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***  troponin_C  ***

elNémo ID: 200207132052144186

Job options:

ID        	=	 200207132052144186
JOBID     	=	 troponin_C
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 troponin_C

HEADER    CONTRACTILE PROTEIN                     26-SEP-11   3TZ1              
TITLE     CRYSTAL STRUCTURE OF THE CA2+-SATURATED C-TERMINAL DOMAIN OF AKAZARA  
TITLE    2 SCALLOP TROPONIN C IN COMPLEX WITH A TROPONIN I FRAGMENT             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TROPONIN C;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C-TERMINAL DOMAIN, UNP RESIDUES 81-153;                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TROPONIN I;                                                
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 143-166;                                      
COMPND  10 SYNONYM: TNI;                                                        
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYS NIPPONENSIS AKAZARA;                    
SOURCE   3 ORGANISM_COMMON: AKAZARA SCALLOP;                                    
SOURCE   4 ORGANISM_TAXID: 6571;                                                
SOURCE   5 GENE: TROPONIN C;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET16B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: CHLAMYS NIPPONENSIS AKAZARA;                    
SOURCE  14 ORGANISM_COMMON: AKAZARA SCALLOP;                                    
SOURCE  15 ORGANISM_TAXID: 6571                                                 
KEYWDS    PROTEIN-PEPTIDE COMPLEX, EF HAND, CA2+-SENSOR, CONTRACTILE PROTEIN    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.YUMOTO,Y.S.KATO,I.OHTSUKI,M.TANOKURA                                
REVDAT   1   23-JAN-13 3TZ1    0                                                
JRNL        AUTH   Y.S.KATO,F.YUMOTO,H.TANAKA,T.MIYAKAWA,Y.MIYAUCHI,            
JRNL        AUTH 2 D.TAKESHITA,Y.SAWANO,T.OJIMA,I.OHTSUKI,M.TANOKURA            
JRNL        TITL   STRUCTURE OF THE CA2+-SATURATED C-TERMINAL DOMAIN OF SCALLOP 
JRNL        TITL 2 TROPONIN C IN COMPLEX WITH A TROPONIN I FRAGMENT             
JRNL        REF    BIOL.CHEM.                    V. 394    55 2012              
JRNL        REFN                   ISSN 1431-6730                               
JRNL        PMID   23096565                                                     
JRNL        DOI    10.1515/HSZ-2012-0152                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.32                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 7950                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.630                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 368                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.3244 -  2.5937    0.99     2585   148  0.2115 0.2200        
REMARK   3     2  2.5937 -  2.0589    1.00     2516   110  0.1797 0.2773        
REMARK   3     3  2.0589 -  1.7987    0.99     2481   110  0.2078 0.2772        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.44                                          
REMARK   3   B_SOL              : 55.34                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.950           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.87                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.70150                                              
REMARK   3    B22 (A**2) : -10.25340                                            
REMARK   3    B33 (A**2) : 3.55190                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005            756                                  
REMARK   3   ANGLE     :  0.978           1006                                  
REMARK   3   CHIRALITY :  0.082            116                                  
REMARK   3   PLANARITY :  0.005            127                                  
REMARK   3   DIHEDRAL  : 13.852            302                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 82:100)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.1328  10.4245 -10.5537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2568 T22:   0.2397                                     
REMARK   3      T33:   0.2071 T12:  -0.0188                                     
REMARK   3      T13:   0.0132 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0676 L22:   0.3667                                     
REMARK   3      L33:   0.2801 L12:  -0.0170                                     
REMARK   3      L13:   0.0368 L23:   0.2170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0981 S12:   0.1964 S13:   0.0565                       
REMARK   3      S21:  -0.4312 S22:  -0.0010 S23:   0.2635                       
REMARK   3      S31:  -0.1710 S32:  -0.0385 S33:  -0.0119                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 101:130)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -10.5327  -1.2151   1.2370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2260 T22:   0.2030                                     
REMARK   3      T33:   0.2236 T12:   0.0135                                     
REMARK   3      T13:  -0.0479 T23:   0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6085 L22:   0.3276                                     
REMARK   3      L33:   0.5721 L12:   0.1239                                     
REMARK   3      L13:   0.1799 L23:   0.1944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0086 S12:  -0.2360 S13:  -0.1900                       
REMARK   3      S21:   0.0682 S22:  -0.0354 S23:  -0.2881                       
REMARK   3      S31:   0.4535 S32:  -0.0491 S33:  -0.0033                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 131:152)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -18.7123  -1.7820 -10.5517              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2563 T22:   0.2609                                     
REMARK   3      T33:   0.1859 T12:   0.0113                                     
REMARK   3      T13:  -0.0338 T23:  -0.0342                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2037 L22:   1.1779                                     
REMARK   3      L33:   0.8046 L12:  -0.3369                                     
REMARK   3      L13:  -0.1133 L23:  -0.4728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2303 S12:   0.3708 S13:  -0.6098                       
REMARK   3      S21:  -0.5028 S22:   0.0823 S23:   0.3506                       
REMARK   3      S31:   0.4507 S32:  -0.3483 S33:   0.0820                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'B'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -19.3603   3.9113   1.2281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1704 T22:   0.1742                                     
REMARK   3      T33:   0.2204 T12:  -0.0155                                     
REMARK   3      T13:   0.0195 T23:  -0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6199 L22:   0.1393                                     
REMARK   3      L33:   0.3670 L12:  -0.0933                                     
REMARK   3      L13:   0.0134 L23:  -0.2250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0294 S12:  -0.1145 S13:  -0.0314                       
REMARK   3      S21:   0.2329 S22:   0.0422 S23:   0.1927                       
REMARK   3      S31:   0.1495 S32:  -0.0248 S33:   0.0011                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3TZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068098.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-06; 31-OCT-06               
REMARK 200  TEMPERATURE           (KELVIN) : 95; 95                             
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY; PHOTON FACTORY     
REMARK 200  BEAMLINE                       : AR-NW12A; AR-NW12A                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000; 0.97854, 0.9791, 0.974      
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR; AREA DETECTOR       
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210; ADSC QUANTUM     
REMARK 200                                   210                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8036                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : 0.05300                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26600                            
REMARK 200   FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 32.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1 M SODIUM ACETATE PH    
REMARK 280  4.6 AND 0.2 M AMMONIUM ACETATE, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       16.06500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.98300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.07550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       29.98300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.06500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       21.07550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6090 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A    79                                                      
REMARK 465     GLU A    80                                                      
REMARK 465     ASP A    81                                                      
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   1  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 133   OD1                                                    
REMARK 620 2 ASP A 131   OD1  81.3                                              
REMARK 620 3 THR A 137   O   149.1  82.5                                        
REMARK 620 4 GLU A 142   OE2  81.2  94.5 126.3                                  
REMARK 620 5 GLU A 142   OE1 131.2 106.1  78.7  50.5                            
REMARK 620 6 SER A 135   OG   78.8  90.6  75.2 158.3 146.8                      
REMARK 620 7 HOH A  12   O    94.4 172.0  98.1  91.6  81.8  81.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1                    
DBREF  3TZ1 A   80   152  UNP    Q27428   Q27428_CHLNI    81    153             
DBREF  3TZ1 B  143   166  UNP    Q7M3Y3   TNNI_CHLNI     143    166             
SEQADV 3TZ1 MET A   79  UNP  Q27428              EXPRESSION TAG                 
SEQRES   1 A   74  MET GLU ASP LEU ASP GLU ARG GLU LEU LYS GLU ALA PHE          
SEQRES   2 A   74  ARG VAL LEU ASP LYS GLU LYS LYS GLY VAL ILE LYS VAL          
SEQRES   3 A   74  ASP VAL LEU ARG TRP ILE LEU LYS SER LEU GLY ASP GLU          
SEQRES   4 A   74  LEU THR GLU ASP GLU ILE GLU ASN MET ILE ALA GLU THR          
SEQRES   5 A   74  ASP THR ASP GLY SER GLY THR VAL ASP TYR GLU GLU PHE          
SEQRES   6 A   74  LYS CYS LEU MET MET SER SER ASP ALA                          
SEQRES   1 B   24  GLY LEU SER PRO GLU LYS LYS LYS MET LEU LYS LYS LEU          
SEQRES   2 B   24  ILE MET GLN LYS ALA ALA GLU ASP LEU ALA ASN                  
HET     CA  A   1       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *27(H2 O)                                                     
HELIX    1   1 ASP A   83  ASP A   95  1                                  13    
HELIX    2   2 VAL A  104  GLY A  115  1                                  12    
HELIX    3   3 THR A  119  ASP A  131  1                                  13    
HELIX    4   4 ASP A  139  SER A  149  1                                  11    
HELIX    5   5 SER B  145  ALA B  165  1                                  21    
SHEET    1   A 2 ILE A 102  LYS A 103  0                                        
SHEET    2   A 2 THR A 137  VAL A 138 -1  O  VAL A 138   N  ILE A 102           
LINK         OD1 ASP A 133                CA    CA A   1     1555   1555  2.33  
LINK         OD1 ASP A 131                CA    CA A   1     1555   1555  2.34  
LINK         O   THR A 137                CA    CA A   1     1555   1555  2.35  
LINK         OE2 GLU A 142                CA    CA A   1     1555   1555  2.58  
LINK         OE1 GLU A 142                CA    CA A   1     1555   1555  2.59  
LINK         OG  SER A 135                CA    CA A   1     1555   1555  2.69  
LINK        CA    CA A   1                 O   HOH A  12     1555   1555  2.63  
SITE     1 AC1  6 HOH A  12  ASP A 131  ASP A 133  SER A 135                    
SITE     2 AC1  6 THR A 137  GLU A 142                                          
CRYST1   32.130   42.151   59.966  90.00  90.00  90.00 P 21 21 21    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      0.031124  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.023724  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016676        0.00000                         
ATOM      1  N   LEU A  82     -30.049   4.090  -6.581  1.00 46.50           N  
ANISOU    1  N   LEU A  82     5128   5872   6668     95   -265   -531       N  
ATOM      2  CA  LEU A  82     -29.160   5.235  -6.732  1.00 46.46           C  
ANISOU    2  CA  LEU A  82     5206   5858   6588     93   -261   -465       C  
ATOM      3  C   LEU A  82     -29.443   5.974  -8.042  1.00 45.18           C  
ANISOU    3  C   LEU A  82     5140   5672   6353    100   -387   -439       C  
ATOM      4  O   LEU A  82     -29.412   5.380  -9.119  1.00 48.81           O  
ANISOU    4  O   LEU A  82     5663   6142   6741     79   -424   -448       O  
ATOM      5  CB  LEU A  82     -27.696   4.783  -6.693  1.00 48.92           C  
ANISOU    5  CB  LEU A  82     5576   6204   6807     53   -142   -435       C  
ATOM      6  CG  LEU A  82     -26.710   5.574  -5.828  1.00 48.09           C  
ANISOU    6  CG  LEU A  82     5478   6101   6692     52    -58   -389       C  
ATOM      7  CD1 LEU A  82     -25.299   5.112  -6.099  1.00 33.43           C  
ANISOU    7  CD1 LEU A  82     3694   4280   4729     11     39   -363       C  
ATOM      8  CD2 LEU A  82     -26.827   7.065  -6.086  1.00 51.08           C  
ANISOU    8  CD2 LEU A  82     5908   6447   7055     74   -139   -341       C  
ATOM      9  N   ASP A  83     -29.731   7.267  -7.936  1.00 37.22           N  
ANISOU    9  N   ASP A  83     4146   4630   5365    130   -455   -407       N  
ATOM     10  CA  ASP A  83     -29.838   8.143  -9.094  1.00 38.60           C  
ANISOU   10  CA  ASP A  83     4426   4779   5462    137   -567   -372       C  
ATOM     11  C   ASP A  83     -28.531   8.077  -9.880  1.00 36.15           C  
ANISOU   11  C   ASP A  83     4238   4489   5010     93   -516   -326       C  
ATOM     12  O   ASP A  83     -27.452   8.165  -9.291  1.00 33.59           O  
ANISOU   12  O   ASP A  83     3924   4184   4655     71   -407   -295       O  
ATOM     13  CB  ASP A  83     -30.083   9.583  -8.627  1.00 43.90           C  
ANISOU   13  CB  ASP A  83     5094   5413   6173    172   -618   -337       C  
ATOM     14  CG  ASP A  83     -30.632  10.471  -9.728  1.00 52.02           C  
ANISOU   14  CG  ASP A  83     6207   6404   7156    193   -761   -317       C  
ATOM     15  OD1 ASP A  83     -29.923  10.678 -10.735  1.00 52.76           O  
ANISOU   15  OD1 ASP A  83     6421   6498   7126    167   -777   -277       O  
ATOM     16  OD2 ASP A  83     -31.769  10.970  -9.579  1.00 52.78           O  
ANISOU   16  OD2 ASP A  83     6248   6470   7337    237   -859   -341       O  
ATOM     17  N   GLU A  84     -28.616   7.918 -11.200  1.00 38.99           N  
ANISOU   17  N   GLU A  84     4688   4844   5282     80   -592   -322       N  
ATOM     18  CA  GLU A  84     -27.400   7.833 -12.014  1.00 38.28           C  
ANISOU   18  CA  GLU A  84     4717   4774   5054     36   -544   -281       C  
ATOM     19  C   GLU A  84     -26.635   9.154 -12.035  1.00 32.92           C  
ANISOU   19  C   GLU A  84     4119   4076   4313     32   -540   -214       C  
ATOM     20  O   GLU A  84     -25.419   9.172 -12.208  1.00 28.38           O  
ANISOU   20  O   GLU A  84     3614   3522   3647     -6   -457   -178       O  
ATOM     21  CB  GLU A  84     -27.696   7.365 -13.441  1.00 45.36           C  
ANISOU   21  CB  GLU A  84     5697   5669   5869     23   -629   -293       C  
ATOM     22  CG  GLU A  84     -26.439   7.172 -14.280  1.00 50.92           C  
ANISOU   22  CG  GLU A  84     6520   6396   6430    -25   -571   -255       C  
ATOM     23  CD  GLU A  84     -26.418   5.860 -15.053  1.00 55.60           C  
ANISOU   23  CD  GLU A  84     7132   7018   6975    -51   -562   -293       C  
ATOM     24  OE1 GLU A  84     -27.395   5.082 -14.961  1.00 61.08           O  
ANISOU   24  OE1 GLU A  84     7748   7713   7746    -33   -602   -348       O  
ATOM     25  OE2 GLU A  84     -25.413   5.608 -15.755  1.00 50.99           O  
ANISOU   25  OE2 GLU A  84     6642   6456   6275    -91   -513   -268       O  
ATOM     26  N   ARG A  85     -27.354  10.258 -11.865  1.00 34.45           N  
ANISOU   26  N   ARG A  85     4304   4228   4558     71   -629   -199       N  
ATOM     27  CA  ARG A  85     -26.709  11.566 -11.755  1.00 31.20           C  
ANISOU   27  CA  ARG A  85     3959   3793   4101     71   -626   -138       C  
ATOM     28  C   ARG A  85     -25.793  11.597 -10.550  1.00 24.73           C  
ANISOU   28  C   ARG A  85     3086   2998   3311     57   -491   -122       C  
