CNRS Nantes University UFIP UFIP
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***  NM_MD2  ***

elNémo ID: 220203174926120771

Job options:

ID        	=	 220203174926120771
JOBID     	=	 NM_MD2
USERID    	=	 Matos
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER NM_MD2

HEADER    TRANSFERASE                             04-JAN-11   3Q71              
TITLE     HUMAN PARP14 (ARTD8) - MACRO DOMAIN 2 IN COMPLEX WITH ADENOSINE-5-    
TITLE    2 DIPHOSPHORIBOSE                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 14;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: MACRO DOMAIN 2;                                            
COMPND   5 SYNONYM: PARP-14, B AGGRESSIVE LYMPHOMA PROTEIN 2;                   
COMPND   6 EC: 2.4.2.30;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BAL2, KIAA1268, PARP14;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) R3 PRARE;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4                                 
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,             
KEYWDS   2 TRANSFERASE, PARP14 MACRO 2                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KARLBERG,M.I.SIPONEN,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,R.COLLINS, 
AUTHOR   2 A.M.EDWARDS,T.EKBLAD,S.FLODIN,A.FLORES,S.GRASLUND,T.KOTENYOVA,       
AUTHOR   3 E.KOUZNETSOVA,M.MOCHE,P.NORDLUND,T.NYMAN,C.PERSSON,A.SEHIC,          
AUTHOR   4 A.G.THORSELL,L.TRESAUGUES,E.WAHLBERG,J.WEIGELT,M.WELIN,H.SCHULER,    
AUTHOR   5 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   3   07-MAR-18 3Q71    1       REMARK                                   
REVDAT   2   20-MAR-13 3Q71    1       JRNL   VERSN                             
REVDAT   1   26-JAN-11 3Q71    0                                                
JRNL        AUTH   A.H.FORST,T.KARLBERG,N.HERZOG,A.G.THORSELL,A.GROSS,          
JRNL        AUTH 2 K.L.FEIJS,P.VERHEUGD,P.KURSULA,B.NIJMEIJER,E.KREMMER,        
JRNL        AUTH 3 H.KLEINE,A.G.LADURNER,H.SCHULER,B.LUSCHER                    
JRNL        TITL   RECOGNITION OF MONO-ADP-RIBOSYLATED ARTD10 SUBSTRATES BY     
JRNL        TITL 2 ARTD8 MACRODOMAINS.                                          
JRNL        REF    STRUCTURE                     V.  21   462 2013              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   23473667                                                     
JRNL        DOI    10.1016/J.STR.2012.12.019                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 13357                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1484                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 971                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 107                          
REMARK   3   BIN FREE R VALUE                    : 0.2750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1568                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.67000                                              
REMARK   3    B22 (A**2) : 0.67000                                              
REMARK   3    B33 (A**2) : -1.01000                                             
REMARK   3    B12 (A**2) : 0.34000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.181         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.112         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.396         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1635 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1093 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2218 ; 1.298 ; 2.002       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2673 ; 0.830 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   202 ; 5.358 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    66 ;32.044 ;25.455       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   291 ;14.700 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;20.401 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   260 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1764 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   294 ; 0.001 ; 0.020       
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):  1007 ; 0.587 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   412 ; 0.109 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1627 ; 1.155 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   628 ; 1.824 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   591 ; 3.190 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3Q71 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063274.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-5                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9077                             
REMARK 200  MONOCHROMATOR                  : BENT SI (220) CRYSTAL              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14842                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : 0.12200                            
REMARK 200   FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.39100                            
REMARK 200   FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3IID                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M AMMONIUM SULFATE, 0.1M SODIUM       
REMARK 280  ACETATE, 0.4M SODIUM CHLORIDE, 4MM ADP-RIBOSE, 4MM MAGNESIUM        
REMARK 280  CHLORIDE, PH 5.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.79333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.89667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       36.89667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       73.79333            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   976                                                      
REMARK 465     HIS A   977                                                      
REMARK 465     HIS A   978                                                      
REMARK 465     HIS A   979                                                      
REMARK 465     HIS A   980                                                      
REMARK 465     HIS A   981                                                      
REMARK 465     HIS A   982                                                      
REMARK 465     SER A   983                                                      
REMARK 465     SER A   984                                                      
REMARK 465     GLY A   985                                                      
REMARK 465     VAL A   986                                                      
REMARK 465     ASP A   987                                                      
REMARK 465     LEU A   988                                                      
REMARK 465     GLY A  1192                                                      
REMARK 465     ASN A  1193                                                      
REMARK 465     LEU A  1194                                                      
REMARK 465     VAL A  1195                                                      
REMARK 465     SER A  1196                                                      
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    LYS A1000       -2.94     73.05                                   
REMARK 500    TRP A1082     -121.90     55.55                                   
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 AR6 A 800                 
DBREF  3Q71 A  999  1196  UNP    Q460N5   PAR14_HUMAN    918   1115             
SEQADV 3Q71 MET A  976  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 HIS A  977  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 HIS A  978  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 HIS A  979  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 HIS A  980  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 HIS A  981  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 HIS A  982  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 SER A  983  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 SER A  984  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 GLY A  985  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 VAL A  986  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 ASP A  987  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 LEU A  988  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 GLY A  989  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 THR A  990  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 GLU A  991  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 ASN A  992  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 LEU A  993  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 TYR A  994  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 PHE A  995  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 GLN A  996  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 SER A  997  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 3Q71 MET A  998  UNP  Q460N5              EXPRESSION TAG                 
SEQRES   1 A  221  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  221  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY LYS THR          
SEQRES   3 A  221  SER TRP GLU LYS GLY SER LEU VAL SER PRO GLY GLY LEU          
SEQRES   4 A  221  GLN MET LEU LEU VAL LYS GLU GLY VAL GLN ASN ALA LYS          
SEQRES   5 A  221  THR ASP VAL VAL VAL ASN SER VAL PRO LEU ASP LEU VAL          
SEQRES   6 A  221  LEU SER ARG GLY PRO LEU SER LYS SER LEU LEU GLU LYS          
SEQRES   7 A  221  ALA GLY PRO GLU LEU GLN GLU GLU LEU ASP THR VAL GLY          
SEQRES   8 A  221  GLN GLY VAL ALA VAL SER MET GLY THR VAL LEU LYS THR          
SEQRES   9 A  221  SER SER TRP ASN LEU ASP CYS ARG TYR VAL LEU HIS VAL          
SEQRES  10 A  221  VAL ALA PRO GLU TRP ARG ASN GLY SER THR SER SER LEU          
SEQRES  11 A  221  LYS ILE MET GLU ASP ILE ILE ARG GLU CYS MET GLU ILE          
SEQRES  12 A  221  THR GLU SER LEU SER LEU LYS SER ILE ALA PHE PRO ALA          
SEQRES  13 A  221  ILE GLY THR GLY ASN LEU GLY PHE PRO LYS ASN ILE PHE          
SEQRES  14 A  221  ALA GLU LEU ILE ILE SER GLU VAL PHE LYS PHE SER SER          
SEQRES  15 A  221  LYS ASN GLN LEU LYS THR LEU GLN GLU VAL HIS PHE LEU          
SEQRES  16 A  221  LEU HIS PRO SER ASP HIS GLU ASN ILE GLN ALA PHE SER          
SEQRES  17 A  221  ASP GLU PHE ALA ARG ARG ALA ASN GLY ASN LEU VAL SER          
HET    AR6  A 800      36                                                       
HETNAM     AR6 [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-              
HETNAM   2 AR6  OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-              
HETNAM   3 AR6  TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN              
HETNAM   4 AR6  PHOSPHATE                                                       
FORMUL   2  AR6    C15 H23 N5 O14 P2                                            
FORMUL   3  HOH   *88(H2 O)                                                     
HELIX    1   1 GLY A 1022  ALA A 1026  5                                   5    
HELIX    2   2 GLY A 1044  GLY A 1055  1                                  12    
HELIX    3   3 PRO A 1056  GLY A 1068  1                                  13    
HELIX    4   4 SER A 1101  LEU A 1122  1                                  22    
HELIX    5   5 PRO A 1140  ASN A 1159  1                                  20    
HELIX    6   6 ASP A 1175  ASN A 1191  1                                  17    
SHEET    1   A 2 TYR A 994  GLN A 996  0                                        
SHEET    2   A 2 TRP A1003  LYS A1005 -1  O  GLU A1004   N  PHE A 995           
SHEET    1   B 7 SER A1007  VAL A1009  0                                        
SHEET    2   B 7 GLN A1015  LYS A1020 -1  O  MET A1016   N  LEU A1008           
SHEET    3   B 7 GLU A1166  LEU A1171  1  O  PHE A1169   N  LEU A1017           
SHEET    4   B 7 SER A1126  PRO A1130  1  N  ILE A1127   O  HIS A1168           
SHEET    5   B 7 VAL A1030  SER A1034  1  N  VAL A1030   O  ALA A1128           
SHEET    6   B 7 TYR A1088  VAL A1092  1  O  VAL A1092   N  ASN A1033           
SHEET    7   B 7 VAL A1076  SER A1080 -1  N  LEU A1077   O  HIS A1091           
SITE     1 AC1 25 HOH A   7  HOH A  13  HOH A  22  HOH A  27                    
SITE     2 AC1 25 HOH A  41  HOH A  59  HOH A  87  GLY A1022                    
SITE     3 AC1 25 VAL A1023  GLN A1024  SER A1034  PRO A1036                    
SITE     4 AC1 25 GLY A1044  PRO A1045  LEU A1046  SER A1049                    
SITE     5 AC1 25 ALA A1131  GLY A1133  THR A1134  GLY A1135                    
SITE     6 AC1 25 ASN A1136  LEU A1137  HIS A1172  ASP A1175                    
SITE     7 AC1 25 ASN A1178                                                     
