moorhen 0.0.1

package/baby-gru/tutorials/moorhen-tutorial-structure-number-2.pdb

@@ -0,0 +1,2018 @@
+HEADER    LIGASE                                  07-OCT-12   4HG7              
+TITLE     CRYSTAL STRUCTURE OF AN MDM2/NUTLIN-3A COMPLEX                        
+COMPND    MOL_ID: 1;                                                            
+COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2;                          
+COMPND   3 CHAIN: A;                                                            
+COMPND   4 FRAGMENT: P53 BINDING DOMAIN (RESIDUES 17-125);                      
+COMPND   5 SYNONYM: DOUBLE MINUTE 2 PROTEIN, HDM2, ONCOPROTEIN MDM2, P53-BINDING
+COMPND   6 PROTEIN MDM2;                                                        
+COMPND   7 EC: 6.3.2.-;                                                         
+COMPND   8 ENGINEERED: YES;                                                     
+COMPND   9 MUTATION: YES                                                        
+SOURCE    MOL_ID: 1;                                                            
+SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
+SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
+SOURCE   4 ORGANISM_TAXID: 9606;                                                
+SOURCE   5 GENE: MDM2;                                                          
+SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
+SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
+SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
+SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
+SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P1                                   
+KEYWDS    MDM2, NUTLIN-3A, SURFACE ENTROPY REDUCTION,                           
+KEYWDS   2 MUTANT VALIDATIO                                                     
+EXPDTA    X-RAY DIFFRACTION                                                     
+AUTHOR    M.E.M.NOBLE,B.ANIL,C.RIEDINGER,J.A.ENDICOTT                           
+REVDAT   2   21-AUG-13 4HG7    1       JRNL                                     
+REVDAT   1 2 31-JUL-13 4HG7    0                                                
+JRNL        AUTH   B.ANIL,C.RIEDINGER,J.A.ENDICOTT,M.E.NOBLE                    
+JRNL        TITL   THE STRUCTURE OF AN MDM2-NUTLIN-3A COMPLEX SOLVED BY THE USE 
+JRNL        TITL 2 OF A VALIDATED MDM2 SURFACE-ENTROPY REDUCTION MUTANT.        
+JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  69  1358 2013              
+JRNL        REFN                   ISSN 0907-4449                               
+JRNL        PMID   23897459                                                     
+JRNL        DOI    10.1107/S0907444913004459                                    
+REMARK   2                                                                      
+REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
+REMARK   3                                                                      
+REMARK   3 REFINEMENT.                                                          
+REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
+REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
+REMARK   3                                                                      
+REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
+REMARK   3                                                                      
+REMARK   3  DATA USED IN REFINEMENT.                                            
+REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
+REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.94                          
+REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.200                          
+REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
+REMARK   3   NUMBER OF REFLECTIONS             : 20070                          
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
+REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
+REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
+REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
+REMARK   3   R VALUE            (WORKING SET) : 0.173                           
+REMARK   3   FREE R VALUE                     : 0.215                           
+REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
+REMARK   3   FREE R VALUE TEST SET COUNT      : 1065                            
+REMARK   3                                                                      
+REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
+REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
+REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
+REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
+REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1299                         
+REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.84                        
+REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
+REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
+REMARK   3   BIN FREE R VALUE                    : 0.3060                       
+REMARK   3                                                                      
+REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
+REMARK   3   PROTEIN ATOMS            : 744                                     
+REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
+REMARK   3   HETEROGEN ATOMS          : 45                                      
+REMARK   3   SOLVENT ATOMS            : 97                                      
+REMARK   3                                                                      
+REMARK   3  B VALUES.                                                           
+REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
+REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.61                          
+REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
+REMARK   3    B11 (A**2) : -0.55000                                             
+REMARK   3    B22 (A**2) : -0.55000                                             
+REMARK   3    B33 (A**2) : 0.83000                                              
+REMARK   3    B12 (A**2) : -0.28000                                             
+REMARK   3    B13 (A**2) : 0.00000                                              
+REMARK   3    B23 (A**2) : 0.00000                                              
+REMARK   3                                                                      
+REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
+REMARK   3   ESU BASED ON R VALUE                            (A): 0.081         
+REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.076         
+REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
+REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.668         
+REMARK   3                                                                      
+REMARK   3 CORRELATION COEFFICIENTS.                                            
+REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
+REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
+REMARK   3                                                                      
+REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
+REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   862 ; 0.014 ; 0.020       
+REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
+REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1181 ; 1.596 ; 2.063       
+REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
+REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   108 ; 5.039 ; 5.000       
+REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    35 ;41.647 ;24.286       
+REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   165 ;12.277 ;15.000       
+REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;16.794 ;15.000       
+REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   132 ; 0.085 ; 0.200       
+REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   646 ; 0.011 ; 0.021       
+REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
+REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
+REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
+REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
+REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
+REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
+REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
+REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
+REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
+REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
+REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
+REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
+REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
+REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
+REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
+REMARK   3                                                                      
+REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
+REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
+REMARK   3                                                                      
+REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
+REMARK   3   RIGID-BOND RESTRAINTS          (A**2):   861 ; 4.481 ; 3.000       
+REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    47 ;28.475 ; 5.000       
+REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):   894 ;13.951 ; 5.000       
+REMARK   3                                                                      
+REMARK   3  NCS RESTRAINTS STATISTICS                                           
+REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
+REMARK   3                                                                      
+REMARK   3  TLS DETAILS                                                         
+REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
+REMARK   3                                                                      
+REMARK   3  BULK SOLVENT MODELLING.                                             
+REMARK   3   METHOD USED : MASK                                                 
+REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
+REMARK   3   VDW PROBE RADIUS   : 1.20                                          
+REMARK   3   ION PROBE RADIUS   : 0.80                                          
+REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
+REMARK   3                                                                      
+REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
+REMARK   3  THE INPUT                                                           
+REMARK   4                                                                      
+REMARK   4 4HG7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
+REMARK 100                                                                      
+REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-12.                  
+REMARK 100 THE RCSB ID CODE IS RCSB075426.                                      
+REMARK 200                                                                      
+REMARK 200 EXPERIMENTAL DETAILS                                                 
+REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
+REMARK 200  DATE OF DATA COLLECTION        : 26-NOV-10                          
+REMARK 200  TEMPERATURE           (KELVIN) : 298                                
+REMARK 200  PH                             : 5.6                                
+REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
+REMARK 200                                                                      
+REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
+REMARK 200  RADIATION SOURCE               : ESRF                               
+REMARK 200  BEAMLINE                       : ID23-2                             
+REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
+REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
+REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
+REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
+REMARK 200  OPTICS                         : NULL                               
+REMARK 200                                                                      
+REMARK 200  DETECTOR TYPE                  : CCD                                
+REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
+REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
+REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
+REMARK 200                                                                      
+REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21274                              
+REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
+REMARK 200  RESOLUTION RANGE LOW       (A) : 33.790                             
+REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
+REMARK 200                                                                      
+REMARK 200 OVERALL.                                                             
+REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
+REMARK 200  DATA REDUNDANCY                : NULL                               
+REMARK 200  R MERGE                    (I) : NULL                               
+REMARK 200  R SYM                      (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
+REMARK 200                                                                      
+REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
+REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
+REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
+REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
+REMARK 200  R SYM FOR SHELL            (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
+REMARK 200                                                                      
+REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
+REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
+REMARK 200 SOFTWARE USED: PHASER                                                
+REMARK 200 STARTING MODEL: NULL                                                 
+REMARK 200                                                                      
+REMARK 200 REMARK: NULL                                                         
+REMARK 280                                                                      
+REMARK 280 CRYSTAL                                                              
+REMARK 280 SOLVENT CONTENT, VS   (%): 64.50                                     
+REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
+REMARK 280                                                                      
+REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M AMMONIUM SULFATE, 0.1 M SODIUM     
+REMARK 280  CITRATE, 1.0 M LITHIUM SULFATE, PH 5.6, VAPOR DIFFUSION, SITTING    
+REMARK 280  DROP, TEMPERATURE 277K                                              
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
+REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
+REMARK 290                                                                      
+REMARK 290      SYMOP   SYMMETRY                                                
+REMARK 290     NNNMMM   OPERATOR                                                
+REMARK 290       1555   X,Y,Z                                                   
+REMARK 290       2555   -Y,X-Y,Z+2/3                                            
+REMARK 290       3555   -X+Y,-X,Z+1/3                                           
+REMARK 290       4555   -X,-Y,Z+1/2                                             
+REMARK 290       5555   Y,-X+Y,Z+1/6                                            
+REMARK 290       6555   X-Y,X,Z+5/6                                             
+REMARK 290       7555   Y,X,-Z+2/3                                              
+REMARK 290       8555   X-Y,-Y,-Z                                               
+REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
+REMARK 290      10555   -Y,-X,-Z+1/6                                            
+REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
+REMARK 290      12555   X,X-Y,-Z+5/6                                            
+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 -0.500000 -0.866025  0.000000        0.00000            
+REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
+REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.46933            
+REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
+REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
+REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.73467            
+REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       52.10200            
+REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
+REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
+REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       17.36733            
+REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
+REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
+REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       86.83667            
+REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
+REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
+REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       69.46933            
+REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
+REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
+REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       34.73467            
+REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
+REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
+REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       17.36733            
+REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       52.10200            
+REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
+REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
+REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       86.83667            
+REMARK 290                                                                      
+REMARK 290 REMARK: NULL                                                         
+REMARK 300                                                                      
+REMARK 300 BIOMOLECULE: 1, 2                                                    
+REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
+REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
+REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
+REMARK 300 BURIED SURFACE AREA.                                                 
+REMARK 350                                                                      
+REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
+REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
+REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
+REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
+REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
+REMARK 350                                                                      
+REMARK 350 BIOMOLECULE: 1                                                       
+REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
+REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
+REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 350                                                                      
+REMARK 350 BIOMOLECULE: 2                                                       
+REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
+REMARK 350 SOFTWARE USED: PISA                                                  
+REMARK 350 TOTAL BURIED SURFACE AREA: 1170 ANGSTROM**2                          
+REMARK 350 SURFACE AREA OF THE COMPLEX: 10140 ANGSTROM**2                       
+REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
+REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
+REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 350   BIOMT1   2  0.500000  0.866025  0.000000      -35.72500            
+REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       61.87752            
+REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -17.36733            
+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     GLY A    12                                                      
+REMARK 465     PRO A    13                                                      
+REMARK 465     LEU A    14                                                      
+REMARK 465     GLY A    15                                                      
+REMARK 465     SER A    16                                                      
+REMARK 465     SER A    17                                                      
+REMARK 800                                                                      
+REMARK 800 SITE                                                                 
+REMARK 800 SITE_IDENTIFIER: AC1                                                 
+REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
+REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NUT A 201                 
+REMARK 800                                                                      
+REMARK 800 SITE_IDENTIFIER: AC2                                                 
+REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
+REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202                 
+REMARK 900                                                                      
+REMARK 900 RELATED ENTRIES                                                      
+REMARK 900 RELATED ID: 4HFZ   RELATED DB: PDB                                   
+REMARK 900 STRUCTURE SOLVED USING THE SAME SURFACE MUTATIONS OF THE             
+REMARK 900 SAME CONSTRUCT                                                       
+DBREF  4HG7 A   17   108  UNP    Q00987   MDM2_HUMAN      17    108             
+SEQADV 4HG7 GLY A   12  UNP  Q00987              EXPRESSION TAG                 
+SEQADV 4HG7 PRO A   13  UNP  Q00987              EXPRESSION TAG                 
+SEQADV 4HG7 LEU A   14  UNP  Q00987              EXPRESSION TAG                 
+SEQADV 4HG7 GLY A   15  UNP  Q00987              EXPRESSION TAG                 
+SEQADV 4HG7 SER A   16  UNP  Q00987              EXPRESSION TAG                 
+SEQADV 4HG7 ALA A   69  UNP  Q00987    GLU    69 ENGINEERED MUTATION            
+SEQADV 4HG7 ALA A   70  UNP  Q00987    LYS    70 ENGINEERED MUTATION            
+SEQRES   1 A   97  GLY PRO LEU GLY SER SER GLN ILE PRO ALA SER GLU GLN          
+SEQRES   2 A   97  GLU THR LEU VAL ARG PRO LYS PRO LEU LEU LEU LYS LEU          
+SEQRES   3 A   97  LEU LYS SER VAL GLY ALA GLN LYS ASP THR TYR THR MET          
+SEQRES   4 A   97  LYS GLU VAL LEU PHE TYR LEU GLY GLN TYR ILE MET THR          
+SEQRES   5 A   97  LYS ARG LEU TYR ASP ALA ALA GLN GLN HIS ILE VAL TYR          
+SEQRES   6 A   97  CYS SER ASN ASP LEU LEU GLY ASP LEU PHE GLY VAL PRO          
+SEQRES   7 A   97  SER PHE SER VAL LYS GLU HIS ARG LYS ILE TYR THR MET          
+SEQRES   8 A   97  ILE TYR ARG ASN LEU VAL                                      
+HET    NUT  A 201      40                                                       
+HET    SO4  A 202       5                                                       
+HETNAM     NUT 4-({(4S,5R)-4,5-BIS(4-CHLOROPHENYL)-2-[4-METHOXY-2-              
+HETNAM   2 NUT (PROPAN-2-YLOXY)PHENYL]-4,5-DIHYDRO-1H-IMIDAZOL-1-               
+HETNAM   3 NUT YL}CARBONYL)PIPERAZIN-2-ONE                                      
+HETNAM     SO4 SULFATE ION                                                      
+HETSYN     NUT NUTLIN 3A                                                        
+FORMUL   2  NUT    C30 H30 CL2 N4 O4                                            
+FORMUL   3  SO4    O4 S 2-                                                      
+FORMUL   4  HOH   *97(H2 O)                                                     
+HELIX    1   1 PRO A   20  GLU A   25  1                                   6    
+HELIX    2   2 LYS A   31  VAL A   41  1                                  11    
+HELIX    3   3 MET A   50  LYS A   64  1                                  15    
+HELIX    4   4 ASP A   80  GLY A   87  1                                   8    
+HELIX    5   5 GLU A   95  ARG A  105  1                                  11    
+SHEET    1   A 2 LEU A  27  VAL A  28  0                                        
+SHEET    2   A 2 TYR A  48  THR A  49 -1  O  TYR A  48   N  VAL A  28           
+SHEET    1   B 2 ILE A  74  TYR A  76  0                                        
+SHEET    2   B 2 SER A  90  SER A  92 -1  O  PHE A  91   N  VAL A  75           
+SITE     1 AC1 14 PRO A  32  LEU A  54  LEU A  57  GLY A  58                    
+SITE     2 AC1 14 ILE A  61  MET A  62  GLN A  72  HIS A  73                    
+SITE     3 AC1 14 VAL A  93  HIS A  96  SO4 A 202  HOH A 307                    
+SITE     4 AC1 14 HOH A 327  HOH A 338                                          
+SITE     1 AC2  9 LYS A  31  GLN A  71  GLN A  72  HIS A  73                    
+SITE     2 AC2  9 NUT A 201  HOH A 320  HOH A 324  HOH A 331                    
+SITE     3 AC2  9 HOH A 347                                                     
+CRYST1   71.450   71.450  104.204  90.00  90.00 120.00 P 65 2 2     12          
+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      0.013996  0.008080  0.000000        0.00000                         
+SCALE2      0.000000  0.016161  0.000000        0.00000                         
+SCALE3      0.000000  0.000000  0.009597        0.00000                         
+ATOM      1  N   GLN A  18     -33.251  16.116 -16.144  1.00 26.63           N  
+ANISOU    1  N   GLN A  18     4640   2822   2656   -316  -1400    183       N  
+ATOM      2  CA  GLN A  18     -33.744  16.395 -14.779  1.00 22.76           C  
+ANISOU    2  CA  GLN A  18     3338   2405   2903   -275  -1288    305       C  
+ATOM      3  C   GLN A  18     -33.202  17.722 -14.291  1.00 22.08           C  
+ANISOU    3  C   GLN A  18     2621   2319   3449   -200   -497     -1       C  
+ATOM      4  O   GLN A  18     -33.766  18.329 -13.368  1.00 24.13           O  
+ANISOU    4  O   GLN A  18     2690   2483   3994   -237   -356   -205       O  
+ATOM      5  CB  GLN A  18     -33.223  15.314 -13.819  1.00 21.88           C  
+ANISOU    5  CB  GLN A  18     3432   1792   3088   -340  -1412    170       C  
+ATOM      6  CG  GLN A  18     -33.750  13.922 -14.126  1.00 22.46           C  
+ANISOU    6  CG  GLN A  18     3459   2103   2971   -580  -1541    -52       C  
+ATOM      7  CD  GLN A  18     -33.207  12.844 -13.217  1.00 25.20           C  
+ANISOU    7  CD  GLN A  18     3273   3187   3115    454  -1263    -53       C  
+ATOM      8  OE1 GLN A  18     -32.919  11.702 -13.662  1.00 29.66           O  
+ANISOU    8  OE1 GLN A  18     3349   3370   4550    232   -747   -698       O  
+ATOM      9  NE2 GLN A  18     -33.110  13.159 -11.948  1.00 17.15           N  
+ANISOU    9  NE2 GLN A  18     1933   1583   2999   -115   -781    -35       N  
+ATOM     10  N   ILE A  19     -32.048  18.114 -14.839  1.00 17.77           N  
+ANISOU   10  N   ILE A  19     2530   1935   2285   -338   -734    207       N  
+ATOM     11  CA  ILE A  19     -31.388  19.371 -14.398  1.00 15.09           C  
+ANISOU   11  CA  ILE A  19     2131   1737   1863     74   -659     62       C  
+ATOM     12  C   ILE A  19     -31.360  20.363 -15.568  1.00 15.53           C  
+ANISOU   12  C   ILE A  19     2361   1674   1864    182   -752     47       C  
+ATOM     13  O   ILE A  19     -30.874  20.015 -16.645  1.00 17.20           O  
+ANISOU   13  O   ILE A  19     2406   2015   2113    362   -660   -123       O  
+ATOM     14  CB  ILE A  19     -29.940  19.163 -13.897  1.00 14.39           C  
+ANISOU   14  CB  ILE A  19     2047   1801   1618    329   -410    228       C  
+ATOM     15  CG1 ILE A  19     -29.853  18.064 -12.782  1.00 12.77           C  
+ANISOU   15  CG1 ILE A  19     1935   1683   1231    127   -401     18       C  
+ATOM     16  CG2 ILE A  19     -29.332  20.499 -13.400  1.00 16.71           C  
+ANISOU   16  CG2 ILE A  19     1954   2286   2110    227   -202   -216       C  
+ATOM     17  CD1 ILE A  19     -30.565  18.411 -11.459  1.00 14.95           C  
+ANISOU   17  CD1 ILE A  19     2162   1975   1541     37   -134   -328       C  
+ATOM     18  N   PRO A  20     -31.850  21.618 -15.350  1.00 15.79           N  
+ANISOU   18  N   PRO A  20     2330   1730   1938    260   -608     14       N  
+ATOM     19  CA  PRO A  20     -31.833  22.555 -16.472  1.00 16.93           C  
+ANISOU   19  CA  PRO A  20     2676   1398   2358    320   -866    -67       C  
+ATOM     20  C   PRO A  20     -30.406  22.832 -17.002  1.00 16.79           C  
+ANISOU   20  C   PRO A  20     2548   1866   1964    138  -1057    145       C  
+ATOM     21  O   PRO A  20     -29.440  22.933 -16.233  1.00 14.85           O  
+ANISOU   21  O   PRO A  20     2305   1747   1591    299   -940    112       O  
+ATOM     22  CB  PRO A  20     -32.480  23.840 -15.887  1.00 18.84           C  
+ANISOU   22  CB  PRO A  20     2717   1295   3145    420   -428     91       C  
+ATOM     23  CG  PRO A  20     -33.228  23.392 -14.660  1.00 21.77           C  
+ANISOU   23  CG  PRO A  20     3463   2238   2569    951   -776    325       C  
+ATOM     24  CD  PRO A  20     -32.571  22.141 -14.171  1.00 17.00           C  
+ANISOU   24  CD  PRO A  20     2395   1895   2169    578   -544    157       C  
+ATOM     25  N   ALA A  21     -30.285  22.997 -18.307  1.00 18.79           N  
+ANISOU   25  N   ALA A  21     2905   2213   2022    250   -396   -137       N  
+ATOM     26  CA  ALA A  21     -28.996  23.235 -18.942  1.00 18.45           C  
+ANISOU   26  CA  ALA A  21     2932   2470   1605    -75   -384     67       C  
+ATOM     27  C   ALA A  21     -28.269  24.431 -18.361  1.00 16.30           C  
+ANISOU   27  C   ALA A  21     2630   1811   1750    274   -555    348       C  
+ATOM     28  O   ALA A  21     -27.044  24.367 -18.157  1.00 17.22           O  
+ANISOU   28  O   ALA A  21     2657   2174   1712    398   -620     64       O  
+ATOM     29  CB  ALA A  21     -29.182  23.417 -20.449  1.00 21.78           C  
+ANISOU   29  CB  ALA A  21     3815   2638   1820    308  -1291    -25       C  
+ATOM     30  N   SER A  22     -28.998  25.516 -18.059  1.00 15.80           N  
+ANISOU   30  N   SER A  22     2616   1886   1500    210   -835    148       N  
+ATOM     31  CA ASER A  22     -28.345  26.723 -17.527  0.80 15.69           C  
+ANISOU   31  CA ASER A  22     2635   1811   1516    415   -676    -30       C  
+ATOM     32  CA BSER A  22     -28.340  26.708 -17.516  0.20 15.19           C  
+ANISOU   32  CA BSER A  22     2460   1748   1563    299   -655    159       C  
+ATOM     33  C   SER A  22     -27.637  26.438 -16.184  1.00 14.66           C  
+ANISOU   33  C   SER A  22     2235   1760   1573    186   -587    265       C  
+ATOM     34  O   SER A  22     -26.570  26.985 -15.905  1.00 15.22           O  
+ANISOU   34  O   SER A  22     2118   1875   1790    210   -331     80       O  
+ATOM     35  CB ASER A  22     -29.349  27.885 -17.393  0.80 18.00           C  
+ANISOU   35  CB ASER A  22     2303   2321   2215    657   -523    449       C  
+ATOM     36  CB BSER A  22     -29.339  27.848 -17.370  0.20 15.24           C  
+ANISOU   36  CB BSER A  22     2316   1870   1603    397   -782    534       C  
+ATOM     37  OG ASER A  22     -30.358  27.609 -16.431  0.80 19.75           O  
+ANISOU   37  OG ASER A  22     2193   2306   3005     85   -402    427       O  
+ATOM     38  OG BSER A  22     -29.824  28.215 -18.642  0.20 15.16           O  
+ANISOU   38  OG BSER A  22     2227   1701   1831    446   -923    671       O  
+ATOM     39  N   GLU A  23     -28.238  25.588 -15.365  1.00 13.27           N  
+ANISOU   39  N   GLU A  23     2096   1531   1415    257   -548     46       N  
+ATOM     40  CA  GLU A  23     -27.706  25.250 -14.063  1.00 11.57           C  
+ANISOU   40  CA  GLU A  23     1771   1462   1163    353   -149     43       C  
+ATOM     41  C   GLU A  23     -26.448  24.374 -14.226  1.00 12.43           C  
+ANISOU   41  C   GLU A  23     1836   1591   1293    464   -281    -52       C  
+ATOM     42  O   GLU A  23     -25.468  24.556 -13.499  1.00 14.56           O  
+ANISOU   42  O   GLU A  23     1996   1841   1695    306   -436    240       O  
+ATOM     43  CB  GLU A  23     -28.777  24.514 -13.238  1.00 12.59           C  
+ANISOU   43  CB  GLU A  23     1860   1612   1309    214   -341    235       C  
+ATOM     44  CG  GLU A  23     -28.287  24.177 -11.848  1.00 12.34           C  
+ANISOU   44  CG  GLU A  23     1650   1493   1543    353   -578    286       C  
+ATOM     45  CD  GLU A  23     -29.328  23.506 -10.983  1.00 13.98           C  
+ANISOU   45  CD  GLU A  23     1851   1683   1775    365   -351    197       C  
+ATOM     46  OE1 GLU A  23     -30.501  23.358 -11.410  1.00 13.47           O  
+ANISOU   46  OE1 GLU A  23     1999   1782   1336    288   -445    222       O  
+ATOM     47  OE2 GLU A  23     -28.941  23.116  -9.853  1.00 13.93           O  
+ANISOU   47  OE2 GLU A  23     2487   1486   1320    427   -150   -209       O  
+ATOM     48  N   GLN A  24     -26.479  23.471 -15.221  1.00 12.50           N  
+ANISOU   48  N   GLN A  24     1584   1550   1615    226   -493   -215       N  
+ATOM     49  CA  GLN A  24     -25.328  22.600 -15.501  1.00 13.66           C  
+ANISOU   49  CA  GLN A  24     1791   1652   1745    283   -194   -182       C  
+ATOM     50  C   GLN A  24     -24.129  23.416 -15.972  1.00 14.42           C  
+ANISOU   50  C   GLN A  24     2127   1758   1593    247   -210    325       C  
+ATOM     51  O   GLN A  24     -22.978  23.016 -15.766  1.00 15.26           O  
+ANISOU   51  O   GLN A  24     2034   2152   1609     90   -218    204       O  
+ATOM     52  CB  GLN A  24     -25.670  21.566 -16.587  1.00 14.10           C  
+ANISOU   52  CB  GLN A  24     1895   1713   1747    132     25   -311       C  
+ATOM     53  CG  GLN A  24     -26.841  20.662 -16.210  1.00 14.46           C  
+ANISOU   53  CG  GLN A  24     2188   1596   1710   -162   -226    -61       C  
+ATOM     54  CD  GLN A  24     -27.020  19.503 -17.177  1.00 18.58           C  
+ANISOU   54  CD  GLN A  24     2896   2075   2085   -166   -348   -473       C  
+ATOM     55  OE1 GLN A  24     -26.041  18.835 -17.539  1.00 22.28           O  
+ANISOU   55  OE1 GLN A  24     3360   2345   2757    335   -464   -571       O  
+ATOM     56  NE2 GLN A  24     -28.266  19.248 -17.603  1.00 19.87           N  
+ANISOU   56  NE2 GLN A  24     3143   2237   2169    121   -820    -43       N  
+ATOM     57  N   GLU A  25     -24.411  24.544 -16.624  1.00 14.67           N  
+ANISOU   57  N   GLU A  25     2350   1814   1406    126   -397    307       N  
+ATOM     58  CA AGLU A  25     -23.328  25.316 -17.231  0.50 15.24           C  
+ANISOU   58  CA AGLU A  25     2618   1938   1233    143   -283    578       C  
+ATOM     59  CA BGLU A  25     -23.390  25.367 -17.271  0.50 15.29           C  
+ANISOU   59  CA BGLU A  25     2542   1946   1320    149   -363    555       C  
+ATOM     60  C   GLU A  25     -22.832  26.463 -16.361  1.00 14.84           C  
+ANISOU   60  C   GLU A  25     2312   1986   1338    370   -461    433       C  
+ATOM     61  O   GLU A  25     -22.020  27.266 -16.793  1.00 21.60           O  
+ANISOU   61  O   GLU A  25     3235   2514   2457   -118   -166    453       O  
+ATOM     62  CB AGLU A  25     -23.710  25.812 -18.634  0.50 16.61           C  
+ANISOU   62  CB AGLU A  25     2822   2281   1206    470   -336    474       C  
+ATOM     63  CB BGLU A  25     -23.934  25.982 -18.586  0.50 17.56           C  
+ANISOU   63  CB BGLU A  25     2931   2446   1291     58   -572    535       C  
+ATOM     64  CG AGLU A  25     -23.992  24.696 -19.628  0.50 22.33           C  
+ANISOU   64  CG AGLU A  25     3403   2803   2278    208   -378   -214       C  
+ATOM     65  CG BGLU A  25     -24.340  24.954 -19.636  0.50 21.22           C  
+ANISOU   65  CG BGLU A  25     3052   3438   1572    220  -1391    130       C  
+ATOM     66  CD AGLU A  25     -22.764  23.851 -19.922  0.50 21.72           C  
+ANISOU   66  CD AGLU A  25     3929   3237   1087    746   -361    -13       C  
+ATOM     67  CD BGLU A  25     -25.021  25.525 -20.879  0.50 26.01           C  
+ANISOU   67  CD BGLU A  25     3651   3640   2591   1145  -1344    203       C  
+ATOM     68  OE1AGLU A  25     -22.915  22.672 -20.297  0.50 30.23           O  
+ANISOU   68  OE1AGLU A  25     5597   3249   2639    543   -127   -348       O  
+ATOM     69  OE1BGLU A  25     -25.758  26.538 -20.824  0.50 27.52           O  
+ANISOU   69  OE1BGLU A  25     3838   3314   3304   1529   -879   1017       O  
+ATOM     70  OE2AGLU A  25     -21.642  24.363 -19.781  0.50 25.51           O  
+ANISOU   70  OE2AGLU A  25     3740   3979   1971    983    -71    -74       O  
+ATOM     71  OE2BGLU A  25     -24.842  24.920 -21.950  0.50 39.48           O  
+ANISOU   71  OE2BGLU A  25     5766   5705   3530    283     55  -1047       O  
+ATOM     72  N   THR A  26     -23.281  26.509 -15.104  1.00 14.27           N  
+ANISOU   72  N   THR A  26     2117   1823   1480    364   -543    171       N  
+ATOM     73  CA  THR A  26     -22.842  27.558 -14.172  1.00 15.62           C  
+ANISOU   73  CA  THR A  26     2160   1926   1849    165   -569     51       C  
+ATOM     74  C   THR A  26     -21.462  27.224 -13.603  1.00 15.85           C  
+ANISOU   74  C   THR A  26     2243   2018   1759    139   -516    219       C  
+ATOM     75  O   THR A  26     -21.225  26.077 -13.205  1.00 15.10           O  
+ANISOU   75  O   THR A  26     2039   1641   2057    -38   -339     96       O  
+ATOM     76  CB  THR A  26     -23.883  27.687 -13.037  1.00 16.30           C  
+ANISOU   76  CB  THR A  26     2216   2042   1934    271   -461    -87       C  
+ATOM     77  OG1 THR A  26     -25.091  28.192 -13.629  1.00 21.42           O  
+ANISOU   77  OG1 THR A  26     2551   2646   2940    360  -1031   -377       O  
+ATOM     78  CG2 THR A  26     -23.447  28.670 -11.975  1.00 17.75           C  
+ANISOU   78  CG2 THR A  26     2486   2193   2063   -226   -285     66       C  
+ATOM     79  N   LEU A  27     -20.570  28.218 -13.588  1.00 15.17           N  
+ANISOU   79  N   LEU A  27     1898   2232   1631     55   -479    130       N  
+ATOM     80  CA  LEU A  27     -19.212  28.063 -13.030  1.00 14.25           C  
+ANISOU   80  CA  LEU A  27     1936   1711   1766    -65   -482    578       C  
+ATOM     81  C   LEU A  27     -19.252  28.024 -11.506  1.00 15.15           C  
+ANISOU   81  C   LEU A  27     2201   1738   1815    125   -550    272       C  
+ATOM     82  O   LEU A  27     -19.839  28.918 -10.873  1.00 15.64           O  
+ANISOU   82  O   LEU A  27     2210   2017   1713    235   -442    373       O  
+ATOM     83  CB  LEU A  27     -18.283  29.193 -13.512  1.00 16.16           C  
+ANISOU   83  CB  LEU A  27     2037   1993   2108   -167   -296    672       C  
+ATOM     84  CG  LEU A  27     -16.777  28.995 -13.263  1.00 19.41           C  
+ANISOU   84  CG  LEU A  27     2214   2139   3022   -159   -394    315       C  
+ATOM     85  CD1 LEU A  27     -16.222  27.959 -14.241  1.00 21.37           C  
+ANISOU   85  CD1 LEU A  27     2366   2303   3450    634   -154    453       C  
+ATOM     86  CD2 LEU A  27     -16.050  30.325 -13.415  1.00 23.69           C  
+ANISOU   86  CD2 LEU A  27     2612   2629   3757   -541   -142    519       C  
+ATOM     87  N   VAL A  28     -18.608  27.015 -10.910  1.00 14.49           N  