ATOM     29  O   ARG A  85     -24.685  12.141 -10.595  1.00 25.97           O  
ANISOU   29  O   ARG A  85     3316   3162   3392     29   -430    -74       O  
ATOM     30  CB  ARG A  85     -27.749  12.674 -11.610  1.00 38.41           C  
ANISOU   30  CB  ARG A  85     4851   4658   5084    122   -744   -133       C  
ATOM     31  CG  ARG A  85     -28.146  13.327 -12.909  1.00 48.85           C  
ANISOU   31  CG  ARG A  85     6287   5944   6329    131   -876   -110       C  
ATOM     32  CD  ARG A  85     -29.211  14.377 -12.647  1.00 54.30           C  
ANISOU   32  CD  ARG A  85     6945   6587   7101    186   -991   -112       C  
ATOM     33  NE  ARG A  85     -30.329  13.808 -11.898  1.00 56.74           N  
ANISOU   33  NE  ARG A  85     7113   6900   7547    222  -1011   -176       N  
ATOM     34  CZ  ARG A  85     -31.388  14.499 -11.490  1.00 59.58           C  
ANISOU   34  CZ  ARG A  85     7410   7225   8003    273  -1100   -194       C  
ATOM     35  NH1 ARG A  85     -31.479  15.797 -11.755  1.00 58.88           N  
ANISOU   35  NH1 ARG A  85     7390   7094   7888    298  -1181   -151       N  
ATOM     36  NH2 ARG A  85     -32.356  13.888 -10.816  1.00 59.07           N  
ANISOU   36  NH2 ARG A  85     7216   7169   8061    300  -1108   -255       N  
ATOM     37  N   GLU A  86     -26.277  11.028  -9.454  1.00 27.81           N  
ANISOU   37  N   GLU A  86     3350   3401   3816     77   -445   -165       N  
ATOM     38  CA  GLU A  86     -25.521  10.988  -8.215  1.00 31.53           C  
ANISOU   38  CA  GLU A  86     3759   3893   4327     69   -320   -157       C  
ATOM     39  C   GLU A  86     -24.324  10.057  -8.369  1.00 24.92           C  
ANISOU   39  C   GLU A  86     2957   3101   3410     21   -205   -155       C  
ATOM     40  O   GLU A  86     -23.228  10.350  -7.893  1.00 24.64           O  
ANISOU   40  O   GLU A  86     2942   3082   3339      0   -112   -123       O  
ATOM     41  CB  GLU A  86     -26.422  10.498  -7.087  1.00 37.91           C  
ANISOU   41  CB  GLU A  86     4427   4702   5275    101   -304   -209       C  
ATOM     42  CG  GLU A  86     -26.059  11.040  -5.739  1.00 35.63           C  
ANISOU   42  CG  GLU A  86     4073   4412   5053    115   -225   -194       C  
ATOM     43  CD  GLU A  86     -26.997  10.550  -4.668  1.00 33.42           C  
ANISOU   43  CD  GLU A  86     3659   4131   4909    146   -212   -247       C  
ATOM     44  OE1 GLU A  86     -28.167  10.251  -4.995  1.00 38.67           O  
ANISOU   44  OE1 GLU A  86     4283   4782   5629    168   -298   -288       O  
ATOM     45  OE2 GLU A  86     -26.558  10.451  -3.508  1.00 30.15           O  
ANISOU   45  OE2 GLU A  86     3182   3730   4544    147   -113   -248       O  
ATOM     46  N   LEU A  87     -24.552   8.928  -9.034  1.00 22.17           N  
ANISOU   46  N   LEU A  87     2613   2774   3036      5   -213   -192       N  
ATOM     47  CA  LEU A  87     -23.495   7.963  -9.319  1.00 18.97           C  
ANISOU   47  CA  LEU A  87     2246   2411   2550    -39   -115   -196       C  
ATOM     48  C   LEU A  87     -22.382   8.590 -10.147  1.00 21.12           C  
ANISOU   48  C   LEU A  87     2645   2687   2692    -74    -99   -141       C  
ATOM     49  O   LEU A  87     -21.198   8.417  -9.851  1.00 21.34           O  
ANISOU   49  O   LEU A  87     2693   2744   2670   -105      8   -123       O  
ATOM     50  CB  LEU A  87     -24.063   6.757 -10.077  1.00 22.19           C  
ANISOU   50  CB  LEU A  87     2650   2835   2948    -48   -150   -243       C  
ATOM     51  CG  LEU A  87     -23.063   5.623 -10.299  1.00 31.71           C  
ANISOU   51  CG  LEU A  87     3882   4085   4082    -90    -48   -255       C  
ATOM     52  CD1 LEU A  87     -22.830   4.895  -8.990  1.00 34.82           C  
ANISOU   52  CD1 LEU A  87     4172   4503   4557    -86     63   -285       C  
ATOM     53  CD2 LEU A  87     -23.552   4.653 -11.377  1.00 31.32           C  
ANISOU   53  CD2 LEU A  87     3863   4044   3992   -102   -104   -290       C  
ATOM     54  N   LYS A  88     -22.764   9.321 -11.190  1.00 21.48           N  
ANISOU   54  N   LYS A  88     2779   2702   2681    -70   -208   -115       N  
ATOM     55  CA  LYS A  88     -21.787   9.972 -12.050  1.00 20.95           C  
ANISOU   55  CA  LYS A  88     2840   2632   2486   -105   -202    -62       C  
ATOM     56  C   LYS A  88     -21.013  11.044 -11.288  1.00 20.68           C  
ANISOU   56  C   LYS A  88     2813   2589   2453   -107   -144    -16       C  
ATOM     57  O   LYS A  88     -19.808  11.191 -11.471  1.00 22.58           O  
ANISOU   57  O   LYS A  88     3119   2850   2608   -146    -66     15       O  
ATOM     58  CB  LYS A  88     -22.463  10.561 -13.295  1.00 21.55           C  
ANISOU   58  CB  LYS A  88     3011   2672   2506    -95   -339    -46       C  
ATOM     59  CG  LYS A  88     -22.934   9.495 -14.270  1.00 30.58           C  
ANISOU   59  CG  LYS A  88     4177   3829   3614   -104   -386    -84       C  
ATOM     60  CD  LYS A  88     -23.452  10.100 -15.558  1.00 30.97           C  
ANISOU   60  CD  LYS A  88     4334   3842   3592    -98   -516    -64       C  
ATOM     61  CE  LYS A  88     -23.921   9.013 -16.514  1.00 31.49           C  
ANISOU   61  CE  LYS A  88     4420   3922   3624   -107   -563   -104       C  
ATOM     62  NZ  LYS A  88     -24.441   9.567 -17.796  1.00 39.83           N  
ANISOU   62  NZ  LYS A  88     5585   4940   4607    -99   -694    -86       N  
ATOM     63  N   GLU A  89     -21.698  11.777 -10.417  1.00 19.78           N  
ANISOU   63  N   GLU A  89     2629   2447   2440    -66   -180    -15       N  
ATOM     64  CA  GLU A  89     -21.029  12.791  -9.607  1.00 22.55           C  
ANISOU   64  CA  GLU A  89     2978   2788   2802    -65   -127     26       C  
ATOM     65  C   GLU A  89     -20.026  12.156  -8.641  1.00 22.91           C  
ANISOU   65  C   GLU A  89     2965   2876   2863    -86     19     15       C  
ATOM     66  O   GLU A  89     -18.916  12.657  -8.470  1.00 21.35           O  
ANISOU   66  O   GLU A  89     2813   2690   2611   -113     92     52       O  
ATOM     67  CB  GLU A  89     -22.049  13.643  -8.841  1.00 23.74           C  
ANISOU   67  CB  GLU A  89     3058   2899   3064    -13   -197     24       C  
ATOM     68  CG  GLU A  89     -21.424  14.710  -7.935  1.00 23.94           C  
ANISOU   68  CG  GLU A  89     3075   2912   3109     -8   -145     64       C  
ATOM     69  CD  GLU A  89     -20.781  15.854  -8.719  1.00 32.83           C  
ANISOU   69  CD  GLU A  89     4329   4013   4131    -31   -178    125       C  
ATOM     70  OE1 GLU A  89     -21.023  15.960  -9.940  1.00 32.85           O  
ANISOU   70  OE1 GLU A  89     4425   4000   4058    -41   -260    137       O  
ATOM     71  OE2 GLU A  89     -20.037  16.651  -8.110  1.00 33.12           O  
ANISOU   71  OE2 GLU A  89     4375   4045   4163    -38   -121    161       O  
ATOM     72  N   ALA A  90     -20.423  11.058  -7.999  1.00 21.00           N  
ANISOU   72  N   ALA A  90     2624   2658   2698    -74     60    -36       N  
ATOM     73  CA  ALA A  90     -19.526  10.322  -7.110  1.00 19.95           C  
ANISOU   73  CA  ALA A  90     2436   2565   2579    -91    194    -51       C  
ATOM     74  C   ALA A  90     -18.288   9.828  -7.852  1.00 20.35           C  
ANISOU   74  C   ALA A  90     2572   2652   2509   -141    265    -38       C  
ATOM     75  O   ALA A  90     -17.163   9.957  -7.362  1.00 17.81           O  
ANISOU   75  O   ALA A  90     2258   2352   2158   -163    364    -20       O  
ATOM     76  CB  ALA A  90     -20.257   9.139  -6.478  1.00 18.32           C  
ANISOU   76  CB  ALA A  90     2123   2374   2465    -72    215   -111       C  
ATOM     77  N   PHE A  91     -18.500   9.240  -9.027  1.00 18.85           N  
ANISOU   77  N   PHE A  91     2443   2469   2252   -160    216    -50       N  
ATOM     78  CA  PHE A  91     -17.386   8.749  -9.840  1.00 18.10           C  
ANISOU   78  CA  PHE A  91     2432   2406   2038   -208    277    -40       C  
ATOM     79  C   PHE A  91     -16.421   9.886 -10.180  1.00 21.97           C  
ANISOU   79  C   PHE A  91     3016   2888   2443   -235    295     17       C  
ATOM     80  O   PHE A  91     -15.202   9.751 -10.043  1.00 21.44           O  
ANISOU   80  O   PHE A  91     2975   2853   2320   -268    396     28       O  
ATOM     81  CB  PHE A  91     -17.907   8.072 -11.112  1.00 21.91           C  
ANISOU   81  CB  PHE A  91     2972   2890   2462   -219    203    -60       C  
ATOM     82  CG  PHE A  91     -16.849   7.318 -11.880  1.00 20.79           C  
ANISOU   82  CG  PHE A  91     2902   2788   2210   -266    272    -62       C  
ATOM     83  CD1 PHE A  91     -16.452   6.053 -11.483  1.00 21.43           C  
ANISOU   83  CD1 PHE A  91     2927   2910   2305   -277    360   -103       C  
ATOM     84  CD2 PHE A  91     -16.263   7.877 -13.002  1.00 24.99           C  
ANISOU   84  CD2 PHE A  91     3557   3314   2623   -300    248    -23       C  
ATOM     85  CE1 PHE A  91     -15.480   5.359 -12.193  1.00 24.11           C  
ANISOU   85  CE1 PHE A  91     3330   3286   2543   -319    423   -107       C  
ATOM     86  CE2 PHE A  91     -15.291   7.193 -13.713  1.00 30.02           C  
ANISOU   86  CE2 PHE A  91     4259   3989   3158   -344    314    -27       C  
ATOM     87  CZ  PHE A  91     -14.904   5.931 -13.312  1.00 25.09           C  
ANISOU   87  CZ  PHE A  91     3575   3406   2550   -353    400    -70       C  
ATOM     88  N   ARG A  92     -16.967  11.015 -10.612  1.00 21.66           N  
ANISOU   88  N   ARG A  92     3030   2805   2395   -220    197     52       N  
ATOM     89  CA  ARG A  92     -16.138  12.166 -10.951  1.00 23.54           C  
ANISOU   89  CA  ARG A  92     3362   3029   2555   -246    206    108       C  
ATOM     90  C   ARG A  92     -15.302  12.628  -9.766  1.00 23.36           C  
ANISOU   90  C   ARG A  92     3289   3017   2570   -247    306    123       C  
ATOM     91  O   ARG A  92     -14.112  12.924  -9.904  1.00 25.24           O  
ANISOU   91  O   ARG A  92     3584   3273   2732   -286    381    151       O  
ATOM     92  CB  ARG A  92     -17.007  13.327 -11.436  1.00 24.05           C  
ANISOU   92  CB  ARG A  92     3479   3038   2622   -220     78    139       C  
ATOM     93  CG  ARG A  92     -17.313  13.301 -12.932  1.00 38.95           C  
ANISOU   93  CG  ARG A  92     5478   4910   4413   -237    -12    149       C  
ATOM     94  CD  ARG A  92     -18.099  14.542 -13.355  1.00 46.04           C  
ANISOU   94  CD  ARG A  92     6432   5750   5311   -209   -138    183       C  
ATOM     95  NE  ARG A  92     -17.248  15.663 -13.755  1.00 54.06           N  
ANISOU   95  NE  ARG A  92     7556   6746   6237   -240   -125    241       N  
ATOM     96  CZ  ARG A  92     -16.708  16.537 -12.910  1.00 55.76           C  
ANISOU   96  CZ  ARG A  92     7753   6953   6480   -240    -74    272       C  
ATOM     97  NH1 ARG A  92     -16.910  16.412 -11.604  1.00 61.62           N  
ANISOU   97  NH1 ARG A  92     8373   7704   7336   -209    -28    249       N  
ATOM     98  NH2 ARG A  92     -15.955  17.530 -13.369  1.00 43.96           N  
ANISOU   98  NH2 ARG A  92     6365   5439   4899   -272    -66    324       N  
ATOM     99  N   VAL A  93     -15.933  12.713  -8.603  1.00 19.87           N  
ANISOU   99  N   VAL A  93     2739   2563   2246   -206    306    105       N  
ATOM    100  CA  VAL A  93     -15.231  13.157  -7.403  1.00 20.64           C  
ANISOU  100  CA  VAL A  93     2783   2670   2390   -202    395    118       C  
ATOM    101  C   VAL A  93     -14.087  12.226  -7.021  1.00 22.36           C  
ANISOU  101  C   VAL A  93     2977   2940   2579   -232    525     97       C  
ATOM    102  O   VAL A  93     -13.008  12.686  -6.640  1.00 19.64           O  
ANISOU  102  O   VAL A  93     2650   2608   2203   -254    604    121       O  
ATOM    103  CB  VAL A  93     -16.189  13.336  -6.202  1.00 20.23           C  
ANISOU  103  CB  VAL A  93     2617   2597   2475   -149    371     97       C  
ATOM    104  CG1 VAL A  93     -15.398  13.672  -4.951  1.00 20.16           C  
ANISOU  104  CG1 VAL A  93     2552   2599   2508   -146    470    107       C  
ATOM    105  CG2 VAL A  93     -17.208  14.434  -6.492  1.00 24.00           C  
ANISOU  105  CG2 VAL A  93     3117   3021   2980   -117    246    121       C  
ATOM    106  N   LEU A  94     -14.317  10.916  -7.140  1.00 18.93           N  
ANISOU  106  N   LEU A  94     2503   2533   2155   -232    545     51       N  
ATOM    107  CA  LEU A  94     -13.333   9.925  -6.711  1.00 19.77           C  
ANISOU  107  CA  LEU A  94     2579   2688   2245   -254    665     24       C  
ATOM    108  C   LEU A  94     -12.278   9.628  -7.776  1.00 24.64           C  
ANISOU  108  C   LEU A  94     3293   3335   2734   -306    706     35       C  
ATOM    109  O   LEU A  94     -11.301   8.928  -7.510  1.00 22.56           O  
ANISOU  109  O   LEU A  94     3016   3112   2442   -327    807     17       O  
ATOM    110  CB  LEU A  94     -14.039   8.626  -6.301  1.00 21.43           C  
ANISOU  110  CB  LEU A  94     2702   2914   2527   -232    673    -32       C  
ATOM    111  CG  LEU A  94     -15.036   8.782  -5.152  1.00 20.32           C  
ANISOU  111  CG  LEU A  94     2455   2748   2517   -184    648    -50       C  
ATOM    112  CD1 LEU A  94     -15.722   7.448  -4.849  1.00 17.34           C  
ANISOU  112  CD1 LEU A  94     2001   2386   2201   -168    658   -107       C  
ATOM    113  CD2 LEU A  94     -14.330   9.321  -3.899  1.00 19.32           C  
ANISOU  113  CD2 LEU A  94     2280   2625   2435   -174    731    -35       C  
ATOM    114  N   ASP A  95     -12.467  10.171  -8.978  1.00 23.65           N  
ANISOU  114  N   ASP A  95     3268   3189   2530   -324    628     64       N  
ATOM    115  CA  ASP A  95     -11.471   9.998 -10.020  1.00 23.44           C  
ANISOU  115  CA  ASP A  95     3341   3187   2378   -375    666     78       C  
ATOM    116  C   ASP A  95     -10.551  11.184  -9.863  1.00 29.86           C  
ANISOU  116  C   ASP A  95     4205   3992   3149   -398    706    125       C  
ATOM    117  O   ASP A  95     -10.777  12.255 -10.431  1.00 28.87           O  
ANISOU  117  O   ASP A  95     4154   3829   2986   -404    635    167       O  
ATOM    118  CB  ASP A  95     -12.186  10.054 -11.375  1.00 24.75           C  
ANISOU  118  CB  ASP A  95     3594   3330   2481   -383    558     87       C  
ATOM    119  CG  ASP A  95     -11.231  10.075 -12.560  1.00 24.89           C  
ANISOU  119  CG  ASP A  95     3730   3365   2360   -437    585    109       C  
ATOM    120  OD1 ASP A  95     -10.031   9.784 -12.376  1.00 27.44           O  
ANISOU  120  OD1 ASP A  95     4060   3727   2640   -470    693    105       O  
ATOM    121  OD2 ASP A  95     -11.703  10.380 -13.682  1.00 29.31           O  
ANISOU  121  OD2 ASP A  95     4380   3900   2858   -445    496    127       O  
ATOM    122  N   LYS A  96      -9.443  10.946  -9.167  1.00 28.62           N  
ANISOU  122  N   LYS A  96     4015   3871   2990   -416    821    117       N  
ATOM    123  CA  LYS A  96      -8.598  12.037  -8.674  1.00 28.91           C  
ANISOU  123  CA  LYS A  96     4069   3900   3015   -430    870    155       C  
ATOM    124  C   LYS A  96      -7.698  12.557  -9.778  1.00 28.40           C  
ANISOU  124  C   LYS A  96     4101   3836   2853   -463    850    185       C  
ATOM    125  O   LYS A  96      -7.331  13.739  -9.805  1.00 30.83           O  
ANISOU  125  O   LYS A  96     4453   4120   3140   -473    837    226       O  
ATOM    126  CB  LYS A  96      -7.751  11.582  -7.472  1.00 21.99           C  
ANISOU  126  CB  LYS A  96     3057   3048   2250   -368    874    129       C  
ATOM    127  CG  LYS A  96      -8.556  11.153  -6.239  1.00 28.72           C  
ANISOU  127  CG  LYS A  96     3806   3897   3211   -327    881    101       C  
ATOM    128  CD  LYS A  96      -9.512  12.245  -5.794  1.00 33.44           C  
ANISOU  128  CD  LYS A  96     4415   4452   3838   -336    900    126       C  
ATOM    129  CE  LYS A  96     -10.230  11.895  -4.494  1.00 27.59           C  
ANISOU  129  CE  LYS A  96     3553   3705   3226   -284    902     96       C  
ATOM    130  NZ  LYS A  96     -11.226  12.956  -4.160  1.00 26.56           N  
ANISOU  130  NZ  LYS A  96     3405   3525   3161   -250    819    121       N  
ATOM    131  N   GLU A  97      -7.335  11.662 -10.688  1.00 30.70           N  
ANISOU  131  N   GLU A  97     4419   4152   3092   -475    844    163       N  
ATOM    132  CA  GLU A  97      -6.422  12.013 -11.768  1.00 30.57           C  
ANISOU  132  CA  GLU A  97     4477   4137   3000   -499    827    183       C  
ATOM    133  C   GLU A  97      -7.173  12.404 -13.032  1.00 30.93           C  
ANISOU  133  C   GLU A  97     4674   4159   2920   -551    783    214       C  
ATOM    134  O   GLU A  97      -6.560  12.731 -14.048  1.00 32.47           O  
ANISOU  134  O   GLU A  97     4942   4349   3046   -574    763    231       O  
ATOM    135  CB  GLU A  97      -5.481  10.842 -12.058  1.00 34.01           C  