CRYST1   66.350   66.350  110.690  90.00  90.00 120.00 P 32 2 1      6          
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      0.015072  0.008702  0.000000        0.00000                         
SCALE2      0.000000  0.017403  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009034        0.00000                         
ATOM      1  N   GLY A 989     -34.551  -7.775 -22.269  1.00 33.14           N  
ATOM      2  CA  GLY A 989     -33.272  -8.072 -23.006  1.00 32.84           C  
ATOM      3  C   GLY A 989     -32.032  -7.857 -22.147  1.00 32.55           C  
ATOM      4  O   GLY A 989     -32.138  -7.331 -21.035  1.00 32.75           O  
ATOM      5  N   THR A 990     -30.862  -8.237 -22.684  1.00 31.98           N  
ATOM      6  CA  THR A 990     -29.555  -8.136 -21.993  1.00 31.38           C  
ATOM      7  C   THR A 990     -29.095  -6.697 -21.712  1.00 31.08           C  
ATOM      8  O   THR A 990     -28.201  -6.462 -20.882  1.00 31.12           O  
ATOM      9  CB  THR A 990     -28.412  -8.804 -22.820  1.00 31.43           C  
ATOM     10  OG1 THR A 990     -28.361  -8.230 -24.133  1.00 30.80           O  
ATOM     11  CG2 THR A 990     -28.637 -10.295 -22.942  1.00 30.57           C  
ATOM     12  N   GLU A 991     -29.676  -5.740 -22.435  1.00 30.05           N  
ATOM     13  CA  GLU A 991     -29.368  -4.334 -22.234  1.00 28.91           C  
ATOM     14  C   GLU A 991     -30.207  -3.770 -21.088  1.00 26.93           C  
ATOM     15  O   GLU A 991     -29.954  -2.652 -20.658  1.00 26.44           O  
ATOM     16  CB  GLU A 991     -29.571  -3.542 -23.540  1.00 29.71           C  
ATOM     17  CG  GLU A 991     -31.048  -3.279 -23.986  1.00 31.90           C  
ATOM     18  CD  GLU A 991     -31.789  -4.508 -24.516  1.00 35.85           C  
ATOM     19  OE1 GLU A 991     -33.008  -4.385 -24.766  1.00 37.95           O  
ATOM     20  OE2 GLU A 991     -31.171  -5.595 -24.687  1.00 38.84           O  
ATOM     21  N   ASN A 992     -31.197  -4.533 -20.603  1.00 24.49           N  
ATOM     22  CA  ASN A 992     -31.992  -4.132 -19.434  1.00 22.91           C  
ATOM     23  C   ASN A 992     -31.150  -4.349 -18.168  1.00 21.29           C  
ATOM     24  O   ASN A 992     -30.842  -5.469 -17.771  1.00 21.57           O  
ATOM     25  CB  ASN A 992     -33.343  -4.880 -19.380  1.00 23.03           C  
ATOM     26  CG  ASN A 992     -34.346  -4.307 -18.312  1.00 23.49           C  
ATOM     27  OD1 ASN A 992     -35.336  -4.973 -17.965  1.00 24.28           O  
ATOM     28  ND2 ASN A 992     -34.098  -3.097 -17.816  1.00 22.58           N  
ATOM     29  N   LEU A 993     -30.745  -3.249 -17.562  1.00 19.38           N  
ATOM     30  CA  LEU A 993     -29.950  -3.290 -16.360  1.00 17.93           C  
ATOM     31  C   LEU A 993     -30.780  -3.818 -15.201  1.00 16.96           C  
ATOM     32  O   LEU A 993     -32.016  -3.738 -15.213  1.00 15.35           O  
ATOM     33  CB  LEU A 993     -29.454  -1.892 -16.022  1.00 17.77           C  
ATOM     34  CG  LEU A 993     -28.464  -1.292 -17.015  1.00 17.54           C  
ATOM     35  CD1 LEU A 993     -28.395   0.214 -16.830  1.00 16.25           C  
ATOM     36  CD2 LEU A 993     -27.085  -1.952 -16.815  1.00 17.61           C  
ATOM     37  N   TYR A 994     -30.070  -4.359 -14.218  1.00 15.74           N  
ATOM     38  CA  TYR A 994     -30.624  -4.632 -12.902  1.00 15.00           C  
ATOM     39  C   TYR A 994     -30.200  -3.520 -11.958  1.00 15.17           C  
ATOM     40  O   TYR A 994     -29.222  -2.812 -12.212  1.00 14.81           O  
ATOM     41  CB  TYR A 994     -30.061  -5.930 -12.341  1.00 14.64           C  
ATOM     42  CG  TYR A 994     -30.703  -7.201 -12.829  1.00 12.36           C  
ATOM     43  CD1 TYR A 994     -31.313  -8.069 -11.929  1.00 11.47           C  
ATOM     44  CD2 TYR A 994     -30.664  -7.562 -14.168  1.00 11.57           C  
ATOM     45  CE1 TYR A 994     -31.880  -9.258 -12.340  1.00 11.46           C  
ATOM     46  CE2 TYR A 994     -31.238  -8.754 -14.607  1.00 12.15           C  
ATOM     47  CZ  TYR A 994     -31.836  -9.611 -13.676  1.00 11.43           C  
ATOM     48  OH  TYR A 994     -32.418 -10.783 -14.085  1.00  7.68           O  
ATOM     49  N   PHE A 995     -30.927  -3.384 -10.851  1.00 15.34           N  
ATOM     50  CA  PHE A 995     -30.470  -2.555  -9.750  1.00 14.85           C  
ATOM     51  C   PHE A 995     -30.364  -3.436  -8.523  1.00 15.46           C  
ATOM     52  O   PHE A 995     -31.131  -4.382  -8.362  1.00 15.48           O  
ATOM     53  CB  PHE A 995     -31.416  -1.369  -9.506  1.00 14.66           C  
ATOM     54  CG  PHE A 995     -32.801  -1.754  -9.068  1.00 12.88           C  
ATOM     55  CD1 PHE A 995     -33.817  -1.912  -9.998  1.00 12.34           C  
ATOM     56  CD2 PHE A 995     -33.095  -1.948  -7.729  1.00 11.58           C  
ATOM     57  CE1 PHE A 995     -35.103  -2.255  -9.597  1.00 11.86           C  
ATOM     58  CE2 PHE A 995     -34.390  -2.289  -7.322  1.00 11.18           C  
ATOM     59  CZ  PHE A 995     -35.385  -2.440  -8.253  1.00 10.74           C  
ATOM     60  N   GLN A 996     -29.398  -3.131  -7.671  1.00 16.29           N  
ATOM     61  CA  GLN A 996     -29.228  -3.844  -6.423  1.00 16.95           C  
ATOM     62  C   GLN A 996     -30.234  -3.303  -5.443  1.00 17.40           C  
ATOM     63  O   GLN A 996     -30.344  -2.083  -5.281  1.00 17.53           O  
ATOM     64  CB  GLN A 996     -27.820  -3.629  -5.872  1.00 17.44           C  
ATOM     65  CG  GLN A 996     -27.519  -4.441  -4.624  1.00 17.55           C  
ATOM     66  CD  GLN A 996     -26.088  -4.311  -4.184  1.00 18.68           C  
ATOM     67  OE1 GLN A 996     -25.458  -3.278  -4.392  1.00 19.63           O  
ATOM     68  NE2 GLN A 996     -25.559  -5.362  -3.564  1.00 18.25           N  
ATOM     69  N   SER A 997     -30.973  -4.214  -4.808  1.00 18.04           N  
ATOM     70  CA  SER A 997     -31.864  -3.881  -3.705  1.00 18.44           C  
ATOM     71  C   SER A 997     -31.098  -3.170  -2.599  1.00 19.12           C  
ATOM     72  O   SER A 997     -29.893  -3.398  -2.418  1.00 18.60           O  
ATOM     73  CB  SER A 997     -32.518  -5.141  -3.153  1.00 18.30           C  
ATOM     74  OG  SER A 997     -33.239  -5.834  -4.171  1.00 19.02           O  
ATOM     75  N   MET A 998     -31.793  -2.311  -1.856  1.00 20.10           N  
ATOM     76  CA  MET A 998     -31.140  -1.500  -0.821  1.00 21.19           C  
ATOM     77  C   MET A 998     -30.489  -2.348   0.267  1.00 21.36           C  
ATOM     78  O   MET A 998     -29.433  -1.979   0.781  1.00 21.47           O  
ATOM     79  CB  MET A 998     -32.111  -0.479  -0.212  1.00 21.60           C  
ATOM     80  CG  MET A 998     -32.300   0.753  -1.098  1.00 23.33           C  
ATOM     81  SD  MET A 998     -33.447   1.939  -0.391  1.00 28.28           S  
ATOM     82  CE  MET A 998     -32.337   2.792   0.740  1.00 26.86           C  
ATOM     83  N   GLY A 999     -31.093  -3.491   0.582  1.00 21.61           N  
ATOM     84  CA  GLY A 999     -30.486  -4.455   1.512  1.00 22.00           C  
ATOM     85  C   GLY A 999     -29.238  -5.164   0.977  1.00 22.12           C  
ATOM     86  O   GLY A 999     -28.568  -5.876   1.715  1.00 22.08           O  
ATOM     87  N   LYS A1000     -28.959  -5.000  -0.318  1.00 22.34           N  
ATOM     88  CA  LYS A1000     -27.719  -5.468  -0.974  1.00 22.48           C  
ATOM     89  C   LYS A1000     -27.585  -6.975  -1.201  1.00 21.57           C  
ATOM     90  O   LYS A1000     -26.630  -7.412  -1.831  1.00 22.13           O  
ATOM     91  CB  LYS A1000     -26.464  -4.915  -0.271  1.00 23.34           C  
ATOM     92  CG  LYS A1000     -26.165  -3.459  -0.642  1.00 25.40           C  
ATOM     93  CD  LYS A1000     -25.902  -2.604   0.574  1.00 28.01           C  
ATOM     94  CE  LYS A1000     -25.852  -1.133   0.199  1.00 29.47           C  
ATOM     95  NZ  LYS A1000     -24.816  -0.881  -0.840  1.00 30.97           N  
ATOM     96  N   THR A1001     -28.542  -7.770  -0.752  1.00 20.25           N  
ATOM     97  CA  THR A1001     -28.430  -9.208  -0.926  1.00 19.29           C  
ATOM     98  C   THR A1001     -29.280  -9.718  -2.092  1.00 17.94           C  
ATOM     99  O   THR A1001     -29.391 -10.921  -2.282  1.00 18.16           O  
ATOM    100  CB  THR A1001     -28.783  -9.945   0.378  1.00 19.22           C  
ATOM    101  OG1 THR A1001     -30.086  -9.545   0.814  1.00 19.88           O  
ATOM    102  CG2 THR A1001     -27.763  -9.610   1.467  1.00 19.76           C  
ATOM    103  N   SER A1002     -29.866  -8.812  -2.872  1.00 16.52           N  
ATOM    104  CA  SER A1002     -30.633  -9.196  -4.055  1.00 15.67           C  
ATOM    105  C   SER A1002     -30.519  -8.166  -5.171  1.00 15.26           C  
ATOM    106  O   SER A1002     -30.092  -7.044  -4.937  1.00 14.53           O  
ATOM    107  CB  SER A1002     -32.105  -9.444  -3.707  1.00 15.34           C  
ATOM    108  OG  SER A1002     -32.779  -8.249  -3.366  1.00 15.44           O  
ATOM    109  N   TRP A1003     -30.872  -8.580  -6.389  1.00 14.90           N  
ATOM    110  CA  TRP A1003     -30.876  -7.692  -7.556  1.00 14.58           C  
ATOM    111  C   TRP A1003     -32.163  -7.902  -8.352  1.00 14.70           C  
ATOM    112  O   TRP A1003     -32.662  -9.029  -8.487  1.00 14.07           O  
ATOM    113  CB  TRP A1003     -29.661  -7.948  -8.445  1.00 14.80           C  
ATOM    114  CG  TRP A1003     -28.341  -7.633  -7.808  1.00 14.43           C  
ATOM    115  CD1 TRP A1003     -27.551  -6.554  -8.060  1.00 14.74           C  
ATOM    116  CD2 TRP A1003     -27.646  -8.417  -6.832  1.00 14.80           C  
ATOM    117  NE1 TRP A1003     -26.422  -6.602  -7.291  1.00 14.81           N  
ATOM    118  CE2 TRP A1003     -26.451  -7.741  -6.533  1.00 15.58           C  
ATOM    119  CE3 TRP A1003     -27.926  -9.622  -6.175  1.00 15.91           C  
ATOM    120  CZ2 TRP A1003     -25.525  -8.228  -5.603  1.00 17.51           C  
ATOM    121  CZ3 TRP A1003     -27.011 -10.110  -5.254  1.00 15.59           C  
ATOM    122  CH2 TRP A1003     -25.825  -9.411  -4.972  1.00 16.45           C  
ATOM    123  N   GLU A1004     -32.709  -6.804  -8.864  1.00 14.74           N  
ATOM    124  CA  GLU A1004     -34.017  -6.833  -9.510  1.00 14.99           C  
ATOM    125  C   GLU A1004     -33.897  -6.273 -10.915  1.00 14.12           C  
ATOM    126  O   GLU A1004     -33.094  -5.392 -11.152  1.00 12.94           O  
ATOM    127  CB  GLU A1004     -35.007  -6.043  -8.656  1.00 15.69           C  
ATOM    128  CG  GLU A1004     -34.839  -6.422  -7.183  1.00 18.63           C  
ATOM    129  CD  GLU A1004     -35.871  -5.857  -6.264  1.00 22.32           C  
ATOM    130  OE1 GLU A1004     -35.467  -5.253  -5.240  1.00 26.16           O  
ATOM    131  OE2 GLU A1004     -37.069  -6.027  -6.541  1.00 25.41           O  
ATOM    132  N   LYS A1005     -34.662  -6.817 -11.854  1.00 14.01           N  
ATOM    133  CA  LYS A1005     -34.654  -6.283 -13.200  1.00 14.48           C  
ATOM    134  C   LYS A1005     -35.010  -4.805 -13.114  1.00 14.80           C  
ATOM    135  O   LYS A1005     -35.879  -4.412 -12.321  1.00 14.36           O  
ATOM    136  CB  LYS A1005     -35.651  -6.992 -14.100  1.00 14.70           C  
ATOM    137  CG  LYS A1005     -35.199  -8.359 -14.545  1.00 16.34           C  
ATOM    138  CD  LYS A1005     -36.139  -8.946 -15.585  1.00 17.52           C  
ATOM    139  CE  LYS A1005     -35.859  -8.390 -16.980  1.00 17.68           C  
ATOM    140  NZ  LYS A1005     -34.468  -8.650 -17.409  1.00 17.81           N  
ATOM    141  N   GLY A1006     -34.331  -3.998 -13.922  1.00 14.68           N  
ATOM    142  CA  GLY A1006     -34.503  -2.553 -13.885  1.00 15.24           C  
ATOM    143  C   GLY A1006     -35.813  -2.132 -14.499  1.00 15.43           C  
ATOM    144  O   GLY A1006     -35.842  -1.636 -15.636  1.00 14.74           O  
ATOM    145  N   SER A1007     -36.878  -2.309 -13.717  1.00 15.80           N  
ATOM    146  CA  SER A1007     -38.245  -2.025 -14.137  1.00 16.82           C  
ATOM    147  C   SER A1007     -39.081  -1.547 -12.945  1.00 17.91           C  
ATOM    148  O   SER A1007     -39.080  -2.183 -11.893  1.00 17.90           O  
ATOM    149  CB  SER A1007     -38.874  -3.281 -14.744  1.00 16.79           C  
ATOM    150  OG  SER A1007     -40.205  -3.047 -15.149  1.00 16.19           O  
ATOM    151  N   LEU A1008     -39.758  -0.409 -13.116  1.00 18.71           N  
ATOM    152  CA  LEU A1008     -40.675   0.144 -12.133  1.00 19.40           C  
ATOM    153  C   LEU A1008     -41.988   0.475 -12.843  1.00 20.31           C  
ATOM    154  O   LEU A1008     -41.976   1.043 -13.937  1.00 20.37           O  
