           C  
ATOM     12  OD1 ASN A   6      17.622  -3.562   8.567  1.00 67.25           O  
ATOM     13  ND2 ASN A   6      18.609  -1.545   8.530  1.00 66.67           N  
ATOM     14  N   ALA A   7      15.827  -0.356  11.564  1.00 59.95           N  
ATOM     15  CA  ALA A   7      14.867   0.664  11.177  1.00 39.16           C  
ATOM     16  C   ALA A   7      15.522   1.748  10.325  1.00 47.31           C  
ATOM     17  O   ALA A   7      16.734   1.968  10.374  1.00 48.13           O  
ATOM     18  CB  ALA A   7      14.225   1.281  12.419  1.00 46.81           C  
ATOM     19  N   LEU A   8      14.694   2.417   9.520  1.00 36.74           N  
ATOM     20  CA  LEU A   8      15.118   3.617   8.813  1.00 34.31           C  
ATOM     21  C   LEU A   8      15.012   4.816   9.742  1.00 28.99           C  
ATOM     22  O   LEU A   8      13.958   5.058  10.333  1.00 26.05           O  
ATOM     23  CB  LEU A   8      14.259   3.849   7.568  1.00 32.92           C  
ATOM     24  CG  LEU A   8      14.469   5.161   6.794  1.00 38.25           C  
ATOM     25  CD1 LEU A   8      15.797   5.163   6.054  1.00 37.17           C  
ATOM     26  CD2 LEU A   8      13.316   5.428   5.830  1.00 35.42           C  
ATOM     27  N   VAL A   9      16.098   5.566   9.863  1.00 27.24           N  
ATOM     28  CA  VAL A   9      16.064   6.828  10.590  1.00 28.03           C  
ATOM     29  C   VAL A   9      15.542   7.902   9.642  1.00 21.75           C  
ATOM     30  O   VAL A   9      16.086   8.103   8.553  1.00 25.52           O  
ATOM     31  CB  VAL A   9      17.451   7.195  11.132  1.00 30.01           C  
ATOM     32  CG1 VAL A   9      17.433   8.599  11.707  1.00 25.26           C  
ATOM     33  CG2 VAL A   9      17.864   6.195  12.189  1.00 38.41           C  
ATOM     34  N   VAL A  10      14.480   8.584  10.058  1.00 17.24           N  
ATOM     35  CA  VAL A  10      13.881   9.660   9.276  1.00 18.52           C  
ATOM     36  C   VAL A  10      14.080  10.954  10.047  1.00 20.25           C  
ATOM     37  O   VAL A  10      13.753  11.033  11.234  1.00 23.20           O  
ATOM     38  CB  VAL A  10      12.393   9.395   8.997  1.00 19.65           C  
ATOM     39  CG1 VAL A  10      11.780  10.550   8.200  1.00 23.23           C  
ATOM     40  CG2 VAL A  10      12.231   8.085   8.244  1.00 20.52           C  
ATOM     41  N   LYS A  11      14.652  11.945   9.392  1.00 16.64           N  
ATOM     42  CA  LYS A  11      14.685  13.328   9.915  1.00 17.25           C  
ATOM     43  C   LYS A  11      13.742  14.256   9.125  1.00 21.98           C  
ATOM     44  O   LYS A  11      13.863  14.203   7.929  1.00 22.11           O  
ATOM     45  CB  LYS A  11      16.127  13.817   9.985  1.00 17.82           C  
ATOM     46  CG  LYS A  11      17.001  12.963  10.882  1.00 23.72           C  
ATOM     47  CD  LYS A  11      18.404  13.466  10.986  1.00 25.17           C  
ATOM     48  CE  LYS A  11      19.328  12.400  11.526  1.00 37.53           C  
ATOM     49  NZ  LYS A  11      20.747  12.740  11.283  1.00 45.57           N  
ATOM     50  N  AVAL A  12      12.995  14.979   9.731  0.70 16.01           N  
ATOM     51  N  BVAL A  12      13.011  14.959   9.712  0.30 16.13           N  
ATOM     52  CA AVAL A  12      12.055  15.848   9.034  0.70 16.87           C  
ATOM     53  CA BVAL A  12      12.092  15.827   8.981  0.30 16.90           C  
ATOM     54  C  AVAL A  12      12.389  17.280   9.414  0.70 16.21           C  
ATOM     55  C  BVAL A  12      12.384  17.271   9.363  0.30 16.29           C  
ATOM     56  O  AVAL A  12      12.611  17.578  10.592  0.70 16.77           O  
ATOM     57  O  BVAL A  12      12.535  17.587  10.548  0.30 16.99           O  
ATOM     58  CB AVAL A  12      10.595  15.509   9.387  0.70 18.59           C  
ATOM     59  CB BVAL A  12      10.617  15.470   9.245  0.30 18.47           C  
ATOM     60  CG1AVAL A  12       9.653  16.354   8.547  0.70 18.51           C  
ATOM     61  CG1BVAL A  12      10.274  15.677  10.721  0.30 17.34           C  
ATOM     62  CG2AVAL A  12      10.318  14.030   9.164  0.70 19.11           C  
ATOM     63  CG2BVAL A  12       9.689  16.266   8.340  0.30 15.65           C  
ATOM     64  N  ASER A  13      12.459  18.156   8.420  0.70 15.33           N  
ATOM     65  N  BSER A  13      12.494  18.214   8.464  0.30 15.33           N  
ATOM     66  CA ASER A  13      12.719  19.568   8.645  0.70 17.75           C  
ATOM     67  CA BSER A  13      12.799  19.611   8.746  0.30 18.10           C  
ATOM     68  C  ASER A  13      11.486  20.390   8.298  0.70 21.85           C  
ATOM     69  C  BSER A  13      11.641  20.488   8.290  0.30 21.82           C  
ATOM     70  O  ASER A  13      10.930  20.264   7.197  0.70 18.91           O  
ATOM     71  O  BSER A  13      11.281  20.483   7.106  0.30 20.37           O  
ATOM     72  CB ASER A  13      13.915  20.039   7.824  0.70 20.04           C  
ATOM     73  CB BSER A  13      14.102  20.035   8.067  0.30 20.61           C  
ATOM     74  OG ASER A  13      14.177  21.398   8.098  0.70 24.59           O  
ATOM     75  OG BSER A  13      14.007  19.954   6.659  0.30 25.31           O  
ATOM     76  N   TYR A  14      11.066  21.237   9.230  1.00 20.90           N  
ATOM     77  CA  TYR A  14      10.010  22.195   8.954  1.00 22.55           C  
ATOM     78  C   TYR A  14      10.251  23.434   9.805  1.00 27.32           C  
ATOM     79  O   TYR A  14      10.613  23.317  10.976  1.00 31.62           O  
ATOM     80  CB  TYR A  14       8.616  21.614   9.257  1.00 21.27           C  
ATOM     81  CG  TYR A  14       7.490  22.596   9.067  1.00 21.24           C  
ATOM     82  CD1 TYR A  14       7.022  22.902   7.800  1.00 28.76           C  
ATOM     83  CD2 TYR A  14       6.887  23.212  10.160  1.00 26.14           C  
ATOM     84  CE1 TYR A  14       5.986  23.803   7.617  1.00 32.82           C  
ATOM     85  CE2 TYR A  14       5.847  24.109   9.986  1.00 25.22           C  
ATOM     86  CZ  TYR A  14       5.404  24.401   8.711  1.00 29.00           C  
ATOM     87  OH  TYR A  14       4.380  25.300   8.536  1.00 33.49           O  
ATOM     88  N   GLY A  15      10.079  24.606   9.202  1.00 30.60           N  
ATOM     89  CA  GLY A  15      10.226  25.855   9.951  1.00 43.62           C  
ATOM     90  C   GLY A  15      11.535  25.985  10.699  1.00 38.28           C  
ATOM     91  O   GLY A  15      11.541  26.384  11.871  1.00 41.79           O  
ATOM     92  N   GLY A  16      12.649  25.636  10.054  1.00 31.49           N  
ATOM     93  CA  GLY A  16      13.963  25.720  10.676  1.00 29.08           C  
ATOM     94  C   GLY A  16      14.233  24.692  11.746  1.00 36.19           C  
ATOM     95  O   GLY A  16      15.237  24.800  12.458  1.00 30.69           O  
ATOM     96  N   VAL A  17      13.370  23.690  11.861  1.00 32.17           N  
ATOM     97  CA  VAL A  17      13.322  22.770  12.983  1.00 30.87           C  
ATOM     98  C   VAL A  17      13.527  21.365  12.446  1.00 25.30           C  
ATOM     99  O   VAL A  17      12.863  20.983  11.481  1.00 30.69           O  
ATOM    100  CB  VAL A  17      11.959  22.874  13.697  1.00 36.21           C  
ATOM    101  CG1 VAL A  17      11.852  21.881  14.782  1.00 26.08           C  
ATOM    102  CG2 VAL A  17      11.734  24.273  14.214  1.00 35.41           C  
ATOM    103  N   LEU A  18      14.403  20.587  13.083  1.00 19.18           N  
ATOM    104  CA  LEU A  18      14.641  19.198  12.694  1.00 18.65           C  
ATOM    105  C   LEU A  18      14.112  18.237  13.751  1.00 17.45           C  
ATOM    106  O   LEU A  18      14.440  18.361  14.937  1.00 21.01           O  
ATOM    107  CB  LEU A  18      16.135  18.942  12.468  1.00 25.44           C  
ATOM    108  CG  LEU A  18      16.600  17.700  11.703  1.00 24.52           C  
ATOM    109  CD1 LEU A  18      16.039  17.665  10.275  1.00 23.35           C  
ATOM    110  CD2 LEU A  18      18.139  17.606  11.676  1.00 26.72           C  
ATOM    111  N   ARG A  19      13.348  17.252  13.322  1.00 15.49           N  
ATOM    112  CA  ARG A  19      12.860  16.214  14.221  1.00 17.54           C  
ATOM    113  C   ARG A  19      13.205  14.854  13.643  1.00 20.78           C  
ATOM    114  O   ARG A  19      13.238  14.673  12.423  1.00 23.20           O  
ATOM    115  CB  ARG A  19      11.342  16.333  14.449  1.00 16.30           C  
ATOM    116  CG  ARG A  19      10.928  17.629  15.154  1.00 15.86           C  
ATOM    117  CD  ARG A  19      11.321  17.609  16.645  1.00 18.22           C  
ATOM    118  NE  ARG A  19      10.915  18.831  17.353  1.00 20.44           N  
ATOM    119  CZ  ARG A  19      11.720  19.878  17.527  1.00 19.77           C  
ATOM    120  NH1 ARG A  19      12.946  19.852  17.012  1.00 19.03           N  