+ANISOU   87  N   VAL A  28     2193   1493   1819   -160   -563    307       N  
+ATOM     88  CA  VAL A  28     -18.543  26.887  -9.458  1.00 15.32           C  
+ANISOU   88  CA  VAL A  28     2067   1758   1995   -378   -533    532       C  
+ATOM     89  C   VAL A  28     -17.112  26.638  -8.995  1.00 15.78           C  
+ANISOU   89  C   VAL A  28     2190   1754   2051   -188   -661    175       C  
+ATOM     90  O   VAL A  28     -16.222  26.321  -9.811  1.00 15.89           O  
+ANISOU   90  O   VAL A  28     2005   1809   2223    -39   -551    473       O  
+ATOM     91  CB  VAL A  28     -19.461  25.735  -8.965  1.00 13.82           C  
+ANISOU   91  CB  VAL A  28     1736   1714   1801   -136   -424    610       C  
+ATOM     92  CG1 VAL A  28     -20.934  26.068  -9.313  1.00 17.35           C  
+ANISOU   92  CG1 VAL A  28     1859   2517   2217    -24   -698    671       C  
+ATOM     93  CG2 VAL A  28     -19.030  24.400  -9.592  1.00 16.56           C  
+ANISOU   93  CG2 VAL A  28     2329   1725   2235   -434   -474    463       C  
+ATOM     94  N   ARG A  29     -16.904  26.762  -7.682  1.00 14.38           N  
+ANISOU   94  N   ARG A  29     1823   1628   2010      3   -704    634       N  
+ATOM     95  CA  ARG A  29     -15.579  26.613  -7.073  1.00 13.71           C  
+ANISOU   95  CA  ARG A  29     1776   1240   2191   -167   -843    241       C  
+ATOM     96  C   ARG A  29     -15.649  25.531  -6.029  1.00 13.63           C  
+ANISOU   96  C   ARG A  29     1898   1374   1907   -253   -739    126       C  
+ATOM     97  O   ARG A  29     -16.136  25.779  -4.930  1.00 14.66           O  
+ANISOU   97  O   ARG A  29     2062   1520   1988   -218   -721    148       O  
+ATOM     98  CB  ARG A  29     -15.109  27.923  -6.425  1.00 15.65           C  
+ANISOU   98  CB  ARG A  29     1991   1406   2549   -729   -476    307       C  
+ATOM     99  CG  ARG A  29     -13.683  27.868  -5.884  1.00 21.97           C  
+ANISOU   99  CG  ARG A  29     2555   2305   3487   -539  -1276    224       C  
+ATOM    100  CD  ARG A  29     -13.241  29.194  -5.290  1.00 27.46           C  
+ANISOU  100  CD  ARG A  29     4330   2716   3385  -1549   -757    368       C  
+ATOM    101  NE  ARG A  29     -13.150  30.249  -6.290  1.00 32.40           N  
+ANISOU  101  NE  ARG A  29     5718   2374   4216  -1757   -892    456       N  
+ATOM    102  CZ  ARG A  29     -12.098  30.469  -7.085  1.00 38.59           C  
+ANISOU  102  CZ  ARG A  29     6046   3877   4736   -601   -243   1252       C  
+ATOM    103  NH1 ARG A  29     -11.008  29.687  -7.031  1.00 33.71           N  
+ANISOU  103  NH1 ARG A  29     4592   3489   4725  -1999   -448    706       N  
+ATOM    104  NH2 ARG A  29     -12.143  31.485  -7.941  1.00 32.09           N  
+ANISOU  104  NH2 ARG A  29     4541   3571   4077   -343  -1348    885       N  
+ATOM    105  N   PRO A  30     -15.181  24.316  -6.348  1.00 13.07           N  
+ANISOU  105  N   PRO A  30     1693   1467   1805   -115   -663    269       N  
+ATOM    106  CA  PRO A  30     -15.167  23.263  -5.294  1.00 13.18           C  
+ANISOU  106  CA  PRO A  30     1905   1272   1828     43   -843    239       C  
+ATOM    107  C   PRO A  30     -14.380  23.676  -4.026  1.00 14.69           C  
+ANISOU  107  C   PRO A  30     2222   1502   1854   -115   -915    298       C  
+ATOM    108  O   PRO A  30     -13.327  24.342  -4.121  1.00 16.92           O  
+ANISOU  108  O   PRO A  30     2160   2071   2196   -149   -807     82       O  
+ATOM    109  CB  PRO A  30     -14.405  22.110  -5.977  1.00 13.49           C  
+ANISOU  109  CB  PRO A  30     2277   1242   1605    115   -788    235       C  
+ATOM    110  CG  PRO A  30     -14.762  22.288  -7.456  1.00 15.77           C  
+ANISOU  110  CG  PRO A  30     2552   1571   1867    -69   -942    969       C  
+ATOM    111  CD  PRO A  30     -14.720  23.808  -7.660  1.00 14.98           C  
+ANISOU  111  CD  PRO A  30     2158   1416   2117    118   -322    321       C  
+ATOM    112  N   LYS A  31     -14.847  23.256  -2.852  1.00 14.59           N  
+ANISOU  112  N   LYS A  31     2113   1686   1741   -220   -994    216       N  
+ATOM    113  CA  LYS A  31     -13.977  23.335  -1.654  1.00 13.86           C  
+ANISOU  113  CA  LYS A  31     1899   1465   1899   -226   -993     85       C  
+ATOM    114  C   LYS A  31     -12.770  22.350  -1.863  1.00 15.59           C  
+ANISOU  114  C   LYS A  31     1973   1674   2275   -103  -1118   -140       C  
+ATOM    115  O   LYS A  31     -12.827  21.470  -2.737  1.00 14.44           O  
+ANISOU  115  O   LYS A  31     2139   1438   1909     56  -1123     47       O  
+ATOM    116  CB  LYS A  31     -14.767  22.947  -0.377  1.00 14.58           C  
+ANISOU  116  CB  LYS A  31     2468   1600   1472    211   -811    -37       C  
+ATOM    117  CG  LYS A  31     -15.923  23.899  -0.039  1.00 17.58           C  
+ANISOU  117  CG  LYS A  31     2326   2106   2245    454   -848    231       C  
+ATOM    118  CD  LYS A  31     -16.698  23.330   1.174  1.00 18.03           C  
+ANISOU  118  CD  LYS A  31     2601   2157   2089    601   -574    207       C  
+ATOM    119  CE  LYS A  31     -17.917  24.171   1.536  1.00 22.36           C  
+ANISOU  119  CE  LYS A  31     3021   3146   2329    825   -362    294       C  
+ATOM    120  NZ  LYS A  31     -18.520  23.621   2.790  1.00 22.36           N  
+ANISOU  120  NZ  LYS A  31     2599   3744   2152    -38   -839    429       N  
+ATOM    121  N   PRO A  32     -11.689  22.496  -1.083  1.00 14.00           N  
+ANISOU  121  N   PRO A  32     1862   1556   1900   -232   -933     80       N  
+ATOM    122  CA  PRO A  32     -10.471  21.711  -1.373  1.00 14.88           C  
+ANISOU  122  CA  PRO A  32     1762   1640   2249   -417  -1129    215       C  
+ATOM    123  C   PRO A  32     -10.620  20.195  -1.342  1.00 15.12           C  
+ANISOU  123  C   PRO A  32     1852   1578   2312   -122  -1028    396       C  
+ATOM    124  O   PRO A  32      -9.906  19.527  -2.091  1.00 17.98           O  
+ANISOU  124  O   PRO A  32     2099   1665   3066   -161   -977     28       O  
+ATOM    125  CB  PRO A  32      -9.494  22.178  -0.287  1.00 16.13           C  
+ANISOU  125  CB  PRO A  32     1937   1600   2588   -449  -1406    239       C  
+ATOM    126  CG  PRO A  32      -9.899  23.610  -0.065  1.00 17.20           C  
+ANISOU  126  CG  PRO A  32     1719   1826   2989   -200   -948    225       C  
+ATOM    127  CD  PRO A  32     -11.432  23.532  -0.055  1.00 15.96           C  
+ANISOU  127  CD  PRO A  32     1743   1545   2777   -552  -1099   -268       C  
+ATOM    128  N   LEU A  33     -11.503  19.630  -0.497  1.00 14.16           N  
+ANISOU  128  N   LEU A  33     1915   1290   2174   -271   -979    276       N  
+ATOM    129  CA  LEU A  33     -11.629  18.164  -0.491  1.00 13.71           C  
+ANISOU  129  CA  LEU A  33     1711   1414   2082   -517   -791    161       C  
+ATOM    130  C   LEU A  33     -12.263  17.635  -1.782  1.00 13.85           C  
+ANISOU  130  C   LEU A  33     1784   1416   2061   -122   -976    240       C  
+ATOM    131  O   LEU A  33     -11.824  16.615  -2.303  1.00 15.54           O  
+ANISOU  131  O   LEU A  33     1737   1665   2499    255  -1029     10       O  
+ATOM    132  CB  LEU A  33     -12.380  17.667   0.750  1.00 15.11           C  
+ANISOU  132  CB  LEU A  33     2073   1711   1957   -291   -689    444       C  
+ATOM    133  CG  LEU A  33     -11.661  17.938   2.072  1.00 16.99           C  
+ANISOU  133  CG  LEU A  33     2367   2149   1939   -247   -782    576       C  
+ATOM    134  CD1 LEU A  33     -12.505  17.536   3.265  1.00 19.43           C  
+ANISOU  134  CD1 LEU A  33     2345   2353   2681   -697   -340    630       C  
+ATOM    135  CD2 LEU A  33     -10.289  17.279   2.121  1.00 19.80           C  
+ANISOU  135  CD2 LEU A  33     2364   2755   2402   -149  -1062    685       C  
+ATOM    136  N   LEU A  34     -13.298  18.296  -2.281  1.00 13.66           N  
+ANISOU  136  N   LEU A  34     1632   1634   1924   -361  -1154    212       N  
+ATOM    137  CA  LEU A  34     -13.846  17.888  -3.563  1.00 12.93           C  
+ANISOU  137  CA  LEU A  34     1544   1714   1653    -21   -876    108       C  
+ATOM    138  C   LEU A  34     -12.805  18.134  -4.651  1.00 13.48           C  
+ANISOU  138  C   LEU A  34     1558   1570   1992    -24   -789    169       C  
+ATOM    139  O   LEU A  34     -12.677  17.308  -5.588  1.00 15.20           O  
+ANISOU  139  O   LEU A  34     1795   1697   2282    150   -909     -9       O  
+ATOM    140  CB  LEU A  34     -15.147  18.621  -3.880  1.00 13.60           C  
+ANISOU  140  CB  LEU A  34     1946   1479   1742    162  -1097    227       C  
+ATOM    141  CG  LEU A  34     -15.764  18.385  -5.268  1.00 13.33           C  
+ANISOU  141  CG  LEU A  34     1680   1486   1896     55   -997   -316       C  
+ATOM    142  CD1 LEU A  34     -16.003  16.885  -5.555  1.00 14.65           C  
+ANISOU  142  CD1 LEU A  34     1914   1564   2088    117   -737   -679       C  
+ATOM    143  CD2 LEU A  34     -17.067  19.162  -5.437  1.00 16.29           C  
+ANISOU  143  CD2 LEU A  34     1920   1803   2465    397   -889   -370       C  
+ATOM    144  N   LEU A  35     -12.069  19.248  -4.547  1.00 13.80           N  
+ANISOU  144  N   LEU A  35     1435   1689   2119   -103   -567    363       N  
+ATOM    145  CA  LEU A  35     -11.061  19.550  -5.571  1.00 15.22           C  
+ANISOU  145  CA  LEU A  35     1952   1599   2230   -314   -248    256       C  
+ATOM    146  C   LEU A  35     -10.012  18.424  -5.630  1.00 18.01           C  
+ANISOU  146  C   LEU A  35     2072   2112   2656    -33   -718    335       C  
+ATOM    147  O   LEU A  35      -9.621  18.009  -6.726  1.00 18.84           O  
+ANISOU  147  O   LEU A  35     2100   2397   2659   -395   -300    149       O  
+ATOM    148  CB  LEU A  35     -10.383  20.916  -5.327  1.00 19.62           C  
+ANISOU  148  CB  LEU A  35     2628   2088   2737   -945   -457    154       C  
+ATOM    149  CG  LEU A  35      -9.569  21.462  -6.513  1.00 22.63           C  
+ANISOU  149  CG  LEU A  35     3041   2287   3271   -659   -305    572       C  
+ATOM    150  CD1 LEU A  35     -10.470  21.765  -7.700  1.00 25.75           C  
+ANISOU  150  CD1 LEU A  35     3898   2736   3148   -501   -527    692       C  
+ATOM    151  CD2 LEU A  35      -8.857  22.738  -6.081  1.00 27.69           C  
+ANISOU  151  CD2 LEU A  35     3380   2700   4438  -1402   -848   1134       C  
+ATOM    152  N   LYS A  36      -9.569  17.940  -4.466  1.00 16.70           N  
+ANISOU  152  N   LYS A  36     1767   2022   2555    -77   -745    375       N  
+ATOM    153  CA  LYS A  36      -8.657  16.773  -4.362  1.00 18.01           C  
+ANISOU  153  CA  LYS A  36     1842   2309   2689    238   -900    206       C  
+ATOM    154  C   LYS A  36      -9.157  15.574  -5.186  1.00 18.81           C  
+ANISOU  154  C   LYS A  36     1797   2192   3155    180   -493     90       C  
+ATOM    155  O   LYS A  36      -8.394  14.946  -5.935  1.00 20.68           O  
+ANISOU  155  O   LYS A  36     2061   3126   2670    638   -557    132       O  
+ATOM    156  CB  LYS A  36      -8.448  16.347  -2.887  1.00 18.31           C  
+ANISOU  156  CB  LYS A  36     1599   2682   2675    389   -979    318       C  
+ATOM    157  CG  LYS A  36      -7.600  15.068  -2.671  1.00 27.44           C  
+ANISOU  157  CG  LYS A  36     3756   3162   3505   1229  -1132    820       C  
+ATOM    158  CD  LYS A  36      -7.466  14.629  -1.183  1.00 26.47           C  
+ANISOU  158  CD  LYS A  36     4085   2674   3297   1594  -1208    432       C  
+ATOM    159  CE  LYS A  36      -6.844  13.245  -0.985  1.00 39.07           C  
+ANISOU  159  CE  LYS A  36     5595   4054   5196   2852  -1446   -288       C  
+ATOM    160  NZ  LYS A  36      -5.442  13.217  -1.459  1.00 52.34           N  
+ANISOU  160  NZ  LYS A  36     6093   6940   6853   3225    139    262       N  
+ATOM    161  N   LEU A  37     -10.435  15.248  -4.996  1.00 16.56           N  
+ANISOU  161  N   LEU A  37     1776   2153   2362    234   -667     87       N  
+ATOM    162  CA ALEU A  37     -11.074  14.181  -5.722  0.80 16.88           C  
+ANISOU  162  CA ALEU A  37     1831   1934   2648    -14   -398    235       C  
+ATOM    163  CA BLEU A  37     -11.110  14.185  -5.745  0.20 16.62           C  
+ANISOU  163  CA BLEU A  37     1799   1959   2556    176   -500    142       C  
+ATOM    164  C   LEU A  37     -10.994  14.398  -7.244  1.00 15.74           C  
+ANISOU  164  C   LEU A  37     1624   1776   2579    410   -458    276       C  
+ATOM    165  O   LEU A  37     -10.601  13.485  -8.004  1.00 19.03           O  
+ANISOU  165  O   LEU A  37     2199   1965   3065    613    -96    124       O  
+ATOM    166  CB ALEU A  37     -12.517  14.074  -5.247  0.80 18.13           C  
+ANISOU  166  CB ALEU A  37     1970   2398   2519    334   -185    597       C  
+ATOM    167  CB BLEU A  37     -12.597  14.123  -5.389  0.20 17.04           C  
+ANISOU  167  CB BLEU A  37     1866   2205   2402    261   -397    220       C  
+ATOM    168  CG ALEU A  37     -13.303  12.825  -5.576  0.80 17.96           C  
+ANISOU  168  CG ALEU A  37     2511   1716   2595    809   -188    178       C  
+ATOM    169  CG BLEU A  37     -13.025  13.500  -4.072  0.20 17.30           C  
+ANISOU  169  CG BLEU A  37     2257   1997   2317    341   -390    115       C  
+ATOM    170  CD1ALEU A  37     -14.388  12.587  -4.514  0.80 21.75           C  
+ANISOU  170  CD1ALEU A  37     2453   2454   3353   -180     88    444       C  
+ATOM    171  CD1BLEU A  37     -14.530  13.288  -4.075  0.20 16.85           C  
+ANISOU  171  CD1BLEU A  37     2218   2209   1975    447     69   -123       C  
+ATOM    172  CD2ALEU A  37     -13.907  12.941  -6.965  0.80 18.88           C  
+ANISOU  172  CD2ALEU A  37     1945   2082   3143    855   -633    -19       C  
+ATOM    173  CD2BLEU A  37     -12.296  12.182  -3.898  0.20 17.49           C  
+ANISOU  173  CD2BLEU A  37     1993   1921   2730    271   -543    -70       C  
+ATOM    174  N   LEU A  38     -11.366  15.583  -7.699  1.00 14.85           N  
+ANISOU  174  N   LEU A  38     1563   1690   2387    118   -377    288       N  
+ATOM    175  CA  LEU A  38     -11.334  15.871  -9.128  1.00 15.76           C  
+ANISOU  175  CA  LEU A  38     1852   1779   2357    625    -83    332       C  
+ATOM    176  C   LEU A  38      -9.913  15.810  -9.692  1.00 17.86           C  
+ANISOU  176  C   LEU A  38     1736   2358   2690    269   -238    464       C  
+ATOM    177  O   LEU A  38      -9.712  15.249 -10.771  1.00 19.22           O  
+ANISOU  177  O   LEU A  38     2253   2563   2487    376   -146    245       O  
+ATOM    178  CB  LEU A  38     -11.965  17.248  -9.413  1.00 17.36           C  
+ANISOU  178  CB  LEU A  38     2438   1870   2286    779   -170    323       C  
+ATOM    179  CG  LEU A  38     -13.399  17.427  -8.890  1.00 19.92           C  
+ANISOU  179  CG  LEU A  38     2042   1979   3544    591   -579     -8       C  
+ATOM    180  CD1 LEU A  38     -13.897  18.828  -9.233  1.00 21.77           C  
+ANISOU  180  CD1 LEU A  38     2939   2158   3172    522  -1159    404       C  
+ATOM    181  CD2 LEU A  38     -14.403  16.354  -9.330  1.00 21.39           C  
+ANISOU  181  CD2 LEU A  38     2251   2679   3194    261   -545    -43       C  
+ATOM    182  N   LYS A  39      -8.941  16.369  -8.958  1.00 17.27           N  
+ANISOU  182  N   LYS A  39     1581   2306   2674    156    -43    373       N  
+ATOM    183  CA ALYS A  39      -7.535  16.370  -9.384  0.80 20.32           C  
+ANISOU  183  CA ALYS A  39     1440   2772   3506    495   -174    261       C  
+ATOM    184  CA BLYS A  39      -7.542  16.372  -9.384  0.20 19.02           C  
+ANISOU  184  CA BLYS A  39     1580   2574   3072    188    -14    383       C  
+ATOM    185  C   LYS A  39      -7.005  14.948  -9.502  1.00 20.77           C  
+ANISOU  185  C   LYS A  39     1914   2602   3373    333    143    357       C  
+ATOM    186  O   LYS A  39      -6.138  14.674 -10.339  1.00 22.91           O  
+ANISOU  186  O   LYS A  39     2043   3079   3581    432    259    210       O  
+ATOM    187  CB ALYS A  39      -6.664  17.118  -8.365  0.80 27.22           C  
+ANISOU  187  CB ALYS A  39     2285   3428   4626   -285   -185   -341       C  
+ATOM    188  CB BLYS A  39      -6.683  17.175  -8.399  0.20 22.26           C  
+ANISOU  188  CB BLYS A  39     1994   3168   3295   -426    -18    381       C  
+ATOM    189  CG ALYS A  39      -6.998  18.593  -8.197  0.80 35.34           C  
+ANISOU  189  CG ALYS A  39     3461   3801   6167    -15    679  -1196       C  
+ATOM    190  CG BLYS A  39      -6.841  18.687  -8.504  0.20 16.46           C  
+ANISOU  190  CG BLYS A  39     1947   2806   1499  -1308    515    897       C  
+ATOM    191  CD ALYS A  39      -6.122  19.481  -9.058  0.80 46.73           C  
+ANISOU  191  CD ALYS A  39     4811   5447   7497   -572    819    -31       C  
+ATOM    192  CD BLYS A  39      -5.676  19.332  -9.235  0.20 24.97           C  
+ANISOU  192  CD BLYS A  39     2380   5093   2014  -1995     41   1153       C  
+ATOM    193  CE ALYS A  39      -6.504  20.944  -8.911  0.80 50.95           C  
+ANISOU  193  CE ALYS A  39     5353   5818   8184   -311   -309  -1517       C  
+ATOM    194  CE BLYS A  39      -5.863  20.837  -9.350  0.20 32.23           C  
+ANISOU  194  CE BLYS A  39     3810   4860   3573   -391   -551    914       C  
+ATOM    195  NZ ALYS A  39      -5.934  21.539  -7.673  0.80 45.67           N  
+ANISOU  195  NZ ALYS A  39     4217   5853   7283   2315  -1128   -828       N  
+ATOM    196  NZ BLYS A  39      -7.231  21.202  -9.814  0.20 27.20           N  
+ANISOU  196  NZ BLYS A  39     4825   2698   2808    -90  -1194   1608       N  
+ATOM    197  N   SER A  40      -7.510  14.045  -8.650  1.00 20.31           N  
+ANISOU  197  N   SER A  40     2050   2341   3323    140   -514    432       N  
+ATOM    198  CA  SER A  40      -7.035  12.661  -8.650  1.00 20.43           C  
+ANISOU  198  CA  SER A  40     2383   2350   3031    379    222    402       C  
+ATOM    199  C   SER A  40      -7.358  11.925  -9.970  1.00 21.56           C  
+ANISOU  199  C   SER A  40     2307   2703   3182    991     99    -57       C  
+ATOM    200  O   SER A  40      -6.747  10.895 -10.276  1.00 26.02           O  
+ANISOU  200  O   SER A  40     2461   3246   4179   1445    863    112       O  
+ATOM    201  CB  SER A  40      -7.577  11.860  -7.450  1.00 21.29           C  
+ANISOU  201  CB  SER A  40     2237   2438   3414    635     92   1087       C  
+ATOM    202  OG  SER A  40      -8.902  11.408  -7.660  1.00 22.40           O  
+ANISOU  202  OG  SER A  40     2618   2577   3313    534     -4    481       O  
+ATOM    203  N   VAL A  41      -8.320  12.450 -10.729  1.00 20.85           N  
+ANISOU  203  N   VAL A  41     2360   3066   2493    256     72    457       N  
+ATOM    204  CA  VAL A  41      -8.633  11.890 -12.054  1.00 22.32           C  
+ANISOU  204  CA  VAL A  41     2144   3185   3151     63   -201    -32       C  
+ATOM    205  C   VAL A  41      -8.337  12.882 -13.186  1.00 25.13           C  
+ANISOU  205  C   VAL A  41     2499   3581   3466    305   -201    220       C  
+ATOM    206  O   VAL A  41      -8.910  12.814 -14.273  1.00 29.35           O  
+ANISOU  206  O   VAL A  41     3330   4044   3775     -2   -700   -206       O  
+ATOM    207  CB  VAL A  41     -10.066  11.325 -12.141  1.00 20.54           C  
+ANISOU  207  CB  VAL A  41     2322   2422   3058   -163    330    -92       C  
+ATOM    208  CG1 VAL A  41     -10.173  10.030 -11.340  1.00 21.52           C  
