CNRS Nantes University UFIP UFIP
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***  HIV protease  ***

elNémo ID: 18120314494149603

Job options:

ID        	=	 18120314494149603
JOBID     	=	 HIV protease
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER HIV protease

HEADER    HYDROLASE                               13-OCT-11   3U71              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF SOUTH AFRICAN WILD TYPE HIV-1 SUBTYPE C 
TITLE    2 PROTEASE                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIV-1 PROTEASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-99;                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 GENE: POL;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-11B                                   
KEYWDS    BETA SHEET, APO, PROTEASE, SOUTH AFRICAN, NON-B SUBTYPE, VIRAL        
KEYWDS   2 POLYPROTEIN, HYDROLASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.NAICKER,S.FANUCCHI,I.A.ACHILONU,M.A.FERNANDES,H.W.DIRR,Y.SAYED      
REVDAT   1   17-OCT-12 3U71    0                                                
JRNL        AUTH   P.NAICKER,S.FANUCCHI,I.A.ACHILONU,M.A.FERNANDES,H.W.DIRR,    
JRNL        AUTH 2 Y.SAYED                                                      
JRNL        TITL   CRYSTAL STRUCTURE ANALYSIS OF SOUTH AFRICAN WILD TYPE HIV-1  
JRNL        TITL 2 SUBTYPE C APO PROTEASE                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.72 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.72                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 3193                           
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 137                             
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) : 2.72                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 208                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 9                            
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 755                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.08000                                              
REMARK   3    B22 (A**2) : 0.08000                                              
REMARK   3    B33 (A**2) : -0.16000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.388         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.313         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.150        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.860                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   767 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1037 ; 1.776 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    98 ; 6.389 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    25 ;38.890 ;25.600       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   147 ;17.039 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ; 6.506 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   124 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   541 ; 0.005 ; 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):   488 ; 0.641 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   793 ; 1.223 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   279 ; 1.702 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   244 ; 2.899 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    99                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6229  -4.5867 -11.2942              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0218 T22:   0.0761                                     
REMARK   3      T33:   0.0419 T12:   0.0143                                     
REMARK   3      T13:  -0.0066 T23:  -0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4157 L22:   0.4314                                     
REMARK   3      L33:   2.5586 L12:   0.4203                                     
REMARK   3      L13:   0.2807 L23:   0.2630                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0378 S12:   0.1505 S13:  -0.0464                       
REMARK   3      S21:  -0.0112 S22:   0.1308 S23:  -0.0616                       
REMARK   3      S31:  -0.0731 S32:  -0.0192 S33:  -0.0930                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 3U71 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068386.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER PLATINUM 135                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 3193                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.697                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.980                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 8.180                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.20000                            
REMARK 200   FOR THE DATA SET  : 91.2040                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41300                            
REMARK 200   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: MOLREP                                                
REMARK 200 STARTING MODEL: 2R8N                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CITRATE TRIBASIC            
REMARK 280  DIHYDRATE, 20% W/V PEG3350, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.98000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       22.96400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       22.96400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.99000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       22.96400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       22.96400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.97000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       22.96400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       22.96400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.99000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       22.96400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       22.96400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.97000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.98000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    35     NH2  ARG A    57              1.90            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A   9       68.02    -69.40                                   
REMARK 500    CYS A  67       43.26     36.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3U71 A    1    99  UNP    Q994Q3   Q994Q3_9HIV1    59    157             
SEQADV 3U71 LYS A    7  UNP  Q994Q3    GLN    65 ENGINEERED MUTATION            
SEQRES   1 A   99  PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL SER ILE          
SEQRES   2 A   99  LYS VAL GLY GLY GLN ILE LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 A   99  GLY ALA ASP ASP THR VAL LEU GLU GLU ILE ASN LEU PRO          
SEQRES   4 A   99  GLY LYS TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 A   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU          
SEQRES   6 A   99  ILE CYS GLY LYS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 A   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN MET LEU THR          
SEQRES   8 A   99  GLN LEU GLY CYS THR LEU ASN PHE                              
HELIX    1   1 GLY A   86  THR A   91  1                                   6    
SHEET    1   A 8 LYS A  43  GLY A  48  0                                        
SHEET    2   A 8 PHE A  53  ILE A  66 -1  O  ILE A  54   N  ILE A  47           
SHEET    3   A 8 LYS A  69  VAL A  77 -1  O  GLY A  73   N  ILE A  62           
SHEET    4   A 8 VAL A  32  LEU A  33  1  N  LEU A  33   O  LEU A  76           
SHEET    5   A 8 ASN A  83  ILE A  85 -1  O  ILE A  84   N  VAL A  32           
SHEET    6   A 8 GLN A  18  LEU A  24  1  N  LEU A  23   O  ASN A  83           
SHEET    7   A 8 LEU A  10  VAL A  15 -1  N  VAL A  11   O  ALA A  22           
SHEET    8   A 8 PHE A  53  ILE A  66 -1  O  GLU A  65   N  LYS A  14           
CRYST1   45.928   45.928   99.960  90.00  90.00  90.00 P 41 21 2     8          
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      0.021773  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.021773  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010004        0.00000                         
ATOM      1  N   PRO A   1       4.813  10.671  -8.002  1.00 31.75           N  
ANISOU    1  N   PRO A   1     5133   3731   3199   -639    -15     -2       N  
ATOM      2  CA  PRO A   1       3.876  11.267  -7.080  1.00 31.87           C  
ANISOU    2  CA  PRO A   1     5285   3605   3217   -509    -28     41       C  
ATOM      3  C   PRO A   1       4.040  10.715  -5.689  1.00 31.10           C  
ANISOU    3  C   PRO A   1     5098   3527   3192   -457    -23     18       C  
ATOM      4  O   PRO A   1       4.600   9.657  -5.533  1.00 30.75           O  
ANISOU    4  O   PRO A   1     4864   3599   3218   -473    -17    -25       O  
ATOM      5  CB  PRO A   1       2.510  10.851  -7.651  1.00 31.02           C  
ANISOU    5  CB  PRO A   1     5136   3479   3167   -335    -38     74       C  
ATOM      6  CG  PRO A   1       2.735   9.596  -8.292  1.00 30.46           C  
ANISOU    6  CG  PRO A   1     4851   3546   3174   -344    -28     36       C  
ATOM      7  CD  PRO A   1       4.149   9.666  -8.851  1.00 32.06           C  
ANISOU    7  CD  PRO A   1     5022   3839   3319   -540    -14     -7       C  
ATOM      8  N   GLN A   2       3.574  11.460  -4.695  1.00 31.76           N  
ANISOU    8  N   GLN A   2     5329   3490   3248   -395    -28     45       N  
ATOM      9  CA  GLN A   2       3.485  11.007  -3.310  1.00 31.42           C  
ANISOU    9  CA  GLN A   2     5222   3447   3269   -326    -25     32       C  
ATOM     10  C   GLN A   2       2.015  10.878  -3.096  1.00 30.56           C  
ANISOU   10  C   GLN A   2     5122   3279   3208   -129    -30     63       C  
ATOM     11  O   GLN A   2       1.285  11.852  -3.316  1.00 31.36           O  
ANISOU   11  O   GLN A   2     5397   3273   3246    -62    -38    100       O  
ATOM     12  CB  GLN A   2       4.025  12.075  -2.361  1.00 32.64           C  
ANISOU   12  CB  GLN A   2     5556   3509   3336   -414    -24     37       C  
ATOM     13  CG  GLN A   2       4.074  11.712  -0.865  1.00 34.43           C  
ANISOU   13  CG  GLN A   2     5732   3734   3614   -369    -21     22       C  
ATOM     14  CD  GLN A   2       4.530  12.903   0.005  1.00 37.22           C  
ANISOU   14  CD  GLN A   2     6295   3981   3864   -462    -19     30       C  
ATOM     15  OE1 GLN A   2       3.934  13.961  -0.037  1.00 39.19           O  
ANISOU   15  OE1 GLN A   2     6758   4093   4039   -420    -21     62       O  
ATOM     16  NE2 GLN A   2       5.580  12.719   0.784  1.00 39.15           N  
ANISOU   16  NE2 GLN A   2     6483   4291   4100   -583    -17      1       N  
ATOM     17  N   ILE A   3       1.566   9.690  -2.704  1.00 28.67           N  
ANISOU   17  N   ILE A   3     4704   3116   3072    -37    -29     49       N  
ATOM     18  CA  ILE A   3       0.137   9.458  -2.604  1.00 27.06           C  
ANISOU   18  CA  ILE A   3     4478   2894   2907    134    -31     74       C  
ATOM     19  C   ILE A   3      -0.251   9.362  -1.158  1.00 26.43           C  
ANISOU   19  C   ILE A   3     4400   2786   2854    208    -26     71       C  
ATOM     20  O   ILE A   3       0.365   8.634  -0.407  1.00 26.27           O  
ANISOU   20  O   ILE A   3     4282   2815   2883    158    -25     44       O  
ATOM     21  CB  ILE A   3      -0.312   8.240  -3.444  1.00 26.02           C  
ANISOU   21  CB  ILE A   3     4165   2870   2850    177    -33     67       C  
ATOM     22  CG1 ILE A   3      -0.032   8.516  -4.914  1.00 24.34           C  
ANISOU   22  CG1 ILE A   3     3976   2676   2594    109    -37     73       C  
ATOM     23  CG2 ILE A   3      -1.807   7.945  -3.267  1.00 26.06           C  
ANISOU   23  CG2 ILE A   3     4130   2885   2884    339    -35     91       C  
ATOM     24  CD1 ILE A   3      -0.917   7.803  -5.821  1.00 21.91           C  
ANISOU   24  CD1 ILE A   3     3565   2432   2325    185    -41     85       C  
ATOM     25  N   THR A   4      -1.261  10.132  -0.777  1.00 26.57           N  
ANISOU   25  N   THR A   4     4535   2726   2833    330    -24     96       N  
ATOM     26  CA  THR A   4      -1.803  10.119   0.582  1.00 26.33           C  
ANISOU   26  CA  THR A   4     4512   2673   2817    413    -14     91       C  
ATOM     27  C   THR A   4      -2.940   9.111   0.764  1.00 25.61           C  
ANISOU   27  C   THR A   4     4263   2675   2793    533    -11     92       C  
ATOM     28  O   THR A   4      -3.692   8.808  -0.179  1.00 26.31           O  
ANISOU   28  O   THR A   4     4285   2816   2892    599    -16    106       O  
ATOM     29  CB  THR A   4      -2.305  11.475   0.928  1.00 27.11           C  
ANISOU   29  CB  THR A   4     4822   2649   2829    491    -12    109       C  
ATOM     30  OG1 THR A   4      -1.242  12.386   0.720  1.00 27.74           O  
ANISOU   30  OG1 THR A   4     5064   2642   2834    355    -16    110       O  
ATOM     31  CG2 THR A   4      -2.652  11.533   2.354  1.00 28.16           C  
ANISOU   31  CG2 THR A   4     4972   2759   2967    551      2     95       C  
ATOM     32  N   LEU A   5      -3.073   8.574   1.967  1.00 24.45           N  
ANISOU   32  N   LEU A   5     4054   2553   2683    548     -3     76       N  
ATOM     33  CA  LEU A   5      -3.968   7.438   2.110  1.00 23.30           C  
ANISOU   33  CA  LEU A   5     3748   2509   2594    613     -3     74       C  
ATOM     34  C   LEU A   5      -5.253   7.760   2.883  1.00 23.55           C  
ANISOU   34  C   LEU A   5     3797   2554   2596    750     12     79       C  
ATOM     35  O   LEU A   5      -5.838   6.917   3.598  1.00 23.02           O  
ANISOU   35  O   LEU A   5     3622   2563   2560    772     18     70       O  
ATOM     36  CB  LEU A   5      -3.198   6.230   2.637  1.00 22.70           C  
ANISOU   36  CB  LEU A   5     3554   2484   2586    518    -14     52       C  
ATOM     37  CG  LEU A   5      -2.011   5.854   1.730  1.00 20.87           C  
ANISOU   37  CG  LEU A   5     3280   2269   2378    408    -28     39       C  
ATOM     38  CD1 LEU A   5      -1.036   4.949   2.420  1.00 18.47           C  
ANISOU   38  CD1 LEU A   5     2899   1995   2124    328    -45     12       C  
ATOM     39  CD2 LEU A   5      -2.475   5.274   0.416  1.00 18.01           C  
ANISOU   39  CD2 LEU A   5     2832   1971   2037    431    -32     45       C  
ATOM     40  N   TRP A   6      -5.676   9.004   2.679  1.00 23.87           N  
ANISOU   40  N   TRP A   6     3982   2520   2566    839     17     91       N  
ATOM     41  CA  TRP A   6      -6.913   9.529   3.171  1.00 24.09           C  
ANISOU   41  CA  TRP A   6     4041   2563   2549    999     30     91       C  
ATOM     42  C   TRP A   6      -8.023   8.955   2.329  1.00 24.47           C  
ANISOU   42  C   TRP A   6     3954   2735   2608   1088     25    103       C  
ATOM     43  O   TRP A   6      -9.044   8.554   2.881  1.00 24.93           O  
ANISOU   43  O   TRP A   6     3914   2895   2662   1172     38     93       O  
ATOM     44  CB  TRP A   6      -6.912  11.047   3.049  1.00 24.89           C  
ANISOU   44  CB  TRP A   6     4361   2529   2564   1073     27     99       C  
ATOM     45  CG  TRP A   6      -5.994  11.692   3.982  1.00 24.22           C  
ANISOU   45  CG  TRP A   6     4423   2329   2450    989     35     86       C  
ATOM     46  CD1 TRP A   6      -4.837  12.327   3.671  1.00 23.86           C  
ANISOU   46  CD1 TRP A   6     4517   2176   2370    862     24     93       C  
ATOM     47  CD2 TRP A   6      -6.127  11.766   5.405  1.00 24.56           C  
ANISOU   47  CD2 TRP A   6     4486   2360   2484   1009     57     62       C  
ATOM     48  NE1 TRP A   6      -4.232  12.803   4.815  1.00 24.56           N  
ANISOU   48  NE1 TRP A   6     4715   2185   2428    800     37     76       N  
ATOM     49  CE2 TRP A   6      -5.009  12.474   5.892  1.00 23.76           C  
ANISOU   49  CE2 TRP A   6     4545   2135   2345    892     56     57       C  
ATOM     50  CE3 TRP A   6      -7.085  11.300   6.319  1.00 25.69           C  