ATOM    121  NH2 ARG A  19      11.309  20.945  18.213  1.00 20.20           N  
ATOM    122  N   ARG A  20      13.518  13.853  14.435  1.00 13.55           N  
ATOM    123  CA  ARG A  20      14.011  12.506  14.181  1.00 14.82           C  
ATOM    124  C   ARG A  20      12.993  11.476  14.638  1.00 16.72           C  
ATOM    125  O   ARG A  20      12.472  11.568  15.753  1.00 20.37           O  
ATOM    126  CB  ARG A  20      15.331  12.274  14.925  1.00 18.97           C  
ATOM    127  CG  ARG A  20      15.961  10.899  14.716  1.00 31.81           C  
ATOM    128  CD  ARG A  20      17.291  10.787  15.488  1.00 26.68           C  
ATOM    129  NE  ARG A  20      17.912   9.489  15.308  1.00 37.61           N  
ATOM    130  CZ  ARG A  20      17.624   8.432  16.051  1.00 42.79           C  
ATOM    131  NH1 ARG A  20      16.713   8.537  17.008  1.00 44.74           N  
ATOM    132  NH2 ARG A  20      18.229   7.273  15.829  1.00 54.78           N  
ATOM    133  N   PHE A  21      12.658  10.528  13.906  1.00 18.84           N  
ATOM    134  CA  PHE A  21      11.963   9.338  14.378  1.00 19.40           C  
ATOM    135  C   PHE A  21      12.458   8.150  13.566  1.00 20.89           C  
ATOM    136  O   PHE A  21      13.164   8.308  12.570  1.00 23.74           O  
ATOM    137  CB  PHE A  21      10.437   9.479  14.303  1.00 18.12           C  
ATOM    138  CG  PHE A  21       9.914   9.789  12.936  1.00 19.99           C  
ATOM    139  CD1 PHE A  21       9.792  11.096  12.517  1.00 21.41           C  
ATOM    140  CD2 PHE A  21       9.507   8.771  12.083  1.00 23.13           C  
ATOM    141  CE1 PHE A  21       9.290  11.397  11.261  1.00 23.78           C  
ATOM    142  CE2 PHE A  21       8.992   9.066  10.821  1.00 24.69           C  
ATOM    143  CZ  PHE A  21       8.892  10.387  10.418  1.00 20.30           C  
ATOM    144  N   ARG A  22      12.094   6.948  13.993  1.00 22.91           N  
ATOM    145  CA  ARG A  22      12.558   5.751  13.305  1.00 24.79           C  
ATOM    146  C   ARG A  22      11.373   4.954  12.791  1.00 23.16           C  
ATOM    147  O   ARG A  22      10.318   4.890  13.430  1.00 26.18           O  
ATOM    148  CB  ARG A  22      13.420   4.880  14.223  1.00 25.90           C  
ATOM    149  CG  ARG A  22      14.643   5.597  14.770  1.00 27.23           C  
ATOM    150  CD  ARG A  22      15.746   4.618  15.156  1.00 38.86           C  
ATOM    151  NE  ARG A  22      15.268   3.563  16.046  1.00 37.78           N  
ATOM    152  CZ  ARG A  22      15.858   2.381  16.182  1.00 41.75           C  
ATOM    153  NH1 ARG A  22      16.950   2.096  15.486  1.00 34.79           N  
ATOM    154  NH2 ARG A  22      15.352   1.479  17.011  1.00 41.19           N  
ATOM    155  N   VAL A  23      11.560   4.331  11.629  1.00 26.26           N  
ATOM    156  CA  VAL A  23      10.504   3.616  10.939  1.00 27.81           C  
ATOM    157  C   VAL A  23      10.938   2.157  10.814  1.00 27.46           C  
ATOM    158  O   VAL A  23      11.993   1.881  10.235  1.00 30.82           O  
ATOM    159  CB  VAL A  23      10.208   4.203   9.550  1.00 29.40           C  
ATOM    160  CG1 VAL A  23       9.181   3.341   8.846  1.00 33.58           C  
ATOM    161  CG2 VAL A  23       9.715   5.642   9.681  1.00 27.81           C  
ATOM    162  N   PRO A  24      10.172   1.208  11.340  1.00 31.68           N  
ATOM    163  CA  PRO A  24      10.555  -0.202  11.208  1.00 42.30           C  
ATOM    164  C   PRO A  24      10.509  -0.667   9.760  1.00 42.92           C  
ATOM    165  O   PRO A  24       9.735  -0.169   8.940  1.00 34.49           O  
ATOM    166  CB  PRO A  24       9.514  -0.934  12.064  1.00 38.16           C  
ATOM    167  CG  PRO A  24       8.344  -0.004  12.115  1.00 41.72           C  
ATOM    168  CD  PRO A  24       8.934   1.377  12.116  1.00 34.84           C  
ATOM    169  N   VAL A  25      11.400  -1.605   9.459  1.00 44.43           N  
ATOM    170  CA  VAL A  25      11.436  -2.254   8.124  1.00 44.83           C  
ATOM    171  C   VAL A  25      10.977  -3.705   8.258  1.00 53.86           C  
ATOM    172  O   VAL A  25      11.188  -4.307   9.326  1.00 44.93           O  
ATOM    173  CB  VAL A  25      12.833  -2.164   7.486  1.00 49.97           C  
ATOM    174  CG1 VAL A  25      13.417  -0.766   7.599  1.00 47.38           C  
ATOM    175  CG2 VAL A  25      13.778  -3.207   8.057  1.00 54.93           C  
ATOM    176  N   LYS A  26      10.351  -4.228   7.212  1.00 52.79           N  
ATOM    177  CA  LYS A  26       9.939  -5.648   7.209  1.00 53.26           C  
ATOM    178  C   LYS A  26      11.147  -6.485   6.779  1.00 51.62           C  
ATOM    179  O   LYS A  26      12.172  -5.901   6.409  1.00 53.15           O  
ATOM    180  CB  LYS A  26       8.759  -5.803   6.250  1.00 54.55           C  
ATOM    181  CG  LYS A  26       7.482  -5.103   6.695  1.00 47.27           C  
ATOM    182  CD  LYS A  26       6.615  -4.656   5.543  1.00 62.97           C  
ATOM    183  CE  LYS A  26       5.508  -3.710   5.962  1.00 70.39           C  
ATOM    184  NZ  LYS A  26       4.245  -3.981   5.233  1.00 63.99           N  
ATOM    185  N   ALA A  27      11.006  -7.801   6.776  1.00 59.52           N  
ATOM    186  CA  ALA A  27      12.124  -8.696   6.405  1.00 59.38           C  
ATOM    187  C   ALA A  27      12.461  -8.445   4.939  1.00 63.63           C  
ATOM    188  O   ALA A  27      13.577  -8.818   4.551  1.00 76.46           O  
ATOM    189  CB  ALA A  27      11.687 -10.104   6.653  1.00 50.89           C  
ATOM    190  N   ASN A  28      11.524  -7.889   4.173  1.00 60.66           N  
ATOM    191  CA  ASN A  28      11.675  -7.516   2.750  1.00 60.77           C  
ATOM    192  C   ASN A  28      12.642  -6.357   2.652  1.00 61.73           C  
ATOM    193  O   ASN A  28      13.271  -6.194   1.613  1.00 58.34           O  
ATOM    194  CB  ASN A  28      10.463  -6.640   2.414  1.00 48.97           C  
ATOM    195  CG  ASN A  28       9.333  -7.386   1.755  1.00 68.96           C  
ATOM    196  OD1 ASN A  28       9.173  -7.321   0.542  1.00 79.17           O  
ATOM    197  ND2 ASN A  28       8.543  -8.083   2.555  1.00 76.81           N  
ATOM    198  N   GLY A  29      12.730  -5.591   3.711  1.00 51.51           N  
ATOM    199  CA  GLY A  29      13.509  -4.357   3.606  1.00 59.79           C  
ATOM    200  C   GLY A  29      12.539  -3.227   3.322  1.00 54.84           C  
ATOM    201  O   GLY A  29      12.951  -2.084   3.421  1.00 59.86           O  
ATOM    202  N   GLN A  30      11.289  -3.582   3.064  1.00 40.26           N  
ATOM    203  CA  GLN A  30      10.213  -2.590   2.815  1.00 53.88           C  
ATOM    204  C   GLN A  30       9.893  -1.832   4.107  1.00 47.44           C  
ATOM    205  O   GLN A  30       9.847  -2.469   5.164  1.00 46.30           O  
ATOM    206  CB  GLN A  30       8.938  -3.352   2.456  1.00 53.01           C  
ATOM    207  CG  GLN A  30       8.678  -3.495   0.970  1.00 64.90           C  
ATOM    208  CD  GLN A  30       7.221  -3.815   0.746  1.00 68.61           C  
ATOM    209  OE1 GLN A  30       6.843  -4.963   0.532  1.00 66.61           O  
ATOM    210  NE2 GLN A  30       6.387  -2.791   0.813  1.00 66.63           N  
ATOM    211  N   LEU A  31       9.637  -0.526   4.004  1.00 48.66           N  
ATOM    212  CA  LEU A  31       9.270   0.282   5.193  1.00 41.84           C  
ATOM    213  C   LEU A  31       7.918  -0.186   5.740  1.00 39.01           C  
ATOM    214  O   LEU A  31       7.018  -0.366   4.916  1.00 41.95           O  
ATOM    215  CB  LEU A  31       9.235   1.760   4.794  1.00 47.42           C  
ATOM    216  CG  LEU A  31      10.591   2.445   4.645  1.00 50.88           C  
ATOM    217  CD1 LEU A  31      10.411   3.915   4.297  1.00 38.73           C  
ATOM    218  CD2 LEU A  31      11.418   2.298   5.911  1.00 43.01           C  
ATOM    219  N  AASP A  32       7.731  -0.229   6.935  0.60 38.63           N  
ATOM    220  N  BASP A  32       7.727  -0.199   6.939  0.40 38.70           N  
ATOM    221  CA AASP A  32       6.404  -0.442   7.511  0.60 42.13           C  
ATOM    222  CA BASP A  32       6.429  -0.515   7.521  0.40 42.13           C  
ATOM    223  C  AASP A  32       5.705   0.905   7.704  0.60 39.69           C  
ATOM    224  C  BASP A  32       5.585   0.747   7.664  0.40 39.86           C  
ATOM    225  O  AASP A  32       5.388   1.329   8.814  0.60 39.80           O  
ATOM    226  O  BASP A  32       5.081   1.041   8.752  0.40 40.88           O  
ATOM    227  CB AASP A  32       6.511  -1.215   8.822  0.60 43.67           C  
ATOM    228  CB BASP A  32       6.606  -1.199   8.882  0.40 43.67           C  
ATOM    229  CG AASP A  32       5.185  -1.820   9.259  0.60 49.13           C  
ATOM    230  CG BASP A  32       5.312  -1.791   9.418  0.40 48.87           C  
