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***  ANTIMICROBIAL PROTEIN 01-DEC-10 3PSM  ***

elNémo ID: 220513152609105178

Job options:

ID        	=	 220513152609105178
JOBID     	=	 ANTIMICROBIAL PROTEIN 01-DEC-10 3PSM
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    ANTIMICROBIAL PROTEIN                   01-DEC-10   3PSM              
TITLE     .98A CRYSTAL STRUCTURE OF A DIMERIC PLANT DEFENSIN SPE10              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEFENSIN;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SPE10                                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PACHYRHIZUS EROSUS;                             
SOURCE   3 ORGANISM_COMMON: JICAMA,POTATO-BEAN,YAM-BEAN;                        
SOURCE   4 ORGANISM_TAXID: 109171                                               
KEYWDS    DIMER, DEFENSIN, ANTIMICROBIAL PROTEIN                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.ZHOU,X.SONG,W.GONG                                                  
REVDAT   1   29-DEC-10 3PSM    0                                                
JRNL        AUTH   H.ZHOU,X.SONG,W.GONG                                         
JRNL        TITL   0.98A CRYSTAL STRUCTURE OF A DIMERIC PLANT DEFENSIN SPE10    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.98 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) : 0.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
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) : 0.125                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.125                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.164                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2635                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 52719                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.120                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.120                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.157                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 0.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 47165                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 758                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 0                                             
REMARK   3   SOLVENT ATOMS      : 183                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 997.37                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 657.62                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 5                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 9169                    
REMARK   3   NUMBER OF RESTRAINTS                     : 10500                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.015                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.030                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.032                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.098                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.102                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.115                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.041                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.101                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R     
REMARK   3  (NO CUTOFF)                                                         
REMARK   4                                                                      
REMARK   4 3PSM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062766.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BSRF                               
REMARK 200  BEAMLINE                       : 3W1A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 130 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55557                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 18.200                             
REMARK 200  R MERGE                    (I) : 0.02800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 31.8300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.480                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING            
REMARK 200 SOFTWARE USED: SHAKE & BAKE                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG 8000, PH 7.5, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       14.05550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    ARG A  34   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG A  45   NH1 -  CZ  -  NH2 ANGL. DEV. =  12.7 DEGREES          
REMARK 500    ARG A  45   NE  -  CZ  -  NH1 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    PHE B  15   CB  -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG B  40   NH1 -  CZ  -  NH2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    ARG B  40   NE  -  CZ  -  NH2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3PSM A    1    47  UNP    Q6B519   Q6B519_9FABA     1     47             
DBREF  3PSM B    1    47  UNP    Q6B519   Q6B519_9FABA     1     47             
SEQRES   1 A   47  LYS THR CYS GLU ASN LEU ALA ASP THR PHE ARG GLY PRO          
SEQRES   2 A   47  CYS PHE THR ASP GLY SER CYS ASP ASP HIS CYS LYS ASN          
SEQRES   3 A   47  LYS GLU HIS LEU ILE LYS GLY ARG CYS ARG ASP ASP PHE          
SEQRES   4 A   47  ARG CYS TRP CYS THR ARG ASN CYS                              
SEQRES   1 B   47  LYS THR CYS GLU ASN LEU ALA ASP THR PHE ARG GLY PRO          
SEQRES   2 B   47  CYS PHE THR ASP GLY SER CYS ASP ASP HIS CYS LYS ASN          
SEQRES   3 B   47  LYS GLU HIS LEU ILE LYS GLY ARG CYS ARG ASP ASP PHE          
SEQRES   4 B   47  ARG CYS TRP CYS THR ARG ASN CYS                              
FORMUL   3  HOH   *183(H2 O)                                                    
HELIX    1   1 THR A   16  LYS A   27  1                                  12    
HELIX    2   2 THR B   16  LYS B   27  1                                  12    
SHEET    1   A 3 THR A   2  LEU A   6  0                                        
SHEET    2   A 3 CYS A  41  ASN A  46 -1  O  CYS A  43   N  ASN A   5           
SHEET    3   A 3 LYS A  32  CYS A  35 -1  N  LYS A  32   O  THR A  44           
SHEET    1   B 3 THR B   2  LEU B   6  0                                        
SHEET    2   B 3 CYS B  41  ASN B  46 -1  O  CYS B  43   N  ASN B   5           
SHEET    3   B 3 LYS B  32  CYS B  35 -1  N  LYS B  32   O  THR B  44           
SSBOND   1 CYS A    3    CYS A   47                          1555   1555  2.04  
SSBOND   2 CYS A   14    CYS A   35                          1555   1555  2.03  
SSBOND   3 CYS A   20    CYS A   41                          1555   1555  2.04  
SSBOND   4 CYS A   24    CYS A   43                          1555   1555  2.04  
SSBOND   5 CYS B    3    CYS B   47                          1555   1555  2.00  
SSBOND   6 CYS B   14    CYS B   35                          1555   1555  2.05  
SSBOND   7 CYS B   20    CYS B   41                          1555   1555  2.03  
SSBOND   8 CYS B   24    CYS B   43                          1555   1555  2.04  
CRYST1   32.714   28.111   54.853  90.00 103.78  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.030568  0.000000  0.007497        0.00000                         
SCALE2      0.000000  0.035573  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018771        0.00000                         
ATOM      1  N  ALYS A   1      -9.066  -4.029  31.714  0.50 18.40           N  
ANISOU    1  N  ALYS A   1     2556   2828   1608    436    226    524       N  
ATOM      2  CA ALYS A   1      -9.903  -3.557  30.628  0.50 29.36           C  
ANISOU    2  CA ALYS A   1     2878   6204   2074   2250    966   1979       C  
ATOM      3  C  ALYS A   1      -8.989  -2.957  29.548  0.50 29.05           C  
ANISOU    3  C  ALYS A   1     2374   6457   2206   2450    954   2086       C  
ATOM      4  O  ALYS A   1      -8.026  -2.254  29.790  0.50 28.17           O  
ANISOU    4  O  ALYS A   1     2750   6529   1425   2305   1121   1571       O  
ATOM      5  CB ALYS A   1     -10.964  -2.513  30.973  0.50 22.96           C  
ANISOU    5  CB ALYS A   1     2152   4948   1626    998    832   1274       C  
ATOM      6  CG ALYS A   1     -12.024  -2.302  29.920  0.50 21.38           C  
ANISOU    6  CG ALYS A   1     2111   4298   1714   1156    780   1107       C  
ATOM      7  CD ALYS A   1     -12.852  -1.072  30.220  0.50 20.72           C  
ANISOU    7  CD ALYS A   1     2035   4497   1342    976    711    328       C  