ANISOU  135  CB  GLU A  97     4857   4609   3454   -477    840    146       C  
ATOM    136  CG  GLU A  97      -4.573  10.483 -10.895  1.00 44.63           C  
ANISOU  136  CG  GLU A  97     6077   5974   4905   -420    852    128       C  
ATOM    137  CD  GLU A  97      -3.872   9.148 -11.089  1.00 54.91           C  
ANISOU  137  CD  GLU A  97     7333   7304   6226   -395    853     96       C  
ATOM    138  OE1 GLU A  97      -3.881   8.626 -12.223  1.00 56.24           O  
ANISOU  138  OE1 GLU A  97     7563   7480   6326   -424    853     87       O  
ATOM    139  OE2 GLU A  97      -3.318   8.616 -10.102  1.00 60.15           O  
ANISOU  139  OE2 GLU A  97     7904   7981   6968   -345    846     83       O  
ATOM    140  N   LYS A  98      -8.502  12.375 -12.964  1.00 25.53           N  
ANISOU  140  N   LYS A  98     3993   3449   2260   -534    717    213       N  
ATOM    141  CA  LYS A  98      -9.343  12.669 -14.124  1.00 30.85           C  
ANISOU  141  CA  LYS A  98     4754   4086   2882   -533    600    231       C  
ATOM    142  C   LYS A  98      -8.976  11.768 -15.299  1.00 34.17           C  
ANISOU  142  C   LYS A  98     5247   4535   3200   -571    613    214       C  
ATOM    143  O   LYS A  98      -8.901  12.218 -16.445  1.00 33.15           O  
ANISOU  143  O   LYS A  98     5235   4387   2973   -600    566    243       O  
ATOM    144  CB  LYS A  98      -9.227  14.146 -14.528  1.00 30.54           C  
ANISOU  144  CB  LYS A  98     4810   4002   2793   -548    552    290       C  
ATOM    145  CG  LYS A  98      -9.598  15.118 -13.422  1.00 37.11           C  
ANISOU  145  CG  LYS A  98     5578   4802   3722   -511    533    310       C  
ATOM    146  CD  LYS A  98     -10.917  14.712 -12.768  1.00 44.73           C  
ANISOU  146  CD  LYS A  98     6440   5751   4806   -449    462    278       C  
ATOM    147  CE  LYS A  98     -11.061  15.328 -11.380  1.00 46.91           C  
ANISOU  147  CE  LYS A  98     6621   6013   5191   -413    484    283       C  
ATOM    148  NZ  LYS A  98     -12.150  14.682 -10.589  1.00 40.72           N  
ANISOU  148  NZ  LYS A  98     5719   5226   4527   -360    449    241       N  
ATOM    149  N   LYS A  99      -8.690  10.505 -14.990  1.00 30.79           N  
ANISOU  149  N   LYS A  99     4752   4153   2793   -571    683    166       N  
ATOM    150  CA  LYS A  99      -8.359   9.512 -16.004  1.00 31.45           C  
ANISOU  150  CA  LYS A  99     4891   4269   2790   -603    701    142       C  
ATOM    151  C   LYS A  99      -9.517   8.572 -16.379  1.00 32.14           C  
ANISOU  151  C   LYS A  99     4949   4351   2913   -572    621    105       C  
ATOM    152  O   LYS A  99      -9.337   7.647 -17.165  1.00 33.12           O  
ANISOU  152  O   LYS A  99     5109   4502   2974   -594    632     80       O  
ATOM    153  CB  LYS A  99      -7.100   8.735 -15.605  1.00 33.97           C  
ANISOU  153  CB  LYS A  99     5103   4623   3179   -578    772    109       C  
ATOM    154  CG  LYS A  99      -5.834   9.597 -15.600  1.00 44.83           C  
ANISOU  154  CG  LYS A  99     6466   5992   4575   -570    787    135       C  
ATOM    155  CD  LYS A  99      -4.585   8.773 -15.310  1.00 54.46           C  
ANISOU  155  CD  LYS A  99     7587   7241   5864   -533    822    106       C  
ATOM    156  CE  LYS A  99      -3.343   9.659 -15.229  1.00 59.92           C  
ANISOU  156  CE  LYS A  99     8265   7929   6574   -526    833    129       C  
ATOM    157  NZ  LYS A  99      -2.568   9.461 -13.964  1.00 60.82           N  
ANISOU  157  NZ  LYS A  99     8258   8057   6794   -474    852    116       N  
ATOM    158  N   GLY A 100     -10.694   8.796 -15.798  1.00 26.49           N  
ANISOU  158  N   GLY A 100     4164   3601   2298   -522    541    100       N  
ATOM    159  CA  GLY A 100     -11.859   7.981 -16.102  1.00 26.34           C  
ANISOU  159  CA  GLY A 100     4112   3575   2323   -492    460     63       C  
ATOM    160  C   GLY A 100     -11.988   6.729 -15.247  1.00 27.56           C  
ANISOU  160  C   GLY A 100     4150   3763   2559   -472    520      9       C  
ATOM    161  O   GLY A 100     -12.785   5.838 -15.541  1.00 24.41           O  
ANISOU  161  O   GLY A 100     3723   3366   2186   -455    473    -28       O  
ATOM    162  N   VAL A 101     -11.191   6.648 -14.188  1.00 26.57           N  
ANISOU  162  N   VAL A 101     3133   3197   3764    127    187   -611       N  
ATOM    163  CA  VAL A 101     -11.250   5.501 -13.281  1.00 24.62           C  
ANISOU  163  CA  VAL A 101     2944   2914   3495    129    164   -578       C  
ATOM    164  C   VAL A 101     -11.042   5.950 -11.844  1.00 24.60           C  
ANISOU  164  C   VAL A 101     2880   2965   3502    151     90   -554       C  
ATOM    165  O   VAL A 101     -10.587   7.064 -11.591  1.00 27.12           O  
ANISOU  165  O   VAL A 101     3108   3332   3863    181     62   -564       O  
ATOM    166  CB  VAL A 101     -10.172   4.439 -13.603  1.00 27.78           C  
ANISOU  166  CB  VAL A 101     3386   3214   3955    190    203   -560       C  
ATOM    167  CG1 VAL A 101     -10.422   3.802 -14.962  1.00 31.29           C  
ANISOU  167  CG1 VAL A 101     3903   3603   4382    165    276   -586       C  
ATOM    168  CG2 VAL A 101      -8.769   5.050 -13.523  1.00 30.96           C  
ANISOU  168  CG2 VAL A 101     3701   3610   4454    274    199   -556       C  
ATOM    169  N   ILE A 102     -11.388   5.076 -10.904  1.00 20.25           N  
ANISOU  169  N   ILE A 102     2380   2405   2909    132     58   -523       N  
ATOM    170  CA  ILE A 102     -11.028   5.277  -9.508  1.00 22.80           C  
ANISOU  170  CA  ILE A 102     2654   2767   3242    161    -10   -494       C  
ATOM    171  C   ILE A 102      -9.913   4.281  -9.189  1.00 20.23           C  
ANISOU  171  C   ILE A 102     2357   2356   2974    229     -9   -454       C  
ATOM    172  O   ILE A 102     -10.095   3.088  -9.349  1.00 24.02           O  
ANISOU  172  O   ILE A 102     2928   2766   3431    214     13   -434       O  
ATOM    173  CB  ILE A 102     -12.235   5.023  -8.585  1.00 23.27           C  
ANISOU  173  CB  ILE A 102     2748   2887   3207     87    -52   -483       C  
ATOM    174  CG1 ILE A 102     -13.409   5.924  -8.990  1.00 25.52           C  
ANISOU  174  CG1 ILE A 102     3008   3254   3434     21    -50   -528       C  
ATOM    175  CG2 ILE A 102     -11.855   5.264  -7.125  1.00 22.41           C  
ANISOU  175  CG2 ILE A 102     2586   2827   3103    115   -122   -454       C  
ATOM    176  CD1 ILE A 102     -14.715   5.578  -8.296  1.00 24.41           C  
ANISOU  176  CD1 ILE A 102     2908   3174   3192    -61    -77   -526       C  
ATOM    177  N   LYS A 103      -8.749   4.772  -8.771  1.00 20.11           N  
ANISOU  177  N   LYS A 103     2263   2341   3036    304    -34   -445       N  
ATOM    178  CA  LYS A 103      -7.653   3.884  -8.409  1.00 24.53           C  
ANISOU  178  CA  LYS A 103     2841   2825   3655    376    -40   -409       C  
ATOM    179  C   LYS A 103      -8.034   3.111  -7.153  1.00 20.79           C  
ANISOU  179  C   LYS A 103     2416   2355   3128    356    -97   -362       C  
ATOM    180  O   LYS A 103      -8.725   3.631  -6.279  1.00 20.72           O  
ANISOU  180  O   LYS A 103     2380   2430   3062    313   -145   -358       O  
ATOM    181  CB  LYS A 103      -6.363   4.675  -8.177  1.00 36.52           C  
ANISOU  181  CB  LYS A 103     4255   4357   5264    458    -60   -412       C  
ATOM    182  CG  LYS A 103      -5.788   5.315  -9.433  1.00 43.57           C  
ANISOU  182  CG  LYS A 103     5103   5235   6218    483      0   -451       C  
ATOM    183  CD  LYS A 103      -4.728   6.348  -9.083  1.00 48.28           C  
ANISOU  183  CD  LYS A 103     5584   5870   6891    542    -28   -457       C  
ATOM    184  CE  LYS A 103      -3.422   5.705  -8.614  1.00 54.42           C  
ANISOU  184  CE  LYS A 103     6364   6604   7710    608    -40   -413       C  
ATOM    185  NZ  LYS A 103      -2.630   5.114  -9.734  1.00 60.60           N  
ANISOU  185  NZ  LYS A 103     7187   7323   8515    632     28   -410       N  
ATOM    186  N   VAL A 104      -7.590   1.867  -7.064  1.00 21.24           N  
ANISOU  186  N   VAL A 104     2546   2321   3203    388    -91   -326       N  
ATOM    187  CA  VAL A 104      -7.947   1.035  -5.925  1.00 24.98           C  
ANISOU  187  CA  VAL A 104     3078   2788   3624    365   -143   -274       C  
ATOM    188  C   VAL A 104      -7.403   1.597  -4.601  1.00 29.42           C  
ANISOU  188  C   VAL A 104     3562   3414   4201    404   -218   -247       C  
ATOM    189  O   VAL A 104      -7.971   1.351  -3.536  1.00 27.10           O  
ANISOU  189  O   VAL A 104     3292   3163   3841    362   -269   -212       O  
ATOM    190  CB  VAL A 104      -7.534  -0.436  -6.167  1.00 27.34           C  
ANISOU  190  CB  VAL A 104     3476   2963   3948    395   -123   -241       C  
ATOM    191  CG1 VAL A 104      -7.193  -1.132  -4.865  1.00 43.80           C  
ANISOU  191  CG1 VAL A 104     5588   5029   6026    420   -191   -177       C  
ATOM    192  CG2 VAL A 104      -8.645  -1.157  -6.924  1.00 26.58           C  
ANISOU  192  CG2 VAL A 104     3483   2831   3785    313    -76   -253       C  
ATOM    193  N   ASP A 105      -6.325   2.375  -4.673  1.00 24.46           N  
ANISOU  193  N   ASP A 105     2839   2799   3657    478   -224   -264       N  
ATOM    194  CA  ASP A 105      -5.782   3.036  -3.487  1.00 28.09           C  
ANISOU  194  CA  ASP A 105     3214   3326   4134    516   -294   -248       C  
ATOM    195  C   ASP A 105      -6.825   3.903  -2.783  1.00 23.22           C  
ANISOU  195  C   ASP A 105     2561   2826   3438    444   -333   -263       C  
ATOM    196  O   ASP A 105      -6.778   4.077  -1.564  1.00 25.50           O  
ANISOU  196  O   ASP A 105     2817   3172   3701    447   -398   -238       O  
ATOM    197  CB  ASP A 105      -4.581   3.916  -3.854  1.00 40.18           C  
ANISOU  197  CB  ASP A 105     4639   4861   5765    594   -286   -277       C  
ATOM    198  CG  ASP A 105      -3.386   3.112  -4.321  1.00 53.60           C  
ANISOU  198  CG  ASP A 105     6356   6460   7551    678   -259   -263       C  
ATOM    199  OD1 ASP A 105      -3.419   1.865  -4.206  1.00 54.83           O  
ANISOU  199  OD1 ASP A 105     6603   6539   7693    685   -259   -225       O  
ATOM    200  OD2 ASP A 105      -2.407   3.736  -4.791  1.00 57.28           O  
ANISOU  200  OD2 ASP A 105     6740   6923   8099    738   -240   -290       O  
ATOM    201  N   VAL A 106      -7.735   4.487  -3.560  1.00 24.26           N  
ANISOU  201  N   VAL A 106     2692   2994   3532    383   -294   -308       N  
ATOM    202  CA  VAL A 106      -8.774   5.356  -3.009  1.00 21.62           C  
ANISOU  202  CA  VAL A 106     2319   2770   3125    316   -327   -333       C  
ATOM    203  C   VAL A 106      -9.747   4.518  -2.197  1.00 22.32           C  
ANISOU  203  C   VAL A 106     2484   2880   3114    248   -354   -298       C  
ATOM    204  O   VAL A 106     -10.122   4.873  -1.082  1.00 19.04           O  
ANISOU  204  O   VAL A 106     2036   2551   2649    223   -409   -290       O  
ATOM    205  CB  VAL A 106      -9.541   6.102  -4.129  1.00 28.17           C  
ANISOU  205  CB  VAL A 106     3137   3626   3940    269   -278   -388       C  
ATOM    206  CG1 VAL A 106     -10.740   6.847  -3.563  1.00 26.29           C  
ANISOU  206  CG1 VAL A 106     2870   3497   3620    198   -313   -416       C  
ATOM    207  CG2 VAL A 106      -8.616   7.051  -4.874  1.00 31.78           C  
ANISOU  207  CG2 VAL A 106     3513   4073   4490    328   -256   -420       C  
ATOM    208  N   LEU A 107     -10.152   3.389  -2.766  1.00 18.87           N  
ANISOU  208  N   LEU A 107     2154   2368   2650    215   -312   -278       N  
ATOM    209  CA  LEU A 107     -10.991   2.435  -2.056  1.00 17.96           C  
ANISOU  209  CA  LEU A 107     2123   2255   2445    148   -333   -237       C  
ATOM    210  C   LEU A 107     -10.325   1.908  -0.794  1.00 16.54           C  
ANISOU  210  C   LEU A 107     1947   2068   2268    187   -396   -176       C  
ATOM    211  O   LEU A 107     -10.964   1.795   0.249  1.00 19.76           O  
ANISOU  211  O   LEU A 107     2366   2543   2597    135   -441   -150       O  
ATOM    212  CB  LEU A 107     -11.305   1.256  -2.971  1.00 25.31           C  
ANISOU  212  CB  LEU A 107     3168   3085   3366    120   -277   -224       C  
ATOM    213  CG  LEU A 107     -12.776   0.941  -3.194  1.00 34.12           C  
ANISOU  213  CG  LEU A 107     4349   4234   4381     11   -255   -238       C  
ATOM    214  CD1 LEU A 107     -13.512   2.184  -3.669  1.00 31.26           C  
ANISOU  214  CD1 LEU A 107     3916   3967   3996    -26   -240   -303       C  
ATOM    215  CD2 LEU A 107     -12.876  -0.196  -4.211  1.00 25.96           C  
ANISOU  215  CD2 LEU A 107     3421   3086   3357     -3   -197   -231       C  
ATOM    216  N   ARG A 108      -9.055   1.526  -0.906  1.00 19.06           N  
ANISOU  216  N   ARG A 108     2261   2304   2677    278   -398   -151       N  
ATOM    217  CA  ARG A 108      -8.299   1.038   0.247  1.00 18.09           C  
ANISOU  217  CA  ARG A 108     2137   2168   2567    327   -461    -92       C  
ATOM    218  C   ARG A 108      -8.269   2.106   1.333  1.00 22.24           C  
ANISOU  218  C   ARG A 108     2563   2815   3071    329   -523   -102       C  
ATOM    219  O   ARG A 108      -8.485   1.816   2.512  1.00 20.65           O  
ANISOU  219  O   ARG A 108     2376   2659   2810    305   -579    -59       O  
ATOM    220  CB  ARG A 108      -6.868   0.680  -0.156  1.00 26.35           C  
ANISOU  220  CB  ARG A 108     3170   3117   3726    435   -452    -79       C  
ATOM    221  CG  ARG A 108      -6.026   0.153   0.992  1.00 28.75           C  
ANISOU  221  CG  ARG A 108     3473   3401   4050    494   -521    -18       C  
ATOM    222  CD  ARG A 108      -4.603  -0.140   0.532  1.00 35.43           C  
ANISOU  222  CD  ARG A 108     4295   4155   5012    605   -510    -15       C  
ATOM    223  NE  ARG A 108      -4.588  -0.976  -0.670  1.00 37.85           N  
ANISOU  223  NE  ARG A 108     4680   4350   5351    611   -442    -26       N  
ATOM    224  CZ  ARG A 108      -4.762  -2.294  -0.666  1.00 42.05           C  
ANISOU  224  CZ  ARG A 108     5325   4787   5864    601   -441     19       C  
ATOM    225  NH1 ARG A 108      -4.963  -2.936   0.478  1.00 47.62           N  
ANISOU  225  NH1 ARG A 108     6082   5495   6517    582   -504     85       N  
ATOM    226  NH2 ARG A 108      -4.739  -2.972  -1.807  1.00 41.33           N  
ANISOU  226  NH2 ARG A 108     5298   4599   5807    609   -377     -2       N  
ATOM    227  N   TRP A 109      -8.005   3.344   0.928  1.00 19.96           N  
ANISOU  227  N   TRP A 109     2175   2579   2830    355   -512   -160       N  
ATOM    228  CA  TRP A 109      -7.959   4.454   1.873  1.00 19.88           C  
ANISOU  228  CA  TRP A 109     2064   2682   2808    360   -568   -180       C  
ATOM    229  C   TRP A 109      -9.291   4.599   2.608  1.00 14.70           C  
ANISOU  229  C   TRP A 109     1424   2126   2034    265   -594   -185       C  
ATOM    230  O   TRP A 109      -9.336   4.717   3.834  1.00 19.83           O  
ANISOU  230  O   TRP A 109     2047   2849   2639    256   -655   -163       O  
ATOM    231  CB  TRP A 109      -7.643   5.767   1.156  1.00 20.67           C  
ANISOU  231  CB  TRP A 109     2065   2815   2974    388   -546   -246       C  
ATOM    232  CG  TRP A 109      -7.734   6.921   2.094  1.00 20.83           C  
ANISOU  232  CG  TRP A 109     1986   2951   2977    385   -603   -274       C  
ATOM    233  CD1 TRP A 109      -8.758   7.796   2.238  1.00 23.50           C  
ANISOU  233  CD1 TRP A 109     2288   3385   3257    323   -612   -322       C  
ATOM    234  CD2 TRP A 109      -6.749   7.263   3.081  1.00 19.89           C  
ANISOU  234  CD2 TRP A 109     1796   2863   2900    448   -664   -258       C  
ATOM    235  NE1 TRP A 109      -8.480   8.699   3.243  1.00 23.68           N  
ANISOU  235  NE1 TRP A 109     2286   3454   3258    309   -613   -301       N  
ATOM    236  CE2 TRP A 109      -7.249   8.389   3.774  1.00 23.88           C  
ANISOU  236  CE2 TRP A 109     2291   3445   3336    376   -640   -262       C  
ATOM    237  CE3 TRP A 109      -5.511   6.751   3.436  1.00 22.29           C  
ANISOU  237  CE3 TRP A 109     2095   3108   3267    525   -685   -214       C  
ATOM    238  CZ2 TRP A 109      -6.536   9.006   4.798  1.00 23.51           C  
ANISOU  238  CZ2 TRP A 109     2224   3420   3287    380   -643   -228       C  
ATOM    239  CZ3 TRP A 109      -4.799   7.356   4.453  1.00 27.12           C  
ANISOU  239  CZ3 TRP A 109     2681   3759   3864    522   -687   -183       C  
ATOM    240  CH2 TRP A 109      -5.316   8.473   5.119  1.00 25.00           C  
ANISOU  240  CH2 TRP A 109     2398   3569   3532    450   -669   -192       C  
ATOM    241  N   ILE A 110     -10.368   4.633   1.839  1.00 15.14           N  
ANISOU  241  N   ILE A 110     1519   2192   2042    194   -546   -219       N  
