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HEADER    APOPTOSIS                               06-NOV-12   2YQ7              
TITLE     STRUCTURE OF BCL-XL BOUND TO BIMLOCK                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BCL-2-LIKE PROTEIN 1;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-26,83-209;                                      
COMPND   5 SYNONYM: BCL-XL, BCL2-L-1, APOPTOSIS REGULATOR BCL-X;                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BCL-2-LIKE PROTEIN 11;                                     
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: BH3 DOMAIN, RESIDUES 147-164;                              
COMPND  11 SYNONYM: BIM BETA 5, BCL2-L-11, BCL2-INTERACTING MEDIATOR OF CELL    
COMPND  12 DEATH, BIMEL;                                                        
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES;                                                       
COMPND  15 OTHER_DETAILS: SIDE CHAINS OF AMINO ACIDS AT POSITIONS 154 AND 158   
COMPND  16 LINKED THROUGH A LACTAM BRIDGE.                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PGEX-6P3;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    CONSTRAINED PEPTIDE, APOPTOSIS, BCL-2 FAMILY                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.SMITH,P.E.CZABOTAR                                                
REVDAT   4   30-OCT-19 2YQ7    1       REMARK LINK                              
REVDAT   3   23-OCT-19 2YQ7    1       SEQADV LINK                              
REVDAT   2   27-FEB-13 2YQ7    1       JRNL                                     
REVDAT   1   28-NOV-12 2YQ7    0                                                
JRNL        AUTH   T.OKAMOTO,K.ZOBEL,A.FEDOROVA,C.QUAN,H.YANG,W.J.FAIRBROTHER,  
JRNL        AUTH 2 D.C.S.HUANG,B.J.SMITH,K.DESHAYES,P.E.CZABOTAR                
JRNL        TITL   STABILIZING THE PRO-APOPTOTIC BIMBH3 HELIX (BIMSAHB) DOES    
JRNL        TITL 2 NOT NECESSARILY ENHANCE AFFINITY OR BIOLOGICAL ACTIVITY.     
JRNL        REF    ACS CHEM.BIOL.                V.   8   297 2013              
JRNL        REFN                   ISSN 1554-8929                               
JRNL        PMID   23151250                                                     
JRNL        DOI    10.1021/CB3005403                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 12009                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 593                             
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 34.0734 -  3.0172    1.00     3012   164  0.1524 0.1965        
REMARK   3     2  3.0172 -  2.3950    0.99     2907   147  0.1688 0.1955        
REMARK   3     3  2.3950 -  2.0923    0.99     2885   162  0.1587 0.2144        
REMARK   3     4  2.0923 -  1.9010    0.89     2612   120  0.2105 0.3011        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.650           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.59                          
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      :  0.006           1368                                  
REMARK   3   ANGLE     :  0.941           1849                                  
REMARK   3   CHIRALITY :  0.066            189                                  
REMARK   3   PLANARITY :  0.004            236                                  
REMARK   3   DIHEDRAL  : 14.888            484                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4778   0.2983  16.9716              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1311 T22:   0.0925                                     
REMARK   3      T33:   0.1526 T12:   0.0060                                     
REMARK   3      T13:  -0.0070 T23:  -0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0738 L22:   0.5141                                     
REMARK   3      L33:   2.0175 L12:   0.1548                                     
REMARK   3      L13:  -0.3597 L23:  -0.1652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0364 S12:   0.1145 S13:   0.0904                       
REMARK   3      S21:  -0.0311 S22:   0.0452 S23:   0.0774                       
REMARK   3      S31:  -0.0039 S32:  -0.0742 S33:  -0.0023                       
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 2YQ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-NOV-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290054730.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-AUG-09                          
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               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0092                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12014                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRY 3FDL CHAIN A                               
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 % (W/V) PEG 400, 5 % PEG 3000, 10 %   
REMARK 280  GLYCEROL AND 0.1 M MES PH 6.5.                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       36.90150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       17.61150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.90150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       17.61150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -11.83474            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       60.21093            
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     ASN A   197                                                      
REMARK 465     ASN A   198                                                      
REMARK 465     ALA A   199                                                      
REMARK 465     ALA A   200                                                      
REMARK 465     ALA A   201                                                      
REMARK 465     GLU A   202                                                      
REMARK 465     SER A   203                                                      
REMARK 465     ARG A   204                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     GLY A   206                                                      
REMARK 465     GLN A   207                                                      
REMARK 465     GLU A   208                                                      
REMARK 465     ARG A   209                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU B 154    OE2                                                 
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   CD   GLU B   154     NZ   LYS B   158              1.34            
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    TRP B 147   C   -  N   -  CA  ANGL. DEV. =  18.4 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 1197                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2YQ6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BCL-XL BOUND TO BIMSAHB                                 
DBREF  2YQ7 A    1    26  UNP    Q07817   B2CL1_HUMAN      1     26             
DBREF  2YQ7 A   83   209  UNP    Q07817   B2CL1_HUMAN     83    209             
DBREF  2YQ7 B  147   164  UNP    O43521   B2L11_HUMAN    147    164             
SEQADV 2YQ7 GLY A   -4  UNP  Q07817              EXPRESSION TAG                 
SEQADV 2YQ7 PRO A   -3  UNP  Q07817              EXPRESSION TAG                 
SEQADV 2YQ7 LEU A   -2  UNP  Q07817              EXPRESSION TAG                 
SEQADV 2YQ7 GLY A   -1  UNP  Q07817              EXPRESSION TAG                 
SEQADV 2YQ7 SER A    0  UNP  Q07817              EXPRESSION TAG                 
SEQADV 2YQ7 ACE B  146  UNP  Q6JTU4              ACETYLATION                    
SEQADV 2YQ7 GLU B  154  UNP  O43521    ARG   154 ENGINEERED MUTATION            
SEQADV 2YQ7 LYS B  158  UNP  O43521    GLU   158 ENGINEERED MUTATION            
SEQADV 2YQ7 NH2 B  165  UNP  Q6JTU4              AMIDATION                      
SEQRES   1 A  158  GLY PRO LEU GLY SER MET SER GLN SER ASN ARG GLU LEU          
SEQRES   2 A  158  VAL VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY          
SEQRES   3 A  158  TYR SER TRP SER GLN MET ALA ALA VAL LYS GLN ALA LEU          
SEQRES   4 A  158  ARG GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG          
SEQRES   5 A  158  ALA PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO          
SEQRES   6 A  158  GLY THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU          
SEQRES   7 A  158  LEU PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA          
SEQRES   8 A  158  PHE PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL          
SEQRES   9 A  158  ASP LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA ALA          
SEQRES  10 A  158  TRP MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP          
SEQRES  11 A  158  ILE GLN GLU ASN GLY GLY TRP ASP THR PHE VAL GLU LEU          
SEQRES  12 A  158  TYR GLY ASN ASN ALA ALA ALA GLU SER ARG LYS GLY GLN          
SEQRES  13 A  158  GLU ARG                                                      
SEQRES   1 B   20  ACE TRP ILE ALA GLN GLU LEU ARG GLU ILE GLY ASP LYS          
SEQRES   2 B   20  PHE ASN ALA TYR TYR ALA NH2                                  
HET    ACE  B 146       3                                                       
HET    NH2  B 165       1                                                       
HET    GOL  A1197       6                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  HOH   *120(H2 O)                                                    
HELIX    1   1 GLY A   -4  GLN A   19  1                                  24    
HELIX    2   2 SER A   25  TYR A  101  1                                  21    
HELIX    3   3 TYR A  101  GLN A  111  1                                  11    
HELIX    4   4 THR A  115  GLY A  117  5                                   3    
HELIX    5   5 THR A  118  PHE A  131  1                                  14    
HELIX    6   6 ASN A  136  LYS A  157  1                                  22    
HELIX    7   7 VAL A  161  LEU A  178  1                                  18    
HELIX    8   8 LEU A  178  ASN A  185  1                                   8    
HELIX    9   9 GLY A  186  GLY A  196  1                                  11    
HELIX   10  10 TRP B  147  ALA B  164  1                                  18    
LINK         C   ACE B 146                 N   TRP B 147     1555   1555  1.33  
LINK         C   ALA B 164                 N   NH2 B 165     1555   1555  1.33  
SITE     1 AC1  5 ASP A  11  LYS A  87  GLN A  88  ARG A  91                    
SITE     2 AC1  5 HOH A2019                                                     
CRYST1   73.803   35.223   61.363  90.00 101.12  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013550  0.000000  0.002663        0.00000                         
SCALE2      0.000000  0.028391  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016608        0.00000                         
ATOM      1  N   GLY A  -4     -13.328 -22.078  38.118  1.00 27.34           N  
ANISOU    1  N   GLY A  -4     4970   2251   3165   -359    744    555       N  
ATOM      2  CA  GLY A  -4     -14.274 -22.047  39.218  1.00 30.53           C  
ANISOU    2  CA  GLY A  -4     5338   2738   3523   -453    774    596       C  
ATOM      3  C   GLY A  -4     -14.428 -20.652  39.797  1.00 25.00           C  
ANISOU    3  C   GLY A  -4     4453   2232   2814   -418    732    558       C  
ATOM      4  O   GLY A  -4     -13.593 -19.773  39.545  1.00 22.52           O  
ANISOU    4  O   GLY A  -4     4058   1977   2521   -303    680    519       O  
ATOM      5  N   PRO A  -3     -15.501 -20.440  40.577  1.00 22.32           N  
ANISOU    5  N   PRO A  -3     4049   1992   2439   -520    758    568       N  
ATOM      6  CA  PRO A  -3     -15.792 -19.153  41.219  1.00 25.58           C  
ANISOU    6  CA  PRO A  -3     4299   2584   2837   -493    732    530       C  
ATOM      7  C   PRO A  -3     -14.641 -18.676  42.105  1.00 27.90           C  
ANISOU    7  C   PRO A  -3     4574   2933   3092   -342    705    561       C  
ATOM      8  O   PRO A  -3     -14.331 -17.487  42.133  1.00 20.32           O  
ANISOU    8  O   PRO A  -3     3498   2078   2143   -277    662    502       O  
ATOM      9  CB  PRO A  -3     -17.015 -19.461  42.093  1.00 30.72           C  
ANISOU    9  CB  PRO A  -3     4934   3300   3437   -622    786    566       C  
ATOM     10  CG  PRO A  -3     -17.604 -20.687  41.550  1.00 32.97           C  
ANISOU   10  CG  PRO A  -3     5340   3457   3730   -755    830    594       C  
ATOM     11  CD  PRO A  -3     -16.531 -21.457  40.856  1.00 23.62           C  
ANISOU   11  CD  PRO A  -3     4301   2100   2575   -676    821    614       C  
ATOM     12  N   LEU A  -2     -14.020 -19.602  42.827  1.00 22.16           N  
ANISOU   12  N   LEU A  -2     3966   2139   2315   -291    730    656       N  
ATOM     13  CA  LEU A  -2     -12.962 -19.262  43.771  1.00 22.12           C  
ANISOU   13  CA  LEU A  -2     3942   2207   2255   -157    704    699       C  
ATOM     14  C   LEU A  -2     -11.709 -18.789  43.039  1.00 21.24           C  
ANISOU   14  C   LEU A  -2     3804   2083   2182    -29    647    661       C  
ATOM     15  O   LEU A  -2     -11.141 -17.754  43.365  1.00 24.94           O  
ANISOU   15  O   LEU A  -2     4170   2670   2636     41    604    622       O  
ATOM     16  CB  LEU A  -2     -12.627 -20.479  44.638  1.00 23.49           C  
ANISOU   16  CB  LEU A  -2     4255   2306   2362   -128    746    824       C  
ATOM     17  CG  LEU A  -2     -11.573 -20.284  45.728  1.00 29.68           C  
ANISOU   17  CG  LEU A  -2     5024   3182   3071      6    722    888       C  
ATOM     18  CD1 LEU A  -2     -12.000 -19.163  46.673  1.00 23.38           C  
ANISOU   18  CD1 LEU A  -2     4089   2571   2222    -21    708    844       C  
ATOM     19  CD2 LEU A  -2     -11.330 -21.597  46.500  1.00 25.29           C  
ANISOU   19  CD2 LEU A  -2     4621   2538   2451     36    769   1027       C  
ATOM     20  N   GLY A  -1     -11.279 -19.560  42.048  1.00 22.67           N  
ANISOU   20  N   GLY A  -1     4083   2122   2408     -4    652    669       N  
ATOM     21  CA  GLY A  -1     -10.120 -19.202  41.260  1.00 21.24           C  
ANISOU   21  CA  GLY A  -1     3879   1929   2263    112    605    636       C  
ATOM     22  C   GLY A  -1     -10.359 -17.952  40.438  1.00 25.98           C  
ANISOU   22  C   GLY A  -1     4347   2603   2919     81    561    525       C  
ATOM     23  O   GLY A  -1      -9.472 -17.106  40.308  1.00 29.57           O  
ANISOU   23  O   GLY A  -1     4724   3132   3380    167    513    491       O  
ATOM     24  N   SER A   0     -11.553 -17.838  39.868  1.00 27.06           N  
ANISOU   24  N   SER A   0     4461   2727   3096    -45    577    474       N  
ATOM     25  CA  SER A   0     -11.904 -16.668  39.074  1.00 27.27           C  
ANISOU   25  CA  SER A   0     4365   2821   3173    -73    540    380       C  
ATOM     26  C   SER A   0     -11.803 -15.386  39.895  1.00 24.36           C  
ANISOU   26  C   SER A   0     3875   2599   2780    -34    512    348       C  
ATOM     27  O   SER A   0     -11.351 -14.351  39.403  1.00 30.50           O  
ANISOU   27  O   SER A   0     4573   3426   3590     11    470    287       O  
ATOM     28  CB  SER A   0     -13.311 -16.806  38.495  1.00 33.32           C  
ANISOU   28  CB  SER A   0     5116   3574   3970   -216    564    344       C  
ATOM     29  OG  SER A   0     -13.770 -15.560  37.999  1.00 37.29           O  
ANISOU   29  OG  SER A   0     5487   4171   4510   -231    531    267       O  
ATOM     30  N   MET A   1     -12.236 -15.460  41.145  1.00 22.15           N  
ANISOU   30  N   MET A   1     3591   2386   2441    -57    541    387       N  
ATOM     31  CA  MET A   1     -12.115 -14.340  42.065  1.00 22.44           C  
ANISOU   31  CA  MET A   1     3531   2558   2439    -22    523    356       C  
ATOM     32  C   MET A   1     -10.641 -13.968  42.242  1.00 22.21           C  
ANISOU   32  C   MET A   1     3493   2559   2388     95    478    361       C  
ATOM     33  O   MET A   1     -10.265 -12.793  42.160  1.00 22.90           O  
ANISOU   33  O   MET A   1     3495   2720   2487    125    441    294       O  
ATOM     34  CB  MET A   1     -12.750 -14.714  43.404  1.00 27.73           C  
ANISOU   34  CB  MET A   1     4216   3288   3034    -65    568    410       C  
ATOM     35  CG  MET A   1     -12.821 -13.593  44.419  1.00 34.79           C  
ANISOU   35  CG  MET A   1     5016   4325   3879    -45    562    368       C  
ATOM     36  SD  MET A   1     -12.139 -14.118  45.995  1.00 88.17           S  
ANISOU   36  SD  MET A   1    11826  11152  10523      7    574    458       S  
ATOM     37  CE  MET A   1     -10.423 -13.736  45.717  1.00 22.65           C  
ANISOU   37  CE  MET A   1     3519   2864   2223    131    507    450       C  
ATOM     38  N   SER A   2      -9.810 -14.983  42.467  1.00 21.34           N  
ANISOU   38  N   SER A   2     3471   2393   2243    159    482    442       N  
ATOM     39  CA  SER A   2      -8.369 -14.797  42.630  1.00 23.56           C  
ANISOU   39  CA  SER A   2     3740   2717   2494    274    440    461       C  
ATOM     40  C   SER A   2      -7.708 -14.246  41.365  1.00 25.93           C  
ANISOU   40  C   SER A   2     4001   2990   2862    310    399    398       C  
ATOM     41  O   SER A   2      -6.847 -13.362  41.426  1.00 26.84           O  
ANISOU   41  O   SER A   2     4042   3191   2966    361    356    362       O  
ATOM     42  CB  SER A   2      -7.708 -16.127  43.044  1.00 24.71           C  
ANISOU   42  CB  SER A   2     3996   2798   2593    348    461    574       C  
ATOM     43  OG  SER A   2      -6.295 -16.000  43.159  1.00 27.96           O  
ANISOU   43  OG  SER A   2     4383   3269   2971    469    419    600       O  
ATOM     44  N   GLN A   3      -8.110 -14.780  40.219  1.00 19.61           N  
ANISOU   44  N   GLN A   3     3252   2073   2126    275    415    385       N  
ATOM     45  CA  GLN A   3      -7.571 -14.348  38.936  1.00 21.98           C  
ANISOU   45  CA  GLN A   3     3522   2342   2487    301    382    329       C  
ATOM     46  C   GLN A   3      -7.977 -12.907  38.642  1.00 22.47           C  
ANISOU   46  C   GLN A   3     3473   2482   2584    255    353    240       C  
ATOM     47  O   GLN A   3      -7.194 -12.123  38.104  1.00 19.43           O  
ANISOU   47  O   GLN A   3     3033   2132   2220    296    314    199       O  
ATOM     48  CB  GLN A   3      -8.074 -15.282  37.829  1.00 27.55           C  
ANISOU   48  CB  GLN A   3     4316   2911   3243    256    411    330       C  
ATOM     49  CG  GLN A   3      -7.432 -15.040  36.482  1.00 46.23           C  
ANISOU   49  CG  GLN A   3     6667   5239   5660    292    383    283       C  
ATOM     50  CD  GLN A   3      -5.956 -15.376  36.485  1.00 63.45           C  
ANISOU   50  CD  GLN A   3     8869   7424   7814    421    367    324       C  
ATOM     51  OE1 GLN A   3      -5.104 -14.494  36.613  1.00 67.88           O  
ANISOU   51  OE1 GLN A   3     9343   8086   8363    476    326    303       O  
ATOM     52  NE2 GLN A   3      -5.643 -16.662  36.348  1.00 69.36           N  
ANISOU   52  NE2 GLN A   3     9737   8064   8552    472    403    383       N  
ATOM     53  N   SER A   4      -9.207 -12.555  39.008  1.00 24.44           N  
ANISOU   53  N   SER A   4     3691   2758   2838    173    376    215       N  
ATOM     54  CA  SER A   4      -9.708 -11.201  38.779  1.00 25.99           C  
ANISOU   54  CA  SER A   4     3791   3018   3067    141    357    136       C  
ATOM     55  C   SER A   4      -8.963 -10.162  39.607  1.00 22.72           C  
ANISOU   55  C   SER A   4     3317   2704   2613    188    331    108       C  
ATOM     56  O   SER A   4      -8.617  -9.089  39.110  1.00 17.50           O  
ANISOU   56  O   SER A   4     2599   2067   1983    198    300     48       O  
ATOM     57  CB  SER A   4     -11.206 -11.127  39.070  1.00 27.14           C  
ANISOU   57  CB  SER A   4     3911   3183   3218     56    394    123       C  
ATOM     58  OG  SER A   4     -11.926 -11.768  38.033  1.00 32.53           O  
ANISOU   58  OG  SER A   4     4623   3789   3946     -6    407    124       O  
ATOM     59  N   ASN A   5      -8.720 -10.485  40.873  1.00 22.42           N  
ANISOU   59  N   ASN A   5     3295   2723   2499    208    343    152       N  
ATOM     60  CA  ASN A   5      -7.947  -9.609  41.735  1.00 21.35           C  
ANISOU   60  CA  ASN A   5     3110   2694   2308    242    317    125       C  
ATOM     61  C   ASN A   5      -6.535  -9.400  41.208  1.00 18.91           C  
ANISOU   61  C   ASN A   5     2785   2398   2002    305    270    123       C  
ATOM     62  O   ASN A   5      -6.007  -8.295  41.259  1.00 20.34           O  
ANISOU   62  O   ASN A   5     2908   2642   2178    304    240     63       O  
ATOM     63  CB  ASN A   5      -7.910 -10.151  43.167  1.00 20.40           C  
ANISOU   63  CB  ASN A   5     3014   2642   2094    253    337    185       C  
ATOM     64  CG  ASN A   5      -9.180  -9.880  43.915  1.00 26.89           C  
ANISOU   64  CG  ASN A   5     3820   3502   2897    188    380    163       C  
ATOM     65  OD1 ASN A   5     -10.011  -9.086  43.478  1.00 27.81           O  
ANISOU   65  OD1 ASN A   5     3891   3611   3064    147    391     95       O  
ATOM     66  ND2 ASN A   5      -9.343 -10.533  45.060  1.00 28.33           N  
ANISOU   66  ND2 ASN A   5     4035   3731   2998    185    408    226       N  
ATOM     67  N   ARG A   6      -5.923 -10.464  40.695  1.00 23.78           N  
ANISOU   67  N   ARG A   6     3456   2954   2625    356    267    186       N  
ATOM     68  CA  ARG A   6      -4.583 -10.362  40.117  1.00 23.55           C  
ANISOU   68  CA  ARG A   6     3405   2947   2597    424    228    189       C  
ATOM     69  C   ARG A   6      -4.566  -9.449  38.898  1.00 24.25           C  
ANISOU   69  C   ARG A   6     3450   3006   2760    394    206    114       C  
ATOM     70  O   ARG A   6      -3.659  -8.627  38.730  1.00 19.70           O  
ANISOU   70  O   ARG A   6     2816   2494   2175    409    170     79       O  
ATOM     71  CB  ARG A   6      -4.052 -11.741  39.731  1.00 28.54           C  
ANISOU   71  CB  ARG A   6     4114   3504   3226    496    242    270       C  
ATOM     72  CG  ARG A   6      -2.906 -11.682  38.742  1.00 34.54           C  
ANISOU   72  CG  ARG A   6     4850   4263   4009    561    212    262       C  
ATOM     73  CD  ARG A   6      -1.634 -12.249  39.324  1.00 42.38           C  
ANISOU   73  CD  ARG A   6     5840   5332   4932    669    196    336       C  
ATOM     74  NE  ARG A   6      -0.481 -11.927  38.489  1.00 42.79           N  
ANISOU   74  NE  ARG A   6     5836   5426   4995    724    164    318       N  
ATOM     75  CZ  ARG A   6       0.671 -11.454  38.955  1.00 38.11           C  
ANISOU   75  CZ  ARG A   6     5162   4976   4342    769    124    327       C  
ATOM     76  NH1 ARG A   6       0.837 -11.251  40.258  1.00 34.27           N  
ANISOU   76  NH1 ARG A   6     4643   4604   3775    769    109    352       N  
ATOM     77  NH2 ARG A   6       1.660 -11.190  38.115  1.00 37.66           N  
ANISOU   77  NH2 ARG A   6     5051   4960   4297    810    100    311       N  
ATOM     78  N   GLU A   7      -5.572  -9.590  38.046  1.00 13.84           N  
ANISOU   78  N   GLU A   7     2155   1596   1506    346    228     93       N  
ATOM     79  CA  GLU A   7      -5.646  -8.788  36.829  1.00 17.82           C  
ANISOU   79  CA  GLU A   7     2622   2070   2077    320    208     33       C  
ATOM     80  C   GLU A   7      -5.870  -7.309  37.141  1.00 15.32           C  
ANISOU   80  C   GLU A   7     2239   1814   1767    283    194    -36       C  
ATOM     81  O   GLU A   7      -5.376  -6.427  36.427  1.00 17.11           O  
ANISOU   81  O   GLU A   7     2429   2047   2025    280    167    -79       O  
ATOM     82  CB  GLU A   7      -6.742  -9.326  35.901  1.00 20.65           C  
ANISOU   82  CB  GLU A   7     3019   2335   2493    272    233     30       C  
ATOM     83  CG  GLU A   7      -6.387 -10.687  35.302  1.00 33.36           C  
ANISOU   83  CG  GLU A   7     4709   3861   4105    304    248     80       C  
ATOM     84  CD  GLU A   7      -7.579 -11.402  34.680  1.00 53.34           C  
ANISOU   84  CD  GLU A   7     7291   6306   6671    234    279     81       C  
ATOM     85  OE1 GLU A   7      -8.680 -10.811  34.634  1.00 60.50           O  
ANISOU   85  OE1 GLU A   7     8153   7232   7601    165    284     46       O  
ATOM     86  OE2 GLU A   7      -7.410 -12.561  34.239  1.00 59.87           O  
ANISOU   86  OE2 GLU A   7     8202   7047   7497    247    300    115       O  
ATOM     87  N   LEU A   8      -6.609  -7.051  38.214  1.00 13.11           N  
ANISOU   87  N   LEU A   8     1952   1574   1455    255    216    -46       N  
ATOM     88  CA  LEU A   8      -6.879  -5.691  38.660  1.00 13.99           C  
ANISOU   88  CA  LEU A   8     2017   1735   1565    227    214   -115       C  
ATOM     89  C   LEU A   8      -5.568  -5.036  39.101  1.00 16.25           C  
ANISOU   89  C   LEU A   8     2275   2096   1803    245    179   -137       C  
ATOM     90  O   LEU A   8      -5.253  -3.900  38.716  1.00 14.12           O  
ANISOU   90  O   LEU A   8     1976   1831   1558    224    161   -196       O  
ATOM     91  CB  LEU A   8      -7.886  -5.730  39.809  1.00 14.07           C  
ANISOU   91  CB  LEU A   8     2028   1781   1536    202    253   -116       C  
ATOM     92  CG  LEU A   8      -8.545  -4.423  40.236  1.00 24.12           C  
ANISOU   92  CG  LEU A   8     3265   3084   2815    178    270   -191       C  
ATOM     93  CD1 LEU A   8      -9.030  -3.622  39.009  1.00 20.89           C  
ANISOU   93  CD1 LEU A   8     2834   2612   2493    170    264   -233       C  
ATOM     94  CD2 LEU A   8      -9.708  -4.724  41.181  1.00 24.61           C  
ANISOU   94  CD2 LEU A   8     3328   3180   2844    157    318   -181       C  
ATOM     95  N   VAL A   9      -4.801  -5.767  39.906  1.00 15.52           N  
ANISOU   95  N   VAL A   9     2192   2066   1638    280    170    -85       N  
ATOM     96  CA  VAL A   9      -3.474  -5.327  40.314  1.00 15.25           C  
ANISOU   96  CA  VAL A   9     2120   2128   1545    296    131    -95       C  
ATOM     97  C   VAL A   9      -2.567  -5.069  39.112  1.00 16.53           C  
ANISOU   97  C   VAL A   9     2258   2272   1751    309    100   -104       C  
ATOM     98  O   VAL A   9      -1.958  -3.995  39.006  1.00 15.40           O  
ANISOU   98  O   VAL A   9     2075   2174   1603    274     75   -160       O  
ATOM     99  CB  VAL A   9      -2.792  -6.355  41.247  1.00 16.46           C  
ANISOU   99  CB  VAL A   9     2284   2358   1612    350    125    -15       C  
ATOM    100  CG1 VAL A   9      -1.294  -6.005  41.434  1.00 15.16           C  
ANISOU  100  CG1 VAL A   9     2063   2311   1387    373     77    -15       C  
ATOM    101  CG2 VAL A   9      -3.522  -6.418  42.592  1.00 16.09           C  
ANISOU  101  CG2 VAL A   9     2252   2360   1501    327    152    -11       C  
ATOM    102  N   VAL A  10      -2.468  -6.048  38.213  1.00 13.50           N  
ANISOU  102  N   VAL A  10     1903   1822   1405    354    104    -53       N  
ATOM    103  CA  VAL A  10      -1.650  -5.878  37.019  1.00 13.54           C  
ANISOU  103  CA  VAL A  10     1885   1813   1447    370     80    -60       C  
ATOM    104  C   VAL A  10      -2.085  -4.675  36.184  1.00 14.25           C  
ANISOU  104  C   VAL A  10     1955   1856   1601    309     75   -130       C  
ATOM    105  O   VAL A  10      -1.257  -3.875  35.732  1.00 14.30           O  
ANISOU  105  O   VAL A  10     1923   1900   1611    290     49   -161       O  
ATOM    106  CB  VAL A  10      -1.614  -7.164  36.154  1.00 15.87           C  
ANISOU  106  CB  VAL A  10     2229   2030   1772    429     96     -3       C  
ATOM    107  CG1 VAL A  10      -0.911  -6.893  34.827  1.00 17.12           C  
ANISOU  107  CG1 VAL A  10     2362   2173   1971    439     77    -21       C  
ATOM    108  CG2 VAL A  10      -0.887  -8.257  36.903  1.00 14.56           C  
ANISOU  108  CG2 VAL A  10     2083   1911   1539    509     98     73       C  
ATOM    109  N   ASP A  11      -3.389  -4.535  35.989  1.00 14.13           N  
ANISOU  109  N   ASP A  11     1967   1767   1636    278    102   -150       N  
ATOM    110  CA  ASP A  11      -3.894  -3.413  35.207  1.00 16.53           C  
ANISOU  110  CA  ASP A  11     2257   2024   2002    236    101   -205       C  
ATOM    111  C   ASP A  11      -3.510  -2.074  35.813  1.00 13.45           C  
ANISOU  111  C   ASP A  11     1840   1682   1588    197     90   -265       C  
ATOM    112  O   ASP A  11      -3.049  -1.177  35.110  1.00 11.78           O  
ANISOU  112  O   ASP A  11     1613   1458   1404    170     73   -297       O  
ATOM    113  CB  ASP A  11      -5.415  -3.468  35.082  1.00 12.31           C  
ANISOU  113  CB  ASP A  11     1740   1427   1511    217    132   -211       C  
ATOM    114  CG  ASP A  11      -5.953  -2.304  34.312  1.00 18.40           C  
ANISOU  114  CG  ASP A  11     2494   2156   2341    191    131   -257       C  
ATOM    115  OD1 ASP A  11      -5.936  -2.383  33.065  1.00 20.27           O  
ANISOU  115  OD1 ASP A  11     2730   2349   2622    192    119   -246       O  
ATOM    116  OD2 ASP A  11      -6.359  -1.303  34.952  1.00 15.43           O  
ANISOU  116  OD2 ASP A  11     2110   1790   1961    175    145   -302       O  
ATOM    117  N   PHE A  12      -3.730  -1.932  37.119  1.00 13.52           N  
ANISOU  117  N   PHE A  12     1852   1744   1543    187    103   -281       N  
ATOM    118  CA  PHE A  12      -3.450  -0.666  37.787  1.00 13.09           C  
ANISOU  118  CA  PHE A  12     1787   1729   1459    141     99   -350       C  
ATOM    119  C   PHE A  12      -1.957  -0.351  37.753  1.00 15.51           C  
ANISOU  119  C   PHE A  12     2060   2113   1719    120     59   -358       C  
ATOM    120  O   PHE A  12      -1.554   0.790  37.497  1.00 13.17           O  
ANISOU  120  O   PHE A  12     1760   1811   1435     66     50   -413       O  
ATOM    121  CB  PHE A  12      -3.956  -0.691  39.231  1.00 13.33           C  
ANISOU  121  CB  PHE A  12     1827   1812   1426    135    124   -367       C  
ATOM    122  CG  PHE A  12      -3.851   0.638  39.931  1.00 14.00           C  
ANISOU  122  CG  PHE A  12     1917   1921   1480     83    130   -453       C  
ATOM    123  CD1 PHE A  12      -2.714   0.977  40.643  1.00 14.42           C  
ANISOU  123  CD1 PHE A  12     1951   2074   1453     45    102   -479       C  
ATOM    124  CD2 PHE A  12      -4.903   1.538  39.891  1.00 13.85           C  
ANISOU  124  CD2 PHE A  12     1924   1830   1508     73    168   -509       C  
ATOM    125  CE1 PHE A  12      -2.620   2.191  41.296  1.00 15.01           C  