ATOM      8  CE ALYS A   1     -13.713  -0.609  29.088  0.50 20.96           C  
ANISOU    8  CE ALYS A   1     1930   4181   1855   1043    904   1148       C  
ATOM      9  NZ  LYS A   1     -14.457   0.649  29.319  1.00 24.23           N  
ANISOU    9  NZ  LYS A   1     1966   4310   2928    943    246    -54       N  
ATOM     10  N   THR A   2      -9.373  -3.264  28.322  1.00 29.41           N  
ANISOU   10  N   THR A   2     2066   6784   2324   1875    857   2109       N  
ATOM     11  CA  THR A   2      -8.725  -2.789  27.132  1.00 29.72           C  
ANISOU   11  CA  THR A   2     1949   6996   2348   1929    946   2150       C  
ATOM     12  C   THR A   2      -9.763  -2.175  26.197  1.00 28.17           C  
ANISOU   12  C   THR A   2     1810   6768   2124   1487    628   1894       C  
ATOM     13  O   THR A   2     -10.961  -2.291  26.343  1.00 35.13           O  
ANISOU   13  O   THR A   2     1831   8771   2747   1996   1159   3014       O  
ATOM     14  CB  THR A   2      -8.015  -3.872  26.321  1.00 32.98           C  
ANISOU   14  CB  THR A   2     2672   7330   2530   2215    983   1912       C  
ATOM     15  OG1 THR A   2      -9.003  -4.777  25.836  1.00 35.93           O  
ANISOU   15  OG1 THR A   2     3294   7165   3192   2154    642   1736       O  
ATOM     16  CG2 THR A   2      -6.969  -4.606  27.173  1.00 36.43           C  
ANISOU   16  CG2 THR A   2     2362   8029   3449   2670   1169   2123       C  
ATOM     17  N   CYS A   3      -9.196  -1.254  25.368  1.00 24.43           N  
ANISOU   17  N   CYS A   3     1774   5886   1623   1666    690   1238       N  
ATOM     18  CA  CYS A   3      -9.938  -0.327  24.545  1.00 21.73           C  
ANISOU   18  CA  CYS A   3     1412   5251   1592   1340    343    778       C  
ATOM     19  C   CYS A   3      -9.287  -0.302  23.177  1.00 17.90           C  
ANISOU   19  C   CYS A   3     1268   3960   1575    764    296    639       C  
ATOM     20  O   CYS A   3      -8.033  -0.332  23.113  1.00 19.69           O  
ANISOU   20  O   CYS A   3     1211   4698   1574    983    306    536       O  
ATOM     21  CB  CYS A   3      -9.930   1.104  25.083  1.00 26.20           C  
ANISOU   21  CB  CYS A   3     2289   5774   1892   2012    454     87       C  
ATOM     22  SG  CYS A   3     -10.961   1.320  26.538  1.00 30.22           S  
ANISOU   22  SG  CYS A   3     2343   7049   2091   2123    722     62       S  
ATOM     23  N   GLU A   4     -10.078  -0.257  22.121  1.00 16.13           N  
ANISOU   23  N   GLU A   4     1207   3294   1627    661    315    652       N  
ATOM     24  CA  GLU A   4      -9.591  -0.246  20.741  1.00 12.99           C  
ANISOU   24  CA  GLU A   4      906   2441   1590    321    193    587       C  
ATOM     25  C   GLU A   4     -10.036   1.049  20.078  1.00 13.32           C  
ANISOU   25  C   GLU A   4     1031   2334   1696    447    223    476       C  
ATOM     26  O   GLU A   4     -11.233   1.341  20.000  1.00 16.82           O  
ANISOU   26  O   GLU A   4     1049   2956   2384    610    334    974       O  
ATOM     27  CB  GLU A   4     -10.057  -1.523  20.043  1.00 14.46           C  
ANISOU   27  CB  GLU A   4     1144   2328   2024    226    273    604       C  
ATOM     28  CG  GLU A   4      -9.399  -1.666  18.688  1.00 14.01           C  
ANISOU   28  CG  GLU A   4     1182   2232   1910    108    261    462       C  
ATOM     29  CD  GLU A   4      -9.744  -2.890  17.887  1.00 14.70           C  
ANISOU   29  CD  GLU A   4     1073   2257   2256   -200     29    418       C  
ATOM     30  OE1 GLU A   4      -8.848  -3.469  17.266  1.00 15.34           O  
ANISOU   30  OE1 GLU A   4     1087   2530   2212   -281     12    -11       O  
ATOM     31  OE2 GLU A   4     -10.922  -3.342  17.983  1.00 22.27           O  
ANISOU   31  OE2 GLU A   4     1092   3858   3510   -473    183   -146       O  
ATOM     32  N   ASN A   5      -9.070   1.853  19.619  1.00 12.43           N  
ANISOU   32  N   ASN A   5     1038   2125   1560    466    256    370       N  
ATOM     33  CA  ASN A   5      -9.342   3.107  18.923  1.00 12.28           C  
ANISOU   33  CA  ASN A   5     1164   2023   1477    551     77    238       C  
ATOM     34  C   ASN A   5      -8.377   3.278  17.783  1.00 10.74           C  
ANISOU   34  C   ASN A   5      975   1628   1476    196     86      8       C  
ATOM     35  O   ASN A   5      -7.348   2.568  17.684  1.00 11.36           O  
ANISOU   35  O   ASN A   5     1162   1600   1552    279    130    -73       O  
ATOM     36  CB  ASN A   5      -9.254   4.282  19.881  1.00 14.41           C  
ANISOU   36  CB  ASN A   5     1752   2251   1473    693    153     26       C  
ATOM     37  CG  ASN A   5     -10.521   4.284  20.737  1.00 18.43           C  
ANISOU   37  CG  ASN A   5     2362   2774   1866   1401    559    379       C  
ATOM     38  OD1 ASN A   5     -11.554   4.791  20.311  1.00 20.53           O  
ANISOU   38  OD1 ASN A   5     1970   3199   2632   1289    552    432       O  
ATOM     39  ND2 ASN A   5     -10.572   3.659  21.894  1.00 21.19           N  
ANISOU   39  ND2 ASN A   5     2544   3659   1846   1743    876    511       N  
ATOM     40  N   LEU A   6      -8.699   4.185  16.871  1.00 11.35           N  
ANISOU   40  N   LEU A   6     1121   1637   1555    225     69     86       N  
ATOM     41  CA  LEU A   6      -7.822   4.428  15.727  1.00 10.99           C  
ANISOU   41  CA  LEU A   6     1226   1496   1453     68    120    -22       C  
ATOM     42  C   LEU A   6      -6.427   4.812  16.171  1.00 10.48           C  
ANISOU   42  C   LEU A   6     1331   1241   1412    -66     72    -83       C  
ATOM     43  O   LEU A   6      -6.213   5.544  17.138  1.00 12.51           O  
ANISOU   43  O   LEU A   6     1645   1597   1509     84     62   -251       O  
ATOM     44  CB  LEU A   6      -8.390   5.561  14.846  1.00 12.15           C  
ANISOU   44  CB  LEU A   6     1342   1664   1609    179     29     50       C  
ATOM     45  CG  LEU A   6      -9.581   5.143  14.023  1.00 13.46           C  
ANISOU   45  CG  LEU A   6     1173   2090   1852    317     19    129       C  
ATOM     46  CD1 LEU A   6     -10.191   6.421  13.405  1.00 17.02           C  
ANISOU   46  CD1 LEU A   6     2003   2545   1917   1100   -279    -91       C  
ATOM     47  CD2 LEU A   6      -9.247   4.161  12.913  1.00 13.90           C  
ANISOU   47  CD2 LEU A   6     1527   1888   1866     93   -142    -12       C  
ATOM     48  N   ALA A   7      -5.434   4.356  15.424  1.00 10.46           N  
ANISOU   48  N   ALA A   7     1193   1256   1526      1     83   -161       N  
ATOM     49  CA  ALA A   7      -4.080   4.854  15.558  1.00 11.00           C  
ANISOU   49  CA  ALA A   7     1288   1396   1495   -212     46    -13       C  
ATOM     50  C   ALA A   7      -4.085   6.369  15.404  1.00 11.41           C  
ANISOU   50  C   ALA A   7     1360   1395   1582   -142     49   -107       C  
ATOM     51  O   ALA A   7      -4.893   6.908  14.620  1.00 14.10           O  
ANISOU   51  O   ALA A   7     1922   1579   1858    -11   -102    125       O  
ATOM     52  CB  ALA A   7      -3.191   4.179  14.539  1.00 11.24           C  
ANISOU   52  CB  ALA A   7     1132   1354   1783   -224    130   -114       C  
ATOM     53  N   ASP A   8      -3.152   7.023  16.021  1.00 14.23           N  
ANISOU   53  N   ASP A   8     2144   1540   1724   -548    -42   -325       N  
ATOM     54  CA  ASP A   8      -3.060   8.449  15.907  1.00 14.08           C  
ANISOU   54  CA  ASP A   8     1771   1457   2121   -242    164   -312       C  
ATOM     55  C   ASP A   8      -2.403   8.919  14.609  1.00 12.52           C  
ANISOU   55  C   ASP A   8     1535   1133   2089    -71    -51   -240       C  
ATOM     56  O   ASP A   8      -2.870   9.891  14.016  1.00 15.16           O  
ANISOU   56  O   ASP A   8     1890   1434   2436    133   -116    -25       O  
ATOM     57  CB  ASP A   8      -2.271   9.009  17.136  1.00 18.16           C  
ANISOU   57  CB  ASP A   8     2875   1951   2072   -764    271   -729       C  
ATOM     58  CG  ASP A   8      -3.086   9.116  18.419  1.00 24.92           C  
ANISOU   58  CG  ASP A   8     3206   3987   2273  -1234    641   -675       C  
ATOM     59  OD1 ASP A   8      -4.335   9.051  18.402  1.00 26.44           O  
ANISOU   59  OD1 ASP A   8     3092   3538   3416   -615    887  -1512       O  
ATOM     60  OD2 ASP A   8      -2.449   9.292  19.489  1.00 38.70           O  
ANISOU   60  OD2 ASP A   8     3491   8911   2301    222    604  -1909       O  
ATOM     61  N   THR A   9      -1.336   8.263  14.163  1.00 11.90           N  