ATOM    242  CA  ILE A 110     -11.715   4.723   2.384  1.00 24.59           C  
ANISOU  242  CA  ILE A 110     2734   3482   3127     98   -561   -231       C  
ATOM    243  C   ILE A 110     -12.002   3.629   3.414  1.00 21.73           C  
ANISOU  243  C   ILE A 110     2448   3120   2688     58   -596   -163       C  
ATOM    244  O   ILE A 110     -12.445   3.902   4.533  1.00 23.70           O  
ANISOU  244  O   ILE A 110     2667   3470   2866     21   -645   -157       O  
ATOM    245  CB  ILE A 110     -12.748   4.668   1.244  1.00 23.62           C  
ANISOU  245  CB  ILE A 110     2658   3346   2971     33   -498   -270       C  
ATOM    246  CG1 ILE A 110     -12.662   5.953   0.403  1.00 20.99           C  
ANISOU  246  CG1 ILE A 110     2239   3041   2694     58   -475   -339       C  
ATOM    247  CG2 ILE A 110     -14.144   4.466   1.797  1.00 27.28           C  
ANISOU  247  CG2 ILE A 110     3157   3893   3315    -70   -508   -274       C  
ATOM    248  CD1 ILE A 110     -13.531   5.912  -0.848  1.00 28.86           C  
ANISOU  248  CD1 ILE A 110     3281   4014   3669      6   -413   -376       C  
ATOM    249  N   LEU A 111     -11.725   2.386   3.041  1.00 19.63           N  
ANISOU  249  N   LEU A 111     2282   2740   2437     66   -572   -111       N  
ATOM    250  CA  LEU A 111     -12.017   1.246   3.918  1.00 18.57           C  
ANISOU  250  CA  LEU A 111     2236   2589   2232     23   -603    -39       C  
ATOM    251  C   LEU A 111     -11.152   1.222   5.171  1.00 22.88           C  
ANISOU  251  C   LEU A 111     2746   3160   2788     77   -675     10       C  
ATOM    252  O   LEU A 111     -11.619   0.878   6.272  1.00 24.74           O  
ANISOU  252  O   LEU A 111     3007   3456   2937     25   -720     52       O  
ATOM    253  CB  LEU A 111     -11.870  -0.060   3.131  1.00 19.10           C  
ANISOU  253  CB  LEU A 111     2419   2515   2324     25   -560      0       C  
ATOM    254  CG  LEU A 111     -12.835  -0.173   1.955  1.00 24.02           C  
ANISOU  254  CG  LEU A 111     3089   3116   2920    -40   -491    -44       C  
ATOM    255  CD1 LEU A 111     -12.590  -1.464   1.187  1.00 18.84           C  
ANISOU  255  CD1 LEU A 111     2545   2315   2297    -31   -451    -10       C  
ATOM    256  CD2 LEU A 111     -14.276  -0.104   2.455  1.00 28.75           C  
ANISOU  256  CD2 LEU A 111     3708   3819   3398   -156   -497    -55       C  
ATOM    257  N   LYS A 112      -9.883   1.584   5.004  1.00 22.14           N  
ANISOU  257  N   LYS A 112     2592   3023   2799    180   -686      5       N  
ATOM    258  CA  LYS A 112      -8.953   1.605   6.117  1.00 20.71           C  
ANISOU  258  CA  LYS A 112     2368   2862   2639    242   -756     47       C  
ATOM    259  C   LYS A 112      -9.298   2.718   7.101  1.00 26.65           C  
ANISOU  259  C   LYS A 112     3024   3763   3339    217   -805     14       C  
ATOM    260  O   LYS A 112      -9.321   2.502   8.316  1.00 28.60           O  
ANISOU  260  O   LYS A 112     3273   4068   3525    201   -864     57       O  
ATOM    261  CB  LYS A 112      -7.516   1.765   5.611  1.00 25.20           C  
ANISOU  261  CB  LYS A 112     2888   3351   3337    358   -752     42       C  
ATOM    262  CG  LYS A 112      -6.458   1.755   6.705  1.00 34.64           C  
ANISOU  262  CG  LYS A 112     4037   4561   4564    431   -825     85       C  
ATOM    263  CD  LYS A 112      -6.669   0.598   7.670  1.00 38.97           C  
ANISOU  263  CD  LYS A 112     4679   5088   5040    400   -872    170       C  
ATOM    264  CE  LYS A 112      -5.435   0.378   8.533  1.00 46.58           C  
ANISOU  264  CE  LYS A 112     5612   6033   6055    490   -940    219       C  
ATOM    265  NZ  LYS A 112      -4.819   1.663   8.975  1.00 44.52           N  
ANISOU  265  NZ  LYS A 112     5214   5867   5833    539   -975    171       N  
ATOM    266  N   SER A 113      -9.538   3.917   6.587  1.00 26.47           N  
ANISOU  266  N   SER A 113     2916   3801   3341    215   -782    -64       N  
ATOM    267  CA  SER A 113      -9.768   5.051   7.479  1.00 30.50           C  
ANISOU  267  CA  SER A 113     3326   4448   3816    202   -830   -105       C  
ATOM    268  C   SER A 113     -11.201   5.186   8.014  1.00 33.42           C  
ANISOU  268  C   SER A 113     3710   4927   4061     96   -836   -125       C  
ATOM    269  O   SER A 113     -11.399   5.489   9.190  1.00 35.51           O  
ANISOU  269  O   SER A 113     3936   5295   4262     74   -891   -121       O  
ATOM    270  CB  SER A 113      -9.294   6.347   6.825  1.00 24.38           C  
ANISOU  270  CB  SER A 113     2445   3690   3128    254   -815   -178       C  
ATOM    271  OG  SER A 113      -9.890   6.511   5.558  1.00 32.60           O  
ANISOU  271  OG  SER A 113     3510   4694   4182    223   -748   -220       O  
ATOM    272  N   LEU A 114     -12.194   4.995   7.150  1.00 29.43           N  
ANISOU  272  N   LEU A 114     3256   4406   3519     30   -779   -151       N  
ATOM    273  CA  LEU A 114     -13.593   5.155   7.552  1.00 32.03           C  
ANISOU  273  CA  LEU A 114     3594   4843   3734    -72   -779   -178       C  
ATOM    274  C   LEU A 114     -14.268   3.841   7.957  1.00 35.59           C  
ANISOU  274  C   LEU A 114     4159   5273   4091   -149   -775   -111       C  
ATOM    275  O   LEU A 114     -15.341   3.843   8.562  1.00 35.77           O  
ANISOU  275  O   LEU A 114     4189   5395   4007   -237   -785   -120       O  
ATOM    276  CB  LEU A 114     -14.395   5.852   6.441  1.00 34.02           C  
ANISOU  276  CB  LEU A 114     3828   5102   3998   -104   -722   -251       C  
ATOM    277  CG  LEU A 114     -13.920   7.235   5.995  1.00 38.65           C  
ANISOU  277  CG  LEU A 114     4358   5634   4692    -47   -674   -284       C  
ATOM    278  CD1 LEU A 114     -14.618   7.666   4.708  1.00 38.67           C  
ANISOU  278  CD1 LEU A 114     4375   5606   4711    -71   -609   -329       C  
ATOM    279  CD2 LEU A 114     -14.145   8.261   7.104  1.00 41.38           C  
ANISOU  279  CD2 LEU A 114     4692   5989   5040    -55   -659   -273       C  
ATOM    280  N   GLY A 115     -13.617   2.719   7.656  1.00 37.42           N  
ANISOU  280  N   GLY A 115     4478   5376   4362   -117   -763    -43       N  
ATOM    281  CA  GLY A 115     -14.180   1.415   7.955  1.00 45.90           C  
ANISOU  281  CA  GLY A 115     5671   6410   5359   -188   -760     26       C  
ATOM    282  C   GLY A 115     -14.076   1.140   9.440  1.00 57.22           C  
ANISOU  282  C   GLY A 115     7105   7913   6722   -206   -828     84       C  
ATOM    283  O   GLY A 115     -13.226   1.715  10.118  1.00 61.68           O  
ANISOU  283  O   GLY A 115     7595   8517   7325   -137   -878     85       O  
ATOM    284  N   ASP A 116     -14.941   0.275   9.956  1.00 63.23           N  
ANISOU  284  N   ASP A 116     7951   8695   7377   -301   -831    132       N  
ATOM    285  CA  ASP A 116     -14.879  -0.072  11.367  1.00 70.16           C  
ANISOU  285  CA  ASP A 116     8841   9640   8178   -327   -895    196       C  
ATOM    286  C   ASP A 116     -14.226  -1.433  11.570  1.00 67.39           C  
ANISOU  286  C   ASP A 116     8601   9159   7844   -304   -916    300       C  
ATOM    287  O   ASP A 116     -14.825  -2.471  11.285  1.00 65.96           O  
ANISOU  287  O   ASP A 116     8530   8911   7619   -373   -888    344       O  
ATOM    288  CB  ASP A 116     -16.277  -0.045  11.996  1.00 77.96           C  
ANISOU  288  CB  ASP A 116     9837  10757   9025   -454   -893    183       C  
ATOM    289  CG  ASP A 116     -16.649   1.325  12.534  1.00 83.47           C  
ANISOU  289  CG  ASP A 116    10413  11591   9711   -446   -895     95       C  
ATOM    290  OD1 ASP A 116     -16.138   2.334  12.006  1.00 84.91           O  
ANISOU  290  OD1 ASP A 116    10512  11759   9990   -366   -881     28       O  
ATOM    291  OD2 ASP A 116     -17.451   1.392  13.490  1.00 85.81           O  
ANISOU  291  OD2 ASP A 116    10710  11940   9952   -490   -869     87       O  
ATOM    292  N   GLU A 117     -12.998  -1.411  12.079  1.00 66.90           N  
ANISOU  292  N   GLU A 117     8509   9063   7847   -207   -968    338       N  
ATOM    293  CA  GLU A 117     -12.254  -2.629  12.388  1.00 66.22           C  
ANISOU  293  CA  GLU A 117     8518   8857   7784   -170  -1001    437       C  
ATOM    294  C   GLU A 117     -12.337  -3.709  11.302  1.00 60.23           C  
ANISOU  294  C   GLU A 117     7874   7941   7069   -177   -947    463       C  
ATOM    295  O   GLU A 117     -12.566  -4.883  11.596  1.00 61.07           O  
ANISOU  295  O   GLU A 117     8095   7979   7131   -224   -960    543       O  
ATOM    296  CB  GLU A 117     -12.653  -3.199  13.754  1.00 73.74           C  
ANISOU  296  CB  GLU A 117     9520   9880   8618   -242  -1059    516       C  
ATOM    297  CG  GLU A 117     -11.834  -4.431  14.154  1.00 80.55           C  
ANISOU  297  CG  GLU A 117    10480  10617   9506   -198  -1104    625       C  
ATOM    298  CD  GLU A 117     -11.732  -4.629  15.654  1.00 83.01           C  
ANISOU  298  CD  GLU A 117    10797  11012   9730   -223  -1184    698       C  
ATOM    299  OE1 GLU A 117     -12.632  -4.163  16.387  1.00 84.91           O  
ANISOU  299  OE1 GLU A 117    11004  11402   9856   -314  -1192    679       O  
ATOM    300  OE2 GLU A 117     -10.741  -5.247  16.100  1.00 82.07           O  
ANISOU  300  OE2 GLU A 117    10714  10813   9655   -150  -1238    773       O  
ATOM    301  N   LEU A 118     -12.166  -3.313  10.046  1.00 49.39           N  
ANISOU  301  N   LEU A 118     6472   6510   5782   -134   -888    396       N  
ATOM    302  CA  LEU A 118     -12.052  -4.290   8.968  1.00 38.64           C  
ANISOU  302  CA  LEU A 118     5209   4994   4478   -122   -839    414       C  
ATOM    303  C   LEU A 118     -10.657  -4.908   9.003  1.00 35.36           C  
ANISOU  303  C   LEU A 118     4817   4454   4163     -6   -873    468       C  
ATOM    304  O   LEU A 118      -9.686  -4.205   9.260  1.00 40.17           O  
ANISOU  304  O   LEU A 118     5333   5090   4840     86   -905    450       O  
ATOM    305  CB  LEU A 118     -12.289  -3.619   7.610  1.00 28.65           C  
ANISOU  305  CB  LEU A 118     3900   3717   3269   -111   -766    322       C  
ATOM    306  CG  LEU A 118     -13.695  -3.078   7.339  1.00 28.46           C  
ANISOU  306  CG  LEU A 118     3860   3797   3157   -220   -725    262       C  
ATOM    307  CD1 LEU A 118     -13.740  -2.236   6.070  1.00 22.04           C  
ANISOU  307  CD1 LEU A 118     2986   2979   2410   -191   -665    173       C  
ATOM    308  CD2 LEU A 118     -14.683  -4.235   7.256  1.00 36.32           C  
ANISOU  308  CD2 LEU A 118     4982   4748   4070   -326   -702    306       C  
ATOM    309  N   THR A 119     -10.548  -6.213   8.756  1.00 38.02           N  
ANISOU  309  N   THR A 119     5276   4656   4514     -9   -868    531       N  
ATOM    310  CA  THR A 119      -9.230  -6.840   8.594  1.00 37.49           C  
ANISOU  310  CA  THR A 119     5234   4456   4556    109   -893    571       C  
ATOM    311  C   THR A 119      -8.631  -6.478   7.236  1.00 33.63           C  
ANISOU  311  C   THR A 119     4701   3895   4182    188   -830    498       C  
ATOM    312  O   THR A 119      -9.339  -6.010   6.344  1.00 29.94           O  
ANISOU  312  O   THR A 119     4216   3455   3703    139   -766    430       O  
ATOM    313  CB  THR A 119      -9.261  -8.385   8.753  1.00 34.27           C  
ANISOU  313  CB  THR A 119     4974   3914   4134     87   -912    662       C  
ATOM    314  OG1 THR A 119      -9.929  -8.986   7.635  1.00 32.00           O  
ANISOU  314  OG1 THR A 119     4769   3541   3850     35   -841    636       O  
ATOM    315  CG2 THR A 119      -9.965  -8.780  10.041  1.00 41.43           C  
ANISOU  315  CG2 THR A 119     5933   4894   4915     -8   -968    739       C  
ATOM    316  N   GLU A 120      -7.326  -6.660   7.078  1.00 30.34           N  
ANISOU  316  N   GLU A 120     4260   3393   3874    308   -850    509       N  
ATOM    317  CA  GLU A 120      -6.720  -6.386   5.781  1.00 32.10           C  
ANISOU  317  CA  GLU A 120     4445   3547   4205    381   -788    442       C  
ATOM    318  C   GLU A 120      -7.238  -7.328   4.691  1.00 28.62           C  
ANISOU  318  C   GLU A 120     4114   2989   3771    343   -724    434       C  
ATOM    319  O   GLU A 120      -7.379  -6.923   3.535  1.00 29.81           O  
ANISOU  319  O   GLU A 120     4240   3128   3960    344   -654    363       O  
ATOM    320  CB  GLU A 120      -5.187  -6.389   5.852  1.00 41.29           C  
ANISOU  320  CB  GLU A 120     5554   4649   5485    520   -822    452       C  
ATOM    321  CG  GLU A 120      -4.552  -7.734   6.112  1.00 55.45           C  
ANISOU  321  CG  GLU A 120     7446   6306   7317    574   -862    529       C  
ATOM    322  CD  GLU A 120      -3.043  -7.632   6.295  1.00 62.04           C  
ANISOU  322  CD  GLU A 120     8211   7100   8262    713   -903    534       C  
ATOM    323  OE1 GLU A 120      -2.510  -6.501   6.190  1.00 56.49           O  
ANISOU  323  OE1 GLU A 120     7381   6477   7604    760   -896    477       O  
ATOM    324  OE2 GLU A 120      -2.396  -8.678   6.546  1.00 67.00           O  
ANISOU  324  OE2 GLU A 120     8908   7616   8933    773   -943    595       O  
ATOM    325  N   ASP A 121      -7.531  -8.577   5.052  1.00 29.93           N  
ANISOU  325  N   ASP A 121     4405   3069   3899    305   -747    507       N  
ATOM    326  CA  ASP A 121      -8.067  -9.524   4.076  1.00 26.92           C  
ANISOU  326  CA  ASP A 121     4134   2574   3520    261   -690    501       C  
ATOM    327  C   ASP A 121      -9.497  -9.166   3.650  1.00 26.84           C  
ANISOU  327  C   ASP A 121     4138   2644   3416    133   -636    456       C  
ATOM    328  O   ASP A 121      -9.859  -9.332   2.488  1.00 28.01           O  
ANISOU  328  O   ASP A 121     4319   2739   3585    113   -568    405       O  
ATOM    329  CB  ASP A 121      -7.976 -10.972   4.594  1.00 29.97           C  
ANISOU  329  CB  ASP A 121     4653   2838   3895    254   -735    594       C  
ATOM    330  CG  ASP A 121      -6.581 -11.565   4.431  1.00 36.20           C  
ANISOU  330  CG  ASP A 121     5451   3498   4806    391   -761    616       C  
ATOM    331  OD1 ASP A 121      -5.677 -10.842   3.949  1.00 38.21           O  
ANISOU  331  OD1 ASP A 121     5604   3766   5149    488   -743    559       O  
ATOM    332  OD2 ASP A 121      -6.387 -12.753   4.789  1.00 42.32           O  
ANISOU  332  OD2 ASP A 121     6334   4158   5588    402   -801    689       O  
ATOM    333  N   GLU A 122     -10.302  -8.678   4.588  1.00 26.37           N  
ANISOU  333  N   GLU A 122     4053   2715   3253     49   -668    473       N  
ATOM    334  CA  GLU A 122     -11.649  -8.199   4.275  1.00 28.66           C  
ANISOU  334  CA  GLU A 122     4336   3100   3452    -67   -622    424       C  
ATOM    335  C   GLU A 122     -11.602  -6.963   3.390  1.00 25.35           C  
ANISOU  335  C   GLU A 122     3807   2747   3077    -36   -573    328       C  
ATOM    336  O   GLU A 122     -12.400  -6.823   2.464  1.00 24.10           O  
ANISOU  336  O   GLU A 122     3664   2597   2897    -94   -512    273       O  
ATOM    337  CB  GLU A 122     -12.421  -7.868   5.551  1.00 27.60           C  
ANISOU  337  CB  GLU A 122     4182   3104   3200   -154   -671    458       C  
ATOM    338  CG  GLU A 122     -12.740  -9.088   6.402  1.00 34.12           C  
ANISOU  338  CG  GLU A 122     5127   3879   3958   -216   -715    556       C  
ATOM    339  CD  GLU A 122     -13.414  -8.722   7.711  1.00 39.13           C  
ANISOU  339  CD  GLU A 122     5734   4659   4475   -298   -764    589       C  
ATOM    340  OE1 GLU A 122     -14.111  -9.588   8.284  1.00 46.29           O  
ANISOU  340  OE1 GLU A 122     6738   5556   5295   -392   -781    655       O  
ATOM    341  OE2 GLU A 122     -13.244  -7.570   8.164  1.00 40.32           O  
ANISOU  341  OE2 GLU A 122     5767   4935   4620   -271   -784    548       O  
ATOM    342  N   ILE A 123     -10.678  -6.057   3.688  1.00 26.07           N  
ANISOU  342  N   ILE A 123     3788   2888   3228     53   -601    308       N  
ATOM    343  CA  ILE A 123     -10.468  -4.905   2.818  1.00 26.68           C  
ANISOU  343  CA  ILE A 123     3764   3012   3362     93   -557    222       C  
ATOM    344  C   ILE A 123     -10.089  -5.368   1.409  1.00 28.20           C  
ANISOU  344  C   ILE A 123     3997   3081   3635    136   -490    188       C  
ATOM    345  O   ILE A 123     -10.664  -4.906   0.427  1.00 21.75           O  
ANISOU  345  O   ILE A 123     3166   2286   2813    100   -431    125       O  
ATOM    346  CB  ILE A 123      -9.414  -3.936   3.382  1.00 23.46           C  
ANISOU  346  CB  ILE A 123     3235   2664   3015    185   -601    211       C  
ATOM    347  CG1 ILE A 123      -9.937  -3.270   4.663  1.00 23.20           C  
ANISOU  347  CG1 ILE A 123     3146   2774   2894    133   -659    224       C  
ATOM    348  CG2 ILE A 123      -9.063  -2.880   2.344  1.00 21.52           C  