+ANISOU  208  CG1 VAL A  41     1818   2620   3736   -204    654    265       C  
+ATOM    209  CG2 VAL A  41     -11.087  12.354 -11.688  1.00 23.39           C  
+ANISOU  209  CG2 VAL A  41     1924   3372   3588    126     -3   -196       C  
+ATOM    210  N   GLY A  42      -7.410  13.792 -12.921  1.00 22.53           N  
+ANISOU  210  N   GLY A  42     2489   2776   3293    465    444    101       N  
+ATOM    211  CA  GLY A  42      -6.778  14.567 -13.977  1.00 26.78           C  
+ANISOU  211  CA  GLY A  42     3437   3456   3280    434    182    797       C  
+ATOM    212  C   GLY A  42      -7.330  15.966 -14.175  1.00 28.06           C  
+ANISOU  212  C   GLY A  42     2937   3446   4275    442    983    535       C  
+ATOM    213  O   GLY A  42      -6.894  16.683 -15.081  1.00 29.01           O  
+ANISOU  213  O   GLY A  42     3508   4133   3378    649   1013    604       O  
+ATOM    214  N   ALA A  43      -8.254  16.396 -13.328  1.00 22.63           N  
+ANISOU  214  N   ALA A  43     2120   3158   3320    131    393    766       N  
+ATOM    215  CA  ALA A  43      -8.718  17.778 -13.451  1.00 26.76           C  
+ANISOU  215  CA  ALA A  43     2737   3161   4268    193    656    756       C  
+ATOM    216  C   ALA A  43      -7.592  18.747 -13.070  1.00 31.60           C  
+ANISOU  216  C   ALA A  43     3305   4195   4504   -193   -148    985       C  
+ATOM    217  O   ALA A  43      -6.753  18.439 -12.215  1.00 34.55           O  
+ANISOU  217  O   ALA A  43     3433   5076   4615   -664   -544    732       O  
+ATOM    218  CB  ALA A  43      -9.971  18.001 -12.625  1.00 24.13           C  
+ANISOU  218  CB  ALA A  43     2563   2942   3662    357    421    895       C  
+ATOM    219  N   GLN A  44      -7.539  19.900 -13.722  1.00 29.02           N  
+ANISOU  219  N   GLN A  44     2507   3463   5054    275   1068    469       N  
+ATOM    220  CA  GLN A  44      -6.370  20.783 -13.560  1.00 36.59           C  
+ANISOU  220  CA  GLN A  44     3982   4096   5821   -670   1429   -273       C  
+ATOM    221  C   GLN A  44      -6.634  22.220 -13.106  1.00 38.50           C  
+ANISOU  221  C   GLN A  44     3455   3678   7494    213    323    287       C  
+ATOM    222  O   GLN A  44      -5.698  23.010 -12.995  1.00 49.02           O  
+ANISOU  222  O   GLN A  44     3009   5657   9957   -236    145    408       O  
+ATOM    223  CB  GLN A  44      -5.545  20.792 -14.848  1.00 41.85           C  
+ANISOU  223  CB  GLN A  44     4356   5111   6431     -2   2037    642       C  
+ATOM    224  CG  GLN A  44      -4.759  19.512 -15.064  1.00 44.13           C  
+ANISOU  224  CG  GLN A  44     4714   5952   6101    306   1851   -252       C  
+ATOM    225  CD  GLN A  44      -3.743  19.664 -16.160  1.00 36.81           C  
+ANISOU  225  CD  GLN A  44     4008   5994   3984    978    487   -134       C  
+ATOM    226  OE1 GLN A  44      -4.096  19.773 -17.343  1.00 50.75           O  
+ANISOU  226  OE1 GLN A  44     7044   8120   4117   -126    -15   1012       O  
+ATOM    227  NE2 GLN A  44      -2.467  19.680 -15.781  1.00 47.46           N  
+ANISOU  227  NE2 GLN A  44     4246   6085   7699   -356     17   -545       N  
+ATOM    228  N   LYS A  45      -7.889  22.552 -12.833  1.00 33.17           N  
+ANISOU  228  N   LYS A  45     3195   4080   5327   -271    588    410       N  
+ATOM    229  CA  LYS A  45      -8.305  23.942 -12.588  1.00 29.68           C  
+ANISOU  229  CA  LYS A  45     2900   3965   4409   -455    301    758       C  
+ATOM    230  C   LYS A  45      -8.889  24.065 -11.184  1.00 28.42           C  
+ANISOU  230  C   LYS A  45     2999   3346   4452   -210    230    786       C  
+ATOM    231  O   LYS A  45      -9.115  23.053 -10.528  1.00 24.06           O  
+ANISOU  231  O   LYS A  45     2254   3049   3838     78   -356    762       O  
+ATOM    232  CB  LYS A  45      -9.380  24.342 -13.600  1.00 36.24           C  
+ANISOU  232  CB  LYS A  45     4538   4767   4461   -115    295   2205       C  
+ATOM    233  CG  LYS A  45      -8.996  24.188 -15.069  1.00 47.61           C  
+ANISOU  233  CG  LYS A  45     6243   6848   4998   1015    -54    566       C  
+ATOM    234  CD  LYS A  45     -10.193  24.471 -15.969  1.00 47.58           C  
+ANISOU  234  CD  LYS A  45     7347   7074   3656    241   -824   -640       C  
+ATOM    235  CE  LYS A  45     -11.296  23.436 -15.778  1.00 54.67           C  
+ANISOU  235  CE  LYS A  45     7562   7231   5976    165   -901   -494       C  
+ATOM    236  NZ  LYS A  45     -12.624  23.910 -16.255  1.00 53.09           N  
+ANISOU  236  NZ  LYS A  45     6576   4874   8722   -368    692    905       N  
+ATOM    237  N   ASP A  46      -9.156  25.298 -10.746  1.00 22.74           N  
+ANISOU  237  N   ASP A  46     1776   3451   3410   -403   -182    290       N  
+ATOM    238  CA  ASP A  46      -9.816  25.549  -9.469  1.00 22.20           C  
+ANISOU  238  CA  ASP A  46     2133   2657   3643   -225   -304    331       C  
+ATOM    239  C   ASP A  46     -11.323  25.763  -9.624  1.00 20.26           C  
+ANISOU  239  C   ASP A  46     2049   2865   2781   -447   -609   1194       C  
+ATOM    240  O   ASP A  46     -12.053  25.720  -8.632  1.00 21.43           O  
+ANISOU  240  O   ASP A  46     2362   2615   3162   -634   -373    693       O  
+ATOM    241  CB  ASP A  46      -9.221  26.800  -8.802  1.00 27.42           C  
+ANISOU  241  CB  ASP A  46     2734   3165   4518   -862   -834    210       C  
+ATOM    242  CG  ASP A  46      -7.786  26.592  -8.336  1.00 34.01           C  
+ANISOU  242  CG  ASP A  46     2796   3390   6734   -470   -997    586       C  
+ATOM    243  OD1 ASP A  46      -7.444  25.474  -7.892  1.00 33.09           O  
+ANISOU  243  OD1 ASP A  46     2422   4588   5560   -202   -960   1587       O  
+ATOM    244  OD2 ASP A  46      -6.996  27.557  -8.405  1.00 43.70           O  
+ANISOU  244  OD2 ASP A  46     2779   5750   8072  -1718   -842    543       O  
+ATOM    245  N   THR A  47     -11.781  26.071 -10.845  1.00 17.73           N  
+ANISOU  245  N   THR A  47     1742   2510   2484   -311   -506    399       N  
+ATOM    246  CA  THR A  47     -13.216  26.316 -11.078  1.00 15.76           C  
+ANISOU  246  CA  THR A  47     1837   1811   2339   -328   -658    380       C  
+ATOM    247  C   THR A  47     -13.683  25.483 -12.252  1.00 17.16           C  
+ANISOU  247  C   THR A  47     2073   2099   2347   -338   -509    369       C  
+ATOM    248  O   THR A  47     -12.905  25.234 -13.162  1.00 20.22           O  
+ANISOU  248  O   THR A  47     2311   2482   2888    -44    129    712       O  
+ATOM    249  CB  THR A  47     -13.522  27.801 -11.344  1.00 18.68           C  
+ANISOU  249  CB  THR A  47     2611   1950   2534   -221   -480    689       C  
+ATOM    250  OG1 THR A  47     -12.814  28.268 -12.496  1.00 23.64           O  
+ANISOU  250  OG1 THR A  47     2992   2440   3548   -763   -141    946       O  
+ATOM    251  CG2 THR A  47     -13.095  28.643 -10.135  1.00 23.97           C  
+ANISOU  251  CG2 THR A  47     3695   2819   2591   -355   -900    357       C  
+ATOM    252  N   TYR A  48     -14.947  25.046 -12.211  1.00 16.31           N  
+ANISOU  252  N   TYR A  48     2019   1892   2283   -427   -676    537       N  
+ATOM    253  CA  TYR A  48     -15.509  24.142 -13.216  1.00 15.12           C  
+ANISOU  253  CA  TYR A  48     1959   1816   1969    133   -724    419       C  
+ATOM    254  C   TYR A  48     -16.980  24.461 -13.392  1.00 14.39           C  
+ANISOU  254  C   TYR A  48     1876   1721   1869    189   -464    463       C  
+ATOM    255  O   TYR A  48     -17.618  24.954 -12.456  1.00 17.68           O  
+ANISOU  255  O   TYR A  48     2049   2311   2356    206   -388    100       O  
+ATOM    256  CB  TYR A  48     -15.462  22.705 -12.691  1.00 17.93           C  
+ANISOU  256  CB  TYR A  48     2177   1753   2881    112   -524    375       C  
+ATOM    257  CG  TYR A  48     -14.063  22.223 -12.426  1.00 22.80           C  
+ANISOU  257  CG  TYR A  48     2134   2752   3777     21   -673    441       C  
+ATOM    258  CD1 TYR A  48     -13.458  22.436 -11.166  1.00 21.36           C  
+ANISOU  258  CD1 TYR A  48     2250   2451   3414   -255   -501    981       C  
+ATOM    259  CD2 TYR A  48     -13.331  21.600 -13.410  1.00 26.80           C  
+ANISOU  259  CD2 TYR A  48     1981   3103   5099     -4   -311   -116       C  
+ATOM    260  CE1 TYR A  48     -12.182  22.003 -10.899  1.00 24.00           C  
+ANISOU  260  CE1 TYR A  48     2320   2684   4114   -104   -444    505       C  
+ATOM    261  CE2 TYR A  48     -12.018  21.160 -13.152  1.00 27.16           C  
+ANISOU  261  CE2 TYR A  48     2566   3311   4440    697   -803    311       C  
+ATOM    262  CZ  TYR A  48     -11.459  21.369 -11.909  1.00 25.51           C  
+ANISOU  262  CZ  TYR A  48     2449   2766   4478     56   -283     82       C  
+ATOM    263  OH  TYR A  48     -10.179  20.943 -11.641  1.00 28.46           O  
+ANISOU  263  OH  TYR A  48     2644   4340   3829    503   -197    483       O  
+ATOM    264  N   THR A  49     -17.571  24.105 -14.525  1.00 14.72           N  
+ANISOU  264  N   THR A  49     1839   1746   2006    162   -531    486       N  
+ATOM    265  CA  THR A  49     -19.054  24.098 -14.542  1.00 14.61           C  
+ANISOU  265  CA  THR A  49     1886   2042   1623    245   -312    484       C  
+ATOM    266  C   THR A  49     -19.559  22.870 -13.769  1.00 14.96           C  
+ANISOU  266  C   THR A  49     2029   1780   1872    184   -301    331       C  
+ATOM    267  O   THR A  49     -18.813  21.881 -13.564  1.00 14.38           O  
+ANISOU  267  O   THR A  49     1777   1828   1858    228   -429     68       O  
+ATOM    268  CB  THR A  49     -19.609  24.015 -15.960  1.00 17.21           C  
+ANISOU  268  CB  THR A  49     2829   2054   1655    101   -511    274       C  
+ATOM    269  OG1 THR A  49     -19.184  22.772 -16.543  1.00 16.36           O  
+ANISOU  269  OG1 THR A  49     2464   2055   1697     70   -237    317       O  
+ATOM    270  CG2 THR A  49     -19.132  25.216 -16.808  1.00 21.46           C  
+ANISOU  270  CG2 THR A  49     2948   2580   2622   -113   -424    841       C  
+ATOM    271  N   MET A  50     -20.827  22.893 -13.358  1.00 14.11           N  
+ANISOU  271  N   MET A  50     2028   1920   1413    148   -364    342       N  
+ATOM    272  CA  MET A  50     -21.381  21.712 -12.683  1.00 13.67           C  
+ANISOU  272  CA  MET A  50     1897   1723   1571      9   -221    155       C  
+ATOM    273  C   MET A  50     -21.291  20.468 -13.595  1.00 13.47           C  
+ANISOU  273  C   MET A  50     1948   1716   1450     21   -341    193       C  
+ATOM    274  O   MET A  50     -20.989  19.353 -13.127  1.00 14.75           O  
+ANISOU  274  O   MET A  50     1818   1992   1793    323   -204    300       O  
+ATOM    275  CB  MET A  50     -22.835  21.950 -12.203  1.00 15.30           C  
+ANISOU  275  CB  MET A  50     1864   2217   1729    519   -489   -293       C  
+ATOM    276  CG  MET A  50     -22.918  22.827 -10.954  1.00 18.31           C  
+ANISOU  276  CG  MET A  50     2820   2453   1683    199   -544   -322       C  
+ATOM    277  SD  MET A  50     -22.226  22.016  -9.473  1.00 19.54           S  
+ANISOU  277  SD  MET A  50     2305   3052   2067   -629   -613    277       S  
+ATOM    278  CE  MET A  50     -23.601  20.990  -8.957  1.00 17.17           C  
+ANISOU  278  CE  MET A  50     1958   2319   2245   -435   -652    127       C  
+ATOM    279  N   LYS A  51     -21.540  20.653 -14.902  1.00 14.69           N  
+ANISOU  279  N   LYS A  51     2101   2075   1404     98   -272    -40       N  
+ATOM    280  CA ALYS A  51     -21.438  19.548 -15.839  0.50 15.78           C  
+ANISOU  280  CA ALYS A  51     2495   2051   1447    303   -191    -24       C  
+ATOM    281  CA BLYS A  51     -21.430  19.558 -15.856  0.50 16.14           C  
+ANISOU  281  CA BLYS A  51     2525   2066   1538    332   -203    -69       C  
+ATOM    282  C   LYS A  51     -20.030  18.919 -15.810  1.00 16.15           C  
+ANISOU  282  C   LYS A  51     2310   1996   1830     72   -569     36       C  
+ATOM    283  O   LYS A  51     -19.888  17.686 -15.854  1.00 15.66           O  
+ANISOU  283  O   LYS A  51     2458   1912   1578    119      0    276       O  
+ATOM    284  CB ALYS A  51     -21.839  19.987 -17.256  0.50 17.96           C  
+ANISOU  284  CB ALYS A  51     3086   2147   1590    413   -463     11       C  
+ATOM    285  CB BLYS A  51     -21.786  20.025 -17.279  0.50 19.05           C  
+ANISOU  285  CB BLYS A  51     3297   2220   1719    407   -590    -23       C  
+ATOM    286  CG ALYS A  51     -22.098  18.826 -18.209  0.50 20.04           C  
+ANISOU  286  CG ALYS A  51     3239   2627   1746    179   -534   -207       C  
+ATOM    287  CG BLYS A  51     -21.732  18.915 -18.324  0.50 22.99           C  
+ANISOU  287  CG BLYS A  51     3790   2664   2278    463   -561   -473       C  
+ATOM    288  CD ALYS A  51     -22.588  19.321 -19.564  0.50 25.57           C  
+ANISOU  288  CD ALYS A  51     3420   4305   1989    119  -1138   -130       C  
+ATOM    289  CD BLYS A  51     -22.379  19.328 -19.639  0.50 30.62           C  
+ANISOU  289  CD BLYS A  51     4244   4696   2692    -28  -1334   -320       C  
+ATOM    290  CE ALYS A  51     -22.693  18.168 -20.541  0.50 31.73           C  
+ANISOU  290  CE ALYS A  51     4733   4145   3178    265  -1168   -447       C  
+ATOM    291  CE BLYS A  51     -22.190  18.235 -20.677  0.50 39.41           C  
+ANISOU  291  CE BLYS A  51     5773   5032   4167     20  -1349  -1117       C  
+ATOM    292  NZ ALYS A  51     -23.177  18.626 -21.871  0.50 31.08           N  
+ANISOU  292  NZ ALYS A  51     4608   3958   3241    726  -1177   -399       N  
+ATOM    293  NZ BLYS A  51     -22.549  16.895 -20.131  0.50 40.66           N  
+ANISOU  293  NZ BLYS A  51     5817   4672   4959    160   -569  -1281       N  
+ATOM    294  N   GLU A  52     -18.987  19.758 -15.755  1.00 14.80           N  
+ANISOU  294  N   GLU A  52     1974   2066   1583    182   -212     71       N  
+ATOM    295  CA  GLU A  52     -17.600  19.258 -15.634  1.00 16.60           C  
+ANISOU  295  CA  GLU A  52     2109   2284   1915    119    -18    383       C  
+ATOM    296  C   GLU A  52     -17.376  18.531 -14.312  1.00 14.00           C  
+ANISOU  296  C   GLU A  52     1902   1900   1517    120   -160    -48       C  
+ATOM    297  O   GLU A  52     -16.707  17.493 -14.271  1.00 14.90           O  
+ANISOU  297  O   GLU A  52     2244   1903   1511    218   -126    429       O  
+ATOM    298  CB  GLU A  52     -16.591  20.404 -15.804  1.00 16.15           C  
+ANISOU  298  CB  GLU A  52     2405   2137   1591    -23    287    413       C  
+ATOM    299  CG  GLU A  52     -16.484  20.903 -17.229  1.00 20.95           C  
+ANISOU  299  CG  GLU A  52     3135   2901   1924    156    582    919       C  
+ATOM    300  CD  GLU A  52     -15.692  22.195 -17.368  1.00 26.18           C  
+ANISOU  300  CD  GLU A  52     4001   3361   2585   -498    970    347       C  
+ATOM    301  OE1 GLU A  52     -15.714  23.017 -16.441  1.00 23.79           O  
+ANISOU  301  OE1 GLU A  52     3655   3024   2360   -556    449    599       O  
+ATOM    302  OE2 GLU A  52     -15.068  22.409 -18.436  0.50 27.20           O  
+ANISOU  302  OE2 GLU A  52     4138   3198   2995  -1739   1307    450       O  
+ATOM    303  N   VAL A  53     -17.917  19.079 -13.210  1.00 13.20           N  
+ANISOU  303  N   VAL A  53     1951   1894   1169     29   -207    182       N  
+ATOM    304  CA  VAL A  53     -17.792  18.386 -11.901  1.00 12.43           C  
+ANISOU  304  CA  VAL A  53     1826   1557   1339    152   -193    259       C  
+ATOM    305  C   VAL A  53     -18.381  16.981 -11.992  1.00 12.23           C  
+ANISOU  305  C   VAL A  53     1700   1714   1233    159   -353    141       C  
+ATOM    306  O   VAL A  53     -17.753  16.006 -11.556  1.00 13.36           O  
+ANISOU  306  O   VAL A  53     1866   1557   1650    248   -288    160       O  
+ATOM    307  CB  VAL A  53     -18.443  19.191 -10.752  1.00 12.85           C  
+ANISOU  307  CB  VAL A  53     2051   1348   1481     45    -96    314       C  
+ATOM    308  CG1 VAL A  53     -18.390  18.383  -9.469  1.00 13.15           C  
+ANISOU  308  CG1 VAL A  53     1605   1885   1505    182   -370    521       C  
+ATOM    309  CG2 VAL A  53     -17.706  20.522 -10.552  1.00 13.54           C  
+ANISOU  309  CG2 VAL A  53     1692   1489   1963     33   -124    -81       C  
+ATOM    310  N   LEU A  54     -19.561  16.862 -12.612  1.00 12.17           N  
+ANISOU  310  N   LEU A  54     1592   1691   1341   -144   -318     79       N  
+ATOM    311  CA  LEU A  54     -20.178  15.536 -12.774  1.00 14.04           C  
+ANISOU  311  CA  LEU A  54     1779   1835   1721    -60   -571   -263       C  
+ATOM    312  C   LEU A  54     -19.363  14.610 -13.652  1.00 15.18           C  
+ANISOU  312  C   LEU A  54     1971   1911   1885     91   -147    132       C  
+ATOM    313  O   LEU A  54     -19.278  13.405 -13.373  1.00 16.02           O  
+ANISOU  313  O   LEU A  54     2276   1731   2078    368   -572    -14       O  
+ATOM    314  CB  LEU A  54     -21.606  15.693 -13.328  1.00 13.90           C  
+ANISOU  314  CB  LEU A  54     1752   1856   1670    118   -519    221       C  
+ATOM    315  CG  LEU A  54     -22.710  15.828 -12.277  1.00 14.83           C  
+ANISOU  315  CG  LEU A  54     2440   1458   1733   -285    -30    -34       C  
+ATOM    316  CD1 LEU A  54     -22.787  14.614 -11.326  1.00 14.86           C  
+ANISOU  316  CD1 LEU A  54     2395   1606   1643   -167   -473     49       C  
+ATOM    317  CD2 LEU A  54     -22.487  17.114 -11.509  1.00 15.87           C  
+ANISOU  317  CD2 LEU A  54     2592   1486   1950   -163     16   -106       C  
+ATOM    318  N   PHE A  55     -18.751  15.157 -14.712  1.00 15.46           N  
+ANISOU  318  N   PHE A  55     2096   1931   1847    113   -132    145       N  
+ATOM    319  CA  PHE A  55     -17.897  14.332 -15.573  1.00 15.52           C  
+ANISOU  319  CA  PHE A  55     1828   2242   1826    111    -23    283       C  
+ATOM    320  C   PHE A  55     -16.752  13.736 -14.759  1.00 16.22           C  
+ANISOU  320  C   PHE A  55     2347   2005   1811    246   -344    -47       C  
+ATOM    321  O   PHE A  55     -16.466  12.540 -14.820  1.00 18.75           O  
+ANISOU  321  O   PHE A  55     2960   2153   2010    691   -353    234       O  
+ATOM    322  CB  PHE A  55     -17.333  15.181 -16.707  1.00 17.06           C  
+ANISOU  322  CB  PHE A  55     2378   2438   1666    263    181    196       C  
+ATOM    323  CG  PHE A  55     -16.285  14.473 -17.502  1.00 21.18           C  
+ANISOU  323  CG  PHE A  55     2933   3096   2017    847    222    -44       C  
+ATOM    324  CD1 PHE A  55     -16.650  13.545 -18.469  1.00 26.81           C  
+ANISOU  324  CD1 PHE A  55     4191   3190   2803   1062     -4   -261       C  
+ATOM    325  CD2 PHE A  55     -14.929  14.681 -17.228  1.00 22.41           C  
+ANISOU  325  CD2 PHE A  55     2958   3211   2345    594    259    457       C  
+ATOM    326  CE1 PHE A  55     -15.678  12.859 -19.186  1.00 29.79           C  
+ANISOU  326  CE1 PHE A  55     4320   3688   3310   1197    416   -295       C  
+ATOM    327  CE2 PHE A  55     -13.957  13.997 -17.933  1.00 27.78           C  
+ANISOU  327  CE2 PHE A  55     3775   3297   3483    857     72   -428       C  
+ATOM    328  CZ  PHE A  55     -14.335  13.094 -18.922  1.00 32.42           C  
+ANISOU  328  CZ  PHE A  55     4527   4330   3459    984    756  -1250       C  
+ATOM    329  N   TYR A  56     -16.064  14.580 -14.009  1.00 14.56           N  
+ANISOU  329  N   TYR A  56     2028   2087   1415    223   -338     10       N  