ANISOU   61  N   THR A   9     1424   1229   1871   -154    -20    -62       N  
ATOM     62  CA  THR A   9      -0.480   8.785  13.094  1.00 13.25           C  
ANISOU   62  CA  THR A   9     1609   1237   2191   -332    121    -68       C  
ATOM     63  C   THR A   9      -0.111   7.738  12.073  1.00 12.47           C  
ANISOU   63  C   THR A   9     1395   1339   2002   -211    173     44       C  
ATOM     64  O   THR A   9       0.814   7.908  11.332  1.00 17.82           O  
ANISOU   64  O   THR A   9     2201   1821   2747   -691    831   -443       O  
ATOM     65  CB  THR A   9       0.800   9.421  13.706  1.00 15.34           C  
ANISOU   65  CB  THR A   9     1640   1276   2911   -350    150   -291       C  
ATOM     66  OG1 THR A   9       1.425   8.429  14.542  1.00 19.05           O  
ANISOU   66  OG1 THR A   9     1716   1790   3732   -188   -482   -207       O  
ATOM     67  CG2 THR A   9       0.419  10.627  14.556  1.00 15.49           C  
ANISOU   67  CG2 THR A   9     1785   1554   2546   -433    112   -346       C  
ATOM     68  N   PHE A  10      -0.836   6.649  11.991  1.00 11.24           N  
ANISOU   68  N   PHE A  10     1296   1257   1719    -82    -79     56       N  
ATOM     69  CA  PHE A  10      -0.596   5.654  10.931  1.00 10.42           C  
ANISOU   69  CA  PHE A  10     1108   1345   1505    -45    -31     80       C  
ATOM     70  C   PHE A  10      -0.888   6.285   9.575  1.00 10.94           C  
ANISOU   70  C   PHE A  10     1214   1196   1746   -136     10    113       C  
ATOM     71  O   PHE A  10      -1.951   6.881   9.407  1.00 12.89           O  
ANISOU   71  O   PHE A  10     1454   1772   1671    222    -29    354       O  
ATOM     72  CB  PHE A  10      -1.459   4.441  11.212  1.00 10.42           C  
ANISOU   72  CB  PHE A  10     1171   1329   1459    -66    -78     76       C  
ATOM     73  CG  PHE A  10      -1.275   3.298  10.203  1.00  9.62           C  
ANISOU   73  CG  PHE A  10     1029   1211   1417    -74    -17     95       C  
ATOM     74  CD1 PHE A  10      -0.373   2.266  10.450  1.00 10.81           C  
ANISOU   74  CD1 PHE A  10     1212   1511   1383     64   -162    112       C  
ATOM     75  CD2 PHE A  10      -1.996   3.246   9.040  1.00 10.25           C  
ANISOU   75  CD2 PHE A  10     1010   1295   1590     14   -187    112       C  
ATOM     76  CE1 PHE A  10      -0.236   1.222   9.574  1.00 11.41           C  
ANISOU   76  CE1 PHE A  10     1376   1216   1743    199   -201    121       C  
ATOM     77  CE2 PHE A  10      -1.848   2.164   8.149  1.00 10.94           C  
ANISOU   77  CE2 PHE A  10     1318   1231   1606   -110   -284     47       C  
ATOM     78  CZ  PHE A  10      -0.970   1.166   8.429  1.00 11.57           C  
ANISOU   78  CZ  PHE A  10     1589   1292   1516     30   -132     62       C  
ATOM     79  N   ARG A  11       0.015   6.089   8.630  1.00 10.92           N  
ANISOU   79  N   ARG A  11     1154   1461   1533   -123    -87     83       N  
ATOM     80  CA  ARG A  11      -0.145   6.690   7.311  1.00 11.44           C  
ANISOU   80  CA  ARG A  11     1324   1465   1556   -217   -165     58       C  
ATOM     81  C   ARG A  11      -0.731   5.777   6.267  1.00 12.72           C  
ANISOU   81  C   ARG A  11     1198   1974   1660   -294   -193    -85       C  
ATOM     82  O   ARG A  11      -0.198   4.679   6.016  1.00 13.63           O  
ANISOU   82  O   ARG A  11     1620   1796   1761   -471    -97   -210       O  
ATOM     83  CB  ARG A  11       1.238   7.140   6.833  1.00 11.41           C  
ANISOU   83  CB  ARG A  11     1379   1509   1447   -297   -115    -86       C  
ATOM     84  CG  ARG A  11       1.178   7.888   5.505  1.00 12.99           C  
ANISOU   84  CG  ARG A  11     1678   1883   1375   -546   -324      0       C  
ATOM     85  CD  ARG A  11       2.494   8.434   5.066  1.00 13.44           C  
ANISOU   85  CD  ARG A  11     1672   1763   1670   -601    -76    -87       C  
ATOM     86  NE  ARG A  11       3.014   9.461   5.936  1.00 12.23           N  
ANISOU   86  NE  ARG A  11     1457   1583   1607   -327   -247     65       N  
ATOM     87  CZ  ARG A  11       2.720  10.726   5.976  1.00 12.60           C  
ANISOU   87  CZ  ARG A  11     1160   1685   1941   -121   -197    -87       C  
ATOM     88  NH1 ARG A  11       1.881  11.232   5.092  1.00 16.26           N  
ANISOU   88  NH1 ARG A  11     1754   2046   2377   -233   -715    191       N  
ATOM     89  NH2 ARG A  11       3.305  11.536   6.867  1.00 12.98           N  
ANISOU   89  NH2 ARG A  11     1312   1668   1954    -27   -279    -71       N  
ATOM     90  N   GLY A  12      -1.782   6.282   5.563  1.00 16.54           N  
ANISOU   90  N   GLY A  12     2064   1963   2257   -740   -950    809       N  
ATOM     91  CA  GLY A  12      -2.367   5.617   4.400  1.00 16.99           C  
ANISOU   91  CA  GLY A  12     2173   2081   2200   -739  -1032    830       C  
ATOM     92  C   GLY A  12      -3.316   4.520   4.830  1.00 13.71           C  
ANISOU   92  C   GLY A  12     1770   1685   1755   -281   -643    472       C  
ATOM     93  O   GLY A  12      -3.545   4.258   6.068  1.00 14.84           O  
ANISOU   93  O   GLY A  12     1944   1891   1803   -314   -561    437       O  
ATOM     94  N   PRO A  13      -3.861   3.826   3.856  1.00 13.57           N  
ANISOU   94  N   PRO A  13     1687   1768   1702   -361   -693    538       N  
ATOM     95  CA  PRO A  13      -4.775   2.735   4.218  1.00 12.59           C  
ANISOU   95  CA  PRO A  13     1455   1795   1533   -146   -419    453       C  
ATOM     96  C   PRO A  13      -4.053   1.616   4.935  1.00 10.81           C  
ANISOU   96  C   PRO A  13     1254   1465   1388   -150   -292    203       C  
ATOM     97  O   PRO A  13      -2.863   1.325   4.662  1.00 12.00           O  
ANISOU   97  O   PRO A  13     1384   1833   1342    -78   -217    300       O  
ATOM     98  CB  PRO A  13      -5.308   2.255   2.847  1.00 14.43           C  
ANISOU   98  CB  PRO A  13     1893   1844   1744   -416   -791    554       C  
ATOM     99  CG  PRO A  13      -5.079   3.480   1.961  1.00 17.18           C  
ANISOU   99  CG  PRO A  13     2208   2513   1808  -1009   -891    855       C  
ATOM    100  CD  PRO A  13      -3.733   3.958   2.406  1.00 16.47           C  
ANISOU  100  CD  PRO A  13     2126   2495   1637   -920   -867    791       C  
ATOM    101  N   CYS A  14      -4.812   0.904   5.737  1.00 10.71           N  
ANISOU  101  N   CYS A  14     1227   1441   1402    100   -259    210       N  
ATOM    102  CA  CYS A  14      -4.279  -0.273   6.443  1.00  9.77           C  
ANISOU  102  CA  CYS A  14     1193   1334   1185     94   -246    134       C  
ATOM    103  C   CYS A  14      -4.621  -1.530   5.654  1.00 10.09           C  
ANISOU  103  C   CYS A  14     1247   1370   1216    165   -346    104       C  
ATOM    104  O   CYS A  14      -5.781  -1.912   5.561  1.00 11.43           O  
ANISOU  104  O   CYS A  14     1338   1677   1327    -41   -445    -18       O  
ATOM    105  CB  CYS A  14      -4.901  -0.335   7.823  1.00  9.30           C  
ANISOU  105  CB  CYS A  14     1003   1255   1274    103   -254     97       C  
ATOM    106  SG  CYS A  14      -4.124  -1.425   9.011  1.00  9.23           S  
ANISOU  106  SG  CYS A  14      987   1333   1187     11   -301     72       S  
ATOM    107  N   PHE A  15      -3.573  -2.099   5.059  1.00 10.83           N  
ANISOU  107  N   PHE A  15     1414   1478   1222    335   -349     47       N  
ATOM    108  CA  PHE A  15      -3.668  -3.313   4.262  1.00 12.25           C  
ANISOU  108  CA  PHE A  15     1725   1671   1258    357   -605   -184       C  
ATOM    109  C   PHE A  15      -3.153  -4.536   4.972  1.00 12.74           C  
ANISOU  109  C   PHE A  15     1820   1436   1584    400   -833   -363       C  
ATOM    110  O   PHE A  15      -3.584  -5.625   4.663  1.00 19.10           O  
ANISOU  110  O   PHE A  15     2707   1541   3011    301  -1813   -346       O  
ATOM    111  CB  PHE A  15      -2.907  -3.148   2.946  1.00 13.94           C  
ANISOU  111  CB  PHE A  15     1891   2123   1284    625   -548   -325       C  
ATOM    112  CG  PHE A  15      -3.509  -2.128   2.024  1.00 15.50           C  
ANISOU  112  CG  PHE A  15     1910   2864   1116    579   -428     73       C  
ATOM    113  CD1 PHE A  15      -2.799  -0.989   1.674  1.00 17.12           C  
ANISOU  113  CD1 PHE A  15     2138   2838   1529    489   -511    236       C  
ATOM    114  CD2 PHE A  15      -4.775  -2.263   1.498  1.00 19.49           C  
