CNRS Nantes University UFIP UFIP
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***  1fd3  ***

elNémo ID: 19020800324465367

Job options:

ID        	=	 19020800324465367
JOBID     	=	 1fd3
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 1fd3

HEADER    ANTIMICROBIAL PROTEIN                   19-JUL-00   1FD3              
TITLE     HUMAN BETA-DEFENSIN 2                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-DEFENSIN 2;                                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HBD-2, SKIN-ANTIMICROBIAL PEPTIDE 1;                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED.              
SOURCE   4 THE SEQUENCE OF THIS PEPTIDE OCCURS NATURALLY IN HUMANS              
SOURCE   5 (HOMO SAPIENS)                                                       
KEYWDS    DEFENSIN, HUMAN BETA-DEFENSIN 2, BETA-DEFENSIN,                       
KEYWDS   2 ANTIMICROBIAL PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.M.HOOVER,J.LUBKOWSKI                                                
REVDAT   3   24-FEB-09 1FD3    1       VERSN                                    
REVDAT   2   01-APR-03 1FD3    1       JRNL                                     
REVDAT   1   01-NOV-00 1FD3    0                                                
JRNL        AUTH   D.M.HOOVER,K.R.RAJASHANKAR,R.BLUMENTHAL,A.PURI,              
JRNL        AUTH 2 J.J.OPPENHEIM,O.CHERTOV,J.LUBKOWSKI                          
JRNL        TITL   THE STRUCTURE OF HUMAN BETA-DEFENSIN-2 SHOWS                 
JRNL        TITL 2 EVIDENCE OF HIGHER ORDER OLIGOMERIZATION.                    
JRNL        REF    J.BIOL.CHEM.                  V. 275 32911 2000              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10906336                                                     
JRNL        DOI    10.1074/JBC.M006098200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.1                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.160                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.163                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.236                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 11.000                 
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 319                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 28662                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.159                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.161                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.234                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 11.000                 
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 304                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 2734                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1215                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 5                                             
REMARK   3   SOLVENT ATOMS      : 194                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1411.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1292.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 1                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 1274                    
REMARK   3   NUMBER OF RESTRAINTS                     : 1449                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.010                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.030                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.060                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.060                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.040                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.060                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FD3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011491.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-OCT-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI CRYSTAL                         
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28662                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.03100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 55.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 6.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELX, MLPHARE, DM, ARP                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRIS HCL, LITHIUM              
REMARK 280  SULFATE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  298.15K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       25.02500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.95500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.02500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.95500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER.                          
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 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO B    41                                                      
REMARK 465     PRO C    41                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    HIS A  16   CB  -  CG  -  CD2 ANGL. DEV. =  16.9 DEGREES          
REMARK 500    HIS A  16   ND1 -  CG  -  CD2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    HIS A  16   CG  -  ND1 -  CE1 ANGL. DEV. =  12.8 DEGREES          
REMARK 500    HIS A  16   ND1 -  CE1 -  NE2 ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    VAL A  18   C   -  N   -  CA  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    PHE A  19   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG B  23   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG C  22   CD  -  NE  -  CZ  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ARG C  22   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG C  23   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  18      -46.40   -134.82                                   
REMARK 500    ARG A  23      -11.63     83.00                                   
REMARK 500    VAL B  18      -41.10   -141.43                                   
REMARK 500    CYS B  30       40.73   -106.30                                   
REMARK 500    VAL C  18      -46.24     67.81                                   
REMARK 500    ARG C  23      -28.97     95.87                                   
REMARK 500    VAL D  18      -39.77   -140.31                                   
REMARK 500    ARG D  23        8.94     80.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B  82        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH D 238        DISTANCE =  6.51 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 195                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FD4   RELATED DB: PDB                                   
REMARK 900 HUMAN BETA-DEFENSIN 2, MONOCLINIC                                    
DBREF  1FD3 A    1    41  UNP    O15263   BD02_HUMAN      24     64             
DBREF  1FD3 B    1    41  UNP    O15263   BD02_HUMAN      24     64             
DBREF  1FD3 C    1    41  UNP    O15263   BD02_HUMAN      24     64             
DBREF  1FD3 D    1    41  UNP    O15263   BD02_HUMAN      24     64             
SEQRES   1 A   41  GLY ILE GLY ASP PRO VAL THR CYS LEU LYS SER GLY ALA          
SEQRES   2 A   41  ILE CYS HIS PRO VAL PHE CYS PRO ARG ARG TYR LYS GLN          
SEQRES   3 A   41  ILE GLY THR CYS GLY LEU PRO GLY THR LYS CYS CYS LYS          
SEQRES   4 A   41  LYS PRO                                                      
SEQRES   1 B   41  GLY ILE GLY ASP PRO VAL THR CYS LEU LYS SER GLY ALA          
SEQRES   2 B   41  ILE CYS HIS PRO VAL PHE CYS PRO ARG ARG TYR LYS GLN          
SEQRES   3 B   41  ILE GLY THR CYS GLY LEU PRO GLY THR LYS CYS CYS LYS          
SEQRES   4 B   41  LYS PRO                                                      
SEQRES   1 C   41  GLY ILE GLY ASP PRO VAL THR CYS LEU LYS SER GLY ALA          
SEQRES   2 C   41  ILE CYS HIS PRO VAL PHE CYS PRO ARG ARG TYR LYS GLN          
SEQRES   3 C   41  ILE GLY THR CYS GLY LEU PRO GLY THR LYS CYS CYS LYS          
SEQRES   4 C   41  LYS PRO                                                      
SEQRES   1 D   41  GLY ILE GLY ASP PRO VAL THR CYS LEU LYS SER GLY ALA          
SEQRES   2 D   41  ILE CYS HIS PRO VAL PHE CYS PRO ARG ARG TYR LYS GLN          
SEQRES   3 D   41  ILE GLY THR CYS GLY LEU PRO GLY THR LYS CYS CYS LYS          
SEQRES   4 D   41  LYS PRO                                                      
HET    SO4  D 195       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *194(H2 O)                                                    
HELIX    1   1 ASP A    4  SER A   11  1                                   8    
HELIX    2   2 ASP B    4  SER B   11  1                                   8    
HELIX    3   3 ASP C    4  SER C   11  1                                   8    
HELIX    4   4 ASP D    4  SER D   11  1                                   8    
SHEET    1   A 3 ILE A  14  HIS A  16  0                                        
SHEET    2   A 3 LYS A  36  LYS A  39 -1  N  LYS A  36   O  HIS A  16           
SHEET    3   A 3 LYS A  25  GLY A  28 -1  N  LYS A  25   O  LYS A  39           
SHEET    1   B 3 ILE B  14  HIS B  16  0                                        
SHEET    2   B 3 LYS B  36  LYS B  39 -1  N  LYS B  36   O  HIS B  16           
SHEET    3   B 3 LYS B  25  GLY B  28 -1  O  LYS B  25   N  LYS B  39           
SHEET    1   C 3 ILE C  14  PRO C  17  0                                        
SHEET    2   C 3 THR C  35  LYS C  39 -1  N  LYS C  36   O  HIS C  16           
SHEET    3   C 3 LYS C  25  THR C  29 -1  N  LYS C  25   O  LYS C  39           
SHEET    1   D 4 ILE D   2  GLY D   3  0                                        
SHEET    2   D 4 LYS D  25  THR D  29  1  O  ILE D  27   N  ILE D   2           
SHEET    3   D 4 LYS D  36  LYS D  39 -1  O  CYS D  37   N  ILE D  27           
SHEET    4   D 4 ILE D  14  HIS D  16 -1  O  ILE D  14   N  CYS D  38           
SSBOND   1 CYS A    8    CYS A   37                          1555   1555  2.06  
SSBOND   2 CYS A   15    CYS A   30                          1555   1555  2.07  
SSBOND   3 CYS A   20    CYS A   38                          1555   1555  2.07  
SSBOND   4 CYS B    8    CYS B   37                          1555   1555  2.07  
SSBOND   5 CYS B   15    CYS B   30                          1555   1555  2.05  
SSBOND   6 CYS B   20    CYS B   38                          1555   1555  2.08  
SSBOND   7 CYS C    8    CYS C   37                          1555   1555  2.05  
SSBOND   8 CYS C   15    CYS C   30                          1555   1555  2.05  
SSBOND   9 CYS C   20    CYS C   38                          1555   1555  2.03  
SSBOND  10 CYS D    8    CYS D   37                          1555   1555  2.08  
SSBOND  11 CYS D   15    CYS D   30                          1555   1555  2.02  
SSBOND  12 CYS D   20    CYS D   38                          1555   1555  2.03  
SITE     1 AC1  9 HOH B  83  LYS D  10  PHE D  19  CYS D  20                    
SITE     2 AC1  9 LYS D  36  HOH D 216  HOH D 223  HOH D 225                    
SITE     3 AC1  9 HOH D 231                                                     
CRYST1   50.050  103.910   28.270  90.00  90.00  90.00 P 21 21 2    16          
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      0.019980  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009624  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.035373        0.00000                         
ATOM      1  N   GLY A   1       4.131  26.056   9.568  1.00 40.99           N  
ANISOU    1  N   GLY A   1     4360   4138   7076   -721  -1108  -2288       N  
ATOM      2  CA  GLY A   1       5.254  26.953   9.671  1.00 31.07           C  
ANISOU    2  CA  GLY A   1     4044   2465   5294    103  -2499   -504       C  
ATOM      3  C   GLY A   1       4.932  28.261  10.360  1.00 29.86           C  
ANISOU    3  C   GLY A   1     4338   2192   4816    261  -1915    128       C  
ATOM      4  O   GLY A   1       3.764  28.568  10.645  1.00 34.58           O  
ANISOU    4  O   GLY A   1     4347   2488   6305    -85  -1503   -431       O  
ATOM      5  N   ILE A   2       6.000  29.026  10.610  1.00 24.89           N  
ANISOU    5  N   ILE A   2     4174   2194   3089    361  -1430   -291       N  
ATOM      6  CA  ILE A   2       5.827  30.381  11.127  1.00 20.01           C  
ANISOU    6  CA  ILE A   2     2659   2235   2709    536   -370    -86       C  
ATOM      7  C   ILE A   2       6.541  31.362  10.209  1.00 20.79           C  
ANISOU    7  C   ILE A   2     2499   2573   2826     51   -940     37       C  
ATOM      8  O   ILE A   2       7.762  31.306  10.001  1.00 19.60           O  
ANISOU    8  O   ILE A   2     2650   1738   3060    223   -528   -272       O  
ATOM      9  CB  ILE A   2       6.371  30.466  12.561  1.00 18.37           C  
ANISOU    9  CB  ILE A   2     2400   1677   2902    196   -613    -53       C  
ATOM     10  CG1 ILE A   2       5.732  29.495  13.544  1.00 18.89           C  
ANISOU   10  CG1 ILE A   2     2355   2057   2767    214   -456    -59       C  
ATOM     11  CG2 ILE A   2       6.282  31.911  13.041  1.00 19.37           C  
ANISOU   11  CG2 ILE A   2     2232   1887   3240    365     31   -334       C  
ATOM     12  CD1 ILE A   2       6.401  29.351  14.891  1.00 19.86           C  
ANISOU   12  CD1 ILE A   2     2510   2453   2584    111   -364   -199       C  
ATOM     13  N   GLY A   3       5.744  32.252   9.632  1.00 20.26           N  
ANISOU   13  N   GLY A   3     2717   2124   2856    267   -634    -66       N  
ATOM     14  CA  GLY A   3       6.182  33.202   8.629  1.00 19.08           C  
ANISOU   14  CA  GLY A   3     1989   2348   2914    358   -266    -98       C  
ATOM     15  C   GLY A   3       5.497  34.545   8.767  1.00 17.24           C  
ANISOU   15  C   GLY A   3     2095   2087   2367    146   -486   -142       C  
ATOM     16  O   GLY A   3       5.455  35.279   7.787  1.00 21.32           O  
ANISOU   16  O   GLY A   3     3306   2537   2257    629   -283   -106       O  
ATOM     17  N   ASP A   4       4.977  34.895   9.950  1.00 16.63           N  
ANISOU   17  N   ASP A   4     2061   2001   2257    159   -541    -53       N  
ATOM     18  CA  ASP A   4       4.377  36.213  10.165  1.00 16.39           C  
ANISOU   18  CA  ASP A   4     1798   2081   2350    166   -407     78       C  
ATOM     19  C   ASP A   4       4.504  36.570  11.649  1.00 16.45           C  
ANISOU   19  C   ASP A   4     2064   1830   2357    457   -369     73       C  
ATOM     20  O   ASP A   4       4.673  35.693  12.506  1.00 15.59           O  
ANISOU   20  O   ASP A   4     1769   1750   2405    340   -507     48       O  
ATOM     21  CB  ASP A   4       2.926  36.269   9.658  1.00 18.51           C  
ANISOU   21  CB  ASP A   4     1848   2362   2822    140   -567   -115       C  
ATOM     22  CG  ASP A   4       1.972  35.620  10.642  1.00 17.09           C  
ANISOU   22  CG  ASP A   4     1652   2341   2500   -140   -984   -139       C  
ATOM     23  OD1 ASP A   4       1.685  34.428  10.397  1.00 20.17           O  
ANISOU   23  OD1 ASP A   4     2205   2299   3161   -104   -784   -177       O  
ATOM     24  OD2 ASP A   4       1.579  36.221  11.667  1.00 18.27           O  
ANISOU   24  OD2 ASP A   4     1843   2375   2724     28   -659    -51       O  
ATOM     25  N   PRO A   5       4.424  37.853  12.030  1.00 16.19           N  
ANISOU   25  N   PRO A   5     1992   1719   2441    131   -426    198       N  
ATOM     26  CA  PRO A   5       4.642  38.225  13.422  1.00 15.82           C  
ANISOU   26  CA  PRO A   5     1801   1756   2456    643   -277     41       C  
ATOM     27  C   PRO A   5       3.544  37.805  14.402  1.00 15.69           C  
ANISOU   27  C   PRO A   5     1709   1781   2471    722   -330     70       C  
ATOM     28  O   PRO A   5       3.863  37.584  15.581  1.00 15.41           O  
ANISOU   28  O   PRO A   5     1596   1734   2524    359   -372    176       O  
ATOM     29  CB  PRO A   5       4.711  39.755  13.396  1.00 17.51           C  
ANISOU   29  CB  PRO A   5     1641   1804   3206    274   -450   -174       C  
ATOM     30  CG  PRO A   5       4.756  40.135  11.957  1.00 21.21           C  
ANISOU   30  CG  PRO A   5     2863   1721   3476     88   -733    369       C  
ATOM     31  CD  PRO A   5       4.193  39.027  11.134  1.00 16.81           C  
ANISOU   31  CD  PRO A   5     1678   1897   2814    176   -477    468       C  
ATOM     32  N   VAL A   6       2.302  37.722  13.955  1.00 16.04           N  
ANISOU   32  N   VAL A   6     1763   2017   2314    702   -300    168       N  
ATOM     33  CA  VAL A   6       1.188  37.347  14.816  1.00 16.21           C  
ANISOU   33  CA  VAL A   6     1781   1705   2671    422   -345    139       C  
ATOM     34  C   VAL A   6       1.305  35.881  15.190  1.00 16.58           C  
ANISOU   34  C   VAL A   6     1740   1778   2782    654   -250    118       C  
ATOM     35  O   VAL A   6       1.269  35.553  16.387  1.00 16.92           O  
ANISOU   35  O   VAL A   6     1879   1757   2795    286   -409    193       O  
ATOM     36  CB  VAL A   6      -0.163  37.729  14.173  1.00 16.44           C  
ANISOU   36  CB  VAL A   6     1779   1821   2649    442   -391    221       C  
ATOM     37  CG1 VAL A   6      -1.327  37.054  14.865  1.00 19.62           C  
ANISOU   37  CG1 VAL A   6     1788   2261   3408    592    -86    547       C  
ATOM     38  CG2 VAL A   6      -0.345  39.250  14.182  1.00 20.15           C  
ANISOU   38  CG2 VAL A   6     1977   1885   3796    497   -830    328       C  
ATOM     39  N   THR A   7       1.514  34.990  14.227  1.00 16.38           N  
ANISOU   39  N   THR A   7     1756   1646   2824    186   -359     71       N  
ATOM     40  CA  THR A   7       1.759  33.589  14.520  1.00 17.48           C  
ANISOU   40  CA  THR A   7     1770   1505   3366     63   -564    -39       C  
ATOM     41  C   THR A   7       2.923  33.420  15.497  1.00 17.35           C  
ANISOU   41  C   THR A   7     1732   1666   3193    194   -402    188       C  
ATOM     42  O   THR A   7       2.866  32.676  16.477  1.00 17.42           O  
ANISOU   42  O   THR A   7     2087   1541   2993    247   -257     -8       O  
ATOM     43  CB  THR A   7       2.016  32.787  13.222  1.00 17.49           C  
ANISOU   43  CB  THR A   7     1721   1607   3320     92   -453     10       C  
ATOM     44  OG1 THR A   7       0.916  33.028  12.336  1.00 21.09           O  
ANISOU   44  OG1 THR A   7     2541   1986   3484    323   -931    -42       O  
ATOM     45  CG2 THR A   7       2.140  31.299  13.521  1.00 19.20           C  
ANISOU   45  CG2 THR A   7     2072   1634   3589    366   -493   -180       C  
ATOM     46  N   CYS A   8       4.025  34.159  15.249  1.00 17.06           N  
ANISOU   46  N   CYS A   8     1861   1449   3171     20   -702     36       N  
ATOM     47  CA  CYS A   8       5.201  34.065  16.095  1.00 14.91           C  
ANISOU   47  CA  CYS A   8     1852   1133   2681    218   -420   -140       C  
ATOM     48  C   CYS A   8       4.890  34.478  17.539  1.00 16.11           C  
ANISOU   48  C   CYS A   8     2074   1424   2624    298   -157    106       C  
ATOM     49  O   CYS A   8       5.146  33.713  18.476  1.00 16.69           O  
ANISOU   49  O   CYS A   8     2116   1428   2798     73   -484    141       O  
ATOM     50  CB  CYS A   8       6.314  34.923  15.506  1.00 14.54           C  
ANISOU   50  CB  CYS A   8     1761   1344   2420    182   -365   -210       C  
ATOM     51  SG  CYS A   8       7.888  34.925  16.412  1.00 15.12           S  
ANISOU   51  SG  CYS A   8     1786   1503   2456    342   -374     -5       S  
ATOM     52  N   LEU A   9       4.365  35.676  17.713  1.00 15.52           N  
ANISOU   52  N   LEU A   9     2153   1395   2349    243   -117     45       N  
ATOM     53  CA  LEU A   9       4.150  36.200  19.050  1.00 14.91           C  
ANISOU   53  CA  LEU A   9     1335   2018   2312    448   -270     -7       C  
ATOM     54  C   LEU A   9       3.102  35.421  19.834  1.00 17.27           C  
ANISOU   54  C   LEU A   9     1587   2403   2571    290   -184    226       C  
ATOM     55  O   LEU A   9       3.195  35.264  21.045  1.00 20.02           O  
ANISOU   55  O   LEU A   9     2399   2622   2586   -113   -103    245       O  
ATOM     56  CB  LEU A   9       3.770  37.687  18.975  1.00 16.63           C  
ANISOU   56  CB  LEU A   9     2114   1869   2334    278   -386   -392       C  
ATOM     57  CG  LEU A   9       4.903  38.649  18.580  1.00 16.77           C  
ANISOU   57  CG  LEU A   9     1998   1930   2445    442   -502    166       C  
ATOM     58  CD1 LEU A   9       4.339  39.973  18.072  1.00 17.30           C  
ANISOU   58  CD1 LEU A   9     2028   1820   2727    514   -787   -146       C  
ATOM     59  CD2 LEU A   9       5.879  38.886  19.725  1.00 17.89           C  
ANISOU   59  CD2 LEU A   9     2222   1608   2967    306   -850    172       C  
ATOM     60  N   LYS A  10       2.073  34.936  19.144  1.00 18.74           N  
ANISOU   60  N   LYS A  10     1850   2299   2970      4   -284    237       N  
ATOM     61  CA  LYS A  10       1.038  34.142  19.797  1.00 22.21           C  
ANISOU   61  CA  LYS A  10     2047   2529   3864    -96    228    120       C  
ATOM     62  C   LYS A  10       1.659  32.915  20.482  1.00 24.67           C  
ANISOU   62  C   LYS A  10     2327   3220   3829   -245    447   1001       C  
ATOM     63  O   LYS A  10       1.145  32.564  21.544  1.00 27.64           O  
ANISOU   63  O   LYS A  10     2503   4415   3586  -1143    177    886       O  
ATOM     64  CB  LYS A  10      -0.068  33.700  18.837  1.00 28.06           C  
ANISOU   64  CB  LYS A  10     2633   3253   4776  -1032   -527   1011       C  
ATOM     65  CG  LYS A  10      -1.292  33.026  19.411  1.00 29.47           C  
ANISOU   65  CG  LYS A  10     2435   4314   4449   -843    -32    549       C  
ATOM     66  CD  LYS A  10      -2.321  33.970  19.995  1.00 32.75           C  
ANISOU   66  CD  LYS A  10     3200   4822   4420   -285   -346     64       C  
ATOM     67  CE  LYS A  10      -3.438  33.214  20.698  1.00 35.44           C  
ANISOU   67  CE  LYS A  10     3072   5704   4690   -505    383   -923       C  
ATOM     68  NZ  LYS A  10      -3.654  31.866  20.083  1.00 45.73           N  
ANISOU   68  NZ  LYS A  10     4962   5027   7385  -1049   -247   -539       N  
ATOM     69  N   SER A  11       2.663  32.290  19.881  1.00 21.75           N  
ANISOU   69  N   SER A  11     2515   2327   3423    -65    -72    828       N  
ATOM     70  CA  SER A  11       3.332  31.147  20.457  1.00 23.46           C  
ANISOU   70  CA  SER A  11     2941   2031   3941   -560   -629   1065       C  
ATOM     71  C   SER A  11       4.283  31.492  21.595  1.00 25.43           C  
ANISOU   71  C   SER A  11     3085   2757   3820   -643   -657   1212       C  
ATOM     72  O   SER A  11       4.879  30.591  22.174  1.00 30.08           O  
ANISOU   72  O   SER A  11     3319   3336   4775   -274  -1172   1324       O  
ATOM     73  CB  SER A  11       4.108  30.433  19.355  1.00 24.81           C  
ANISOU   73  CB  SER A  11     3159   1647   4621    -25   -923    623       C  
ATOM     74  OG  SER A  11       5.369  31.058  19.206  1.00 25.00           O  
ANISOU   74  OG  SER A  11     2792   2206   4501    231   -700    660       O  
ATOM     75  N   GLY A  12       4.449  32.773  21.922  1.00 22.85           N  
ANISOU   75  N   GLY A  12     2498   3055   3129   -578   -134    650       N  
ATOM     76  CA  GLY A  12       5.246  33.232  23.054  1.00 25.42           C  
ANISOU   76  CA  GLY A  12     2591   4115   2951   -776     16    597       C  
ATOM     77  C   GLY A  12       6.710  33.468  22.699  1.00 18.58           C  
ANISOU   77  C   GLY A  12     2222   2485   2352     57   -201    844       C  
ATOM     78  O   GLY A  12       7.541  33.612  23.610  1.00 19.66           O  
ANISOU   78  O   GLY A  12     2698   2281   2491      3   -348    136       O  
ATOM     79  N   ALA A  13       7.021  33.455  21.414  1.00 17.95           N  
ANISOU   79  N   ALA A  13     2282   2163   2374    146   -264    514       N  
ATOM     80  CA  ALA A  13       8.349  33.784  20.902  1.00 16.49           C  
ANISOU   80  CA  ALA A  13     2402   1787   2078    351    -63    317       C  
ATOM     81  C   ALA A  13       8.533  35.291  20.725  1.00 16.19           C  
ANISOU   81  C   ALA A  13     2337   1711   2102    314    -80     48       C  
ATOM     82  O   ALA A  13       7.586  36.050  20.908  1.00 17.17           O  
ANISOU   82  O   ALA A  13     2188   1802   2535    291   -344    -46       O  
ATOM     83  CB  ALA A  13       8.580  33.050  19.556  1.00 17.00           C  
ANISOU   83  CB  ALA A  13     2499   1692   2270    114   -362     26       C  
ATOM     84  N   ILE A  14       9.751  35.678  20.345  1.00 16.12           N  
ANISOU   84  N   ILE A  14     2216   1658   2251    476   -308    459       N  
ATOM     85  CA  ILE A  14      10.090  37.039  19.931  1.00 16.12           C  
ANISOU   85  CA  ILE A  14     2261   1498   2364    502    -84    224       C  
ATOM     86  C   ILE A  14      10.276  37.168  18.421  1.00 15.21           C  
ANISOU   86  C   ILE A  14     1890   1434   2456    429    143    246       C  
ATOM     87  O   ILE A  14      10.671  36.200  17.734  1.00 13.98           O  
ANISOU   87  O   ILE A  14     1516   1463   2333    371   -327     20       O  
ATOM     88  CB AILE A  14      11.436  37.437  20.590  0.50 27.58           C  
ANISOU   88  CB AILE A  14     3706   3306   3467   -941  -1132    286       C  
ATOM     89  CB BILE A  14      11.341  37.621  20.631  0.50 22.06           C  
ANISOU   89  CB BILE A  14     2725   2779   2880   -248   -234    -28       C  
ATOM     90  CG1AILE A  14      11.510  37.250  22.122  0.50 32.38           C  
ANISOU   90  CG1AILE A  14     4311   4660   3330   -600  -1301   -120       C  
ATOM     91  CG1BILE A  14      12.641  37.051  20.033  0.50 22.50           C  
ANISOU   91  CG1BILE A  14     2348   2326   3873   -407   -288    -76       C  
ATOM     92  CG2AILE A  14      11.858  38.847  20.180  0.50 45.19           C  
ANISOU   92  CG2AILE A  14     5548   4648   6973  -2727  -1491   1731       C  
ATOM     93  CG2BILE A  14      11.228  37.475  22.148  0.50 22.41           C  
ANISOU   93  CG2BILE A  14     3665   2067   2782    564   -795    217       C  
ATOM     94  CD1AILE A  14      12.921  37.432  22.650  0.50 40.48           C  
ANISOU   94  CD1AILE A  14     4291   6802   4289    746  -1902   -542       C  
ATOM     95  CD1BILE A  14      13.899  37.590  20.661  0.50 22.56           C  
ANISOU   95  CD1BILE A  14     2704   2601   3267   -279   -840    428       C  
ATOM     96  N   CYS A  15      10.052  38.354  17.865  1.00 13.77           N  
ANISOU   96  N   CYS A  15     1770   1411   2052    300   -649     24       N  
ATOM     97  CA  CYS A  15      10.404  38.694  16.505  1.00 13.45           C  
ANISOU   97  CA  CYS A  15     1903   1086   2120    444   -315    -67       C  
ATOM     98  C   CYS A  15      11.627  39.644  16.586  1.00 13.71           C  
ANISOU   98  C   CYS A  15     1999   1416   1793    319   -308   -247       C  
ATOM     99  O   CYS A  15      11.483  40.735  17.132  1.00 13.45           O  
ANISOU   99  O   CYS A  15     1662   1393   2056    282   -174   -267       O  
ATOM    100  CB  CYS A  15       9.309  39.361  15.665  1.00 14.04           C  
ANISOU  100  CB  CYS A  15     2027   1482   1824    197   -352    137       C  
ATOM    101  SG  CYS A  15       7.865  38.353  15.232  1.00 15.56           S  
ANISOU  101  SG  CYS A  15     1849   1572   2492    299   -348    -48       S  
ATOM    102  N   HIS A  16      12.761  39.167  16.026  1.00 14.75           N  
ANISOU  102  N   HIS A  16     2164   1273   2167    283     77   -185       N  
ATOM    103  CA  HIS A  16      14.004  39.956  16.023  1.00 16.63           C  
ANISOU  103  CA  HIS A  16     2176   1519   2623    227    132    -35       C  
ATOM    104  C   HIS A  16      14.369  40.305  14.586  1.00 19.15           C  
ANISOU  104  C   HIS A  16     2648   1761   2867    105    675   -169       C  
ATOM    105  O   HIS A  16      14.257  39.422  13.713  1.00 20.57           O  
ANISOU  105  O   HIS A  16     3031   2021   2765   -366    885   -278       O  
ATOM    106  CB AHIS A  16      15.113  39.211  16.778  0.50 24.41           C  
ANISOU  106  CB AHIS A  16     2496   3012   3767    702   -576    -98       C  
ATOM    107  CB BHIS A  16      15.166  39.225  16.682  0.50 23.34           C  
ANISOU  107  CB BHIS A  16     2379   2687   3801    552   -432    -59       C  
ATOM    108  CG AHIS A  16      16.298  39.971  17.274  0.50 28.44           C  
ANISOU  108  CG AHIS A  16     2753   3559   4495    287   -836    169       C  
ATOM    109  CG BHIS A  16      16.245  40.062  17.274  0.50 27.99           C  
ANISOU  109  CG BHIS A  16     2675   3407   4552     75   -785    177       C  
ATOM    110  ND1AHIS A  16      17.025  40.570  16.306  0.50 29.60           N  
ANISOU  110  ND1AHIS A  16     3198   3236   4813    154   -672    254       N  
ATOM    111  ND1BHIS A  16      17.212  40.713  16.513  0.50 29.39           N  
ANISOU  111  ND1BHIS A  16     2651   3475   5040     70   -459    -31       N  
ATOM    112  CD2AHIS A  16      17.069  40.344  18.319  0.50 29.35           C  
ANISOU  112  CD2AHIS A  16     2803   3566   4784    129   -932     70       C  
ATOM    113  CD2BHIS A  16      16.559  40.357  18.558  0.50 25.64           C  
ANISOU  113  CD2BHIS A  16     2207   2766   4767    381   -873   -120       C  
ATOM    114  CE1AHIS A  16      18.090  41.262  16.579  0.50 29.81           C  
ANISOU  114  CE1AHIS A  16     2778   3362   5185    401   -651    233       C  
ATOM    115  CE1BHIS A  16      18.036  41.365  17.294  0.50 30.30           C  
ANISOU  115  CE1BHIS A  16     2669   3679   5166     -8   -495   -107       C  
ATOM    116  NE2AHIS A  16      18.129  41.120  17.904  0.50 32.07           N  
ANISOU  116  NE2AHIS A  16     3069   4011   5106   -173   -587   -137       N  
