Welcome to PDBbind-CN database

Browse entries in the PDBbind-CN Database

HEADER    RNA BINDING PROTEIN/RNA                 05-AUG-10   2XNR              
TITLE     STRUCTURAL INSIGHTS INTO CIS ELEMENT RECOGNITION OF NON-              
TITLE    2 POLYADENYLATED RNAS BY THE NAB3-RRM                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEAR POLYADENYLATED RNA-BINDING PROTEIN 3;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RNA RECOGNITION MOTIF, RESIDUES 329-404;                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: 5'-R(*UP*UP*CP*UP*UP*AP*UP*UP*CP*UP*UP*A)-3';              
COMPND   8 CHAIN: C                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;                             
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  13 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  14 ORGANISM_TAXID: 4932                                                 
KEYWDS    RNA BINDING PROTEIN-RNA COMPLEX, TRANSCRIPTION TERMINATION, RNA       
KEYWDS   2 RECOGNITION, RRM, RNA PROCESSING                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.M.LUNDE,M.HORNER,A.MEINHART                                         
REVDAT   3   16-FEB-11 2XNR    1       JRNL                                     
REVDAT   2   15-SEP-10 2XNR    1       JRNL                                     
REVDAT   1   08-SEP-10 2XNR    0                                                
JRNL        AUTH   B.M.LUNDE,M.HORNER,A.MEINHART                                
JRNL        TITL   STRUCTURAL INSIGHTS INTO CIS ELEMENT RECOGNITION OF          
JRNL        TITL 2 NON-POLYADENYLATED RNAS BY THE NAB3-RRM.                     
JRNL        REF    NUCLEIC ACIDS RES.            V.  39   337 2011              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   20805243                                                     
JRNL        DOI    10.1093/NAR/GKQ751                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00                         
REMARK   3   NUMBER OF REFLECTIONS             : 9510                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.16150                         
REMARK   3   R VALUE            (WORKING SET) : 0.16032                         
REMARK   3   FREE R VALUE                     : 0.18420                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 501                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.600                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.642                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 690                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.218                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 36                           
REMARK   3   BIN FREE R VALUE                    : 0.311                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 604                                     
REMARK   3   NUCLEIC ACID ATOMS       : 65                                      
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 47                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.685                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.32                                                 
REMARK   3    B22 (A**2) : 0.32                                                 
REMARK   3    B33 (A**2) : -0.64                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.086         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.083         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.052         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.294         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   692 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):   938 ; 1.252 ; 2.085       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    31 ;37.858 ;25.161       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   119 ;11.191 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ; 8.955 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   104 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   497 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   379 ; 0.695 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   607 ; 1.385 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   313 ; 2.163 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   331 ; 3.434 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   328        A   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3471   7.9607   5.1212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0676 T22:   0.0564                                     
REMARK   3      T33:   0.0521 T12:  -0.0015                                     
REMARK   3      T13:   0.0085 T23:  -0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8918 L22:   2.9275                                     
REMARK   3      L33:   2.0092 L12:  -0.0851                                     
REMARK   3      L13:  -0.1525 L23:  -0.0104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0263 S12:   0.0007 S13:  -0.0291                       
REMARK   3      S21:   0.0216 S22:  -0.0778 S23:  -0.0372                       
REMARK   3      S31:  -0.0090 S32:   0.0574 S33:   0.0515                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     0        C     4                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2540   0.8904   8.9613              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0855 T22:   0.0838                                     
REMARK   3      T33:   0.0882 T12:   0.0334                                     
REMARK   3      T13:   0.0144 T23:  -0.0596                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.0938 L22:   7.7740                                     
REMARK   3      L33:  28.4041 L12:  -0.6189                                     
REMARK   3      L13:  -7.4358 L23:   2.9779                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4745 S12:   0.6839 S13:  -0.8360                       
REMARK   3      S21:   0.1759 S22:   0.2636 S23:  -0.5354                       
REMARK   3      S31:   1.2672 S32:   0.7203 S33:   0.2109                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2XNR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-44978.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978243                           
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PILATUS 6M                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9510                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.3                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.91                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.43                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.26                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2XNQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 85MM SODIUM ACETATE BUFFER PH 4.6,       
REMARK 280  170MM AMMONIUM ACETATE, 25.5% (W/V) PEG 4000, 15% (V/V) GLYCEROL    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.21000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.60500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       61.81500            
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: 1080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 5920 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.5 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   308                                                      
REMARK 465     GLY A   309                                                      
REMARK 465     SER A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     HIS A   312                                                      
REMARK 465     HIS A   313                                                      
REMARK 465     HIS A   314                                                      
REMARK 465     HIS A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     HIS A   317                                                      
REMARK 465     SER A   318                                                      
REMARK 465     SER A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     LEU A   321                                                      
REMARK 465     VAL A   322                                                      
REMARK 465     PRO A   323                                                      
REMARK 465     ARG A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     ALA A   403                                                      
REMARK 465     ARG A   404                                                      
REMARK 465       A C     5                                                      
REMARK 465       U C     6                                                      
REMARK 465       U C     7                                                      
REMARK 465       C C     8                                                      
REMARK 465       U C     9                                                      
REMARK 465       U C    10                                                      
REMARK 465       A C    11                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE A 395    CD1                                                 
REMARK 470       U C   0    O5'  C5'  C4'  O4'  C3'  C2'  O2'  C1'              
REMARK 470       U C   0    N1   C2   O2   N3   C4   O4   C5   C6               
REMARK 470       U C   4    C5'  C4'  O4'  C3'  C2'  O2'  C1'  N1   C2   O2   N3
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 336       48.64   -145.49                                   
REMARK 500    ASN A 364     -117.06     56.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2XNQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL INSIGHTS INTO CIS ELEMENT                                
REMARK 900  RECOGNITION OF NON-POLYADENYLATED RNAS BY                           
REMARK 900  THE NAB3-RRM                                                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE OF NAB3-RRM DOMAIN WITH N-TERMINAL HIS-TAG AND              
REMARK 999 THROMBIN CLEAVAGE SITE                                               
DBREF  2XNR A  329   404  UNP    P38996   NAB3_YEAST     329    404             
DBREF  2XNR C    0    11  PDB    2XNR     2XNR             0     11             
SEQADV 2XNR MET A  308  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR GLY A  309  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR SER A  310  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR SER A  311  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR HIS A  312  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR HIS A  313  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR HIS A  314  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR HIS A  315  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR HIS A  316  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR HIS A  317  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR SER A  318  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR SER A  319  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR GLY A  320  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR LEU A  321  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR VAL A  322  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR PRO A  323  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR ARG A  324  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR GLY A  325  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR SER A  326  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR HIS A  327  UNP  P38996              EXPRESSION TAG                 
SEQADV 2XNR MET A  328  UNP  P38996              EXPRESSION TAG                 
SEQRES   1 A   97  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A   97  LEU VAL PRO ARG GLY SER HIS MET LYS SER ARG LEU PHE          
SEQRES   3 A   97  ILE GLY ASN LEU PRO LEU LYS ASN VAL SER LYS GLU ASP          
SEQRES   4 A   97  LEU PHE ARG ILE PHE SER PRO TYR GLY HIS ILE MET GLN          
SEQRES   5 A   97  ILE ASN ILE LYS ASN ALA PHE GLY PHE ILE GLN PHE ASP          
SEQRES   6 A   97  ASN PRO GLN SER VAL ARG ASP ALA ILE GLU CYS GLU SER          
SEQRES   7 A   97  GLN GLU MET ASN PHE GLY LYS LYS LEU ILE LEU GLU VAL          
SEQRES   8 A   97  SER SER SER ASN ALA ARG                                      
SEQRES   1 C   12    U   U   C   U   U   A   U   U   C   U   U   A              
HET    ACT  A1000       4                                                       
HET    ACT  A1001       4                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   3  ACT    2(C2 H3 O2 1-)                                               
FORMUL   4  HOH   *47(H2 O)                                                     
HELIX    1   1 SER A  343  SER A  352  1                                  10    
HELIX    2   2 PRO A  353  GLY A  355  5                                   3    
HELIX    3   3 ASN A  373  SER A  385  1                                  13    
SHEET    1  AA 4 ILE A 357  LYS A 363  0                                        
SHEET    2  AA 4 PHE A 366  PHE A 371 -1  O  PHE A 366   N  LYS A 363           
SHEET    3  AA 4 ARG A 331  ILE A 334 -1  O  LEU A 332   N  ILE A 369           
SHEET    4  AA 4 LEU A 396  VAL A 398 -1  O  GLU A 397   N  PHE A 333           
SITE     1 AC1  3 LYS A 329  ILE A 360  HOH A2047                               
SITE     1 AC2  4 LYS A 329  SER A 330  ARG A 331  GLN A 370                    
CRYST1   30.640   30.640   82.420  90.00  90.00  90.00 P 41          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      0.032637  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.032637  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012133        0.00000                         
ATOM      1  N   MET A 328      23.789  17.566   5.899  1.00 38.87           N  
ANISOU    1  N   MET A 328     4285   4953   5530   -940    -69    201       N  
ATOM      2  CA  MET A 328      23.400  16.282   6.556  1.00 37.31           C  
ANISOU    2  CA  MET A 328     4075   4810   5289   -815   -152    191       C  
ATOM      3  C   MET A 328      22.091  16.437   7.330  1.00 34.80           C  
ANISOU    3  C   MET A 328     3962   4439   4823   -776   -217    148       C  
ATOM      4  O   MET A 328      21.572  17.545   7.459  1.00 36.08           O  
ANISOU    4  O   MET A 328     4262   4524   4924   -839   -215    123       O  
ATOM      5  CB  MET A 328      24.533  15.763   7.458  1.00 39.69           C  
ANISOU    5  CB  MET A 328     4198   5182   5701   -843   -294    200       C  
ATOM      6  CG  MET A 328      24.776  16.556   8.753  1.00 42.79           C  
ANISOU    6  CG  MET A 328     4637   5546   6077   -962   -476    166       C  
ATOM      7  SD  MET A 328      25.578  15.555  10.037  1.00 50.91           S  
ANISOU    7  SD  MET A 328     5537   6652   7156   -926   -692    172       S  
ATOM      8  CE  MET A 328      24.374  14.245  10.310  1.00 47.72           C  
ANISOU    8  CE  MET A 328     5278   6248   6606   -744   -671    172       C  
ATOM      9  N   LYS A 329      21.557  15.328   7.833  1.00 31.33           N  
ANISOU    9  N   LYS A 329     3544   4031   4328   -669   -261    141       N  
ATOM     10  CA  LYS A 329      20.295  15.319   8.577  1.00 27.13           C  
ANISOU   10  CA  LYS A 329     3187   3455   3666   -625   -298    104       C  
ATOM     11  C   LYS A 329      19.074  15.544   7.687  1.00 22.92           C  
ANISOU   11  C   LYS A 329     2767   2879   3063   -564   -178     94       C  
ATOM     12  O   LYS A 329      17.981  15.758   8.201  1.00 22.14           O  
ANISOU   12  O   LYS A 329     2799   2738   2874   -535   -188     62       O  
ATOM     13  CB  LYS A 329      20.289  16.372   9.696  1.00 28.59           C  
ANISOU   13  CB  LYS A 329     3478   3585   3801   -724   -405     67       C  
ATOM     14  CG  LYS A 329      21.082  16.055  10.953  1.00 31.31           C  