+ATOM    330  CA  TYR A  56     -14.920  14.060 -13.228  1.00 16.29           C  
+ANISOU  330  CA  TYR A  56     2032   2074   2083      1   -461    183       C  
+ATOM    331  C   TYR A  56     -15.326  13.149 -12.075  1.00 16.29           C  
+ANISOU  331  C   TYR A  56     2257   1846   2084    392   -163     51       C  
+ATOM    332  O   TYR A  56     -14.615  12.185 -11.784  1.00 15.02           O  
+ANISOU  332  O   TYR A  56     1969   1535   2201    219    141    185       O  
+ATOM    333  CB  TYR A  56     -14.063  15.216 -12.730  1.00 16.34           C  
+ANISOU  333  CB  TYR A  56     2024   2124   2061   -256   -124    251       C  
+ATOM    334  CG  TYR A  56     -13.246  15.850 -13.847  1.00 19.35           C  
+ANISOU  334  CG  TYR A  56     2283   2439   2630   -105    409    448       C  
+ATOM    335  CD1 TYR A  56     -12.200  15.154 -14.457  1.00 23.33           C  
+ANISOU  335  CD1 TYR A  56     2833   2864   3165    348    433    113       C  
+ATOM    336  CD2 TYR A  56     -13.506  17.160 -14.268  1.00 18.97           C  
+ANISOU  336  CD2 TYR A  56     2538   2251   2416   -404     71    391       C  
+ATOM    337  CE1 TYR A  56     -11.438  15.739 -15.466  1.00 26.23           C  
+ANISOU  337  CE1 TYR A  56     2883   3579   3502    179    553    109       C  
+ATOM    338  CE2 TYR A  56     -12.759  17.741 -15.284  1.00 24.67           C  
+ANISOU  338  CE2 TYR A  56     3133   3561   2680   -149    785    302       C  
+ATOM    339  CZ  TYR A  56     -11.732  17.026 -15.874  1.00 28.60           C  
+ANISOU  339  CZ  TYR A  56     3486   3827   3551   -169   1143    576       C  
+ATOM    340  OH  TYR A  56     -11.005  17.631 -16.859  1.00 33.24           O  
+ANISOU  340  OH  TYR A  56     3913   4345   4370   -276   1504   1118       O  
+ATOM    341  N   LEU A  57     -16.448  13.446 -11.411  1.00 13.76           N  
+ANISOU  341  N   LEU A  57     1938   1701   1590     71   -292     78       N  
+ATOM    342  CA ALEU A  57     -16.943  12.529 -10.365  0.80 13.84           C  
+ANISOU  342  CA ALEU A  57     2047   1508   1702    288     43    -12       C  
+ATOM    343  CA BLEU A  57     -16.987  12.565 -10.385  0.20 13.71           C  
+ANISOU  343  CA BLEU A  57     1990   1575   1642    256    -93     21       C  
+ATOM    344  C   LEU A  57     -17.272  11.197 -11.002  1.00 13.42           C  
+ANISOU  344  C   LEU A  57     1963   1569   1567    472   -176    -21       C  
+ATOM    345  O   LEU A  57     -16.991  10.183 -10.428  1.00 13.47           O  
+ANISOU  345  O   LEU A  57     1899   1587   1629    403   -104     49       O  
+ATOM    346  CB ALEU A  57     -18.195  13.045  -9.658  0.80 16.48           C  
+ANISOU  346  CB ALEU A  57     1849   2163   2247    217     27   -291       C  
+ATOM    347  CB BLEU A  57     -18.270  13.164  -9.812  0.20 14.24           C  
+ANISOU  347  CB BLEU A  57     1966   1703   1741    196    -57    -48       C  
+ATOM    348  CG ALEU A  57     -18.016  14.137  -8.621  0.80 14.32           C  
+ANISOU  348  CG ALEU A  57     1431   2086   1920    222   -246    -67       C  
+ATOM    349  CG BLEU A  57     -18.811  12.546  -8.530  0.20 13.28           C  
+ANISOU  349  CG BLEU A  57     2009   1306   1731    331   -128     17       C  
+ATOM    350  CD1ALEU A  57     -19.365  14.744  -8.217  0.80 16.63           C  
+ANISOU  350  CD1ALEU A  57     2066   1964   2289    578    250    -93       C  
+ATOM    351  CD1BLEU A  57     -17.685  12.314  -7.544  0.20 14.50           C  
+ANISOU  351  CD1BLEU A  57     2148   1524   1834    214   -274     26       C  
+ATOM    352  CD2ALEU A  57     -17.309  13.555  -7.407  0.80 19.69           C  
+ANISOU  352  CD2ALEU A  57     3185   2661   1635    391   -667   -112       C  
+ATOM    353  CD2BLEU A  57     -19.873  13.451  -7.923  0.20 12.64           C  
+ANISOU  353  CD2BLEU A  57     1739   1213   1850    278   -404    -92       C  
+ATOM    354  N   GLY A  58     -17.881  11.195 -12.188  1.00 14.25           N  
+ANISOU  354  N   GLY A  58     2266   1724   1421    390   -272    -38       N  
+ATOM    355  CA  GLY A  58     -18.175   9.933 -12.879  1.00 15.10           C  
+ANISOU  355  CA  GLY A  58     2042   2026   1668    226   -169   -245       C  
+ATOM    356  C   GLY A  58     -16.906   9.176 -13.180  1.00 15.09           C  
+ANISOU  356  C   GLY A  58     2244   1684   1805    327    -76    -64       C  
+ATOM    357  O   GLY A  58     -16.863   7.962 -12.974  1.00 15.91           O  
+ANISOU  357  O   GLY A  58     2495   1585   1964    415   -407   -203       O  
+ATOM    358  N   GLN A  59     -15.856   9.885 -13.623  1.00 15.83           N  
+ANISOU  358  N   GLN A  59     2242   1907   1865    391    -62    -56       N  
+ATOM    359  CA AGLN A  59     -14.567   9.246 -13.901  0.50 16.61           C  
+ANISOU  359  CA AGLN A  59     2078   2114   2118    276     22    175       C  
+ATOM    360  CA BGLN A  59     -14.541   9.277 -13.898  0.50 16.52           C  
+ANISOU  360  CA BGLN A  59     2074   2063   2140    265     -8    154       C  
+ATOM    361  C   GLN A  59     -13.975   8.634 -12.629  1.00 16.89           C  
+ANISOU  361  C   GLN A  59     2344   1956   2115    591    -58    -76       C  
+ATOM    362  O   GLN A  59     -13.421   7.525 -12.653  1.00 17.86           O  
+ANISOU  362  O   GLN A  59     2601   1885   2298    612    396    142       O  
+ATOM    363  CB AGLN A  59     -13.613  10.255 -14.540  0.50 22.46           C  
+ANISOU  363  CB AGLN A  59     2962   2877   2694   -112    623    422       C  
+ATOM    364  CB BGLN A  59     -13.555  10.336 -14.412  0.50 21.05           C  
+ANISOU  364  CB BGLN A  59     2646   2601   2749    -85    479    215       C  
+ATOM    365  CG AGLN A  59     -13.878  10.422 -16.025  0.50 27.61           C  
+ANISOU  365  CG AGLN A  59     3793   4098   2599   -358    861     -7       C  
+ATOM    366  CG BGLN A  59     -13.759  10.778 -15.854  0.50 25.33           C  
+ANISOU  366  CG BGLN A  59     3674   3139   2809   -125    146     -7       C  
+ATOM    367  CD AGLN A  59     -13.336   9.251 -16.816  0.50 33.08           C  
+ANISOU  367  CD AGLN A  59     4991   4549   3028     42    594   -633       C  
+ATOM    368  CD BGLN A  59     -12.461  11.274 -16.472  0.50 30.06           C  
+ANISOU  368  CD BGLN A  59     4121   3463   3838   -527    706   -262       C  
+ATOM    369  OE1AGLN A  59     -12.158   9.222 -17.163  0.50 39.26           O  
+ANISOU  369  OE1AGLN A  59     5124   5515   4276    235    781  -1721       O  
+ATOM    370  OE1BGLN A  59     -11.679  11.971 -15.820  0.50 35.52           O  
+ANISOU  370  OE1BGLN A  59     5006   4224   4265   -500   -331   -352       O  
+ATOM    371  NE2AGLN A  59     -14.189   8.274 -17.096  0.50 35.18           N  
+ANISOU  371  NE2AGLN A  59     4693   5743   2930   -347    886   -641       N  
+ATOM    372  NE2BGLN A  59     -12.219  10.908 -17.728  0.50 31.89           N  
+ANISOU  372  NE2BGLN A  59     4543   3794   3777    400  -1077  -1160       N  
+ATOM    373  N   TYR A  60     -14.111   9.349 -11.517  1.00 16.08           N  
+ANISOU  373  N   TYR A  60     2232   2124   1753    306     63     51       N  
+ATOM    374  CA  TYR A  60     -13.626   8.859 -10.232  1.00 14.67           C  
+ANISOU  374  CA  TYR A  60     1945   1832   1794    259   -207   -170       C  
+ATOM    375  C   TYR A  60     -14.342   7.568  -9.804  1.00 16.46           C  
+ANISOU  375  C   TYR A  60     1931   1926   2396    471   -272    136       C  
+ATOM    376  O   TYR A  60     -13.697   6.572  -9.389  1.00 16.83           O  
+ANISOU  376  O   TYR A  60     2274   2089   2031    587   -375    205       O  
+ATOM    377  CB  TYR A  60     -13.809   9.966  -9.211  1.00 14.37           C  
+ANISOU  377  CB  TYR A  60     2128   1362   1969    397   -482    -92       C  
+ATOM    378  CG  TYR A  60     -13.387   9.609  -7.799  1.00 15.32           C  
+ANISOU  378  CG  TYR A  60     1927   1769   2122    549   -480    183       C  
+ATOM    379  CD1 TYR A  60     -12.071   9.792  -7.383  1.00 15.79           C  
+ANISOU  379  CD1 TYR A  60     1841   1867   2290    430   -428    156       C  
+ATOM    380  CD2 TYR A  60     -14.314   9.102  -6.870  1.00 16.61           C  
+ANISOU  380  CD2 TYR A  60     2314   1742   2255    594   -310    266       C  
+ATOM    381  CE1 TYR A  60     -11.672   9.489  -6.075  1.00 16.07           C  
+ANISOU  381  CE1 TYR A  60     1954   1810   2339    154   -661    181       C  
+ATOM    382  CE2 TYR A  60     -13.924   8.789  -5.567  1.00 17.80           C  
+ANISOU  382  CE2 TYR A  60     2249   2078   2433    401   -767    172       C  
+ATOM    383  CZ  TYR A  60     -12.595   8.982  -5.180  1.00 17.14           C  
+ANISOU  383  CZ  TYR A  60     2164   1858   2491    151   -575    -16       C  
+ATOM    384  OH  TYR A  60     -12.199   8.670  -3.896  1.00 19.94           O  
+ANISOU  384  OH  TYR A  60     2251   2282   3040     28  -1042    260       O  
+ATOM    385  N   ILE A  61     -15.674   7.569  -9.915  1.00 14.03           N  
+ANISOU  385  N   ILE A  61     1777   1593   1957    175    -98     29       N  
+ATOM    386  CA  ILE A  61     -16.456   6.356  -9.618  1.00 12.84           C  
+ANISOU  386  CA  ILE A  61     1641   1440   1796    285   -317      9       C  
+ATOM    387  C   ILE A  61     -16.059   5.165 -10.485  1.00 15.20           C  
+ANISOU  387  C   ILE A  61     2313   1563   1899    405   -125    -11       C  
+ATOM    388  O   ILE A  61     -15.937   4.027 -10.009  1.00 18.05           O  
+ANISOU  388  O   ILE A  61     2814   1904   2137    800   -235    256       O  
+ATOM    389  CB  ILE A  61     -17.969   6.691  -9.788  1.00 13.26           C  
+ANISOU  389  CB  ILE A  61     1530   1412   2096    316   -242    -12       C  
+ATOM    390  CG1 ILE A  61     -18.430   7.590  -8.639  1.00 15.01           C  
+ANISOU  390  CG1 ILE A  61     2017   1437   2247    617   -196     29       C  
+ATOM    391  CG2 ILE A  61     -18.851   5.432  -9.960  1.00 14.62           C  
+ANISOU  391  CG2 ILE A  61     2056   1471   2028     90   -241    185       C  
+ATOM    392  CD1 ILE A  61     -19.742   8.318  -8.929  1.00 14.67           C  
+ANISOU  392  CD1 ILE A  61     1773   1715   2087    648    204    201       C  
+ATOM    393  N   MET A  62     -15.818   5.407 -11.764  1.00 16.49           N  
+ANISOU  393  N   MET A  62     2466   1834   1964    274    -33   -308       N  
+ATOM    394  CA  MET A  62     -15.409   4.306 -12.649  1.00 16.93           C  
+ANISOU  394  CA  MET A  62     2717   1896   1817    785    203    -91       C  
+ATOM    395  C   MET A  62     -14.000   3.792 -12.353  1.00 19.20           C  
+ANISOU  395  C   MET A  62     2879   1753   2664    928    101   -189       C  
+ATOM    396  O   MET A  62     -13.768   2.577 -12.364  1.00 24.13           O  
+ANISOU  396  O   MET A  62     3851   1797   3518   1257   -183   -228       O  
+ATOM    397  CB  MET A  62     -15.533   4.726 -14.136  1.00 18.01           C  
+ANISOU  397  CB  MET A  62     2898   2115   1828    955   -102   -109       C  
+ATOM    398  CG  MET A  62     -16.932   5.133 -14.589  1.00 19.50           C  
+ANISOU  398  CG  MET A  62     2893   1847   2666    363   -573    161       C  
+ATOM    399  SD  MET A  62     -18.184   3.903 -14.223  1.00 22.09           S  
+ANISOU  399  SD  MET A  62     3149   2313   2930    189      4    -46       S  
+ATOM    400  CE  MET A  62     -17.679   2.577 -15.326  1.00 27.05           C  
+ANISOU  400  CE  MET A  62     4079   2362   3835   -901   -616  -1322       C  
+ATOM    401  N   THR A  63     -13.067   4.717 -12.093  1.00 20.09           N  
+ANISOU  401  N   THR A  63     2461   2210   2961    791    117     29       N  
+ATOM    402  CA  THR A  63     -11.663   4.405 -11.797  1.00 23.17           C  
+ANISOU  402  CA  THR A  63     2864   2302   3635   1066   -275    453       C  
+ATOM    403  C   THR A  63     -11.544   3.603 -10.508  1.00 23.62           C  
+ANISOU  403  C   THR A  63     3217   2441   3313   1198   -106    278       C  
+ATOM    404  O   THR A  63     -10.791   2.621 -10.455  1.00 27.28           O  
+ANISOU  404  O   THR A  63     3342   2841   4181   1525     43    550       O  
+ATOM    405  CB  THR A  63     -10.803   5.704 -11.716  1.00 25.07           C  
+ANISOU  405  CB  THR A  63     2627   3021   3877    483   -254    360       C  
+ATOM    406  OG1 THR A  63     -10.809   6.342 -12.998  1.00 29.29           O  
+ANISOU  406  OG1 THR A  63     3226   3413   4489    -41    174    668       O  
+ATOM    407  CG2 THR A  63      -9.360   5.423 -11.332  1.00 32.50           C  
+ANISOU  407  CG2 THR A  63     2955   3674   5718    995   -330    758       C  
+ATOM    408  N   LYS A  64     -12.298   3.998  -9.484  1.00 22.91           N  
+ANISOU  408  N   LYS A  64     2718   2620   3365    632     33    397       N  
+ATOM    409  CA  LYS A  64     -12.250   3.308  -8.193  1.00 22.69           C  
+ANISOU  409  CA  LYS A  64     2380   2604   3634    919   -535    474       C  
+ATOM    410  C   LYS A  64     -13.254   2.155  -8.085  1.00 24.11           C  
+ANISOU  410  C   LYS A  64     3415   2239   3507    629   -428    161       C  
+ATOM    411  O   LYS A  64     -13.351   1.489  -7.033  1.00 23.48           O  
+ANISOU  411  O   LYS A  64     3096   2146   3677    853   -300    427       O  
+ATOM    412  CB  LYS A  64     -12.454   4.288  -7.044  1.00 24.23           C  
+ANISOU  412  CB  LYS A  64     2669   2629   3905    482   -786    213       C  
+ATOM    413  CG  LYS A  64     -11.319   5.278  -6.906  1.00 27.70           C  
+ANISOU  413  CG  LYS A  64     3098   3089   4336    -65   -391     22       C  
+ATOM    414  CD  LYS A  64     -11.369   5.913  -5.546  1.00 30.06           C  
+ANISOU  414  CD  LYS A  64     3760   3493   4168    452  -1117    -35       C  
+ATOM    415  CE  LYS A  64     -10.432   5.268  -4.549  1.00 30.71           C  
+ANISOU  415  CE  LYS A  64     2683   3977   5008   1332   -890   -508       C  
+ATOM    416  NZ  LYS A  64     -10.377   6.203  -3.384  1.00 30.44           N  
+ANISOU  416  NZ  LYS A  64     2493   3995   5078    520   -929   -638       N  
+ATOM    417  N   ARG A  65     -13.981   1.919  -9.168  1.00 20.28           N  
+ANISOU  417  N   ARG A  65     2992   1980   2733    848     94     -3       N  
+ATOM    418  CA  ARG A  65     -14.936   0.795  -9.240  1.00 23.07           C  
+ANISOU  418  CA  ARG A  65     3978   1821   2963    826     45   -149       C  
+ATOM    419  C   ARG A  65     -15.971   0.846  -8.101  1.00 21.86           C  
+ANISOU  419  C   ARG A  65     3539   1844   2921   1158   -206    184       C  
+ATOM    420  O   ARG A  65     -16.259  -0.158  -7.454  1.00 22.60           O  
+ANISOU  420  O   ARG A  65     3718   1970   2897    767   -105     90       O  
+ATOM    421  CB  ARG A  65     -14.188  -0.565  -9.310  1.00 26.46           C  
+ANISOU  421  CB  ARG A  65     3971   2171   3910   1174    384    149       C  
+ATOM    422  CG  ARG A  65     -13.310  -0.709 -10.552  1.00 31.62           C  
+ANISOU  422  CG  ARG A  65     4639   2847   4526   1238    772   -690       C  
+ATOM    423  CD  ARG A  65     -13.025  -2.172 -10.861  0.50 34.39           C  
+ANISOU  423  CD  ARG A  65     5260   3522   4284   2382    883  -1168       C  
+ATOM    424  NE  ARG A  65     -11.811  -2.646 -10.210  0.50 48.05           N  
+ANISOU  424  NE  ARG A  65     5670   5163   7422   1175  -1062   -782       N  
+ATOM    425  CZ  ARG A  65     -11.370  -3.899 -10.287  0.50 52.27           C  
+ANISOU  425  CZ  ARG A  65     7271   5508   7080   1789   -703  -1399       C  
+ATOM    426  NH1 ARG A  65     -12.053  -4.800 -10.981  0.50 53.80           N  
+ANISOU  426  NH1 ARG A  65     6732   4659   9047    723   -622   -362       N  
+ATOM    427  NH2 ARG A  65     -10.253  -4.252  -9.669  0.50 57.07           N  
+ANISOU  427  NH2 ARG A  65     7837   5859   7987    420  -2027   -733       N  
+ATOM    428  N   LEU A  66     -16.568   2.026  -7.899  1.00 19.58           N  
+ANISOU  428  N   LEU A  66     3316   1729   2393    859   -282    -39       N  
+ATOM    429  CA  LEU A  66     -17.564   2.217  -6.852  1.00 15.96           C  
+ANISOU  429  CA  LEU A  66     2596   1459   2009    525   -547   -341       C  
+ATOM    430  C   LEU A  66     -18.941   1.808  -7.371  1.00 17.95           C  
+ANISOU  430  C   LEU A  66     2784   2281   1754    543   -954    -39       C  
+ATOM    431  O   LEU A  66     -19.939   1.920  -6.663  1.00 21.37           O  
+ANISOU  431  O   LEU A  66     2939   2809   2369   -176   -674   -980       O  
+ATOM    432  CB  LEU A  66     -17.580   3.691  -6.334  1.00 16.49           C  
+ANISOU  432  CB  LEU A  66     2614   1161   2487     32   -766     25       C  
+ATOM    433  CG  LEU A  66     -16.209   4.221  -5.858  1.00 16.00           C  
+ANISOU  433  CG  LEU A  66     2440   1496   2141    214   -885     88       C  
+ATOM    434  CD1 LEU A  66     -16.339   5.660  -5.345  1.00 18.27           C  
+ANISOU  434  CD1 LEU A  66     2952   1914   2074    446   -479   -351       C  
+ATOM    435  CD2 LEU A  66     -15.674   3.276  -4.787  1.00 17.28           C  
+ANISOU  435  CD2 LEU A  66     2456   1631   2475    641   -914     72       C  
+ATOM    436  N   TYR A  67     -18.996   1.400  -8.641  1.00 20.02           N  
+ANISOU  436  N   TYR A  67     3142   2087   2375    659  -1008   -912       N  
+ATOM    437  CA  TYR A  67     -20.209   0.799  -9.227  1.00 20.32           C  
+ANISOU  437  CA  TYR A  67     3519   1937   2263   -104   -671   -478       C  
+ATOM    438  C   TYR A  67     -20.465  -0.660  -8.739  1.00 21.05           C  
+ANISOU  438  C   TYR A  67     3371   1913   2714    516   -686   -211       C  
+ATOM    439  O   TYR A  67     -19.565  -1.302  -8.178  1.00 26.68           O  
+ANISOU  439  O   TYR A  67     4605   2252   3279   1189  -1428   -832       O  
+ATOM    440  CB  TYR A  67     -20.136   0.891 -10.757  1.00 20.67           C  
+ANISOU  440  CB  TYR A  67     3548   1916   2390    663   -798   -199       C  
+ATOM    441  CG  TYR A  67     -18.927   0.229 -11.390  1.00 22.02           C  
+ANISOU  441  CG  TYR A  67     3598   2236   2531    794  -1081   -177       C  
+ATOM    442  CD1 TYR A  67     -18.889  -1.158 -11.571  1.00 22.55           C  
+ANISOU  442  CD1 TYR A  67     3062   2226   3279   1180  -1155   -750       C  
+ATOM    443  CD2 TYR A  67     -17.853   0.977 -11.841  1.00 24.01           C  
+ANISOU  443  CD2 TYR A  67     3562   2523   3037    730   -450      2       C  
+ATOM    444  CE1 TYR A  67     -17.804  -1.777 -12.158  1.00 26.76           C  
+ANISOU  444  CE1 TYR A  67     3576   3301   3290    631   -822  -1900       C  
+ATOM    445  CE2 TYR A  67     -16.749   0.355 -12.443  1.00 31.02           C  
+ANISOU  445  CE2 TYR A  67     4358   2974   4454    689    148   -719       C  
+ATOM    446  CZ  TYR A  67     -16.744  -1.021 -12.604  1.00 26.64           C  
+ANISOU  446  CZ  TYR A  67     3962   2826   3333   1129   -376   -471       C  
+ATOM    447  OH  TYR A  67     -15.684  -1.695 -13.181  1.00 33.31           O  
+ANISOU  447  OH  TYR A  67     4358   4941   3355   1515   -567   -968       O  
+ATOM    448  N   ASP A  68     -21.681  -1.176  -8.977  1.00 23.68           N  
+ANISOU  448  N   ASP A  68     4166   1926   2902    115   -975   -441       N  
+ATOM    449  CA  ASP A  68     -22.049  -2.567  -8.656  1.00 26.24           C  
+ANISOU  449  CA  ASP A  68     4985   2171   2813   -127   -609   -260       C  
+ATOM    450  C   ASP A  68     -22.565  -3.220  -9.909  1.00 21.14           C  
+ANISOU  450  C   ASP A  68     4024   1487   2519    487   -390   -315       C  