ANISOU  114  CD2 PHE A  15     1891   3792   1722    389   -630    767       C  
ATOM    115  CE1 PHE A  15      -3.341  -0.047   0.802  1.00 18.56           C  
ANISOU  115  CE1 PHE A  15     2088   3194   1771    555   -305    524       C  
ATOM    116  CE2 PHE A  15      -5.282  -1.313   0.649  1.00 23.67           C  
ANISOU  116  CE2 PHE A  15     1914   4190   2888    339   -876   1336       C  
ATOM    117  CZ  PHE A  15      -4.603  -0.205   0.293  1.00 21.62           C  
ANISOU  117  CZ  PHE A  15     2319   3644   2254    505   -709    830       C  
ATOM    118  N   THR A  16      -2.185  -4.392   5.865  1.00 10.37           N  
ANISOU  118  N   THR A  16     1354   1416   1167    332   -402   -156       N  
ATOM    119  CA  THR A  16      -1.556  -5.515   6.549  1.00  9.97           C  
ANISOU  119  CA  THR A  16     1412   1160   1214    159   -343    -49       C  
ATOM    120  C   THR A  16      -1.669  -5.314   8.040  1.00  9.02           C  
ANISOU  120  C   THR A  16      995   1168   1262    133   -303    -44       C  
ATOM    121  O   THR A  16      -1.349  -4.241   8.562  1.00  8.95           O  
ANISOU  121  O   THR A  16     1003   1191   1205     84   -251    -28       O  
ATOM    122  CB  THR A  16      -0.116  -5.756   6.098  1.00 10.41           C  
ANISOU  122  CB  THR A  16     1436   1407   1114    274   -335    -88       C  
ATOM    123  OG1 THR A  16       0.726  -4.743   6.655  1.00 10.38           O  
ANISOU  123  OG1 THR A  16     1204   1462   1279    200   -130    -36       O  
ATOM    124  CG2 THR A  16      -0.021  -5.809   4.573  1.00 12.75           C  
ANISOU  124  CG2 THR A  16     1861   1811   1171    437   -235   -135       C  
ATOM    125  N   ASP A  17      -2.091  -6.377   8.743  1.00  8.90           N  
ANISOU  125  N   ASP A  17     1039   1124   1217     92   -314   -113       N  
ATOM    126  CA  ASP A  17      -2.097  -6.282  10.200  1.00  8.80           C  
ANISOU  126  CA  ASP A  17     1078   1064   1202     32   -214   -114       C  
ATOM    127  C   ASP A  17      -0.705  -6.087  10.734  1.00  8.48           C  
ANISOU  127  C   ASP A  17     1061   1065   1097     83   -278    -21       C  
ATOM    128  O   ASP A  17      -0.533  -5.368  11.744  1.00  9.05           O  
ANISOU  128  O   ASP A  17     1099   1170   1171     66   -211   -132       O  
ATOM    129  CB  ASP A  17      -2.731  -7.524  10.812  1.00 10.33           C  
ANISOU  129  CB  ASP A  17     1292   1220   1412    -60   -254    -40       C  
ATOM    130  CG  ASP A  17      -4.258  -7.478  10.691  1.00 11.49           C  
ANISOU  130  CG  ASP A  17     1260   1259   1845   -287   -207    -68       C  
ATOM    131  OD1 ASP A  17      -4.851  -6.548  10.225  1.00 11.44           O  
ANISOU  131  OD1 ASP A  17     1113   1330   1906     -7   -213   -251       O  
ATOM    132  OD2 ASP A  17      -4.881  -8.451  11.227  1.00 16.43           O  
ANISOU  132  OD2 ASP A  17     1497   1704   3041   -411   -254    559       O  
ATOM    133  N   GLY A  18       0.330  -6.666  10.115  1.00  8.53           N  
ANISOU  133  N   GLY A  18     1010   1073   1158    145   -275   -132       N  
ATOM    134  CA  GLY A  18       1.670  -6.442  10.623  1.00  8.85           C  
ANISOU  134  CA  GLY A  18     1071   1205   1087    130   -243   -126       C  
ATOM    135  C   GLY A  18       2.074  -5.010  10.618  1.00  8.36           C  
ANISOU  135  C   GLY A  18      908   1212   1055    237   -189   -137       C  
ATOM    136  O   GLY A  18       2.694  -4.498  11.553  1.00  8.53           O  
ANISOU  136  O   GLY A  18     1007   1116   1116    169   -211    -82       O  
ATOM    137  N   SER A  19       1.723  -4.240   9.556  1.00  8.54           N  
ANISOU  137  N   SER A  19      975   1220   1051    153   -164    -87       N  
ATOM    138  CA  SER A  19       2.079  -2.833   9.520  1.00  8.39           C  
ANISOU  138  CA  SER A  19      824   1268   1095     50    -72    -59       C  
ATOM    139  C   SER A  19       1.415  -2.073  10.699  1.00  7.85           C  
ANISOU  139  C   SER A  19      846   1135   1000     86   -190    -19       C  
ATOM    140  O   SER A  19       2.040  -1.189  11.310  1.00  8.38           O  
ANISOU  140  O   SER A  19      866   1138   1179     44   -100    -34       O  
ATOM    141  CB  SER A  19       1.691  -2.174   8.219  1.00  9.39           C  
ANISOU  141  CB  SER A  19     1128   1367   1073     95     10    -18       C  
ATOM    142  OG  SER A  19       0.288  -2.084   8.006  1.00  9.68           O  
ANISOU  142  OG  SER A  19     1186   1380   1114     97   -183     27       O  
ATOM    143  N   CYS A  20       0.174  -2.409  10.999  1.00  7.69           N  
ANISOU  143  N   CYS A  20      789   1037   1094     85   -139    -77       N  
ATOM    144  CA  CYS A  20      -0.534  -1.735  12.075  1.00  7.73           C  
ANISOU  144  CA  CYS A  20      843   1007   1085    -27   -121    -89       C  
ATOM    145  C   CYS A  20      -0.060  -2.155  13.430  1.00  7.85           C  
ANISOU  145  C   CYS A  20      721   1093   1168     38   -165   -110       C  
ATOM    146  O   CYS A  20       0.116  -1.326  14.340  1.00  8.04           O  
ANISOU  146  O   CYS A  20      789   1111   1153     -4   -191   -104       O  
ATOM    147  CB  CYS A  20      -2.036  -1.992  11.910  1.00  8.12           C  
ANISOU  147  CB  CYS A  20      826   1108   1151    116   -208    -87       C  
ATOM    148  SG  CYS A  20      -3.072  -1.231  13.161  1.00  8.20           S  
ANISOU  148  SG  CYS A  20      732   1123   1260     16   -148     14       S  
ATOM    149  N   ASP A  21       0.177  -3.452  13.614  1.00  7.78           N  
ANISOU  149  N   ASP A  21      789   1099   1069     52   -173   -108       N  
ATOM    150  CA  ASP A  21       0.711  -3.944  14.892  1.00  7.83           C  
ANISOU  150  CA  ASP A  21      826   1181    967    105   -123    -54       C  
ATOM    151  C   ASP A  21       2.059  -3.323  15.192  1.00  7.73           C  
ANISOU  151  C   ASP A  21      836   1020   1082    129   -157    -99       C  
ATOM    152  O   ASP A  21       2.343  -2.929  16.326  1.00  8.37           O  
ANISOU  152  O   ASP A  21      910   1193   1078     62   -226    -89       O  
ATOM    153  CB  ASP A  21       0.779  -5.464  14.842  1.00  8.37           C  
ANISOU  153  CB  ASP A  21      893   1176   1112     87   -186   -103       C  
ATOM    154  CG  ASP A  21       0.854  -6.149  16.180  1.00  8.38           C  
ANISOU  154  CG  ASP A  21      873   1157   1154     89   -107    -28       C  
ATOM    155  OD1 ASP A  21       0.242  -5.658  17.145  1.00  9.39           O  
ANISOU  155  OD1 ASP A  21     1122   1326   1120    164   -148    -61       O  
ATOM    156  OD2 ASP A  21       1.533  -7.204  16.248  1.00 10.17           O  
ANISOU  156  OD2 ASP A  21     1342   1271   1251    262    -15     52       O  
ATOM    157  N   ASP A  22       2.912  -3.199  14.171  1.00  7.95           N  
ANISOU  157  N   ASP A  22      788   1157   1078     58   -192    -97       N  
ATOM    158  CA  ASP A  22       4.195  -2.528  14.302  1.00  8.54           C  
ANISOU  158  CA  ASP A  22      782   1222   1239     84    -79    -27       C  
ATOM    159  C   ASP A  22       3.997  -1.099  14.785  1.00  8.20           C  
ANISOU  159  C   ASP A  22      753   1175   1189      7    -66     -6       C  
ATOM    160  O   ASP A  22       4.564  -0.650  15.777  1.00  8.99           O  
ANISOU  160  O   ASP A  22      863   1357   1195     16   -213   -132       O  
ATOM    161  CB  ASP A  22       4.917  -2.585  12.948  1.00  9.69           C  
ANISOU  161  CB  ASP A  22      938   1568   1175    171    -42    -49       C  
ATOM    162  CG  ASP A  22       6.168  -1.769  12.802  1.00 10.74           C  
ANISOU  162  CG  ASP A  22      912   1701   1467    197     -8    135       C  
ATOM    163  OD1 ASP A  22       6.781  -1.422  13.829  1.00 11.35           O  
ANISOU  163  OD1 ASP A  22      960   1647   1707    -29     59    -59       O  
ATOM    164  OD2 ASP A  22       6.518  -1.422  11.643  1.00 16.22           O  
ANISOU  164  OD2 ASP A  22     1346   3185   1631   -214     81    571       O  
ATOM    165  N   HIS A  23       3.144  -0.339  14.056  1.00  8.47           N  
ANISOU  165  N   HIS A  23      828   1144   1245     -1   -101    -20       N  
ATOM    166  CA  HIS A  23       2.872   1.028  14.456  1.00  8.71           C  
ANISOU  166  CA  HIS A  23      857   1039   1416   -104   -191    -42       C  
ATOM    167  C   HIS A  23       2.406   1.108  15.904  1.00  8.68           C  
ANISOU  167  C   HIS A  23      745   1160   1391    -32   -198   -180       C  