ATOM    155  CB  LEU A1008     -40.129   1.436 -11.530  1.00 19.55           C  
ATOM    156  CG  LEU A1008     -38.859   1.449 -10.685  1.00 19.67           C  
ATOM    157  CD1 LEU A1008     -38.431   2.892 -10.436  1.00 20.32           C  
ATOM    158  CD2 LEU A1008     -39.052   0.703  -9.376  1.00 19.51           C  
ATOM    159  N   VAL A1009     -43.109   0.124 -12.217  1.00 20.93           N  
ATOM    160  CA  VAL A1009     -44.442   0.432 -12.738  1.00 21.32           C  
ATOM    161  C   VAL A1009     -45.163   1.343 -11.738  1.00 21.33           C  
ATOM    162  O   VAL A1009     -45.295   1.002 -10.562  1.00 21.11           O  
ATOM    163  CB  VAL A1009     -45.262  -0.862 -12.974  1.00 21.85           C  
ATOM    164  CG1 VAL A1009     -46.636  -0.546 -13.548  1.00 21.48           C  
ATOM    165  CG2 VAL A1009     -44.502  -1.821 -13.908  1.00 21.88           C  
ATOM    166  N   SER A1010     -45.577   2.519 -12.194  1.00 21.20           N  
ATOM    167  CA  SER A1010     -46.418   3.418 -11.392  1.00 21.55           C  
ATOM    168  C   SER A1010     -47.776   2.768 -11.099  1.00 21.91           C  
ATOM    169  O   SER A1010     -48.186   1.840 -11.798  1.00 22.20           O  
ATOM    170  CB  SER A1010     -46.675   4.718 -12.146  1.00 21.42           C  
ATOM    171  OG  SER A1010     -47.593   4.476 -13.196  1.00 21.32           O  
ATOM    172  N   PRO A1011     -48.496   3.274 -10.083  1.00 22.43           N  
ATOM    173  CA  PRO A1011     -49.847   2.750  -9.798  1.00 22.48           C  
ATOM    174  C   PRO A1011     -50.771   2.825 -11.007  1.00 22.36           C  
ATOM    175  O   PRO A1011     -51.577   1.919 -11.237  1.00 22.62           O  
ATOM    176  CB  PRO A1011     -50.352   3.674  -8.693  1.00 22.89           C  
ATOM    177  CG  PRO A1011     -49.100   4.198  -8.028  1.00 22.99           C  
ATOM    178  CD  PRO A1011     -48.066   4.289  -9.104  1.00 22.38           C  
ATOM    179  N   GLY A1012     -50.634   3.902 -11.777  1.00 22.01           N  
ATOM    180  CA  GLY A1012     -51.389   4.088 -13.010  1.00 21.81           C  
ATOM    181  C   GLY A1012     -51.011   3.162 -14.155  1.00 21.38           C  
ATOM    182  O   GLY A1012     -51.713   3.120 -15.157  1.00 21.83           O  
ATOM    183  N   GLY A1013     -49.911   2.427 -14.023  1.00 20.86           N  
ATOM    184  CA  GLY A1013     -49.533   1.405 -15.011  1.00 20.34           C  
ATOM    185  C   GLY A1013     -48.450   1.817 -16.011  1.00 19.62           C  
ATOM    186  O   GLY A1013     -48.175   1.087 -16.953  1.00 19.94           O  
ATOM    187  N   LEU A1014     -47.831   2.978 -15.818  1.00 19.00           N  
ATOM    188  CA  LEU A1014     -46.745   3.424 -16.694  1.00 18.09           C  
ATOM    189  C   LEU A1014     -45.423   2.781 -16.281  1.00 17.75           C  
ATOM    190  O   LEU A1014     -44.980   2.943 -15.145  1.00 17.55           O  
ATOM    191  CB  LEU A1014     -46.614   4.951 -16.657  1.00 17.89           C  
ATOM    192  CG  LEU A1014     -45.618   5.554 -17.646  1.00 16.99           C  
ATOM    193  CD1 LEU A1014     -45.915   5.087 -19.066  1.00 14.70           C  
ATOM    194  CD2 LEU A1014     -45.650   7.081 -17.550  1.00 16.69           C  
ATOM    195  N   GLN A1015     -44.791   2.071 -17.212  1.00 17.14           N  
ATOM    196  CA  GLN A1015     -43.571   1.341 -16.921  1.00 16.87           C  
ATOM    197  C   GLN A1015     -42.340   2.169 -17.259  1.00 16.62           C  
ATOM    198  O   GLN A1015     -42.294   2.806 -18.312  1.00 16.49           O  
ATOM    199  CB  GLN A1015     -43.545   0.035 -17.709  1.00 17.36           C  
ATOM    200  CG  GLN A1015     -42.322  -0.844 -17.452  1.00 18.21           C  
ATOM    201  CD  GLN A1015     -42.376  -2.151 -18.240  1.00 21.01           C  
ATOM    202  OE1 GLN A1015     -42.822  -2.187 -19.392  1.00 23.40           O  
ATOM    203  NE2 GLN A1015     -41.910  -3.225 -17.625  1.00 21.38           N  
ATOM    204  N   MET A1016     -41.357   2.152 -16.354  1.00 15.94           N  
ATOM    205  CA  MET A1016     -40.045   2.766 -16.550  1.00 15.73           C  
ATOM    206  C   MET A1016     -38.983   1.676 -16.587  1.00 15.02           C  
ATOM    207  O   MET A1016     -38.962   0.814 -15.712  1.00 14.05           O  
ATOM    208  CB  MET A1016     -39.697   3.682 -15.380  1.00 15.91           C  
ATOM    209  CG  MET A1016     -40.441   4.995 -15.359  1.00 18.44           C  
ATOM    210  SD  MET A1016     -40.521   5.685 -13.681  1.00 20.88           S  
ATOM    211  CE  MET A1016     -42.099   5.043 -13.137  1.00 18.62           C  
ATOM    212  N   LEU A1017     -38.070   1.772 -17.549  1.00 14.81           N  
ATOM    213  CA  LEU A1017     -37.050   0.765 -17.795  1.00 15.18           C  
ATOM    214  C   LEU A1017     -35.638   1.370 -17.803  1.00 15.38           C  
ATOM    215  O   LEU A1017     -35.402   2.440 -18.373  1.00 15.10           O  
ATOM    216  CB  LEU A1017     -37.303   0.089 -19.140  1.00 15.35           C  
ATOM    217  CG  LEU A1017     -38.522  -0.811 -19.253  1.00 16.75           C  
ATOM    218  CD1 LEU A1017     -38.843  -1.152 -20.718  1.00 17.41           C  
ATOM    219  CD2 LEU A1017     -38.266  -2.084 -18.456  1.00 18.60           C  
ATOM    220  N   LEU A1018     -34.705   0.668 -17.173  1.00 15.77           N  
ATOM    221  CA  LEU A1018     -33.301   1.054 -17.182  1.00 16.40           C  
ATOM    222  C   LEU A1018     -32.627   0.311 -18.295  1.00 16.62           C  
ATOM    223  O   LEU A1018     -32.543  -0.919 -18.236  1.00 16.62           O  
ATOM    224  CB  LEU A1018     -32.596   0.654 -15.898  1.00 16.56           C  
ATOM    225  CG  LEU A1018     -32.756   1.442 -14.615  1.00 17.05           C  
ATOM    226  CD1 LEU A1018     -31.705   0.933 -13.636  1.00 17.78           C  
ATOM    227  CD2 LEU A1018     -32.604   2.929 -14.872  1.00 19.32           C  
ATOM    228  N   VAL A1019     -32.134   1.048 -19.287  1.00 16.75           N  
ATOM    229  CA  VAL A1019     -31.530   0.454 -20.483  1.00 17.24           C  
ATOM    230  C   VAL A1019     -30.117   0.988 -20.676  1.00 18.30           C  
ATOM    231  O   VAL A1019     -29.877   2.203 -20.575  1.00 18.45           O  
ATOM    232  CB  VAL A1019     -32.371   0.740 -21.747  1.00 17.13           C  
ATOM    233  CG1 VAL A1019     -31.778   0.062 -22.958  1.00 17.04           C  
ATOM    234  CG2 VAL A1019     -33.804   0.274 -21.547  1.00 16.58           C  
ATOM    235  N   LYS A1020     -29.187   0.072 -20.934  1.00 19.01           N  
ATOM    236  CA  LYS A1020     -27.792   0.397 -21.176  1.00 20.18           C  
ATOM    237  C   LYS A1020     -27.545   0.244 -22.669  1.00 20.52           C  
ATOM    238  O   LYS A1020     -27.420  -0.864 -23.174  1.00 20.34           O  
ATOM    239  CB  LYS A1020     -26.894  -0.551 -20.379  1.00 20.58           C  
ATOM    240  CG  LYS A1020     -25.408  -0.238 -20.452  1.00 22.84           C  
ATOM    241  CD  LYS A1020     -24.551  -1.507 -20.280  1.00 25.62           C  
ATOM    242  CE  LYS A1020     -23.816  -1.595 -18.954  1.00 27.60           C  
ATOM    243  NZ  LYS A1020     -22.345  -1.316 -19.094  1.00 29.88           N  
ATOM    244  N   GLU A1021     -27.523   1.358 -23.384  1.00 21.33           N  
ATOM    245  CA  GLU A1021     -27.280   1.341 -24.823  1.00 22.31           C  
ATOM    246  C   GLU A1021     -27.076   2.740 -25.351  1.00 22.48           C  
ATOM    247  O   GLU A1021     -27.463   3.727 -24.719  1.00 22.23           O  
ATOM    248  CB  GLU A1021     -28.419   0.667 -25.608  1.00 22.79           C  
ATOM    249  CG  GLU A1021     -29.745   1.412 -25.621  1.00 25.16           C  
ATOM    250  CD  GLU A1021     -30.844   0.670 -26.379  1.00 28.82           C  
ATOM    251  OE1 GLU A1021     -31.984   1.184 -26.445  1.00 32.65           O  
ATOM    252  OE2 GLU A1021     -30.585  -0.436 -26.898  1.00 31.31           O  
ATOM    253  N   GLY A1022     -26.457   2.815 -26.519  1.00 22.93           N  
ATOM    254  CA  GLY A1022     -26.335   4.081 -27.225  1.00 22.94           C  
ATOM    255  C   GLY A1022     -27.700   4.499 -27.728  1.00 23.18           C  
ATOM    256  O   GLY A1022     -28.478   3.672 -28.206  1.00 22.92           O  
ATOM    257  N   VAL A1023     -27.991   5.792 -27.605  1.00 23.91           N  
ATOM    258  CA  VAL A1023     -29.248   6.382 -28.082  1.00 24.07           C  
ATOM    259  C   VAL A1023     -29.469   6.051 -29.554  1.00 24.38           C  
ATOM    260  O   VAL A1023     -30.605   5.909 -30.006  1.00 24.59           O  
ATOM    261  CB  VAL A1023     -29.237   7.915 -27.902  1.00 24.02           C  
ATOM    262  CG1 VAL A1023     -28.155   8.555 -28.805  1.00 24.58           C  
ATOM    263  CG2 VAL A1023     -30.594   8.495 -28.194  1.00 24.07           C  
ATOM    264  N   GLN A1024     -28.371   5.917 -30.289  1.00 24.79           N  
ATOM    265  CA  GLN A1024     -28.423   5.529 -31.701  1.00 25.40           C  
ATOM    266  C   GLN A1024     -29.065   4.168 -31.954  1.00 25.01           C  
ATOM    267  O   GLN A1024     -29.446   3.877 -33.077  1.00 25.04           O  
ATOM    268  CB  GLN A1024     -27.017   5.532 -32.319  1.00 25.69           C  
ATOM    269  CG  GLN A1024     -26.008   4.583 -31.660  1.00 26.40           C  
ATOM    270  CD  GLN A1024     -25.147   5.278 -30.620  1.00 26.81           C  
ATOM    271  OE1 GLN A1024     -25.645   6.031 -29.781  1.00 27.41           O  
ATOM    272  NE2 GLN A1024     -23.851   5.027 -30.672  1.00 28.49           N  
ATOM    273  N   ASN A1025     -29.148   3.328 -30.924  1.00 24.63           N  
ATOM    274  CA  ASN A1025     -29.730   1.996 -31.061  1.00 24.02           C  
ATOM    275  C   ASN A1025     -31.130   1.883 -30.429  1.00 23.19           C  
ATOM    276  O   ASN A1025     -31.687   0.791 -30.365  1.00 22.75           O  
ATOM    277  CB  ASN A1025     -28.766   0.967 -30.457  1.00 24.12           C  
ATOM    278  CG  ASN A1025     -27.436   0.911 -31.210  1.00 25.74           C  
ATOM    279  OD1 ASN A1025     -27.417   0.819 -32.438  1.00 27.59           O  
ATOM    280  ND2 ASN A1025     -26.324   0.968 -30.479  1.00 26.74           N  
ATOM    281  N   ALA A1026     -31.697   3.010 -29.986  1.00 21.93           N  
ATOM    282  CA  ALA A1026     -33.051   3.022 -29.405  1.00 21.33           C  
ATOM    283  C   ALA A1026     -34.091   2.505 -30.388  1.00 20.63           C  
ATOM    284  O   ALA A1026     -34.065   2.865 -31.563  1.00 20.75           O  
ATOM    285  CB  ALA A1026     -33.425   4.427 -28.974  1.00 21.31           C  
ATOM    286  N   LYS A1027     -35.009   1.673 -29.902  1.00 19.74           N  
ATOM    287  CA  LYS A1027     -36.114   1.141 -30.706  1.00 19.03           C  
ATOM    288  C   LYS A1027     -37.506   1.544 -30.189  1.00 17.56           C  
ATOM    289  O   LYS A1027     -38.521   0.970 -30.600  1.00 16.91           O  
ATOM    290  CB  LYS A1027     -36.016  -0.385 -30.792  1.00 19.89           C  
ATOM    291  CG  LYS A1027     -35.113  -0.877 -31.925  1.00 22.34           C  
ATOM    292  CD  LYS A1027     -35.298  -2.391 -32.193  1.00 26.17           C  
ATOM    293  CE  LYS A1027     -34.774  -2.779 -33.578  1.00 26.96           C  
ATOM    294  NZ  LYS A1027     -33.429  -2.186 -33.818  1.00 27.71           N  
ATOM    295  N   THR A1028     -37.563   2.540 -29.315  1.00 15.72           N  
ATOM    296  CA  THR A1028     -38.855   3.081 -28.861  1.00 14.77           C  
ATOM    297  C   THR A1028     -39.524   3.877 -29.998  1.00 14.14           C  
ATOM    298  O   THR A1028     -38.893   4.163 -31.007  1.00 14.31           O  
ATOM    299  CB  THR A1028     -38.646   3.972 -27.635  1.00 14.33           C  
ATOM    300  OG1 THR A1028     -37.626   4.938 -27.919  1.00 13.16           O  
ATOM    301  CG2 THR A1028     -38.215   3.140 -26.459  1.00 13.51           C  
ATOM    302  N   ASP A1029     -40.794   4.230 -29.847  1.00 13.50           N  
ATOM    303  CA  ASP A1029     -41.463   5.033 -30.852  1.00 12.69           C  
ATOM    304  C   ASP A1029     -40.822   6.422 -30.914  1.00 11.98           C  
ATOM    305  O   ASP A1029     -40.646   6.979 -31.998  1.00 11.71           O  
ATOM    306  CB  ASP A1029     -42.955   5.186 -30.549  1.00 12.96           C  
ATOM    307  CG  ASP A1029     -43.729   3.869 -30.638  1.00 14.97           C  
ATOM    308  OD1 ASP A1029     -43.374   3.011 -31.461  1.00 16.01           O  
ATOM    309  OD2 ASP A1029     -44.712   3.702 -29.871  1.00 18.71           O  
ATOM    310  N   VAL A1030     -40.502   6.977 -29.747  1.00 10.48           N  
ATOM    311  CA  VAL A1030     -39.935   8.308 -29.650  1.00 10.08           C  
ATOM    312  C   VAL A1030     -38.601   8.267 -28.913  1.00 10.08           C  