ANISOU   14  CG  LYS A 329     3779   3960   4155   -766   -572     62       C  
ATOM     15  CD  LYS A 329      20.806  17.147  11.981  1.00 36.03           C  
ANISOU   15  CD  LYS A 329     4543   4482   4664   -855   -659     11       C  
ATOM     16  CE  LYS A 329      21.312  16.780  13.355  1.00 39.38           C  
ANISOU   16  CE  LYS A 329     4991   4925   5047   -881   -839     -1       C  
ATOM     17  NZ  LYS A 329      22.804  16.906  13.478  1.00 43.19           N  
ANISOU   17  NZ  LYS A 329     5294   5457   5660   -978   -970     18       N  
ATOM     18  N   SER A 330      19.240  15.472   6.366  1.00 19.90           N  
ANISOU   18  N   SER A 330     2335   2507   2720   -540    -67    121       N  
ATOM     19  CA  SER A 330      18.110  15.688   5.451  1.00 16.98           C  
ANISOU   19  CA  SER A 330     2075   2097   2280   -479     22    114       C  
ATOM     20  C   SER A 330      17.513  14.384   4.902  1.00 14.95           C  
ANISOU   20  C   SER A 330     1804   1877   1999   -368     63    116       C  
ATOM     21  O   SER A 330      16.662  14.427   4.014  1.00 13.72           O  
ANISOU   21  O   SER A 330     1721   1698   1794   -316    122    111       O  
ATOM     22  CB  SER A 330      18.514  16.595   4.274  1.00 17.30           C  
ANISOU   22  CB  SER A 330     2129   2102   2343   -527    118    142       C  
ATOM     23  OG  SER A 330      18.901  17.883   4.723  1.00 20.76           O  
ANISOU   23  OG  SER A 330     2610   2483   2797   -638     86    137       O  
ATOM     24  N   ARG A 331      17.909  13.248   5.475  1.00 14.61           N  
ANISOU   24  N   ARG A 331     1682   1883   1986   -332     18    121       N  
ATOM     25  CA  ARG A 331      17.365  11.950   5.077  1.00 13.87           C  
ANISOU   25  CA  ARG A 331     1589   1809   1872   -236     51    118       C  
ATOM     26  C   ARG A 331      16.544  11.339   6.211  1.00 12.48           C  
ANISOU   26  C   ARG A 331     1470   1626   1646   -208    -17     96       C  
ATOM     27  O   ARG A 331      16.971  11.355   7.372  1.00 13.10           O  
ANISOU   27  O   ARG A 331     1539   1712   1726   -241   -100     98       O  
ATOM     28  CB  ARG A 331      18.498  11.014   4.689  1.00 15.38           C  
ANISOU   28  CB  ARG A 331     1655   2046   2141   -202     79    147       C  
ATOM     29  CG  ARG A 331      18.043   9.718   4.030  1.00 18.93           C  
ANISOU   29  CG  ARG A 331     2125   2499   2569   -106    132    141       C  
ATOM     30  CD  ARG A 331      19.226   8.750   3.822  1.00 25.79           C  
ANISOU   30  CD  ARG A 331     2873   3405   3523    -55    160    169       C  
ATOM     31  NE  ARG A 331      20.357   9.363   3.138  1.00 32.70           N  
ANISOU   31  NE  ARG A 331     3646   4304   4476    -92    232    195       N  
ATOM     32  CZ  ARG A 331      20.600   9.262   1.831  0.80 37.32           C  
ANISOU   32  CZ  ARG A 331     4233   4883   5061    -60    364    202       C  
ATOM     33  NH1 ARG A 331      19.779   8.568   1.044  1.00 38.89           N  
ANISOU   33  NH1 ARG A 331     4543   5053   5180     10    417    179       N  
ATOM     34  NH2 ARG A 331      21.670   9.860   1.304  1.00 40.96           N  
ANISOU   34  NH2 ARG A 331     4594   5365   5602   -106    447    231       N  
ATOM     35  N   LEU A 332      15.364  10.831   5.864  1.00 10.50           N  
ANISOU   35  N   LEU A 332     1282   1359   1347   -154     18     75       N  
ATOM     36  CA  LEU A 332      14.506  10.136   6.800  1.00 10.25           C  
ANISOU   36  CA  LEU A 332     1301   1318   1276   -130    -12     57       C  
ATOM     37  C   LEU A 332      14.719   8.624   6.690  1.00 10.84           C  
ANISOU   37  C   LEU A 332     1340   1407   1370    -75     -6     71       C  
ATOM     38  O   LEU A 332      14.771   8.080   5.594  1.00 10.96           O  
ANISOU   38  O   LEU A 332     1334   1427   1404    -35     46     72       O  
ATOM     39  CB  LEU A 332      13.030  10.495   6.503  1.00  9.99           C  
ANISOU   39  CB  LEU A 332     1337   1257   1202   -113     24     24       C  
ATOM     40  CG  LEU A 332      11.966   9.699   7.251  1.00 10.01           C  
ANISOU   40  CG  LEU A 332     1377   1248   1178    -92     27      5       C  
ATOM     41  CD1 LEU A 332      11.905  10.151   8.705  1.00 12.11           C  
ANISOU   41  CD1 LEU A 332     1702   1497   1403   -126     -3     -1       C  
ATOM     42  CD2 LEU A 332      10.629   9.924   6.583  1.00  9.35           C  
ANISOU   42  CD2 LEU A 332     1311   1151   1091    -66     63    -24       C  
ATOM     43  N   PHE A 333      14.862   7.962   7.837  1.00 10.13           N  
ANISOU   43  N   PHE A 333     1268   1315   1267    -70    -59     83       N  
ATOM     44  CA  PHE A 333      14.948   6.496   7.922  1.00 10.52           C  
ANISOU   44  CA  PHE A 333     1314   1357   1325    -14    -57     99       C  
ATOM     45  C   PHE A 333      13.603   5.897   8.331  1.00 10.61           C  
ANISOU   45  C   PHE A 333     1412   1331   1287    -11    -28     78       C  
ATOM     46  O   PHE A 333      12.929   6.398   9.245  1.00 10.47           O  
ANISOU   46  O   PHE A 333     1456   1299   1222    -47    -37     66       O  
ATOM     47  CB  PHE A 333      16.002   6.106   8.962  1.00 11.26           C  
ANISOU   47  CB  PHE A 333     1382   1463   1433     -4   -143    137       C  
ATOM     48  CG  PHE A 333      16.050   4.637   9.264  1.00 12.89           C  
ANISOU   48  CG  PHE A 333     1616   1644   1638     60   -150    160       C  
ATOM     49  CD1 PHE A 333      16.484   3.723   8.299  1.00 12.97           C  
ANISOU   49  CD1 PHE A 333     1575   1651   1704    128   -101    169       C  
ATOM     50  CD2 PHE A 333      15.675   4.164  10.518  1.00 14.96           C  
ANISOU   50  CD2 PHE A 333     1976   1874   1835     57   -197    176       C  
ATOM     51  CE1 PHE A 333      16.549   2.355   8.586  1.00 13.86           C  
ANISOU   51  CE1 PHE A 333     1729   1721   1815    193   -107    191       C  
ATOM     52  CE2 PHE A 333      15.735   2.794  10.810  1.00 14.24           C  
ANISOU   52  CE2 PHE A 333     1930   1742   1738    116   -202    206       C  
ATOM     53  CZ  PHE A 333      16.186   1.895   9.833  1.00 14.22           C  
ANISOU   53  CZ  PHE A 333     1871   1732   1801    186   -161    213       C  
ATOM     54  N   ILE A 334      13.203   4.830   7.638  1.00  9.92           N  
ANISOU   54  N   ILE A 334     1331   1224   1214     26     14     71       N  
ATOM     55  CA  ILE A 334      12.019   4.063   8.000  1.00 10.85           C  
ANISOU   55  CA  ILE A 334     1513   1302   1306     16     44     54       C  
ATOM     56  C   ILE A 334      12.494   2.653   8.325  1.00 11.38           C  
ANISOU   56  C   ILE A 334     1611   1334   1379     57     36     84       C  
ATOM     57  O   ILE A 334      13.109   2.010   7.488  1.00 11.82           O  
ANISOU   57  O   ILE A 334     1638   1383   1470    106     48     88       O  
ATOM     58  CB  ILE A 334      10.978   4.017   6.858  1.00 10.82           C  
ANISOU   58  CB  ILE A 334     1503   1292   1318     11     88     12       C  
ATOM     59  CG1 ILE A 334      10.650   5.433   6.364  1.00 11.71           C  
ANISOU   59  CG1 ILE A 334     1589   1434   1427     -6     87     -8       C  
ATOM     60  CG2 ILE A 334       9.721   3.300   7.338  1.00 11.64           C  
ANISOU   60  CG2 ILE A 334     1647   1358   1417    -19    119     -6       C  
ATOM     61  CD1 ILE A 334       9.898   5.494   5.029  1.00 14.19           C  
ANISOU   61  CD1 ILE A 334     1895   1747   1750      5    101    -42       C  
ATOM     62  N   GLY A 335      12.209   2.180   9.535  1.00 11.88           N  
ANISOU   62  N   GLY A 335     1749   1363   1401     42     24    106       N  
ATOM     63  CA  GLY A 335      12.842   0.952  10.035  1.00 12.53           C  
ANISOU   63  CA  GLY A 335     1880   1403   1480     91     -3    149       C  
ATOM     64  C   GLY A 335      12.082  -0.356   9.897  1.00 13.37           C  
ANISOU   64  C   GLY A 335     2060   1435   1585     91     53    145       C  
ATOM     65  O   GLY A 335      12.648  -1.426  10.141  1.00 15.17           O  
ANISOU   65  O   GLY A 335     2337   1612   1813    144     36    181       O  
ATOM     66  N   ASN A 336      10.803  -0.272   9.538  1.00 12.71           N  
ANISOU   66  N   ASN A 336     1982   1340   1506     31    114    102       N  
ATOM     67  CA  ASN A 336       9.933  -1.447   9.567  1.00 13.36           C  
ANISOU   67  CA  ASN A 336     2135   1347   1595      0    167     94       C  
ATOM     68  C   ASN A 336       8.891  -1.463   8.457  1.00 12.77           C  
ANISOU   68  C   ASN A 336     2013   1273   1565    -45    203     33       C  
ATOM     69  O   ASN A 336       7.713  -1.738   8.695  1.00 14.50           O  
ANISOU   69  O   ASN A 336     2245   1464   1801   -115    250     12       O  
ATOM     70  CB  ASN A 336       9.258  -1.592  10.946  1.00 13.59           C  
ANISOU   70  CB  ASN A 336     2252   1338   1572    -52    206    122       C  
ATOM     71  CG  ASN A 336       8.330  -0.420  11.278  1.00 12.67           C  
ANISOU   71  CG  ASN A 336     2094   1272   1449   -109    246     90       C  
ATOM     72  OD1 ASN A 336       8.438   0.661  10.704  1.00 12.78           O  
ANISOU   72  OD1 ASN A 336     2024   1348   1482    -98    218     62       O  
ATOM     73  ND2 ASN A 336       7.420  -0.643  12.221  1.00 15.94           N  
ANISOU   73  ND2 ASN A 336     2575   1648   1835   -165    323     99       N  
ATOM     74  N   LEU A 337       9.324  -1.221   7.230  1.00 12.51           N  
ANISOU   74  N   LEU A 337     1928   1270   1555     -7    179      5       N  
ATOM     75  CA  LEU A 337       8.414  -1.396   6.096  1.00 12.53           C  
ANISOU   75  CA  LEU A 337     1912   1263   1586    -42    186    -53       C  
ATOM     76  C   LEU A 337       7.990  -2.856   5.991  1.00 13.61           C  
ANISOU   76  C   LEU A 337     2127   1307   1737    -70    210    -66       C  
ATOM     77  O   LEU A 337       8.776  -3.755   6.317  1.00 14.55           O  
ANISOU   77  O   LEU A 337     2318   1368   1842    -23    218    -31       O  
ATOM     78  CB  LEU A 337       9.084  -1.015   4.800  1.00 12.49           C  
ANISOU   78  CB  LEU A 337     1881   1290   1576     12    164    -74       C  
ATOM     79  CG  LEU A 337       9.475   0.461   4.628  1.00 12.03           C  
ANISOU   79  CG  LEU A 337     1754   1311   1507     29    146    -66       C  
ATOM     80  CD1 LEU A 337      10.339   0.587   3.387  1.00 13.39           C  
ANISOU   80  CD1 LEU A 337     1923   1496   1667     85    151    -75       C  
ATOM     81  CD2 LEU A 337       8.220   1.332   4.552  1.00 14.20           C  
ANISOU   81  CD2 LEU A 337     1987   1615   1792    -23    134    -99       C  
ATOM     82  N   PRO A 338       6.752  -3.100   5.526  1.00 14.38           N  
ANISOU   82  N   PRO A 338     2209   1384   1869   -147    214   -116       N  
ATOM     83  CA  PRO A 338       6.401  -4.470   5.109  1.00 14.86           C  
ANISOU   83  CA  PRO A 338     2350   1348   1948   -184    224   -143       C  
ATOM     84  C   PRO A 338       7.429  -4.972   4.099  1.00 15.19           C  
ANISOU   84  C   PRO A 338     2456   1358   1958    -99    206   -157       C  
ATOM     85  O   PRO A 338       8.032  -4.176   3.373  1.00 14.76           O  
ANISOU   85  O   PRO A 338     2359   1367   1881    -39    184   -164       O  
ATOM     86  CB  PRO A 338       5.038  -4.302   4.449  1.00 16.72           C  
ANISOU   86  CB  PRO A 338     2521   1599   2234   -274    197   -207       C  
ATOM     87  CG  PRO A 338       4.465  -3.058   5.076  1.00 16.21           C  
ANISOU   87  CG  PRO A 338     2347   1621   2191   -291    208   -195       C  
ATOM     88  CD  PRO A 338       5.636  -2.150   5.341  1.00 14.63           C  
ANISOU   88  CD  PRO A 338     2145   1477   1935   -201    202   -152       C  
ATOM     89  N   LEU A 339       7.632  -6.285   4.046  1.00 15.85           N  
ANISOU   89  N   LEU A 339     2649   1333   2040    -92    228   -159       N  
ATOM     90  CA  LEU A 339       8.674  -6.857   3.195  1.00 17.13           C  
ANISOU   90  CA  LEU A 339     2884   1452   2174      7    234   -169       C  
ATOM     91  C   LEU A 339       8.208  -7.096   1.763  1.00 17.92           C  
ANISOU   91  C   LEU A 339     3031   1523   2256    -18    208   -251       C  
ATOM     92  O   LEU A 339       9.015  -7.449   0.899  1.00 19.86           O  
ANISOU   92  O   LEU A 339     3346   1736   2465     67    228   -271       O  
ATOM     93  CB  LEU A 339       9.175  -8.180   3.799  1.00 17.47           C  
ANISOU   93  CB  LEU A 339     3045   1374   2218     47    270   -132       C  
ATOM     94  CG  LEU A 339      10.194  -8.058   4.928  1.00 20.78           C  
ANISOU   94  CG  LEU A 339     3448   1814   2633    133    275    -46       C  
ATOM     95  CD1 LEU A 339      11.361  -7.187   4.473  1.00 19.59           C  
ANISOU   95  CD1 LEU A 339     3201   1760   2482    237    262    -32       C  
ATOM     96  CD2 LEU A 339       9.586  -7.494   6.201  1.00 22.60           C  
ANISOU   96  CD2 LEU A 339     3639   2087   2861     58    271     -3       C  
ATOM     97  N   LYS A 340       6.903  -6.977   1.534  1.00 18.05           N  
ANISOU   97  N   LYS A 340     3016   1545   2296   -132    165   -300       N  
ATOM     98  CA  LYS A 340       6.336  -7.060   0.188  1.00 19.42           C  
ANISOU   98  CA  LYS A 340     3230   1704   2445   -166    105   -381       C  
ATOM     99  C   LYS A 340       5.254  -6.017   0.020  1.00 19.33           C  
ANISOU   99  C   LYS A 340     3095   1786   2465   -237     37   -405       C  
ATOM    100  O   LYS A 340       4.719  -5.502   1.006  1.00 19.42           O  
ANISOU  100  O   LYS A 340     3000   1847   2532   -282     53   -370       O  
ATOM    101  CB  LYS A 340       5.703  -8.425  -0.065  1.00 21.00           C  
ANISOU  101  CB  LYS A 340     3547   1772   2661   -248     94   -435       C  
ATOM    102  CG  LYS A 340       6.574  -9.592   0.238  1.00 22.08           C  
ANISOU  102  CG  LYS A 340     3819   1790   2780   -184    163   -410       C  
ATOM    103  CD  LYS A 340       5.869 -10.837  -0.161  1.00 21.36           C  
ANISOU  103  CD  LYS A 340     3857   1559   2699   -279    144   -475       C  
ATOM    104  CE  LYS A 340       6.131 -11.167  -1.615  1.00 20.89           C  
ANISOU  104  CE  LYS A 340     3925   1448   2563   -237    110   -556       C  
ATOM    105  NZ  LYS A 340       5.482 -12.443  -1.988  1.00 20.70           N  
ANISOU  105  NZ  LYS A 340     4053   1269   2545   -337     83   -627       N  
ATOM    106  N   ASN A 341       4.923  -5.732  -1.238  1.00 19.81           N  
ANISOU  106  N   ASN A 341     3182   1862   2483   -239    -38   -465       N  
ATOM    107  CA  ASN A 341       3.792  -4.864  -1.570  1.00 20.28           C  
ANISOU  107  CA  ASN A 341     3133   1996   2576   -299   -130   -496       C  
ATOM    108  C   ASN A 341       3.982  -3.437  -1.053  1.00 18.52           C  
ANISOU  108  C   ASN A 341     2791   1884   2363   -247   -111   -440       C  
ATOM    109  O   ASN A 341       3.048  -2.834  -0.546  1.00 19.06           O  
ANISOU  109  O   ASN A 341     2736   2004   2502   -296   -136   -437       O  
ATOM    110  CB  ASN A 341       2.475  -5.468  -1.052  1.00 21.59           C  
ANISOU  110  CB  ASN A 341     3229   2129   2846   -433   -161   -526       C  
ATOM    111  CG  ASN A 341       1.248  -4.917  -1.767  1.00 25.46           C  
ANISOU  111  CG  ASN A 341     3623   2673   3379   -495   -288   -581       C  
ATOM    112  OD1 ASN A 341       1.255  -4.709  -2.983  1.00 29.72           O  
ANISOU  112  OD1 ASN A 341     4231   3217   3846   -465   -385   -627       O  
ATOM    113  ND2 ASN A 341       0.185  -4.691  -1.014  1.00 28.79           N  