ANISOU   50  CE3 TRP A   6     4526   2593   2639   1102     78     42       C  
ATOM     51  CZ2 TRP A   6      -4.810  12.714   7.244  1.00 23.31           C  
ANISOU   51  CZ2 TRP A   6     4551   2037   2268    870     74     35       C  
ATOM     52  CZ3 TRP A   6      -6.895  11.555   7.667  1.00 25.07           C  
ANISOU   52  CZ3 TRP A   6     4512   2472   2540   1083     97     19       C  
ATOM     53  CH2 TRP A   6      -5.761  12.254   8.116  1.00 23.72           C  
ANISOU   53  CH2 TRP A   6     4503   2170   2337    970     95     17       C  
ATOM     54  N   LYS A   7      -7.827   8.941   1.005  1.00 24.10           N  
ANISOU   54  N   LYS A   7     3901   2689   2564   1062      6    123       N  
ATOM     55  CA  LYS A   7      -8.759   8.316   0.080  1.00 24.46           C  
ANISOU   55  CA  LYS A   7     3814   2860   2620   1119     -1    137       C  
ATOM     56  C   LYS A   7      -8.218   6.984  -0.395  1.00 23.52           C  
ANISOU   56  C   LYS A   7     3552   2809   2573    984     -7    132       C  
ATOM     57  O   LYS A   7      -7.019   6.724  -0.302  1.00 23.60           O  
ANISOU   57  O   LYS A   7     3583   2762   2619    860    -10    120       O  
ATOM     58  CB  LYS A   7      -8.960   9.173  -1.165  1.00 25.59           C  
ANISOU   58  CB  LYS A   7     4052   2959   2711   1183    -23    165       C  
ATOM     59  CG  LYS A   7      -9.483  10.584  -0.955  1.00 29.13           C  
ANISOU   59  CG  LYS A   7     4677   3316   3075   1336    -30    174       C  
ATOM     60  CD  LYS A   7      -9.064  11.488  -2.125  1.00 32.69           C  
ANISOU   60  CD  LYS A   7     5286   3659   3473   1326    -59    204       C  
ATOM     61  CE  LYS A   7      -9.960  11.326  -3.367  1.00 34.53           C  
ANISOU   61  CE  LYS A   7     5441   3987   3689   1413    -84    231       C  
ATOM     62  NZ  LYS A   7     -11.376  11.813  -3.136  1.00 34.11           N  
ANISOU   62  NZ  LYS A   7     5379   4000   3580   1640    -92    233       N  
ATOM     63  N   ARG A   8      -9.088   6.139  -0.945  1.00 22.86           N  
ANISOU   63  N   ARG A   8     3328   2854   2502   1010    -10    139       N  
ATOM     64  CA  ARG A   8      -8.609   4.949  -1.628  1.00 21.44           C  
ANISOU   64  CA  ARG A   8     3042   2724   2379    893    -18    134       C  
ATOM     65  C   ARG A   8      -7.633   5.361  -2.751  1.00 21.27           C  
ANISOU   65  C   ARG A   8     3092   2629   2359    824    -30    141       C  
ATOM     66  O   ARG A   8      -7.993   6.184  -3.583  1.00 22.36           O  
ANISOU   66  O   ARG A   8     3298   2748   2448    886    -40    164       O  
ATOM     67  CB  ARG A   8      -9.771   4.204  -2.245  1.00 21.11           C  
ANISOU   67  CB  ARG A   8     2868   2824   2328    930    -21    145       C  
ATOM     68  CG  ARG A   8     -10.574   3.369  -1.341  1.00 19.94           C  
ANISOU   68  CG  ARG A   8     2614   2780   2180    934    -11    134       C  
ATOM     69  CD  ARG A   8     -11.541   2.675  -2.217  1.00 22.13           C  
ANISOU   69  CD  ARG A   8     2772   3197   2438    938    -16    146       C  
ATOM     70  NE  ARG A   8     -12.258   1.635  -1.517  1.00 26.07           N  
ANISOU   70  NE  ARG A   8     3162   3811   2930    895     -9    135       N  
ATOM     71  CZ  ARG A   8     -13.453   1.800  -0.972  1.00 28.19           C  
ANISOU   71  CZ  ARG A   8     3366   4204   3139    975      4    134       C  
ATOM     72  NH1 ARG A   8     -14.066   2.978  -1.069  1.00 31.51           N  
ANISOU   72  NH1 ARG A   8     3820   4643   3507   1128      9    141       N  
ATOM     73  NH2 ARG A   8     -14.040   0.789  -0.343  1.00 26.76           N  
ANISOU   73  NH2 ARG A   8     3091   4134   2942    903     11    124       N  
ATOM     74  N   PRO A   9      -6.408   4.793  -2.789  1.00 20.29           N  
ANISOU   74  N   PRO A   9     2952   2472   2282    699    -33    119       N  
ATOM     75  CA  PRO A   9      -5.446   5.175  -3.841  1.00 20.23           C  
ANISOU   75  CA  PRO A   9     3000   2419   2265    619    -40    118       C  
ATOM     76  C   PRO A   9      -5.849   4.693  -5.227  1.00 19.78           C  
ANISOU   76  C   PRO A   9     2870   2434   2209    612    -47    128       C  
ATOM     77  O   PRO A   9      -5.209   3.816  -5.795  1.00 19.04           O  
ANISOU   77  O   PRO A   9     2701   2378   2156    524    -48    105       O  
ATOM     78  CB  PRO A   9      -4.141   4.499  -3.391  1.00 19.55           C  
ANISOU   78  CB  PRO A   9     2876   2320   2229    504    -40     82       C  
ATOM     79  CG  PRO A   9      -4.590   3.359  -2.589  1.00 18.96           C  
ANISOU   79  CG  PRO A   9     2697   2302   2204    520    -42     70       C  
ATOM     80  CD  PRO A   9      -5.859   3.759  -1.900  1.00 19.28           C  
ANISOU   80  CD  PRO A   9     2752   2360   2211    628    -33     92       C  
ATOM     81  N   LEU A  10      -6.923   5.261  -5.752  1.00 20.55           N  
ANISOU   81  N   LEU A  10     2992   2558   2259    711    -54    161       N  
ATOM     82  CA  LEU A  10      -7.432   4.862  -7.059  1.00 20.90           C  
ANISOU   82  CA  LEU A  10     2968   2679   2293    709    -64    176       C  
ATOM     83  C   LEU A  10      -6.793   5.751  -8.080  1.00 21.89           C  
ANISOU   83  C   LEU A  10     3206   2736   2375    665    -74    190       C  
ATOM     84  O   LEU A  10      -6.882   6.969  -8.006  1.00 23.22           O  
ANISOU   84  O   LEU A  10     3517   2819   2483    723    -84    214       O  
ATOM     85  CB  LEU A  10      -8.953   4.962  -7.140  1.00 20.85           C  
ANISOU   85  CB  LEU A  10     2911   2760   2248    839    -71    204       C  
ATOM     86  CG  LEU A  10      -9.705   3.904  -6.333  1.00 20.45           C  
ANISOU   86  CG  LEU A  10     2727   2815   2226    852    -60    190       C  
ATOM     87  CD1 LEU A  10     -11.130   4.340  -6.074  1.00 20.35           C  
ANISOU   87  CD1 LEU A  10     2681   2892   2156    995    -63    210       C  
ATOM     88  CD2 LEU A  10      -9.653   2.521  -6.980  1.00 18.76           C  
ANISOU   88  CD2 LEU A  10     2393   2683   2051    750    -61    176       C  
ATOM     89  N   VAL A  11      -6.117   5.137  -9.032  1.00 22.17           N  
ANISOU   89  N   VAL A  11     3188   2803   2432    557    -72    173       N  
ATOM     90  CA  VAL A  11      -5.413   5.889 -10.057  1.00 22.40           C  
ANISOU   90  CA  VAL A  11     3315   2782   2412    483    -79    182       C  
ATOM     91  C   VAL A  11      -5.876   5.458 -11.436  1.00 22.69           C  
ANISOU   91  C   VAL A  11     3287   2896   2436    467    -88    195       C  
ATOM     92  O   VAL A  11      -6.398   4.342 -11.628  1.00 21.76           O  
ANISOU   92  O   VAL A  11     3033   2873   2360    471    -84    184       O  
ATOM     93  CB  VAL A  11      -3.875   5.733  -9.930  1.00 21.72           C  
ANISOU   93  CB  VAL A  11     3238   2667   2347    342    -64    138       C  
ATOM     94  CG1 VAL A  11      -3.393   6.378  -8.673  1.00 22.21           C  
ANISOU   94  CG1 VAL A  11     3389   2647   2402    346    -59    132       C  
ATOM     95  CG2 VAL A  11      -3.490   4.280  -9.919  1.00 20.00           C  
ANISOU   95  CG2 VAL A  11     2861   2531   2204    290    -52     93       C  
ATOM     96  N   SER A  12      -5.678   6.365 -12.387  1.00 23.80           N  
ANISOU   96  N   SER A  12     3541   2992   2510    437   -103    221       N  
ATOM     97  CA  SER A  12      -5.836   6.052 -13.791  1.00 24.47           C  
ANISOU   97  CA  SER A  12     3583   3140   2574    387   -111    231       C  
ATOM     98  C   SER A  12      -4.611   5.289 -14.376  1.00 23.75           C  
ANISOU   98  C   SER A  12     3422   3087   2514    230    -87    178       C  
ATOM     99  O   SER A  12      -3.432   5.685 -14.186  1.00 23.83           O  
ANISOU   99  O   SER A  12     3492   3050   2511    132    -75    151       O  
ATOM    100  CB  SER A  12      -6.131   7.320 -14.579  1.00 25.82           C  
ANISOU  100  CB  SER A  12     3914   3245   2652    418   -142    282       C  
ATOM    101  OG  SER A  12      -6.942   7.009 -15.706  1.00 28.14           O  
ANISOU  101  OG  SER A  12     4148   3621   2923    443   -160    309       O  
ATOM    102  N   ILE A  13      -4.923   4.200 -15.087  1.00 22.52           N  
ANISOU  102  N   ILE A  13     3138   3027   2391    207    -81    162       N  
ATOM    103  CA  ILE A  13      -3.924   3.325 -15.686  1.00 20.96           C  
ANISOU  103  CA  ILE A  13     2858   2880   2223     86    -58    104       C  
ATOM    104  C   ILE A  13      -4.122   3.097 -17.181  1.00 20.28           C  
ANISOU  104  C   ILE A  13     2745   2857   2100     28    -60    109       C  
ATOM    105  O   ILE A  13      -5.248   2.992 -17.658  1.00 19.87           O  
ANISOU  105  O   ILE A  13     2672   2847   2031     89    -78    150       O  
ATOM    106  CB  ILE A  13      -3.832   1.947 -14.950  1.00 20.52           C  
ANISOU  106  CB  ILE A  13     2675   2870   2252     99    -44     57       C  
ATOM    107  CG1 ILE A  13      -4.987   1.038 -15.256  1.00 18.47           C  
ANISOU  107  CG1 ILE A  13     2328   2680   2007    147    -51     72       C  
ATOM    108  CG2 ILE A  13      -3.743   2.111 -13.442  1.00 21.20           C  
ANISOU  108  CG2 ILE A  13     2783   2900   2372    158    -46     56       C  
ATOM    109  CD1 ILE A  13      -4.661  -0.316 -14.876  1.00 18.02           C  
ANISOU  109  CD1 ILE A  13     2179   2654   2012    121    -41     20       C  
ATOM    110  N   LYS A  14      -3.003   3.033 -17.896  1.00 19.70           N  
ANISOU  110  N   LYS A  14     2669   2803   2010    -95    -41     66       N  
ATOM    111  CA  LYS A  14      -2.966   2.743 -19.328  1.00 18.87           C  
ANISOU  111  CA  LYS A  14     2535   2764   1869   -176    -36     56       C  
ATOM    112  C   LYS A  14      -2.388   1.364 -19.529  1.00 18.28           C  
ANISOU  112  C   LYS A  14     2327   2763   1851   -223     -8    -18       C  
ATOM    113  O   LYS A  14      -1.209   1.141 -19.313  1.00 18.04           O  
ANISOU  113  O   LYS A  14     2267   2747   1839   -286     13    -80       O  
ATOM    114  CB  LYS A  14      -2.097   3.748 -20.058  1.00 18.86           C  
ANISOU  114  CB  LYS A  14     2638   2739   1787   -292    -33     57       C  
ATOM    115  CG  LYS A  14      -2.610   5.140 -20.044  1.00 18.38           C  
ANISOU  115  CG  LYS A  14     2743   2587   1651   -254    -67    132       C  
ATOM    116  CD  LYS A  14      -1.544   5.990 -20.627  1.00 20.86           C  
ANISOU  116  CD  LYS A  14     3166   2878   1883   -403    -60    121       C  
ATOM    117  CE  LYS A  14      -2.089   7.046 -21.535  1.00 23.91           C  
ANISOU  117  CE  LYS A  14     3707   3208   2167   -415    -98    190       C  
ATOM    118  NZ  LYS A  14      -1.069   8.125 -21.652  1.00 27.22           N  
ANISOU  118  NZ  LYS A  14     4282   3565   2492   -556    -98    190       N  
ATOM    119  N   VAL A  15      -3.251   0.446 -19.934  1.00 18.41           N  
ANISOU  119  N   VAL A  15     2270   2832   1890   -190    -12    -14       N  
ATOM    120  CA  VAL A  15      -2.917  -0.956 -20.163  1.00 18.33           C  
ANISOU  120  CA  VAL A  15     2156   2878   1927   -220      7    -81       C  
ATOM    121  C   VAL A  15      -3.667  -1.416 -21.398  1.00 18.92           C  
ANISOU  121  C   VAL A  15     2201   3017   1967   -254      5    -67       C  
ATOM    122  O   VAL A  15      -4.870  -1.205 -21.480  1.00 19.45           O  
ANISOU  122  O   VAL A  15     2280   3098   2012   -201    -17     -3       O  
ATOM    123  CB  VAL A  15      -3.339  -1.853 -18.968  1.00 17.36           C  
ANISOU  123  CB  VAL A  15     1985   2736   1873   -138      0    -90       C  
ATOM    124  CG1 VAL A  15      -4.808  -1.850 -18.816  1.00 18.11           C  
ANISOU  124  CG1 VAL A  15     2079   2847   1955    -71    -21    -25       C  
ATOM    125  CG2 VAL A  15      -2.902  -3.278 -19.161  1.00 17.06           C  
ANISOU  125  CG2 VAL A  15     1874   2732   1876   -164     13   -162       C  
ATOM    126  N   GLY A  16      -2.949  -2.006 -22.357  1.00 19.58           N  
ANISOU  126  N   GLY A  16     2245   3153   2041   -341     29   -128       N  
ATOM    127  CA  GLY A  16      -3.547  -2.665 -23.524  1.00 19.84           C  
ANISOU  127  CA  GLY A  16     2242   3251   2043   -387     33   -130       C  
ATOM    128  C   GLY A  16      -4.455  -1.813 -24.389  1.00 20.30           C  
ANISOU  128  C   GLY A  16     2351   3331   2030   -401      9    -51       C  
ATOM    129  O   GLY A  16      -5.431  -2.312 -24.937  1.00 20.14           O  
ANISOU  129  O   GLY A  16     2298   3362   1990   -399     -2    -24       O  
ATOM    130  N   GLY A  17      -4.147  -0.523 -24.491  1.00 21.03           N  
ANISOU  130  N   GLY A  17     2531   3383   2075   -417     -1    -13       N  
ATOM    131  CA  GLY A  17      -4.912   0.383 -25.347  1.00 22.82           C  
ANISOU  131  CA  GLY A  17     2829   3616   2223   -423    -32     62       C  
ATOM    132  C   GLY A  17      -6.176   0.941 -24.723  1.00 23.87           C  
ANISOU  132  C   GLY A  17     2994   3724   2348   -291    -74    143       C  
ATOM    133  O   GLY A  17      -6.914   1.714 -25.346  1.00 24.86           O  
ANISOU  133  O   GLY A  17     3182   3856   2407   -264   -110    211       O  
ATOM    134  N   GLN A  18      -6.416   0.527 -23.491  1.00 24.17           N  
ANISOU  134  N   GLN A  18     2989   3742   2451   -206    -71    134       N  
ATOM    135  CA  GLN A  18      -7.518   0.966 -22.699  1.00 25.06           C  
ANISOU  135  CA  GLN A  18     3114   3846   2561    -76   -101    194       C  
ATOM    136  C   GLN A  18      -6.962   1.867 -21.644  1.00 24.70           C  
ANISOU  136  C   GLN A  18     3155   3699   2530    -25   -103    198       C  
ATOM    137  O   GLN A  18      -5.791   1.751 -21.275  1.00 24.42           O  
ANISOU  137  O   GLN A  18     3128   3621   2529    -89    -76    145       O  
ATOM    138  CB  GLN A  18      -8.148  -0.227 -21.971  1.00 25.84           C  
ANISOU  138  CB  GLN A  18     3102   3999   2715    -37    -92    173       C  
ATOM    139  CG  GLN A  18      -8.729  -1.338 -22.853  1.00 28.39           C  
ANISOU  139  CG  GLN A  18     3339   4423   3024   -100    -87    161       C  
ATOM    140  CD  GLN A  18      -9.433  -0.780 -24.041  1.00 33.80           C  
ANISOU  140  CD  GLN A  18     4043   5168   3631   -110   -114    216       C  
ATOM    141  OE1 GLN A  18     -10.273   0.131 -23.923  1.00 36.36           O  
ANISOU  141  OE1 GLN A  18     4401   5503   3910    -12   -150    282       O  
ATOM    142  NE2 GLN A  18      -9.082  -1.294 -25.218  1.00 37.31           N  
ANISOU  142  NE2 GLN A  18     4470   5653   4051   -223    -99    187       N  
ATOM    143  N   ILE A  19      -7.818   2.755 -21.151  1.00 24.77           N  
ANISOU  143  N   ILE A  19     3225   3677   2508     95   -135    259       N  
ATOM    144  CA  ILE A  19      -7.558   3.483 -19.925  1.00 24.26           C  
ANISOU  144  CA  ILE A  19     3236   3520   2461    168   -137    264       C  
ATOM    145  C   ILE A  19      -8.591   3.030 -18.909  1.00 24.08           C  
ANISOU  145  C   ILE A  19     3131   3542   2473    287   -142    275       C  
ATOM    146  O   ILE A  19      -9.767   3.248 -19.124  1.00 24.97           O  
ANISOU  146  O   ILE A  19     3223   3717   2545    379   -169    322       O  
ATOM    147  CB  ILE A  19      -7.645   4.994 -20.118  1.00 24.82           C  
ANISOU  147  CB  ILE A  19     3474   3501   2453    217   -171    319       C  
ATOM    148  CG1 ILE A  19      -6.543   5.506 -21.075  1.00 24.45           C  
ANISOU  148  CG1 ILE A  19     3525   3410   2356     70   -166    307       C  
ATOM    149  CG2 ILE A  19      -7.548   5.647 -18.790  1.00 25.00           C  
ANISOU  149  CG2 ILE A  19     3571   3434   2491    303   -172    322       C  
ATOM    150  CD1 ILE A  19      -6.652   7.001 -21.461  1.00 24.08           C  
ANISOU  150  CD1 ILE A  19     3677   3262   2209     97   -209    368       C  
ATOM    151  N   LYS A  20      -8.140   2.377 -17.833  1.00 23.47           N  