ATOM    313  O   VAL A1030     -38.436   7.503 -27.964  1.00 10.15           O  
ATOM    314  CB  VAL A1030     -40.886   9.289 -28.905  1.00  9.92           C  
ATOM    315  CG1 VAL A1030     -40.262  10.673 -28.836  1.00  8.30           C  
ATOM    316  CG2 VAL A1030     -42.219   9.364 -29.586  1.00  9.61           C  
ATOM    317  N   VAL A1031     -37.657   9.071 -29.389  1.00 10.10           N  
ATOM    318  CA  VAL A1031     -36.365   9.301 -28.751  1.00 10.65           C  
ATOM    319  C   VAL A1031     -36.197  10.802 -28.546  1.00 10.32           C  
ATOM    320  O   VAL A1031     -36.558  11.585 -29.421  1.00 10.29           O  
ATOM    321  CB  VAL A1031     -35.198   8.828 -29.643  1.00 10.69           C  
ATOM    322  CG1 VAL A1031     -33.873   9.173 -28.993  1.00 12.01           C  
ATOM    323  CG2 VAL A1031     -35.311   7.343 -29.898  1.00 10.87           C  
ATOM    324  N   VAL A1032     -35.634  11.190 -27.408  1.00  9.97           N  
ATOM    325  CA  VAL A1032     -35.498  12.575 -27.049  1.00 10.10           C  
ATOM    326  C   VAL A1032     -34.039  12.985 -27.219  1.00 10.77           C  
ATOM    327  O   VAL A1032     -33.132  12.270 -26.802  1.00 11.10           O  
ATOM    328  CB  VAL A1032     -35.986  12.836 -25.600  1.00 10.54           C  
ATOM    329  CG1 VAL A1032     -35.689  14.288 -25.161  1.00  8.88           C  
ATOM    330  CG2 VAL A1032     -37.483  12.515 -25.466  1.00  9.25           C  
ATOM    331  N   ASN A1033     -33.828  14.134 -27.850  1.00 11.11           N  
ATOM    332  CA  ASN A1033     -32.500  14.672 -28.101  1.00 11.59           C  
ATOM    333  C   ASN A1033     -32.426  16.063 -27.494  1.00 11.58           C  
ATOM    334  O   ASN A1033     -33.412  16.764 -27.536  1.00 12.41           O  
ATOM    335  CB  ASN A1033     -32.288  14.761 -29.623  1.00 10.96           C  
ATOM    336  CG  ASN A1033     -30.841  15.069 -30.009  1.00 11.97           C  
ATOM    337  OD1 ASN A1033     -29.889  14.687 -29.316  1.00 11.24           O  
ATOM    338  ND2 ASN A1033     -30.674  15.750 -31.141  1.00 12.22           N  
ATOM    339  N   SER A1034     -31.292  16.476 -26.932  1.00 11.96           N  
ATOM    340  CA  SER A1034     -31.164  17.863 -26.503  1.00 12.43           C  
ATOM    341  C   SER A1034     -30.286  18.623 -27.475  1.00 12.15           C  
ATOM    342  O   SER A1034     -29.214  18.173 -27.838  1.00 11.44           O  
ATOM    343  CB  SER A1034     -30.664  18.029 -25.064  1.00 12.80           C  
ATOM    344  OG  SER A1034     -29.371  17.539 -24.904  1.00 15.28           O  
ATOM    345  N   VAL A1035     -30.781  19.783 -27.889  1.00 11.93           N  
ATOM    346  CA  VAL A1035     -30.161  20.563 -28.925  1.00 12.31           C  
ATOM    347  C   VAL A1035     -29.995  22.012 -28.457  1.00 12.97           C  
ATOM    348  O   VAL A1035     -30.757  22.484 -27.613  1.00 12.93           O  
ATOM    349  CB  VAL A1035     -31.023  20.518 -30.181  1.00 11.88           C  
ATOM    350  CG1 VAL A1035     -31.226  19.054 -30.606  1.00 11.48           C  
ATOM    351  CG2 VAL A1035     -32.363  21.206 -29.927  1.00 11.22           C  
ATOM    352  N   PRO A1036     -29.000  22.725 -29.010  1.00 13.84           N  
ATOM    353  CA  PRO A1036     -28.845  24.149 -28.710  1.00 13.95           C  
ATOM    354  C   PRO A1036     -29.885  24.991 -29.440  1.00 13.73           C  
ATOM    355  O   PRO A1036     -30.611  24.488 -30.309  1.00 12.90           O  
ATOM    356  CB  PRO A1036     -27.449  24.458 -29.256  1.00 14.19           C  
ATOM    357  CG  PRO A1036     -27.340  23.523 -30.448  1.00 14.50           C  
ATOM    358  CD  PRO A1036     -27.992  22.261 -29.988  1.00 13.96           C  
ATOM    359  N   LEU A1037     -29.948  26.265 -29.081  1.00 14.25           N  
ATOM    360  CA  LEU A1037     -30.876  27.217 -29.714  1.00 15.04           C  
ATOM    361  C   LEU A1037     -30.743  27.276 -31.232  1.00 15.21           C  
ATOM    362  O   LEU A1037     -31.752  27.355 -31.932  1.00 15.67           O  
ATOM    363  CB  LEU A1037     -30.683  28.629 -29.135  1.00 15.28           C  
ATOM    364  CG  LEU A1037     -31.302  28.868 -27.754  1.00 16.04           C  
ATOM    365  CD1 LEU A1037     -30.743  30.151 -27.103  1.00 17.34           C  
ATOM    366  CD2 LEU A1037     -32.797  28.922 -27.863  1.00 16.08           C  
ATOM    367  N   ASP A1038     -29.515  27.238 -31.735  1.00 15.50           N  
ATOM    368  CA  ASP A1038     -29.287  27.314 -33.177  1.00 16.58           C  
ATOM    369  C   ASP A1038     -29.529  25.963 -33.910  1.00 16.59           C  
ATOM    370  O   ASP A1038     -29.396  25.884 -35.127  1.00 16.38           O  
ATOM    371  CB  ASP A1038     -27.890  27.896 -33.481  1.00 16.87           C  
ATOM    372  CG  ASP A1038     -26.738  26.968 -33.074  1.00 18.68           C  
ATOM    373  OD1 ASP A1038     -25.558  27.352 -33.254  1.00 19.34           O  
ATOM    374  OD2 ASP A1038     -26.984  25.850 -32.572  1.00 22.23           O  
ATOM    375  N   LEU A1039     -29.890  24.917 -33.164  1.00 16.46           N  
ATOM    376  CA  LEU A1039     -30.311  23.622 -33.731  1.00 16.32           C  
ATOM    377  C   LEU A1039     -29.218  22.841 -34.455  1.00 16.44           C  
ATOM    378  O   LEU A1039     -29.525  21.879 -35.149  1.00 16.42           O  
ATOM    379  CB  LEU A1039     -31.511  23.773 -34.686  1.00 15.84           C  
ATOM    380  CG  LEU A1039     -32.767  24.432 -34.147  1.00 15.57           C  
ATOM    381  CD1 LEU A1039     -33.825  24.447 -35.257  1.00 14.47           C  
ATOM    382  CD2 LEU A1039     -33.274  23.709 -32.888  1.00 14.24           C  
ATOM    383  N   VAL A1040     -27.958  23.230 -34.278  1.00 16.77           N  
ATOM    384  CA  VAL A1040     -26.837  22.477 -34.827  1.00 17.00           C  
ATOM    385  C   VAL A1040     -26.676  21.151 -34.047  1.00 16.95           C  
ATOM    386  O   VAL A1040     -26.461  21.154 -32.839  1.00 16.26           O  
ATOM    387  CB  VAL A1040     -25.546  23.332 -34.802  1.00 17.34           C  
ATOM    388  CG1 VAL A1040     -24.286  22.468 -34.972  1.00 17.43           C  
ATOM    389  CG2 VAL A1040     -25.620  24.428 -35.876  1.00 17.47           C  
ATOM    390  N   LEU A1041     -26.784  20.025 -34.752  1.00 17.06           N  
ATOM    391  CA  LEU A1041     -26.809  18.704 -34.107  1.00 17.21           C  
ATOM    392  C   LEU A1041     -25.432  18.090 -33.858  1.00 17.54           C  
ATOM    393  O   LEU A1041     -25.321  17.047 -33.212  1.00 17.59           O  
ATOM    394  CB  LEU A1041     -27.658  17.744 -34.930  1.00 17.01           C  
ATOM    395  CG  LEU A1041     -29.129  18.127 -35.028  1.00 16.90           C  
ATOM    396  CD1 LEU A1041     -29.864  17.211 -35.994  1.00 16.02           C  
ATOM    397  CD2 LEU A1041     -29.746  18.076 -33.638  1.00 15.67           C  
ATOM    398  N   SER A1042     -24.384  18.738 -34.345  1.00 18.09           N  
ATOM    399  CA  SER A1042     -23.041  18.170 -34.262  1.00 18.77           C  
ATOM    400  C   SER A1042     -22.202  18.755 -33.122  1.00 19.18           C  
ATOM    401  O   SER A1042     -21.004  18.534 -33.081  1.00 19.23           O  
ATOM    402  CB  SER A1042     -22.310  18.400 -35.583  1.00 18.50           C  
ATOM    403  OG  SER A1042     -22.190  19.784 -35.831  1.00 19.31           O  
ATOM    404  N   ARG A1043     -22.803  19.491 -32.194  1.00 19.72           N  
ATOM    405  CA  ARG A1043     -21.990  20.140 -31.159  1.00 20.39           C  
ATOM    406  C   ARG A1043     -21.809  19.347 -29.877  1.00 20.08           C  
ATOM    407  O   ARG A1043     -20.732  19.382 -29.298  1.00 21.51           O  
ATOM    408  CB  ARG A1043     -22.525  21.526 -30.834  1.00 20.79           C  
ATOM    409  CG  ARG A1043     -21.527  22.386 -30.066  1.00 22.13           C  
ATOM    410  CD  ARG A1043     -21.550  23.833 -30.553  1.00 23.76           C  
ATOM    411  NE  ARG A1043     -22.880  24.424 -30.393  1.00 25.25           N  
ATOM    412  CZ  ARG A1043     -23.589  25.024 -31.350  1.00 24.60           C  
ATOM    413  NH1 ARG A1043     -24.792  25.506 -31.067  1.00 24.47           N  
ATOM    414  NH2 ARG A1043     -23.122  25.151 -32.578  1.00 25.10           N  
ATOM    415  N   GLY A1044     -22.851  18.651 -29.423  1.00 19.43           N  
ATOM    416  CA  GLY A1044     -22.777  17.824 -28.226  1.00 18.47           C  
ATOM    417  C   GLY A1044     -22.695  16.340 -28.541  1.00 18.10           C  
ATOM    418  O   GLY A1044     -23.206  15.890 -29.562  1.00 18.45           O  
ATOM    419  N   PRO A1045     -22.066  15.555 -27.658  1.00 17.66           N  
ATOM    420  CA  PRO A1045     -21.888  14.132 -27.932  1.00 17.31           C  
ATOM    421  C   PRO A1045     -23.178  13.332 -28.124  1.00 16.75           C  
ATOM    422  O   PRO A1045     -23.207  12.446 -28.973  1.00 17.59           O  
ATOM    423  CB  PRO A1045     -21.102  13.618 -26.718  1.00 17.37           C  
ATOM    424  CG  PRO A1045     -21.194  14.691 -25.692  1.00 17.85           C  
ATOM    425  CD  PRO A1045     -21.434  15.966 -26.395  1.00 17.78           C  
ATOM    426  N   LEU A1046     -24.227  13.627 -27.372  1.00 15.88           N  
ATOM    427  CA  LEU A1046     -25.488  12.900 -27.518  1.00 15.39           C  
ATOM    428  C   LEU A1046     -26.065  13.132 -28.900  1.00 15.41           C  
ATOM    429  O   LEU A1046     -26.321  12.187 -29.638  1.00 15.18           O  
ATOM    430  CB  LEU A1046     -26.510  13.328 -26.452  1.00 15.39           C  
ATOM    431  CG  LEU A1046     -27.902  12.674 -26.447  1.00 15.00           C  
ATOM    432  CD1 LEU A1046     -27.801  11.198 -26.106  1.00 14.81           C  
ATOM    433  CD2 LEU A1046     -28.847  13.403 -25.472  1.00 12.28           C  
ATOM    434  N   SER A1047     -26.256  14.398 -29.242  1.00 15.45           N  
ATOM    435  CA  SER A1047     -26.860  14.774 -30.504  1.00 15.65           C  
ATOM    436  C   SER A1047     -26.013  14.320 -31.678  1.00 15.95           C  
ATOM    437  O   SER A1047     -26.534  13.891 -32.700  1.00 15.60           O  
ATOM    438  CB  SER A1047     -27.055  16.283 -30.567  1.00 15.86           C  
ATOM    439  OG  SER A1047     -27.806  16.610 -31.700  1.00 16.12           O  
ATOM    440  N   LYS A1048     -24.700  14.398 -31.515  1.00 16.40           N  
ATOM    441  CA  LYS A1048     -23.788  14.005 -32.566  1.00 17.23           C  
ATOM    442  C   LYS A1048     -23.919  12.500 -32.821  1.00 16.47           C  
ATOM    443  O   LYS A1048     -23.947  12.090 -33.966  1.00 15.32           O  
ATOM    444  CB  LYS A1048     -22.360  14.420 -32.185  1.00 17.82           C  
ATOM    445  CG  LYS A1048     -21.297  14.291 -33.271  1.00 20.94           C  
ATOM    446  CD  LYS A1048     -19.962  14.813 -32.716  1.00 24.45           C  
ATOM    447  CE  LYS A1048     -18.759  14.426 -33.577  1.00 26.95           C  
ATOM    448  NZ  LYS A1048     -18.460  15.442 -34.602  1.00 27.60           N  
ATOM    449  N   SER A1049     -24.037  11.698 -31.755  1.00 16.18           N  
ATOM    450  CA  SER A1049     -24.325  10.262 -31.893  1.00 16.14           C  
ATOM    451  C   SER A1049     -25.608  10.045 -32.696  1.00 15.76           C  
ATOM    452  O   SER A1049     -25.656   9.169 -33.571  1.00 15.40           O  
ATOM    453  CB  SER A1049     -24.465   9.557 -30.530  1.00 16.30           C  
ATOM    454  OG  SER A1049     -23.265   9.595 -29.771  1.00 16.70           O  
ATOM    455  N   LEU A1050     -26.643  10.836 -32.410  1.00 14.89           N  
ATOM    456  CA  LEU A1050     -27.901  10.687 -33.132  1.00 14.78           C  
ATOM    457  C   LEU A1050     -27.749  11.083 -34.592  1.00 14.13           C  
ATOM    458  O   LEU A1050     -28.303  10.412 -35.472  1.00 13.44           O  
ATOM    459  CB  LEU A1050     -29.045  11.485 -32.501  1.00 15.05           C  
ATOM    460  CG  LEU A1050     -29.922  10.772 -31.470  1.00 16.75           C  
ATOM    461  CD1 LEU A1050     -30.956  11.749 -30.898  1.00 17.90           C  
ATOM    462  CD2 LEU A1050     -30.617   9.553 -32.042  1.00 17.22           C  
ATOM    463  N   LEU A1051     -27.009  12.166 -34.839  1.00 13.68           N  
ATOM    464  CA  LEU A1051     -26.804  12.662 -36.192  1.00 14.47           C  
ATOM    465  C   LEU A1051     -26.063  11.631 -37.055  1.00 14.45           C  
ATOM    466  O   LEU A1051     -26.471  11.345 -38.158  1.00 13.35           O  
ATOM    467  CB  LEU A1051     -26.034  13.993 -36.189  1.00 14.36           C  
ATOM    468  CG  LEU A1051     -25.715  14.623 -37.556  1.00 14.96           C  
ATOM    469  CD1 LEU A1051     -26.986  14.922 -38.321  1.00 11.95           C  
ATOM    470  CD2 LEU A1051     -24.857  15.908 -37.408  1.00 14.57           C  