ATOM    117  NE2BHIS A  16      17.681  41.169  18.551  0.50 26.36           N  
ANISOU  117  NE2BHIS A  16     1856   2977   5183    498   -323   -403       N  
ATOM    118  N   PRO A  17      14.729  41.554  14.310  1.00 16.16           N  
ANISOU  118  N   PRO A  17     2006   1784   2351    127   -276     60       N  
ATOM    119  CA  PRO A  17      14.969  42.004  12.929  1.00 19.30           C  
ANISOU  119  CA  PRO A  17     2814   1921   2599    153    521    -96       C  
ATOM    120  C   PRO A  17      16.195  41.523  12.199  1.00 23.20           C  
ANISOU  120  C   PRO A  17     3079   2580   3157    553    664   -284       C  
ATOM    121  O   PRO A  17      16.258  41.653  10.961  1.00 29.40           O  
ANISOU  121  O   PRO A  17     4214   3800   3155    260   1346   -152       O  
ATOM    122  CB  PRO A  17      15.051  43.536  13.078  1.00 19.53           C  
ANISOU  122  CB  PRO A  17     2989   1780   2654    312    -31    230       C  
ATOM    123  CG  PRO A  17      15.495  43.773  14.478  1.00 21.46           C  
ANISOU  123  CG  PRO A  17     3289   1999   2864   -367    -71     99       C  
ATOM    124  CD  PRO A  17      14.779  42.701  15.256  1.00 16.68           C  
ANISOU  124  CD  PRO A  17     2141   1687   2509    352     74     26       C  
ATOM    125  N   VAL A  18      17.220  40.980  12.741  1.00 25.06           N  
ANISOU  125  N   VAL A  18     2698   1874   4950    124    413     79       N  
ATOM    126  CA  VAL A  18      18.509  40.518  12.325  1.00 26.55           C  
ANISOU  126  CA  VAL A  18     2900   2756   4433    344    924    813       C  
ATOM    127  C   VAL A  18      18.931  39.148  12.868  1.00 24.91           C  
ANISOU  127  C   VAL A  18     2505   2829   4132    492    223    421       C  
ATOM    128  O   VAL A  18      19.411  38.412  12.006  1.00 25.39           O  
ANISOU  128  O   VAL A  18     2717   2742   4188    155     10     65       O  
ATOM    129  CB  VAL A  18      19.612  41.544  12.695  1.00 30.86           C  
ANISOU  129  CB  VAL A  18     2469   3051   6205    421   -316   1719       C  
ATOM    130  CG1 VAL A  18      20.862  41.269  11.862  1.00 33.28           C  
ANISOU  130  CG1 VAL A  18     3165   3140   6338   -275    490   1846       C  
ATOM    131  CG2 VAL A  18      19.211  42.991  12.480  1.00 40.13           C  
ANISOU  131  CG2 VAL A  18     2936   2824   9487    -14   -176   2006       C  
ATOM    132  N   PHE A  19      18.830  38.734  14.126  1.00 23.32           N  
ANISOU  132  N   PHE A  19     2036   2802   4022    506   -348    390       N  
ATOM    133  CA  PHE A  19      19.451  37.480  14.597  1.00 21.34           C  
ANISOU  133  CA  PHE A  19     1775   2332   4002    324   -153     16       C  
ATOM    134  C   PHE A  19      18.725  36.986  15.827  1.00 21.90           C  
ANISOU  134  C   PHE A  19     2061   2004   4257    346    147     43       C  
ATOM    135  O   PHE A  19      18.025  37.791  16.437  1.00 22.76           O  
ANISOU  135  O   PHE A  19     2545   1871   4233    421    260     83       O  
ATOM    136  CB  PHE A  19      20.947  37.697  14.871  1.00 23.29           C  
ANISOU  136  CB  PHE A  19     1631   2641   4577    608     89   -192       C  
ATOM    137  CG  PHE A  19      21.212  38.761  15.940  1.00 23.48           C  
ANISOU  137  CG  PHE A  19     1811   2852   4257   -157    -24     60       C  
ATOM    138  CD1 PHE A  19      21.231  38.532  17.286  1.00 26.33           C  
ANISOU  138  CD1 PHE A  19     2602   3004   4397   -704   -712    381       C  
ATOM    139  CD2 PHE A  19      21.438  40.064  15.519  1.00 25.16           C  
ANISOU  139  CD2 PHE A  19     2469   2994   4097   -547   -794    215       C  
ATOM    140  CE1 PHE A  19      21.457  39.524  18.217  1.00 28.74           C  
ANISOU  140  CE1 PHE A  19     2993   3604   4321   -756   -483     30       C  
ATOM    141  CE2 PHE A  19      21.647  41.063  16.440  1.00 28.25           C  
ANISOU  141  CE2 PHE A  19     3365   2813   4554     91   -581    -69       C  
ATOM    142  CZ  PHE A  19      21.633  40.816  17.787  1.00 26.71           C  
ANISOU  142  CZ  PHE A  19     2598   3166   4383   -192    -28   -490       C  
ATOM    143  N   CYS A  20      18.821  35.730  16.225  1.00 21.05           N  
ANISOU  143  N   CYS A  20     2155   2048   3794    670   -349    -53       N  
ATOM    144  CA  CYS A  20      18.280  35.263  17.482  1.00 20.83           C  
ANISOU  144  CA  CYS A  20     1987   1987   3942    275   -511     56       C  
ATOM    145  C   CYS A  20      19.340  35.505  18.564  1.00 19.73           C  
ANISOU  145  C   CYS A  20     1619   2070   3805    107   -277    162       C  
ATOM    146  O   CYS A  20      20.491  35.054  18.427  1.00 23.18           O  
ANISOU  146  O   CYS A  20     1624   3143   4041    267    -40    167       O  
ATOM    147  CB  CYS A  20      17.871  33.788  17.463  1.00 22.00           C  
ANISOU  147  CB  CYS A  20     1849   1955   4556    345   -653   -101       C  
ATOM    148  SG  CYS A  20      16.443  33.485  16.364  1.00 20.25           S  
ANISOU  148  SG  CYS A  20     2303   1860   3531    402   -498   -173       S  
ATOM    149  N   PRO A  21      18.988  36.223  19.620  1.00 22.31           N  
ANISOU  149  N   PRO A  21     2062   2253   4162    797   -812   -192       N  
ATOM    150  CA  PRO A  21      20.027  36.500  20.631  1.00 25.20           C  
ANISOU  150  CA  PRO A  21     2465   3194   3915    511   -790   -189       C  
ATOM    151  C   PRO A  21      20.364  35.264  21.477  1.00 26.31           C  
ANISOU  151  C   PRO A  21     2907   3142   3946    175  -1561   -344       C  
ATOM    152  O   PRO A  21      19.722  34.210  21.399  1.00 26.96           O  
ANISOU  152  O   PRO A  21     2149   3471   4625     76  -1344    312       O  
ATOM    153  CB  PRO A  21      19.414  37.621  21.453  1.00 27.33           C  
ANISOU  153  CB  PRO A  21     3289   3422   3675    569   -682   -337       C  
ATOM    154  CG  PRO A  21      18.023  37.802  21.027  1.00 27.25           C  
ANISOU  154  CG  PRO A  21     3240   2908   4205    924   -539   -540       C  
ATOM    155  CD  PRO A  21      17.706  36.817  19.955  1.00 24.42           C  
ANISOU  155  CD  PRO A  21     2233   2440   4604    705   -438   -412       C  
ATOM    156  N   ARG A  22      21.395  35.431  22.295  1.00 31.74           N  
ANISOU  156  N   ARG A  22     3146   4051   4865    -96  -2143     26       N  
ATOM    157  CA  ARG A  22      21.882  34.448  23.241  1.00 33.63           C  
ANISOU  157  CA  ARG A  22     3217   4750   4809   -183  -2003    502       C  
ATOM    158  C   ARG A  22      20.750  33.700  23.946  1.00 32.75           C  
ANISOU  158  C   ARG A  22     3872   4952   3619   -496  -1432   -480       C  
ATOM    159  O   ARG A  22      19.857  34.369  24.461  1.00 37.35           O  
ANISOU  159  O   ARG A  22     4939   5466   3788   -619   -815  -1480       O  
ATOM    160  CB  ARG A  22      22.763  35.155  24.283  1.00 43.79           C  
ANISOU  160  CB  ARG A  22     4059   6570   6010  -1048  -3280    864       C  
ATOM    161  CG  ARG A  22      24.244  35.182  23.943  1.00 53.98           C  
ANISOU  161  CG  ARG A  22     4105   8818   7585  -1306  -3048   -464       C  
ATOM    162  CD  ARG A  22      25.112  34.776  25.119  1.00 58.34           C  
ANISOU  162  CD  ARG A  22     3853  10340   7975   -723  -3720  -1536       C  
ATOM    163  NE  ARG A  22      26.511  34.616  24.783  1.00 60.37           N  
ANISOU  163  NE  ARG A  22     4250  10754   7935   -328  -3003  -1356       N  
ATOM    164  CZ  ARG A  22      27.283  35.683  24.569  1.00 64.39           C  
ANISOU  164  CZ  ARG A  22     4601  11293   8569   -539  -1761   -764       C  
ATOM    165  NH1 ARG A  22      26.787  36.912  24.652  1.00 73.80           N  
ANISOU  165  NH1 ARG A  22     5448  10914  11679   -628    590    847       N  
ATOM    166  NH2 ARG A  22      28.554  35.505  24.266  1.00 66.96           N  
ANISOU  166  NH2 ARG A  22     4558  12320   8563    -47  -1919    579       N  
ATOM    167  N   ARG A  23      20.828  32.386  23.902  1.00 33.63           N  
ANISOU  167  N   ARG A  23     2795   4899   5084   -195  -1805    527       N  
ATOM    168  CA  ARG A  23      19.918  31.437  24.525  1.00 33.50           C  
ANISOU  168  CA  ARG A  23     2991   5352   4384    -57  -1654    838       C  
ATOM    169  C   ARG A  23      18.657  31.149  23.709  1.00 29.96           C  
ANISOU  169  C   ARG A  23     2851   4212   4320   -137  -1555   1362       C  
ATOM    170  O   ARG A  23      17.905  30.210  24.043  1.00 31.51           O  
ANISOU  170  O   ARG A  23     3696   4283   3995   -482  -1680   1614       O  
ATOM    171  CB  ARG A  23      19.499  31.925  25.913  1.00 40.64           C  
ANISOU  171  CB  ARG A  23     4429   6154   4859   -766  -1312    -79       C  
ATOM    172  CG  ARG A  23      20.572  32.044  26.966  1.00 49.25           C  
ANISOU  172  CG  ARG A  23     6244   7204   5267   -931  -2312   -725       C  
ATOM    173  CD  ARG A  23      20.230  33.119  27.979  1.00 58.61           C  
ANISOU  173  CD  ARG A  23     8301   7793   6175   -893  -2162  -1536       C  
ATOM    174  NE  ARG A  23      20.678  34.458  27.634  1.00 64.86           N  
ANISOU  174  NE  ARG A  23     9895   7480   7269   -817  -2337  -1517       N  
ATOM    175  CZ  ARG A  23      21.558  35.251  28.228  1.00 65.83           C  
ANISOU  175  CZ  ARG A  23    10938   6678   7398   -689  -2667  -1776       C  
ATOM    176  NH1 ARG A  23      22.216  34.890  29.325  1.00 69.77           N  
ANISOU  176  NH1 ARG A  23    12660   6866   6985    638  -3314  -3339       N  
ATOM    177  NH2 ARG A  23      21.832  36.463  27.739  1.00 74.82           N  
ANISOU  177  NH2 ARG A  23    11834   7882   8713  -1829  -1410   -879       N  
ATOM    178  N   TYR A  24      18.375  31.922  22.666  1.00 22.18           N  
ANISOU  178  N   TYR A  24     2353   2805   3271     28   -820    319       N  
ATOM    179  CA  TYR A  24      17.232  31.680  21.789  1.00 21.65           C  
ANISOU  179  CA  TYR A  24     2487   2254   3483    433  -1090     90       C  
ATOM    180  C   TYR A  24      17.596  30.903  20.535  1.00 21.20           C  
ANISOU  180  C   TYR A  24     2261   2084   3711    320   -868    -10       C  
ATOM    181  O   TYR A  24      18.713  31.049  20.016  1.00 25.49           O  
ANISOU  181  O   TYR A  24     2508   2835   4342    145   -505    -48       O  
ATOM    182  CB  TYR A  24      16.582  33.012  21.352  1.00 21.63           C  
ANISOU  182  CB  TYR A  24     2736   1949   3533    299  -1028   -111       C  
ATOM    183  CG  TYR A  24      15.901  33.788  22.444  1.00 25.28           C  
ANISOU  183  CG  TYR A  24     2771   2852   3983    718  -1243   -617       C  
ATOM    184  CD1 TYR A  24      16.662  34.536  23.347  1.00 28.61           C  
ANISOU  184  CD1 TYR A  24     3287   3158   4426    977  -1515  -1193       C  
ATOM    185  CD2 TYR A  24      14.518  33.770  22.570  1.00 25.00           C  
ANISOU  185  CD2 TYR A  24     2933   2338   4227    368   -603    -57       C  
ATOM    186  CE1 TYR A  24      16.057  35.249  24.360  1.00 30.94           C  
ANISOU  186  CE1 TYR A  24     3690   3559   4506    240   -693  -1240       C  
ATOM    187  CE2 TYR A  24      13.926  34.480  23.588  1.00 27.82           C  
ANISOU  187  CE2 TYR A  24     3191   3158   4224    668   -641   -287       C  
ATOM    188  CZ  TYR A  24      14.684  35.220  24.464  1.00 32.32           C  
ANISOU  188  CZ  TYR A  24     3737   3568   4976    269   -403  -1040       C  
ATOM    189  OH  TYR A  24      14.057  35.923  25.467  1.00 36.84           O  
ANISOU  189  OH  TYR A  24     3950   4908   5141    676   -529  -1590       O  
ATOM    190  N   LYS A  25      16.704  30.091  19.983  1.00 20.78           N  
ANISOU  190  N   LYS A  25     2584   1708   3601    340  -1078    276       N  
ATOM    191  CA  LYS A  25      16.905  29.405  18.705  1.00 22.34           C  
ANISOU  191  CA  LYS A  25     2572   2212   3703    177  -1048     35       C  
ATOM    192  C   LYS A  25      15.816  29.806  17.695  1.00 19.39           C  
ANISOU  192  C   LYS A  25     1899   2062   3407   -119   -634    141       C  
ATOM    193  O   LYS A  25      14.693  30.189  18.049  1.00 20.13           O  
ANISOU  193  O   LYS A  25     2359   1836   3453    333   -497    -11       O  
ATOM    194  CB  LYS A  25      16.970  27.878  18.858  1.00 22.71           C  
ANISOU  194  CB  LYS A  25     3286   2244   3100    568   -586    -52       C  
ATOM    195  CG  LYS A  25      17.942  27.433  19.917  1.00 31.66           C  
ANISOU  195  CG  LYS A  25     4700   3088   4239    962  -1550    469       C  
ATOM    196  CD  LYS A  25      18.502  26.054  20.074  1.00 42.88           C  
ANISOU  196  CD  LYS A  25     5560   4303   6429   2487   -523   1311       C  
ATOM    197  CE  LYS A  25      19.903  25.836  19.543  1.00 48.09           C  
ANISOU  197  CE  LYS A  25     5981   4734   7558   2218    362   1375       C  
ATOM    198  NZ  LYS A  25      20.360  24.411  19.452  1.00 42.43           N  
ANISOU  198  NZ  LYS A  25     4062   3961   8100    457    881   -424       N  
ATOM    199  N   GLN A  26      16.125  29.814  16.408  1.00 20.23           N  
ANISOU  199  N   GLN A  26     2263   1983   3438    459   -577   -130       N  
ATOM    200  CA  GLN A  26      15.224  30.249  15.345  1.00 18.59           C  
ANISOU  200  CA  GLN A  26     2002   1919   3142    267   -322   -104       C  
ATOM    201  C   GLN A  26      14.198  29.151  15.057  1.00 18.08           C  
ANISOU  201  C   GLN A  26     1933   1628   3310    519   -204   -375       C  
ATOM    202  O   GLN A  26      14.535  27.986  14.792  1.00 21.30           O  
ANISOU  202  O   GLN A  26     2171   1743   4178    734   -550   -586       O  
ATOM    203  CB  GLN A  26      15.949  30.634  14.058  1.00 19.42           C  
ANISOU  203  CB  GLN A  26     2125   2171   3082    212   -135   -485       C  
ATOM    204  CG  GLN A  26      15.097  30.973  12.870  1.00 17.98           C  
ANISOU  204  CG  GLN A  26     2231   1678   2923    322     40   -410       C  
ATOM    205  CD  GLN A  26      15.783  31.539  11.658  1.00 19.57           C  
ANISOU  205  CD  GLN A  26     2205   1951   3281    159     39   -130       C  
ATOM    206  OE1 GLN A  26      17.011  31.658  11.638  1.00 27.73           O  
ANISOU  206  OE1 GLN A  26     2231   3679   4626    427    509    718       O  
ATOM    207  NE2 GLN A  26      15.036  31.935  10.633  1.00 25.41           N  
ANISOU  207  NE2 GLN A  26     3315   3661   2678   -425   -426   -249       N  
ATOM    208  N   ILE A  27      12.917  29.518  15.131  1.00 18.98           N  
ANISOU  208  N   ILE A  27     1846   1710   3657    515   -145   -390       N  
ATOM    209  CA  ILE A  27      11.809  28.597  14.871  1.00 18.10           C  
ANISOU  209  CA  ILE A  27     2024   1530   3322    513   -300   -280       C  
ATOM    210  C   ILE A  27      10.969  29.034  13.682  1.00 17.64           C  
ANISOU  210  C   ILE A  27     1993   1566   3145    383    -65   -148       C  
ATOM    211  O   ILE A  27       9.987  28.383  13.320  1.00 19.37           O  
ANISOU  211  O   ILE A  27     2556   1464   3342    209   -664    -57       O  
ATOM    212  CB  ILE A  27      10.888  28.383  16.116  1.00 17.03           C  
ANISOU  212  CB  ILE A  27     2123   1271   3078    277   -538   -177       C  
ATOM    213  CG1 ILE A  27      10.194  29.658  16.571  1.00 15.94           C  
ANISOU  213  CG1 ILE A  27     2277   1466   2313    409   -441    -75       C  
ATOM    214  CG2 ILE A  27      11.628  27.700  17.257  1.00 19.31           C  
ANISOU  214  CG2 ILE A  27     2374   1473   3489    382   -768    -11       C  
ATOM    215  CD1 ILE A  27       9.081  29.424  17.567  1.00 17.22           C  
ANISOU  215  CD1 ILE A  27     2113   1472   2959    271   -338    274       C  
ATOM    216  N   GLY A  28      11.344  30.126  12.989  1.00 17.63           N  
ANISOU  216  N   GLY A  28     2011   1567   3122    505    194   -129       N  
ATOM    217  CA  GLY A  28      10.643  30.614  11.812  1.00 17.83           C  
ANISOU  217  CA  GLY A  28     2385   1654   2737    317     96   -373       C  
ATOM    218  C   GLY A  28      11.069  32.034  11.474  1.00 16.71           C  
ANISOU  218  C   GLY A  28     2219   1665   2465    280   -501   -358       C  
ATOM    219  O   GLY A  28      12.155  32.473  11.924  1.00 17.36           O  
ANISOU  219  O   GLY A  28     2103   1830   2661    350   -429   -519       O  
ATOM    220  N   THR A  29      10.220  32.733  10.725  1.00 15.88           N  
ANISOU  220  N   THR A  29     1839   1784   2412    431   -141   -373       N  
ATOM    221  CA  THR A  29      10.455  34.130  10.400  1.00 16.47           C  
ANISOU  221  CA  THR A  29     2239   1826   2192    478   -324   -271       C  
ATOM    222  C   THR A  29       9.223  34.899  10.868  1.00 16.36           C  
ANISOU  222  C   THR A  29     2064   1652   2501    367   -386   -249       C  
ATOM    223  O   THR A  29       8.188  34.363  11.257  1.00 17.94           O  
ANISOU  223  O   THR A  29     2243   1732   2842    221   -238   -316       O  
ATOM    224  CB  THR A  29      10.701  34.392   8.907  1.00 18.25           C  
ANISOU  224  CB  THR A  29     2693   2050   2191    -68   -275   -428       C  
ATOM    225  OG1 THR A  29       9.462  34.172   8.218  1.00 22.91           O  
ANISOU  225  OG1 THR A  29     2944   3426   2336   -166   -607   -131       O  
ATOM    226  CG2 THR A  29      11.673  33.426   8.282  1.00 21.63           C  
ANISOU  226  CG2 THR A  29     2742   2578   2898   -461    504   -863       C  
ATOM    227  N   CYS A  30       9.256  36.196  10.880  1.00 17.34           N  
ANISOU  227  N   CYS A  30     2141   1687   2758    420    -71    -84       N  
ATOM    228  CA  CYS A  30       8.167  37.143  11.034  1.00 14.99           C  
ANISOU  228  CA  CYS A  30     1776   1570   2348    177   -260    -76       C  
ATOM    229  C   CYS A  30       7.804  37.920   9.770  1.00 16.79           C  
ANISOU  229  C   CYS A  30     1941   2165   2273    329   -285     -4       C  
ATOM    230  O   CYS A  30       7.277  39.027   9.811  1.00 18.46           O  
ANISOU  230  O   CYS A  30     2400   2248   2367    577   -618     35       O  
ATOM    231  CB  CYS A  30       8.412  38.091  12.225  1.00 14.28           C  
ANISOU  231  CB  CYS A  30     1518   1453   2456    283   -444    -27       C  
ATOM    232  SG  CYS A  30       8.669  37.145  13.758  1.00 15.61           S  
ANISOU  232  SG  CYS A  30     2097   1457   2379    321   -482   -111       S  
ATOM    233  N   GLY A  31       8.004  37.355   8.588  1.00 17.46           N  
ANISOU  233  N   GLY A  31     1969   2338   2328    153   -403   -122       N  
ATOM    234  CA  GLY A  31       7.510  37.754   7.305  1.00 20.81           C  
ANISOU  234  CA  GLY A  31     2472   3172   2265     22   -541    -23       C  
ATOM    235  C   GLY A  31       8.429  38.744   6.627  1.00 22.28           C  
ANISOU  235  C   GLY A  31     3184   2986   2294     98    -75     -2       C  
ATOM    236  O   GLY A  31       9.013  38.471   5.581  1.00 26.01           O  
ANISOU  236  O   GLY A  31     3736   3442   2705   -364    369   -585       O  
ATOM    237  N   LEU A  32       8.619  39.916   7.248  1.00 19.68           N  
ANISOU  237  N   LEU A  32     2634   3027   1815    197    -68     93       N  
ATOM    238  CA  LEU A  32       9.548  40.906   6.708  1.00 21.09           C  
ANISOU  238  CA  LEU A  32     2872   3157   1986    -26   -258    235       C  
ATOM    239  C   LEU A  32      10.936  40.329   6.481  1.00 21.03           C  
ANISOU  239  C   LEU A  32     2443   3632   1916   -390   -557     68       C  
ATOM    240  O   LEU A  32      11.379  39.534   7.324  1.00 22.30           O  
ANISOU  240  O   LEU A  32     2351   3816   2307    -63    -37    485       O  
ATOM    241  CB ALEU A  32       9.600  42.055   7.715  0.50 29.12           C  
ANISOU  241  CB ALEU A  32     3920   3641   3501   -444     15   -678       C  
ATOM    242  CB BLEU A  32       9.740  42.065   7.660  0.50 27.91           C  
ANISOU  242  CB BLEU A  32     3944   3278   3382   -209   -375   -339       C  
ATOM    243  CG ALEU A  32      10.132  43.420   7.299  0.50 27.22           C  
ANISOU  243  CG ALEU A  32     4119   3266   2958    209    168   -600       C  
ATOM    244  CG BLEU A  32       8.678  43.146   7.646  0.50 31.82           C  
ANISOU  244  CG BLEU A  32     4384   3852   3854    341    748   -508       C  
ATOM    245  CD1ALEU A  32       9.319  43.929   6.118  0.50 40.42           C  
ANISOU  245  CD1ALEU A  32     5346   6583   3431   2542    661    586       C  
ATOM    246  CD1BLEU A  32       8.649  43.761   9.034  0.50 38.77           C  
ANISOU  246  CD1BLEU A  32     6002   5465   3265    787   1454   -157       C  
ATOM    247  CD2ALEU A  32      10.076  44.411   8.452  0.50 42.09           C  
ANISOU  247  CD2ALEU A  32     8713   3557   3723   -455   1707  -1125       C  
ATOM    248  CD2BLEU A  32       8.996  44.162   6.559  0.50 37.73           C  
ANISOU  248  CD2BLEU A  32     5224   6190   2920   1751   -719   1045       C  
ATOM    249  N   PRO A  33      11.588  40.701   5.401  1.00 21.38           N  
ANISOU  249  N   PRO A  33     2731   3199   2194     61   -288    296       N  
ATOM    250  CA  PRO A  33      12.896  40.095   5.093  1.00 21.77           C  
ANISOU  250  CA  PRO A  33     2664   3272   2334     85   -278    319       C  
ATOM    251  C   PRO A  33      13.916  40.214   6.221  1.00 24.59           C  
ANISOU  251  C   PRO A  33     3065   3961   2318    650   -503    -23       C  
ATOM    252  O   PRO A  33      14.042  41.292   6.807  1.00 25.31           O  
ANISOU  252  O   PRO A  33     3405   3636   2576   -375   -523    376       O  
ATOM    253  CB  PRO A  33      13.359  40.854   3.835  1.00 23.90           C  
ANISOU  253  CB  PRO A  33     2990   3705   2386    433    -47    553       C  
ATOM    254  CG  PRO A  33      12.133  41.421   3.233  1.00 25.30           C  
ANISOU  254  CG  PRO A  33     3203   4214   2197    805     36    454       C  
ATOM    255  CD  PRO A  33      11.171  41.644   4.349  1.00 20.94           C  
ANISOU  255  CD  PRO A  33     3230   2760   1965    436   -157   -107       C  
ATOM    256  N   GLY A  34      14.614  39.127   6.535  1.00 22.81           N  
ANISOU  256  N   GLY A  34     2022   4130   2514    390    263    574       N  
ATOM    257  CA  GLY A  34      15.656  39.106   7.552  1.00 24.68           C  
ANISOU  257  CA  GLY A  34     2263   4304   2812    210     66   1121       C  
ATOM    258  C   GLY A  34      15.185  38.914   8.961  1.00 21.55           C  
ANISOU  258  C   GLY A  34     2168   3378   2644    359    -12    640       C  
ATOM    259  O   GLY A  34      15.996  38.684   9.879  1.00 23.27           O  
ANISOU  259  O   GLY A  34     2307   3932   2602    200   -307     32       O  
ATOM    260  N   THR A  35      13.854  38.993   9.151  1.00 20.28           N  
ANISOU  260  N   THR A  35     2152   2773   2781    271      6    677       N  
ATOM    261  CA  THR A  35      13.347  38.842  10.513  1.00 18.68           C  
ANISOU  261  CA  THR A  35     2113   2320   2662     42    -58    494       C  
ATOM    262  C   THR A  35      13.367  37.367  10.916  1.00 15.89           C  
ANISOU  262  C   THR A  35     2081   2042   1916    243   -159   -105       C  
ATOM    263  O   THR A  35      13.257  36.462  10.071  1.00 22.03           O  
ANISOU  263  O   THR A  35     3446   2742   2182   -208   -465   -498       O  
ATOM    264  CB  THR A  35      11.945  39.434  10.749  1.00 17.49           C  
ANISOU  264  CB  THR A  35     2291   2348   2006    396   -411    332       C  
ATOM    265  OG1 THR A  35      11.005  38.844   9.859  1.00 18.62           O  
ANISOU  265  OG1 THR A  35     2292   2694   2087    307   -231    -26       O  
ATOM    266  CG2 THR A  35      11.860  40.935  10.468  1.00 20.78           C  
ANISOU  266  CG2 THR A  35     2770   2339   2785    237   -282    483       C  
ATOM    267  N   LYS A  36      13.536  37.144  12.218  1.00 16.65           N  
ANISOU  267  N   LYS A  36     2539   1825   1961    320   -262   -165       N  
ATOM    268  CA  LYS A  36      13.651  35.853  12.845  1.00 15.10           C  
ANISOU  268  CA  LYS A  36     2071   1638   2027    274   -450   -289       C  
ATOM    269  C   LYS A  36      12.607  35.684  13.948  1.00 15.92           C  
ANISOU  269  C   LYS A  36     2334   1289   2426    467   -127   -139       C  
ATOM    270  O   LYS A  36      12.493  36.569  14.786  1.00 15.05           O  
ANISOU  270  O   LYS A  36     1979   1561   2180    184   -250   -166       O  
ATOM    271  CB  LYS A  36      15.037  35.625  13.464  1.00 18.74           C  
ANISOU  271  CB  LYS A  36     2052   1723   3344    129   -762   -168       C  
ATOM    272  CG  LYS A  36      16.156  35.913  12.499  1.00 24.82           C  
ANISOU  272  CG  LYS A  36     2017   3237   4179   1010   -325    587       C  
ATOM    273  CD  LYS A  36      16.180  35.102  11.233  1.00 36.32           C  
ANISOU  273  CD  LYS A  36     4252   4572   4978    533   1319   -394       C  
ATOM    274  CE  LYS A  36      17.583  35.081  10.610  1.00 47.93           C  
ANISOU  274  CE  LYS A  36     4913   7044   6253    -79   2348   -685       C  
ATOM    275  NZ  LYS A  36      17.597  35.211   9.123  1.00 51.76           N  
ANISOU  275  NZ  LYS A  36     4379   8834   6453  -2474   2228    590       N  
ATOM    276  N   CYS A  37      11.867  34.563  13.972  1.00 15.73           N  
ANISOU  276  N   CYS A  37     1966   1465   2545    441   -320   -145       N  
ATOM    277  CA  CYS A  37      11.050  34.158  15.095  1.00 14.39           C  
ANISOU  277  CA  CYS A  37     1804   1398   2264    362   -582   -240       C  
ATOM    278  C   CYS A  37      11.935  33.324  16.019  1.00 16.48           C  
ANISOU  278  C   CYS A  37     2271   1485   2507    572   -743   -186       C  
ATOM    279  O   CYS A  37      12.423  32.274  15.579  1.00 16.62           O  
ANISOU  279  O   CYS A  37     1906   1637   2773    585   -705   -282       O  
ATOM    280  CB  CYS A  37       9.798  33.413  14.661  1.00 15.43           C  
ANISOU  280  CB  CYS A  37     1721   1150   2990    441   -494   -190       C  
ATOM    281  SG  CYS A  37       8.667  33.058  16.018  1.00 15.92           S  
ANISOU  281  SG  CYS A  37     1859   1439   2753    260   -614    -88       S  
ATOM    282  N   CYS A  38      12.161  33.761  17.265  1.00 16.20           N  
ANISOU  282  N   CYS A  38     2323   1524   2306    495   -620    100       N  
ATOM    283  CA  CYS A  38      13.127  33.139  18.167  1.00 16.52           C  
ANISOU  283  CA  CYS A  38     2037   1753   2488    424   -642     48       C  
ATOM    284  C   CYS A  38      12.505  32.736  19.494  1.00 16.96           C  
ANISOU  284  C   CYS A  38     2271   1835   2338    479   -764    117       C  
ATOM    285  O   CYS A  38      11.688  33.453  20.063  1.00 16.87           O  
ANISOU  285  O   CYS A  38     1938   1783   2690    330   -393    518       O  
ATOM    286  CB  CYS A  38      14.291  34.099  18.401  1.00 18.65           C  
ANISOU  286  CB  CYS A  38     2209   1892   2985    300   -682      0       C  
ATOM    287  SG  CYS A  38      15.035  34.873  16.986  1.00 18.03           S  
ANISOU  287  SG  CYS A  38     1813   1885   3153    264   -619      5       S  
ATOM    288  N   LYS A  39      12.885  31.578  20.028  1.00 18.33           N  
ANISOU  288  N   LYS A  39     2561   1871   2533    563   -739    191       N  
ATOM    289  CA  LYS A  39      12.343  31.034  21.249  1.00 19.69           C  
ANISOU  289  CA  LYS A  39     2949   1954   2580    574   -691    289       C  
ATOM    290  C   LYS A  39      13.413  30.238  21.976  1.00 20.31           C  
ANISOU  290  C   LYS A  39     2773   2012   2933    380   -567    690       C  
ATOM    291  O   LYS A  39      14.235  29.562  21.354  1.00 22.29           O  
ANISOU  291  O   LYS A  39     2906   2210   3352    615   -611    491       O  
ATOM    292  CB  LYS A  39      11.147  30.140  20.908  1.00 20.53           C  
ANISOU  292  CB  LYS A  39     2667   2180   2954    594   -455    370       C  
ATOM    293  CG  LYS A  39      10.398  29.712  22.138  1.00 29.02           C  
ANISOU  293  CG  LYS A  39     2992   4005   4028    789    -68   1867       C  
ATOM    294  CD  LYS A  39       8.912  29.676  22.045  1.00 34.73           C  
ANISOU  294  CD  LYS A  39     2960   5751   4484   1215    116   2499       C  
ATOM    295  CE  LYS A  39       8.273  30.025  23.388  1.00 34.55           C  
ANISOU  295  CE  LYS A  39     3391   5000   4738    907    613   2685       C  
ATOM    296  NZ  LYS A  39       6.993  29.287  23.565  1.00 45.70           N  
ANISOU  296  NZ  LYS A  39     4383   5331   7648    282   1811   3270       N  
ATOM    297  N   LYS A  40      13.381  30.289  23.288  1.00 23.09           N  
ANISOU  297  N   LYS A  40     2937   2936   2899    450   -841    676       N  
ATOM    298  CA  LYS A  40      14.367  29.484  24.062  1.00 31.50           C  
ANISOU  298  CA  LYS A  40     4730   3414   3824    933  -1371   1489       C  
ATOM    299  C   LYS A  40      13.946  28.022  23.980  1.00 32.80           C  
ANISOU  299  C   LYS A  40     3335   3607   5519    766  -1564   1709       C  
ATOM    300  O   LYS A  40      12.739  27.760  24.092  1.00 41.16           O  
ANISOU  300  O   LYS A  40     3509   5121   7007    691   -709   3367       O  
ATOM    301  CB  LYS A  40      14.448  30.031  25.483  1.00 32.37           C  
ANISOU  301  CB  LYS A  40     4103   4654   3541    994  -1500   1634       C  
ATOM    302  CG  LYS A  40      14.816  31.501  25.611  1.00 35.39           C  
ANISOU  302  CG  LYS A  40     5106   4772   3568    996  -1244    636       C  
ATOM    303  CD  LYS A  40      15.321  31.778  27.022  1.00 40.05           C  
ANISOU  303  CD  LYS A  40     6457   5664   3097   1788   -773     99       C  
ATOM    304  CE  LYS A  40      15.111  33.194  27.479  1.00 45.42           C  
ANISOU  304  CE  LYS A  40     7978   5624   3657   2185  -1699     67       C  