ANISOU  125  CE1 PHE A  12     2044   2166   1495    -17    111   -567       C  
ATOM    126  CE2 PHE A  12      -4.811   2.762  40.542  1.00 14.46           C  
ANISOU  126  CE2 PHE A  12     2024   1912   1557     29    183   -594       C  
ATOM    127  CZ  PHE A  12      -3.672   3.085  41.244  1.00 15.07           C  
ANISOU  127  CZ  PHE A  12     2093   2078   1553    -24    155   -628       C  
ATOM    128  N   LEU A  13      -1.132  -1.360  38.025  1.00 13.29           N  
ANISOU  128  N   LEU A  13     1756   1909   1384    161     39   -299       N  
ATOM    129  CA  LEU A  13       0.309  -1.132  38.039  1.00 13.70           C  
ANISOU  129  CA  LEU A  13     1757   2065   1383    146      0   -298       C  
ATOM    130  C   LEU A  13       0.817  -0.776  36.650  1.00 17.54           C  
ANISOU  130  C   LEU A  13     2227   2509   1927    134    -14   -302       C  
ATOM    131  O   LEU A  13       1.693   0.094  36.505  1.00 13.58           O  
ANISOU  131  O   LEU A  13     1692   2064   1406     75    -37   -339       O  
ATOM    132  CB  LEU A  13       1.074  -2.335  38.613  1.00 15.70           C  
ANISOU  132  CB  LEU A  13     1984   2418   1564    215    -17   -222       C  
ATOM    133  CG  LEU A  13       0.818  -2.661  40.083  1.00 16.08           C  
ANISOU  133  CG  LEU A  13     2040   2539   1531    223    -10   -209       C  
ATOM    134  CD1 LEU A  13       1.676  -3.854  40.576  1.00 15.72           C  
ANISOU  134  CD1 LEU A  13     1968   2595   1411    306    -29   -118       C  
ATOM    135  CD2 LEU A  13       1.057  -1.440  40.942  1.00 16.39           C  
ANISOU  135  CD2 LEU A  13     2059   2655   1513    136    -21   -290       C  
ATOM    136  N   SER A  14       0.277  -1.444  35.632  1.00 12.68           N  
ANISOU  136  N   SER A  14     1637   1804   1379    180      0   -265       N  
ATOM    137  CA  SER A  14       0.662  -1.163  34.255  1.00 18.19           C  
ANISOU  137  CA  SER A  14     2322   2461   2128    171    -10   -266       C  
ATOM    138  C   SER A  14       0.392   0.301  33.928  1.00 15.71           C  
ANISOU  138  C   SER A  14     2019   2099   1853     94     -8   -330       C  
ATOM    139  O   SER A  14       1.204   0.982  33.312  1.00 16.06           O  
ANISOU  139  O   SER A  14     2038   2166   1899     50    -25   -347       O  
ATOM    140  CB  SER A  14      -0.123  -2.041  33.278  1.00 20.89           C  
ANISOU  140  CB  SER A  14     2700   2705   2530    219     10   -228       C  
ATOM    141  OG  SER A  14       0.228  -3.402  33.410  1.00 27.58           O  
ANISOU  141  OG  SER A  14     3555   3576   3348    292     13   -169       O  
ATOM    142  N   TYR A  15      -0.768   0.770  34.356  1.00 17.25           N  
ANISOU  142  N   TYR A  15     2253   2224   2076     80     18   -363       N  
ATOM    143  CA  TYR A  15      -1.190   2.139  34.107  1.00 14.85           C  
ANISOU  143  CA  TYR A  15     1976   1852   1812     25     30   -420       C  
ATOM    144  C   TYR A  15      -0.273   3.138  34.800  1.00 16.19           C  
ANISOU  144  C   TYR A  15     2139   2085   1929    -50     17   -476       C  
ATOM    145  O   TYR A  15       0.201   4.092  34.178  1.00 17.44           O  
ANISOU  145  O   TYR A  15     2304   2215   2108   -107     10   -504       O  
ATOM    146  CB  TYR A  15      -2.637   2.303  34.567  1.00 12.12           C  
ANISOU  146  CB  TYR A  15     1667   1439   1499     46     67   -440       C  
ATOM    147  CG  TYR A  15      -3.199   3.687  34.409  1.00 12.34           C  
ANISOU  147  CG  TYR A  15     1732   1387   1570     15     88   -495       C  
ATOM    148  CD1 TYR A  15      -3.270   4.288  33.157  1.00 25.38           C  
ANISOU  148  CD1 TYR A  15     3394   2965   3283      8     84   -486       C  
ATOM    149  CD2 TYR A  15      -3.698   4.378  35.504  1.00 12.89           C  
ANISOU  149  CD2 TYR A  15     1831   1451   1615      0    117   -553       C  
ATOM    150  CE1 TYR A  15      -3.801   5.546  32.997  1.00 23.04           C  
ANISOU  150  CE1 TYR A  15     3142   2583   3027     -8    108   -527       C  
ATOM    151  CE2 TYR A  15      -4.246   5.645  35.358  1.00 16.99           C  
ANISOU  151  CE2 TYR A  15     2397   1881   2176    -14    146   -603       C  
ATOM    152  CZ  TYR A  15      -4.289   6.224  34.092  1.00 25.67           C  
ANISOU  152  CZ  TYR A  15     3511   2900   3341    -14    141   -586       C  
ATOM    153  OH  TYR A  15      -4.814   7.487  33.916  1.00 23.15           O  
ANISOU  153  OH  TYR A  15     3249   2483   3066    -16    172   -626       O  
ATOM    154  N   LYS A  16      -0.001   2.922  36.081  1.00 14.04           N  
ANISOU  154  N   LYS A  16     1854   1901   1581    -58     13   -492       N  
ATOM    155  CA ALYS A  16       0.875   3.834  36.816  0.93 15.09           C  
ANISOU  155  CA ALYS A  16     1978   2109   1648   -144     -2   -552       C  
ATOM    156  CA BLYS A  16       0.873   3.825  36.821  0.07 17.28           C  
ANISOU  156  CA BLYS A  16     2254   2386   1924   -144     -2   -552       C  
ATOM    157  C   LYS A  16       2.272   3.868  36.221  1.00 18.11           C  
ANISOU  157  C   LYS A  16     2302   2578   2001   -184    -40   -533       C  
ATOM    158  O   LYS A  16       2.883   4.936  36.128  1.00 16.15           O  
ANISOU  158  O   LYS A  16     2058   2338   1738   -279    -47   -585       O  
ATOM    159  CB ALYS A  16       0.927   3.481  38.304  0.93 20.35           C  
ANISOU  159  CB ALYS A  16     2633   2876   2224   -144     -3   -566       C  
ATOM    160  CB BLYS A  16       0.927   3.445  38.301  0.07 20.35           C  
ANISOU  160  CB BLYS A  16     2632   2877   2224   -142     -4   -564       C  
ATOM    161  CG ALYS A  16      -0.359   3.806  39.028  0.93 24.94           C  
ANISOU  161  CG ALYS A  16     3271   3385   2820   -132     41   -608       C  
ATOM    162  CG BLYS A  16      -0.310   3.868  39.067  0.07 22.84           C  
ANISOU  162  CG BLYS A  16     3005   3123   2551   -137     40   -613       C  
ATOM    163  CD ALYS A  16      -0.600   5.290  38.999  0.93 24.20           C  
ANISOU  163  CD ALYS A  16     3234   3208   2753   -203     65   -697       C  
ATOM    164  CD BLYS A  16      -0.551   5.356  38.891  0.07 23.61           C  
ANISOU  164  CD BLYS A  16     3160   3128   2684   -206     64   -698       C  
ATOM    165  CE ALYS A  16      -2.074   5.612  38.861  0.93 23.42           C  
ANISOU  165  CE ALYS A  16     3189   2984   2727   -152    115   -714       C  
ATOM    166  CE BLYS A  16      -1.960   5.747  39.294  0.07 23.08           C  
ANISOU  166  CE BLYS A  16     3149   2965   2654   -170    117   -735       C  
ATOM    167  NZ ALYS A  16      -2.194   7.063  38.565  0.93 19.37           N  
ANISOU  167  NZ ALYS A  16     2740   2367   2253   -205    140   -787       N  
ATOM    168  NZ BLYS A  16      -2.999   4.995  38.546  0.07 22.24           N  
ANISOU  168  NZ BLYS A  16     3036   2790   2624    -83    133   -670       N  
ATOM    169  N   LEU A  17       2.777   2.704  35.808  1.00 16.15           N  
ANISOU  169  N   LEU A  17     2003   2393   1742   -113    -59   -459       N  
ATOM    170  CA  LEU A  17       4.104   2.655  35.192  1.00 15.02           C  
ANISOU  170  CA  LEU A  17     1791   2347   1568   -135    -91   -435       C  
ATOM    171  C   LEU A  17       4.103   3.475  33.896  1.00 17.63           C  
ANISOU  171  C   LEU A  17     2143   2586   1969   -184    -83   -451       C  
ATOM    172  O   LEU A  17       5.016   4.262  33.655  1.00 19.34           O  
ANISOU  172  O   LEU A  17     2331   2858   2160   -272    -99   -478       O  
ATOM    173  CB  LEU A  17       4.574   1.207  34.944  1.00 14.24           C  
ANISOU  173  CB  LEU A  17     1644   2318   1449    -27   -103   -352       C  
ATOM    174  CG  LEU A  17       4.997   0.383  36.172  1.00 16.40           C  
ANISOU  174  CG  LEU A  17     1879   2719   1632     24   -119   -317       C  
ATOM    175  CD1 LEU A  17       5.095  -1.106  35.831  1.00 19.35           C  
ANISOU  175  CD1 LEU A  17     2245   3098   2011    153   -114   -229       C  
ATOM    176  CD2 LEU A  17       6.314   0.872  36.769  1.00 15.82           C  
ANISOU  176  CD2 LEU A  17     1724   2826   1463    -43   -157   -335       C  
ATOM    177  N   SER A  18       3.064   3.302  33.081  1.00 16.51           N  
ANISOU  177  N   SER A  18     2051   2312   1910   -134    -59   -433       N  
ATOM    178  CA  SER A  18       2.977   3.999  31.793  1.00 19.97           C  
ANISOU  178  CA  SER A  18     2511   2664   2413   -167    -53   -435       C  
ATOM    179  C   SER A  18       2.944   5.519  31.960  1.00 20.63           C  
ANISOU  179  C   SER A  18     2643   2690   2507   -270    -42   -500       C  
ATOM    180  O   SER A  18       3.437   6.257  31.110  1.00 20.23           O  
ANISOU  180  O   SER A  18     2596   2616   2476   -333    -45   -503       O  
ATOM    181  CB  SER A  18       1.763   3.518  30.979  1.00 20.14           C  
ANISOU  181  CB  SER A  18     2573   2569   2511    -95    -32   -402       C  
ATOM    182  OG  SER A  18       0.553   4.058  31.489  1.00 22.34           O  
ANISOU  182  OG  SER A  18     2908   2755   2824    -93     -5   -436       O  
ATOM    183  N   GLN A  19       2.394   5.987  33.072  1.00 14.47           N  
ANISOU  183  N   GLN A  19     1905   1884   1708   -291    -25   -553       N  
ATOM    184  CA  GLN A  19       2.304   7.419  33.312  1.00 18.61           C  
ANISOU  184  CA  GLN A  19     2494   2334   2241   -383     -6   -624       C  
ATOM    185  C   GLN A  19       3.683   8.028  33.517  1.00 23.75           C  
ANISOU  185  C   GLN A  19     3113   3087   2825   -504    -31   -657       C  
ATOM    186  O   GLN A  19       3.852   9.240  33.411  1.00 25.27           O  
ANISOU  186  O   GLN A  19     3364   3212   3026   -602    -16   -709       O  
ATOM    187  CB  GLN A  19       1.382   7.707  34.505  1.00 22.91           C  
ANISOU  187  CB  GLN A  19     3093   2836   2774   -369     24   -679       C  
ATOM    188  CG  GLN A  19      -0.093   7.468  34.179  1.00 26.66           C  
ANISOU  188  CG  GLN A  19     3607   3197   3326   -271     56   -654       C  
ATOM    189  CD  GLN A  19      -1.022   7.738  35.349  1.00 27.58           C  
ANISOU  189  CD  GLN A  19     3768   3283   3427   -250     92   -707       C  
ATOM    190  OE1 GLN A  19      -0.702   7.429  36.501  1.00 21.22           O  
ANISOU  190  OE1 GLN A  19     2944   2573   2546   -270     86   -735       O  
ATOM    191  NE2 GLN A  19      -2.188   8.310  35.056  1.00 25.08           N  
ANISOU  191  NE2 GLN A  19     3506   2844   3178   -204    131   -719       N  
ATOM    192  N   LYS A  20       4.671   7.182  33.807  1.00 16.68           N  
ANISOU  192  N   LYS A  20     2124   2355   1858   -497    -66   -625       N  
ATOM    193  CA  LYS A  20       6.031   7.655  34.018  1.00 20.12           C  
ANISOU  193  CA  LYS A  20     2504   2924   2217   -612    -95   -650       C  
ATOM    194  C   LYS A  20       6.918   7.249  32.849  1.00 25.18           C  
ANISOU  194  C   LYS A  20     3069   3635   2863   -603   -115   -588       C  
ATOM    195  O   LYS A  20       8.136   7.395  32.904  1.00 29.56           O  
ANISOU  195  O   LYS A  20     3547   4336   3349   -681   -142   -591       O  
ATOM    196  CB  LYS A  20       6.596   7.107  35.327  1.00 24.48           C  
ANISOU  196  CB  LYS A  20     2992   3645   2665   -614   -122   -661       C  
ATOM    197  CG  LYS A  20       5.879   7.588  36.569  1.00 31.79           C  
ANISOU  197  CG  LYS A  20     3987   4529   3564   -643   -102   -733       C  
ATOM    198  CD  LYS A  20       6.224   9.032  36.887  1.00 36.90           C  
ANISOU  198  CD  LYS A  20     4692   5144   4183   -803    -91   -828       C  
ATOM    199  CE  LYS A  20       5.573   9.471  38.186  1.00 46.38           C  
ANISOU  199  CE  LYS A  20     5963   6316   5344   -828    -67   -908       C  
ATOM    200  NZ  LYS A  20       4.108   9.205  38.157  1.00 52.35           N  
ANISOU  200  NZ  LYS A  20     6787   6923   6181   -707    -25   -895       N  
ATOM    201  N   GLY A  21       6.303   6.733  31.791  1.00 25.05           N  
ANISOU  201  N   GLY A  21     3069   3525   2923   -511   -101   -535       N  
ATOM    202  CA  GLY A  21       7.048   6.321  30.615  1.00 26.33           C  
ANISOU  202  CA  GLY A  21     3169   3744   3092   -493   -112   -479       C  
ATOM    203  C   GLY A  21       7.713   4.961  30.758  1.00 27.53           C  
ANISOU  203  C   GLY A  21     3226   4041   3191   -394   -134   -423       C  
ATOM    204  O   GLY A  21       8.631   4.636  30.016  1.00 24.46           O  
ANISOU  204  O   GLY A  21     2764   3748   2780   -386   -145   -385       O  
ATOM    205  N   TYR A  22       7.251   4.172  31.723  1.00 21.13           N  
ANISOU  205  N   TYR A  22     2420   3248   2359   -315   -136   -414       N  
ATOM    206  CA  TYR A  22       7.743   2.811  31.932  1.00 22.67           C  
ANISOU  206  CA  TYR A  22     2547   3555   2510   -201   -149   -353       C  
ATOM    207  C   TYR A  22       6.676   1.861  31.436  1.00 21.10           C  
ANISOU  207  C   TYR A  22     2407   3230   2380    -86   -124   -314       C  
ATOM    208  O   TYR A  22       5.569   2.293  31.116  1.00 16.19           O  
ANISOU  208  O   TYR A  22     1861   2462   1827    -99   -103   -337       O  
ATOM    209  CB  TYR A  22       7.991   2.551  33.427  1.00 17.80           C  
ANISOU  209  CB  TYR A  22     1900   3052   1810   -197   -168   -362       C  
ATOM    210  CG  TYR A  22       9.042   3.427  34.047  1.00 21.22           C  
ANISOU  210  CG  TYR A  22     2269   3633   2159   -323   -197   -406       C  
ATOM    211  CD1 TYR A  22      10.137   3.861  33.312  1.00 19.86           C  
ANISOU  211  CD1 TYR A  22     2024   3558   1962   -393   -212   -402       C  
ATOM    212  CD2 TYR A  22       8.945   3.820  35.372  1.00 19.33           C  
ANISOU  212  CD2 TYR A  22     2042   3445   1856   -381   -208   -454       C  
ATOM    213  CE1 TYR A  22      11.096   4.660  33.880  1.00 24.23           C  
ANISOU  213  CE1 TYR A  22     2517   4256   2433   -527   -239   -446       C  
ATOM    214  CE2 TYR A  22       9.895   4.621  35.943  1.00 23.47           C  
ANISOU  214  CE2 TYR A  22     2511   4110   2295   -512   -236   -502       C  
ATOM    215  CZ  TYR A  22      10.968   5.035  35.192  1.00 21.32           C  
ANISOU  215  CZ  TYR A  22     2165   3933   2003   -589   -252   -498       C  
ATOM    216  OH  TYR A  22      11.907   5.830  35.773  1.00 25.51           O  
ANISOU  216  OH  TYR A  22     2637   4612   2442   -736   -280   -548       O  
ATOM    217  N   SER A  23       6.978   0.565  31.382  1.00 16.38           N  
ANISOU  217  N   SER A  23     1776   2687   1760     28   -125   -254       N  
ATOM    218  CA  SER A  23       5.952  -0.394  30.990  1.00 17.41           C  
ANISOU  218  CA  SER A  23     1972   2694   1948    122    -99   -223       C  
ATOM    219  C   SER A  23       6.057  -1.679  31.793  1.00 22.64           C  
ANISOU  219  C   SER A  23     2629   3409   2566    229    -98   -171       C  
ATOM    220  O   SER A  23       7.155  -2.114  32.148  1.00 19.75           O  
ANISOU  220  O   SER A  23     2191   3184   2131    272   -115   -137       O  
ATOM    221  CB  SER A  23       6.017  -0.699  29.486  1.00 22.85           C  
ANISOU  221  CB  SER A  23     2667   3331   2686    154    -86   -200       C  
ATOM    222  OG  SER A  23       7.177  -1.447  29.177  1.00 32.52           O  
ANISOU  222  OG  SER A  23     3822   4672   3862    222    -92   -158       O  
ATOM    223  N   TRP A  24       4.901  -2.282  32.057  1.00 18.29           N  
ANISOU  223  N   TRP A  24     2152   2747   2052    271    -75   -161       N  
ATOM    224  CA  TRP A  24       4.811  -3.567  32.742  1.00 19.01           C  
ANISOU  224  CA  TRP A  24     2262   2850   2110    370    -64   -106       C  
ATOM    225  C   TRP A  24       5.438  -4.659  31.887  1.00 20.29           C  
ANISOU  225  C   TRP A  24     2417   3019   2273    472    -52    -52       C  
ATOM    226  O   TRP A  24       6.151  -5.531  32.390  1.00 24.16           O  
ANISOU  226  O   TRP A  24     2882   3591   2707    564    -54      3       O  
ATOM    227  CB  TRP A  24       3.335  -3.888  33.028  1.00 17.60           C  
ANISOU  227  CB  TRP A  24     2169   2540   1980    370    -36   -111       C  
ATOM    228  CG  TRP A  24       3.080  -5.297  33.443  1.00 16.32           C  
ANISOU  228  CG  TRP A  24     2051   2349   1800    464    -16    -49       C  
ATOM    229  CD1 TRP A  24       2.728  -6.340  32.633  1.00 15.69           C  
ANISOU  229  CD1 TRP A  24     2029   2174   1759    525     11    -16       C  
ATOM    230  CD2 TRP A  24       3.153  -5.825  34.771  1.00 13.73           C  
ANISOU  230  CD2 TRP A  24     1726   2083   1407    502    -17    -12       C  
ATOM    231  NE1 TRP A  24       2.584  -7.487  33.376  1.00 19.47           N  
ANISOU  231  NE1 TRP A  24     2554   2639   2206    598     30     41       N  
ATOM    232  CE2 TRP A  24       2.836  -7.197  34.692  1.00 20.94           C  
ANISOU  232  CE2 TRP A  24     2704   2924   2327    589     13     50       C  
ATOM    233  CE3 TRP A  24       3.458  -5.271  36.021  1.00 20.03           C  
ANISOU  233  CE3 TRP A  24     2482   2992   2135    467    -39    -25       C  
ATOM    234  CZ2 TRP A  24       2.819  -8.025  35.811  1.00 21.04           C  
ANISOU  234  CZ2 TRP A  24     2743   2967   2283    647     21    108       C  
ATOM    235  CZ3 TRP A  24       3.437  -6.094  37.134  1.00 20.69           C  
ANISOU  235  CZ3 TRP A  24     2583   3122   2157    525    -34     31       C  
ATOM    236  CH2 TRP A  24       3.122  -7.458  37.021  1.00 17.62           C  
ANISOU  236  CH2 TRP A  24     2260   2655   1780    617     -4    102       C  
ATOM    237  N   SER A  25       5.185  -4.597  30.581  1.00 15.22           N  
ANISOU  237  N   SER A  25     1799   2294   1690    462    -38    -67       N  
ATOM    238  CA  SER A  25       5.682  -5.605  29.660  1.00 19.49           C  
ANISOU  238  CA  SER A  25     2347   2825   2234    555    -19    -29       C  
ATOM    239  C   SER A  25       5.593  -5.061  28.246  1.00 19.51           C  
ANISOU  239  C   SER A  25     2350   2778   2286    505    -14    -61       C  
ATOM    240  O   SER A  25       5.030  -3.997  28.021  1.00 18.30           O  
ANISOU  240  O   SER A  25     2201   2582   2169    408    -24   -103       O  
ATOM    241  CB  SER A  25       4.817  -6.855  29.750  1.00 20.53           C  
ANISOU  241  CB  SER A  25     2575   2837   2390    626     15      3       C  
ATOM    242  OG  SER A  25       3.516  -6.558  29.270  1.00 20.51           O  
ANISOU  242  OG  SER A  25     2633   2707   2452    555     26    -34       O  
ATOM    243  N   GLN A  26       6.129  -5.803  27.288  1.00 18.16           N  
ANISOU  243  N   GLN A  26     2179   2610   2112    577      5    -39       N  
ATOM    244  CA  GLN A  26       6.121  -5.331  25.905  1.00 25.64           C  
ANISOU  244  CA  GLN A  26     3122   3526   3094    532     10    -65       C  
ATOM    245  C   GLN A  26       4.692  -5.236  25.402  1.00 22.37           C  
ANISOU  245  C   GLN A  26     2790   2966   2744    480     21    -92       C  
ATOM    246  O   GLN A  26       4.318  -4.277  24.725  1.00 20.50           O  
ANISOU  246  O   GLN A  26     2547   2701   2540    399     10   -119       O  
ATOM    247  CB  GLN A  26       6.946  -6.250  25.013  1.00 31.76           C  
ANISOU  247  CB  GLN A  26     3887   4335   3846    629     36    -41       C  
ATOM    248  CG  GLN A  26       7.206  -5.669  23.646  1.00 44.47           C  
ANISOU  248  CG  GLN A  26     5471   5956   5471    580     39    -65       C  
ATOM    249  CD  GLN A  26       7.809  -4.267  23.699  1.00 53.54           C  
ANISOU  249  CD  GLN A  26     6535   7205   6605    476      8    -81       C  
ATOM    250  OE1 GLN A  26       8.651  -3.967  24.551  1.00 57.19           O  
ANISOU  250  OE1 GLN A  26     6922   7789   7018    472    -12    -70       O  
ATOM    251  NE2 GLN A  26       7.371  -3.401  22.789  1.00 47.37           N  
ANISOU  251  NE2 GLN A  26     5767   6372   5860    387      4   -106       N  
ATOM    252  N   MET A  83       3.886  -6.231  25.760  1.00 19.51           N  
ANISOU  252  N   MET A  83     2503   2515   2396    525     42    -78       N  
ATOM    253  CA  MET A  83       2.469  -6.205  25.439  1.00 15.94           C  
ANISOU  253  CA  MET A  83     2116   1945   1996    471     50    -99       C  
ATOM    254  C   MET A  83       1.785  -4.947  25.987  1.00 15.70           C  
ANISOU  254  C   MET A  83     2065   1911   1991    384     28   -126       C  
ATOM    255  O   MET A  83       1.021  -4.281  25.283  1.00 17.29           O  
ANISOU  255  O   MET A  83     2276   2060   2234    326     24   -148       O  
ATOM    256  CB  MET A  83       1.799  -7.460  25.995  1.00 26.17           C  
ANISOU  256  CB  MET A  83     3490   3163   3291    520     77    -77       C  
ATOM    257  CG  MET A  83       0.352  -7.618  25.596  1.00 32.77           C  
ANISOU  257  CG  MET A  83     4386   3892   4172    462     89    -97       C  
ATOM    258  SD  MET A  83       0.189  -7.759  23.806  1.00 91.62           S  
ANISOU  258  SD  MET A  83    11862  11302  11647    440     96   -122       S  
ATOM    259  CE  MET A  83      -1.585  -7.908  23.680  1.00 24.42           C  
ANISOU  259  CE  MET A  83     3403   2699   3176    362    102   -139       C  
ATOM    260  N   ALA A  84       2.050  -4.625  27.248  1.00 14.02           N  
ANISOU  260  N   ALA A  84     1825   1754   1749    381     17   -124       N  
ATOM    261  CA  ALA A  84       1.518  -3.403  27.856  1.00 12.31           C  
ANISOU  261  CA  ALA A  84     1596   1535   1548    305      3   -158       C  
ATOM    262  C   ALA A  84       1.956  -2.134  27.102  1.00 18.31           C  
ANISOU  262  C   ALA A  84     2318   2316   2324    238    -14   -184       C  
ATOM    263  O   ALA A  84       1.150  -1.220  26.875  1.00 18.21           O  
ANISOU  263  O   ALA A  84     2324   2241   2352    183    -14   -209       O  
ATOM    264  CB  ALA A  84       1.931  -3.327  29.322  1.00 11.32           C  
ANISOU  264  CB  ALA A  84     1446   1485   1372    311     -7   -155       C  
ATOM    265  N   ALA A  85       3.226  -2.094  26.711  1.00 16.18           N  
ANISOU  265  N   ALA A  85     1996   2135   2018    246    -24   -174       N  
ATOM    266  CA  ALA A  85       3.765  -0.987  25.927  1.00 17.25           C  
ANISOU  266  CA  ALA A  85     2098   2297   2161    176    -36   -191       C  
ATOM    267  C   ALA A  85       3.023  -0.817  24.602  1.00 15.77           C  
ANISOU  267  C   ALA A  85     1946   2021   2025    161    -27   -190       C  
ATOM    268  O   ALA A  85       2.736   0.307  24.196  1.00 14.57           O  
ANISOU  268  O   ALA A  85     1802   1832   1901     94    -33   -206       O  
ATOM    269  CB  ALA A  85       5.253  -1.198  25.671  1.00 15.76           C  
ANISOU  269  CB  ALA A  85     1836   2236   1917    196    -44   -172       C  
ATOM    270  N   VAL A  86       2.707  -1.931  23.935  1.00 12.21           N  
ANISOU  270  N   VAL A  86     1523   1534   1581    222    -12   -172       N  
ATOM    271  CA  VAL A  86       1.989  -1.872  22.660  1.00 13.08           C  
ANISOU  271  CA  VAL A  86     1663   1577   1727    204     -6   -172       C  
ATOM    272  C   VAL A  86       0.578  -1.342  22.865  1.00 13.40           C  
ANISOU  272  C   VAL A  86     1743   1534   1817    169     -9   -183       C  
ATOM    273  O   VAL A  86       0.109  -0.484  22.103  1.00 15.43           O  
ANISOU  273  O   VAL A  86     2004   1757   2103    127    -15   -184       O  
ATOM    274  CB  VAL A  86       1.917  -3.256  21.970  1.00 15.39           C  
ANISOU  274  CB  VAL A  86     1989   1847   2010    268     14   -160       C  
ATOM    275  CG1 VAL A  86       1.078  -3.181  20.699  1.00 16.83           C  
ANISOU  275  CG1 VAL A  86     2201   1972   2220    237     15   -165       C  
ATOM    276  CG2 VAL A  86       3.312  -3.784  21.669  1.00 14.69           C  
ANISOU  276  CG2 VAL A  86     1861   1846   1874    323     23   -146       C  
ATOM    277  N   LYS A  87      -0.106  -1.860  23.887  1.00 16.12           N  
ANISOU  277  N   LYS A  87     2111   1849   2164    192      0   -187       N  
ATOM    278  CA  LYS A  87      -1.467  -1.428  24.169  1.00 18.45           C  
ANISOU  278  CA  LYS A  87     2431   2081   2499    167      3   -197       C  
ATOM    279  C   LYS A  87      -1.477   0.056  24.416  1.00 14.62           C  
ANISOU  279  C   LYS A  87     1933   1590   2032    121     -6   -215       C  
ATOM    280  O   LYS A  87      -2.355   0.771  23.932  1.00 14.96           O  
ANISOU  280  O   LYS A  87     1987   1583   2113    103     -6   -215       O  
ATOM    281  CB  LYS A  87      -2.030  -2.125  25.413  1.00 17.56           C  
ANISOU  281  CB  LYS A  87     2338   1958   2376    192     16   -197       C  
ATOM    282  CG  LYS A  87      -2.380  -3.584  25.222  1.00 20.59           C  
ANISOU  282  CG  LYS A  87     2760   2314   2751    227     33   -179       C  
ATOM    283  CD  LYS A  87      -2.824  -4.181  26.560  1.00 21.77           C  
ANISOU  283  CD  LYS A  87     2931   2459   2884    245     48   -172       C  
ATOM    284  CE  LYS A  87      -3.061  -5.676  26.459  1.00 28.27           C  
ANISOU  284  CE  LYS A  87     3806   3240   3694    276     70   -149       C  
ATOM    285  NZ  LYS A  87      -3.436  -6.244  27.789  1.00 26.78           N  
ANISOU  285  NZ  LYS A  87     3642   3049   3484    290     87   -133       N  
ATOM    286  N   GLN A  88      -0.508   0.522  25.193  1.00 13.80           N  
ANISOU  286  N   GLN A  88     1807   1538   1897    103    -12   -230       N  
ATOM    287  CA  GLN A  88      -0.465   1.939  25.542  1.00 16.84           C  
ANISOU  287  CA  GLN A  88     2198   1907   2295     48    -15   -257       C  
ATOM    288  C   GLN A  88      -0.169   2.796  24.316  1.00 13.43           C  
ANISOU  288  C   GLN A  88     1765   1454   1884      7    -21   -245       C  
ATOM    289  O   GLN A  88      -0.773   3.848  24.131  1.00 14.98           O  
ANISOU  289  O   GLN A  88     1991   1584   2117    -19    -16   -252       O  
ATOM    290  CB  GLN A  88       0.550   2.206  26.656  1.00 22.58           C  
ANISOU  290  CB  GLN A  88     2900   2706   2971     20    -22   -281       C  
ATOM    291  CG  GLN A  88       0.624   3.674  27.111  1.00 29.76           C  
ANISOU  291  CG  GLN A  88     3830   3589   3888    -53    -20   -322       C  
ATOM    292  CD  GLN A  88      -0.667   4.179  27.766  1.00 34.61           C  
ANISOU  292  CD  GLN A  88     4492   4120   4538    -41      1   -347       C  
ATOM    293  OE1 GLN A  88      -1.487   3.398  28.255  1.00 36.82           O  
ANISOU  293  OE1 GLN A  88     4775   4393   4821     10     11   -340       O  
ATOM    294  NE2 GLN A  88      -0.844   5.501  27.776  1.00 35.51           N  
ANISOU  294  NE2 GLN A  88     4646   4171   4676    -88     13   -377       N  
ATOM    295  N   ALA A  89       0.761   2.347  23.483  1.00 15.67           N  
ANISOU  295  N   ALA A  89     2018   1794   2142      8    -29   -225       N  
ATOM    296  CA  ALA A  89       1.101   3.102  22.277  1.00 14.14           C  
ANISOU  296  CA  ALA A  89     1821   1592   1958    -34    -33   -208       C  
ATOM    297  C   ALA A  89      -0.112   3.188  21.369  1.00 16.85           C  
ANISOU  297  C   ALA A  89     2196   1861   2345    -15    -31   -186       C  
ATOM    298  O   ALA A  89      -0.381   4.223  20.775  1.00 15.34           O  
ANISOU  298  O   ALA A  89     2025   1623   2179    -48    -32   -172       O  
ATOM    299  CB  ALA A  89       2.267   2.458  21.547  1.00 16.60           C  
ANISOU  299  CB  ALA A  89     2087   1991   2227    -26    -37   -190       C  
ATOM    300  N   LEU A  90      -0.866   2.097  21.273  1.00 16.50           N  
ANISOU  300  N   LEU A  90     2157   1807   2306     36    -28   -180       N  
ATOM    301  CA  LEU A  90      -2.018   2.099  20.386  1.00 14.42           C  
ANISOU  301  CA  LEU A  90     1909   1498   2072     46    -31   -159       C  
ATOM    302  C   LEU A  90      -3.114   3.025  20.901  1.00 14.04           C  
ANISOU  302  C   LEU A  90     1881   1388   2065     48    -26   -162       C  
ATOM    303  O   LEU A  90      -3.701   3.783  20.127  1.00 14.54           O  
ANISOU  303  O   LEU A  90     1952   1417   2154     44    -31   -136       O  
ATOM    304  CB  LEU A  90      -2.528   0.674  20.161  1.00 11.50           C  
ANISOU  304  CB  LEU A  90     1543   1136   1690     82    -27   -158       C  
ATOM    305  CG  LEU A  90      -3.548   0.447  19.058  1.00 21.02           C  
ANISOU  305  CG  LEU A  90     2754   2326   2907     79    -35   -140       C  
ATOM    306  CD1 LEU A  90      -3.077   1.060  17.742  1.00 21.86           C  
ANISOU  306  CD1 LEU A  90     2851   2451   3003     55    -46   -115       C  
ATOM    307  CD2 LEU A  90      -3.747  -1.051  18.900  1.00 17.85           C  
ANISOU  307  CD2 LEU A  90     2369   1931   2482     96    -26   -151       C  
ATOM    308  N   ARG A  91      -3.379   2.979  22.207  1.00 10.44           N  
ANISOU  308  N   ARG A  91     1431    922   1612     60    -15   -190       N  
ATOM    309  CA  ARG A  91      -4.327   3.903  22.818  1.00 12.49           C  
ANISOU  309  CA  ARG A  91     1712   1128   1907     70     -2   -200       C  
ATOM    310  C   ARG A  91      -3.960   5.353  22.551  1.00 14.86           C  
ANISOU  310  C   ARG A  91     2040   1381   2226     38      1   -199       C  
ATOM    311  O   ARG A  91      -4.818   6.161  22.183  1.00 12.54           O  
ANISOU  311  O   ARG A  91     1767   1030   1968     59      9   -180       O  
ATOM    312  CB  ARG A  91      -4.402   3.695  24.334  1.00 16.13           C  
ANISOU  312  CB  ARG A  91     2178   1597   2354     78     13   -238       C  
ATOM    313  CG  ARG A  91      -5.090   2.404  24.757  1.00 17.24           C  
ANISOU  313  CG  ARG A  91     2305   1763   2484    110     18   -233       C  
ATOM    314  CD  ARG A  91      -5.214   2.351  26.281  1.00 17.89           C  
ANISOU  314  CD  ARG A  91     2394   1856   2548    117     36   -265       C  
ATOM    315  NE  ARG A  91      -5.911   1.154  26.745  1.00 17.97           N  
ANISOU  315  NE  ARG A  91     2398   1884   2545    139     46   -255       N  
ATOM    316  CZ  ARG A  91      -6.528   1.071  27.922  1.00 23.27           C  
ANISOU  316  CZ  ARG A  91     3072   2562   3206    150     67   -272       C  
ATOM    317  NH1 ARG A  91      -6.533   2.118  28.738  1.00 17.02           N  