ATOM    471  N   GLU A1052     -24.975  11.088 -36.528  1.00 15.43           N  
ATOM    472  CA  GLU A1052     -24.157  10.125 -37.274  1.00 16.62           C  
ATOM    473  C   GLU A1052     -24.949   8.896 -37.675  1.00 16.16           C  
ATOM    474  O   GLU A1052     -24.908   8.484 -38.818  1.00 16.36           O  
ATOM    475  CB  GLU A1052     -22.906   9.745 -36.482  1.00 16.96           C  
ATOM    476  CG  GLU A1052     -21.839  10.835 -36.521  1.00 20.60           C  
ATOM    477  CD  GLU A1052     -20.665  10.579 -35.570  1.00 26.42           C  
ATOM    478  OE1 GLU A1052     -20.533   9.428 -35.059  1.00 28.66           O  
ATOM    479  OE2 GLU A1052     -19.882  11.539 -35.339  1.00 28.75           O  
ATOM    480  N   LYS A1053     -25.720   8.341 -36.749  1.00 16.46           N  
ATOM    481  CA  LYS A1053     -26.549   7.180 -37.048  1.00 16.21           C  
ATOM    482  C   LYS A1053     -27.688   7.525 -38.009  1.00 15.75           C  
ATOM    483  O   LYS A1053     -27.955   6.781 -38.953  1.00 15.46           O  
ATOM    484  CB  LYS A1053     -27.107   6.580 -35.746  1.00 16.62           C  
ATOM    485  CG  LYS A1053     -28.102   5.424 -35.924  1.00 17.54           C  
ATOM    486  CD  LYS A1053     -27.453   4.208 -36.554  1.00 18.94           C  
ATOM    487  CE  LYS A1053     -28.409   3.018 -36.602  1.00 20.11           C  
ATOM    488  NZ  LYS A1053     -27.730   1.863 -37.266  1.00 21.19           N  
ATOM    489  N   ALA A1054     -28.368   8.645 -37.765  1.00 15.44           N  
ATOM    490  CA  ALA A1054     -29.582   8.992 -38.529  1.00 14.71           C  
ATOM    491  C   ALA A1054     -29.278   9.425 -39.968  1.00 14.48           C  
ATOM    492  O   ALA A1054     -30.035   9.129 -40.878  1.00 13.79           O  
ATOM    493  CB  ALA A1054     -30.368  10.086 -37.810  1.00 14.33           C  
ATOM    494  N   GLY A1055     -28.169  10.135 -40.156  1.00 14.48           N  
ATOM    495  CA  GLY A1055     -27.836  10.739 -41.436  1.00 14.73           C  
ATOM    496  C   GLY A1055     -28.112  12.241 -41.455  1.00 14.95           C  
ATOM    497  O   GLY A1055     -28.861  12.738 -40.621  1.00 14.37           O  
ATOM    498  N   PRO A1056     -27.527  12.964 -42.435  1.00 14.99           N  
ATOM    499  CA  PRO A1056     -27.595  14.425 -42.520  1.00 15.10           C  
ATOM    500  C   PRO A1056     -29.024  14.953 -42.659  1.00 14.62           C  
ATOM    501  O   PRO A1056     -29.304  16.112 -42.345  1.00 14.69           O  
ATOM    502  CB  PRO A1056     -26.771  14.747 -43.778  1.00 15.35           C  
ATOM    503  CG  PRO A1056     -26.823  13.480 -44.599  1.00 15.34           C  
ATOM    504  CD  PRO A1056     -26.771  12.388 -43.569  1.00 15.41           C  
ATOM    505  N   GLU A1057     -29.927  14.106 -43.115  1.00 13.99           N  
ATOM    506  CA  GLU A1057     -31.309  14.508 -43.222  1.00 13.81           C  
ATOM    507  C   GLU A1057     -31.912  14.943 -41.887  1.00 13.02           C  
ATOM    508  O   GLU A1057     -32.864  15.720 -41.872  1.00 13.23           O  
ATOM    509  CB  GLU A1057     -32.155  13.402 -43.820  1.00 13.72           C  
ATOM    510  CG  GLU A1057     -31.764  13.035 -45.226  1.00 14.53           C  
ATOM    511  CD  GLU A1057     -30.687  11.961 -45.291  1.00 13.64           C  
ATOM    512  OE1 GLU A1057     -30.452  11.481 -46.390  1.00 12.84           O  
ATOM    513  OE2 GLU A1057     -30.078  11.601 -44.259  1.00 15.02           O  
ATOM    514  N   LEU A1058     -31.370  14.447 -40.778  1.00 12.19           N  
ATOM    515  CA  LEU A1058     -31.905  14.796 -39.458  1.00 11.56           C  
ATOM    516  C   LEU A1058     -31.686  16.294 -39.225  1.00 11.73           C  
ATOM    517  O   LEU A1058     -32.597  17.005 -38.807  1.00 10.77           O  
ATOM    518  CB  LEU A1058     -31.244  13.970 -38.360  1.00 11.00           C  
ATOM    519  CG  LEU A1058     -31.866  14.031 -36.958  1.00 10.33           C  
ATOM    520  CD1 LEU A1058     -33.200  13.310 -36.933  1.00 10.06           C  
ATOM    521  CD2 LEU A1058     -30.899  13.438 -35.937  1.00  7.28           C  
ATOM    522  N   GLN A1059     -30.481  16.759 -39.544  1.00 12.00           N  
ATOM    523  CA  GLN A1059     -30.153  18.163 -39.449  1.00 12.78           C  
ATOM    524  C   GLN A1059     -30.993  19.013 -40.416  1.00 13.06           C  
ATOM    525  O   GLN A1059     -31.385  20.131 -40.089  1.00 13.39           O  
ATOM    526  CB  GLN A1059     -28.672  18.359 -39.727  1.00 12.99           C  
ATOM    527  CG  GLN A1059     -28.213  19.788 -39.606  1.00 13.54           C  
ATOM    528  CD  GLN A1059     -28.299  20.281 -38.190  1.00 12.03           C  
ATOM    529  OE1 GLN A1059     -27.508  19.890 -37.351  1.00 12.51           O  
ATOM    530  NE2 GLN A1059     -29.268  21.131 -37.919  1.00 11.64           N  
ATOM    531  N   GLU A1060     -31.263  18.469 -41.595  1.00 12.87           N  
ATOM    532  CA  GLU A1060     -31.993  19.180 -42.633  1.00 12.74           C  
ATOM    533  C   GLU A1060     -33.445  19.336 -42.255  1.00 12.88           C  
ATOM    534  O   GLU A1060     -34.032  20.413 -42.442  1.00 12.38           O  
ATOM    535  CB  GLU A1060     -31.885  18.434 -43.972  1.00 12.47           C  
ATOM    536  CG  GLU A1060     -30.489  18.522 -44.599  1.00 12.89           C  
ATOM    537  CD  GLU A1060     -30.184  17.393 -45.570  1.00 12.84           C  
ATOM    538  OE1 GLU A1060     -28.997  17.020 -45.688  1.00 11.51           O  
ATOM    539  OE2 GLU A1060     -31.131  16.884 -46.213  1.00 14.24           O  
ATOM    540  N   GLU A1061     -34.032  18.254 -41.737  1.00 13.19           N  
ATOM    541  CA  GLU A1061     -35.420  18.285 -41.328  1.00 13.18           C  
ATOM    542  C   GLU A1061     -35.599  19.113 -40.056  1.00 13.27           C  
ATOM    543  O   GLU A1061     -36.597  19.815 -39.917  1.00 13.52           O  
ATOM    544  CB  GLU A1061     -35.957  16.882 -41.106  1.00 13.51           C  
ATOM    545  CG  GLU A1061     -37.478  16.842 -41.087  1.00 12.88           C  
ATOM    546  CD  GLU A1061     -38.010  15.502 -40.666  1.00 13.53           C  
ATOM    547  OE1 GLU A1061     -39.180  15.474 -40.246  1.00 13.96           O  
ATOM    548  OE2 GLU A1061     -37.273  14.484 -40.737  1.00 12.29           O  
ATOM    549  N   LEU A1062     -34.647  19.035 -39.135  1.00 13.51           N  
ATOM    550  CA  LEU A1062     -34.720  19.858 -37.922  1.00 13.82           C  
ATOM    551  C   LEU A1062     -34.724  21.337 -38.319  1.00 14.66           C  
ATOM    552  O   LEU A1062     -35.558  22.111 -37.847  1.00 13.89           O  
ATOM    553  CB  LEU A1062     -33.553  19.578 -36.964  1.00 13.22           C  
ATOM    554  CG  LEU A1062     -33.591  20.363 -35.629  1.00 12.59           C  
ATOM    555  CD1 LEU A1062     -35.001  20.324 -35.019  1.00  9.74           C  
ATOM    556  CD2 LEU A1062     -32.572  19.821 -34.637  1.00 10.62           C  
ATOM    557  N   ASP A1063     -33.799  21.706 -39.205  1.00 15.95           N  
ATOM    558  CA  ASP A1063     -33.688  23.094 -39.666  1.00 17.18           C  
ATOM    559  C   ASP A1063     -34.948  23.538 -40.370  1.00 17.45           C  
ATOM    560  O   ASP A1063     -35.329  24.690 -40.262  1.00 18.49           O  
ATOM    561  CB  ASP A1063     -32.485  23.300 -40.587  1.00 17.06           C  
ATOM    562  CG  ASP A1063     -31.183  23.343 -39.842  1.00 17.64           C  
ATOM    563  OD1 ASP A1063     -31.176  23.735 -38.652  1.00 18.95           O  
ATOM    564  OD2 ASP A1063     -30.160  22.969 -40.444  1.00 17.54           O  
ATOM    565  N   THR A1064     -35.596  22.620 -41.072  1.00 18.09           N  
ATOM    566  CA  THR A1064     -36.874  22.909 -41.718  1.00 18.72           C  
ATOM    567  C   THR A1064     -37.931  23.260 -40.677  1.00 18.96           C  
ATOM    568  O   THR A1064     -38.603  24.277 -40.782  1.00 18.19           O  
ATOM    569  CB  THR A1064     -37.368  21.700 -42.532  1.00 18.82           C  
ATOM    570  OG1 THR A1064     -36.412  21.407 -43.562  1.00 21.17           O  
ATOM    571  CG2 THR A1064     -38.730  21.966 -43.150  1.00 18.17           C  
ATOM    572  N   VAL A1065     -38.071  22.396 -39.676  1.00 19.68           N  
ATOM    573  CA  VAL A1065     -39.052  22.603 -38.618  1.00 20.10           C  
ATOM    574  C   VAL A1065     -38.783  23.920 -37.888  1.00 20.56           C  
ATOM    575  O   VAL A1065     -39.703  24.660 -37.600  1.00 20.77           O  
ATOM    576  CB  VAL A1065     -39.075  21.397 -37.635  1.00 20.10           C  
ATOM    577  CG1 VAL A1065     -39.979  21.681 -36.450  1.00 20.63           C  
ATOM    578  CG2 VAL A1065     -39.549  20.147 -38.359  1.00 19.96           C  
ATOM    579  N   GLY A1066     -37.518  24.227 -37.619  1.00 21.61           N  
ATOM    580  CA  GLY A1066     -37.173  25.428 -36.866  1.00 22.48           C  
ATOM    581  C   GLY A1066     -37.393  26.751 -37.596  1.00 23.35           C  
ATOM    582  O   GLY A1066     -37.457  27.802 -36.963  1.00 22.39           O  
ATOM    583  N   GLN A1067     -37.509  26.703 -38.922  1.00 24.99           N  
ATOM    584  CA  GLN A1067     -37.600  27.928 -39.736  1.00 26.45           C  
ATOM    585  C   GLN A1067     -38.843  28.745 -39.458  1.00 26.52           C  
ATOM    586  O   GLN A1067     -38.764  29.967 -39.383  1.00 26.78           O  
ATOM    587  CB  GLN A1067     -37.520  27.631 -41.244  1.00 26.89           C  
ATOM    588  CG  GLN A1067     -36.106  27.834 -41.820  1.00 29.28           C  
ATOM    589  CD  GLN A1067     -36.078  27.881 -43.346  1.00 31.40           C  
ATOM    590  OE1 GLN A1067     -37.116  27.770 -44.014  1.00 32.28           O  
ATOM    591  NE2 GLN A1067     -34.880  28.055 -43.901  1.00 32.89           N  
ATOM    592  N   GLY A1068     -39.977  28.074 -39.297  1.00 26.89           N  
ATOM    593  CA  GLY A1068     -41.247  28.761 -39.062  1.00 27.62           C  
ATOM    594  C   GLY A1068     -41.538  29.248 -37.641  1.00 27.65           C  
ATOM    595  O   GLY A1068     -42.522  29.948 -37.419  1.00 28.26           O  
ATOM    596  N   VAL A1069     -40.695  28.884 -36.679  1.00 27.44           N  
ATOM    597  CA  VAL A1069     -40.981  29.130 -35.262  1.00 26.57           C  
ATOM    598  C   VAL A1069     -39.804  29.810 -34.592  1.00 26.06           C  
ATOM    599  O   VAL A1069     -38.651  29.604 -34.983  1.00 26.21           O  
ATOM    600  CB  VAL A1069     -41.295  27.810 -34.546  1.00 26.85           C  
ATOM    601  CG1 VAL A1069     -42.372  27.060 -35.312  1.00 25.90           C  
ATOM    602  CG2 VAL A1069     -40.033  26.962 -34.394  1.00 26.04           C  
ATOM    603  N   ALA A1070     -40.090  30.634 -33.588  1.00 25.40           N  
ATOM    604  CA  ALA A1070     -39.031  31.354 -32.881  1.00 25.01           C  
ATOM    605  C   ALA A1070     -38.521  30.433 -31.792  1.00 24.31           C  
ATOM    606  O   ALA A1070     -39.138  30.342 -30.738  1.00 25.48           O  
ATOM    607  CB  ALA A1070     -39.560  32.684 -32.284  1.00 24.81           C  
ATOM    608  N   VAL A1071     -37.401  29.762 -32.051  1.00 23.05           N  
ATOM    609  CA  VAL A1071     -36.874  28.732 -31.162  1.00 21.81           C  
ATOM    610  C   VAL A1071     -36.400  29.349 -29.866  1.00 21.04           C  
ATOM    611  O   VAL A1071     -35.497  30.183 -29.858  1.00 20.99           O  
ATOM    612  CB  VAL A1071     -35.668  27.971 -31.790  1.00 21.93           C  
ATOM    613  CG1 VAL A1071     -35.064  26.974 -30.799  1.00 20.69           C  
ATOM    614  CG2 VAL A1071     -36.065  27.265 -33.074  1.00 20.61           C  
ATOM    615  N   SER A1072     -36.979  28.918 -28.755  1.00 19.95           N  
ATOM    616  CA  SER A1072     -36.552  29.446 -27.469  1.00 19.41           C  
ATOM    617  C   SER A1072     -36.378  28.344 -26.441  1.00 18.46           C  
ATOM    618  O   SER A1072     -36.654  27.168 -26.722  1.00 18.64           O  
ATOM    619  CB  SER A1072     -37.525  30.533 -26.998  1.00 19.47           C  
ATOM    620  OG  SER A1072     -38.854  30.057 -26.989  1.00 20.93           O  
ATOM    621  N   MET A1073     -35.902  28.730 -25.258  1.00 17.34           N  
ATOM    622  CA  MET A1073     -35.674  27.811 -24.152  1.00 16.50           C  
ATOM    623  C   MET A1073     -36.891  26.909 -23.986  1.00 15.18           C  
ATOM    624  O   MET A1073     -38.003  27.390 -23.984  1.00 14.72           O  
ATOM    625  CB  MET A1073     -35.388  28.601 -22.864  1.00 16.82           C  
ATOM    626  CG  MET A1073     -35.015  27.767 -21.657  1.00 17.86           C  
ATOM    627  SD  MET A1073     -33.742  26.526 -22.005  1.00 19.60           S  
ATOM    628  CE  MET A1073     -32.412  27.578 -22.624  1.00 17.59           C  