ATOM    305  NZ  LYS A  40      14.537  33.310  28.856  1.00 66.07           N  
ANISOU  305  NZ  LYS A  40    10372   9967   4764   1920   -385  -2890       N  
ATOM    306  N   PRO A  41      14.880  27.096  23.775  1.00 33.21           N  
ANISOU  306  N   PRO A  41     3537   3485   5596    685  -2054    565       N  
ATOM    307  CA  PRO A  41      14.595  25.664  23.774  1.00 37.12           C  
ANISOU  307  CA  PRO A  41     4757   3506   5842    455   -981    921       C  
ATOM    308  C   PRO A  41      13.815  25.210  25.003  1.00 42.38           C  
ANISOU  308  C   PRO A  41     5571   4233   6298    806   -100    831       C  
ATOM    309  O   PRO A  41      12.961  24.313  24.891  1.00 52.98           O  
ANISOU  309  O   PRO A  41     7302   4431   8399   -352   -520   3088       O  
ATOM    310  CB  PRO A  41      16.014  25.066  23.821  1.00 38.30           C  
ANISOU  310  CB  PRO A  41     5150   3136   6267    873   -541     16       C  
ATOM    311  CG  PRO A  41      16.826  26.053  23.042  1.00 38.95           C  
ANISOU  311  CG  PRO A  41     5029   3274   6498    505   -217   -479       C  
ATOM    312  CD  PRO A  41      16.299  27.392  23.476  1.00 34.66           C  
ANISOU  312  CD  PRO A  41     3714   3162   6293    918  -1281    112       C  
ATOM    313  OXT PRO A  41      14.091  25.786  26.091  1.00 52.27           O  
ANISOU  313  OXT PRO A  41     9490   4886   5484   2176  -1333   1410       O  
TER     314      PRO A  41                                                      
ATOM    315  N  AGLY B   1      21.825   4.133   7.777  0.50 36.67           N  
ANISOU  315  N  AGLY B   1     4931   2769   6232  -1258   1028   1125       N  
ATOM    316  N  BGLY B   1      19.608   3.135   7.793  0.50 48.13           N  
ANISOU  316  N  BGLY B   1     5429   7742   5118   -261  -1645    466       N  
ATOM    317  CA AGLY B   1      20.962   3.024   8.154  0.50 30.19           C  
ANISOU  317  CA AGLY B   1     4484   2973   4015  -1430    276    847       C  
ATOM    318  CA BGLY B   1      21.004   3.023   8.144  0.50 30.65           C  
ANISOU  318  CA BGLY B   1     4354   3247   4046  -1322    418    985       C  
ATOM    319  C   GLY B   1      21.353   2.172   9.337  1.00 22.80           C  
ANISOU  319  C   GLY B   1     3399   2468   2795  -1084    481   -264       C  
ATOM    320  O   GLY B   1      22.383   2.330   9.978  1.00 24.55           O  
ANISOU  320  O   GLY B   1     3178   2345   3806  -1007    377   -724       O  
ATOM    321  N   ILE B   2      20.516   1.206   9.684  1.00 19.30           N  
ANISOU  321  N   ILE B   2     2856   1814   2665   -552   -167    -20       N  
ATOM    322  CA  ILE B   2      20.791   0.150  10.662  1.00 18.59           C  
ANISOU  322  CA  ILE B   2     2179   2440   2443   -430   -454    122       C  
ATOM    323  C   ILE B   2      21.884  -0.786  10.137  1.00 18.33           C  
ANISOU  323  C   ILE B   2     1919   2398   2647   -562   -726   -154       C  
ATOM    324  O   ILE B   2      22.045  -1.053   8.925  1.00 17.63           O  
ANISOU  324  O   ILE B   2     2006   2040   2652   -518   -524     48       O  
ATOM    325  CB  ILE B   2      19.468  -0.569  11.016  1.00 17.92           C  
ANISOU  325  CB  ILE B   2     2157   1805   2845   -144   -392    350       C  
ATOM    326  CG1 ILE B   2      18.549   0.357  11.816  1.00 21.00           C  
ANISOU  326  CG1 ILE B   2     2726   2341   2910     34    146    443       C  
ATOM    327  CG2 ILE B   2      19.765  -1.882  11.742  1.00 20.97           C  
ANISOU  327  CG2 ILE B   2     3267   2299   2403    158   -182    639       C  
ATOM    328  CD1 ILE B   2      17.162  -0.049  12.220  1.00 20.50           C  
ANISOU  328  CD1 ILE B   2     2794   2233   2765   -248     79   -266       C  
ATOM    329  N   GLY B   3      22.726  -1.307  11.033  1.00 18.75           N  
ANISOU  329  N   GLY B   3     2018   2345   2760   -629   -675    138       N  
ATOM    330  CA  GLY B   3      23.893  -2.119  10.693  1.00 19.58           C  
ANISOU  330  CA  GLY B   3     1895   2800   2746   -572   -478    511       C  
ATOM    331  C   GLY B   3      24.100  -3.322  11.606  1.00 18.97           C  
ANISOU  331  C   GLY B   3     2162   2391   2656   -621   -724    238       C  
ATOM    332  O   GLY B   3      25.150  -3.961  11.583  1.00 23.57           O  
ANISOU  332  O   GLY B   3     2416   2505   4035   -441   -243    684       O  
ATOM    333  N   ASP B   4      23.115  -3.684  12.436  1.00 18.20           N  
ANISOU  333  N   ASP B   4     2467   1732   2717   -650   -516     52       N  
ATOM    334  CA  ASP B   4      23.258  -4.845  13.335  1.00 18.14           C  
ANISOU  334  CA  ASP B   4     2185   2196   2511   -456   -595    175       C  
ATOM    335  C   ASP B   4      21.897  -5.483  13.522  1.00 14.84           C  
ANISOU  335  C   ASP B   4     2077   1663   1897   -276   -453   -108       C  
ATOM    336  O   ASP B   4      20.861  -4.794  13.480  1.00 16.48           O  
ANISOU  336  O   ASP B   4     2278   1835   2149    -11   -302    152       O  
ATOM    337  CB  ASP B   4      23.903  -4.472  14.659  1.00 19.95           C  
ANISOU  337  CB  ASP B   4     1746   2719   3117     44  -1063   -157       C  
ATOM    338  CG  ASP B   4      22.989  -3.758  15.635  1.00 23.29           C  
ANISOU  338  CG  ASP B   4     2782   2861   3206   -507   -539   -694       C  
ATOM    339  OD1 ASP B   4      22.974  -2.498  15.590  1.00 25.14           O  
ANISOU  339  OD1 ASP B   4     3176   2855   3520   -111   -725   -711       O  
ATOM    340  OD2 ASP B   4      22.332  -4.440  16.451  1.00 24.96           O  
ANISOU  340  OD2 ASP B   4     3325   3588   2570    122   -645     85       O  
ATOM    341  N   PRO B   5      21.865  -6.795  13.734  1.00 15.78           N  
ANISOU  341  N   PRO B   5     2064   1751   2182    -88   -557     99       N  
ATOM    342  CA  PRO B   5      20.562  -7.467  13.795  1.00 15.27           C  
ANISOU  342  CA  PRO B   5     2153   1537   2114   -161   -359    -12       C  
ATOM    343  C   PRO B   5      19.675  -7.103  14.986  1.00 15.63           C  
ANISOU  343  C   PRO B   5     2108   1758   2072    -19   -484     47       C  
ATOM    344  O   PRO B   5      18.438  -7.011  14.825  1.00 16.31           O  
ANISOU  344  O   PRO B   5     2086   1852   2260    -69   -441    -45       O  
ATOM    345  CB  PRO B   5      20.965  -8.927  13.876  1.00 19.89           C  
ANISOU  345  CB  PRO B   5     2545   1624   3389     58    -49      1       C  
ATOM    346  CG  PRO B   5      22.403  -9.084  13.611  1.00 20.61           C  
ANISOU  346  CG  PRO B   5     2465   1883   3481    160   -286    138       C  
ATOM    347  CD  PRO B   5      22.995  -7.744  13.875  1.00 15.55           C  
ANISOU  347  CD  PRO B   5     2195   2107   1608    204   -418   -224       C  
ATOM    348  N   VAL B   6      20.199  -6.859  16.174  1.00 15.82           N  
ANISOU  348  N   VAL B   6     2176   1974   1859   -299   -344    286       N  
ATOM    349  CA  VAL B   6      19.374  -6.545  17.354  1.00 15.55           C  
ANISOU  349  CA  VAL B   6     1934   1888   2085   -440   -249    202       C  
ATOM    350  C   VAL B   6      18.647  -5.213  17.208  1.00 15.84           C  
ANISOU  350  C   VAL B   6     2155   1824   2041   -425   -553    -98       C  
ATOM    351  O   VAL B   6      17.470  -5.115  17.508  1.00 17.70           O  
ANISOU  351  O   VAL B   6     2259   2212   2253    -57   -496    -85       O  
ATOM    352  CB  VAL B   6      20.234  -6.615  18.623  1.00 17.17           C  
ANISOU  352  CB  VAL B   6     2668   2035   1820   -367   -280    503       C  
ATOM    353  CG1 VAL B   6      19.506  -6.073  19.843  1.00 20.78           C  
ANISOU  353  CG1 VAL B   6     3457   2476   1962    161   -228    389       C  
ATOM    354  CG2 VAL B   6      20.691  -8.056  18.846  1.00 19.18           C  
ANISOU  354  CG2 VAL B   6     2499   2133   2657   -173   -646    260       C  
ATOM    355  N   THR B   7      19.337  -4.190  16.699  1.00 17.04           N  
ANISOU  355  N   THR B   7     2737   1859   1879   -388   -557    112       N  
ATOM    356  CA  THR B   7      18.745  -2.891  16.426  1.00 15.89           C  
ANISOU  356  CA  THR B   7     2356   1909   1773   -435   -408      8       C  
ATOM    357  C   THR B   7      17.607  -3.032  15.421  1.00 15.71           C  
ANISOU  357  C   THR B   7     2197   1758   2012   -285   -366   -215       C  
ATOM    358  O   THR B   7      16.499  -2.492  15.635  1.00 17.24           O  
ANISOU  358  O   THR B   7     2414   1731   2406     -3   -438   -335       O  
ATOM    359  CB  THR B   7      19.831  -1.895  15.974  1.00 15.28           C  
ANISOU  359  CB  THR B   7     2215   1718   1873   -290   -319   -137       C  
ATOM    360  OG1 THR B   7      20.769  -1.733  17.051  1.00 17.94           O  
ANISOU  360  OG1 THR B   7     2366   1963   2486   -424   -656   -178       O  
ATOM    361  CG2 THR B   7      19.214  -0.534  15.730  1.00 18.87           C  
ANISOU  361  CG2 THR B   7     2662   1772   2736   -150   -357     64       C  
ATOM    362  N   CYS B   8      17.871  -3.789  14.351  1.00 13.96           N  
ANISOU  362  N   CYS B   8     1875   1624   1804   -254   -321     44       N  
ATOM    363  CA  CYS B   8      16.835  -4.058  13.344  1.00 13.63           C  
ANISOU  363  CA  CYS B   8     1987   1250   1942   -198   -454     98       C  
ATOM    364  C   CYS B   8      15.546  -4.591  13.991  1.00 14.83           C  
ANISOU  364  C   CYS B   8     1976   1485   2175   -378   -565    255       C  
ATOM    365  O   CYS B   8      14.430  -4.078  13.802  1.00 14.97           O  
ANISOU  365  O   CYS B   8     2049   1672   1967   -149   -349     51       O  
ATOM    366  CB  CYS B   8      17.359  -4.998  12.259  1.00 15.81           C  
ANISOU  366  CB  CYS B   8     2516   1537   1956   -135   -528    -66       C  
ATOM    367  SG  CYS B   8      16.166  -5.282  10.908  1.00 14.43           S  
ANISOU  367  SG  CYS B   8     1978   1561   1943   -400   -304     76       S  
ATOM    368  N   LEU B   9      15.686  -5.671  14.746  1.00 14.44           N  
ANISOU  368  N   LEU B   9     1896   1564   2027   -237   -234    170       N  
ATOM    369  CA  LEU B   9      14.546  -6.378  15.377  1.00 14.23           C  
ANISOU  369  CA  LEU B   9     1974   1598   1836   -236   -147     82       C  
ATOM    370  C   LEU B   9      13.862  -5.528  16.439  1.00 15.18           C  
ANISOU  370  C   LEU B   9     2040   1749   1976    -85   -227    -20       C  
ATOM    371  O   LEU B   9      12.616  -5.533  16.515  1.00 16.28           O  
ANISOU  371  O   LEU B   9     2080   1933   2175   -265     75    -70       O  
ATOM    372  CB  LEU B   9      15.036  -7.722  15.891  1.00 14.64           C  
ANISOU  372  CB  LEU B   9     2319   1583   1659   -209   -253     89       C  
ATOM    373  CG  LEU B   9      15.471  -8.728  14.802  1.00 16.12           C  
ANISOU  373  CG  LEU B   9     2359   1821   1946     56   -591   -255       C  
ATOM    374  CD1 LEU B   9      16.296  -9.864  15.390  1.00 16.92           C  
ANISOU  374  CD1 LEU B   9     2648   1972   1807    210   -476   -174       C  
ATOM    375  CD2 LEU B   9      14.256  -9.272  14.041  1.00 17.37           C  
ANISOU  375  CD2 LEU B   9     2373   1712   2514     20   -672   -302       C  
ATOM    376  N   LYS B  10      14.646  -4.808  17.239  1.00 17.09           N  
ANISOU  376  N   LYS B  10     2171   2115   2209   -210     16   -400       N  
ATOM    377  CA  LYS B  10      14.086  -3.937  18.263  1.00 19.68           C  
ANISOU  377  CA  LYS B  10     2524   2475   2479     44    -71   -707       C  
ATOM    378  C   LYS B  10      13.171  -2.870  17.680  1.00 20.19           C  
ANISOU  378  C   LYS B  10     2702   2791   2177    302    -99   -847       C  
ATOM    379  O   LYS B  10      12.210  -2.468  18.353  1.00 22.90           O  
ANISOU  379  O   LYS B  10     2877   3015   2809    497    510    -46       O  
ATOM    380  CB  LYS B  10      15.173  -3.293  19.113  1.00 19.81           C  
ANISOU  380  CB  LYS B  10     2671   2372   2482    156   -222   -689       C  
ATOM    381  CG  LYS B  10      15.610  -4.178  20.271  1.00 20.60           C  
ANISOU  381  CG  LYS B  10     2567   2940   2319   -160     59   -303       C  
ATOM    382  CD  LYS B  10      16.478  -3.341  21.199  1.00 24.23           C  
ANISOU  382  CD  LYS B  10     3467   3076   2664     26   -609   -452       C  
ATOM    383  CE  LYS B  10      16.815  -4.130  22.456  1.00 29.82           C  
ANISOU  383  CE  LYS B  10     4989   3183   3157   -986  -1377     18       C  
ATOM    384  NZ  LYS B  10      17.533  -3.239  23.434  1.00 37.16           N  
ANISOU  384  NZ  LYS B  10     5149   5799   3172   -989  -1415  -1202       N  
ATOM    385  N   SER B  11      13.475  -2.442  16.461  1.00 18.65           N  
ANISOU  385  N   SER B  11     2273   2119   2696   -204    224   -489       N  
ATOM    386  CA  SER B  11      12.638  -1.433  15.816  1.00 19.43           C  
ANISOU  386  CA  SER B  11     2387   2204   2790   -124    175   -515       C  
ATOM    387  C   SER B  11      11.346  -1.990  15.221  1.00 20.29           C  
ANISOU  387  C   SER B  11     2507   2034   3171    -87    -78   -381       C  
ATOM    388  O   SER B  11      10.513  -1.187  14.766  1.00 21.63           O  
ANISOU  388  O   SER B  11     2875   1927   3418    -82   -417   -327       O  
ATOM    389  CB  SER B  11      13.418  -0.714  14.719  1.00 19.63           C  
ANISOU  389  CB  SER B  11     2641   1925   2894   -119    176   -451       C  
ATOM    390  OG  SER B  11      13.524  -1.449  13.547  1.00 17.41           O  
ANISOU  390  OG  SER B  11     2415   1894   2307     30   -442    -52       O  
ATOM    391  N   GLY B  12      11.217  -3.309  15.190  1.00 17.33           N  
ANISOU  391  N   GLY B  12     2326   1989   2270    -12     19   -329       N  
ATOM    392  CA  GLY B  12      10.066  -3.953  14.598  1.00 19.24           C  
ANISOU  392  CA  GLY B  12     2347   2368   2597   -322    101   -295       C  
ATOM    393  C   GLY B  12      10.256  -4.358  13.148  1.00 17.26           C  
ANISOU  393  C   GLY B  12     2260   1795   2501   -459    -88   -148       C  
ATOM    394  O   GLY B  12       9.300  -4.834  12.528  1.00 20.13           O  
ANISOU  394  O   GLY B  12     2200   2460   2988   -405   -287   -366       O  
ATOM    395  N   ALA B  13      11.442  -4.182  12.573  1.00 17.12           N  
ANISOU  395  N   ALA B  13     2391   1639   2473   -576     82   -295       N  
ATOM    396  CA  ALA B  13      11.775  -4.628  11.238  1.00 15.19           C  
ANISOU  396  CA  ALA B  13     2069   1435   2267   -312   -361   -155       C  
ATOM    397  C   ALA B  13      12.250  -6.088  11.212  1.00 15.00           C  
ANISOU  397  C   ALA B  13     1923   1674   2103     13   -389     -5       C  
ATOM    398  O   ALA B  13      12.428  -6.736  12.247  1.00 15.01           O  
ANISOU  398  O   ALA B  13     2083   1548   2072   -393   -273     26       O  
ATOM    399  CB  ALA B  13      12.811  -3.706  10.611  1.00 15.91           C  
ANISOU  399  CB  ALA B  13     1967   1851   2226   -364   -249   -124       C  
ATOM    400  N   ILE B  14      12.444  -6.579   9.985  1.00 13.88           N  
ANISOU  400  N   ILE B  14     1846   1406   2023   -164   -194    155       N  
ATOM    401  CA  ILE B  14      12.719  -7.994   9.719  1.00 14.73           C  
ANISOU  401  CA  ILE B  14     1906   1561   2130   -215   -304     -9       C  
ATOM    402  C   ILE B  14      14.091  -8.203   9.081  1.00 13.52           C  
ANISOU  402  C   ILE B  14     2028   1291   1819   -220   -241    -67       C  
ATOM    403  O   ILE B  14      14.438  -7.466   8.136  1.00 14.99           O  
ANISOU  403  O   ILE B  14     1813   1733   2148     -6   -316    341       O  
ATOM    404  CB  ILE B  14      11.629  -8.578   8.793  1.00 15.42           C  
ANISOU  404  CB  ILE B  14     2098   1670   2091   -533   -372    193       C  
ATOM    405  CG1 ILE B  14      10.199  -8.357   9.292  1.00 19.37           C  
ANISOU  405  CG1 ILE B  14     1997   2683   2680   -284   -558   -259       C  
ATOM    406  CG2 ILE B  14      11.841 -10.048   8.503  1.00 16.05           C  
ANISOU  406  CG2 ILE B  14     1993   1638   2469   -564   -634    216       C  
ATOM    407  CD1 ILE B  14       9.213  -8.103   8.182  1.00 31.96           C  
ANISOU  407  CD1 ILE B  14     2819   4422   4903   -203  -1748   1470       C  
ATOM    408  N   CYS B  15      14.892  -9.133   9.551  1.00 13.00           N  
ANISOU  408  N   CYS B  15     1674   1514   1752   -433   -347    151       N  
ATOM    409  CA  CYS B  15      16.164  -9.413   8.902  1.00 12.73           C  
ANISOU  409  CA  CYS B  15     1768   1417   1653   -429   -176    282       C  
ATOM    410  C   CYS B  15      16.037 -10.511   7.828  1.00 14.35           C  
ANISOU  410  C   CYS B  15     1980   1515   1958   -288   -319    100       C  
ATOM    411  O   CYS B  15      15.670 -11.653   8.136  1.00 14.82           O  
ANISOU  411  O   CYS B  15     1786   1508   2336   -341   -505    105       O  
ATOM    412  CB  CYS B  15      17.207  -9.864   9.900  1.00 13.63           C  
ANISOU  412  CB  CYS B  15     1885   1436   1858   -107   -227    108       C  
ATOM    413  SG  CYS B  15      17.857  -8.686  11.115  1.00 15.67           S  
ANISOU  413  SG  CYS B  15     2153   1774   2026   -382   -549    155       S  
ATOM    414  N   HIS B  16      16.400 -10.205   6.601  1.00 15.56           N  
ANISOU  414  N   HIS B  16     2297   1806   1808   -334   -357    -58       N  
ATOM    415  CA  HIS B  16      16.404 -11.135   5.478  1.00 15.51           C  
ANISOU  415  CA  HIS B  16     2188   1652   2052     14   -527   -155       C  
ATOM    416  C   HIS B  16      17.838 -11.456   5.071  1.00 17.18           C  
ANISOU  416  C   HIS B  16     2220   1962   2344   -109   -238    -58       C  
ATOM    417  O   HIS B  16      18.717 -10.566   5.169  1.00 18.14           O  
ANISOU  417  O   HIS B  16     2394   2023   2474   -230   -214    -10       O  
ATOM    418  CB  HIS B  16      15.567 -10.550   4.327  1.00 16.76           C  
ANISOU  418  CB  HIS B  16     2278   2404   1685    -51   -297     49       C  
ATOM    419  CG  HIS B  16      14.085 -10.704   4.493  1.00 17.23           C  
ANISOU  419  CG  HIS B  16     2132   2147   2267    -21   -543   -197       C  
ATOM    420  ND1 HIS B  16      13.344 -11.676   3.869  1.00 19.76           N  
ANISOU  420  ND1 HIS B  16     2573   2029   2905    -99   -666   -191       N  
ATOM    421  CD2 HIS B  16      13.209  -9.987   5.260  1.00 16.02           C  
ANISOU  421  CD2 HIS B  16     2163   1879   2047   -123   -305    237       C  
ATOM    422  CE1 HIS B  16      12.081 -11.556   4.221  1.00 20.23           C  
ANISOU  422  CE1 HIS B  16     2358   2797   2531   -459   -881    102       C  
ATOM    423  NE2 HIS B  16      11.959 -10.542   5.078  1.00 19.07           N  
ANISOU  423  NE2 HIS B  16     2126   2565   2556   -146   -417    363       N  
ATOM    424  N   PRO B  17      18.155 -12.681   4.652  1.00 17.18           N  
ANISOU  424  N   PRO B  17     2064   2081   2383    -13   -362   -253       N  
ATOM    425  CA  PRO B  17      19.552 -13.019   4.364  1.00 19.72           C  
ANISOU  425  CA  PRO B  17     2268   2446   2780    100    -68    -95       C  
ATOM    426  C   PRO B  17      20.142 -12.390   3.112  1.00 20.49           C  
ANISOU  426  C   PRO B  17     2627   2919   2240    150    -18   -394       C  
ATOM    427  O   PRO B  17      21.381 -12.224   3.050  1.00 23.19           O  
ANISOU  427  O   PRO B  17     2768   3757   2288   -343    -35    -28       O  
ATOM    428  CB  PRO B  17      19.533 -14.549   4.216  1.00 19.78           C  
ANISOU  428  CB  PRO B  17     2453   2481   2582    362   -650   -464       C  
ATOM    429  CG  PRO B  17      18.137 -14.829   3.734  1.00 21.06           C  
ANISOU  429  CG  PRO B  17     2421   2391   3190    703   -922   -812       C  
ATOM    430  CD  PRO B  17      17.273 -13.858   4.483  1.00 17.65           C  
ANISOU  430  CD  PRO B  17     2402   2010   2294    -46    -84   -341       C  
ATOM    431  N   VAL B  18      19.324 -12.042   2.117  1.00 22.40           N  
ANISOU  431  N   VAL B  18     2894   3331   2287    470    -55   -440       N  
ATOM    432  CA  VAL B  18      19.898 -11.530   0.875  1.00 22.92           C  
ANISOU  432  CA  VAL B  18     2612   3904   2191    315   -315   -368       C  
ATOM    433  C   VAL B  18      19.080 -10.394   0.274  1.00 22.02           C  
ANISOU  433  C   VAL B  18     2344   3717   2307     45   -167   -178       C  
ATOM    434  O   VAL B  18      19.695  -9.460  -0.221  1.00 23.01           O  
ANISOU  434  O   VAL B  18     2620   3922   2202   -318   -287   -228       O  
ATOM    435  CB  VAL B  18      20.007 -12.637  -0.196  1.00 22.77           C  
ANISOU  435  CB  VAL B  18     2629   3794   2228     74     30   -361       C  
ATOM    436  CG1 VAL B  18      20.645 -12.026  -1.431  1.00 26.38           C  
ANISOU  436  CG1 VAL B  18     2912   4596   2514   -439    362   -382       C  
ATOM    437  CG2 VAL B  18      20.791 -13.867   0.244  1.00 29.06           C  
ANISOU  437  CG2 VAL B  18     4131   4712   2197   1367      3   -619       C  
ATOM    438  N   PHE B  19      17.764 -10.393   0.240  1.00 20.58           N  
ANISOU  438  N   PHE B  19     2342   3229   2248     59   -198   -471       N  
ATOM    439  CA  PHE B  19      16.907  -9.393  -0.386  1.00 21.28           C  
ANISOU  439  CA  PHE B  19     2599   3146   2342    181   -448   -686       C  
ATOM    440  C   PHE B  19      15.652  -9.099   0.453  1.00 17.74           C  
ANISOU  440  C   PHE B  19     2481   2651   1609    118   -669   -241       C  
ATOM    441  O   PHE B  19      15.058 -10.037   0.996  1.00 20.73           O  
ANISOU  441  O   PHE B  19     3114   2724   2039    173   -516     64       O  
ATOM    442  CB  PHE B  19      16.362  -9.825  -1.743  1.00 26.06           C  
ANISOU  442  CB  PHE B  19     3339   4590   1972    481   -404   -793       C  
ATOM    443  CG  PHE B  19      17.330 -10.201  -2.830  1.00 30.15           C  
ANISOU  443  CG  PHE B  19     3052   6097   2306    777   -467   -973       C  
ATOM    444  CD1 PHE B  19      17.577 -11.545  -3.096  1.00 33.78           C  
ANISOU  444  CD1 PHE B  19     3411   6565   2858   1667   -575  -1487       C  
ATOM    445  CD2 PHE B  19      17.991  -9.255  -3.573  1.00 34.12           C  
ANISOU  445  CD2 PHE B  19     3329   7485   2152   1185   -278    151       C  
ATOM    446  CE1 PHE B  19      18.461 -11.945  -4.059  1.00 35.11           C  
ANISOU  446  CE1 PHE B  19     3362   7144   2836   1235   -470  -1560       C  
ATOM    447  CE2 PHE B  19      18.880  -9.640  -4.567  1.00 37.65           C  
ANISOU  447  CE2 PHE B  19     4027   7746   2533    921     56   -549       C  
ATOM    448  CZ  PHE B  19      19.116 -10.978  -4.807  1.00 37.91           C  
ANISOU  448  CZ  PHE B  19     3980   7872   2553    803   -792  -1160       C  
ATOM    449  N   CYS B  20      15.218  -7.846   0.552  1.00 18.17           N  
ANISOU  449  N   CYS B  20     2499   2642   1763    -20   -255   -260       N  
ATOM    450  CA  CYS B  20      13.920  -7.541   1.140  1.00 18.04           C  
ANISOU  450  CA  CYS B  20     2277   2450   2127   -118   -383   -161       C  
ATOM    451  C   CYS B  20      12.781  -8.062   0.271  1.00 19.62           C  
ANISOU  451  C   CYS B  20     2554   2756   2143   -167   -503   -307       C  
ATOM    452  O   CYS B  20      12.899  -8.123  -0.955  1.00 20.07           O  
ANISOU  452  O   CYS B  20     2757   2722   2148    147   -526   -246       O  
ATOM    453  CB  CYS B  20      13.731  -6.031   1.387  1.00 16.87           C  
ANISOU  453  CB  CYS B  20     2193   2396   1820    -41   -419     15       C  
ATOM    454  SG  CYS B  20      14.770  -5.237   2.627  1.00 17.30           S  
ANISOU  454  SG  CYS B  20     2321   2071   2182   -305   -525    223       S  
ATOM    455  N   PRO B  21      11.657  -8.446   0.849  1.00 18.50           N  
ANISOU  455  N   PRO B  21     2575   2354   2101   -377   -729   -127       N  
ATOM    456  CA  PRO B  21      10.466  -8.715   0.028  1.00 19.99           C  
ANISOU  456  CA  PRO B  21     2702   2487   2405   -355   -825   -293       C  
ATOM    457  C   PRO B  21      10.180  -7.480  -0.848  1.00 21.03           C  
ANISOU  457  C   PRO B  21     2603   2744   2645     -8   -907   -149       C  
ATOM    458  O   PRO B  21      10.497  -6.346  -0.492  1.00 21.76           O  
ANISOU  458  O   PRO B  21     2887   2674   2706   -281  -1001    149       O  
ATOM    459  CB  PRO B  21       9.361  -8.935   1.051  1.00 22.98           C  
ANISOU  459  CB  PRO B  21     2371   3180   3179     39   -670    259       C  
ATOM    460  CG  PRO B  21      10.083  -9.455   2.241  1.00 24.13           C  
ANISOU  460  CG  PRO B  21     2619   3746   2803   -764   -735    441       C  
ATOM    461  CD  PRO B  21      11.374  -8.656   2.280  1.00 21.42           C  
ANISOU  461  CD  PRO B  21     2938   3006   2196   -804   -567    -71       C  
ATOM    462  N   ARG B  22       9.602  -7.716  -2.011  1.00 23.03           N  
ANISOU  462  N   ARG B  22     2875   3329   2547   -106   -917   -172       N  
ATOM    463  CA  ARG B  22       9.280  -6.713  -3.009  1.00 27.84           C  
ANISOU  463  CA  ARG B  22     4589   3423   2566   -152  -1322   -144       C  
ATOM    464  C   ARG B  22       8.721  -5.391  -2.490  1.00 27.29           C  
ANISOU  464  C   ARG B  22     4114   2999   3256   -503   -763    224       C  
ATOM    465  O   ARG B  22       9.236  -4.373  -2.981  1.00 27.91           O  
ANISOU  465  O   ARG B  22     4005   3385   3212   -864  -1123    405       O  
ATOM    466  CB  ARG B  22       8.223  -7.254  -4.003  1.00 34.28           C  
ANISOU  466  CB  ARG B  22     5737   4477   2813   -171  -2159   -278       C  
ATOM    467  CG  ARG B  22       7.512  -6.202  -4.807  1.00 42.64           C  
ANISOU  467  CG  ARG B  22     6076   5756   4370    379  -2732    340       C  
ATOM    468  CD  ARG B  22       6.662  -6.748  -5.952  1.00 51.44           C  
ANISOU  468  CD  ARG B  22     6493   8377   4674    313  -3461    301       C  
ATOM    469  NE  ARG B  22       5.746  -5.740  -6.479  1.00 54.77           N  
ANISOU  469  NE  ARG B  22     6242   9173   5394    847  -3233    340       N  
ATOM    470  CZ  ARG B  22       4.534  -5.460  -6.008  1.00 61.82           C  
ANISOU  470  CZ  ARG B  22     7126   9916   6446   1369  -2284   -313       C  
ATOM    471  NH1 ARG B  22       4.046  -6.118  -4.958  1.00 73.84           N  
ANISOU  471  NH1 ARG B  22     9374  11249   7435    126   -433   -656       N  
ATOM    472  NH2 ARG B  22       3.787  -4.514  -6.573  1.00 69.90           N  
ANISOU  472  NH2 ARG B  22     9367   9162   8029   3574  -2296  -2229       N  
ATOM    473  N   ARG B  23       7.699  -5.371  -1.629  1.00 24.22           N  
ANISOU  473  N   ARG B  23     3390   3215   2596   -582  -1429    127       N  
ATOM    474  CA  ARG B  23       7.059  -4.146  -1.133  1.00 25.79           C  
ANISOU  474  CA  ARG B  23     3719   3077   3004   -391   -927    565       C  
ATOM    475  C   ARG B  23       7.659  -3.576   0.150  1.00 26.08           C  
ANISOU  475  C   ARG B  23     3617   2847   3446    278  -1006    -62       C  
ATOM    476  O   ARG B  23       7.235  -2.492   0.624  1.00 30.26           O  
ANISOU  476  O   ARG B  23     3307   3399   4793    635  -1036   -643       O  
ATOM    477  CB  ARG B  23       5.572  -4.364  -0.869  1.00 29.38           C  
ANISOU  477  CB  ARG B  23     3795   4098   3270   -553   -646   -144       C  
ATOM    478  CG  ARG B  23       4.589  -4.249  -1.996  1.00 36.93           C  
ANISOU  478  CG  ARG B  23     3715   5991   4325   -576  -1087    831       C  
ATOM    479  CD  ARG B  23       3.118  -4.316  -1.610  1.00 41.25           C  
ANISOU  479  CD  ARG B  23     3838   7094   4742  -1602   -981    455       C  
ATOM    480  NE  ARG B  23       2.740  -5.674  -1.225  1.00 49.44           N  
ANISOU  480  NE  ARG B  23     5170   7458   6158  -2339  -1157    776       N  
ATOM    481  CZ  ARG B  23       2.377  -6.129  -0.033  1.00 51.39           C  
ANISOU  481  CZ  ARG B  23     5803   7180   6541  -2829   -683    760       C  
ATOM    482  NH1 ARG B  23       2.297  -5.357   1.054  1.00 49.99           N  
ANISOU  482  NH1 ARG B  23     4879   7997   6119  -2110  -1327    729       N  
ATOM    483  NH2 ARG B  23       2.077  -7.426   0.088  1.00 57.70           N  
ANISOU  483  NH2 ARG B  23     7401   6526   7996  -1370  -1641   1733       N  
ATOM    484  N   TYR B  24       8.618  -4.266   0.755  1.00 24.24           N  
ANISOU  484  N   TYR B  24     2833   2639   3737     25  -1112   -648       N  
ATOM    485  CA  TYR B  24       9.225  -3.785   1.999  1.00 21.54           C  
ANISOU  485  CA  TYR B  24     2454   2264   3468    223   -677   -698       C  
ATOM    486  C   TYR B  24      10.319  -2.772   1.720  1.00 20.67           C  
ANISOU  486  C   TYR B  24     2995   2849   2011   -234  -1166     81       C  
ATOM    487  O   TYR B  24      10.956  -2.841   0.665  1.00 26.22           O  
ANISOU  487  O   TYR B  24     4963   2359   2640    -74    -68    215       O  
ATOM    488  CB  TYR B  24       9.759  -4.971   2.817  1.00 20.21           C  
ANISOU  488  CB  TYR B  24     2263   2286   3128   -107   -321   -433       C  
ATOM    489  CG  TYR B  24       8.678  -5.695   3.567  1.00 24.62           C  
ANISOU  489  CG  TYR B  24     3082   3559   2714   -934    -50   -785       C  
ATOM    490  CD1 TYR B  24       7.519  -6.055   2.899  1.00 29.09           C  
ANISOU  490  CD1 TYR B  24     2918   4945   3191  -1396     99   -830       C  
ATOM    491  CD2 TYR B  24       8.752  -6.004   4.915  1.00 32.58           C  
ANISOU  491  CD2 TYR B  24     4967   4308   3104  -1909   -483     21       C  
ATOM    492  CE1 TYR B  24       6.491  -6.706   3.521  1.00 36.46           C  
ANISOU  492  CE1 TYR B  24     4388   5080   4384  -2666      2   -239       C  
ATOM    493  CE2 TYR B  24       7.707  -6.670   5.561  1.00 39.67           C  