ANISOU  348  CG2 ILE A 123     2897   2439   2843    232   -552    129       C  
ATOM    349  CD1 ILE A 123      -8.912  -2.404   5.370  1.00 26.96           C  
ANISOU  349  CD1 ILE A 123     3511   3310   3424    219   -712    219       C  
ATOM    350  N   GLU A 124      -9.145  -6.300   1.301  1.00 25.30           N  
ANISOU  350  N   GLU A 124     3685   2587   3341    213   -501    228       N  
ATOM    351  CA  GLU A 124      -8.747  -6.802  -0.017  1.00 26.21           C  
ANISOU  351  CA  GLU A 124     3841   2585   3534    257   -437    193       C  
ATOM    352  C   GLU A 124      -9.925  -7.463  -0.730  1.00 24.00           C  
ANISOU  352  C   GLU A 124     3662   2268   3189    156   -385    179       C  
ATOM    353  O   GLU A 124     -10.039  -7.386  -1.946  1.00 25.73           O  
ANISOU  353  O   GLU A 124     3885   2451   3439    157   -318    121       O  
ATOM    354  CB  GLU A 124      -7.570  -7.788   0.080  1.00 27.39           C  
ANISOU  354  CB  GLU A 124     4036   2600   3769    358   -464    239       C  
ATOM    355  CG  GLU A 124      -6.250  -7.152   0.506  1.00 34.86           C  
ANISOU  355  CG  GLU A 124     4876   3569   4801    473   -503    239       C  
ATOM    356  CD  GLU A 124      -5.573  -6.373  -0.608  1.00 46.28           C  
ANISOU  356  CD  GLU A 124     6235   5016   6334    541   -445    162       C  
ATOM    357  OE1 GLU A 124      -5.940  -6.562  -1.789  1.00 49.84           O  
ANISOU  357  OE1 GLU A 124     6723   5420   6794    516   -374    115       O  
ATOM    358  OE2 GLU A 124      -4.665  -5.571  -0.299  1.00 52.19           O  
ANISOU  358  OE2 GLU A 124     6877   5813   7141    616   -471    148       O  
ATOM    359  N   ASN A 125     -10.792  -8.118   0.033  1.00 25.45           N  
ANISOU  359  N   ASN A 125     3925   2463   3281     66   -415    233       N  
ATOM    360  CA  ASN A 125     -11.955  -8.788  -0.539  1.00 28.48           C  
ANISOU  360  CA  ASN A 125     4407   2817   3598    -40   -371    225       C  
ATOM    361  C   ASN A 125     -12.965  -7.790  -1.094  1.00 28.51           C  
ANISOU  361  C   ASN A 125     4352   2937   3545   -114   -326    152       C  
ATOM    362  O   ASN A 125     -13.537  -7.997  -2.167  1.00 28.12           O  
ANISOU  362  O   ASN A 125     4343   2853   3489   -156   -265    107       O  
ATOM    363  CB  ASN A 125     -12.622  -9.684   0.506  1.00 33.98           C  
ANISOU  363  CB  ASN A 125     5196   3507   4207   -124   -418    304       C  
ATOM    364  CG  ASN A 125     -13.673 -10.596  -0.097  1.00 36.94           C  
ANISOU  364  CG  ASN A 125     5687   3822   4526   -226   -374    303       C  
ATOM    365  OD1 ASN A 125     -13.486 -11.148  -1.185  1.00 39.93           O  
ANISOU  365  OD1 ASN A 125     6118   4093   4962   -201   -325    272       O  
ATOM    366  ND2 ASN A 125     -14.791 -10.756   0.607  1.00 38.24           N  
ANISOU  366  ND2 ASN A 125     5889   4061   4578   -345   -392    333       N  
ATOM    367  N   MET A 126     -13.173  -6.699  -0.361  1.00 22.90           N  
ANISOU  367  N   MET A 126     3543   2363   2794   -128   -358    140       N  
ATOM    368  CA  MET A 126     -14.109  -5.664  -0.788  1.00 22.82           C  
ANISOU  368  CA  MET A 126     3468   2470   2734   -191   -325     71       C  
ATOM    369  C   MET A 126     -13.570  -4.924  -2.009  1.00 24.89           C  
ANISOU  369  C   MET A 126     3665   2714   3078   -123   -274      0       C  
ATOM    370  O   MET A 126     -14.324  -4.556  -2.912  1.00 22.95           O  
ANISOU  370  O   MET A 126     3416   2498   2807   -174   -223    -56       O  
ATOM    371  CB  MET A 126     -14.410  -4.708   0.366  1.00 20.21           C  
ANISOU  371  CB  MET A 126     3049   2286   2343   -215   -378     73       C  
ATOM    372  CG  MET A 126     -15.149  -5.381   1.523  1.00 28.99           C  
ANISOU  372  CG  MET A 126     4224   3437   3354   -303   -422    137       C  
ATOM    373  SD  MET A 126     -15.067  -4.527   3.112  1.00 31.56           S  
ANISOU  373  SD  MET A 126     4455   3910   3626   -303   -499    160       S  
ATOM    374  CE  MET A 126     -16.278  -3.227   2.883  1.00 30.20           C  
ANISOU  374  CE  MET A 126     4193   3898   3385   -378   -474     71       C  
ATOM    375  N   ILE A 127     -12.256  -4.724  -2.043  1.00 21.30           N  
ANISOU  375  N   ILE A 127     3160   2212   2721    -11   -286      6       N  
ATOM    376  CA  ILE A 127     -11.607  -4.200  -3.238  1.00 20.24           C  
ANISOU  376  CA  ILE A 127     2976   2043   2672     56   -234    -53       C  
ATOM    377  C   ILE A 127     -11.830  -5.125  -4.441  1.00 21.89           C  
ANISOU  377  C   ILE A 127     3280   2142   2895     38   -170    -72       C  
ATOM    378  O   ILE A 127     -12.234  -4.686  -5.519  1.00 25.91           O  
ANISOU  378  O   ILE A 127     3775   2667   3404     15   -113   -131       O  
ATOM    379  CB  ILE A 127     -10.099  -3.987  -3.012  1.00 27.50           C  
ANISOU  379  CB  ILE A 127     3830   2923   3694    179   -260    -39       C  
ATOM    380  CG1 ILE A 127      -9.868  -2.823  -2.042  1.00 24.12           C  
ANISOU  380  CG1 ILE A 127     3289   2615   3259    198   -314    -41       C  
ATOM    381  CG2 ILE A 127      -9.407  -3.698  -4.330  1.00 28.16           C  
ANISOU  381  CG2 ILE A 127     3881   2954   3864    243   -198    -94       C  
ATOM    382  CD1 ILE A 127      -8.410  -2.613  -1.697  1.00 27.97           C  
ANISOU  382  CD1 ILE A 127     3710   3074   3844    314   -347    -25       C  
ATOM    383  N   ALA A 128     -11.585  -6.420  -4.249  1.00 21.19           N  
ANISOU  383  N   ALA A 128     3291   1941   2817     47   -180    -21       N  
ATOM    384  CA  ALA A 128     -11.736  -7.376  -5.334  1.00 24.01           C  
ANISOU  384  CA  ALA A 128     3744   2187   3194     35   -123    -40       C  
ATOM    385  C   ALA A 128     -13.178  -7.450  -5.836  1.00 25.18           C  
ANISOU  385  C   ALA A 128     3943   2376   3250    -86    -85    -70       C  
ATOM    386  O   ALA A 128     -13.421  -7.678  -7.024  1.00 28.23           O  
ANISOU  386  O   ALA A 128     4365   2715   3647   -101    -24   -118       O  
ATOM    387  CB  ALA A 128     -11.257  -8.753  -4.883  1.00 30.11           C  
ANISOU  387  CB  ALA A 128     4618   2831   3993     64   -153     25       C  
ATOM    388  N   GLU A 129     -14.124  -7.263  -4.924  1.00 29.08           N  
ANISOU  388  N   GLU A 129     4438   2961   3650   -172   -122    -44       N  
ATOM    389  CA  GLU A 129     -15.550  -7.270  -5.246  1.00 36.91           C  
ANISOU  389  CA  GLU A 129     5467   4011   4547   -292    -93    -73       C  
ATOM    390  C   GLU A 129     -15.902  -6.104  -6.166  1.00 32.17           C  
ANISOU  390  C   GLU A 129     4784   3493   3947   -298    -50   -151       C  
ATOM    391  O   GLU A 129     -16.828  -6.182  -6.976  1.00 32.82           O  
ANISOU  391  O   GLU A 129     4900   3586   3982   -370     -6   -192       O  
ATOM    392  CB  GLU A 129     -16.373  -7.186  -3.952  1.00 44.90           C  
ANISOU  392  CB  GLU A 129     6477   5121   5461   -375   -147    -30       C  
ATOM    393  CG  GLU A 129     -17.795  -6.656  -4.118  1.00 49.91           C  
ANISOU  393  CG  GLU A 129     7094   5869   5999   -486   -126    -75       C  
ATOM    394  CD  GLU A 129     -18.794  -7.733  -4.507  1.00 52.92           C  
ANISOU  394  CD  GLU A 129     7592   6200   6318   -588    -95    -68       C  
ATOM    395  OE1 GLU A 129     -18.372  -8.888  -4.745  1.00 53.89           O  
ANISOU  395  OE1 GLU A 129     7811   6188   6477   -571    -86    -32       O  
ATOM    396  OE2 GLU A 129     -20.004  -7.416  -4.570  1.00 51.04           O  
ANISOU  396  OE2 GLU A 129     7344   6054   5994   -686    -82   -101       O  
ATOM    397  N   THR A 130     -15.148  -5.026  -6.035  1.00 26.78           N  
ANISOU  397  N   THR A 130     3993   2865   3317   -223    -66   -170       N  
ATOM    398  CA  THR A 130     -15.384  -3.807  -6.801  1.00 27.79           C  
ANISOU  398  CA  THR A 130     4035   3073   3452   -221    -36   -237       C  
ATOM    399  C   THR A 130     -14.624  -3.831  -8.120  1.00 29.74           C  
ANISOU  399  C   THR A 130     4281   3238   3779   -155     23   -276       C  
ATOM    400  O   THR A 130     -15.200  -3.642  -9.196  1.00 29.68           O  
ANISOU  400  O   THR A 130     4286   3237   3753   -193     74   -326       O  
ATOM    401  CB  THR A 130     -15.009  -2.547  -6.019  1.00 25.21           C  
ANISOU  401  CB  THR A 130     3588   2851   3139   -181    -82   -243       C  
ATOM    402  OG1 THR A 130     -15.550  -2.622  -4.695  1.00 25.91           O  
ANISOU  402  OG1 THR A 130     3678   3011   3156   -232   -140   -202       O  
ATOM    403  CG2 THR A 130     -15.567  -1.317  -6.720  1.00 24.69           C  
ANISOU  403  CG2 THR A 130     3447   2876   3060   -204    -58   -309       C  
ATOM    404  N   ASP A 131     -13.308  -3.992  -8.019  1.00 26.97           N  
ANISOU  404  N   ASP A 131     3919   3144   3185    356     58   -553       N  
ATOM    405  CA  ASP A 131     -12.470  -4.012  -9.196  1.00 25.01           C  
ANISOU  405  CA  ASP A 131     3804   2896   2802    458     76   -718       C  
ATOM    406  C   ASP A 131     -12.438  -5.471  -9.618  1.00 33.43           C  
ANISOU  406  C   ASP A 131     4969   3790   3941    408    -59   -853       C  
ATOM    407  O   ASP A 131     -11.626  -6.276  -9.141  1.00 37.00           O  
ANISOU  407  O   ASP A 131     5469   4105   4484    429    -32   -894       O  
ATOM    408  CB  ASP A 131     -11.076  -3.528  -8.776  1.00 28.17           C  
ANISOU  408  CB  ASP A 131     4197   3312   3196    549    245   -692       C  
ATOM    409  CG  ASP A 131     -10.021  -3.776  -9.830  1.00 25.45           C  
ANISOU  409  CG  ASP A 131     3856   2974   2840    537    260   -756       C  
ATOM    410  OD1 ASP A 131     -10.389  -3.826 -11.012  1.00 25.14           O  
ANISOU  410  OD1 ASP A 131     3886   2960   2706    543    201   -838       O  
ATOM    411  OD2 ASP A 131      -8.825  -3.918  -9.478  1.00 25.88           O  
ANISOU  411  OD2 ASP A 131     3841   3012   2978    524    321   -724       O  
ATOM    412  N   THR A 132     -13.273  -5.793 -10.594  1.00 28.92           N  
ANISOU  412  N   THR A 132     4442   3226   3319    352   -205   -931       N  
ATOM    413  CA  THR A 132     -13.558  -7.199 -10.860  1.00 34.68           C  
ANISOU  413  CA  THR A 132     5248   3789   4139    267   -363  -1033       C  
ATOM    414  C   THR A 132     -12.559  -7.837 -11.816  1.00 34.75           C  
ANISOU  414  C   THR A 132     5442   3700   4063    363   -362  -1222       C  
ATOM    415  O   THR A 132     -12.432  -9.068 -11.877  1.00 34.11           O  
ANISOU  415  O   THR A 132     5415   3474   4071    307   -435  -1280       O  
ATOM    416  CB  THR A 132     -15.017  -7.399 -11.338  1.00 44.50           C  
ANISOU  416  CB  THR A 132     6447   5064   5398    137   -547  -1017       C  
ATOM    417  OG1 THR A 132     -15.323  -6.448 -12.365  1.00 46.29           O  
ANISOU  417  OG1 THR A 132     6693   5446   5448    191   -550  -1048       O  
ATOM    418  CG2 THR A 132     -15.986  -7.188 -10.176  1.00 45.41           C  
ANISOU  418  CG2 THR A 132     6381   5216   5658     24   -558   -824       C  
ATOM    419  N   ASP A 133     -11.831  -7.010 -12.557  1.00 30.47           N  
ANISOU  419  N   ASP A 133     4880   3300   3398    446   -218  -1197       N  
ATOM    420  CA  ASP A 133     -10.814  -7.552 -13.454  1.00 31.67           C  
ANISOU  420  CA  ASP A 133     5076   3428   3528    475   -152  -1247       C  
ATOM    421  C   ASP A 133      -9.394  -7.512 -12.877  1.00 35.17           C  
ANISOU  421  C   ASP A 133     5440   3873   4048    512     18  -1175       C  
ATOM    422  O   ASP A 133      -8.438  -7.913 -13.539  1.00 41.48           O  
ANISOU  422  O   ASP A 133     6257   4659   4845    535     75  -1211       O  
ATOM    423  CB  ASP A 133     -10.899  -6.952 -14.867  1.00 31.91           C  
ANISOU  423  CB  ASP A 133     5140   3568   3416    505   -148  -1281       C  
ATOM    424  CG  ASP A 133     -10.851  -5.440 -14.870  1.00 31.59           C  
ANISOU  424  CG  ASP A 133     5000   3696   3308    540    -38  -1174       C  
ATOM    425  OD1 ASP A 133     -10.393  -4.874 -13.868  1.00 23.29           O  
ANISOU  425  OD1 ASP A 133     3848   2681   2322    548     67  -1070       O  
ATOM    426  OD2 ASP A 133     -11.272  -4.819 -15.869  1.00 34.24           O  
ANISOU  426  OD2 ASP A 133     5352   4122   3535    550    -59  -1185       O  
ATOM    427  N   GLY A 134      -9.267  -7.045 -11.637  1.00 32.76           N  
ANISOU  427  N   GLY A 134     5041   3586   3819    512     83  -1074       N  
ATOM    428  CA  GLY A 134      -7.973  -6.951 -10.983  1.00 38.14           C  
ANISOU  428  CA  GLY A 134     5619   4283   4588    526    209  -1002       C  
ATOM    429  C   GLY A 134      -7.016  -6.010 -11.693  1.00 39.39           C  
ANISOU  429  C   GLY A 134     5700   4572   4696    544    302   -961       C  
ATOM    430  O   GLY A 134      -5.806  -6.224 -11.697  1.00 40.79           O  
ANISOU  430  O   GLY A 134     5836   4740   4920    560    352   -955       O  
ATOM    431  N   SER A 135      -7.559  -4.961 -12.299  1.00 36.34           N  
ANISOU  431  N   SER A 135     5302   4295   4212    545    304   -931       N  
ATOM    432  CA  SER A 135      -6.731  -4.020 -13.047  1.00 35.06           C  
ANISOU  432  CA  SER A 135     5106   4224   3990    578    359   -883       C  
ATOM    433  C   SER A 135      -6.108  -2.976 -12.127  1.00 34.32           C  
ANISOU  433  C   SER A 135     4923   4196   3920    594    405   -743       C  
ATOM    434  O   SER A 135      -5.208  -2.233 -12.528  1.00 33.64           O  
ANISOU  434  O   SER A 135     4835   4154   3793    640    437   -684       O  
ATOM    435  CB  SER A 135      -7.544  -3.346 -14.158  1.00 31.52           C  
ANISOU  435  CB  SER A 135     4698   3851   3428    580    332   -902       C  
ATOM    436  OG  SER A 135      -8.427  -2.365 -13.628  1.00 28.04           O  
ANISOU  436  OG  SER A 135     4190   3492   2970    548    333   -819       O  
ATOM    437  N   GLY A 136      -6.592  -2.927 -10.886  1.00 29.38           N  
ANISOU  437  N   GLY A 136     4234   3566   3363    554    402   -688       N  
ATOM    438  CA  GLY A 136      -6.137  -1.942  -9.925  1.00 26.42           C  
ANISOU  438  CA  GLY A 136     3793   3244   3001    557    429   -547       C  
ATOM    439  C   GLY A 136      -6.833  -0.607 -10.128  1.00 26.11           C  
ANISOU  439  C   GLY A 136     3729   3297   2896    551    429   -461       C  
ATOM    440  O   GLY A 136      -6.463   0.397  -9.527  1.00 25.29           O  
ANISOU  440  O   GLY A 136     3592   3223   2793    555    442   -336       O  
ATOM    441  N   THR A 137      -7.846  -0.598 -10.987  1.00 23.50           N  
ANISOU  441  N   THR A 137     3424   2997   2507    540    407   -527       N  
ATOM    442  CA  THR A 137      -8.623   0.608 -11.241  1.00 22.40           C  
ANISOU  442  CA  THR A 137     3258   2944   2308    537    401   -452       C  
ATOM    443  C   THR A 137     -10.095   0.227 -11.343  1.00 25.02           C  
ANISOU  443  C   THR A 137     3597   3297   2612    487    372   -514       C  
ATOM    444  O   THR A 137     -10.431  -0.848 -11.837  1.00 21.41           O  
ANISOU  444  O   THR A 137     3232   2785   2119    509    327   -634       O  
ATOM    445  CB  THR A 137      -8.213   1.256 -12.568  1.00 23.37           C  
ANISOU  445  CB  THR A 137     3421   3105   2355    589    401   -462       C  
ATOM    446  OG1 THR A 137      -8.338   0.289 -13.618  1.00 27.76           O  
ANISOU  446  OG1 THR A 137     4053   3627   2866    595    381   -598       O  
ATOM    447  CG2 THR A 137      -6.777   1.739 -12.506  1.00 30.62           C  
ANISOU  447  CG2 THR A 137     4337   4005   3291    634    430   -397       C  
ATOM    448  N   VAL A 138     -10.975   1.102 -10.893  1.00 21.88           N  
ANISOU  448  N   VAL A 138     3145   2969   2199    466    373   -422       N  
ATOM    449  CA  VAL A 138     -12.405   0.836 -10.990  1.00 22.65           C  
ANISOU  449  CA  VAL A 138     3287   3117   2203    496    327   -451       C  
ATOM    450  C   VAL A 138     -12.979   1.682 -12.114  1.00 25.17           C  
ANISOU  450  C   VAL A 138     3606   3520   2438    487    303   -446       C  
ATOM    451  O   VAL A 138     -13.023   2.904 -11.999  1.00 23.10           O  
ANISOU  451  O   VAL A 138     3268   3299   2211    461    331   -337       O  
ATOM    452  CB  VAL A 138     -13.121   1.175  -9.661  1.00 22.69           C  
ANISOU  452  CB  VAL A 138     3218   3162   2240    490    355   -328       C  
ATOM    453  CG1 VAL A 138     -14.619   0.943  -9.784  1.00 20.68           C  
ANISOU  453  CG1 VAL A 138     2988   3017   1851    536    294   -344       C  
ATOM    454  CG2 VAL A 138     -12.551   0.332  -8.518  1.00 24.75           C  