ANISOU  113  ND2 ASN A 341     3889   3132   3918   -576   -287   -576       N  
ATOM    114  N   VAL A 342       5.200  -2.925  -1.187  1.00 17.08           N  
ANISOU  114  N   VAL A 342     2644   1728   2117   -149    -61   -400       N  
ATOM    115  CA  VAL A 342       5.540  -1.537  -0.830  1.00 15.78           C  
ANISOU  115  CA  VAL A 342     2392   1653   1949   -102    -46   -351       C  
ATOM    116  C   VAL A 342       6.244  -0.911  -2.027  1.00 15.50           C  
ANISOU  116  C   VAL A 342     2422   1639   1827    -30    -57   -356       C  
ATOM    117  O   VAL A 342       7.250  -1.449  -2.489  1.00 17.62           O  
ANISOU  117  O   VAL A 342     2780   1870   2046     25     -1   -354       O  
ATOM    118  CB  VAL A 342       6.489  -1.478   0.403  1.00 15.13           C  
ANISOU  118  CB  VAL A 342     2282   1581   1885    -67     38   -284       C  
ATOM    119  CG1 VAL A 342       6.900  -0.042   0.695  1.00 14.37           C  
ANISOU  119  CG1 VAL A 342     2115   1564   1780    -30     46   -244       C  
ATOM    120  CG2 VAL A 342       5.815  -2.075   1.635  1.00 16.50           C  
ANISOU  120  CG2 VAL A 342     2423   1725   2122   -136     64   -271       C  
ATOM    121  N   SER A 343       5.728   0.204  -2.540  1.00 13.94           N  
ANISOU  121  N   SER A 343     2188   1495   1611    -24   -118   -361       N  
ATOM    122  CA  SER A 343       6.398   0.888  -3.655  1.00 13.45           C  
ANISOU  122  CA  SER A 343     2208   1447   1454     41   -115   -355       C  
ATOM    123  C   SER A 343       6.987   2.220  -3.233  1.00 12.42           C  
ANISOU  123  C   SER A 343     2015   1376   1329     76    -71   -295       C  
ATOM    124  O   SER A 343       6.570   2.801  -2.246  1.00 12.12           O  
ANISOU  124  O   SER A 343     1875   1373   1356     53    -76   -272       O  
ATOM    125  CB  SER A 343       5.442   1.139  -4.830  1.00 14.33           C  
ANISOU  125  CB  SER A 343     2377   1555   1511     30   -234   -404       C  
ATOM    126  OG  SER A 343       4.415   2.040  -4.448  1.00 14.11           O  
ANISOU  126  OG  SER A 343     2235   1580   1547      8   -310   -397       O  
ATOM    127  N   LYS A 344       7.918   2.720  -4.037  1.00 12.88           N  
ANISOU  127  N   LYS A 344     2145   1438   1312    129    -22   -274       N  
ATOM    128  CA  LYS A 344       8.445   4.066  -3.830  1.00 13.04           C  
ANISOU  128  CA  LYS A 344     2123   1501   1330    148     13   -221       C  
ATOM    129  C   LYS A 344       7.309   5.076  -3.920  1.00 13.35           C  
ANISOU  129  C   LYS A 344     2134   1563   1374    137    -80   -227       C  
ATOM    130  O   LYS A 344       7.291   6.054  -3.173  1.00 13.40           O  
ANISOU  130  O   LYS A 344     2070   1598   1423    134    -70   -193       O  
ATOM    131  CB  LYS A 344       9.530   4.392  -4.858  1.00 13.81           C  
ANISOU  131  CB  LYS A 344     2314   1588   1345    195     92   -200       C  
ATOM    132  CG  LYS A 344      10.790   3.580  -4.665  1.00 15.48           C  
ANISOU  132  CG  LYS A 344     2516   1786   1578    223    203   -185       C  
ATOM    133  CD  LYS A 344      11.830   3.959  -5.707  1.00 20.39           C  
ANISOU  133  CD  LYS A 344     3216   2402   2129    267    307   -163       C  
ATOM    134  CE  LYS A 344      13.144   3.257  -5.462  1.00 23.66           C  
ANISOU  134  CE  LYS A 344     3584   2813   2594    307    426   -142       C  
ATOM    135  NZ  LYS A 344      14.235   3.926  -6.241  1.00 26.81           N  
ANISOU  135  NZ  LYS A 344     4006   3221   2958    335    552   -106       N  
ATOM    136  N   GLU A 345       6.357   4.840  -4.818  1.00 14.36           N  
ANISOU  136  N   GLU A 345     2319   1674   1461    137   -179   -271       N  
ATOM    137  CA  GLU A 345       5.197   5.733  -4.917  1.00 15.96           C  
ANISOU  137  CA  GLU A 345     2477   1901   1686    142   -285   -276       C  
ATOM    138  C   GLU A 345       4.350   5.780  -3.654  1.00 14.57           C  
ANISOU  138  C   GLU A 345     2148   1752   1634    105   -298   -281       C  
ATOM    139  O   GLU A 345       3.867   6.861  -3.290  1.00 14.86           O  
ANISOU  139  O   GLU A 345     2126   1814   1707    128   -319   -260       O  
ATOM    140  CB  GLU A 345       4.322   5.390  -6.117  1.00 17.68           C  
ANISOU  140  CB  GLU A 345     2776   2099   1843    147   -417   -325       C  
ATOM    141  CG  GLU A 345       4.894   5.879  -7.439  1.00 24.15           C  
ANISOU  141  CG  GLU A 345     3770   2892   2515    200   -420   -310       C  
ATOM    142  CD  GLU A 345       3.843   6.408  -8.431  1.00 30.04           C  
ANISOU  142  CD  GLU A 345     4581   3635   3200    230   -586   -329       C  
ATOM    143  OE1 GLU A 345       2.655   6.601  -8.061  1.00 32.13           O  
ANISOU  143  OE1 GLU A 345     4721   3928   3559    220   -703   -349       O  
ATOM    144  OE2 GLU A 345       4.224   6.638  -9.600  1.00 33.39           O  
ANISOU  144  OE2 GLU A 345     5184   4026   3477    270   -599   -322       O  
ATOM    145  N   ASP A 346       4.158   4.634  -2.994  1.00 14.45           N  
ANISOU  145  N   ASP A 346     2084   1725   1680     52   -275   -306       N  
ATOM    146  CA  ASP A 346       3.473   4.594  -1.696  1.00 13.93           C  
ANISOU  146  CA  ASP A 346     1891   1678   1722     12   -249   -304       C  
ATOM    147  C   ASP A 346       4.181   5.552  -0.744  1.00 13.30           C  
ANISOU  147  C   ASP A 346     1787   1621   1647     36   -167   -253       C  
ATOM    148  O   ASP A 346       3.532   6.366  -0.081  1.00 12.67           O  
ANISOU  148  O   ASP A 346     1633   1563   1619     42   -166   -246       O  
ATOM    149  CB  ASP A 346       3.510   3.195  -1.051  1.00 14.30           C  
ANISOU  149  CB  ASP A 346     1930   1692   1811    -49   -203   -321       C  
ATOM    150  CG  ASP A 346       2.646   2.167  -1.755  1.00 16.42           C  
ANISOU  150  CG  ASP A 346     2212   1928   2100   -101   -284   -380       C  
ATOM    151  OD1 ASP A 346       2.995   0.960  -1.638  1.00 16.67           O  
ANISOU  151  OD1 ASP A 346     2301   1907   2126   -137   -247   -395       O  
ATOM    152  OD2 ASP A 346       1.612   2.528  -2.380  1.00 19.13           O  
ANISOU  152  OD2 ASP A 346     2508   2292   2469   -107   -392   -413       O  
ATOM    153  N   LEU A 347       5.508   5.433  -0.663  1.00 12.40           N  
ANISOU  153  N   LEU A 347     1730   1496   1484     49    -99   -221       N  
ATOM    154  CA  LEU A 347       6.290   6.250   0.259  1.00 11.74           C  
ANISOU  154  CA  LEU A 347     1626   1430   1406     56    -38   -177       C  
ATOM    155  C   LEU A 347       6.230   7.713  -0.141  1.00 11.83           C  
ANISOU  155  C   LEU A 347     1652   1451   1391     89    -58   -159       C  
ATOM    156  O   LEU A 347       6.106   8.595   0.720  1.00 11.74           O  
ANISOU  156  O   LEU A 347     1606   1447   1406     87    -39   -143       O  
ATOM    157  CB  LEU A 347       7.736   5.751   0.359  1.00 11.95           C  
ANISOU  157  CB  LEU A 347     1685   1447   1406     63     24   -148       C  
ATOM    158  CG  LEU A 347       7.883   4.353   0.976  1.00 12.44           C  
ANISOU  158  CG  LEU A 347     1744   1485   1496     43     48   -154       C  
ATOM    159  CD1 LEU A 347       9.368   3.997   0.986  1.00 13.58           C  
ANISOU  159  CD1 LEU A 347     1907   1626   1626     74    100   -121       C  
ATOM    160  CD2 LEU A 347       7.288   4.300   2.379  1.00 15.95           C  
ANISOU  160  CD2 LEU A 347     2139   1934   1989      5     59   -148       C  
ATOM    161  N   PHE A 348       6.286   7.976  -1.440  1.00 12.10           N  
ANISOU  161  N   PHE A 348     1759   1475   1364    121    -95   -161       N  
ATOM    162  CA  PHE A 348       6.126   9.328  -1.928  1.00 12.76           C  
ANISOU  162  CA  PHE A 348     1882   1553   1414    158   -121   -139       C  
ATOM    163  C   PHE A 348       4.793   9.945  -1.503  1.00 13.04           C  
ANISOU  163  C   PHE A 348     1847   1597   1509    178   -182   -156       C  
ATOM    164  O   PHE A 348       4.762  11.079  -1.038  1.00 12.74           O  
ANISOU  164  O   PHE A 348     1807   1551   1484    199   -164   -135       O  
ATOM    165  CB  PHE A 348       6.275   9.394  -3.444  1.00 13.52           C  
ANISOU  165  CB  PHE A 348     2092   1628   1415    192   -157   -138       C  
ATOM    166  CG  PHE A 348       6.085  10.762  -3.969  1.00 13.31           C  
ANISOU  166  CG  PHE A 348     2130   1583   1345    234   -187   -107       C  
ATOM    167  CD1 PHE A 348       7.163  11.634  -4.034  1.00 14.28           C  
ANISOU  167  CD1 PHE A 348     2311   1684   1428    228   -104    -58       C  
ATOM    168  CD2 PHE A 348       4.822  11.212  -4.332  1.00 14.49           C  
ANISOU  168  CD2 PHE A 348     2271   1730   1504    279   -299   -123       C  
ATOM    169  CE1 PHE A 348       6.996  12.927  -4.478  1.00 14.84           C  
ANISOU  169  CE1 PHE A 348     2461   1721   1458    262   -124    -25       C  
ATOM    170  CE2 PHE A 348       4.647  12.512  -4.781  1.00 15.94           C  
ANISOU  170  CE2 PHE A 348     2527   1883   1646    332   -330    -87       C  
ATOM    171  CZ  PHE A 348       5.741  13.365  -4.851  1.00 14.26           C  
ANISOU  171  CZ  PHE A 348     2399   1636   1381    321   -238    -37       C  
ATOM    172  N   ARG A 349       3.696   9.208  -1.643  1.00 13.89           N  
ANISOU  172  N   ARG A 349     1894   1718   1665    171   -250   -198       N  
ATOM    173  CA  ARG A 349       2.383   9.741  -1.253  1.00 14.87           C  
ANISOU  173  CA  ARG A 349     1920   1857   1872    196   -299   -216       C  
ATOM    174  C   ARG A 349       2.315  10.090   0.233  1.00 14.44           C  
ANISOU  174  C   ARG A 349     1795   1810   1883    180   -207   -208       C  
ATOM    175  O   ARG A 349       1.698  11.094   0.617  1.00 15.48           O  
ANISOU  175  O   ARG A 349     1890   1939   2055    225   -205   -204       O  
ATOM    176  CB  ARG A 349       1.259   8.769  -1.644  1.00 16.17           C  
ANISOU  176  CB  ARG A 349     2008   2039   2098    171   -387   -264       C  
ATOM    177  CG  ARG A 349       0.964   8.734  -3.132  1.00 20.88           C  
ANISOU  177  CG  ARG A 349     2680   2627   2627    205   -518   -280       C  
ATOM    178  CD  ARG A 349      -0.146   7.723  -3.411  1.00 28.25           C  
ANISOU  178  CD  ARG A 349     3525   3575   3635    159   -618   -337       C  
ATOM    179  NE  ARG A 349      -0.190   7.305  -4.808  1.00 35.50           N  
ANISOU  179  NE  ARG A 349     4555   4474   4460    165   -743   -363       N  
ATOM    180  CZ  ARG A 349       0.261   6.141  -5.275  1.00 37.02           C  
ANISOU  180  CZ  ARG A 349     4836   4637   4593    112   -740   -395       C  
ATOM    181  NH1 ARG A 349       0.803   5.248  -4.458  1.00 37.53           N  
ANISOU  181  NH1 ARG A 349     4881   4688   4691     52   -624   -398       N  
ATOM    182  NH2 ARG A 349       0.160   5.866  -6.574  1.00 40.44           N  
ANISOU  182  NH2 ARG A 349     5395   5045   4924    124   -859   -424       N  
ATOM    183  N   ILE A 350       2.953   9.276   1.067  1.00 13.23           N  
ANISOU  183  N   ILE A 350     1638   1656   1731    122   -131   -204       N  
ATOM    184  CA  ILE A 350       2.933   9.501   2.500  1.00 12.38           C  
ANISOU  184  CA  ILE A 350     1497   1549   1660    102    -48   -197       C  
ATOM    185  C   ILE A 350       3.780  10.727   2.872  1.00 12.16           C  
ANISOU  185  C   ILE A 350     1537   1502   1581    123    -14   -166       C  
ATOM    186  O   ILE A 350       3.365  11.562   3.688  1.00 13.08           O  
ANISOU  186  O   ILE A 350     1643   1607   1720    142     24   -170       O  
ATOM    187  CB  ILE A 350       3.430   8.261   3.282  1.00 12.14           C  
ANISOU  187  CB  ILE A 350     1469   1515   1629     40      9   -195       C  
ATOM    188  CG1 ILE A 350       2.491   7.070   3.056  1.00 12.94           C  
ANISOU  188  CG1 ILE A 350     1507   1618   1791      1    -13   -228       C  
ATOM    189  CG2 ILE A 350       3.505   8.583   4.773  1.00 13.22           C  
ANISOU  189  CG2 ILE A 350     1607   1644   1770     22     89   -183       C  
ATOM    190  CD1 ILE A 350       3.118   5.727   3.415  1.00 13.51           C  
ANISOU  190  CD1 ILE A 350     1621   1667   1846    -51     24   -221       C  
ATOM    191  N   PHE A 351       4.966  10.833   2.283  1.00 10.63           N  
ANISOU  191  N   PHE A 351     1415   1300   1324    116    -19   -139       N  
ATOM    192  CA  PHE A 351       5.952  11.786   2.787  1.00 10.03           C  
ANISOU  192  CA  PHE A 351     1393   1204   1213    104     18   -111       C  
ATOM    193  C   PHE A 351       6.137  13.063   1.979  1.00 10.67           C  
ANISOU  193  C   PHE A 351     1542   1255   1259    139     -2    -90       C  
ATOM    194  O   PHE A 351       6.735  14.025   2.480  1.00 10.64           O  
ANISOU  194  O   PHE A 351     1583   1222   1239    121     26    -73       O  
ATOM    195  CB  PHE A 351       7.292  11.065   3.022  1.00 10.28           C  
ANISOU  195  CB  PHE A 351     1436   1247   1223     59     46    -88       C  
ATOM    196  CG  PHE A 351       7.214  10.077   4.152  1.00  9.74           C  
ANISOU  196  CG  PHE A 351     1334   1190   1178     28     70    -97       C  
ATOM    197  CD1 PHE A 351       7.129   8.714   3.892  1.00 11.48           C  
ANISOU  197  CD1 PHE A 351     1533   1418   1411     20     67   -106       C  
ATOM    198  CD2 PHE A 351       7.155  10.521   5.479  1.00 10.19           C  
ANISOU  198  CD2 PHE A 351     1403   1237   1233      8     97    -98       C  
ATOM    199  CE1 PHE A 351       6.994   7.794   4.933  1.00 12.59           C  
ANISOU  199  CE1 PHE A 351     1662   1554   1568     -8     94   -107       C  
ATOM    200  CE2 PHE A 351       7.023   9.596   6.527  1.00 10.72           C  
ANISOU  200  CE2 PHE A 351     1466   1305   1304    -19    124   -100       C  
ATOM    201  CZ  PHE A 351       6.952   8.243   6.247  1.00 11.71           C  
ANISOU  201  CZ  PHE A 351     1567   1436   1447    -27    123   -100       C  
ATOM    202  N   SER A 352       5.620  13.101   0.754  1.00 11.47           N  
ANISOU  202  N   SER A 352     1665   1353   1341    184    -57    -91       N  
ATOM    203  CA  SER A 352       5.702  14.316  -0.053  1.00 12.89           C  
ANISOU  203  CA  SER A 352     1932   1491   1475    225    -78    -63       C  
ATOM    204  C   SER A 352       5.108  15.586   0.591  1.00 12.89           C  
ANISOU  204  C   SER A 352     1946   1449   1501    264    -74    -63       C  
ATOM    205  O   SER A 352       5.592  16.665   0.295  1.00 13.18           O  
ANISOU  205  O   SER A 352     2077   1434   1498    271    -61    -33       O  
ATOM    206  CB  SER A 352       5.097  14.104  -1.448  1.00 13.92           C  
ANISOU  206  CB  SER A 352     2102   1622   1566    277   -158    -65       C  
ATOM    207  OG  SER A 352       3.736  13.712  -1.354  1.00 17.39           O  
ANISOU  207  OG  SER A 352     2452   2087   2069    315   -229   -102       O  
ATOM    208  N   PRO A 353       4.082  15.471   1.468  1.00 12.99           N  
ANISOU  208  N   PRO A 353     1875   1478   1583    289    -70    -97       N  
ATOM    209  CA  PRO A 353       3.570  16.709   2.091  1.00 13.40           C  
ANISOU  209  CA  PRO A 353     1955   1480   1657    340    -47   -102       C  
ATOM    210  C   PRO A 353       4.620  17.463   2.905  1.00 12.82           C  
ANISOU  210  C   PRO A 353     1968   1360   1544    283     15    -89       C  
ATOM    211  O   PRO A 353       4.448  18.665   3.121  1.00 14.29           O  
ANISOU  211  O   PRO A 353     2228   1479   1722    320     29    -86       O  
ATOM    212  CB  PRO A 353       2.484  16.198   3.044  1.00 13.74           C  
ANISOU  212  CB  PRO A 353     1882   1556   1781    358    -16   -143       C  