ANISOU  493  CE2 TYR B  24     5717   5412   3944  -2108    -76   1014       C  
ATOM    494  CZ  TYR B  24       6.585  -7.017   4.859  1.00 42.14           C  
ANISOU  494  CZ  TYR B  24     5534   5736   4742  -2920    298    664       C  
ATOM    495  OH  TYR B  24       5.510  -7.668   5.414  1.00 53.88           O  
ANISOU  495  OH  TYR B  24     7089   7734   5650  -4306   1648   -153       O  
ATOM    496  N   LYS B  25      10.529  -1.823   2.618  1.00 19.59           N  
ANISOU  496  N   LYS B  25     2481   2372   2588    -67   -877      2       N  
ATOM    497  CA  LYS B  25      11.547  -0.782   2.477  1.00 19.92           C  
ANISOU  497  CA  LYS B  25     2573   2470   2526   -163   -760    312       C  
ATOM    498  C   LYS B  25      12.824  -1.234   3.191  1.00 17.52           C  
ANISOU  498  C   LYS B  25     2605   1944   2110   -172   -840   -157       C  
ATOM    499  O   LYS B  25      12.812  -1.663   4.333  1.00 19.89           O  
ANISOU  499  O   LYS B  25     2627   2488   2442   -152   -693    304       O  
ATOM    500  CB  LYS B  25      11.067   0.563   2.989  1.00 23.86           C  
ANISOU  500  CB  LYS B  25     3219   2120   3726    127  -1214    593       C  
ATOM    501  CG  LYS B  25      11.969   1.620   3.568  1.00 37.33           C  
ANISOU  501  CG  LYS B  25     5402   2572   6209   -528  -1738   -422       C  
ATOM    502  CD  LYS B  25      11.204   2.828   4.112  1.00 50.42           C  
ANISOU  502  CD  LYS B  25     7582   3502   8074     94  -1608  -1823       C  
ATOM    503  CE  LYS B  25      11.058   2.924   5.617  1.00 54.34           C  
ANISOU  503  CE  LYS B  25     8224   4243   8180    538   -619  -1728       C  
ATOM    504  NZ  LYS B  25      11.041   4.319   6.148  1.00 46.65           N  
ANISOU  504  NZ  LYS B  25     6217   4078   7432   -636    -57  -1477       N  
ATOM    505  N   GLN B  26      13.980  -1.174   2.525  1.00 17.92           N  
ANISOU  505  N   GLN B  26     2740   1902   2166    135   -684    -63       N  
ATOM    506  CA  GLN B  26      15.259  -1.421   3.140  1.00 17.77           C  
ANISOU  506  CA  GLN B  26     2554   2049   2149   -288   -583    131       C  
ATOM    507  C   GLN B  26      15.711  -0.227   3.976  1.00 17.30           C  
ANISOU  507  C   GLN B  26     2656   1772   2146   -409   -439    325       C  
ATOM    508  O   GLN B  26      15.840   0.880   3.472  1.00 20.85           O  
ANISOU  508  O   GLN B  26     3424   1902   2596   -399   -732    576       O  
ATOM    509  CB  GLN B  26      16.329  -1.760   2.089  1.00 19.54           C  
ANISOU  509  CB  GLN B  26     2753   2411   2260   -111   -413    139       C  
ATOM    510  CG  GLN B  26      17.699  -2.065   2.609  1.00 19.72           C  
ANISOU  510  CG  GLN B  26     2792   2181   2518     27   -324    450       C  
ATOM    511  CD  GLN B  26      18.790  -2.395   1.629  1.00 29.55           C  
ANISOU  511  CD  GLN B  26     3035   4043   4151     62    284   -689       C  
ATOM    512  OE1 GLN B  26      18.583  -3.001   0.582  1.00 36.41           O  
ANISOU  512  OE1 GLN B  26     4446   5650   3737   1258     77  -1046       O  
ATOM    513  NE2 GLN B  26      20.028  -2.009   1.933  1.00 47.28           N  
ANISOU  513  NE2 GLN B  26     3078   6688   8200   -902    996  -2334       N  
ATOM    514  N   ILE B  27      15.948  -0.445   5.267  1.00 15.53           N  
ANISOU  514  N   ILE B  27     2124   1587   2191   -358   -516    289       N  
ATOM    515  CA  ILE B  27      16.420   0.581   6.197  1.00 15.66           C  
ANISOU  515  CA  ILE B  27     2197   1486   2268   -494   -509    378       C  
ATOM    516  C   ILE B  27      17.802   0.298   6.777  1.00 14.70           C  
ANISOU  516  C   ILE B  27     2324   1637   1624   -353   -423    440       C  
ATOM    517  O   ILE B  27      18.351   0.983   7.664  1.00 18.44           O  
ANISOU  517  O   ILE B  27     2550   2047   2407   -323   -850     80       O  
ATOM    518  CB  ILE B  27      15.389   0.828   7.344  1.00 16.29           C  
ANISOU  518  CB  ILE B  27     2232   1459   2500   -494   -425     88       C  
ATOM    519  CG1 ILE B  27      15.128  -0.377   8.227  1.00 16.84           C  
ANISOU  519  CG1 ILE B  27     2403   1824   2173   -462   -294    209       C  
ATOM    520  CG2 ILE B  27      14.075   1.356   6.769  1.00 17.70           C  
ANISOU  520  CG2 ILE B  27     2451   1634   2642   -177   -467    -27       C  
ATOM    521  CD1 ILE B  27      14.377  -0.029   9.522  1.00 17.66           C  
ANISOU  521  CD1 ILE B  27     2004   2253   2453   -461   -262    -63       C  
ATOM    522  N   GLY B  28      18.472  -0.703   6.223  1.00 18.35           N  
ANISOU  522  N   GLY B  28     2109   1741   3122   -420   -338     12       N  
ATOM    523  CA  GLY B  28      19.867  -0.991   6.551  1.00 17.87           C  
ANISOU  523  CA  GLY B  28     2052   1940   2796   -512   -378    300       C  
ATOM    524  C   GLY B  28      20.200  -2.442   6.304  1.00 16.72           C  
ANISOU  524  C   GLY B  28     1982   1982   2388   -425   -333    402       C  
ATOM    525  O   GLY B  28      19.596  -3.103   5.444  1.00 16.43           O  
ANISOU  525  O   GLY B  28     2189   1863   2191   -481   -236    513       O  
ATOM    526  N   THR B  29      21.169  -2.952   7.036  1.00 17.32           N  
ANISOU  526  N   THR B  29     1878   2347   2355   -280   -177    459       N  
ATOM    527  CA  THR B  29      21.576  -4.360   7.001  1.00 18.30           C  
ANISOU  527  CA  THR B  29     2065   2332   2556   -206   -195    453       C  
ATOM    528  C   THR B  29      21.346  -4.969   8.360  1.00 15.79           C  
ANISOU  528  C   THR B  29     1898   1772   2331   -491   -458     69       C  
ATOM    529  O   THR B  29      20.994  -4.267   9.324  1.00 18.71           O  
ANISOU  529  O   THR B  29     2663   1925   2519   -192   -206     62       O  
ATOM    530  CB  THR B  29      23.045  -4.505   6.587  1.00 17.60           C  
ANISOU  530  CB  THR B  29     2042   2228   2418   -173   -356    429       C  
ATOM    531  OG1 THR B  29      23.875  -3.949   7.634  1.00 20.87           O  
ANISOU  531  OG1 THR B  29     2199   3321   2408   -282   -266     -8       O  
ATOM    532  CG2 THR B  29      23.394  -3.711   5.347  1.00 22.67           C  
ANISOU  532  CG2 THR B  29     2225   3808   2582    -70   -113   1025       C  
ATOM    533  N   CYS B  30      21.482  -6.268   8.513  1.00 17.07           N  
ANISOU  533  N   CYS B  30     2279   1778   2430   -577   -586      2       N  
ATOM    534  CA  CYS B  30      21.674  -7.014   9.758  1.00 17.87           C  
ANISOU  534  CA  CYS B  30     1915   2095   2780   -157   -372    387       C  
ATOM    535  C   CYS B  30      23.074  -7.562  10.000  1.00 18.20           C  
ANISOU  535  C   CYS B  30     1916   2217   2783      7     98    371       C  
ATOM    536  O   CYS B  30      23.405  -8.613  10.524  1.00 18.66           O  
ANISOU  536  O   CYS B  30     2217   2254   2621     -2   -581    298       O  
ATOM    537  CB  CYS B  30      20.620  -8.122   9.891  1.00 18.44           C  
ANISOU  537  CB  CYS B  30     2044   2109   2854   -200   -432    531       C  
ATOM    538  SG  CYS B  30      18.932  -7.368   9.975  1.00 15.27           S  
ANISOU  538  SG  CYS B  30     1986   1681   2134   -362   -484    117       S  
ATOM    539  N   GLY B  31      24.083  -6.787   9.684  1.00 18.97           N  
ANISOU  539  N   GLY B  31     1902   2882   2422   -441   -667    530       N  
ATOM    540  CA  GLY B  31      25.488  -6.897   9.941  1.00 22.03           C  
ANISOU  540  CA  GLY B  31     1976   3081   3315   -283   -994     58       C  
ATOM    541  C   GLY B  31      26.245  -7.799   8.992  1.00 20.59           C  
ANISOU  541  C   GLY B  31     1917   2887   3020   -356   -796    385       C  
ATOM    542  O   GLY B  31      27.190  -7.323   8.341  1.00 20.64           O  
ANISOU  542  O   GLY B  31     2301   2783   2757   -622   -879    528       O  
ATOM    543  N   LEU B  32      25.861  -9.083   8.964  1.00 19.93           N  
ANISOU  543  N   LEU B  32     1820   2980   2774   -548   -508    293       N  
ATOM    544  CA  LEU B  32      26.559 -10.051   8.108  1.00 20.86           C  
ANISOU  544  CA  LEU B  32     2125   3239   2561   -455   -816     33       C  
ATOM    545  C   LEU B  32      26.496  -9.623   6.653  1.00 22.59           C  
ANISOU  545  C   LEU B  32     2101   3876   2606   -680   -687    214       C  
ATOM    546  O   LEU B  32      25.505  -9.037   6.213  1.00 22.54           O  
ANISOU  546  O   LEU B  32     2685   3422   2458   -255   -506    297       O  
ATOM    547  CB  LEU B  32      25.961 -11.443   8.271  1.00 20.75           C  
ANISOU  547  CB  LEU B  32     2124   3235   2527   -317   -522   -120       C  
ATOM    548  CG  LEU B  32      26.191 -12.240   9.556  1.00 19.73           C  
ANISOU  548  CG  LEU B  32     1834   2907   2756     38   -198    -43       C  
ATOM    549  CD1 LEU B  32      25.331 -13.520   9.505  1.00 24.09           C  
ANISOU  549  CD1 LEU B  32     2279   3952   2923   -905    -32    123       C  
ATOM    550  CD2 LEU B  32      27.657 -12.570   9.785  1.00 19.94           C  
ANISOU  550  CD2 LEU B  32     1919   1870   3788     56   -319    -95       C  
ATOM    551  N   PRO B  33      27.508  -9.924   5.858  1.00 25.84           N  
ANISOU  551  N   PRO B  33     1967   5091   2761   -645   -653     17       N  
ATOM    552  CA  PRO B  33      27.427  -9.654   4.425  1.00 29.24           C  
ANISOU  552  CA  PRO B  33     2305   6041   2763    219   -451     53       C  
ATOM    553  C   PRO B  33      26.157 -10.133   3.726  1.00 24.54           C  
ANISOU  553  C   PRO B  33     2157   5248   1919    362   -115     82       C  
ATOM    554  O   PRO B  33      25.738 -11.285   3.875  1.00 29.39           O  
ANISOU  554  O   PRO B  33     2351   5391   3424    282   -544    805       O  
ATOM    555  CB  PRO B  33      28.581 -10.479   3.815  1.00 33.93           C  
ANISOU  555  CB  PRO B  33     2337   7464   3090    904   -637   -167       C  
ATOM    556  CG  PRO B  33      29.569 -10.579   4.933  1.00 33.13           C  
ANISOU  556  CG  PRO B  33     2672   7029   2887    748   -700   -360       C  
ATOM    557  CD  PRO B  33      28.811 -10.506   6.229  1.00 29.48           C  
ANISOU  557  CD  PRO B  33     2285   5831   3084   -140   -482    468       C  
ATOM    558  N   GLY B  34      25.563  -9.257   2.930  1.00 25.00           N  
ANISOU  558  N   GLY B  34     2396   4593   2511    396   -405   -212       N  
ATOM    559  CA  GLY B  34      24.378  -9.522   2.166  1.00 23.35           C  
ANISOU  559  CA  GLY B  34     2330   4276   2266    499   -344    -24       C  
ATOM    560  C   GLY B  34      23.060  -9.317   2.867  1.00 21.80           C  
ANISOU  560  C   GLY B  34     2339   3724   2219    344   -417   -248       C  
ATOM    561  O   GLY B  34      21.984  -9.257   2.255  1.00 21.14           O  
ANISOU  561  O   GLY B  34     2177   3232   2624   -115   -497    242       O  
ATOM    562  N   THR B  35      23.090  -9.228   4.189  1.00 21.33           N  
ANISOU  562  N   THR B  35     2425   3491   2189    206   -210    103       N  
ATOM    563  CA  THR B  35      21.806  -9.223   4.888  1.00 18.64           C  
ANISOU  563  CA  THR B  35     2101   2645   2336   -181   -387     53       C  
ATOM    564  C   THR B  35      21.130  -7.854   4.810  1.00 18.38           C  
ANISOU  564  C   THR B  35     2123   2510   2348   -318   -317     76       C  
ATOM    565  O   THR B  35      21.736  -6.812   4.529  1.00 19.70           O  
ANISOU  565  O   THR B  35     2287   2547   2651   -354    -26   -112       O  
ATOM    566  CB  THR B  35      21.953  -9.703   6.336  1.00 16.88           C  
ANISOU  566  CB  THR B  35     1957   2373   2081    -24   -313   -356       C  
ATOM    567  OG1 THR B  35      22.878  -8.866   7.025  1.00 18.17           O  
ANISOU  567  OG1 THR B  35     2071   2421   2414   -508   -466    294       O  
ATOM    568  CG2 THR B  35      22.501 -11.119   6.443  1.00 18.51           C  
ANISOU  568  CG2 THR B  35     2127   2314   2594   -224   -116     90       C  
ATOM    569  N   LYS B  36      19.802  -7.856   5.015  1.00 16.66           N  
ANISOU  569  N   LYS B  36     2228   2225   1877   -253   -236     73       N  
ATOM    570  CA  LYS B  36      18.921  -6.719   4.814  1.00 16.15           C  
ANISOU  570  CA  LYS B  36     2077   2173   1884   -402   -427    -93       C  
ATOM    571  C   LYS B  36      17.993  -6.512   6.019  1.00 14.74           C  
ANISOU  571  C   LYS B  36     1940   1850   1811   -393   -490    125       C  
ATOM    572  O   LYS B  36      17.403  -7.480   6.481  1.00 15.02           O  
ANISOU  572  O   LYS B  36     2272   1576   1860   -344   -291   -153       O  
ATOM    573  CB  LYS B  36      18.118  -6.892   3.514  1.00 17.02           C  
ANISOU  573  CB  LYS B  36     1718   3004   1744   -541   -215    102       C  
ATOM    574  CG  LYS B  36      18.956  -7.166   2.275  1.00 19.67           C  
ANISOU  574  CG  LYS B  36     2321   3353   1798   -630     52     72       C  
ATOM    575  CD  LYS B  36      19.651  -5.908   1.805  1.00 22.45           C  
ANISOU  575  CD  LYS B  36     2680   3671   2178   -539    204    786       C  
ATOM    576  CE  LYS B  36      20.426  -6.063   0.515  1.00 23.37           C  
ANISOU  576  CE  LYS B  36     2763   3498   2620   -390    527    616       C  
ATOM    577  NZ  LYS B  36      21.393  -7.198   0.590  1.00 30.26           N  
ANISOU  577  NZ  LYS B  36     3458   4174   3864    316    -66   -120       N  
ATOM    578  N   CYS B  37      17.894  -5.271   6.509  1.00 14.68           N  
ANISOU  578  N   CYS B  37     1892   1712   1972   -459   -292    172       N  
ATOM    579  CA  CYS B  37      16.905  -4.891   7.491  1.00 13.73           C  
ANISOU  579  CA  CYS B  37     1810   1727   1679   -485   -402    353       C  
ATOM    580  C   CYS B  37      15.683  -4.237   6.781  1.00 13.95           C  
ANISOU  580  C   CYS B  37     1926   1655   1719   -410   -544    191       C  
ATOM    581  O   CYS B  37      15.867  -3.185   6.127  1.00 15.43           O  
ANISOU  581  O   CYS B  37     2311   1643   1907   -411   -587    286       O  
ATOM    582  CB  CYS B  37      17.445  -3.936   8.534  1.00 14.05           C  
ANISOU  582  CB  CYS B  37     2059   1653   1626   -356   -660    443       C  
ATOM    583  SG  CYS B  37      16.299  -3.507   9.855  1.00 15.16           S  
ANISOU  583  SG  CYS B  37     2104   1552   2104   -264   -454    177       S  
ATOM    584  N   CYS B  38      14.514  -4.840   6.864  1.00 14.74           N  
ANISOU  584  N   CYS B  38     1854   1806   1941   -396   -586      2       N  
ATOM    585  CA  CYS B  38      13.354  -4.589   5.993  1.00 14.69           C  
ANISOU  585  CA  CYS B  38     1890   1784   1907   -274   -522    307       C  
ATOM    586  C   CYS B  38      12.107  -4.221   6.772  1.00 15.57           C  
ANISOU  586  C   CYS B  38     1863   2095   1957   -220   -548    467       C  
ATOM    587  O   CYS B  38      11.735  -4.945   7.690  1.00 15.28           O  
ANISOU  587  O   CYS B  38     1915   1860   2030   -204   -416    368       O  
ATOM    588  CB  CYS B  38      13.100  -5.820   5.118  1.00 15.38           C  
ANISOU  588  CB  CYS B  38     1606   2106   2131   -473   -793    167       C  
ATOM    589  SG  CYS B  38      14.559  -6.482   4.284  1.00 16.07           S  
ANISOU  589  SG  CYS B  38     2327   1886   1894   -142   -544    145       S  
ATOM    590  N   LYS B  39      11.518  -3.081   6.383  1.00 17.43           N  
ANISOU  590  N   LYS B  39     2471   1889   2262    -35   -256    405       N  
ATOM    591  CA  LYS B  39      10.411  -2.529   7.149  1.00 18.09           C  
ANISOU  591  CA  LYS B  39     2429   2030   2414     22   -524    -53       C  
ATOM    592  C   LYS B  39       9.114  -2.556   6.353  1.00 20.88           C  
ANISOU  592  C   LYS B  39     2463   2694   2775   -187   -714   -748       C  
ATOM    593  O   LYS B  39       9.082  -2.335   5.156  1.00 22.62           O  
ANISOU  593  O   LYS B  39     2808   2933   2853    403   -947   -623       O  
ATOM    594  CB  LYS B  39      10.758  -1.094   7.542  1.00 22.47           C  
ANISOU  594  CB  LYS B  39     2669   2796   3072   -607   -360   -929       C  
ATOM    595  CG  LYS B  39       9.743  -0.369   8.377  1.00 24.78           C  
ANISOU  595  CG  LYS B  39     3371   2570   3474   -670    -61  -1196       C  
ATOM    596  CD  LYS B  39      10.156   1.083   8.555  1.00 24.20           C  
ANISOU  596  CD  LYS B  39     3403   2218   3573   -526   -525   -414       C  
ATOM    597  CE  LYS B  39       9.008   1.988   8.137  1.00 37.68           C  
ANISOU  597  CE  LYS B  39     4291   3841   6184   1275    228   -450       C  
ATOM    598  NZ  LYS B  39       8.021   2.050   9.249  1.00 47.20           N  
ANISOU  598  NZ  LYS B  39     5554   6131   6251   1463    617  -2864       N  
ATOM    599  N   LYS B  40       7.967  -2.739   6.976  1.00 30.93           N  
ANISOU  599  N   LYS B  40     2622   5404   3725  -1069   -642   -223       N  
ATOM    600  CA  LYS B  40       6.679  -2.536   6.322  1.00 35.50           C  
ANISOU  600  CA  LYS B  40     2465   6426   4596   -715   -359   1411       C  
ATOM    601  C   LYS B  40       6.430  -1.051   6.057  1.00 46.82           C  
ANISOU  601  C   LYS B  40     3427   6504   7858   -147   -109   1458       C  
ATOM    602  O   LYS B  40       6.556  -0.245   6.993  1.00 53.55           O  
ANISOU  602  O   LYS B  40     4430   6537   9379   1496  -2635    737       O  
ATOM    603  CB  LYS B  40       5.587  -3.136   7.191  1.00 42.47           C  
ANISOU  603  CB  LYS B  40     2975   7474   5688  -1399    604    524       C  
ATOM    604  CG  LYS B  40       5.736  -4.625   7.463  1.00 49.99           C  
ANISOU  604  CG  LYS B  40     5651   7886   5457  -1848    866   2087       C  
ATOM    605  CD  LYS B  40       6.323  -4.899   8.833  1.00 58.38           C  
ANISOU  605  CD  LYS B  40     7381   9234   5565   -989    186   1464       C  
ATOM    606  CE  LYS B  40       5.304  -5.270   9.890  1.00 59.46           C  
ANISOU  606  CE  LYS B  40     8125   9620   4845  -1376   -116   2032       C  
ATOM    607  NZ  LYS B  40       5.140  -6.751   9.996  1.00 62.15           N  
ANISOU  607  NZ  LYS B  40     9665   9374   4577   -926   1524   1187       N  
TER     608      LYS B  40                                                      
ATOM    609  N  AGLY C   1      11.164  27.328   6.690  0.50 53.20           N  
ANISOU  609  N  AGLY C   1     7038   5043   8131    548     -4   2088       N  
ATOM    610  N  BGLY C   1      13.313  27.645   5.320  0.50 54.48           N  
ANISOU  610  N  BGLY C   1     9318   4263   7120    428   1962   1665       N  
ATOM    611  CA AGLY C   1      12.586  27.138   6.488  0.50 48.08           C  
ANISOU  611  CA AGLY C   1     7338   4081   6850    176   1136   1539       C  
ATOM    612  CA BGLY C   1      12.591  27.136   6.477  0.50 48.44           C  
ANISOU  612  CA BGLY C   1     7536   4080   6789    249   1141   1524       C  
ATOM    613  C   GLY C   1      13.195  25.892   7.084  1.00 40.74           C  
ANISOU  613  C   GLY C   1     6266   3368   5845     42   1409    589       C  
ATOM    614  O   GLY C   1      14.374  25.586   6.883  1.00 38.64           O  
ANISOU  614  O   GLY C   1     6538   3703   4441     -2   2282    375       O  
ATOM    615  N   ILE C   2      12.389  25.156   7.837  1.00 31.49           N  
ANISOU  615  N   ILE C   2     4975   3109   3880    676    902    -82       N  
ATOM    616  CA  ILE C   2      12.869  23.952   8.518  1.00 30.63           C  
ANISOU  616  CA  ILE C   2     4904   2842   3893    457    614   -262       C  
ATOM    617  C   ILE C   2      12.330  22.724   7.794  1.00 28.74           C  
ANISOU  617  C   ILE C   2     4679   3090   3150    -15   1194    -58       C  
ATOM    618  O   ILE C   2      11.114  22.517   7.763  1.00 25.47           O  
ANISOU  618  O   ILE C   2     4499   1751   3428    863    447    703       O  
ATOM    619  CB  ILE C   2      12.464  23.970   9.992  1.00 27.85           C  
ANISOU  619  CB  ILE C   2     4669   1991   3921    456    672   -335       C  
ATOM    620  CG1 ILE C   2      13.035  25.149  10.778  1.00 28.76           C  
ANISOU  620  CG1 ILE C   2     4377   2510   4040     15    590   -308       C  
ATOM    621  CG2 ILE C   2      12.839  22.637  10.658  1.00 26.35           C  
ANISOU  621  CG2 ILE C   2     2999   2484   4528    -74   -385    172       C  
ATOM    622  CD1 ILE C   2      12.249  25.433  12.068  1.00 27.46           C  
ANISOU  622  CD1 ILE C   2     2461   3315   4659   -221    206  -1458       C  
ATOM    623  N   GLY C   3      13.267  21.969   7.221  1.00 24.55           N  
ANISOU  623  N   GLY C   3     4158   2040   3130    -14    620    472       N  
ATOM    624  CA  GLY C   3      13.016  20.819   6.403  1.00 24.58           C  
ANISOU  624  CA  GLY C   3     3792   1935   3612    136    292    412       C  
ATOM    625  C   GLY C   3      13.952  19.632   6.558  1.00 23.21           C  
ANISOU  625  C   GLY C   3     3096   2614   3109    428    830    189       C  
ATOM    626  O   GLY C   3      14.006  18.825   5.596  1.00 27.28           O  
ANISOU  626  O   GLY C   3     4793   2682   2891    763    784    342       O  
ATOM    627  N   ASP C   4      14.682  19.493   7.663  1.00 24.85           N  
ANISOU  627  N   ASP C   4     3680   2659   3102    590    706    369       N  
ATOM    628  CA  ASP C   4      15.579  18.365   7.954  1.00 25.87           C  
ANISOU  628  CA  ASP C   4     3389   3210   3231    832   1152    722       C  
ATOM    629  C   ASP C   4      15.633  18.065   9.448  1.00 22.14           C  
ANISOU  629  C   ASP C   4     2881   2327   3204   -246    556    482       C  
ATOM    630  O   ASP C   4      15.364  18.940  10.294  1.00 22.80           O  
ANISOU  630  O   ASP C   4     3034   2391   3237   -122    724    535       O  
ATOM    631  CB  ASP C   4      16.955  18.606   7.340  1.00 28.21           C  
ANISOU  631  CB  ASP C   4     3613   3373   3731    549   1332    858       C  
ATOM    632  CG  ASP C   4      17.828  19.520   8.160  1.00 31.66           C  
ANISOU  632  CG  ASP C   4     4182   3555   4293    -88   1256    959       C  
ATOM    633  OD1 ASP C   4      17.868  20.719   7.827  1.00 32.94           O  
ANISOU  633  OD1 ASP C   4     4437   3622   4457   -169   1720   1110       O  
ATOM    634  OD2 ASP C   4      18.438  19.007   9.119  1.00 27.92           O  
ANISOU  634  OD2 ASP C   4     3043   3112   4454    439   1308    275       O  
ATOM    635  N   PRO C   5      15.897  16.830   9.882  1.00 21.57           N  
ANISOU  635  N   PRO C   5     1979   2714   3501    453    701    640       N  
ATOM    636  CA  PRO C   5      15.839  16.490  11.308  1.00 21.91           C  
ANISOU  636  CA  PRO C   5     2130   2657   3537    306    502    739       C  
ATOM    637  C   PRO C   5      16.856  17.216  12.164  1.00 21.91           C  
ANISOU  637  C   PRO C   5     1872   2646   3806    513    267    845       C  
ATOM    638  O   PRO C   5      16.474  17.628  13.267  1.00 22.04           O  
ANISOU  638  O   PRO C   5     1639   2423   4314     99    442    299       O  
ATOM    639  CB  PRO C   5      16.086  14.955  11.321  1.00 25.57           C  
ANISOU  639  CB  PRO C   5     3174   2689   3853    430     78    718       C  
ATOM    640  CG  PRO C   5      15.679  14.510   9.943  1.00 25.83           C  
ANISOU  640  CG  PRO C   5     3775   2632   3409    906    702    679       C  
ATOM    641  CD  PRO C   5      16.222  15.621   9.091  1.00 23.52           C  
ANISOU  641  CD  PRO C   5     2488   2706   3743    483    504    481       C  
ATOM    642  N   VAL C   6      18.096  17.411  11.707  1.00 24.37           N  
ANISOU  642  N   VAL C   6     2344   2852   4063    -70    753    424       N  
ATOM    643  CA  VAL C   6      19.124  18.079  12.533  1.00 24.86           C  
ANISOU  643  CA  VAL C   6     1934   2783   4727    239    578    388       C  
ATOM    644  C   VAL C   6      18.666  19.513  12.806  1.00 24.91           C  
ANISOU  644  C   VAL C   6     1666   2715   5083    103    658    273       C  
ATOM    645  O   VAL C   6      18.697  19.943  13.969  1.00 26.46           O  
ANISOU  645  O   VAL C   6     1923   2792   5337    -88     30    -40       O  
ATOM    646  CB  VAL C   6      20.543  18.037  11.933  1.00 23.16           C  
ANISOU  646  CB  VAL C   6     2348   2384   4068    -50    922     16       C  
ATOM    647  CG1 VAL C   6      21.585  18.746  12.770  1.00 25.68           C  
ANISOU  647  CG1 VAL C   6     1966   2564   5226    241    343     72       C  
ATOM    648  CG2 VAL C   6      21.004  16.585  11.749  1.00 26.26           C  
ANISOU  648  CG2 VAL C   6     2578   2563   4837    291    797    -33       C  
ATOM    649  N   THR C   7      18.248  20.245  11.774  1.00 26.00           N  
ANISOU  649  N   THR C   7     2501   2290   5088   -134    817    384       N  
ATOM    650  CA  THR C   7      17.782  21.628  11.983  1.00 25.28           C  
ANISOU  650  CA  THR C   7     2760   2021   4825   -536    824    384       C  
ATOM    651  C   THR C   7      16.599  21.680  12.923  1.00 24.65           C  
ANISOU  651  C   THR C   7     2616   1904   4845   -273    691    275       C  
ATOM    652  O   THR C   7      16.508  22.557  13.802  1.00 25.49           O  
ANISOU  652  O   THR C   7     2623   2147   4914    353    143    107       O  
ATOM    653  CB  THR C   7      17.427  22.245  10.621  1.00 28.92           C  
ANISOU  653  CB  THR C   7     3617   2418   4955    -22    896    572       C  
ATOM    654  OG1 THR C   7      18.663  22.363   9.886  1.00 31.37           O  
ANISOU  654  OG1 THR C   7     4311   3050   4559     -3   1374    192       O  
ATOM    655  CG2 THR C   7      16.827  23.639  10.747  1.00 28.68           C  
ANISOU  655  CG2 THR C   7     3833   2686   4377    254    116    -37       C  
ATOM    656  N   CYS C   8      15.666  20.742  12.775  1.00 22.93           N  
ANISOU  656  N   CYS C   8     2125   2308   4277   -212    234    636       N  
ATOM    657  CA  CYS C   8      14.490  20.694  13.643  1.00 21.30           C  
ANISOU  657  CA  CYS C   8     1717   2204   4173    115    -56    219       C  
ATOM    658  C   CYS C   8      14.895  20.520  15.098  1.00 20.27           C  
ANISOU  658  C   CYS C   8     1438   2221   4043    325     17   -143       C  
ATOM    659  O   CYS C   8      14.467  21.307  15.948  1.00 21.55           O  
ANISOU  659  O   CYS C   8     2150   1609   4430    217    -38   -190       O  
ATOM    660  CB  CYS C   8      13.508  19.593  13.216  1.00 19.12           C  
ANISOU  660  CB  CYS C   8     1834   2077   3353     66    181    288       C  
ATOM    661  SG  CYS C   8      12.061  19.403  14.306  1.00 17.47           S  
ANISOU  661  SG  CYS C   8     1895   1594   3150    239    176     26       S  
ATOM    662  N   LEU C   9      15.728  19.507  15.394  1.00 18.91           N  
ANISOU  662  N   LEU C   9     1792   1786   3606    188    339     78       N  
ATOM    663  CA  LEU C   9      16.185  19.219  16.748  1.00 19.70           C  
ANISOU  663  CA  LEU C   9     2067   1760   3657    306    146   -214       C  
ATOM    664  C   LEU C   9      17.022  20.350  17.327  1.00 23.93           C  
ANISOU  664  C   LEU C   9     2374   2292   4428    -28     14   -601       C  
ATOM    665  O   LEU C   9      16.901  20.699  18.506  1.00 26.46           O  
ANISOU  665  O   LEU C   9     2540   2676   4839    269     20  -1241       O  
ATOM    666  CB  LEU C   9      16.956  17.903  16.767  1.00 20.60           C  
ANISOU  666  CB  LEU C   9     2003   2048   3777    471    -81   -165       C  
ATOM    667  CG  LEU C   9      16.138  16.649  16.476  1.00 20.91           C  
ANISOU  667  CG  LEU C   9     2552   1670   3722    531     65    -97       C  
ATOM    668  CD1 LEU C   9      17.022  15.407  16.488  1.00 29.21           C  
ANISOU  668  CD1 LEU C   9     4461   1930   4708   1394   1443    497       C  
ATOM    669  CD2 LEU C   9      14.990  16.485  17.470  1.00 24.01           C  
ANISOU  669  CD2 LEU C   9     2801   1729   4594    306    546    -17       C  
ATOM    670  N   LYS C  10      17.875  20.954  16.493  1.00 23.43           N  
ANISOU  670  N   LYS C  10     2113   1801   4988    267   -422    388       N  
ATOM    671  CA  LYS C  10      18.656  22.090  16.945  1.00 29.52           C  
ANISOU  671  CA  LYS C  10     2333   1939   6943    161   -406    -99       C  
ATOM    672  C   LYS C  10      17.739  23.224  17.411  1.00 32.03           C  
ANISOU  672  C   LYS C  10     2536   2715   6918    217   -514  -1154       C  
ATOM    673  O   LYS C  10      18.202  23.957  18.285  1.00 37.76           O  
ANISOU  673  O   LYS C  10     4534   3204   6609    229  -1122  -1106       O  
ATOM    674  CB  LYS C  10      19.557  22.643  15.843  1.00 34.04           C  
ANISOU  674  CB  LYS C  10     2177   2600   8157   -373    267   -330       C  
ATOM    675  CG  LYS C  10      20.541  21.656  15.193  1.00 40.33           C  
ANISOU  675  CG  LYS C  10     3497   3771   8055    237    536   -932       C  
ATOM    676  CD  LYS C  10      21.819  21.732  15.980  1.00 38.55           C  
ANISOU  676  CD  LYS C  10     2903   2623   9119    565    601   -663       C  
ATOM    677  CE  LYS C  10      23.057  21.061  15.448  1.00 36.76           C  
ANISOU  677  CE  LYS C  10     3024   2520   8422   -457   1817   -465       C  
ATOM    678  NZ  LYS C  10      24.177  21.873  16.061  1.00 45.22           N  
ANISOU  678  NZ  LYS C  10     2937   5947   8297    106    354  -1190       N  
ATOM    679  N   SER C  11      16.546  23.386  16.859  1.00 27.84           N  
ANISOU  679  N   SER C  11     2229   1869   6479    199     78   -262       N  
ATOM    680  CA  SER C  11      15.699  24.540  17.136  1.00 31.45           C  
ANISOU  680  CA  SER C  11     3124   1926   6897    439   -255   -827       C  
ATOM    681  C   SER C  11      14.896  24.372  18.424  1.00 32.70           C  