+ATOM    451  O   ASP A  68     -23.507  -2.711 -10.473  1.00 23.87           O  
+ANISOU  451  O   ASP A  68     3685   2105   3279    701   -648   -803       O  
+ATOM    452  CB  ASP A  68     -23.194  -2.643  -7.624  1.00 27.35           C  
+ANISOU  452  CB  ASP A  68     5136   2699   2556    612   -643    -34       C  
+ATOM    453  CG  ASP A  68     -23.656  -4.095  -7.381  1.00 28.91           C  
+ANISOU  453  CG  ASP A  68     4378   3680   2924    167   -172   1498       C  
+ATOM    454  OD1 ASP A  68     -22.810  -4.920  -6.969  0.50 29.10           O  
+ANISOU  454  OD1 ASP A  68     6490   2135   2429   1394   1085   1135       O  
+ATOM    455  OD2 ASP A  68     -24.843  -4.431  -7.596  0.50 31.73           O  
+ANISOU  455  OD2 ASP A  68     5345   2281   4428   -910  -1486    554       O  
+ATOM    456  N   ALA A  69     -21.973  -4.334 -10.356  1.00 20.92           N  
+ANISOU  456  N   ALA A  69     4309   1504   2136    325   -208   -234       N  
+ATOM    457  CA  ALA A  69     -22.403  -4.944 -11.636  1.00 22.12           C  
+ANISOU  457  CA  ALA A  69     4228   1638   2537    587   -232   -843       C  
+ATOM    458  C   ALA A  69     -23.878  -5.384 -11.702  1.00 24.70           C  
+ANISOU  458  C   ALA A  69     4382   2144   2858    600   -430   -374       C  
+ATOM    459  O   ALA A  69     -24.543  -5.262 -12.775  1.00 29.92           O  
+ANISOU  459  O   ALA A  69     5421   2941   3004   -389   -770   -462       O  
+ATOM    460  CB  ALA A  69     -21.497  -6.123 -11.976  1.00 27.17           C  
+ANISOU  460  CB  ALA A  69     4281   2370   3671    913    323  -1072       C  
+ATOM    461  N   ALA A  70     -24.398  -5.900 -10.584  1.00 26.18           N  
+ANISOU  461  N   ALA A  70     4615   1549   3783     77    737   -867       N  
+ATOM    462  CA  ALA A  70     -25.763  -6.488 -10.600  1.00 23.96           C  
+ANISOU  462  CA  ALA A  70     4699   2160   2245    -41   -730   -170       C  
+ATOM    463  C   ALA A  70     -26.882  -5.450 -10.470  1.00 24.64           C  
+ANISOU  463  C   ALA A  70     4618   2860   1883    226   -639   -169       C  
+ATOM    464  O   ALA A  70     -27.924  -5.597 -11.104  1.00 31.81           O  
+ANISOU  464  O   ALA A  70     5009   3496   3582    528   -977  -1001       O  
+ATOM    465  CB  ALA A  70     -25.901  -7.587  -9.548  1.00 28.26           C  
+ANISOU  465  CB  ALA A  70     4670   2837   3230    -57    241    504       C  
+ATOM    466  N   GLN A  71     -26.648  -4.397  -9.679  1.00 27.52           N  
+ANISOU  466  N   GLN A  71     5126   1746   3584   -307   1023   -144       N  
+ATOM    467  CA  GLN A  71     -27.596  -3.313  -9.530  1.00 23.82           C  
+ANISOU  467  CA  GLN A  71     3924   2035   3090   -391   -363   -180       C  
+ATOM    468  C   GLN A  71     -26.814  -2.001  -9.779  1.00 21.82           C  
+ANISOU  468  C   GLN A  71     4194   1619   2478     51   -312    293       C  
+ATOM    469  O   GLN A  71     -26.339  -1.283  -8.854  1.00 21.85           O  
+ANISOU  469  O   GLN A  71     3917   2424   1960    143   -185    272       O  
+ATOM    470  CB  GLN A  71     -28.248  -3.349  -8.142  1.00 34.25           C  
+ANISOU  470  CB  GLN A  71     5823   3563   3626    560    606   -461       C  
+ATOM    471  CG  GLN A  71     -29.470  -2.440  -7.994  1.00 27.96           C  
+ANISOU  471  CG  GLN A  71     4805   2594   3224   -446    593   -199       C  
+ATOM    472  CD  GLN A  71     -30.317  -2.816  -6.787  1.00 36.46           C  
+ANISOU  472  CD  GLN A  71     4884   5458   3509  -1300    -11   1338       C  
+ATOM    473  OE1 GLN A  71     -31.549  -2.749  -6.838  1.00 39.21           O  
+ANISOU  473  OE1 GLN A  71     4770   5783   4345   -292   -139    -29       O  
+ATOM    474  NE2 GLN A  71     -29.660  -3.206  -5.694  1.00 27.43           N  
+ANISOU  474  NE2 GLN A  71     3592   2979   3850   -892   -538   -149       N  
+ATOM    475  N   GLN A  72     -26.679  -1.712 -11.064  1.00 18.12           N  
+ANISOU  475  N   GLN A  72     3284   1375   2224    -29   -210   -122       N  
+ATOM    476  CA  GLN A  72     -25.805  -0.675 -11.530  1.00 20.42           C  
+ANISOU  476  CA  GLN A  72     4170   1572   2015   -461   -165   -435       C  
+ATOM    477  C   GLN A  72     -26.204   0.718 -11.130  1.00 18.32           C  
+ANISOU  477  C   GLN A  72     3137   1653   2168   -236   -474   -528       C  
+ATOM    478  O   GLN A  72     -25.353   1.620 -11.166  1.00 18.89           O  
+ANISOU  478  O   GLN A  72     3258   1789   2129   -378   -712   -220       O  
+ATOM    479  CB  GLN A  72     -25.806  -0.725 -13.052  1.00 20.88           C  
+ANISOU  479  CB  GLN A  72     3650   2365   1915   -214   -290   -757       C  
+ATOM    480  CG  GLN A  72     -24.930  -1.823 -13.491  1.00 27.09           C  
+ANISOU  480  CG  GLN A  72     4169   4069   2055    542   -238  -1078       C  
+ATOM    481  CD  GLN A  72     -24.862  -1.876 -14.986  1.00 20.01           C  
+ANISOU  481  CD  GLN A  72     2677   3060   1867    408   -744   -451       C  
+ATOM    482  OE1 GLN A  72     -24.706  -0.850 -15.682  1.00 18.80           O  
+ANISOU  482  OE1 GLN A  72     2202   2994   1945    683   -620   -561       O  
+ATOM    483  NE2 GLN A  72     -24.962  -3.062 -15.480  1.00 20.84           N  
+ANISOU  483  NE2 GLN A  72     2295   2931   2692   -263   -177   -371       N  
+ATOM    484  N   HIS A  73     -27.467   0.898 -10.733  1.00 17.02           N  
+ANISOU  484  N   HIS A  73     3161   1443   1862   -158   -859   -393       N  
+ATOM    485  CA  HIS A  73     -27.967   2.238 -10.419  1.00 16.27           C  
+ANISOU  485  CA  HIS A  73     2652   1468   2059    -46   -935   -206       C  
+ATOM    486  C   HIS A  73     -27.558   2.762  -9.071  1.00 14.57           C  
+ANISOU  486  C   HIS A  73     2313   1411   1811   -132   -746     82       C  
+ATOM    487  O   HIS A  73     -27.869   3.912  -8.748  1.00 15.51           O  
+ANISOU  487  O   HIS A  73     2853   1455   1583   -137   -796      3       O  
+ATOM    488  CB  HIS A  73     -29.494   2.352 -10.637  1.00 20.23           C  
+ANISOU  488  CB  HIS A  73     2566   2588   2532   -326   -986     -1       C  
+ATOM    489  CG  HIS A  73     -30.325   1.984  -9.435  1.00 18.02           C  
+ANISOU  489  CG  HIS A  73     2817   1764   2263   -623   -967   -586       C  
+ATOM    490  ND1 HIS A  73     -30.735   0.701  -9.187  1.00 22.87           N  
+ANISOU  490  ND1 HIS A  73     3261   2164   3264   -968   -239   -350       N  
+ATOM    491  CD2 HIS A  73     -30.843   2.773  -8.405  1.00 16.23           C  
+ANISOU  491  CD2 HIS A  73     2448   1822   1894   -349   -640    -13       C  
+ATOM    492  CE1 HIS A  73     -31.467   0.686  -8.050  1.00 25.89           C  
+ANISOU  492  CE1 HIS A  73     3474   2759   3602   -874   -102   -262       C  
+ATOM    493  NE2 HIS A  73     -31.521   1.954  -7.567  1.00 23.21           N  
+ANISOU  493  NE2 HIS A  73     3345   2201   3271   -821   -304    300       N  
+ATOM    494  N   ILE A  74     -26.862   1.941  -8.274  1.00 13.68           N  
+ANISOU  494  N   ILE A  74     2425   1315   1456    -85   -778    -49       N  
+ATOM    495  CA  ILE A  74     -26.412   2.372  -6.920  1.00 13.35           C  
+ANISOU  495  CA  ILE A  74     2553    941   1578     19   -726   -234       C  
+ATOM    496  C   ILE A  74     -24.900   2.455  -6.887  1.00 14.64           C  
+ANISOU  496  C   ILE A  74     2657   1338   1565     78   -613    -47       C  
+ATOM    497  O   ILE A  74     -24.221   1.482  -7.265  1.00 16.13           O  
+ANISOU  497  O   ILE A  74     2519   1609   1998    207   -519   -303       O  
+ATOM    498  CB  ILE A  74     -26.932   1.435  -5.803  1.00 14.77           C  
+ANISOU  498  CB  ILE A  74     2485   1520   1607    -93   -774   -118       C  
+ATOM    499  CG1 ILE A  74     -28.469   1.325  -5.878  1.00 17.92           C  
+ANISOU  499  CG1 ILE A  74     2570   1774   2464   -126   -164    131       C  
+ATOM    500  CG2 ILE A  74     -26.420   1.885  -4.443  1.00 14.95           C  
+ANISOU  500  CG2 ILE A  74     2842   1342   1494    132   -694    -74       C  
+ATOM    501  CD1 ILE A  74     -29.062   0.269  -4.976  1.00 24.06           C  
+ANISOU  501  CD1 ILE A  74     3516   2583   3040  -1192   -292    381       C  
+ATOM    502  N   VAL A  75     -24.381   3.606  -6.462  1.00 14.11           N  
+ANISOU  502  N   VAL A  75     2287   1496   1577   -138   -576    233       N  
+ATOM    503  CA  VAL A  75     -22.950   3.793  -6.231  1.00 13.66           C  
+ANISOU  503  CA  VAL A  75     2165   1437   1586    -30   -588     47       C  
+ATOM    504  C   VAL A  75     -22.680   3.519  -4.756  1.00 13.20           C  
+ANISOU  504  C   VAL A  75     2053   1251   1709    379   -561    -61       C  
+ATOM    505  O   VAL A  75     -23.403   4.006  -3.892  1.00 15.17           O  
+ANISOU  505  O   VAL A  75     2698   1562   1503    325   -443   -101       O  
+ATOM    506  CB  VAL A  75     -22.533   5.239  -6.620  1.00 15.13           C  
+ANISOU  506  CB  VAL A  75     2349   1846   1554   -417   -529    246       C  
+ATOM    507  CG1 VAL A  75     -21.123   5.558  -6.112  1.00 15.29           C  
+ANISOU  507  CG1 VAL A  75     2219   1739   1851   -234   -687    208       C  
+ATOM    508  CG2 VAL A  75     -22.655   5.435  -8.141  1.00 18.88           C  
+ANISOU  508  CG2 VAL A  75     2591   3076   1504   -163   -784    177       C  
+ATOM    509  N   TYR A  76     -21.638   2.734  -4.494  1.00 11.99           N  
+ANISOU  509  N   TYR A  76     2133   1031   1391    302   -983     69       N  
+ATOM    510  CA  TYR A  76     -21.221   2.385  -3.156  1.00 11.81           C  
+ANISOU  510  CA  TYR A  76     2292    972   1220    114   -825    -49       C  
+ATOM    511  C   TYR A  76     -19.930   3.112  -2.789  1.00 14.91           C  
+ANISOU  511  C   TYR A  76     2316   1416   1933     23   -613    -69       C  
+ATOM    512  O   TYR A  76     -18.860   2.823  -3.347  1.00 18.23           O  
+ANISOU  512  O   TYR A  76     2400   2319   2204    -18   -341   -452       O  
+ATOM    513  CB  TYR A  76     -21.059   0.852  -3.093  1.00 15.72           C  
+ANISOU  513  CB  TYR A  76     2802    979   2190    131   -865    130       C  
+ATOM    514  CG  TYR A  76     -22.388   0.162  -3.225  1.00 16.34           C  
+ANISOU  514  CG  TYR A  76     2921   1369   1919     77   -694   -161       C  
+ATOM    515  CD1 TYR A  76     -22.895  -0.212  -4.484  1.00 17.33           C  
+ANISOU  515  CD1 TYR A  76     2951   1246   2386    194  -1111   -334       C  
+ATOM    516  CD2 TYR A  76     -23.188  -0.039  -2.099  1.00 17.43           C  
+ANISOU  516  CD2 TYR A  76     2808   1571   2243    268   -586    253       C  
+ATOM    517  CE1 TYR A  76     -24.127  -0.820  -4.585  1.00 18.07           C  
+ANISOU  517  CE1 TYR A  76     2918   1221   2727    175   -491   -183       C  
+ATOM    518  CE2 TYR A  76     -24.432  -0.639  -2.198  1.00 18.56           C  
+ANISOU  518  CE2 TYR A  76     3010   1598   2443    100   -514   -270       C  
+ATOM    519  CZ  TYR A  76     -24.912  -0.981  -3.440  1.00 17.70           C  
+ANISOU  519  CZ  TYR A  76     3260    984   2478   -375   -675   -125       C  
+ATOM    520  OH  TYR A  76     -26.158  -1.565  -3.537  1.00 20.37           O  
+ANISOU  520  OH  TYR A  76     3070   1413   3255   -198  -1464   -368       O  
+ATOM    521  N   CYS A  77     -20.028   4.040  -1.841  1.00 15.82           N  
+ANISOU  521  N   CYS A  77     2615   1517   1878   -184   -714    -94       N  
+ATOM    522  CA  CYS A  77     -18.931   4.955  -1.533  1.00 14.86           C  
+ANISOU  522  CA  CYS A  77     2364   1342   1937      4   -575   -221       C  
+ATOM    523  C   CYS A  77     -18.537   4.960  -0.053  1.00 16.39           C  
+ANISOU  523  C   CYS A  77     2710   1456   2060    -54   -694    -73       C  
+ATOM    524  O   CYS A  77     -17.921   5.914   0.414  1.00 18.38           O  
+ANISOU  524  O   CYS A  77     2971   1266   2744    126  -1071   -304       O  
+ATOM    525  CB  CYS A  77     -19.265   6.370  -2.027  1.00 15.87           C  
+ANISOU  525  CB  CYS A  77     2293   1598   2138   -134   -694    167       C  
+ATOM    526  SG  CYS A  77     -20.893   6.969  -1.532  1.00 16.49           S  
+ANISOU  526  SG  CYS A  77     2678   1571   2014   -122   -466     93       S  
+ATOM    527  N   SER A  78     -18.871   3.893   0.677  1.00 17.72           N  
+ANISOU  527  N   SER A  78     3275   1428   2026    113   -673     16       N  
+ATOM    528  CA ASER A  78     -18.465   3.780   2.073  0.50 20.01           C  
+ANISOU  528  CA ASER A  78     3718   1592   2290   -310  -1099    228       C  
+ATOM    529  CA BSER A  78     -18.467   3.737   2.079  0.50 20.73           C  
+ANISOU  529  CA BSER A  78     3733   1783   2359   -345  -1170    341       C  
+ATOM    530  C   SER A  78     -16.934   3.634   2.138  1.00 22.15           C  
+ANISOU  530  C   SER A  78     3850   1847   2717    -20  -1014    278       C  
+ATOM    531  O   SER A  78     -16.298   3.086   1.211  1.00 27.74           O  
+ANISOU  531  O   SER A  78     3617   2681   4241    642   -574    245       O  
+ATOM    532  CB ASER A  78     -19.146   2.573   2.703  0.50 22.23           C  
+ANISOU  532  CB ASER A  78     4755   2262   1427   -763  -1300    520       C  
+ATOM    533  CB BSER A  78     -19.141   2.494   2.702  0.50 26.68           C  
+ANISOU  533  CB BSER A  78     4930   2324   2880   -976  -1477    787       C  
+ATOM    534  OG ASER A  78     -18.658   1.427   2.060  0.50 23.99           O  
+ANISOU  534  OG ASER A  78     3852   1605   3657   -672   -954    862       O  
+ATOM    535  OG BSER A  78     -19.215   2.576   4.123  0.50 29.11           O  
+ANISOU  535  OG BSER A  78     4423   3762   2872   -848  -1838   1860       O  
+ATOM    536  N   ASN A  79     -16.324   4.145   3.198  1.00 24.79           N  
+ANISOU  536  N   ASN A  79     4076   2690   2651   -445  -1348   1043       N  
+ATOM    537  CA  ASN A  79     -14.856   4.069   3.314  1.00 26.09           C  
+ANISOU  537  CA  ASN A  79     4008   2834   3069    127  -1118    626       C  
+ATOM    538  C   ASN A  79     -14.099   4.685   2.136  1.00 27.24           C  
+ANISOU  538  C   ASN A  79     4063   2723   3562    455  -1022   1190       C  
+ATOM    539  O   ASN A  79     -13.000   4.238   1.774  1.00 28.62           O  
+ANISOU  539  O   ASN A  79     4290   2735   3850    450   -681   1801       O  
+ATOM    540  CB  ASN A  79     -14.418   2.617   3.499  1.00 29.79           C  
+ANISOU  540  CB  ASN A  79     4166   3091   4059    152   -878   1557       C  
+ATOM    541  CG  ASN A  79     -14.801   2.069   4.856  1.00 32.67           C  
+ANISOU  541  CG  ASN A  79     4718   4131   3565    609   -640   1133       C  
+ATOM    542  OD1 ASN A  79     -14.939   0.869   5.023  1.00 38.45           O  
+ANISOU  542  OD1 ASN A  79     5561   4109   4939    328    372    670       O  
+ATOM    543  ND2 ASN A  79     -14.983   2.957   5.834  1.00 38.42           N  
+ANISOU  543  ND2 ASN A  79     6733   4376   3487  -1012   -863    682       N  
+ATOM    544  N   ASP A  80     -14.712   5.690   1.519  1.00 22.58           N  
+ANISOU  544  N   ASP A  80     3879   1766   2932    278   -562    692       N  
+ATOM    545  CA  ASP A  80     -14.081   6.437   0.446  1.00 19.78           C  
+ANISOU  545  CA  ASP A  80     2797   1937   2779    -53  -1014    688       C  
+ATOM    546  C   ASP A  80     -14.285   7.924   0.710  1.00 19.05           C  
+ANISOU  546  C   ASP A  80     2710   2127   2399    257   -917    508       C  
+ATOM    547  O   ASP A  80     -15.301   8.324   1.308  1.00 18.93           O  
+ANISOU  547  O   ASP A  80     2662   1808   2721    333   -996    533       O  
+ATOM    548  CB  ASP A  80     -14.696   6.041  -0.896  1.00 20.37           C  
+ANISOU  548  CB  ASP A  80     2918   2198   2623    -87   -528    212       C  
+ATOM    549  CG  ASP A  80     -13.897   6.577  -2.080  1.00 21.34           C  
+ANISOU  549  CG  ASP A  80     3104   2099   2904    260   -332    319       C  
+ATOM    550  OD1 ASP A  80     -13.058   5.828  -2.599  1.00 23.73           O  
+ANISOU  550  OD1 ASP A  80     2848   2586   3582    614     31    658       O  
+ATOM    551  OD2 ASP A  80     -14.088   7.747  -2.454  1.00 21.93           O  
+ANISOU  551  OD2 ASP A  80     3127   2293   2910    265   -783    654       O  
+ATOM    552  N   LEU A  81     -13.326   8.746   0.289  1.00 19.99           N  
+ANISOU  552  N   LEU A  81     2877   1754   2964     39  -1287    653       N  
+ATOM    553  CA  LEU A  81     -13.499  10.214   0.393  1.00 20.55           C  
+ANISOU  553  CA  LEU A  81     2669   1805   3332    -12  -1143    656       C  
+ATOM    554  C   LEU A  81     -14.852  10.651  -0.139  1.00 17.26           C  
+ANISOU  554  C   LEU A  81     2379   1957   2220    -50   -732    169       C  
+ATOM    555  O   LEU A  81     -15.494  11.509   0.445  1.00 18.28           O  
+ANISOU  555  O   LEU A  81     2154   1892   2898    148   -851    291       O  
+ATOM    556  CB  LEU A  81     -12.389  10.975  -0.352  1.00 21.57           C  
+ANISOU  556  CB  LEU A  81     1940   2095   4160     54   -722    472       C  
+ATOM    557  CG  LEU A  81     -12.421  12.518  -0.302  1.00 24.33           C  
+ANISOU  557  CG  LEU A  81     2770   2204   4268    389   -726    701       C  
+ATOM    558  CD1 LEU A  81     -12.406  13.031   1.119  1.00 26.74           C  
+ANISOU  558  CD1 LEU A  81     3220   2517   4420     -4  -1081   -305       C  
+ATOM    559  CD2 LEU A  81     -11.242  13.088  -1.055  1.00 28.45           C  
+ANISOU  559  CD2 LEU A  81     2151   3186   5472    342   -527    598       C  
+ATOM    560  N   LEU A  82     -15.302  10.026  -1.223  1.00 14.83           N  
+ANISOU  560  N   LEU A  82     1952   1383   2298     -4   -883    202       N  
+ATOM    561  CA  LEU A  82     -16.596  10.436  -1.818  1.00 14.98           C  
+ANISOU  561  CA  LEU A  82     2028   1492   2169     89   -873    192       C  
+ATOM    562  C   LEU A  82     -17.738  10.280  -0.820  1.00 15.04           C  
+ANISOU  562  C   LEU A  82     2382   1424   1906     70   -701    201       C  
+ATOM    563  O   LEU A  82     -18.598  11.164  -0.707  1.00 15.06           O  
+ANISOU  563  O   LEU A  82     2302   1543   1873    114   -865    -14       O  
+ATOM    564  CB  LEU A  82     -16.912   9.658  -3.108  1.00 12.91           C  
+ANISOU  564  CB  LEU A  82     1548   1646   1708    143   -626    284       C  
+ATOM    565  CG  LEU A  82     -18.230  10.005  -3.793  1.00 13.76           C  
+ANISOU  565  CG  LEU A  82     1851   1427   1949    354   -809    287       C  
+ATOM    566  CD1 LEU A  82     -18.331  11.492  -4.103  1.00 14.36           C  
+ANISOU  566  CD1 LEU A  82     2235   1473   1748    445   -233    475       C  
+ATOM    567  CD2 LEU A  82     -18.438   9.158  -5.033  1.00 18.48           C  
+ANISOU  567  CD2 LEU A  82     2735   2224   2060    272   -408   -223       C  
+ATOM    568  N   GLY A  83     -17.770   9.150  -0.111  1.00 14.64           N  
+ANISOU  568  N   GLY A  83     2376   1548   1636    -82   -812    260       N  
+ATOM    569  CA  GLY A  83     -18.803   8.969   0.942  1.00 16.19           C  
+ANISOU  569  CA  GLY A  83     2778   1321   2050    -75   -374     20       C  
+ATOM    570  C   GLY A  83     -18.697   9.963   2.096  1.00 17.03           C  
+ANISOU  570  C   GLY A  83     2719   1787   1965    -40   -733    -58       C  
+ATOM    571  O   GLY A  83     -19.717  10.415   2.621  1.00 17.32           O  
+ANISOU  571  O   GLY A  83     2939   1704   1935     10   -558   -123       O  