ANISOU  317  NH1 ARG A  91     2292   1760   2416    146     80   -307       N  
ATOM    318  NH2 ARG A  91      -7.153  -0.050  28.278  1.00 21.53           N  
ANISOU  318  NH2 ARG A  91     2851   2358   2974    159     78   -256       N  
ATOM    319  N   GLU A  92      -2.690   5.693  22.760  1.00 11.63           N  
ANISOU  319  N   GLU A  92     1633    996   1789    -13     -2   -217       N  
ATOM    320  CA  GLU A  92      -2.274   7.081  22.590  1.00 16.13           C  
ANISOU  320  CA  GLU A  92     2243   1512   2372    -64      6   -221       C  
ATOM    321  C   GLU A  92      -2.357   7.506  21.127  1.00 11.41           C  
ANISOU  321  C   GLU A  92     1652    890   1791    -69     -2   -167       C  
ATOM    322  O   GLU A  92      -2.804   8.612  20.819  1.00 18.10           O  
ANISOU  322  O   GLU A  92     2546   1658   2672    -70     10   -149       O  
ATOM    323  CB  GLU A  92      -0.861   7.283  23.127  1.00 20.77           C  
ANISOU  323  CB  GLU A  92     2820   2154   2917   -136      2   -252       C  
ATOM    324  CG  GLU A  92      -0.754   7.010  24.620  1.00 26.29           C  
ANISOU  324  CG  GLU A  92     3515   2884   3589   -136      7   -303       C  
ATOM    325  CD  GLU A  92       0.662   7.169  25.152  1.00 36.39           C  
ANISOU  325  CD  GLU A  92     4768   4244   4814   -210     -3   -331       C  
ATOM    326  OE1 GLU A  92       1.558   7.572  24.377  1.00 39.06           O  
ANISOU  326  OE1 GLU A  92     5092   4609   5138   -269    -11   -315       O  
ATOM    327  OE2 GLU A  92       0.874   6.896  26.351  1.00 41.72           O  
ANISOU  327  OE2 GLU A  92     5430   4967   5453   -214     -4   -368       O  
ATOM    328  N   ALA A  93      -1.938   6.613  20.233  1.00 13.29           N  
ANISOU  328  N   ALA A  93     1849   1196   2004    -67    -19   -142       N  
ATOM    329  CA  ALA A  93      -1.976   6.901  18.801  1.00 14.68           C  
ANISOU  329  CA  ALA A  93     2027   1370   2183    -75    -28    -91       C  
ATOM    330  C   ALA A  93      -3.405   7.102  18.316  1.00 14.96           C  
ANISOU  330  C   ALA A  93     2073   1357   2254    -19    -30    -55       C  
ATOM    331  O   ALA A  93      -3.681   8.027  17.549  1.00 13.20           O  
ANISOU  331  O   ALA A  93     1878   1088   2048    -21    -30    -11       O  
ATOM    332  CB  ALA A  93      -1.302   5.795  18.028  1.00 15.71           C  
ANISOU  332  CB  ALA A  93     2111   1586   2270    -77    -41    -81       C  
ATOM    333  N   GLY A  94      -4.310   6.220  18.742  1.00 12.24           N  
ANISOU  333  N   GLY A  94     1705   1031   1914     29    -33    -69       N  
ATOM    334  CA  GLY A  94      -5.731   6.414  18.478  1.00 15.05           C  
ANISOU  334  CA  GLY A  94     2057   1363   2300     81    -34    -40       C  
ATOM    335  C   GLY A  94      -6.255   7.745  18.994  1.00 17.20           C  
ANISOU  335  C   GLY A  94     2372   1551   2614    109    -13    -34       C  
ATOM    336  O   GLY A  94      -6.983   8.454  18.291  1.00 16.95           O  
ANISOU  336  O   GLY A  94     2350   1488   2604    146    -14     16       O  
ATOM    337  N   ASP A  95      -5.887   8.103  20.223  1.00 16.94           N  
ANISOU  337  N   ASP A  95     2368   1481   2586     95      9    -86       N  
ATOM    338  CA  ASP A  95      -6.310   9.388  20.782  1.00 12.37           C  
ANISOU  338  CA  ASP A  95     1847    808   2044    119     38    -94       C  
ATOM    339  C   ASP A  95      -5.789  10.543  19.918  1.00 13.95           C  
ANISOU  339  C   ASP A  95     2103    941   2256     88     42    -54       C  
ATOM    340  O   ASP A  95      -6.515  11.498  19.592  1.00 16.05           O  
ANISOU  340  O   ASP A  95     2410   1130   2557    139     58    -15       O  
ATOM    341  CB  ASP A  95      -5.763   9.559  22.205  1.00 16.26           C  
ANISOU  341  CB  ASP A  95     2370   1283   2526     85     60   -166       C  
ATOM    342  CG  ASP A  95      -6.625   8.888  23.271  1.00 23.56           C  
ANISOU  342  CG  ASP A  95     3264   2237   3450    135     72   -200       C  
ATOM    343  OD1 ASP A  95      -7.787   8.512  22.989  1.00 23.21           O  
ANISOU  343  OD1 ASP A  95     3184   2213   3423    198     71   -170       O  
ATOM    344  OD2 ASP A  95      -6.127   8.746  24.414  1.00 22.67           O  
ANISOU  344  OD2 ASP A  95     3162   2139   3314    104     83   -256       O  
ATOM    345  N   GLU A  96      -4.521  10.443  19.540  1.00 14.84           N  
ANISOU  345  N   GLU A  96     2215   1087   2338      6     30    -58       N  
ATOM    346  CA  GLU A  96      -3.848  11.527  18.838  1.00 15.80           C  
ANISOU  346  CA  GLU A  96     2392   1148   2462    -49     37    -25       C  
ATOM    347  C   GLU A  96      -4.441  11.696  17.453  1.00 17.84           C  
ANISOU  347  C   GLU A  96     2644   1406   2729     -7     23     59       C  
ATOM    348  O   GLU A  96      -4.688  12.813  17.000  1.00 20.97           O  
ANISOU  348  O   GLU A  96     3104   1713   3151      6     39    105       O  
ATOM    349  CB  GLU A  96      -2.349  11.233  18.718  1.00 15.42           C  
ANISOU  349  CB  GLU A  96     2321   1169   2368   -148     26    -46       C  
ATOM    350  CG  GLU A  96      -1.544  12.469  18.353  1.00 18.43           C  
ANISOU  350  CG  GLU A  96     2770   1484   2749   -234     43    -30       C  
ATOM    351  CD  GLU A  96      -0.043  12.230  18.389  1.00 22.08           C  
ANISOU  351  CD  GLU A  96     3196   2034   3160   -340     34    -56       C  
ATOM    352  OE1 GLU A  96       0.380  11.057  18.384  1.00 27.34           O  
ANISOU  352  OE1 GLU A  96     3781   2816   3790   -329     14    -70       O  
ATOM    353  OE2 GLU A  96       0.709  13.225  18.430  1.00 21.90           O  
ANISOU  353  OE2 GLU A  96     3227   1965   3130   -435     51    -63       O  
ATOM    354  N   PHE A  97      -4.649  10.558  16.799  1.00 14.91           N  
ANISOU  354  N   PHE A  97     2200   1135   2331     12     -6     76       N  
ATOM    355  CA  PHE A  97      -5.272  10.459  15.483  1.00 13.63           C  
ANISOU  355  CA  PHE A  97     2012   1006   2160     48    -28    149       C  
ATOM    356  C   PHE A  97      -6.628  11.147  15.538  1.00 18.74           C  
ANISOU  356  C   PHE A  97     2678   1594   2849    140    -18    190       C  
ATOM    357  O   PHE A  97      -6.911  12.045  14.752  1.00 15.95           O  
ANISOU  357  O   PHE A  97     2360   1194   2507    166    -16    260       O  
ATOM    358  CB  PHE A  97      -5.409   8.962  15.113  1.00 15.21           C  
ANISOU  358  CB  PHE A  97     2137   1318   2323     52    -54    134       C  
ATOM    359  CG  PHE A  97      -6.095   8.690  13.798  1.00 15.23           C  
ANISOU  359  CG  PHE A  97     2105   1378   2303     78    -81    196       C  
ATOM    360  CD1 PHE A  97      -5.481   9.003  12.595  1.00 12.97           C  
ANISOU  360  CD1 PHE A  97     1827   1116   1984     39    -91    245       C  
ATOM    361  CD2 PHE A  97      -7.343   8.073  13.767  1.00 17.59           C  
ANISOU  361  CD2 PHE A  97     2359   1722   2604    131    -96    202       C  
ATOM    362  CE1 PHE A  97      -6.120   8.742  11.374  1.00 15.28           C  
ANISOU  362  CE1 PHE A  97     2086   1474   2245     59   -117    301       C  
ATOM    363  CE2 PHE A  97      -7.988   7.805  12.558  1.00 18.61           C  
ANISOU  363  CE2 PHE A  97     2449   1921   2702    144   -124    256       C  
ATOM    364  CZ  PHE A  97      -7.373   8.133  11.359  1.00 18.60           C  
ANISOU  364  CZ  PHE A  97     2459   1943   2665    110   -136    304       C  
ATOM    365  N   GLU A  98      -7.457  10.744  16.495  1.00 17.69           N  
ANISOU  365  N   GLU A  98     2519   1468   2735    193    -10    150       N  
ATOM    366  CA  GLU A  98      -8.802  11.291  16.623  1.00 21.00           C  
ANISOU  366  CA  GLU A  98     2937   1854   3189    292      2    185       C  
ATOM    367  C   GLU A  98      -8.809  12.770  17.022  1.00 20.54           C  
ANISOU  367  C   GLU A  98     2974   1658   3173    325     42    196       C  
ATOM    368  O   GLU A  98      -9.755  13.496  16.724  1.00 25.98           O  
ANISOU  368  O   GLU A  98     3677   2306   3889    417     54    253       O  
ATOM    369  CB  GLU A  98      -9.608  10.456  17.622  1.00 20.60           C  
ANISOU  369  CB  GLU A  98     2832   1853   3142    329      7    134       C  
ATOM    370  CG  GLU A  98      -9.915   9.043  17.116  1.00 16.04           C  
ANISOU  370  CG  GLU A  98     2171   1397   2526    307    -28    135       C  
ATOM    371  CD  GLU A  98     -10.224   8.060  18.236  1.00 26.20           C  
ANISOU  371  CD  GLU A  98     3423   2723   3807    302    -19     72       C  
ATOM    372  OE1 GLU A  98     -10.717   8.497  19.301  1.00 24.35           O  
ANISOU  372  OE1 GLU A  98     3204   2448   3600    345     12     44       O  
ATOM    373  OE2 GLU A  98      -9.954   6.846  18.057  1.00 24.09           O  
ANISOU  373  OE2 GLU A  98     3122   2523   3506    255    -38     51       O  
ATOM    374  N   LEU A  99      -7.747  13.222  17.681  1.00 23.12           N  
ANISOU  374  N   LEU A  99     3368   1916   3502    249     65    141       N  
ATOM    375  CA  LEU A  99      -7.657  14.616  18.107  1.00 22.39           C  
ANISOU  375  CA  LEU A  99     3385   1677   3445    259    109    137       C  
ATOM    376  C   LEU A  99      -7.224  15.538  16.966  1.00 23.32           C  
ANISOU  376  C   LEU A  99     3568   1728   3565    234    110    216       C  
ATOM    377  O   LEU A  99      -7.876  16.548  16.680  1.00 22.83           O  
ANISOU  377  O   LEU A  99     3572   1566   3537    312    135    273       O  
ATOM    378  CB  LEU A  99      -6.693  14.757  19.284  1.00 18.24           C  
ANISOU  378  CB  LEU A  99     2907   1112   2910    170    132     42       C  
ATOM    379  CG  LEU A  99      -6.408  16.196  19.696  1.00 34.22           C  
ANISOU  379  CG  LEU A  99     5063   2977   4963    147    180     24       C  
ATOM    380  CD1 LEU A  99      -7.691  16.869  20.167  1.00 36.70           C  
ANISOU  380  CD1 LEU A  99     5415   3212   5318    277    215     30       C  
ATOM    381  CD2 LEU A  99      -5.339  16.234  20.765  1.00 36.67           C  
ANISOU  381  CD2 LEU A  99     5405   3281   5246     32    193    -73       C  
ATOM    382  N   ARG A 100      -6.119  15.187  16.320  1.00 16.54           N  
ANISOU  382  N   ARG A 100     2691    926   2668    129     86    223       N  
ATOM    383  CA  ARG A 100      -5.584  15.973  15.220  1.00 17.26           C  
ANISOU  383  CA  ARG A 100     2838    971   2751     85     87    298       C  
ATOM    384  C   ARG A 100      -6.583  16.106  14.079  1.00 17.68           C  
ANISOU  384  C   ARG A 100     2866   1044   2806    183     68    404       C  
ATOM    385  O   ARG A 100      -6.757  17.194  13.515  1.00 18.76           O  
ANISOU  385  O   ARG A 100     3085   1081   2963    214     89    480       O  
ATOM    386  CB  ARG A 100      -4.289  15.343  14.694  1.00 20.20           C  
ANISOU  386  CB  ARG A 100     3164   1440   3069    -36     63    285       C  
ATOM    387  CG  ARG A 100      -3.788  15.944  13.385  1.00 25.21           C  
ANISOU  387  CG  ARG A 100     3833   2064   3682    -84     59    373       C  
ATOM    388  CD  ARG A 100      -3.414  17.418  13.533  1.00 18.62           C  
ANISOU  388  CD  ARG A 100     3132   1067   2875   -131    103    394       C  
ATOM    389  NE  ARG A 100      -2.957  18.003  12.275  1.00 21.79           N  
ANISOU  389  NE  ARG A 100     3571   1455   3253   -181    103    487       N  
ATOM    390  CZ  ARG A 100      -3.758  18.540  11.354  1.00 25.56           C  
ANISOU  390  CZ  ARG A 100     4082   1890   3741    -95    101    594       C  
ATOM    391  NH1 ARG A 100      -5.075  18.562  11.538  1.00 21.99           N  
ANISOU  391  NH1 ARG A 100     3619   1411   3324     49     98    619       N  
ATOM    392  NH2 ARG A 100      -3.246  19.059  10.240  1.00 20.80           N  
ANISOU  392  NH2 ARG A 100     3516   1280   3108   -152    102    680       N  
ATOM    393  N   TYR A 101      -7.227  14.999  13.729  1.00 19.62           N  
ANISOU  393  N   TYR A 101     3004   1422   3028    229     30    412       N  
ATOM    394  CA  TYR A 101      -8.103  14.983  12.556  1.00 24.94           C  
ANISOU  394  CA  TYR A 101     3634   2155   3686    305      2    510       C  
ATOM    395  C   TYR A 101      -9.567  14.925  12.976  1.00 29.09           C  
ANISOU  395  C   TYR A 101     4116   2697   4240    434      3    523       C  
ATOM    396  O   TYR A 101     -10.391  14.259  12.338  1.00 25.25           O  
ANISOU  396  O   TYR A 101     3538   2329   3726    481    -34    564       O  
ATOM    397  CB  TYR A 101      -7.729  13.823  11.622  1.00 17.69           C  
ANISOU  397  CB  TYR A 101     2629   1387   2706    245    -43    516       C  
ATOM    398  CG  TYR A 101      -6.249  13.828  11.280  1.00 16.36           C  
ANISOU  398  CG  TYR A 101     2489   1220   2505    124    -39    497       C  
ATOM    399  CD1 TYR A 101      -5.736  14.742  10.371  1.00 17.20           C  
ANISOU  399  CD1 TYR A 101     2656   1280   2598     87    -31    574       C  
ATOM    400  CD2 TYR A 101      -5.367  12.949  11.896  1.00 22.95           C  
ANISOU  400  CD2 TYR A 101     3290   2109   3321     50    -40    408       C  
ATOM    401  CE1 TYR A 101      -4.387  14.778  10.066  1.00 21.24           C  
ANISOU  401  CE1 TYR A 101     3186   1807   3076    -30    -23    559       C  
ATOM    402  CE2 TYR A 101      -4.006  12.969  11.598  1.00 21.14           C  
ANISOU  402  CE2 TYR A 101     3074   1901   3059    -55    -34    395       C  
ATOM    403  CZ  TYR A 101      -3.525  13.893  10.680  1.00 20.59           C  
ANISOU  403  CZ  TYR A 101     3057   1793   2975    -99    -25    468       C  
ATOM    404  OH  TYR A 101      -2.181  13.938  10.370  1.00 21.35           O  
ANISOU  404  OH  TYR A 101     3156   1924   3032   -209    -17    457       O  
ATOM    405  N   ARG A 102      -9.878  15.650  14.050  1.00 24.14           N  
ANISOU  405  N   ARG A 102     3553   1956   3663    487     48    486       N  
ATOM    406  CA  ARG A 102     -11.212  15.629  14.656  1.00 29.14           C  
ANISOU  406  CA  ARG A 102     4143   2606   4324    612     60    486       C  
ATOM    407  C   ARG A 102     -12.346  15.936  13.669  1.00 31.56           C  
ANISOU  407  C   ARG A 102     4401   2965   4625    730     40    600       C  
ATOM    408  O   ARG A 102     -13.350  15.226  13.631  1.00 34.76           O  
ANISOU  408  O   ARG A 102     4697   3495   5014    788     15    610       O  
ATOM    409  CB  ARG A 102     -11.270  16.586  15.854  1.00 32.67           C  
ANISOU  409  CB  ARG A 102     4691   2901   4823    654    122    433       C  
ATOM    410  CG  ARG A 102     -12.580  16.535  16.634  1.00 37.78           C  
ANISOU  410  CG  ARG A 102     5289   3572   5495    783    144    418       C  
ATOM    411  CD  ARG A 102     -12.825  15.163  17.254  1.00 44.37           C  
ANISOU  411  CD  ARG A 102     6011   4545   6302    745    119    348       C  
ATOM    412  NE  ARG A 102     -11.880  14.873  18.328  1.00 53.08           N  
ANISOU  412  NE  ARG A 102     7156   5608   7402    646    138    242       N  
ATOM    413  CZ  ARG A 102     -11.829  13.721  18.992  1.00 56.07           C  
ANISOU  413  CZ  ARG A 102     7465   6084   7758    597    122    176       C  
ATOM    414  NH1 ARG A 102     -12.672  12.740  18.694  1.00 55.84           N  
ANISOU  414  NH1 ARG A 102     7325   6185   7707    626     91    198       N  
ATOM    415  NH2 ARG A 102     -10.932  13.551  19.956  1.00 57.82           N  
ANISOU  415  NH2 ARG A 102     7726   6272   7971    516    138     90       N  
ATOM    416  N   ARG A 103     -12.179  16.984  12.870  1.00 28.97           N  
ANISOU  416  N   ARG A 103     4152   2550   4304    760     50    690       N  
ATOM    417  CA  ARG A 103     -13.197  17.366  11.896  1.00 29.91           C  
ANISOU  417  CA  ARG A 103     4230   2722   4413    881     30    813       C  
ATOM    418  C   ARG A 103     -13.487  16.221  10.924  1.00 29.72           C  
ANISOU  418  C   ARG A 103     4072   2899   4322    842    -38    843       C  
ATOM    419  O   ARG A 103     -14.637  15.808  10.758  1.00 26.01           O  
ANISOU  419  O   ARG A 103     3496   2552   3835    925    -64    877       O  
ATOM    420  CB  ARG A 103     -12.761  18.611  11.127  1.00 36.21           C  
ANISOU  420  CB  ARG A 103     5140   3410   5209    878     41    889       C  
ATOM    421  CG  ARG A 103     -13.737  19.046  10.047  1.00 47.04           C  
ANISOU  421  CG  ARG A 103     6464   4858   6549    983      8   1007       C  
ATOM    422  CD  ARG A 103     -15.111  19.292  10.640  1.00 59.31           C  
ANISOU  422  CD  ARG A 103     7960   6452   8123   1118     16    995       C  
ATOM    423  NE  ARG A 103     -16.082  19.697   9.628  1.00 73.13           N  
ANISOU  423  NE  ARG A 103     9654   8291   9840   1221    -15   1107       N  
ATOM    424  CZ  ARG A 103     -17.364  19.938   9.885  1.00 82.02           C  
ANISOU  424  CZ  ARG A 103    10711   9481  10971   1346    -12   1122       C  
ATOM    425  NH1 ARG A 103     -17.827  19.811  11.121  1.00 84.98           N  
ANISOU  425  NH1 ARG A 103    11067   9838  11383   1382     22   1034       N  
ATOM    426  NH2 ARG A 103     -18.183  20.305   8.907  1.00 84.87           N  
ANISOU  426  NH2 ARG A 103    11018   9932  11296   1432    -42   1227       N  
ATOM    427  N   ALA A 104     -12.432  15.708  10.300  1.00 24.95           N  
ANISOU  427  N   ALA A 104     3473   2332   3676    712    -63    825       N  
ATOM    428  CA  ALA A 104     -12.546  14.634   9.318  1.00 29.91           C  
ANISOU  428  CA  ALA A 104     3996   3135   4234    660   -121    842       C  
ATOM    429  C   ALA A 104     -13.085  13.339   9.926  1.00 25.98           C  
ANISOU  429  C   ALA A 104     3395   2754   3723    639   -141    757       C  
ATOM    430  O   ALA A 104     -13.899  12.649   9.313  1.00 24.10           O  
ANISOU  430  O   ALA A 104     3057   2662   3439    654   -183    786       O  
ATOM    431  CB  ALA A 104     -11.195  14.377   8.658  1.00 27.50           C  
ANISOU  431  CB  ALA A 104     3728   2831   3889    528   -131    827       C  
ATOM    432  N   PHE A 105     -12.618  13.010  11.125  1.00 20.08           N  
ANISOU  432  N   PHE A 105     2675   1944   3010    597   -111    655       N  
ATOM    433  CA  PHE A 105     -13.035  11.777  11.785  1.00 29.32           C  
ANISOU  433  CA  PHE A 105     3765   3207   4168    569   -123    575       C  
ATOM    434  C   PHE A 105     -14.511  11.822  12.173  1.00 34.05           C  
ANISOU  434  C   PHE A 105     4289   3866   4782    677   -122    600       C  
ATOM    435  O   PHE A 105     -15.229  10.833  11.998  1.00 24.71           O  
ANISOU  435  O   PHE A 105     3007   2819   3562    659   -153    589       O  
ATOM    436  CB  PHE A 105     -12.165  11.461  13.006  1.00 28.22           C  
ANISOU  436  CB  PHE A 105     3675   2992   4056    505    -90    469       C  
ATOM    437  CG  PHE A 105     -12.362  10.063  13.543  1.00 27.39           C  
ANISOU  437  CG  PHE A 105     3500   2978   3928    457   -104    395       C  
ATOM    438  CD1 PHE A 105     -11.849   8.969  12.865  1.00 25.90           C  
ANISOU  438  CD1 PHE A 105     3279   2873   3688    372   -135    373       C  
ATOM    439  CD2 PHE A 105     -13.066   9.848  14.716  1.00 28.72           C  
ANISOU  439  CD2 PHE A 105     3643   3144   4124    498    -80    347       C  
ATOM    440  CE1 PHE A 105     -12.035   7.679  13.349  1.00 27.86           C  
ANISOU  440  CE1 PHE A 105     3481   3187   3917    329   -141    308       C  
ATOM    441  CE2 PHE A 105     -13.248   8.560  15.213  1.00 27.76           C  
ANISOU  441  CE2 PHE A 105     3468   3099   3980    448    -89    286       C  
ATOM    442  CZ  PHE A 105     -12.737   7.480  14.525  1.00 27.34           C  
ANISOU  442  CZ  PHE A 105     3393   3114   3880    364   -119    268       C  
ATOM    443  N   SER A 106     -14.956  12.962  12.698  1.00 29.17           N  
ANISOU  443  N   SER A 106     3720   3149   4215    785    -82    633       N  
ATOM    444  CA  SER A 106     -16.369  13.151  13.025  1.00 31.78           C  
ANISOU  444  CA  SER A 106     3975   3542   4559    909    -74    668       C  
ATOM    445  C   SER A 106     -17.209  13.055  11.763  1.00 34.65           C  
ANISOU  445  C   SER A 106     4243   4050   4872    955   -125    771       C  
ATOM    446  O   SER A 106     -18.262  12.413  11.751  1.00 36.78           O  
ANISOU  446  O   SER A 106     4393   4468   5113    981   -149    779       O  
ATOM    447  CB  SER A 106     -16.597  14.507  13.687  1.00 36.35           C  
ANISOU  447  CB  SER A 106     4642   3970   5199   1031    -15    690       C  
ATOM    448  OG  SER A 106     -15.892  14.589  14.909  1.00 41.11           O  
ANISOU  448  OG  SER A 106     5327   4455   5839    982     30    587       O  
ATOM    449  N   ASP A 107     -16.734  13.705  10.703  1.00 28.65           N  
ANISOU  449  N   ASP A 107     3535   3254   4095    958   -141    853       N  
ATOM    450  CA  ASP A 107     -17.382  13.643   9.398  1.00 30.74           C  
ANISOU  450  CA  ASP A 107     3718   3663   4299    990   -194    957       C  
ATOM    451  C   ASP A 107     -17.650  12.201   8.968  1.00 32.69           C  
ANISOU  451  C   ASP A 107     3850   4093   4477    884   -247    912       C  
ATOM    452  O   ASP A 107     -18.796  11.820   8.732  1.00 26.34           O  
ANISOU  452  O   ASP A 107     2926   3445   3637    926   -278    946       O  
ATOM    453  CB  ASP A 107     -16.534  14.354   8.342  1.00 41.40           C  
ANISOU  453  CB  ASP A 107     5154   4945   5631    966   -203   1034       C  
ATOM    454  CG  ASP A 107     -16.680  15.866   8.399  1.00 63.39           C  
ANISOU  454  CG  ASP A 107     8037   7581   8468   1098   -160   1124       C  
ATOM    455  OD1 ASP A 107     -17.284  16.369   9.377  1.00 69.09           O  
ANISOU  455  OD1 ASP A 107     8776   8236   9238   1183   -118   1085       O  
ATOM    456  OD2 ASP A 107     -16.175  16.549   7.479  1.00 71.67           O  
ANISOU  456  OD2 ASP A 107     9154   8581   9497   1091   -166   1206       O  
ATOM    457  N   LEU A 108     -16.600  11.390   8.894  1.00 26.69           N  
ANISOU  457  N   LEU A 108     3128   3317   3697    747   -254    833       N  
ATOM    458  CA  LEU A 108     -16.765  10.027   8.388  1.00 26.19           C  
ANISOU  458  CA  LEU A 108     2982   3406   3565    642   -299    788       C  
ATOM    459  C   LEU A 108     -17.614   9.150   9.312  1.00 32.17           C  
ANISOU  459  C   LEU A 108     3660   4236   4329    631   -294    719       C  
ATOM    460  O   LEU A 108     -18.388   8.311   8.841  1.00 39.17           O  
ANISOU  460  O   LEU A 108     4447   5280   5157    588   -333    719       O  
ATOM    461  CB  LEU A 108     -15.410   9.376   8.088  1.00 27.39           C  
ANISOU  461  CB  LEU A 108     3198   3515   3693    515   -299    721       C  
ATOM    462  CG  LEU A 108     -14.468   8.943   9.211  1.00 32.74           C  
ANISOU  462  CG  LEU A 108     3943   4082   4415    455   -259    615       C  
ATOM    463  CD1 LEU A 108     -14.667   7.464   9.551  1.00 32.26           C  
ANISOU  463  CD1 LEU A 108     3830   4103   4325    374   -271    527       C  
ATOM    464  CD2 LEU A 108     -13.019   9.219   8.797  1.00 31.45           C  
ANISOU  464  CD2 LEU A 108     3867   3836   4247    392   -247    607       C  
ATOM    465  N   THR A 109     -17.487   9.353  10.619  1.00 30.50           N  
ANISOU  465  N   THR A 109     3491   3915   4183    663   -245    661       N  
ATOM    466  CA  THR A 109     -18.278   8.573  11.566  1.00 38.89           C  
ANISOU  466  CA  THR A 109     4483   5042   5251    653   -234    601       C  
ATOM    467  C   THR A 109     -19.738   8.995  11.547  1.00 38.82           C  
ANISOU  467  C   THR A 109     4367   5147   5237    763   -242    671       C  
ATOM    468  O   THR A 109     -20.617   8.216  11.912  1.00 40.36           O  
ANISOU  468  O   THR A 109     4465   5461   5408    737   -250    643       O  
ATOM    469  CB  THR A 109     -17.746   8.679  13.011  1.00 43.71           C  
ANISOU  469  CB  THR A 109     5167   5517   5923    657   -179    519       C  
ATOM    470  OG1 THR A 109     -17.752  10.048  13.429  1.00 49.47           O  
ANISOU  470  OG1 THR A 109     5958   6129   6709    772   -140    558       O  
ATOM    471  CG2 THR A 109     -16.341   8.118  13.108  1.00 42.37           C  
ANISOU  471  CG2 THR A 109     5082   5266   5751    547   -174    449       C  
ATOM    472  N   SER A 110     -20.004  10.225  11.119  1.00 33.81           N  
ANISOU  472  N   SER A 110     3747   4478   4621    889   -237    766       N  
ATOM    473  CA  SER A 110     -21.381  10.691  11.050  1.00 32.11           C  
ANISOU  473  CA  SER A 110     3422   4381   4398   1017   -243    846       C  
ATOM    474  C   SER A 110     -22.083  10.017   9.880  1.00 40.80           C  
ANISOU  474  C   SER A 110     4397   5695   5410    967   -312    899       C  
ATOM    475  O   SER A 110     -23.306  10.027   9.783  1.00 44.13           O  
ANISOU  475  O   SER A 110     4689   6275   5802   1036   -330    952       O  
ATOM    476  CB  SER A 110     -21.447  12.215  10.917  1.00 32.05           C  
ANISOU  476  CB  SER A 110     3479   4262   4435   1180   -212    940       C  
ATOM    477  OG  SER A 110     -21.140  12.640   9.598  1.00 30.99           O  
ANISOU  477  OG  SER A 110     3365   4147   4262   1184   -252   1033       O  
ATOM    478  N   GLN A 111     -21.299   9.423   8.989  1.00 45.24           N  
ANISOU  478  N   GLN A 111     4993   6271   5923    843   -350    881       N  
ATOM    479  CA  GLN A 111     -21.860   8.728   7.843  1.00 50.14           C  
ANISOU  479  CA  GLN A 111     5509   7092   6449    773   -415    916       C  
ATOM    480  C   GLN A 111     -22.199   7.286   8.204  1.00 49.14           C  
ANISOU  480  C   GLN A 111     5319   7068   6285    634   -428    817       C  
ATOM    481  O   GLN A 111     -22.762   6.550   7.394  1.00 46.52           O  
ANISOU  481  O   GLN A 111     4896   6909   5869    551   -479    825       O  
ATOM    482  CB  GLN A 111     -20.891   8.774   6.662  1.00 54.16           C  
ANISOU  482  CB  GLN A 111     6089   7576   6915    707   -445    942       C  
ATOM    483  CG  GLN A 111     -20.708  10.160   6.072  1.00 67.03           C  
ANISOU  483  CG  GLN A 111     7771   9136   8562    832   -441   1062       C  
ATOM    484  CD  GLN A 111     -21.986  10.701   5.452  1.00 82.87           C  
ANISOU  484  CD  GLN A 111     9654  11307  10524    953   -478   1186       C  
ATOM    485  OE1 GLN A 111     -22.837  11.273   6.142  1.00 88.74           O  
ANISOU  485  OE1 GLN A 111    10365  12041  11310   1067   -445   1202       O  
ATOM    486  NE2 GLN A 111     -22.129  10.521   4.142  1.00 87.00           N  
ANISOU  486  NE2 GLN A 111    10127  11974  10955    908   -536   1247       N  
ATOM    487  N   LEU A 112     -21.852   6.893   9.426  1.00 49.75           N  
ANISOU  487  N   LEU A 112     5449   7034   6419    603   -380    726       N  
ATOM    488  CA  LEU A 112     -22.136   5.546   9.915  1.00 53.51           C  
ANISOU  488  CA  LEU A 112     5886   7578   6868    475   -381    634       C  
ATOM    489  C   LEU A 112     -23.595   5.414  10.321  1.00 50.84           C  
ANISOU  489  C   LEU A 112     5404   7402   6511    512   -386    660       C  
ATOM    490  O   LEU A 112     -24.026   5.993  11.319  1.00 55.00           O  
ANISOU  490  O   LEU A 112     5915   7890   7094    617   -343    667       O  
ATOM    491  CB  LEU A 112     -21.257   5.205  11.119  1.00 55.04           C  
ANISOU  491  CB  LEU A 112     6185   7602   7124    440   -327    539       C  
ATOM    492  CG  LEU A 112     -19.762   4.999  10.897  1.00 57.76           C  
ANISOU  492  CG  LEU A 112     6658   7808   7480    374   -319    491       C  
ATOM    493  CD1 LEU A 112     -19.069   4.786  12.236  1.00 57.61           C  
ANISOU  493  CD1 LEU A 112     6721   7649   7521    363   -267    411       C  
ATOM    494  CD2 LEU A 112     -19.524   3.820   9.961  1.00 58.36           C  
ANISOU  494  CD2 LEU A 112     6730   7965   7480    236   -356    452       C  
ATOM    495  N   HIS A 113     -24.354   4.652   9.542  1.00 39.36           N  
ANISOU  495  N   HIS A 113     3843   6140   4972    420   -437    670       N  
ATOM    496  CA  HIS A 113     -25.737   4.372   9.888  1.00 36.51           C  
ANISOU  496  CA  HIS A 113     3330   5962   4579    424   -445    688       C  
ATOM    497  C   HIS A 113     -25.922   2.871   9.887  1.00 37.37           C  
ANISOU  497  C   HIS A 113     3417   6152   4629    227   -461    599       C  
ATOM    498  O   HIS A 113     -26.423   2.286   8.934  1.00 43.08           O  
ANISOU  498  O   HIS A 113     4064   7041   5265    126   -514    609       O  
ATOM    499  CB  HIS A 113     -26.675   5.061   8.907  1.00 38.73           C  
ANISOU  499  CB  HIS A 113     3479   6433   4804    515   -496    805       C  
ATOM    500  CG  HIS A 113     -26.319   6.493   8.664  1.00 46.68           C  
ANISOU  500  CG  HIS A 113     4540   7334   5861    697   -483    899       C  
ATOM    501  ND1 HIS A 113     -25.892   6.958   7.439  1.00 49.61           N  
ANISOU  501  ND1 HIS A 113     4950   7707   6193    711   -522    964       N  
ATOM    502  CD2 HIS A 113     -26.282   7.555   9.504  1.00 50.35           C  
ANISOU  502  CD2 HIS A 113     5058   7662   6412    858   -425    925       C  
ATOM    503  CE1 HIS A 113     -25.631   8.251   7.529  1.00 52.70           C  
ANISOU  503  CE1 HIS A 113     5418   7960   6644    866   -487   1028       C  
ATOM    504  NE2 HIS A 113     -25.860   8.637   8.771  1.00 54.37           N  
ANISOU  504  NE2 HIS A 113     5646   8080   6933    955   -428   1001       N  
ATOM    505  N   ILE A 114     -25.485   2.249  10.969  1.00 35.86           N  
ANISOU  505  N   ILE A 114     3304   5836   4485    169   -412    512       N  
ATOM    506  CA  ILE A 114     -25.448   0.804  11.031  1.00 36.71           C  
ANISOU  506  CA  ILE A 114     3435   5967   4547    -17   -414    423       C  
ATOM    507  C   ILE A 114     -26.741   0.215  11.581  1.00 29.64           C  
ANISOU  507  C   ILE A 114     2409   5236   3617    -81   -411    415       C  
ATOM    508  O   ILE A 114     -27.450   0.843  12.379  1.00 22.26           O  
ANISOU  508  O   ILE A 114     1394   4347   2718     29   -383    453       O  
ATOM    509  CB  ILE A 114     -24.234   0.316  11.837  1.00 45.13           C  