ATOM    168  O   HIS A  23       2.888   1.916  16.719  1.00  9.67           O  
ANISOU  168  O   HIS A  23      879   1204   1592    -53   -270   -233       O  
ATOM    169  CB  HIS A  23       1.820   1.642  13.499  1.00  9.20           C  
ANISOU  169  CB  HIS A  23      921   1134   1440    -31   -191      2       C  
ATOM    170  CG  HIS A  23       1.398   3.018  13.980  1.00 10.41           C  
ANISOU  170  CG  HIS A  23     1054   1146   1754    -55   -353     12       C  
ATOM    171  ND1 HIS A  23       2.061   4.157  13.545  1.00 11.99           N  
ANISOU  171  ND1 HIS A  23     1320   1184   2050   -204   -405    152       N  
ATOM    172  CD2 HIS A  23       0.420   3.361  14.860  1.00 11.54           C  
ANISOU  172  CD2 HIS A  23     1156   1124   2104    117   -226   -234       C  
ATOM    173  CE1 HIS A  23       1.491   5.161  14.192  1.00 12.72           C  
ANISOU  173  CE1 HIS A  23     1280   1184   2368     47   -603     50       C  
ATOM    174  NE2 HIS A  23       0.536   4.720  14.985  1.00 13.10           N  
ANISOU  174  NE2 HIS A  23     1430   1141   2405     74   -370   -226       N  
ATOM    175  N   CYS A  24       1.376   0.334  16.234  1.00  8.18           N  
ANISOU  175  N   CYS A  24      865   1078   1166    -47   -181   -169       N  
ATOM    176  CA  CYS A  24       0.763   0.438  17.562  1.00  8.51           C  
ANISOU  176  CA  CYS A  24      799   1174   1260     67   -149   -262       C  
ATOM    177  C   CYS A  24       1.743   0.059  18.664  1.00  8.57           C  
ANISOU  177  C   CYS A  24      838   1240   1179   -107   -174   -266       C  
ATOM    178  O   CYS A  24       1.805   0.722  19.681  1.00 10.28           O  
ANISOU  178  O   CYS A  24     1048   1549   1309     55   -259   -363       O  
ATOM    179  CB  CYS A  24      -0.492  -0.418  17.631  1.00  8.72           C  
ANISOU  179  CB  CYS A  24      792   1271   1250     50   -143   -264       C  
ATOM    180  SG  CYS A  24      -1.816   0.200  16.535  1.00  8.61           S  
ANISOU  180  SG  CYS A  24      778   1290   1202     33   -121   -176       S  
ATOM    181  N   LYS A  25       2.520  -1.026  18.459  1.00  8.60           N  
ANISOU  181  N   LYS A  25      784   1395   1089     13   -227   -201       N  
ATOM    182  CA  LYS A  25       3.479  -1.472  19.471  1.00  9.09           C  
ANISOU  182  CA  LYS A  25      910   1427   1118    -40   -211   -123       C  
ATOM    183  C   LYS A  25       4.668  -0.533  19.569  1.00  9.53           C  
ANISOU  183  C   LYS A  25      887   1354   1381     77   -328   -245       C  
ATOM    184  O   LYS A  25       5.159  -0.257  20.677  1.00 12.11           O  
ANISOU  184  O   LYS A  25     1135   2107   1361   -145   -308   -449       O  
ATOM    185  CB  LYS A  25       3.951  -2.890  19.165  1.00  9.02           C  
ANISOU  185  CB  LYS A  25      768   1433   1225     29   -297   -117       C  
ATOM    186  CG  LYS A  25       2.940  -3.957  19.434  1.00  9.01           C  
ANISOU  186  CG  LYS A  25      859   1435   1129     67   -138    -31       C  
ATOM    187  CD  LYS A  25       3.353  -5.330  18.950  1.00  9.68           C  
ANISOU  187  CD  LYS A  25      903   1436   1339    -11   -204    -30       C  
ATOM    188  CE  LYS A  25       2.440  -6.425  19.512  1.00 11.96           C  
ANISOU  188  CE  LYS A  25     1954   1435   1154   -119   -112     97       C  
ATOM    189  NZ  LYS A  25       2.552  -7.697  18.819  1.00 11.64           N  
ANISOU  189  NZ  LYS A  25     1280   1533   1608     90    -54     41       N  
ATOM    190  N   ASN A  26       5.204  -0.115  18.438  1.00  9.83           N  
ANISOU  190  N   ASN A  26      935   1341   1458   -201   -274   -220       N  
ATOM    191  CA  ASN A  26       6.530   0.520  18.384  1.00 10.14           C  
ANISOU  191  CA  ASN A  26      992   1350   1512   -141   -355   -146       C  
ATOM    192  C   ASN A  26       6.518   1.999  18.245  1.00 11.22           C  
ANISOU  192  C   ASN A  26     1030   1389   1843   -169   -332   -286       C  
ATOM    193  O   ASN A  26       7.531   2.636  18.608  1.00 16.03           O  
ANISOU  193  O   ASN A  26     1450   1558   3083   -427   -976   -162       O  
ATOM    194  CB  ASN A  26       7.348  -0.122  17.249  1.00 10.56           C  
ANISOU  194  CB  ASN A  26      837   1428   1746   -155   -172    -96       C  
ATOM    195  CG  ASN A  26       7.527  -1.592  17.502  1.00 10.52           C  
ANISOU  195  CG  ASN A  26      893   1498   1608    -17   -280   -179       C  
ATOM    196  OD1 ASN A  26       7.889  -1.986  18.643  1.00 12.74           O  
ANISOU  196  OD1 ASN A  26     1550   1536   1756    172   -570   -220       O  
ATOM    197  ND2 ASN A  26       7.305  -2.410  16.504  1.00 10.64           N  
ANISOU  197  ND2 ASN A  26      959   1416   1668     19   -317   -175       N  
ATOM    198  N   LYS A  27       5.451   2.600  17.723  1.00 10.56           N  
ANISOU  198  N   LYS A  27      901   1210   1902   -189   -218   -299       N  
ATOM    199  CA  LYS A  27       5.299   4.034  17.674  1.00 12.10           C  
ANISOU  199  CA  LYS A  27     1208   1218   2171   -234   -319   -224       C  
ATOM    200  C   LYS A  27       4.443   4.559  18.818  1.00 12.81           C  
ANISOU  200  C   LYS A  27     1098   1255   2512    -83   -408   -507       C  
ATOM    201  O   LYS A  27       4.724   5.591  19.410  1.00 16.46           O  
ANISOU  201  O   LYS A  27     1805   1527   2921   -354   -102   -861       O  
ATOM    202  CB  LYS A  27       4.773   4.528  16.343  1.00 14.95           C  
ANISOU  202  CB  LYS A  27     1939   1269   2473   -519   -715     85       C  
ATOM    203  CG  LYS A  27       5.705   4.176  15.221  1.00 19.06           C  
ANISOU  203  CG  LYS A  27     2779   2276   2187   -856   -403    115       C  
ATOM    204  CD  LYS A  27       6.786   5.234  15.137  1.00 22.23           C  
ANISOU  204  CD  LYS A  27     1984   2697   3766   -536    130   -664       C  
ATOM    205  CE  LYS A  27       7.665   5.008  13.918  1.00 25.88           C  
ANISOU  205  CE  LYS A  27     2586   3544   3704  -1063    372   -876       C  
ATOM    206  NZ  LYS A  27       8.461   3.746  14.093  1.00 34.49           N  
ANISOU  206  NZ  LYS A  27     2556   4631   5917    131   -384  -2904       N  
ATOM    207  N   GLU A  28       3.368   3.858  19.147  1.00 14.14           N  
ANISOU  207  N   GLU A  28     1208   1542   2622   -172    -26   -884       N  
ATOM    208  CA  GLU A  28       2.463   4.312  20.202  1.00 15.62           C  
ANISOU  208  CA  GLU A  28     1343   1839   2752     59    -58  -1086       C  
ATOM    209  C   GLU A  28       2.643   3.558  21.516  1.00 16.15           C  
ANISOU  209  C   GLU A  28     1426   2307   2404     -4   -187  -1378       C  
ATOM    210  O   GLU A  28       2.085   3.956  22.554  1.00 18.31           O  
ANISOU  210  O   GLU A  28     1580   2975   2404     82   -283  -1544       O  
ATOM    211  CB  GLU A  28       1.004   4.275  19.716  1.00 14.99           C  
ANISOU  211  CB  GLU A  28     1222   1524   2949   -158     33   -637       C  
ATOM    212  CG  GLU A  28       0.738   5.184  18.543  1.00 18.23           C  
ANISOU  212  CG  GLU A  28     1682   2213   3034    176   -156   -474       C  
ATOM    213  CD  GLU A  28      -0.732   5.466  18.267  1.00 18.35           C  
ANISOU  213  CD  GLU A  28     1723   2150   3100    420   -195  -1073       C  
ATOM    214  OE1 GLU A  28      -1.533   5.619  19.213  1.00 21.58           O  
ANISOU  214  OE1 GLU A  28     2179   2505   3516    492    450   -193       O  
ATOM    215  OE2 GLU A  28      -1.074   5.598  17.062  1.00 26.04           O  
ANISOU  215  OE2 GLU A  28     1803   4963   3128    927   -561  -2176       O  
ATOM    216  N   HIS A  29       3.478   2.520  21.549  1.00 14.72           N  
ANISOU  216  N   HIS A  29     1170   2254   2168   -123   -302  -1029       N  
ATOM    217  CA  HIS A  29       3.765   1.778  22.775  1.00 17.17           C  
ANISOU  217  CA  HIS A  29     1445   3229   1850   -153   -536  -1040       C  
ATOM    218  C   HIS A  29       2.476   1.243  23.410  1.00 14.71           C  
ANISOU  218  C   HIS A  29     1398   2560   1630    291   -459   -904       C  
ATOM    219  O   HIS A  29       2.341   1.139  24.659  1.00 18.01           O  
ANISOU  219  O   HIS A  29     1617   3652   1574    319   -518   -952       O  
ATOM    220  CB  HIS A  29       4.664   2.569  23.751  1.00 24.17           C  
ANISOU  220  CB  HIS A  29     1786   4867   2530   -429   -687  -1917       C  