ATOM    213  CG  PRO A 353       2.030  14.910   2.408  1.00 14.72           C  
ANISOU  213  CG  PRO A 353     1915   1740   1938    341    -69   -156       C  
ATOM    214  CD  PRO A 353       3.269  14.298   1.852  1.00 13.23           C  
ANISOU  214  CD  PRO A 353     1790   1559   1676    278    -76   -133       C  
ATOM    215  N   TYR A 354       5.686  16.770   3.348  1.00 11.19           N  
ANISOU  215  N   TYR A 354     1753   1181   1315    195     43    -83       N  
ATOM    216  CA  TYR A 354       6.685  17.360   4.265  1.00 11.42           C  
ANISOU  216  CA  TYR A 354     1845   1177   1319    127     79    -78       C  
ATOM    217  C   TYR A 354       7.810  18.136   3.617  1.00 11.82           C  
ANISOU  217  C   TYR A 354     1973   1186   1333     80     78    -41       C  
ATOM    218  O   TYR A 354       8.491  18.918   4.293  1.00 12.73           O  
ANISOU  218  O   TYR A 354     2147   1254   1435     22     94    -41       O  
ATOM    219  CB  TYR A 354       7.230  16.293   5.232  1.00 10.78           C  
ANISOU  219  CB  TYR A 354     1711   1143   1240     63     95    -89       C  
ATOM    220  CG  TYR A 354       6.083  15.690   5.973  1.00 11.32           C  
ANISOU  220  CG  TYR A 354     1725   1234   1340     98    121   -122       C  
ATOM    221  CD1 TYR A 354       5.404  16.430   6.950  1.00 11.32           C  
ANISOU  221  CD1 TYR A 354     1766   1195   1342    125    166   -151       C  
ATOM    222  CD2 TYR A 354       5.600  14.423   5.629  1.00 11.23           C  
ANISOU  222  CD2 TYR A 354     1628   1275   1362    105    112   -127       C  
ATOM    223  CE1 TYR A 354       4.304  15.912   7.603  1.00 11.64           C  
ANISOU  223  CE1 TYR A 354     1748   1254   1419    157    216   -179       C  
ATOM    224  CE2 TYR A 354       4.495  13.895   6.269  1.00 12.81           C  
ANISOU  224  CE2 TYR A 354     1769   1492   1606    124    149   -155       C  
ATOM    225  CZ  TYR A 354       3.860  14.636   7.263  1.00 13.33           C  
ANISOU  225  CZ  TYR A 354     1862   1525   1677    149    208   -178       C  
ATOM    226  OH  TYR A 354       2.758  14.117   7.905  1.00 15.69           O  
ANISOU  226  OH  TYR A 354     2094   1840   2028    165    272   -204       O  
ATOM    227  N   GLY A 355       7.984  17.968   2.312  1.00 11.69           N  
ANISOU  227  N   GLY A 355     1967   1178   1297     99     63    -11       N  
ATOM    228  CA  GLY A 355       9.009  18.722   1.614  1.00 12.61           C  
ANISOU  228  CA  GLY A 355     2162   1249   1380     52     88     31       C  
ATOM    229  C   GLY A 355       9.275  18.071   0.274  1.00 13.42           C  
ANISOU  229  C   GLY A 355     2267   1383   1450     68     90     59       C  
ATOM    230  O   GLY A 355       8.639  17.068  -0.076  1.00 14.89           O  
ANISOU  230  O   GLY A 355     2400   1620   1639    115     57     40       O  
ATOM    231  N   HIS A 356      10.241  18.623  -0.450  1.00 13.88           N  
ANISOU  231  N   HIS A 356     2392   1404   1476     22    138    102       N  
ATOM    232  CA  HIS A 356      10.626  18.076  -1.764  1.00 14.37           C  
ANISOU  232  CA  HIS A 356     2487   1485   1488     36    167    131       C  
ATOM    233  C   HIS A 356      11.552  16.890  -1.609  1.00 13.49           C  
ANISOU  233  C   HIS A 356     2271   1444   1411    -10    209    124       C  
ATOM    234  O   HIS A 356      12.634  17.000  -1.039  1.00 13.44           O  
ANISOU  234  O   HIS A 356     2207   1448   1453    -88    254    137       O  
ATOM    235  CB  HIS A 356      11.260  19.154  -2.632  1.00 16.14           C  
ANISOU  235  CB  HIS A 356     2838   1634   1660      6    226    185       C  
ATOM    236  CG  HIS A 356      10.315  20.267  -2.970  1.00 20.34           C  
ANISOU  236  CG  HIS A 356     3498   2083   2147     74    177    200       C  
ATOM    237  ND1 HIS A 356      10.478  21.545  -2.491  1.00 26.22           N  
ANISOU  237  ND1 HIS A 356     4317   2741   2903     39    196    216       N  
ATOM    238  CD2 HIS A 356       9.181  20.276  -3.708  1.00 24.92           C  
ANISOU  238  CD2 HIS A 356     4143   2651   2676    182    100    200       C  
ATOM    239  CE1 HIS A 356       9.495  22.306  -2.938  1.00 27.46           C  
ANISOU  239  CE1 HIS A 356     4585   2830   3017    134    142    230       C  
ATOM    240  NE2 HIS A 356       8.689  21.558  -3.671  1.00 26.54           N  
ANISOU  240  NE2 HIS A 356     4455   2763   2866    224     76    221       N  
ATOM    241  N   ILE A 357      11.076  15.745  -2.083  1.00 12.20           N  
ANISOU  241  N   ILE A 357     2082   1325   1229     42    184    102       N  
ATOM    242  CA  ILE A 357      11.821  14.498  -2.007  1.00 11.88           C  
ANISOU  242  CA  ILE A 357     1957   1340   1217     23    222     93       C  
ATOM    243  C   ILE A 357      12.723  14.371  -3.235  1.00 13.25           C  
ANISOU  243  C   ILE A 357     2189   1505   1342     19    312    126       C  
ATOM    244  O   ILE A 357      12.249  14.469  -4.389  1.00 14.80           O  
ANISOU  244  O   ILE A 357     2502   1671   1449     67    308    133       O  
ATOM    245  CB  ILE A 357      10.868  13.293  -1.931  1.00 11.35           C  
ANISOU  245  CB  ILE A 357     1852   1307   1152     72    161     48       C  
ATOM    246  CG1 ILE A 357      10.115  13.291  -0.587  1.00  9.98           C  
ANISOU  246  CG1 ILE A 357     1609   1147   1037     66    109     19       C  
ATOM    247  CG2 ILE A 357      11.641  11.986  -2.172  1.00 11.73           C  
ANISOU  247  CG2 ILE A 357     1858   1390   1211     71    209     42       C  
ATOM    248  CD1 ILE A 357       8.946  12.337  -0.564  1.00 10.51           C  
ANISOU  248  CD1 ILE A 357     1642   1236   1116    104     52    -22       C  
ATOM    249  N   MET A 358      14.016  14.147  -2.979  1.00 12.75           N  
ANISOU  249  N   MET A 358     2043   1465   1334    -33    392    146       N  
ATOM    250  CA  MET A 358      15.011  14.030  -4.028  1.00 14.55           C  
ANISOU  250  CA  MET A 358     2302   1689   1537    -41    511    179       C  
ATOM    251  C   MET A 358      15.257  12.598  -4.460  1.00 14.52           C  
ANISOU  251  C   MET A 358     2269   1721   1526     11    549    156       C  
ATOM    252  O   MET A 358      15.605  12.335  -5.617  1.00 15.62           O  
ANISOU  252  O   MET A 358     2493   1844   1597     41    639    167       O  
ATOM    253  CB  MET A 358      16.334  14.646  -3.562  1.00 15.38           C  
ANISOU  253  CB  MET A 358     2312   1800   1731   -130    588    216       C  
ATOM    254  CG  MET A 358      16.249  16.097  -3.083  1.00 18.66           C  
ANISOU  254  CG  MET A 358     2768   2163   2158   -201    559    235       C  
ATOM    255  SD  MET A 358      15.946  17.295  -4.403  1.00 24.72           S  
ANISOU  255  SD  MET A 358     3741   2838   2813   -198    622    281       S  
ATOM    256  CE  MET A 358      14.148  17.403  -4.410  1.00 23.03           C  
ANISOU  256  CE  MET A 358     3637   2597   2517    -96    478    246       C  
ATOM    257  N   GLN A 359      15.105  11.675  -3.520  1.00 13.53           N  
ANISOU  257  N   GLN A 359     2041   1635   1464     25    488    124       N  
ATOM    258  CA  GLN A 359      15.405  10.278  -3.767  1.00 14.50           C  
ANISOU  258  CA  GLN A 359     2135   1780   1595     75    522    102       C  
ATOM    259  C   GLN A 359      14.693   9.415  -2.746  1.00 13.23           C  
ANISOU  259  C   GLN A 359     1917   1637   1472     90    422     66       C  
ATOM    260  O   GLN A 359      14.568   9.816  -1.599  1.00 12.68           O  
ANISOU  260  O   GLN A 359     1780   1581   1455     52    362     69       O  
ATOM    261  CB  GLN A 359      16.921  10.047  -3.661  1.00 16.35           C  
ANISOU  261  CB  GLN A 359     2254   2043   1914     60    629    134       C  
ATOM    262  CG  GLN A 359      17.361   8.624  -3.905  1.00 21.35           C  
ANISOU  262  CG  GLN A 359     2857   2689   2566    129    680    115       C  
ATOM    263  CD  GLN A 359      18.861   8.500  -4.111  1.00 26.99           C  
ANISOU  263  CD  GLN A 359     3459   3429   3365    133    813    149       C  
ATOM    264  OE1 GLN A 359      19.521   9.429  -4.595  1.00 31.81           O  
ANISOU  264  OE1 GLN A 359     4060   4038   3987     84    906    186       O  
ATOM    265  NE2 GLN A 359      19.406   7.339  -3.771  1.00 29.44           N  
ANISOU  265  NE2 GLN A 359     3683   3758   3743    194    829    140       N  
ATOM    266  N   ILE A 360      14.244   8.238  -3.186  1.00 12.89           N  
ANISOU  266  N   ILE A 360     1919   1583   1394    140    412     30       N  
ATOM    267  CA  ILE A 360      13.649   7.205  -2.317  1.00 12.46           C  
ANISOU  267  CA  ILE A 360     1823   1534   1377    150    342     -1       C  
ATOM    268  C   ILE A 360      14.336   5.880  -2.573  1.00 13.71           C  
ANISOU  268  C   ILE A 360     1975   1684   1551    199    401    -10       C  
ATOM    269  O   ILE A 360      14.420   5.438  -3.720  1.00 14.48           O  
ANISOU  269  O   ILE A 360     2163   1753   1584    238    457    -29       O  
ATOM    270  CB  ILE A 360      12.133   7.037  -2.551  1.00 12.55           C  
ANISOU  270  CB  ILE A 360     1903   1526   1341    153    253    -44       C  
ATOM    271  CG1 ILE A 360      11.432   8.387  -2.307  1.00 12.31           C  
ANISOU  271  CG1 ILE A 360     1875   1498   1303    127    200    -33       C  
ATOM    272  CG2 ILE A 360      11.559   5.913  -1.657  1.00 12.23           C  
ANISOU  272  CG2 ILE A 360     1820   1481   1346    148    205    -72       C  
ATOM    273  CD1 ILE A 360       9.906   8.345  -2.406  1.00 14.96           C  
ANISOU  273  CD1 ILE A 360     2236   1825   1623    136    105    -71       C  
ATOM    274  N   ASN A 361      14.870   5.275  -1.513  1.00 14.20           N  
ANISOU  274  N   ASN A 361     1943   1761   1691    204    390      4       N  
ATOM    275  CA  ASN A 361      15.460   3.936  -1.596  1.00 15.47           C  
ANISOU  275  CA  ASN A 361     2099   1902   1878    266    434     -3       C  
ATOM    276  C   ASN A 361      14.752   2.995  -0.626  1.00 14.91           C  
ANISOU  276  C   ASN A 361     2033   1808   1826    262    358    -21       C  
ATOM    277  O   ASN A 361      14.441   3.372   0.512  1.00 14.27           O  
ANISOU  277  O   ASN A 361     1903   1746   1774    220    293     -5       O  
ATOM    278  CB  ASN A 361      16.965   3.975  -1.293  1.00 17.32           C  
ANISOU  278  CB  ASN A 361     2212   2170   2198    293    499     41       C  
ATOM    279  CG  ASN A 361      17.743   4.843  -2.276  1.00 21.46           C  
ANISOU  279  CG  ASN A 361     2725   2712   2716    285    606     63       C  
ATOM    280  OD1 ASN A 361      18.525   5.694  -1.869  1.00 29.87           O  
ANISOU  280  OD1 ASN A 361     3683   3817   3850    242    618    101       O  
ATOM    281  ND2 ASN A 361      17.523   4.636  -3.566  1.00 27.23           N  
ANISOU  281  ND2 ASN A 361     3578   3408   3360    319    683     38       N  
ATOM    282  N   ILE A 362      14.472   1.780  -1.088  1.00 14.87           N  
ANISOU  282  N   ILE A 362     2106   1749   1795    302    374    -54       N  
ATOM    283  CA  ILE A 362      13.901   0.745  -0.227  1.00 15.02           C  
ANISOU  283  CA  ILE A 362     2143   1728   1835    296    323    -65       C  
ATOM    284  C   ILE A 362      14.853  -0.439  -0.229  1.00 15.76           C  
ANISOU  284  C   ILE A 362     2244   1780   1963    378    377    -54       C  
ATOM    285  O   ILE A 362      15.256  -0.914  -1.292  1.00 16.40           O  
ANISOU  285  O   ILE A 362     2387   1829   2016    435    451    -78       O  
ATOM    286  CB  ILE A 362      12.517   0.301  -0.711  1.00 14.67           C  
ANISOU  286  CB  ILE A 362     2194   1639   1741    254    277   -122       C  
ATOM    287  CG1 ILE A 362      11.547   1.488  -0.670  1.00 15.04           C  
ANISOU  287  CG1 ILE A 362     2216   1729   1771    192    219   -129       C  
ATOM    288  CG2 ILE A 362      11.985  -0.883   0.136  1.00 15.78           C  
ANISOU  288  CG2 ILE A 362     2362   1723   1910    236    248   -130       C  
ATOM    289  CD1 ILE A 362      10.298   1.267  -1.508  1.00 16.22           C  
ANISOU  289  CD1 ILE A 362     2439   1850   1875    161    164   -186       C  
ATOM    290  N   LYS A 363      15.227  -0.894   0.964  1.00 15.79           N  
ANISOU  290  N   LYS A 363     2197   1780   2021    394    342    -16       N  
ATOM    291  CA  LYS A 363      16.056  -2.084   1.096  1.00 17.51           C  
ANISOU  291  CA  LYS A 363     2426   1949   2280    487    377      1       C  
ATOM    292  C   LYS A 363      15.348  -2.970   2.090  1.00 16.90           C  
ANISOU  292  C   LYS A 363     2414   1809   2197    464    318      6       C  
ATOM    293  O   LYS A 363      15.581  -2.896   3.292  1.00 16.45           O  
ANISOU  293  O   LYS A 363     2313   1769   2166    459    262     53       O  
ATOM    294  CB  LYS A 363      17.492  -1.781   1.549  1.00 18.15           C  
ANISOU  294  CB  LYS A 363     2369   2085   2443    550    389     58       C  
ATOM    295  CG  LYS A 363      18.420  -3.031   1.555  1.00 23.93           C  
ANISOU  295  CG  LYS A 363     3100   2763   3231    676    432     77       C  
ATOM    296  CD  LYS A 363      18.734  -3.539   0.132  1.00 29.31           C  
ANISOU  296  CD  LYS A 363     3845   3400   3891    749    559     35       C  
ATOM    297  CE  LYS A 363      19.192  -4.993   0.140  1.00 33.23           C  
ANISOU  297  CE  LYS A 363     4406   3804   4417    870    599     35       C  
ATOM    298  NZ  LYS A 363      19.838  -5.369  -1.152  1.00 36.44           N  
ANISOU  298  NZ  LYS A 363     4850   4178   4819    965    744      1       N  
ATOM    299  N   ASN A 364      14.451  -3.789   1.555  1.00 17.36           N  
ANISOU  299  N   ASN A 364     2593   1791   2213    440    330    -44       N  
ATOM    300  CA  ASN A 364      13.625  -4.684   2.357  1.00 17.75           C  
ANISOU  300  CA  ASN A 364     2721   1765   2257    396    294    -45       C  
ATOM    301  C   ASN A 364      12.829  -3.923   3.416  1.00 16.12           C  
ANISOU  301  C   ASN A 364     2469   1607   2048    303    238    -24       C  
ATOM    302  O   ASN A 364      12.016  -3.105   3.042  1.00 16.68           O  
ANISOU  302  O   ASN A 364     2513   1722   2101    235    223    -57       O  
ATOM    303  CB  ASN A 364      14.453  -5.857   2.892  1.00 18.96           C  
ANISOU  303  CB  ASN A 364     2919   1843   2442    492    309     -5       C  
ATOM    304  CG  ASN A 364      15.162  -6.606   1.773  1.00 21.00           C  
ANISOU  304  CG  ASN A 364     3231   2043   2703    594    385    -35       C  
ATOM    305  OD1 ASN A 364      14.519  -7.135   0.868  1.00 27.14           O  
ANISOU  305  OD1 ASN A 364     4122   2753   3436    568    413    -99       O  
ATOM    306  ND2 ASN A 364      16.482  -6.624   1.816  1.00 22.01           N  
ANISOU  306  ND2 ASN A 364     3278   2199   2886    710    417      7       N  
ATOM    307  N   ALA A 365      13.051  -4.166   4.710  1.00 15.95           N  
ANISOU  307  N   ALA A 365     2449   1574   2039    308    209     30       N  
ATOM    308  CA  ALA A 365      12.321  -3.440   5.768  1.00 15.26           C  
ANISOU  308  CA  ALA A 365     2339   1525   1934    226    175     47       C  
ATOM    309  C   ALA A 365      12.729  -1.977   5.922  1.00 14.21           C  
ANISOU  309  C   ALA A 365     2104   1493   1803    215    146     59       C  
ATOM    310  O   ALA A 365      12.041  -1.207   6.606  1.00 14.44           O  
ANISOU  310  O   ALA A 365     2121   1553   1812    149    130     58       O  
ATOM    311  CB  ALA A 365      12.475  -4.138   7.114  1.00 16.17           C  
ANISOU  311  CB  ALA A 365     2521   1587   2035    236    155    103       C  
ATOM    312  N   PHE A 366      13.837  -1.593   5.300  1.00 14.03           N  