ATOM    231  OD1AASP A  32       4.162  -1.572   8.587  0.60 54.82           O  
ATOM    232  OD1BASP A  32       4.471  -2.227   8.605  0.40 53.47           O  
ATOM    233  OD2AASP A  32       5.165  -2.545  10.277  0.60 50.96           O  
ATOM    234  OD2BASP A  32       5.134  -1.814  10.655  0.40 49.90           O  
ATOM    235  N  ALEU A  33       5.482   1.585   6.580  0.60 38.64           N  
ATOM    236  N  BLEU A  33       5.431   1.506   6.581  0.40 38.67           N  
ATOM    237  CA ALEU A  33       4.880   2.910   6.580  0.60 36.40           C  
ATOM    238  CA BLEU A  33       4.578   2.685   6.609  0.40 36.89           C  
ATOM    239  C  ALEU A  33       4.448   3.264   5.165  0.60 36.75           C  
ATOM    240  C  BLEU A  33       3.995   2.929   5.224  0.40 36.66           C  
ATOM    241  O  ALEU A  33       5.168   2.979   4.202  0.60 33.43           O  
ATOM    242  O  BLEU A  33       4.300   2.226   4.257  0.40 37.46           O  
ATOM    243  CB ALEU A  33       5.861   3.965   7.112  0.60 34.43           C  
ATOM    244  CB BLEU A  33       5.334   3.924   7.111  0.40 35.10           C  
ATOM    245  CG ALEU A  33       5.271   5.320   7.518  0.60 29.62           C  
ATOM    246  CG BLEU A  33       6.694   4.386   6.572  0.40 34.11           C  
ATOM    247  CD1ALEU A  33       4.340   5.172   8.706  0.60 27.93           C  
ATOM    248  CD1BLEU A  33       6.781   4.478   5.054  0.40 37.44           C  
ATOM    249  CD2ALEU A  33       6.376   6.306   7.842  0.60 28.07           C  
ATOM    250  CD2BLEU A  33       7.026   5.742   7.185  0.40 34.55           C  
ATOM    251  N  AGLU A  34       3.276   3.880   5.048  0.60 33.69           N  
ATOM    252  N  BGLU A  34       3.160   3.959   5.144  0.40 33.80           N  
ATOM    253  CA AGLU A  34       2.765   4.414   3.792  0.60 31.90           C  
ATOM    254  CA BGLU A  34       2.557   4.431   3.909  0.40 32.30           C  
ATOM    255  C  AGLU A  34       2.624   5.930   3.911  0.60 30.88           C  
ATOM    256  C  BGLU A  34       2.573   5.951   3.937  0.40 30.91           C  
ATOM    257  O  AGLU A  34       2.827   6.515   4.983  0.60 26.81           O  
ATOM    258  O  BGLU A  34       2.862   6.568   4.969  0.40 26.90           O  
ATOM    259  CB AGLU A  34       1.428   3.763   3.419  0.60 33.79           C  
ATOM    260  CB BGLU A  34       1.122   3.909   3.734  0.40 35.40           C  
ATOM    261  CG AGLU A  34       0.354   3.904   4.486  0.60 35.57           C  
ATOM    262  CG BGLU A  34       0.528   3.206   4.958  0.40 38.36           C  
ATOM    263  CD AGLU A  34      -1.038   4.010   3.902  0.60 40.91           C  
ATOM    264  CD BGLU A  34       0.510   4.069   6.218  0.40 39.40           C  
ATOM    265  OE1AGLU A  34      -1.275   4.930   3.087  0.60 38.69           O  
ATOM    266  OE1BGLU A  34       1.442   3.930   7.041  0.40 39.24           O  
ATOM    267  OE2AGLU A  34      -1.898   3.174   4.255  0.60 52.51           O  
ATOM    268  OE2BGLU A  34      -0.427   4.874   6.388  0.40 34.63           O  
ATOM    269  N   MET A  35       2.253   6.562   2.792  1.00 28.48           N  
ATOM    270  CA  MET A  35       2.248   8.020   2.730  1.00 26.02           C  
ATOM    271  C   MET A  35       1.269   8.616   3.731  1.00 28.00           C  
ATOM    272  O   MET A  35       1.559   9.648   4.346  1.00 23.85           O  
ATOM    273  CB  MET A  35       1.928   8.492   1.309  1.00 27.97           C  
ATOM    274  CG  MET A  35       3.133   8.450   0.342  1.00 28.34           C  
ATOM    275  SD  MET A  35       4.488   9.587   0.751  1.00 31.13           S  
ATOM    276  CE  MET A  35       3.521  11.080   0.993  1.00 28.43           C  
ATOM    277  N   ALA A  36       0.124   7.961   3.946  1.00 22.80           N  
ATOM    278  CA  ALA A  36      -0.835   8.491   4.910  1.00 26.83           C  
ATOM    279  C   ALA A  36      -0.251   8.516   6.320  1.00 23.06           C  
ATOM    280  O   ALA A  36      -0.436   9.491   7.066  1.00 23.07           O  
ATOM    281  CB  ALA A  36      -2.122   7.669   4.884  1.00 28.17           C  
ATOM    282  N   GLY A  37       0.424   7.443   6.725  1.00 23.50           N  
ATOM    283  CA  GLY A  37       0.996   7.417   8.060  1.00 25.09           C  
ATOM    284  C   GLY A  37       2.157   8.380   8.217  1.00 21.60           C  
ATOM    285  O   GLY A  37       2.358   8.941   9.299  1.00 20.36           O  
ATOM    286  N   LEU A  38       2.925   8.591   7.141  1.00 19.92           N  
ATOM    287  CA  LEU A  38       4.006   9.576   7.171  1.00 16.56           C  
ATOM    288  C   LEU A  38       3.448  10.979   7.356  1.00 19.68           C  
ATOM    289  O   LEU A  38       3.947  11.765   8.173  1.00 17.08           O  
ATOM    290  CB  LEU A  38       4.818   9.485   5.877  1.00 18.67           C  
ATOM    291  CG  LEU A  38       5.891  10.553   5.734  1.00 16.32           C  
ATOM    292  CD1 LEU A  38       6.885  10.455   6.902  1.00 20.72           C  
ATOM    293  CD2 LEU A  38       6.576  10.408   4.371  1.00 23.40           C  
ATOM    294  N   LYS A  39       2.405  11.312   6.597  1.00 17.53           N  
ATOM    295  CA  LYS A  39       1.802  12.629   6.730  1.00 16.48           C  
ATOM    296  C   LYS A  39       1.213  12.821   8.123  1.00 15.23           C  
ATOM    297  O   LYS A  39       1.272  13.921   8.683  1.00 18.81           O  
ATOM    298  CB  LYS A  39       0.747  12.824   5.631  1.00 18.08           C  
ATOM    299  CG  LYS A  39       1.384  13.067   4.276  1.00 22.03           C  
ATOM    300  CD  LYS A  39       0.367  13.304   3.185  1.00 27.79           C  
ATOM    301  CE  LYS A  39      -0.264  14.681   3.319  1.00 25.90           C  
ATOM    302  NZ  LYS A  39      -1.204  14.971   2.190  1.00 28.76           N  
ATOM    303  N   GLU A  40       0.630  11.767   8.697  1.00 16.40           N  
ATOM    304  CA  GLU A  40       0.033  11.893  10.022  1.00 15.29           C  
ATOM    305  C   GLU A  40       1.103  12.121  11.081  1.00 15.48           C  
ATOM    306  O   GLU A  40       0.897  12.872  12.036  1.00 19.16           O  
ATOM    307  CB  GLU A  40      -0.792  10.648  10.342  1.00 19.99           C  
ATOM    308  CG  GLU A  40      -2.081  10.571   9.517  1.00 21.24           C  
ATOM    309  CD  GLU A  40      -2.708   9.182   9.539  1.00 35.78           C  
ATOM    310  OE1 GLU A  40      -2.096   8.253  10.099  1.00 37.22           O  
ATOM    311  OE2 GLU A  40      -3.811   9.017   8.978  1.00 35.38           O  
ATOM    312  N   LYS A  41       2.243  11.455  10.935  1.00 16.97           N  
ATOM    313  CA  LYS A  41       3.325  11.663  11.884  1.00 14.98           C  
ATOM    314  C   LYS A  41       3.873  13.078  11.760  1.00 16.45           C  
ATOM    315  O   LYS A  41       4.053  13.778  12.758  1.00 17.10           O  
ATOM    316  CB  LYS A  41       4.408  10.609  11.641  1.00 16.95           C  
ATOM    317  CG  LYS A  41       5.536  10.646  12.653  1.00 18.20           C  
ATOM    318  CD  LYS A  41       5.102   9.974  13.963  1.00 27.93           C  
ATOM    319  CE  LYS A  41       6.233   9.958  14.965  1.00 28.95           C  
ATOM    320  NZ  LYS A  41       5.979   8.947  16.038  1.00 31.29           N  
ATOM    321  N   ILE A  42       4.095  13.541  10.529  1.00 15.00           N  
ATOM    322  CA  ILE A  42       4.618  14.887  10.337  1.00 13.26           C  
ATOM    323  C   ILE A  42       3.638  15.932  10.859  1.00 18.66           C  
ATOM    324  O   ILE A  42       4.040  16.917  11.488  1.00 16.33           O  
ATOM    325  CB  ILE A  42       4.968  15.103   8.854  1.00 16.44           C  
ATOM    326  CG1 ILE A  42       6.227  14.291   8.503  1.00 17.47           C  
ATOM    327  CG2 ILE A  42       5.185  16.580   8.577  1.00 17.29           C  
ATOM    328  CD1 ILE A  42       6.497  14.165   6.957  1.00 16.86           C  
ATOM    329  N   ALA A  43       2.337  15.726  10.631  1.00 16.03           N  
ATOM    330  CA  ALA A  43       1.325  16.643  11.152  1.00 16.00           C  
ATOM    331  C   ALA A  43       1.364  16.714  12.676  1.00 18.36           C  
ATOM    332  O   ALA A  43       1.260  17.797  13.260  1.00 18.68           O  
ATOM    333  CB  ALA A  43      -0.066  16.207  10.671  1.00 18.18           C  
ATOM    334  N   ALA A  44       1.498  15.567  13.339  1.00 20.29           N  
ATOM    335  CA  ALA A  44       1.570  15.567  14.801  1.00 20.24           C  
ATOM    336  C   ALA A  44       2.817  16.294  15.302  1.00 18.80           C  
ATOM    337  O   ALA A  44       2.780  16.968  16.345  1.00 25.33           O  
ATOM    338  CB  ALA A  44       1.537  14.130  15.318  1.00 23.48           C  
ATOM    339  N   LEU A  45       3.937  16.165  14.581  1.00 16.64           N  
ATOM    340  CA  LEU A  45       5.196  16.765  15.017  1.00 15.85           C  