ANISOU  681  C   SER C  11     3311   2243   6871    521    -56  -1536       C  
ATOM    682  O   SER C  11      14.100  25.255  18.744  1.00 40.08           O  
ANISOU  682  O   SER C  11     3369   3178   8682    963    113  -2003       O  
ATOM    683  CB  SER C  11      14.735  24.788  15.967  1.00 34.58           C  
ANISOU  683  CB  SER C  11     3365   2298   7475    793   -420     50       C  
ATOM    684  OG  SER C  11      13.615  23.914  16.069  1.00 38.78           O  
ANISOU  684  OG  SER C  11     3047   2656   9031    703   -767  -1409       O  
ATOM    685  N   GLY C  12      15.117  23.240  19.089  1.00 30.61           N  
ANISOU  685  N   GLY C  12     3024   2987   5619    151   -742  -1309       N  
ATOM    686  CA  GLY C  12      14.424  22.797  20.280  1.00 31.03           C  
ANISOU  686  CA  GLY C  12     3122   4022   4648     36  -1116  -1881       C  
ATOM    687  C   GLY C  12      13.064  22.189  20.020  1.00 28.85           C  
ANISOU  687  C   GLY C  12     2971   4328   3663      8  -1036  -1188       C  
ATOM    688  O   GLY C  12      12.237  22.140  20.926  1.00 36.19           O  
ANISOU  688  O   GLY C  12     3833   6397   3520   -972   -723  -1829       O  
ATOM    689  N   ALA C  13      12.803  21.744  18.812  1.00 24.19           N  
ANISOU  689  N   ALA C  13     2421   3038   3731    180   -549  -1276       N  
ATOM    690  CA  ALA C  13      11.571  21.052  18.417  1.00 17.82           C  
ANISOU  690  CA  ALA C  13     1892   2445   2433    510   -142   -663       C  
ATOM    691  C   ALA C  13      11.808  19.547  18.328  1.00 20.58           C  
ANISOU  691  C   ALA C  13     2508   2476   2835    684   -771   -813       C  
ATOM    692  O   ALA C  13      12.917  19.045  18.495  1.00 23.08           O  
ANISOU  692  O   ALA C  13     2545   2503   3722    740   -500   -467       O  
ATOM    693  CB  ALA C  13      11.059  21.618  17.098  1.00 20.21           C  
ANISOU  693  CB  ALA C  13     2120   2976   2584    381     97    -62       C  
ATOM    694  N   ILE C  14      10.778  18.768  18.073  1.00 21.79           N  
ANISOU  694  N   ILE C  14     2562   2463   3255    675   -420  -1272       N  
ATOM    695  CA  ILE C  14      10.774  17.307  17.997  1.00 21.86           C  
ANISOU  695  CA  ILE C  14     2581   2490   3235    704   -217  -1201       C  
ATOM    696  C   ILE C  14      10.254  16.854  16.650  1.00 19.37           C  
ANISOU  696  C   ILE C  14     1852   2160   3347    198    -18  -1020       C  
ATOM    697  O   ILE C  14       9.248  17.412  16.235  1.00 19.21           O  
ANISOU  697  O   ILE C  14     2617   1848   2835    466    -22   -379       O  
ATOM    698  CB AILE C  14       9.892  16.802  19.156  0.50 32.63           C  
ANISOU  698  CB AILE C  14     4602   4505   3292   -119   -384    293       C  
ATOM    699  CB BILE C  14       9.868  16.663  19.055  0.50 31.35           C  
ANISOU  699  CB BILE C  14     4498   4043   3369   -168   -376    -17       C  
ATOM    700  CG1AILE C  14      10.350  15.479  19.792  0.50 36.75           C  
ANISOU  700  CG1AILE C  14     4938   4972   4054    582   -317    518       C  
ATOM    701  CG1BILE C  14      10.203  17.043  20.497  0.50 33.82           C  
ANISOU  701  CG1BILE C  14     4883   4732   3235    354   -590    100       C  
ATOM    702  CG2AILE C  14       8.413  16.676  18.801  0.50 39.60           C  
ANISOU  702  CG2AILE C  14     3455   6212   5381    962   1296   1325       C  
ATOM    703  CG2BILE C  14       9.822  15.145  18.894  0.50 29.55           C  
ANISOU  703  CG2BILE C  14     3764   3951   3512    486    725    170       C  
ATOM    704  CD1AILE C  14      11.520  15.767  20.712  0.50 48.17           C  
ANISOU  704  CD1AILE C  14     5671   8285   4345    636  -1150   1239       C  
ATOM    705  CD1BILE C  14       9.960  15.877  21.435  0.50 38.77           C  
ANISOU  705  CD1BILE C  14     5126   6116   3487    734   1726    668       C  
ATOM    706  N   CYS C  15      10.839  15.848  15.990  1.00 16.46           N  
ANISOU  706  N   CYS C  15     1857   2008   2391    170    216   -452       N  
ATOM    707  CA  CYS C  15      10.312  15.285  14.750  1.00 15.01           C  
ANISOU  707  CA  CYS C  15     1941   1591   2170    -15    287    -61       C  
ATOM    708  C   CYS C  15       9.290  14.184  15.092  1.00 17.53           C  
ANISOU  708  C   CYS C  15     2209   2113   2341   -400    349     54       C  
ATOM    709  O   CYS C  15       9.577  13.336  15.959  1.00 19.01           O  
ANISOU  709  O   CYS C  15     2442   1877   2904   -489    370    253       O  
ATOM    710  CB  CYS C  15      11.423  14.707  13.876  1.00 14.54           C  
ANISOU  710  CB  CYS C  15     1820   1450   2254     40    177   -214       C  
ATOM    711  SG  CYS C  15      12.647  15.914  13.292  1.00 17.92           S  
ANISOU  711  SG  CYS C  15     1976   1555   3280    139    565    172       S  
ATOM    712  N   HIS C  16       8.151  14.195  14.453  1.00 18.32           N  
ANISOU  712  N   HIS C  16     2428   1882   2652   -406    101   -325       N  
ATOM    713  CA  HIS C  16       7.137  13.170  14.615  1.00 21.10           C  
ANISOU  713  CA  HIS C  16     2222   2081   3712   -430    298   -354       C  
ATOM    714  C   HIS C  16       6.605  12.742  13.246  1.00 22.32           C  
ANISOU  714  C   HIS C  16     2148   2251   4083   -679    -81   -331       C  
ATOM    715  O   HIS C  16       6.436  13.573  12.366  1.00 24.39           O  
ANISOU  715  O   HIS C  16     3343   2235   3688   -747     -3   -551       O  
ATOM    716  CB AHIS C  16       5.937  13.625  15.421  0.50 32.66           C  
ANISOU  716  CB AHIS C  16     3183   4675   4550   -239   1538   -149       C  
ATOM    717  CB BHIS C  16       5.941  13.632  15.434  0.50 32.86           C  
ANISOU  717  CB BHIS C  16     3181   4722   4584   -207   1554   -163       C  
ATOM    718  CG AHIS C  16       4.955  12.678  16.018  0.50 36.11           C  
ANISOU  718  CG AHIS C  16     3331   5774   4617   -719   1240    447       C  
ATOM    719  CG BHIS C  16       6.104  13.795  16.914  0.50 34.47           C  
ANISOU  719  CG BHIS C  16     3387   5168   4541   -344   1796   -150       C  
ATOM    720  ND1AHIS C  16       3.744  12.347  15.440  0.50 44.12           N  
ANISOU  720  ND1AHIS C  16     4908   7200   4657  -2436    411    525       N  
ATOM    721  ND1BHIS C  16       5.678  12.854  17.831  0.50 37.10           N  
ANISOU  721  ND1BHIS C  16     3519   5862   4715   -952   1494    182       N  
ATOM    722  CD2AHIS C  16       4.953  11.998  17.197  0.50 38.74           C  
ANISOU  722  CD2AHIS C  16     3805   6436   4478   -878   1247    530       C  
ATOM    723  CD2BHIS C  16       6.640  14.803  17.649  0.50 36.13           C  
ANISOU  723  CD2BHIS C  16     4321   4983   4424   -304   1122    127       C  
ATOM    724  CE1AHIS C  16       3.064  11.504  16.192  0.50 46.25           C  
ANISOU  724  CE1AHIS C  16     4784   7587   5201  -2496    853    555       C  
ATOM    725  CE1BHIS C  16       5.951  13.272  19.054  0.50 39.99           C  
ANISOU  725  CE1BHIS C  16     4639   5859   4697  -1098   1271    296       C  
ATOM    726  NE2AHIS C  16       3.790  11.273  17.276  0.50 44.63           N  
ANISOU  726  NE2AHIS C  16     4909   7033   5014  -1952   1173    831       N  
ATOM    727  NE2BHIS C  16       6.540  14.462  18.966  0.50 37.88           N  
ANISOU  727  NE2BHIS C  16     4562   5371   4459   -602   1549    121       N  
ATOM    728  N   PRO C  17       6.262  11.461  13.127  1.00 24.13           N  
ANISOU  728  N   PRO C  17     2661   2316   4193   -770    -21   -426       N  
ATOM    729  CA  PRO C  17       5.561  10.955  11.958  1.00 30.83           C  
ANISOU  729  CA  PRO C  17     3726   2544   5443   -797  -1335   -499       C  
ATOM    730  C   PRO C  17       4.088  11.404  11.905  1.00 32.56           C  
ANISOU  730  C   PRO C  17     3334   2806   6231  -1349  -1197   -288       C  
ATOM    731  O   PRO C  17       3.339  11.347  12.874  1.00 37.56           O  
ANISOU  731  O   PRO C  17     3748   4500   6024   -967  -1091   -821       O  
ATOM    732  CB  PRO C  17       5.620   9.429  12.157  1.00 35.67           C  
ANISOU  732  CB  PRO C  17     4621   2543   6387  -1165  -2409   -369       C  
ATOM    733  CG  PRO C  17       5.636   9.292  13.654  1.00 36.36           C  
ANISOU  733  CG  PRO C  17     4868   2522   6424  -1394   -984     46       C  
ATOM    734  CD  PRO C  17       6.530  10.419  14.137  1.00 29.66           C  
ANISOU  734  CD  PRO C  17     4341   1960   4970   -519   -814   -456       C  
ATOM    735  N   VAL C  18       3.710  11.868  10.734  1.00 32.74           N  
ANISOU  735  N   VAL C  18     3072   3126   6241   -764  -1156   -430       N  
ATOM    736  CA  VAL C  18       2.388  12.209  10.261  1.00 31.46           C  
ANISOU  736  CA  VAL C  18     2849   3815   5290   -738   -859  -1397       C  
ATOM    737  C   VAL C  18       1.727  13.415  10.914  1.00 30.04           C  
ANISOU  737  C   VAL C  18     3492   3116   4805   -528   -419   -353       C  
ATOM    738  O   VAL C  18       1.173  14.233  10.188  1.00 39.42           O  
ANISOU  738  O   VAL C  18     4657   5064   5257    746  -1461   -423       O  
ATOM    739  CB  VAL C  18       1.400  11.039  10.461  1.00 33.41           C  
ANISOU  739  CB  VAL C  18     2982   3626   6087   -742   -851  -1527       C  
ATOM    740  CG1 VAL C  18       0.072  11.377   9.777  1.00 31.29           C  
ANISOU  740  CG1 VAL C  18     2512   3324   6053   -706   -192   -867       C  
ATOM    741  CG2 VAL C  18       1.981   9.720   9.943  1.00 39.63           C  
ANISOU  741  CG2 VAL C  18     2680   3504   8875   -451    400   -902       C  
ATOM    742  N   PHE C  19       1.735  13.564  12.217  1.00 26.05           N  
ANISOU  742  N   PHE C  19     2171   2876   4850   -436   -346   -395       N  
ATOM    743  CA  PHE C  19       1.054  14.739  12.774  1.00 28.61           C  
ANISOU  743  CA  PHE C  19     2080   3496   5295    -41   -467   -591       C  
ATOM    744  C   PHE C  19       1.783  15.243  14.006  1.00 28.39           C  
ANISOU  744  C   PHE C  19     2514   3517   4754   -152    -99   -645       C  
ATOM    745  O   PHE C  19       2.489  14.438  14.621  1.00 28.22           O  
ANISOU  745  O   PHE C  19     2779   3677   4267   -364    -90   -326       O  
ATOM    746  CB  PHE C  19      -0.385  14.346  13.063  1.00 30.29           C  
ANISOU  746  CB  PHE C  19     2041   4057   5412    106   -440    297       C  
ATOM    747  CG  PHE C  19      -0.448  13.250  14.114  1.00 30.09           C  
ANISOU  747  CG  PHE C  19     2516   3997   4919    273   -441     44       C  
ATOM    748  CD1 PHE C  19      -0.654  13.568  15.443  1.00 31.97           C  
ANISOU  748  CD1 PHE C  19     2702   4523   4922   -656   -716   -362       C  
ATOM    749  CD2 PHE C  19      -0.304  11.927  13.750  1.00 30.68           C  
ANISOU  749  CD2 PHE C  19     2562   3865   5229   -383   -170    -20       C  
ATOM    750  CE1 PHE C  19      -0.698  12.562  16.394  1.00 32.84           C  
ANISOU  750  CE1 PHE C  19     2873   4867   4738   -671   -229   -283       C  
ATOM    751  CE2 PHE C  19      -0.349  10.921  14.693  1.00 30.57           C  
ANISOU  751  CE2 PHE C  19     2563   3871   5180   -715   -252    -34       C  
ATOM    752  CZ  PHE C  19      -0.554  11.246  16.018  1.00 32.05           C  
ANISOU  752  CZ  PHE C  19     2510   4568   5098  -1339   -443   -121       C  
ATOM    753  N   CYS C  20       1.632  16.498  14.386  1.00 29.99           N  
ANISOU  753  N   CYS C  20     2449   3843   5103     71    318  -1054       N  
ATOM    754  CA  CYS C  20       2.142  17.003  15.662  1.00 28.97           C  
ANISOU  754  CA  CYS C  20     2302   3694   5013    239    438  -1061       C  
ATOM    755  C   CYS C  20       1.191  16.628  16.784  1.00 32.11           C  
ANISOU  755  C   CYS C  20     2987   3876   5338   -118    940  -1373       C  
ATOM    756  O   CYS C  20      -0.027  16.802  16.640  1.00 35.51           O  
ANISOU  756  O   CYS C  20     2793   4940   5759   -618   1016  -1335       O  
ATOM    757  CB  CYS C  20       2.309  18.531  15.631  1.00 27.87           C  
ANISOU  757  CB  CYS C  20     2140   3674   4774    511    442  -1078       C  
ATOM    758  SG  CYS C  20       3.672  19.056  14.595  1.00 25.29           S  
ANISOU  758  SG  CYS C  20     2060   3619   3931    478    -74   -826       S  
ATOM    759  N   PRO C  21       1.689  16.105  17.891  1.00 33.99           N  
ANISOU  759  N   PRO C  21     3274   3712   5928  -1092    899   -376       N  
ATOM    760  CA  PRO C  21       0.756  15.706  18.971  1.00 40.09           C  
ANISOU  760  CA  PRO C  21     4010   4563   6658  -1576   1340    -54       C  
ATOM    761  C   PRO C  21       0.166  16.922  19.668  1.00 44.51           C  
ANISOU  761  C   PRO C  21     4375   5599   6939  -1033   2265   -170       C  
ATOM    762  O   PRO C  21       0.652  18.060  19.585  1.00 38.90           O  
ANISOU  762  O   PRO C  21     3900   5444   5437   -953   1918  -1476       O  
ATOM    763  CB  PRO C  21       1.656  14.869  19.872  1.00 44.12           C  
ANISOU  763  CB  PRO C  21     5236   5447   6079   -946   1551    296       C  
ATOM    764  CG  PRO C  21       3.064  15.288  19.594  1.00 38.85           C  
ANISOU  764  CG  PRO C  21     4670   4289   5804    -80   1194    178       C  
ATOM    765  CD  PRO C  21       3.098  15.834  18.197  1.00 35.84           C  
ANISOU  765  CD  PRO C  21     3639   3857   6124   -355    840    488       C  
ATOM    766  N   ARG C  22      -0.939  16.735  20.378  1.00 56.16           N  
ANISOU  766  N   ARG C  22     4915   7695   8727  -2098   3162  -1142       N  
ATOM    767  CA  ARG C  22      -1.686  17.851  20.930  1.00 64.81           C  
ANISOU  767  CA  ARG C  22     5798   9359   9467  -2019   4408  -2472       C  
ATOM    768  C   ARG C  22      -0.828  18.738  21.842  1.00 63.93           C  
ANISOU  768  C   ARG C  22     6489   9083   8717  -1692   3933  -2147       C  
ATOM    769  O   ARG C  22      -0.015  18.214  22.611  1.00 67.57           O  
ANISOU  769  O   ARG C  22     6490  10186   8997   -866   3994  -2354       O  
ATOM    770  CB  ARG C  22      -2.891  17.344  21.730  1.00 72.06           C  
ANISOU  770  CB  ARG C  22     6575  10908   9897  -2432   4839  -1966       C  
ATOM    771  CG  ARG C  22      -2.455  16.955  23.134  1.00 78.84           C  
ANISOU  771  CG  ARG C  22     8013  11755  10186  -2193   4783  -1160       C  
ATOM    772  CD  ARG C  22      -3.600  16.766  24.095  1.00 80.11           C  
ANISOU  772  CD  ARG C  22     8246  11726  10465  -2278   4927   -512       C  
ATOM    773  NE  ARG C  22      -4.136  15.421  24.156  1.00 83.10           N  
ANISOU  773  NE  ARG C  22     8278  11606  11690  -2144   4831   -502       N  
ATOM    774  CZ  ARG C  22      -3.679  14.197  24.254  1.00 85.89           C  
ANISOU  774  CZ  ARG C  22     8295  11732  12609  -2085   4238   -172       C  
ATOM    775  NH1 ARG C  22      -2.397  13.855  24.334  1.00 83.35           N  
ANISOU  775  NH1 ARG C  22     8085  11321  12263  -2556   4004    577       N  
ATOM    776  NH2 ARG C  22      -4.579  13.201  24.271  1.00 86.06           N  
ANISOU  776  NH2 ARG C  22     7503  11308  13889  -1540   4772   -936       N  
ATOM    777  N   ARG C  23      -1.040  20.032  21.672  1.00 61.49           N  
ANISOU  777  N   ARG C  23     6271   8971   8120  -2533   4879  -1441       N  
ATOM    778  CA  ARG C  23      -0.341  21.159  22.254  1.00 61.73           C  
ANISOU  778  CA  ARG C  23     7198   9059   7198  -2131   3940  -1521       C  
ATOM    779  C   ARG C  23       0.751  21.714  21.339  1.00 46.62           C  
ANISOU  779  C   ARG C  23     4837   6202   6673   -906   2544  -1434       C  
ATOM    780  O   ARG C  23       1.064  22.909  21.407  1.00 40.24           O  
ANISOU  780  O   ARG C  23     3944   5212   6135    929   1120   -553       O  
ATOM    781  CB  ARG C  23       0.275  20.803  23.619  1.00 75.17           C  
ANISOU  781  CB  ARG C  23     9593  11591   7379  -3090   3521   -222       C  
ATOM    782  CG  ARG C  23      -0.775  20.447  24.661  1.00 86.03           C  
ANISOU  782  CG  ARG C  23    10924  13558   8205  -2959   4471    544       C  
ATOM    783  CD  ARG C  23      -0.351  20.731  26.092  1.00 90.56           C  
ANISOU  783  CD  ARG C  23    11902  14692   7816  -2789   4482   1217       C  
ATOM    784  NE  ARG C  23      -0.931  19.795  27.045  1.00 95.71           N  
ANISOU  784  NE  ARG C  23    12192  15297   8875  -2551   5168   1822       N  
ATOM    785  CZ  ARG C  23      -1.015  19.901  28.360  1.00 96.30           C  
ANISOU  785  CZ  ARG C  23    12046  15555   8988  -3094   5900   1734       C  
ATOM    786  NH1 ARG C  23      -0.558  20.934  29.053  1.00 95.38           N  
ANISOU  786  NH1 ARG C  23    10251  16883   9108  -3725   7022    859       N  
ATOM    787  NH2 ARG C  23      -1.587  18.918  29.044  1.00103.40           N  
ANISOU  787  NH2 ARG C  23    13343  16350   9594  -3947   5054   2624       N  
ATOM    788  N   TYR C  24       1.352  20.886  20.490  1.00 37.51           N  
ANISOU  788  N   TYR C  24     4041   4989   5223   -417   1255   -507       N  
ATOM    789  CA  TYR C  24       2.512  21.296  19.714  1.00 30.52           C  
ANISOU  789  CA  TYR C  24     3160   3924   4512    218    557   -185       C  
ATOM    790  C   TYR C  24       2.187  22.037  18.435  1.00 28.87           C  
ANISOU  790  C   TYR C  24     2177   3931   4862    623    173   -180       C  
ATOM    791  O   TYR C  24       1.260  21.678  17.708  1.00 49.49           O  
ANISOU  791  O   TYR C  24     5811   5564   7431  -1416  -2650    802       O  
ATOM    792  CB  TYR C  24       3.319  20.049  19.306  1.00 29.15           C  
ANISOU  792  CB  TYR C  24     3194   3310   4573     39     82    138       C  
ATOM    793  CG  TYR C  24       4.077  19.325  20.378  1.00 33.15           C  
ANISOU  793  CG  TYR C  24     3307   4301   4987   -123     66    946       C  
ATOM    794  CD1 TYR C  24       3.409  18.622  21.361  1.00 40.74           C  
ANISOU  794  CD1 TYR C  24     4385   6151   4943   -577    246   1444       C  
ATOM    795  CD2 TYR C  24       5.458  19.330  20.419  1.00 34.02           C  
ANISOU  795  CD2 TYR C  24     3256   4847   4823   1071    489    231       C  
ATOM    796  CE1 TYR C  24       4.090  17.947  22.352  1.00 41.61           C  
ANISOU  796  CE1 TYR C  24     4696   6019   5094    291    876   1630       C  
ATOM    797  CE2 TYR C  24       6.155  18.658  21.409  1.00 33.09           C  
ANISOU  797  CE2 TYR C  24     3489   4732   4353   1084    437   -169       C  
ATOM    798  CZ  TYR C  24       5.464  17.969  22.378  1.00 39.43           C  
ANISOU  798  CZ  TYR C  24     4700   5181   5098    433    341    559       C  
ATOM    799  OH  TYR C  24       6.128  17.294  23.367  1.00 43.86           O  
ANISOU  799  OH  TYR C  24     5469   6411   4786   -783   -822    704       O  
ATOM    800  N   LYS C  25       2.959  23.068  18.083  1.00 29.03           N  
ANISOU  800  N   LYS C  25     2279   4383   4367    577    533     63       N  
ATOM    801  CA  LYS C  25       2.722  23.788  16.837  1.00 29.87           C  
ANISOU  801  CA  LYS C  25     2707   4438   4205    771    417   -148       C  
ATOM    802  C   LYS C  25       3.695  23.314  15.759  1.00 27.28           C  
ANISOU  802  C   LYS C  25     2435   3970   3960    793     79   -162       C  
ATOM    803  O   LYS C  25       4.877  23.101  15.994  1.00 27.00           O  
ANISOU  803  O   LYS C  25     2787   3143   4330   1357   -317   -833       O  
ATOM    804  CB  LYS C  25       2.842  25.292  17.001  1.00 31.88           C  
ANISOU  804  CB  LYS C  25     3952   4325   3838   1561   -430   -271       C  
ATOM    805  CG  LYS C  25       1.712  25.950  17.779  1.00 37.34           C  
ANISOU  805  CG  LYS C  25     3711   5137   5338   2275   -507   -242       C  
ATOM    806  CD  LYS C  25       0.418  26.102  17.019  1.00 39.34           C  
ANISOU  806  CD  LYS C  25     3519   4686   6741    984   -946    176       C  
ATOM    807  CE  LYS C  25      -0.828  26.215  17.864  1.00 40.14           C  
ANISOU  807  CE  LYS C  25     3451   4181   7621   1007   -640    732       C  
ATOM    808  NZ  LYS C  25      -0.846  27.302  18.867  1.00 40.78           N  
ANISOU  808  NZ  LYS C  25     4715   4525   6254    332    435   1174       N  
ATOM    809  N   GLN C  26       3.163  23.158  14.564  1.00 26.31           N  
ANISOU  809  N   GLN C  26     2563   3305   4128    680   -102   -185       N  
ATOM    810  CA  GLN C  26       3.984  22.737  13.444  1.00 23.49           C  
ANISOU  810  CA  GLN C  26     2899   2131   3897    699   -234    -62       C  
ATOM    811  C   GLN C  26       4.831  23.902  12.926  1.00 24.77           C  
ANISOU  811  C   GLN C  26     3036   2093   4282    785    -69    171       C  
ATOM    812  O   GLN C  26       4.339  24.992  12.616  1.00 26.30           O  
ANISOU  812  O   GLN C  26     3520   2481   3992   1140     59    546       O  
ATOM    813  CB  GLN C  26       3.099  22.147  12.350  1.00 26.57           C  
ANISOU  813  CB  GLN C  26     2786   2905   4404    842   -550   -363       C  
ATOM    814  CG  GLN C  26       3.936  21.795  11.135  1.00 26.76           C  
ANISOU  814  CG  GLN C  26     2877   2954   4337    824   -757   -779       C  
ATOM    815  CD  GLN C  26       3.185  20.880  10.200  1.00 33.50           C  
ANISOU  815  CD  GLN C  26     3591   4001   5135     32   -687  -1345       C  
ATOM    816  OE1 GLN C  26       2.165  20.290  10.548  1.00 34.92           O  
ANISOU  816  OE1 GLN C  26     2932   3893   6443    458   -706  -1413       O  
ATOM    817  NE2 GLN C  26       3.799  20.839   9.028  1.00 40.22           N  
ANISOU  817  NE2 GLN C  26     5661   5498   4121  -1376  -1102   -915       N  
ATOM    818  N   ILE C  27       6.138  23.703  12.877  1.00 21.62           N  
ANISOU  818  N   ILE C  27     2941   1869   3405    597   -330   -568       N  
ATOM    819  CA  ILE C  27       7.042  24.784  12.457  1.00 20.75           C  
ANISOU  819  CA  ILE C  27     2883   1972   3029    717   -592   -210       C  
ATOM    820  C   ILE C  27       7.797  24.358  11.209  1.00 21.53           C  
ANISOU  820  C   ILE C  27     3009   1885   3288    457   -438   -352       C  
ATOM    821  O   ILE C  27       8.569  25.136  10.642  1.00 25.92           O  
ANISOU  821  O   ILE C  27     3601   2192   4054    219    245   -415       O  
ATOM    822  CB  ILE C  27       7.999  25.229  13.581  1.00 20.95           C  
ANISOU  822  CB  ILE C  27     2559   2162   3239    643   -428   -358       C  
ATOM    823  CG1 ILE C  27       9.007  24.153  13.985  1.00 19.68           C  
ANISOU  823  CG1 ILE C  27     2416   1894   3167    331   -467   -118       C  
ATOM    824  CG2 ILE C  27       7.246  25.706  14.804  1.00 22.47           C  
ANISOU  824  CG2 ILE C  27     2751   2653   3134    746   -546   -506       C  
ATOM    825  CD1 ILE C  27      10.124  24.649  14.859  1.00 19.71           C  
ANISOU  825  CD1 ILE C  27     2296   2172   3023    465   -266   -642       C  
ATOM    826  N   GLY C  28       7.603  23.130  10.723  1.00 21.37           N  
ANISOU  826  N   GLY C  28     3131   1887   3100    660   -651   -358       N  
ATOM    827  CA  GLY C  28       8.308  22.702   9.516  1.00 24.75           C  
ANISOU  827  CA  GLY C  28     4411   1924   3069    607   -170   -165       C  
ATOM    828  C   GLY C  28       8.112  21.202   9.331  1.00 21.93           C  
ANISOU  828  C   GLY C  28     3362   2010   2959    542   -491   -449       C  
ATOM    829  O   GLY C  28       7.186  20.637   9.897  1.00 21.14           O  
ANISOU  829  O   GLY C  28     2861   1936   3236    798   -561   -492       O  
ATOM    830  N   THR C  29       8.986  20.629   8.542  1.00 21.56           N  
ANISOU  830  N   THR C  29     3864   1866   2461    666   -176    159       N  
ATOM    831  CA  THR C  29       9.043  19.180   8.367  1.00 21.39           C  
ANISOU  831  CA  THR C  29     3166   1970   2990    500   -176   -298       C  
ATOM    832  C   THR C  29      10.420  18.727   8.822  1.00 21.55           C  
ANISOU  832  C   THR C  29     3316   1822   3049    469   -327    -13       C  
ATOM    833  O   THR C  29      11.342  19.491   9.111  1.00 20.74           O  
ANISOU  833  O   THR C  29     3014   1783   3084    390     81    206       O  
ATOM    834  CB  THR C  29       8.771  18.791   6.907  1.00 24.58           C  
ANISOU  834  CB  THR C  29     3696   2377   3268   -431   -664   -333       C  
ATOM    835  OG1 THR C  29       9.861  19.229   6.092  1.00 30.01           O  
ANISOU  835  OG1 THR C  29     4867   3289   3245    -27    422   -440       O  
ATOM    836  CG2 THR C  29       7.552  19.535   6.385  1.00 29.23           C  
ANISOU  836  CG2 THR C  29     4464   3089   3553    -42  -1098     61       C  
ATOM    837  N   CYS C  30      10.622  17.443   8.905  1.00 20.86           N  
ANISOU  837  N   CYS C  30     2823   1818   3283    319    501    202       N  
ATOM    838  CA  CYS C  30      11.928  16.789   9.104  1.00 19.87           C  
ANISOU  838  CA  CYS C  30     2815   1472   3263    142    439    159       C  
ATOM    839  C   CYS C  30      12.452  16.049   7.894  1.00 20.12           C  
ANISOU  839  C   CYS C  30     2575   1958   3114    301    296     99       C  
ATOM    840  O   CYS C  30      13.232  15.089   7.973  1.00 21.63           O  
ANISOU  840  O   CYS C  30     2874   2007   3336    456    545    183       O  
ATOM    841  CB  CYS C  30      11.923  15.900  10.346  1.00 19.34           C  
ANISOU  841  CB  CYS C  30     2736   1376   3237    245    575    108       C  
ATOM    842  SG  CYS C  30      11.592  16.891  11.829  1.00 18.33           S  
ANISOU  842  SG  CYS C  30     2392   1380   3194    263    525    156       S  
ATOM    843  N   GLY C  31      12.125  16.462   6.677  1.00 22.98           N  
ANISOU  843  N   GLY C  31     2715   2786   3232    436    714    661       N  
ATOM    844  CA  GLY C  31      12.749  15.967   5.478  1.00 26.68           C  
ANISOU  844  CA  GLY C  31     3009   3822   3304   -608   1305    479       C  
ATOM    845  C   GLY C  31      12.147  14.686   4.971  1.00 29.90           C  
ANISOU  845  C   GLY C  31     4860   3558   2940   -306    546    399       C  
ATOM    846  O   GLY C  31      11.616  14.673   3.858  1.00 28.74           O  
ANISOU  846  O   GLY C  31     5074   3142   2703    616    729    171       O  
ATOM    847  N   LEU C  32      12.216  13.626   5.775  1.00 25.99           N  
ANISOU  847  N   LEU C  32     4104   3232   2537    333    792     40       N  
ATOM    848  CA  LEU C  32      11.550  12.384   5.364  1.00 25.20           C  
ANISOU  848  CA  LEU C  32     4037   3008   2529    627    644    -83       C  
ATOM    849  C   LEU C  32      10.069  12.654   5.089  1.00 27.04           C  
ANISOU  849  C   LEU C  32     4247   2845   3182    825    130   -448       C  
ATOM    850  O   LEU C  32       9.460  13.505   5.754  1.00 26.95           O  
ANISOU  850  O   LEU C  32     3987   2918   3333    443    732   -467       O  
ATOM    851  CB  LEU C  32      11.674  11.329   6.435  1.00 23.70           C  
ANISOU  851  CB  LEU C  32     3823   2913   2271    773    751   -281       C  
ATOM    852  CG  LEU C  32      12.972  10.595   6.644  1.00 27.92           C  
ANISOU  852  CG  LEU C  32     4397   3168   3043   1339    354   -682       C  
ATOM    853  CD1 LEU C  32      14.063  11.600   6.996  1.00 44.69           C  
ANISOU  853  CD1 LEU C  32     3520   5712   7749    481   1015  -1614       C  
ATOM    854  CD2 LEU C  32      12.762   9.577   7.743  1.00 34.20           C  
ANISOU  854  CD2 LEU C  32     5178   4430   3388   2481    984    215       C  
ATOM    855  N   PRO C  33       9.505  11.949   4.116  1.00 31.13           N  
ANISOU  855  N   PRO C  33     4798   4120   2908   1371   -222   -882       N  
ATOM    856  CA  PRO C  33       8.122  12.249   3.728  1.00 33.79           C  
ANISOU  856  CA  PRO C  33     4672   4520   3647   1190   -370  -1005       C  
ATOM    857  C   PRO C  33       7.221  12.063   4.941  1.00 31.60           C  
ANISOU  857  C   PRO C  33     4386   4229   3393   1053   -705   -914       C  
ATOM    858  O   PRO C  33       7.421  11.142   5.725  1.00 35.57           O  
ANISOU  858  O   PRO C  33     6029   3167   4318   -187   -843   -781       O  
ATOM    859  CB  PRO C  33       7.792  11.213   2.669  1.00 34.61           C  
ANISOU  859  CB  PRO C  33     4756   4882   3512    402     -9   -965       C  
ATOM    860  CG  PRO C  33       9.075  10.646   2.232  1.00 34.53           C  
ANISOU  860  CG  PRO C  33     4755   4453   3914     94     91  -1509       C  
ATOM    861  CD  PRO C  33      10.078  10.857   3.316  1.00 31.59           C  
ANISOU  861  CD  PRO C  33     4770   4207   3026    886    342  -1059       C  
ATOM    862  N   GLY C  34       6.265  12.976   5.099  1.00 35.87           N  
ANISOU  862  N   GLY C  34     4685   4851   4094   1344   -539  -1818       N  
ATOM    863  CA  GLY C  34       5.295  12.865   6.171  1.00 35.50           C  
ANISOU  863  CA  GLY C  34     4283   4742   4463    577   -571  -1934       C  
ATOM    864  C   GLY C  34       5.673  13.378   7.533  1.00 31.14           C  
ANISOU  864  C   GLY C  34     3469   3981   4381   -244     37  -1928       C  
ATOM    865  O   GLY C  34       4.788  13.658   8.390  1.00 29.07           O  
ANISOU  865  O   GLY C  34     3065   3598   4382   -297     -3  -1354       O  
ATOM    866  N   THR C  35       6.972  13.546   7.795  1.00 27.68           N  
ANISOU  866  N   THR C  35     3359   3236   3922   -453    527  -1413       N  
ATOM    867  CA  THR C  35       7.407  13.981   9.125  1.00 22.93           C  
ANISOU  867  CA  THR C  35     2721   2332   3661   -415    517   -804       C  
ATOM    868  C   THR C  35       7.181  15.466   9.378  1.00 21.64           C  
ANISOU  868  C   THR C  35     2673   2280   3267   -456    525   -558       C  
ATOM    869  O   THR C  35       7.258  16.318   8.490  1.00 22.96           O  