ANISOU  454  CG2 VAL A 138     3486   3321   2596    503    387   -324       C  
ATOM    455  N   ASP A 139     -13.400   1.057 -13.213  1.00 23.06           N  
ANISOU  455  N   ASP A 139     3437   3260   2065    523    224   -569       N  
ATOM    456  CA  ASP A 139     -13.996   1.852 -14.289  1.00 23.34           C  
ANISOU  456  CA  ASP A 139     3473   3377   2020    519    198   -560       C  
ATOM    457  C   ASP A 139     -15.470   2.129 -13.985  1.00 22.30           C  
ANISOU  457  C   ASP A 139     3305   3367   1803    526    128   -517       C  
ATOM    458  O   ASP A 139     -16.007   1.628 -12.994  1.00 22.48           O  
ANISOU  458  O   ASP A 139     3305   3421   1815    533     91   -502       O  
ATOM    459  CB  ASP A 139     -13.775   1.213 -15.678  1.00 26.92           C  
ANISOU  459  CB  ASP A 139     4035   3793   2400    538    138   -695       C  
ATOM    460  CG  ASP A 139     -14.349  -0.189 -15.790  1.00 30.43           C  
ANISOU  460  CG  ASP A 139     4591   4182   2791    550    -14   -844       C  
ATOM    461  OD1 ASP A 139     -15.536  -0.384 -15.456  1.00 30.83           O  
ANISOU  461  OD1 ASP A 139     4641   4289   2785    534   -144   -866       O  
ATOM    462  OD2 ASP A 139     -13.609  -1.100 -16.224  1.00 32.18           O  
ANISOU  462  OD2 ASP A 139     4891   4293   3041    555    -27   -940       O  
ATOM    463  N   TYR A 140     -16.132   2.933 -14.812  1.00 26.30           N  
ANISOU  463  N   TYR A 140     3792   3953   2247    520    105   -486       N  
ATOM    464  CA  TYR A 140     -17.490   3.358 -14.464  1.00 26.07           C  
ANISOU  464  CA  TYR A 140     3686   4064   2157    510     49   -405       C  
ATOM    465  C   TYR A 140     -18.471   2.190 -14.471  1.00 19.57           C  
ANISOU  465  C   TYR A 140     2897   3318   1222    493   -156   -508       C  
ATOM    466  O   TYR A 140     -19.403   2.140 -13.668  1.00 23.80           O  
ANISOU  466  O   TYR A 140     3294   3869   1878    395   -203   -366       O  
ATOM    467  CB  TYR A 140     -17.991   4.481 -15.379  1.00 28.40           C  
ANISOU  467  CB  TYR A 140     3953   4411   2428    505     59   -355       C  
ATOM    468  CG  TYR A 140     -19.387   4.952 -15.026  1.00 27.15           C  
ANISOU  468  CG  TYR A 140     3691   4398   2227    488      8   -251       C  
ATOM    469  CD1 TYR A 140     -20.474   4.629 -15.832  1.00 30.42           C  
ANISOU  469  CD1 TYR A 140     4116   4926   2516    471   -151   -298       C  
ATOM    470  CD2 TYR A 140     -19.619   5.709 -13.888  1.00 27.63           C  
ANISOU  470  CD2 TYR A 140     3635   4462   2401    468     96    -99       C  
ATOM    471  CE1 TYR A 140     -21.753   5.053 -15.512  1.00 28.73           C  
ANISOU  471  CE1 TYR A 140     3776   4853   2287    432   -209   -172       C  
ATOM    472  CE2 TYR A 140     -20.896   6.133 -13.555  1.00 24.68           C  
ANISOU  472  CE2 TYR A 140     3148   4216   2015    444     64     18       C  
ATOM    473  CZ  TYR A 140     -21.955   5.807 -14.377  1.00 25.00           C  
ANISOU  473  CZ  TYR A 140     3179   4395   1923    424    -81     -6       C  
ATOM    474  OH  TYR A 140     -23.225   6.227 -14.052  1.00 30.53           O  
ANISOU  474  OH  TYR A 140     3744   5218   2639    380   -121    137       O  
ATOM    475  N   GLU A 141     -18.254   1.240 -15.370  1.00 23.59           N  
ANISOU  475  N   GLU A 141     3532   3726   1704    486   -282   -680       N  
ATOM    476  CA  GLU A 141     -19.129   0.081 -15.426  1.00 26.19           C  
ANISOU  476  CA  GLU A 141     3838   3952   2159    346   -492   -708       C  
ATOM    477  C   GLU A 141     -19.008  -0.751 -14.152  1.00 24.78           C  
ANISOU  477  C   GLU A 141     3587   3636   2192    259   -485   -637       C  
ATOM    478  O   GLU A 141     -20.005  -1.231 -13.617  1.00 27.26           O  
ANISOU  478  O   GLU A 141     3788   3920   2649    130   -598   -544       O  
ATOM    479  CB  GLU A 141     -18.827  -0.767 -16.659  1.00 36.46           C  
ANISOU  479  CB  GLU A 141     5315   5159   3379    363   -621   -916       C  
ATOM    480  CG  GLU A 141     -19.757  -1.939 -16.831  1.00 51.33           C  
ANISOU  480  CG  GLU A 141     7189   6936   5379    214   -853   -955       C  
ATOM    481  CD  GLU A 141     -19.439  -2.743 -18.072  1.00 64.40           C  
ANISOU  481  CD  GLU A 141     9040   8492   6937    237   -980  -1164       C  
ATOM    482  OE1 GLU A 141     -19.681  -2.233 -19.188  1.00 66.87           O  
ANISOU  482  OE1 GLU A 141     9404   8891   7111    278   -998  -1201       O  
ATOM    483  OE2 GLU A 141     -18.937  -3.879 -17.929  1.00 70.09           O  
ANISOU  483  OE2 GLU A 141     9848   9037   7747    205  -1028  -1259       O  
ATOM    484  N   GLU A 142     -17.786  -0.914 -13.661  1.00 24.43           N  
ANISOU  484  N   GLU A 142     3604   3509   2169    332   -352   -675       N  
ATOM    485  CA  GLU A 142     -17.568  -1.641 -12.412  1.00 23.41           C  
ANISOU  485  CA  GLU A 142     3414   3251   2229    266   -330   -606       C  
ATOM    486  C   GLU A 142     -18.202  -0.888 -11.256  1.00 19.46           C  
ANISOU  486  C   GLU A 142     2747   2838   1807    226   -250   -394       C  
ATOM    487  O   GLU A 142     -18.794  -1.476 -10.350  1.00 20.59           O  
ANISOU  487  O   GLU A 142     2795   2908   2119    120   -303   -295       O  
ATOM    488  CB  GLU A 142     -16.076  -1.835 -12.152  1.00 22.83           C  
ANISOU  488  CB  GLU A 142     3438   3088   2148    367   -194   -683       C  
ATOM    489  CG  GLU A 142     -15.403  -2.751 -13.145  1.00 29.32           C  
ANISOU  489  CG  GLU A 142     4430   3793   2919    407   -265   -885       C  
ATOM    490  CD  GLU A 142     -13.921  -2.803 -12.941  1.00 29.05           C  
ANISOU  490  CD  GLU A 142     4477   3692   2867    523   -114   -948       C  
ATOM    491  OE1 GLU A 142     -13.336  -1.750 -12.593  1.00 24.44           O  
ANISOU  491  OE1 GLU A 142     3800   3202   2283    557     55   -819       O  
ATOM    492  OE2 GLU A 142     -13.344  -3.898 -13.095  1.00 28.83           O  
ANISOU  492  OE2 GLU A 142     4535   3512   2906    513   -156  -1047       O  
ATOM    493  N   PHE A 143     -18.077   0.429 -11.299  1.00 18.54           N  
ANISOU  493  N   PHE A 143     2603   2877   1565    315   -115   -321       N  
ATOM    494  CA  PHE A 143     -18.613   1.269 -10.245  1.00 19.07           C  
ANISOU  494  CA  PHE A 143     2531   3034   1680    297    -19   -120       C  
ATOM    495  C   PHE A 143     -20.137   1.143 -10.217  1.00 17.95           C  
ANISOU  495  C   PHE A 143     2266   2942   1612    181   -155    -15       C  
ATOM    496  O   PHE A 143     -20.740   1.003  -9.155  1.00 20.16           O  
ANISOU  496  O   PHE A 143     2429   3197   2034    105   -149    135       O  
ATOM    497  CB  PHE A 143     -18.188   2.718 -10.482  1.00 18.04           C  
ANISOU  497  CB  PHE A 143     2416   3060   1378    420    142    -81       C  
ATOM    498  CG  PHE A 143     -18.491   3.635  -9.335  1.00 16.67           C  
ANISOU  498  CG  PHE A 143     2130   2943   1262    414    262    115       C  
ATOM    499  CD1 PHE A 143     -17.927   3.417  -8.093  1.00 17.80           C  
ANISOU  499  CD1 PHE A 143     2248   2971   1543    395    334    181       C  
ATOM    500  CD2 PHE A 143     -19.331   4.736  -9.511  1.00 19.71           C  
ANISOU  500  CD2 PHE A 143     2436   3364   1689    388    251    199       C  
ATOM    501  CE1 PHE A 143     -18.203   4.280  -7.025  1.00 22.67           C  
ANISOU  501  CE1 PHE A 143     2788   3498   2327    341    345    291       C  
ATOM    502  CE2 PHE A 143     -19.614   5.591  -8.454  1.00 19.34           C  
ANISOU  502  CE2 PHE A 143     2313   3228   1809    351    279    303       C  
ATOM    503  CZ  PHE A 143     -19.042   5.365  -7.213  1.00 22.77           C  
ANISOU  503  CZ  PHE A 143     2749   3537   2365    327    308    330       C  
ATOM    504  N   LYS A 144     -20.752   1.164 -11.398  1.00 20.53           N  
ANISOU  504  N   LYS A 144     2621   3335   1845    167   -281    -93       N  
ATOM    505  CA  LYS A 144     -22.204   1.083 -11.503  1.00 23.02           C  
ANISOU  505  CA  LYS A 144     2814   3709   2224     59   -423      2       C  
ATOM    506  C   LYS A 144     -22.719  -0.267 -11.026  1.00 26.67           C  
ANISOU  506  C   LYS A 144     3229   4015   2890    -85   -571      5       C  
ATOM    507  O   LYS A 144     -23.734  -0.352 -10.325  1.00 30.44           O  
ANISOU  507  O   LYS A 144     3559   4506   3501   -182   -614    160       O  
ATOM    508  CB  LYS A 144     -22.655   1.357 -12.943  1.00 27.06           C  
ANISOU  508  CB  LYS A 144     3383   4317   2580     81   -537   -100       C  
ATOM    509  CG  LYS A 144     -24.156   1.354 -13.117  1.00 36.66           C  
ANISOU  509  CG  LYS A 144     4464   5609   3855    -27   -689      2       C  
ATOM    510  CD  LYS A 144     -24.575   1.872 -14.482  1.00 44.44           C  
ANISOU  510  CD  LYS A 144     5502   6718   4663     15   -779    -78       C  
ATOM    511  CE  LYS A 144     -26.094   1.935 -14.576  1.00 51.15           C  
ANISOU  511  CE  LYS A 144     6196   7655   5582    -92   -926     45       C  
ATOM    512  NZ  LYS A 144     -26.566   2.446 -15.893  1.00 56.26           N  
ANISOU  512  NZ  LYS A 144     6890   8427   6058    -52  -1026    -25       N  
ATOM    513  N   CYS A 145     -22.008  -1.321 -11.404  1.00 27.22           N  
ANISOU  513  N   CYS A 145     3425   3933   2983    -96   -643   -163       N  
ATOM    514  CA  CYS A 145     -22.360  -2.676 -10.992  1.00 30.85           C  
ANISOU  514  CA  CYS A 145     3866   4225   3631   -227   -780   -180       C  
ATOM    515  C   CYS A 145     -22.429  -2.776  -9.476  1.00 26.17           C  
ANISOU  515  C   CYS A 145     3159   3578   3208   -270   -682    -13       C  
ATOM    516  O   CYS A 145     -23.352  -3.371  -8.928  1.00 32.91           O  
ANISOU  516  O   CYS A 145     3902   4378   4224   -394   -776     85       O  
ATOM    517  CB  CYS A 145     -21.343  -3.681 -11.531  1.00 34.91           C  
ANISOU  517  CB  CYS A 145     4556   4581   4127   -200   -825   -384       C  
ATOM    518  SG  CYS A 145     -21.568  -4.095 -13.278  1.00 52.89           S  
ANISOU  518  SG  CYS A 145     6979   6855   6262   -204  -1016   -588       S  
ATOM    519  N   LEU A 146     -21.443  -2.196  -8.800  1.00 22.15           N  
ANISOU  519  N   LEU A 146     2678   3079   2658   -165   -493     21       N  
ATOM    520  CA  LEU A 146     -21.419  -2.229  -7.342  1.00 22.71           C  
ANISOU  520  CA  LEU A 146     2660   3098   2870   -190   -390    177       C  
ATOM    521  C   LEU A 146     -22.561  -1.404  -6.781  1.00 23.33           C  
ANISOU  521  C   LEU A 146     2579   3306   2981   -226   -356    385       C  
ATOM    522  O   LEU A 146     -23.342  -1.866  -5.942  1.00 21.36           O  
ANISOU  522  O   LEU A 146     2218   3002   2896   -324   -393    515       O  
ATOM    523  CB  LEU A 146     -20.094  -1.686  -6.805  1.00 20.39           C  
ANISOU  523  CB  LEU A 146     2438   2799   2511    -65   -202    166       C  
ATOM    524  CG  LEU A 146     -20.088  -1.379  -5.297  1.00 17.95           C  
ANISOU  524  CG  LEU A 146     2042   2472   2306    -67    -74    347       C  
ATOM    525  CD1 LEU A 146     -20.305  -2.662  -4.474  1.00 24.47           C  
ANISOU  525  CD1 LEU A 146     2838   3123   3338   -173   -150    374       C  
ATOM    526  CD2 LEU A 146     -18.794  -0.705  -4.894  1.00 19.42           C  
ANISOU  526  CD2 LEU A 146     2301   2672   2406     57    100    332       C  
ATOM    527  N   MET A 147     -22.664  -0.171  -7.261  1.00 23.52           N  
ANISOU  527  N   MET A 147     2592   3500   2844   -142   -279    419       N  
ATOM    528  CA  MET A 147     -23.527   0.799  -6.613  1.00 26.71           C  
ANISOU  528  CA  MET A 147     2862   4033   3255   -141   -197    627       C  
ATOM    529  C   MET A 147     -25.018   0.609  -6.902  1.00 29.42           C  
ANISOU  529  C   MET A 147     3072   4432   3675   -251   -344    716       C  
ATOM    530  O   MET A 147     -25.856   0.873  -6.041  1.00 34.41           O  
ANISOU  530  O   MET A 147     3569   5100   4407   -295   -304    908       O  
ATOM    531  CB  MET A 147     -23.061   2.214  -6.959  1.00 22.70           C  
ANISOU  531  CB  MET A 147     2396   3682   2548     -6    -49    639       C  
ATOM    532  CG  MET A 147     -21.618   2.500  -6.528  1.00 19.73           C  
ANISOU  532  CG  MET A 147     2128   3257   2111     99    108    581       C  
ATOM    533  SD  MET A 147     -21.337   2.349  -4.745  1.00 25.16           S  
ANISOU  533  SD  MET A 147     2765   3843   2952     82    230    738       S  
ATOM    534  CE  MET A 147     -22.555   3.499  -4.125  1.00 28.92           C  
ANISOU  534  CE  MET A 147     3142   4378   3469     99    236    855       C  
ATOM    535  N   MET A 148     -25.353   0.174  -8.113  1.00 23.58           N  
ANISOU  535  N   MET A 148     2371   3701   2888   -294   -513    583       N  
ATOM    536  CA  MET A 148     -26.758   0.033  -8.494  1.00 23.47           C  
ANISOU  536  CA  MET A 148     2228   3749   2940   -400   -668    662       C  
ATOM    537  C   MET A 148     -27.332  -1.392  -8.437  1.00 34.79           C  
ANISOU  537  C   MET A 148     3624   5030   4565   -557   -858    628       C  
ATOM    538  O   MET A 148     -28.497  -1.615  -8.758  1.00 35.14           O  
ANISOU  538  O   MET A 148     3556   5113   4683   -661  -1005    690       O  
ATOM    539  CB  MET A 148     -27.038   0.748  -9.827  1.00 29.10           C  
ANISOU  539  CB  MET A 148     2978   4611   3466   -347   -732    584       C  
ATOM    540  CG  MET A 148     -26.931   2.274  -9.684  1.00 32.77           C  
ANISOU  540  CG  MET A 148     3420   5252   3780   -218   -546    693       C  
ATOM    541  SD  MET A 148     -27.066   3.237 -11.200  1.00102.20           S  
ANISOU  541  SD  MET A 148    12279  14222  12330   -126   -582    601       S  
ATOM    542  CE  MET A 148     -28.842   3.370 -11.388  1.00 66.87           C  
ANISOU  542  CE  MET A 148     7610   9862   7935   -231   -731    760       C  
ATOM    543  N   SER A 149     -26.509  -2.344  -8.011  1.00 34.27           N  
ANISOU  543  N   SER A 149     3648   4791   4583   -575   -853    536       N  
ATOM    544  CA  SER A 149     -26.937  -3.739  -7.880  1.00 43.64           C  
ANISOU  544  CA  SER A 149     4816   5813   5954   -721  -1019    500       C  
ATOM    545  C   SER A 149     -28.021  -3.917  -6.814  1.00 43.24           C  
ANISOU  545  C   SER A 149     4577   5750   6103   -827  -1022    717       C  
ATOM    546  O   SER A 149     -27.930  -3.345  -5.725  1.00 40.00           O  
ANISOU  546  O   SER A 149     4102   5369   5728   -777   -852    873       O  
ATOM    547  CB  SER A 149     -25.740  -4.632  -7.540  1.00 38.12           C  
ANISOU  547  CB  SER A 149     4257   4933   5296   -697   -981    369       C  
ATOM    548  OG  SER A 149     -25.201  -4.272  -6.280  1.00 42.69           O  
ANISOU  548  OG  SER A 149     4806   5492   5922   -637   -792    488       O  
ATOM    549  N   SER A 150     -29.033  -4.722  -7.135  1.00 42.91           N  
ANISOU  549  N   SER A 150     4454   5660   6191   -974  -1217    728       N  
ATOM    550  CA  SER A 150     -30.078  -5.088  -6.181  1.00 43.82           C  
ANISOU  550  CA  SER A 150     4390   5740   6521  -1091  -1238    925       C  
ATOM    551  C   SER A 150     -30.110  -6.602  -6.015  1.00 42.05           C  
ANISOU  551  C   SER A 150     4195   5306   6476  -1226  -1380    849       C  
ATOM    552  O   SER A 150     -30.396  -7.326  -6.968  1.00 39.16           O  
ANISOU  552  O   SER A 150     3876   4886   6117  -1314  -1581    715       O  
ATOM    553  CB  SER A 150     -31.445  -4.588  -6.648  1.00 50.62           C  
ANISOU  553  CB  SER A 150     5093   6747   7395  -1152  -1336   1045       C  
ATOM    554  OG  SER A 150     -32.476  -5.127  -5.836  1.00 55.63           O  
ANISOU  554  OG  SER A 150     5647   7301   8187  -1208  -1310   1177       O  
ATOM    555  N   ASP A 151     -29.805  -7.073  -4.808  1.00 37.63           N  
ANISOU  555  N   ASP A 151     3619   4624   6052  -1236  -1275    932       N  
ATOM    556  CA  ASP A 151     -29.664  -8.510  -4.557  1.00 39.92           C  
ANISOU  556  CA  ASP A 151     3985   4706   6475  -1315  -1356    842       C  
ATOM    557  C   ASP A 151     -30.884  -9.214  -3.950  1.00 46.20           C  
ANISOU  557  C   ASP A 151     4696   5450   7410  -1378  -1374    959       C  
ATOM    558  O   ASP A 151     -30.857 -10.430  -3.744  1.00 42.94           O  
ANISOU  558  O   ASP A 151     4336   4878   7100  -1441  -1440    894       O  
ATOM    559  CB  ASP A 151     -28.422  -8.771  -3.699  1.00 40.16           C  
ANISOU  559  CB  ASP A 151     4111   4615   6533  -1253  -1221    812       C  
ATOM    560  CG  ASP A 151     -27.164  -8.172  -4.302  1.00 40.92           C  
ANISOU  560  CG  ASP A 151     4369   4763   6418  -1104  -1135    655       C  