ANISOU  312  N   PHE A 366     2010   1513   1807    277    151     69       N  
ATOM    313  CA  PHE A 366      14.384  -0.254   5.509  1.00 13.65           C  
ANISOU  313  CA  PHE A 366     1869   1548   1770    258    123     86       C  
ATOM    314  C   PHE A 366      14.049   0.685   4.359  1.00 13.61           C  
ANISOU  314  C   PHE A 366     1837   1581   1755    228    157     47       C  
ATOM    315  O   PHE A 366      14.249   0.344   3.175  1.00 14.40           O  
ANISOU  315  O   PHE A 366     1953   1665   1853    267    208     23       O  
ATOM    316  CB  PHE A 366      15.907  -0.284   5.739  1.00 14.77           C  
ANISOU  316  CB  PHE A 366     1926   1721   1966    331    100    133       C  
ATOM    317  CG  PHE A 366      16.349  -1.188   6.872  1.00 15.70           C  
ANISOU  317  CG  PHE A 366     2077   1800   2090    379     42    181       C  
ATOM    318  CD1 PHE A 366      17.576  -1.823   6.808  1.00 19.51           C  
ANISOU  318  CD1 PHE A 366     2499   2278   2635    482     32    217       C  
ATOM    319  CD2 PHE A 366      15.541  -1.395   7.996  1.00 16.24           C  
ANISOU  319  CD2 PHE A 366     2239   1831   2099    330      4    193       C  
ATOM    320  CE1 PHE A 366      18.010  -2.656   7.845  1.00 21.26           C  
ANISOU  320  CE1 PHE A 366     2760   2458   2859    542    -39    268       C  
ATOM    321  CE2 PHE A 366      15.962  -2.244   9.044  1.00 18.87           C  
ANISOU  321  CE2 PHE A 366     2632   2118   2419    380    -53    246       C  
ATOM    322  CZ  PHE A 366      17.203  -2.867   8.961  1.00 20.47           C  
ANISOU  322  CZ  PHE A 366     2780   2315   2682    490    -85    285       C  
ATOM    323  N   GLY A 367      13.564   1.873   4.714  1.00 12.37           N  
ANISOU  323  N   GLY A 367     1655   1464   1580    167    131     43       N  
ATOM    324  CA  GLY A 367      13.304   2.912   3.719  1.00 11.25           C  
ANISOU  324  CA  GLY A 367     1497   1352   1424    145    153     18       C  
ATOM    325  C   GLY A 367      14.177   4.113   4.002  1.00 10.85           C  
ANISOU  325  C   GLY A 367     1378   1351   1394    127    139     47       C  
ATOM    326  O   GLY A 367      14.483   4.414   5.166  1.00 10.46           O  
ANISOU  326  O   GLY A 367     1306   1315   1353    103     89     71       O  
ATOM    327  N   PHE A 368      14.589   4.782   2.928  1.00 10.92           N  
ANISOU  327  N   PHE A 368     1369   1378   1404    131    184     45       N  
ATOM    328  CA  PHE A 368      15.377   5.998   3.043  1.00 11.40           C  
ANISOU  328  CA  PHE A 368     1369   1474   1489     95    182     70       C  
ATOM    329  C   PHE A 368      14.805   7.052   2.117  1.00 11.64           C  
ANISOU  329  C   PHE A 368     1447   1498   1476     68    211     54       C  
ATOM    330  O   PHE A 368      14.749   6.858   0.898  1.00 13.67           O  
ANISOU  330  O   PHE A 368     1747   1743   1703     99    266     43       O  
ATOM    331  CB  PHE A 368      16.839   5.712   2.678  1.00 12.37           C  
ANISOU  331  CB  PHE A 368     1402   1622   1678    131    229    101       C  
ATOM    332  CG  PHE A 368      17.464   4.630   3.498  1.00 12.81           C  
ANISOU  332  CG  PHE A 368     1409   1677   1780    180    191    123       C  
ATOM    333  CD1 PHE A 368      18.116   4.943   4.687  1.00 12.94           C  
ANISOU  333  CD1 PHE A 368     1357   1722   1839    154    107    153       C  
ATOM    334  CD2 PHE A 368      17.401   3.287   3.085  1.00 11.52           C  
ANISOU  334  CD2 PHE A 368     1286   1477   1615    257    229    113       C  
ATOM    335  CE1 PHE A 368      18.700   3.936   5.446  1.00 13.70           C  
ANISOU  335  CE1 PHE A 368     1419   1815   1973    213     54    180       C  
ATOM    336  CE2 PHE A 368      17.974   2.281   3.849  1.00 13.13           C  
ANISOU  336  CE2 PHE A 368     1460   1668   1861    316    190    140       C  
ATOM    337  CZ  PHE A 368      18.637   2.611   5.036  1.00 13.93           C  
ANISOU  337  CZ  PHE A 368     1486   1802   2003    298     99    178       C  
ATOM    338  N   ILE A 369      14.393   8.176   2.698  1.00 10.46           N  
ANISOU  338  N   ILE A 369     1309   1350   1316     17    172     53       N  
ATOM    339  CA  ILE A 369      13.801   9.246   1.918  1.00 10.96           C  
ANISOU  339  CA  ILE A 369     1430   1397   1338      3    187     44       C  
ATOM    340  C   ILE A 369      14.671  10.475   2.063  1.00 10.52           C  
ANISOU  340  C   ILE A 369     1347   1344   1306    -52    200     72       C  
ATOM    341  O   ILE A 369      14.777  11.040   3.152  1.00 11.17           O  
ANISOU  341  O   ILE A 369     1413   1426   1405    -96    151     73       O  
ATOM    342  CB  ILE A 369      12.366   9.519   2.357  1.00 10.71           C  
ANISOU  342  CB  ILE A 369     1444   1347   1278      1    140     14       C  
ATOM    343  CG1 ILE A 369      11.501   8.250   2.113  1.00 13.47           C  
ANISOU  343  CG1 ILE A 369     1808   1690   1618     36    130    -16       C  
ATOM    344  CG2 ILE A 369      11.795  10.715   1.596  1.00 12.21           C  
ANISOU  344  CG2 ILE A 369     1694   1515   1432      3    142     11       C  
ATOM    345  CD1 ILE A 369      10.021   8.433   2.308  1.00 17.56           C  
ANISOU  345  CD1 ILE A 369     2344   2197   2130     35     95    -48       C  
ATOM    346  N   GLN A 370      15.286  10.879   0.953  1.00 10.34           N  
ANISOU  346  N   GLN A 370     1335   1316   1279    -54    271     93       N  
ATOM    347  CA  GLN A 370      16.159  12.042   0.938  1.00 11.45           C  
ANISOU  347  CA  GLN A 370     1451   1450   1451   -121    301    123       C  
ATOM    348  C   GLN A 370      15.345  13.276   0.589  1.00 11.62           C  
ANISOU  348  C   GLN A 370     1580   1420   1413   -139    293    120       C  
ATOM    349  O   GLN A 370      14.816  13.387  -0.526  1.00 11.95           O  
ANISOU  349  O   GLN A 370     1711   1438   1392    -99    327    122       O  
ATOM    350  CB  GLN A 370      17.279  11.837  -0.084  1.00 12.52           C  
ANISOU  350  CB  GLN A 370     1542   1599   1616   -117    409    154       C  
ATOM    351  CG  GLN A 370      18.263  13.000  -0.150  1.00 15.89           C  
ANISOU  351  CG  GLN A 370     1926   2017   2094   -205    457    189       C  
ATOM    352  CD  GLN A 370      19.144  13.024   1.056  1.00 19.88           C  
ANISOU  352  CD  GLN A 370     2297   2559   2699   -263    391    195       C  
ATOM    353  OE1 GLN A 370      19.896  12.077   1.300  1.00 22.76           O  
ANISOU  353  OE1 GLN A 370     2543   2970   3133   -230    392    203       O  
ATOM    354  NE2 GLN A 370      19.069  14.104   1.823  1.00 20.16           N  
ANISOU  354  NE2 GLN A 370     2355   2566   2738   -345    324    191       N  
ATOM    355  N   PHE A 371      15.228  14.186   1.549  1.00 11.73           N  
ANISOU  355  N   PHE A 371     1603   1412   1440   -192    241    114       N  
ATOM    356  CA  PHE A 371      14.643  15.503   1.301  1.00 11.85           C  
ANISOU  356  CA  PHE A 371     1724   1365   1412   -209    240    117       C  
ATOM    357  C   PHE A 371      15.765  16.485   0.976  1.00 13.11           C  
ANISOU  357  C   PHE A 371     1883   1495   1603   -295    296    154       C  
ATOM    358  O   PHE A 371      16.956  16.137   1.027  1.00 14.11           O  
ANISOU  358  O   PHE A 371     1902   1660   1798   -343    330    174       O  
ATOM    359  CB  PHE A 371      13.897  16.020   2.537  1.00 11.82           C  
ANISOU  359  CB  PHE A 371     1752   1337   1403   -218    169     84       C  
ATOM    360  CG  PHE A 371      12.623  15.284   2.850  1.00 10.74           C  
ANISOU  360  CG  PHE A 371     1621   1217   1243   -143    134     50       C  
ATOM    361  CD1 PHE A 371      11.414  15.651   2.256  1.00 11.15           C  
ANISOU  361  CD1 PHE A 371     1739   1239   1259    -79    126     37       C  
ATOM    362  CD2 PHE A 371      12.622  14.243   3.786  1.00 11.27           C  
ANISOU  362  CD2 PHE A 371     1625   1326   1330   -140    105     32       C  
ATOM    363  CE1 PHE A 371      10.239  14.980   2.575  1.00 11.60           C  
ANISOU  363  CE1 PHE A 371     1773   1316   1318    -24     96      4       C  
ATOM    364  CE2 PHE A 371      11.440  13.573   4.104  1.00 12.97           C  
ANISOU  364  CE2 PHE A 371     1844   1551   1534    -89     89      3       C  
ATOM    365  CZ  PHE A 371      10.247  13.953   3.503  1.00 12.61           C  
ANISOU  365  CZ  PHE A 371     1838   1483   1469    -37     87    -13       C  
ATOM    366  N   ASP A 372      15.385  17.719   0.650  1.00 14.33           N  
ANISOU  366  N   ASP A 372     2152   1575   1718   -314    307    165       N  
ATOM    367  CA  ASP A 372      16.366  18.773   0.398  1.00 15.79           C  
ANISOU  367  CA  ASP A 372     2356   1712   1934   -415    364    200       C  
ATOM    368  C   ASP A 372      16.703  19.647   1.619  1.00 15.94           C  
ANISOU  368  C   ASP A 372     2370   1693   1995   -510    303    181       C  
ATOM    369  O   ASP A 372      17.394  20.661   1.480  1.00 17.32           O  
ANISOU  369  O   ASP A 372     2576   1807   2196   -609    339    204       O  
ATOM    370  CB  ASP A 372      15.928  19.651  -0.786  1.00 16.86           C  
ANISOU  370  CB  ASP A 372     2646   1767   1992   -391    424    234       C  
ATOM    371  CG  ASP A 372      14.632  20.405  -0.512  1.00 18.28           C  
ANISOU  371  CG  ASP A 372     2951   1880   2115   -329    354    212       C  
ATOM    372  OD1 ASP A 372      14.258  21.265  -1.343  1.00 21.92           O  
ANISOU  372  OD1 ASP A 372     3553   2261   2515   -304    382    244       O  
ATOM    373  OD2 ASP A 372      13.986  20.160   0.535  1.00 17.31           O  
ANISOU  373  OD2 ASP A 372     2792   1778   2007   -299    278    166       O  
ATOM    374  N   ASN A 373      16.223  19.266   2.802  1.00 14.90           N  
ANISOU  374  N   ASN A 373     2213   1586   1862   -488    214    137       N  
ATOM    375  CA  ASN A 373      16.502  20.027   4.024  1.00 14.69           C  
ANISOU  375  CA  ASN A 373     2209   1519   1853   -573    145    109       C  
ATOM    376  C   ASN A 373      16.180  19.168   5.264  1.00 14.58           C  
ANISOU  376  C   ASN A 373     2150   1559   1830   -540     61     70       C  
ATOM    377  O   ASN A 373      15.401  18.215   5.159  1.00 13.71           O  
ANISOU  377  O   ASN A 373     2023   1493   1694   -444     66     61       O  
ATOM    378  CB  ASN A 373      15.663  21.312   4.036  1.00 15.50           C  
ANISOU  378  CB  ASN A 373     2480   1512   1897   -565    149     95       C  
ATOM    379  CG  ASN A 373      14.222  21.033   4.335  1.00 14.59           C  
ANISOU  379  CG  ASN A 373     2424   1395   1725   -443    126     61       C  
ATOM    380  OD1 ASN A 373      13.825  21.050   5.497  1.00 15.32           O  
ANISOU  380  OD1 ASN A 373     2540   1479   1800   -439     77     18       O  
ATOM    381  ND2 ASN A 373      13.442  20.694   3.307  1.00 15.28           N  
ANISOU  381  ND2 ASN A 373     2528   1494   1784   -344    159     78       N  
ATOM    382  N   PRO A 374      16.760  19.514   6.435  1.00 15.06           N  
ANISOU  382  N   PRO A 374     2208   1609   1907   -625    -18     46       N  
ATOM    383  CA  PRO A 374      16.534  18.742   7.663  1.00 14.87           C  
ANISOU  383  CA  PRO A 374     2171   1625   1855   -599    -98     16       C  
ATOM    384  C   PRO A 374      15.189  18.964   8.358  1.00 14.30           C  
ANISOU  384  C   PRO A 374     2230   1505   1696   -532    -97    -28       C  
ATOM    385  O   PRO A 374      14.750  18.104   9.123  1.00 14.26           O  
ANISOU  385  O   PRO A 374     2221   1538   1659   -485   -123    -44       O  
ATOM    386  CB  PRO A 374      17.676  19.203   8.576  1.00 15.89           C  
ANISOU  386  CB  PRO A 374     2272   1747   2019   -722   -194      6       C  
ATOM    387  CG  PRO A 374      17.957  20.586   8.140  1.00 17.64           C  
ANISOU  387  CG  PRO A 374     2564   1883   2257   -812   -163      6       C  
ATOM    388  CD  PRO A 374      17.772  20.571   6.644  1.00 16.68           C  
ANISOU  388  CD  PRO A 374     2418   1762   2157   -762    -43     50       C  
ATOM    389  N   GLN A 375      14.561  20.117   8.141  1.00 14.85           N  
ANISOU  389  N   GLN A 375     2420   1488   1734   -527    -60    -44       N  
ATOM    390  CA  GLN A 375      13.271  20.402   8.787  1.00 14.48           C  
ANISOU  390  CA  GLN A 375     2487   1394   1622   -452    -41    -87       C  
ATOM    391  C   GLN A 375      12.174  19.436   8.294  1.00 13.52           C  
ANISOU  391  C   GLN A 375     2309   1328   1502   -333      6    -81       C  
ATOM    392  O   GLN A 375      11.331  18.976   9.082  1.00 13.81           O  
ANISOU  392  O   GLN A 375     2365   1375   1505   -282     17   -111       O  
ATOM    393  CB  GLN A 375      12.846  21.863   8.570  1.00 15.61           C  
ANISOU  393  CB  GLN A 375     2768   1423   1742   -453     -9   -103       C  
ATOM    394  CG  GLN A 375      11.613  22.263   9.406  1.00 16.78           C  
ANISOU  394  CG  GLN A 375     3033   1513   1831   -373     20   -154       C  
ATOM    395  CD  GLN A 375      11.847  22.107  10.915  1.00 18.81           C  
ANISOU  395  CD  GLN A 375     3352   1764   2030   -424    -27   -200       C  
ATOM    396  OE1 GLN A 375      12.863  22.548  11.464  1.00 21.63           O  
ANISOU  396  OE1 GLN A 375     3753   2092   2375   -538    -98   -212       O  
ATOM    397  NE2 GLN A 375      10.903  21.466  11.586  1.00 20.96           N  
ANISOU  397  NE2 GLN A 375     3633   2064   2265   -344     11   -225       N  
ATOM    398  N   SER A 376      12.193  19.122   6.995  1.00 12.46           N  
ANISOU  398  N   SER A 376     2110   1224   1401   -299     38    -45       N  
ATOM    399  CA  SER A 376      11.249  18.172   6.438  1.00 11.62           C  
ANISOU  399  CA  SER A 376     1947   1168   1299   -205     62    -43       C  
ATOM    400  C   SER A 376      11.312  16.829   7.153  1.00 11.08           C  
ANISOU  400  C   SER A 376     1805   1168   1236   -202     43    -50       C  
ATOM    401  O   SER A 376      10.282  16.214   7.390  1.00 10.70           O  
ANISOU  401  O   SER A 376     1745   1138   1183   -143     62    -70       O  
ATOM    402  CB  SER A 376      11.519  17.959   4.952  1.00 10.87           C  
ANISOU  402  CB  SER A 376     1816   1094   1222   -185     86     -4       C  
ATOM    403  OG  SER A 376      11.149  19.114   4.214  1.00 12.37           O  
ANISOU  403  OG  SER A 376     2098   1211   1392   -161    105      8       O  
ATOM    404  N   VAL A 377      12.524  16.383   7.483  1.00 11.04           N  
ANISOU  404  N   VAL A 377     1747   1198   1250   -266      6    -32       N  
ATOM    405  CA  VAL A 377      12.704  15.097   8.164  1.00 11.38           C  
ANISOU  405  CA  VAL A 377     1735   1294   1294   -256    -21    -29       C  
ATOM    406  C   VAL A 377      12.066  15.171   9.553  1.00 11.63           C  
ANISOU  406  C   VAL A 377     1852   1300   1268   -256    -34    -62       C  
ATOM    407  O   VAL A 377      11.358  14.266   9.958  1.00 11.65           O  
ANISOU  407  O   VAL A 377     1850   1321   1254   -215    -11    -69       O  
ATOM    408  CB  VAL A 377      14.193  14.734   8.262  1.00 12.04           C  
ANISOU  408  CB  VAL A 377     1738   1416   1419   -313    -72      1       C  
ATOM    409  CG1 VAL A 377      14.407  13.488   9.124  1.00 13.16           C  
ANISOU  409  CG1 VAL A 377     1849   1598   1553   -293   -118      8       C  
ATOM    410  CG2 VAL A 377      14.761  14.541   6.859  1.00 13.04           C  
ANISOU  410  CG2 VAL A 377     1785   1569   1601   -302    -24     33       C  
ATOM    411  N   ARG A 378      12.340  16.251  10.278  1.00 12.36           N  
ANISOU  411  N   ARG A 378     2032   1340   1324   -309    -64    -84       N  