ANISOU  509  CB  ILE A 114     4660   6817   5672    -55   -365    339       C  
ATOM    510  CG1 ILE A 114     -24.010   1.211  13.053  1.00 51.37           C  
ANISOU  510  CG1 ILE A 114     5483   7485   6550     84   -312    350       C  
ATOM    511  CG2 ILE A 114     -22.987   0.344  10.973  1.00 50.82           C  
ANISOU  511  CG2 ILE A 114     5495   7429   6386    -73   -381    326       C  
ATOM    512  CD1 ILE A 114     -24.741   0.761  14.284  1.00 57.46           C  
ANISOU  512  CD1 ILE A 114     6206   8290   7336     63   -272    317       C  
ATOM    513  N   THR A 115     -27.062  -0.975  11.094  1.00 24.42           N  
ANISOU  513  N   THR A 115     1727   4672   2880   -263   -437    365       N  
ATOM    514  CA  THR A 115     -28.106  -1.803  11.674  1.00 22.95           C  
ANISOU  514  CA  THR A 115     1448   4617   2657   -375   -427    335       C  
ATOM    515  C   THR A 115     -27.390  -3.117  11.926  1.00 22.17           C  
ANISOU  515  C   THR A 115     1490   4382   2551   -542   -401    233       C  
ATOM    516  O   THR A 115     -26.309  -3.346  11.371  1.00 21.37           O  
ANISOU  516  O   THR A 115     1518   4149   2454   -566   -406    197       O  
ATOM    517  CB  THR A 115     -29.268  -2.041  10.696  1.00 27.16           C  
ANISOU  517  CB  THR A 115     1826   5407   3086   -459   -486    373       C  
ATOM    518  OG1 THR A 115     -28.789  -2.758   9.554  1.00 31.71           O  
ANISOU  518  OG1 THR A 115     2475   5979   3593   -596   -525    330       O  
ATOM    519  CG2 THR A 115     -29.904  -0.724  10.256  1.00 30.93           C  
ANISOU  519  CG2 THR A 115     2213   5975   3564   -272   -502    479       C  
ATOM    520  N   PRO A 116     -27.958  -3.982  12.775  1.00 23.06           N  
ANISOU  520  N   PRO A 116     1584   4522   2654   -651   -368    188       N  
ATOM    521  CA  PRO A 116     -27.235  -5.237  12.999  1.00 26.56           C  
ANISOU  521  CA  PRO A 116     2181   4818   3093   -798   -339     98       C  
ATOM    522  C   PRO A 116     -27.081  -6.019  11.694  1.00 27.75           C  
ANISOU  522  C   PRO A 116     2371   5012   3160   -946   -383     57       C  
ATOM    523  O   PRO A 116     -26.035  -6.630  11.461  1.00 21.56           O  
ANISOU  523  O   PRO A 116     1742   4066   2384   -993   -366     -3       O  
ATOM    524  CB  PRO A 116     -28.140  -5.987  13.979  1.00 24.38           C  
ANISOU  524  CB  PRO A 116     1852   4609   2802   -904   -303     74       C  
ATOM    525  CG  PRO A 116     -28.884  -4.892  14.704  1.00 29.71           C  
ANISOU  525  CG  PRO A 116     2388   5383   3516   -747   -289    145       C  
ATOM    526  CD  PRO A 116     -29.136  -3.853  13.650  1.00 23.32           C  
ANISOU  526  CD  PRO A 116     1478   4695   2686   -635   -345    218       C  
ATOM    527  N   GLY A 117     -28.097  -5.959  10.838  1.00 23.64           N  
ANISOU  527  N   GLY A 117     1707   4717   2558  -1011   -437     90       N  
ATOM    528  CA  GLY A 117     -28.076  -6.685   9.578  1.00 30.70           C  
ANISOU  528  CA  GLY A 117     2653   5650   3362  -1143   -469     49       C  
ATOM    529  C   GLY A 117     -27.126  -6.134   8.525  1.00 31.14           C  
ANISOU  529  C   GLY A 117     2751   5671   3409  -1081   -511     64       C  
ATOM    530  O   GLY A 117     -26.796  -6.829   7.559  1.00 28.41           O  
ANISOU  530  O   GLY A 117     2492   5306   2998  -1187   -523     11       O  
ATOM    531  N   THR A 118     -26.693  -4.886   8.684  1.00 23.06           N  
ANISOU  531  N   THR A 118     1710   4597   2454   -884   -512    137       N  
ATOM    532  CA  THR A 118     -25.774  -4.282   7.712  1.00 24.84           C  
ANISOU  532  CA  THR A 118     1998   4765   2677   -806   -537    162       C  
ATOM    533  C   THR A 118     -24.391  -3.944   8.273  1.00 26.48           C  
ANISOU  533  C   THR A 118     2355   4728   2978   -698   -489    143       C  
ATOM    534  O   THR A 118     -23.542  -3.409   7.554  1.00 23.07           O  
ANISOU  534  O   THR A 118     1979   4237   2548   -633   -502    165       O  
ATOM    535  CB  THR A 118     -26.347  -2.986   7.104  1.00 27.37           C  
ANISOU  535  CB  THR A 118     2180   5238   2981   -666   -586    279       C  
ATOM    536  OG1 THR A 118     -26.482  -1.994   8.129  1.00 25.64           O  
ANISOU  536  OG1 THR A 118     1925   4960   2855   -494   -552    337       O  
ATOM    537  CG2 THR A 118     -27.700  -3.251   6.450  1.00 28.99           C  
ANISOU  537  CG2 THR A 118     2258   5668   3090   -744   -621    304       C  
ATOM    538  N   ALA A 119     -24.157  -4.252   9.544  1.00 20.30           N  
ANISOU  538  N   ALA A 119     1633   3815   2265   -685   -433    106       N  
ATOM    539  CA  ALA A 119     -22.907  -3.840  10.181  1.00 21.25           C  
ANISOU  539  CA  ALA A 119     1875   3730   2471   -577   -390     95       C  
ATOM    540  C   ALA A 119     -21.680  -4.562   9.627  1.00 18.33           C  
ANISOU  540  C   ALA A 119     1649   3231   2084   -639   -379     28       C  
ATOM    541  O   ALA A 119     -20.631  -3.947   9.457  1.00 17.56           O  
ANISOU  541  O   ALA A 119     1618   3030   2025   -548   -371     43       O  
ATOM    542  CB  ALA A 119     -22.982  -3.991  11.706  1.00 18.45           C  
ANISOU  542  CB  ALA A 119     1541   3284   2183   -547   -336     74       C  
ATOM    543  N   TYR A 120     -21.796  -5.853   9.344  1.00 18.76           N  
ANISOU  543  N   TYR A 120     1756   3290   2080   -794   -373    -45       N  
ATOM    544  CA  TYR A 120     -20.635  -6.592   8.844  1.00 18.29           C  
ANISOU  544  CA  TYR A 120     1841   3105   2005   -839   -353   -113       C  
ATOM    545  C   TYR A 120     -20.202  -6.050   7.479  1.00 18.99           C  
ANISOU  545  C   TYR A 120     1919   3253   2043   -814   -394    -87       C  
ATOM    546  O   TYR A 120     -19.021  -5.754   7.254  1.00 24.49           O  
ANISOU  546  O   TYR A 120     2697   3843   2767   -744   -378    -90       O  
ATOM    547  CB  TYR A 120     -20.922  -8.095   8.748  1.00 22.16           C  
ANISOU  547  CB  TYR A 120     2402   3581   2437  -1013   -334   -200       C  
ATOM    548  CG  TYR A 120     -19.728  -8.894   8.277  1.00 28.52           C  
ANISOU  548  CG  TYR A 120     3365   4247   3226  -1043   -303   -273       C  
ATOM    549  CD1 TYR A 120     -18.563  -8.947   9.031  1.00 31.81           C  
ANISOU  549  CD1 TYR A 120     3886   4487   3713   -950   -254   -287       C  
ATOM    550  CD2 TYR A 120     -19.755  -9.579   7.070  1.00 38.22           C  
ANISOU  550  CD2 TYR A 120     4631   5527   4362  -1160   -322   -328       C  
ATOM    551  CE1 TYR A 120     -17.465  -9.670   8.604  1.00 31.73           C  
ANISOU  551  CE1 TYR A 120     4009   4360   3685   -960   -222   -348       C  
ATOM    552  CE2 TYR A 120     -18.658 -10.303   6.633  1.00 38.50           C  
ANISOU  552  CE2 TYR A 120     4813   5435   4381  -1174   -286   -397       C  
ATOM    553  CZ  TYR A 120     -17.520 -10.348   7.408  1.00 40.97           C  
ANISOU  553  CZ  TYR A 120     5221   5576   4768  -1067   -235   -404       C  
ATOM    554  OH  TYR A 120     -16.426 -11.061   6.980  1.00 52.39           O  
ANISOU  554  OH  TYR A 120     6803   6906   6196  -1064   -195   -468       O  
ATOM    555  N   GLN A 121     -21.172  -5.914   6.582  1.00 19.58           N  
ANISOU  555  N   GLN A 121     1886   3512   2040   -875   -448    -56       N  
ATOM    556  CA  GLN A 121     -20.923  -5.365   5.255  1.00 27.55           C  
ANISOU  556  CA  GLN A 121     2870   4608   2988   -856   -493    -19       C  
ATOM    557  C   GLN A 121     -20.291  -3.980   5.358  1.00 27.48           C  
ANISOU  557  C   GLN A 121     2851   4543   3049   -682   -493     66       C  
ATOM    558  O   GLN A 121     -19.300  -3.700   4.691  1.00 26.91           O  
ANISOU  558  O   GLN A 121     2844   4414   2967   -647   -492     69       O  
ATOM    559  CB  GLN A 121     -22.217  -5.308   4.444  1.00 33.53           C  
ANISOU  559  CB  GLN A 121     3488   5600   3652   -933   -556     18       C  
ATOM    560  CG  GLN A 121     -22.019  -5.046   2.958  1.00 48.47           C  
ANISOU  560  CG  GLN A 121     5364   7600   5452   -954   -604     41       C  
ATOM    561  CD  GLN A 121     -21.371  -6.217   2.227  1.00 58.28           C  
ANISOU  561  CD  GLN A 121     6731   8791   6622  -1092   -588    -69       C  
ATOM    562  OE1 GLN A 121     -20.237  -6.607   2.524  1.00 55.99           O  
ANISOU  562  OE1 GLN A 121     6577   8318   6379  -1069   -535   -126       O  
ATOM    563  NE2 GLN A 121     -22.093  -6.781   1.259  1.00 63.34           N  
ANISOU  563  NE2 GLN A 121     7325   9597   7145  -1232   -630    -99       N  
ATOM    564  N   SER A 122     -20.855  -3.126   6.209  1.00 22.60           N  
ANISOU  564  N   SER A 122     2154   3937   2496   -578   -490    132       N  
ATOM    565  CA  SER A 122     -20.286  -1.800   6.455  1.00 27.51           C  
ANISOU  565  CA  SER A 122     2782   4480   3189   -417   -481    207       C  
ATOM    566  C   SER A 122     -18.836  -1.869   6.958  1.00 25.98           C  
ANISOU  566  C   SER A 122     2724   4089   3058   -382   -432    160       C  
ATOM    567  O   SER A 122     -17.968  -1.119   6.497  1.00 20.84           O  
ANISOU  567  O   SER A 122     2113   3383   2421   -315   -432    196       O  
ATOM    568  CB  SER A 122     -21.151  -1.027   7.455  1.00 28.40           C  
ANISOU  568  CB  SER A 122     2807   4619   3365   -317   -472    264       C  
ATOM    569  OG  SER A 122     -22.472  -0.882   6.967  1.00 35.67           O  
ANISOU  569  OG  SER A 122     3586   5742   4224   -332   -518    319       O  
ATOM    570  N   PHE A 123     -18.579  -2.758   7.913  1.00 16.74           N  
ANISOU  570  N   PHE A 123     1619   2821   1921   -429   -390     86       N  
ATOM    571  CA  PHE A 123     -17.229  -2.928   8.431  1.00 18.36           C  
ANISOU  571  CA  PHE A 123     1940   2859   2176   -397   -345     42       C  
ATOM    572  C   PHE A 123     -16.282  -3.378   7.324  1.00 17.69           C  
ANISOU  572  C   PHE A 123     1927   2758   2035   -443   -349      7       C  
ATOM    573  O   PHE A 123     -15.249  -2.755   7.095  1.00 15.20           O  
ANISOU  573  O   PHE A 123     1654   2379   1742   -378   -339     27       O  
ATOM    574  CB  PHE A 123     -17.203  -3.938   9.584  1.00 21.43           C  
ANISOU  574  CB  PHE A 123     2385   3162   2596   -443   -301    -25       C  
ATOM    575  CG  PHE A 123     -15.821  -4.253  10.091  1.00 15.41           C  
ANISOU  575  CG  PHE A 123     1735   2247   1872   -410   -258    -68       C  
ATOM    576  CD1 PHE A 123     -15.208  -3.438  11.028  1.00 19.65           C  
ANISOU  576  CD1 PHE A 123     2286   2698   2481   -309   -235    -43       C  
ATOM    577  CD2 PHE A 123     -15.136  -5.370   9.636  1.00 17.90           C  
ANISOU  577  CD2 PHE A 123     2143   2512   2146   -479   -239   -135       C  
ATOM    578  CE1 PHE A 123     -13.937  -3.722  11.495  1.00 21.02           C  
ANISOU  578  CE1 PHE A 123     2548   2758   2682   -281   -200    -78       C  
ATOM    579  CE2 PHE A 123     -13.867  -5.659  10.101  1.00 19.29           C  
ANISOU  579  CE2 PHE A 123     2409   2565   2354   -434   -199   -167       C  
ATOM    580  CZ  PHE A 123     -13.267  -4.833  11.036  1.00 17.86           C  
ANISOU  580  CZ  PHE A 123     2227   2319   2242   -337   -183   -136       C  
ATOM    581  N   GLU A 124     -16.636  -4.464   6.646  1.00 16.33           N  
ANISOU  581  N   GLU A 124     1772   2646   1788   -562   -359    -50       N  
ATOM    582  CA  GLU A 124     -15.720  -5.088   5.697  1.00 24.99           C  
ANISOU  582  CA  GLU A 124     2953   3715   2827   -611   -349   -104       C  
ATOM    583  C   GLU A 124     -15.423  -4.205   4.499  1.00 21.78           C  
ANISOU  583  C   GLU A 124     2511   3389   2376   -575   -385    -45       C  
ATOM    584  O   GLU A 124     -14.291  -4.168   4.008  1.00 18.88           O  
ANISOU  584  O   GLU A 124     2209   2967   1997   -552   -365    -61       O  
ATOM    585  CB  GLU A 124     -16.239  -6.452   5.249  1.00 26.65           C  
ANISOU  585  CB  GLU A 124     3202   3964   2961   -755   -347   -186       C  
ATOM    586  CG  GLU A 124     -16.044  -7.530   6.300  1.00 36.73           C  
ANISOU  586  CG  GLU A 124     4569   5111   4277   -791   -294   -257       C  
ATOM    587  CD  GLU A 124     -14.577  -7.904   6.492  1.00 40.46           C  
ANISOU  587  CD  GLU A 124     5161   5435   4778   -732   -243   -299       C  
ATOM    588  OE1 GLU A 124     -13.812  -7.828   5.506  1.00 55.01           O  
ANISOU  588  OE1 GLU A 124     7036   7289   6577   -721   -244   -311       O  
ATOM    589  OE2 GLU A 124     -14.190  -8.273   7.623  1.00 27.54           O  
ANISOU  589  OE2 GLU A 124     3579   3682   3203   -694   -201   -316       O  
ATOM    590  N   GLN A 125     -16.435  -3.483   4.045  1.00 17.37           N  
ANISOU  590  N   GLN A 125     1845   2967   1789   -566   -435     28       N  
ATOM    591  CA  GLN A 125     -16.280  -2.651   2.865  1.00 26.50           C  
ANISOU  591  CA  GLN A 125     2963   4212   2892   -535   -473     97       C  
ATOM    592  C   GLN A 125     -15.396  -1.447   3.146  1.00 26.15           C  
ANISOU  592  C   GLN A 125     2941   4073   2920   -411   -455    164       C  
ATOM    593  O   GLN A 125     -14.593  -1.049   2.299  1.00 20.37           O  
ANISOU  593  O   GLN A 125     2240   3343   2155   -396   -458    189       O  
ATOM    594  CB  GLN A 125     -17.634  -2.195   2.337  1.00 30.26           C  
ANISOU  594  CB  GLN A 125     3313   4869   3316   -545   -533    169       C  
ATOM    595  CG  GLN A 125     -18.403  -3.283   1.611  1.00 41.13           C  
ANISOU  595  CG  GLN A 125     4662   6381   4586   -694   -562    108       C  
ATOM    596  CD  GLN A 125     -19.701  -2.767   1.031  1.00 50.60           C  
ANISOU  596  CD  GLN A 125     5717   7788   5722   -700   -628    189       C  
ATOM    597  OE1 GLN A 125     -20.116  -1.641   1.320  1.00 52.60           O  
ANISOU  597  OE1 GLN A 125     5892   8071   6022   -578   -645    292       O  
ATOM    598  NE2 GLN A 125     -20.347  -3.581   0.201  1.00 54.86           N  
ANISOU  598  NE2 GLN A 125     6221   8474   6148   -840   -664    144       N  
ATOM    599  N   VAL A 126     -15.547  -0.857   4.326  1.00 16.61           N  
ANISOU  599  N   VAL A 126     1720   2786   1805   -330   -436    193       N  
ATOM    600  CA  VAL A 126     -14.662   0.236   4.719  1.00 16.00           C  
ANISOU  600  CA  VAL A 126     1680   2602   1799   -229   -412    242       C  
ATOM    601  C   VAL A 126     -13.222  -0.278   4.863  1.00 15.23           C  
ANISOU  601  C   VAL A 126     1680   2393   1713   -248   -369    174       C  
ATOM    602  O   VAL A 126     -12.286   0.321   4.337  1.00 16.07           O  
ANISOU  602  O   VAL A 126     1819   2473   1814   -221   -362    204       O  
ATOM    603  CB  VAL A 126     -15.119   0.910   6.041  1.00 21.17           C  
ANISOU  603  CB  VAL A 126     2309   3188   2545   -145   -394    270       C  
ATOM    604  CG1 VAL A 126     -14.027   1.827   6.579  1.00 18.07           C  
ANISOU  604  CG1 VAL A 126     1980   2663   2222    -70   -360    290       C  
ATOM    605  CG2 VAL A 126     -16.434   1.692   5.827  1.00 21.09           C  
ANISOU  605  CG2 VAL A 126     2195   3291   2526    -90   -431    358       C  
ATOM    606  N   VAL A 127     -13.051  -1.390   5.577  1.00 14.80           N  
ANISOU  606  N   VAL A 127     1672   2280   1672   -292   -338     88       N  
ATOM    607  CA  VAL A 127     -11.712  -1.899   5.865  1.00 16.04           C  
ANISOU  607  CA  VAL A 127     1915   2334   1845   -289   -294     30       C  
ATOM    608  C   VAL A 127     -10.998  -2.387   4.594  1.00 14.51           C  
ANISOU  608  C   VAL A 127     1759   2184   1571   -337   -293      0       C  
ATOM    609  O   VAL A 127      -9.813  -2.118   4.406  1.00 14.20           O  
ANISOU  609  O   VAL A 127     1758   2102   1535   -306   -269      1       O  
ATOM    610  CB  VAL A 127     -11.740  -2.993   6.960  1.00 16.39           C  
ANISOU  610  CB  VAL A 127     2004   2301   1921   -313   -259    -44       C  
ATOM    611  CG1 VAL A 127     -10.400  -3.663   7.073  1.00 14.00           C  
ANISOU  611  CG1 VAL A 127     1786   1917   1618   -305   -216   -101       C  
ATOM    612  CG2 VAL A 127     -12.129  -2.384   8.319  1.00 13.31           C  
ANISOU  612  CG2 VAL A 127     1586   1857   1613   -252   -250    -15       C  
ATOM    613  N   ASN A 128     -11.716  -3.089   3.720  1.00 19.44           N  
ANISOU  613  N   ASN A 128     2370   2901   2115   -418   -317    -28       N  
ATOM    614  CA  ASN A 128     -11.148  -3.471   2.423  1.00 15.77           C  
ANISOU  614  CA  ASN A 128     1938   2494   1561   -465   -318    -56       C  
ATOM    615  C   ASN A 128     -10.667  -2.273   1.615  1.00 19.60           C  
ANISOU  615  C   ASN A 128     2391   3030   2028   -419   -338     28       C  
ATOM    616  O   ASN A 128      -9.572  -2.297   1.050  1.00 17.39           O  
ANISOU  616  O   ASN A 128     2153   2738   1717   -414   -312     13       O  
ATOM    617  CB  ASN A 128     -12.149  -4.268   1.597  1.00 16.73           C  
ANISOU  617  CB  ASN A 128     2041   2725   1590   -571   -349    -95       C  
ATOM    618  CG  ASN A 128     -12.320  -5.673   2.114  1.00 31.46           C  
ANISOU  618  CG  ASN A 128     3976   4526   3453   -641   -315   -198       C  
ATOM    619  OD1 ASN A 128     -11.486  -6.166   2.872  1.00 33.27           O  
ANISOU  619  OD1 ASN A 128     4279   4629   3732   -603   -264   -243       O  
ATOM    620  ND2 ASN A 128     -13.393  -6.329   1.707  1.00 28.56           N  
ANISOU  620  ND2 ASN A 128     3586   4245   3020   -746   -342   -232       N  
ATOM    621  N   GLU A 129     -11.482  -1.222   1.560  1.00 16.90           N  
ANISOU  621  N   GLU A 129     1975   2744   1702   -383   -379    122       N  
ATOM    622  CA  GLU A 129     -11.094  -0.030   0.814  1.00 19.05           C  
ANISOU  622  CA  GLU A 129     2226   3052   1958   -338   -396    215       C  
ATOM    623  C   GLU A 129      -9.925   0.686   1.505  1.00 15.72           C  
ANISOU  623  C   GLU A 129     1849   2509   1615   -273   -356    234       C  
ATOM    624  O   GLU A 129      -9.033   1.221   0.848  1.00 15.84           O  
ANISOU  624  O   GLU A 129     1884   2530   1605   -267   -346    268       O  
ATOM    625  CB  GLU A 129     -12.290   0.907   0.646  1.00 20.13           C  
ANISOU  625  CB  GLU A 129     2281   3271   2098   -298   -446    317       C  
ATOM    626  CG  GLU A 129     -11.988   2.177  -0.142  1.00 27.27           C  
ANISOU  626  CG  GLU A 129     3173   4204   2984   -246   -463    429       C  
ATOM    627  CD  GLU A 129     -11.479   1.890  -1.548  1.00 39.64           C  
ANISOU  627  CD  GLU A 129     4753   5868   4440   -308   -474    426       C  
ATOM    628  OE1 GLU A 129     -11.959   0.924  -2.181  1.00 42.55           O  
ANISOU  628  OE1 GLU A 129     5105   6339   4723   -387   -495    367       O  
ATOM    629  OE2 GLU A 129     -10.586   2.626  -2.016  1.00 43.62           O  
ANISOU  629  OE2 GLU A 129     5289   6348   4939   -285   -459    478       O  
ATOM    630  N   LEU A 130      -9.927   0.682   2.831  1.00 15.03           N  
ANISOU  630  N   LEU A 130     1773   2320   1615   -235   -333    209       N  
ATOM    631  CA  LEU A 130      -8.842   1.320   3.591  1.00 16.16           C  
ANISOU  631  CA  LEU A 130     1955   2357   1828   -186   -297    218       C  
ATOM    632  C   LEU A 130      -7.472   0.747   3.197  1.00 14.19           C  
ANISOU  632  C   LEU A 130     1753   2096   1541   -213   -261    164       C  
ATOM    633  O   LEU A 130      -6.507   1.491   3.026  1.00 15.25           O  
ANISOU  633  O   LEU A 130     1901   2210   1683   -198   -245    199       O  
ATOM    634  CB  LEU A 130      -9.073   1.180   5.108  1.00 13.73           C  
ANISOU  634  CB  LEU A 130     1655   1958   1605   -152   -277    183       C  
ATOM    635  CG  LEU A 130      -7.964   1.641   6.077  1.00 13.10           C  
ANISOU  635  CG  LEU A 130     1613   1774   1589   -116   -240    172       C  
ATOM    636  CD1 LEU A 130      -7.548   3.098   5.812  1.00 13.35           C  
ANISOU  636  CD1 LEU A 130     1648   1782   1642    -86   -242    253       C  
ATOM    637  CD2 LEU A 130      -8.383   1.459   7.542  1.00 12.59           C  
ANISOU  637  CD2 LEU A 130     1551   1640   1594    -86   -225    139       C  
ATOM    638  N   PHE A 131      -7.407  -0.570   3.021  1.00 14.20           N  
ANISOU  638  N   PHE A 131     1783   2115   1499   -254   -246     80       N  
ATOM    639  CA  PHE A 131      -6.130  -1.247   2.775  1.00 14.09           C  
ANISOU  639  CA  PHE A 131     1815   2086   1454   -260   -203     20       C  
ATOM    640  C   PHE A 131      -5.973  -1.729   1.325  1.00 16.73           C  
ANISOU  640  C   PHE A 131     2159   2516   1682   -310   -206     -1       C  
ATOM    641  O   PHE A 131      -5.047  -2.488   1.010  1.00 15.98           O  
ANISOU  641  O   PHE A 131     2106   2419   1548   -313   -166    -63       O  
ATOM    642  CB  PHE A 131      -5.963  -2.428   3.749  1.00 13.67           C  
ANISOU  642  CB  PHE A 131     1806   1956   1431   -251   -169    -64       C  
ATOM    643  CG  PHE A 131      -5.862  -2.012   5.209  1.00 13.48           C  
ANISOU  643  CG  PHE A 131     1777   1845   1499   -201   -159    -51       C  
ATOM    644  CD1 PHE A 131      -4.751  -1.334   5.672  1.00 13.94           C  
ANISOU  644  CD1 PHE A 131     1833   1869   1593   -161   -138    -29       C  
ATOM    645  CD2 PHE A 131      -6.867  -2.317   6.104  1.00 12.76           C  
ANISOU  645  CD2 PHE A 131     1681   1718   1452   -203   -169    -63       C  
ATOM    646  CE1 PHE A 131      -4.647  -0.962   7.006  1.00 13.63           C  
ANISOU  646  CE1 PHE A 131     1792   1759   1628   -125   -130    -24       C  
ATOM    647  CE2 PHE A 131      -6.772  -1.949   7.449  1.00 12.19           C  
ANISOU  647  CE2 PHE A 131     1606   1572   1455   -158   -157    -55       C  
ATOM    648  CZ  PHE A 131      -5.666  -1.272   7.896  1.00 11.85           C  
ANISOU  648  CZ  PHE A 131     1566   1494   1444   -119   -139    -37       C  
ATOM    649  N   ARG A 132      -6.864  -1.283   0.442  1.00 15.45           N  
ANISOU  649  N   ARG A 132     1958   2444   1469   -343   -251     52       N  
ATOM    650  CA  ARG A 132      -6.848  -1.752  -0.948  1.00 16.27           C  
ANISOU  650  CA  ARG A 132     2068   2653   1460   -400   -259     29       C  
ATOM    651  C   ARG A 132      -5.496  -1.540  -1.644  1.00 16.42           C  
ANISOU  651  C   ARG A 132     2108   2695   1435   -390   -223     32       C  
ATOM    652  O   ARG A 132      -5.024  -2.419  -2.357  1.00 18.54           O  
ANISOU  652  O   ARG A 132     2413   3002   1627   -421   -194    -39       O  
ATOM    653  CB  ARG A 132      -7.978  -1.111  -1.753  1.00 21.44           C  
ANISOU  653  CB  ARG A 132     2663   3418   2064   -428   -320    107       C  
ATOM    654  CG  ARG A 132      -8.022  -1.569  -3.207  1.00 31.87           C  
ANISOU  654  CG  ARG A 132     3987   4866   3256   -496   -333     84       C  
ATOM    655  CD  ARG A 132      -9.253  -1.028  -3.922  1.00 42.21           C  
ANISOU  655  CD  ARG A 132     5227   6303   4509   -523   -400    163       C  
ATOM    656  NE  ARG A 132     -10.462  -1.770  -3.576  1.00 51.85           N  
ANISOU  656  NE  ARG A 132     6422   7554   5724   -572   -428    116       N  
ATOM    657  CZ  ARG A 132     -10.934  -2.804  -4.268  1.00 60.98           C  
ANISOU  657  CZ  ARG A 132     7591   8795   6783   -668   -440     36       C  
ATOM    658  NH1 ARG A 132     -10.301  -3.230  -5.353  1.00 61.01           N  
ANISOU  658  NH1 ARG A 132     7636   8859   6686   -716   -423     -9       N  
ATOM    659  NH2 ARG A 132     -12.045  -3.413  -3.874  1.00 66.81           N  
ANISOU  659  NH2 ARG A 132     8302   9561   7521   -724   -465     -1       N  
ATOM    660  N   ASP A 133      -4.875  -0.384  -1.437  1.00 16.17           N  
ANISOU  660  N   ASP A 133     2056   2639   1448   -351   -219    111       N  
ATOM    661  CA  ASP A 133      -3.583  -0.102  -2.077  1.00 16.40           C  
ANISOU  661  CA  ASP A 133     2094   2703   1434   -352   -184    123       C  
ATOM    662  C   ASP A 133      -2.405  -0.009  -1.108  1.00 18.34           C  
ANISOU  662  C   ASP A 133     2351   2869   1748   -309   -138    102       C  
ATOM    663  O   ASP A 133      -1.368   0.569  -1.424  1.00 15.94           O  
ANISOU  663  O   ASP A 133     2036   2592   1427   -310   -114    136       O  
ATOM    664  CB  ASP A 133      -3.643   1.130  -2.993  1.00 25.11           C  
ANISOU  664  CB  ASP A 133     3167   3876   2497   -367   -212    235       C  
ATOM    665  CG  ASP A 133      -3.999   2.415  -2.255  1.00 24.37           C  
ANISOU  665  CG  ASP A 133     3057   3709   2495   -330   -235    330       C  
ATOM    666  OD1 ASP A 133      -4.036   2.435  -1.003  1.00 22.07           O  
ANISOU  666  OD1 ASP A 133     2773   3317   2296   -295   -225    306       O  
ATOM    667  OD2 ASP A 133      -4.236   3.424  -2.952  1.00 25.11           O  
ANISOU  667  OD2 ASP A 133     3135   3844   2561   -334   -259    431       O  
ATOM    668  N   GLY A 134      -2.560  -0.599   0.071  1.00 16.06           N  
ANISOU  668  N   GLY A 134     2080   2493   1529   -278   -127     48       N  
ATOM    669  CA  GLY A 134      -1.431  -0.743   0.964  1.00 19.41           C  
ANISOU  669  CA  GLY A 134     2512   2863   2001   -237    -85     17       C  
ATOM    670  C   GLY A 134      -1.766  -0.810   2.431  1.00 17.90           C  
ANISOU  670  C   GLY A 134     2326   2573   1902   -202    -88      2       C  
ATOM    671  O   GLY A 134      -2.852  -0.435   2.862  1.00 13.72           O  
ANISOU  671  O   GLY A 134     1788   2009   1417   -205   -123     32       O  
ATOM    672  N   VAL A 135      -0.805  -1.302   3.197  1.00 17.48           N  
ANISOU  672  N   VAL A 135     2282   2485   1873   -163    -50    -42       N  
ATOM    673  CA  VAL A 135      -0.885  -1.283   4.636  1.00 16.08           C  
ANISOU  673  CA  VAL A 135     2108   2226   1777   -129    -49    -51       C  
ATOM    674  C   VAL A 135       0.242  -0.382   5.121  1.00 15.60           C  
ANISOU  674  C   VAL A 135     2015   2170   1742   -120    -35    -16       C  
ATOM    675  O   VAL A 135       1.360  -0.458   4.613  1.00 14.07           O  
ANISOU  675  O   VAL A 135     1804   2038   1502   -118     -6    -22       O  
ATOM    676  CB  VAL A 135      -0.695  -2.690   5.220  1.00 15.45           C  
ANISOU  676  CB  VAL A 135     2068   2106   1696    -90    -16   -128       C  
ATOM    677  CG1 VAL A 135      -0.752  -2.655   6.742  1.00 19.95           C  
ANISOU  677  CG1 VAL A 135     2638   2601   2342    -54    -16   -130       C  
ATOM    678  CG2 VAL A 135      -1.747  -3.660   4.645  1.00 17.61           C  
ANISOU  678  CG2 VAL A 135     2384   2375   1932   -121    -24   -173       C  
ATOM    679  N   ASN A 136      -0.060   0.494   6.075  1.00 12.96           N  
ANISOU  679  N   ASN A 136     1672   1777   1476   -120    -53     18       N  
ATOM    680  CA  ASN A 136       0.978   1.230   6.785  1.00 14.89           C  
ANISOU  680  CA  ASN A 136     1894   2016   1748   -122    -39     35       C  
ATOM    681  C   ASN A 136       0.533   1.468   8.226  1.00 13.50           C  
ANISOU  681  C   ASN A 136     1727   1759   1644   -102    -49     26       C  
ATOM    682  O   ASN A 136      -0.609   1.177   8.568  1.00 13.09           O  
ANISOU  682  O   ASN A 136     1693   1659   1621    -86    -66     17       O  
ATOM    683  CB  ASN A 136       1.398   2.510   6.021  1.00 13.39           C  
ANISOU  683  CB  ASN A 136     1689   1859   1540   -175    -44    102       C  
ATOM    684  CG  ASN A 136       0.310   3.572   5.970  1.00 12.96           C  
ANISOU  684  CG  ASN A 136     1654   1744   1525   -191    -76    163       C  
ATOM    685  OD1 ASN A 136      -0.221   3.973   7.000  1.00 12.63           O  
ANISOU  685  OD1 ASN A 136     1626   1626   1548   -174    -86    163       O  
ATOM    686  ND2 ASN A 136       0.004   4.062   4.763  1.00 13.48           N  
ANISOU  686  ND2 ASN A 136     1723   1851   1550   -217    -90    219       N  
ATOM    687  N   TRP A 137       1.420   1.963   9.081  1.00 12.71           N  
ANISOU  687  N   TRP A 137     1608   1654   1565   -107    -37     25       N  
ATOM    688  CA  TRP A 137       1.076   2.074  10.498  1.00 15.30           C  
ANISOU  688  CA  TRP A 137     1946   1917   1951    -88    -43      6       C  
ATOM    689  C   TRP A 137      -0.085   3.042  10.747  1.00 15.48           C  
ANISOU  689  C   TRP A 137     1993   1865   2025    -99    -65     40       C  
ATOM    690  O   TRP A 137      -0.915   2.803  11.610  1.00 14.46           O  
ANISOU  690  O   TRP A 137     1876   1684   1934    -70    -72     21       O  
ATOM    691  CB  TRP A 137       2.293   2.467  11.335  1.00 14.89           C  
ANISOU  691  CB  TRP A 137     1866   1891   1900   -103    -29     -4       C  
ATOM    692  CG  TRP A 137       3.310   1.356  11.488  1.00 16.50           C  
ANISOU  692  CG  TRP A 137     2038   2167   2062    -60     -6    -39       C  
ATOM    693  CD1 TRP A 137       4.616   1.371  11.072  1.00 16.97           C  
ANISOU  693  CD1 TRP A 137     2050   2323   2073    -72     14    -36       C  
ATOM    694  CD2 TRP A 137       3.098   0.070  12.097  1.00 15.33           C  
ANISOU  694  CD2 TRP A 137     1907   2003   1916      9      5    -79       C  
ATOM    695  NE1 TRP A 137       5.225   0.177  11.394  1.00 15.70           N  
ANISOU  695  NE1 TRP A 137     1872   2208   1885      0     36    -69       N  
ATOM    696  CE2 TRP A 137       4.318  -0.631  12.032  1.00 15.04           C  
ANISOU  696  CE2 TRP A 137     1834   2047   1832     50     31    -95       C  
ATOM    697  CE3 TRP A 137       2.001  -0.545  12.710  1.00 15.70           C  
ANISOU  697  CE3 TRP A 137     1994   1975   1996     39     -3    -98       C  
ATOM    698  CZ2 TRP A 137       4.466  -1.921  12.541  1.00 20.18           C  
ANISOU  698  CZ2 TRP A 137     2502   2693   2473    130     52   -126       C  
ATOM    699  CZ3 TRP A 137       2.151  -1.820  13.211  1.00 22.90           C  
ANISOU  699  CZ3 TRP A 137     2924   2880   2896    101     17   -130       C  
ATOM    700  CH2 TRP A 137       3.376  -2.498  13.119  1.00 22.65           C  
ANISOU  700  CH2 TRP A 137     2869   2917   2822    150     44   -142       C  
ATOM    701  N   GLY A 138      -0.145   4.120   9.981  1.00 11.79           N  