ATOM    629  N   GLY A1074     -36.676  25.596 -23.934  1.00 14.04           N  
ATOM    630  CA  GLY A1074     -37.766  24.643 -23.720  1.00 13.09           C  
ATOM    631  C   GLY A1074     -38.504  24.179 -24.959  1.00 12.36           C  
ATOM    632  O   GLY A1074     -39.344  23.288 -24.873  1.00 11.98           O  
ATOM    633  N   THR A1075     -38.207  24.757 -26.122  1.00 12.07           N  
ATOM    634  CA  THR A1075     -38.967  24.417 -27.333  1.00 11.71           C  
ATOM    635  C   THR A1075     -38.696  22.960 -27.685  1.00 10.95           C  
ATOM    636  O   THR A1075     -37.582  22.476 -27.499  1.00 10.49           O  
ATOM    637  CB  THR A1075     -38.623  25.345 -28.538  1.00 12.29           C  
ATOM    638  OG1 THR A1075     -38.973  26.696 -28.223  1.00 13.26           O  
ATOM    639  CG2 THR A1075     -39.382  24.924 -29.796  1.00 12.00           C  
ATOM    640  N   VAL A1076     -39.727  22.261 -28.142  1.00 10.47           N  
ATOM    641  CA  VAL A1076     -39.596  20.871 -28.587  1.00 10.48           C  
ATOM    642  C   VAL A1076     -39.883  20.807 -30.075  1.00 10.79           C  
ATOM    643  O   VAL A1076     -40.935  21.267 -30.526  1.00 10.96           O  
ATOM    644  CB  VAL A1076     -40.576  19.921 -27.852  1.00 10.19           C  
ATOM    645  CG1 VAL A1076     -40.490  18.502 -28.411  1.00  8.90           C  
ATOM    646  CG2 VAL A1076     -40.287  19.923 -26.349  1.00 10.51           C  
ATOM    647  N   LEU A1077     -38.963  20.219 -30.837  1.00 11.18           N  
ATOM    648  CA  LEU A1077     -39.157  20.080 -32.272  1.00 11.27           C  
ATOM    649  C   LEU A1077     -39.136  18.607 -32.698  1.00 11.60           C  
ATOM    650  O   LEU A1077     -38.222  17.872 -32.360  1.00 11.11           O  
ATOM    651  CB  LEU A1077     -38.094  20.875 -33.024  1.00 11.20           C  
ATOM    652  CG  LEU A1077     -37.891  22.313 -32.551  1.00 10.75           C  
ATOM    653  CD1 LEU A1077     -36.747  22.401 -31.533  1.00  8.38           C  
ATOM    654  CD2 LEU A1077     -37.630  23.225 -33.737  1.00 11.62           C  
ATOM    655  N   LYS A1078     -40.160  18.199 -33.452  1.00 12.08           N  
ATOM    656  CA  LYS A1078     -40.301  16.832 -33.904  1.00 12.63           C  
ATOM    657  C   LYS A1078     -39.766  16.653 -35.323  1.00 12.58           C  
ATOM    658  O   LYS A1078     -40.085  17.436 -36.224  1.00 12.13           O  
ATOM    659  CB  LYS A1078     -41.773  16.416 -33.859  1.00 13.27           C  
ATOM    660  CG  LYS A1078     -42.075  15.064 -34.485  1.00 15.18           C  
ATOM    661  CD  LYS A1078     -43.550  14.663 -34.319  1.00 18.90           C  
ATOM    662  CE  LYS A1078     -44.438  15.198 -35.426  1.00 21.41           C  
ATOM    663  NZ  LYS A1078     -44.682  14.178 -36.480  1.00 23.02           N  
ATOM    664  N   THR A1079     -38.952  15.617 -35.503  1.00 12.36           N  
ATOM    665  CA  THR A1079     -38.566  15.137 -36.826  1.00 12.36           C  
ATOM    666  C   THR A1079     -38.790  13.634 -36.950  1.00 12.83           C  
ATOM    667  O   THR A1079     -38.931  12.923 -35.940  1.00 12.37           O  
ATOM    668  CB  THR A1079     -37.065  15.385 -37.145  1.00 12.15           C  
ATOM    669  OG1 THR A1079     -36.250  14.533 -36.329  1.00 11.44           O  
ATOM    670  CG2 THR A1079     -36.676  16.837 -36.923  1.00 11.33           C  
ATOM    671  N   SER A1080     -38.780  13.163 -38.201  1.00 12.94           N  
ATOM    672  CA  SER A1080     -38.701  11.732 -38.507  1.00 13.17           C  
ATOM    673  C   SER A1080     -37.297  11.233 -38.170  1.00 13.19           C  
ATOM    674  O   SER A1080     -36.418  12.020 -37.818  1.00 12.76           O  
ATOM    675  CB  SER A1080     -39.045  11.468 -39.975  1.00 13.30           C  
ATOM    676  OG  SER A1080     -38.057  12.012 -40.838  1.00 13.86           O  
ATOM    677  N   SER A1081     -37.091   9.923 -38.283  1.00 13.33           N  
ATOM    678  CA  SER A1081     -35.935   9.261 -37.680  1.00 13.71           C  
ATOM    679  C   SER A1081     -34.856   8.836 -38.653  1.00 13.34           C  
ATOM    680  O   SER A1081     -33.739   8.533 -38.235  1.00 12.60           O  
ATOM    681  CB  SER A1081     -36.404   8.026 -36.917  1.00 14.16           C  
ATOM    682  OG  SER A1081     -37.242   7.239 -37.743  1.00 16.20           O  
ATOM    683  N   TRP A1082     -35.187   8.793 -39.938  1.00 13.88           N  
ATOM    684  CA  TRP A1082     -34.226   8.466 -40.978  1.00 14.20           C  
ATOM    685  C   TRP A1082     -33.564   7.119 -40.696  1.00 14.64           C  
ATOM    686  O   TRP A1082     -34.261   6.149 -40.568  1.00 13.64           O  
ATOM    687  CB  TRP A1082     -33.251   9.624 -41.132  1.00 14.33           C  
ATOM    688  CG  TRP A1082     -34.013  10.828 -41.525  1.00 15.76           C  
ATOM    689  CD1 TRP A1082     -34.495  11.813 -40.698  1.00 15.92           C  
ATOM    690  CD2 TRP A1082     -34.460  11.151 -42.837  1.00 15.73           C  
ATOM    691  NE1 TRP A1082     -35.181  12.743 -41.433  1.00 15.70           N  
ATOM    692  CE2 TRP A1082     -35.182  12.359 -42.747  1.00 15.18           C  
ATOM    693  CE3 TRP A1082     -34.304  10.543 -44.095  1.00 16.28           C  
ATOM    694  CZ2 TRP A1082     -35.746  12.978 -43.865  1.00 15.51           C  
ATOM    695  CZ3 TRP A1082     -34.870  11.161 -45.203  1.00 15.73           C  
ATOM    696  CH2 TRP A1082     -35.579  12.367 -45.078  1.00 15.14           C  
ATOM    697  N   ASN A1083     -32.244   7.042 -40.574  1.00 15.87           N  
ATOM    698  CA  ASN A1083     -31.624   5.739 -40.326  1.00 17.43           C  
ATOM    699  C   ASN A1083     -31.661   5.244 -38.868  1.00 17.68           C  
ATOM    700  O   ASN A1083     -31.109   4.191 -38.576  1.00 17.50           O  
ATOM    701  CB  ASN A1083     -30.192   5.706 -40.873  1.00 17.96           C  
ATOM    702  CG  ASN A1083     -30.148   5.456 -42.372  1.00 20.67           C  
ATOM    703  OD1 ASN A1083     -31.131   5.000 -42.970  1.00 23.66           O  
ATOM    704  ND2 ASN A1083     -29.001   5.759 -42.995  1.00 23.99           N  
ATOM    705  N   LEU A1084     -32.325   5.976 -37.969  1.00 18.20           N  
ATOM    706  CA  LEU A1084     -32.560   5.489 -36.607  1.00 18.19           C  
ATOM    707  C   LEU A1084     -33.681   4.441 -36.614  1.00 18.62           C  
ATOM    708  O   LEU A1084     -34.429   4.343 -37.571  1.00 18.63           O  
ATOM    709  CB  LEU A1084     -32.910   6.649 -35.662  1.00 18.07           C  
ATOM    710  CG  LEU A1084     -31.806   7.672 -35.415  1.00 17.64           C  
ATOM    711  CD1 LEU A1084     -32.365   8.964 -34.808  1.00 16.88           C  
ATOM    712  CD2 LEU A1084     -30.735   7.068 -34.524  1.00 18.55           C  
ATOM    713  N   ASP A1085     -33.786   3.672 -35.536  1.00 19.33           N  
ATOM    714  CA  ASP A1085     -34.786   2.612 -35.410  1.00 20.52           C  
ATOM    715  C   ASP A1085     -36.079   3.071 -34.723  1.00 19.97           C  
ATOM    716  O   ASP A1085     -36.958   2.255 -34.457  1.00 19.67           O  
ATOM    717  CB  ASP A1085     -34.209   1.448 -34.595  1.00 21.34           C  
ATOM    718  CG  ASP A1085     -33.198   0.623 -35.371  1.00 25.73           C  
ATOM    719  OD1 ASP A1085     -33.500  -0.577 -35.608  1.00 30.32           O  
ATOM    720  OD2 ASP A1085     -32.114   1.159 -35.748  1.00 31.53           O  
ATOM    721  N   CYS A1086     -36.177   4.353 -34.392  1.00 19.28           N  
ATOM    722  CA  CYS A1086     -37.372   4.880 -33.757  1.00 18.81           C  
ATOM    723  C   CYS A1086     -38.261   5.486 -34.824  1.00 19.00           C  
ATOM    724  O   CYS A1086     -37.900   5.473 -35.983  1.00 19.46           O  
ATOM    725  CB  CYS A1086     -36.989   5.907 -32.689  1.00 19.21           C  
ATOM    726  SG  CYS A1086     -35.961   7.291 -33.266  1.00 16.97           S  
ATOM    727  N   ARG A1087     -39.429   5.986 -34.452  1.00 18.78           N  
ATOM    728  CA  ARG A1087     -40.313   6.646 -35.414  1.00 19.19           C  
ATOM    729  C   ARG A1087     -40.076   8.154 -35.457  1.00 17.98           C  
ATOM    730  O   ARG A1087     -39.994   8.740 -36.538  1.00 17.77           O  
ATOM    731  CB  ARG A1087     -41.784   6.380 -35.087  1.00 19.68           C  
ATOM    732  CG  ARG A1087     -42.301   5.094 -35.671  1.00 24.37           C  
ATOM    733  CD  ARG A1087     -43.588   4.644 -35.002  1.00 29.43           C  
ATOM    734  NE  ARG A1087     -44.151   3.494 -35.707  1.00 34.09           N  
ATOM    735  CZ  ARG A1087     -45.053   2.646 -35.204  1.00 37.68           C  
ATOM    736  NH1 ARG A1087     -45.518   2.788 -33.960  1.00 38.64           N  
ATOM    737  NH2 ARG A1087     -45.490   1.635 -35.957  1.00 38.78           N  
ATOM    738  N   TYR A1088     -40.008   8.789 -34.288  1.00 16.32           N  
ATOM    739  CA  TYR A1088     -39.769  10.226 -34.234  1.00 15.58           C  
ATOM    740  C   TYR A1088     -38.707  10.598 -33.221  1.00 13.90           C  
ATOM    741  O   TYR A1088     -38.551   9.936 -32.207  1.00 14.00           O  
ATOM    742  CB  TYR A1088     -41.054  10.990 -33.900  1.00 15.66           C  
ATOM    743  CG  TYR A1088     -42.190  10.732 -34.840  1.00 17.85           C  
ATOM    744  CD1 TYR A1088     -42.147  11.176 -36.162  1.00 20.36           C  
ATOM    745  CD2 TYR A1088     -43.324  10.053 -34.411  1.00 19.80           C  
ATOM    746  CE1 TYR A1088     -43.217  10.938 -37.035  1.00 21.75           C  
ATOM    747  CE2 TYR A1088     -44.383   9.811 -35.263  1.00 21.36           C  
ATOM    748  CZ  TYR A1088     -44.329  10.250 -36.570  1.00 23.02           C  
ATOM    749  OH  TYR A1088     -45.398   9.999 -37.397  1.00 25.25           O  
ATOM    750  N   VAL A1089     -37.998  11.683 -33.499  1.00 12.22           N  
ATOM    751  CA  VAL A1089     -37.128  12.297 -32.524  1.00 10.46           C  
ATOM    752  C   VAL A1089     -37.778  13.597 -32.062  1.00 10.00           C  
ATOM    753  O   VAL A1089     -38.244  14.387 -32.893  1.00  9.76           O  
ATOM    754  CB  VAL A1089     -35.757  12.589 -33.121  1.00 10.14           C  
ATOM    755  CG1 VAL A1089     -34.826  13.215 -32.088  1.00  9.11           C  
ATOM    756  CG2 VAL A1089     -35.147  11.312 -33.692  1.00 10.24           C  
ATOM    757  N   LEU A1090     -37.813  13.806 -30.745  1.00  8.86           N  
ATOM    758  CA  LEU A1090     -38.198  15.088 -30.163  1.00  9.14           C  
ATOM    759  C   LEU A1090     -36.942  15.800 -29.708  1.00  8.76           C  
ATOM    760  O   LEU A1090     -36.282  15.368 -28.751  1.00  8.89           O  
ATOM    761  CB  LEU A1090     -39.158  14.900 -28.979  1.00  8.98           C  
ATOM    762  CG  LEU A1090     -40.534  14.353 -29.322  1.00  8.07           C  
ATOM    763  CD1 LEU A1090     -41.384  14.234 -28.060  1.00  5.96           C  
ATOM    764  CD2 LEU A1090     -41.235  15.213 -30.379  1.00  6.12           C  
ATOM    765  N   HIS A1091     -36.595  16.870 -30.418  1.00  8.74           N  
ATOM    766  CA  HIS A1091     -35.397  17.648 -30.129  1.00  8.76           C  
ATOM    767  C   HIS A1091     -35.807  18.744 -29.157  1.00  9.22           C  
ATOM    768  O   HIS A1091     -36.743  19.475 -29.442  1.00  9.39           O  
ATOM    769  CB  HIS A1091     -34.815  18.273 -31.405  1.00  8.88           C  
ATOM    770  CG  HIS A1091     -34.504  17.278 -32.488  1.00  8.51           C  
ATOM    771  ND1 HIS A1091     -33.235  16.789 -32.711  1.00  8.60           N  
ATOM    772  CD2 HIS A1091     -35.303  16.691 -33.416  1.00  8.83           C  
ATOM    773  CE1 HIS A1091     -33.269  15.930 -33.717  1.00  9.57           C  
ATOM    774  NE2 HIS A1091     -34.512  15.853 -34.165  1.00  8.52           N  
ATOM    775  N   VAL A1092     -35.137  18.832 -28.005  1.00  9.14           N  
ATOM    776  CA  VAL A1092     -35.510  19.788 -26.974  1.00  9.35           C  
ATOM    777  C   VAL A1092     -34.362  20.739 -26.661  1.00  9.65           C  
ATOM    778  O   VAL A1092     -33.204  20.335 -26.582  1.00 10.35           O  
ATOM    779  CB  VAL A1092     -35.995  19.075 -25.680  1.00  9.29           C  
ATOM    780  CG1 VAL A1092     -37.019  17.996 -26.029  1.00  8.29           C  
ATOM    781  CG2 VAL A1092     -34.810  18.517 -24.872  1.00  9.81           C  
ATOM    782  N   VAL A1093     -34.681  22.017 -26.525  1.00 10.09           N  
ATOM    783  CA  VAL A1093     -33.700  22.997 -26.087  1.00 10.15           C  
ATOM    784  C   VAL A1093     -33.757  23.016 -24.568  1.00 10.84           C  
ATOM    785  O   VAL A1093     -34.681  23.584 -23.974  1.00 10.73           O  
ATOM    786  CB  VAL A1093     -33.975  24.399 -26.649  1.00 10.51           C  