ANISOU  151  N   LYS A  20     3004   3447   2464    278   -116    232       N  
ATOM    152  CA  LYS A  20      -8.997   1.863 -16.771  1.00 23.29           C  
ANISOU  152  CA  LYS A  20     2907   3469   2472    364   -116    236       C  
ATOM    153  C   LYS A  20      -8.677   2.575 -15.467  1.00 22.86           C  
ANISOU  153  C   LYS A  20     2926   3324   2436    431   -113    234       C  
ATOM    154  O   LYS A  20      -7.779   3.411 -15.411  1.00 22.71           O  
ANISOU  154  O   LYS A  20     3015   3207   2404    402   -112    230       O  
ATOM    155  CB  LYS A  20      -8.764   0.381 -16.542  1.00 23.13           C  
ANISOU  155  CB  LYS A  20     2780   3496   2510    289    -94    186       C  
ATOM    156  CG  LYS A  20      -9.141  -0.569 -17.667  1.00 26.55           C  
ANISOU  156  CG  LYS A  20     3137   4022   2929    215    -93    177       C  
ATOM    157  CD  LYS A  20     -10.545  -0.320 -18.243  1.00 31.98           C  
ANISOU  157  CD  LYS A  20     3786   4814   3551    273   -118    234       C  
ATOM    158  CE  LYS A  20     -10.910  -1.391 -19.298  1.00 33.56           C  
ANISOU  158  CE  LYS A  20     3907   5111   3732    179   -114    222       C  
ATOM    159  NZ  LYS A  20     -12.026  -0.968 -20.209  1.00 34.44           N  
ANISOU  159  NZ  LYS A  20     3992   5327   3767    215   -143    278       N  
ATOM    160  N   GLU A  21      -9.415   2.243 -14.415  1.00 22.60           N  
ANISOU  160  N   GLU A  21     2837   3328   2423    508   -111    237       N  
ATOM    161  CA  GLU A  21      -9.118   2.771 -13.089  1.00 22.53           C  
ANISOU  161  CA  GLU A  21     2887   3238   2434    563   -104    229       C  
ATOM    162  C   GLU A  21      -8.815   1.637 -12.106  1.00 21.16           C  
ANISOU  162  C   GLU A  21     2634   3079   2327    517    -86    188       C  
ATOM    163  O   GLU A  21      -9.581   0.671 -12.032  1.00 20.92           O  
ANISOU  163  O   GLU A  21     2503   3142   2303    512    -85    185       O  
ATOM    164  CB  GLU A  21     -10.298   3.574 -12.592  1.00 23.84           C  
ANISOU  164  CB  GLU A  21     3075   3431   2550    714   -121    269       C  
ATOM    165  CG  GLU A  21      -9.990   4.385 -11.349  1.00 26.41           C  
ANISOU  165  CG  GLU A  21     3497   3657   2880    779   -115    264       C  
ATOM    166  CD  GLU A  21     -11.239   4.900 -10.653  1.00 30.08           C  
ANISOU  166  CD  GLU A  21     3951   4175   3303    940   -125    286       C  
ATOM    167  OE1 GLU A  21     -12.007   4.080 -10.069  1.00 30.42           O  
ANISOU  167  OE1 GLU A  21     3867   4330   3359    959   -114    276       O  
ATOM    168  OE2 GLU A  21     -11.431   6.133 -10.686  1.00 30.98           O  
ANISOU  168  OE2 GLU A  21     4190   4217   3361   1045   -144    312       O  
ATOM    169  N   ALA A  22      -7.722   1.757 -11.350  1.00 19.68           N  
ANISOU  169  N   ALA A  22     2497   2803   2178    479    -75    157       N  
ATOM    170  CA  ALA A  22      -7.213   0.630 -10.587  1.00 18.39           C  
ANISOU  170  CA  ALA A  22     2270   2640   2075    426    -65    116       C  
ATOM    171  C   ALA A  22      -6.644   1.036  -9.270  1.00 18.21           C  
ANISOU  171  C   ALA A  22     2301   2541   2075    446    -60    104       C  
ATOM    172  O   ALA A  22      -6.164   2.143  -9.137  1.00 19.53           O  
ANISOU  172  O   ALA A  22     2565   2636   2217    459    -60    114       O  
ATOM    173  CB  ALA A  22      -6.157  -0.043 -11.372  1.00 18.49           C  
ANISOU  173  CB  ALA A  22     2259   2649   2117    325    -59     74       C  
ATOM    174  N   LEU A  23      -6.633   0.129  -8.303  1.00 17.46           N  
ANISOU  174  N   LEU A  23     2156   2455   2022    435    -60     82       N  
ATOM    175  CA  LEU A  23      -6.225   0.473  -6.943  1.00 16.89           C  
ANISOU  175  CA  LEU A  23     2130   2319   1967    457    -58     75       C  
ATOM    176  C   LEU A  23      -4.794   0.071  -6.671  1.00 17.29           C  
ANISOU  176  C   LEU A  23     2187   2319   2062    383    -60     32       C  
ATOM    177  O   LEU A  23      -4.399  -1.067  -6.965  1.00 18.04           O  
ANISOU  177  O   LEU A  23     2220   2439   2193    336    -67      0       O  
ATOM    178  CB  LEU A  23      -7.135  -0.219  -5.941  1.00 16.35           C  
ANISOU  178  CB  LEU A  23     2009   2298   1905    489    -60     80       C  
ATOM    179  CG  LEU A  23      -6.894  -0.099  -4.435  1.00 15.18           C  
ANISOU  179  CG  LEU A  23     1894   2100   1772    506    -59     72       C  
ATOM    180  CD1 LEU A  23      -7.502   1.134  -3.908  1.00 14.52           C  
ANISOU  180  CD1 LEU A  23     1871   1999   1643    596    -48     98       C  
ATOM    181  CD2 LEU A  23      -7.512  -1.261  -3.763  1.00 12.77           C  
ANISOU  181  CD2 LEU A  23     1524   1849   1478    483    -66     67       C  
ATOM    182  N   LEU A  24      -4.015   0.995  -6.102  1.00 17.35           N  
ANISOU  182  N   LEU A  24     2271   2258   2060    376    -56     29       N  
ATOM    183  CA  LEU A  24      -2.658   0.703  -5.619  1.00 16.16           C  
ANISOU  183  CA  LEU A  24     2117   2078   1943    313    -61    -11       C  
ATOM    184  C   LEU A  24      -2.749  -0.040  -4.304  1.00 15.94           C  
ANISOU  184  C   LEU A  24     2063   2040   1953    333    -73    -20       C  
ATOM    185  O   LEU A  24      -3.026   0.559  -3.261  1.00 15.63           O  
ANISOU  185  O   LEU A  24     2076   1963   1900    367    -70     -2       O  
ATOM    186  CB  LEU A  24      -1.853   1.990  -5.421  1.00 16.31           C  
ANISOU  186  CB  LEU A  24     2234   2039   1923    280    -53     -8       C  
ATOM    187  CG  LEU A  24      -1.658   2.893  -6.638  1.00 16.78           C  
ANISOU  187  CG  LEU A  24     2355   2092   1928    241    -45      3       C  
ATOM    188  CD1 LEU A  24      -0.421   3.793  -6.518  1.00 14.38           C  
ANISOU  188  CD1 LEU A  24     2130   1748   1583    152    -39    -12       C  
ATOM    189  CD2 LEU A  24      -1.600   2.037  -7.900  1.00 15.54           C  
ANISOU  189  CD2 LEU A  24     2108   2006   1787    206    -44    -17       C  
ATOM    190  N   ASP A  25      -2.505  -1.344  -4.356  1.00 15.74           N  
ANISOU  190  N   ASP A  25     1970   2042   1969    311    -89    -50       N  
ATOM    191  CA  ASP A  25      -2.795  -2.241  -3.237  1.00 15.63           C  
ANISOU  191  CA  ASP A  25     1939   2018   1980    324   -109    -52       C  
ATOM    192  C   ASP A  25      -1.585  -3.025  -2.747  1.00 15.44           C  
ANISOU  192  C   ASP A  25     1898   1970   1997    298   -135    -95       C  
ATOM    193  O   ASP A  25      -1.250  -4.056  -3.309  1.00 15.93           O  
ANISOU  193  O   ASP A  25     1920   2049   2082    286   -152   -127       O  
ATOM    194  CB  ASP A  25      -3.880  -3.218  -3.678  1.00 15.73           C  
ANISOU  194  CB  ASP A  25     1907   2081   1989    327   -113    -41       C  
ATOM    195  CG  ASP A  25      -4.389  -4.059  -2.556  1.00 17.25           C  
ANISOU  195  CG  ASP A  25     2099   2268   2186    325   -132    -35       C  
ATOM    196  OD1 ASP A  25      -3.684  -4.135  -1.539  1.00 21.78           O  
ANISOU  196  OD1 ASP A  25     2700   2792   2782    322   -149    -47       O  
ATOM    197  OD2 ASP A  25      -5.492  -4.634  -2.668  1.00 17.95           O  
ANISOU  197  OD2 ASP A  25     2162   2408   2249    316   -132    -16       O  
ATOM    198  N   THR A  26      -0.945  -2.572  -1.683  1.00 15.41           N  
ANISOU  198  N   THR A  26     1927   1930   1997    295   -143    -97       N  
ATOM    199  CA  THR A  26       0.274  -3.234  -1.222  1.00 15.76           C  
ANISOU  199  CA  THR A  26     1949   1966   2073    281   -174   -139       C  
ATOM    200  C   THR A  26      -0.020  -4.588  -0.553  1.00 16.42           C  
ANISOU  200  C   THR A  26     2026   2029   2183    300   -212   -144       C  
ATOM    201  O   THR A  26       0.890  -5.441  -0.370  1.00 17.46           O  
ANISOU  201  O   THR A  26     2139   2153   2342    309   -249   -182       O  
ATOM    202  CB  THR A  26       1.088  -2.327  -0.306  1.00 15.76           C  
ANISOU  202  CB  THR A  26     1985   1943   2060    260   -174   -139       C  
ATOM    203  OG1 THR A  26       0.347  -2.045   0.879  1.00 16.74           O  
ANISOU  203  OG1 THR A  26     2161   2026   2173    278   -173   -104       O  
ATOM    204  CG2 THR A  26       1.372  -1.016  -0.987  1.00 15.26           C  
ANISOU  204  CG2 THR A  26     1955   1888   1955    224   -140   -133       C  
ATOM    205  N   GLY A  27      -1.297  -4.790  -0.224  1.00 16.12           N  
ANISOU  205  N   GLY A  27     2008   1988   2128    305   -206   -107       N  
ATOM    206  CA  GLY A  27      -1.764  -6.007   0.386  1.00 16.47           C  
ANISOU  206  CA  GLY A  27     2067   2012   2177    299   -240   -103       C  
ATOM    207  C   GLY A  27      -1.859  -7.154  -0.602  1.00 17.37           C  
ANISOU  207  C   GLY A  27     2163   2137   2299    290   -256   -127       C  
ATOM    208  O   GLY A  27      -1.936  -8.311  -0.181  1.00 17.07           O  
ANISOU  208  O   GLY A  27     2160   2063   2263    281   -296   -134       O  
ATOM    209  N   ALA A  28      -1.851  -6.823  -1.903  1.00 18.31           N  
ANISOU  209  N   ALA A  28     2244   2297   2415    290   -228   -138       N  
ATOM    210  CA  ALA A  28      -1.994  -7.788  -3.016  1.00 19.53           C  
ANISOU  210  CA  ALA A  28     2382   2468   2569    277   -235   -163       C  
ATOM    211  C   ALA A  28      -0.641  -8.205  -3.576  1.00 20.75           C  
ANISOU  211  C   ALA A  28     2514   2615   2754    300   -252   -224       C  
ATOM    212  O   ALA A  28       0.214  -7.356  -3.826  1.00 21.24           O  
ANISOU  212  O   ALA A  28     2542   2704   2823    306   -234   -242       O  
ATOM    213  CB  ALA A  28      -2.812  -7.206  -4.111  1.00 19.16           C  
ANISOU  213  CB  ALA A  28     2303   2481   2494    260   -196   -140       C  
ATOM    214  N   ASP A  29      -0.439  -9.509  -3.765  1.00 22.05           N  
ANISOU  214  N   ASP A  29     2701   2747   2926    312   -288   -258       N  
ATOM    215  CA  ASP A  29       0.829  -9.981  -4.279  1.00 23.42           C  
ANISOU  215  CA  ASP A  29     2847   2925   3123    356   -306   -326       C  
ATOM    216  C   ASP A  29       0.875  -9.650  -5.736  1.00 23.53           C  
ANISOU  216  C   ASP A  29     2809   3003   3127    334   -265   -348       C  
ATOM    217  O   ASP A  29       1.854  -9.095  -6.179  1.00 23.97           O  
ANISOU  217  O   ASP A  29     2809   3109   3189    343   -248   -386       O  
ATOM    218  CB  ASP A  29       1.013 -11.494  -4.113  1.00 24.96           C  
ANISOU  218  CB  ASP A  29     3105   3055   3323    392   -361   -360       C  
ATOM    219  CG  ASP A  29       0.944 -11.962  -2.669  1.00 26.79           C  
ANISOU  219  CG  ASP A  29     3408   3213   3556    406   -411   -335       C  
ATOM    220  OD1 ASP A  29       1.538 -11.314  -1.776  1.00 29.18           O  
ANISOU  220  OD1 ASP A  29     3690   3521   3876    426   -419   -328       O  
ATOM    221  OD2 ASP A  29       0.311 -13.019  -2.442  1.00 29.55           O  
ANISOU  221  OD2 ASP A  29     3844   3497   3883    386   -446   -324       O  
ATOM    222  N   ASP A  30      -0.214  -9.963  -6.449  1.00 24.30           N  
ANISOU  222  N   ASP A  30     2924   3109   3200    294   -248   -323       N  
ATOM    223  CA  ASP A  30      -0.322  -9.949  -7.939  1.00 25.09           C  
ANISOU  223  CA  ASP A  30     2988   3263   3282    266   -216   -345       C  
ATOM    224  C   ASP A  30      -1.212  -8.820  -8.525  1.00 24.64           C  
ANISOU  224  C   ASP A  30     2904   3261   3196    221   -173   -290       C  
ATOM    225  O   ASP A  30      -1.879  -8.109  -7.773  1.00 24.61           O  
ANISOU  225  O   ASP A  30     2914   3253   3182    221   -167   -236       O  
ATOM    226  CB  ASP A  30      -0.823 -11.326  -8.433  1.00 25.50           C  
ANISOU  226  CB  ASP A  30     3088   3283   3318    253   -237   -365       C  
ATOM    227  CG  ASP A  30      -0.127 -12.500  -7.730  1.00 27.58           C  
ANISOU  227  CG  ASP A  30     3412   3466   3599    309   -292   -411       C  
ATOM    228  OD1 ASP A  30       1.121 -12.573  -7.753  1.00 30.41           O  
ANISOU  228  OD1 ASP A  30     3738   3831   3984    375   -305   -471       O  
ATOM    229  OD2 ASP A  30      -0.821 -13.361  -7.151  1.00 28.31           O  
ANISOU  229  OD2 ASP A  30     3588   3494   3671    288   -326   -387       O  
ATOM    230  N   THR A  31      -1.223  -8.662  -9.856  1.00 24.64           N  
ANISOU  230  N   THR A  31     2872   3312   3176    191   -146   -306       N  
ATOM    231  CA  THR A  31      -2.032  -7.616 -10.498  1.00 23.98           C  
ANISOU  231  CA  THR A  31     2774   3278   3058    159   -115   -254       C  
ATOM    232  C   THR A  31      -3.203  -8.188 -11.276  1.00 24.62           C  
ANISOU  232  C   THR A  31     2854   3394   3104    122   -111   -229       C  
ATOM    233  O   THR A  31      -3.031  -8.894 -12.258  1.00 25.51           O  
ANISOU  233  O   THR A  31     2959   3524   3207     94   -107   -268       O  
ATOM    234  CB  THR A  31      -1.189  -6.740 -11.404  1.00 23.68           C  
ANISOU  234  CB  THR A  31     2706   3280   3008    138    -88   -278       C  
ATOM    235  OG1 THR A  31      -0.274  -5.998 -10.602  1.00 24.44           O  
ANISOU  235  OG1 THR A  31     2805   3358   3120    154    -89   -286       O  
ATOM    236  CG2 THR A  31      -2.033  -5.764 -12.165  1.00 22.80           C  
ANISOU  236  CG2 THR A  31     2601   3207   2855    110    -66   -223       C  
ATOM    237  N   VAL A  32      -4.410  -7.879 -10.828  1.00 24.91           N  
ANISOU  237  N   VAL A  32     2897   3452   3115    120   -111   -169       N  
ATOM    238  CA  VAL A  32      -5.603  -8.405 -11.466  1.00 25.32           C  
ANISOU  238  CA  VAL A  32     2937   3561   3121     75   -109   -142       C  
ATOM    239  C   VAL A  32      -6.500  -7.295 -11.971  1.00 25.64           C  
ANISOU  239  C   VAL A  32     2946   3675   3121     84    -90    -86       C  
ATOM    240  O   VAL A  32      -6.863  -6.410 -11.219  1.00 25.56           O  
ANISOU  240  O   VAL A  32     2938   3667   3106    132    -88    -49       O  
ATOM    241  CB  VAL A  32      -6.433  -9.240 -10.513  1.00 25.42           C  
ANISOU  241  CB  VAL A  32     2973   3566   3116     54   -131   -122       C  
ATOM    242  CG1 VAL A  32      -7.285 -10.197 -11.316  1.00 24.85           C  
ANISOU  242  CG1 VAL A  32     2902   3544   2993    -20   -134   -120       C  
ATOM    243  CG2 VAL A  32      -5.537  -9.955  -9.482  1.00 24.54           C  
ANISOU  243  CG2 VAL A  32     2915   3361   3048     76   -160   -160       C  
ATOM    244  N   LEU A  33      -6.862  -7.388 -13.245  1.00 26.54           N  
ANISOU  244  N   LEU A  33     3036   3847   3201     43    -80    -84       N  
ATOM    245  CA  LEU A  33      -7.683  -6.415 -13.934  1.00 27.11           C  
ANISOU  245  CA  LEU A  33     3082   3991   3227     57    -71    -33       C  
ATOM    246  C   LEU A  33      -8.926  -7.118 -14.437  1.00 28.57           C  
ANISOU  246  C   LEU A  33     3229   4269   3357      7    -77     -8       C  
ATOM    247  O   LEU A  33      -8.932  -8.327 -14.645  1.00 28.64           O  
ANISOU  247  O   LEU A  33     3246   4274   3360    -58    -82    -39       O  
ATOM    248  CB  LEU A  33      -6.912  -5.824 -15.108  1.00 26.56           C  
ANISOU  248  CB  LEU A  33     3019   3918   3154     38    -57    -50       C  
ATOM    249  CG  LEU A  33      -5.607  -5.037 -14.897  1.00 25.12           C  
ANISOU  249  CG  LEU A  33     2870   3671   3004     56    -48    -78       C  
ATOM    250  CD1 LEU A  33      -5.414  -4.128 -16.072  1.00 23.57           C  
ANISOU  250  CD1 LEU A  33     2686   3500   2768     28    -36    -64       C  
ATOM    251  CD2 LEU A  33      -5.577  -4.189 -13.648  1.00 23.37           C  
ANISOU  251  CD2 LEU A  33     2680   3401   2797    119    -53    -50       C  
ATOM    252  N   GLU A  34     -10.000  -6.365 -14.596  1.00 30.50           N  