ATOM    412  CA  ARG A 378      11.779  16.426  11.623  1.00 12.88           C  
ANISOU  412  CA  ARG A 378     2212   1368   1314   -309    -64   -121       C  
ATOM    413  C   ARG A 378      10.251  16.466  11.581  1.00 12.52           C  
ANISOU  413  C   ARG A 378     2198   1302   1258   -227     31   -147       C  
ATOM    414  O   ARG A 378       9.584  15.810  12.390  1.00 12.17           O  
ANISOU  414  O   ARG A 378     2184   1265   1177   -200     70   -160       O  
ATOM    415  CB  ARG A 378      12.360  17.683  12.288  1.00 14.55           C  
ANISOU  415  CB  ARG A 378     2534   1512   1483   -385   -115   -149       C  
ATOM    416  CG  ARG A 378      13.806  17.491  12.717  1.00 16.90           C  
ANISOU  416  CG  ARG A 378     2791   1838   1792   -475   -231   -131       C  
ATOM    417  CD  ARG A 378      14.299  18.657  13.589  1.00 20.49           C  
ANISOU  417  CD  ARG A 378     3375   2219   2192   -565   -302   -170       C  
ATOM    418  NE  ARG A 378      14.400  19.905  12.831  1.00 22.42           N  
ANISOU  418  NE  ARG A 378     3645   2398   2476   -606   -271   -178       N  
ATOM    419  CZ  ARG A 378      15.506  20.343  12.231  1.00 24.20           C  
ANISOU  419  CZ  ARG A 378     3791   2627   2777   -696   -316   -153       C  
ATOM    420  NH1 ARG A 378      16.635  19.641  12.286  1.00 25.62           N  
ANISOU  420  NH1 ARG A 378     3835   2882   3016   -749   -399   -122       N  
ATOM    421  NH2 ARG A 378      15.483  21.488  11.560  1.00 23.75           N  
ANISOU  421  NH2 ARG A 378     3787   2495   2744   -732   -270   -156       N  
ATOM    422  N   ASP A 379       9.701  17.193  10.607  1.00 12.45           N  
ANISOU  422  N   ASP A 379     2175   1267   1287   -185     69   -149       N  
ATOM    423  CA  ASP A 379       8.252  17.318  10.456  1.00 13.00           C  
ANISOU  423  CA  ASP A 379     2245   1321   1372    -98    145   -173       C  
ATOM    424  C   ASP A 379       7.626  15.956  10.142  1.00 12.15           C  
ANISOU  424  C   ASP A 379     2030   1282   1305    -61    169   -160       C  
ATOM    425  O   ASP A 379       6.565  15.599  10.694  1.00 12.49           O  
ANISOU  425  O   ASP A 379     2066   1327   1353    -21    234   -182       O  
ATOM    426  CB  ASP A 379       7.884  18.331   9.365  1.00 13.40           C  
ANISOU  426  CB  ASP A 379     2303   1331   1458    -51    154   -168       C  
ATOM    427  CG  ASP A 379       8.285  19.761   9.711  1.00 16.90           C  
ANISOU  427  CG  ASP A 379     2877   1681   1863    -84    147   -185       C  
ATOM    428  OD1 ASP A 379       8.262  20.607   8.783  1.00 18.37           O  
ANISOU  428  OD1 ASP A 379     3088   1821   2069    -61    145   -168       O  
ATOM    429  OD2 ASP A 379       8.620  20.060  10.887  1.00 18.62           O  
ANISOU  429  OD2 ASP A 379     3189   1862   2024   -134    140   -215       O  
ATOM    430  N   ALA A 380       8.289  15.184   9.276  1.00 11.12           N  
ANISOU  430  N   ALA A 380     1818   1200   1206    -78    127   -127       N  
ATOM    431  CA  ALA A 380       7.807  13.847   8.923  1.00 10.69           C  
ANISOU  431  CA  ALA A 380     1680   1196   1186    -54    141   -118       C  
ATOM    432  C   ALA A 380       7.763  12.951  10.158  1.00 11.19           C  
ANISOU  432  C   ALA A 380     1768   1267   1216    -78    162   -121       C  
ATOM    433  O   ALA A 380       6.783  12.230  10.365  1.00 11.40           O  
ANISOU  433  O   ALA A 380     1765   1304   1264    -57    215   -132       O  
ATOM    434  CB  ALA A 380       8.672  13.228   7.845  1.00 10.50           C  
ANISOU  434  CB  ALA A 380     1595   1208   1186    -65    101    -87       C  
ATOM    435  N   ILE A 381       8.816  12.993  10.972  1.00 11.09           N  
ANISOU  435  N   ILE A 381     1815   1248   1152   -127    115   -108       N  
ATOM    436  CA  ILE A 381       8.853  12.148  12.180  1.00 12.07           C  
ANISOU  436  CA  ILE A 381     1994   1369   1221   -145    121   -102       C  
ATOM    437  C   ILE A 381       7.737  12.574  13.128  1.00 13.44           C  
ANISOU  437  C   ILE A 381     2253   1504   1350   -129    210   -137       C  
ATOM    438  O   ILE A 381       7.032  11.732  13.678  1.00 14.33           O  
ANISOU  438  O   ILE A 381     2376   1617   1451   -122    277   -135       O  
ATOM    439  CB  ILE A 381      10.214  12.262  12.901  1.00 11.69           C  
ANISOU  439  CB  ILE A 381     2000   1320   1122   -196     25    -83       C  
ATOM    440  CG1 ILE A 381      11.323  11.632  12.041  1.00 10.95           C  
ANISOU  440  CG1 ILE A 381     1798   1271   1090   -201    -40    -45       C  
ATOM    441  CG2 ILE A 381      10.158  11.585  14.273  1.00 13.03           C  
ANISOU  441  CG2 ILE A 381     2274   1472   1205   -207     23    -77       C  
ATOM    442  CD1 ILE A 381      12.720  12.176  12.366  1.00 13.81           C  
ANISOU  442  CD1 ILE A 381     2159   1639   1449   -255   -143    -31       C  
ATOM    443  N   GLU A 382       7.582  13.881  13.324  1.00 14.23           N  
ANISOU  443  N   GLU A 382     2420   1561   1426   -123    223   -168       N  
ATOM    444  CA  GLU A 382       6.619  14.375  14.308  1.00 16.61           C  
ANISOU  444  CA  GLU A 382     2820   1816   1677    -98    321   -206       C  
ATOM    445  C   GLU A 382       5.175  14.073  13.910  1.00 17.84           C  
ANISOU  445  C   GLU A 382     2879   1986   1912    -38    430   -220       C  
ATOM    446  O   GLU A 382       4.376  13.678  14.759  1.00 19.33           O  
ANISOU  446  O   GLU A 382     3103   2164   2079    -29    535   -233       O  
ATOM    447  CB  GLU A 382       6.818  15.868  14.526  1.00 17.54           C  
ANISOU  447  CB  GLU A 382     3041   1870   1754    -99    309   -241       C  
ATOM    448  CG  GLU A 382       8.138  16.215  15.226  1.00 20.97           C  
ANISOU  448  CG  GLU A 382     3586   2279   2103   -178    201   -240       C  
ATOM    449  CD  GLU A 382       8.270  15.585  16.618  1.00 26.75           C  
ANISOU  449  CD  GLU A 382     4443   2999   2721   -206    202   -242       C  
ATOM    450  OE1 GLU A 382       9.228  14.810  16.820  1.00 26.96           O  
ANISOU  450  OE1 GLU A 382     4454   3062   2727   -249    101   -206       O  
ATOM    451  OE2 GLU A 382       7.412  15.845  17.499  1.00 30.27           O  
ANISOU  451  OE2 GLU A 382     5007   3397   3096   -177    309   -277       O  
ATOM    452  N   CYS A 383       4.847  14.221  12.626  1.00 17.21           N  
ANISOU  452  N   CYS A 383     2679   1933   1926     -1    405   -215       N  
ATOM    453  CA  CYS A 383       3.475  14.017  12.162  1.00 19.14           C  
ANISOU  453  CA  CYS A 383     2812   2198   2264     56    477   -231       C  
ATOM    454  C   CYS A 383       3.146  12.573  11.795  1.00 18.38           C  
ANISOU  454  C   CYS A 383     2609   2151   2222     31    480   -212       C  
ATOM    455  O   CYS A 383       2.086  12.054  12.177  1.00 19.64           O  
ANISOU  455  O   CYS A 383     2713   2318   2431     37    574   -226       O  
ATOM    456  CB  CYS A 383       3.151  14.957  10.998  1.00 19.25           C  
ANISOU  456  CB  CYS A 383     2768   2206   2341    119    434   -237       C  
ATOM    457  SG  CYS A 383       3.070  16.692  11.529  1.00 27.70           S  
ANISOU  457  SG  CYS A 383     3969   3190   3365    168    471   -269       S  
ATOM    458  N   GLU A 384       4.047  11.900  11.089  1.00 16.59           N  
ANISOU  458  N   GLU A 384     2358   1952   1993     -2    390   -183       N  
ATOM    459  CA  GLU A 384       3.736  10.562  10.597  1.00 16.18           C  
ANISOU  459  CA  GLU A 384     2222   1932   1995    -23    386   -171       C  
ATOM    460  C   GLU A 384       3.923   9.468  11.629  1.00 16.27           C  
ANISOU  460  C   GLU A 384     2291   1931   1960    -71    432   -152       C  
ATOM    461  O   GLU A 384       3.391   8.365  11.465  1.00 17.05           O  
ANISOU  461  O   GLU A 384     2335   2038   2107    -96    461   -147       O  
ATOM    462  CB  GLU A 384       4.513  10.239   9.320  1.00 15.63           C  
ANISOU  462  CB  GLU A 384     2111   1887   1940    -23    289   -152       C  
ATOM    463  CG  GLU A 384       3.996  10.967   8.087  1.00 17.11           C  
ANISOU  463  CG  GLU A 384     2238   2085   2178     27    247   -167       C  
ATOM    464  CD  GLU A 384       2.501  10.783   7.819  1.00 16.21           C  
ANISOU  464  CD  GLU A 384     2021   1985   2151     55    276   -196       C  
ATOM    465  OE1 GLU A 384       1.957   9.665   7.969  1.00 17.68           O  
ANISOU  465  OE1 GLU A 384     2152   2185   2382     17    304   -203       O  
ATOM    466  OE2 GLU A 384       1.865  11.769   7.421  1.00 17.37           O  
ANISOU  466  OE2 GLU A 384     2139   2127   2333    114    265   -211       O  
ATOM    467  N   SER A 385       4.658   9.752  12.698  1.00 15.17           N  
ANISOU  467  N   SER A 385     2274   1765   1724    -89    432   -140       N  
ATOM    468  CA  SER A 385       4.779   8.756  13.755  1.00 16.51           C  
ANISOU  468  CA  SER A 385     2528   1914   1832   -126    474   -115       C  
ATOM    469  C   SER A 385       3.426   8.474  14.408  1.00 18.15           C  
ANISOU  469  C   SER A 385     2731   2103   2064   -134    621   -132       C  
ATOM    470  O   SER A 385       3.223   7.359  14.905  1.00 19.39           O  
ANISOU  470  O   SER A 385     2919   2241   2206   -172    674   -107       O  
ATOM    471  CB  SER A 385       5.807   9.148  14.799  1.00 16.88           C  
ANISOU  471  CB  SER A 385     2721   1934   1758   -142    424   -100       C  
ATOM    472  OG  SER A 385       7.098   9.143  14.223  1.00 17.38           O  
ANISOU  472  OG  SER A 385     2758   2020   1824   -146    295    -76       O  
ATOM    473  N   GLN A 386       2.519   9.456  14.351  1.00 17.57           N  
ANISOU  473  N   GLN A 386     2610   2030   2036    -96    690   -171       N  
ATOM    474  CA  GLN A 386       1.161   9.390  14.946  1.00 19.50           C  
ANISOU  474  CA  GLN A 386     2818   2262   2328    -92    852   -193       C  
ATOM    475  C   GLN A 386       0.151   8.705  14.028  1.00 18.64           C  
ANISOU  475  C   GLN A 386     2522   2190   2371   -101    871   -202       C  
ATOM    476  O   GLN A 386      -1.011   8.553  14.381  1.00 19.02           O  
ANISOU  476  O   GLN A 386     2494   2238   2494   -107   1002   -220       O  
ATOM    477  CB  GLN A 386       0.609  10.803  15.211  1.00 20.63           C  
ANISOU  477  CB  GLN A 386     2977   2388   2475    -26    917   -235       C  
ATOM    478  CG  GLN A 386       1.476  11.757  16.008  1.00 23.66           C  
ANISOU  478  CG  GLN A 386     3545   2725   2718    -16    889   -244       C  
ATOM    479  CD  GLN A 386       0.843  13.129  16.115  1.00 24.11           C  
ANISOU  479  CD  GLN A 386     3616   2751   2793     57    958   -290       C  
ATOM    480  OE1 GLN A 386      -0.355  13.259  16.381  1.00 27.36           O  
ANISOU  480  OE1 GLN A 386     3962   3159   3275    100   1103   -315       O  
ATOM    481  NE2 GLN A 386       1.638  14.164  15.897  1.00 26.07           N  
ANISOU  481  NE2 GLN A 386     3944   2972   2990     73    860   -301       N  
ATOM    482  N   GLU A 387       0.578   8.337  12.833  1.00 17.83           N  
ANISOU  482  N   GLU A 387     2342   2117   2315   -105    741   -195       N  
ATOM    483  CA  GLU A 387      -0.329   7.828  11.811  1.00 18.86           C  
ANISOU  483  CA  GLU A 387     2304   2280   2580   -113    720   -213       C  
ATOM    484  C   GLU A 387      -0.116   6.342  11.566  1.00 19.02           C  
ANISOU  484  C   GLU A 387     2324   2291   2612   -185    694   -192       C  
ATOM    485  O   GLU A 387       0.945   5.797  11.880  1.00 19.30           O  
ANISOU  485  O   GLU A 387     2478   2302   2555   -205    658   -159       O  
ATOM    486  CB  GLU A 387      -0.154   8.602  10.498  1.00 18.81           C  
ANISOU  486  CB  GLU A 387     2230   2305   2610    -54    590   -228       C  
ATOM    487  CG  GLU A 387      -0.435  10.123  10.561  1.00 20.76           C  
ANISOU  487  CG  GLU A 387     2481   2548   2860     28    604   -248       C  
ATOM    488  CD  GLU A 387      -1.908  10.474  10.811  1.00 26.39           C  
ANISOU  488  CD  GLU A 387     3068   3272   3689     68    705   -279       C  
ATOM    489  OE1 GLU A 387      -2.800   9.672  10.450  1.00 29.81           O  
ANISOU  489  OE1 GLU A 387     3358   3734   4235     35    717   -290       O  
ATOM    490  OE2 GLU A 387      -2.182  11.558  11.373  1.00 28.07           O  
ANISOU  490  OE2 GLU A 387     3318   3460   3888    133    776   -295       O  
ATOM    491  N   MET A 388      -1.129   5.697  10.995  1.00 19.78           N  
ANISOU  491  N   MET A 388     2284   2402   2829   -223    706   -214       N  
ATOM    492  CA  MET A 388      -0.995   4.321  10.520  1.00 20.26           C  
ANISOU  492  CA  MET A 388     2342   2442   2912   -293    665   -205       C  
ATOM    493  C   MET A 388      -0.659   4.353   9.051  1.00 18.92           C  
ANISOU  493  C   MET A 388     2124   2299   2764   -264    511   -224       C  
ATOM    494  O   MET A 388      -1.332   5.032   8.267  1.00 19.30           O  
ANISOU  494  O   MET A 388     2060   2387   2886   -226    454   -255       O  
ATOM    495  CB  MET A 388      -2.310   3.567  10.686  1.00 22.20           C  
ANISOU  495  CB  MET A 388     2470   2681   3284   -371    758   -224       C  
ATOM    496  CG  MET A 388      -2.835   3.567  12.087  1.00 26.10           C  
ANISOU  496  CG  MET A 388     3003   3147   3765   -402    943   -207       C  
ATOM    497  SD  MET A 388      -1.764   2.624  13.159  1.00 32.59           S  
ANISOU  497  SD  MET A 388     4060   3895   4429   -444    992   -147       S  
ATOM    498  CE  MET A 388      -2.164   0.954  12.640  1.00 32.54           C  
ANISOU  498  CE  MET A 388     4016   3840   4508   -556    987   -143       C  
ATOM    499  N   ASN A 389       0.376   3.604   8.674  1.00 17.79           N  
ANISOU  499  N   ASN A 389     2074   2131   2554   -275    446   -203       N  
ATOM    500  CA  ASN A 389       0.757   3.457   7.279  1.00 17.62           C  
ANISOU  500  CA  ASN A 389     2038   2122   2534   -252    322   -221       C  
ATOM    501  C   ASN A 389       1.073   1.987   7.028  1.00 18.06           C  
ANISOU  501  C   ASN A 389     2152   2127   2584   -308    309   -218       C  
ATOM    502  O   ASN A 389       1.760   1.369   7.830  1.00 17.79           O  
ANISOU  502  O   ASN A 389     2217   2052   2492   -320    359   -180       O  
ATOM    503  CB  ASN A 389       1.971   4.336   6.951  1.00 16.54           C  
ANISOU  503  CB  ASN A 389     1971   2003   2309   -180    264   -200       C  
ATOM    504  CG  ASN A 389       1.635   5.824   6.931  1.00 16.86           C  
ANISOU  504  CG  ASN A 389     1970   2078   2358   -124    259   -209       C  
ATOM    505  OD1 ASN A 389       0.851   6.272   6.100  1.00 18.26           O  
ANISOU  505  OD1 ASN A 389     2064   2280   2595    -98    206   -237       O  
ATOM    506  ND2 ASN A 389       2.232   6.587   7.848  1.00 17.66           N  
ANISOU  506  ND2 ASN A 389     2139   2173   2397   -102    303   -187       N  
ATOM    507  N   PHE A 390       0.577   1.445   5.915  1.00 19.26           N  
ANISOU  507  N   PHE A 390     2255   2275   2788   -336    234   -258       N  
ATOM    508  CA  PHE A 390       0.720   0.009   5.609  1.00 20.37           C  
ANISOU  508  CA  PHE A 390     2460   2350   2931   -396    223   -267       C  
ATOM    509  C   PHE A 390       0.163  -0.864   6.750  1.00 21.51           C  
ANISOU  509  C   PHE A 390     2615   2441   3117   -482    337   -248       C  
ATOM    510  O   PHE A 390       0.689  -1.951   7.031  1.00 23.00           O  
ANISOU  510  O   PHE A 390     2914   2556   3267   -511    365   -225       O  
ATOM    511  CB  PHE A 390       2.185  -0.358   5.348  1.00 19.63           C  