ATOM    221  CG  HIS A  29       6.006   2.769  23.128  1.00 30.31           C  
ANISOU  221  CG  HIS A  29     1631   6645   3242   -947   -637  -2467       C  
ATOM    222  ND1 HIS A  29       6.949   1.759  22.944  1.00 36.20           N  
ANISOU  222  ND1 HIS A  29     1487   7961   4309   -294   -523  -2177       N  
ATOM    223  CD2 HIS A  29       6.535   3.896  22.591  1.00 37.05           C  
ANISOU  223  CD2 HIS A  29     2440   7037   4598  -1902    178  -2791       C  
ATOM    224  CE1 HIS A  29       8.011   2.261  22.341  1.00 38.66           C  
ANISOU  224  CE1 HIS A  29     1692   9438   3558   -796   -400  -2709       C  
ATOM    225  NE2 HIS A  29       7.779   3.552  22.124  1.00 42.32           N  
ANISOU  225  NE2 HIS A  29     1928   9080   5071  -1858   -156  -2408       N  
ATOM    226  N   LEU A  30       1.594   0.798  22.570  1.00 13.22           N  
ANISOU  226  N   LEU A  30     1225   2462   1338    210   -299   -601       N  
ATOM    227  CA  LEU A  30       0.317   0.215  22.997  1.00 12.93           C  
ANISOU  227  CA  LEU A  30     1173   2367   1373    354   -217   -540       C  
ATOM    228  C   LEU A  30       0.411  -1.295  22.922  1.00 12.08           C  
ANISOU  228  C   LEU A  30     1089   2431   1070    415   -231   -258       C  
ATOM    229  O   LEU A  30       1.482  -1.881  22.669  1.00 13.36           O  
ANISOU  229  O   LEU A  30     1212   2278   1587    422   -265   -164       O  
ATOM    230  CB  LEU A  30      -0.845   0.831  22.217  1.00 12.49           C  
ANISOU  230  CB  LEU A  30     1184   2278   1282    263   -188   -274       C  
ATOM    231  CG  LEU A  30      -0.906   2.361  22.268  1.00 13.52           C  
ANISOU  231  CG  LEU A  30     1330   2318   1488    296   -245   -560       C  
ATOM    232  CD1 LEU A  30      -2.071   2.904  21.446  1.00 14.09           C  
ANISOU  232  CD1 LEU A  30     1338   2349   1667    260   -215   -331       C  
ATOM    233  CD2 LEU A  30      -0.945   2.845  23.717  1.00 18.66           C  
ANISOU  233  CD2 LEU A  30     1921   3266   1903    947   -686  -1245       C  
ATOM    234  N   ILE A  31      -0.693  -1.977  23.126  1.00 12.15           N  
ANISOU  234  N   ILE A  31     1140   2313   1165    435   -193   -144       N  
ATOM    235  CA  ILE A  31      -0.657  -3.434  23.234  1.00 12.33           C  
ANISOU  235  CA  ILE A  31     1143   2396   1147    532   -200     46       C  
ATOM    236  C   ILE A  31      -0.475  -4.118  21.887  1.00 10.87           C  
ANISOU  236  C   ILE A  31      940   2059   1131    288   -122     10       C  
ATOM    237  O   ILE A  31       0.369  -4.997  21.737  1.00 11.44           O  
ANISOU  237  O   ILE A  31     1214   1952   1180    440   -175    101       O  
ATOM    238  CB  ILE A  31      -1.913  -3.980  23.927  1.00 12.99           C  
ANISOU  238  CB  ILE A  31     1306   2497   1132    559    -45    176       C  
ATOM    239  CG1 ILE A  31      -2.045  -3.449  25.351  1.00 14.18           C  
ANISOU  239  CG1 ILE A  31     1418   2772   1199    452    -47     13       C  
ATOM    240  CG2 ILE A  31      -1.928  -5.500  23.904  1.00 15.09           C  
ANISOU  240  CG2 ILE A  31     1556   2517   1661    431     70    121       C  
ATOM    241  CD1 ILE A  31      -3.421  -3.730  25.922  1.00 18.83           C  
ANISOU  241  CD1 ILE A  31     1562   4159   1435    235    281     -6       C  
ATOM    242  N   LYS A  32      -1.269  -3.737  20.905  1.00 10.69           N  
ANISOU  242  N   LYS A  32     1084   1951   1028    308   -127     14       N  
ATOM    243  CA  LYS A  32      -1.312  -4.391  19.610  1.00 10.23           C  
ANISOU  243  CA  LYS A  32     1104   1636   1149    135   -122    -20       C  
ATOM    244  C   LYS A  32      -2.083  -3.532  18.648  1.00  8.78           C  
ANISOU  244  C   LYS A  32      806   1393   1136    -35    -76    -38       C  
ATOM    245  O   LYS A  32      -2.764  -2.561  19.038  1.00  9.57           O  
ANISOU  245  O   LYS A  32      872   1662   1102    231    -76    -76       O  
ATOM    246  CB  LYS A  32      -1.905  -5.794  19.684  1.00 11.39           C  
ANISOU  246  CB  LYS A  32     1170   1726   1430     44   -144    261       C  
ATOM    247  CG  LYS A  32      -3.346  -5.810  20.121  1.00 14.59           C  
ANISOU  247  CG  LYS A  32     1314   2039   2189     -2      0    481       C  
ATOM    248  CD  LYS A  32      -3.900  -7.222  20.217  1.00 21.77           C  
ANISOU  248  CD  LYS A  32     1734   2294   4245   -319     32   1222       C  
ATOM    249  CE  LYS A  32      -5.365  -7.237  20.613  1.00 29.14           C  
ANISOU  249  CE  LYS A  32     2036   3874   5163   -942    651   1206       C  
ATOM    250  NZ  LYS A  32      -5.845  -8.631  20.555  1.00 38.65           N  
ANISOU  250  NZ  LYS A  32     2880   4319   7488  -1798    197   1530       N  
ATOM    251  N   GLY A  33      -1.978  -3.866  17.377  1.00  8.66           N  
ANISOU  251  N   GLY A  33      819   1345   1127    100   -137     -6       N  
ATOM    252  CA  GLY A  33      -2.752  -3.232  16.344  1.00  8.54           C  
ANISOU  252  CA  GLY A  33      862   1241   1142     23   -170    -37       C  
ATOM    253  C   GLY A  33      -3.238  -4.226  15.309  1.00  8.37           C  
ANISOU  253  C   GLY A  33      836   1235   1111    -23   -113     53       C  
ATOM    254  O   GLY A  33      -2.606  -5.254  15.075  1.00  9.08           O  
ANISOU  254  O   GLY A  33      909   1225   1315    114   -210    -42       O  
ATOM    255  N   ARG A  34      -4.318  -3.845  14.635  1.00  8.42           N  
ANISOU  255  N   ARG A  34      744   1215   1241    -14   -158    -67       N  
ATOM    256  CA  ARG A  34      -4.837  -4.599  13.512  1.00  8.63           C  
ANISOU  256  CA  ARG A  34      869   1194   1218    -93   -247    -24       C  
ATOM    257  C   ARG A  34      -5.553  -3.650  12.560  1.00  8.59           C  
ANISOU  257  C   ARG A  34      806   1159   1300    -29   -254      2       C  
ATOM    258  O   ARG A  34      -6.106  -2.623  12.993  1.00  8.92           O  
ANISOU  258  O   ARG A  34      870   1215   1303    -34   -243      0       O  
ATOM    259  CB  ARG A  34      -5.791  -5.704  13.929  1.00 10.10           C  
ANISOU  259  CB  ARG A  34     1082   1263   1493   -215   -163     59       C  
ATOM    260  CG  ARG A  34      -7.039  -5.148  14.619  1.00 11.47           C  
ANISOU  260  CG  ARG A  34     1114   1568   1677   -354    -50    115       C  
ATOM    261  CD  ARG A  34      -8.073  -6.200  14.843  1.00 13.56           C  
ANISOU  261  CD  ARG A  34     1065   1952   2137   -503   -122    259       C  
ATOM    262  NE  ARG A  34      -9.200  -5.652  15.587  1.00 13.60           N  
ANISOU  262  NE  ARG A  34     1010   2130   2029   -483   -142    348       N  
ATOM    263  CZ  ARG A  34     -10.399  -6.220  15.643  1.00 14.80           C  
ANISOU  263  CZ  ARG A  34      967   2465   2190   -491   -336    693       C  
ATOM    264  NH1 ARG A  34     -10.649  -7.337  14.980  1.00 17.13           N  
ANISOU  264  NH1 ARG A  34     1291   2598   2620   -806   -570    547       N  
ATOM    265  NH2 ARG A  34     -11.292  -5.585  16.395  1.00 18.28           N  
ANISOU  265  NH2 ARG A  34      885   3258   2803   -457   -242    390       N  
ATOM    266  N   CYS A  35      -5.606  -4.020  11.300  1.00  8.90           N  
ANISOU  266  N   CYS A  35      885   1211   1285     37   -312    -64       N  
ATOM    267  CA  CYS A  35      -6.567  -3.328  10.405  1.00  9.23           C  
ANISOU  267  CA  CYS A  35      890   1289   1326     -4   -344     49       C  
ATOM    268  C   CYS A  35      -7.965  -3.839  10.686  1.00  9.69           C  
ANISOU  268  C   CYS A  35      918   1245   1519   -125   -327    -26       C  
ATOM    269  O   CYS A  35      -8.180  -4.990  11.024  1.00 12.15           O  
ANISOU  269  O   CYS A  35     1046   1346   2227   -102   -237    158       O  
ATOM    270  CB  CYS A  35      -6.259  -3.628   8.952  1.00 10.07           C  
ANISOU  270  CB  CYS A  35     1135   1353   1337    -59   -328    -29       C  
ATOM    271  SG  CYS A  35      -4.533  -3.332   8.442  1.00  9.72           S  
ANISOU  271  SG  CYS A  35     1145   1275   1272     56   -218     56       S  
ATOM    272  N   ARG A  36      -8.940  -2.986  10.533  1.00 10.64           N  
ANISOU  272  N   ARG A  36      886   1368   1789    -87   -469     45       N  
ATOM    273  CA  ARG A  36     -10.337  -3.409  10.575  1.00 12.08           C  
ANISOU  273  CA  ARG A  36      899   1789   1902   -188   -512    212       C  
ATOM    274  C   ARG A  36     -10.937  -3.308   9.179  1.00 13.53           C  