+ATOM    572  N   ASP A  84     -17.483  10.345   2.481  1.00 15.65           N  
+ANISOU  572  N   ASP A  84     2870   1354   1721    162  -1016    233       N  
+ATOM    573  CA  ASP A  84     -17.344  11.371   3.537  1.00 17.85           C  
+ANISOU  573  CA  ASP A  84     3044   1408   2328    -64  -1349     34       C  
+ATOM    574  C   ASP A  84     -17.897  12.720   3.055  1.00 17.36           C  
+ANISOU  574  C   ASP A  84     2853   1786   1955    284   -761    277       C  
+ATOM    575  O   ASP A  84     -18.555  13.442   3.812  1.00 19.45           O  
+ANISOU  575  O   ASP A  84     3341   1998   2050    232   -749   -203       O  
+ATOM    576  CB  ASP A  84     -15.879  11.530   3.981  1.00 20.71           C  
+ANISOU  576  CB  ASP A  84     2882   1917   3070    -40  -1501    435       C  
+ATOM    577  CG  ASP A  84     -15.271  10.247   4.563  1.00 26.17           C  
+ANISOU  577  CG  ASP A  84     3766   2151   4026    330  -1305    686       C  
+ATOM    578  OD1 ASP A  84     -16.004   9.340   5.039  0.50 23.74           O  
+ANISOU  578  OD1 ASP A  84     4590   1929   2501   -178  -2106    767       O  
+ATOM    579  OD2 ASP A  84     -14.029  10.172   4.541  0.50 28.13           O  
+ANISOU  579  OD2 ASP A  84     3394   2062   5229    127  -3050    144       O  
+ATOM    580  N   LEU A  85     -17.641  13.056   1.793  1.00 15.39           N  
+ANISOU  580  N   LEU A  85     2415   1613   1817     73  -1139    454       N  
+ATOM    581  CA  LEU A  85     -18.120  14.344   1.226  1.00 15.37           C  
+ANISOU  581  CA  LEU A  85     2465   1356   2016      2   -680    364       C  
+ATOM    582  C   LEU A  85     -19.637  14.381   1.005  1.00 15.74           C  
+ANISOU  582  C   LEU A  85     2474   1493   2014    -23   -560   -133       C  
+ATOM    583  O   LEU A  85     -20.271  15.391   1.230  1.00 14.88           O  
+ANISOU  583  O   LEU A  85     2367   1315   1970   -146   -485    154       O  
+ATOM    584  CB  LEU A  85     -17.406  14.633  -0.082  1.00 16.72           C  
+ANISOU  584  CB  LEU A  85     2113   1782   2457    -16   -568    552       C  
+ATOM    585  CG  LEU A  85     -15.884  14.826   0.086  1.00 18.12           C  
+ANISOU  585  CG  LEU A  85     2085   2388   2410   -203   -650    219       C  
+ATOM    586  CD1 LEU A  85     -15.345  15.247  -1.271  1.00 20.19           C  
+ANISOU  586  CD1 LEU A  85     2474   2542   2655    674   -132    696       C  
+ATOM    587  CD2 LEU A  85     -15.455  15.834   1.171  1.00 20.90           C  
+ANISOU  587  CD2 LEU A  85     2754   2546   2640    -17   -931     88       C  
+ATOM    588  N   PHE A  86     -20.204  13.273   0.509  1.00 14.45           N  
+ANISOU  588  N   PHE A  86     2324   1302   1863    -84   -796    194       N  
+ATOM    589  CA  PHE A  86     -21.632  13.176   0.282  1.00 15.31           C  
+ANISOU  589  CA  PHE A  86     2453   1672   1688   -375   -556     55       C  
+ATOM    590  C   PHE A  86     -22.423  12.845   1.561  1.00 17.39           C  
+ANISOU  590  C   PHE A  86     2927   1893   1784   -457   -517    255       C  
+ATOM    591  O   PHE A  86     -23.637  13.079   1.611  1.00 17.93           O  
+ANISOU  591  O   PHE A  86     3063   2006   1743    190   -208   -238       O  
+ATOM    592  CB  PHE A  86     -21.905  12.136  -0.789  1.00 14.38           C  
+ANISOU  592  CB  PHE A  86     2206   1837   1417    -80   -689      7       C  
+ATOM    593  CG  PHE A  86     -21.776  12.655  -2.217  1.00 13.84           C  
+ANISOU  593  CG  PHE A  86     2211   1490   1558    240   -648    184       C  
+ATOM    594  CD1 PHE A  86     -21.137  13.866  -2.510  1.00 16.23           C  
+ANISOU  594  CD1 PHE A  86     2431   1752   1982    264   -395    497       C  
+ATOM    595  CD2 PHE A  86     -22.303  11.916  -3.270  1.00 15.03           C  
+ANISOU  595  CD2 PHE A  86     2236   1706   1768     85   -504    -98       C  
+ATOM    596  CE1 PHE A  86     -21.052  14.340  -3.829  1.00 13.83           C  
+ANISOU  596  CE1 PHE A  86     1983   1666   1603    302   -315     60       C  
+ATOM    597  CE2 PHE A  86     -22.209  12.372  -4.581  1.00 14.97           C  
+ANISOU  597  CE2 PHE A  86     2168   1552   1968      1   -381    156       C  
+ATOM    598  CZ  PHE A  86     -21.582  13.588  -4.865  1.00 14.18           C  
+ANISOU  598  CZ  PHE A  86     2064   1475   1848     74   -244     39       C  
+ATOM    599  N   GLY A  87     -21.735  12.308   2.579  1.00 16.12           N  
+ANISOU  599  N   GLY A  87     3097   1459   1566    -84   -581   -232       N  
+ATOM    600  CA  GLY A  87     -22.375  12.011   3.861  1.00 17.82           C  
+ANISOU  600  CA  GLY A  87     3235   1528   2007   -235   -320   -151       C  
+ATOM    601  C   GLY A  87     -23.225  10.765   3.843  1.00 18.28           C  
+ANISOU  601  C   GLY A  87     3323   1583   2037   -287    -48   -247       C  
+ATOM    602  O   GLY A  87     -24.099  10.608   4.714  1.00 20.48           O  
+ANISOU  602  O   GLY A  87     3571   2216   1993   -467     52   -412       O  
+ATOM    603  N   VAL A  88     -22.968   9.885   2.863  1.00 15.30           N  
+ANISOU  603  N   VAL A  88     2845   1381   1584   -508   -353   -116       N  
+ATOM    604  CA  VAL A  88     -23.773   8.627   2.687  1.00 13.90           C  
+ANISOU  604  CA  VAL A  88     2806   1051   1423   -227   -520   -207       C  
+ATOM    605  C   VAL A  88     -22.862   7.467   2.278  1.00 14.17           C  
+ANISOU  605  C   VAL A  88     2904   1236   1242     76   -353    275       C  
+ATOM    606  O   VAL A  88     -21.812   7.707   1.661  1.00 17.48           O  
+ANISOU  606  O   VAL A  88     2916   1515   2207   -267   -316    -74       O  
+ATOM    607  CB  VAL A  88     -24.909   8.766   1.611  1.00 15.42           C  
+ANISOU  607  CB  VAL A  88     2593   1790   1473     24   -374     66       C  
+ATOM    608  CG1 VAL A  88     -25.978   9.778   2.033  1.00 20.38           C  
+ANISOU  608  CG1 VAL A  88     3263   1990   2489    142   -292   -736       C  
+ATOM    609  CG2 VAL A  88     -24.345   9.158   0.245  1.00 18.44           C  
+ANISOU  609  CG2 VAL A  88     3145   1911   1950   -407     -4    438       C  
+ATOM    610  N   PRO A  89     -23.236   6.209   2.615  1.00 15.13           N  
+ANISOU  610  N   PRO A  89     2791   1389   1566   -267   -265     -2       N  
+ATOM    611  CA  PRO A  89     -22.436   5.043   2.184  1.00 15.49           C  
+ANISOU  611  CA  PRO A  89     2935   1210   1740   -321   -460    -21       C  
+ATOM    612  C   PRO A  89     -22.804   4.568   0.779  1.00 15.11           C  
+ANISOU  612  C   PRO A  89     2787   1368   1583     12   -580    194       C  
+ATOM    613  O   PRO A  89     -22.081   3.756   0.195  1.00 16.75           O  
+ANISOU  613  O   PRO A  89     2676   1715   1972   -217   -470    190       O  
+ATOM    614  CB  PRO A  89     -22.800   3.975   3.215  1.00 18.14           C  
+ANISOU  614  CB  PRO A  89     3443   1309   2140   -158   -415    237       C  
+ATOM    615  CG  PRO A  89     -24.224   4.327   3.571  1.00 17.94           C  
+ANISOU  615  CG  PRO A  89     3368   1292   2155   -224     33    226       C  
+ATOM    616  CD  PRO A  89     -24.244   5.838   3.626  1.00 17.86           C  
+ANISOU  616  CD  PRO A  89     3362   1327   2095   -621     35    189       C  
+ATOM    617  N   SER A  90     -23.917   5.073   0.241  1.00 14.72           N  
+ANISOU  617  N   SER A  90     2649   1480   1463   -101   -656    -55       N  
+ATOM    618  CA  SER A  90     -24.379   4.691  -1.109  1.00 13.69           C  
+ANISOU  618  CA  SER A  90     2678   1181   1339   -178   -790    307       C  
+ATOM    619  C   SER A  90     -25.396   5.712  -1.570  1.00 14.31           C  
+ANISOU  619  C   SER A  90     2429   1386   1621    -68   -367    275       C  
+ATOM    620  O   SER A  90     -25.974   6.422  -0.746  1.00 16.30           O  
+ANISOU  620  O   SER A  90     2893   1604   1695    -14   -511   -149       O  
+ATOM    621  CB  SER A  90     -25.051   3.287  -1.118  1.00 15.82           C  
+ANISOU  621  CB  SER A  90     2822   1178   2009   -107   -353    251       C  
+ATOM    622  OG  SER A  90     -26.282   3.288  -0.361  1.00 18.72           O  
+ANISOU  622  OG  SER A  90     2880   1657   2574   -334   -486    276       O  
+ATOM    623  N   PHE A  91     -25.619   5.782  -2.883  1.00 14.24           N  
+ANISOU  623  N   PHE A  91     2462   1218   1731     81   -574    329       N  
+ATOM    624  CA  PHE A  91     -26.649   6.671  -3.406  1.00 13.29           C  
+ANISOU  624  CA  PHE A  91     2160   1326   1563     61   -578    116       C  
+ATOM    625  C   PHE A  91     -27.108   6.195  -4.758  1.00 13.41           C  
+ANISOU  625  C   PHE A  91     2030   1408   1657    -41   -401   -159       C  
+ATOM    626  O   PHE A  91     -26.366   5.498  -5.494  1.00 13.72           O  
+ANISOU  626  O   PHE A  91     2062   1199   1951    164   -337   -171       O  
+ATOM    627  CB  PHE A  91     -26.201   8.166  -3.479  1.00 13.47           C  
+ANISOU  627  CB  PHE A  91     2288   1277   1551     90   -389   -190       C  
+ATOM    628  CG  PHE A  91     -25.031   8.432  -4.388  1.00 13.00           C  
+ANISOU  628  CG  PHE A  91     2279   1167   1490     61   -431    161       C  
+ATOM    629  CD1 PHE A  91     -25.219   8.774  -5.754  1.00 13.71           C  
+ANISOU  629  CD1 PHE A  91     2702   1164   1343    187   -335   -169       C  
+ATOM    630  CD2 PHE A  91     -23.720   8.328  -3.900  1.00 15.66           C  
+ANISOU  630  CD2 PHE A  91     2300   1445   2203    216   -429      9       C  
+ATOM    631  CE1 PHE A  91     -24.124   9.017  -6.574  1.00 14.41           C  
+ANISOU  631  CE1 PHE A  91     2175   1372   1928    367   -447   -302       C  
+ATOM    632  CE2 PHE A  91     -22.625   8.605  -4.717  1.00 14.94           C  
+ANISOU  632  CE2 PHE A  91     2226   1470   1977     81   -343   -155       C  
+ATOM    633  CZ  PHE A  91     -22.827   8.944  -6.062  1.00 15.42           C  
+ANISOU  633  CZ  PHE A  91     2309   1518   2031    188   -581   -216       C  
+ATOM    634  N   SER A  92     -28.341   6.552  -5.091  1.00 13.72           N  
+ANISOU  634  N   SER A  92     2075   1454   1684    292   -341   -150       N  
+ATOM    635  CA  SER A  92     -28.888   6.206  -6.420  1.00 15.10           C  
+ANISOU  635  CA  SER A  92     2279   1638   1820    -69   -651     78       C  
+ATOM    636  C   SER A  92     -28.495   7.225  -7.498  1.00 15.76           C  
+ANISOU  636  C   SER A  92     2373   1744   1871    142   -177    -71       C  
+ATOM    637  O   SER A  92     -28.685   8.445  -7.323  1.00 15.61           O  
+ANISOU  637  O   SER A  92     2362   1731   1836     15   -288   -226       O  
+ATOM    638  CB  SER A  92     -30.411   6.121  -6.352  1.00 18.24           C  
+ANISOU  638  CB  SER A  92     2181   2475   2274   -122   -675    140       C  
+ATOM    639  OG  SER A  92     -30.934   6.040  -7.673  1.00 17.75           O  
+ANISOU  639  OG  SER A  92     2749   1732   2263   -418   -724     25       O  
+ATOM    640  N   VAL A  93     -27.988   6.728  -8.624  1.00 13.61           N  
+ANISOU  640  N   VAL A  93     2035   1668   1468    -64   -553    -44       N  
+ATOM    641  CA  VAL A  93     -27.641   7.599  -9.764  1.00 13.38           C  
+ANISOU  641  CA  VAL A  93     2108   1333   1641    -13   -528    -61       C  
+ATOM    642  C   VAL A  93     -28.853   8.228 -10.450  1.00 14.84           C  
+ANISOU  642  C   VAL A  93     2291   1463   1884    132   -586   -170       C  
+ATOM    643  O   VAL A  93     -28.687   9.187 -11.224  1.00 17.10           O  
+ANISOU  643  O   VAL A  93     2539   1854   2103    298   -449    126       O  
+ATOM    644  CB  VAL A  93     -26.827   6.821 -10.839  1.00 13.45           C  
+ANISOU  644  CB  VAL A  93     1719   1621   1771     -7   -598   -208       C  
+ATOM    645  CG1 VAL A  93     -25.540   6.232 -10.223  1.00 17.67           C  
+ANISOU  645  CG1 VAL A  93     2456   2346   1909    425   -852    231       C  
+ATOM    646  CG2 VAL A  93     -27.711   5.761 -11.552  1.00 14.97           C  
+ANISOU  646  CG2 VAL A  93     2338   1503   1848    -73   -681   -319       C  
+ATOM    647  N   LYS A  94     -30.056   7.701 -10.171  1.00 15.50           N  
+ANISOU  647  N   LYS A  94     2090   1574   2226    184   -730   -248       N  
+ATOM    648  CA  LYS A  94     -31.319   8.179 -10.783  1.00 16.46           C  
+ANISOU  648  CA  LYS A  94     2006   1811   2436    293   -583    -63       C  
+ATOM    649  C   LYS A  94     -31.775   9.537 -10.262  1.00 17.56           C  
+ANISOU  649  C   LYS A  94     2446   1838   2385    137   -792   -282       C  
+ATOM    650  O   LYS A  94     -32.550  10.236 -10.931  1.00 20.59           O  
+ANISOU  650  O   LYS A  94     2455   2138   3226    248   -705    155       O  
+ATOM    651  CB  LYS A  94     -32.454   7.152 -10.604  1.00 21.65           C  
+ANISOU  651  CB  LYS A  94     2619   2033   3571   -179  -1220   -285       C  
+ATOM    652  CG  LYS A  94     -32.159   5.748 -11.130  1.00 29.65           C  
+ANISOU  652  CG  LYS A  94     3444   2469   5351    507  -1902   -976       C  
+ATOM    653  CD  LYS A  94     -33.346   4.808 -10.913  1.00 41.63           C  
+ANISOU  653  CD  LYS A  94     4693   3981   7144   -716  -2529  -1126       C  
+ATOM    654  CE  LYS A  94     -33.164   3.456 -11.602  1.00 43.68           C  
+ANISOU  654  CE  LYS A  94     5783   4069   6741   1662  -3316   -799       C  
+ATOM    655  NZ  LYS A  94     -33.112   3.547 -13.097  0.50 46.50           N  
+ANISOU  655  NZ  LYS A  94     8149   2909   6608   4006  -5758  -1762       N  
+ATOM    656  N   GLU A  95     -31.274   9.896  -9.083  1.00 15.63           N  
+ANISOU  656  N   GLU A  95     2317   1496   2124    118   -379    -73       N  
+ATOM    657  CA AGLU A  95     -31.741  11.049  -8.316  0.50 16.75           C  
+ANISOU  657  CA AGLU A  95     2505   1552   2305   -124     90    -91       C  
+ATOM    658  CA BGLU A  95     -31.772  11.063  -8.359  0.50 17.30           C  
+ANISOU  658  CA BGLU A  95     2613   1542   2416   -159    135   -148       C  
+ATOM    659  C   GLU A  95     -30.867  12.271  -8.600  1.00 14.34           C  
+ANISOU  659  C   GLU A  95     1978   1476   1994     32   -375    203       C  
+ATOM    660  O   GLU A  95     -30.044  12.669  -7.742  1.00 15.58           O  
+ANISOU  660  O   GLU A  95     2422   1455   2042    -27   -224    -43       O  
+ATOM    661  CB AGLU A  95     -31.679  10.704  -6.820  0.50 18.93           C  
+ANISOU  661  CB AGLU A  95     2681   2065   2443   -689     49    281       C  
+ATOM    662  CB BGLU A  95     -31.912  10.725  -6.872  0.50 21.65           C  
+ANISOU  662  CB BGLU A  95     3156   2472   2596   -748     90    289       C  
+ATOM    663  CG AGLU A  95     -32.551   9.525  -6.402  0.50 20.54           C  
+ANISOU  663  CG AGLU A  95     2690   1665   3447   -401   -117    535       C  
+ATOM    664  CG BGLU A  95     -32.982   9.672  -6.594  0.50 26.24           C  
+ANISOU  664  CG BGLU A  95     3659   2174   4133   -932     21      5       C  
+ATOM    665  CD AGLU A  95     -34.030   9.835  -6.513  0.50 23.57           C  
+ANISOU  665  CD AGLU A  95     2538   2288   4127   -513    -10    143       C  
+ATOM    666  CD BGLU A  95     -33.057   9.296  -5.134  0.50 33.65           C  
+ANISOU  666  CD BGLU A  95     4974   3586   4224   -451    541    230       C  
+ATOM    667  OE1AGLU A  95     -34.408  11.037  -6.440  0.50 22.49           O  
+ANISOU  667  OE1AGLU A  95     2547   2223   3775   -427     23    876       O  
+ATOM    668  OE1BGLU A  95     -32.018   8.877  -4.586  0.50 42.34           O  
+ANISOU  668  OE1BGLU A  95     5693   5458   4933   1057    630   -263       O  
+ATOM    669  OE2AGLU A  95     -34.809   8.869  -6.672  0.50 23.79           O  
+ANISOU  669  OE2AGLU A  95     2137   2822   4080   -611   -111     28       O  
+ATOM    670  OE2BGLU A  95     -34.149   9.412  -4.536  0.50 40.91           O  
+ANISOU  670  OE2BGLU A  95     4954   3966   6624    284    882   -372       O  
+ATOM    671  N   HIS A  96     -31.012  12.866  -9.800  1.00 12.99           N  
+ANISOU  671  N   HIS A  96     1944   1216   1776   -169   -455   -142       N  
+ATOM    672  CA  HIS A  96     -30.008  13.901 -10.209  1.00 12.81           C  
+ANISOU  672  CA  HIS A  96     1949   1339   1578   -167   -195   -144       C  
+ATOM    673  C   HIS A  96     -30.061  15.120  -9.321  1.00 11.11           C  
+ANISOU  673  C   HIS A  96     1461   1218   1539     73   -207   -129       C  
+ATOM    674  O   HIS A  96     -29.016  15.677  -8.971  1.00 12.01           O  
+ANISOU  674  O   HIS A  96     1573   1380   1610     99   -464    -22       O  
+ATOM    675  CB  HIS A  96     -30.121  14.310 -11.671  1.00 13.32           C  
+ANISOU  675  CB  HIS A  96     2037   1436   1587    250   -575   -213       C  
+ATOM    676  CG  HIS A  96     -29.731  13.202 -12.638  1.00 14.10           C  
+ANISOU  676  CG  HIS A  96     1986   1638   1731    173   -533   -408       C  
+ATOM    677  ND1 HIS A  96     -29.542  13.419 -13.958  1.00 16.74           N  
+ANISOU  677  ND1 HIS A  96     2584   1954   1819   -397   -406   -553       N  
+ATOM    678  CD2 HIS A  96     -29.536  11.830 -12.438  1.00 14.00           C  
+ANISOU  678  CD2 HIS A  96     1636   1755   1927    191   -263   -248       C  
+ATOM    679  CE1 HIS A  96     -29.193  12.267 -14.561  1.00 17.49           C  
+ANISOU  679  CE1 HIS A  96     2819   1908   1918    101   -382   -256       C  
+ATOM    680  NE2 HIS A  96     -29.221  11.290 -13.652  1.00 15.45           N  
+ANISOU  680  NE2 HIS A  96     2214   1893   1761    271   -326   -226       N  
+ATOM    681  N   ARG A  97     -31.261  15.560  -8.956  1.00 13.02           N  
+ANISOU  681  N   ARG A  97     1725   1562   1659    367   -130   -152       N  
+ATOM    682  CA  ARG A  97     -31.385  16.729  -8.041  1.00 12.43           C  
+ANISOU  682  CA  ARG A  97     1566   1492   1663    209   -170   -158       C  
+ATOM    683  C   ARG A  97     -30.725  16.433  -6.696  1.00 12.92           C  
+ANISOU  683  C   ARG A  97     1853   1360   1696   -113   -246     15       C  
+ATOM    684  O   ARG A  97     -29.995  17.282  -6.168  1.00 12.18           O  
+ANISOU  684  O   ARG A  97     1735   1477   1415     47   -378   -184       O  
+ATOM    685  CB  ARG A  97     -32.877  17.076  -7.813  1.00 14.36           C  
+ANISOU  685  CB  ARG A  97     1463   1928   2063    263   -356   -178       C  
+ATOM    686  CG  ARG A  97     -33.137  18.191  -6.765  1.00 14.24           C  
+ANISOU  686  CG  ARG A  97     1602   1488   2319    102   -325   -134       C  
+ATOM    687  CD  ARG A  97     -32.365  19.475  -7.075  1.00 12.16           C  
+ANISOU  687  CD  ARG A  97     1428   1652   1539    100   -329     53       C  
+ATOM    688  NE  ARG A  97     -32.680  20.055  -8.407  1.00 13.38           N  
+ANISOU  688  NE  ARG A  97     1701   1701   1682    616   -194    285       N  
+ATOM    689  CZ  ARG A  97     -31.875  20.930  -9.034  1.00 13.14           C  
+ANISOU  689  CZ  ARG A  97     1811   1617   1562    177   -508    208       C  
+ATOM    690  NH1 ARG A  97     -30.711  21.281  -8.469  1.00 12.52           N  
+ANISOU  690  NH1 ARG A  97     1785   1567   1403    375   -341    -83       N  
+ATOM    691  NH2 ARG A  97     -32.226  21.456 -10.233  1.00 13.85           N  
+ANISOU  691  NH2 ARG A  97     1872   1817   1571    718   -573    110       N  
+ATOM    692  N   LYS A  98     -30.936  15.234  -6.134  1.00 12.60           N  
+ANISOU  692  N   LYS A  98     1768   1328   1688    186   -202    187       N  
+ATOM    693  CA  LYS A  98     -30.284  14.914  -4.844  1.00 13.65           C  