ANISOU  252  N   GLU A  34     3435   4600   3551     41    -78     46       N  
ATOM    253  CA  GLU A  34     -11.238  -6.906 -15.155  1.00 32.77           C  
ANISOU  253  CA  GLU A  34     3668   5009   3772     -9    -84     73       C  
ATOM    254  C   GLU A  34     -10.978  -7.246 -16.594  1.00 33.52           C  
ANISOU  254  C   GLU A  34     3763   5122   3849    -77    -78     55       C  
ATOM    255  O   GLU A  34      -9.911  -6.945 -17.118  1.00 33.90           O  
ANISOU  255  O   GLU A  34     3846   5099   3933    -75    -69     24       O  
ATOM    256  CB  GLU A  34     -12.325  -5.855 -15.112  1.00 33.58           C  
ANISOU  256  CB  GLU A  34     3722   5213   3823     69    -89    131       C  
ATOM    257  CG  GLU A  34     -12.119  -4.719 -16.133  1.00 36.28           C  
ANISOU  257  CG  GLU A  34     4081   5551   4151    118    -91    155       C  
ATOM    258  CD  GLU A  34     -12.786  -3.428 -15.698  1.00 41.14           C  
ANISOU  258  CD  GLU A  34     4694   6199   4735    244   -102    202       C  
ATOM    259  OE1 GLU A  34     -13.630  -3.468 -14.751  1.00 43.22           O  
ANISOU  259  OE1 GLU A  34     4911   6530   4977    292   -105    217       O  
ATOM    260  OE2 GLU A  34     -12.452  -2.375 -16.295  1.00 43.44           O  
ANISOU  260  OE2 GLU A  34     5040   6447   5018    295   -110    222       O  
ATOM    261  N   GLU A  35     -11.952  -7.844 -17.256  1.00 34.67           N  
ANISOU  261  N   GLU A  35     3866   5374   3931   -145    -84     73       N  
ATOM    262  CA  GLU A  35     -11.729  -8.263 -18.628  1.00 35.55           C  
ANISOU  262  CA  GLU A  35     3982   5504   4020   -222    -77     53       C  
ATOM    263  C   GLU A  35     -11.118  -7.182 -19.531  1.00 35.86           C  
ANISOU  263  C   GLU A  35     4033   5521   4068   -184    -71     60       C  
ATOM    264  O   GLU A  35     -11.640  -6.061 -19.641  1.00 36.72           O  
ANISOU  264  O   GLU A  35     4125   5676   4148   -114    -82    113       O  
ATOM    265  CB  GLU A  35     -13.004  -8.787 -19.249  1.00 36.24           C  
ANISOU  265  CB  GLU A  35     4014   5732   4021   -299    -86     85       C  
ATOM    266  CG  GLU A  35     -12.727  -9.667 -20.420  1.00 37.02           C  
ANISOU  266  CG  GLU A  35     4139   5830   4098   -407    -78     49       C  
ATOM    267  CD  GLU A  35     -12.023 -10.942 -20.005  1.00 37.31           C  
ANISOU  267  CD  GLU A  35     4249   5760   4168   -464    -74    -15       C  
ATOM    268  OE1 GLU A  35     -10.969 -11.227 -20.595  1.00 37.33           O  
ANISOU  268  OE1 GLU A  35     4297   5679   4206   -474    -62    -70       O  
ATOM    269  OE2 GLU A  35     -12.511 -11.658 -19.100  1.00 38.09           O  
ANISOU  269  OE2 GLU A  35     4363   5858   4248   -498    -86    -12       O  
ATOM    270  N   ILE A  36     -10.005  -7.541 -20.165  1.00 35.40           N  
ANISOU  270  N   ILE A  36     4012   5394   4041   -230    -55      4       N  
ATOM    271  CA  ILE A  36      -9.329  -6.677 -21.104  1.00 35.11           C  
ANISOU  271  CA  ILE A  36     3994   5345   4001   -229    -46      2       C  
ATOM    272  C   ILE A  36      -8.599  -7.525 -22.160  1.00 35.48           C  
ANISOU  272  C   ILE A  36     4052   5383   4046   -319    -26    -62       C  
ATOM    273  O   ILE A  36      -8.229  -8.680 -21.918  1.00 35.12           O  
ANISOU  273  O   ILE A  36     4020   5298   4025   -350    -20   -118       O  
ATOM    274  CB  ILE A  36      -8.421  -5.679 -20.363  1.00 34.58           C  
ANISOU  274  CB  ILE A  36     3965   5191   3980   -158    -42     -2       C  
ATOM    275  CG1 ILE A  36      -7.715  -4.758 -21.325  1.00 34.92           C  
ANISOU  275  CG1 ILE A  36     4041   5222   4003   -181    -33     -3       C  
ATOM    276  CG2 ILE A  36      -7.385  -6.379 -19.537  1.00 34.86           C  
ANISOU  276  CG2 ILE A  36     4018   5145   4081   -154    -32    -66       C  
ATOM    277  CD1 ILE A  36      -6.640  -4.009 -20.682  1.00 35.11           C  
ANISOU  277  CD1 ILE A  36     4109   5166   4064   -149    -25    -23       C  
ATOM    278  N   ASN A  37      -8.431  -6.957 -23.346  1.00 36.29           N  
ANISOU  278  N   ASN A  37     4155   5521   4110   -358    -19    -54       N  
ATOM    279  CA  ASN A  37      -7.846  -7.688 -24.456  1.00 37.12           C  
ANISOU  279  CA  ASN A  37     4264   5639   4201   -446      2   -115       C  
ATOM    280  C   ASN A  37      -6.366  -7.450 -24.672  1.00 36.69           C  
ANISOU  280  C   ASN A  37     4228   5532   4180   -452     28   -183       C  
ATOM    281  O   ASN A  37      -5.935  -6.622 -25.499  1.00 36.78           O  
ANISOU  281  O   ASN A  37     4249   5566   4159   -488     38   -178       O  
ATOM    282  CB  ASN A  37      -8.620  -7.442 -25.741  1.00 38.65           C  
ANISOU  282  CB  ASN A  37     4441   5924   4318   -511     -3    -72       C  
ATOM    283  CG  ASN A  37      -9.574  -8.570 -26.061  1.00 41.15           C  
ANISOU  283  CG  ASN A  37     4735   6305   4592   -579     -9    -70       C  
ATOM    284  OD1 ASN A  37     -10.419  -8.960 -25.230  1.00 43.89           O  
ANISOU  284  OD1 ASN A  37     5064   6675   4935   -557    -26    -40       O  
ATOM    285  ND2 ASN A  37      -9.444  -9.109 -27.270  1.00 42.74           N  
ANISOU  285  ND2 ASN A  37     4943   6544   4752   -673      5   -104       N  
ATOM    286  N   LEU A  38      -5.599  -8.233 -23.929  1.00 35.95           N  
ANISOU  286  N   LEU A  38     4140   5378   4141   -422     36   -249       N  
ATOM    287  CA  LEU A  38      -4.165  -8.152 -23.945  1.00 35.09           C  
ANISOU  287  CA  LEU A  38     4028   5239   4064   -415     58   -324       C  
ATOM    288  C   LEU A  38      -3.552  -9.082 -24.967  1.00 35.91           C  
ANISOU  288  C   LEU A  38     4123   5369   4150   -472     84   -410       C  
ATOM    289  O   LEU A  38      -4.130 -10.133 -25.319  1.00 35.21           O  
ANISOU  289  O   LEU A  38     4050   5283   4042   -502     81   -426       O  
ATOM    290  CB  LEU A  38      -3.588  -8.440 -22.559  1.00 34.46           C  
ANISOU  290  CB  LEU A  38     3955   5087   4050   -335     48   -353       C  
ATOM    291  CG  LEU A  38      -4.161  -7.609 -21.423  1.00 32.24           C  
ANISOU  291  CG  LEU A  38     3687   4774   3787   -274     25   -277       C  
ATOM    292  CD1 LEU A  38      -3.625  -8.095 -20.117  1.00 30.87           C  
ANISOU  292  CD1 LEU A  38     3522   4532   3673   -209     13   -309       C  
ATOM    293  CD2 LEU A  38      -3.823  -6.180 -21.652  1.00 32.58           C  
ANISOU  293  CD2 LEU A  38     3741   4828   3808   -280     32   -243       C  
ATOM    294  N   PRO A  39      -2.355  -8.680 -25.445  1.00 36.91           N  
ANISOU  294  N   PRO A  39     4228   5522   4274   -492    111   -471       N  
ATOM    295  CA  PRO A  39      -1.538  -9.415 -26.408  1.00 37.61           C  
ANISOU  295  CA  PRO A  39     4295   5650   4342   -534    143   -570       C  
ATOM    296  C   PRO A  39      -0.980 -10.670 -25.757  1.00 37.50           C  
ANISOU  296  C   PRO A  39     4288   5582   4375   -457    138   -653       C  
ATOM    297  O   PRO A  39      -0.909 -10.736 -24.518  1.00 37.31           O  
ANISOU  297  O   PRO A  39     4276   5496   4403   -379    113   -638       O  
ATOM    298  CB  PRO A  39      -0.389  -8.437 -26.701  1.00 37.85           C  
ANISOU  298  CB  PRO A  39     4291   5732   4356   -565    168   -603       C  
ATOM    299  CG  PRO A  39      -0.306  -7.575 -25.460  1.00 37.10           C  
ANISOU  299  CG  PRO A  39     4208   5587   4299   -506    146   -549       C  
ATOM    300  CD  PRO A  39      -1.710  -7.408 -25.033  1.00 36.65           C  
ANISOU  300  CD  PRO A  39     4191   5487   4246   -481    114   -448       C  
ATOM    301  N   GLY A  40      -0.602 -11.648 -26.581  1.00 37.49           N  
ANISOU  301  N   GLY A  40     4290   5601   4352   -477    159   -739       N  
ATOM    302  CA  GLY A  40       0.161 -12.778 -26.098  1.00 36.56           C  
ANISOU  302  CA  GLY A  40     4188   5433   4270   -388    153   -835       C  
ATOM    303  C   GLY A  40      -0.627 -14.033 -25.765  1.00 36.03           C  
ANISOU  303  C   GLY A  40     4208   5276   4204   -367    124   -832       C  
ATOM    304  O   GLY A  40      -1.841 -14.126 -25.981  1.00 35.62           O  
ANISOU  304  O   GLY A  40     4194   5219   4120   -438    112   -758       O  
ATOM    305  N   LYS A  41       0.130 -15.009 -25.269  1.00 35.73           N  
ANISOU  305  N   LYS A  41     4203   5176   4195   -271    110   -918       N  
ATOM    306  CA  LYS A  41      -0.337 -16.298 -24.821  1.00 34.80           C  
ANISOU  306  CA  LYS A  41     4195   4949   4075   -238     76   -933       C  
ATOM    307  C   LYS A  41      -0.520 -16.048 -23.373  1.00 33.13           C  
ANISOU  307  C   LYS A  41     3997   4674   3915   -178     36   -872       C  
ATOM    308  O   LYS A  41       0.215 -15.260 -22.779  1.00 32.70           O  
ANISOU  308  O   LYS A  41     3872   4648   3903   -121     38   -873       O  
ATOM    309  CB  LYS A  41       0.769 -17.346 -24.976  1.00 35.85           C  
ANISOU  309  CB  LYS A  41     4363   5045   4213   -136     75  -1064       C  
ATOM    310  CG  LYS A  41       0.301 -18.793 -25.063  1.00 37.51           C  
ANISOU  310  CG  LYS A  41     4721   5143   4388   -131     48  -1100       C  
ATOM    311  CD  LYS A  41       1.486 -19.765 -25.145  1.00 41.15           C  
ANISOU  311  CD  LYS A  41     5222   5559   4853      6     42  -1236       C  
ATOM    312  CE  LYS A  41       2.318 -19.626 -26.452  1.00 42.90           C  
ANISOU  312  CE  LYS A  41     5358   5898   5042      3     99  -1338       C  
ATOM    313  NZ  LYS A  41       3.620 -20.382 -26.436  1.00 43.64           N  
ANISOU  313  NZ  LYS A  41     5451   5984   5143    168     95  -1480       N  
ATOM    314  N   TRP A  42      -1.489 -16.732 -22.804  1.00 32.15           N  
ANISOU  314  N   TRP A  42     3966   4471   3777   -204      2   -822       N  
ATOM    315  CA  TRP A  42      -1.753 -16.626 -21.412  1.00 31.33           C  
ANISOU  315  CA  TRP A  42     3887   4305   3712   -158    -35   -766       C  
ATOM    316  C   TRP A  42      -1.812 -18.013 -20.902  1.00 32.34           C  
ANISOU  316  C   TRP A  42     4148   4311   3826   -124    -77   -805       C  
ATOM    317  O   TRP A  42      -2.156 -18.904 -21.648  1.00 33.16           O  
ANISOU  317  O   TRP A  42     4334   4387   3878   -178    -75   -837       O  
ATOM    318  CB  TRP A  42      -3.087 -15.952 -21.203  1.00 30.27           C  
ANISOU  318  CB  TRP A  42     3732   4213   3554   -247    -37   -652       C  
ATOM    319  CG  TRP A  42      -4.207 -16.554 -21.972  1.00 29.00           C  
ANISOU  319  CG  TRP A  42     3622   4073   3321   -362    -35   -624       C  
ATOM    320  CD1 TRP A  42      -4.632 -16.193 -23.210  1.00 27.39           C  
ANISOU  320  CD1 TRP A  42     3373   3961   3070   -447     -4   -610       C  
ATOM    321  CD2 TRP A  42      -5.081 -17.604 -21.538  1.00 29.37           C  
ANISOU  321  CD2 TRP A  42     3776   4057   3323   -420    -67   -602       C  
ATOM    322  NE1 TRP A  42      -5.709 -16.954 -23.586  1.00 27.28           N  
ANISOU  322  NE1 TRP A  42     3423   3953   2987   -551    -13   -582       N  
ATOM    323  CE2 TRP A  42      -6.015 -17.820 -22.572  1.00 28.31           C  
ANISOU  323  CE2 TRP A  42     3648   3992   3113   -544    -51   -577       C  
ATOM    324  CE3 TRP A  42      -5.168 -18.384 -20.368  1.00 28.86           C  
ANISOU  324  CE3 TRP A  42     3811   3888   3265   -391   -110   -600       C  
ATOM    325  CZ2 TRP A  42      -7.010 -18.781 -22.482  1.00 27.78           C  
ANISOU  325  CZ2 TRP A  42     3678   3901   2974   -648    -74   -552       C  
ATOM    326  CZ3 TRP A  42      -6.160 -19.325 -20.277  1.00 27.97           C  
ANISOU  326  CZ3 TRP A  42     3805   3742   3080   -496   -134   -573       C  
ATOM    327  CH2 TRP A  42      -7.067 -19.523 -21.334  1.00 28.51           C  
ANISOU  327  CH2 TRP A  42     3873   3889   3070   -628   -114   -551       C  
ATOM    328  N   LYS A  43      -1.457 -18.187 -19.639  1.00 33.11           N  
ANISOU  328  N   LYS A  43     4280   4332   3967    -39   -117   -800       N  
ATOM    329  CA  LYS A  43      -1.559 -19.464 -18.933  1.00 34.81           C  
ANISOU  329  CA  LYS A  43     4648   4411   4165     -6   -170   -822       C  
ATOM    330  C   LYS A  43      -2.722 -19.358 -17.948  1.00 34.65           C  
ANISOU  330  C   LYS A  43     4668   4366   4128    -84   -196   -720       C  
ATOM    331  O   LYS A  43      -3.016 -18.279 -17.459  1.00 33.71           O  
ANISOU  331  O   LYS A  43     4452   4316   4040    -96   -183   -653       O  
ATOM    332  CB  LYS A  43      -0.239 -19.745 -18.192  1.00 35.40           C  
ANISOU  332  CB  LYS A  43     4730   4426   4293    155   -202   -895       C  
ATOM    333  CG  LYS A  43      -0.242 -20.879 -17.133  1.00 38.21           C  
ANISOU  333  CG  LYS A  43     5249   4626   4640    214   -273   -903       C  
ATOM    334  CD  LYS A  43       0.864 -20.693 -16.087  1.00 41.29           C  
ANISOU  334  CD  LYS A  43     5604   4991   5093    364   -308   -934       C  
ATOM    335  CE  LYS A  43       2.268 -20.622 -16.738  1.00 43.86           C  
ANISOU  335  CE  LYS A  43     5835   5386   5444    493   -287  -1046       C  
ATOM    336  NZ  LYS A  43       3.160 -19.597 -16.096  1.00 43.20           N  
ANISOU  336  NZ  LYS A  43     5604   5391   5418    563   -280  -1046       N  
ATOM    337  N   PRO A  44      -3.402 -20.473 -17.658  1.00 36.06           N  
ANISOU  337  N   PRO A  44     4999   4451   4251   -145   -234   -709       N  
ATOM    338  CA  PRO A  44      -4.446 -20.379 -16.642  1.00 36.05           C  
ANISOU  338  CA  PRO A  44     5026   4444   4226   -225   -258   -619       C  
ATOM    339  C   PRO A  44      -3.880 -20.498 -15.236  1.00 36.15           C  
ANISOU  339  C   PRO A  44     5085   4364   4286   -128   -305   -617       C  
ATOM    340  O   PRO A  44      -3.072 -21.378 -14.985  1.00 36.75           O  
ANISOU  340  O   PRO A  44     5269   4323   4369    -38   -346   -683       O  
ATOM    341  CB  PRO A  44      -5.335 -21.567 -16.966  1.00 37.18           C  
ANISOU  341  CB  PRO A  44     5323   4530   4274   -351   -280   -614       C  
ATOM    342  CG  PRO A  44      -4.406 -22.577 -17.595  1.00 37.95           C  
ANISOU  342  CG  PRO A  44     5536   4519   4363   -275   -295   -717       C  
ATOM    343  CD  PRO A  44      -3.357 -21.800 -18.308  1.00 37.40           C  
ANISOU  343  CD  PRO A  44     5322   4527   4361   -166   -252   -775       C  
ATOM    344  N   LYS A  45      -4.298 -19.606 -14.342  1.00 35.96           N  
ANISOU  344  N   LYS A  45     4981   4394   4288   -140   -301   -545       N  
ATOM    345  CA  LYS A  45      -3.780 -19.566 -12.973  1.00 36.81           C  
ANISOU  345  CA  LYS A  45     5116   4429   4440    -57   -342   -537       C  
ATOM    346  C   LYS A  45      -4.924 -19.552 -11.962  1.00 37.35           C  
ANISOU  346  C   LYS A  45     5221   4502   4466   -156   -360   -453       C  
ATOM    347  O   LYS A  45      -5.976 -19.002 -12.253  1.00 37.40           O  
ANISOU  347  O   LYS A  45     5154   4618   4436   -254   -326   -396       O  
ATOM    348  CB  LYS A  45      -2.874 -18.346 -12.754  1.00 35.67           C  
ANISOU  348  CB  LYS A  45     4827   4350   4375     44   -316   -545       C  
ATOM    349  CG  LYS A  45      -1.867 -18.512 -11.587  1.00 36.83           C  
ANISOU  349  CG  LYS A  45     5006   4414   4572    162   -363   -572       C  
ATOM    350  CD  LYS A  45      -1.037 -17.244 -11.273  1.00 35.95           C  
ANISOU  350  CD  LYS A  45     4753   4378   4525    236   -338   -572       C  
ATOM    351  CE  LYS A  45      -0.099 -17.430 -10.065  1.00 36.50           C  
ANISOU  351  CE  LYS A  45     4852   4380   4636    343   -388   -594       C  
ATOM    352  NZ  LYS A  45       0.573 -16.165  -9.620  1.00 34.51           N  
ANISOU  352  NZ  LYS A  45     4475   4205   4433    384   -364   -583       N  
ATOM    353  N   MET A  46      -4.729 -20.185 -10.799  1.00 38.63           N  