ANISOU  274  C   ARG A  36     1094   2139   1909   -470   -513    353       C  
ATOM    275  O   ARG A  36     -10.247  -3.000   8.201  1.00 13.31           O  
ANISOU  275  O   ARG A  36     1261   1973   1824   -329   -558     55       O  
ATOM    276  CB  ARG A  36     -11.134  -2.699  11.698  1.00 13.18           C  
ANISOU  276  CB  ARG A  36      868   2132   2008   -199   -395    212       C  
ATOM    277  CG  ARG A  36     -10.625  -3.178  13.060  1.00 13.85           C  
ANISOU  277  CG  ARG A  36     1096   2208   1957    -44   -378    203       C  
ATOM    278  CD  ARG A  36     -11.296  -2.592  14.247  1.00 16.54           C  
ANISOU  278  CD  ARG A  36     1472   2771   2042   -253   -160     95       C  
ATOM    279  NE  ARG A  36     -12.679  -2.977  14.337  1.00 15.62           N  
ANISOU  279  NE  ARG A  36     1572   2027   2335   -285     18     71       N  
ATOM    280  CZ  ARG A  36     -13.720  -2.253  14.501  1.00 22.52           C  
ANISOU  280  CZ  ARG A  36     1463   2279   4814   -325   -208   -692       C  
ATOM    281  NH1 ARG A  36     -13.658  -0.907  14.652  1.00 33.46           N  
ANISOU  281  NH1 ARG A  36     1926   2149   8639   -229   -415   -641       N  
ATOM    282  NH2 ARG A  36     -14.933  -2.820  14.545  1.00 22.60           N  
ANISOU  282  NH2 ARG A  36     1605   2639   4343   -619    839   -137       N  
ATOM    283  N   ASP A  37     -12.210  -3.576   9.033  1.00 14.02           N  
ANISOU  283  N   ASP A  37     1219   1964   2146   -387   -777    289       N  
ATOM    284  CA  ASP A  37     -12.871  -3.675   7.741  1.00 15.85           C  
ANISOU  284  CA  ASP A  37     1554   2366   2102   -752   -867    281       C  
ATOM    285  C   ASP A  37     -13.060  -2.335   7.070  1.00 14.27           C  
ANISOU  285  C   ASP A  37     1131   2352   1941   -429   -682    180       C  
ATOM    286  O   ASP A  37     -13.448  -2.284   5.889  1.00 16.75           O  
ANISOU  286  O   ASP A  37     1728   2631   2006   -533   -804    232       O  
ATOM    287  CB  ASP A  37     -14.209  -4.392   7.888  1.00 18.05           C  
ANISOU  287  CB  ASP A  37     1507   3060   2292   -892  -1004    753       C  
ATOM    288  CG  ASP A  37     -15.247  -3.710   8.739  1.00 23.25           C  
ANISOU  288  CG  ASP A  37     1703   5010   2120  -1290   -648     99       C  
ATOM    289  OD1 ASP A  37     -16.410  -4.122   8.692  1.00 22.57           O  
ANISOU  289  OD1 ASP A  37     1410   3512   3654   -593   -843    642       O  
ATOM    290  OD2 ASP A  37     -14.924  -2.805   9.514  1.00 40.45           O  
ANISOU  290  OD2 ASP A  37     2247   8237   4884  -2326    815  -3018       O  
ATOM    291  N   ASP A  38     -12.710  -1.278   7.733  1.00 13.23           N  
ANISOU  291  N   ASP A  38     1068   2253   1707    -58   -457    200       N  
ATOM    292  CA  ASP A  38     -12.567   0.100   7.260  1.00 14.10           C  
ANISOU  292  CA  ASP A  38     1016   2263   2079    -33   -559    272       C  
ATOM    293  C   ASP A  38     -11.217   0.436   6.620  1.00 13.14           C  
ANISOU  293  C   ASP A  38     1146   1975   1870     37   -548    344       C  
ATOM    294  O   ASP A  38     -10.981   1.575   6.188  1.00 14.07           O  
ANISOU  294  O   ASP A  38     1283   1848   2216    -44   -638    332       O  
ATOM    295  CB  ASP A  38     -12.835   1.129   8.361  1.00 14.55           C  
ANISOU  295  CB  ASP A  38     1084   2224   2221    156   -460    314       C  
ATOM    296  CG  ASP A  38     -11.871   1.016   9.529  1.00 13.50           C  
ANISOU  296  CG  ASP A  38     1113   2125   1890    102   -319    254       C  
ATOM    297  OD1 ASP A  38     -11.979   1.839  10.423  1.00 15.80           O  
ANISOU  297  OD1 ASP A  38     1392   2388   2222    405   -503    -56       O  
ATOM    298  OD2 ASP A  38     -11.007   0.093   9.539  1.00 11.19           O  
ANISOU  298  OD2 ASP A  38      797   2085   1368     17   -342    158       O  
ATOM    299  N   PHE A  39     -10.325  -0.534   6.530  1.00 11.86           N  
ANISOU  299  N   PHE A  39     1145   1736   1624   -144   -465    250       N  
ATOM    300  CA  PHE A  39      -8.982  -0.269   6.004  1.00 11.22           C  
ANISOU  300  CA  PHE A  39     1254   1622   1386    -69   -372    245       C  
ATOM    301  C   PHE A  39      -8.282   0.823   6.769  1.00 10.63           C  
ANISOU  301  C   PHE A  39     1182   1415   1442     40   -405    309       C  
ATOM    302  O   PHE A  39      -7.465   1.577   6.206  1.00 11.02           O  
ANISOU  302  O   PHE A  39     1185   1558   1446     -9   -342    289       O  
ATOM    303  CB  PHE A  39      -8.981   0.015   4.512  1.00 13.50           C  
ANISOU  303  CB  PHE A  39     1764   1984   1381   -348   -556    331       C  
ATOM    304  CG  PHE A  39      -9.385  -1.185   3.677  1.00 13.84           C  
ANISOU  304  CG  PHE A  39     1935   1943   1381   -507   -569    446       C  
ATOM    305  CD1 PHE A  39     -10.736  -1.439   3.445  1.00 17.14           C  
ANISOU  305  CD1 PHE A  39     2107   2565   1839   -831   -885    543       C  
ATOM    306  CD2 PHE A  39      -8.410  -2.001   3.156  1.00 15.86           C  
ANISOU  306  CD2 PHE A  39     2536   2034   1454    -71   -709    316       C  
ATOM    307  CE1 PHE A  39     -11.053  -2.538   2.632  1.00 20.49           C  
ANISOU  307  CE1 PHE A  39     3077   2901   1806  -1499   -865    528       C  
ATOM    308  CE2 PHE A  39      -8.748  -3.074   2.341  1.00 19.58           C  
ANISOU  308  CE2 PHE A  39     3727   2261   1451   -407   -447    191       C  
ATOM    309  CZ  PHE A  39     -10.068  -3.331   2.095  1.00 22.00           C  
ANISOU  309  CZ  PHE A  39     4148   2824   1385  -1125   -936    184       C  
ATOM    310  N   ARG A  40      -8.465   0.860   8.077  1.00  9.75           N  
ANISOU  310  N   ARG A  40      856   1424   1424    135   -335    198       N  
ATOM    311  CA  ARG A  40      -7.700   1.727   8.969  1.00  9.91           C  
ANISOU  311  CA  ARG A  40      905   1349   1510    110   -244    150       C  
ATOM    312  C   ARG A  40      -7.074   0.873  10.077  1.00  9.43           C  
ANISOU  312  C   ARG A  40      844   1331   1409    121   -191     30       C  
ATOM    313  O   ARG A  40      -7.488  -0.251  10.354  1.00  9.62           O  
ANISOU  313  O   ARG A  40      828   1334   1492     31   -313     30       O  
ATOM    314  CB  ARG A  40      -8.594   2.791   9.601  1.00 11.81           C  
ANISOU  314  CB  ARG A  40     1227   1633   1627    433   -341     26       C  
ATOM    315  CG  ARG A  40      -9.101   3.772   8.533  1.00 13.62           C  
ANISOU  315  CG  ARG A  40     1469   1824   1881    631   -207    187       C  
ATOM    316  CD  ARG A  40      -9.838   4.947   9.152  1.00 14.53           C  
ANISOU  316  CD  ARG A  40     1381   1909   2229    607    -99    239       C  
ATOM    317  NE  ARG A  40     -11.054   4.438   9.755  1.00 14.49           N  
ANISOU  317  NE  ARG A  40     1317   2077   2111    582    -73      4       N  
ATOM    318  CZ  ARG A  40     -12.059   5.174  10.186  1.00 14.94           C  
ANISOU  318  CZ  ARG A  40     1261   2332   2081    691   -305     -3       C  
ATOM    319  NH1 ARG A  40     -11.974   6.483  10.087  1.00 17.21           N  
ANISOU  319  NH1 ARG A  40     1580   2274   2685    915   -223   -306       N  
ATOM    320  NH2 ARG A  40     -13.120   4.550  10.733  1.00 17.48           N  
ANISOU  320  NH2 ARG A  40     1097   2867   2678    845    -89    142       N  
ATOM    321  N   CYS A  41      -6.021   1.444  10.663  1.00  8.63           N  
ANISOU  321  N   CYS A  41      809   1142   1329     69   -191     12       N  
ATOM    322  CA  CYS A  41      -5.261   0.816  11.727  1.00  8.35           C  
ANISOU  322  CA  CYS A  41      814   1079   1280    -18   -158      3       C  
ATOM    323  C   CYS A  41      -5.827   1.204  13.079  1.00  8.66           C  
ANISOU  323  C   CYS A  41      774   1181   1334     36   -162     -5       C  
ATOM    324  O   CYS A  41      -5.971   2.394  13.390  1.00  9.45           O  
ANISOU  324  O   CYS A  41      891   1189   1511     93    -35    -57       O  
ATOM    325  CB  CYS A  41      -3.803   1.289  11.624  1.00  8.64           C  
ANISOU  325  CB  CYS A  41      790   1158   1336     50   -123     74       C  
ATOM    326  SG  CYS A  41      -2.719   0.770  12.980  1.00  8.36           S  
ANISOU  326  SG  CYS A  41      752   1133   1293     17   -158    -50       S  
ATOM    327  N   TRP A  42      -6.182   0.200  13.869  1.00  8.55           N  