ANISOU  511  CB  PHE A 390     2495   2226   2737   -338    198   -238       C  
ATOM    512  CG  PHE A 390       2.878   0.525   4.345  1.00 18.71           C  
ANISOU  512  CG  PHE A 390     2384   2156   2569   -257    122   -245       C  
ATOM    513  CD1 PHE A 390       2.663   0.360   2.984  1.00 19.40           C  
ANISOU  513  CD1 PHE A 390     2474   2242   2655   -252     36   -289       C  
ATOM    514  CD2 PHE A 390       3.765   1.506   4.765  1.00 18.40           C  
ANISOU  514  CD2 PHE A 390     2362   2153   2475   -195    137   -206       C  
ATOM    515  CE1 PHE A 390       3.319   1.170   2.060  1.00 18.09           C  
ANISOU  515  CE1 PHE A 390     2336   2109   2427   -180    -16   -288       C  
ATOM    516  CE2 PHE A 390       4.425   2.326   3.851  1.00 17.30           C  
ANISOU  516  CE2 PHE A 390     2233   2047   2293   -134     85   -207       C  
ATOM    517  CZ  PHE A 390       4.198   2.159   2.493  1.00 16.79           C  
ANISOU  517  CZ  PHE A 390     2179   1979   2220   -124     17   -244       C  
ATOM    518  N   GLY A 391      -0.878  -0.366   7.421  1.00 22.38           N  
ANISOU  518  N   GLY A 391     2619   2582   3302   -517    413   -253       N  
ATOM    519  CA  GLY A 391      -1.523  -1.082   8.523  1.00 22.85           C  
ANISOU  519  CA  GLY A 391     2686   2592   3404   -606    550   -233       C  
ATOM    520  C   GLY A 391      -0.688  -1.194   9.789  1.00 22.43           C  
ANISOU  520  C   GLY A 391     2787   2498   3236   -582    643   -170       C  
ATOM    521  O   GLY A 391      -0.956  -2.043  10.651  1.00 23.43           O  
ANISOU  521  O   GLY A 391     2983   2558   3360   -654    750   -140       O  
ATOM    522  N   LYS A 392       0.321  -0.334   9.914  1.00 20.88           N  
ANISOU  522  N   LYS A 392     2652   2337   2944   -486    596   -148       N  
ATOM    523  CA  LYS A 392       1.218  -0.409  11.052  1.00 20.16           C  
ANISOU  523  CA  LYS A 392     2710   2212   2737   -458    644    -91       C  
ATOM    524  C   LYS A 392       1.697   0.964  11.486  1.00 18.83           C  
ANISOU  524  C   LYS A 392     2552   2098   2503   -384    630    -84       C  
ATOM    525  O   LYS A 392       1.444   1.965  10.815  1.00 17.99           O  
ANISOU  525  O   LYS A 392     2347   2050   2438   -345    584   -119       O  
ATOM    526  CB  LYS A 392       2.388  -1.352  10.752  1.00 20.78           C  
ANISOU  526  CB  LYS A 392     2903   2239   2754   -431    571    -60       C  
ATOM    527  CG  LYS A 392       3.413  -0.819   9.772  1.00 20.35           C  
ANISOU  527  CG  LYS A 392     2829   2230   2673   -348    452    -71       C  
ATOM    528  CD  LYS A 392       4.259  -1.960   9.190  1.00 21.82           C  
ANISOU  528  CD  LYS A 392     3091   2358   2840   -326    400    -59       C  
ATOM    529  CE  LYS A 392       5.003  -2.762  10.264  1.00 21.88           C  
ANISOU  529  CE  LYS A 392     3238   2298   2778   -310    430      5       C  
ATOM    530  NZ  LYS A 392       5.925  -3.757   9.632  1.00 19.90           N  
ANISOU  530  NZ  LYS A 392     3052   1991   2517   -259    378     17       N  
ATOM    531  N   LYS A 393       2.387   1.001  12.620  1.00 17.96           N  
ANISOU  531  N   LYS A 393     2578   1961   2286   -367    664    -39       N  
ATOM    532  CA  LYS A 393       3.044   2.207  13.064  1.00 16.83           C  
ANISOU  532  CA  LYS A 393     2474   1854   2066   -308    629    -34       C  
ATOM    533  C   LYS A 393       4.497   2.142  12.622  1.00 16.26           C  
ANISOU  533  C   LYS A 393     2445   1791   1944   -256    501     -9       C  
ATOM    534  O   LYS A 393       5.254   1.271  13.054  1.00 17.55           O  
ANISOU  534  O   LYS A 393     2705   1911   2052   -250    476     34       O  
ATOM    535  CB  LYS A 393       2.938   2.356  14.585  1.00 18.02           C  
ANISOU  535  CB  LYS A 393     2758   1968   2119   -323    728     -5       C  
ATOM    536  CG  LYS A 393       1.530   2.706  15.060  1.00 18.70           C  
ANISOU  536  CG  LYS A 393     2789   2056   2260   -360    883    -34       C  
ATOM    537  CD  LYS A 393       1.439   2.657  16.572  1.00 18.52           C  
ANISOU  537  CD  LYS A 393     2936   1982   2120   -380   1005     -2       C  
ATOM    538  CE  LYS A 393       1.324   1.227  17.077  1.00 18.86           C  
ANISOU  538  CE  LYS A 393     3077   1952   2138   -445   1073     47       C  
ATOM    539  NZ  LYS A 393       1.131   1.214  18.552  1.00 21.49           N  
ANISOU  539  NZ  LYS A 393     3595   2228   2341   -465   1209     81       N  
ATOM    540  N   LEU A 394       4.871   3.060  11.745  1.00 15.10           N  
ANISOU  540  N   LEU A 394     2221   1696   1820   -214    426    -34       N  
ATOM    541  CA  LEU A 394       6.230   3.063  11.203  1.00 14.24           C  
ANISOU  541  CA  LEU A 394     2122   1602   1685   -169    324    -14       C  
ATOM    542  C   LEU A 394       7.234   3.648  12.188  1.00 14.15           C  
ANISOU  542  C   LEU A 394     2194   1595   1589   -150    282     18       C  
ATOM    543  O   LEU A 394       6.966   4.617  12.914  1.00 14.59           O  
ANISOU  543  O   LEU A 394     2285   1657   1602   -158    308      6       O  
ATOM    544  CB  LEU A 394       6.299   3.819   9.875  1.00 13.35           C  
ANISOU  544  CB  LEU A 394     1915   1536   1623   -141    272    -47       C  
ATOM    545  CG  LEU A 394       5.533   3.190   8.712  1.00 13.73           C  
ANISOU  545  CG  LEU A 394     1895   1581   1741   -154    269    -80       C  
ATOM    546  CD1 LEU A 394       5.602   4.135   7.507  1.00 15.26           C  
ANISOU  546  CD1 LEU A 394     2027   1817   1954   -118    214   -105       C  
ATOM    547  CD2 LEU A 394       6.045   1.787   8.346  1.00 15.34           C  
ANISOU  547  CD2 LEU A 394     2142   1742   1946   -155    253    -66       C  
ATOM    548  N   ILE A 395       8.386   3.000  12.218  1.00 14.17           N  
ANISOU  548  N   ILE A 395     2228   1587   1569   -121    212     56       N  
ATOM    549  CA  ILE A 395       9.573   3.498  12.884  1.00 14.27           C  
ANISOU  549  CA  ILE A 395     2283   1614   1523    -99    129     86       C  
ATOM    550  C   ILE A 395      10.176   4.568  11.981  1.00 13.43           C  
ANISOU  550  C   ILE A 395     2081   1561   1460    -86     78     64       C  
ATOM    551  O   ILE A 395      10.603   4.268  10.876  1.00 13.41           O  
ANISOU  551  O   ILE A 395     2002   1576   1516    -59     62     62       O  
ATOM    552  CB  ILE A 395      10.577   2.346  13.091  1.00 15.11           C  
ANISOU  552  CB  ILE A 395     2427   1694   1619    -59     67    137       C  
ATOM    553  CG1 ILE A 395      10.029   1.318  14.103  1.00 18.01           C  
ANISOU  553  CG1 ILE A 395     2927   1991   1925    -75    118    169       C  
ATOM    554  CG2 ILE A 395      11.948   2.881  13.485  1.00 16.68           C  
ANISOU  554  CG2 ILE A 395     2615   1925   1795    -31    -49    164       C  
ATOM    555  N   LEU A 396      10.168   5.813  12.447  1.00 12.40           N  
ANISOU  555  N   LEU A 396     1971   1444   1294   -107     65     46       N  
ATOM    556  CA  LEU A 396      10.637   6.955  11.657  1.00 11.38           C  
ANISOU  556  CA  LEU A 396     1773   1350   1202   -108     31     27       C  
ATOM    557  C   LEU A 396      11.707   7.687  12.450  1.00 11.68           C  
ANISOU  557  C   LEU A 396     1848   1394   1196   -131    -55     41       C  
ATOM    558  O   LEU A 396      11.474   8.064  13.622  1.00 12.40           O  
ANISOU  558  O   LEU A 396     2046   1459   1207   -155    -61     34       O  
ATOM    559  CB  LEU A 396       9.490   7.931  11.346  1.00 11.57           C  
ANISOU  559  CB  LEU A 396     1789   1371   1237   -116     96    -16       C  
ATOM    560  CG  LEU A 396       8.296   7.316  10.621  1.00 12.39           C  
ANISOU  560  CG  LEU A 396     1841   1473   1394   -103    162    -36       C  
ATOM    561  CD1 LEU A 396       7.234   8.378  10.460  1.00 14.68           C  
ANISOU  561  CD1 LEU A 396     2113   1761   1702    -96    208    -74       C  
ATOM    562  CD2 LEU A 396       8.725   6.800   9.259  1.00 11.14           C  
ANISOU  562  CD2 LEU A 396     1611   1334   1287    -81    131    -32       C  
ATOM    563  N   GLU A 397      12.873   7.878  11.817  1.00 11.10           N  
ANISOU  563  N   GLU A 397     1690   1353   1175   -127   -118     58       N  
ATOM    564  CA  GLU A 397      14.029   8.455  12.507  1.00 11.99           C  
ANISOU  564  CA  GLU A 397     1807   1478   1271   -159   -222     73       C  
ATOM    565  C   GLU A 397      14.851   9.333  11.577  1.00 11.76           C  
ANISOU  565  C   GLU A 397     1674   1478   1316   -185   -241     71       C  
ATOM    566  O   GLU A 397      14.747   9.239  10.355  1.00 12.02           O  
ANISOU  566  O   GLU A 397     1635   1526   1406   -161   -178     70       O  
ATOM    567  CB  GLU A 397      14.946   7.344  13.069  1.00 12.82           C  
ANISOU  567  CB  GLU A 397     1902   1592   1378   -126   -306    120       C  
ATOM    568  CG  GLU A 397      14.259   6.223  13.886  1.00 13.37           C  
ANISOU  568  CG  GLU A 397     2084   1619   1375    -95   -279    139       C  
ATOM    569  CD  GLU A 397      13.922   6.615  15.338  1.00 16.22           C  
ANISOU  569  CD  GLU A 397     2606   1945   1613   -131   -310    133       C  
ATOM    570  OE1 GLU A 397      13.415   5.748  16.071  1.00 18.43           O  
ANISOU  570  OE1 GLU A 397     2995   2184   1823   -114   -279    155       O  
ATOM    571  OE2 GLU A 397      14.165   7.769  15.740  1.00 17.81           O  
ANISOU  571  OE2 GLU A 397     2839   2149   1780   -179   -358    106       O  
ATOM    572  N   VAL A 398      15.670  10.207  12.154  1.00 12.98           N  
ANISOU  572  N   VAL A 398     1833   1636   1464   -243   -327     69       N  
ATOM    573  CA  VAL A 398      16.664  10.901  11.345  1.00 13.91           C  
ANISOU  573  CA  VAL A 398     1837   1780   1668   -281   -344     77       C  
ATOM    574  C   VAL A 398      17.676   9.852  10.918  1.00 15.27           C  
ANISOU  574  C   VAL A 398     1879   2000   1924   -233   -369    120       C  
ATOM    575  O   VAL A 398      18.179   9.098  11.770  1.00 15.96           O  
ANISOU  575  O   VAL A 398     1967   2098   2001   -208   -459    144       O  
ATOM    576  CB  VAL A 398      17.359  12.019  12.162  1.00 14.88           C  
ANISOU  576  CB  VAL A 398     1991   1888   1773   -371   -446     62       C  
ATOM    577  CG1 VAL A 398      18.409  12.728  11.344  1.00 17.18           C  
ANISOU  577  CG1 VAL A 398     2155   2205   2169   -429   -453     75       C  
ATOM    578  CG2 VAL A 398      16.329  13.000  12.676  1.00 15.02           C  
ANISOU  578  CG2 VAL A 398     2163   1845   1698   -401   -411     16       C  
ATOM    579  N   SER A 399      17.966   9.784   9.617  1.00 15.61           N  
ANISOU  579  N   SER A 399     1824   2064   2042   -212   -287    129       N  
ATOM    580  CA  SER A 399      18.876   8.757   9.106  1.00 17.32           C  
ANISOU  580  CA  SER A 399     1919   2319   2343   -149   -280    165       C  
ATOM    581  C   SER A 399      20.319   9.064   9.455  1.00 20.23           C  
ANISOU  581  C   SER A 399     2155   2730   2803   -186   -372    191       C  
ATOM    582  O   SER A 399      20.773  10.192   9.328  1.00 20.14           O  
ANISOU  582  O   SER A 399     2102   2724   2827   -274   -383    183       O  
ATOM    583  CB  SER A 399      18.757   8.567   7.600  1.00 16.69           C  
ANISOU  583  CB  SER A 399     1796   2243   2301   -110   -152    163       C  
ATOM    584  OG  SER A 399      19.603   7.495   7.196  1.00 17.87           O  
ANISOU  584  OG  SER A 399     1846   2419   2524    -35   -132    192       O  
ATOM    585  N   SER A 400      21.016   8.024   9.885  1.00 22.25           N  
ANISOU  585  N   SER A 400     2342   3010   3102   -119   -440    224       N  
ATOM    586  CA  SER A 400      22.423   8.112  10.246  1.00 26.01           C  
ANISOU  586  CA  SER A 400     2659   3536   3688   -135   -547    254       C  
ATOM    587  C   SER A 400      23.286   7.403   9.204  1.00 28.13           C  
ANISOU  587  C   SER A 400     2758   3844   4087    -56   -458    284       C  
ATOM    588  O   SER A 400      24.518   7.400   9.310  1.00 30.26           O  
ANISOU  588  O   SER A 400     2850   4165   4484    -55   -522    312       O  
ATOM    589  CB  SER A 400      22.615   7.469  11.612  1.00 26.54           C  
ANISOU  589  CB  SER A 400     2781   3598   3706   -100   -710    275       C  
ATOM    590  OG  SER A 400      22.221   6.113  11.574  1.00 27.32           O  
ANISOU  590  OG  SER A 400     2935   3673   3774     16   -671    298       O  
ATOM    591  N   SER A 401      22.641   6.824   8.190  1.00 28.82           N  
ANISOU  591  N   SER A 401     2897   3905   4146     10   -311    274       N  
ATOM    592  CA  SER A 401      23.310   5.958   7.217  1.00 31.19           C  
ANISOU  592  CA  SER A 401     3084   4224   4541    108   -207    295       C  
ATOM    593  C   SER A 401      24.211   6.745   6.274  1.00 33.09           C  
ANISOU  593  C   SER A 401     3173   4507   4894     58   -110    302       C  
ATOM    594  O   SER A 401      23.783   7.738   5.681  1.00 32.77           O  
ANISOU  594  O   SER A 401     3188   4451   4811    -26    -35    282       O  
ATOM    595  CB  SER A 401      22.283   5.160   6.409  1.00 29.98           C  
ANISOU  595  CB  SER A 401     3066   4020   4305    177    -87    271       C  
ATOM    596  OG  SER A 401      22.906   4.388   5.389  1.00 32.54           O  
ANISOU  596  OG  SER A 401     3310   4349   4703    271     29    282       O  
ATOM    597  N   ASN A 402      25.457   6.289   6.148  1.00 35.46           N  
ANISOU  597  N   ASN A 402     3278   4855   5338    115   -107    336       N  
ATOM    598  CA  ASN A 402      26.400   6.839   5.170  1.00 37.74           C  
ANISOU  598  CA  ASN A 402     3401   5184   5753     80     23    349       C  
ATOM    599  C   ASN A 402      26.427   6.049   3.854  1.00 38.26           C  
ANISOU  599  C   ASN A 402     3476   5233   5828    190    225    347       C  
ATOM    600  O   ASN A 402      25.614   5.142   3.627  1.00 37.48           O  
ANISOU  600  O   ASN A 402     3527   5084   5628    279    257    328       O  
ATOM    601  CB  ASN A 402      27.809   6.914   5.769  1.00 40.02           C  
ANISOU  601  CB  ASN A 402     3440   5544   6223     68    -80    384       C  
ATOM    602  CG  ASN A 402      27.892   7.867   6.958  1.00 41.37           C  
ANISOU  602  CG  ASN A 402     3609   5727   6383    -65   -280    378       C  
ATOM    603  OD1 ASN A 402      27.683   9.075   6.823  1.00 44.43           O  
ANISOU  603  OD1 ASN A 402     4040   6100   6743   -204   -260    358       O  
ATOM    604  ND2 ASN A 402      28.218   7.328   8.125  1.00 43.67           N  
ANISOU  604  ND2 ASN A 402     3866   6037   6689    -21   -477    395       N  
TER     605      ASN A 402                                                      
ATOM    606  O3'   U C   0      12.523  -3.731  14.170  1.00 55.99           O  
ANISOU  606  O3'   U C   0     9646   4982   6645  -2316   2058   -268       O  
ATOM    607  P     U C   1      13.973  -3.503  14.822  1.00 52.24           P  
ANISOU  607  P     U C   1     9518   4111   6222  -1167   1713    247       P  
ATOM    608  OP1   U C   1      14.747  -4.753  14.603  1.00 57.31           O  
ANISOU  608  OP1   U C   1    11063   3706   7006   -877   2044    347       O  
ATOM    609  OP2   U C   1      13.756  -2.986  16.198  1.00 50.21           O  
ANISOU  609  OP2   U C   1     9261   4147   5670   -933   1629    656       O  
ATOM    610  O5'   U C   1      14.618  -2.336  13.944  1.00 43.32           O  
ANISOU  610  O5'   U C   1     7586   3656   5219   -737   1155     38       O  
ATOM    611  C5'   U C   1      15.666  -2.531  12.994  1.00 39.17           C  