ATOM    787  CG1 VAL A1093     -32.909  25.397 -26.138  1.00  9.20           C  
ATOM    788  CG2 VAL A1093     -34.031  24.364 -28.191  1.00  8.97           C  
ATOM    789  N   ALA A1094     -32.784  22.349 -23.958  1.00 11.15           N  
ATOM    790  CA  ALA A1094     -32.742  22.157 -22.523  1.00 11.82           C  
ATOM    791  C   ALA A1094     -31.881  23.255 -21.887  1.00 12.04           C  
ATOM    792  O   ALA A1094     -30.965  23.744 -22.510  1.00 11.94           O  
ATOM    793  CB  ALA A1094     -32.172  20.779 -22.202  1.00 10.91           C  
ATOM    794  N   PRO A1095     -32.150  23.602 -20.623  1.00 12.98           N  
ATOM    795  CA  PRO A1095     -31.421  24.674 -19.937  1.00 13.33           C  
ATOM    796  C   PRO A1095     -30.073  24.262 -19.350  1.00 14.23           C  
ATOM    797  O   PRO A1095     -29.853  23.089 -19.028  1.00 14.06           O  
ATOM    798  CB  PRO A1095     -32.358  25.035 -18.797  1.00 12.98           C  
ATOM    799  CG  PRO A1095     -32.979  23.732 -18.437  1.00 13.47           C  
ATOM    800  CD  PRO A1095     -33.190  23.018 -19.755  1.00 12.97           C  
ATOM    801  N   GLU A1096     -29.190  25.239 -19.186  1.00 15.52           N  
ATOM    802  CA  GLU A1096     -27.965  25.038 -18.426  1.00 16.81           C  
ATOM    803  C   GLU A1096     -28.286  24.894 -16.943  1.00 17.02           C  
ATOM    804  O   GLU A1096     -29.247  25.492 -16.436  1.00 16.74           O  
ATOM    805  CB  GLU A1096     -27.010  26.214 -18.615  1.00 17.65           C  
ATOM    806  CG  GLU A1096     -26.644  26.499 -20.066  1.00 20.60           C  
ATOM    807  CD  GLU A1096     -25.494  27.473 -20.196  1.00 25.02           C  
ATOM    808  OE1 GLU A1096     -24.541  27.399 -19.398  1.00 29.45           O  
ATOM    809  OE2 GLU A1096     -25.523  28.310 -21.114  1.00 28.89           O  
ATOM    810  N   TRP A1097     -27.477  24.105 -16.247  1.00 17.50           N  
ATOM    811  CA  TRP A1097     -27.664  23.897 -14.814  1.00 18.36           C  
ATOM    812  C   TRP A1097     -27.640  25.252 -14.064  1.00 19.55           C  
ATOM    813  O   TRP A1097     -28.516  25.524 -13.237  1.00 18.40           O  
ATOM    814  CB  TRP A1097     -26.592  22.934 -14.304  1.00 18.09           C  
ATOM    815  CG  TRP A1097     -26.638  22.589 -12.851  1.00 17.59           C  
ATOM    816  CD1 TRP A1097     -25.615  22.715 -11.952  1.00 16.53           C  
ATOM    817  CD2 TRP A1097     -27.739  22.025 -12.129  1.00 16.66           C  
ATOM    818  NE1 TRP A1097     -26.016  22.273 -10.724  1.00 17.76           N  
ATOM    819  CE2 TRP A1097     -27.317  21.854 -10.799  1.00 16.66           C  
ATOM    820  CE3 TRP A1097     -29.039  21.640 -12.481  1.00 16.48           C  
ATOM    821  CZ2 TRP A1097     -28.145  21.317  -9.815  1.00 17.50           C  
ATOM    822  CZ3 TRP A1097     -29.867  21.112 -11.499  1.00 16.88           C  
ATOM    823  CH2 TRP A1097     -29.417  20.956 -10.180  1.00 16.05           C  
ATOM    824  N   ARG A1098     -26.668  26.097 -14.413  1.00 21.30           N  
ATOM    825  CA  ARG A1098     -26.482  27.415 -13.804  1.00 23.01           C  
ATOM    826  C   ARG A1098     -26.512  27.268 -12.288  1.00 23.59           C  
ATOM    827  O   ARG A1098     -27.306  27.898 -11.601  1.00 23.12           O  
ATOM    828  CB  ARG A1098     -27.531  28.424 -14.290  1.00 23.76           C  
ATOM    829  CG  ARG A1098     -27.764  28.394 -15.801  1.00 27.03           C  
ATOM    830  CD  ARG A1098     -28.198  29.728 -16.408  1.00 31.28           C  
ATOM    831  NE  ARG A1098     -29.047  30.527 -15.517  1.00 35.07           N  
ATOM    832  CZ  ARG A1098     -28.664  31.636 -14.872  1.00 38.07           C  
ATOM    833  NH1 ARG A1098     -29.525  32.271 -14.082  1.00 39.53           N  
ATOM    834  NH2 ARG A1098     -27.431  32.122 -14.996  1.00 39.31           N  
ATOM    835  N   ASN A1099     -25.649  26.388 -11.790  1.00 24.76           N  
ATOM    836  CA  ASN A1099     -25.483  26.162 -10.354  1.00 25.97           C  
ATOM    837  C   ASN A1099     -26.769  25.799  -9.613  1.00 25.80           C  
ATOM    838  O   ASN A1099     -26.969  26.212  -8.476  1.00 26.28           O  
ATOM    839  CB  ASN A1099     -24.833  27.391  -9.692  1.00 26.46           C  
ATOM    840  CG  ASN A1099     -24.029  27.018  -8.466  1.00 29.03           C  
ATOM    841  OD1 ASN A1099     -23.153  26.152  -8.538  1.00 32.96           O  
ATOM    842  ND2 ASN A1099     -24.330  27.646  -7.326  1.00 30.94           N  
ATOM    843  N   GLY A1100     -27.641  25.028 -10.255  1.00 25.46           N  
ATOM    844  CA  GLY A1100     -28.855  24.553  -9.598  1.00 25.04           C  
ATOM    845  C   GLY A1100     -29.949  25.595  -9.541  1.00 24.61           C  
ATOM    846  O   GLY A1100     -30.785  25.568  -8.649  1.00 24.75           O  
ATOM    847  N   SER A1101     -29.953  26.501 -10.509  1.00 23.80           N  
ATOM    848  CA  SER A1101     -31.049  27.439 -10.673  1.00 23.60           C  
ATOM    849  C   SER A1101     -32.409  26.741 -10.594  1.00 23.10           C  
ATOM    850  O   SER A1101     -32.637  25.737 -11.279  1.00 23.24           O  
ATOM    851  CB  SER A1101     -30.913  28.147 -12.028  1.00 23.69           C  
ATOM    852  OG  SER A1101     -32.163  28.623 -12.474  1.00 23.88           O  
ATOM    853  N   THR A1102     -33.314  27.279  -9.779  1.00 22.12           N  
ATOM    854  CA  THR A1102     -34.661  26.724  -9.663  1.00 21.70           C  
ATOM    855  C   THR A1102     -35.427  26.845 -10.987  1.00 20.73           C  
ATOM    856  O   THR A1102     -36.313  26.044 -11.300  1.00 20.32           O  
ATOM    857  CB  THR A1102     -35.480  27.434  -8.569  1.00 21.83           C  
ATOM    858  OG1 THR A1102     -35.530  28.831  -8.851  1.00 21.93           O  
ATOM    859  CG2 THR A1102     -34.864  27.213  -7.181  1.00 22.39           C  
ATOM    860  N   SER A1103     -35.096  27.881 -11.735  1.00 19.76           N  
ATOM    861  CA  SER A1103     -35.593  28.071 -13.093  1.00 19.42           C  
ATOM    862  C   SER A1103     -35.245  26.852 -13.973  1.00 18.21           C  
ATOM    863  O   SER A1103     -36.120  26.262 -14.610  1.00 17.61           O  
ATOM    864  CB  SER A1103     -34.993  29.372 -13.660  1.00 19.56           C  
ATOM    865  OG  SER A1103     -35.413  29.601 -14.983  1.00 21.74           O  
ATOM    866  N   SER A1104     -33.978  26.452 -13.950  1.00 17.22           N  
ATOM    867  CA  SER A1104     -33.505  25.294 -14.714  1.00 16.79           C  
ATOM    868  C   SER A1104     -34.198  23.972 -14.333  1.00 16.36           C  
ATOM    869  O   SER A1104     -34.541  23.182 -15.208  1.00 16.09           O  
ATOM    870  CB  SER A1104     -31.982  25.149 -14.573  1.00 16.83           C  
ATOM    871  OG  SER A1104     -31.320  26.321 -15.047  1.00 16.97           O  
ATOM    872  N   LEU A1105     -34.409  23.736 -13.039  1.00 15.90           N  
ATOM    873  CA  LEU A1105     -35.152  22.560 -12.587  1.00 15.60           C  
ATOM    874  C   LEU A1105     -36.526  22.496 -13.220  1.00 15.35           C  
ATOM    875  O   LEU A1105     -36.893  21.474 -13.814  1.00 14.66           O  
ATOM    876  CB  LEU A1105     -35.322  22.551 -11.066  1.00 15.74           C  
ATOM    877  CG  LEU A1105     -34.088  22.261 -10.211  1.00 16.48           C  
ATOM    878  CD1 LEU A1105     -34.383  22.573  -8.747  1.00 17.22           C  
ATOM    879  CD2 LEU A1105     -33.653  20.808 -10.375  1.00 17.29           C  
ATOM    880  N   LYS A1106     -37.260  23.605 -13.085  1.00 15.13           N  
ATOM    881  CA  LYS A1106     -38.636  23.732 -13.547  1.00 15.35           C  
ATOM    882  C   LYS A1106     -38.712  23.513 -15.051  1.00 14.27           C  
ATOM    883  O   LYS A1106     -39.583  22.787 -15.517  1.00 13.71           O  
ATOM    884  CB  LYS A1106     -39.185  25.140 -13.257  1.00 16.06           C  
ATOM    885  CG  LYS A1106     -39.643  25.397 -11.831  1.00 19.61           C  
ATOM    886  CD  LYS A1106     -39.936  26.918 -11.577  1.00 23.39           C  
ATOM    887  CE  LYS A1106     -41.095  27.123 -10.555  1.00 26.64           C  
ATOM    888  NZ  LYS A1106     -41.545  28.561 -10.419  1.00 27.79           N  
ATOM    889  N   ILE A1107     -37.810  24.168 -15.788  1.00 13.36           N  
ATOM    890  CA  ILE A1107     -37.768  24.078 -17.258  1.00 12.88           C  
ATOM    891  C   ILE A1107     -37.497  22.647 -17.733  1.00 12.06           C  
ATOM    892  O   ILE A1107     -38.191  22.154 -18.610  1.00 12.55           O  
ATOM    893  CB  ILE A1107     -36.731  25.064 -17.862  1.00 12.73           C  
ATOM    894  CG1 ILE A1107     -37.269  26.492 -17.761  1.00 13.07           C  
ATOM    895  CG2 ILE A1107     -36.448  24.746 -19.311  1.00 11.41           C  
ATOM    896  CD1 ILE A1107     -36.233  27.576 -18.075  1.00 13.36           C  
ATOM    897  N   MET A1108     -36.509  21.990 -17.132  1.00 11.38           N  
ATOM    898  CA  MET A1108     -36.185  20.589 -17.429  1.00 10.62           C  
ATOM    899  C   MET A1108     -37.362  19.662 -17.123  1.00 10.15           C  
ATOM    900  O   MET A1108     -37.746  18.850 -17.949  1.00  9.93           O  
ATOM    901  CB  MET A1108     -34.947  20.158 -16.634  1.00 10.32           C  
ATOM    902  CG  MET A1108     -34.398  18.763 -16.977  1.00 10.88           C  
ATOM    903  SD  MET A1108     -33.954  18.575 -18.729  1.00 10.73           S  
ATOM    904  CE  MET A1108     -32.181  18.800 -18.670  1.00  7.87           C  
ATOM    905  N   GLU A1109     -37.944  19.793 -15.938  1.00  9.84           N  
ATOM    906  CA  GLU A1109     -39.124  18.997 -15.575  1.00  9.98           C  
ATOM    907  C   GLU A1109     -40.262  19.185 -16.571  1.00  9.67           C  
ATOM    908  O   GLU A1109     -40.937  18.230 -16.951  1.00  9.42           O  
ATOM    909  CB  GLU A1109     -39.623  19.375 -14.183  1.00  9.80           C  
ATOM    910  CG  GLU A1109     -38.703  18.940 -13.059  1.00 11.65           C  
ATOM    911  CD  GLU A1109     -39.160  19.426 -11.677  1.00 14.89           C  
ATOM    912  OE1 GLU A1109     -40.087  20.259 -11.574  1.00 13.43           O  
ATOM    913  OE2 GLU A1109     -38.572  18.958 -10.685  1.00 18.46           O  
ATOM    914  N   ASP A1110     -40.485  20.421 -16.987  1.00  9.97           N  
ATOM    915  CA  ASP A1110     -41.590  20.696 -17.905  1.00 10.70           C  
ATOM    916  C   ASP A1110     -41.285  20.139 -19.316  1.00 10.10           C  
ATOM    917  O   ASP A1110     -42.181  19.639 -19.989  1.00 10.82           O  
ATOM    918  CB  ASP A1110     -41.964  22.189 -17.915  1.00 10.42           C  
ATOM    919  CG  ASP A1110     -43.416  22.436 -18.377  1.00 13.79           C  
ATOM    920  OD1 ASP A1110     -43.719  23.572 -18.867  1.00 17.36           O  
ATOM    921  OD2 ASP A1110     -44.254  21.511 -18.239  1.00 13.34           O  
ATOM    922  N   ILE A1111     -40.029  20.206 -19.750  1.00  9.70           N  
ATOM    923  CA  ILE A1111     -39.622  19.538 -20.991  1.00  9.42           C  
ATOM    924  C   ILE A1111     -39.981  18.041 -20.929  1.00  9.04           C  
ATOM    925  O   ILE A1111     -40.564  17.473 -21.851  1.00  8.13           O  
ATOM    926  CB  ILE A1111     -38.099  19.676 -21.242  1.00  9.43           C  
ATOM    927  CG1 ILE A1111     -37.741  21.094 -21.674  1.00  9.44           C  
ATOM    928  CG2 ILE A1111     -37.621  18.685 -22.304  1.00  9.76           C  
ATOM    929  CD1 ILE A1111     -36.216  21.384 -21.589  1.00  9.39           C  
ATOM    930  N   ILE A1112     -39.648  17.409 -19.814  1.00  9.31           N  
ATOM    931  CA  ILE A1112     -39.817  15.967 -19.706  1.00  8.86           C  
ATOM    932  C   ILE A1112     -41.304  15.649 -19.748  1.00  9.29           C  
ATOM    933  O   ILE A1112     -41.720  14.740 -20.455  1.00  9.35           O  
ATOM    934  CB  ILE A1112     -39.109  15.438 -18.452  1.00  8.91           C  
ATOM    935  CG1 ILE A1112     -37.593  15.571 -18.644  1.00  8.65           C  
ATOM    936  CG2 ILE A1112     -39.502  13.972 -18.122  1.00  7.02           C  
ATOM    937  CD1 ILE A1112     -36.815  15.627 -17.309  1.00  8.42           C  
ATOM    938  N   ARG A1113     -42.100  16.423 -19.010  1.00  9.74           N  
ATOM    939  CA  ARG A1113     -43.545  16.260 -18.994  1.00  9.94           C  
ATOM    940  C   ARG A1113     -44.084  16.408 -20.410  1.00  9.89           C  
ATOM    941  O   ARG A1113     -44.895  15.605 -20.857  1.00 10.09           O  
ATOM    942  CB  ARG A1113     -44.227  17.312 -18.101  1.00 10.19           C  
ATOM    943  CG  ARG A1113     -45.749  17.118 -17.991  1.00 11.08           C  
ATOM    944  CD  ARG A1113     -46.466  18.321 -17.369  1.00 13.78           C  