ANISOU  701  N   GLY A 138     1531   1392   1554   -135    -74     95       N  
ATOM    702  CA  GLY A 138      -1.234   5.077  10.113  1.00 12.55           C  
ANISOU  702  CA  GLY A 138     1653   1417   1696   -128    -91    136       C  
ATOM    703  C   GLY A 138      -2.592   4.506   9.728  1.00 15.20           C  
ANISOU  703  C   GLY A 138     1985   1758   2032    -92   -112    142       C  
ATOM    704  O   GLY A 138      -3.595   4.784  10.390  1.00 11.72           O  
ANISOU  704  O   GLY A 138     1550   1266   1636    -60   -120    147       O  
ATOM    705  N   ARG A 139      -2.642   3.725   8.652  1.00 11.94           N  
ANISOU  705  N   ARG A 139     1558   1414   1563   -100   -119    139       N  
ATOM    706  CA  ARG A 139      -3.902   3.083   8.275  1.00 11.95           C  
ANISOU  706  CA  ARG A 139     1551   1438   1553    -85   -141    137       C  
ATOM    707  C   ARG A 139      -4.300   2.042   9.309  1.00 11.47           C  
ANISOU  707  C   ARG A 139     1494   1350   1516    -63   -133     74       C  
ATOM    708  O   ARG A 139      -5.476   1.829   9.554  1.00 11.46           O  
ANISOU  708  O   ARG A 139     1483   1342   1531    -52   -148     75       O  
ATOM    709  CB  ARG A 139      -3.811   2.434   6.894  1.00 12.31           C  
ANISOU  709  CB  ARG A 139     1589   1567   1523   -112   -148    136       C  
ATOM    710  CG  ARG A 139      -3.628   3.457   5.776  1.00 12.91           C  
ANISOU  710  CG  ARG A 139     1659   1679   1566   -135   -160    210       C  
ATOM    711  CD  ARG A 139      -3.450   2.778   4.429  1.00 13.32           C  
ANISOU  711  CD  ARG A 139     1703   1825   1532   -165   -164    202       C  
ATOM    712  NE  ARG A 139      -3.317   3.752   3.350  1.00 13.96           N  
ANISOU  712  NE  ARG A 139     1780   1951   1575   -188   -176    282       N  
ATOM    713  CZ  ARG A 139      -3.361   3.450   2.060  1.00 18.46           C  
ANISOU  713  CZ  ARG A 139     2339   2612   2061   -217   -186    296       C  
ATOM    714  NH1 ARG A 139      -3.525   2.188   1.682  1.00 15.31           N  
ANISOU  714  NH1 ARG A 139     1941   2264   1611   -230   -183    225       N  
ATOM    715  NH2 ARG A 139      -3.234   4.416   1.154  1.00 15.15           N  
ANISOU  715  NH2 ARG A 139     1919   2229   1609   -235   -197    381       N  
ATOM    716  N   ILE A 140      -3.316   1.379   9.902  1.00 11.18           N  
ANISOU  716  N   ILE A 140     1467   1305   1475    -57   -107     26       N  
ATOM    717  CA  ILE A 140      -3.620   0.455  10.985  1.00 10.80           C  
ANISOU  717  CA  ILE A 140     1431   1222   1450    -34    -96    -22       C  
ATOM    718  C   ILE A 140      -4.234   1.181  12.197  1.00 11.20           C  
ANISOU  718  C   ILE A 140     1479   1216   1562    -15   -100    -11       C  
ATOM    719  O   ILE A 140      -5.230   0.730  12.762  1.00 11.07           O  
ANISOU  719  O   ILE A 140     1462   1181   1564     -3   -103    -26       O  
ATOM    720  CB  ILE A 140      -2.378  -0.366  11.387  1.00 11.68           C  
ANISOU  720  CB  ILE A 140     1554   1344   1541    -15    -66    -65       C  
ATOM    721  CG1 ILE A 140      -2.017  -1.333  10.245  1.00 11.02           C  
ANISOU  721  CG1 ILE A 140     1484   1307   1395    -21    -54    -89       C  
ATOM    722  CG2 ILE A 140      -2.649  -1.116  12.706  1.00 13.27           C  
ANISOU  722  CG2 ILE A 140     1772   1498   1771     15    -54    -99       C  
ATOM    723  CD1 ILE A 140      -0.687  -2.069  10.441  1.00 11.98           C  
ANISOU  723  CD1 ILE A 140     1611   1452   1490     16    -19   -122       C  
ATOM    724  N   VAL A 141      -3.645   2.304  12.594  1.00 11.02           N  
ANISOU  724  N   VAL A 141     1457   1166   1565    -17    -96     10       N  
ATOM    725  CA  VAL A 141      -4.250   3.135  13.640  1.00 10.58           C  
ANISOU  725  CA  VAL A 141     1408   1051   1562      1    -95     17       C  
ATOM    726  C   VAL A 141      -5.667   3.539  13.226  1.00 12.79           C  
ANISOU  726  C   VAL A 141     1676   1324   1859     22   -113     56       C  
ATOM    727  O   VAL A 141      -6.587   3.445  14.023  1.00 12.95           O  
ANISOU  727  O   VAL A 141     1688   1323   1908     48   -111     45       O  
ATOM    728  CB  VAL A 141      -3.392   4.383  13.959  1.00 11.45           C  
ANISOU  728  CB  VAL A 141     1535   1126   1691    -20    -85     33       C  
ATOM    729  CG1 VAL A 141      -4.142   5.338  14.895  1.00 12.49           C  
ANISOU  729  CG1 VAL A 141     1687   1184   1875      3    -79     38       C  
ATOM    730  CG2 VAL A 141      -2.050   3.960  14.579  1.00 10.79           C  
ANISOU  730  CG2 VAL A 141     1444   1071   1586    -39    -70     -7       C  
ATOM    731  N   ALA A 142      -5.845   3.950  11.970  1.00 13.38           N  
ANISOU  731  N   ALA A 142     1743   1433   1909     11   -131    105       N  
ATOM    732  CA  ALA A 142      -7.175   4.302  11.460  1.00 14.12           C  
ANISOU  732  CA  ALA A 142     1812   1546   2008     36   -153    152       C  
ATOM    733  C   ALA A 142      -8.181   3.139  11.548  1.00 11.54           C  
ANISOU  733  C   ALA A 142     1454   1268   1664     33   -165    121       C  
ATOM    734  O   ALA A 142      -9.345   3.341  11.855  1.00 11.77           O  
ANISOU  734  O   ALA A 142     1453   1306   1714     63   -174    140       O  
ATOM    735  CB  ALA A 142      -7.070   4.793  10.034  1.00 13.41           C  
ANISOU  735  CB  ALA A 142     1717   1500   1878     21   -173    212       C  
ATOM    736  N   PHE A 143      -7.715   1.938  11.237  1.00 12.27           N  
ANISOU  736  N   PHE A 143     1555   1392   1714     -4   -160     75       N  
ATOM    737  CA  PHE A 143      -8.498   0.706  11.362  1.00 11.28           C  
ANISOU  737  CA  PHE A 143     1420   1297   1569    -26   -163     35       C  
ATOM    738  C   PHE A 143      -8.998   0.505  12.799  1.00 15.48           C  
ANISOU  738  C   PHE A 143     1951   1784   2146     -4   -146      9       C  
ATOM    739  O   PHE A 143     -10.178   0.235  13.023  1.00 11.21           O  
ANISOU  739  O   PHE A 143     1378   1272   1608     -9   -155     12       O  
ATOM    740  CB  PHE A 143      -7.609  -0.462  10.895  1.00 11.17           C  
ANISOU  740  CB  PHE A 143     1442   1294   1508    -60   -148    -15       C  
ATOM    741  CG  PHE A 143      -8.063  -1.828  11.340  1.00 13.88           C  
ANISOU  741  CG  PHE A 143     1808   1628   1839    -85   -135    -69       C  
ATOM    742  CD1 PHE A 143      -9.026  -2.528  10.624  1.00 13.36           C  
ANISOU  742  CD1 PHE A 143     1732   1612   1730   -136   -151    -82       C  
ATOM    743  CD2 PHE A 143      -7.462  -2.448  12.424  1.00 16.40           C  
ANISOU  743  CD2 PHE A 143     2163   1889   2179    -63   -104   -107       C  
ATOM    744  CE1 PHE A 143      -9.406  -3.813  11.009  1.00 13.92           C  
ANISOU  744  CE1 PHE A 143     1839   1662   1787   -175   -134   -134       C  
ATOM    745  CE2 PHE A 143      -7.835  -3.725  12.814  1.00 16.61           C  
ANISOU  745  CE2 PHE A 143     2226   1893   2192    -87    -87   -150       C  
ATOM    746  CZ  PHE A 143      -8.807  -4.407  12.114  1.00 14.02           C  
ANISOU  746  CZ  PHE A 143     1898   1601   1828   -147    -99   -165       C  
ATOM    747  N   PHE A 144      -8.108   0.642  13.780  1.00 14.29           N  
ANISOU  747  N   PHE A 144     1829   1576   2023     16   -122    -14       N  
ATOM    748  CA  PHE A 144      -8.524   0.530  15.190  1.00 17.58           C  
ANISOU  748  CA  PHE A 144     2247   1956   2476     38   -104    -37       C  
ATOM    749  C   PHE A 144      -9.515   1.629  15.589  1.00 17.79           C  
ANISOU  749  C   PHE A 144     2243   1974   2541     75   -109     -2       C  
ATOM    750  O   PHE A 144     -10.560   1.357  16.209  1.00 14.40           O  
ANISOU  750  O   PHE A 144     1787   1560   2124     85   -104     -8       O  
ATOM    751  CB  PHE A 144      -7.310   0.546  16.127  1.00 14.99           C  
ANISOU  751  CB  PHE A 144     1951   1586   2159     51    -82    -65       C  
ATOM    752  CG  PHE A 144      -6.639  -0.792  16.272  1.00 11.52           C  
ANISOU  752  CG  PHE A 144     1539   1149   1688     40    -67   -103       C  
ATOM    753  CD1 PHE A 144      -5.654  -1.185  15.391  1.00  9.88           C  
ANISOU  753  CD1 PHE A 144     1346    963   1445     31    -65   -109       C  
ATOM    754  CD2 PHE A 144      -7.018  -1.669  17.280  1.00 14.37           C  
ANISOU  754  CD2 PHE A 144     1915   1490   2053     45    -50   -128       C  
ATOM    755  CE1 PHE A 144      -5.042  -2.426  15.516  1.00 14.26           C  
ANISOU  755  CE1 PHE A 144     1933   1513   1971     40    -45   -141       C  
ATOM    756  CE2 PHE A 144      -6.412  -2.907  17.411  1.00 12.36           C  
ANISOU  756  CE2 PHE A 144     1700   1225   1771     46    -32   -154       C  
ATOM    757  CZ  PHE A 144      -5.422  -3.280  16.535  1.00 16.86           C  
ANISOU  757  CZ  PHE A 144     2288   1810   2310     50    -28   -162       C  
ATOM    758  N   SER A 145      -9.184   2.871  15.250  1.00 10.87           N  
ANISOU  758  N   SER A 145     1374   1072   1684     99   -113     34       N  
ATOM    759  CA  SER A 145     -10.085   3.991  15.535  1.00 11.31           C  
ANISOU  759  CA  SER A 145     1413   1106   1777    151   -110     72       C  
ATOM    760  C   SER A 145     -11.500   3.818  14.930  1.00 17.61           C  
ANISOU  760  C   SER A 145     2150   1979   2562    168   -132    109       C  
ATOM    761  O   SER A 145     -12.505   4.154  15.561  1.00 12.10           O  
ANISOU  761  O   SER A 145     1420   1289   1890    214   -123    119       O  
ATOM    762  CB  SER A 145      -9.465   5.313  15.077  1.00 11.64           C  
ANISOU  762  CB  SER A 145     1489   1096   1836    167   -109    112       C  
ATOM    763  OG  SER A 145      -8.445   5.725  15.986  1.00 17.69           O  
ANISOU  763  OG  SER A 145     2302   1796   2622    154    -84     75       O  
ATOM    764  N   PHE A 146     -11.560   3.321  13.698  1.00 12.80           N  
ANISOU  764  N   PHE A 146     1521   1435   1907    130   -161    129       N  
ATOM    765  CA  PHE A 146     -12.828   3.039  13.021  1.00 12.51           C  
ANISOU  765  CA  PHE A 146     1417   1495   1840    127   -189    161       C  
ATOM    766  C   PHE A 146     -13.621   1.985  13.793  1.00 13.73           C  
ANISOU  766  C   PHE A 146     1542   1685   1990     96   -180    116       C  
ATOM    767  O   PHE A 146     -14.830   2.126  14.005  1.00 16.01           O  
ANISOU  767  O   PHE A 146     1766   2034   2282    120   -185    140       O  
ATOM    768  CB  PHE A 146     -12.558   2.574  11.573  1.00 13.44           C  
ANISOU  768  CB  PHE A 146     1531   1679   1896     73   -219    175       C  
ATOM    769  CG  PHE A 146     -13.776   2.039  10.860  1.00 17.67           C  
ANISOU  769  CG  PHE A 146     1997   2333   2384     42   -252    193       C  
ATOM    770  CD1 PHE A 146     -14.901   2.830  10.689  1.00 22.92           C  
ANISOU  770  CD1 PHE A 146     2591   3062   3055     99   -272    260       C  
ATOM    771  CD2 PHE A 146     -13.790   0.748  10.352  1.00 17.46           C  
ANISOU  771  CD2 PHE A 146     1975   2358   2302    -45   -261    143       C  
ATOM    772  CE1 PHE A 146     -16.026   2.335  10.029  1.00 20.52           C  
ANISOU  772  CE1 PHE A 146     2208   2893   2698     63   -307    278       C  
ATOM    773  CE2 PHE A 146     -14.912   0.247   9.686  1.00 14.02           C  
ANISOU  773  CE2 PHE A 146     1473   2041   1811    -94   -294    153       C  
ATOM    774  CZ  PHE A 146     -16.027   1.040   9.530  1.00 15.79           C  
ANISOU  774  CZ  PHE A 146     1613   2349   2038    -44   -319    222       C  
ATOM    775  N   GLY A 147     -12.934   0.931  14.225  1.00 13.99           N  
ANISOU  775  N   GLY A 147     1621   1684   2012     45   -162     56       N  
ATOM    776  CA  GLY A 147     -13.571  -0.116  15.014  1.00 13.45           C  
ANISOU  776  CA  GLY A 147     1543   1631   1937      7   -147     16       C  
ATOM    777  C   GLY A 147     -14.136   0.431  16.316  1.00 16.63           C  
ANISOU  777  C   GLY A 147     1922   2011   2384     60   -122     19       C  
ATOM    778  O   GLY A 147     -15.250   0.096  16.713  1.00 17.43           O  
ANISOU  778  O   GLY A 147     1971   2170   2480     48   -119     20       O  
ATOM    779  N   GLY A 148     -13.376   1.302  16.972  1.00 13.07           N  
ANISOU  779  N   GLY A 148     1510   1483   1972    114   -103     17       N  
ATOM    780  CA  GLY A 148     -13.834   1.913  18.205  1.00 13.36           C  
ANISOU  780  CA  GLY A 148     1536   1492   2046    167    -75     12       C  
ATOM    781  C   GLY A 148     -15.078   2.740  17.967  1.00 15.45           C  
ANISOU  781  C   GLY A 148     1733   1812   2325    226    -81     60       C  
ATOM    782  O   GLY A 148     -16.034   2.694  18.743  1.00 16.80           O  
ANISOU  782  O   GLY A 148     1858   2021   2504    250    -62     56       O  
ATOM    783  N   ALA A 149     -15.065   3.500  16.879  1.00 12.73           N  
ANISOU  783  N   ALA A 149     1379   1480   1979    255   -106    111       N  
ATOM    784  CA  ALA A 149     -16.174   4.378  16.540  1.00 13.58           C  
ANISOU  784  CA  ALA A 149     1422   1641   2096    331   -114    172       C  
ATOM    785  C   ALA A 149     -17.431   3.556  16.282  1.00 16.44           C  
ANISOU  785  C   ALA A 149     1689   2138   2420    297   -133    183       C  
ATOM    786  O   ALA A 149     -18.525   3.936  16.704  1.00 14.71           O  
ANISOU  786  O   ALA A 149     1399   1978   2211    357   -122    209       O  
ATOM    787  CB  ALA A 149     -15.831   5.217  15.318  1.00 15.96           C  
ANISOU  787  CB  ALA A 149     1738   1933   2392    359   -140    234       C  
ATOM    788  N   LEU A 150     -17.268   2.428  15.592  1.00 14.76           N  
ANISOU  788  N   LEU A 150     1474   1976   2160    198   -160    161       N  
ATOM    789  CA  LEU A 150     -18.394   1.543  15.315  1.00 17.26           C  
ANISOU  789  CA  LEU A 150     1708   2420   2430    135   -179    162       C  
ATOM    790  C   LEU A 150     -18.973   0.957  16.601  1.00 15.84           C  
ANISOU  790  C   LEU A 150     1507   2248   2262    116   -144    123       C  
ATOM    791  O   LEU A 150     -20.188   0.792  16.726  1.00 16.76           O  
ANISOU  791  O   LEU A 150     1530   2478   2359    109   -147    141       O  
ATOM    792  CB  LEU A 150     -17.964   0.388  14.411  1.00 19.38           C  
ANISOU  792  CB  LEU A 150     2007   2713   2644     21   -204    128       C  
ATOM    793  CG  LEU A 150     -18.194   0.423  12.905  1.00 30.48           C  
ANISOU  793  CG  LEU A 150     3374   4214   3994    -10   -252    167       C  
ATOM    794  CD1 LEU A 150     -18.025  -0.993  12.373  1.00 36.38           C  
ANISOU  794  CD1 LEU A 150     4153   4986   4682   -140   -262    108       C  
ATOM    795  CD2 LEU A 150     -19.565   0.975  12.544  1.00 29.90           C  
ANISOU  795  CD2 LEU A 150     3178   4282   3899     31   -280    232       C  
ATOM    796  N   CYS A 151     -18.102   0.611  17.546  1.00 14.75           N  
ANISOU  796  N   CYS A 151     1452   2004   2149    103   -110     72       N  
ATOM    797  CA  CYS A 151     -18.576   0.065  18.818  1.00 15.77           C  
ANISOU  797  CA  CYS A 151     1571   2137   2284     84    -74     39       C  
ATOM    798  C   CYS A 151     -19.338   1.112  19.601  1.00 14.24           C  
ANISOU  798  C   CYS A 151     1321   1966   2124    186    -48     64       C  
ATOM    799  O   CYS A 151     -20.417   0.836  20.114  1.00 14.65           O  
ANISOU  799  O   CYS A 151     1296   2106   2162    177    -33     68       O  
ATOM    800  CB  CYS A 151     -17.431  -0.515  19.660  1.00 13.27           C  
ANISOU  800  CB  CYS A 151     1354   1710   1980     57    -47    -12       C  
ATOM    801  SG  CYS A 151     -16.746  -2.050  18.982  1.00 18.94           S  
ANISOU  801  SG  CYS A 151     2140   2403   2653    -56    -60    -48       S  
ATOM    802  N   VAL A 152     -18.787   2.320  19.688  1.00 13.97           N  
ANISOU  802  N   VAL A 152     1326   1852   2131    279    -38     79       N  
ATOM    803  CA  VAL A 152     -19.482   3.409  20.377  1.00 14.58           C  
ANISOU  803  CA  VAL A 152     1366   1933   2241    390     -6     99       C  
ATOM    804  C   VAL A 152     -20.841   3.701  19.747  1.00 19.34           C  
ANISOU  804  C   VAL A 152     1850   2673   2826    437    -24    159       C  
ATOM    805  O   VAL A 152     -21.846   3.874  20.454  1.00 19.84           O  
ANISOU  805  O   VAL A 152     1840   2808   2892    487      5    166       O  
ATOM    806  CB  VAL A 152     -18.642   4.695  20.393  1.00 14.48           C  
ANISOU  806  CB  VAL A 152     1432   1798   2271    472      7    106       C  
ATOM    807  CG1 VAL A 152     -19.508   5.896  20.775  1.00 19.59           C  
ANISOU  807  CG1 VAL A 152     2043   2450   2950    602     39    138       C  
ATOM    808  CG2 VAL A 152     -17.497   4.543  21.363  1.00 13.71           C  
ANISOU  808  CG2 VAL A 152     1428   1592   2187    438     33     43       C  
ATOM    809  N   GLU A 153     -20.875   3.758  18.419  1.00 17.10           N  
ANISOU  809  N   GLU A 153     1539   2439   2519    423    -71    206       N  
ATOM    810  CA  GLU A 153     -22.130   4.018  17.708  1.00 25.19           C  
ANISOU  810  CA  GLU A 153     2440   3615   3515    466    -97    272       C  
ATOM    811  C   GLU A 153     -23.158   2.907  17.975  1.00 24.78           C  
ANISOU  811  C   GLU A 153     2289   3710   3417    375   -101    254       C  
ATOM    812  O   GLU A 153     -24.343   3.173  18.218  1.00 18.34           O  
ANISOU  812  O   GLU A 153     1358   3019   2590    430    -91    289       O  
ATOM    813  CB  GLU A 153     -21.875   4.207  16.204  1.00 24.41           C  
ANISOU  813  CB  GLU A 153     2337   3549   3387    453   -151    325       C  
ATOM    814  CG  GLU A 153     -23.134   4.399  15.352  1.00 35.12           C  
ANISOU  814  CG  GLU A 153     3557   5088   4700    489   -189    400       C  
ATOM    815  CD  GLU A 153     -23.769   5.780  15.497  1.00 50.94           C  
ANISOU  815  CD  GLU A 153     5516   7098   6739    666   -169    473       C  
ATOM    816  OE1 GLU A 153     -23.479   6.495  16.483  1.00 59.70           O  
ANISOU  816  OE1 GLU A 153     6691   8084   7907    753   -115    451       O  
ATOM    817  OE2 GLU A 153     -24.570   6.153  14.616  1.00 55.33           O  
ANISOU  817  OE2 GLU A 153     5975   7788   7261    721   -205    554       O  
ATOM    818  N   SER A 154     -22.692   1.664  17.954  1.00 16.73           N  
ANISOU  818  N   SER A 154     1316   2672   2368    235   -110    201       N  
ATOM    819  CA  SER A 154     -23.547   0.520  18.266  1.00 17.14           C  
ANISOU  819  CA  SER A 154     1300   2836   2375    124   -107    176       C  
ATOM    820  C   SER A 154     -24.174   0.633  19.656  1.00 17.71           C  
ANISOU  820  C   SER A 154     1334   2928   2469    167    -53    162       C  
ATOM    821  O   SER A 154     -25.372   0.406  19.830  1.00 20.36           O  
ANISOU  821  O   SER A 154     1549   3413   2772    148    -48    182       O  
ATOM    822  CB  SER A 154     -22.743  -0.775  18.156  1.00 16.40           C  
ANISOU  822  CB  SER A 154     1304   2670   2258    -17   -111    116       C  
ATOM    823  OG  SER A 154     -22.209  -0.906  16.853  1.00 22.01           O  
ANISOU  823  OG  SER A 154     2047   3376   2941    -57   -156    124       O  
ATOM    824  N   VAL A 155     -23.366   0.980  20.649  1.00 16.68           N  
ANISOU  824  N   VAL A 155     1298   2657   2384    219    -12    126       N  
ATOM    825  CA  VAL A 155     -23.894   1.140  21.999  1.00 17.22           C  
ANISOU  825  CA  VAL A 155     1338   2739   2466    264     43    108       C  
ATOM    826  C   VAL A 155     -24.849   2.334  22.076  1.00 21.53           C  
ANISOU  826  C   VAL A 155     1785   3367   3030    409     60    156       C  
ATOM    827  O   VAL A 155     -25.880   2.247  22.730  1.00 18.76           O  
ANISOU  827  O   VAL A 155     1337   3128   2661    426     91    162       O  
ATOM    828  CB  VAL A 155     -22.785   1.225  23.062  1.00 16.06           C  
ANISOU  828  CB  VAL A 155     1315   2435   2352    280     81     55       C  
ATOM    829  CG1 VAL A 155     -23.381   1.472  24.446  1.00 18.94           C  
ANISOU  829  CG1 VAL A 155     1648   2826   2722    331    140     36       C  
ATOM    830  CG2 VAL A 155     -21.972  -0.077  23.074  1.00 15.28           C  
ANISOU  830  CG2 VAL A 155     1301   2275   2230    148     70     16       C  
ATOM    831  N   ASP A 156     -24.518   3.428  21.385  1.00 20.23           N  
ANISOU  831  N   ASP A 156     1645   3146   2896    516     43    195       N  
ATOM    832  CA  ASP A 156     -25.395   4.599  21.318  1.00 19.19           C  
ANISOU  832  CA  ASP A 156     1431   3079   2782    673     60    252       C  
ATOM    833  C   ASP A 156     -26.806   4.209  20.893  1.00 29.10           C  
ANISOU  833  C   ASP A 156     2515   4557   3986    658     39    301       C  
ATOM    834  O   ASP A 156     -27.791   4.673  21.473  1.00 26.22           O  
ANISOU  834  O   ASP A 156     2052   4288   3621    756     77    323       O  
ATOM    835  CB  ASP A 156     -24.866   5.626  20.308  1.00 26.48           C  
ANISOU  835  CB  ASP A 156     2406   3924   3732    762     32    304       C  
ATOM    836  CG  ASP A 156     -23.669   6.414  20.825  1.00 38.14           C  
ANISOU  836  CG  ASP A 156     4035   5194   5264    812     64    266       C  
ATOM    837  OD1 ASP A 156     -23.329   6.290  22.023  1.00 43.22           O  
ANISOU  837  OD1 ASP A 156     4734   5764   5922    799    110    201       O  
ATOM    838  OD2 ASP A 156     -23.074   7.173  20.026  1.00 36.76           O  
ANISOU  838  OD2 ASP A 156     3921   4936   5109    859     43    303       O  
ATOM    839  N   LYS A 157     -26.890   3.353  19.876  1.00 24.26           N  
ANISOU  839  N   LYS A 157     1863   4032   3323    533    -19    315       N  
ATOM    840  CA  LYS A 157     -28.170   2.982  19.263  1.00 21.52           C  
ANISOU  840  CA  LYS A 157     1348   3914   2916    497    -52    364       C  
ATOM    841  C   LYS A 157     -28.779   1.716  19.854  1.00 21.70           C  
ANISOU  841  C   LYS A 157     1311   4042   2892    342    -39    321       C  
ATOM    842  O   LYS A 157     -29.628   1.081  19.231  1.00 22.55           O  
ANISOU  842  O   LYS A 157     1301   4330   2936    245    -75    343       O  
ATOM    843  CB  LYS A 157     -27.999   2.812  17.749  1.00 29.07           C  
ANISOU  843  CB  LYS A 157     2290   4923   3831    440   -125    404       C  
ATOM    844  CG  LYS A 157     -27.699   4.107  17.025  1.00 34.30           C  
ANISOU  844  CG  LYS A 157     2977   5529   4525    598   -141    473       C  
ATOM    845  CD  LYS A 157     -28.068   4.014  15.552  1.00 44.32           C  
ANISOU  845  CD  LYS A 157     4165   6942   5732    562   -214    537       C  
ATOM    846  CE  LYS A 157     -26.827   3.981  14.667  1.00 45.77           C  
ANISOU  846  CE  LYS A 157     4480   6990   5919    510   -247    525       C  
ATOM    847  NZ  LYS A 157     -27.171   4.002  13.214  1.00 47.36           N  
ANISOU  847  NZ  LYS A 157     4606   7334   6053    487   -317    592       N  
ATOM    848  N   GLU A 158     -28.346   1.364  21.059  1.00 21.01           N  
ANISOU  848  N   GLU A 158     1305   3846   2830    313     14    260       N  
ATOM    849  CA  GLU A 158     -28.796   0.161  21.747  1.00 22.40           C  
ANISOU  849  CA  GLU A 158     1454   4091   2967    164     37    220       C  
ATOM    850  C   GLU A 158     -28.568  -1.118  20.938  1.00 26.36           C  
ANISOU  850  C   GLU A 158     1990   4607   3419    -30     -9    196       C  
ATOM    851  O   GLU A 158     -29.362  -2.060  21.009  1.00 21.61           O  
ANISOU  851  O   GLU A 158     1314   4133   2762   -168     -9    187       O  
ATOM    852  CB  GLU A 158     -30.259   0.285  22.148  1.00 26.90           C  
ANISOU  852  CB  GLU A 158     1845   4875   3502    194     60    256       C  
ATOM    853  CG  GLU A 158     -30.558   1.592  22.842  1.00 38.19           C  
ANISOU  853  CG  GLU A 158     3239   6296   4976    403    110    281       C  
ATOM    854  CD  GLU A 158     -32.042   1.835  22.974  1.00 50.50           C  
ANISOU  854  CD  GLU A 158     4597   8094   6496    461    127    331       C  
ATOM    855  OE1 GLU A 158     -32.735   0.960  23.534  1.00 51.40           O  
ANISOU  855  OE1 GLU A 158     4634   8333   6564    340    148    313       O  
ATOM    856  OE2 GLU A 158     -32.515   2.897  22.511  1.00 58.39           O  
ANISOU  856  OE2 GLU A 158     5553   9125   7507    617    118    385       O  
ATOM    857  N   MET A 159     -27.468  -1.151  20.195  1.00 24.62           N  
ANISOU  857  N   MET A 159     1888   4251   3215    -45    -42    181       N  
ATOM    858  CA  MET A 159     -27.083  -2.345  19.444  1.00 21.65           C  
ANISOU  858  CA  MET A 159     1573   3857   2795   -215    -76    146       C  
ATOM    859  C   MET A 159     -25.844  -2.968  20.070  1.00 19.28           C  
ANISOU  859  C   MET A 159     1443   3356   2526   -259    -47     87       C  
ATOM    860  O   MET A 159     -24.912  -3.359  19.366  1.00 21.07           O  
ANISOU  860  O   MET A 159     1771   3485   2750   -305    -71     63       O  
ATOM    861  CB  MET A 159     -26.827  -1.992  17.976  1.00 20.49           C  
ANISOU  861  CB  MET A 159     1419   3738   2629   -203   -138    177       C  
ATOM    862  CG  MET A 159     -28.048  -1.406  17.266  1.00 24.18           C  
ANISOU  862  CG  MET A 159     1711   4421   3055   -156   -175    246       C  
ATOM    863  SD  MET A 159     -27.604  -0.762  15.648  1.00 23.52           S  
ANISOU  863  SD  MET A 159     1633   4350   2952   -106   -243    296       S  
ATOM    864  CE  MET A 159     -29.124   0.055  15.171  1.00 23.13           C  
ANISOU  864  CE  MET A 159     1365   4562   2861     -8   -275    392       C  
ATOM    865  N   GLN A 160     -25.851  -3.074  21.401  1.00 21.38           N  
ANISOU  865  N   GLN A 160     1735   3575   2814   -241      8     66       N  
ATOM    866  CA  GLN A 160     -24.709  -3.585  22.160  1.00 25.16           C  
ANISOU  866  CA  GLN A 160     2363   3879   3319   -261     38     20       C  
ATOM    867  C   GLN A 160     -24.242  -4.958  21.682  1.00 22.05           C  
ANISOU  867  C   GLN A 160     2061   3427   2890   -415     25    -15       C  
ATOM    868  O   GLN A 160     -23.083  -5.334  21.871  1.00 21.30           O  
ANISOU  868  O   GLN A 160     2097   3183   2815   -415     35    -45       O  
ATOM    869  CB  GLN A 160     -25.045  -3.666  23.658  1.00 33.16           C  
ANISOU  869  CB  GLN A 160     3367   4892   4339   -245     97      9       C  
ATOM    870  CG  GLN A 160     -25.420  -2.343  24.302  1.00 35.33           C  
ANISOU  870  CG  GLN A 160     3574   5201   4648    -87    124     30       C  
ATOM    871  CD  GLN A 160     -26.919  -2.078  24.292  1.00 41.91           C  
ANISOU  871  CD  GLN A 160     4239   6232   5453    -72    132     67       C  
ATOM    872  OE1 GLN A 160     -27.655  -2.598  23.450  1.00 37.78           O  
ANISOU  872  OE1 GLN A 160     3631   5837   4885   -164     97     88       O  
ATOM    873  NE2 GLN A 160     -27.379  -1.265  25.240  1.00 47.46           N  
ANISOU  873  NE2 GLN A 160     4890   6969   6175     45    179     74       N  
ATOM    874  N   VAL A 161     -25.146  -5.705  21.063  1.00 20.12           N  
ANISOU  874  N   VAL A 161     1750   3303   2590   -544      6    -13       N  
ATOM    875  CA  VAL A 161     -24.816  -7.038  20.578  1.00 25.87           C  
ANISOU  875  CA  VAL A 161     2576   3973   3280   -699      0    -53       C  
ATOM    876  C   VAL A 161     -23.710  -6.995  19.518  1.00 25.70           C  
ANISOU  876  C   VAL A 161     2649   3851   3267   -677    -34    -71       C  
ATOM    877  O   VAL A 161     -23.012  -7.989  19.308  1.00 22.55           O  
ANISOU  877  O   VAL A 161     2372   3342   2853   -758    -25   -112       O  
ATOM    878  CB  VAL A 161     -26.066  -7.758  20.013  1.00 32.02           C  
ANISOU  878  CB  VAL A 161     3259   4918   3990   -858    -19    -53       C  
ATOM    879  CG1 VAL A 161     -26.485  -7.153  18.679  1.00 33.26           C  
ANISOU  879  CG1 VAL A 161     3313   5206   4116   -841    -80    -26       C  
ATOM    880  CG2 VAL A 161     -25.801  -9.243  19.853  1.00 37.60           C  
ANISOU  880  CG2 VAL A 161     4091   5538   4658  -1032     -4   -103       C  
ATOM    881  N   LEU A 162     -23.535  -5.845  18.869  1.00 21.84           N  
ANISOU  881  N   LEU A 162     2107   3393   2799   -561    -68    -38       N  
ATOM    882  CA  LEU A 162     -22.543  -5.718  17.791  1.00 16.57           C  
ANISOU  882  CA  LEU A 162     1512   2652   2132   -542   -101    -48       C  
ATOM    883  C   LEU A 162     -21.122  -5.595  18.312  1.00 21.51           C  
ANISOU  883  C   LEU A 162     2265   3103   2806   -465    -76    -70       C  
ATOM    884  O   LEU A 162     -20.158  -5.895  17.602  1.00 20.52           O  
ANISOU  884  O   LEU A 162     2225   2897   2674   -477    -88    -93       O  
ATOM    885  CB  LEU A 162     -22.853  -4.505  16.905  1.00 20.68           C  
ANISOU  885  CB  LEU A 162     1935   3268   2654   -447   -145      5       C  
ATOM    886  CG  LEU A 162     -24.119  -4.597  16.041  1.00 26.24           C  
ANISOU  886  CG  LEU A 162     2505   4169   3294   -519   -187     34       C  
ATOM    887  CD1 LEU A 162     -24.262  -3.363  15.155  1.00 18.30           C  
ANISOU  887  CD1 LEU A 162     1420   3241   2291   -404   -229     98       C  
ATOM    888  CD2 LEU A 162     -24.092  -5.857  15.194  1.00 30.64           C  
ANISOU  888  CD2 LEU A 162     3115   4742   3785   -690   -206    -16       C  
ATOM    889  N   VAL A 163     -20.988  -5.155  19.556  1.00 16.05           N  
ANISOU  889  N   VAL A 163     1579   2363   2157   -387    -39    -64       N  
ATOM    890  CA  VAL A 163     -19.668  -4.892  20.107  1.00 16.83           C  
ANISOU  890  CA  VAL A 163     1778   2320   2296   -311    -19    -80       C  
ATOM    891  C   VAL A 163     -18.763  -6.120  20.062  1.00 17.72           C  
ANISOU  891  C   VAL A 163     2014   2328   2391   -382     -5   -120       C  
ATOM    892  O   VAL A 163     -17.648  -6.047  19.553  1.00 13.25           O  
ANISOU  892  O   VAL A 163     1515   1685   1833   -347    -15   -132       O  
ATOM    893  CB  VAL A 163     -19.753  -4.310  21.527  1.00 18.49           C  
ANISOU  893  CB  VAL A 163     1974   2509   2542   -233     19    -75       C  