+ANISOU  693  CA  LYS A  98     1780   1492   1911    -85   -424    263       C  
+ATOM    694  C   LYS A  98     -28.748  14.880  -4.971  1.00 12.56           C  
+ANISOU  694  C   LYS A  98     1782   1439   1551    197   -339    -32       C  
+ATOM    695  O   LYS A  98     -28.057  15.344  -4.051  1.00 12.49           O  
+ANISOU  695  O   LYS A  98     1725   1299   1719    242   -483     19       O  
+ATOM    696  CB  LYS A  98     -30.800  13.586  -4.263  1.00 13.77           C  
+ANISOU  696  CB  LYS A  98     1938   1482   1811   -143     18    183       C  
+ATOM    697  CG  LYS A  98     -32.297  13.599  -3.974  1.00 22.24           C  
+ANISOU  697  CG  LYS A  98     2016   2794   3638   -288    308    700       C  
+ATOM    698  CD  LYS A  98     -32.729  12.361  -3.208  1.00 27.95           C  
+ANISOU  698  CD  LYS A  98     3463   3310   3846  -1173    505    594       C  
+ATOM    699  CE  LYS A  98     -34.229  12.395  -2.958  1.00 35.22           C  
+ANISOU  699  CE  LYS A  98     3364   4637   5379  -1170    329    931       C  
+ATOM    700  NZ  LYS A  98     -34.598  11.331  -1.991  1.00 40.82           N  
+ANISOU  700  NZ  LYS A  98     5389   4813   5308   -858   1179    779       N  
+ATOM    701  N   ILE A  99     -28.233  14.383  -6.102  1.00 10.87           N  
+ANISOU  701  N   ILE A  99     1322   1278   1529     -7   -442    101       N  
+ATOM    702  CA  ILE A  99     -26.770  14.405  -6.357  1.00 11.63           C  
+ANISOU  702  CA  ILE A  99     1552   1104   1762    121   -122   -176       C  
+ATOM    703  C   ILE A  99     -26.265  15.863  -6.464  1.00 10.82           C  
+ANISOU  703  C   ILE A  99     1680   1150   1280     16   -491    -47       C  
+ATOM    704  O   ILE A  99     -25.270  16.225  -5.824  1.00 11.75           O  
+ANISOU  704  O   ILE A  99     1672   1324   1467    139   -506   -187       O  
+ATOM    705  CB  ILE A  99     -26.407  13.559  -7.583  1.00 10.21           C  
+ANISOU  705  CB  ILE A  99     1495   1198   1183    -41   -205    121       C  
+ATOM    706  CG1 ILE A  99     -26.681  12.091  -7.246  1.00 12.89           C  
+ANISOU  706  CG1 ILE A  99     2277   1069   1549   -255   -557   -170       C  
+ATOM    707  CG2 ILE A  99     -24.939  13.735  -7.949  1.00 11.84           C  
+ANISOU  707  CG2 ILE A  99     1384   1503   1609    280    -87   -149       C  
+ATOM    708  CD1 ILE A  99     -26.735  11.187  -8.470  1.00 14.00           C  
+ANISOU  708  CD1 ILE A  99     2231   1465   1622     -8   -587   -460       C  
+ATOM    709  N   TYR A 100     -26.975  16.704  -7.226  1.00 10.74           N  
+ANISOU  709  N   TYR A 100     1620   1097   1362    199   -230    -34       N  
+ATOM    710  CA  TYR A 100     -26.627  18.128  -7.274  1.00 11.24           C  
+ANISOU  710  CA  TYR A 100     1988   1077   1205    221   -426    -79       C  
+ATOM    711  C   TYR A 100     -26.568  18.741  -5.867  1.00 11.66           C  
+ANISOU  711  C   TYR A 100     1890   1342   1197      0   -191    -98       C  
+ATOM    712  O   TYR A 100     -25.600  19.438  -5.540  1.00 11.05           O  
+ANISOU  712  O   TYR A 100     1724   1159   1314    257   -364   -167       O  
+ATOM    713  CB  TYR A 100     -27.555  18.926  -8.205  1.00 11.25           C  
+ANISOU  713  CB  TYR A 100     1922   1366    985    225   -367      2       C  
+ATOM    714  CG  TYR A 100     -26.993  19.039  -9.635  1.00 10.03           C  
+ANISOU  714  CG  TYR A 100     1804    952   1051    180   -269   -150       C  
+ATOM    715  CD1 TYR A 100     -26.669  17.902 -10.412  1.00 13.19           C  
+ANISOU  715  CD1 TYR A 100     2025   1373   1613    381   -332   -539       C  
+ATOM    716  CD2 TYR A 100     -26.705  20.282 -10.166  1.00 10.97           C  
+ANISOU  716  CD2 TYR A 100     1576   1304   1289     74   -318    325       C  
+ATOM    717  CE1 TYR A 100     -26.107  18.047 -11.666  1.00 14.65           C  
+ANISOU  717  CE1 TYR A 100     2118   1783   1663     48   -366   -140       C  
+ATOM    718  CE2 TYR A 100     -26.170  20.435 -11.441  1.00 12.00           C  
+ANISOU  718  CE2 TYR A 100     1941   1498   1119     63   -376   -132       C  
+ATOM    719  CZ  TYR A 100     -25.853  19.324 -12.180  1.00 13.25           C  
+ANISOU  719  CZ  TYR A 100     2001   1648   1386    273   -503   -262       C  
+ATOM    720  OH  TYR A 100     -25.255  19.475 -13.424  1.00 15.32           O  
+ANISOU  720  OH  TYR A 100     2474   1877   1468    324   -371     78       O  
+ATOM    721  N   THR A 101     -27.567  18.451  -5.030  1.00 11.08           N  
+ANISOU  721  N   THR A 101     1797   1264   1146    276   -155    -27       N  
+ATOM    722  CA  THR A 101     -27.568  18.979  -3.652  1.00 10.90           C  
+ANISOU  722  CA  THR A 101     1805   1249   1086    229   -103     64       C  
+ATOM    723  C   THR A 101     -26.322  18.537  -2.875  1.00 12.15           C  
+ANISOU  723  C   THR A 101     1900   1294   1420    149   -311    -81       C  
+ATOM    724  O   THR A 101     -25.711  19.335  -2.162  1.00 13.34           O  
+ANISOU  724  O   THR A 101     2107   1331   1628    146   -293   -277       O  
+ATOM    725  CB  THR A 101     -28.871  18.546  -2.945  1.00 12.01           C  
+ANISOU  725  CB  THR A 101     1694   1718   1149    326    -94    181       C  
+ATOM    726  OG1 THR A 101     -29.973  19.143  -3.646  1.00 13.24           O  
+ANISOU  726  OG1 THR A 101     1901   1385   1742    414   -203    278       O  
+ATOM    727  CG2 THR A 101     -28.903  18.970  -1.476  1.00 14.48           C  
+ANISOU  727  CG2 THR A 101     2477   1648   1375    -86     59   -159       C  
+ATOM    728  N   MET A 102     -25.969  17.257  -2.977  1.00 12.60           N  
+ANISOU  728  N   MET A 102     2050   1425   1312    476   -418   -149       N  
+ATOM    729  CA  MET A 102     -24.766  16.754  -2.284  1.00 11.35           C  
+ANISOU  729  CA  MET A 102     1770   1005   1536    270   -344    -66       C  
+ATOM    730  C   MET A 102     -23.497  17.455  -2.801  1.00 11.91           C  
+ANISOU  730  C   MET A 102     1966   1202   1355     83   -430     56       C  
+ATOM    731  O   MET A 102     -22.582  17.740  -2.011  1.00 13.57           O  
+ANISOU  731  O   MET A 102     2001   1425   1729   -100   -536    -16       O  
+ATOM    732  CB  MET A 102     -24.666  15.220  -2.423  1.00 11.63           C  
+ANISOU  732  CB  MET A 102     1911    931   1575     86   -366    264       C  
+ATOM    733  CG  MET A 102     -25.748  14.520  -1.611  1.00 14.98           C  
+ANISOU  733  CG  MET A 102     2232   1556   1901   -299     44    -46       C  
+ATOM    734  SD  MET A 102     -25.590  12.705  -1.554  1.00 16.80           S  
+ANISOU  734  SD  MET A 102     2586   1647   2147      0   -527    285       S  
+ATOM    735  CE  MET A 102     -26.029  12.276  -3.227  1.00 17.26           C  
+ANISOU  735  CE  MET A 102     2776   1691   2089   -108   -584    133       C  
+ATOM    736  N   ILE A 103     -23.436  17.714  -4.109  1.00 10.36           N  
+ANISOU  736  N   ILE A 103     1633    916   1386     77   -356    -58       N  
+ATOM    737  CA  ILE A 103     -22.311  18.459  -4.665  1.00 10.49           C  
+ANISOU  737  CA  ILE A 103     1715   1194   1076    -15   -414    -65       C  
+ATOM    738  C   ILE A 103     -22.320  19.910  -4.183  1.00 11.05           C  
+ANISOU  738  C   ILE A 103     1661   1194   1341    170   -572   -119       C  
+ATOM    739  O   ILE A 103     -21.270  20.412  -3.774  1.00 11.83           O  
+ANISOU  739  O   ILE A 103     1624   1277   1591    114   -606   -207       O  
+ATOM    740  CB  ILE A 103     -22.293  18.396  -6.200  1.00 12.05           C  
+ANISOU  740  CB  ILE A 103     2034   1506   1037      9   -380   -101       C  
+ATOM    741  CG1 ILE A 103     -22.083  16.910  -6.621  1.00 12.76           C  
+ANISOU  741  CG1 ILE A 103     1876   1572   1400      0   -611   -229       C  
+ATOM    742  CG2 ILE A 103     -21.203  19.328  -6.765  1.00 13.74           C  
+ANISOU  742  CG2 ILE A 103     2108   1852   1259    -92   -316    -47       C  
+ATOM    743  CD1 ILE A 103     -22.304  16.644  -8.100  1.00 14.54           C  
+ANISOU  743  CD1 ILE A 103     1979   2137   1406   -164   -430   -434       C  
+ATOM    744  N   TYR A 104     -23.480  20.580  -4.171  1.00 11.87           N  
+ANISOU  744  N   TYR A 104     1976   1120   1410    394   -162   -152       N  
+ATOM    745  CA  TYR A 104     -23.509  22.002  -3.713  1.00 11.87           C  
+ANISOU  745  CA  TYR A 104     1889   1262   1357    299   -571   -331       C  
+ATOM    746  C   TYR A 104     -22.959  22.139  -2.289  1.00 12.10           C  
+ANISOU  746  C   TYR A 104     2281   1072   1242    198   -560    -64       C  
+ATOM    747  O   TYR A 104     -22.309  23.142  -1.978  1.00 12.85           O  
+ANISOU  747  O   TYR A 104     1989   1439   1452    -27   -700     36       O  
+ATOM    748  CB  TYR A 104     -24.927  22.583  -3.763  1.00 12.62           C  
+ANISOU  748  CB  TYR A 104     1782   1669   1343    344   -495    201       C  
+ATOM    749  CG  TYR A 104     -25.394  22.905  -5.182  1.00 11.59           C  
+ANISOU  749  CG  TYR A 104     1950   1179   1274    138   -560      0       C  
+ATOM    750  CD1 TYR A 104     -26.574  22.362  -5.700  1.00 11.98           C  
+ANISOU  750  CD1 TYR A 104     1717   1604   1231    216   -591    -56       C  
+ATOM    751  CD2 TYR A 104     -24.666  23.790  -5.991  1.00 13.44           C  
+ANISOU  751  CD2 TYR A 104     1908   1763   1434    155   -397    380       C  
+ATOM    752  CE1 TYR A 104     -27.017  22.678  -7.007  1.00 11.47           C  
+ANISOU  752  CE1 TYR A 104     1668   1397   1289    369   -485    130       C  
+ATOM    753  CE2 TYR A 104     -25.095  24.088  -7.312  1.00 14.07           C  
+ANISOU  753  CE2 TYR A 104     2113   1678   1555     66   -573    431       C  
+ATOM    754  CZ  TYR A 104     -26.297  23.546  -7.784  1.00 13.18           C  
+ANISOU  754  CZ  TYR A 104     1921   1426   1658    363   -425     85       C  
+ATOM    755  OH  TYR A 104     -26.712  23.807  -9.080  1.00 14.97           O  
+ANISOU  755  OH  TYR A 104     2270   1602   1814    318   -527     73       O  
+ATOM    756  N   ARG A 105     -23.173  21.126  -1.448  1.00 12.14           N  
+ANISOU  756  N   ARG A 105     2182   1262   1166    318   -331     36       N  
+ATOM    757  CA  ARG A 105     -22.638  21.171  -0.071  1.00 13.34           C  
+ANISOU  757  CA  ARG A 105     2378   1318   1371    267   -687    102       C  
+ATOM    758  C   ARG A 105     -21.108  21.289  -0.046  1.00 13.91           C  
+ANISOU  758  C   ARG A 105     2384   1309   1589    291   -835   -207       C  
+ATOM    759  O   ARG A 105     -20.516  21.752   0.964  1.00 17.90           O  
+ANISOU  759  O   ARG A 105     3098   2225   1478    207   -978   -296       O  
+ATOM    760  CB  ARG A 105     -23.002  19.894   0.686  1.00 19.47           C  
+ANISOU  760  CB  ARG A 105     3274   1711   2410     21   -386    571       C  
+ATOM    761  CG  ARG A 105     -24.474  19.688   0.902  1.00 24.14           C  
+ANISOU  761  CG  ARG A 105     3694   2521   2956     10   -154    824       C  
+ATOM    762  CD  ARG A 105     -24.757  18.799   2.108  1.00 36.91           C  
+ANISOU  762  CD  ARG A 105     5606   4919   3500  -1183   1549   1291       C  
+ATOM    763  NE  ARG A 105     -26.099  18.249   1.994  1.00 37.62           N  
+ANISOU  763  NE  ARG A 105     6411   4678   3204  -1333    186    671       N  
+ATOM    764  CZ  ARG A 105     -26.356  16.956   1.875  0.50 36.67           C  
+ANISOU  764  CZ  ARG A 105     5321   4201   4410   -401   -357    479       C  
+ATOM    765  NH1 ARG A 105     -25.358  16.073   1.880  0.50 28.47           N  
+ANISOU  765  NH1 ARG A 105     4890   3947   1980   -755  -1018   -898       N  
+ATOM    766  NH2 ARG A 105     -27.609  16.548   1.766  0.50 35.82           N  
+ANISOU  766  NH2 ARG A 105     4570   4266   4771    621   -605   1982       N  
+ATOM    767  N   ASN A 106     -20.497  20.829  -1.143  1.00 13.70           N  
+ANISOU  767  N   ASN A 106     2137   1415   1652    146   -490    176       N  
+ATOM    768  CA  ASN A 106     -19.064  20.692  -1.293  1.00 13.67           C  
+ANISOU  768  CA  ASN A 106     2317   1135   1742    243   -515    -96       C  
+ATOM    769  C   ASN A 106     -18.429  21.804  -2.096  1.00 12.73           C  
+ANISOU  769  C   ASN A 106     2149   1398   1288    206   -774     20       C  
+ATOM    770  O   ASN A 106     -17.236  21.734  -2.407  1.00 15.41           O  
+ANISOU  770  O   ASN A 106     2228   1587   2037    230   -796    -36       O  
+ATOM    771  CB  ASN A 106     -18.777  19.310  -1.910  1.00 12.91           C  
+ANISOU  771  CB  ASN A 106     2330    965   1608    292   -684    131       C  
+ATOM    772  CG  ASN A 106     -18.905  18.215  -0.899  1.00 15.55           C  
+ANISOU  772  CG  ASN A 106     2669   1203   2035     49  -1185    419       C  
+ATOM    773  OD1 ASN A 106     -19.928  17.499  -0.829  1.00 18.59           O  
+ANISOU  773  OD1 ASN A 106     2632   1985   2446   -146   -940    128       O  
+ATOM    774  ND2 ASN A 106     -17.898  18.087  -0.091  1.00 16.95           N  
+ANISOU  774  ND2 ASN A 106     2421   1467   2552     64  -1246    600       N  
+ATOM    775  N   LEU A 107     -19.219  22.840  -2.426  1.00 13.23           N  
+ANISOU  775  N   LEU A 107     2207   1225   1593    268   -691    -92       N  
+ATOM    776  CA  LEU A 107     -18.708  24.016  -3.144  1.00 13.69           C  
+ANISOU  776  CA  LEU A 107     2049   1264   1887    121   -870     32       C  
+ATOM    777  C   LEU A 107     -18.558  25.220  -2.235  1.00 14.58           C  
+ANISOU  777  C   LEU A 107     2456   1416   1668   -198   -659     -9       C  
+ATOM    778  O   LEU A 107     -19.277  25.341  -1.238  1.00 16.54           O  
+ANISOU  778  O   LEU A 107     2635   1403   2246   -132   -598   -182       O  
+ATOM    779  CB  LEU A 107     -19.664  24.431  -4.273  1.00 13.20           C  
+ANISOU  779  CB  LEU A 107     2094   1360   1558     99   -726     35       C  
+ATOM    780  CG  LEU A 107     -20.039  23.305  -5.243  1.00 13.11           C  
+ANISOU  780  CG  LEU A 107     1848   1614   1518    129   -751    -57       C  
+ATOM    781  CD1 LEU A 107     -21.078  23.793  -6.221  1.00 17.03           C  
+ANISOU  781  CD1 LEU A 107     2429   2003   2037    173  -1106    440       C  
+ATOM    782  CD2 LEU A 107     -18.812  22.771  -5.992  1.00 14.60           C  
+ANISOU  782  CD2 LEU A 107     1755   1744   2046    451   -544    175       C  
+ATOM    783  N   VAL A 108     -17.657  26.129  -2.588  1.00 14.48           N  
+ANISOU  783  N   VAL A 108     1915   1248   2338    -96   -995    148       N  
+ATOM    784  CA  VAL A 108     -17.527  27.397  -1.845  1.00 16.27           C  
+ANISOU  784  CA  VAL A 108     2552   1568   2062     48   -955   -103       C  
+ATOM    785  C   VAL A 108     -18.851  28.186  -1.931  1.00 18.26           C  
+ANISOU  785  C   VAL A 108     2591   1959   2388     92   -716    149       C  
+ATOM    786  O   VAL A 108     -19.513  28.172  -2.975  1.00 17.46           O  
+ANISOU  786  O   VAL A 108     2415   1896   2320    310   -571    281       O  
+ATOM    787  CB  VAL A 108     -16.356  28.209  -2.388  1.00 17.17           C  
+ANISOU  787  CB  VAL A 108     2362   1254   2906    121  -1025    187       C  
+ATOM    788  CG1 VAL A 108     -16.270  29.592  -1.727  1.00 20.21           C  
+ANISOU  788  CG1 VAL A 108     3074   1300   3301   -487   -613     54       C  
+ATOM    789  CG2 VAL A 108     -15.046  27.455  -2.150  1.00 18.12           C  
+ANISOU  789  CG2 VAL A 108     2476   1640   2768    398  -1009     59       C  
+ATOM    790  OXT VAL A 108     -19.318  28.816  -0.958  1.00 22.60           O  
+ANISOU  790  OXT VAL A 108     3589   2063   2932    323   -417    166       O  
+TER     791      VAL A 108                                                      
+CONECT  792  793                                                                
+CONECT  793  792  794  801                                                      
+CONECT  794  793  795  800                                                      
+CONECT  795  794  796                                                           
+CONECT  796  795  797  798                                                      
+CONECT  797  796                                                                
+CONECT  798  796  799                                                           
+CONECT  799  798  800                                                           
+CONECT  800  794  799                                                           
+CONECT  801  793  802  815                                                      
+CONECT  802  801  803  824                                                      
+CONECT  803  802  804  806                                                      
+CONECT  804  803  805                                                           
+CONECT  805  804  812                                                           
+CONECT  806  803  807  811                                                      
+CONECT  807  806  808                                                           
+CONECT  808  807  809  810                                                      
+CONECT  809  808                                                                
+CONECT  810  808                                                                
+CONECT  811  806  812                                                           
+CONECT  812  805  811  813                                                      
+CONECT  813  812  814                                                           
+CONECT  814  813                                                                
+CONECT  815  801  816  823                                                      
+CONECT  816  815  817  822                                                      
+CONECT  817  816  818                                                           
+CONECT  818  817  819                                                           
+CONECT  819  818  820  821                                                      
+CONECT  820  819                                                                
+CONECT  821  819  822                                                           
+CONECT  822  816  821                                                           
+CONECT  823  815  824  825                                                      
+CONECT  824  802  823                                                           
+CONECT  825  823  826  831                                                      
+CONECT  826  825  827                                                           
+CONECT  827  826  828                                                           
+CONECT  828  827  829  830                                                      
+CONECT  829  828                                                                
+CONECT  830  828  831                                                           
+CONECT  831  825  830                                                           
+CONECT  832  833  834  835  836                                                 
+CONECT  833  832                                                                
+CONECT  834  832                                                                
+CONECT  835  832                                                                
+CONECT  836  832                                                                
+MASTER      307    0    2    5    4    0    7    6  886    1   45    8          
+END