ANISOU  353  N   MET A  46     5496   4554   4625   -131   -415   -450       N  
ATOM    354  CA  MET A  46      -5.650 -20.047  -9.658  1.00 39.22           C  
ANISOU  354  CA  MET A  46     5591   4645   4666   -216   -430   -376       C  
ATOM    355  C   MET A  46      -5.180 -18.953  -8.712  1.00 38.41           C  
ANISOU  355  C   MET A  46     5381   4576   4636   -128   -422   -351       C  
ATOM    356  O   MET A  46      -4.044 -19.004  -8.216  1.00 38.94           O  
ANISOU  356  O   MET A  46     5466   4568   4760    -10   -452   -391       O  
ATOM    357  CB  MET A  46      -5.747 -21.328  -8.818  1.00 40.62           C  
ANISOU  357  CB  MET A  46     5969   4678   4786   -257   -500   -378       C  
ATOM    358  CG  MET A  46      -6.423 -22.562  -9.441  1.00 43.55           C  
ANISOU  358  CG  MET A  46     6501   4990   5054   -385   -521   -388       C  
ATOM    359  SD  MET A  46      -7.819 -22.283 -10.537  1.00 48.23           S  
ANISOU  359  SD  MET A  46     7005   5752   5569   -560   -460   -346       S  
ATOM    360  CE  MET A  46      -9.000 -21.399  -9.528  1.00 47.58           C  
ANISOU  360  CE  MET A  46     6802   5816   5457   -654   -438   -255       C  
ATOM    361  N   ILE A  47      -6.042 -17.977  -8.447  1.00 37.43           N  
ANISOU  361  N   ILE A  47     5149   4567   4502   -182   -384   -289       N  
ATOM    362  CA  ILE A  47      -5.811 -17.084  -7.332  1.00 36.65           C  
ANISOU  362  CA  ILE A  47     4989   4483   4450   -124   -383   -259       C  
ATOM    363  C   ILE A  47      -6.973 -17.135  -6.374  1.00 37.06           C  
ANISOU  363  C   ILE A  47     5065   4575   4442   -225   -389   -197       C  
ATOM    364  O   ILE A  47      -7.943 -17.843  -6.601  1.00 38.14           O  
ANISOU  364  O   ILE A  47     5256   4737   4495   -346   -394   -177       O  
ATOM    365  CB  ILE A  47      -5.536 -15.650  -7.753  1.00 35.61           C  
ANISOU  365  CB  ILE A  47     4709   4447   4373    -62   -331   -250       C  
ATOM    366  CG1 ILE A  47      -6.732 -15.092  -8.520  1.00 35.63           C  
ANISOU  366  CG1 ILE A  47     4630   4578   4327   -138   -286   -207       C  
ATOM    367  CG2 ILE A  47      -4.251 -15.583  -8.536  1.00 35.32           C  
ANISOU  367  CG2 ILE A  47     4645   4383   4391     28   -326   -316       C  
ATOM    368  CD1 ILE A  47      -6.916 -13.593  -8.396  1.00 33.28           C  
ANISOU  368  CD1 ILE A  47     4218   4369   4057    -91   -247   -169       C  
ATOM    369  N   GLY A  48      -6.866 -16.374  -5.296  1.00 37.04           N  
ANISOU  369  N   GLY A  48     5018   4584   4471   -182   -387   -169       N  
ATOM    370  CA  GLY A  48      -7.761 -16.509  -4.167  1.00 37.31           C  
ANISOU  370  CA  GLY A  48     5085   4642   4448   -266   -400   -122       C  
ATOM    371  C   GLY A  48      -7.093 -17.460  -3.182  1.00 38.04           C  
ANISOU  371  C   GLY A  48     5324   4586   4541   -255   -467   -138       C  
ATOM    372  O   GLY A  48      -5.915 -17.301  -2.809  1.00 37.48           O  
ANISOU  372  O   GLY A  48     5262   4435   4541   -141   -491   -168       O  
ATOM    373  N   GLY A  49      -7.843 -18.483  -2.791  1.00 38.76           N  
ANISOU  373  N   GLY A  49     5536   4645   4543   -381   -501   -119       N  
ATOM    374  CA  GLY A  49      -7.426 -19.373  -1.725  1.00 38.76           C  
ANISOU  374  CA  GLY A  49     5697   4507   4523   -392   -571   -120       C  
ATOM    375  C   GLY A  49      -8.402 -19.269  -0.573  1.00 38.69           C  
ANISOU  375  C   GLY A  49     5696   4559   4444   -510   -570    -67       C  
ATOM    376  O   GLY A  49      -8.865 -20.297  -0.050  1.00 39.87           O  
ANISOU  376  O   GLY A  49     5997   4646   4503   -632   -616    -51       O  
ATOM    377  N   ILE A  50      -8.737 -18.035  -0.190  1.00 37.38           N  
ANISOU  377  N   ILE A  50     5376   4516   4307   -478   -517    -41       N  
ATOM    378  CA  ILE A  50      -9.601 -17.815   0.970  1.00 37.20           C  
ANISOU  378  CA  ILE A  50     5343   4569   4222   -571   -509      0       C  
ATOM    379  C   ILE A  50     -11.103 -17.714   0.614  1.00 37.62           C  
ANISOU  379  C   ILE A  50     5315   4803   4176   -706   -462     29       C  
ATOM    380  O   ILE A  50     -11.555 -16.735   0.023  1.00 38.14           O  
ANISOU  380  O   ILE A  50     5224   5005   4260   -659   -404     35       O  
ATOM    381  CB  ILE A  50      -9.103 -16.638   1.836  1.00 36.31           C  
ANISOU  381  CB  ILE A  50     5139   4474   4182   -461   -487      7       C  
ATOM    382  CG1 ILE A  50      -7.733 -16.986   2.450  1.00 36.35           C  
ANISOU  382  CG1 ILE A  50     5244   4312   4253   -366   -549    -15       C  
ATOM    383  CG2 ILE A  50     -10.094 -16.363   2.936  1.00 36.32           C  
ANISOU  383  CG2 ILE A  50     5114   4573   4110   -556   -469     44       C  
ATOM    384  CD1 ILE A  50      -6.804 -15.814   2.696  1.00 35.95           C  
ANISOU  384  CD1 ILE A  50     5094   4264   4300   -227   -526    -28       C  
ATOM    385  N   GLY A  51     -11.870 -18.744   0.971  1.00 37.92           N  
ANISOU  385  N   GLY A  51     5463   4846   4097   -878   -491     46       N  
ATOM    386  CA  GLY A  51     -13.288 -18.791   0.640  1.00 37.52           C  
ANISOU  386  CA  GLY A  51     5337   4986   3933  -1027   -452     70       C  
ATOM    387  C   GLY A  51     -13.566 -19.524  -0.657  1.00 37.62           C  
ANISOU  387  C   GLY A  51     5390   5004   3900  -1102   -455     57       C  
ATOM    388  O   GLY A  51     -14.721 -19.861  -0.944  1.00 38.00           O  
ANISOU  388  O   GLY A  51     5409   5198   3830  -1262   -436     75       O  
ATOM    389  N   GLY A  52     -12.489 -19.770  -1.419  1.00 36.90           N  
ANISOU  389  N   GLY A  52     5362   4761   3894   -990   -478     21       N  
ATOM    390  CA  GLY A  52     -12.498 -20.432  -2.741  1.00 35.83           C  
ANISOU  390  CA  GLY A  52     5276   4600   3735  -1029   -481     -1       C  
ATOM    391  C   GLY A  52     -11.482 -19.798  -3.687  1.00 33.98           C  
ANISOU  391  C   GLY A  52     4964   4320   3625   -848   -460    -39       C  
ATOM    392  O   GLY A  52     -10.951 -18.716  -3.418  1.00 33.23           O  
ANISOU  392  O   GLY A  52     4755   4246   3624   -710   -435    -39       O  
ATOM    393  N   PHE A  53     -11.231 -20.464  -4.810  1.00 33.51           N  
ANISOU  393  N   PHE A  53     4972   4203   3557   -861   -469    -71       N  
ATOM    394  CA  PHE A  53     -10.325 -19.968  -5.853  1.00 31.79           C  
ANISOU  394  CA  PHE A  53     4682   3959   3438   -716   -446   -112       C  
ATOM    395  C   PHE A  53     -11.055 -19.311  -7.041  1.00 30.85           C  
ANISOU  395  C   PHE A  53     4414   4006   3301   -747   -388   -100       C  
ATOM    396  O   PHE A  53     -12.196 -19.638  -7.354  1.00 31.15           O  
ANISOU  396  O   PHE A  53     4441   4157   3237   -893   -376    -72       O  
ATOM    397  CB  PHE A  53      -9.518 -21.138  -6.415  1.00 32.66           C  
ANISOU  397  CB  PHE A  53     4962   3899   3546   -697   -492   -167       C  
ATOM    398  CG  PHE A  53      -8.478 -21.682  -5.491  1.00 32.19           C  
ANISOU  398  CG  PHE A  53     5039   3662   3528   -604   -556   -192       C  
ATOM    399  CD1 PHE A  53      -8.658 -22.917  -4.884  1.00 33.70           C  
ANISOU  399  CD1 PHE A  53     5444   3724   3634   -699   -621   -189       C  
ATOM    400  CD2 PHE A  53      -7.304 -20.989  -5.262  1.00 31.32           C  
ANISOU  400  CD2 PHE A  53     4853   3514   3530   -427   -555   -221       C  
ATOM    401  CE1 PHE A  53      -7.697 -23.437  -4.040  1.00 33.76           C  
ANISOU  401  CE1 PHE A  53     5587   3564   3675   -601   -689   -210       C  
ATOM    402  CE2 PHE A  53      -6.334 -21.498  -4.423  1.00 32.16           C  
ANISOU  402  CE2 PHE A  53     5074   3473   3670   -333   -619   -246       C  
ATOM    403  CZ  PHE A  53      -6.529 -22.722  -3.811  1.00 33.38           C  
ANISOU  403  CZ  PHE A  53     5441   3495   3745   -411   -688   -240       C  
ATOM    404  N   ILE A  54     -10.366 -18.417  -7.733  1.00 29.25           N  
ANISOU  404  N   ILE A  54     4103   3822   3189   -615   -356   -121       N  
ATOM    405  CA  ILE A  54     -10.904 -17.745  -8.901  1.00 28.14           C  
ANISOU  405  CA  ILE A  54     3833   3819   3037   -624   -309   -109       C  
ATOM    406  C   ILE A  54      -9.901 -18.010 -10.002  1.00 27.85           C  
ANISOU  406  C   ILE A  54     3830   3698   3053   -557   -308   -166       C  
ATOM    407  O   ILE A  54      -8.714 -17.732  -9.842  1.00 27.16           O  
ANISOU  407  O   ILE A  54     3746   3521   3052   -431   -316   -203       O  
ATOM    408  CB  ILE A  54     -11.028 -16.215  -8.658  1.00 27.53           C  
ANISOU  408  CB  ILE A  54     3596   3848   3013   -526   -269    -78       C  
ATOM    409  CG1 ILE A  54     -12.068 -15.905  -7.553  1.00 28.29           C  
ANISOU  409  CG1 ILE A  54     3646   4048   3052   -580   -265    -29       C  
ATOM    410  CG2 ILE A  54     -11.255 -15.436  -9.974  1.00 26.85           C  
ANISOU  410  CG2 ILE A  54     3396   3869   2934   -498   -230    -73       C  
ATOM    411  CD1 ILE A  54     -13.391 -15.289  -8.029  1.00 29.71           C  
ANISOU  411  CD1 ILE A  54     3692   4435   3160   -629   -229     10       C  
ATOM    412  N   LYS A  55     -10.387 -18.572 -11.108  1.00 28.07           N  
ANISOU  412  N   LYS A  55     3879   3766   3018   -649   -299   -176       N  
ATOM    413  CA  LYS A  55      -9.577 -18.872 -12.280  1.00 27.87           C  
ANISOU  413  CA  LYS A  55     3883   3682   3025   -603   -292   -234       C  
ATOM    414  C   LYS A  55      -9.361 -17.621 -13.137  1.00 26.24           C  
ANISOU  414  C   LYS A  55     3520   3577   2872   -527   -244   -229       C  
ATOM    415  O   LYS A  55     -10.311 -17.035 -13.652  1.00 27.06           O  
ANISOU  415  O   LYS A  55     3526   3822   2933   -583   -217   -185       O  
ATOM    416  CB  LYS A  55     -10.256 -19.977 -13.090  1.00 29.27           C  
ANISOU  416  CB  LYS A  55     4159   3862   3101   -749   -300   -244       C  
ATOM    417  CG  LYS A  55      -9.524 -20.403 -14.385  1.00 32.28           C  
ANISOU  417  CG  LYS A  55     4580   4186   3496   -717   -290   -310       C  
ATOM    418  CD  LYS A  55      -8.421 -21.462 -14.172  1.00 35.28           C  
ANISOU  418  CD  LYS A  55     5129   4373   3900   -642   -333   -383       C  
ATOM    419  CE  LYS A  55      -8.596 -22.680 -15.110  1.00 36.81           C  
ANISOU  419  CE  LYS A  55     5473   4501   4011   -737   -345   -427       C  
ATOM    420  NZ  LYS A  55      -9.812 -23.509 -14.776  1.00 36.31           N  
ANISOU  420  NZ  LYS A  55     5528   4445   3822   -930   -370   -380       N  
ATOM    421  N   VAL A  56      -8.114 -17.199 -13.281  1.00 24.41           N  
ANISOU  421  N   VAL A  56     3266   3281   2726   -402   -239   -275       N  
ATOM    422  CA  VAL A  56      -7.795 -16.032 -14.098  1.00 22.01           C  
ANISOU  422  CA  VAL A  56     2839   3058   2465   -344   -198   -274       C  
ATOM    423  C   VAL A  56      -6.842 -16.378 -15.259  1.00 21.92           C  
ANISOU  423  C   VAL A  56     2844   3010   2474   -314   -185   -346       C  
ATOM    424  O   VAL A  56      -6.435 -17.545 -15.440  1.00 22.74           O  
ANISOU  424  O   VAL A  56     3057   3021   2561   -322   -209   -402       O  
ATOM    425  CB  VAL A  56      -7.290 -14.857 -13.239  1.00 21.17           C  
ANISOU  425  CB  VAL A  56     2661   2955   2427   -243   -190   -253       C  
ATOM    426  CG1 VAL A  56      -8.319 -14.516 -12.196  1.00 20.88           C  
ANISOU  426  CG1 VAL A  56     2602   2970   2359   -274   -196   -187       C  
ATOM    427  CG2 VAL A  56      -5.988 -15.172 -12.563  1.00 19.77           C  
ANISOU  427  CG2 VAL A  56     2535   2662   2312   -152   -216   -306       C  
ATOM    428  N   ARG A  57      -6.520 -15.383 -16.072  1.00 20.45           N  
ANISOU  428  N   ARG A  57     2559   2896   2312   -282   -150   -347       N  
ATOM    429  CA  ARG A  57      -5.674 -15.615 -17.210  1.00 19.79           C  
ANISOU  429  CA  ARG A  57     2475   2804   2238   -266   -131   -416       C  
ATOM    430  C   ARG A  57      -4.387 -14.880 -17.005  1.00 18.96           C  
ANISOU  430  C   ARG A  57     2316   2685   2203   -162   -120   -455       C  
ATOM    431  O   ARG A  57      -4.372 -13.663 -17.016  1.00 18.46           O  
ANISOU  431  O   ARG A  57     2172   2683   2158   -147    -99   -418       O  
ATOM    432  CB  ARG A  57      -6.353 -15.098 -18.452  1.00 19.89           C  
ANISOU  432  CB  ARG A  57     2424   2928   2205   -341    -98   -386       C  
ATOM    433  CG  ARG A  57      -7.291 -16.076 -19.077  1.00 21.60           C  
ANISOU  433  CG  ARG A  57     2699   3164   2342   -455   -104   -380       C  
ATOM    434  CD  ARG A  57      -7.706 -15.565 -20.398  1.00 22.40           C  
ANISOU  434  CD  ARG A  57     2734   3373   2404   -515    -74   -363       C  
ATOM    435  NE  ARG A  57      -8.345 -14.291 -20.176  1.00 24.58           N  
ANISOU  435  NE  ARG A  57     2913   3743   2682   -497    -67   -285       N  
ATOM    436  CZ  ARG A  57      -8.973 -13.595 -21.106  1.00 26.02           C  
ANISOU  436  CZ  ARG A  57     3029   4033   2823   -538    -51   -243       C  
ATOM    437  NH1 ARG A  57      -9.051 -14.043 -22.351  1.00 27.98           N  
ANISOU  437  NH1 ARG A  57     3288   4318   3024   -616    -37   -269       N  
ATOM    438  NH2 ARG A  57      -9.518 -12.438 -20.791  1.00 24.88           N  
ANISOU  438  NH2 ARG A  57     2813   3958   2679   -496    -52   -175       N  
ATOM    439  N   GLN A  58      -3.303 -15.615 -16.817  1.00 19.00           N  
ANISOU  439  N   GLN A  58     2369   2611   2239    -90   -138   -533       N  
ATOM    440  CA  GLN A  58      -2.011 -14.998 -16.575  1.00 18.96           C  
ANISOU  440  CA  GLN A  58     2300   2612   2289      2   -131   -579       C  
ATOM    441  C   GLN A  58      -1.275 -14.623 -17.847  1.00 19.29           C  
ANISOU  441  C   GLN A  58     2273   2729   2325     -1    -90   -636       C  
ATOM    442  O   GLN A  58      -0.913 -15.487 -18.626  1.00 20.92           O  
ANISOU  442  O   GLN A  58     2514   2923   2511      3    -86   -707       O  
ATOM    443  CB  GLN A  58      -1.127 -15.911 -15.764  1.00 18.73           C  
ANISOU  443  CB  GLN A  58     2338   2487   2291     98   -173   -640       C  
ATOM    444  CG  GLN A  58       0.072 -15.208 -15.344  1.00 19.87           C  
ANISOU  444  CG  GLN A  58     2404   2661   2484    183   -169   -675       C  
ATOM    445  CD  GLN A  58       1.134 -16.103 -14.824  1.00 24.15           C  
ANISOU  445  CD  GLN A  58     2989   3136   3050    297   -209   -754       C  
ATOM    446  OE1 GLN A  58       0.883 -17.040 -14.066  1.00 26.06           O  
ANISOU  446  OE1 GLN A  58     3341   3271   3287    326   -259   -749       O  
ATOM    447  NE2 GLN A  58       2.362 -15.814 -15.217  1.00 27.32           N  
ANISOU  447  NE2 GLN A  58     3305   3606   3470    364   -192   -829       N  
ATOM    448  N   TYR A  59      -1.044 -13.335 -18.042  1.00 18.89           N  
ANISOU  448  N   TYR A  59     2137   2755   2285    -14    -61   -608       N  
ATOM    449  CA  TYR A  59      -0.334 -12.842 -19.192  1.00 19.47           C  
ANISOU  449  CA  TYR A  59     2145   2909   2342    -37    -21   -656       C  
ATOM    450  C   TYR A  59       0.983 -12.290 -18.728  1.00 20.27           C  
ANISOU  450  C   TYR A  59     2186   3036   2477     25    -17   -704       C  
ATOM    451  O   TYR A  59       1.054 -11.683 -17.677  1.00 20.88           O  
ANISOU  451  O   TYR A  59     2257   3091   2584     55    -33   -661       O  
ATOM    452  CB  TYR A  59      -1.091 -11.697 -19.824  1.00 19.04           C  
ANISOU  452  CB  TYR A  59     2054   2924   2254   -118      3   -580       C  
ATOM    453  CG  TYR A  59      -2.332 -12.095 -20.575  1.00 19.45           C  
ANISOU  453  CG  TYR A  59     2137   2994   2257   -195      5   -537       C  
ATOM    454  CD1 TYR A  59      -3.534 -12.247 -19.910  1.00 19.45           C  