ANISOU  327  N   TRP A  42      725   1253   1272      2   -116     13       N  
ATOM    328  CA  TRP A  42      -6.744   0.344  15.196  1.00  9.04           C  
ANISOU  328  CA  TRP A  42      738   1427   1270    137    -44    -88       C  
ATOM    329  C   TRP A  42      -5.789  -0.283  16.207  1.00  8.92           C  
ANISOU  329  C   TRP A  42      772   1432   1187    105    -43    -60       C  
ATOM    330  O   TRP A  42      -5.353  -1.410  16.064  1.00  9.60           O  
ANISOU  330  O   TRP A  42      875   1430   1341     79   -210    -19       O  
ATOM    331  CB  TRP A  42      -8.097  -0.388  15.287  1.00 10.14           C  
ANISOU  331  CB  TRP A  42      798   1648   1406     45    -57    132       C  
ATOM    332  CG  TRP A  42      -9.182   0.262  14.450  1.00 10.19           C  
ANISOU  332  CG  TRP A  42      821   1555   1498     51   -110    147       C  
ATOM    333  CD1 TRP A  42      -9.298   0.235  13.084  1.00 11.09           C  
ANISOU  333  CD1 TRP A  42      946   1649   1619    103   -220    142       C  
ATOM    334  CD2 TRP A  42     -10.303   0.999  14.949  1.00 11.07           C  
ANISOU  334  CD2 TRP A  42      815   1609   1783     72    -23    194       C  
ATOM    335  NE1 TRP A  42     -10.433   0.949  12.744  1.00 12.29           N  
ANISOU  335  NE1 TRP A  42      878   2032   1760    126   -377    190       N  
ATOM    336  CE2 TRP A  42     -11.060   1.424  13.835  1.00 12.29           C  
ANISOU  336  CE2 TRP A  42      842   1906   1923     76   -101    331       C  
ATOM    337  CE3 TRP A  42     -10.735   1.376  16.228  1.00 11.82           C  
ANISOU  337  CE3 TRP A  42      869   1761   1861    207    -61     -8       C  
ATOM    338  CZ2 TRP A  42     -12.199   2.188  13.965  1.00 14.20           C  
ANISOU  338  CZ2 TRP A  42      830   2233   2333    203   -186    331       C  
ATOM    339  CZ3 TRP A  42     -11.909   2.129  16.327  1.00 13.63           C  
ANISOU  339  CZ3 TRP A  42      968   1937   2274    276    180    142       C  
ATOM    340  CH2 TRP A  42     -12.614   2.502  15.200  1.00 14.58           C  
ANISOU  340  CH2 TRP A  42      971   2008   2561    373   -199    -81       C  
ATOM    341  N   CYS A  43      -5.479   0.503  17.253  1.00  9.09           N  
ANISOU  341  N   CYS A  43      812   1365   1279    163    -46    -44       N  
ATOM    342  CA  CYS A  43      -4.643   0.057  18.308  1.00  9.21           C  
ANISOU  342  CA  CYS A  43      809   1494   1197    147    -88   -171       C  
ATOM    343  C   CYS A  43      -5.487  -0.318  19.533  1.00 10.63           C  
ANISOU  343  C   CYS A  43      843   1929   1266    248    -78     -3       C  
ATOM    344  O   CYS A  43      -6.480   0.351  19.867  1.00 12.04           O  
ANISOU  344  O   CYS A  43     1033   2069   1471    436    158    109       O  
ATOM    345  CB  CYS A  43      -3.645   1.133  18.778  1.00 10.19           C  
ANISOU  345  CB  CYS A  43      977   1530   1363    172   -115   -239       C  
ATOM    346  SG  CYS A  43      -2.556   1.820  17.520  1.00  9.89           S  
ANISOU  346  SG  CYS A  43      955   1414   1388    135   -103   -236       S  
ATOM    347  N   THR A  44      -5.052  -1.328  20.235  1.00 10.57           N  
ANISOU  347  N   THR A  44      908   1938   1171    353     64    -26       N  
ATOM    348  CA  THR A  44      -5.587  -1.723  21.546  1.00 12.62           C  
ANISOU  348  CA  THR A  44      937   2513   1346    340     48    217       C  
ATOM    349  C   THR A  44      -4.648  -1.260  22.639  1.00 12.64           C  
ANISOU  349  C   THR A  44     1002   2550   1249    306    139     95       C  
ATOM    350  O   THR A  44      -3.443  -1.426  22.536  1.00 12.11           O  
ANISOU  350  O   THR A  44     1081   2162   1359    397    -93    -31       O  
ATOM    351  CB  THR A  44      -5.778  -3.245  21.606  1.00 14.07           C  
ANISOU  351  CB  THR A  44     1373   2630   1343   -107    104    321       C  
ATOM    352  OG1 THR A  44      -6.731  -3.611  20.593  1.00 16.07           O  
ANISOU  352  OG1 THR A  44     1385   3074   1647   -465    -80    427       O  
ATOM    353  CG2 THR A  44      -6.340  -3.708  22.928  1.00 17.13           C  
ANISOU  353  CG2 THR A  44     1538   3301   1670   -255    130    664       C  
ATOM    354  N   ARG A  45      -5.225  -0.687  23.689  1.00 14.44           N  
ANISOU  354  N   ARG A  45     1306   2953   1229    738     33     91       N  
ATOM    355  CA  ARG A  45      -4.489  -0.181  24.830  1.00 16.62           C  
ANISOU  355  CA  ARG A  45     1655   3373   1286    945    -66   -157       C  
ATOM    356  C   ARG A  45      -5.186  -0.558  26.133  1.00 18.54           C  
ANISOU  356  C   ARG A  45     1764   4078   1201   1324    -20    -35       C  
ATOM    357  O   ARG A  45      -6.379  -0.806  26.177  1.00 20.94           O  
ANISOU  357  O   ARG A  45     1772   4910   1275   1467    164    223       O  
ATOM    358  CB  ARG A  45      -4.413   1.338  24.764  1.00 18.42           C  
ANISOU  358  CB  ARG A  45     2018   3324   1656    982   -190   -469       C  
ATOM    359  CG  ARG A  45      -5.773   2.023  24.969  1.00 23.59           C  
ANISOU  359  CG  ARG A  45     2861   4126   1975   1943    173    244       C  
ATOM    360  CD  ARG A  45      -5.563   3.554  25.049  1.00 29.58           C  
ANISOU  360  CD  ARG A  45     4099   4064   3077   2333   -186   -132       C  
ATOM    361  NE  ARG A  45      -6.968   4.008  25.173  1.00 30.18           N  
ANISOU  361  NE  ARG A  45     4303   4630   2535   2683   -360   -440       N  
ATOM    362  CZ  ARG A  45      -7.936   4.112  24.281  1.00 29.88           C  
ANISOU  362  CZ  ARG A  45     4320   4232   2800   2828   -556  -1280       C  
ATOM    363  NH1 ARG A  45      -7.502   3.770  23.099  1.00 31.87           N  
ANISOU  363  NH1 ARG A  45     5267   4360   2483   2614   -216   -741       N  
ATOM    364  NH2 ARG A  45      -9.124   4.545  24.706  1.00 29.92           N  
ANISOU  364  NH2 ARG A  45     3554   3995   3820   1504     42   -857       N  
ATOM    365  N   ASN A  46      -4.408  -0.621  27.226  1.00 20.16           N  
ANISOU  365  N   ASN A  46     2353   4095   1210   1183   -222   -290       N  
ATOM    366  CA  ASN A  46      -4.988  -0.677  28.572  1.00 22.42           C  
ANISOU  366  CA  ASN A  46     2838   4510   1170   1421   -166     61       C  
ATOM    367  C   ASN A  46      -5.784   0.583  28.849  1.00 27.50           C  
ANISOU  367  C   ASN A  46     3650   5304   1494   2032    -16   -601       C  
ATOM    368  O   ASN A  46      -5.292   1.673  28.503  1.00 29.15           O  
ANISOU  368  O   ASN A  46     4549   4747   1778   2561     73   -348       O  
ATOM    369  CB  ASN A  46      -3.826  -0.846  29.550  1.00 26.27           C  
ANISOU  369  CB  ASN A  46     3361   5328   1293   1596   -574   -509       C  
ATOM    370  CG  ASN A  46      -3.116  -2.174  29.379  1.00 24.57           C  
ANISOU  370  CG  ASN A  46     2942   5085   1309   1423   -698    -53       C  
ATOM    371  OD1 ASN A  46      -1.927  -2.221  28.968  1.00 26.07           O  
ANISOU  371  OD1 ASN A  46     2951   5046   1909   1327   -671   -396       O  
ATOM    372  ND2 ASN A  46      -3.796  -3.253  29.616  1.00 28.01           N  
ANISOU  372  ND2 ASN A  46     3374   5308   1961   1243   -292     86       N  
ATOM    373  N   CYS A  47      -6.994   0.440  29.429  1.00 30.96           N  
ANISOU  373  N   CYS A  47     3421   6810   1532   2279   -140   -714       N  
ATOM    374  CA  CYS A  47      -7.950   1.541  29.622  1.00 27.75           C  
ANISOU  374  CA  CYS A  47     3258   5358   1929   1201    330   -977       C  
ATOM    375  C   CYS A  47      -8.763   1.314  30.887  1.00 38.93           C  
ANISOU  375  C   CYS A  47     4435   8479   1878   2612    809   -194       C  
ATOM    376  O   CYS A  47      -8.350   0.494  31.735  1.00 40.30           O  
ANISOU  376  O   CYS A  47     4721   8858   1733   2424    679    -82       O  
ATOM    377  CB  CYS A  47      -8.924   1.775  28.402  1.00 21.38           C  
ANISOU  377  CB  CYS A  47     3394   3031   1699   1583    711   -619       C  
ATOM    378  SG  CYS A  47      -9.957   0.376  28.036  1.00 25.49           S  
ANISOU  378  SG  CYS A  47     2558   4973   2153    697    509   -116       S  
ATOM    379  OXT CYS A  47      -9.826   1.909  31.095  1.00 52.27           O  
ANISOU  379  OXT CYS A  47     5334  12196   2329   4368   1475    768       O  
TER     380      CYS A  47                                                      
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.