ATOM    341  C   LEU A  45       5.178  18.278  14.926  1.00 20.19           C  
ATOM    342  O   LEU A  45       5.838  18.947  15.727  1.00 22.32           O  
ATOM    343  CB  LEU A  45       6.370  16.243  14.181  1.00 20.26           C  
ATOM    344  CG  LEU A  45       6.828  14.805  14.414  1.00 20.07           C  
ATOM    345  CD1 LEU A  45       7.854  14.410  13.351  1.00 19.69           C  
ATOM    346  CD2 LEU A  45       7.387  14.631  15.818  1.00 20.23           C  
ATOM    347  N   PHE A  46       4.480  18.842  13.941  1.00 17.75           N  
ATOM    348  CA  PHE A  46       4.600  20.265  13.661  1.00 15.99           C  
ATOM    349  C   PHE A  46       3.263  20.990  13.740  1.00 17.44           C  
ATOM    350  O   PHE A  46       3.178  22.165  13.345  1.00 21.08           O  
ATOM    351  CB  PHE A  46       5.245  20.469  12.278  1.00 17.48           C  
ATOM    352  CG  PHE A  46       6.668  19.960  12.187  1.00 17.33           C  
ATOM    353  CD1 PHE A  46       7.698  20.613  12.858  1.00 16.97           C  
ATOM    354  CD2 PHE A  46       6.976  18.828  11.454  1.00 19.56           C  
ATOM    355  CE1 PHE A  46       9.002  20.142  12.793  1.00 16.91           C  
ATOM    356  CE2 PHE A  46       8.284  18.355  11.379  1.00 20.03           C  
ATOM    357  CZ  PHE A  46       9.300  19.029  12.049  1.00 17.44           C  
ATOM    358  N  AASN A  47       2.219  20.331  14.235  0.66 20.61           N  
ATOM    359  N  BASN A  47       2.210  20.314  14.206  0.34 20.56           N  
ATOM    360  CA AASN A  47       0.875  20.895  14.322  0.66 23.86           C  
ATOM    361  CA BASN A  47       0.872  20.891  14.333  0.34 23.89           C  
ATOM    362  C  AASN A  47       0.400  21.401  12.961  0.66 24.72           C  
ATOM    363  C  BASN A  47       0.342  21.373  12.984  0.34 24.70           C  
ATOM    364  O  AASN A  47       0.021  22.561  12.787  0.66 21.14           O  
ATOM    365  O  BASN A  47      -0.141  22.498  12.840  0.34 21.46           O  
ATOM    366  CB AASN A  47       0.793  22.008  15.376  0.66 24.55           C  
ATOM    367  CB BASN A  47       0.854  22.016  15.372  0.34 24.62           C  
ATOM    368  CG AASN A  47      -0.635  22.309  15.768  0.66 28.37           C  
ATOM    369  CG BASN A  47       1.055  21.501  16.776  0.34 29.11           C  
ATOM    370  OD1AASN A  47      -1.462  21.405  15.827  0.66 30.50           O  
ATOM    371  OD1BASN A  47       0.186  20.823  17.329  0.34 30.24           O  
ATOM    372  ND2AASN A  47      -0.940  23.581  16.011  0.66 30.19           N  
ATOM    373  ND2BASN A  47       2.212  21.801  17.357  0.34 29.13           N  
ATOM    374  N   LEU A  48       0.428  20.498  11.990  1.00 18.18           N  
ATOM    375  CA  LEU A  48      -0.106  20.753  10.658  1.00 15.71           C  
ATOM    376  C   LEU A  48      -1.357  19.901  10.464  1.00 16.35           C  
ATOM    377  O   LEU A  48      -1.710  19.097  11.324  1.00 18.22           O  
ATOM    378  CB  LEU A  48       0.944  20.432   9.594  1.00 15.75           C  
ATOM    379  CG  LEU A  48       2.415  20.736   9.876  1.00 17.19           C  
ATOM    380  CD1 LEU A  48       3.295  20.262   8.716  1.00 19.54           C  
ATOM    381  CD2 LEU A  48       2.633  22.207  10.144  1.00 22.12           C  
ATOM    382  N  ASER A  49      -2.030  20.099   9.321  0.56 16.91           N  
ATOM    383  N  BSER A  49      -2.040  20.074   9.335  0.44 16.97           N  
ATOM    384  CA ASER A  49      -3.119  19.213   8.910  0.56 19.78           C  
ATOM    385  CA BSER A  49      -3.150  19.182   9.023  0.44 19.64           C  
ATOM    386  C  ASER A  49      -2.551  17.963   8.252  0.56 16.82           C  
ATOM    387  C  BSER A  49      -2.639  17.985   8.237  0.44 16.88           C  
ATOM    388  O  ASER A  49      -1.726  18.061   7.340  0.56 19.16           O  
ATOM    389  O  BSER A  49      -1.931  18.147   7.238  0.44 19.41           O  
ATOM    390  CB ASER A  49      -4.060  19.903   7.916  0.56 16.03           C  
ATOM    391  CB BSER A  49      -4.254  19.877   8.232  0.44 16.72           C  
ATOM    392  OG ASER A  49      -4.729  21.012   8.476  0.56 18.84           O  
ATOM    393  OG BSER A  49      -5.403  19.046   8.234  0.44 17.03           O  
ATOM    394  N   ALA A  50      -3.023  16.789   8.684  1.00 19.65           N  
ATOM    395  CA  ALA A  50      -2.573  15.561   8.040  1.00 21.87           C  
ATOM    396  C   ALA A  50      -3.061  15.449   6.603  1.00 24.37           C  
ATOM    397  O   ALA A  50      -2.422  14.762   5.793  1.00 22.96           O  
ATOM    398  CB  ALA A  50      -3.036  14.352   8.849  1.00 19.73           C  
ATOM    399  N   ASP A  51      -4.156  16.127   6.251  1.00 21.67           N  
ATOM    400  CA  ASP A  51      -4.612  16.113   4.870  1.00 19.10           C  
ATOM    401  C   ASP A  51      -4.212  17.356   4.092  1.00 25.25           C  
ATOM    402  O   ASP A  51      -4.698  17.557   2.970  1.00 23.70           O  
ATOM    403  CB  ASP A  51      -6.132  15.904   4.779  1.00 21.67           C  
ATOM    404  CG  ASP A  51      -6.965  16.956   5.506  1.00 23.95           C  
ATOM    405  OD1 ASP A  51      -6.444  17.880   6.149  1.00 20.67           O  
ATOM    406  OD2 ASP A  51      -8.208  16.869   5.379  1.00 24.97           O  
ATOM    407  N   ALA A  52      -3.324  18.184   4.635  1.00 21.62           N  
ATOM    408  CA  ALA A  52      -2.784  19.267   3.832  1.00 19.32           C  
ATOM    409  C   ALA A  52      -1.971  18.726   2.659  1.00 26.78           C  
ATOM    410  O   ALA A  52      -1.401  17.631   2.714  1.00 22.64           O  
ATOM    411  CB  ALA A  52      -1.906  20.181   4.680  1.00 21.81           C  
ATOM    412  N  AGLU A  53      -1.880  19.523   1.587  0.70 21.65           N  
ATOM    413  N  BGLU A  53      -1.978  19.487   1.569  0.30 21.82           N  
ATOM    414  CA AGLU A  53      -1.074  19.154   0.416  0.70 22.18           C  
ATOM    415  CA BGLU A  53      -1.080  19.232   0.451  0.30 22.46           C  
ATOM    416  C  AGLU A  53       0.369  19.623   0.618  0.70 25.11           C  
ATOM    417  C  BGLU A  53       0.285  19.749   0.876  0.30 25.63           C  
ATOM    418  O  AGLU A  53       0.828  20.619   0.057  0.70 31.64           O  
ATOM    419  O  BGLU A  53       0.586  20.939   0.777  0.30 28.06           O  
ATOM    420  CB AGLU A  53      -1.685  19.728  -0.859  0.70 26.05           C  
ATOM    421  CB BGLU A  53      -1.582  19.904  -0.821  0.30 26.36           C  
ATOM    422  CG AGLU A  53      -2.850  18.922  -1.376  0.70 29.70           C  
ATOM    423  CG BGLU A  53      -0.943  19.365  -2.084  0.30 25.86           C  
ATOM    424  CD AGLU A  53      -3.049  19.080  -2.868  0.70 34.77           C  
ATOM    425  CD BGLU A  53      -1.151  17.872  -2.247  0.30 31.10           C  
ATOM    426  OE1AGLU A  53      -2.621  20.118  -3.414  0.70 32.25           O  
ATOM    427  OE1BGLU A  53      -2.245  17.379  -1.895  0.30 34.34           O  
ATOM    428  OE2AGLU A  53      -3.630  18.164  -3.490  0.70 41.85           O  
ATOM    429  OE2BGLU A  53      -0.221  17.188  -2.725  0.30 37.30           O  
ATOM    430  N   LEU A  54       1.104  18.851   1.410  1.00 22.91           N  
ATOM    431  CA  LEU A  54       2.460  19.187   1.811  1.00 22.06           C  
ATOM    432  C   LEU A  54       3.431  18.747   0.734  1.00 21.79           C  
ATOM    433  O   LEU A  54       3.276  17.669   0.161  1.00 30.93           O  
ATOM    434  CB  LEU A  54       2.813  18.488   3.120  1.00 23.44           C  
ATOM    435  CG  LEU A  54       1.846  18.731   4.281  1.00 24.64           C  
ATOM    436  CD1 LEU A  54       2.168  17.824   5.454  1.00 24.08           C  
ATOM    437  CD2 LEU A  54       1.936  20.172   4.703  1.00 25.20           C  
ATOM    438  N   SER A  55       4.429  19.569   0.462  1.00 21.03           N  
ATOM    439  CA  SER A  55       5.539  19.138  -0.374  1.00 21.97           C  
ATOM    440  C   SER A  55       6.573  18.457   0.521  1.00 19.68           C  
ATOM    441  O   SER A  55       7.142  19.095   1.411  1.00 21.82           O  
ATOM    442  CB  SER A  55       6.152  20.318  -1.130  1.00 29.19           C  
ATOM    443  OG  SER A  55       7.471  20.033  -1.563  1.00 34.42           O  
ATOM    444  N   LEU A  56       6.812  17.169   0.285  1.00 16.32           N  
ATOM    445  CA  LEU A  56       7.767  16.371   1.044  1.00 18.71           C  
ATOM    446  C   LEU A  56       8.886  15.981   0.089  1.00 18.59           C  
ATOM    447  O   LEU A  56       8.648  15.234  -0.864  1.00 18.92           O  
ATOM    448  CB  LEU A  56       7.092  15.137   1.637  1.00 19.64           C  
ATOM    449  CG  LEU A  56       5.825  15.439   2.452  1.00 22.15           C  