ANISOU  454  CD1 TYR A  59     2170   2971   2246   -211    -18   -463       C  
ATOM    455  CD2 TYR A  59      -2.319 -12.266 -21.948  1.00 18.70           C  
ANISOU  455  CD2 TYR A  59     2029   2956   2118   -260     32   -569       C  
ATOM    456  CE1 TYR A  59      -4.667 -12.597 -20.571  1.00 19.68           C  
ANISOU  456  CE1 TYR A  59     2215   3042   2220   -290    -18   -424       C  
ATOM    457  CE2 TYR A  59      -3.476 -12.618 -22.623  1.00 19.95           C  
ANISOU  457  CE2 TYR A  59     2212   3143   2225   -338     31   -526       C  
ATOM    458  CZ  TYR A  59      -4.641 -12.782 -21.913  1.00 18.80           C  
ANISOU  458  CZ  TYR A  59     2093   2980   2067   -353      4   -454       C  
ATOM    459  OH  TYR A  59      -5.810 -13.110 -22.517  1.00 19.36           O  
ANISOU  459  OH  TYR A  59     2176   3102   2077   -438      1   -410       O  
ATOM    460  N   ASP A  60       2.039 -12.454 -19.506  1.00 21.05           N  
ANISOU  460  N   ASP A  60     2234   3198   2565     39      6   -794       N  
ATOM    461  CA  ASP A  60       3.307 -11.997 -19.018  1.00 21.23           C  
ANISOU  461  CA  ASP A  60     2187   3268   2609     93      8   -845       C  
ATOM    462  C   ASP A  60       3.811 -10.736 -19.703  1.00 21.13           C  
ANISOU  462  C   ASP A  60     2099   3365   2562     11     51   -842       C  
ATOM    463  O   ASP A  60       3.401 -10.405 -20.806  1.00 21.69           O  
ANISOU  463  O   ASP A  60     2167   3482   2590    -74     81   -827       O  
ATOM    464  CB  ASP A  60       4.323 -13.136 -19.073  1.00 22.45           C  
ANISOU  464  CB  ASP A  60     2330   3425   2772    195     -4   -961       C  
ATOM    465  CG  ASP A  60       4.172 -14.097 -17.921  1.00 22.86           C  
ANISOU  465  CG  ASP A  60     2465   3358   2862    294    -61   -958       C  
ATOM    466  OD1 ASP A  60       3.805 -13.658 -16.814  1.00 25.74           O  
ANISOU  466  OD1 ASP A  60     2852   3672   3255    297    -87   -885       O  
ATOM    467  OD2 ASP A  60       4.426 -15.291 -18.109  1.00 23.83           O  
ANISOU  467  OD2 ASP A  60     2641   3432   2980    368    -83  -1029       O  
ATOM    468  N   GLN A  61       4.700 -10.039 -19.009  1.00 20.73           N  
ANISOU  468  N   GLN A  61     1998   3354   2522     29     49   -854       N  
ATOM    469  CA  GLN A  61       5.394  -8.893 -19.534  1.00 20.39           C  
ANISOU  469  CA  GLN A  61     1894   3417   2435    -56     85   -863       C  
ATOM    470  C   GLN A  61       4.524  -7.938 -20.274  1.00 19.42           C  
ANISOU  470  C   GLN A  61     1813   3295   2270   -166    106   -781       C  
ATOM    471  O   GLN A  61       4.798  -7.583 -21.406  1.00 19.45           O  
ANISOU  471  O   GLN A  61     1788   3380   2219   -251    140   -807       O  
ATOM    472  CB  GLN A  61       6.537  -9.350 -20.363  1.00 21.66           C  
ANISOU  472  CB  GLN A  61     1968   3697   2565    -51    114   -981       C  
ATOM    473  CG  GLN A  61       7.455 -10.132 -19.463  1.00 24.34           C  
ANISOU  473  CG  GLN A  61     2264   4040   2942     78     83  -1057       C  
ATOM    474  CD  GLN A  61       8.516 -10.886 -20.208  1.00 25.22           C  
ANISOU  474  CD  GLN A  61     2289   4266   3027    130    103  -1190       C  
ATOM    475  OE1 GLN A  61       8.535 -10.912 -21.441  1.00 24.73           O  
ANISOU  475  OE1 GLN A  61     2202   4275   2918     63    144  -1230       O  
ATOM    476  NE2 GLN A  61       9.403 -11.531 -19.456  1.00 26.54           N  
ANISOU  476  NE2 GLN A  61     2410   4453   3220    261     72  -1262       N  
ATOM    477  N   ILE A  62       3.479  -7.509 -19.570  1.00 18.16           N  
ANISOU  477  N   ILE A  62     1722   3046   2131   -157     82   -682       N  
ATOM    478  CA  ILE A  62       2.480  -6.586 -20.072  1.00 16.85           C  
ANISOU  478  CA  ILE A  62     1606   2866   1928   -227     89   -591       C  
ATOM    479  C   ILE A  62       2.896  -5.242 -19.524  1.00 17.23           C  
ANISOU  479  C   ILE A  62     1674   2914   1955   -262     90   -551       C  
ATOM    480  O   ILE A  62       3.395  -5.168 -18.401  1.00 17.27           O  
ANISOU  480  O   ILE A  62     1672   2892   1994   -213     75   -559       O  
ATOM    481  CB  ILE A  62       1.040  -6.984 -19.561  1.00 15.51           C  
ANISOU  481  CB  ILE A  62     1493   2615   1786   -181     60   -514       C  
ATOM    482  CG1 ILE A  62       0.629  -8.400 -20.002  1.00 13.38           C  
ANISOU  482  CG1 ILE A  62     1225   2334   1525   -162     55   -554       C  
ATOM    483  CG2 ILE A  62      -0.001  -5.932 -19.898  1.00 14.70           C  
ANISOU  483  CG2 ILE A  62     1435   2506   1643   -223     59   -419       C  
ATOM    484  CD1 ILE A  62       0.625  -8.685 -21.476  1.00 11.20           C  
ANISOU  484  CD1 ILE A  62      931   2121   1202   -231     82   -591       C  
ATOM    485  N   LEU A  63       2.695  -4.198 -20.314  1.00 17.74           N  
ANISOU  485  N   LEU A  63     1776   3004   1959   -351    105   -508       N  
ATOM    486  CA  LEU A  63       3.052  -2.844 -19.937  1.00 18.80           C  
ANISOU  486  CA  LEU A  63     1962   3127   2054   -403    105   -466       C  
ATOM    487  C   LEU A  63       1.828  -2.050 -19.536  1.00 18.91           C  
ANISOU  487  C   LEU A  63     2071   3051   2063   -370     81   -360       C  
ATOM    488  O   LEU A  63       0.838  -2.008 -20.253  1.00 19.23           O  
ANISOU  488  O   LEU A  63     2140   3083   2080   -373     74   -312       O  
ATOM    489  CB  LEU A  63       3.792  -2.171 -21.097  1.00 19.95           C  
ANISOU  489  CB  LEU A  63     2104   3359   2116   -533    135   -496       C  
ATOM    490  CG  LEU A  63       3.960  -0.667 -21.292  1.00 20.44           C  
ANISOU  490  CG  LEU A  63     2260   3409   2097   -637    136   -442       C  
ATOM    491  CD1 LEU A  63       5.210  -0.179 -20.672  1.00 20.40           C  
ANISOU  491  CD1 LEU A  63     2233   3450   2067   -694    147   -487       C  
ATOM    492  CD2 LEU A  63       3.991  -0.391 -22.786  1.00 22.64           C  
ANISOU  492  CD2 LEU A  63     2552   3753   2297   -753    156   -448       C  
ATOM    493  N   ILE A  64       1.897  -1.459 -18.357  1.00 19.54           N  
ANISOU  493  N   ILE A  64     2193   3069   2160   -330     65   -328       N  
ATOM    494  CA  ILE A  64       0.882  -0.553 -17.873  1.00 20.02           C  
ANISOU  494  CA  ILE A  64     2349   3050   2207   -288     44   -237       C  
ATOM    495  C   ILE A  64       1.612   0.771 -17.555  1.00 21.16           C  
ANISOU  495  C   ILE A  64     2577   3165   2295   -354     47   -221       C  
ATOM    496  O   ILE A  64       2.795   0.793 -17.205  1.00 21.02           O  
ANISOU  496  O   ILE A  64     2524   3186   2273   -407     60   -277       O  
ATOM    497  CB  ILE A  64       0.180  -1.052 -16.569  1.00 19.43           C  
ANISOU  497  CB  ILE A  64     2267   2915   2198   -177     23   -212       C  
ATOM    498  CG1 ILE A  64       1.140  -1.003 -15.399  1.00 21.32           C  
ANISOU  498  CG1 ILE A  64     2496   3134   2468   -165     21   -246       C  
ATOM    499  CG2 ILE A  64      -0.370  -2.463 -16.657  1.00 18.29           C  
ANISOU  499  CG2 ILE A  64     2052   2792   2102   -130     18   -236       C  
ATOM    500  CD1 ILE A  64       0.440  -0.904 -14.074  1.00 25.77           C  
ANISOU  500  CD1 ILE A  64     3096   3625   3067    -79      1   -201       C  
ATOM    501  N   GLU A  65       0.911   1.882 -17.661  1.00 21.87           N  
ANISOU  501  N   GLU A  65     2785   3191   2333   -351     31   -146       N  
ATOM    502  CA  GLU A  65       1.521   3.113 -17.290  1.00 23.04           C  
ANISOU  502  CA  GLU A  65     3042   3291   2421   -414     29   -127       C  
ATOM    503  C   GLU A  65       0.648   3.705 -16.230  1.00 23.52           C  
ANISOU  503  C   GLU A  65     3190   3248   2495   -307      5    -63       C  
ATOM    504  O   GLU A  65      -0.559   3.591 -16.304  1.00 23.24           O  
ANISOU  504  O   GLU A  65     3162   3189   2475   -210    -11    -16       O  
ATOM    505  CB  GLU A  65       1.602   4.025 -18.487  1.00 23.82           C  
ANISOU  505  CB  GLU A  65     3236   3392   2420   -521     29   -100       C  
ATOM    506  CG  GLU A  65       2.082   5.397 -18.166  1.00 25.13           C  
ANISOU  506  CG  GLU A  65     3556   3486   2502   -597     20    -69       C  
ATOM    507  CD  GLU A  65       1.817   6.362 -19.276  1.00 28.23           C  
ANISOU  507  CD  GLU A  65     4087   3846   2791   -675      5    -19       C  
ATOM    508  OE1 GLU A  65       2.075   6.019 -20.462  1.00 25.71           O  
ANISOU  508  OE1 GLU A  65     3714   3611   2440   -765     20    -46       O  
ATOM    509  OE2 GLU A  65       1.334   7.471 -18.938  1.00 32.20           O  
ANISOU  509  OE2 GLU A  65     4761   4232   3240   -642    -23     46       O  
ATOM    510  N   ILE A  66       1.274   4.295 -15.221  1.00 24.81           N  
ANISOU  510  N   ILE A  66     3410   3364   2650   -324      5    -68       N  
ATOM    511  CA  ILE A  66       0.575   4.973 -14.147  1.00 26.21           C  
ANISOU  511  CA  ILE A  66     3686   3441   2830   -229    -13    -15       C  
ATOM    512  C   ILE A  66       1.234   6.309 -13.809  1.00 27.92           C  
ANISOU  512  C   ILE A  66     4059   3583   2964   -310    -16      1       C  
ATOM    513  O   ILE A  66       2.451   6.384 -13.627  1.00 28.17           O  
ANISOU  513  O   ILE A  66     4072   3656   2974   -426      0    -44       O  
ATOM    514  CB  ILE A  66       0.525   4.122 -12.866  1.00 25.68           C  
ANISOU  514  CB  ILE A  66     3528   3376   2850   -147    -12    -40       C  
ATOM    515  CG1 ILE A  66       0.018   2.705 -13.168  1.00 24.78           C  
ANISOU  515  CG1 ILE A  66     3275   3332   2808    -91    -11    -64       C  
ATOM    516  CG2 ILE A  66      -0.331   4.831 -11.805  1.00 26.19           C  
ANISOU  516  CG2 ILE A  66     3691   3347   2912    -43    -28     12       C  
ATOM    517  CD1 ILE A  66      -0.471   1.965 -11.967  1.00 24.04           C  
ANISOU  517  CD1 ILE A  66     3129   3220   2783      1    -20    -65       C  
ATOM    518  N   CYS A  67       0.420   7.354 -13.719  1.00 29.47           N  
ANISOU  518  N   CYS A  67     4413   3676   3107   -248    -38     66       N  
ATOM    519  CA  CYS A  67       0.917   8.703 -13.452  1.00 32.03           C  
ANISOU  519  CA  CYS A  67     4930   3903   3336   -324    -47     90       C  
ATOM    520  C   CYS A  67       2.262   9.004 -14.110  1.00 32.31           C  
ANISOU  520  C   CYS A  67     4984   3993   3297   -528    -30     52       C  
ATOM    521  O   CYS A  67       3.140   9.584 -13.478  1.00 33.37           O  
ANISOU  521  O   CYS A  67     5189   4104   3383   -626    -23     35       O  
ATOM    522  CB  CYS A  67       1.050   8.948 -11.954  1.00 32.22           C  
ANISOU  522  CB  CYS A  67     4991   3864   3385   -275    -46     86       C  
ATOM    523  SG  CYS A  67      -0.460   8.651 -11.030  1.00 38.13           S  
ANISOU  523  SG  CYS A  67     5713   4567   4205    -52    -59    122       S  
ATOM    524  N   GLY A  68       2.436   8.607 -15.364  1.00 32.10           N  
ANISOU  524  N   GLY A  68     4890   4051   3253   -601    -21     34       N  
ATOM    525  CA  GLY A  68       3.597   9.038 -16.120  1.00 32.13           C  
ANISOU  525  CA  GLY A  68     4928   4116   3163   -803     -5      2       C  
ATOM    526  C   GLY A  68       4.660   7.974 -16.175  1.00 31.48           C  
ANISOU  526  C   GLY A  68     4637   4193   3128   -876     28    -85       C  
ATOM    527  O   GLY A  68       5.513   7.993 -17.037  1.00 32.11           O  
ANISOU  527  O   GLY A  68     4682   4374   3144  -1027     48   -127       O  
ATOM    528  N   LYS A  69       4.594   7.020 -15.266  1.00 30.25           N  
ANISOU  528  N   LYS A  69     4344   4066   3081   -762     33   -117       N  
ATOM    529  CA  LYS A  69       5.660   6.051 -15.142  1.00 29.65           C  
ANISOU  529  CA  LYS A  69     4086   4130   3048   -806     57   -203       C  
ATOM    530  C   LYS A  69       5.223   4.688 -15.737  1.00 27.81           C  
ANISOU  530  C   LYS A  69     3695   3967   2903   -712     64   -238       C  
ATOM    531  O   LYS A  69       4.124   4.225 -15.477  1.00 26.69           O  
ANISOU  531  O   LYS A  69     3548   3763   2830   -576     48   -200       O  
ATOM    532  CB  LYS A  69       6.110   6.012 -13.663  1.00 29.67           C  
ANISOU  532  CB  LYS A  69     4069   4113   3090   -769     52   -218       C  
ATOM    533  CG  LYS A  69       7.052   4.860 -13.251  1.00 32.30           C  
ANISOU  533  CG  LYS A  69     4207   4576   3487   -754     63   -303       C  
ATOM    534  CD  LYS A  69       8.552   5.167 -13.369  1.00 35.24           C  
ANISOU  534  CD  LYS A  69     4526   5085   3779   -919     82   -367       C  
ATOM    535  CE  LYS A  69       9.409   3.913 -13.073  1.00 34.41           C  
ANISOU  535  CE  LYS A  69     4212   5121   3739   -865     87   -457       C  
ATOM    536  NZ  LYS A  69      10.879   4.209 -13.016  1.00 34.22           N  
ANISOU  536  NZ  LYS A  69     4112   5257   3632  -1011    104   -525       N  
ATOM    537  N   LYS A  70       6.080   4.079 -16.557  1.00 27.27           N  
ANISOU  537  N   LYS A  70     3506   4035   2820   -793     89   -311       N  
ATOM    538  CA  LYS A  70       5.796   2.786 -17.204  1.00 26.28           C  
ANISOU  538  CA  LYS A  70     3247   3975   2763   -719     98   -354       C  
ATOM    539  C   LYS A  70       6.346   1.579 -16.436  1.00 24.84           C  
ANISOU  539  C   LYS A  70     2918   3851   2666   -631     98   -425       C  
ATOM    540  O   LYS A  70       7.390   1.654 -15.785  1.00 24.48           O  
ANISOU  540  O   LYS A  70     2823   3867   2609   -669    102   -472       O  
ATOM    541  CB  LYS A  70       6.322   2.769 -18.639  1.00 27.33           C  
ANISOU  541  CB  LYS A  70     3340   4218   2825   -843    125   -398       C  
ATOM    542  CG  LYS A  70       5.765   3.903 -19.534  1.00 31.24           C  
ANISOU  542  CG  LYS A  70     3991   4652   3226   -935    117   -326       C  
ATOM    543  CD  LYS A  70       6.675   4.244 -20.729  1.00 38.02           C  
ANISOU  543  CD  LYS A  70     4837   5630   3978  -1119    146   -373       C  
ATOM    544  CE  LYS A  70       8.037   4.904 -20.289  1.00 42.53           C  
ANISOU  544  CE  LYS A  70     5409   6283   4468  -1268    164   -418       C  
ATOM    545  NZ  LYS A  70       8.297   6.305 -20.797  1.00 45.09           N  
ANISOU  545  NZ  LYS A  70     5909   6575   4647  -1454    160   -372       N  
ATOM    546  N   ALA A  71       5.619   0.469 -16.515  1.00 23.44           N  
ANISOU  546  N   ALA A  71     2682   3655   2567   -515     89   -431       N  
ATOM    547  CA  ALA A  71       5.986  -0.778 -15.848  1.00 22.23           C  
ANISOU  547  CA  ALA A  71     2420   3532   2494   -416     80   -492       C  
ATOM    548  C   ALA A  71       5.744  -1.973 -16.742  1.00 21.79           C  
ANISOU  548  C   ALA A  71     2288   3519   2469   -372     87   -539       C  
ATOM    549  O   ALA A  71       4.748  -2.009 -17.444  1.00 22.40           O  
ANISOU  549  O   ALA A  71     2409   3558   2542   -370     88   -494       O  
ATOM    550  CB  ALA A  71       5.195  -0.937 -14.632  1.00 21.39           C  
ANISOU  550  CB  ALA A  71     2359   3316   2450   -311     50   -438       C  
ATOM    551  N   ILE A  72       6.638  -2.959 -16.706  1.00 21.29           N  
ANISOU  551  N   ILE A  72     2118   3538   2434   -331     90   -631       N  
ATOM    552  CA  ILE A  72       6.414  -4.251 -17.375  1.00 19.94           C  
ANISOU  552  CA  ILE A  72     1892   3386   2297   -267     92   -683       C  
ATOM    553  C   ILE A  72       6.187  -5.390 -16.368  1.00 19.21           C  
ANISOU  553  C   ILE A  72     1791   3224   2284   -131     56   -696       C  
ATOM    554  O   ILE A  72       7.059  -5.732 -15.603  1.00 20.04           O  
ANISOU  554  O   ILE A  72     1843   3359   2410    -77     39   -747       O  
ATOM    555  CB  ILE A  72       7.532  -4.560 -18.377  1.00 20.10           C  