ATOM    894  CG1 VAL A 163     -18.372  -4.271  22.177  1.00 14.09           C  
ANISOU  894  CG1 VAL A 163     1522   1820   2011   -182     38    -97       C  
ATOM    895  CG2 VAL A 163     -20.359  -2.921  21.470  1.00 18.08           C  
ANISOU  895  CG2 VAL A 163     1827   2526   2516   -128     10    -38       C  
ATOM    896  N   SER A 164     -19.238  -7.254  20.565  1.00 14.25           N  
ANISOU  896  N   SER A 164     1605   1885   1925   -479     22   -138       N  
ATOM    897  CA  SER A 164     -18.399  -8.453  20.528  1.00 17.93           C  
ANISOU  897  CA  SER A 164     2201   2236   2374   -535     42   -172       C  
ATOM    898  C   SER A 164     -18.151  -8.953  19.100  1.00 15.61           C  
ANISOU  898  C   SER A 164     1946   1939   2045   -598     15   -197       C  
ATOM    899  O   SER A 164     -17.114  -9.571  18.828  1.00 16.74           O  
ANISOU  899  O   SER A 164     2197   1978   2184   -592     28   -224       O  
ATOM    900  CB  SER A 164     -19.003  -9.566  21.378  1.00 26.06           C  
ANISOU  900  CB  SER A 164     3269   3251   3381   -632     82   -180       C  
ATOM    901  OG  SER A 164     -20.205 -10.015  20.790  1.00 36.03           O  
ANISOU  901  OG  SER A 164     4471   4617   4601   -756     70   -185       O  
ATOM    902  N   ARG A 165     -19.109  -8.717  18.203  1.00 17.16           N  
ANISOU  902  N   ARG A 165     2052   2258   2211   -657    -20   -190       N  
ATOM    903  CA  ARG A 165     -18.971  -9.126  16.799  1.00 16.21           C  
ANISOU  903  CA  ARG A 165     1957   2156   2045   -725    -49   -216       C  
ATOM    904  C   ARG A 165     -17.875  -8.324  16.094  1.00 14.61           C  
ANISOU  904  C   ARG A 165     1774   1916   1863   -621    -72   -207       C  
ATOM    905  O   ARG A 165     -17.019  -8.892  15.417  1.00 17.44           O  
ANISOU  905  O   ARG A 165     2223   2204   2200   -638    -67   -242       O  
ATOM    906  CB  ARG A 165     -20.287  -8.968  16.041  1.00 17.66           C  
ANISOU  906  CB  ARG A 165     2022   2507   2182   -810    -88   -202       C  
ATOM    907  CG  ARG A 165     -21.407  -9.917  16.497  1.00 18.81           C  
ANISOU  907  CG  ARG A 165     2146   2710   2289   -953    -69   -219       C  
ATOM    908  CD  ARG A 165     -22.685  -9.646  15.701  1.00 18.26           C  
ANISOU  908  CD  ARG A 165     1934   2838   2166  -1030   -114   -199       C  
ATOM    909  NE  ARG A 165     -23.859 -10.286  16.292  1.00 19.24           N  
ANISOU  909  NE  ARG A 165     2000   3051   2258  -1155    -96   -202       N  
ATOM    910  CZ  ARG A 165     -25.109 -10.091  15.871  1.00 26.39           C  
ANISOU  910  CZ  ARG A 165     2758   4155   3114  -1227   -130   -179       C  
ATOM    911  NH1 ARG A 165     -25.364  -9.280  14.847  1.00 25.43           N  
ANISOU  911  NH1 ARG A 165     2535   4160   2969  -1178   -186   -147       N  
ATOM    912  NH2 ARG A 165     -26.106 -10.713  16.472  1.00 29.07           N  
ANISOU  912  NH2 ARG A 165     3047   4576   3423  -1348   -108   -183       N  
ATOM    913  N   ILE A 166     -17.914  -7.006  16.266  1.00 14.22           N  
ANISOU  913  N   ILE A 166     1642   1910   1851   -515    -90   -161       N  
ATOM    914  CA  ILE A 166     -16.894  -6.103  15.715  1.00 13.60           C  
ANISOU  914  CA  ILE A 166     1578   1795   1795   -420   -108   -144       C  
ATOM    915  C   ILE A 166     -15.484  -6.495  16.189  1.00 14.65           C  
ANISOU  915  C   ILE A 166     1822   1795   1950   -377    -76   -172       C  
ATOM    916  O   ILE A 166     -14.536  -6.520  15.395  1.00 14.01           O  
ANISOU  916  O   ILE A 166     1788   1679   1856   -360    -83   -185       O  
ATOM    917  CB  ILE A 166     -17.206  -4.633  16.101  1.00 18.00           C  
ANISOU  917  CB  ILE A 166     2049   2394   2396   -314   -120    -91       C  
ATOM    918  CG1 ILE A 166     -18.505  -4.171  15.445  1.00 18.76           C  
ANISOU  918  CG1 ILE A 166     2028   2636   2465   -332   -155    -51       C  
ATOM    919  CG2 ILE A 166     -16.074  -3.690  15.706  1.00 12.83           C  
ANISOU  919  CG2 ILE A 166     1424   1681   1768   -226   -129    -73       C  
ATOM    920  CD1 ILE A 166     -19.176  -3.027  16.189  1.00 21.39           C  
ANISOU  920  CD1 ILE A 166     2275   3011   2840   -233   -149     -4       C  
ATOM    921  N   ALA A 167     -15.352  -6.791  17.481  1.00 12.65           N  
ANISOU  921  N   ALA A 167     1601   1481   1724   -356    -41   -178       N  
ATOM    922  CA  ALA A 167     -14.072  -7.224  18.047  1.00 15.72           C  
ANISOU  922  CA  ALA A 167     2084   1761   2127   -310    -11   -197       C  
ATOM    923  C   ALA A 167     -13.561  -8.478  17.350  1.00 15.30           C  
ANISOU  923  C   ALA A 167     2127   1652   2035   -367      3   -237       C  
ATOM    924  O   ALA A 167     -12.377  -8.597  17.053  1.00 12.64           O  
ANISOU  924  O   ALA A 167     1846   1258   1696   -317     12   -249       O  
ATOM    925  CB  ALA A 167     -14.211  -7.486  19.543  1.00 12.73           C  
ANISOU  925  CB  ALA A 167     1722   1346   1769   -294     23   -192       C  
ATOM    926  N   ALA A 168     -14.459  -9.424  17.097  1.00 17.11           N  
ANISOU  926  N   ALA A 168     2375   1898   2229   -475     10   -259       N  
ATOM    927  CA  ALA A 168     -14.081 -10.652  16.416  1.00 18.70           C  
ANISOU  927  CA  ALA A 168     2684   2033   2390   -538     31   -306       C  
ATOM    928  C   ALA A 168     -13.707 -10.392  14.959  1.00 15.95           C  
ANISOU  928  C   ALA A 168     2328   1725   2008   -544      2   -324       C  
ATOM    929  O   ALA A 168     -12.755 -10.973  14.451  1.00 15.10           O  
ANISOU  929  O   ALA A 168     2307   1548   1881   -525     23   -356       O  
ATOM    930  CB  ALA A 168     -15.201 -11.703  16.508  1.00 20.96           C  
ANISOU  930  CB  ALA A 168     2998   2326   2641   -674     47   -330       C  
ATOM    931  N   TRP A 169     -14.453  -9.524  14.289  1.00 13.86           N  
ANISOU  931  N   TRP A 169     1957   1576   1732   -563    -43   -299       N  
ATOM    932  CA  TRP A 169     -14.144  -9.182  12.891  1.00 14.87           C  
ANISOU  932  CA  TRP A 169     2070   1758   1821   -569    -74   -305       C  
ATOM    933  C   TRP A 169     -12.767  -8.512  12.781  1.00 13.26           C  
ANISOU  933  C   TRP A 169     1886   1507   1645   -456    -69   -290       C  
ATOM    934  O   TRP A 169     -12.008  -8.768  11.841  1.00 13.38           O  
ANISOU  934  O   TRP A 169     1947   1510   1625   -455    -66   -316       O  
ATOM    935  CB  TRP A 169     -15.202  -8.231  12.327  1.00 14.30           C  
ANISOU  935  CB  TRP A 169     1870   1826   1735   -588   -125   -262       C  
ATOM    936  CG  TRP A 169     -16.615  -8.769  12.364  1.00 15.44           C  
ANISOU  936  CG  TRP A 169     1965   2056   1844   -703   -136   -270       C  
ATOM    937  CD1 TRP A 169     -16.996 -10.079  12.406  1.00 19.97           C  
ANISOU  937  CD1 TRP A 169     2611   2597   2379   -823   -111   -325       C  
ATOM    938  CD2 TRP A 169     -17.825  -8.000  12.383  1.00 16.96           C  
ANISOU  938  CD2 TRP A 169     2022   2386   2034   -709   -173   -221       C  
ATOM    939  NE1 TRP A 169     -18.370 -10.176  12.434  1.00 19.55           N  
ANISOU  939  NE1 TRP A 169     2470   2663   2297   -921   -133   -315       N  
ATOM    940  CE2 TRP A 169     -18.902  -8.914  12.420  1.00 23.04           C  
ANISOU  940  CE2 TRP A 169     2776   3219   2759   -845   -171   -249       C  
ATOM    941  CE3 TRP A 169     -18.104  -6.632  12.349  1.00 20.08           C  
ANISOU  941  CE3 TRP A 169     2314   2857   2460   -611   -203   -153       C  
ATOM    942  CZ2 TRP A 169     -20.233  -8.502  12.443  1.00 18.78           C  
ANISOU  942  CZ2 TRP A 169     2101   2835   2200   -882   -202   -211       C  
ATOM    943  CZ3 TRP A 169     -19.433  -6.226  12.369  1.00 20.29           C  
ANISOU  943  CZ3 TRP A 169     2215   3025   2471   -632   -231   -113       C  
ATOM    944  CH2 TRP A 169     -20.477  -7.158  12.418  1.00 20.85           C  
ANISOU  944  CH2 TRP A 169     2254   3175   2493   -765   -231   -141       C  
ATOM    945  N   MET A 170     -12.459  -7.653  13.744  1.00 12.95           N  
ANISOU  945  N   MET A 170     1810   1449   1663   -370    -66   -251       N  
ATOM    946  CA  MET A 170     -11.195  -6.914  13.762  1.00 12.71           C  
ANISOU  946  CA  MET A 170     1787   1386   1658   -277    -63   -233       C  
ATOM    947  C   MET A 170     -10.012  -7.833  14.041  1.00 14.64           C  
ANISOU  947  C   MET A 170     2125   1541   1895   -246    -23   -269       C  
ATOM    948  O   MET A 170      -8.957  -7.718  13.405  1.00 14.62           O  
ANISOU  948  O   MET A 170     2144   1534   1877   -206    -18   -275       O  
ATOM    949  CB  MET A 170     -11.231  -5.822  14.825  1.00 11.48           C  
ANISOU  949  CB  MET A 170     1576   1227   1557   -209    -67   -193       C  
ATOM    950  CG  MET A 170     -12.108  -4.619  14.471  1.00 11.61           C  
ANISOU  950  CG  MET A 170     1502   1322   1587   -198   -103   -147       C  
ATOM    951  SD  MET A 170     -12.202  -3.467  15.848  1.00 12.90           S  
ANISOU  951  SD  MET A 170     1626   1460   1815   -119    -93   -115       S  
ATOM    952  CE  MET A 170     -10.558  -2.743  15.775  1.00 12.70           C  
ANISOU  952  CE  MET A 170     1639   1381   1807    -58    -87   -111       C  
ATOM    953  N   ALA A 171     -10.189  -8.731  15.005  1.00 12.00           N  
ANISOU  953  N   ALA A 171     1845   1143   1570   -257      9   -285       N  
ATOM    954  CA  ALA A 171      -9.143  -9.695  15.366  1.00 14.23           C  
ANISOU  954  CA  ALA A 171     2224   1339   1846   -213     51   -309       C  
ATOM    955  C   ALA A 171      -8.832 -10.624  14.202  1.00 16.93           C  
ANISOU  955  C   ALA A 171     2640   1654   2136   -249     69   -357       C  
ATOM    956  O   ALA A 171      -7.670 -10.913  13.913  1.00 20.72           O  
ANISOU  956  O   ALA A 171     3167   2101   2604   -184     93   -371       O  
ATOM    957  CB  ALA A 171      -9.568 -10.500  16.596  1.00 20.03           C  
ANISOU  957  CB  ALA A 171     3007   2009   2595   -227     82   -308       C  
ATOM    958  N   THR A 172      -9.874 -11.084  13.522  1.00 16.58           N  
ANISOU  958  N   THR A 172     2605   1635   2057   -355     59   -385       N  
ATOM    959  CA  THR A 172      -9.692 -11.925  12.339  1.00 15.22           C  
ANISOU  959  CA  THR A 172     2510   1446   1828   -406     75   -440       C  
ATOM    960  C   THR A 172      -8.961 -11.183  11.213  1.00 14.28           C  
ANISOU  960  C   THR A 172     2347   1395   1683   -367     53   -437       C  
ATOM    961  O   THR A 172      -8.033 -11.721  10.604  1.00 14.37           O  
ANISOU  961  O   THR A 172     2426   1370   1663   -332     84   -473       O  
ATOM    962  CB  THR A 172     -11.047 -12.449  11.831  1.00 23.89           C  
ANISOU  962  CB  THR A 172     3610   2582   2884   -549     60   -472       C  
ATOM    963  OG1 THR A 172     -11.622 -13.300  12.830  1.00 21.94           O  
ANISOU  963  OG1 THR A 172     3422   2262   2652   -597     91   -479       O  
ATOM    964  CG2 THR A 172     -10.875 -13.243  10.542  1.00 27.87           C  
ANISOU  964  CG2 THR A 172     4195   3077   3319   -613     74   -539       C  
ATOM    965  N   TYR A 173      -9.380  -9.951  10.945  1.00 15.67           N  
ANISOU  965  N   TYR A 173     2414   1669   1873   -368      4   -391       N  
ATOM    966  CA  TYR A 173      -8.746  -9.141   9.910  1.00 20.30           C  
ANISOU  966  CA  TYR A 173     2956   2321   2434   -337    -18   -374       C  
ATOM    967  C   TYR A 173      -7.275  -8.893  10.237  1.00 19.72           C  
ANISOU  967  C   TYR A 173     2899   2209   2384   -232      9   -363       C  
ATOM    968  O   TYR A 173      -6.404  -8.989   9.365  1.00 16.89           O  
ANISOU  968  O   TYR A 173     2562   1869   1987   -209     23   -382       O  
ATOM    969  CB  TYR A 173      -9.475  -7.806   9.687  1.00 13.04           C  
ANISOU  969  CB  TYR A 173     1925   1498   1530   -344    -72   -313       C  
ATOM    970  CG  TYR A 173      -9.024  -7.149   8.399  1.00 16.48           C  
ANISOU  970  CG  TYR A 173     2330   2008   1924   -339    -94   -296       C  
ATOM    971  CD1 TYR A 173      -7.930  -6.288   8.379  1.00 17.79           C  
ANISOU  971  CD1 TYR A 173     2476   2173   2112   -264    -91   -261       C  
ATOM    972  CD2 TYR A 173      -9.657  -7.428   7.195  1.00 15.83           C  
ANISOU  972  CD2 TYR A 173     2241   2003   1770   -420   -118   -315       C  
ATOM    973  CE1 TYR A 173      -7.490  -5.709   7.188  1.00 16.30           C  
ANISOU  973  CE1 TYR A 173     2263   2053   1878   -267   -107   -240       C  
ATOM    974  CE2 TYR A 173      -9.220  -6.855   5.998  1.00 20.82           C  
ANISOU  974  CE2 TYR A 173     2848   2709   2354   -417   -137   -296       C  
ATOM    975  CZ  TYR A 173      -8.138  -6.000   6.010  1.00 15.23           C  
ANISOU  975  CZ  TYR A 173     2123   1992   1672   -339   -129   -256       C  
ATOM    976  OH  TYR A 173      -7.712  -5.428   4.838  1.00 23.48           O  
ANISOU  976  OH  TYR A 173     3144   3112   2666   -342   -144   -231       O  
ATOM    977  N   LEU A 174      -7.009  -8.578  11.497  1.00 15.97           N  
ANISOU  977  N   LEU A 174     2408   1695   1965   -174     16   -334       N  
ATOM    978  CA  LEU A 174      -5.643  -8.372  11.960  1.00 16.66           C  
ANISOU  978  CA  LEU A 174     2499   1761   2070    -82     39   -321       C  
ATOM    979  C   LEU A 174      -4.802  -9.634  11.741  1.00 18.41           C  
ANISOU  979  C   LEU A 174     2813   1925   2258    -44     89   -368       C  
ATOM    980  O   LEU A 174      -3.711  -9.568  11.160  1.00 17.81           O  
ANISOU  980  O   LEU A 174     2736   1876   2156      8    106   -374       O  
ATOM    981  CB  LEU A 174      -5.665  -7.935  13.431  1.00 22.18           C  
ANISOU  981  CB  LEU A 174     3170   2433   2825    -41     37   -289       C  
ATOM    982  CG  LEU A 174      -4.405  -7.493  14.174  1.00 28.27           C  
ANISOU  982  CG  LEU A 174     3921   3205   3616     41     48   -267       C  
ATOM    983  CD1 LEU A 174      -3.687  -6.373  13.444  1.00 20.52           C  
ANISOU  983  CD1 LEU A 174     2879   2289   2627     51     28   -244       C  
ATOM    984  CD2 LEU A 174      -4.800  -7.036  15.577  1.00 30.36           C  
ANISOU  984  CD2 LEU A 174     4157   3451   3926     54     40   -242       C  
ATOM    985  N   ASN A 175      -5.321 -10.782  12.174  1.00 15.16           N  
ANISOU  985  N   ASN A 175     2484   1435   1842    -70    118   -399       N  
ATOM    986  CA  ASN A 175      -4.623 -12.063  12.010  1.00 18.87           C  
ANISOU  986  CA  ASN A 175     3063   1825   2281    -27    174   -443       C  
ATOM    987  C   ASN A 175      -4.323 -12.416  10.556  1.00 21.41           C  
ANISOU  987  C   ASN A 175     3423   2171   2542    -50    189   -493       C  
ATOM    988  O   ASN A 175      -3.213 -12.843  10.222  1.00 20.55           O  
ANISOU  988  O   ASN A 175     3353   2047   2407     31    229   -512       O  
ATOM    989  CB  ASN A 175      -5.442 -13.214  12.612  1.00 19.32           C  
ANISOU  989  CB  ASN A 175     3218   1781   2341    -78    202   -468       C  
ATOM    990  CG  ASN A 175      -5.284 -13.332  14.111  1.00 28.29           C  
ANISOU  990  CG  ASN A 175     4359   2867   3522    -18    215   -426       C  
ATOM    991  OD1 ASN A 175      -4.655 -12.495  14.754  1.00 26.97           O  
ANISOU  991  OD1 ASN A 175     4115   2747   3384     53    197   -382       O  
ATOM    992  ND2 ASN A 175      -5.857 -14.392  14.678  1.00 37.23           N  
ANISOU  992  ND2 ASN A 175     5587   3903   4655    -55    248   -440       N  
ATOM    993  N   ASP A 176      -5.318 -12.258   9.689  1.00 14.78           N  
ANISOU  993  N   ASP A 176     2568   1378   1671   -158    158   -513       N  
ATOM    994  CA  ASP A 176      -5.191 -12.770   8.323  1.00 17.29           C  
ANISOU  994  CA  ASP A 176     2938   1715   1918   -199    175   -573       C  
ATOM    995  C   ASP A 176      -4.629 -11.765   7.330  1.00 22.20           C  
ANISOU  995  C   ASP A 176     3475   2449   2509   -182    148   -550       C  
ATOM    996  O   ASP A 176      -3.941 -12.145   6.383  1.00 24.36           O  
ANISOU  996  O   ASP A 176     3790   2739   2727   -162    178   -592       O  
ATOM    997  CB  ASP A 176      -6.535 -13.288   7.814  1.00 19.52           C  
ANISOU  997  CB  ASP A 176     3255   2000   2162   -340    157   -615       C  
ATOM    998  CG  ASP A 176      -6.997 -14.535   8.552  1.00 26.64           C  
ANISOU  998  CG  ASP A 176     4273   2775   3074   -377    200   -653       C  
ATOM    999  OD1 ASP A 176      -6.134 -15.294   9.056  1.00 29.11           O  
ANISOU  999  OD1 ASP A 176     4677   2984   3401   -286    257   -667       O  
ATOM   1000  OD2 ASP A 176      -8.222 -14.752   8.621  1.00 25.22           O  
ANISOU 1000  OD2 ASP A 176     4092   2606   2886   -496    177   -665       O  
ATOM   1001  N   HIS A 177      -4.923 -10.487   7.535  1.00 16.60           N  
ANISOU 1001  N   HIS A 177     2656   1816   1835   -188     95   -484       N  
ATOM   1002  CA  HIS A 177      -4.629  -9.501   6.503  1.00 15.68           C  
ANISOU 1002  CA  HIS A 177     2469   1805   1686   -195     65   -455       C  
ATOM   1003  C   HIS A 177      -3.625  -8.416   6.889  1.00 19.37           C  
ANISOU 1003  C   HIS A 177     2863   2307   2190   -117     59   -395       C  
ATOM   1004  O   HIS A 177      -3.038  -7.793   6.006  1.00 19.87           O  
ANISOU 1004  O   HIS A 177     2887   2444   2218   -113     53   -377       O  
ATOM   1005  CB  HIS A 177      -5.929  -8.875   5.979  1.00 17.08           C  
ANISOU 1005  CB  HIS A 177     2585   2056   1847   -288      7   -428       C  
ATOM   1006  CG  HIS A 177      -6.846  -9.863   5.327  1.00 26.07           C  
ANISOU 1006  CG  HIS A 177     3782   3197   2926   -388      8   -491       C  
ATOM   1007  ND1 HIS A 177      -6.467 -10.627   4.243  1.00 31.99           N  
ANISOU 1007  ND1 HIS A 177     4602   3956   3597   -418     38   -558       N  
ATOM   1008  CD2 HIS A 177      -8.122 -10.221   5.610  1.00 24.50           C  
ANISOU 1008  CD2 HIS A 177     3584   2998   2729   -475    -14   -502       C  
ATOM   1009  CE1 HIS A 177      -7.467 -11.413   3.888  1.00 33.10           C  
ANISOU 1009  CE1 HIS A 177     4790   4095   3693   -526     32   -611       C  
ATOM   1010  NE2 HIS A 177      -8.486 -11.182   4.699  1.00 30.11           N  
ANISOU 1010  NE2 HIS A 177     4364   3715   3361   -565     -1   -576       N  
ATOM   1011  N   LEU A 178      -3.421  -8.189   8.184  1.00 16.82           N  
ANISOU 1011  N   LEU A 178     2522   1936   1932    -66     61   -367       N  
ATOM   1012  CA  LEU A 178      -2.470  -7.163   8.625  1.00 15.82           C  
ANISOU 1012  CA  LEU A 178     2330   1844   1837     -9     55   -317       C  
ATOM   1013  C   LEU A 178      -1.158  -7.738   9.181  1.00 19.21           C  
ANISOU 1013  C   LEU A 178     2782   2251   2266     80    100   -332       C  
ATOM   1014  O   LEU A 178      -0.080  -7.184   8.967  1.00 17.97           O  
ANISOU 1014  O   LEU A 178     2577   2154   2096    118    108   -311       O  
ATOM   1015  CB  LEU A 178      -3.119  -6.214   9.648  1.00 11.84           C  
ANISOU 1015  CB  LEU A 178     1774   1327   1398    -19     19   -269       C  
ATOM   1016  CG  LEU A 178      -4.356  -5.472   9.125  1.00 16.19           C  
ANISOU 1016  CG  LEU A 178     2285   1916   1951    -84    -26   -239       C  
ATOM   1017  CD1 LEU A 178      -4.983  -4.595  10.211  1.00 14.24           C  
ANISOU 1017  CD1 LEU A 178     1995   1647   1769    -76    -50   -197       C  
ATOM   1018  CD2 LEU A 178      -3.986  -4.642   7.900  1.00 19.41           C  
ANISOU 1018  CD2 LEU A 178     2655   2400   2320   -101    -44   -208       C  
ATOM   1019  N   GLU A 179      -1.260  -8.846   9.902  1.00 20.42           N  
ANISOU 1019  N   GLU A 179     3005   2324   2430    114    132   -363       N  
ATOM   1020  CA  GLU A 179      -0.090  -9.492  10.497  1.00 21.44           C  
ANISOU 1020  CA  GLU A 179     3157   2431   2556    215    176   -369       C  
ATOM   1021  C   GLU A 179       1.071  -9.788   9.525  1.00 18.30           C  
ANISOU 1021  C   GLU A 179     2762   2089   2102    271    214   -392       C  
ATOM   1022  O   GLU A 179       2.242  -9.654   9.907  1.00 21.01           O  
ANISOU 1022  O   GLU A 179     3061   2479   2443    352    233   -371       O  
ATOM   1023  CB  GLU A 179      -0.513 -10.768  11.236  1.00 20.50           C  
ANISOU 1023  CB  GLU A 179     3136   2202   2449    239    209   -397       C  
ATOM   1024  CG  GLU A 179       0.608 -11.446  11.987  1.00 29.28           C  
ANISOU 1024  CG  GLU A 179     4275   3290   3561    360    252   -388       C  
ATOM   1025  CD  GLU A 179       1.026 -10.683  13.223  1.00 37.23           C  
ANISOU 1025  CD  GLU A 179     5202   4336   4607    397    227   -334       C  
ATOM   1026  OE1 GLU A 179       0.219  -9.889  13.746  1.00 40.01           O  
ANISOU 1026  OE1 GLU A 179     5513   4692   4997    330    184   -311       O  
ATOM   1027  OE2 GLU A 179       2.170 -10.882  13.680  1.00 47.06           O  
ANISOU 1027  OE2 GLU A 179     6425   5616   5841    495    250   -315       O  
ATOM   1028  N   PRO A 180       0.767 -10.200   8.276  1.00 23.41           N  
ANISOU 1028  N   PRO A 180     3455   2743   2697    227    227   -436       N  
ATOM   1029  CA  PRO A 180       1.910 -10.404   7.375  1.00 23.91           C  
ANISOU 1029  CA  PRO A 180     3511   2870   2702    285    268   -458       C  
ATOM   1030  C   PRO A 180       2.723  -9.131   7.150  1.00 23.20           C  
ANISOU 1030  C   PRO A 180     3306   2900   2609    286    244   -405       C  
ATOM   1031  O   PRO A 180       3.948  -9.191   7.244  1.00 19.18           O  
ANISOU 1031  O   PRO A 180     2759   2447   2080    367    277   -396       O  
ATOM   1032  CB  PRO A 180       1.252 -10.869   6.073  1.00 22.28           C  
ANISOU 1032  CB  PRO A 180     3368   2662   2436    212    276   -514       C  
ATOM   1033  CG  PRO A 180      -0.006 -11.526   6.514  1.00 23.40           C  
ANISOU 1033  CG  PRO A 180     3586   2702   2602    148    264   -541       C  
ATOM   1034  CD  PRO A 180      -0.484 -10.714   7.685  1.00 23.12           C  
ANISOU 1034  CD  PRO A 180     3485   2660   2640    134    217   -478       C  
ATOM   1035  N   TRP A 181       2.064  -8.005   6.883  1.00 15.19           N  
ANISOU 1035  N   TRP A 181     2237   1924   1610    198    191   -366       N  
ATOM   1036  CA  TRP A 181       2.777  -6.736   6.738  1.00 14.46           C  
ANISOU 1036  CA  TRP A 181     2051   1925   1520    184    170   -311       C  
ATOM   1037  C   TRP A 181       3.478  -6.355   8.037  1.00 18.31           C  
ANISOU 1037  C   TRP A 181     2488   2415   2054    234    167   -278       C  
ATOM   1038  O   TRP A 181       4.644  -5.952   8.032  1.00 18.08           O  
ANISOU 1038  O   TRP A 181     2395   2470   2005    265    182   -258       O  
ATOM   1039  CB  TRP A 181       1.825  -5.603   6.323  1.00 13.51           C  
ANISOU 1039  CB  TRP A 181     1899   1821   1415     91    115   -269       C  
ATOM   1040  CG  TRP A 181       2.547  -4.313   6.062  1.00 15.05           C  
ANISOU 1040  CG  TRP A 181     2017   2095   1607     66    100   -212       C  
ATOM   1041  CD1 TRP A 181       3.075  -3.892   4.870  1.00 14.47           C  
ANISOU 1041  CD1 TRP A 181     1916   2110   1473     38    109   -197       C  
ATOM   1042  CD2 TRP A 181       2.837  -3.282   7.015  1.00 15.06           C  
ANISOU 1042  CD2 TRP A 181     1968   2093   1662     58     79   -165       C  
ATOM   1043  NE1 TRP A 181       3.672  -2.660   5.026  1.00 14.69           N  
ANISOU 1043  NE1 TRP A 181     1881   2184   1518      8     95   -138       N  
ATOM   1044  CE2 TRP A 181       3.544  -2.267   6.333  1.00 13.98           C  
ANISOU 1044  CE2 TRP A 181     1779   2035   1497     17     76   -122       C  
ATOM   1045  CE3 TRP A 181       2.574  -3.121   8.379  1.00 12.30           C  
ANISOU 1045  CE3 TRP A 181     1616   1681   1376     74     64   -158       C  
ATOM   1046  CZ2 TRP A 181       3.979  -1.114   6.967  1.00 19.95           C  
ANISOU 1046  CZ2 TRP A 181     2491   2801   2290    -14     60    -77       C  
ATOM   1047  CZ3 TRP A 181       3.013  -1.971   9.011  1.00 16.18           C  
ANISOU 1047  CZ3 TRP A 181     2059   2188   1899     49     47   -118       C  
ATOM   1048  CH2 TRP A 181       3.706  -0.985   8.306  1.00 20.25           C  
ANISOU 1048  CH2 TRP A 181     2532   2774   2389      2     46    -80       C  
ATOM   1049  N   ILE A 182       2.763  -6.483   9.152  1.00 16.89           N  
ANISOU 1049  N   ILE A 182     2332   2156   1930    234    148   -274       N  
ATOM   1050  CA  ILE A 182       3.303  -6.099  10.459  1.00 15.79           C  
ANISOU 1050  CA  ILE A 182     2149   2022   1831    271    140   -245       C  
ATOM   1051  C   ILE A 182       4.600  -6.856  10.759  1.00 18.32           C  
ANISOU 1051  C   ILE A 182     2456   2386   2119    373    184   -254       C  
ATOM   1052  O   ILE A 182       5.598  -6.267  11.197  1.00 18.38           O  
ANISOU 1052  O   ILE A 182     2386   2477   2122    392    181   -225       O  
ATOM   1053  CB  ILE A 182       2.257  -6.337  11.577  1.00 14.75           C  
ANISOU 1053  CB  ILE A 182     2057   1796   1752    261    121   -245       C  
ATOM   1054  CG1 ILE A 182       1.098  -5.324  11.457  1.00 13.37           C  
ANISOU 1054  CG1 ILE A 182     1866   1601   1612    175     76   -223       C  
ATOM   1055  CG2 ILE A 182       2.895  -6.286  12.969  1.00 20.56           C  
ANISOU 1055  CG2 ILE A 182     2762   2537   2512    315    123   -226       C  
ATOM   1056  CD1 ILE A 182      -0.078  -5.624  12.378  1.00 14.98           C  
ANISOU 1056  CD1 ILE A 182     2107   1726   1860    160     63   -228       C  
ATOM   1057  N   GLN A 183       4.595  -8.160  10.501  1.00 18.12           N  
ANISOU 1057  N   GLN A 183     2507   2309   2069    437    226   -294       N  
ATOM   1058  CA  GLN A 183       5.787  -8.963  10.750  1.00 24.32           C  
ANISOU 1058  CA  GLN A 183     3286   3132   2822    558    274   -299       C  
ATOM   1059  C   GLN A 183       6.936  -8.586   9.814  1.00 25.54           C  
ANISOU 1059  C   GLN A 183     3367   3417   2922    578    296   -295       C  
ATOM   1060  O   GLN A 183       8.094  -8.586  10.215  1.00 24.75           O  
ANISOU 1060  O   GLN A 183     3195   3407   2800    654    315   -273       O  
ATOM   1061  CB  GLN A 183       5.473 -10.457  10.672  1.00 20.85           C  
ANISOU 1061  CB  GLN A 183     2967   2584   2371    626    323   -343       C  
ATOM   1062  CG  GLN A 183       4.851 -11.001  11.956  1.00 36.29           C  
ANISOU 1062  CG  GLN A 183     4979   4435   4372    647    317   -331       C  
ATOM   1063  CD  GLN A 183       5.517 -10.462  13.231  1.00 47.70           C  
ANISOU 1063  CD  GLN A 183     6340   5944   5840    692    294   -278       C  
ATOM   1064  OE1 GLN A 183       6.725 -10.616  13.434  1.00 53.17           O  
ANISOU 1064  OE1 GLN A 183     6978   6722   6503    788    317   -257       O  
ATOM   1065  NE2 GLN A 183       4.722  -9.821  14.089  1.00 42.34           N  
ANISOU 1065  NE2 GLN A 183     5646   5235   5208    620    249   -256       N  
ATOM   1066  N   GLU A 184       6.603  -8.245   8.575  1.00 21.83           N  
ANISOU 1066  N   GLU A 184     2905   2969   2422    507    293   -312       N  
ATOM   1067  CA  GLU A 184       7.609  -7.843   7.596  1.00 21.01           C  
ANISOU 1067  CA  GLU A 184     2732   2993   2259    512    316   -307       C  
ATOM   1068  C   GLU A 184       8.184  -6.467   7.918  1.00 18.98           C  
ANISOU 1068  C   GLU A 184     2362   2837   2014    450    279   -250       C  
ATOM   1069  O   GLU A 184       9.243  -6.098   7.419  1.00 20.05           O  
ANISOU 1069  O   GLU A 184     2418   3097   2102    457    300   -235       O  
ATOM   1070  CB  GLU A 184       7.004  -7.835   6.190  1.00 24.40           C  
ANISOU 1070  CB  GLU A 184     3205   3419   2646    443    319   -337       C  
ATOM   1071  CG  GLU A 184       7.478  -8.970   5.302  1.00 45.17           C  
ANISOU 1071  CG  GLU A 184     5892   6059   5209    521    386   -396       C  
ATOM   1072  CD  GLU A 184       8.974  -8.907   5.025  1.00 58.10           C  
ANISOU 1072  CD  GLU A 184     7443   7836   6795    601    431   -384       C  
ATOM   1073  OE1 GLU A 184       9.499  -7.795   4.795  1.00 63.59           O  
ANISOU 1073  OE1 GLU A 184     8036   8646   7478    541    407   -337       O  
ATOM   1074  OE2 GLU A 184       9.625  -9.971   5.044  1.00 62.65           O  
ANISOU 1074  OE2 GLU A 184     8054   8409   7343    726    492   -418       O  
ATOM   1075  N   ASN A 185       7.482  -5.702   8.749  1.00 16.24           N  
ANISOU 1075  N   ASN A 185     2009   2434   1727    383    229   -222       N  
ATOM   1076  CA  ASN A 185       7.898  -4.331   9.019  1.00 21.83           C  
ANISOU 1076  CA  ASN A 185     2635   3212   2449    305    196   -176       C  
ATOM   1077  C   ASN A 185       8.291  -4.056  10.466  1.00 25.45           C  
ANISOU 1077  C   ASN A 185     3049   3680   2941    323    178   -156       C  
ATOM   1078  O   ASN A 185       8.153  -2.940  10.959  1.00 24.94           O  
ANISOU 1078  O   ASN A 185     2954   3616   2908    242    142   -129       O  
ATOM   1079  CB  ASN A 185       6.847  -3.339   8.516  1.00 18.11           C  
ANISOU 1079  CB  ASN A 185     2189   2688   2005    197    156   -154       C  
ATOM   1080  CG  ASN A 185       6.837  -3.248   6.999  1.00 25.37           C  
ANISOU 1080  CG  ASN A 185     3114   3656   2869    161    169   -155       C  
ATOM   1081  OD1 ASN A 185       7.508  -2.392   6.419  1.00 19.35           O  
ANISOU 1081  OD1 ASN A 185     2295   2982   2076    108    171   -121       O  
ATOM   1082  ND2 ASN A 185       6.125  -4.166   6.349  1.00 18.35           N  
ANISOU 1082  ND2 ASN A 185     2297   2717   1960    182    183   -196       N  
ATOM   1083  N   GLY A 186       8.791  -5.087  11.132  1.00 24.07           N  
ANISOU 1083  N   GLY A 186     2877   3513   2756    432    204   -170       N  
ATOM   1084  CA  GLY A 186       9.392  -4.920  12.436  1.00 28.22           C  
ANISOU 1084  CA  GLY A 186     3345   4086   3292    460    190   -148       C  
ATOM   1085  C   GLY A 186       8.507  -5.270  13.610  1.00 25.43           C  
ANISOU 1085  C   GLY A 186     3052   3620   2990    477    170   -152       C  