ANISOU  869  O   THR C  35     3109   2610   3005   -329    -45   -450       O  
ATOM    870  CB  THR C  35       8.881  13.625   9.337  1.00 22.70           C  
ANISOU  870  CB  THR C  35     2459   2614   3552   -408   1232   -990       C  
ATOM    871  OG1 THR C  35       9.657  14.218   8.314  1.00 23.86           O  
ANISOU  871  OG1 THR C  35     3176   2804   3087    -61   1059   -560       O  
ATOM    872  CG2 THR C  35       9.095  12.133   9.190  1.00 25.30           C  
ANISOU  872  CG2 THR C  35     3629   2689   3295    230   1275   -469       C  
ATOM    873  N   LYS C  36       6.866  15.726  10.643  1.00 18.74           N  
ANISOU  873  N   LYS C  36     1905   2217   3000     33   -136   -429       N  
ATOM    874  CA  LYS C  36       6.570  17.090  11.058  1.00 19.79           C  
ANISOU  874  CA  LYS C  36     1687   2439   3394     55    -91   -757       C  
ATOM    875  C   LYS C  36       7.529  17.509  12.173  1.00 17.23           C  
ANISOU  875  C   LYS C  36     1678   1786   3082    141   -100   -236       C  
ATOM    876  O   LYS C  36       7.821  16.673  13.017  1.00 19.07           O  
ANISOU  876  O   LYS C  36     2382   1744   3118   -195    132    -16       O  
ATOM    877  CB  LYS C  36       5.130  17.230  11.519  1.00 24.00           C  
ANISOU  877  CB  LYS C  36     1644   3214   4262    -26    -81  -1346       C  
ATOM    878  CG  LYS C  36       4.002  16.955  10.528  1.00 32.52           C  
ANISOU  878  CG  LYS C  36     1819   5167   5371   -195   -575  -1671       C  
ATOM    879  CD  LYS C  36       2.708  17.525  11.102  1.00 43.41           C  
ANISOU  879  CD  LYS C  36     1895   7291   7307    901   -414   -919       C  
ATOM    880  CE  LYS C  36       1.587  17.510  10.078  1.00 51.85           C  
ANISOU  880  CE  LYS C  36     2813   8692   8195   1470  -1319    332       C  
ATOM    881  NZ  LYS C  36       0.489  18.436  10.475  1.00 63.15           N  
ANISOU  881  NZ  LYS C  36     3637   9581  10777   2598  -1833   -120       N  
ATOM    882  N   CYS C  37       7.945  18.767  12.066  1.00 16.79           N  
ANISOU  882  N   CYS C  37     2416   1562   2402    266   -235   -240       N  
ATOM    883  CA  CYS C  37       8.769  19.398  13.091  1.00 16.75           C  
ANISOU  883  CA  CYS C  37     2078   1778   2509    233     57   -491       C  
ATOM    884  C   CYS C  37       7.821  20.118  14.051  1.00 17.47           C  
ANISOU  884  C   CYS C  37     2300   1660   2678    560     41   -375       C  
ATOM    885  O   CYS C  37       7.071  20.979  13.573  1.00 18.62           O  
ANISOU  885  O   CYS C  37     2395   1674   3005    551    -82   -238       O  
ATOM    886  CB  CYS C  37       9.798  20.381  12.543  1.00 17.91           C  
ANISOU  886  CB  CYS C  37     2276   1632   2896    242      0   -163       C  
ATOM    887  SG  CYS C  37      10.920  21.023  13.792  1.00 17.79           S  
ANISOU  887  SG  CYS C  37     2149   1547   3062    241    -11   -122       S  
ATOM    888  N   CYS C  38       7.863  19.750  15.331  1.00 17.57           N  
ANISOU  888  N   CYS C  38     1926   2076   2674    638    247   -251       N  
ATOM    889  CA  CYS C  38       6.802  20.125  16.255  1.00 19.53           C  
ANISOU  889  CA  CYS C  38     1809   2741   2870    271    211   -708       C  
ATOM    890  C   CYS C  38       7.388  20.774  17.516  1.00 20.47           C  
ANISOU  890  C   CYS C  38     2397   2505   2876    647     14   -725       C  
ATOM    891  O   CYS C  38       8.222  20.176  18.188  1.00 19.55           O  
ANISOU  891  O   CYS C  38     2446   2244   2736    386    -10   -596       O  
ATOM    892  CB  CYS C  38       5.973  18.884  16.569  1.00 20.66           C  
ANISOU  892  CB  CYS C  38     1966   2939   2946    187    401   -568       C  
ATOM    893  SG  CYS C  38       5.261  17.940  15.198  1.00 21.43           S  
ANISOU  893  SG  CYS C  38     1959   2687   3499    231    236   -783       S  
ATOM    894  N   LYS C  39       6.948  21.986  17.828  1.00 22.01           N  
ANISOU  894  N   LYS C  39     2633   2639   3091    803    100   -814       N  
ATOM    895  CA  LYS C  39       7.407  22.763  18.969  1.00 22.53           C  
ANISOU  895  CA  LYS C  39     3098   2519   2944    523    219   -715       C  
ATOM    896  C   LYS C  39       6.368  22.793  20.081  1.00 23.43           C  
ANISOU  896  C   LYS C  39     2944   2961   2999     34    170   -933       C  
ATOM    897  O   LYS C  39       5.230  23.200  19.941  1.00 28.41           O  
ANISOU  897  O   LYS C  39     3082   3460   4251    423    674   -291       O  
ATOM    898  CB  LYS C  39       7.729  24.195  18.516  1.00 24.82           C  
ANISOU  898  CB  LYS C  39     4209   2601   2620    359    260   -610       C  
ATOM    899  CG  LYS C  39       8.383  25.102  19.530  1.00 29.32           C  
ANISOU  899  CG  LYS C  39     4750   2897   3493   -231   -346   -570       C  
ATOM    900  CD  LYS C  39       9.808  24.732  19.918  1.00 28.19           C  
ANISOU  900  CD  LYS C  39     4385   2715   3610   -423    108   -583       C  
ATOM    901  CE  LYS C  39      10.472  25.885  20.668  1.00 32.75           C  
ANISOU  901  CE  LYS C  39     5165   3742   3537   -886   -329   -854       C  
ATOM    902  NZ  LYS C  39      11.097  25.452  21.952  1.00 34.08           N  
ANISOU  902  NZ  LYS C  39     3362   5978   3608   -271    121   -607       N  
ATOM    903  N   LYS C  40       6.767  22.350  21.260  1.00 29.53           N  
ANISOU  903  N   LYS C  40     4069   4177   2975    384    409   -456       N  
ATOM    904  CA  LYS C  40       5.834  22.328  22.392  1.00 34.93           C  
ANISOU  904  CA  LYS C  40     5071   4666   3532    285   1203   -384       C  
ATOM    905  C   LYS C  40       5.601  23.708  22.979  1.00 36.27           C  
ANISOU  905  C   LYS C  40     5290   5102   3388    201   1106   -929       C  
ATOM    906  O   LYS C  40       6.367  24.649  22.713  1.00 38.12           O  
ANISOU  906  O   LYS C  40     5317   5301   3864   -223   1406  -1953       O  
ATOM    907  CB  LYS C  40       6.403  21.373  23.435  1.00 45.27           C  
ANISOU  907  CB  LYS C  40     7404   5371   4427   -160   1283   1130       C  
ATOM    908  CG  LYS C  40       5.536  20.973  24.605  1.00 55.72           C  
ANISOU  908  CG  LYS C  40     7788   7503   5879  -1063   1765   2063       C  
ATOM    909  CD  LYS C  40       4.046  21.184  24.412  1.00 61.53           C  
ANISOU  909  CD  LYS C  40     7681   8840   6859  -1068   1902   1696       C  
ATOM    910  CE  LYS C  40       3.322  21.344  25.736  1.00 59.90           C  
ANISOU  910  CE  LYS C  40     7337   8967   6455  -1175   1736   3082       C  
ATOM    911  NZ  LYS C  40       3.130  20.023  26.400  1.00 63.33           N  
ANISOU  911  NZ  LYS C  40     7202   8738   8122   -997    955   3439       N  
TER     912      LYS C  40                                                      
ATOM    913  N  AGLY D   1      25.014   1.594  17.489  0.50 53.58           N  
ANISOU  913  N  AGLY D   1     4802   6323   9234   2115  -2334    917       N  
ATOM    914  N  BGLY D   1      23.130   1.039  18.549  0.50 50.38           N  
ANISOU  914  N  BGLY D   1     8047   4755   6338   -714   -164   3015       N  
ATOM    915  CA AGLY D   1      23.658   1.142  17.145  0.50 41.90           C  
ANISOU  915  CA AGLY D   1     5431   4233   6254   1391  -1742    764       C  
ATOM    916  CA BGLY D   1      23.492   1.055  17.143  0.50 40.96           C  
ANISOU  916  CA BGLY D   1     5661   4093   5809   1518  -1311    791       C  
ATOM    917  C   GLY D   1      22.959   2.246  16.378  1.00 28.41           C  
ANISOU  917  C   GLY D   1     3427   3386   3982    708   -378    389       C  
ATOM    918  O   GLY D   1      23.559   2.701  15.394  1.00 38.58           O  
ANISOU  918  O   GLY D   1     3035   4671   6951   1221   1508   1491       O  
ATOM    919  N   ILE D   2      21.795   2.786  16.706  1.00 18.66           N  
ANISOU  919  N   ILE D   2     3108   1690   2292   -518    -68     13       N  
ATOM    920  CA  ILE D   2      21.361   4.005  15.978  1.00 15.24           C  
ANISOU  920  CA  ILE D   2     2145   1673   1973   -499    367   -118       C  
ATOM    921  C   ILE D   2      22.027   5.168  16.691  1.00 14.07           C  
ANISOU  921  C   ILE D   2     1835   1619   1892   -220     36      5       C  
ATOM    922  O   ILE D   2      21.989   5.271  17.942  1.00 15.63           O  
ANISOU  922  O   ILE D   2     2349   1667   1922   -166    269   -145       O  
ATOM    923  CB  ILE D   2      19.826   4.198  15.896  1.00 16.09           C  
ANISOU  923  CB  ILE D   2     2209   1963   1940   -637    173   -375       C  
ATOM    924  CG1 ILE D   2      19.139   3.077  15.113  1.00 16.97           C  
ANISOU  924  CG1 ILE D   2     2160   1615   2671     55   -258   -643       C  
ATOM    925  CG2 ILE D   2      19.506   5.601  15.404  1.00 17.67           C  
ANISOU  925  CG2 ILE D   2     2509   1690   2514     -5     76  -1039       C  
ATOM    926  CD1 ILE D   2      17.646   2.959  15.250  1.00 22.25           C  
ANISOU  926  CD1 ILE D   2     2266   2596   3593   -542    -25  -1496       C  
ATOM    927  N   GLY D   3      22.644   6.031  15.910  1.00 13.20           N  
ANISOU  927  N   GLY D   3     1667   1394   1953    -70     51    -32       N  
ATOM    928  CA  GLY D   3      23.316   7.219  16.417  1.00 13.74           C  
ANISOU  928  CA  GLY D   3     1609   1659   1952   -234     16    -32       C  
ATOM    929  C   GLY D   3      23.139   8.483  15.602  1.00 13.80           C  
ANISOU  929  C   GLY D   3     1795   1386   2063   -255    -14   -183       C  
ATOM    930  O   GLY D   3      24.038   9.331  15.607  1.00 16.21           O  
ANISOU  930  O   GLY D   3     1748   1678   2731   -403    196     -6       O  
ATOM    931  N   ASP D   4      22.049   8.646  14.851  1.00 13.90           N  
ANISOU  931  N   ASP D   4     1697   1644   1938   -149    158     88       N  
ATOM    932  CA  ASP D   4      21.751   9.856  14.049  1.00 14.01           C  
ANISOU  932  CA  ASP D   4     1572   1540   2212   -284    276    188       C  
ATOM    933  C   ASP D   4      20.240   9.979  13.879  1.00 13.71           C  
ANISOU  933  C   ASP D   4     1623   1329   2257   -179    127   -244       C  
ATOM    934  O   ASP D   4      19.493   8.963  13.942  1.00 14.45           O  
ANISOU  934  O   ASP D   4     1602   1392   2497   -283    377   -197       O  
ATOM    935  CB  ASP D   4      22.462   9.806  12.703  1.00 14.65           C  
ANISOU  935  CB  ASP D   4     1726   1579   2262   -180    316    302       C  
ATOM    936  CG  ASP D   4      21.727   8.924  11.713  1.00 13.57           C  
ANISOU  936  CG  ASP D   4     1440   1625   2089   -106    473    253       C  
ATOM    937  OD1 ASP D   4      22.060   7.727  11.631  1.00 14.82           O  
ANISOU  937  OD1 ASP D   4     1775   1794   2062    100    104    104       O  
ATOM    938  OD2 ASP D   4      20.827   9.439  11.005  1.00 14.81           O  
ANISOU  938  OD2 ASP D   4     1671   1700   2254     -6    340    269       O  
ATOM    939  N   PRO D   5      19.710  11.172  13.669  1.00 13.82           N  
ANISOU  939  N   PRO D   5     1573   1260   2417   -124    505   -394       N  
ATOM    940  CA  PRO D   5      18.250  11.353  13.630  1.00 14.31           C  
ANISOU  940  CA  PRO D   5     1606   1541   2289    -97    498    -80       C  
ATOM    941  C   PRO D   5      17.546  10.822  12.392  1.00 13.77           C  
ANISOU  941  C   PRO D   5     1666   1357   2209     29    322    241       C  
ATOM    942  O   PRO D   5      16.367  10.468  12.473  1.00 14.81           O  
ANISOU  942  O   PRO D   5     1758   1582   2289   -175    436     61       O  
ATOM    943  CB  PRO D   5      18.092  12.880  13.684  1.00 15.13           C  
ANISOU  943  CB  PRO D   5     1794   1553   2404    181    198    -20       C  
ATOM    944  CG  PRO D   5      19.392  13.415  13.207  1.00 21.27           C  
ANISOU  944  CG  PRO D   5     1965   1612   4504   -124    248    529       C  
ATOM    945  CD  PRO D   5      20.468  12.441  13.503  1.00 14.92           C  
ANISOU  945  CD  PRO D   5     1700   1353   2617   -236    321   -153       C  
ATOM    946  N   VAL D   6      18.255  10.764  11.262  1.00 13.62           N  
ANISOU  946  N   VAL D   6     1627   1406   2140     -1    310    189       N  
ATOM    947  CA  VAL D   6      17.624  10.272  10.033  1.00 14.05           C  
ANISOU  947  CA  VAL D   6     1486   1709   2145     -4    166    324       C  
ATOM    948  C   VAL D   6      17.367   8.775  10.186  1.00 14.00           C  
ANISOU  948  C   VAL D   6     1618   1702   1999   -196    162    200       C  
ATOM    949  O   VAL D   6      16.239   8.298   9.934  1.00 15.69           O  
ANISOU  949  O   VAL D   6     1779   1795   2386   -141    114   -418       O  
ATOM    950  CB  VAL D   6      18.450  10.595   8.758  1.00 15.62           C  
ANISOU  950  CB  VAL D   6     2083   1621   2230   -119    432    256       C  
ATOM    951  CG1 VAL D   6      17.808   9.911   7.570  1.00 16.94           C  
ANISOU  951  CG1 VAL D   6     2101   2179   2158    287    283    171       C  
ATOM    952  CG2 VAL D   6      18.562  12.102   8.569  1.00 18.55           C  
ANISOU  952  CG2 VAL D   6     2582   1650   2817    126    638    524       C  
ATOM    953  N   THR D   7      18.363   7.989  10.603  1.00 14.28           N  
ANISOU  953  N   THR D   7     1810   1329   2285    -70     76   -250       N  
ATOM    954  CA  THR D   7      18.109   6.552  10.802  1.00 13.56           C  
ANISOU  954  CA  THR D   7     1807   1487   1860   -253    186   -135       C  
ATOM    955  C   THR D   7      16.999   6.319  11.813  1.00 15.54           C  
ANISOU  955  C   THR D   7     1864   1622   2417   -201    507   -393       C  
ATOM    956  O   THR D   7      16.135   5.432  11.675  1.00 14.74           O  
ANISOU  956  O   THR D   7     1614   1644   2344   -132    268   -198       O  
ATOM    957  CB  THR D   7      19.429   5.875  11.227  1.00 15.45           C  
ANISOU  957  CB  THR D   7     1894   1515   2462     21    577    216       C  
ATOM    958  OG1 THR D   7      20.436   6.154  10.270  1.00 15.89           O  
ANISOU  958  OG1 THR D   7     2028   1736   2275    169    613   -131       O  
ATOM    959  CG2 THR D   7      19.310   4.362  11.353  1.00 17.72           C  
ANISOU  959  CG2 THR D   7     2456   1459   2816    -65    357   -191       C  
ATOM    960  N   CYS D   8      16.967   7.093  12.909  1.00 13.60           N  
ANISOU  960  N   CYS D   8     1750   1204   2214     14    420   -102       N  
ATOM    961  CA  CYS D   8      15.950   6.964  13.957  1.00 12.87           C  
ANISOU  961  CA  CYS D   8     1550   1344   1995   -136    140    -15       C  
ATOM    962  C   CYS D   8      14.563   7.060  13.348  1.00 12.88           C  
ANISOU  962  C   CYS D   8     1618   1609   1667   -160    107    -13       C  
ATOM    963  O   CYS D   8      13.704   6.200  13.527  1.00 13.66           O  
ANISOU  963  O   CYS D   8     1597   1505   2089    -88    279    -83       O  
ATOM    964  CB  CYS D   8      16.207   8.014  15.065  1.00 13.26           C  
ANISOU  964  CB  CYS D   8     1437   1468   2134   -179    125   -182       C  
ATOM    965  SG  CYS D   8      15.102   7.851  16.482  1.00 14.60           S  
ANISOU  965  SG  CYS D   8     1788   1444   2315   -105    348   -210       S  
ATOM    966  N   LEU D   9      14.301   8.130  12.584  1.00 12.72           N  
ANISOU  966  N   LEU D   9     1425   1586   1820      3    270    -44       N  
ATOM    967  CA  LEU D   9      13.013   8.382  11.975  1.00 13.42           C  
ANISOU  967  CA  LEU D   9     1293   1615   2192    102    242   -102       C  
ATOM    968  C   LEU D   9      12.674   7.331  10.931  1.00 14.26           C  
ANISOU  968  C   LEU D   9     1506   1846   2066    -30     68    -77       C  
ATOM    969  O   LEU D   9      11.528   6.852  10.872  1.00 18.28           O  
ANISOU  969  O   LEU D   9     1640   2227   3079   -249     14   -280       O  
ATOM    970  CB  LEU D   9      12.985   9.801  11.400  1.00 14.45           C  
ANISOU  970  CB  LEU D   9     1531   1751   2209     96     98     -5       C  
ATOM    971  CG  LEU D   9      12.894  10.930  12.411  1.00 15.19           C  
ANISOU  971  CG  LEU D   9     1832   1604   2336    227    217     35       C  
ATOM    972  CD1 LEU D   9      13.159  12.275  11.707  1.00 18.81           C  
ANISOU  972  CD1 LEU D   9     2170   1694   3283      3    367    260       C  
ATOM    973  CD2 LEU D   9      11.560  10.919  13.105  1.00 19.34           C  
ANISOU  973  CD2 LEU D   9     2486   2032   2829    211    927     11       C  
ATOM    974  N   LYS D  10      13.657   6.939  10.106  1.00 17.17           N  
ANISOU  974  N   LYS D  10     2078   2123   2323   -470    554   -464       N  
ATOM    975  CA  LYS D  10      13.368   5.907   9.107  1.00 19.36           C  
ANISOU  975  CA  LYS D  10     2185   2426   2744   -313    150   -830       C  
ATOM    976  C   LYS D  10      12.913   4.576   9.705  1.00 20.00           C  
ANISOU  976  C   LYS D  10     2319   2041   3238    -58    222   -918       C  
ATOM    977  O   LYS D  10      12.154   3.806   9.062  1.00 21.06           O  
ANISOU  977  O   LYS D  10     2706   2625   2671   -763    573   -759       O  
ATOM    978  CB  LYS D  10      14.585   5.592   8.225  1.00 20.29           C  
ANISOU  978  CB  LYS D  10     2243   3151   2316     85      8   -802       C  
ATOM    979  CG  LYS D  10      15.083   6.642   7.306  1.00 22.30           C  
ANISOU  979  CG  LYS D  10     2167   3457   2850   -158    132   -555       C  
ATOM    980  CD  LYS D  10      16.104   6.246   6.298  1.00 27.90           C  
ANISOU  980  CD  LYS D  10     3473   3768   3359   -219   1045   -710       C  
ATOM    981  CE  LYS D  10      16.117   7.070   5.026  1.00 31.70           C  
ANISOU  981  CE  LYS D  10     4447   3950   3645    533   1632   -462       C  
ATOM    982  NZ  LYS D  10      17.050   6.524   4.016  1.00 35.01           N  
ANISOU  982  NZ  LYS D  10     4790   4915   3596    233   1806   -976       N  
ATOM    983  N   SER D  11      13.385   4.299  10.911  1.00 18.15           N  
ANISOU  983  N   SER D  11     1642   1805   3450   -364    208   -717       N  
ATOM    984  CA  SER D  11      13.034   3.079  11.631  1.00 20.65           C  
ANISOU  984  CA  SER D  11     2188   1822   3837   -185    297   -544       C  
ATOM    985  C   SER D  11      11.643   3.133  12.279  1.00 21.48           C  
ANISOU  985  C   SER D  11     2580   1861   3722   -274    690   -154       C  
ATOM    986  O   SER D  11      11.251   2.108  12.821  1.00 22.48           O  
ANISOU  986  O   SER D  11     3150   1950   3441   -543    420   -135       O  
ATOM    987  CB ASER D  11      14.062   2.767  12.729  0.50 25.91           C  
ANISOU  987  CB ASER D  11     3053   2694   4098    299    -83   -269       C  
ATOM    988  CB BSER D  11      14.053   2.801  12.742  0.50 28.89           C  
ANISOU  988  CB BSER D  11     3086   3127   4762    122   -364    286       C  
ATOM    989  OG ASER D  11      13.766   3.550  13.884  0.50 26.69           O  
ANISOU  989  OG ASER D  11     3872   2743   3528   -551    176    -63       O  
ATOM    990  OG BSER D  11      15.259   2.167  12.356  0.50 42.15           O  
ANISOU  990  OG BSER D  11     3839   4611   7567   1710  -1178   -732       O  
ATOM    991  N   GLY D  12      10.968   4.269  12.245  1.00 16.95           N  
ANISOU  991  N   GLY D  12     1563   2042   2836   -470    -29   -249       N  
ATOM    992  CA  GLY D  12       9.666   4.497  12.804  1.00 17.81           C  
ANISOU  992  CA  GLY D  12     1735   2263   2769   -345     52    198       C  
ATOM    993  C   GLY D  12       9.692   4.971  14.247  1.00 17.66           C  
ANISOU  993  C   GLY D  12     1763   2401   2545   -515    274    536       C  
ATOM    994  O   GLY D  12       8.629   4.968  14.888  1.00 25.73           O  
ANISOU  994  O   GLY D  12     2076   3957   3742  -1156    904   -854       O  
ATOM    995  N   ALA D  13      10.878   5.358  14.689  1.00 15.86           N  
ANISOU  995  N   ALA D  13     1605   1851   2569   -113    444   -232       N  
ATOM    996  CA  ALA D  13      11.118   5.896  16.022  1.00 16.47           C  
ANISOU  996  CA  ALA D  13     1991   1807   2462   -351    610    -53       C  
ATOM    997  C   ALA D  13      11.139   7.429  16.051  1.00 16.53           C  
ANISOU  997  C   ALA D  13     2142   1826   2315   -483    386    -78       C  
ATOM    998  O   ALA D  13      11.002   8.079  15.019  1.00 18.35           O  
ANISOU  998  O   ALA D  13     2815   1926   2232   -140    731    -25       O  
ATOM    999  CB  ALA D  13      12.451   5.368  16.524  1.00 18.95           C  
ANISOU  999  CB  ALA D  13     2352   2328   2520     19    149   -530       C  
ATOM   1000  N   ILE D  14      11.314   7.978  17.270  1.00 17.39           N  
ANISOU 1000  N   ILE D  14     2467   1820   2320   -576    274      3       N  
ATOM   1001  CA  ILE D  14      11.383   9.436  17.427  1.00 17.77           C  
ANISOU 1001  CA  ILE D  14     2626   1820   2308   -292    354   -153       C  
ATOM   1002  C   ILE D  14      12.578   9.803  18.301  1.00 17.67           C  
ANISOU 1002  C   ILE D  14     2659   1450   2605   -260    164    -48       C  
ATOM   1003  O   ILE D  14      12.963   9.048  19.165  1.00 19.04           O  
ANISOU 1003  O   ILE D  14     2683   1691   2861   -235     94    146       O  
ATOM   1004  CB  ILE D  14      10.068  10.018  17.943  1.00 23.77           C  
ANISOU 1004  CB  ILE D  14     2719   3098   3214    419     85   -333       C  
ATOM   1005  CG1 ILE D  14       9.690   9.515  19.322  1.00 25.90           C  
ANISOU 1005  CG1 ILE D  14     2817   3298   3727    746   1172   -291       C  
ATOM   1006  CG2 ILE D  14       8.919   9.770  16.971  1.00 29.73           C  
ANISOU 1006  CG2 ILE D  14     2931   4028   4338    587   -293  -1781       C  
ATOM   1007  CD1 ILE D  14       8.462  10.159  19.918  1.00 39.24           C  
ANISOU 1007  CD1 ILE D  14     3006   6492   5412   1287   1424  -1505       C  
ATOM   1008  N   CYS D  15      13.207  10.955  18.041  1.00 16.63           N  
ANISOU 1008  N   CYS D  15     2422   1631   2264   -199    458    -78       N  
ATOM   1009  CA  CYS D  15      14.292  11.556  18.804  1.00 15.90           C  
ANISOU 1009  CA  CYS D  15     2102   1581   2359    -39    605   -315       C  
ATOM   1010  C   CYS D  15      13.725  12.429  19.913  1.00 17.12           C  
ANISOU 1010  C   CYS D  15     2708   1413   2384     -7    638   -274       C  
ATOM   1011  O   CYS D  15      12.847  13.234  19.610  1.00 18.58           O  
ANISOU 1011  O   CYS D  15     2599   1973   2488    344    637   -550       O  
ATOM   1012  CB  CYS D  15      15.153  12.405  17.880  1.00 15.76           C  
ANISOU 1012  CB  CYS D  15     2500   1599   1889   -217    313   -241       C  
ATOM   1013  SG  CYS D  15      16.033  11.487  16.598  1.00 17.50           S  
ANISOU 1013  SG  CYS D  15     2347   1884   2419   -283    703   -430       S  
ATOM   1014  N   HIS D  16      14.165  12.229  21.146  1.00 17.39           N  
ANISOU 1014  N   HIS D  16     2551   1818   2238    -15    880   -223       N  
ATOM   1015  CA  HIS D  16      13.819  13.038  22.316  1.00 18.85           C  
ANISOU 1015  CA  HIS D  16     2901   1863   2398     50   1055   -364       C  
ATOM   1016  C   HIS D  16      15.047  13.544  23.038  1.00 22.67           C  
ANISOU 1016  C   HIS D  16     3481   2521   2611     -9    574   -621       C  
ATOM   1017  O   HIS D  16      16.038  12.816  23.083  1.00 23.60           O  
ANISOU 1017  O   HIS D  16     3114   2551   3304   -256    357   -820       O  
ATOM   1018  CB  HIS D  16      12.952  12.203  23.254  1.00 23.29           C  
ANISOU 1018  CB  HIS D  16     3676   2342   2833    141   1663    -18       C  
ATOM   1019  CG  HIS D  16      11.517  12.209  22.913  1.00 28.72           C  
ANISOU 1019  CG  HIS D  16     3504   2773   4637   -506   1721    -65       C  
ATOM   1020  ND1 HIS D  16      10.627  13.108  23.455  1.00 33.06           N  
ANISOU 1020  ND1 HIS D  16     3453   4657   4451    182   1714   -491       N  
ATOM   1021  CD2 HIS D  16      10.792  11.410  22.105  1.00 33.53           C  
ANISOU 1021  CD2 HIS D  16     4529   3819   4391   -200    579   -121       C  
ATOM   1022  CE1 HIS D  16       9.405  12.874  22.980  1.00 37.45           C  
ANISOU 1022  CE1 HIS D  16     3589   5631   5009    103   1342    108       C  
ATOM   1023  NE2 HIS D  16       9.479  11.846  22.156  1.00 37.02           N  
ANISOU 1023  NE2 HIS D  16     4387   5053   4626   -135    152    517       N  
ATOM   1024  N   PRO D  17      14.993  14.780  23.514  1.00 24.62           N  
ANISOU 1024  N   PRO D  17     3340   2897   3117   -146    853  -1185       N  
ATOM   1025  CA  PRO D  17      16.182  15.432  24.056  1.00 28.94           C  
ANISOU 1025  CA  PRO D  17     4039   3469   3488   -139     44  -1436       C  
ATOM   1026  C   PRO D  17      16.821  14.754  25.238  1.00 29.62           C  
ANISOU 1026  C   PRO D  17     4259   3411   3584    363    141  -1403       C  
ATOM   1027  O   PRO D  17      18.071  14.815  25.345  1.00 48.01           O  
ANISOU 1027  O   PRO D  17     4422   7556   6263   -647   -546   2155       O  
ATOM   1028  CB  PRO D  17      15.708  16.829  24.484  1.00 33.08           C  
ANISOU 1028  CB  PRO D  17     5253   3071   4243    -15   -901  -1349       C  
ATOM   1029  CG  PRO D  17      14.267  16.932  24.124  1.00 31.99           C  
ANISOU 1029  CG  PRO D  17     5478   2392   4285    360  -1168   -852       C  
ATOM   1030  CD  PRO D  17      13.829  15.672  23.454  1.00 26.51           C  
ANISOU 1030  CD  PRO D  17     3877   2406   3790    -16    429   -911       C  
ATOM   1031  N   VAL D  18      16.105  14.142  26.167  1.00 29.14           N  
ANISOU 1031  N   VAL D  18     4475   2603   3994  -1119   -809  -1298       N  
ATOM   1032  CA  VAL D  18      16.852  13.634  27.334  1.00 31.26           C  
ANISOU 1032  CA  VAL D  18     4149   3859   3871  -1448   -642   -947       C  
ATOM   1033  C   VAL D  18      16.362  12.273  27.815  1.00 28.89           C  
ANISOU 1033  C   VAL D  18     3978   4046   2951   -934    808   -765       C  
ATOM   1034  O   VAL D  18      17.200  11.447  28.214  1.00 27.63           O  
ANISOU 1034  O   VAL D  18     3882   4047   2569  -1375      5   -899       O  
ATOM   1035  CB  VAL D  18      16.805  14.573  28.554  1.00 29.24           C  
ANISOU 1035  CB  VAL D  18     3698   4195   3219  -1478    307   -647       C  
ATOM   1036  CG1 VAL D  18      17.561  13.941  29.720  1.00 33.76           C  
ANISOU 1036  CG1 VAL D  18     4744   4892   3191   -602    171   -838       C  
ATOM   1037  CG2 VAL D  18      17.384  15.941  28.245  1.00 32.15           C  
ANISOU 1037  CG2 VAL D  18     4454   4101   3659  -1891     62  -1061       C  
ATOM   1038  N   PHE D  19      15.062  12.060  27.813  1.00 27.08           N  
ANISOU 1038  N   PHE D  19     4023   3870   2394  -1067    180   -867       N  
ATOM   1039  CA  PHE D  19      14.424  10.853  28.300  1.00 26.36           C  
ANISOU 1039  CA  PHE D  19     3719   3413   2884   -926    -93  -1124       C  
ATOM   1040  C   PHE D  19      13.390  10.385  27.274  1.00 26.89           C  
ANISOU 1040  C   PHE D  19     4178   2773   3267   -246   -852  -1070       C  
ATOM   1041  O   PHE D  19      12.752  11.234  26.648  1.00 28.50           O  
ANISOU 1041  O   PHE D  19     5522   2732   2576  -1111   -542    323       O  
ATOM   1042  CB  PHE D  19      13.694  11.075  29.621  1.00 25.99           C  
ANISOU 1042  CB  PHE D  19     3427   3943   2505   -631   -209   -171       C  
ATOM   1043  CG  PHE D  19      14.586  11.565  30.750  1.00 21.64           C  
ANISOU 1043  CG  PHE D  19     2653   3420   2151   -699    254    112       C  
ATOM   1044  CD1 PHE D  19      14.604  12.891  31.142  1.00 24.90           C  
ANISOU 1044  CD1 PHE D  19     3823   3524   2114   -241   -146    -98       C  
ATOM   1045  CD2 PHE D  19      15.404  10.669  31.419  1.00 22.86           C  
ANISOU 1045  CD2 PHE D  19     2565   3657   2465    -94    349   -304       C  
ATOM   1046  CE1 PHE D  19      15.439  13.315  32.166  1.00 24.13           C  
ANISOU 1046  CE1 PHE D  19     3764   3245   2157    -73   -195   -104       C  
ATOM   1047  CE2 PHE D  19      16.256  11.092  32.420  1.00 21.78           C  
ANISOU 1047  CE2 PHE D  19     2671   3249   2356   -254    284    142       C  
ATOM   1048  CZ  PHE D  19      16.280  12.411  32.781  1.00 22.02           C  
ANISOU 1048  CZ  PHE D  19     2899   3368   2102    -54    413    -88       C  
ATOM   1049  N   CYS D  20      13.224   9.082  27.140  1.00 21.22           N  
ANISOU 1049  N   CYS D  20     3305   2701   2058   -319    -86   -734       N  
ATOM   1050  CA  CYS D  20      12.152   8.606  26.246  1.00 19.56           C  
ANISOU 1050  CA  CYS D  20     2943   2350   2140   -883    101    113       C  
ATOM   1051  C   CYS D  20      10.808   8.849  26.941  1.00 22.90           C  
ANISOU 1051  C   CYS D  20     3226   3120   2356   -259    306    270       C  
ATOM   1052  O   CYS D  20      10.734   8.844  28.168  1.00 24.37           O  
ANISOU 1052  O   CYS D  20     3448   3500   2312   -340    226   -411       O  
ATOM   1053  CB  CYS D  20      12.297   7.134  25.895  1.00 18.44           C  
ANISOU 1053  CB  CYS D  20     2682   2221   2103   -890    -10    239       C  
ATOM   1054  SG  CYS D  20      13.689   6.756  24.785  1.00 20.70           S  
ANISOU 1054  SG  CYS D  20     2881   2535   2451   -726    166    145       S  
ATOM   1055  N   PRO D  21       9.725   9.024  26.200  1.00 23.13           N  
ANISOU 1055  N   PRO D  21     3364   3036   2391    272    265     47       N  
ATOM   1056  CA  PRO D  21       8.374   9.078  26.785  1.00 25.58           C  
ANISOU 1056  CA  PRO D  21     3376   3617   2725    480    279   -538       C  
ATOM   1057  C   PRO D  21       8.012   7.795  27.526  1.00 26.21           C  