ANISOU  555  CB  ILE A  72     1811   3554   2271   -319    125   -787       C  
ATOM    556  CG1 ILE A  72       7.282  -3.783 -19.654  1.00 20.68           C  
ANISOU  556  CG1 ILE A  72     1919   3669   2269   -450    157   -762       C  
ATOM    557  CG2 ILE A  72       7.538  -5.978 -18.783  1.00 20.38           C  
ANISOU  557  CG2 ILE A  72     1794   3602   2345   -225    121   -859       C  
ATOM    558  CD1 ILE A  72       7.794  -2.389 -19.574  1.00 23.45           C  
ANISOU  558  CD1 ILE A  72     2310   4054   2545   -577    169   -730       C  
ATOM    559  N   GLY A  73       5.009  -5.985 -16.345  1.00 18.37           N  
ANISOU  559  N   GLY A  73     1740   3028   2213    -82     39   -649       N  
ATOM    560  CA  GLY A  73       4.823  -7.102 -15.424  1.00 17.33           C  
ANISOU  560  CA  GLY A  73     1616   2826   2141     26      2   -663       C  
ATOM    561  C   GLY A  73       3.766  -8.097 -15.831  1.00 16.42           C  
ANISOU  561  C   GLY A  73     1545   2651   2041     54     -8   -647       C  
ATOM    562  O   GLY A  73       3.094  -7.921 -16.847  1.00 15.89           O  
ANISOU  562  O   GLY A  73     1492   2602   1942     -5     13   -622       O  
ATOM    563  N   THR A  74       3.638  -9.143 -15.020  1.00 16.33           N  
ANISOU  563  N   THR A  74     1561   2570   2071    138    -45   -661       N  
ATOM    564  CA  THR A  74       2.594 -10.147 -15.176  1.00 16.02           C  
ANISOU  564  CA  THR A  74     1584   2463   2038    152    -62   -640       C  
ATOM    565  C   THR A  74       1.296  -9.513 -14.794  1.00 15.57           C  
ANISOU  565  C   THR A  74     1574   2368   1974    111    -63   -538       C  
ATOM    566  O   THR A  74       1.206  -8.865 -13.757  1.00 15.25           O  
ANISOU  566  O   THR A  74     1546   2297   1950    128    -75   -492       O  
ATOM    567  CB  THR A  74       2.780 -11.334 -14.223  1.00 15.87           C  
ANISOU  567  CB  THR A  74     1611   2363   2053    242   -110   -671       C  
ATOM    568  OG1 THR A  74       4.139 -11.778 -14.246  1.00 17.60           O  
ANISOU  568  OG1 THR A  74     1778   2624   2283    315   -119   -767       O  
ATOM    569  CG2 THR A  74       1.896 -12.457 -14.608  1.00 14.69           C  
ANISOU  569  CG2 THR A  74     1536   2154   1891    234   -125   -668       C  
ATOM    570  N   VAL A  75       0.291  -9.717 -15.637  1.00 15.89           N  
ANISOU  570  N   VAL A  75     1634   2418   1984     61    -51   -507       N  
ATOM    571  CA  VAL A  75      -1.067  -9.278 -15.375  1.00 15.35           C  
ANISOU  571  CA  VAL A  75     1597   2336   1899     33    -55   -417       C  
ATOM    572  C   VAL A  75      -2.032 -10.415 -15.609  1.00 15.61           C  
ANISOU  572  C   VAL A  75     1669   2349   1913     11    -70   -409       C  
ATOM    573  O   VAL A  75      -1.999 -11.077 -16.627  1.00 15.65           O  
ANISOU  573  O   VAL A  75     1676   2374   1895    -21    -60   -449       O  
ATOM    574  CB  VAL A  75      -1.440  -8.078 -16.237  1.00 15.30           C  
ANISOU  574  CB  VAL A  75     1571   2388   1853    -18    -27   -371       C  
ATOM    575  CG1 VAL A  75      -2.803  -7.526 -15.831  1.00 14.51           C  
ANISOU  575  CG1 VAL A  75     1493   2285   1732    -16    -36   -282       C  
ATOM    576  CG2 VAL A  75      -0.378  -7.021 -16.087  1.00 15.32           C  
ANISOU  576  CG2 VAL A  75     1555   2407   1858    -20    -13   -387       C  
ATOM    577  N   LEU A  76      -2.895 -10.614 -14.632  1.00 16.51           N  
ANISOU  577  N   LEU A  76     1818   2426   2028     18    -93   -357       N  
ATOM    578  CA  LEU A  76      -3.880 -11.668 -14.636  1.00 17.58           C  
ANISOU  578  CA  LEU A  76     1999   2546   2131    -23   -111   -341       C  
ATOM    579  C   LEU A  76      -5.234 -11.018 -14.916  1.00 18.53           C  
ANISOU  579  C   LEU A  76     2090   2742   2205    -72    -98   -264       C  
ATOM    580  O   LEU A  76      -5.607 -10.029 -14.280  1.00 18.59           O  
ANISOU  580  O   LEU A  76     2074   2770   2217    -42    -94   -212       O  
ATOM    581  CB  LEU A  76      -3.921 -12.358 -13.266  1.00 17.31           C  
ANISOU  581  CB  LEU A  76     2025   2433   2116      6   -149   -338       C  
ATOM    582  CG  LEU A  76      -2.670 -12.511 -12.403  1.00 15.64           C  
ANISOU  582  CG  LEU A  76     1829   2153   1958     87   -172   -385       C  
ATOM    583  CD1 LEU A  76      -3.000 -12.892 -10.975  1.00 13.68           C  
ANISOU  583  CD1 LEU A  76     1639   1841   1718    102   -209   -354       C  
ATOM    584  CD2 LEU A  76      -1.829 -13.546 -13.006  1.00 14.95           C  
ANISOU  584  CD2 LEU A  76     1774   2029   1875    115   -184   -467       C  
ATOM    585  N   VAL A  77      -5.970 -11.592 -15.857  1.00 19.89           N  
ANISOU  585  N   VAL A  77     2267   2962   2329   -142    -92   -259       N  
ATOM    586  CA  VAL A  77      -7.251 -11.056 -16.286  1.00 20.65           C  
ANISOU  586  CA  VAL A  77     2321   3155   2371   -186    -84   -192       C  
ATOM    587  C   VAL A  77      -8.367 -12.018 -15.878  1.00 22.63           C  
ANISOU  587  C   VAL A  77     2598   3428   2569   -253   -103   -167       C  
ATOM    588  O   VAL A  77      -8.335 -13.201 -16.206  1.00 23.33           O  
ANISOU  588  O   VAL A  77     2747   3482   2634   -313   -113   -204       O  
ATOM    589  CB  VAL A  77      -7.239 -10.773 -17.812  1.00 19.96           C  
ANISOU  589  CB  VAL A  77     2202   3130   2251   -229    -61   -199       C  
ATOM    590  CG1 VAL A  77      -8.483 -10.089 -18.247  1.00 18.71           C  
ANISOU  590  CG1 VAL A  77     1995   3077   2036   -253    -59   -127       C  
ATOM    591  CG2 VAL A  77      -6.082  -9.903 -18.132  1.00 18.40           C  
ANISOU  591  CG2 VAL A  77     1988   2911   2091   -185    -44   -229       C  
ATOM    592  N   GLY A  78      -9.330 -11.496 -15.129  1.00 24.47           N  
ANISOU  592  N   GLY A  78     2796   3723   2778   -244   -107   -107       N  
ATOM    593  CA  GLY A  78     -10.521 -12.240 -14.736  1.00 27.17           C  
ANISOU  593  CA  GLY A  78     3143   4126   3051   -325   -121    -77       C  
ATOM    594  C   GLY A  78     -11.441 -11.328 -13.955  1.00 29.00           C  
ANISOU  594  C   GLY A  78     3306   4449   3261   -283   -118    -18       C  
ATOM    595  O   GLY A  78     -11.067 -10.173 -13.686  1.00 28.78           O  
ANISOU  595  O   GLY A  78     3249   4407   3276   -186   -108     -3       O  
ATOM    596  N   PRO A  79     -12.633 -11.840 -13.562  1.00 30.89           N  
ANISOU  596  N   PRO A  79     3524   4787   3425   -360   -126     12       N  
ATOM    597  CA  PRO A  79     -13.685 -11.096 -12.829  1.00 31.72           C  
ANISOU  597  CA  PRO A  79     3547   5015   3489   -325   -121     61       C  
ATOM    598  C   PRO A  79     -13.218 -10.633 -11.467  1.00 31.80           C  
ANISOU  598  C   PRO A  79     3582   4947   3553   -244   -123     59       C  
ATOM    599  O   PRO A  79     -13.089 -11.437 -10.551  1.00 32.34           O  
ANISOU  599  O   PRO A  79     3711   4955   3621   -295   -139     45       O  
ATOM    600  CB  PRO A  79     -14.806 -12.119 -12.655  1.00 32.84           C  
ANISOU  600  CB  PRO A  79     3679   5265   3531   -462   -130     75       C  
ATOM    601  CG  PRO A  79     -14.159 -13.454 -12.779  1.00 33.60           C  
ANISOU  601  CG  PRO A  79     3899   5234   3634   -558   -148     31       C  
ATOM    602  CD  PRO A  79     -12.939 -13.279 -13.669  1.00 31.73           C  
ANISOU  602  CD  PRO A  79     3700   4881   3475   -493   -142     -7       C  
ATOM    603  N   THR A  80     -12.942  -9.340 -11.355  1.00 32.09           N  
ANISOU  603  N   THR A  80     3586   4976   3631   -125   -111     75       N  
ATOM    604  CA  THR A  80     -12.456  -8.737 -10.114  1.00 31.72           C  
ANISOU  604  CA  THR A  80     3565   4853   3633    -44   -110     73       C  
ATOM    605  C   THR A  80     -13.252  -7.460  -9.796  1.00 32.59           C  
ANISOU  605  C   THR A  80     3608   5059   3713     55    -97    112       C  
ATOM    606  O   THR A  80     -13.376  -6.561 -10.663  1.00 33.23           O  
ANISOU  606  O   THR A  80     3661   5176   3786    119    -91    131       O  
ATOM    607  CB  THR A  80     -10.962  -8.404 -10.175  1.00 30.79           C  
ANISOU  607  CB  THR A  80     3509   4588   3601      8   -110     39       C  
ATOM    608  OG1 THR A  80     -10.655  -7.436  -9.168  1.00 29.43           O  
ANISOU  608  OG1 THR A  80     3347   4372   3461     95   -105     50       O  
ATOM    609  CG2 THR A  80     -10.619  -7.807 -11.493  1.00 30.70           C  
ANISOU  609  CG2 THR A  80     3482   4586   3596     29    -99     38       C  
ATOM    610  N   PRO A  81     -13.786  -7.376  -8.549  1.00 32.65           N  
ANISOU  610  N   PRO A  81     3600   5106   3699     73    -95    122       N  
ATOM    611  CA  PRO A  81     -14.664  -6.295  -8.050  1.00 32.41           C  
ANISOU  611  CA  PRO A  81     3506   5180   3629    176    -82    150       C  
ATOM    612  C   PRO A  81     -14.084  -4.907  -8.304  1.00 31.54           C  
ANISOU  612  C   PRO A  81     3430   4992   3559    307    -76    158       C  
ATOM    613  O   PRO A  81     -14.819  -3.938  -8.524  1.00 31.95           O  
ANISOU  613  O   PRO A  81     3439   5129   3568    408    -72    184       O  
ATOM    614  CB  PRO A  81     -14.711  -6.558  -6.535  1.00 32.45           C  
ANISOU  614  CB  PRO A  81     3531   5164   3634    161    -80    140       C  
ATOM    615  CG  PRO A  81     -14.441  -8.004  -6.390  1.00 33.00           C  
ANISOU  615  CG  PRO A  81     3648   5187   3702     19    -97    121       C  
ATOM    616  CD  PRO A  81     -13.512  -8.387  -7.505  1.00 32.45           C  
ANISOU  616  CD  PRO A  81     3629   5016   3683     -5   -107    102       C  
ATOM    617  N   VAL A  82     -12.760  -4.830  -8.241  1.00 30.27           N  
ANISOU  617  N   VAL A  82     3353   4673   3474    304    -78    135       N  
ATOM    618  CA  VAL A  82     -12.018  -3.608  -8.500  1.00 29.19           C  
ANISOU  618  CA  VAL A  82     3273   4448   3370    390    -74    139       C  
ATOM    619  C   VAL A  82     -10.654  -4.024  -9.062  1.00 27.08           C  
ANISOU  619  C   VAL A  82     3059   4065   3163    328    -78    106       C  
ATOM    620  O   VAL A  82     -10.164  -5.115  -8.745  1.00 27.32           O  
ANISOU  620  O   VAL A  82     3100   4055   3224    256    -86     76       O  
ATOM    621  CB  VAL A  82     -11.953  -2.702  -7.199  1.00 29.99           C  
ANISOU  621  CB  VAL A  82     3414   4500   3479    480    -66    143       C  
ATOM    622  CG1 VAL A  82     -11.523  -3.509  -5.950  1.00 29.87           C  
ANISOU  622  CG1 VAL A  82     3419   4432   3498    422    -68    119       C  
ATOM    623  CG2 VAL A  82     -11.121  -1.389  -7.409  1.00 30.57           C  
ANISOU  623  CG2 VAL A  82     3575   4463   3574    552    -64    148       C  
ATOM    624  N   ASN A  83     -10.074  -3.196  -9.931  1.00 24.59           N  
ANISOU  624  N   ASN A  83     2778   3707   2854    354    -75    110       N  
ATOM    625  CA  ASN A  83      -8.790  -3.508 -10.541  1.00 21.77           C  
ANISOU  625  CA  ASN A  83     2456   3273   2543    295    -74     72       C  
ATOM    626  C   ASN A  83      -7.687  -3.274  -9.593  1.00 20.67           C  
ANISOU  626  C   ASN A  83     2367   3033   2451    304    -73     46       C  
ATOM    627  O   ASN A  83      -7.552  -2.170  -9.092  1.00 21.24           O  
ANISOU  627  O   ASN A  83     2487   3065   2516    360    -69     63       O  
ATOM    628  CB  ASN A  83      -8.528  -2.626 -11.736  1.00 21.54           C  
ANISOU  628  CB  ASN A  83     2451   3241   2491    302    -70     85       C  
ATOM    629  CG  ASN A  83      -9.538  -2.799 -12.781  1.00 20.75           C  
ANISOU  629  CG  ASN A  83     2300   3242   2339    292    -75    112       C  
ATOM    630  OD1 ASN A  83     -10.053  -3.899 -12.963  1.00 21.27           O  
ANISOU  630  OD1 ASN A  83     2312   3372   2396    235    -77    103       O  
ATOM    631  ND2 ASN A  83      -9.858  -1.723 -13.483  1.00 18.67           N  
ANISOU  631  ND2 ASN A  83     2063   2995   2033    342    -81    148       N  
ATOM    632  N   ILE A  84      -6.863  -4.297  -9.388  1.00 19.49           N  
ANISOU  632  N   ILE A  84     2217   2842   2345    252    -81      2       N  
ATOM    633  CA  ILE A  84      -5.761  -4.251  -8.424  1.00 17.70           C  
ANISOU  633  CA  ILE A  84     2026   2535   2163    259    -87    -26       C  
ATOM    634  C   ILE A  84      -4.402  -4.089  -9.072  1.00 16.78           C  
ANISOU  634  C   ILE A  84     1919   2384   2070    230    -82    -68       C  
ATOM    635  O   ILE A  84      -4.048  -4.845  -9.920  1.00 16.44           O  
ANISOU  635  O   ILE A  84     1850   2360   2035    193    -83   -103       O  
ATOM    636  CB  ILE A  84      -5.741  -5.537  -7.555  1.00 17.38           C  
ANISOU  636  CB  ILE A  84     1983   2472   2147    235   -108    -48       C  
ATOM    637  CG1 ILE A  84      -7.037  -5.675  -6.769  1.00 16.28           C  
ANISOU  637  CG1 ILE A  84     1832   2380   1972    244   -110    -10       C  
ATOM    638  CG2 ILE A  84      -4.529  -5.558  -6.643  1.00 16.67           C  
ANISOU  638  CG2 ILE A  84     1924   2307   2102    247   -122    -80       C  
ATOM    639  CD1 ILE A  84      -7.451  -4.407  -6.099  1.00 16.19           C  
ANISOU  639  CD1 ILE A  84     1833   2375   1942    310    -95     22       C  
ATOM    640  N   ILE A  85      -3.641  -3.096  -8.645  1.00 16.70           N  
ANISOU  640  N   ILE A  85     1948   2333   2064    242    -76    -70       N  
ATOM    641  CA  ILE A  85      -2.230  -3.034  -8.961  1.00 16.54           C  
ANISOU  641  CA  ILE A  85     1925   2298   2061    203    -73   -118       C  
ATOM    642  C   ILE A  85      -1.515  -3.528  -7.707  1.00 16.75           C  
ANISOU  642  C   ILE A  85     1952   2285   2127    218    -92   -145       C  
ATOM    643  O   ILE A  85      -1.347  -2.785  -6.772  1.00 17.42           O  
ANISOU  643  O   ILE A  85     2076   2334   2208    232    -92   -127       O  
ATOM    644  CB  ILE A  85      -1.801  -1.594  -9.274  1.00 16.46           C  
ANISOU  644  CB  ILE A  85     1968   2273   2011    183    -57   -100       C  
ATOM    645  CG1 ILE A  85      -2.674  -0.971 -10.354  1.00 16.50           C  
ANISOU  645  CG1 ILE A  85     1996   2305   1968    186    -47    -59       C  
ATOM    646  CG2 ILE A  85      -0.384  -1.554  -9.776  1.00 17.31           C  
ANISOU  646  CG2 ILE A  85     2056   2401   2118    119    -49   -154       C  
ATOM    647  CD1 ILE A  85      -2.542  -1.679 -11.683  1.00 18.58           C  
ANISOU  647  CD1 ILE A  85     2205   2625   2228    136    -41    -88       C  
ATOM    648  N   GLY A  86      -1.125  -4.790  -7.661  1.00 17.12           N  
ANISOU  648  N   GLY A  86     1965   2333   2206    218   -112   -188       N  
ATOM    649  CA  GLY A  86      -0.436  -5.318  -6.500  1.00 17.38           C  
ANISOU  649  CA  GLY A  86     2004   2327   2273    241   -139   -212       C  
ATOM    650  C   GLY A  86       1.076  -5.190  -6.588  1.00 18.37           C  
ANISOU  650  C   GLY A  86     2098   2471   2410    232   -143   -268       C  
ATOM    651  O   GLY A  86       1.607  -4.502  -7.442  1.00 18.90           O  
ANISOU  651  O   GLY A  86     2145   2582   2453    193   -118   -285       O  
ATOM    652  N   ARG A  87       1.794  -5.892  -5.725  1.00 18.97           N  
ANISOU  652  N   ARG A  87     2166   2526   2516    264   -177   -301       N  
ATOM    653  CA  ARG A  87       3.189  -5.579  -5.541  1.00 19.51           C  
ANISOU  653  CA  ARG A  87     2194   2631   2585    259   -182   -348       C  
ATOM    654  C   ARG A  87       4.067  -5.916  -6.723  1.00 20.23           C  
ANISOU  654  C   ARG A  87     2218   2800   2669    249   -171   -415       C  
ATOM    655  O   ARG A  87       5.076  -5.249  -6.929  1.00 21.55           O  
ANISOU  655  O   ARG A  87     2341   3033   2811    210   -156   -447       O  
ATOM    656  CB  ARG A  87       3.744  -6.202  -4.259  1.00 20.08           C  