ATOM   1086  O   GLY A 186       8.918  -5.096  14.749  1.00 27.13           O  
ANISOU 1086  O   GLY A 186     3224   3875   3210    494    154   -134       O  
ATOM   1087  N   GLY A 187       7.301  -5.767  13.345  1.00 24.23           N  
ANISOU 1087  N   GLY A 187     2997   3341   2868    467    170   -175       N  
ATOM   1088  CA  GLY A 187       6.386  -6.139  14.413  1.00 21.84           C  
ANISOU 1088  CA  GLY A 187     2752   2934   2611    476    155   -178       C  
ATOM   1089  C   GLY A 187       5.870  -4.958  15.217  1.00 17.75           C  
ANISOU 1089  C   GLY A 187     2206   2403   2135    389    110   -160       C  
ATOM   1090  O   GLY A 187       6.242  -3.807  14.961  1.00 20.26           O  
ANISOU 1090  O   GLY A 187     2467   2781   2451    318     91   -146       O  
ATOM   1091  N   TRP A 188       5.019  -5.238  16.199  1.00 18.28           N  
ANISOU 1091  N   TRP A 188     2320   2387   2239    394     99   -163       N  
ATOM   1092  CA  TRP A 188       4.447  -4.183  17.046  1.00 20.10           C  
ANISOU 1092  CA  TRP A 188     2534   2596   2508    323     64   -154       C  
ATOM   1093  C   TRP A 188       5.503  -3.426  17.848  1.00 16.97           C  
ANISOU 1093  C   TRP A 188     2059   2296   2093    310     50   -139       C  
ATOM   1094  O   TRP A 188       5.306  -2.271  18.205  1.00 15.37           O  
ANISOU 1094  O   TRP A 188     1837   2092   1912    232     26   -138       O  
ATOM   1095  CB  TRP A 188       3.368  -4.757  17.964  1.00 17.28           C  
ANISOU 1095  CB  TRP A 188     2238   2145   2184    338     63   -161       C  
ATOM   1096  CG  TRP A 188       2.084  -5.015  17.253  1.00 21.17           C  
ANISOU 1096  CG  TRP A 188     2790   2552   2701    301     62   -176       C  
ATOM   1097  CD1 TRP A 188       1.593  -6.223  16.838  1.00 22.96           C  
ANISOU 1097  CD1 TRP A 188     3086   2719   2920    331     87   -194       C  
ATOM   1098  CD2 TRP A 188       1.121  -4.034  16.864  1.00 17.49           C  
ANISOU 1098  CD2 TRP A 188     2320   2057   2268    226     37   -172       C  
ATOM   1099  NE1 TRP A 188       0.378  -6.047  16.221  1.00 20.34           N  
ANISOU 1099  NE1 TRP A 188     2782   2339   2608    266     73   -204       N  
ATOM   1100  CE2 TRP A 188       0.066  -4.713  16.225  1.00 19.64           C  
ANISOU 1100  CE2 TRP A 188     2645   2272   2545    210     42   -187       C  
ATOM   1101  CE3 TRP A 188       1.044  -2.647  17.004  1.00 22.64           C  
ANISOU 1101  CE3 TRP A 188     2934   2724   2943    171     12   -158       C  
ATOM   1102  CZ2 TRP A 188      -1.051  -4.050  15.723  1.00 17.02           C  
ANISOU 1102  CZ2 TRP A 188     2311   1918   2237    151     18   -180       C  
ATOM   1103  CZ3 TRP A 188      -0.064  -1.988  16.500  1.00 21.99           C  
ANISOU 1103  CZ3 TRP A 188     2865   2601   2891    123     -5   -150       C  
ATOM   1104  CH2 TRP A 188      -1.097  -2.695  15.872  1.00 20.51           C  
ANISOU 1104  CH2 TRP A 188     2713   2376   2704    118     -4   -158       C  
ATOM   1105  N   ASP A 189       6.635  -4.070  18.116  1.00 18.55           N  
ANISOU 1105  N   ASP A 189     2214   2585   2247    386     67   -129       N  
ATOM   1106  CA  ASP A 189       7.739  -3.389  18.787  1.00 20.11           C  
ANISOU 1106  CA  ASP A 189     2321   2906   2412    365     51   -115       C  
ATOM   1107  C   ASP A 189       8.233  -2.207  17.967  1.00 24.10           C  
ANISOU 1107  C   ASP A 189     2776   3474   2909    267     41   -114       C  
ATOM   1108  O   ASP A 189       8.624  -1.185  18.516  1.00 21.33           O  
ANISOU 1108  O   ASP A 189     2378   3173   2552    188     19   -113       O  
ATOM   1109  CB  ASP A 189       8.890  -4.353  19.059  1.00 29.20           C  
ANISOU 1109  CB  ASP A 189     3421   4163   3509    478     73    -97       C  
ATOM   1110  CG  ASP A 189       8.510  -5.437  20.046  1.00 41.88           C  
ANISOU 1110  CG  ASP A 189     5082   5711   5121    572     82    -86       C  
ATOM   1111  OD1 ASP A 189       7.468  -5.278  20.713  1.00 39.05           O  
ANISOU 1111  OD1 ASP A 189     4780   5255   4802    531     67    -96       O  
ATOM   1112  OD2 ASP A 189       9.243  -6.446  20.149  1.00 52.17           O  
ANISOU 1112  OD2 ASP A 189     6373   7064   6387    692    109    -66       O  
ATOM   1113  N   THR A 190       8.198  -2.345  16.648  1.00 20.66           N  
ANISOU 1113  N   THR A 190     2353   3030   2465    267     60   -114       N  
ATOM   1114  CA  THR A 190       8.565  -1.247  15.763  1.00 17.89           C  
ANISOU 1114  CA  THR A 190     1966   2727   2104    171     54   -104       C  
ATOM   1115  C   THR A 190       7.524  -0.121  15.799  1.00 18.76           C  
ANISOU 1115  C   THR A 190     2127   2732   2267     74     28   -104       C  
ATOM   1116  O   THR A 190       7.863   1.061  15.740  1.00 22.25           O  
ANISOU 1116  O   THR A 190     2545   3201   2710    -20     16    -93       O  
ATOM   1117  CB  THR A 190       8.788  -1.762  14.328  1.00 26.60           C  
ANISOU 1117  CB  THR A 190     3073   3858   3176    203     84   -104       C  
ATOM   1118  OG1 THR A 190       9.995  -2.531  14.304  1.00 30.84           O  
ANISOU 1118  OG1 THR A 190     3544   4516   3656    289    112   -101       O  
ATOM   1119  CG2 THR A 190       8.913  -0.612  13.343  1.00 29.59           C  
ANISOU 1119  CG2 THR A 190     3432   4264   3547     97     77    -85       C  
ATOM   1120  N   PHE A 191       6.255  -0.484  15.926  1.00 13.10           N  
ANISOU 1120  N   PHE A 191     1484   1899   1595     98     23   -114       N  
ATOM   1121  CA  PHE A 191       5.208   0.534  16.086  1.00 13.25           C  
ANISOU 1121  CA  PHE A 191     1546   1823   1665     29      1   -110       C  
ATOM   1122  C   PHE A 191       5.423   1.350  17.365  1.00 12.56           C  
ANISOU 1122  C   PHE A 191     1444   1738   1591    -16    -13   -119       C  
ATOM   1123  O   PHE A 191       5.245   2.572  17.376  1.00 16.59           O  
ANISOU 1123  O   PHE A 191     1968   2211   2123    -95    -23   -114       O  
ATOM   1124  CB  PHE A 191       3.828  -0.120  16.108  1.00 11.92           C  
ANISOU 1124  CB  PHE A 191     1443   1554   1533     68     -1   -120       C  
ATOM   1125  CG  PHE A 191       2.705   0.847  16.419  1.00 14.60           C  
ANISOU 1125  CG  PHE A 191     1817   1806   1924     21    -19   -114       C  
ATOM   1126  CD1 PHE A 191       2.204   1.692  15.438  1.00 18.99           C  
ANISOU 1126  CD1 PHE A 191     2388   2332   2494    -24    -28    -89       C  
ATOM   1127  CD2 PHE A 191       2.159   0.906  17.691  1.00 13.99           C  
ANISOU 1127  CD2 PHE A 191     1756   1683   1875     31    -25   -130       C  
ATOM   1128  CE1 PHE A 191       1.181   2.585  15.720  1.00 19.15           C  
ANISOU 1128  CE1 PHE A 191     2440   2274   2561    -48    -40    -78       C  
ATOM   1129  CE2 PHE A 191       1.131   1.800  17.980  1.00 22.92           C  
ANISOU 1129  CE2 PHE A 191     2918   2738   3051      2    -34   -127       C  
ATOM   1130  CZ  PHE A 191       0.643   2.636  16.992  1.00 16.01           C  
ANISOU 1130  CZ  PHE A 191     2058   1830   2194    -32    -41   -100       C  
ATOM   1131  N   VAL A 192       5.795   0.671  18.447  1.00 14.60           N  
ANISOU 1131  N   VAL A 192     1680   2035   1831     35    -13   -133       N  
ATOM   1132  CA  VAL A 192       6.010   1.357  19.721  1.00 13.77           C  
ANISOU 1132  CA  VAL A 192     1560   1945   1726     -9    -28   -148       C  
ATOM   1133  C   VAL A 192       7.141   2.369  19.548  1.00 16.16           C  
ANISOU 1133  C   VAL A 192     1806   2339   1995   -100    -33   -145       C  
ATOM   1134  O   VAL A 192       7.028   3.512  19.998  1.00 15.37           O  
ANISOU 1134  O   VAL A 192     1726   2203   1911   -189    -43   -159       O  
ATOM   1135  CB  VAL A 192       6.325   0.383  20.882  1.00 13.03           C  
ANISOU 1135  CB  VAL A 192     1445   1902   1606     66    -28   -154       C  
ATOM   1136  CG1 VAL A 192       6.661   1.162  22.171  1.00 16.23           C  
ANISOU 1136  CG1 VAL A 192     1826   2348   1995      6    -46   -173       C  
ATOM   1137  CG2 VAL A 192       5.143  -0.569  21.126  1.00 12.31           C  
ANISOU 1137  CG2 VAL A 192     1421   1710   1548    136    -19   -156       C  
ATOM   1138  N   GLU A 193       8.205   1.956  18.863  1.00 17.26           N  
ANISOU 1138  N   GLU A 193     1879   2592   2086    -82    -23   -128       N  
ATOM   1139  CA  GLU A 193       9.357   2.835  18.618  1.00 26.10           C  
ANISOU 1139  CA  GLU A 193     2932   3822   3164   -177    -25   -121       C  
ATOM   1140  C   GLU A 193       8.970   4.095  17.845  1.00 27.16           C  
ANISOU 1140  C   GLU A 193     3114   3875   3328   -284    -24   -112       C  
ATOM   1141  O   GLU A 193       9.524   5.169  18.082  1.00 30.47           O  
ANISOU 1141  O   GLU A 193     3519   4323   3734   -397    -29   -117       O  
ATOM   1142  CB  GLU A 193      10.466   2.084  17.877  1.00 35.12           C  
ANISOU 1142  CB  GLU A 193     3991   5106   4247   -123     -7   -101       C  
ATOM   1143  CG  GLU A 193      11.170   1.025  18.716  1.00 44.77           C  
ANISOU 1143  CG  GLU A 193     5149   6437   5426    -21     -6   -100       C  
ATOM   1144  CD  GLU A 193      12.135   0.165  17.905  1.00 57.74           C  
ANISOU 1144  CD  GLU A 193     6720   8205   7015     65     22    -79       C  
ATOM   1145  OE1 GLU A 193      12.177   0.313  16.665  1.00 60.62           O  
ANISOU 1145  OE1 GLU A 193     7091   8566   7377     44     41    -71       O  
ATOM   1146  OE2 GLU A 193      12.851  -0.666  18.507  1.00 64.41           O  
ANISOU 1146  OE2 GLU A 193     7502   9154   7817    161     27    -69       O  
ATOM   1147  N   LEU A 194       7.996   3.966  16.950  1.00 28.69           N  
ANISOU 1147  N   LEU A 194     3371   3969   3562   -252    -18    -96       N  
ATOM   1148  CA  LEU A 194       7.587   5.067  16.080  1.00 33.87           C  
ANISOU 1148  CA  LEU A 194     4076   4550   4244   -332    -16    -72       C  
ATOM   1149  C   LEU A 194       6.496   5.980  16.657  1.00 36.82           C  
ANISOU 1149  C   LEU A 194     4532   4780   4678   -364    -25    -81       C  
ATOM   1150  O   LEU A 194       6.590   7.200  16.540  1.00 43.71           O  
ANISOU 1150  O   LEU A 194     5440   5606   5563   -457    -22    -70       O  
ATOM   1151  CB  LEU A 194       7.133   4.529  14.714  1.00 32.59           C  
ANISOU 1151  CB  LEU A 194     3930   4374   4080   -282     -6    -45       C  
ATOM   1152  CG  LEU A 194       8.188   3.922  13.788  1.00 34.67           C  
ANISOU 1152  CG  LEU A 194     4125   4768   4281   -265     13    -32       C  
ATOM   1153  CD1 LEU A 194       7.540   3.242  12.584  1.00 28.46           C  
ANISOU 1153  CD1 LEU A 194     3370   3953   3491   -208     22    -20       C  
ATOM   1154  CD2 LEU A 194       9.194   4.985  13.334  1.00 34.95           C  
ANISOU 1154  CD2 LEU A 194     4118   4880   4280   -380     20     -7       C  
ATOM   1155  N   TYR A 195       5.461   5.396  17.261  1.00 30.92           N  
ANISOU 1155  N   TYR A 195     3820   3960   3967   -287    -31    -98       N  
ATOM   1156  CA  TYR A 195       4.284   6.162  17.692  1.00 36.68           C  
ANISOU 1156  CA  TYR A 195     4623   4558   4754   -295    -33   -103       C  
ATOM   1157  C   TYR A 195       4.146   6.263  19.205  1.00 40.68           C  
ANISOU 1157  C   TYR A 195     5141   5045   5270   -295    -36   -147       C  
ATOM   1158  O   TYR A 195       3.219   6.913  19.706  1.00 37.33           O  
ANISOU 1158  O   TYR A 195     4776   4518   4889   -295    -32   -160       O  
ATOM   1159  CB  TYR A 195       3.000   5.544  17.133  1.00 32.49           C  
ANISOU 1159  CB  TYR A 195     4124   3963   4256   -216    -36    -86       C  
ATOM   1160  CG  TYR A 195       2.815   5.710  15.645  1.00 28.46           C  
ANISOU 1160  CG  TYR A 195     3622   3452   3742   -224    -36    -41       C  
ATOM   1161  CD1 TYR A 195       3.479   4.885  14.748  1.00 25.20           C  
ANISOU 1161  CD1 TYR A 195     3165   3128   3282   -207    -32    -32       C  
ATOM   1162  CD2 TYR A 195       1.956   6.679  15.134  1.00 33.16           C  
ANISOU 1162  CD2 TYR A 195     4268   3959   4374   -240    -39     -6       C  
ATOM   1163  CE1 TYR A 195       3.308   5.029  13.375  1.00 29.43           C  
ANISOU 1163  CE1 TYR A 195     3707   3672   3802   -219    -32      7       C  
ATOM   1164  CE2 TYR A 195       1.776   6.830  13.762  1.00 31.60           C  
ANISOU 1164  CE2 TYR A 195     4074   3771   4161   -246    -42     43       C  
ATOM   1165  CZ  TYR A 195       2.450   5.998  12.891  1.00 27.89           C  
ANISOU 1165  CZ  TYR A 195     3559   3397   3639   -241    -39     47       C  
ATOM   1166  OH  TYR A 195       2.276   6.145  11.536  1.00 31.34           O  
ANISOU 1166  OH  TYR A 195     4002   3854   4054   -251    -42     92       O  
ATOM   1167  N   GLY A 196       5.058   5.609  19.924  1.00 41.85           N  
ANISOU 1167  N   GLY A 196     5230   5298   5372   -287    -41   -169       N  
ATOM   1168  CA  GLY A 196       5.041   5.609  21.377  1.00 46.62           C  
ANISOU 1168  CA  GLY A 196     5835   5909   5968   -288    -46   -208       C  
ATOM   1169  C   GLY A 196       5.794   6.778  21.982  1.00 47.22           C  
ANISOU 1169  C   GLY A 196     5912   6008   6021   -403    -48   -238       C  
ATOM   1170  O   GLY A 196       5.418   7.275  23.044  1.00 52.34           O  
ANISOU 1170  O   GLY A 196     6599   6608   6678   -428    -47   -277       O  
TER    1171      GLY A 196                                                      
HETATM 1172  C   ACE B 146     -15.460   5.520  -0.030  1.00 51.05           C  
ANISOU 1172  C   ACE B 146     5961   7374   6062     40   -572    797       C  
HETATM 1173  O   ACE B 146     -14.424   5.442   0.624  1.00 47.58           O  
ANISOU 1173  O   ACE B 146     5604   6790   5684     27   -524    736       O  
HETATM 1174  CH3 ACE B 146     -15.935   4.416  -0.936  1.00 52.96           C  
ANISOU 1174  CH3 ACE B 146     6148   7785   6190    -69   -614    749       C  
ATOM   1175  N   TRP B 147     -16.354   6.413   0.371  1.00 50.69           N  
ANISOU 1175  N   TRP B 147     5865   7334   6062    150   -583    886       N  
ATOM   1176  CA  TRP B 147     -16.418   7.751   0.942  1.00 49.02           C  
ANISOU 1176  CA  TRP B 147     5682   7007   5936    281   -558    975       C  
ATOM   1177  C   TRP B 147     -15.834   7.785   2.354  1.00 38.14           C  
ANISOU 1177  C   TRP B 147     4375   5448   4666    297   -499    896       C  
ATOM   1178  O   TRP B 147     -14.863   8.489   2.618  1.00 31.78           O  
ANISOU 1178  O   TRP B 147     3663   4500   3914    317   -461    906       O  
ATOM   1179  CB  TRP B 147     -17.863   8.239   0.959  1.00 64.87           C  
ANISOU 1179  CB  TRP B 147     7583   9127   7937    383   -591   1066       C  
ATOM   1180  CG  TRP B 147     -17.991   9.715   1.106  1.00 77.89           C  
ANISOU 1180  CG  TRP B 147     9267  10682   9646    533   -572   1187       C  
ATOM   1181  CD1 TRP B 147     -18.207  10.618   0.109  1.00 84.24           C  
ANISOU 1181  CD1 TRP B 147    10062  11541  10404    607   -599   1325       C  
ATOM   1182  CD2 TRP B 147     -17.910  10.469   2.323  1.00 84.32           C  
ANISOU 1182  CD2 TRP B 147    10142  11323  10574    627   -517   1181       C  
ATOM   1183  NE1 TRP B 147     -18.271  11.889   0.627  1.00 88.53           N  
ANISOU 1183  NE1 TRP B 147    10665  11942  11031    746   -561   1407       N  
ATOM   1184  CE2 TRP B 147     -18.088  11.826   1.984  1.00 89.04           C  
ANISOU 1184  CE2 TRP B 147    10774  11865  11193    758   -509   1315       C  
ATOM   1185  CE3 TRP B 147     -17.708  10.130   3.666  1.00 85.45           C  
ANISOU 1185  CE3 TRP B 147    10318  11352  10797    614   -471   1075       C  
ATOM   1186  CZ2 TRP B 147     -18.068  12.844   2.938  1.00 90.18           C  
ANISOU 1186  CZ2 TRP B 147    10993  11834  11438    872   -454   1337       C  
ATOM   1187  CZ3 TRP B 147     -17.687  11.142   4.612  1.00 86.33           C  
ANISOU 1187  CZ3 TRP B 147    10493  11306  11002    723   -421   1097       C  
ATOM   1188  CH2 TRP B 147     -17.867  12.482   4.243  1.00 88.58           C  
ANISOU 1188  CH2 TRP B 147    10819  11529  11308    848   -411   1222       C  
ATOM   1189  N   ILE B 148     -16.444   7.034   3.266  1.00 34.40           N  
ANISOU 1189  N   ILE B 148     3857   4991   4220    280   -492    819       N  
ATOM   1190  CA  ILE B 148     -15.919   6.893   4.619  1.00 28.80           C  
ANISOU 1190  CA  ILE B 148     3209   4134   3599    282   -441    736       C  
ATOM   1191  C   ILE B 148     -14.484   6.395   4.563  1.00 24.76           C  
ANISOU 1191  C   ILE B 148     2786   3537   3085    196   -415    661       C  
ATOM   1192  O   ILE B 148     -13.589   6.918   5.239  1.00 23.93           O  
ANISOU 1192  O   ILE B 148     2757   3293   3043    216   -374    643       O  
ATOM   1193  CB  ILE B 148     -16.760   5.882   5.443  1.00 29.28           C  
ANISOU 1193  CB  ILE B 148     3206   4252   3666    247   -441    660       C  
ATOM   1194  CG1 ILE B 148     -18.163   6.429   5.705  1.00 41.52           C  
ANISOU 1194  CG1 ILE B 148     4658   5889   5228    344   -457    731       C  
ATOM   1195  CG2 ILE B 148     -16.097   5.566   6.764  1.00 30.16           C  
ANISOU 1195  CG2 ILE B 148     3385   4223   3851    233   -390    570       C  
ATOM   1196  CD1 ILE B 148     -18.971   5.578   6.662  1.00 40.59           C  
ANISOU 1196  CD1 ILE B 148     4479   5819   5124    312   -448    661       C  
ATOM   1197  N   ALA B 149     -14.261   5.379   3.739  1.00 23.10           N  
ANISOU 1197  N   ALA B 149     2563   3418   2795    100   -437    615       N  
ATOM   1198  CA  ALA B 149     -12.950   4.756   3.665  1.00 21.85           C  
ANISOU 1198  CA  ALA B 149     2478   3198   2626     27   -409    538       C  
ATOM   1199  C   ALA B 149     -11.926   5.684   3.020  1.00 24.27           C  
ANISOU 1199  C   ALA B 149     2839   3454   2927     41   -398    598       C  
ATOM   1200  O   ALA B 149     -10.769   5.725   3.438  1.00 21.46           O  
ANISOU 1200  O   ALA B 149     2547   3003   2604     21   -360    557       O  
ATOM   1201  CB  ALA B 149     -13.042   3.453   2.917  1.00 25.92           C  
ANISOU 1201  CB  ALA B 149     2974   3819   3054    -72   -429    471       C  
ATOM   1202  N   GLN B 150     -12.356   6.435   2.011  1.00 23.17           N  
ANISOU 1202  N   GLN B 150     2672   3389   2741     72   -430    702       N  
ATOM   1203  CA  GLN B 150     -11.489   7.431   1.382  1.00 24.18           C  
ANISOU 1203  CA  GLN B 150     2856   3468   2863     85   -417    776       C  
ATOM   1204  C   GLN B 150     -10.995   8.451   2.399  1.00 25.24           C  
ANISOU 1204  C   GLN B 150     3057   3437   3097    141   -375    794       C  
ATOM   1205  O   GLN B 150      -9.807   8.758   2.444  1.00 27.46           O  
ANISOU 1205  O   GLN B 150     3401   3639   3392    103   -343    780       O  
ATOM   1206  CB  GLN B 150     -12.220   8.158   0.248  1.00 38.65           C  
ANISOU 1206  CB  GLN B 150     4648   5403   4634    128   -460    903       C  
ATOM   1207  CG  GLN B 150     -11.595   7.958  -1.122  1.00 53.44           C  
ANISOU 1207  CG  GLN B 150     6529   7371   6405     58   -476    926       C  
ATOM   1208  CD  GLN B 150     -12.127   6.726  -1.833  1.00 63.56           C  
ANISOU 1208  CD  GLN B 150     7746   8814   7588    -16   -514    867       C  
ATOM   1209  OE1 GLN B 150     -13.313   6.650  -2.161  1.00 69.46           O  
ANISOU 1209  OE1 GLN B 150     8415   9682   8294      6   -560    909       O  
ATOM   1210  NE2 GLN B 150     -11.251   5.753  -2.075  1.00 62.20           N  
ANISOU 1210  NE2 GLN B 150     7608   8652   7375   -105   -493    766       N  
ATOM   1211  N   GLU B 151     -11.905   8.977   3.216  1.00 25.75           N  
ANISOU 1211  N   GLU B 151     3104   3455   3226    227   -372    821       N  
ATOM   1212  CA  GLU B 151     -11.529  10.002   4.188  1.00 28.16           C  
ANISOU 1212  CA  GLU B 151     3481   3599   3621    281   -328    833       C  
ATOM   1213  C   GLU B 151     -10.673   9.404   5.307  1.00 23.14           C  
ANISOU 1213  C   GLU B 151     2882   2880   3031    226   -292    716       C  
ATOM   1214  O   GLU B 151      -9.712  10.026   5.778  1.00 20.41           O  
ANISOU 1214  O   GLU B 151     2608   2420   2726    209   -256    704       O  
ATOM   1215  CB  GLU B 151     -12.764  10.693   4.760  1.00 38.47           C  
ANISOU 1215  CB  GLU B 151     4758   4882   4976    398   -329    888       C  
ATOM   1216  CG  GLU B 151     -12.447  11.940   5.573  1.00 52.01           C  
ANISOU 1216  CG  GLU B 151     6565   6422   6776    463   -281    913       C  
ATOM   1217  CD  GLU B 151     -13.665  12.830   5.783  1.00 59.06           C  
ANISOU 1217  CD  GLU B 151     7438   7297   7704    603   -279    998       C  
ATOM   1218  OE1 GLU B 151     -14.797  12.298   5.839  1.00 59.77           O  
ANISOU 1218  OE1 GLU B 151     7428   7508   7775    649   -307   1001       O  
ATOM   1219  OE2 GLU B 151     -13.487  14.064   5.884  1.00 61.78           O  
ANISOU 1219  OE2 GLU B 151     7870   7510   8093    669   -246   1064       O  
ATOM   1220  N   LEU B 152     -11.019   8.187   5.708  1.00 16.78           N  
ANISOU 1220  N   LEU B 152     2026   2137   2211    193   -302    633       N  
ATOM   1221  CA  LEU B 152     -10.265   7.444   6.705  1.00 20.98           C  
ANISOU 1221  CA  LEU B 152     2585   2611   2773    147   -272    528       C  
ATOM   1222  C   LEU B 152      -8.849   7.166   6.208  1.00 22.03           C  
ANISOU 1222  C   LEU B 152     2760   2740   2872     73   -258    497       C  
ATOM   1223  O   LEU B 152      -7.883   7.282   6.959  1.00 14.23           O  
ANISOU 1223  O   LEU B 152     1815   1673   1920     53   -226    453       O  
ATOM   1224  CB  LEU B 152     -10.964   6.122   6.992  1.00 24.88           C  
ANISOU 1224  CB  LEU B 152     3025   3183   3245    120   -287    459       C  
ATOM   1225  CG  LEU B 152     -10.561   5.392   8.269  1.00 27.67           C  
ANISOU 1225  CG  LEU B 152     3401   3473   3640    100   -256    365       C  
ATOM   1226  CD1 LEU B 152     -10.829   6.280   9.473  1.00 23.16           C  
ANISOU 1226  CD1 LEU B 152     2849   2806   3145    166   -230    373       C  
ATOM   1227  CD2 LEU B 152     -11.334   4.075   8.375  1.00 26.07           C  
ANISOU 1227  CD2 LEU B 152     3153   3347   3406     63   -270    310       C  
ATOM   1228  N   ARG B 153      -8.750   6.801   4.932  1.00 17.76           N  
ANISOU 1228  N   ARG B 153     2198   2296   2254     34   -282    523       N  
ATOM   1229  CA  ARG B 153      -7.482   6.496   4.293  1.00 18.19           C  
ANISOU 1229  CA  ARG B 153     2279   2371   2261    -30   -266    498       C  
ATOM   1230  C   ARG B 153      -6.606   7.741   4.212  1.00 16.65           C  
ANISOU 1230  C   ARG B 153     2135   2101   2090    -33   -244    558       C  
ATOM   1231  O   ARG B 153      -5.405   7.683   4.472  1.00 14.92           O  
ANISOU 1231  O   ARG B 153     1943   1852   1874    -77   -214    518       O  
ATOM   1232  CB  ARG B 153      -7.724   5.939   2.888  1.00 25.17           C  
ANISOU 1232  CB  ARG B 153     3131   3384   3049    -67   -296    518       C  
ATOM   1233  CG  ARG B 153      -6.512   5.264   2.273  1.00 37.15           C  
ANISOU 1233  CG  ARG B 153     4666   4941   4507   -130   -275    467       C  
ATOM   1234  CD  ARG B 153      -6.386   5.587   0.783  1.00 39.97           C  
ANISOU 1234  CD  ARG B 153     5015   5395   4777   -159   -293    534       C  
ATOM   1235  NE  ARG B 153      -7.555   5.180   0.005  1.00 31.32           N  
ANISOU 1235  NE  ARG B 153     3874   4408   3619   -162   -338    555       N  
ATOM   1236  CZ  ARG B 153      -7.725   3.961  -0.492  1.00 44.33           C  
ANISOU 1236  CZ  ARG B 153     5505   6141   5197   -211   -347    481       C  
ATOM   1237  NH1 ARG B 153      -6.809   3.021  -0.280  1.00 51.56           N  
ANISOU 1237  NH1 ARG B 153     6452   7034   6103   -245   -310    384       N  
ATOM   1238  NH2 ARG B 153      -8.813   3.675  -1.190  1.00 45.40           N  
ANISOU 1238  NH2 ARG B 153     5595   6386   5270   -227   -391    502       N  
ATOM   1239  N   GLU B 154      -7.219   8.868   3.871  1.00 17.04           N  
ANISOU 1239  N   GLU B 154     2198   2122   2154     14   -255    656       N  
ATOM   1240  CA  GLU B 154      -6.489  10.125   3.731  1.00 23.31           C  
ANISOU 1240  CA  GLU B 154     3057   2831   2970      5   -231    723       C  
ATOM   1241  C   GLU B 154      -5.870  10.548   5.056  1.00 20.52           C  
ANISOU 1241  C   GLU B 154     2754   2352   2693     -3   -193    669       C  
ATOM   1242  O   GLU B 154      -4.696  10.900   5.106  1.00 17.76           O  
ANISOU 1242  O   GLU B 154     2442   1966   2340    -67   -166    658       O  
ATOM   1243  CB  GLU B 154      -7.409  11.234   3.212  1.00 22.51           C  
ANISOU 1243  CB  GLU B 154     2971   2707   2876     77   -247    843       C  
ATOM   1244  CG  GLU B 154      -6.673  12.494   2.743  1.00 21.66           C  
ANISOU 1244  CG  GLU B 154     2942   2518   2771     55   -223    930       C  
ATOM   1245  CD  GLU B 154      -6.273  13.421   3.875  1.00 22.89           C  
ANISOU 1245  CD  GLU B 154     3179   2506   3012     61   -179    913       C  
ATOM   1246  OE1 GLU B 154      -7.087  13.733   4.738  1.00 22.82           O  
ANISOU 1246  OE1 GLU B 154     3181   2424   3066    139   -173    905       O  
ATOM   1247  N   ILE B 155      -6.650  10.523   6.136  1.00 17.18           N  
ANISOU 1247  N   ILE B 155     2326   1874   2330     56   -189    634       N  
ATOM   1248  CA  ILE B 155      -6.089  10.929   7.423  1.00 15.52           C  
ANISOU 1248  CA  ILE B 155     2164   1552   2183     45   -154    578       C  
ATOM   1249  C   ILE B 155      -5.117   9.882   7.981  1.00 14.62           C  
ANISOU 1249  C   ILE B 155     2026   1475   2052    -18   -143    478       C  
ATOM   1250  O   ILE B 155      -4.147  10.230   8.645  1.00 14.96           O  
ANISOU 1250  O   ILE B 155     2104   1464   2117    -64   -117    443       O  
ATOM   1251  CB  ILE B 155      -7.155  11.373   8.473  1.00 16.42           C  
ANISOU 1251  CB  ILE B 155     2290   1587   2364    131   -144    573       C  
ATOM   1252  CG1 ILE B 155      -8.251  10.329   8.653  1.00 15.21           C  
ANISOU 1252  CG1 ILE B 155     2057   1522   2201    175   -170    541       C  
ATOM   1253  CG2 ILE B 155      -7.784  12.716   8.080  1.00 21.75           C  
ANISOU 1253  CG2 ILE B 155     3016   2184   3065    200   -137    676       C  
ATOM   1254  CD1 ILE B 155      -9.247  10.716   9.761  1.00 15.71           C  
ANISOU 1254  CD1 ILE B 155     2122   1522   2325    258   -155    530       C  
ATOM   1255  N   GLY B 156      -5.355   8.608   7.692  1.00 14.42           N  
ANISOU 1255  N   GLY B 156     1944   1547   1987    -21   -163    436       N  
ATOM   1256  CA  GLY B 156      -4.403   7.575   8.066  1.00 13.42           C  
ANISOU 1256  CA  GLY B 156     1802   1459   1840    -65   -150    354       C  
ATOM   1257  C   GLY B 156      -3.042   7.806   7.420  1.00 15.89           C  
ANISOU 1257  C   GLY B 156     2126   1802   2111   -130   -134    364       C  
ATOM   1258  O   GLY B 156      -1.994   7.630   8.052  1.00 13.37           O  
ANISOU 1258  O   GLY B 156     1807   1477   1794   -164   -112    315       O  
ATOM   1259  N   ASP B 157      -3.052   8.195   6.150  1.00 14.66           N  
ANISOU 1259  N   ASP B 157     1971   1692   1909   -147   -145    433       N  
ATOM   1260  CA  ASP B 157      -1.809   8.463   5.421  1.00 15.88           C  
ANISOU 1260  CA  ASP B 157     2129   1889   2014   -214   -127    452       C  
ATOM   1261  C   ASP B 157      -1.104   9.727   5.918  1.00 15.79           C  
ANISOU 1261  C   ASP B 157     2169   1790   2042   -257   -102    482       C  
ATOM   1262  O   ASP B 157       0.132   9.781   5.986  1.00 15.14           O  
ANISOU 1262  O   ASP B 157     2080   1734   1937   -323    -79    460       O  
ATOM   1263  CB  ASP B 157      -2.076   8.546   3.916  1.00 15.25           C  
ANISOU 1263  CB  ASP B 157     2040   1889   1867   -223   -145    522       C  
ATOM   1264  CG  ASP B 157      -2.369   7.187   3.310  1.00 14.96           C  
ANISOU 1264  CG  ASP B 157     1958   1957   1768   -215   -161    472       C  
ATOM   1265  OD1 ASP B 157      -2.127   6.161   3.990  1.00 14.30           O  
ANISOU 1265  OD1 ASP B 157     1858   1880   1694   -206   -150    385       O  
ATOM   1266  OD2 ASP B 157      -2.848   7.138   2.161  1.00 17.24           O  
ANISOU 1266  OD2 ASP B 157     2234   2320   1998   -218   -183    519       O  
ATOM   1267  N   LYS B 158      -1.892  10.743   6.256  1.00 15.47           N  
ANISOU 1267  N   LYS B 158     2179   1645   2055   -221   -104    532       N  
ATOM   1268  CA  LYS B 158      -1.342  11.946   6.874  1.00 15.98           C  
ANISOU 1268  CA  LYS B 158     2311   1599   2163   -264    -75    548       C  
ATOM   1269  C   LYS B 158      -0.656  11.603   8.190  1.00 16.76           C  
ANISOU 1269  C   LYS B 158     2400   1678   2289   -295    -58    453       C  
ATOM   1270  O   LYS B 158       0.463  12.055   8.444  1.00 16.90           O  
ANISOU 1270  O   LYS B 158     2435   1690   2298   -379    -36    438       O  
ATOM   1271  CB  LYS B 158      -2.432  13.001   7.094  1.00 19.20           C  
ANISOU 1271  CB  LYS B 158     2783   1885   2628   -197    -74    609       C  
ATOM   1272  CG  LYS B 158      -2.945  13.620   5.799  1.00 23.96           C  
ANISOU 1272  CG  LYS B 158     3406   2497   3199   -171    -88    724       C  
ATOM   1273  CD  LYS B 158      -4.130  14.556   6.047  1.00 27.78           C  
ANISOU 1273  CD  LYS B 158     3945   2871   3740    -74    -86    789       C  
ATOM   1274  CE  LYS B 158      -4.683  15.114   4.732  1.00 25.74           C  
ANISOU 1274  CE  LYS B 158     3698   2638   3442    -34   -104    916       C  
ATOM   1275  NZ  LYS B 158      -5.101  14.056   3.791  1.00 30.12           N  
ANISOU 1275  NZ  LYS B 158     4159   3358   3927    -20   -147    923       N  
ATOM   1276  N   PHE B 159      -1.329  10.802   9.014  1.00 14.66           N  
ANISOU 1276  N   PHE B 159     2104   1416   2051   -232    -69    394       N  
ATOM   1277  CA  PHE B 159      -0.810  10.385  10.318  1.00 14.12           C  
ANISOU 1277  CA  PHE B 159     2024   1339   2003   -247    -57    308       C  
ATOM   1278  C   PHE B 159       0.470   9.583  10.098  1.00 18.04           C  