ANISOU 1057  C   PRO D  21     3057   3890   3010    -99    729   -644       C  
ATOM   1058  O   PRO D  21       8.650   6.750  27.374  1.00 26.47           O  
ANISOU 1058  O   PRO D  21     3543   3268   3248   -526   1308   -473       O  
ATOM   1059  CB  PRO D  21       7.450   9.199  25.580  1.00 32.50           C  
ANISOU 1059  CB  PRO D  21     3557   5155   3635    483   -293   -289       C  
ATOM   1060  CG  PRO D  21       8.308   9.741  24.501  1.00 30.37           C  
ANISOU 1060  CG  PRO D  21     4389   4211   2939    997   -369   -122       C  
ATOM   1061  CD  PRO D  21       9.687   9.201  24.745  1.00 24.36           C  
ANISOU 1061  CD  PRO D  21     4059   2749   2448    404    168    387       C  
ATOM   1062  N   ARG D  22       6.963   7.891  28.348  1.00 31.68           N  
ANISOU 1062  N   ARG D  22     3653   4699   3685   -422   1325  -1432       N  
ATOM   1063  CA  ARG D  22       6.439   6.694  28.965  1.00 33.37           C  
ANISOU 1063  CA  ARG D  22     3489   5463   3727   -868   1511  -1197       C  
ATOM   1064  C   ARG D  22       5.854   5.804  27.834  1.00 31.25           C  
ANISOU 1064  C   ARG D  22     3991   4660   3224   -872    842   -224       C  
ATOM   1065  O   ARG D  22       5.195   6.245  26.887  1.00 34.99           O  
ANISOU 1065  O   ARG D  22     4350   4835   4111   -866    374    268       O  
ATOM   1066  CB  ARG D  22       5.359   6.935  30.009  1.00 41.32           C  
ANISOU 1066  CB  ARG D  22     4562   7202   3936   -237   2109   -888       C  
ATOM   1067  CG  ARG D  22       5.526   6.236  31.341  1.00 47.69           C  
ANISOU 1067  CG  ARG D  22     5841   8031   4247    315   2533   -323       C  
ATOM   1068  CD  ARG D  22       4.372   6.603  32.273  1.00 52.55           C  
ANISOU 1068  CD  ARG D  22     5967   8911   5087   -790   3471   -348       C  
ATOM   1069  NE  ARG D  22       3.156   5.890  31.923  1.00 58.76           N  
ANISOU 1069  NE  ARG D  22     6721   8926   6679  -1344   3834  -1544       N  
ATOM   1070  CZ  ARG D  22       1.906   6.253  32.092  1.00 62.42           C  
ANISOU 1070  CZ  ARG D  22     6269   9393   8056  -1216   1922  -2276       C  
ATOM   1071  NH1 ARG D  22       1.597   7.415  32.647  1.00 58.12           N  
ANISOU 1071  NH1 ARG D  22     4909  10828   6348     65   -966  -3419       N  
ATOM   1072  NH2 ARG D  22       0.931   5.445  31.699  1.00 73.40           N  
ANISOU 1072  NH2 ARG D  22     7297   9288  11302  -1753   1506  -2572       N  
ATOM   1073  N   ARG D  23       6.133   4.535  27.974  1.00 29.16           N  
ANISOU 1073  N   ARG D  23     3528   4649   2903  -1082    842     24       N  
ATOM   1074  CA  ARG D  23       5.721   3.419  27.188  1.00 28.50           C  
ANISOU 1074  CA  ARG D  23     3343   4427   3059   -700    337    188       C  
ATOM   1075  C   ARG D  23       6.585   3.320  25.938  1.00 27.91           C  
ANISOU 1075  C   ARG D  23     3695   3963   2947  -1143    398    -11       C  
ATOM   1076  O   ARG D  23       6.207   2.493  25.096  1.00 36.36           O  
ANISOU 1076  O   ARG D  23     5036   4371   4407  -1636   1126  -1231       O  
ATOM   1077  CB  ARG D  23       4.236   3.455  26.786  1.00 34.62           C  
ANISOU 1077  CB  ARG D  23     3344   5241   4567   -848    130    -44       C  
ATOM   1078  CG  ARG D  23       3.330   3.219  27.974  1.00 37.18           C  
ANISOU 1078  CG  ARG D  23     3047   6315   4766   -638    363   -665       C  
ATOM   1079  CD  ARG D  23       1.887   3.624  27.689  1.00 44.98           C  
ANISOU 1079  CD  ARG D  23     3024   7730   6337   -701    -31    -97       C  
ATOM   1080  NE  ARG D  23       1.683   5.047  27.942  1.00 51.18           N  
ANISOU 1080  NE  ARG D  23     3463   8073   7911    470  -1261   -374       N  
ATOM   1081  CZ  ARG D  23       1.115   5.956  27.171  1.00 57.20           C  
ANISOU 1081  CZ  ARG D  23     4072   9149   8514   1411   -895    181       C  
ATOM   1082  NH1 ARG D  23       0.603   5.678  25.974  1.00 55.81           N  
ANISOU 1082  NH1 ARG D  23     2698  10955   7553   -813    -50   1956       N  
ATOM   1083  NH2 ARG D  23       1.041   7.215  27.603  1.00 73.88           N  
ANISOU 1083  NH2 ARG D  23     7713   8834  11523   2202  -1169    225       N  
ATOM   1084  N   TYR D  24       7.649   4.102  25.840  1.00 26.07           N  
ANISOU 1084  N   TYR D  24     3127   3942   2837   -704    117    191       N  
ATOM   1085  CA  TYR D  24       8.612   4.002  24.747  1.00 24.59           C  
ANISOU 1085  CA  TYR D  24     3096   3337   2910   -585    107    116       C  
ATOM   1086  C   TYR D  24       9.920   3.417  25.303  1.00 23.84           C  
ANISOU 1086  C   TYR D  24     3159   2988   2912   -701    194    642       C  
ATOM   1087  O   TYR D  24      10.301   3.647  26.456  1.00 26.55           O  
ANISOU 1087  O   TYR D  24     3358   3625   3106     20      5     59       O  
ATOM   1088  CB  TYR D  24       8.956   5.323  24.061  1.00 20.53           C  
ANISOU 1088  CB  TYR D  24     2849   2783   2170    -70    135   -360       C  
ATOM   1089  CG  TYR D  24       7.953   6.010  23.175  1.00 21.75           C  
ANISOU 1089  CG  TYR D  24     2221   3568   2476   -320    242      9       C  
ATOM   1090  CD1 TYR D  24       6.699   6.389  23.645  1.00 28.45           C  
ANISOU 1090  CD1 TYR D  24     2343   5624   2840    168    119   -351       C  
ATOM   1091  CD2 TYR D  24       8.225   6.281  21.853  1.00 20.94           C  
ANISOU 1091  CD2 TYR D  24     2676   2719   2562   -615    184    229       C  
ATOM   1092  CE1 TYR D  24       5.779   7.019  22.815  1.00 29.92           C  
ANISOU 1092  CE1 TYR D  24     2744   5471   3154    740    358   -151       C  
ATOM   1093  CE2 TYR D  24       7.329   6.902  21.020  1.00 24.85           C  
ANISOU 1093  CE2 TYR D  24     3233   3509   2698    220    377    325       C  
ATOM   1094  CZ  TYR D  24       6.101   7.270  21.498  1.00 30.89           C  
ANISOU 1094  CZ  TYR D  24     3200   4910   3626    526    573    773       C  
ATOM   1095  OH  TYR D  24       5.175   7.895  20.684  1.00 41.35           O  
ANISOU 1095  OH  TYR D  24     4414   7018   4279   2311   1110   1798       O  
ATOM   1096  N   LYS D  25      10.618   2.675  24.455  1.00 21.10           N  
ANISOU 1096  N   LYS D  25     2802   2418   2798   -975   -311    419       N  
ATOM   1097  CA  LYS D  25      11.949   2.181  24.847  1.00 22.81           C  
ANISOU 1097  CA  LYS D  25     2958   2551   3156   -782   -113    833       C  
ATOM   1098  C   LYS D  25      13.050   2.759  23.977  1.00 20.91           C  
ANISOU 1098  C   LYS D  25     2897   2522   2528   -629     33    180       C  
ATOM   1099  O   LYS D  25      12.837   3.024  22.784  1.00 20.76           O  
ANISOU 1099  O   LYS D  25     3412   1993   2485   -610     38     44       O  
ATOM   1100  CB  LYS D  25      11.957   0.664  24.698  1.00 25.29           C  
ANISOU 1100  CB  LYS D  25     3181   2615   3812   -628    231    449       C  
ATOM   1101  CG  LYS D  25      11.151  -0.047  25.764  1.00 31.50           C  
ANISOU 1101  CG  LYS D  25     4380   3162   4424   -851   -266   2018       C  
ATOM   1102  CD ALYS D  25      11.293  -1.548  25.748  0.50 38.67           C  
ANISOU 1102  CD ALYS D  25     5821   3201   5671   -730   -337   1816       C  
ATOM   1103  CD BLYS D  25      11.072  -1.544  25.511  0.50 38.09           C  
ANISOU 1103  CD BLYS D  25     5547   3191   5732   -925   -266   1908       C  
ATOM   1104  CE ALYS D  25      12.677  -2.156  25.699  0.50 41.57           C  
ANISOU 1104  CE ALYS D  25     6512   3525   5758    128   -429    848       C  
ATOM   1105  CE BLYS D  25      12.036  -2.287  26.414  0.50 38.67           C  
ANISOU 1105  CE BLYS D  25     5822   2986   5886      6   -282   1087       C  
ATOM   1106  NZ ALYS D  25      12.862  -3.043  24.506  0.50 54.43           N  
ANISOU 1106  NZ ALYS D  25     8032   5763   6886   -204    -99   -748       N  
ATOM   1107  NZ BLYS D  25      11.759  -3.739  26.568  0.50 25.55           N  
ANISOU 1107  NZ BLYS D  25     2448   3168   4094   -466   -624    740       N  
ATOM   1108  N   GLN D  26      14.230   2.931  24.564  1.00 22.89           N  
ANISOU 1108  N   GLN D  26     2774   2624   3300   -393   -185   1060       N  
ATOM   1109  CA  GLN D  26      15.405   3.414  23.838  1.00 20.55           C  
ANISOU 1109  CA  GLN D  26     2650   2505   2655   -286   -301    719       C  
ATOM   1110  C   GLN D  26      16.029   2.350  22.938  1.00 22.00           C  
ANISOU 1110  C   GLN D  26     2754   1886   3720   -477   -173    545       C  
ATOM   1111  O   GLN D  26      16.332   1.261  23.402  1.00 26.25           O  
ANISOU 1111  O   GLN D  26     3177   2128   4670   -374   -341    880       O  
ATOM   1112  CB  GLN D  26      16.485   3.887  24.829  1.00 23.41           C  
ANISOU 1112  CB  GLN D  26     2893   3131   2872   -404   -519    644       C  
ATOM   1113  CG  GLN D  26      17.678   4.553  24.216  1.00 22.72           C  
ANISOU 1113  CG  GLN D  26     2882   2858   2891   -478   -285    -15       C  
ATOM   1114  CD  GLN D  26      18.745   5.107  25.119  1.00 23.69           C  
ANISOU 1114  CD  GLN D  26     3632   2974   2396   -920   -253   -136       C  
ATOM   1115  OE1 GLN D  26      18.743   4.957  26.351  1.00 35.33           O  
ANISOU 1115  OE1 GLN D  26     4747   6305   2370   -885   -179    -69       O  
ATOM   1116  NE2 GLN D  26      19.721   5.781  24.549  1.00 26.16           N  
ANISOU 1116  NE2 GLN D  26     3220   3526   3193   -969   -324    -80       N  
ATOM   1117  N   ILE D  27      16.233   2.673  21.683  1.00 19.64           N  
ANISOU 1117  N   ILE D  27     2475   1589   3399   -191   -327    -70       N  
ATOM   1118  CA  ILE D  27      16.881   1.835  20.686  1.00 20.93           C  
ANISOU 1118  CA  ILE D  27     2586   1536   3831    163   -565   -162       C  
ATOM   1119  C   ILE D  27      18.152   2.497  20.150  1.00 22.30           C  
ANISOU 1119  C   ILE D  27     2380   2014   4082    213   -232   -731       C  
ATOM   1120  O   ILE D  27      18.799   1.989  19.222  1.00 25.91           O  
ANISOU 1120  O   ILE D  27     2748   2671   4426     22   -149  -1379       O  
ATOM   1121  CB  ILE D  27      15.892   1.431  19.570  1.00 21.05           C  
ANISOU 1121  CB  ILE D  27     2761   1781   3454   -187   -339   -124       C  
ATOM   1122  CG1 ILE D  27      15.401   2.572  18.692  1.00 20.31           C  
ANISOU 1122  CG1 ILE D  27     2593   1693   3432   -531   -591   -159       C  
ATOM   1123  CG2 ILE D  27      14.699   0.711  20.173  1.00 26.61           C  
ANISOU 1123  CG2 ILE D  27     3660   2117   4333  -1210   -516    198       C  
ATOM   1124  CD1 ILE D  27      14.679   2.063  17.452  1.00 20.58           C  
ANISOU 1124  CD1 ILE D  27     2410   2110   3301   -282   -362   -506       C  
ATOM   1125  N   GLY D  28      18.557   3.636  20.680  1.00 18.17           N  
ANISOU 1125  N   GLY D  28     2813   2088   2004   -218   -349    -42       N  
ATOM   1126  CA  GLY D  28      19.736   4.329  20.253  1.00 18.60           C  
ANISOU 1126  CA  GLY D  28     2773   1800   2494    112     27   -141       C  
ATOM   1127  C   GLY D  28      19.833   5.755  20.726  1.00 16.98           C  
ANISOU 1127  C   GLY D  28     2727   1843   1882    -31    296    -37       C  
ATOM   1128  O   GLY D  28      19.132   6.118  21.668  1.00 16.40           O  
ANISOU 1128  O   GLY D  28     2421   1926   1884   -163    200    -41       O  
ATOM   1129  N   THR D  29      20.703   6.538  20.085  1.00 17.74           N  
ANISOU 1129  N   THR D  29     2476   2054   2209   -190    382   -164       N  
ATOM   1130  CA  THR D  29      20.728   7.987  20.269  1.00 17.28           C  
ANISOU 1130  CA  THR D  29     2168   2096   2303   -294    321   -283       C  
ATOM   1131  C   THR D  29      20.416   8.601  18.920  1.00 16.59           C  
ANISOU 1131  C   THR D  29     2121   1705   2477   -511     36   -280       C  
ATOM   1132  O   THR D  29      20.295   7.975  17.887  1.00 17.82           O  
ANISOU 1132  O   THR D  29     2200   2089   2480   -568     -4   -426       O  
ATOM   1133  CB  THR D  29      22.063   8.563  20.772  1.00 19.10           C  
ANISOU 1133  CB  THR D  29     2386   2662   2209   -338     83   -535       C  
ATOM   1134  OG1 THR D  29      23.003   8.550  19.685  1.00 19.61           O  
ANISOU 1134  OG1 THR D  29     2249   2442   2760   -372    352   -222       O  
ATOM   1135  CG2 THR D  29      22.606   7.705  21.901  1.00 21.60           C  
ANISOU 1135  CG2 THR D  29     2735   3022   2449   -595   -141   -265       C  
ATOM   1136  N   CYS D  30      20.269   9.884  18.852  1.00 18.02           N  
ANISOU 1136  N   CYS D  30     2367   1851   2631   -362    299   -275       N  
ATOM   1137  CA  CYS D  30      20.243  10.681  17.643  1.00 17.67           C  
ANISOU 1137  CA  CYS D  30     2619   1436   2657   -414    231   -408       C  
ATOM   1138  C   CYS D  30      21.502  11.534  17.462  1.00 16.95           C  
ANISOU 1138  C   CYS D  30     2455   1502   2484   -235    174   -253       C  
ATOM   1139  O   CYS D  30      21.455  12.505  16.700  1.00 17.52           O  
ANISOU 1139  O   CYS D  30     2492   1719   2447   -253    443    -97       O  
ATOM   1140  CB  CYS D  30      18.950  11.512  17.500  1.00 17.61           C  
ANISOU 1140  CB  CYS D  30     2452   2057   2183   -328    589   -102       C  
ATOM   1141  SG  CYS D  30      17.475  10.440  17.549  1.00 17.45           S  
ANISOU 1141  SG  CYS D  30     2588   1541   2502   -283    488   -254       S  
ATOM   1142  N   GLY D  31      22.626  11.140  18.065  1.00 17.44           N  
ANISOU 1142  N   GLY D  31     2368   1795   2464    -62    331   -348       N  
ATOM   1143  CA  GLY D  31      23.958  11.693  17.816  1.00 18.79           C  
ANISOU 1143  CA  GLY D  31     2454   1959   2726   -262    323   -567       C  
ATOM   1144  C   GLY D  31      24.227  12.998  18.519  1.00 17.35           C  
ANISOU 1144  C   GLY D  31     2468   1965   2160   -108    232   -512       C  
ATOM   1145  O   GLY D  31      25.273  13.217  19.154  1.00 18.31           O  
ANISOU 1145  O   GLY D  31     2461   2054   2440   -329    156   -245       O  
ATOM   1146  N   LEU D  32      23.315  13.943  18.413  1.00 17.31           N  
ANISOU 1146  N   LEU D  32     2145   1865   2567   -315    547   -286       N  
ATOM   1147  CA  LEU D  32      23.443  15.220  19.134  1.00 17.93           C  
ANISOU 1147  CA  LEU D  32     2252   1753   2806   -315    692   -278       C  
ATOM   1148  C   LEU D  32      23.517  14.943  20.638  1.00 19.39           C  
ANISOU 1148  C   LEU D  32     2334   2375   2658   -235    684   -564       C  
ATOM   1149  O   LEU D  32      22.870  14.006  21.115  1.00 19.71           O  
ANISOU 1149  O   LEU D  32     2845   2572   2072   -626     68   -365       O  
ATOM   1150  CB  LEU D  32      22.285  16.148  18.840  1.00 18.86           C  
ANISOU 1150  CB  LEU D  32     2065   1845   3256   -404    468   -455       C  
ATOM   1151  CG  LEU D  32      22.072  16.506  17.359  1.00 23.17           C  
ANISOU 1151  CG  LEU D  32     2686   2491   3626    -22    376    206       C  
ATOM   1152  CD1 LEU D  32      20.873  17.426  17.206  1.00 28.39           C  
ANISOU 1152  CD1 LEU D  32     3688   3350   3749   1024    267   -209       C  
ATOM   1153  CD2 LEU D  32      23.340  17.109  16.788  1.00 26.37           C  
ANISOU 1153  CD2 LEU D  32     3337   2562   4121   -414    461   1003       C  
ATOM   1154  N   PRO D  33      24.264  15.733  21.383  1.00 21.99           N  
ANISOU 1154  N   PRO D  33     3034   2436   2885   -686    742   -615       N  
ATOM   1155  CA  PRO D  33      24.449  15.432  22.821  1.00 22.23           C  
ANISOU 1155  CA  PRO D  33     2843   2792   2812   -958    583   -721       C  
ATOM   1156  C   PRO D  33      23.157  15.217  23.596  1.00 23.42           C  
ANISOU 1156  C   PRO D  33     2838   3194   2868   -854    547   -346       C  
ATOM   1157  O   PRO D  33      22.197  15.968  23.423  1.00 23.37           O  
ANISOU 1157  O   PRO D  33     2823   2844   3214   -856    470  -1015       O  
ATOM   1158  CB  PRO D  33      25.246  16.653  23.313  1.00 24.85           C  
ANISOU 1158  CB  PRO D  33     3559   2717   3165  -1235    637   -673       C  
ATOM   1159  CG  PRO D  33      26.102  16.963  22.123  1.00 26.18           C  
ANISOU 1159  CG  PRO D  33     3884   2810   3253  -1484    671   -490       C  
ATOM   1160  CD  PRO D  33      25.074  16.914  21.000  1.00 24.45           C  
ANISOU 1160  CD  PRO D  33     3461   2635   3195   -915    868   -588       C  
ATOM   1161  N   GLY D  34      23.133  14.149  24.376  1.00 24.94           N  
ANISOU 1161  N   GLY D  34     3273   3156   3046   -968    681   -379       N  
ATOM   1162  CA  GLY D  34      22.073  13.729  25.260  1.00 27.23           C  
ANISOU 1162  CA  GLY D  34     3644   3866   2835  -1576    501   -253       C  
ATOM   1163  C   GLY D  34      20.827  13.202  24.606  1.00 27.63           C  
ANISOU 1163  C   GLY D  34     3584   3779   3136  -1572    789   -985       C  
ATOM   1164  O   GLY D  34      19.877  12.746  25.267  1.00 29.53           O  
ANISOU 1164  O   GLY D  34     3940   4001   3281  -1909    910   -954       O  
ATOM   1165  N   THR D  35      20.721  13.199  23.282  1.00 22.94           N  
ANISOU 1165  N   THR D  35     2801   2706   3208  -1126    639   -741       N  
ATOM   1166  CA  THR D  35      19.478  12.723  22.649  1.00 21.13           C  
ANISOU 1166  CA  THR D  35     2462   2294   3271   -810    931  -1083       C  
ATOM   1167  C   THR D  35      19.297  11.204  22.668  1.00 19.96           C  
ANISOU 1167  C   THR D  35     2485   2271   2826   -625    534   -794       C  
ATOM   1168  O   THR D  35      20.236  10.427  22.656  1.00 21.20           O  
ANISOU 1168  O   THR D  35     2657   2459   2938   -484     62   -712       O  
ATOM   1169  CB  THR D  35      19.381  13.193  21.197  1.00 20.84           C  
ANISOU 1169  CB  THR D  35     2006   2319   3594   -733    597   -538       C  
ATOM   1170  OG1 THR D  35      20.548  12.752  20.479  1.00 19.61           O  
ANISOU 1170  OG1 THR D  35     2221   2340   2892   -673    484   -515       O  
ATOM   1171  CG2 THR D  35      19.377  14.712  21.059  1.00 23.82           C  
ANISOU 1171  CG2 THR D  35     2430   2346   4274   -699    949   -666       C  
ATOM   1172  N   LYS D  36      18.026  10.810  22.678  1.00 17.97           N  
ANISOU 1172  N   LYS D  36     2600   2124   2105   -765    775   -741       N  
ATOM   1173  CA  LYS D  36      17.641   9.404  22.644  1.00 17.19           C  
ANISOU 1173  CA  LYS D  36     2431   2041   2060   -532    344   -540       C  
ATOM   1174  C   LYS D  36      16.732   9.073  21.458  1.00 15.82           C  
ANISOU 1174  C   LYS D  36     2000   1923   2088   -394    418   -434       C  
ATOM   1175  O   LYS D  36      15.861   9.879  21.109  1.00 16.39           O  
ANISOU 1175  O   LYS D  36     2335   1609   2283   -415    380   -387       O  
ATOM   1176  CB  LYS D  36      16.973   8.979  23.957  1.00 19.95           C  
ANISOU 1176  CB  LYS D  36     3146   2347   2088   -776    462   -365       C  
ATOM   1177  CG  LYS D  36      17.909   9.006  25.162  1.00 24.28           C  
ANISOU 1177  CG  LYS D  36     3772   3338   2116  -1206    190   -290       C  
ATOM   1178  CD  LYS D  36      17.475   8.130  26.310  1.00 35.09           C  
ANISOU 1178  CD  LYS D  36     5924   4793   2614  -1011    194    854       C  
ATOM   1179  CE  LYS D  36      18.268   8.355  27.591  1.00 38.16           C  
ANISOU 1179  CE  LYS D  36     6376   4840   3284  -1008   -698   1639       C  
ATOM   1180  NZ  LYS D  36      19.059   7.181  28.047  1.00 48.98           N  
ANISOU 1180  NZ  LYS D  36     6524   6546   5542   1899  -1710  -1446       N  
ATOM   1181  N   CYS D  37      16.917   7.923  20.842  1.00 15.13           N  
ANISOU 1181  N   CYS D  37     2214   1674   1859   -409    101   -206       N  
ATOM   1182  CA  CYS D  37      16.052   7.372  19.804  1.00 14.34           C  
ANISOU 1182  CA  CYS D  37     1779   1716   1955   -243    177   -170       C  
ATOM   1183  C   CYS D  37      15.080   6.405  20.476  1.00 14.11           C  
ANISOU 1183  C   CYS D  37     1966   1293   2104   -194    167   -263       C  
ATOM   1184  O   CYS D  37      15.540   5.432  21.076  1.00 16.01           O  
ANISOU 1184  O   CYS D  37     2153   1459   2470   -187     91    -78       O  
ATOM   1185  CB  CYS D  37      16.823   6.656  18.703  1.00 15.64           C  
ANISOU 1185  CB  CYS D  37     2726   1509   1706   -310    303   -169       C  
ATOM   1186  SG  CYS D  37      15.774   6.084  17.349  1.00 15.15           S  
ANISOU 1186  SG  CYS D  37     2131   1414   2212   -191     73   -132       S  
ATOM   1187  N   CYS D  38      13.796   6.676  20.431  1.00 14.56           N  
ANISOU 1187  N   CYS D  38     1943   1511   2078   -303    225    108       N  
ATOM   1188  CA  CYS D  38      12.731   6.054  21.217  1.00 15.88           C  
ANISOU 1188  CA  CYS D  38     2057   1771   2204   -276    239    318       C  
ATOM   1189  C   CYS D  38      11.590   5.474  20.386  1.00 16.67           C  
ANISOU 1189  C   CYS D  38     1913   2194   2229   -483    470    314       C  
ATOM   1190  O   CYS D  38      11.118   6.094  19.461  1.00 17.31           O  
ANISOU 1190  O   CYS D  38     2153   2225   2198   -455    167    194       O  
ATOM   1191  CB  CYS D  38      12.191   7.106  22.191  1.00 17.57           C  
ANISOU 1191  CB  CYS D  38     2228   2181   2265   -351    528    195       C  
ATOM   1192  SG  CYS D  38      13.385   7.982  23.192  1.00 19.23           S  
ANISOU 1192  SG  CYS D  38     2770   2256   2280   -573    501    -44       S  
ATOM   1193  N   LYS D  39      11.167   4.226  20.696  1.00 19.04           N  
ANISOU 1193  N   LYS D  39     3108   2132   1993   -857    304     11       N  
ATOM   1194  CA  LYS D  39      10.063   3.613  19.954  1.00 20.30           C  
ANISOU 1194  CA  LYS D  39     2994   2160   2557   -688    216   -266       C  
ATOM   1195  C   LYS D  39       9.201   2.789  20.906  1.00 19.43           C  
ANISOU 1195  C   LYS D  39     2769   1859   2756   -625   -230    132       C  
ATOM   1196  O   LYS D  39       9.643   2.149  21.847  1.00 20.43           O  
ANISOU 1196  O   LYS D  39     2392   2414   2957   -640   -393    262       O  
ATOM   1197  CB  LYS D  39      10.538   2.766  18.777  1.00 23.69           C  
ANISOU 1197  CB  LYS D  39     2562   2905   3534   -955    292  -1237       C  
ATOM   1198  CG  LYS D  39       9.464   2.403  17.738  1.00 21.84           C  
ANISOU 1198  CG  LYS D  39     2754   2448   3098  -1158    254   -628       C  
ATOM   1199  CD  LYS D  39      10.075   1.808  16.497  1.00 27.28           C  
ANISOU 1199  CD  LYS D  39     3165   4319   2881   -148   -125   -765       C  
ATOM   1200  CE  LYS D  39       9.039   1.542  15.416  1.00 29.21           C  
ANISOU 1200  CE  LYS D  39     3070   4908   3120  -1020      1   -974       C  
ATOM   1201  NZ  LYS D  39       8.342   0.275  15.678  1.00 30.78           N  
ANISOU 1201  NZ  LYS D  39     3710   4303   3683   -545   -129   -704       N  
ATOM   1202  N   LYS D  40       7.900   2.793  20.632  1.00 22.06           N  
ANISOU 1202  N   LYS D  40     2730   2945   2708   -386   -231    809       N  
ATOM   1203  CA  LYS D  40       6.990   1.931  21.381  1.00 25.77           C  
ANISOU 1203  CA  LYS D  40     2853   3775   3163   -758    160    690       C  
ATOM   1204  C   LYS D  40       7.193   0.471  20.968  1.00 24.88           C  
ANISOU 1204  C   LYS D  40     3244   3573   2635  -1477    -37    670       C  
ATOM   1205  O   LYS D  40       7.236   0.113  19.778  1.00 31.28           O  
ANISOU 1205  O   LYS D  40     5153   4095   2639  -1887   -427    453       O  
ATOM   1206  CB  LYS D  40       5.512   2.229  21.166  1.00 32.00           C  
ANISOU 1206  CB  LYS D  40     2777   5952   3429   -544    231     83       C  
ATOM   1207  CG  LYS D  40       4.934   3.366  21.972  1.00 40.97           C  
ANISOU 1207  CG  LYS D  40     4298   6400   4867   1137     22     85       C  
ATOM   1208  CD  LYS D  40       3.487   3.613  21.568  1.00 43.40           C  
ANISOU 1208  CD  LYS D  40     3938   6888   5664    799    570   1230       C  
ATOM   1209  CE  LYS D  40       2.600   3.650  22.800  1.00 48.55           C  
ANISOU 1209  CE  LYS D  40     5034   7232   6180   1388   1300    583       C  
ATOM   1210  NZ  LYS D  40       1.174   3.934  22.456  1.00 58.66           N  
ANISOU 1210  NZ  LYS D  40     4960  10498   6830   2110   1398   -721       N  
ATOM   1211  N   PRO D  41       7.332  -0.380  21.966  1.00 28.25           N  
ANISOU 1211  N   PRO D  41     4209   3726   2797  -1050   -240    754       N  
ATOM   1212  CA  PRO D  41       7.370  -1.808  21.659  1.00 31.73           C  
ANISOU 1212  CA  PRO D  41     5264   3614   3177  -1578    121    850       C  
ATOM   1213  C   PRO D  41       5.954  -2.225  21.284  1.00 33.39           C  
ANISOU 1213  C   PRO D  41     4800   3512   4374  -1724    938    819       C  
ATOM   1214  O   PRO D  41       4.978  -1.597  21.720  1.00 41.62           O  
ANISOU 1214  O   PRO D  41     5465   4194   6155   -552    -16   -158       O  
ATOM   1215  CB  PRO D  41       7.856  -2.422  22.960  1.00 37.92           C  
ANISOU 1215  CB  PRO D  41     7126   3871   3411   -612    209   1124       C  
ATOM   1216  CG  PRO D  41       7.352  -1.493  23.992  1.00 36.06           C  
ANISOU 1216  CG  PRO D  41     6745   3843   3113   -722   -178   1077       C  
ATOM   1217  CD  PRO D  41       7.493  -0.114  23.391  1.00 31.86           C  
ANISOU 1217  CD  PRO D  41     5582   3929   2595  -1018    442    903       C  
ATOM   1218  OXT PRO D  41       5.867  -3.171  20.524  1.00 37.66           O  
ANISOU 1218  OXT PRO D  41     3882   4748   5677  -1488    558   -461       O  
TER    1219      PRO D  41                                                      
HETATM 1220  S   SO4 D 195      14.524   6.339   1.409  1.00 30.32           S  
ANISOU 1220  S   SO4 D 195     4355   3651   3515   -166    -28    102       S  
HETATM 1221  O1  SO4 D 195      13.652   6.770   2.543  1.00 35.66           O  
ANISOU 1221  O1  SO4 D 195     3495   5918   4138   -644      5   -829       O  
HETATM 1222  O2  SO4 D 195      15.536   5.382   1.897  1.00 31.89           O  
ANISOU 1222  O2  SO4 D 195     4837   2910   4368   -298   -323    103       O  
HETATM 1223  O3  SO4 D 195      15.122   7.499   0.737  1.00 36.17           O  
ANISOU 1223  O3  SO4 D 195     5705   4136   3901    -63   -117   1103       O  
HETATM 1224  O4  SO4 D 195      13.672   5.608   0.412  1.00 39.45           O  
ANISOU 1224  O4  SO4 D 195     5471   5839   3678   -646   -530   -398       O  
HETATM 1225  O   HOH A  42      11.346  35.841  25.819  1.00 28.86           O  
ANISOU 1225  O   HOH A  42     3859   2945   4160     80  -1657   -149       O  
HETATM 1226  O   HOH A  43      20.577  33.971  14.487  1.00 35.02           O  
ANISOU 1226  O   HOH A  43     3065   2999   7243   1063     12  -1394       O  
HETATM 1227  O   HOH A  44      10.290  34.012  23.922  1.00 22.43           O  
ANISOU 1227  O   HOH A  44     3302   2274   2945    188   -427    187       O  
HETATM 1228  O   HOH A  45       1.379  30.248  16.938  1.00 24.01           O  
ANISOU 1228  O   HOH A  45     3042   2525   3555   -632   -426     58       O  
HETATM 1229  O   HOH A  46      11.750  31.872  24.910  1.00 32.48           O  
ANISOU 1229  O   HOH A  46     4548   3352   4440    817    -19   1317       O  
HETATM 1230  O   HOH A  47      18.977  29.096  15.827  1.00 30.68           O  
ANISOU 1230  O   HOH A  47     2215   4514   4930      9    143   -351       O  
HETATM 1231  O   HOH A  48      17.270  37.048  27.369  1.00 59.38           O  
ANISOU 1231  O   HOH A  48    10563   6470   5531  -3173   -157  -2366       O  
HETATM 1232  O   HOH A  49       2.841  32.290   9.231  1.00 26.74           O  
ANISOU 1232  O   HOH A  49     3512   2779   3867   -529   -975   -102       O  
HETATM 1233  O   HOH A  50      14.725  42.944   9.499  1.00 39.17           O  
ANISOU 1233  O   HOH A  50     4955   5466   4464   -642   1072   1589       O  
HETATM 1234  O   HOH A  51       9.195  30.492   7.755  1.00 38.21           O  
ANISOU 1234  O   HOH A  51     5880   4494   4144   1274    141  -1606       O  
HETATM 1235  O   HOH A  52      12.912  35.814   3.800  0.50 65.72           O  
ANISOU 1235  O   HOH A  52     4044   6098  14830   1484   1796    534       O  
HETATM 1236  O   HOH A  53       6.980  33.444  26.504  1.00 43.39           O  
ANISOU 1236  O   HOH A  53     5404   7772   3309   -575   -290   2466       O  
HETATM 1237  O   HOH A  54      14.879  35.735   7.884  1.00 36.66           O  
ANISOU 1237  O   HOH A  54     6576   3844   3512   -325   1260   -793       O  
HETATM 1238  O   HOH A  55      16.021  32.925   7.912  1.00 34.69           O  
ANISOU 1238  O   HOH A  55     5184   4177   3820    472   -388   -103       O  
HETATM 1239  O   HOH A  56      10.932  31.226  29.097  1.00 69.35           O  
ANISOU 1239  O   HOH A  56     9073   7577   9701  -1431  -3778  -2500       O  
HETATM 1240  O   HOH A  57       3.251  32.064   6.299  1.00 40.36           O  
ANISOU 1240  O   HOH A  57     4472   5304   5557     60   -214  -2095       O  
HETATM 1241  O   HOH A  58      13.087  29.338   9.619  1.00 30.33           O  
ANISOU 1241  O   HOH A  58     3448   3622   4454    983    990   -863       O  
HETATM 1242  O   HOH A  59      -1.061  29.911  15.331  1.00 38.70           O  
ANISOU 1242  O   HOH A  59     2445   7157   5103  -1064   -460   1793       O  
HETATM 1243  O   HOH A  60      10.376  30.394  27.030  1.00 50.88           O  
ANISOU 1243  O   HOH A  60     5565   8069   5699  -1203  -1526   1494       O  
HETATM 1244  O   HOH A  61       8.413  35.587  28.115  1.00 52.84           O  
ANISOU 1244  O   HOH A  61     8686   6408   4983   3390   1074    199       O  
HETATM 1245  O   HOH A  62      10.443  27.021  24.711  1.00 37.41           O  
ANISOU 1245  O   HOH A  62     4528   3921   5765    457  -1080   1384       O  