ANISOU  656  CB  ARG A  87     2273   2671   2686    306   -228   -363       C  
ATOM    657  CG  ARG A  87       3.020  -5.798  -2.963  1.00 19.19           C  
ANISOU  657  CG  ARG A  87     2225   2493   2573    305   -237   -302       C  
ATOM    658  CD  ARG A  87       3.690  -6.405  -1.738  1.00 20.11           C  
ANISOU  658  CD  ARG A  87     2348   2579   2710    343   -287   -319       C  
ATOM    659  NE  ARG A  87       3.461  -7.844  -1.652  1.00 20.63           N  
ANISOU  659  NE  ARG A  87     2435   2602   2799    393   -331   -336       N  
ATOM    660  CZ  ARG A  87       4.303  -8.776  -2.091  1.00 19.29           C  
ANISOU  660  CZ  ARG A  87     2233   2451   2644    446   -362   -398       C  
ATOM    661  NH1 ARG A  87       5.458  -8.441  -2.654  1.00 20.65           N  
ANISOU  661  NH1 ARG A  87     2325   2709   2812    455   -351   -454       N  
ATOM    662  NH2 ARG A  87       3.974 -10.047  -1.981  1.00 18.59           N  
ANISOU  662  NH2 ARG A  87     2198   2299   2565    489   -405   -408       N  
ATOM    663  N   ASN A  88       3.722  -6.928  -7.509  1.00 20.20           N  
ANISOU  663  N   ASN A  88     2203   2794   2676    274   -176   -441       N  
ATOM    664  CA  ASN A  88       4.570  -7.255  -8.673  1.00 20.43           C  
ANISOU  664  CA  ASN A  88     2164   2904   2692    269   -160   -514       C  
ATOM    665  C   ASN A  88       4.776  -6.011  -9.517  1.00 20.20           C  
ANISOU  665  C   ASN A  88     2114   2941   2618    182   -114   -504       C  
ATOM    666  O   ASN A  88       5.870  -5.801 -10.064  1.00 21.34           O  
ANISOU  666  O   ASN A  88     2191   3179   2738    151    -99   -564       O  
ATOM    667  CB  ASN A  88       4.028  -8.414  -9.526  1.00 20.37           C  
ANISOU  667  CB  ASN A  88     2168   2877   2692    295   -165   -539       C  
ATOM    668  CG  ASN A  88       2.773  -8.037 -10.309  1.00 21.45           C  
ANISOU  668  CG  ASN A  88     2339   3006   2806    236   -135   -481       C  
ATOM    669  OD1 ASN A  88       1.860  -7.374  -9.789  1.00 22.94           O  
ANISOU  669  OD1 ASN A  88     2569   3157   2987    216   -130   -408       O  
ATOM    670  ND2 ASN A  88       2.717  -8.462 -11.562  1.00 21.03           N  
ANISOU  670  ND2 ASN A  88     2264   2992   2735    214   -115   -516       N  
ATOM    671  N   MET A  89       3.736  -5.172  -9.572  1.00 19.03           N  
ANISOU  671  N   MET A  89     2027   2750   2451    143    -96   -429       N  
ATOM    672  CA  MET A  89       3.736  -3.982 -10.401  1.00 18.03           C  
ANISOU  672  CA  MET A  89     1916   2661   2273     63    -60   -407       C  
ATOM    673  C   MET A  89       4.072  -2.787  -9.576  1.00 17.29           C  
ANISOU  673  C   MET A  89     1868   2546   2153     27    -57   -374       C  
ATOM    674  O   MET A  89       4.636  -1.835 -10.068  1.00 17.75           O  
ANISOU  674  O   MET A  89     1939   2645   2159    -52    -35   -379       O  
ATOM    675  CB  MET A  89       2.392  -3.790 -11.078  1.00 18.06           C  
ANISOU  675  CB  MET A  89     1966   2634   2262     57    -49   -348       C  
ATOM    676  CG  MET A  89       2.149  -4.710 -12.268  1.00 18.43           C  
ANISOU  676  CG  MET A  89     1972   2719   2308     52    -41   -382       C  
ATOM    677  SD  MET A  89       3.196  -4.281 -13.669  1.00 20.87           S  
ANISOU  677  SD  MET A  89     2231   3129   2567    -33     -7   -440       S  
ATOM    678  CE  MET A  89       2.126  -4.655 -15.036  1.00 16.60           C  
ANISOU  678  CE  MET A  89     1700   2601   2004    -57      6   -418       C  
ATOM    679  N   LEU A  90       3.777  -2.827  -8.297  1.00 16.69           N  
ANISOU  679  N   LEU A  90     1827   2407   2106     75    -80   -344       N  
ATOM    680  CA  LEU A  90       4.198  -1.704  -7.485  1.00 16.77           C  
ANISOU  680  CA  LEU A  90     1887   2396   2085     35    -76   -320       C  
ATOM    681  C   LEU A  90       5.715  -1.582  -7.467  1.00 17.88           C  
ANISOU  681  C   LEU A  90     1965   2625   2204    -19    -76   -383       C  
ATOM    682  O   LEU A  90       6.237  -0.532  -7.733  1.00 18.34           O  
ANISOU  682  O   LEU A  90     2054   2713   2201   -110    -55   -380       O  
ATOM    683  CB  LEU A  90       3.522  -1.692  -6.108  1.00 16.34           C  
ANISOU  683  CB  LEU A  90     1888   2261   2059     91    -97   -275       C  
ATOM    684  CG  LEU A  90       2.046  -1.236  -6.254  1.00 14.83           C  
ANISOU  684  CG  LEU A  90     1765   2014   1856    121    -84   -208       C  
ATOM    685  CD1 LEU A  90       1.253  -1.462  -5.024  1.00 15.35           C  
ANISOU  685  CD1 LEU A  90     1862   2023   1946    179   -100   -173       C  
ATOM    686  CD2 LEU A  90       1.910   0.198  -6.644  1.00 13.26           C  
ANISOU  686  CD2 LEU A  90     1648   1793   1595     76    -62   -172       C  
ATOM    687  N   THR A  91       6.430  -2.677  -7.251  1.00 19.32           N  
ANISOU  687  N   THR A  91     2060   2857   2423     32   -100   -444       N  
ATOM    688  CA  THR A  91       7.896  -2.654  -7.328  1.00 20.68           C  
ANISOU  688  CA  THR A  91     2143   3147   2566     -6   -101   -515       C  
ATOM    689  C   THR A  91       8.420  -2.163  -8.650  1.00 21.95           C  
ANISOU  689  C   THR A  91     2264   3408   2667   -100    -62   -551       C  
ATOM    690  O   THR A  91       9.478  -1.545  -8.671  1.00 23.32           O  
ANISOU  690  O   THR A  91     2396   3680   2782   -187    -50   -586       O  
ATOM    691  CB  THR A  91       8.508  -4.015  -7.134  1.00 20.44           C  
ANISOU  691  CB  THR A  91     2022   3161   2581     92   -136   -583       C  
ATOM    692  OG1 THR A  91       7.980  -4.889  -8.122  1.00 21.89           O  
ANISOU  692  OG1 THR A  91     2193   3334   2788    138   -130   -604       O  
ATOM    693  CG2 THR A  91       8.150  -4.547  -5.815  1.00 20.17           C  
ANISOU  693  CG2 THR A  91     2030   3036   2595    172   -180   -552       C  
ATOM    694  N   GLN A  92       7.714  -2.447  -9.753  1.00 22.75           N  
ANISOU  694  N   GLN A  92     2376   3495   2773    -96    -44   -545       N  
ATOM    695  CA  GLN A  92       8.190  -2.010 -11.088  1.00 24.13           C  
ANISOU  695  CA  GLN A  92     2516   3767   2883   -195     -7   -580       C  
ATOM    696  C   GLN A  92       8.125  -0.487 -11.243  1.00 24.61           C  
ANISOU  696  C   GLN A  92     2675   3807   2866   -322     14   -525       C  
ATOM    697  O   GLN A  92       9.036   0.123 -11.828  1.00 26.12           O  
ANISOU  697  O   GLN A  92     2839   4103   2982   -441     38   -562       O  
ATOM    698  CB  GLN A  92       7.478  -2.705 -12.254  1.00 23.61           C  
ANISOU  698  CB  GLN A  92     2440   3695   2835   -166      5   -588       C  
ATOM    699  CG  GLN A  92       7.532  -4.248 -12.265  1.00 25.56           C  
ANISOU  699  CG  GLN A  92     2617   3950   3144    -50    -16   -647       C  
ATOM    700  CD  GLN A  92       8.943  -4.871 -12.262  1.00 28.13           C  
ANISOU  700  CD  GLN A  92     2822   4403   3463    -18    -22   -751       C  
ATOM    701  OE1 GLN A  92       9.922  -4.293 -12.749  1.00 27.50           O  
ANISOU  701  OE1 GLN A  92     2675   4453   3321   -105      3   -799       O  
ATOM    702  NE2 GLN A  92       9.034  -6.073 -11.698  1.00 29.80           N  
ANISOU  702  NE2 GLN A  92     3009   4582   3731    108    -61   -787       N  
ATOM    703  N   LEU A  93       7.082   0.128 -10.683  1.00 23.76           N  
ANISOU  703  N   LEU A  93     2688   3571   2769   -297      5   -442       N  
ATOM    704  CA  LEU A  93       6.946   1.585 -10.714  1.00 23.49           C  
ANISOU  704  CA  LEU A  93     2780   3487   2658   -394     18   -387       C  
ATOM    705  C   LEU A  93       7.917   2.314  -9.795  1.00 24.03           C  
ANISOU  705  C   LEU A  93     2871   3579   2680   -472     15   -397       C  
ATOM    706  O   LEU A  93       7.938   3.550  -9.751  1.00 24.65           O  
ANISOU  706  O   LEU A  93     3074   3609   2681   -568     23   -356       O  
ATOM    707  CB  LEU A  93       5.510   1.989 -10.409  1.00 22.33           C  
ANISOU  707  CB  LEU A  93     2750   3203   2532   -320      7   -302       C  
ATOM    708  CG  LEU A  93       4.539   1.356 -11.389  1.00 21.52           C  
ANISOU  708  CG  LEU A  93     2623   3096   2458   -264     10   -289       C  
ATOM    709  CD1 LEU A  93       3.177   1.376 -10.787  1.00 22.23           C  
ANISOU  709  CD1 LEU A  93     2775   3087   2583   -161     -5   -223       C  
ATOM    710  CD2 LEU A  93       4.541   2.055 -12.725  1.00 20.49           C  
ANISOU  710  CD2 LEU A  93     2539   2993   2252   -358     29   -278       C  
ATOM    711  N   GLY A  94       8.740   1.552  -9.086  1.00 24.20           N  
ANISOU  711  N   GLY A  94     2780   3674   2739   -434      0   -453       N  
ATOM    712  CA  GLY A  94       9.676   2.136  -8.119  1.00 25.58           C  
ANISOU  712  CA  GLY A  94     2959   3888   2871   -505     -7   -465       C  
ATOM    713  C   GLY A  94       8.963   2.649  -6.877  1.00 25.50           C  
ANISOU  713  C   GLY A  94     3070   3737   2882   -460    -24   -397       C  
ATOM    714  O   GLY A  94       9.381   3.640  -6.244  1.00 26.14           O  
ANISOU  714  O   GLY A  94     3234   3798   2898   -552    -22   -377       O  
ATOM    715  N   CYS A  95       7.896   1.935  -6.524  1.00 24.77           N  
ANISOU  715  N   CYS A  95     2985   3553   2872   -326    -41   -365       N  
ATOM    716  CA  CYS A  95       6.967   2.346  -5.508  1.00 23.91           C  
ANISOU  716  CA  CYS A  95     2985   3315   2783   -268    -51   -301       C  
ATOM    717  C   CYS A  95       7.352   1.834  -4.152  1.00 24.09           C  
ANISOU  717  C   CYS A  95     2967   3336   2847   -221    -79   -314       C  
ATOM    718  O   CYS A  95       7.657   0.652  -3.957  1.00 24.15           O  
ANISOU  718  O   CYS A  95     2868   3392   2914   -150   -104   -355       O  
ATOM    719  CB  CYS A  95       5.600   1.832  -5.850  1.00 23.34           C  
ANISOU  719  CB  CYS A  95     2929   3173   2763   -164    -53   -264       C  
ATOM    720  SG  CYS A  95       4.332   2.759  -5.140  1.00 23.54           S  
ANISOU  720  SG  CYS A  95     3102   3066   2774   -114    -51   -186       S  
ATOM    721  N   THR A  96       7.326   2.762  -3.207  1.00 24.56           N  
ANISOU  721  N   THR A  96     3129   3330   2870   -259    -79   -278       N  
ATOM    722  CA  THR A  96       7.600   2.482  -1.818  1.00 23.88           C  
ANISOU  722  CA  THR A  96     3033   3229   2812   -228   -105   -279       C  
ATOM    723  C   THR A  96       6.454   3.033  -0.985  1.00 23.09           C  
ANISOU  723  C   THR A  96     3059   2996   2717   -177   -102   -217       C  
ATOM    724  O   THR A  96       5.752   3.960  -1.417  1.00 22.37           O  
ANISOU  724  O   THR A  96     3080   2835   2583   -189    -78   -178       O  
ATOM    725  CB  THR A  96       8.905   3.166  -1.373  1.00 25.17           C  
ANISOU  725  CB  THR A  96     3191   3467   2903   -351   -106   -307       C  
ATOM    726  OG1 THR A  96       8.841   4.580  -1.668  1.00 25.60           O  
ANISOU  726  OG1 THR A  96     3389   3471   2867   -463    -78   -274       O  
ATOM    727  CG2 THR A  96      10.111   2.516  -2.077  1.00 25.24           C  
ANISOU  727  CG2 THR A  96     3043   3642   2904   -388   -112   -381       C  
ATOM    728  N   LEU A  97       6.258   2.399   0.176  1.00 22.43           N  
ANISOU  728  N   LEU A  97     2954   2884   2682   -111   -127   -211       N  
ATOM    729  CA  LEU A  97       5.544   2.941   1.320  1.00 21.64           C  
ANISOU  729  CA  LEU A  97     2958   2688   2574    -84   -125   -168       C  
ATOM    730  C   LEU A  97       6.555   3.692   2.161  1.00 22.71           C  
ANISOU  730  C   LEU A  97     3138   2835   2654   -180   -130   -177       C  
ATOM    731  O   LEU A  97       7.706   3.264   2.275  1.00 23.92           O  
ANISOU  731  O   LEU A  97     3197   3084   2805   -227   -151   -218       O  
ATOM    732  CB  LEU A  97       4.999   1.807   2.166  1.00 20.76           C  
ANISOU  732  CB  LEU A  97     2795   2558   2531      6   -154   -163       C  
ATOM    733  CG  LEU A  97       3.734   1.082   1.760  1.00 18.64           C  
ANISOU  733  CG  LEU A  97     2510   2264   2308     95   -151   -142       C  
ATOM    734  CD1 LEU A  97       3.590  -0.050   2.683  1.00 17.59           C  
ANISOU  734  CD1 LEU A  97     2334   2124   2224    143   -188   -146       C  
ATOM    735  CD2 LEU A  97       2.567   1.999   1.912  1.00 18.86           C  
ANISOU  735  CD2 LEU A  97     2638   2222   2303    126   -122    -97       C  
ATOM    736  N   ASN A  98       6.133   4.786   2.777  1.00 23.07           N  
ANISOU  736  N   ASN A  98     3325   2790   2648   -205   -112   -142       N  
ATOM    737  CA  ASN A  98       7.054   5.691   3.451  1.00 24.00           C  
ANISOU  737  CA  ASN A  98     3516   2910   2691   -322   -110   -147       C  
ATOM    738  C   ASN A  98       6.383   6.342   4.657  1.00 24.74           C  
ANISOU  738  C   ASN A  98     3742   2893   2764   -294   -103   -112       C  
ATOM    739  O   ASN A  98       5.258   6.849   4.541  1.00 25.35           O  
ANISOU  739  O   ASN A  98     3919   2877   2833   -222    -82    -81       O  
ATOM    740  CB  ASN A  98       7.471   6.800   2.483  1.00 24.50           C  
ANISOU  740  CB  ASN A  98     3670   2973   2663   -435    -85   -147       C  
ATOM    741  CG  ASN A  98       8.518   6.366   1.492  1.00 23.82           C  
ANISOU  741  CG  ASN A  98     3455   3027   2567   -512    -88   -193       C  
ATOM    742  OD1 ASN A  98       8.226   6.066   0.346  1.00 22.57           O  
ANISOU  742  OD1 ASN A  98     3253   2895   2428   -484    -78   -200       O  
ATOM    743  ND2 ASN A  98       9.755   6.374   1.923  1.00 25.53           N  
ANISOU  743  ND2 ASN A  98     3608   3348   2743   -615   -101   -229       N  
ATOM    744  N   PHE A  99       7.059   6.336   5.804  1.00 25.29           N  
ANISOU  744  N   PHE A  99     3809   2980   2819   -347   -121   -121       N  
ATOM    745  CA  PHE A  99       6.598   7.052   7.003  1.00 25.64           C  
ANISOU  745  CA  PHE A  99     3987   2925   2827   -345   -111    -96       C  
ATOM    746  C   PHE A  99       7.717   7.358   7.988  1.00 26.70           C  
ANISOU  746  C   PHE A  99     4135   3098   2910   -463   -128   -110       C  
ATOM    747  O   PHE A  99       7.507   7.656   9.161  1.00 27.03           O  
ANISOU  747  O   PHE A  99     4255   3081   2934   -465   -128    -96       O  
ATOM    748  CB  PHE A  99       5.427   6.347   7.708  1.00 24.87           C  
ANISOU  748  CB  PHE A  99     3867   2781   2798   -212   -115    -77       C  
ATOM    749  CG  PHE A  99       5.695   4.928   8.135  1.00 23.38           C  
ANISOU  749  CG  PHE A  99     3530   2665   2687   -172   -156    -92       C  
ATOM    750  CD1 PHE A  99       5.631   3.881   7.221  1.00 22.13           C  
ANISOU  750  CD1 PHE A  99     3249   2566   2591   -116   -172   -107       C  
ATOM    751  CD2 PHE A  99       5.920   4.632   9.472  1.00 24.02           C  
ANISOU  751  CD2 PHE A  99     3611   2741   2773   -184   -181    -89       C  
ATOM    752  CE1 PHE A  99       5.844   2.561   7.621  1.00 22.57           C  
ANISOU  752  CE1 PHE A  99     3197   2667   2709    -70   -216   -121       C  
ATOM    753  CE2 PHE A  99       6.136   3.307   9.894  1.00 25.10           C  
ANISOU  753  CE2 PHE A  99     3634   2928   2973   -141   -228    -99       C  
ATOM    754  CZ  PHE A  99       6.100   2.271   8.963  1.00 23.96           C  
ANISOU  754  CZ  PHE A  99     3382   2834   2888    -80   -247   -115       C  
ATOM    755  OXT PHE A  99       8.882   7.323   7.614  1.00 28.03           O  
ANISOU  755  OXT PHE A  99     4231   3371   3045   -566   -140   -138       O  
TER     756      PHE A  99                                                      
MASTER      300    0    0    1    8    0    0    6  755    1    0    8          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.