ATOM    450  CD1 LEU A  56       5.184  14.150   2.992  1.00 24.66           C  
ATOM    451  CD2 LEU A  56       6.180  16.383   3.579  1.00 16.79           C  
ATOM    452  N   THR A  57      10.089  16.525   0.306  1.00 14.10           N  
ATOM    453  CA  THR A  57      11.184  16.311  -0.632  1.00 15.46           C  
ATOM    454  C   THR A  57      12.438  15.832   0.085  1.00 20.21           C  
ATOM    455  O   THR A  57      12.656  16.153   1.256  1.00 18.19           O  
ATOM    456  CB  THR A  57      11.522  17.597  -1.415  1.00 20.25           C  
ATOM    457  OG1 THR A  57      11.765  18.685  -0.514  1.00 21.55           O  
ATOM    458  CG2 THR A  57      10.367  17.954  -2.365  1.00 18.63           C  
ATOM    459  N   TYR A  58      13.274  15.071  -0.622  1.00 14.85           N  
ATOM    460  CA  TYR A  58      14.627  14.813  -0.151  1.00 15.25           C  
ATOM    461  C   TYR A  58      15.610  14.977  -1.296  1.00 17.59           C  
ATOM    462  O   TYR A  58      15.225  14.925  -2.463  1.00 17.22           O  
ATOM    463  CB  TYR A  58      14.769  13.423   0.478  1.00 17.58           C  
ATOM    464  CG  TYR A  58      14.643  12.212  -0.423  1.00 17.86           C  
ATOM    465  CD1 TYR A  58      15.775  11.624  -0.998  1.00 18.26           C  
ATOM    466  CD2 TYR A  58      13.404  11.604  -0.635  1.00 19.33           C  
ATOM    467  CE1 TYR A  58      15.667  10.478  -1.776  1.00 17.69           C  
ATOM    468  CE2 TYR A  58      13.287  10.461  -1.407  1.00 21.17           C  
ATOM    469  CZ  TYR A  58      14.429   9.907  -1.982  1.00 25.20           C  
ATOM    470  OH  TYR A  58      14.321   8.770  -2.758  1.00 25.47           O  
ATOM    471  N   SER A  59      16.879  15.227  -0.952  1.00 16.69           N  
ATOM    472  CA  SER A  59      17.930  15.391  -1.957  1.00 16.45           C  
ATOM    473  C   SER A  59      18.676  14.081  -2.139  1.00 20.76           C  
ATOM    474  O   SER A  59      19.253  13.549  -1.182  1.00 25.36           O  
ATOM    475  CB  SER A  59      18.901  16.520  -1.598  1.00 23.92           C  
ATOM    476  OG  SER A  59      18.214  17.723  -1.316  1.00 25.16           O  
ATOM    477  N   ALA A  60      18.692  13.587  -3.370  1.00 21.34           N  
ATOM    478  CA  ALA A  60      19.303  12.308  -3.682  1.00 21.61           C  
ATOM    479  C   ALA A  60      20.805  12.481  -3.887  1.00 29.35           C  
ATOM    480  O   ALA A  60      21.326  13.596  -3.967  1.00 25.71           O  
ATOM    481  CB  ALA A  60      18.641  11.701  -4.916  1.00 24.68           C  
ATOM    482  N   ALA A  61      21.509  11.347  -3.962  1.00 31.62           N  
ATOM    483  CA  ALA A  61      22.959  11.386  -4.097  1.00 38.47           C  
ATOM    484  C   ALA A  61      23.411  11.948  -5.439  1.00 25.73           C  
ATOM    485  O   ALA A  61      24.555  12.404  -5.544  1.00 41.80           O  
ATOM    486  CB  ALA A  61      23.549   9.988  -3.892  1.00 38.95           C  
ATOM    487  N   ASP A  62      22.563  11.921  -6.468  1.00 27.07           N  
ATOM    488  CA  ASP A  62      22.930  12.484  -7.762  1.00 29.81           C  
ATOM    489  C   ASP A  62      22.615  13.966  -7.864  1.00 29.63           C  
ATOM    490  O   ASP A  62      22.644  14.511  -8.971  1.00 27.98           O  
ATOM    491  CB  ASP A  62      22.243  11.731  -8.919  1.00 27.71           C  
ATOM    492  CG  ASP A  62      20.713  11.799  -8.865  1.00 30.09           C  
ATOM    493  OD1 ASP A  62      20.150  12.502  -7.994  1.00 29.84           O  
ATOM    494  OD2 ASP A  62      20.064  11.128  -9.696  1.00 31.51           O  
ATOM    495  N   GLY A  63      22.315  14.627  -6.740  1.00 26.48           N  
ATOM    496  CA  GLY A  63      22.022  16.045  -6.740  1.00 26.27           C  
ATOM    497  C   GLY A  63      20.641  16.430  -7.217  1.00 21.18           C  
ATOM    498  O   GLY A  63      20.363  17.634  -7.352  1.00 22.66           O  
ATOM    499  N   ALA A  64      19.772  15.469  -7.505  1.00 18.99           N  
ATOM    500  CA  ALA A  64      18.412  15.777  -7.913  1.00 14.67           C  
ATOM    501  C   ALA A  64      17.498  15.635  -6.702  1.00 17.29           C  
ATOM    502  O   ALA A  64      17.811  14.899  -5.771  1.00 22.92           O  
ATOM    503  CB  ALA A  64      17.939  14.858  -9.033  1.00 20.80           C  
ATOM    504  N   VAL A  65      16.444  16.394  -6.675  1.00 17.51           N  
ATOM    505  CA  VAL A  65      15.475  16.327  -5.575  1.00 13.40           C  
ATOM    506  C   VAL A  65      14.417  15.297  -5.917  1.00 17.32           C  
ATOM    507  O   VAL A  65      13.934  15.234  -7.055  1.00 18.45           O  
ATOM    508  CB  VAL A  65      14.844  17.710  -5.317  1.00 15.25           C  
ATOM    509  CG1 VAL A  65      13.608  17.621  -4.384  1.00 15.39           C  
ATOM    510  CG2 VAL A  65      15.871  18.658  -4.726  1.00 19.51           C  
ATOM    511  N   VAL A  66      14.028  14.497  -4.922  1.00 13.48           N  
ATOM    512  CA  VAL A  66      12.955  13.525  -5.031  1.00 13.91           C  
ATOM    513  C   VAL A  66      11.747  14.043  -4.262  1.00 19.69           C  
ATOM    514  O   VAL A  66      11.855  14.369  -3.072  1.00 17.70           O  
ATOM    515  CB  VAL A  66      13.374  12.155  -4.480  1.00 14.15           C  
ATOM    516  CG1 VAL A  66      12.211  11.178  -4.610  1.00 20.42           C  
ATOM    517  CG2 VAL A  66      14.651  11.626  -5.136  1.00 17.85           C  
ATOM    518  N   ALA A  67      10.597  14.107  -4.922  1.00 16.42           N  
ATOM    519  CA  ALA A  67       9.349  14.441  -4.236  1.00 17.20           C  
ATOM    520  C   ALA A  67       8.598  13.174  -3.857  1.00 20.39           C  
ATOM    521  O   ALA A  67       8.319  12.326  -4.712  1.00 25.34           O  
ATOM    522  CB  ALA A  67       8.458  15.321  -5.100  1.00 19.69           C  
ATOM    523  N   LEU A  68       8.242  13.068  -2.584  1.00 16.40           N  
ATOM    524  CA  LEU A  68       7.416  11.965  -2.108  1.00 14.37           C  
ATOM    525  C   LEU A  68       5.969  12.335  -2.392  1.00 22.94           C  
ATOM    526  O   LEU A  68       5.356  13.115  -1.654  1.00 25.60           O  
ATOM    527  CB  LEU A  68       7.660  11.717  -0.625  1.00 16.19           C  
ATOM    528  CG  LEU A  68       9.100  11.414  -0.219  1.00 18.58           C  
ATOM    529  CD1 LEU A  68       9.171  11.340   1.316  1.00 23.02           C  
ATOM    530  CD2 LEU A  68       9.596  10.121  -0.842  1.00 21.31           C  
ATOM    531  N   VAL A  69       5.425  11.818  -3.494  1.00 20.87           N  
ATOM    532  CA  VAL A  69       4.032  12.092  -3.834  1.00 19.74           C  
ATOM    533  C   VAL A  69       3.144  10.854  -3.762  1.00 26.71           C  
ATOM    534  O   VAL A  69       1.920  11.008  -3.615  1.00 30.65           O  
ATOM    535  CB  VAL A  69       3.906  12.771  -5.217  1.00 22.24           C  
ATOM    536  CG1 VAL A  69       4.484  14.173  -5.173  1.00 25.03           C  
ATOM    537  CG2 VAL A  69       4.598  11.967  -6.314  1.00 30.12           C  
ATOM    538  N   ASP A  70       3.701   9.642  -3.815  1.00 24.00           N  
ATOM    539  CA  ASP A  70       2.880   8.447  -3.691  1.00 29.07           C  
ATOM    540  C   ASP A  70       3.668   7.334  -3.009  1.00 25.53           C  
ATOM    541  O   ASP A  70       4.861   7.466  -2.720  1.00 23.80           O  
ATOM    542  CB  ASP A  70       2.335   7.997  -5.064  1.00 27.89           C  
ATOM    543  CG  ASP A  70       3.428   7.789  -6.098  1.00 32.98           C  
ATOM    544  OD1 ASP A  70       4.397   7.065  -5.795  1.00 29.61           O  
ATOM    545  OD2 ASP A  70       3.318   8.330  -7.229  1.00 31.20           O  
ATOM    546  N   ASP A  71       2.971   6.223  -2.751  1.00 26.11           N  
ATOM    547  CA  ASP A  71       3.588   5.106  -2.040  1.00 29.54           C  
ATOM    548  C   ASP A  71       4.745   4.497  -2.821  1.00 25.92           C  
ATOM    549  O   ASP A  71       5.661   3.923  -2.220  1.00 35.24           O  
ATOM    550  CB  ASP A  71       2.542   4.032  -1.733  1.00 28.43           C  
ATOM    551  CG  ASP A  71       1.655   4.396  -0.563  1.00 34.10           C  
ATOM    552  OD1 ASP A  71       2.067   5.250   0.240  1.00 33.11           O  
ATOM    553  OD2 ASP A  71       0.555   3.816  -0.442  1.00 38.95           O  
ATOM    554  N   ASN A  72       4.728   4.598  -4.157  1.00 29.69           N  
ATOM    555  CA  ASN A  72       5.847   4.078  -4.931  1.00 24.57           C  
ATOM    556  C   ASN A  72       7.136   4.831  -4.632  1.00 23.01           C  
ATOM    557  O   ASN A  72       8.220   4.231  -4.638  1.00 27.07           O  
ATOM    558  CB  ASN A  72       5.529   4.137  -6.425  1.00 31.03           C  
ATOM    559  CG  ASN A  72       4.375   3.233  -6.804  1.00 39.35           C  