HETATM 1246  O   HOH A  63      14.289  31.584   6.774  0.50 65.35           O  
ANISOU 1246  O   HOH A  63     3175   4087  17568    564   1512  -2479       O  
HETATM 1247  O   HOH A  64      11.767  36.679   6.055  1.00 48.97           O  
ANISOU 1247  O   HOH A  64     5822   5050   7736   -122   1284   1981       O  
HETATM 1248  O   HOH A  65      19.295  31.586  13.279  1.00 39.88           O  
ANISOU 1248  O   HOH A  65     2460   5238   7454    536    108    445       O  
HETATM 1249  O   HOH A  66      14.333  45.486   9.851  1.00 31.45           O  
ANISOU 1249  O   HOH A  66     3145   3361   5444   1033   1229    417       O  
HETATM 1250  O   HOH A  67      15.030  38.639  26.212  1.00 39.36           O  
ANISOU 1250  O   HOH A  67     3710   6753   4494    123   -754   -103       O  
HETATM 1251  O   HOH A  68       9.423  34.368   5.566  1.00 48.28           O  
ANISOU 1251  O   HOH A  68     7721   7470   3151   -368    697    544       O  
HETATM 1252  O   HOH A  69      19.006  41.878  20.877  1.00 32.46           O  
ANISOU 1252  O   HOH A  69     3786   4275   4272    483  -1123  -1186       O  
HETATM 1253  O   HOH A  70      21.459  40.301  22.157  1.00 40.11           O  
ANISOU 1253  O   HOH A  70     6292   4241   4709    177    140   -777       O  
HETATM 1254  O   HOH A  71      15.177  27.811  10.696  1.00 45.52           O  
ANISOU 1254  O   HOH A  71     3703   4898   8694    222  -1806   1168       O  
HETATM 1255  O   HOH A  72      14.717  46.977   7.901  1.00 48.20           O  
ANISOU 1255  O   HOH A  72     4513   9815   3985    966   1131   1727       O  
HETATM 1256  O   HOH A  73       5.925  34.422   5.232  1.00 38.79           O  
ANISOU 1256  O   HOH A  73     7013   3112   4612    220    208   -763       O  
HETATM 1257  O   HOH A  74      24.545  30.749  22.062  1.00 58.15           O  
ANISOU 1257  O   HOH A  74     7317   5738   9040   -532  -2739    375       O  
HETATM 1258  O   HOH A  75       3.228  28.462   4.440  1.00 57.10           O  
ANISOU 1258  O   HOH A  75     5400   9836   6457  -1151   -875  -1691       O  
HETATM 1259  O   HOH A  76      16.592  27.345  27.287  1.00 45.49           O  
ANISOU 1259  O   HOH A  76     5164   6636   5482   1426  -1199   1966       O  
HETATM 1260  O   HOH A  77      21.009  32.591  31.200  1.00 47.47           O  
ANISOU 1260  O   HOH A  77     4599   3773   9665  -1058    409    433       O  
HETATM 1261  O   HOH A  78      16.200  27.037  13.161  1.00 47.45           O  
ANISOU 1261  O   HOH A  78     6560   4412   7055   1157   -130  -2130       O  
HETATM 1262  O   HOH A  79      18.867  37.283  25.250  1.00 47.53           O  
ANISOU 1262  O   HOH A  79     5230   5750   7079    484  -1220  -2211       O  
HETATM 1263  O   HOH A  80      17.162  39.121  24.668  0.50 47.24           O  
ANISOU 1263  O   HOH A  80     8778   4056   5112   1829    495   -428       O  
HETATM 1264  O   HOH A  81       5.152  23.551   8.175  1.00 46.07           O  
ANISOU 1264  O   HOH A  81     6130   6133   5242   1293  -3573    -85       O  
HETATM 1265  O   HOH A  82      18.907  22.498  21.391  1.00 57.42           O  
ANISOU 1265  O   HOH A  82     7199   8258   6360   2096  -2121   1120       O  
HETATM 1266  O   HOH A  83      17.465  42.580   8.572  1.00 41.58           O  
ANISOU 1266  O   HOH A  83     5233   4497   6068    264    686    312       O  
HETATM 1267  O   HOH A  84      14.886  36.929   4.045  1.00 56.22           O  
ANISOU 1267  O   HOH A  84     5398   6668   9296     88   -339   1925       O  
HETATM 1268  O   HOH A  85      18.347  28.585  26.065  1.00 51.99           O  
ANISOU 1268  O   HOH A  85     6327   7180   6246   -235  -3588   1527       O  
HETATM 1269  O   HOH A  86      23.479  42.206  20.641  1.00 54.26           O  
ANISOU 1269  O   HOH A  86     6303   9480   4833   1086     22  -1134       O  
HETATM 1270  O   HOH A  87      18.792  41.272  26.766  1.00 64.42           O  
ANISOU 1270  O   HOH A  87     5810  12381   6287   1824   1345   1909       O  
HETATM 1271  O   HOH A  88       9.600  37.299   3.269  1.00 53.77           O  
ANISOU 1271  O   HOH A  88     7751   6304   6375   -627  -3098   2395       O  
HETATM 1272  O   HOH A  89      13.406  44.149   6.416  1.00 47.97           O  
ANISOU 1272  O   HOH A  89     4995   6389   6841  -2565  -1938   2445       O  
HETATM 1273  O   HOH A  90       7.095  36.332   2.884  1.00 47.11           O  
ANISOU 1273  O   HOH A  90     5287   6940   5671  -1858  -1236  -1185       O  
HETATM 1274  O   HOH A  91       3.878  29.717   6.791  1.00 72.43           O  
ANISOU 1274  O   HOH A  91     8385  11176   7961   -644  -4008   -738       O  
HETATM 1275  O   HOH A  92       6.832  28.923  20.160  1.00 45.44           O  
ANISOU 1275  O   HOH A  92     4255   5784   7226    758   -326   2473       O  
HETATM 1276  O   HOH A  93      30.681  37.484  25.725  1.00 68.53           O  
HETATM 1277  O   HOH B  42      16.730 -13.029   1.215  1.00 23.21           O  
ANISOU 1277  O   HOH B  42     3346   2768   2705   -120   -854   -369       O  
HETATM 1278  O   HOH B  43      14.224 -13.362   1.932  1.00 24.16           O  
ANISOU 1278  O   HOH B  43     2890   2750   3540    -23   -428   -529       O  
HETATM 1279  O   HOH B  44      23.758   0.228   7.047  1.00 29.72           O  
ANISOU 1279  O   HOH B  44     2553   3256   5485   -602    -35    881       O  
HETATM 1280  O   HOH B  45      10.843 -12.459  -0.327  1.00 36.65           O  
ANISOU 1280  O   HOH B  45     6152   3255   4518  -1314   -614    115       O  
HETATM 1281  O   HOH B  46      14.156   0.289  -0.400  1.00 37.10           O  
ANISOU 1281  O   HOH B  46     4822   5162   4114    907  -2192    320       O  
HETATM 1282  O   HOH B  47      23.601  -6.137   2.600  1.00 31.34           O  
ANISOU 1282  O   HOH B  47     3516   3661   4732   -319   1412    556       O  
HETATM 1283  O   HOH B  48      16.625  -4.979  -3.077  1.00 65.55           O  
ANISOU 1283  O   HOH B  48     7643   5443  11818  -3279  -2070   1342       O  
HETATM 1284  O   HOH B  49       6.955  -5.781  13.780  1.00 34.74           O  
ANISOU 1284  O   HOH B  49     2987   4856   5356   -572    911   -556       O  
HETATM 1285  O   HOH B  50       6.444  -7.950  -0.979  1.00 37.29           O  
ANISOU 1285  O   HOH B  50     3385   5012   5770    730   -617   1083       O  
HETATM 1286  O   HOH B  51      23.176  -6.840  16.953  1.00 29.38           O  
ANISOU 1286  O   HOH B  51     3893   3626   3642   -284   1008    626       O  
HETATM 1287  O   HOH B  52       9.056 -10.956   5.958  1.00 30.94           O  
ANISOU 1287  O   HOH B  52     2457   5449   3851   -173   -802    901       O  
HETATM 1288  O   HOH B  53      22.410   2.727  12.764  1.00 29.60           O  
ANISOU 1288  O   HOH B  53     3186   4324   3736   -552    201   -473       O  
HETATM 1289  O   HOH B  54      22.968  -0.406  13.760  1.00 37.62           O  
ANISOU 1289  O   HOH B  54     8056   3314   2924   -459  -1763    464       O  
HETATM 1290  O   HOH B  55      23.078  -3.523  19.165  1.00 48.20           O  
ANISOU 1290  O   HOH B  55     9389   5652   3274   -361  -1647   -853       O  
HETATM 1291  O   HOH B  56      27.781  -6.903   1.774  1.00 32.61           O  
ANISOU 1291  O   HOH B  56     4129   4568   3695  -1253   -851   1201       O  
HETATM 1292  O   HOH B  57      16.953  -5.849  -0.985  1.00 34.87           O  
ANISOU 1292  O   HOH B  57     3277   6645   3327  -2222    571    208       O  
HETATM 1293  O   HOH B  58       8.353 -10.395  -2.277  1.00 32.13           O  
ANISOU 1293  O   HOH B  58     4397   4117   3694  -1244    378  -1400       O  
HETATM 1294  O   HOH B  59       8.845  -1.387  11.707  1.00 27.91           O  
ANISOU 1294  O   HOH B  59     3770   2896   3938   -221    316    192       O  
HETATM 1295  O   HOH B  60       7.540  -5.714  16.656  1.00 34.72           O  
ANISOU 1295  O   HOH B  60     5272   4072   3849     15    634     85       O  
HETATM 1296  O   HOH B  61      13.340 -12.104  -0.088  1.00 33.37           O  
ANISOU 1296  O   HOH B  61     4172   4214   4294  -1297   -437  -1315       O  
HETATM 1297  O   HOH B  62      25.933  -6.275   5.335  1.00 34.90           O  
ANISOU 1297  O   HOH B  62     2655   5490   5115    -28   -254   2090       O  
HETATM 1298  O   HOH B  63       5.991  -0.629   9.179  1.00 37.42           O  
ANISOU 1298  O   HOH B  63     3777   5110   5330     41    238  -1276       O  
HETATM 1299  O   HOH B  64      26.025  -4.301  19.672  1.00 50.10           O  
ANISOU 1299  O   HOH B  64     4389  10960   3687   2110    581    954       O  
HETATM 1300  O   HOH B  65      20.277   0.857   3.566  1.00 47.11           O  
ANISOU 1300  O   HOH B  65     4335   6093   7471  -1509  -2531   2132       O  
HETATM 1301  O   HOH B  66      18.886  -4.575  25.162  1.00 41.48           O  
ANISOU 1301  O   HOH B  66     4072   5110   6580   -350   -530   1138       O  
HETATM 1302  O   HOH B  67       5.550  -7.806  12.624  1.00 36.79           O  
ANISOU 1302  O   HOH B  67     4775   4080   5124    -35    771   -242       O  
HETATM 1303  O   HOH B  68      26.099 -13.550   5.442  1.00 44.03           O  
ANISOU 1303  O   HOH B  68     6049   5597   5083   1084   -982  -1992       O  
HETATM 1304  O   HOH B  69       2.643  -7.701  14.090  1.00 65.06           O  
ANISOU 1304  O   HOH B  69     4346   5615  14760   1600  -1201  -1761       O  
HETATM 1305  O   HOH B  70       8.769   4.491   4.022  1.00 60.73           O  
ANISOU 1305  O   HOH B  70    12226   4045   6803  -1227   1553   -412       O  
HETATM 1306  O   HOH B  71      23.101  -3.746   1.451  1.00 43.01           O  
ANISOU 1306  O   HOH B  71     6260   4974   5107   -696    663    781       O  
HETATM 1307  O   HOH B  72      18.300   3.564   5.549  1.00 35.61           O  
ANISOU 1307  O   HOH B  72     3169   3744   6619   -198   -212     15       O  
HETATM 1308  O   HOH B  73      24.686  -4.286  -1.242  0.50 48.39           O  
ANISOU 1308  O   HOH B  73     8223   5120   5043   2704  -1707    301       O  
HETATM 1309  O   HOH B  74      14.459  -7.029  -3.033  1.00 30.54           O  
ANISOU 1309  O   HOH B  74     4424   4020   3159   -372      3    263       O  
HETATM 1310  O   HOH B  75      23.372 -13.683   3.655  1.00 53.53           O  
ANISOU 1310  O   HOH B  75     5285   5103   9951   1091    457  -1225       O  
HETATM 1311  O   HOH B  76      15.577  -1.127  -1.637  1.00 47.10           O  
ANISOU 1311  O   HOH B  76     6450   7222   4225  -1955    553  -1038       O  
HETATM 1312  O   HOH B  77       2.568  -9.220  -5.723  1.00 64.36           O  
ANISOU 1312  O   HOH B  77     6989  10988   6477  -1217    221   3959       O  
HETATM 1313  O   HOH B  78      17.471   2.418   0.801  1.00 63.20           O  
ANISOU 1313  O   HOH B  78     9816   6143   8052   -474  -1399  -2321       O  
HETATM 1314  O   HOH B  79       8.388  -3.464  10.052  1.00 33.68           O  
ANISOU 1314  O   HOH B  79     4827   4812   3159     33     34    840       O  
HETATM 1315  O   HOH B  80      19.334  -0.936  19.459  1.00 50.34           O  
ANISOU 1315  O   HOH B  80     8028   6129   4970    555  -1039  -2836       O  
HETATM 1316  O   HOH B  81      22.973  -9.306  -1.302  1.00 45.02           O  
ANISOU 1316  O   HOH B  81     6512   5450   5144   -500   -886  -1033       O  
HETATM 1317  O   HOH B  82      24.150 -15.877  -1.014  1.00 53.34           O  
ANISOU 1317  O   HOH B  82     7558   7585   5122  -1275    438   1753       O  
HETATM 1318  O   HOH B  83      13.482   4.815   4.685  1.00 66.50           O  
ANISOU 1318  O   HOH B  83    10638   8949   5679   -785  -3844  -1739       O  
HETATM 1319  O   HOH C  42       8.781  27.851  10.919  1.00 22.65           O  
ANISOU 1319  O   HOH C  42     3088   2271   3247    284   -654   -382       O  
HETATM 1320  O   HOH C  43      16.190  22.620   7.287  1.00 35.31           O  
ANISOU 1320  O   HOH C  43     4668   3474   5273   -791   -652   -574       O  
HETATM 1321  O   HOH C  44       9.126  18.258   3.499  1.00 52.09           O  
ANISOU 1321  O   HOH C  44     5476   8071   6244   1714  -2125  -1456       O  
HETATM 1322  O   HOH C  45      -2.896  16.751  16.190  1.00 41.98           O  
ANISOU 1322  O   HOH C  45     3728   6998   5224   1203   -440  -1666       O  
HETATM 1323  O   HOH C  46       9.428  21.180  21.587  1.00 34.69           O  
ANISOU 1323  O   HOH C  46     4416   4139   4625    603   -258    778       O  
HETATM 1324  O   HOH C  47      12.154  13.505  16.939  1.00 21.27           O  
ANISOU 1324  O   HOH C  47     3282   2200   2600    648    -82    278       O  
HETATM 1325  O   HOH C  48       5.430  26.449  20.324  1.00 35.96           O  
ANISOU 1325  O   HOH C  48     3562   5319   4784    273   1001    164       O  
HETATM 1326  O   HOH C  49      16.151  16.974   4.439  1.00 46.08           O  
ANISOU 1326  O   HOH C  49     5007   6188   6313    551   1631  -1782       O  
HETATM 1327  O   HOH C  50      22.921  20.158  19.168  1.00 42.82           O  
ANISOU 1327  O   HOH C  50     5514   4636   6118  -1143    984  -1018       O  
HETATM 1328  O   HOH C  51      20.572  24.783  12.946  1.00 38.96           O  
ANISOU 1328  O   HOH C  51     2841   7129   4832   -265    588    449       O  
HETATM 1329  O   HOH C  52       0.247  23.422  14.307  1.00 44.71           O  
ANISOU 1329  O   HOH C  52     5027   6503   5457    251    851    542       O  
HETATM 1330  O   HOH C  53      11.590  14.238   1.118  1.00 40.86           O  
ANISOU 1330  O   HOH C  53     6074   6468   2984   1850   -423   -156       O  
HETATM 1331  O   HOH C  54      -2.016  13.811   6.528  1.00 39.10           O  
ANISOU 1331  O   HOH C  54     3816   4684   6358   -375   1104    934       O  
HETATM 1332  O   HOH C  55       2.497  27.540  14.057  1.00 40.67           O  
ANISOU 1332  O   HOH C  55     6093   4112   5250   -310  -1167   -130       O  
HETATM 1333  O   HOH C  56      21.521  22.349  11.103  1.00 37.50           O  
ANISOU 1333  O   HOH C  56     3706   5443   5100    675     73    477       O  
HETATM 1334  O   HOH C  57       5.827  16.364   6.046  1.00 37.93           O  
ANISOU 1334  O   HOH C  57     5510   4056   4844  -1621   -813   -447       O  
HETATM 1335  O   HOH C  58      20.392  23.934   9.226  1.00 60.55           O  
ANISOU 1335  O   HOH C  58     5154  11906   5947  -1077   2963   -725       O  
HETATM 1336  O   HOH C  59      19.540  15.823   8.189  1.00 40.05           O  
ANISOU 1336  O   HOH C  59     4078   3719   7421   1731    503    133       O  
HETATM 1337  O   HOH C  60      -1.703  17.990   8.798  1.00 51.85           O  
ANISOU 1337  O   HOH C  60     4666   6712   8323   -746  -1831   3147       O  
HETATM 1338  O   HOH C  61       2.446  27.330  20.728  1.00 39.78           O  
ANISOU 1338  O   HOH C  61     5955   3578   5582   1005   -650   -539       O  
HETATM 1339  O   HOH C  62      11.018  28.631   8.800  1.00 34.59           O  
ANISOU 1339  O   HOH C  62     4659   4163   4320   -298   -853  -1109       O  
HETATM 1340  O   HOH C  63      17.396  24.690   6.187  1.00 57.89           O  
ANISOU 1340  O   HOH C  63    10391   5932   5673   -866   2844    377       O  
HETATM 1341  O   HOH C  64      -0.241  17.912  13.065  1.00 43.29           O  
ANISOU 1341  O   HOH C  64     5311   6500   4636   1104  -1231   -649       O  
HETATM 1342  O   HOH C  65      18.256  15.294   5.872  1.00 50.03           O  
ANISOU 1342  O   HOH C  65     8274   4959   5775  -1953    942   -260       O  
HETATM 1343  O   HOH C  66       9.274  25.852   8.009  1.00 37.96           O  
ANISOU 1343  O   HOH C  66     6136   3848   4438   1501    841   -696       O  
HETATM 1344  O   HOH C  67      17.314  18.859   2.544  1.00 46.96           O  
ANISOU 1344  O   HOH C  67     6111   4104   7627    -44  -1972    891       O  
HETATM 1345  O   HOH C  68      -0.381  15.401   8.850  1.00 43.42           O  
ANISOU 1345  O   HOH C  68     4659   6762   5077   1551  -1213    878       O  
HETATM 1346  O   HOH C  69       4.459  19.823  29.126  1.00 54.62           O  
ANISOU 1346  O   HOH C  69     6294  10349   4108   2221    -66   1124       O  
HETATM 1347  O   HOH C  70       2.917  16.496   7.270  1.00 45.37           O  
ANISOU 1347  O   HOH C  70     3935   5546   7756   -157   -859    744       O  
HETATM 1348  O   HOH C  71      21.241  27.487  15.913  1.00 56.77           O  
ANISOU 1348  O   HOH C  71     4775  10307   6486  -2064   1012   -591       O  
HETATM 1349  O   HOH C  72       8.155  26.644  23.031  1.00 58.12           O  
ANISOU 1349  O   HOH C  72     8690   3079  10312   -958   3552   -353       O  
HETATM 1350  O   HOH C  73      13.254  26.838  20.706  1.00 33.03           O  
ANISOU 1350  O   HOH C  73     4416   3356   4779    435    409     25       O  
HETATM 1351  O   HOH C  74       8.346  16.664  23.848  1.00 56.39           O  
ANISOU 1351  O   HOH C  74    11134   5389   4902   2505    507   1655       O  
HETATM 1352  O   HOH C  75       0.726  29.267  19.545  1.00 33.19           O  
ANISOU 1352  O   HOH C  75     4297   4373   3940  -1173    502   -325       O  
HETATM 1353  O   HOH C  76      10.417  12.473  -0.461  1.00 49.50           O  
ANISOU 1353  O   HOH C  76     6586   6565   5658   2150   2832    627       O  
HETATM 1354  O   HOH C  77      14.424  16.141   2.605  1.00 60.77           O  
ANISOU 1354  O   HOH C  77     7880   9080   6129   3303  -2706  -3388       O  
HETATM 1355  O   HOH C  78       6.978  15.262  21.611  1.00 39.35           O  
ANISOU 1355  O   HOH C  78     4221   6249   4479   1090    158   1633       O  
HETATM 1356  O   HOH C  79       5.541  25.567  25.374  0.50 44.11           O  
ANISOU 1356  O   HOH C  79     2881   9820   4058  -1518   1112  -3616       O  
HETATM 1357  O   HOH C  80       8.819  15.935   4.639  1.00 55.35           O  
ANISOU 1357  O   HOH C  80     5285  11588   4157   1442   -737   -882       O  
HETATM 1358  O   HOH C  81      19.288  20.548   4.736  1.00 55.50           O  
ANISOU 1358  O   HOH C  81     6252   8258   6577  -1368    540   2944       O  
HETATM 1359  O   HOH C  82      17.719  25.086  13.750  1.00 40.84           O  
ANISOU 1359  O   HOH C  82     4980   3391   7146  -1175   1414   -464       O  
HETATM 1360  O   HOH C  83       2.242   9.716  14.063  1.00 56.03           O  
ANISOU 1360  O   HOH C  83     4910   7599   8781   1812   1276   3305       O  
HETATM 1361  O   HOH C  84       3.426  16.243  25.958  0.50 56.30           O  
ANISOU 1361  O   HOH C  84     4769   4367  12256    426   1182   3021       O  
HETATM 1362  O   HOH C  85       8.174   8.404   5.959  1.00 42.88           O  
ANISOU 1362  O   HOH C  85     7439   4583   4271   -162   2510    161       O  
HETATM 1363  O   HOH C  86       1.368   8.494  18.564  1.00 64.20           O  
ANISOU 1363  O   HOH C  86     6755   8697   8941   3672    650   1788       O  
HETATM 1364  O   HOH C  87      20.227  18.220   1.080  1.00 71.17           O  
ANISOU 1364  O   HOH C  87    12004   8422   6614  -1829  -2942   2373       O  
HETATM 1365  O   HOH C  88      18.644  18.551  21.130  0.50 43.87           O  
ANISOU 1365  O   HOH C  88     4749   6076   5845   1913    174   1273       O  
HETATM 1366  O   HOH C  89      -0.323  20.219  16.872  1.00 53.67           O  
ANISOU 1366  O   HOH C  89     9257   4276   6860   3348  -1403   -855       O  
HETATM 1367  O   HOH C  90       6.055  10.351   8.914  1.00 55.82           O  
ANISOU 1367  O   HOH C  90     6572   4564  10072  -2574  -2394   -104       O  
HETATM 1368  O   HOH C  91      18.897  26.295  16.034  1.00 52.41           O  
ANISOU 1368  O   HOH C  91     7660   4707   7547   -681  -3015    100       O  
HETATM 1369  O   HOH D 196      23.288   5.902  13.207  1.00 16.68           O  
ANISOU 1369  O   HOH D 196     2306   1559   2473    235    596     51       O  
HETATM 1370  O   HOH D 197      11.440  -0.436  11.784  1.00 21.02           O  
ANISOU 1370  O   HOH D 197     3074   1925   2988   -454    179      6       O  
HETATM 1371  O   HOH D 198      22.728  10.521  23.811  1.00 32.79           O  
ANISOU 1371  O   HOH D 198     3328   3826   5307   -334    453   -580       O  
HETATM 1372  O   HOH D 199       6.326   4.058  18.403  1.00 23.39           O  
ANISOU 1372  O   HOH D 199     2525   3414   2949    436    332    807       O  
HETATM 1373  O   HOH D 200      15.466  -1.276  23.923  1.00 25.83           O  
ANISOU 1373  O   HOH D 200     3928   3026   2860   -119    -42    754       O  
HETATM 1374  O   HOH D 201       5.524  10.582  28.444  1.00 40.41           O  
ANISOU 1374  O   HOH D 201     2846   8310   4199    755   -548  -2304       O  
HETATM 1375  O   HOH D 202      26.540   9.721  16.748  1.00 29.93           O  
ANISOU 1375  O   HOH D 202     3102   3840   4429    900   -312  -1450       O  
HETATM 1376  O   HOH D 203       6.131   3.870  13.985  1.00 39.15           O  
ANISOU 1376  O   HOH D 203     3702   6437   4736    428   -949   -418       O  
HETATM 1377  O   HOH D 204       7.723   6.035  17.315  1.00 30.32           O  
ANISOU 1377  O   HOH D 204     3363   5071   3086    448    893   -132       O  
HETATM 1378  O   HOH D 205      27.041  11.010  19.096  1.00 25.24           O  
ANISOU 1378  O   HOH D 205     2474   3050   4068   -174     86   -739       O  
HETATM 1379  O   HOH D 206      14.879  -4.019  26.830  1.00 39.14           O  
ANISOU 1379  O   HOH D 206     5044   3368   6460   -377    937   1511       O  
HETATM 1380  O   HOH D 207      25.830   7.088  19.779  1.00 38.89           O  
ANISOU 1380  O   HOH D 207     3800   6391   4586   -206    923   -695       O  
HETATM 1381  O   HOH D 208      23.374  -0.998  20.191  1.00 42.88           O  
ANISOU 1381  O   HOH D 208     5260   5024   6008  -1720  -2161    723       O  
HETATM 1382  O   HOH D 209      22.196   6.280  25.825  1.00 55.01           O  
ANISOU 1382  O   HOH D 209     5850   9744   5307  -1527  -1155   -931       O  
HETATM 1383  O   HOH D 210       6.925  -1.649  14.048  1.00 33.71           O  
ANISOU 1383  O   HOH D 210     3972   5286   3550    169   -257    449       O  
HETATM 1384  O   HOH D 211      28.881  11.599  20.495  1.00 37.07           O  
ANISOU 1384  O   HOH D 211     5230   4609   4246  -1377    166   -891       O  
HETATM 1385  O   HOH D 212      12.870  -1.699  22.402  1.00 29.97           O  
ANISOU 1385  O   HOH D 212     3877   3773   3737   -313    -66    766       O  
HETATM 1386  O   HOH D 213      25.743  12.995  25.092  1.00 42.06           O  
ANISOU 1386  O   HOH D 213     6309   5395   4277    590   -619   1198       O  
HETATM 1387  O   HOH D 214       9.227   7.748  11.886  1.00 42.44           O  
ANISOU 1387  O   HOH D 214     2617   3167  10340    686   -176   1108       O  
HETATM 1388  O   HOH D 215      13.682  14.346  26.701  1.00 52.16           O  
ANISOU 1388  O   HOH D 215    11335   3532   4949    183  -1139   -861       O  
HETATM 1389  O   HOH D 216      10.735   4.953  28.905  1.00 30.05           O  
ANISOU 1389  O   HOH D 216     3648   4182   3588   -798    187    343       O  
HETATM 1390  O   HOH D 217      20.080   7.480   7.484  1.00 32.80           O  
ANISOU 1390  O   HOH D 217     3481   5109   3874   1219    -64    220       O  
HETATM 1391  O   HOH D 218      21.091  19.432  20.759  1.00 51.25           O  
ANISOU 1391  O   HOH D 218     4654   9911   4910   -970   -632  -1770       O  
HETATM 1392  O   HOH D 219       1.354   8.364  30.348  1.00 51.21           O  
ANISOU 1392  O   HOH D 219     7491   7434   4531   -887    300  -1130       O  
HETATM 1393  O   HOH D 220      23.797  11.508  21.877  1.00 42.00           O  
ANISOU 1393  O   HOH D 220     6944   4529   4484    208    319    111       O  
HETATM 1394  O   HOH D 221      29.361  14.726  24.134  1.00 57.49           O  
ANISOU 1394  O   HOH D 221    11244   5970   4630    858    445  -2869       O  
HETATM 1395  O   HOH D 222       5.362   7.793  17.801  1.00 45.51           O  
ANISOU 1395  O   HOH D 222     5229   5720   6341   -194   2570  -2397       O  
HETATM 1396  O   HOH D 223      11.405   7.846  30.615  1.00 37.98           O  
ANISOU 1396  O   HOH D 223     7078   3923   3429   -275   1433    346       O  
HETATM 1397  O   HOH D 224      10.563  -0.377  21.820  1.00 37.86           O  
ANISOU 1397  O   HOH D 224     4976   5054   4356  -1046  -1680    456       O  
HETATM 1398  O   HOH D 225      15.729   3.606   4.003  1.00 31.08           O  
ANISOU 1398  O   HOH D 225     4703   3268   3837    -57    273   -162       O  
HETATM 1399  O   HOH D 226      18.522   8.650   2.689  1.00 37.17           O  
ANISOU 1399  O   HOH D 226     5121   3921   5080   -300   -725   -539       O  
HETATM 1400  O   HOH D 227      27.554   6.197  21.992  0.50 43.86           O  
ANISOU 1400  O   HOH D 227     4751   8182   3730  -1304   1757   1125       O  
HETATM 1401  O   HOH D 228      18.909  11.249   1.926  1.00 47.92           O  
ANISOU 1401  O   HOH D 228     3325   9184   5698    474  -1697   -310       O  
HETATM 1402  O   HOH D 229       7.073  -2.745  16.744  1.00 50.61           O  
ANISOU 1402  O   HOH D 229     8900   3859   6470  -1749   -476  -1006       O  
HETATM 1403  O   HOH D 230      24.117   4.867  24.416  1.00 57.90           O  
ANISOU 1403  O   HOH D 230     8170   7502   6329  -2502  -4199   -408       O  
HETATM 1404  O   HOH D 231      14.305   3.078  -0.560  1.00 40.17           O  
ANISOU 1404  O   HOH D 231     7878   4612   2773   -250      2   1857       O  
HETATM 1405  O   HOH D 232      16.255   3.185  10.347  1.00 44.23           O  
ANISOU 1405  O   HOH D 232     5530   4685   6592  -1524    507    161       O  
HETATM 1406  O   HOH D 233      20.733  11.520  28.274  0.50 44.14           O  
ANISOU 1406  O   HOH D 233     5431   6642   4697  -2360   2168   -832       O  
HETATM 1407  O   HOH D 234      19.487  16.438  24.575  1.00 40.65           O  
ANISOU 1407  O   HOH D 234     5330   3683   6433   -386   2448    -47       O  
HETATM 1408  O   HOH D 235      28.546  13.896  21.460  1.00 65.88           O  
ANISOU 1408  O   HOH D 235     8051   8439   8542   4126   3067   -610       O  
HETATM 1409  O   HOH D 236       5.812   1.726  17.193  1.00 49.19           O  
ANISOU 1409  O   HOH D 236     5744   8675   4273     87   1724  -2155       O  
HETATM 1410  O   HOH D 237      22.550   3.983  22.283  1.00 71.83           O  
ANISOU 1410  O   HOH D 237     7012  13659   6619  -5014  -2087   1519       O  
HETATM 1411  O   HOH D 238      28.342  17.205  26.806  1.00 39.31           O  
ANISOU 1411  O   HOH D 238     6170   4466   4302   1199    616   -512       O  
HETATM 1412  O   HOH D 239      19.795  18.175  26.397  1.00 54.94           O  
ANISOU 1412  O   HOH D 239    11488   3982   5403  -2108   3063  -1293       O  
HETATM 1413  O   HOH D 240      23.641  16.836  26.968  1.00 47.91           O  
ANISOU 1413  O   HOH D 240     3715   7167   7322    860    676  -1498       O  
HETATM 1414  O   HOH D 241       9.711  14.910  24.915  1.00 71.04           O  
ANISOU 1414  O   HOH D 241    14693   8482   3816  -1126   2236   -714       O  
HETATM 1415  O   HOH D 242       2.931   3.445  31.523  1.00 62.43           O  
ANISOU 1415  O   HOH D 242    10218   8329   5173  -1333   2599    126       O  
HETATM 1416  O   HOH D 243       9.210  -1.638  17.713  1.00 51.80           O  
ANISOU 1416  O   HOH D 243     7546   4537   7598    113   -754   2499       O  
HETATM 1417  O   HOH D 244       7.678  -4.549  20.205  1.00 46.33           O  
ANISOU 1417  O   HOH D 244     5603   6180   5819    427   1484   -922       O  
HETATM 1418  O   HOH D 245       3.652   9.822  31.386  1.00 48.02           O  
ANISOU 1418  O   HOH D 245     7403   6872   3969   -327   -140    371       O  
CONECT   51  281                                                                
CONECT  101  232                                                                
CONECT  148  287                                                                
CONECT  232  101                                                                
CONECT  281   51                                                                
CONECT  287  148                                                                
CONECT  367  583                                                                
CONECT  413  538                                                                
CONECT  454  589                                                                
CONECT  538  413                                                                
CONECT  583  367                                                                
CONECT  589  454                                                                
CONECT  661  887                                                                
CONECT  711  842                                                                
CONECT  758  893                                                                
CONECT  842  711                                                                
CONECT  887  661                                                                
CONECT  893  758                                                                
CONECT  965 1186                                                                
CONECT 1013 1141                                                                
CONECT 1054 1192                                                                
CONECT 1141 1013                                                                
CONECT 1186  965                                                                
CONECT 1192 1054                                                                
CONECT 1220 1221 1222 1223 1224                                                 
CONECT 1221 1220                                                                
CONECT 1222 1220                                                                
CONECT 1223 1220                                                                
CONECT 1224 1220                                                                
MASTER      270    0    1    4   13    0    3    6 1414    4   29   16          
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.