ANISOU  611  C5'   U C   1     7044   2959   4879   -360   1032   -116       C  
ATOM    612  C4'   U C   1      16.406  -1.221  12.784  1.00 31.53           C  
ANISOU  612  C4'   U C   1     5436   2624   3920     53    555    -82       C  
ATOM    613  O4'   U C   1      15.558  -0.108  13.191  1.00 27.22           O  
ANISOU  613  O4'   U C   1     4522   2575   3245   -145    416    -48       O  
ATOM    614  C3'   U C   1      17.720  -1.069  13.549  1.00 32.10           C  
ANISOU  614  C3'   U C   1     5524   2736   3937    751    295    191       C  
ATOM    615  O3'   U C   1      18.687  -0.409  12.724  1.00 29.55           O  
ANISOU  615  O3'   U C   1     4689   2838   3701    911     70     12       O  
ATOM    616  C2'   U C   1      17.318  -0.210  14.746  1.00 29.72           C  
ANISOU  616  C2'   U C   1     5131   2747   3415    711    118    366       C  
ATOM    617  O2'   U C   1      18.376   0.582  15.244  1.00 31.43           O  
ANISOU  617  O2'   U C   1     5024   3418   3500   1033   -240    378       O  
ATOM    618  C1'   U C   1      16.258   0.690  14.123  1.00 24.79           C  
ANISOU  618  C1'   U C   1     4165   2405   2849    243    152    142       C  
ATOM    619  N1    U C   1      15.289   1.260  15.115  1.00 23.23           N  
ANISOU  619  N1    U C   1     3976   2407   2445    129    210    214       N  
ATOM    620  C2    U C   1      15.116   2.622  15.139  1.00 19.86           C  
ANISOU  620  C2    U C   1     3301   2264   1983    215     75    113       C  
ATOM    621  O2    U C   1      15.703   3.349  14.375  1.00 18.59           O  
ANISOU  621  O2    U C   1     2983   2128   1952    272    -59     28       O  
ATOM    622  N3    U C   1      14.214   3.105  16.047  1.00 21.62           N  
ANISOU  622  N3    U C   1     3549   2678   1989    235    198    117       N  
ATOM    623  C4    U C   1      13.484   2.355  16.942  1.00 26.09           C  
ANISOU  623  C4    U C   1     4278   3304   2330     71    441    235       C  
ATOM    624  O4    U C   1      12.706   2.915  17.713  1.00 30.41           O  
ANISOU  624  O4    U C   1     4762   4156   2639    129    581    188       O  
ATOM    625  C5    U C   1      13.713   0.926  16.868  1.00 29.30           C  
ANISOU  625  C5    U C   1     5023   3326   2785   -146    606    408       C  
ATOM    626  C6    U C   1      14.582   0.438  15.973  1.00 25.66           C  
ANISOU  626  C6    U C   1     4624   2553   2574    -55    492    378       C  
ATOM    627  P     C C   2      20.246  -0.790  12.685  1.00 33.93           P  
ANISOU  627  P     C C   2     5042   3618   4234   1590    -60     47       P  
ATOM    628  OP1   C C   2      20.432  -2.242  12.747  1.00 40.13           O  
ANISOU  628  OP1   C C   2     6435   3770   5044   2131    234    180       O  
ATOM    629  OP2   C C   2      20.926   0.106  13.643  1.00 36.43           O  
ANISOU  629  OP2   C C   2     4946   4563   4331   1714   -427    137       O  
ATOM    630  O5'   C C   2      20.660  -0.271  11.236  1.00 31.59           O  
ANISOU  630  O5'   C C   2     4269   3676   4060   1324    -28   -281       O  
ATOM    631  C5'   C C   2      20.045  -0.755  10.050  1.00 29.62           C  
ANISOU  631  C5'   C C   2     4191   3171   3891   1019    247   -536       C  
ATOM    632  C4'   C C   2      20.268   0.226   8.907  1.00 25.34           C  
ANISOU  632  C4'   C C   2     3165   3175   3289    692    202   -688       C  
ATOM    633  O4'   C C   2      19.453   1.408   9.126  1.00 20.62           O  
ANISOU  633  O4'   C C   2     2505   2701   2628    324     67   -519       O  
ATOM    634  C3'   C C   2      21.694   0.746   8.721  1.00 27.57           C  
ANISOU  634  C3'   C C   2     2923   4016   3537    885    120   -717       C  
ATOM    635  O3'   C C   2      21.870   1.033   7.368  1.00 28.81           O  
ANISOU  635  O3'   C C   2     2859   4495   3592    629    298   -888       O  
ATOM    636  C2'   C C   2      21.654   2.052   9.503  1.00 24.73           C  
ANISOU  636  C2'   C C   2     2428   3824   3142    545    -95   -547       C  
ATOM    637  O2'   C C   2      22.651   2.984   9.137  1.00 28.18           O  
ANISOU  637  O2'   C C   2     2417   4781   3511    226    -78   -635       O  
ATOM    638  C1'   C C   2      20.269   2.557   9.097  1.00 20.52           C  
ANISOU  638  C1'   C C   2     2207   3001   2588    216    -25   -445       C  
ATOM    639  N1    C C   2      19.763   3.549  10.066  1.00 18.09           N  
ANISOU  639  N1    C C   2     2065   2538   2269     78   -139   -291       N  
ATOM    640  C2    C C   2      19.639   4.897   9.673  1.00 18.45           C  
ANISOU  640  C2    C C   2     2206   2543   2262   -188    -48   -185       C  
ATOM    641  O2    C C   2      19.937   5.235   8.522  1.00 19.31           O  
ANISOU  641  O2    C C   2     2238   2809   2291   -334    110   -131       O  
ATOM    642  N3    C C   2      19.205   5.798  10.584  1.00 17.65           N  
ANISOU  642  N3    C C   2     2392   2162   2153   -240    -63   -134       N  
ATOM    643  C4    C C   2      18.892   5.417  11.825  1.00 17.14           C  
ANISOU  643  C4    C C   2     2398   2042   2070    -92   -205   -193       C  
ATOM    644  N4    C C   2      18.473   6.370  12.659  1.00 18.14           N  
ANISOU  644  N4    C C   2     2831   1928   2135   -140   -162   -230       N  
ATOM    645  C5    C C   2      19.013   4.057  12.250  1.00 17.77           C  
ANISOU  645  C5    C C   2     2368   2236   2149    150   -315   -197       C  
ATOM    646  C6    C C   2      19.443   3.169  11.347  1.00 18.96           C  
ANISOU  646  C6    C C   2     2356   2478   2371    251   -257   -239       C  
ATOM    647  P     U C   3      23.240   0.769   6.577  1.00 36.08           P  
ANISOU  647  P     U C   3     3280   6002   4425    883    479  -1124       P  
ATOM    648  OP1   U C   3      23.936   2.063   6.366  1.00 37.49           O  
ANISOU  648  OP1   U C   3     2985   6765   4493    384    477  -1038       O  
ATOM    649  OP2   U C   3      23.995  -0.360   7.176  1.00 39.90           O  
ANISOU  649  OP2   U C   3     3739   6435   4985   1701    493  -1206       O  
ATOM    650  O5'   U C   3      22.651   0.304   5.168  1.00 37.11           O  
ANISOU  650  O5'   U C   3     3627   6089   4385    702    755  -1388       O  
ATOM    651  C5'   U C   3      21.784  -0.815   5.029  1.00 40.70           C  
ANISOU  651  C5'   U C   3     4615   5978   4872    762    887  -1646       C  
ATOM    652  C4'   U C   3      21.392  -0.963   3.563  1.00 44.05           C  
ANISOU  652  C4'   U C   3     5028   6755   4952    411   1101  -2014       C  
ATOM    653  O4'   U C   3      20.641   0.213   3.161  1.00 41.42           O  
ANISOU  653  O4'   U C   3     4514   6871   4353    -39    909  -1697       O  
ATOM    654  C3'   U C   3      22.543  -1.066   2.559  1.00 49.96           C  
ANISOU  654  C3'   U C   3     5417   8075   5491    642   1379  -2282       C  
ATOM    655  O3'   U C   3      22.164  -1.913   1.483  1.00 56.51           O  
ANISOU  655  O3'   U C   3     6514   8928   6030    506   1669  -2863       O  
ATOM    656  C2'   U C   3      22.681   0.368   2.057  1.00 47.83           C  
ANISOU  656  C2'   U C   3     4743   8478   4953    217   1290  -1884       C  
ATOM    657  O2'   U C   3      23.327   0.454   0.802  1.00 53.00           O  
ANISOU  657  O2'   U C   3     5107   9833   5197    136   1602  -2087       O  
ATOM    658  C1'   U C   3      21.199   0.735   1.963  1.00 44.58           C  
ANISOU  658  C1'   U C   3     4624   7948   4368   -147   1075  -1705       C  
ATOM    659  N1    U C   3      20.892   2.216   1.818  1.00 42.95           N  
ANISOU  659  N1    U C   3     4362   8003   3954   -374    957  -1111       N  
ATOM    660  C2    U C   3      20.262   2.671   0.665  1.00 45.87           C  
ANISOU  660  C2    U C   3     4738   8953   3735   -502    989   -958       C  
ATOM    661  O2    U C   3      19.922   1.952  -0.253  1.00 50.52           O  
ANISOU  661  O2    U C   3     5259  10022   3916   -574   1054  -1378       O  
ATOM    662  N3    U C   3      20.030   4.025   0.615  1.00 46.45           N  
ANISOU  662  N3    U C   3     4979   9035   3636   -509    972   -292       N  
ATOM    663  C4    U C   3      20.355   4.961   1.585  1.00 44.53           C  
ANISOU  663  C4    U C   3     4945   8190   3784   -563    977     87       C  
ATOM    664  O4    U C   3      20.079   6.146   1.403  1.00 47.30           O  
ANISOU  664  O4    U C   3     5658   8381   3933   -542   1084    655       O  
ATOM    665  C5    U C   3      21.013   4.420   2.752  1.00 40.72           C  
ANISOU  665  C5    U C   3     4305   7312   3854   -588    886   -237       C  
ATOM    666  C6    U C   3      21.251   3.100   2.823  1.00 39.79           C  
ANISOU  666  C6    U C   3     3990   7256   3874   -408    858   -736       C  
ATOM    667  P     U C   4      22.934  -3.277   1.147  1.00 66.68           P  
ANISOU  667  P     U C   4     8112   9841   7383   1109   2133  -3486       P  
ATOM    668  OP1   U C   4      24.387  -3.010   1.025  1.00 69.66           O  
ANISOU  668  OP1   U C   4     7855  10869   7743   1717   2264  -3398       O  
ATOM    669  OP2   U C   4      22.245  -3.908  -0.001  1.00 70.93           O  
ANISOU  669  OP2   U C   4     8997  10438   7514    620   2409  -4186       O  
ATOM    670  O5'   U C   4      22.648  -4.141   2.467  1.00 66.38           O  
ANISOU  670  O5'   U C   4     8747   8648   7826   1498   2127  -3354       O  
TER     671        U C   4                                                      
HETATM  672  C   ACT A1000      12.362   8.654  -6.332  1.00 37.07           C  
HETATM  673  O   ACT A1000      12.328   9.880  -6.059  1.00 37.36           O  
HETATM  674  OXT ACT A1000      11.264   8.143  -6.673  1.00 37.59           O  
HETATM  675  CH3 ACT A1000      13.636   7.856  -6.257  1.00 36.20           C  
HETATM  676  C   ACT A1001      22.200  13.153   4.226  1.00 56.95           C  
HETATM  677  O   ACT A1001      22.465  12.771   5.389  1.00 57.07           O  
HETATM  678  OXT ACT A1001      22.609  12.424   3.294  1.00 56.95           O  
HETATM  679  CH3 ACT A1001      21.434  14.414   3.968  1.00 56.61           C  
HETATM  680  O   HOH A2001      10.218  -5.186  10.763  1.00 19.13           O  
HETATM  681  O   HOH A2002       3.885  -8.695  -3.647  1.00 20.90           O  
HETATM  682  O   HOH A2003      -0.348  -1.954   1.792  1.00 29.96           O  
HETATM  683  O   HOH A2004      -0.604   1.946   1.307  1.00 41.72           O  
HETATM  684  O   HOH A2005      16.519  16.351  10.414  1.00  9.01           O  
HETATM  685  O   HOH A2006      17.555   7.922  -0.239  1.00 24.88           O  
HETATM  686  O   HOH A2007      19.910  12.453   7.510  1.00 15.69           O  
HETATM  687  O   HOH A2008      12.435  -3.993  11.031  1.00 18.48           O  
HETATM  688  O   HOH A2009       8.686  -5.093   8.625  1.00 15.80           O  
HETATM  689  O   HOH A2010      11.477  -6.724   0.547  1.00 27.47           O  
HETATM  690  O   HOH A2011       6.043  -8.039   5.664  1.00 10.03           O  
HETATM  691  O   HOH A2012       4.178  -7.554   3.436  1.00 22.38           O  
HETATM  692  O   HOH A2013       1.931  -3.051   2.092  1.00 26.05           O  
HETATM  693  O   HOH A2014       6.416  -6.803  -3.417  1.00 18.73           O  
HETATM  694  O   HOH A2015      -0.156  -6.365   1.483  1.00 31.91           O  
HETATM  695  O   HOH A2016       9.402  -3.444  -1.292  1.00 23.39           O  
HETATM  696  O   HOH A2017       7.355  -4.410  -2.554  1.00 27.05           O  
HETATM  697  O   HOH A2018       6.782   3.337  -7.305  1.00  9.95           O  
HETATM  698  O   HOH A2019       0.641   5.398   0.313  1.00 23.50           O  
HETATM  699  O   HOH A2020      -0.195   4.897  -1.969  1.00 24.62           O  
HETATM  700  O   HOH A2021      -0.012  12.806  -0.357  1.00 25.30           O  
HETATM  701  O   HOH A2022       0.937  11.934   4.654  1.00 16.47           O  
HETATM  702  O   HOH A2023      11.301  20.866   0.735  1.00 10.52           O  
HETATM  703  O   HOH A2024      10.031  14.750  -5.647  1.00 10.43           O  
HETATM  704  O   HOH A2025      16.947  13.324  -7.632  1.00 14.01           O  
HETATM  705  O   HOH A2026      14.318  -4.039  -1.482  1.00 18.79           O  
HETATM  706  O   HOH A2027      13.049  -6.303  -1.631  1.00 26.51           O  
HETATM  707  O   HOH A2028       9.841  -3.360   1.440  1.00 15.06           O  
HETATM  708  O   HOH A2029      11.548  20.811  14.335  1.00 29.32           O  
HETATM  709  O   HOH A2030       7.071  20.173   6.450  1.00  8.74           O  
HETATM  710  O   HOH A2031       8.335  19.264  13.476  1.00 25.59           O  
HETATM  711  O   HOH A2032       7.473  23.109   9.173  1.00 17.00           O  
HETATM  712  O   HOH A2033       4.550  11.577  17.557  1.00 33.95           O  
HETATM  713  O   HOH A2034       8.130   6.602  14.640  1.00 17.21           O  
HETATM  714  O   HOH A2035      -1.512  15.638  16.695  1.00 10.20           O  
HETATM  715  O   HOH A2036       3.390   5.528  10.665  1.00 12.44           O  
HETATM  716  O   HOH A2037      -0.378  13.421  12.178  1.00 22.14           O  
HETATM  717  O   HOH A2038      -0.498   5.128   4.249  1.00 29.41           O  
HETATM  718  O   HOH A2039      -1.038   2.670   3.830  1.00 26.90           O  
HETATM  719  O   HOH A2040      -2.559   2.104   7.354  1.00 19.08           O  
HETATM  720  O   HOH A2041       5.285   5.259  14.946  1.00 17.77           O  
HETATM  721  O   HOH A2042      15.057   8.136  18.193  1.00  6.24           O  
HETATM  722  O   HOH A2043      10.460   5.529  15.558  1.00 17.58           O  
HETATM  723  O   HOH A2044      26.809   6.780  10.648  1.00 16.76           O  
HETATM  724  O   HOH A2045      30.346   9.034   6.281  1.00 22.48           O  
HETATM  725  O   HOH A2046       9.899  11.918  -5.710  1.00 35.04           O  
HETATM  726  O   HOH A2047       9.084   9.441  -5.930  1.00 36.55           O  
CONECT  672  673  674  675                                                      
CONECT  673  672                                                                
CONECT  674  672                                                                
CONECT  675  672                                                                
CONECT  676  677  678  679                                                      
CONECT  677  676                                                                
CONECT  678  676                                                                
CONECT  679  676                                                                
MASTER      353    0    2    3    4    0    2    6  724    2    8    9          
END

Display Options: Goto PDB code: 3D presentation of molecule is powered by 3Dmol, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button: left to rotate,middle to shift,right to zoom

Related entries of code: 2xnr

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
2kkf	RCSB PDB PDBbind	12-mer
3bsu	RCSB PDB PDBbind	12-mer
3kjp	RCSB PDB PDBbind	12-mer
3lwl	RCSB PDB PDBbind	12-mer
3lwm	RCSB PDB PDBbind	12-mer
3m8r	RCSB PDB PDBbind	12-mer
3m8s	RCSB PDB PDBbind	12-mer
3nmr	RCSB PDB PDBbind	12-mer
3odh	RCSB PDB PDBbind	12-mer
5exh	RCSB PDB PDBbind	12-mer
5mpf	RCSB PDB PDBbind	12-mer

Entry Information

PDB ID	2xnr
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	Nab3-RRM(404)
Ligand Name	12-mer
EC.Number	E.C.-.-.-.-
Resolution	1.6(Å)
Affinity (Kd/Ki/IC50)	Kd=110uM
Release Year	2010
Protein/NA Sequence	Check fasta file
Primary Reference	(2011) Nucleic Acids Res. Vol. 39: pp. 337-346

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): P38996
Entrez Gene ID	NCBI Entrez Gene ID: 855911
ASD	Information of known allosteric effects of PDB entries

This site has been visited

times since Nov 2007.

Technical Support（技术支持）: yingsaisi@foxmail.com