ATOM    560  OD1 ASN A  72       4.345   2.062  -6.429  1.00 40.50           O  
ATOM    561  ND2 ASN A  72       3.418   3.770  -7.552  1.00 47.46           N  
ATOM    562  N   ASP A  73       7.044   6.139  -4.379  1.00 22.03           N  
ATOM    563  CA  ASP A  73       8.219   6.908  -3.989  1.00 20.81           C  
ATOM    564  C   ASP A  73       8.773   6.445  -2.643  1.00 21.65           C  
ATOM    565  O   ASP A  73       9.988   6.473  -2.431  1.00 21.44           O  
ATOM    566  CB  ASP A  73       7.885   8.395  -3.910  1.00 26.00           C  
ATOM    567  CG  ASP A  73       7.357   8.938  -5.210  1.00 30.00           C  
ATOM    568  OD1 ASP A  73       8.002   8.710  -6.261  1.00 27.40           O  
ATOM    569  OD2 ASP A  73       6.308   9.600  -5.179  1.00 25.13           O  
ATOM    570  N   LEU A  74       7.891   6.074  -1.714  1.00 23.41           N  
ATOM    571  CA  LEU A  74       8.368   5.607  -0.411  1.00 25.87           C  
ATOM    572  C   LEU A  74       8.900   4.190  -0.503  1.00 31.93           C  
ATOM    573  O   LEU A  74       9.910   3.851   0.134  1.00 36.20           O  
ATOM    574  CB  LEU A  74       7.256   5.690   0.632  1.00 33.87           C  
ATOM    575  CG  LEU A  74       7.170   6.983   1.425  1.00 35.56           C  
ATOM    576  CD1 LEU A  74       5.886   6.964   2.261  1.00 48.77           C  
ATOM    577  CD2 LEU A  74       8.412   7.142   2.289  1.00 38.17           C  
ATOM    578  N   PHE A  75       8.226   3.332  -1.272  1.00 35.99           N  
ATOM    579  CA  PHE A  75       8.740   1.997  -1.550  1.00 38.58           C  
ATOM    580  C   PHE A  75      10.155   2.064  -2.107  1.00 43.02           C  
ATOM    581  O   PHE A  75      11.014   1.247  -1.759  1.00 37.17           O  
ATOM    582  CB  PHE A  75       7.807   1.282  -2.528  1.00 40.14           C  
ATOM    583  CG  PHE A  75       8.178  -0.147  -2.809  1.00 49.72           C  
ATOM    584  CD1 PHE A  75       7.928  -1.142  -1.879  1.00 58.71           C  
ATOM    585  CD2 PHE A  75       8.739  -0.504  -4.021  1.00 57.99           C  
ATOM    586  CE1 PHE A  75       8.257  -2.462  -2.148  1.00 59.60           C  
ATOM    587  CE2 PHE A  75       9.058  -1.828  -4.294  1.00 60.28           C  
ATOM    588  CZ  PHE A  75       8.828  -2.801  -3.352  1.00 64.24           C  
ATOM    589  N   ASP A  76      10.419   3.054  -2.956  1.00 30.11           N  
ATOM    590  CA  ASP A  76      11.729   3.184  -3.568  1.00 31.86           C  
ATOM    591  C   ASP A  76      12.788   3.748  -2.629  1.00 32.40           C  
ATOM    592  O   ASP A  76      13.979   3.654  -2.939  1.00 27.92           O  
ATOM    593  CB  ASP A  76      11.628   4.044  -4.818  1.00 27.34           C  
ATOM    594  CG  ASP A  76      12.590   3.591  -5.891  1.00 40.88           C  
ATOM    595  OD1 ASP A  76      12.547   2.396  -6.254  1.00 48.17           O  
ATOM    596  OD2 ASP A  76      13.390   4.421  -6.366  1.00 36.22           O  
ATOM    597  N   VAL A  77      12.438   4.279  -1.474  1.00 30.42           N  
ATOM    598  CA  VAL A  77      13.472   4.641  -0.470  1.00 32.71           C  
ATOM    599  C   VAL A  77      14.141   3.348   0.006  1.00 40.53           C  
ATOM    600  O   VAL A  77      15.350   3.310   0.114  1.00 41.35           O  
ATOM    601  CB  VAL A  77      12.856   5.430   0.694  1.00 30.96           C  
ATOM    602  CG1 VAL A  77      13.767   5.459   1.906  1.00 31.44           C  
ATOM    603  CG2 VAL A  77      12.489   6.842   0.271  1.00 23.65           C  
ATOM    604  N   THR A  78      13.340   2.336   0.262  1.00 42.00           N  
ATOM    605  CA  THR A  78      13.839   1.022   0.739  1.00 48.31           C  
ATOM    606  C   THR A  78      14.529   0.280  -0.406  1.00 50.61           C  
ATOM    607  O   THR A  78      15.590  -0.296  -0.175  1.00 48.16           O  
ATOM    608  CB  THR A  78      12.627   0.223   1.233  1.00 46.23           C  
ATOM    609  OG1 THR A  78      12.040  -0.499   0.155  1.00 61.74           O  
ATOM    610  CG2 THR A  78      11.557   1.086   1.856  1.00 54.48           C  
ATOM    611  N   ASN A  79      13.919   0.286  -1.585  1.00 42.26           N  
ATOM    612  CA  ASN A  79      14.479  -0.452  -2.740  1.00 47.38           C  
ATOM    613  C   ASN A  79      15.901   0.010  -2.947  1.00 48.46           C  
ATOM    614  O   ASN A  79      16.755  -0.794  -3.272  1.00 54.68           O  
ATOM    615  CB  ASN A  79      13.727  -0.176  -4.032  1.00 39.46           C  
ATOM    616  CG  ASN A  79      12.361  -0.802  -4.097  1.00 51.64           C  
ATOM    617  OD1 ASN A  79      11.941  -1.477  -3.166  1.00 51.04           O  
ATOM    618  ND2 ASN A  79      11.676  -0.569  -5.201  1.00 46.38           N  
ATOM    619  N   GLN A  80      16.111   1.272  -2.696  1.00 41.18           N  
ATOM    620  CA  GLN A  80      17.454   1.900  -2.877  1.00 38.14           C  
ATOM    621  C   GLN A  80      18.393   1.696  -1.665  1.00 56.46           C  
ATOM    622  O   GLN A  80      19.484   2.274  -1.656  1.00 61.40           O  
ATOM    623  CB  GLN A  80      17.339   3.391  -3.203  1.00 43.10           C  
ATOM    624  CG  GLN A  80      16.832   3.695  -4.603  1.00 36.50           C  
ATOM    625  CD  GLN A  80      16.591   5.168  -4.822  1.00 40.64           C  
ATOM    626  OE1 GLN A  80      15.914   5.831  -4.048  1.00 51.55           O  
ATOM    627  NE2 GLN A  80      17.150   5.697  -5.896  1.00 45.92           N  
ATOM    628  N   ARG A  81      17.938   0.973  -0.656  1.00 52.54           N  
ATOM    629  CA  ARG A  81      18.760   0.687   0.538  1.00 56.63           C  
ATOM    630  C   ARG A  81      19.243   1.955   1.236  1.00 63.64           C  
ATOM    631  O   ARG A  81      20.348   1.945   1.747  1.00 68.58           O  
ATOM    632  CB  ARG A  81      19.878  -0.287   0.198  1.00 57.79           C  
ATOM    633  CG  ARG A  81      19.404  -1.662  -0.245  1.00 66.72           C  
ATOM    634  CD  ARG A  81      20.617  -2.538  -0.480  1.00 71.88           C  
ATOM    635  NE  ARG A  81      20.306  -3.730  -1.248  1.00 74.22           N  
ATOM    636  CZ  ARG A  81      20.026  -4.915  -0.719  1.00 75.96           C  
ATOM    637  NH1 ARG A  81      20.016  -5.074   0.593  1.00 75.32           N  
ATOM    638  NH2 ARG A  81      19.754  -5.937  -1.509  1.00 79.78           N  
ATOM    639  N   LEU A  82      18.441   3.018   1.241  1.00 59.78           N  
ATOM    640  CA  LEU A  82      18.778   4.178   2.100  1.00 56.29           C  
ATOM    641  C   LEU A  82      18.612   3.766   3.566  1.00 48.34           C  
ATOM    642  O   LEU A  82      17.655   3.034   3.863  1.00 53.56           O  
ATOM    643  CB  LEU A  82      17.883   5.370   1.741  1.00 43.40           C  
ATOM    644  CG  LEU A  82      17.837   5.737   0.259  1.00 58.86           C  
ATOM    645  CD1 LEU A  82      17.144   7.074   0.053  1.00 48.03           C  
ATOM    646  CD2 LEU A  82      19.236   5.764  -0.336  1.00 59.25           C  
ATOM    647  N   LYS A  83      19.475   4.274   4.427  1.00 50.94           N  
ATOM    648  CA  LYS A  83      19.365   3.997   5.886  1.00 59.05           C  
ATOM    649  C   LYS A  83      19.019   5.274   6.633  1.00 53.08           C  
ATOM    650  O   LYS A  83      18.575   5.191   7.779  1.00 52.18           O  
ATOM    651  CB  LYS A  83      20.740   3.596   6.406  1.00 58.91           C  
ATOM    652  CG  LYS A  83      20.765   3.211   7.881  1.00 52.66           C  
ATOM    653  CD  LYS A  83      22.151   3.044   8.459  1.00 69.90           C  
ATOM    654  CE  LYS A  83      22.145   2.592   9.902  1.00 64.14           C  
ATOM    655  NZ  LYS A  83      21.662   1.197  10.038  1.00 68.07           N  
ATOM    656  N   PHE A  84      19.054   6.361   6.148  1.00 42.33           N  
ATOM    657  CA  PHE A  84      18.839   7.781   6.510  1.00 41.54           C  
ATOM    658  C   PHE A  84      18.067   8.455   5.383  1.00 36.93           C  
ATOM    659  O   PHE A  84      18.405   8.255   4.227  1.00 37.54           O  
ATOM    660  CB  PHE A  84      20.159   8.464   6.858  1.00 37.22           C  
ATOM    661  CG  PHE A  84      20.043   9.930   7.171  1.00 50.94           C  
ATOM    662  CD1 PHE A  84      19.154  10.377   8.131  1.00 47.89           C  
ATOM    663  CD2 PHE A  84      20.830  10.861   6.516  1.00 52.82           C  
ATOM    664  CE1 PHE A  84      19.044  11.724   8.423  1.00 47.73           C  
ATOM    665  CE2 PHE A  84      20.718  12.210   6.808  1.00 48.62           C  
ATOM    666  CZ  PHE A  84      19.834  12.636   7.770  1.00 41.61           C  
ATOM    667  N   LEU A  85      16.982   9.082   5.985  1.00 26.36           N  
ATOM    668  CA  LEU A  85      16.199   9.930   5.077  1.00 27.31           C  
ATOM    669  C   LEU A  85      15.970  11.282   5.735  1.00 23.31           C  