ATOM    561  OD1 ASP A 151     -26.889  -8.434  -5.494  1.00 43.98           O  
ANISOU  561  OD1 ASP A 151     4868   5143   6697  -1101  -1256    470       O  
ATOM    562  OD2 ASP A 151     -26.457  -7.428  -3.589  1.00 35.35           O  
ANISOU  562  OD2 ASP A 151     3682   4103   5647   -986   -944    718       O  
ATOM    563  N   ALA A 152     -31.951  -8.470  -3.667  1.00 48.26           N  
ANISOU  563  N   ALA A 152     4831   5840   7666  -1354  -1316   1127       N  
ATOM    564  CA  ALA A 152     -33.139  -9.075  -3.059  1.00 48.30           C  
ANISOU  564  CA  ALA A 152     4752   5800   7802  -1405  -1333   1246       C  
ATOM    565  C   ALA A 152     -33.841 -10.048  -4.004  1.00 52.44           C  
ANISOU  565  C   ALA A 152     5266   6263   8395  -1543  -1552   1151       C  
ATOM    566  O   ALA A 152     -33.866  -9.839  -5.218  1.00 49.13           O  
ANISOU  566  O   ALA A 152     4869   5906   7892  -1581  -1687   1042       O  
ATOM    567  CB  ALA A 152     -34.108  -8.003  -2.584  1.00 51.55           C  
ANISOU  567  CB  ALA A 152     5052   6355   8179  -1335  -1223   1440       C  
TER     568      ALA A 152                                                      
ATOM    569  N   GLY B 143     -18.123 -13.314  -3.442  1.00 40.73           N  
ANISOU  569  N   GLY B 143     5459   4372   5643   -171   -333     -6       N  
ATOM    570  CA  GLY B 143     -19.302 -12.579  -3.019  1.00 43.09           C  
ANISOU  570  CA  GLY B 143     5709   4687   5976   -226   -271     23       C  
ATOM    571  C   GLY B 143     -19.042 -11.775  -1.762  1.00 40.17           C  
ANISOU  571  C   GLY B 143     5352   4366   5545   -211   -214     52       C  
ATOM    572  O   GLY B 143     -18.098 -12.043  -1.019  1.00 38.14           O  
ANISOU  572  O   GLY B 143     5151   4114   5226   -169   -218     65       O  
ATOM    573  N   LEU B 144     -19.871 -10.767  -1.531  1.00 35.23           N  
ANISOU  573  N   LEU B 144     4672   3778   4938   -244   -161     62       N  
ATOM    574  CA  LEU B 144     -19.804 -10.008  -0.295  1.00 30.01           C  
ANISOU  574  CA  LEU B 144     4021   3157   4224   -237   -101     89       C  
ATOM    575  C   LEU B 144     -21.088 -10.199   0.479  1.00 24.96           C  
ANISOU  575  C   LEU B 144     3373   2487   3622   -291    -37    145       C  
ATOM    576  O   LEU B 144     -22.173 -10.188  -0.108  1.00 31.73           O  
ANISOU  576  O   LEU B 144     4181   3326   4550   -339    -26    151       O  
ATOM    577  CB  LEU B 144     -19.623  -8.515  -0.588  1.00 32.97           C  
ANISOU  577  CB  LEU B 144     4339   3607   4580   -222    -89     51       C  
ATOM    578  CG  LEU B 144     -18.214  -7.941  -0.666  1.00 34.23           C  
ANISOU  578  CG  LEU B 144     4514   3821   4671   -162   -126     12       C  
ATOM    579  CD1 LEU B 144     -18.316  -6.433  -0.812  1.00 29.73           C  
ANISOU  579  CD1 LEU B 144     3883   3315   4098   -162   -100    -14       C  
ATOM    580  CD2 LEU B 144     -17.417  -8.310   0.577  1.00 33.81           C  
ANISOU  580  CD2 LEU B 144     4533   3771   4544   -131   -112     39       C  
ATOM    581  N   SER B 145     -20.979 -10.355   1.795  1.00 25.50           N  
ANISOU  581  N   SER B 145     3487   2559   3644   -284      7    189       N  
ATOM    582  CA  SER B 145     -22.169 -10.343   2.634  1.00 29.12           C  
ANISOU  582  CA  SER B 145     3932   3004   4128   -330     77    244       C  
ATOM    583  C   SER B 145     -22.884  -9.024   2.396  1.00 27.84           C  
ANISOU  583  C   SER B 145     3697   2892   3987   -349    118    225       C  
ATOM    584  O   SER B 145     -22.252  -8.041   2.008  1.00 27.71           O  
ANISOU  584  O   SER B 145     3658   2928   3942   -318    103    176       O  
ATOM    585  CB  SER B 145     -21.795 -10.485   4.108  1.00 31.44           C  
ANISOU  585  CB  SER B 145     4280   3313   4352   -309    120    288       C  
ATOM    586  OG  SER B 145     -20.989  -9.398   4.531  1.00 26.89           O  
ANISOU  586  OG  SER B 145     3706   2809   3704   -267    131    254       O  
ATOM    587  N   PRO B 146     -24.199  -8.986   2.603  1.00 29.47           N  
ANISOU  587  N   PRO B 146     3866   3084   4246   -400    169    265       N  
ATOM    588  CA  PRO B 146     -24.901  -7.716   2.415  1.00 29.58           C  
ANISOU  588  CA  PRO B 146     3811   3146   4281   -415    213    251       C  
ATOM    589  C   PRO B 146     -24.459  -6.640   3.416  1.00 30.06           C  
ANISOU  589  C   PRO B 146     3883   3268   4270   -381    260    241       C  
ATOM    590  O   PRO B 146     -24.475  -5.465   3.066  1.00 28.20           O  
ANISOU  590  O   PRO B 146     3601   3078   4037   -372    272    204       O  
ATOM    591  CB  PRO B 146     -26.381  -8.075   2.613  1.00 32.43           C  
ANISOU  591  CB  PRO B 146     4140   3477   4707   -475    262    308       C  
ATOM    592  CG  PRO B 146     -26.389  -9.452   3.215  1.00 31.19           C  
ANISOU  592  CG  PRO B 146     4041   3260   4548   -488    254    359       C  
ATOM    593  CD  PRO B 146     -25.132 -10.124   2.771  1.00 31.10           C  
ANISOU  593  CD  PRO B 146     4083   3226   4508   -448    181    323       C  
ATOM    594  N   GLU B 147     -24.080  -7.029   4.631  1.00 28.20           N  
ANISOU  594  N   GLU B 147     3706   3034   3973   -363    286    273       N  
ATOM    595  CA  GLU B 147     -23.540  -6.062   5.587  1.00 29.12           C  
ANISOU  595  CA  GLU B 147     3839   3210   4014   -328    324    257       C  
ATOM    596  C   GLU B 147     -22.313  -5.376   5.010  1.00 21.78           C  
ANISOU  596  C   GLU B 147     2911   2317   3047   -285    271    192       C  
ATOM    597  O   GLU B 147     -22.199  -4.148   5.041  1.00 23.76           O  
ANISOU  597  O   GLU B 147     3130   2615   3282   -271    292    156       O  
ATOM    598  CB  GLU B 147     -23.151  -6.734   6.902  1.00 33.17           C  
ANISOU  598  CB  GLU B 147     4420   3722   4461   -311    347    301       C  
ATOM    599  CG  GLU B 147     -24.306  -7.287   7.703  1.00 48.17           C  
ANISOU  599  CG  GLU B 147     6319   5599   6384   -349    408    373       C  
ATOM    600  CD  GLU B 147     -23.826  -8.023   8.940  1.00 57.93           C  
ANISOU  600  CD  GLU B 147     7621   6836   7553   -329    424    419       C  
ATOM    601  OE1 GLU B 147     -22.802  -7.592   9.518  1.00 58.72           O  
ANISOU  601  OE1 GLU B 147     7757   6981   7572   -285    418    392       O  
ATOM    602  OE2 GLU B 147     -24.457  -9.036   9.322  1.00 63.69           O  
ANISOU  602  OE2 GLU B 147     8367   7523   8311   -357    442    484       O  
ATOM    603  N   LYS B 148     -21.388  -6.167   4.480  1.00 20.98           N  
ANISOU  603  N   LYS B 148     2845   2192   2934   -261    204    177       N  
ATOM    604  CA  LYS B 148     -20.160  -5.603   3.926  1.00 26.41           C  
ANISOU  604  CA  LYS B 148     3534   2917   3583   -217    150    121       C  
ATOM    605  C   LYS B 148     -20.393  -4.827   2.636  1.00 24.51           C  
ANISOU  605  C   LYS B 148     3223   2692   3399   -226    126     78       C  
ATOM    606  O   LYS B 148     -19.787  -3.781   2.420  1.00 22.50           O  
ANISOU  606  O   LYS B 148     2946   2485   3120   -200    115     37       O  
ATOM    607  CB  LYS B 148     -19.102  -6.683   3.709  1.00 28.85           C  
ANISOU  607  CB  LYS B 148     3900   3200   3863   -186     86    120       C  
ATOM    608  CG  LYS B 148     -18.296  -6.998   4.959  1.00 33.08           C  
ANISOU  608  CG  LYS B 148     4503   3752   4314   -154     98    143       C  
ATOM    609  CD  LYS B 148     -16.975  -7.670   4.605  1.00 42.67           C  
ANISOU  609  CD  LYS B 148     5762   4962   5489   -109     29    127       C  
ATOM    610  CE  LYS B 148     -16.363  -8.308   5.837  1.00 51.62           C  
ANISOU  610  CE  LYS B 148     6964   6098   6550    -85     42    167       C  
ATOM    611  NZ  LYS B 148     -16.559  -7.438   7.034  1.00 56.59           N  
ANISOU  611  NZ  LYS B 148     7595   6780   7127    -87    105    177       N  
ATOM    612  N   LYS B 149     -21.271  -5.330   1.776  1.00 26.12           N  
ANISOU  612  N   LYS B 149     3390   2856   3677   -263    115     89       N  
ATOM    613  CA  LYS B 149     -21.564  -4.619   0.535  1.00 22.66           C  
ANISOU  613  CA  LYS B 149     2880   2437   3294   -273     93     53       C  
ATOM    614  C   LYS B 149     -22.237  -3.275   0.831  1.00 21.09           C  
ANISOU  614  C   LYS B 149     2626   2278   3107   -286    155     49       C  
ATOM    615  O   LYS B 149     -21.902  -2.248   0.233  1.00 21.43           O  
ANISOU  615  O   LYS B 149     2625   2362   3155   -269    142     11       O  
ATOM    616  CB  LYS B 149     -22.426  -5.481  -0.400  1.00 25.21           C  
ANISOU  616  CB  LYS B 149     3174   2711   3692   -314     70     67       C  
ATOM    617  CG  LYS B 149     -22.580  -4.888  -1.798  1.00 28.22           C  
ANISOU  617  CG  LYS B 149     3484   3117   4123   -319     35     28       C  
ATOM    618  CD  LYS B 149     -23.355  -5.832  -2.710  1.00 31.84           C  
ANISOU  618  CD  LYS B 149     3919   3527   4650   -359      6     38       C  
ATOM    619  CE  LYS B 149     -23.337  -5.353  -4.161  1.00 36.10           C  
ANISOU  619  CE  LYS B 149     4391   4097   5228   -357    -39     -3       C  
ATOM    620  NZ  LYS B 149     -24.147  -6.258  -5.039  1.00 43.29           N  
ANISOU  620  NZ  LYS B 149     5279   4965   6205   -400    -68      3       N  
ATOM    621  N   LYS B 150     -23.178  -3.272   1.768  1.00 22.10           N  
ANISOU  621  N   LYS B 150     2758   2397   3242   -314    223     91       N  
ATOM    622  CA  LYS B 150     -23.839  -2.026   2.155  1.00 22.56           C  
ANISOU  622  CA  LYS B 150     2771   2492   3310   -323    288     89       C  
ATOM    623  C   LYS B 150     -22.847  -1.038   2.772  1.00 23.34           C  
ANISOU  623  C   LYS B 150     2890   2637   3339   -280    294     52       C  
ATOM    624  O   LYS B 150     -22.899   0.162   2.492  1.00 19.70           O  
ANISOU  624  O   LYS B 150     2382   2211   2893   -273    309     22       O  
ATOM    625  CB  LYS B 150     -24.988  -2.294   3.128  1.00 24.27           C  
ANISOU  625  CB  LYS B 150     2993   2692   3539   -356    361    145       C  
ATOM    626  CG  LYS B 150     -26.193  -2.984   2.507  1.00 33.59           C  
ANISOU  626  CG  LYS B 150     4132   3831   4798   -407    367    184       C  
ATOM    627  CD  LYS B 150     -27.286  -3.198   3.543  1.00 42.61           C  
ANISOU  627  CD  LYS B 150     5279   4964   5949   -437    442    244       C  
ATOM    628  CE  LYS B 150     -28.484  -3.911   2.946  1.00 49.67           C  
ANISOU  628  CE  LYS B 150     6132   5818   6924   -492    445    287       C  
ATOM    629  NZ  LYS B 150     -28.072  -5.171   2.263  1.00 55.32           N  
ANISOU  629  NZ  LYS B 150     6878   6482   7659   -502    373    286       N  
ATOM    630  N   MET B 151     -21.955  -1.538   3.626  1.00 22.07           N  
ANISOU  630  N   MET B 151     2801   2480   3106   -252    281     55       N  
ATOM    631  CA  MET B 151     -20.930  -0.681   4.225  1.00 25.14           C  
ANISOU  631  CA  MET B 151     3214   2914   3424   -212    279     19       C  
ATOM    632  C   MET B 151     -20.037  -0.077   3.151  1.00 20.79           C  
ANISOU  632  C   MET B 151     2633   2388   2881   -187    218    -31       C  
ATOM    633  O   MET B 151     -19.724   1.112   3.188  1.00 20.21           O  
ANISOU  633  O   MET B 151     2532   2351   2795   -172    228    -65       O  
ATOM    634  CB  MET B 151     -20.073  -1.460   5.224  1.00 27.74           C  
ANISOU  634  CB  MET B 151     3624   3244   3673   -187    268     35       C  
ATOM    635  CG  MET B 151     -19.000  -0.609   5.881  1.00 28.35           C  
ANISOU  635  CG  MET B 151     3727   3372   3673   -149    263     -2       C  
ATOM    636  SD  MET B 151     -17.732  -1.583   6.712  1.00 37.82           S  
ANISOU  636  SD  MET B 151     5013   4578   4780   -113    227     13       S  
ATOM    637  CE  MET B 151     -18.731  -2.900   7.396  1.00 58.48           C  
ANISOU  637  CE  MET B 151     7661   7145   7412   -143    269     86       C  
ATOM    638  N   LEU B 152     -19.632  -0.898   2.187  1.00 19.10           N  
ANISOU  638  N   LEU B 152     2420   2152   2687   -182    154    -34       N  
ATOM    639  CA  LEU B 152     -18.781  -0.444   1.078  1.00 17.60           C  
ANISOU  639  CA  LEU B 152     2196   1987   2503   -157     91    -76       C  
ATOM    640  C   LEU B 152     -19.429   0.701   0.316  1.00 19.85           C  
ANISOU  640  C   LEU B 152     2399   2294   2849   -173    110    -95       C  
ATOM    641  O   LEU B 152     -18.804   1.742   0.075  1.00 19.51           O  
ANISOU  641  O   LEU B 152     2329   2290   2795   -151     96   -128       O  
ATOM    642  CB  LEU B 152     -18.490  -1.619   0.128  1.00 17.46           C  
ANISOU  642  CB  LEU B 152     2191   1938   2506   -152     26    -74       C  
ATOM    643  CG  LEU B 152     -17.721  -1.378  -1.176  1.00 24.41           C  
ANISOU  643  CG  LEU B 152     3033   2844   3399   -126    -42   -111       C  
ATOM    644  CD1 LEU B 152     -16.361  -0.751  -0.920  1.00 21.97           C  
ANISOU  644  CD1 LEU B 152     2744   2581   3022    -80    -72   -140       C  
ATOM    645  CD2 LEU B 152     -17.564  -2.692  -1.946  1.00 26.35           C  
ANISOU  645  CD2 LEU B 152     3300   3051   3660   -123    -98   -107       C  
ATOM    646  N   LYS B 153     -20.693   0.518  -0.061  1.00 17.26           N  
ANISOU  646  N   LYS B 153     2028   1940   2589   -213    141    -70       N  
ATOM    647  CA  LYS B 153     -21.421   1.559  -0.793  1.00 16.64           C  
ANISOU  647  CA  LYS B 153     1867   1882   2574   -231    163    -80       C  
ATOM    648  C   LYS B 153     -21.567   2.830   0.038  1.00 19.76           C  
ANISOU  648  C   LYS B 153     2250   2304   2953   -224    223    -91       C  
ATOM    649  O   LYS B 153     -21.436   3.946  -0.476  1.00 17.05           O  
ANISOU  649  O   LYS B 153     1854   1991   2634   -215    222   -117       O  
ATOM    650  CB  LYS B 153     -22.810   1.051  -1.197  1.00 21.03           C  
ANISOU  650  CB  LYS B 153     2384   2406   3201   -278    191    -44       C  
ATOM    651  CG  LYS B 153     -22.771  -0.163  -2.133  1.00 22.72           C  
ANISOU  651  CG  LYS B 153     2604   2589   3441   -289    130    -40       C  
ATOM    652  CD  LYS B 153     -24.130  -0.856  -2.229  1.00 28.14           C  
ANISOU  652  CD  LYS B 153     3269   3236   4187   -341    161      2       C  
ATOM    653  CE  LYS B 153     -25.175   0.059  -2.860  1.00 38.01           C  
ANISOU  653  CE  LYS B 153     4430   4508   5504   -369    196      8       C  
ATOM    654  NZ  LYS B 153     -26.485  -0.633  -3.026  1.00 39.10           N  
ANISOU  654  NZ  LYS B 153     4542   4612   5702   -422    220     50       N  
ATOM    655  N   LYS B 154     -21.866   2.655   1.323  1.00 19.42           N  
ANISOU  655  N   LYS B 154     2256   2252   2871   -229    276    -70       N  
ATOM    656  CA  LYS B 154     -22.044   3.792   2.223  1.00 21.44           C  
ANISOU  656  CA  LYS B 154     2508   2532   3106   -222    337    -83       C  
ATOM    657  C   LYS B 154     -20.772   4.621   2.340  1.00 18.67           C  
ANISOU  657  C   LYS B 154     2173   2217   2706   -184    304   -130       C  
ATOM    658  O   LYS B 154     -20.794   5.861   2.265  1.00 20.50           O  
ANISOU  658  O   LYS B 154     2364   2470   2955   -177    325   -157       O  
ATOM    659  CB  LYS B 154     -22.462   3.311   3.618  1.00 26.60           C  
ANISOU  659  CB  LYS B 154     3219   3175   3713   -229    394    -52       C  
ATOM    660  CG  LYS B 154     -22.638   4.463   4.599  1.00 34.73           C  
ANISOU  660  CG  LYS B 154     4250   4232   4715   -218    457    -70       C  
ATOM    661  CD  LYS B 154     -23.127   4.006   5.967  1.00 40.80           C  
ANISOU  661  CD  LYS B 154     5069   4998   5437   -224    517    -37       C  
ATOM    662  CE  LYS B 154     -23.911   5.132   6.637  1.00 46.56           C  
ANISOU  662  CE  LYS B 154     5771   5746   6173   -225    596    -46       C  
ATOM    663  NZ  LYS B 154     -23.762   5.159   8.116  1.00 50.59           N  
ANISOU  663  NZ  LYS B 154     6341   6278   6604   -209    642    -44       N  
ATOM    664  N   LEU B 155     -19.655   3.934   2.551  1.00 15.80           N  
ANISOU  664  N   LEU B 155     1867   1857   2280   -159    252   -137       N  
ATOM    665  CA  LEU B 155     -18.358   4.597   2.715  1.00 22.31           C  
ANISOU  665  CA  LEU B 155     2711   2717   3050   -124    215   -177       C  
ATOM    666  C   LEU B 155     -17.882   5.300   1.441  1.00 19.97           C  
ANISOU  666  C   LEU B 155     2352   2441   2796   -113    165   -205       C  
ATOM    667  O   LEU B 155     -17.277   6.380   1.487  1.00 21.08           O  
ANISOU  667  O   LEU B 155     2474   2610   2924    -96    159   -237       O  