ANISOU 1278  C   PHE B 159     2466   1945   2444   -301    -52    270       C  
ATOM   1279  O   PHE B 159       1.484   9.795  10.769  1.00 17.35           O  
ANISOU 1279  O   PHE B 159     2375   1867   2353   -360    -36    234       O  
ATOM   1280  CB  PHE B 159      -1.858   9.508  11.017  1.00 14.62           C  
ANISOU 1280  CB  PHE B 159     2059   1403   2092   -167    -71    265       C  
ATOM   1281  CG  PHE B 159      -1.584   9.255  12.476  1.00 16.81           C  
ANISOU 1281  CG  PHE B 159     2336   1654   2397   -168    -58    191       C  
ATOM   1282  CD1 PHE B 159      -1.466  10.305  13.365  1.00 22.63           C  
ANISOU 1282  CD1 PHE B 159     3129   2296   3173   -191    -38    178       C  
ATOM   1283  CD2 PHE B 159      -1.490   7.966  12.964  1.00 22.59           C  
ANISOU 1283  CD2 PHE B 159     3021   2451   3112   -146    -65    134       C  
ATOM   1284  CE1 PHE B 159      -1.231  10.075  14.711  1.00 24.29           C  
ANISOU 1284  CE1 PHE B 159     3338   2495   3398   -196    -28    108       C  
ATOM   1285  CE2 PHE B 159      -1.261   7.730  14.312  1.00 26.70           C  
ANISOU 1285  CE2 PHE B 159     3540   2954   3650   -143    -55     75       C  
ATOM   1286  CZ  PHE B 159      -1.123   8.783  15.182  1.00 24.74           C  
ANISOU 1286  CZ  PHE B 159     3338   2630   3434   -170    -39     61       C  
ATOM   1287  N   ASN B 160       0.417   8.658   9.146  1.00 14.00           N  
ANISOU 1287  N   ASN B 160     1910   1524   1884   -280    -64    277       N  
ATOM   1288  CA  ASN B 160       1.593   7.855   8.815  1.00 17.50           C  
ANISOU 1288  CA  ASN B 160     2302   2076   2270   -312    -53    245       C  
ATOM   1289  C   ASN B 160       2.781   8.700   8.362  1.00 17.03           C  
ANISOU 1289  C   ASN B 160     2242   2049   2178   -402    -33    278       C  
ATOM   1290  O   ASN B 160       3.921   8.476   8.790  1.00 18.63           O  
ANISOU 1290  O   ASN B 160     2406   2317   2357   -442    -17    241       O  
ATOM   1291  CB  ASN B 160       1.265   6.840   7.726  1.00 17.12           C  
ANISOU 1291  CB  ASN B 160     2225   2109   2171   -278    -63    247       C  
ATOM   1292  CG  ASN B 160       2.403   5.888   7.481  1.00 16.87           C  
ANISOU 1292  CG  ASN B 160     2145   2182   2083   -286    -44    204       C  
ATOM   1293  OD1 ASN B 160       2.727   5.078   8.350  1.00 18.89           O  
ANISOU 1293  OD1 ASN B 160     2381   2450   2348   -253    -36    145       O  
ATOM   1294  ND2 ASN B 160       3.021   5.972   6.299  1.00 16.83           N  
ANISOU 1294  ND2 ASN B 160     2123   2257   2016   -323    -33    236       N  
ATOM   1295  N   ALA B 161       2.506   9.666   7.491  1.00 14.92           N  
ANISOU 1295  N   ALA B 161     2017   1744   1907   -433    -34    354       N  
ATOM   1296  CA  ALA B 161       3.550  10.513   6.925  1.00 23.70           C  
ANISOU 1296  CA  ALA B 161     3138   2884   2984   -530    -13    397       C  
ATOM   1297  C   ALA B 161       4.272  11.304   8.016  1.00 21.04           C  
ANISOU 1297  C   ALA B 161     2825   2490   2678   -605      5    368       C  
ATOM   1298  O   ALA B 161       5.477  11.529   7.943  1.00 21.35           O  
ANISOU 1298  O   ALA B 161     2834   2601   2678   -694     24    364       O  
ATOM   1299  CB  ALA B 161       2.964  11.449   5.884  1.00 23.33           C  
ANISOU 1299  CB  ALA B 161     3148   2785   2933   -540    -16    494       C  
ATOM   1300  N   TYR B 162       3.527  11.720   9.029  1.00 17.67           N  
ANISOU 1300  N   TYR B 162     2452   1946   2317   -571      1    346       N  
ATOM   1301  CA  TYR B 162       4.103  12.486  10.136  1.00 19.42           C  
ANISOU 1301  CA  TYR B 162     2708   2106   2565   -646     18    308       C  
ATOM   1302  C   TYR B 162       5.091  11.663  10.965  1.00 19.13           C  
ANISOU 1302  C   TYR B 162     2590   2180   2497   -669     18    232       C  
ATOM   1303  O   TYR B 162       6.190  12.128  11.287  1.00 19.89           O  
ANISOU 1303  O   TYR B 162     2670   2320   2567   -773     32    215       O  
ATOM   1304  CB  TYR B 162       2.994  13.016  11.048  1.00 16.79           C  
ANISOU 1304  CB  TYR B 162     2449   1627   2303   -588     17    293       C  
ATOM   1305  CG  TYR B 162       3.497  13.967  12.101  1.00 19.61           C  
ANISOU 1305  CG  TYR B 162     2865   1901   2684   -673     39    253       C  
ATOM   1306  CD1 TYR B 162       3.721  15.305  11.801  1.00 18.92           C  
ANISOU 1306  CD1 TYR B 162     2871   1709   2608   -758     65    299       C  
ATOM   1307  CD2 TYR B 162       3.773  13.523  13.391  1.00 21.09           C  
ANISOU 1307  CD2 TYR B 162     3022   2115   2876   -676     36    169       C  
ATOM   1308  CE1 TYR B 162       4.182  16.178  12.759  1.00 26.83           C  
ANISOU 1308  CE1 TYR B 162     3939   2628   3626   -850     88    253       C  
ATOM   1309  CE2 TYR B 162       4.235  14.394  14.355  1.00 16.95           C  
ANISOU 1309  CE2 TYR B 162     2553   1524   2364   -765     55    124       C  
ATOM   1310  CZ  TYR B 162       4.432  15.712  14.037  1.00 22.94           C  
ANISOU 1310  CZ  TYR B 162     3408   2174   3133   -855     82    161       C  
ATOM   1311  OH  TYR B 162       4.897  16.576  15.000  1.00 29.42           O  
ANISOU 1311  OH  TYR B 162     4295   2922   3960   -958    104    107       O  
ATOM   1312  N   TYR B 163       4.705  10.438  11.304  1.00 16.67           N  
ANISOU 1312  N   TYR B 163     2228   1920   2187   -574      2    189       N  
ATOM   1313  CA  TYR B 163       5.510   9.621  12.215  1.00 15.81           C  
ANISOU 1313  CA  TYR B 163     2050   1904   2054   -571      1    125       C  
ATOM   1314  C   TYR B 163       6.452   8.637  11.532  1.00 26.69           C  
ANISOU 1314  C   TYR B 163     3340   3435   3365   -559      7    122       C  
ATOM   1315  O   TYR B 163       7.571   8.419  11.998  1.00 23.17           O  
ANISOU 1315  O   TYR B 163     2830   3093   2882   -597     14     93       O  
ATOM   1316  CB  TYR B 163       4.611   8.871  13.195  1.00 14.40           C  
ANISOU 1316  CB  TYR B 163     1877   1680   1914   -476    -12     79       C  
ATOM   1317  CG  TYR B 163       4.140   9.742  14.330  1.00 23.78           C  
ANISOU 1317  CG  TYR B 163     3128   2757   3152   -498    -10     53       C  
ATOM   1318  CD1 TYR B 163       5.036  10.190  15.297  1.00 22.13           C  
ANISOU 1318  CD1 TYR B 163     2910   2571   2927   -577     -3     11       C  
ATOM   1319  CD2 TYR B 163       2.802  10.118  14.445  1.00 22.78           C  
ANISOU 1319  CD2 TYR B 163     3065   2509   3080   -439    -12     68       C  
ATOM   1320  CE1 TYR B 163       4.623  10.996  16.341  1.00 22.07           C  
ANISOU 1320  CE1 TYR B 163     2969   2460   2958   -603      4    -23       C  
ATOM   1321  CE2 TYR B 163       2.374  10.924  15.501  1.00 26.46           C  
ANISOU 1321  CE2 TYR B 163     3594   2871   3589   -450     -2     39       C  
ATOM   1322  CZ  TYR B 163       3.290  11.356  16.445  1.00 26.00           C  
ANISOU 1322  CZ  TYR B 163     3538   2828   3514   -534      8    -10       C  
ATOM   1323  OH  TYR B 163       2.887  12.149  17.499  1.00 26.69           O  
ANISOU 1323  OH  TYR B 163     3695   2812   3636   -551     22    -50       O  
ATOM   1324  N   ALA B 164       6.000   8.039  10.436  1.00 21.62           N  
ANISOU 1324  N   ALA B 164     2693   2817   2705   -503      5    149       N  
ATOM   1325  CA  ALA B 164       6.780   6.984   9.798  1.00 28.92           C  
ANISOU 1325  CA  ALA B 164     3545   3877   3567   -471     17    136       C  
ATOM   1326  C   ALA B 164       7.413   7.430   8.488  1.00 34.91           C  
ANISOU 1326  C   ALA B 164     4285   4708   4271   -535     33    187       C  
ATOM   1327  O   ALA B 164       7.105   8.502   7.973  1.00 32.87           O  
ANISOU 1327  O   ALA B 164     4080   4385   4026   -598     32    241       O  
ATOM   1328  CB  ALA B 164       5.921   5.744   9.583  1.00 28.25           C  
ANISOU 1328  CB  ALA B 164     3467   3779   3487   -364      8    112       C  
HETATM 1329  N   NH2 B 165       8.250   6.579   7.904  1.00 41.80           N  
ANISOU 1329  N   NH2 B 165     5089   5714   5080   -510     52    173       N  
TER    1330      NH2 B 165                                                      
HETATM 1331  C1  GOL A1197      -3.524  -1.979  29.640  1.00 56.09           C  
ANISOU 1331  C1  GOL A1197     7239   6861   7212    195     51   -229       C  
HETATM 1332  O1  GOL A1197      -2.721  -3.108  29.927  1.00 58.31           O  
ANISOU 1332  O1  GOL A1197     7526   7178   7450    235     50   -197       O  
HETATM 1333  C2  GOL A1197      -2.661  -0.789  29.223  1.00 54.09           C  
ANISOU 1333  C2  GOL A1197     6961   6629   6963    164     32   -254       C  
HETATM 1334  O2  GOL A1197      -3.478   0.314  28.893  1.00 58.45           O  
ANISOU 1334  O2  GOL A1197     7520   7128   7559    136     38   -278       O  
HETATM 1335  C3  GOL A1197      -1.754  -0.379  30.375  1.00 49.15           C  
ANISOU 1335  C3  GOL A1197     6317   6075   6284    149     23   -275       C  
HETATM 1336  O3  GOL A1197      -1.227   0.902  30.116  1.00 42.06           O  
ANISOU 1336  O3  GOL A1197     5408   5181   5393     96     12   -308       O  
HETATM 1337  O   HOH A2001     -13.830 -20.796  36.065  1.00 43.24           O  
ANISOU 1337  O   HOH A2001     6818   4344   5268   -430    675    388       O  
HETATM 1338  O   HOH A2002     -10.722 -20.855  38.653  1.00 38.71           O  
ANISOU 1338  O   HOH A2002     6299   3818   4590     -8    656    580       O  
HETATM 1339  O   HOH A2003     -12.232 -24.519  37.577  1.00 48.77           O  
ANISOU 1339  O   HOH A2003     6504   5544   6481   -336     34   -268       O  
HETATM 1340  O   HOH A2004      -2.661 -14.335  43.955  1.00 36.61           O  
ANISOU 1340  O   HOH A2004     5450   3844   4616   -303    206   -407       O  
HETATM 1341  O   HOH A2005     -10.742 -19.234  36.798  1.00 42.07           O  
ANISOU 1341  O   HOH A2005     6544   4331   5108    -28    578    417       O  
HETATM 1342  O   HOH A2006     -12.497 -10.163  42.679  1.00 33.55           O  
ANISOU 1342  O   HOH A2006     4639   4245   3864     20    469    124       O  
HETATM 1343  O   HOH A2007      -4.903 -12.860  43.375  1.00 39.70           O  
ANISOU 1343  O   HOH A2007     5595   5056   4433    490    300    423       O  
HETATM 1344  O   HOH A2008       2.728   6.526  41.173  1.00 26.60           O  
ANISOU 1344  O   HOH A2008     3456   3882   2769   -478    -24   -830       O  
HETATM 1345  O   HOH A2009       0.923   8.827  29.524  1.00 43.92           O  
ANISOU 1345  O   HOH A2009     5810   5208   5671   -341     33   -533       O  
HETATM 1346  O   HOH A2010      10.664  -1.893  33.409  1.00 49.55           O  
ANISOU 1346  O   HOH A2010     5675   7487   5665    260   -198    -89       O  
HETATM 1347  O   HOH A2011     -11.927  -8.704  41.036  1.00 42.95           O  
ANISOU 1347  O   HOH A2011     5762   5397   5159     62    408     24       O  
HETATM 1348  O   HOH A2012      -1.571 -11.937  35.724  1.00 39.32           O  
ANISOU 1348  O   HOH A2012     5459   4758   4722    639    193    221       O  
HETATM 1349  O   HOH A2013       0.266 -12.990  42.097  1.00 42.41           O  
ANISOU 1349  O   HOH A2013     5970   4741   5403   -451    148   -332       O  
HETATM 1350  O   HOH A2014      -4.732  -6.993  33.804  1.00 28.54           O  
ANISOU 1350  O   HOH A2014     3897   3387   3559    304    145    -71       O  
HETATM 1351  O   HOH A2015      -8.221  -8.868  32.616  1.00 42.09           O  
ANISOU 1351  O   HOH A2015     5712   4926   5355    171    220    -49       O  
HETATM 1352  O   HOH A2016      -6.091  -4.906  31.686  1.00 33.80           O  
ANISOU 1352  O   HOH A2016     4499   3992   4350    217    126   -163       O  
HETATM 1353  O   HOH A2017      -6.980  -0.725  37.341  1.00 23.27           O  
ANISOU 1353  O   HOH A2017     3108   2863   2869    162    188   -355       O  
HETATM 1354  O   HOH A2018       2.724  -0.532  31.522  1.00 17.30           O  
ANISOU 1354  O   HOH A2018     2130   2391   2053    141    -48   -254       O  
HETATM 1355  O   HOH A2019      -1.297  -5.175  30.646  1.00 40.22           O  
ANISOU 1355  O   HOH A2019     5257   4950   5077    339     56   -125       O  
HETATM 1356  O   HOH A2020      -3.055   9.341  32.352  1.00 44.37           O  
ANISOU 1356  O   HOH A2020     6002   5072   5786   -151    146   -643       O  
HETATM 1357  O   HOH A2021       2.551   6.929  38.095  1.00 25.18           O  
ANISOU 1357  O   HOH A2021     3301   3463   2803   -439    -14   -758       O  
HETATM 1358  O   HOH A2022      -0.204   7.096  30.557  1.00 30.81           O  
ANISOU 1358  O   HOH A2022     4104   3604   3997   -205     34   -513       O  
HETATM 1359  O   HOH A2023       1.399   9.235  37.638  1.00 51.09           O  
ANISOU 1359  O   HOH A2023     6757   6465   6191   -519     61   -878       O  
HETATM 1360  O   HOH A2024       1.517   9.804  40.643  1.00 44.02           O  
ANISOU 1360  O   HOH A2024     5904   5720   5103   -629     81  -1039       O  
HETATM 1361  O   HOH A2025       3.865   2.533  28.313  1.00 37.22           O  
ANISOU 1361  O   HOH A2025     4628   4851   4664    -66    -63   -309       O  
HETATM 1362  O   HOH A2026       9.981   0.085  31.760  1.00 33.82           O  
ANISOU 1362  O   HOH A2026     3755   5301   3794     50   -179   -195       O  
HETATM 1363  O   HOH A2027       8.793  -3.779  29.162  1.00 42.31           O  
ANISOU 1363  O   HOH A2027     4979   6085   5011    462    -80    -48       O  
HETATM 1364  O   HOH A2028       7.077  -8.527  32.542  1.00 42.23           O  
ANISOU 1364  O   HOH A2028     5222   5889   4934    869     -8    162       O  
HETATM 1365  O   HOH A2029       7.358  -6.294  35.124  1.00 44.98           O  
ANISOU 1365  O   HOH A2029     5431   6499   5160    665    -94     96       O  
HETATM 1366  O   HOH A2030       1.639 -10.063  32.290  1.00 34.06           O  
ANISOU 1366  O   HOH A2030     4584   4247   4109    712    107    113       O  
HETATM 1367  O   HOH A2031       4.659  -8.813  26.809  1.00 43.59           O  
ANISOU 1367  O   HOH A2031     5624   5562   5378    746     90     10       O  
HETATM 1368  O   HOH A2032       2.814  -7.494  21.481  1.00 50.72           O  
ANISOU 1368  O   HOH A2032     6591   6267   6412    515    102   -128       O  
HETATM 1369  O   HOH A2033       2.207   0.613  29.092  1.00 23.58           O  
ANISOU 1369  O   HOH A2033     2955   3045   2960     79    -39   -272       O  
HETATM 1370  O   HOH A2034       4.062   2.437  24.961  1.00 20.89           O  
ANISOU 1370  O   HOH A2034     2554   2718   2664    -53    -54   -247       O  
HETATM 1371  O   HOH A2035       1.648  18.986  10.517  1.00 47.51           O  
ANISOU 1371  O   HOH A2035     6865   4835   6350   -702    134    529       O  
HETATM 1372  O   HOH A2036      -1.374  16.994   5.013  1.00 37.39           O  
ANISOU 1372  O   HOH A2036     5354   3937   4917   -336     -5    908       O  
HETATM 1373  O   HOH A2037      -4.666   4.368  29.101  1.00 23.81           O  
ANISOU 1373  O   HOH A2037     3191   2596   3259     73     71   -373       O  
HETATM 1374  O   HOH A2038     -23.482 -10.345  11.519  1.00 37.64           O  
ANISOU 1374  O   HOH A2038     4320   5583   4397  -1313   -251   -265       O  
HETATM 1375  O   HOH A2039      -2.347  10.553  22.661  1.00 19.48           O  
ANISOU 1375  O   HOH A2039     2833   1710   2861   -147     55   -237       O  
HETATM 1376  O   HOH A2040     -14.387 -12.188  10.200  1.00 35.00           O  
ANISOU 1376  O   HOH A2040     5232   2958   5110   1154     95   1087       O  
HETATM 1377  O   HOH A2041     -10.977 -10.853   7.627  1.00 24.89           O  
ANISOU 1377  O   HOH A2041     3594   3013   2849   -627    -47   -487       O  
HETATM 1378  O   HOH A2042      -8.581  12.202  21.099  1.00 30.96           O  
ANISOU 1378  O   HOH A2042     4324   2937   4504    295    114    -47       O  
HETATM 1379  O   HOH A2043      -3.611   9.709  25.007  1.00 22.70           O  
ANISOU 1379  O   HOH A2043     3223   2140   3263    -59     79   -323       O  
HETATM 1380  O   HOH A2044      -8.322  -5.451  -1.790  1.00 50.45           O  
ANISOU 1380  O   HOH A2044     6516   7034   5619   -603   -241   -244       O  
HETATM 1381  O  AHOH A2045       1.400   8.333  18.283  0.48 16.13           O  
ANISOU 1381  O  AHOH A2045     2199   1640   2289   -280    -22    -94       O  
HETATM 1382  O  BHOH A2045       0.823   9.070  19.794  0.52 21.40           O  
ANISOU 1382  O  BHOH A2045     2923   2218   2990   -282     -7   -145       O  
HETATM 1383  O   HOH A2046      -4.260   7.034  -1.293  1.00 43.22           O  
ANISOU 1383  O   HOH A2046     5473   5875   5073   -241   -259    666       O  
HETATM 1384  O   HOH A2047     -10.442  10.402  21.306  1.00 41.49           O  
ANISOU 1384  O   HOH A2047     5502   4439   5824    388     91    -33       O  
HETATM 1385  O   HOH A2048     -12.438   5.349  17.948  1.00 17.88           O  
ANISOU 1385  O   HOH A2048     2398   2714   1683   -315     38   -790       O  
HETATM 1386  O   HOH A2049      10.308   1.125  10.430  1.00 40.88           O  
ANISOU 1386  O   HOH A2049     4773   5879   4880    -81    107    -25       O  
HETATM 1387  O   HOH A2050      -0.436  18.121  10.726  1.00 28.22           O  
ANISOU 1387  O   HOH A2050     4368   2393   3961   -448     99    537       O  
HETATM 1388  O   HOH A2051      -2.520  17.668   7.267  1.00 36.25           O  
ANISOU 1388  O   HOH A2051     5816   3757   4198     21    445   -787       O  
HETATM 1389  O   HOH A2052      -9.735  16.871  10.401  1.00 37.44           O  
ANISOU 1389  O   HOH A2052     5274   3675   5275    504     -6    780       O  
HETATM 1390  O   HOH A2053      -0.906  16.277   8.898  1.00 24.82           O  
ANISOU 1390  O   HOH A2053     3752   2231   3447   -361     29    606       O  
HETATM 1391  O   HOH A2054     -16.662   7.847  18.012  1.00 33.16           O  
ANISOU 1391  O   HOH A2054     3973   3925   4699    601    -27    227       O  
HETATM 1392  O   HOH A2055     -10.182  19.344  12.862  1.00 39.59           O  
ANISOU 1392  O   HOH A2055     5792   3567   5685    621    121    692       O  
HETATM 1393  O   HOH A2056     -31.937  -6.160  22.917  1.00 47.80           O  
ANISOU 1393  O   HOH A2056     4494   7778   5891   -794     84    110       O  
HETATM 1394  O   HOH A2057     -30.386  -6.843  20.162  1.00 33.39           O  
ANISOU 1394  O   HOH A2057     4314   4069   4306   -733    -10   -206       O  
HETATM 1395  O   HOH A2058     -16.729 -13.583  20.034  1.00 41.55           O  
ANISOU 1395  O   HOH A2058     5700   4822   5267   -802    158   -293       O  
HETATM 1396  O   HOH A2059      -6.578 -16.001   5.133  1.00 49.94           O  
ANISOU 1396  O   HOH A2059     7405   5756   5813   -502    259   -850       O  
HETATM 1397  O   HOH A2060      -0.032  -6.820   2.733  1.00 40.29           O  
ANISOU 1397  O   HOH A2060     5401   5288   4618    -68    108   -366       O  
HETATM 1398  O   HOH A2061     -24.126  -8.515  12.833  1.00 36.86           O  
ANISOU 1398  O   HOH A2061     4032   5580   4395  -1086   -254   -144       O  
HETATM 1399  O   HOH A2062     -24.200  -7.611   9.666  1.00 24.15           O  
ANISOU 1399  O   HOH A2062     2311   4216   2651  -1098   -384   -103       O  
HETATM 1400  O   HOH A2063     -23.935  -7.082   6.769  1.00 24.19           O  
ANISOU 1400  O   HOH A2063     2267   4414   2508  -1132   -491    -78       O  
HETATM 1401  O   HOH A2064     -12.621  -9.909   9.556  1.00 19.92           O  
ANISOU 1401  O   HOH A2064     2824   2424   2320   -625    -86   -395       O  
HETATM 1402  O   HOH A2065     -14.563  -2.141  -0.257  1.00 34.57           O  
ANISOU 1402  O   HOH A2065     4049   5354   3733   -566   -503    134       O  
HETATM 1403  O   HOH A2066      -7.962  -4.611   0.794  1.00 28.29           O  
ANISOU 1403  O   HOH A2066     3688   4030   3032   -463   -217   -180       O  
HETATM 1404  O   HOH A2067      -8.640  -6.262   2.734  1.00 24.74           O  
ANISOU 1404  O   HOH A2067     3316   3415   2670   -480   -176   -283       O  
HETATM 1405  O   HOH A2068     -15.426  -4.957  -0.314  1.00 50.20           O  
ANISOU 1405  O   HOH A2068     6100   7368   5605   -815   -485    -86       O  
HETATM 1406  O   HOH A2069     -12.586  -1.810  -1.642  1.00 34.47           O  
ANISOU 1406  O   HOH A2069     4130   5313   3653   -549   -470    135       O  
HETATM 1407  O   HOH A2070      -6.156  -4.728  -3.369  1.00 23.70           O  
ANISOU 1407  O   HOH A2070     3145   3723   2137   -548   -192   -214       O  
HETATM 1408  O   HOH A2071      -0.655   3.208  -2.201  1.00 32.29           O  
ANISOU 1408  O   HOH A2071     4075   4697   3496   -348   -128    336       O  
HETATM 1409  O   HOH A2072      -2.371   5.452  -1.482  1.00 40.91           O  
ANISOU 1409  O   HOH A2072     5177   5656   4711   -310   -198    514       O  
HETATM 1410  O   HOH A2073       1.112  -3.231   1.743  1.00 23.65           O  
ANISOU 1410  O   HOH A2073     3104   3375   2506   -125     47   -161       O  
HETATM 1411  O   HOH A2074       4.048   2.720   8.100  1.00 16.79           O  
ANISOU 1411  O   HOH A2074     2051   2334   1995   -176      3     55       O  
HETATM 1412  O   HOH A2075       7.964  -0.045  10.376  1.00 25.95           O  
ANISOU 1412  O   HOH A2075     3039   3759   3063     12     89    -61       O  
HETATM 1413  O   HOH A2076     -18.762   6.716  17.097  1.00 27.51           O  
ANISOU 1413  O   HOH A2076     3056   3475   3920    598    -77    290       O  
HETATM 1414  O   HOH A2077     -21.621   8.417  22.835  1.00 44.25           O  
ANISOU 1414  O   HOH A2077     5108   5559   6144    937    175    152       O  
HETATM 1415  O   HOH A2078     -31.898   1.768  18.114  1.00 38.61           O  
ANISOU 1415  O   HOH A2078     3026   6762   4880    338   -127    472       O  
HETATM 1416  O   HOH A2079     -30.860  -3.683  23.161  1.00 49.66           O  
ANISOU 1416  O   HOH A2079     4769   7849   6251   -378     91    146       O  
HETATM 1417  O   HOH A2080     -28.352  -5.285  21.118  1.00 33.53           O  
ANISOU 1417  O   HOH A2080     3071   5462   4206   -594     -1     64       O  
HETATM 1418  O   HOH A2081     -32.949  -1.785  23.811  1.00 39.82           O  
ANISOU 1418  O   HOH A2081     3190   6940   4999    -97    138    241       O  
HETATM 1419  O   HOH A2082     -21.625  -7.474  22.274  1.00 27.92           O  
ANISOU 1419  O   HOH A2082     3178   3799   3632   -561     71   -108       O  
HETATM 1420  O   HOH A2083     -30.383  -1.389  26.315  1.00 44.96           O  
ANISOU 1420  O   HOH A2083     4234   7074   5775     33    251    125       O  
HETATM 1421  O   HOH A2084     -23.016 -10.055  21.259  1.00 52.29           O  
ANISOU 1421  O   HOH A2084     6302   6962   6605   -917     73   -151       O  
HETATM 1422  O   HOH A2085     -15.585 -11.107  20.391  1.00 24.19           O  
ANISOU 1422  O   HOH A2085     3352   2695   3142   -550    108   -242       O  
HETATM 1423  O   HOH A2086     -20.136 -11.965  18.962  1.00 45.20           O  
ANISOU 1423  O   HOH A2086     5780   5717   5679   -978     61   -261       O  
HETATM 1424  O   HOH A2087     -23.900 -12.258  18.212  1.00 46.26           O  
ANISOU 1424  O   HOH A2087     5604   6286   5685  -1314     11   -247       O  
HETATM 1425  O   HOH A2088     -28.295  -9.228  14.537  1.00 28.63           O  
ANISOU 1425  O   HOH A2088     2592   5032   3254  -1356   -239    -89       O  
HETATM 1426  O   HOH A2089     -11.826 -13.629  15.777  1.00 37.83           O  
ANISOU 1426  O   HOH A2089     5458   4160   4754   -528    139   -410       O  
HETATM 1427  O   HOH A2090     -14.475 -13.017  12.353  1.00 33.70           O  
ANISOU 1427  O   HOH A2090     5027   2789   4990   1130    136    890       O  
HETATM 1428  O   HOH A2091     -20.311 -12.276  13.835  1.00 42.78           O  
ANISOU 1428  O   HOH A2091     5450   5611   5194  -1198    -74   -367       O  
HETATM 1429  O   HOH A2092      -4.728  -6.383   3.234  1.00 47.66           O  
ANISOU 1429  O   HOH A2092     6312   6182   5615   -282    -48   -319       O  
HETATM 1430  O   HOH A2093      -0.592 -14.314   9.390  1.00 30.88           O  
ANISOU 1430  O   HOH A2093     4782   3309   3642    254    354   -573       O  
HETATM 1431  O   HOH A2094      -5.317 -17.525   7.340  1.00 36.71           O  
ANISOU 1431  O   HOH A2094     5872   3822   4255   -284    365   -807       O  
HETATM 1432  O   HOH A2095      -9.848 -13.413   7.337  1.00 29.73           O  
ANISOU 1432  O   HOH A2095     4483   3412   3403   -653     69   -636       O  
HETATM 1433  O   HOH A2096      -0.687  -7.951   5.277  1.00 32.42           O  
ANISOU 1433  O   HOH A2096     4476   4093   3750     -4    121   -395       O  
HETATM 1434  O   HOH A2097      -1.905  -9.950   3.572  1.00 35.66           O  
ANISOU 1434  O   HOH A2097     5045   4469   4036   -114    154   -535       O  
HETATM 1435  O   HOH A2098      -4.163  -9.809   2.941  1.00 32.14           O  
ANISOU 1435  O   HOH A2098     4586   4067   3558   -292     75   -538       O  
HETATM 1436  O   HOH A2099       5.148 -11.591   6.849  1.00 35.85           O  
ANISOU 1436  O   HOH A2099     5010   4492   4119    560    406   -489       O  
HETATM 1437  O   HOH A2100       3.894  -7.698   3.288  1.00 43.78           O  
ANISOU 1437  O   HOH A2100     5912   6098   4627   -493    -11   -483       O  
HETATM 1438  O   HOH A2101       4.780  -8.004  16.675  1.00 27.96           O  
ANISOU 1438  O   HOH A2101     3686   3492   3447    565    166   -182       O  
HETATM 1439  O   HOH A2102       7.199   0.289   5.914  1.00 40.59           O  
ANISOU 1439  O   HOH A2102     4948   5681   4793    -83    114    -15       O  
HETATM 1440  O   HOH A2103       7.176  -6.910  17.786  1.00 29.06           O  
ANISOU 1440  O   HOH A2103     3629   3883   3531    618    143   -129       O  
HETATM 1441  O   HOH A2104       8.886   5.923  20.936  1.00 38.80           O  
ANISOU 1441  O   HOH A2104     4632   5297   4813   -452    -58   -195       O  
HETATM 1442  O   HOH A2105       6.888   8.015  19.116  1.00 44.15           O  
ANISOU 1442  O   HOH A2105     5512   5643   5620   -536    -32   -155       O  
HETATM 1443  O   HOH A2106       4.287  10.093  20.415  1.00 30.27           O  
ANISOU 1443  O   HOH A2106     3986   3518   3996   -543     -8   -200       O  
HETATM 1444  O   HOH A2107       7.210   9.005  24.313  1.00 44.06           O  
ANISOU 1444  O   HOH A2107     5533   5665   5545   -668    -54   -353       O  
HETATM 1445  O   HOH B2001       4.820   8.803   3.880  1.00 49.67           O  
ANISOU 1445  O   HOH B2001     6299   6501   6071   -545      5    428       O  
HETATM 1446  O   HOH B2002       3.435  15.708   8.372  1.00 26.47           O  
ANISOU 1446  O   HOH B2002     3838   2725   3493   -746     59    523       O  
HETATM 1447  O   HOH B2003       0.623  14.718   4.896  1.00 34.23           O  
ANISOU 1447  O   HOH B2003     4764   3835   4406   -477    -19    748       O  
HETATM 1448  O   HOH B2004     -16.512   3.776   2.221  1.00 44.59           O  
ANISOU 1448  O   HOH B2004     5096   6511   5334    -19   -539    611       O  
HETATM 1449  O   HOH B2005      -7.783   8.412   0.459  1.00 38.66           O  
ANISOU 1449  O   HOH B2005     4860   5159   4671    -39   -332    786       O  
HETATM 1450  O   HOH B2006      -3.248  11.677   2.791  1.00 44.70           O  
ANISOU 1450  O   HOH B2006     5881   5472   5630   -181   -158    785       O  
HETATM 1451  O   HOH B2007      -7.589  16.061   7.144  1.00 36.52           O  
ANISOU 1451  O   HOH B2007     5106   3784   4986    259    -81    898       O  
HETATM 1452  O   HOH B2008       1.952   8.135   4.610  1.00 29.67           O  
ANISOU 1452  O   HOH B2008     3822   3813   3637   -382    -57    406       O  
HETATM 1453  O   HOH B2009      -4.065   9.397   0.816  1.00 56.56           O  
ANISOU 1453  O   HOH B2009     7252   7271   6965   -180   -222    749       O  
HETATM 1454  O   HOH B2010       1.142  14.727   7.735  1.00 22.89           O  
ANISOU 1454  O   HOH B2010     3352   2275   3071   -509     10    570       O  
HETATM 1455  O   HOH B2011       4.990   3.699   5.333  1.00 30.01           O  
ANISOU 1455  O   HOH B2011     3696   4158   3549   -278     24    144       O  
HETATM 1456  O   HOH B2012       6.130  14.626   7.792  1.00 38.40           O  
ANISOU 1456  O   HOH B2012     5168   4556   4865   -925     71    471       O  
HETATM 1457  O   HOH B2013       7.034  10.900   5.552  1.00 41.69           O  
ANISOU 1457  O   HOH B2013     5300   5441   5099   -766     51    428       O  
CONECT 1172 1173 1174 1175                                                      
CONECT 1173 1172                                                                
CONECT 1174 1172                                                                
CONECT 1175 1172                                                                
CONECT 1326 1329                                                                
CONECT 1329 1326                                                                
CONECT 1331 1332 1333                                                           
CONECT 1332 1331                                                                
CONECT 1333 1331 1334 1335                                                      
CONECT 1334 1333                                                                
CONECT 1335 1333 1336                                                           
CONECT 1336 1335                                                                
MASTER      278    0    3   10    0    0    2    6 1448    2   12   15          
END

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Related entries of code: 2yq7

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
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Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
1fmo	RCSB PDB PDBbind	20-mer
1t5z	RCSB PDB PDBbind	20-mer
1t63	RCSB PDB PDBbind	20-mer
1xj7	RCSB PDB PDBbind	20-mer
1xqh	RCSB PDB PDBbind	20-mer
2kwj	RCSB PDB PDBbind	20-mer
2kwo	RCSB PDB PDBbind	20-mer
2qur	RCSB PDB PDBbind	20-mer
4a1u	RCSB PDB PDBbind	20-mer
4ehq	RCSB PDB PDBbind	20-mer

Entry Information

PDB ID	2yq7
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	BCL-2-LIKE PROTEIN 1
Ligand Name	20-mer
EC.Number	E.C.-.-.-.-
Resolution	1.9(Å)
Affinity (Kd/Ki/IC50)	Ki=35nM
Release Year	2012
Protein/NA Sequence	Check fasta file
Primary Reference	(2013) Acs Chem.Biol. Vol. 8: pp. 297

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): O43521 Q07817
Entrez Gene ID	NCBI Entrez Gene ID: 10018 598
ASD	Information of known allosteric effects of PDB entries

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