ATOM    670  O   LEU A  85      15.435  11.312   6.808  1.00 30.33           O  
ATOM    671  CB  LEU A  85      14.893   9.215   4.765  1.00 22.37           C  
ATOM    672  CG  LEU A  85      13.943   9.952   3.834  1.00 27.42           C  
ATOM    673  CD1 LEU A  85      14.589  10.148   2.477  1.00 26.37           C  
ATOM    674  CD2 LEU A  85      12.650   9.175   3.697  1.00 26.59           C  
ATOM    675  N   LYS A  86      16.401  12.338   5.072  1.00 20.82           N  
ATOM    676  CA  LYS A  86      16.086  13.683   5.539  1.00 19.73           C  
ATOM    677  C   LYS A  86      15.040  14.273   4.614  1.00 21.61           C  
ATOM    678  O   LYS A  86      15.315  14.471   3.422  1.00 19.71           O  
ATOM    679  CB  LYS A  86      17.303  14.598   5.579  1.00 20.72           C  
ATOM    680  CG  LYS A  86      16.932  15.984   6.089  1.00 26.47           C  
ATOM    681  CD  LYS A  86      17.951  17.043   5.727  1.00 32.15           C  
ATOM    682  CE  LYS A  86      17.739  18.314   6.557  1.00 33.19           C  
ATOM    683  NZ  LYS A  86      17.040  19.398   5.835  1.00 45.03           N  
ATOM    684  N   ILE A  87      13.862  14.575   5.167  1.00 15.95           N  
ATOM    685  CA  ILE A  87      12.718  15.081   4.406  1.00 16.50           C  
ATOM    686  C   ILE A  87      12.521  16.556   4.731  1.00 17.25           C  
ATOM    687  O   ILE A  87      12.341  16.925   5.897  1.00 18.13           O  
ATOM    688  CB  ILE A  87      11.438  14.294   4.726  1.00 18.46           C  
ATOM    689  CG1 ILE A  87      11.578  12.810   4.380  1.00 21.52           C  
ATOM    690  CG2 ILE A  87      10.213  14.941   4.039  1.00 22.49           C  
ATOM    691  CD1 ILE A  87      10.369  11.989   4.830  1.00 22.76           C  
ATOM    692  N   ASN A  88      12.515  17.409   3.705  1.00 15.76           N  
ATOM    693  CA  ASN A  88      12.142  18.797   3.909  1.00 16.84           C  
ATOM    694  C   ASN A  88      10.643  18.950   3.668  1.00 19.19           C  
ATOM    695  O   ASN A  88      10.110  18.438   2.672  1.00 19.80           O  
ATOM    696  CB  ASN A  88      12.909  19.725   2.958  1.00 19.49           C  
ATOM    697  CG  ASN A  88      14.354  19.943   3.374  1.00 36.15           C  
ATOM    698  OD1 ASN A  88      14.711  19.776   4.534  1.00 30.14           O  
ATOM    699  ND2 ASN A  88      15.191  20.332   2.418  1.00 45.67           N  
ATOM    700  N   VAL A  89       9.970  19.690   4.553  1.00 16.86           N  
ATOM    701  CA  VAL A  89       8.523  19.901   4.475  1.00 18.36           C  
ATOM    702  C   VAL A  89       8.255  21.328   4.056  1.00 18.94           C  
ATOM    703  O   VAL A  89       8.715  22.269   4.709  1.00 20.79           O  
ATOM    704  CB  VAL A  89       7.823  19.639   5.826  1.00 19.48           C  
ATOM    705  CG1 VAL A  89       6.314  19.863   5.672  1.00 20.33           C  
ATOM    706  CG2 VAL A  89       8.098  18.261   6.301  1.00 20.62           C  
ATOM    707  N   ASN A  90       7.492  21.506   2.990  1.00 19.33           N  
ATOM    708  CA  ASN A  90       7.016  22.830   2.643  1.00 25.62           C  
ATOM    709  C   ASN A  90       5.511  22.787   2.458  1.00 32.80           C  
ATOM    710  O   ASN A  90       4.961  21.807   1.946  1.00 28.62           O  
ATOM    711  CB  ASN A  90       7.704  23.355   1.391  1.00 32.46           C  
ATOM    712  CG  ASN A  90       9.139  23.716   1.646  1.00 30.94           C  
ATOM    713  OD1 ASN A  90       9.446  24.841   2.036  1.00 45.96           O  
ATOM    714  ND2 ASN A  90      10.035  22.758   1.447  1.00 30.36           N  
ATOM    715  N   ALA A  91       4.844  23.840   2.905  1.00 34.48           N  
ATOM    716  CA  ALA A  91       3.396  23.887   2.896  1.00 36.31           C  
ATOM    717  C   ALA A  91       2.913  24.952   1.921  1.00 49.50           C  
ATOM    718  O   ALA A  91       3.579  25.969   1.707  1.00 51.30           O  
ATOM    719  CB  ALA A  91       2.854  24.166   4.298  1.00 37.17           C  
ATOM    720  N   GLY A  92       1.748  24.702   1.331  1.00 53.73           N  
ATOM    721  CA  GLY A  92       1.199  25.579   0.316  1.00 49.45           C  
ATOM    722  C   GLY A  92       1.202  24.935  -1.058  1.00 68.95           C  
ATOM    723  O   GLY A  92       2.072  24.119  -1.371  1.00 70.10           O  
TER     724      GLY A  92                                                      
HETATM  725  C1  GOL A 101      11.303  23.330   5.609  1.00 37.00           C  
HETATM  726  O1  GOL A 101      10.371  24.250   6.119  1.00 41.69           O  
HETATM  727  C2  GOL A 101      12.599  24.089   5.331  1.00 52.24           C  
HETATM  728  O2  GOL A 101      13.283  23.566   4.234  1.00 53.54           O  
HETATM  729  C3  GOL A 101      13.419  23.955   6.626  1.00 39.18           C  
HETATM  730  O3  GOL A 101      12.542  23.779   7.696  1.00 42.75           O  
HETATM  731  C1  GOL A 102       0.529  13.574  -0.730  1.00 43.85           C  
HETATM  732  O1  GOL A 102       0.369  12.642  -1.758  1.00 61.22           O  
HETATM  733  C2  GOL A 102       1.880  14.288  -0.997  1.00 42.38           C  
HETATM  734  O2  GOL A 102       1.752  15.350  -1.894  1.00 48.00           O  
HETATM  735  C3  GOL A 102       2.348  14.750   0.395  1.00 50.17           C  
HETATM  736  O3  GOL A 102       1.562  15.866   0.723  1.00 38.79           O  
HETATM  737  C1  GOL A 103      10.226   6.879  -7.312  1.00 26.70           C  
HETATM  738  O1  GOL A 103      10.781   5.664  -7.801  1.00 40.53           O  
HETATM  739  C2  GOL A 103      11.144   7.537  -6.307  1.00 36.71           C  
HETATM  740  O2  GOL A 103      10.765   8.896  -6.113  1.00 41.83           O  
HETATM  741  C3  GOL A 103      12.609   7.450  -6.674  1.00 36.03           C  
HETATM  742  O3  GOL A 103      13.436   7.403  -5.516  1.00 53.78           O  
HETATM  743  C1  GOL A 104       7.339  18.304  18.189  1.00 35.85           C  
HETATM  744  O1  GOL A 104       8.137  19.171  17.468  1.00 30.41           O  
HETATM  745  C2  GOL A 104       6.950  18.972  19.531  1.00 53.06           C  
HETATM  746  O2  GOL A 104       5.739  18.485  20.030  1.00 55.13           O  
HETATM  747  C3  GOL A 104       6.928  20.492  19.238  1.00 44.88           C  
HETATM  748  O3  GOL A 104       8.260  20.919  19.322  1.00 44.11           O  
HETATM  749  C1  GOL A 105     -10.651  14.388   6.183  1.00 52.54           C  
HETATM  750  O1  GOL A 105     -11.749  14.467   7.044  1.00 47.00           O  
HETATM  751  C2  GOL A 105     -10.167  12.965   6.295  1.00 53.23           C  
HETATM  752  O2  GOL A 105      -9.055  12.725   5.489  1.00 40.52           O  
HETATM  753  C3  GOL A 105      -9.821  12.828   7.767  1.00 36.49           C  
HETATM  754  O3  GOL A 105     -11.019  12.750   8.440  1.00 66.60           O  
HETATM  755  C1  PEG A 106      17.412  21.434   8.284  1.00 40.63           C  
HETATM  756  O1  PEG A 106      16.694  21.879   7.160  1.00 50.37           O  
HETATM  757  C2  PEG A 106      16.795  21.995   9.559  1.00 42.32           C  
HETATM  758  O2  PEG A 106      17.572  23.068   9.997  1.00 59.91           O  
HETATM  759  C3  PEG A 106      18.447  22.712  11.021  1.00 40.84           C  
HETATM  760  C4  PEG A 106      18.103  23.538  12.250  1.00 36.44           C  
HETATM  761  O4  PEG A 106      17.007  22.982  12.906  1.00 38.74           O  
HETATM  762  S   SO4 A 107       8.149  -9.092   7.658  1.00 78.79           S  
HETATM  763  O1  SO4 A 107       8.961  -9.116   6.443  1.00 69.82           O  
HETATM  764  O2  SO4 A 107       6.770  -8.776   7.303  1.00 68.58           O  
HETATM  765  O3  SO4 A 107       8.685  -8.119   8.608  1.00 74.47           O  
HETATM  766  O4  SO4 A 107       8.184 -10.393   8.302  1.00 68.65           O  
HETATM  767  S   SO4 A 108       0.000   0.000   7.684  0.50126.50           S  
HETATM  768  O1  SO4 A 108       0.603  -0.735   6.574  0.50 90.13           O  
HETATM  769  O2  SO4 A 108      -1.207  -0.009   6.858  0.50 82.80           O  
HETATM  770  O3  SO4 A 108      -0.364  -0.278   9.073  0.50103.98           O  
HETATM  771  O4  SO4 A 108       1.127   0.903   7.921  0.50 83.83           O  
HETATM  772 CL    CL A 109      20.859  14.966  13.005  0.38 28.10          CL  
HETATM  773  C1 ASIN A 110      -5.978  12.270   8.351  0.37 38.18           C  
HETATM  774  C1 BSIN A 110      -5.812  12.254   8.127  0.63 37.33           C  
HETATM  775  O1 ASIN A 110      -6.618  13.162   7.758  0.37 33.85           O  
HETATM  776  O1 BSIN A 110      -6.319  13.256   7.583  0.63 33.49           O  
HETATM  777  O2 ASIN A 110      -6.195  12.077   9.568  0.37 45.84           O  
HETATM  778  O2 BSIN A 110      -6.145  11.987   9.303  0.63 46.08           O  