ATOM    668  CB  LEU B 155     -17.317   3.572   3.179  1.00 20.80           C  
ANISOU  668  CB  LEU B 155     2593   2526   2784   -100    171   -170       C  
ATOM    669  CG  LEU B 155     -17.614   3.028   4.572  1.00 23.65           C  
ANISOU  669  CG  LEU B 155     3017   2878   3092   -105    221   -143       C  
ATOM    670  CD1 LEU B 155     -16.556   2.023   4.984  1.00 24.18           C  
ANISOU  670  CD1 LEU B 155     3153   2947   3088    -80    176   -132       C  
ATOM    671  CD2 LEU B 155     -17.689   4.175   5.564  1.00 29.49           C  
ANISOU  671  CD2 LEU B 155     3760   3647   3798   -101    274   -167       C  
ATOM    672  N   ILE B 156     -18.152   4.684   0.300  1.00 17.34           N  
ANISOU  672  N   ILE B 156     1983   2092   2511   -123    129   -192       N  
ATOM    673  CA  ILE B 156     -17.804   5.298  -0.974  1.00 17.40           C  
ANISOU  673  CA  ILE B 156     1924   2124   2562   -112     83   -212       C  
ATOM    674  C   ILE B 156     -18.554   6.619  -1.142  1.00 19.37           C  
ANISOU  674  C   ILE B 156     2105   2385   2869   -128    131   -220       C  
ATOM    675  O   ILE B 156     -17.962   7.645  -1.495  1.00 17.01           O  
ANISOU  675  O   ILE B 156     1770   2115   2577   -110    113   -245       O  
ATOM    676  CB  ILE B 156     -18.103   4.327  -2.135  1.00 18.57           C  
ANISOU  676  CB  ILE B 156     2048   2256   2752   -123     40   -197       C  
ATOM    677  CG1 ILE B 156     -16.976   3.288  -2.227  1.00 16.72           C  
ANISOU  677  CG1 ILE B 156     1871   2020   2460    -93    -25   -202       C  
ATOM    678  CG2 ILE B 156     -18.254   5.077  -3.451  1.00 20.91           C  
ANISOU  678  CG2 ILE B 156     2255   2578   3110   -124     16   -208       C  
ATOM    679  CD1 ILE B 156     -17.281   2.130  -3.174  1.00 20.25           C  
ANISOU  679  CD1 ILE B 156     2312   2441   2940   -102    -64   -189       C  
ATOM    680  N   MET B 157     -19.849   6.611  -0.841  1.00 16.48           N  
ANISOU  680  N   MET B 157     1722   1997   2545   -159    195   -195       N  
ATOM    681  CA  MET B 157     -20.656   7.832  -0.970  1.00 18.73           C  
ANISOU  681  CA  MET B 157     1941   2289   2888   -172    247   -198       C  
ATOM    682  C   MET B 157     -20.278   8.897   0.055  1.00 20.13           C  
ANISOU  682  C   MET B 157     2142   2480   3029   -156    284   -227       C  
ATOM    683  O   MET B 157     -20.247  10.094  -0.260  1.00 19.94           O  
ANISOU  683  O   MET B 157     2066   2470   3040   -150    295   -247       O  
ATOM    684  CB  MET B 157     -22.156   7.523  -0.900  1.00 19.83           C  
ANISOU  684  CB  MET B 157     2052   2402   3079   -209    307   -160       C  
ATOM    685  CG  MET B 157     -22.653   6.647  -2.048  1.00 19.25           C  
ANISOU  685  CG  MET B 157     1942   2318   3056   -231    271   -136       C  
ATOM    686  SD  MET B 157     -22.229   7.278  -3.690  1.00 26.81           S  
ANISOU  686  SD  MET B 157     2813   3308   4064   -219    211   -155       S  
ATOM    687  CE  MET B 157     -23.292   8.718  -3.795  1.00 31.18           C  
ANISOU  687  CE  MET B 157     3283   3874   4690   -235    281   -146       C  
ATOM    688  N   GLN B 158     -19.990   8.469   1.280  1.00 19.78           N  
ANISOU  688  N   GLN B 158     2173   2429   2913   -149    304   -228       N  
ATOM    689  CA  GLN B 158     -19.545   9.400   2.309  1.00 19.96           C  
ANISOU  689  CA  GLN B 158     2226   2468   2891   -132    334   -261       C  
ATOM    690  C   GLN B 158     -18.276  10.117   1.859  1.00 19.63           C  
ANISOU  690  C   GLN B 158     2173   2453   2833   -106    274   -298       C  
ATOM    691  O   GLN B 158     -18.148  11.330   2.017  1.00 20.39           O  
ANISOU  691  O   GLN B 158     2244   2559   2944   -100    293   -328       O  
ATOM    692  CB  GLN B 158     -19.280   8.667   3.626  1.00 24.67           C  
ANISOU  692  CB  GLN B 158     2908   3063   3404   -126    352   -255       C  
ATOM    693  CG  GLN B 158     -20.526   8.142   4.313  1.00 41.69           C  
ANISOU  693  CG  GLN B 158     5076   5196   5568   -149    422   -217       C  
ATOM    694  CD  GLN B 158     -20.213   7.524   5.663  1.00 53.92           C  
ANISOU  694  CD  GLN B 158     6706   6750   7031   -140    442   -210       C  
ATOM    695  OE1 GLN B 158     -19.066   7.556   6.118  1.00 57.86           O  
ANISOU  695  OE1 GLN B 158     7252   7271   7462   -116    405   -236       O  
ATOM    696  NE2 GLN B 158     -21.228   6.957   6.310  1.00 57.84           N  
ANISOU  696  NE2 GLN B 158     7217   7231   7528   -159    499   -170       N  
ATOM    697  N   LYS B 159     -17.335   9.368   1.301  1.00 16.21           N  
ANISOU  697  N   LYS B 159     1758   2031   2371    -91    203   -296       N  
ATOM    698  CA  LYS B 159     -16.082   9.955   0.814  1.00 18.99           C  
ANISOU  698  CA  LYS B 159     2096   2413   2706    -66    141   -325       C  
ATOM    699  C   LYS B 159     -16.319  10.943  -0.333  1.00 20.28           C  
ANISOU  699  C   LYS B 159     2170   2587   2950    -69    132   -330       C  
ATOM    700  O   LYS B 159     -15.748  12.033  -0.354  1.00 18.59           O  
ANISOU  700  O   LYS B 159     1931   2390   2741    -58    122   -357       O  
ATOM    701  CB  LYS B 159     -15.092   8.858   0.396  1.00 21.25           C  
ANISOU  701  CB  LYS B 159     2418   2711   2946    -46     68   -316       C  
ATOM    702  CG  LYS B 159     -13.740   9.384  -0.132  1.00 21.61           C  
ANISOU  702  CG  LYS B 159     2448   2794   2969    -17      1   -339       C  
ATOM    703  CD  LYS B 159     -12.996  10.224   0.907  1.00 19.53           C  
ANISOU  703  CD  LYS B 159     2220   2550   2652     -6      9   -370       C  
ATOM    704  CE  LYS B 159     -11.559  10.538   0.455  1.00 19.58           C  
ANISOU  704  CE  LYS B 159     2219   2595   2626     22    -64   -386       C  
ATOM    705  NZ  LYS B 159     -10.995  11.681   1.239  1.00 21.68           N  
ANISOU  705  NZ  LYS B 159     2496   2877   2866     24    -54   -421       N  
ATOM    706  N   ALA B 160     -17.167  10.571  -1.286  1.00 20.15           N  
ANISOU  706  N   ALA B 160     2101   2560   2997    -86    134   -303       N  
ATOM    707  CA  ALA B 160     -17.507  11.478  -2.382  1.00 19.83           C  
ANISOU  707  CA  ALA B 160     1968   2531   3034    -91    131   -301       C  
ATOM    708  C   ALA B 160     -18.108  12.785  -1.847  1.00 19.34           C  
ANISOU  708  C   ALA B 160     1878   2461   3011    -99    196   -315       C  
ATOM    709  O   ALA B 160     -17.750  13.876  -2.298  1.00 21.78           O  
ANISOU  709  O   ALA B 160     2136   2785   3355    -90    184   -330       O  
ATOM    710  CB  ALA B 160     -18.468  10.809  -3.340  1.00 22.66           C  
ANISOU  710  CB  ALA B 160     2279   2880   3450   -112    132   -269       C  
ATOM    711  N   ALA B 161     -19.022  12.677  -0.886  1.00 20.12           N  
ANISOU  711  N   ALA B 161     2008   2534   3103   -116    265   -308       N  
ATOM    712  CA  ALA B 161     -19.658  13.868  -0.304  1.00 20.17           C  
ANISOU  712  CA  ALA B 161     1992   2529   3142   -120    334   -323       C  
ATOM    713  C   ALA B 161     -18.649  14.746   0.432  1.00 23.91           C  
ANISOU  713  C   ALA B 161     2500   3013   3570   -100    323   -368       C  
ATOM    714  O   ALA B 161     -18.683  15.981   0.356  1.00 22.04           O  
ANISOU  714  O   ALA B 161     2222   2774   3377    -96    343   -389       O  
ATOM    715  CB  ALA B 161     -20.780  13.455   0.642  1.00 20.81           C  
ANISOU  715  CB  ALA B 161     2106   2587   3214   -138    408   -304       C  
ATOM    716  N   GLU B 162     -17.752  14.093   1.157  1.00 19.16           N  
ANISOU  716  N   GLU B 162     1974   2421   2883    -88    292   -382       N  
ATOM    717  CA  GLU B 162     -16.705  14.767   1.913  1.00 22.05           C  
ANISOU  717  CA  GLU B 162     2382   2802   3195    -70    274   -424       C  
ATOM    718  C   GLU B 162     -15.763  15.533   0.991  1.00 21.20           C  
ANISOU  718  C   GLU B 162     2224   2715   3117    -58    213   -439       C  
ATOM    719  O   GLU B 162     -15.403  16.686   1.256  1.00 25.26           O  
ANISOU  719  O   GLU B 162     2725   3229   3644    -53    219   -471       O  
ATOM    720  CB  GLU B 162     -15.911  13.702   2.667  1.00 32.68           C  
ANISOU  720  CB  GLU B 162     3812   4161   4444    -60    243   -425       C  
ATOM    721  CG  GLU B 162     -15.029  14.194   3.777  1.00 41.97           C  
ANISOU  721  CG  GLU B 162     5046   5353   5548    -46    239   -465       C  
ATOM    722  CD  GLU B 162     -14.336  13.034   4.470  1.00 42.63           C  
ANISOU  722  CD  GLU B 162     5207   5453   5538    -36    211   -455       C  
ATOM    723  OE1 GLU B 162     -14.388  12.958   5.716  1.00 48.48           O  
ANISOU  723  OE1 GLU B 162     6008   6198   6217    -35    249   -469       O  
ATOM    724  OE2 GLU B 162     -13.749  12.189   3.760  1.00 31.06           O  
ANISOU  724  OE2 GLU B 162     3742   3997   4062    -26    152   -433       O  
ATOM    725  N   ASP B 163     -15.361  14.891  -0.097  1.00 19.74           N  
ANISOU  725  N   ASP B 163     2009   2547   2945    -52    153   -414       N  
ATOM    726  CA  ASP B 163     -14.364  15.466  -0.997  1.00 20.32           C  
ANISOU  726  CA  ASP B 163     2036   2648   3036    -36     88   -421       C  
ATOM    727  C   ASP B 163     -14.949  16.576  -1.855  1.00 24.99           C  
ANISOU  727  C   ASP B 163     2536   3235   3725    -44    108   -414       C  
ATOM    728  O   ASP B 163     -14.262  17.542  -2.177  1.00 27.17           O  
ANISOU  728  O   ASP B 163     2775   3524   4023    -35     79   -429       O  
ATOM    729  CB  ASP B 163     -13.725  14.381  -1.873  1.00 18.33           C  
ANISOU  729  CB  ASP B 163     1784   2421   2761    -22     18   -398       C  
ATOM    730  CG  ASP B 163     -12.762  13.480  -1.091  1.00 23.04           C  
ANISOU  730  CG  ASP B 163     2467   3029   3260     -6    -16   -406       C  
ATOM    731  OD1 ASP B 163     -12.548  13.726   0.122  1.00 23.92           O  
ANISOU  731  OD1 ASP B 163     2636   3135   3319     -7     11   -430       O  
ATOM    732  OD2 ASP B 163     -12.223  12.524  -1.700  1.00 27.12           O  
ANISOU  732  OD2 ASP B 163     2992   3562   3750      9    -71   -389       O  
ATOM    733  N   LEU B 164     -16.221  16.442  -2.216  1.00 24.13           N  
ANISOU  733  N   LEU B 164     2387   3107   3675    -62    156   -389       N  
ATOM    734  CA  LEU B 164     -16.913  17.510  -2.924  1.00 21.13           C  
ANISOU  734  CA  LEU B 164     1920   2722   3388    -70    186   -378       C  
ATOM    735  C   LEU B 164     -16.823  18.772  -2.075  1.00 30.28           C  
ANISOU  735  C   LEU B 164     3089   3861   4557    -67    226   -414       C  
ATOM    736  O   LEU B 164     -16.623  19.866  -2.586  1.00 30.92           O  
ANISOU  736  O   LEU B 164     3109   3943   4694    -63    218   -419       O  
ATOM    737  CB  LEU B 164     -18.386  17.153  -3.149  1.00 25.12           C  
ANISOU  737  CB  LEU B 164     2394   3208   3944    -91    244   -346       C  
ATOM    738  CG  LEU B 164     -19.265  18.203  -3.842  1.00 29.76           C  
ANISOU  738  CG  LEU B 164     2895   3789   4624    -98    282   -326       C  
ATOM    739  CD1 LEU B 164     -18.798  18.442  -5.275  1.00 33.39           C  
ANISOU  739  CD1 LEU B 164     3363   4275   5050    -82    202   -279       C  
ATOM    740  CD2 LEU B 164     -20.735  17.803  -3.827  1.00 29.87           C  
ANISOU  740  CD2 LEU B 164     2909   3783   4658   -118    338   -289       C  
ATOM    741  N   ALA B 165     -16.960  18.599  -0.760  1.00 28.31           N  
ANISOU  741  N   ALA B 165     2915   3593   4248    -70    267   -440       N  
ATOM    742  CA  ALA B 165     -17.001  19.720   0.182  1.00 32.69           C  
ANISOU  742  CA  ALA B 165     3489   4127   4806    -68    313   -481       C  
ATOM    743  C   ALA B 165     -15.653  20.411   0.397  1.00 41.18           C  
ANISOU  743  C   ALA B 165     4582   5215   5850    -56    260   -519       C  
ATOM    744  O   ALA B 165     -15.568  21.414   1.114  1.00 43.66           O  
ANISOU  744  O   ALA B 165     4910   5510   6168    -55    289   -559       O  
ATOM    745  CB  ALA B 165     -17.594  19.281   1.513  1.00 33.65           C  
ANISOU  745  CB  ALA B 165     3685   4231   4869    -72    374   -496       C  
ATOM    746  N   ASN B 166     -14.605  19.855  -0.206  1.00 41.87           N  
ANISOU  746  N   ASN B 166     4670   5334   5903    -46    182   -507       N  
ATOM    747  CA  ASN B 166     -13.333  20.552  -0.367  1.00 51.96           C  
ANISOU  747  CA  ASN B 166     5939   6632   7171    -35    122   -529       C  
ATOM    748  C   ASN B 166     -12.261  19.665  -0.981  1.00 53.17           C  
ANISOU  748  C   ASN B 166     6101   6826   7274    -21     40   -508       C  
ATOM    749  O   ASN B 166     -12.027  19.718  -2.188  1.00 56.80           O  
ANISOU  749  O   ASN B 166     6493   7308   7780    -14     -3   -479       O  
ATOM    750  CB  ASN B 166     -12.840  21.148   0.948  1.00 61.23           C  
ANISOU  750  CB  ASN B 166     7179   7794   8291    -36    138   -582       C  
ATOM    751  CG  ASN B 166     -12.504  22.618   0.820  1.00 67.02           C  
ANISOU  751  CG  ASN B 166     7868   8512   9084    -38    134   -609       C  
ATOM    752  OD1 ASN B 166     -12.359  23.135  -0.289  1.00 71.84           O  
ANISOU  752  OD1 ASN B 166     8400   9130   9766    -36    104   -584       O  
ATOM    753  ND2 ASN B 166     -12.378  23.302   1.953  1.00 69.94           N  
ANISOU  753  ND2 ASN B 166     8287   8862   9425    -42    163   -661       N  
TER     754      ASN B 166                                                      
HETATM  755 CA    CA A   1     -11.010  -2.795 -13.016  1.00 27.32          CA  
HETATM  756  O   HOH A   2     -18.078  -3.928  -9.551  1.00 24.82           O  
HETATM  757  O   HOH A   3      -8.856   7.771  -8.383  1.00 21.07           O  
HETATM  758  O   HOH A   4     -14.338  11.413 -14.262  1.00 38.13           O  
HETATM  759  O   HOH A   5      -6.264  -9.987   7.349  1.00 34.37           O  
HETATM  760  O   HOH A   7     -21.539  14.748 -12.062  1.00 34.35           O  
HETATM  761  O   HOH A   8      -7.549  -7.498  -3.617  1.00 35.77           O  
HETATM  762  O   HOH A   9     -24.190  14.028 -12.221  1.00 33.71           O  
HETATM  763  O   HOH A  10     -14.779   4.411 -16.817  1.00 33.04           O  
HETATM  764  O   HOH A  11     -16.699 -10.698  -4.438  1.00 51.79           O  
HETATM  765  O   HOH A  12     -11.366  -1.704 -15.381  1.00 35.54           O  
HETATM  766  O   HOH A  14      -5.690  -7.489   9.654  1.00 45.22           O  
HETATM  767  O   HOH A  15      -7.685  -4.937  -7.478  1.00 37.85           O  
HETATM  768  O   HOH A  16      -9.078 -11.146   0.607  1.00 31.21           O  
HETATM  769  O   HOH A  17      -7.989  -6.968  -6.092  1.00 37.50           O  
HETATM  770  O   HOH A  18     -19.488 -10.381  -6.429  1.00 38.72           O  
HETATM  771  O   HOH A  19     -10.370  -8.844  -8.838  1.00 44.48           O  
HETATM  772  O   HOH A  20     -11.240  -0.420   8.926  1.00 41.01           O  
HETATM  773  O   HOH A  21      -6.332   7.218 -12.432  1.00 33.36           O  
HETATM  774  O   HOH A  22     -31.371   7.152 -12.156  1.00 53.66           O  
HETATM  775  O   HOH A  24     -10.247 -13.371   0.883  1.00 31.96           O  
HETATM  776  O   HOH A  25      -6.700  -7.238 -15.465  1.00 40.08           O  
HETATM  777  O   HOH A  27     -16.967   1.731 -18.191  1.00 43.17           O  
HETATM  778  O   HOH A 153      -8.164   8.818 -10.974  1.00 28.95           O  
HETATM  779  O   HOH B   6     -20.684  17.626  -0.051  1.00 26.09           O  
HETATM  780  O   HOH B  13     -20.407  -9.335   7.275  1.00 46.51           O  
HETATM  781  O   HOH B  23     -19.656  12.997   4.284  1.00 45.55           O  
HETATM  782  O   HOH B  26     -24.627  -9.658   6.136  1.00 29.88           O  
CONECT  410  755                                                                
CONECT  425  755                                                                
CONECT  436  755                                                                
CONECT  444  755                                                                
CONECT  491  755                                                                
CONECT  492  755                                                                
CONECT  755  410  425  436  444                                                 
CONECT  755  491  492  765                                                      
CONECT  765  755                                                                
MASTER      288    0    1    5    2    0    2    6  780    2    9    8          
END                                                                             



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