HETATM  779  C2 ASIN A 110      -4.977  11.425   7.606  0.37 31.14           C  
HETATM  780  C2 BSIN A 110      -4.826  11.378   7.390  0.63 28.94           C  
HETATM  781  C3 ASIN A 110      -4.592  12.072   6.287  0.37 35.75           C  
HETATM  782  C3 BSIN A 110      -4.298  12.043   6.128  0.63 36.79           C  
HETATM  783  C4 ASIN A 110      -3.650  11.144   5.563  0.37 34.39           C  
HETATM  784  C4 BSIN A 110      -5.347  11.945   5.048  0.63 35.90           C  
HETATM  785  O3 ASIN A 110      -4.093  10.197   4.877  0.37 41.01           O  
HETATM  786  O3 BSIN A 110      -6.334  11.189   5.198  0.63 34.65           O  
HETATM  787  O4 ASIN A 110      -2.419  11.318   5.639  0.37 30.18           O  
HETATM  788  O4 BSIN A 110      -5.270  12.637   4.013  0.63 25.94           O  
HETATM  789  O   HOH A 201      -7.378  13.638   5.888  1.00 56.84           O  
HETATM  790  O   HOH A 202      -7.815  10.427   3.877  1.00 58.40           O  
HETATM  791  O   HOH A 203       9.046   4.398  -8.158  1.00 41.59           O  
HETATM  792  O   HOH A 204      16.661  18.383   0.091  1.00 37.86           O  
HETATM  793  O   HOH A 205      -9.486  12.020   3.389  1.00 54.60           O  
HETATM  794  O   HOH A 206       3.071  16.893  -2.903  1.00 40.70           O  
HETATM  795  O   HOH A 207     -13.274  12.370   8.653  1.00 43.46           O  
HETATM  796  O   HOH A 208      11.973   7.712  -3.481  1.00 27.79           O  
HETATM  797  O   HOH A 209       8.482  11.273  -7.086  1.00 22.80           O  
HETATM  798  O   HOH A 210     -12.235  11.805  10.538  1.00 40.24           O  
HETATM  799  O   HOH A 211     -13.421  15.529   8.778  1.00 46.25           O  
HETATM  800  O   HOH A 212       1.396   9.926  -8.204  1.00 48.78           O  
HETATM  801  O   HOH A 213       9.660  20.175   0.245  1.00 22.07           O  
HETATM  802  O   HOH A 214     -13.360  14.974   4.942  1.00 53.68           O  
HETATM  803  O   HOH A 215      17.390  15.298   1.910  1.00 22.14           O  
HETATM  804  O   HOH A 216       5.960  -8.870   2.925  1.00 61.42           O  
HETATM  805  O   HOH A 217      10.425  13.251  16.466  1.00 17.66           O  
HETATM  806  O   HOH A 218       5.426  15.928  -1.818  1.00 26.00           O  
HETATM  807  O   HOH A 219      15.736  -1.763   3.643  1.00 60.07           O  
HETATM  808  O   HOH A 220       0.258   5.985  -3.457  1.00 40.08           O  
HETATM  809  O   HOH A 221      -1.658  13.226  13.167  1.00 37.49           O  
HETATM  810  O   HOH A 222      -3.854  14.898   1.217  1.00 56.09           O  
HETATM  811  O   HOH A 223      14.667  18.569  -0.368  1.00 30.70           O  
HETATM  812  O   HOH A 224       3.482  23.245  19.541  1.00 51.29           O  
HETATM  813  O   HOH A 225      21.564   0.000   3.685  0.50 52.26           O  
HETATM  814  O   HOH A 226      -8.852  16.798   2.312  1.00 40.68           O  
HETATM  815  O   HOH A 227      18.416  11.955   2.664  1.00 38.44           O  
HETATM  816  O   HOH A 228      -7.407  18.684   1.642  1.00 41.45           O  
HETATM  817  O   HOH A 229      17.508  27.092  11.821  1.00 41.09           O  
HETATM  818  O   HOH A 230      16.665  -5.923  -0.170  1.00 62.70           O  
HETATM  819  O   HOH A 231       5.467   1.350   1.201  1.00 46.46           O  
HETATM  820  O   HOH A 232      -1.382  23.196  -2.661  1.00 43.69           O  
HETATM  821  O   HOH A 233      20.015  10.700   0.542  1.00 54.53           O  
HETATM  822  O   HOH A 234       3.887  28.841  10.196  1.00 50.02           O  
HETATM  823  O   HOH A 235       3.878   6.128 -11.307  1.00 50.80           O  
CONECT  725  726  727                                                           
CONECT  726  725                                                                
CONECT  727  725  728  729                                                      
CONECT  728  727                                                                
CONECT  729  727  730                                                           
CONECT  730  729                                                                
CONECT  731  732  733                                                           
CONECT  732  731                                                                
CONECT  733  731  734  735                                                      
CONECT  734  733                                                                
CONECT  735  733  736                                                           
CONECT  736  735                                                                
CONECT  737  738  739                                                           
CONECT  738  737                                                                
CONECT  739  737  740  741                                                      
CONECT  740  739                                                                
CONECT  741  739  742                                                           
CONECT  742  741                                                                
CONECT  743  744  745                                                           
CONECT  744  743                                                                
CONECT  745  743  746  747                                                      
CONECT  746  745                                                                
CONECT  747  745  748                                                           
CONECT  748  747                                                                
CONECT  749  750  751                                                           
CONECT  750  749                                                                
CONECT  751  749  752  753                                                      
CONECT  752  751                                                                
CONECT  753  751  754                                                           
CONECT  754  753                                                                
CONECT  755  756  757                                                           
CONECT  756  755                                                                
CONECT  757  755  758                                                           
CONECT  758  757  759                                                           
CONECT  759  758  760                                                           
CONECT  760  759  761                                                           
CONECT  761  760                                                                
CONECT  762  763  764  765  766                                                 
CONECT  763  762                                                                
CONECT  764  762                                                                
CONECT  765  762                                                                
CONECT  766  762                                                                
CONECT  767  768  769  770  771                                                 
CONECT  768  767                                                                
CONECT  769  767                                                                
CONECT  770  767                                                                
CONECT  771  767                                                                
CONECT  773  775  777  779                                                      
CONECT  774  776  778  780                                                      
CONECT  775  773                                                                
CONECT  776  774                                                                
CONECT  777  773                                                                
CONECT  778  774                                                                
CONECT  779  773  781                                                           
CONECT  780  774  782                                                           
CONECT  781  779  783                                                           
CONECT  782  780  784                                                           
CONECT  783  781  785  787                                                      
CONECT  784  782  786  788                                                      
CONECT  785  783                                                                
CONECT  786  784                                                                
CONECT  787  783                                                                
CONECT  788  784                                                                
MASTER      324    0   10    2    5    0   21    6  753    1   63    8          
END                                                                             