ATOM    945  NE  ARG A1113     -46.275  19.511 -18.207  1.00 15.86           N  
ATOM    946  CZ  ARG A1113     -46.897  19.743 -19.360  1.00 16.99           C  
ATOM    947  NH1 ARG A1113     -46.615  20.840 -20.053  1.00 17.96           N  
ATOM    948  NH2 ARG A1113     -47.795  18.890 -19.836  1.00 18.26           N  
ATOM    949  N   GLU A1114     -43.640  17.454 -21.100  1.00  9.32           N  
ATOM    950  CA  GLU A1114     -44.164  17.754 -22.413  1.00  9.44           C  
ATOM    951  C   GLU A1114     -43.871  16.645 -23.399  1.00  9.18           C  
ATOM    952  O   GLU A1114     -44.726  16.298 -24.206  1.00  8.62           O  
ATOM    953  CB  GLU A1114     -43.594  19.082 -22.938  1.00  9.56           C  
ATOM    954  CG  GLU A1114     -44.019  19.450 -24.362  1.00  9.73           C  
ATOM    955  CD  GLU A1114     -45.521  19.677 -24.521  1.00 10.97           C  
ATOM    956  OE1 GLU A1114     -46.249  19.797 -23.505  1.00  8.47           O  
ATOM    957  OE2 GLU A1114     -45.978  19.741 -25.682  1.00 11.91           O  
ATOM    958  N   CYS A1115     -42.661  16.102 -23.358  1.00  9.18           N  
ATOM    959  CA  CYS A1115     -42.315  15.032 -24.291  1.00  9.39           C  
ATOM    960  C   CYS A1115     -43.244  13.829 -24.125  1.00  9.06           C  
ATOM    961  O   CYS A1115     -43.624  13.201 -25.113  1.00  8.58           O  
ATOM    962  CB  CYS A1115     -40.854  14.612 -24.149  1.00  9.52           C  
ATOM    963  SG  CYS A1115     -39.690  15.829 -24.813  1.00 10.60           S  
ATOM    964  N   MET A1116     -43.610  13.513 -22.890  1.00  9.14           N  
ATOM    965  CA  MET A1116     -44.541  12.413 -22.664  1.00  9.95           C  
ATOM    966  C   MET A1116     -45.941  12.781 -23.145  1.00 10.33           C  
ATOM    967  O   MET A1116     -46.593  11.959 -23.785  1.00 10.70           O  
ATOM    968  CB  MET A1116     -44.560  11.974 -21.201  1.00  9.88           C  
ATOM    969  CG  MET A1116     -43.252  11.315 -20.757  1.00  9.59           C  
ATOM    970  SD  MET A1116     -43.329  10.818 -19.033  1.00  8.02           S  
ATOM    971  CE  MET A1116     -43.201  12.443 -18.261  1.00  6.02           C  
ATOM    972  N   GLU A1117     -46.387  14.007 -22.879  1.00 11.27           N  
ATOM    973  CA  GLU A1117     -47.673  14.487 -23.412  1.00 12.10           C  
ATOM    974  C   GLU A1117     -47.724  14.361 -24.935  1.00 12.17           C  
ATOM    975  O   GLU A1117     -48.700  13.874 -25.492  1.00 12.42           O  
ATOM    976  CB  GLU A1117     -47.937  15.950 -23.026  1.00 12.54           C  
ATOM    977  CG  GLU A1117     -49.328  16.442 -23.487  1.00 16.10           C  
ATOM    978  CD  GLU A1117     -49.648  17.868 -23.063  1.00 20.76           C  
ATOM    979  OE1 GLU A1117     -50.101  18.668 -23.914  1.00 24.54           O  
ATOM    980  OE2 GLU A1117     -49.452  18.201 -21.879  1.00 24.74           O  
ATOM    981  N   ILE A1118     -46.667  14.806 -25.607  1.00 11.95           N  
ATOM    982  CA  ILE A1118     -46.620  14.742 -27.056  1.00 11.72           C  
ATOM    983  C   ILE A1118     -46.749  13.284 -27.492  1.00 12.01           C  
ATOM    984  O   ILE A1118     -47.535  12.963 -28.379  1.00 12.70           O  
ATOM    985  CB  ILE A1118     -45.320  15.384 -27.615  1.00 11.42           C  
ATOM    986  CG1 ILE A1118     -45.386  16.906 -27.485  1.00  9.71           C  
ATOM    987  CG2 ILE A1118     -45.094  15.003 -29.091  1.00 11.20           C  
ATOM    988  CD1 ILE A1118     -44.044  17.595 -27.580  1.00  8.18           C  
ATOM    989  N   THR A1119     -46.001  12.399 -26.845  1.00 12.17           N  
ATOM    990  CA  THR A1119     -45.991  10.989 -27.226  1.00 12.16           C  
ATOM    991  C   THR A1119     -47.389  10.387 -27.143  1.00 12.53           C  
ATOM    992  O   THR A1119     -47.826   9.694 -28.066  1.00 12.68           O  
ATOM    993  CB  THR A1119     -44.973  10.197 -26.375  1.00 12.17           C  
ATOM    994  OG1 THR A1119     -43.674  10.769 -26.552  1.00 11.59           O  
ATOM    995  CG2 THR A1119     -44.921   8.737 -26.796  1.00 11.70           C  
ATOM    996  N   GLU A1120     -48.099  10.673 -26.056  1.00 13.15           N  
ATOM    997  CA  GLU A1120     -49.491  10.245 -25.902  1.00 13.88           C  
ATOM    998  C   GLU A1120     -50.381  10.863 -27.000  1.00 14.60           C  
ATOM    999  O   GLU A1120     -51.207  10.170 -27.601  1.00 14.28           O  
ATOM   1000  CB  GLU A1120     -49.990  10.592 -24.496  1.00 14.21           C  
ATOM   1001  CG  GLU A1120     -51.480  10.392 -24.217  1.00 14.76           C  
ATOM   1002  CD  GLU A1120     -51.908   8.941 -24.092  1.00 15.87           C  
ATOM   1003  OE1 GLU A1120     -53.128   8.724 -23.921  1.00 18.60           O  
ATOM   1004  OE2 GLU A1120     -51.064   8.015 -24.164  1.00 14.91           O  
ATOM   1005  N   SER A1121     -50.175  12.144 -27.301  1.00 15.38           N  
ATOM   1006  CA  SER A1121     -50.994  12.829 -28.300  1.00 16.21           C  
ATOM   1007  C   SER A1121     -50.814  12.216 -29.696  1.00 16.40           C  
ATOM   1008  O   SER A1121     -51.730  12.244 -30.524  1.00 16.03           O  
ATOM   1009  CB  SER A1121     -50.702  14.331 -28.315  1.00 16.59           C  
ATOM   1010  OG  SER A1121     -49.452  14.625 -28.947  1.00 19.12           O  
ATOM   1011  N   LEU A1122     -49.648  11.625 -29.939  1.00 16.22           N  
ATOM   1012  CA  LEU A1122     -49.383  10.966 -31.220  1.00 16.23           C  
ATOM   1013  C   LEU A1122     -49.865   9.510 -31.242  1.00 16.11           C  
ATOM   1014  O   LEU A1122     -49.621   8.794 -32.207  1.00 16.14           O  
ATOM   1015  CB  LEU A1122     -47.887  11.055 -31.554  1.00 15.75           C  
ATOM   1016  CG  LEU A1122     -47.372  12.491 -31.724  1.00 15.95           C  
ATOM   1017  CD1 LEU A1122     -45.866  12.529 -31.774  1.00 13.03           C  
ATOM   1018  CD2 LEU A1122     -47.989  13.154 -32.973  1.00 16.04           C  
ATOM   1019  N   SER A1123     -50.542   9.087 -30.177  1.00 16.23           N  
ATOM   1020  CA  SER A1123     -51.025   7.718 -30.026  1.00 16.60           C  
ATOM   1021  C   SER A1123     -49.895   6.705 -30.071  1.00 16.30           C  
ATOM   1022  O   SER A1123     -50.076   5.610 -30.605  1.00 17.23           O  
ATOM   1023  CB  SER A1123     -52.093   7.385 -31.093  1.00 16.76           C  
ATOM   1024  OG  SER A1123     -53.212   8.234 -30.914  1.00 18.12           O  
ATOM   1025  N   LEU A1124     -48.747   7.060 -29.497  1.00 15.57           N  
ATOM   1026  CA  LEU A1124     -47.577   6.184 -29.488  1.00 15.39           C  
ATOM   1027  C   LEU A1124     -47.373   5.537 -28.113  1.00 15.16           C  
ATOM   1028  O   LEU A1124     -47.885   6.027 -27.112  1.00 15.41           O  
ATOM   1029  CB  LEU A1124     -46.332   6.962 -29.929  1.00 15.04           C  
ATOM   1030  CG  LEU A1124     -46.394   7.461 -31.376  1.00 14.41           C  
ATOM   1031  CD1 LEU A1124     -45.292   8.482 -31.661  1.00 13.60           C  
ATOM   1032  CD2 LEU A1124     -46.322   6.280 -32.359  1.00 14.26           C  
ATOM   1033  N   LYS A1125     -46.609   4.446 -28.082  1.00 15.20           N  
ATOM   1034  CA  LYS A1125     -46.523   3.564 -26.911  1.00 15.32           C  
ATOM   1035  C   LYS A1125     -45.318   3.825 -26.015  1.00 14.29           C  
ATOM   1036  O   LYS A1125     -45.410   3.656 -24.800  1.00 14.77           O  
ATOM   1037  CB  LYS A1125     -46.487   2.093 -27.354  1.00 16.23           C  
ATOM   1038  CG  LYS A1125     -46.885   1.090 -26.255  1.00 19.97           C  
ATOM   1039  CD  LYS A1125     -46.185  -0.286 -26.355  1.00 23.89           C  
ATOM   1040  CE  LYS A1125     -46.747  -1.158 -27.481  1.00 27.14           C  
ATOM   1041  NZ  LYS A1125     -46.422  -2.645 -27.323  1.00 29.23           N  
ATOM   1042  N   SER A1126     -44.187   4.213 -26.597  1.00 12.73           N  
ATOM   1043  CA  SER A1126     -42.944   4.261 -25.851  1.00 11.86           C  
ATOM   1044  C   SER A1126     -42.052   5.443 -26.222  1.00 11.36           C  
ATOM   1045  O   SER A1126     -42.059   5.919 -27.369  1.00 11.15           O  
ATOM   1046  CB  SER A1126     -42.159   2.950 -26.039  1.00 11.78           C  
ATOM   1047  OG  SER A1126     -41.854   2.741 -27.396  1.00 10.81           O  
ATOM   1048  N   ILE A1127     -41.271   5.877 -25.240  1.00 10.10           N  
ATOM   1049  CA  ILE A1127     -40.357   6.986 -25.399  1.00 10.24           C  
ATOM   1050  C   ILE A1127     -39.074   6.673 -24.634  1.00 10.07           C  
ATOM   1051  O   ILE A1127     -39.119   6.112 -23.543  1.00 11.25           O  
ATOM   1052  CB  ILE A1127     -41.008   8.350 -24.963  1.00  9.82           C  
ATOM   1053  CG1 ILE A1127     -40.001   9.505 -25.052  1.00  9.19           C  
ATOM   1054  CG2 ILE A1127     -41.588   8.271 -23.572  1.00  8.88           C  
ATOM   1055  CD1 ILE A1127     -40.631  10.874 -24.869  1.00  9.62           C  
ATOM   1056  N   ALA A1128     -37.941   6.997 -25.242  1.00  9.39           N  
ATOM   1057  CA  ALA A1128     -36.637   6.865 -24.624  1.00  9.25           C  
ATOM   1058  C   ALA A1128     -36.087   8.249 -24.336  1.00  9.07           C  
ATOM   1059  O   ALA A1128     -35.992   9.087 -25.245  1.00  9.09           O  
ATOM   1060  CB  ALA A1128     -35.658   6.105 -25.563  1.00  8.75           C  
ATOM   1061  N   PHE A1129     -35.721   8.468 -23.078  1.00  8.86           N  
ATOM   1062  CA  PHE A1129     -34.960   9.623 -22.651  1.00  9.03           C  
ATOM   1063  C   PHE A1129     -33.536   9.170 -22.373  1.00  9.42           C  
ATOM   1064  O   PHE A1129     -33.305   8.336 -21.489  1.00  9.57           O  
ATOM   1065  CB  PHE A1129     -35.492  10.179 -21.331  1.00  8.86           C  
ATOM   1066  CG  PHE A1129     -36.817  10.880 -21.432  1.00  9.31           C  
ATOM   1067  CD1 PHE A1129     -36.884  12.212 -21.775  1.00  8.80           C  
ATOM   1068  CD2 PHE A1129     -37.992  10.217 -21.128  1.00  8.79           C  
ATOM   1069  CE1 PHE A1129     -38.096  12.850 -21.838  1.00  9.99           C  
ATOM   1070  CE2 PHE A1129     -39.208  10.852 -21.180  1.00  7.81           C  
ATOM   1071  CZ  PHE A1129     -39.264  12.176 -21.521  1.00  9.54           C  
ATOM   1072  N   PRO A1130     -32.563   9.725 -23.094  1.00  9.72           N  
ATOM   1073  CA  PRO A1130     -31.221   9.648 -22.547  1.00  9.57           C  
ATOM   1074  C   PRO A1130     -31.100  10.658 -21.418  1.00  9.97           C  
ATOM   1075  O   PRO A1130     -32.056  11.396 -21.150  1.00  9.12           O  
ATOM   1076  CB  PRO A1130     -30.326  10.026 -23.724  1.00  9.70           C  
ATOM   1077  CG  PRO A1130     -31.170  10.801 -24.643  1.00 10.62           C  
ATOM   1078  CD  PRO A1130     -32.629  10.531 -24.322  1.00 10.07           C  
ATOM   1079  N   ALA A1131     -29.944  10.700 -20.760  1.00 10.59           N  
ATOM   1080  CA  ALA A1131     -29.761  11.598 -19.612  1.00 10.69           C  
ATOM   1081  C   ALA A1131     -29.478  13.021 -20.087  1.00 11.07           C  
ATOM   1082  O   ALA A1131     -28.384  13.551 -19.875  1.00 10.85           O  
ATOM   1083  CB  ALA A1131     -28.635  11.093 -18.714  1.00 10.58           C  
ATOM   1084  N   ILE A1132     -30.475  13.643 -20.712  1.00 11.33           N  
ATOM   1085  CA  ILE A1132     -30.324  14.986 -21.245  1.00 11.57           C  
ATOM   1086  C   ILE A1132     -29.958  15.927 -20.117  1.00 12.33           C  
ATOM   1087  O   ILE A1132     -30.346  15.710 -18.972  1.00 12.24           O  
ATOM   1088  CB  ILE A1132     -31.608  15.501 -21.980  1.00 11.61           C  
ATOM   1089  CG1 ILE A1132     -32.838  15.477 -21.058  1.00 11.22           C  
ATOM   1090  CG2 ILE A1132     -31.883  14.675 -23.246  1.00 10.12           C  
ATOM   1091  CD1 ILE A1132     -34.074  16.147 -21.654  1.00  9.02           C  
ATOM   1092  N   GLY A1133     -29.174  16.952 -20.439  1.00 12.79           N  
ATOM   1093  CA  GLY A1133     -28.735  17.928 -19.444  1.00 13.17           C  
ATOM   1094  C   GLY A1133     -27.516  17.555 -18.611  1.00 13.19           C  
ATOM   1095  O   GLY A1133     -26.908  18.420 -17.982  1.00 13.04           O  
ATOM   1096  N   THR A1134     -27.148  16.279 -18.589  1.00 13.50           N  
ATOM   1097  CA  THR A1134     -26.103  15.804 -17.669  1.00 13.06           C  
ATOM   1098  C   THR A1134     -24.700  15.829 -18.258  1.00 13.65           C  
ATOM   1099  O   THR A1134     -23.746  15.381 -17.612  1.00 14.26           O  
ATOM   1100  CB  THR A1134     -26.408  14.385 -17.164  1.00 12.72           C  
ATOM   1101  OG1 THR A1134     -26.401  13.460 -18.257  1.00 11.92           O  
ATOM   1102  CG2 THR A1134     -27.760  14.350 -16.473  1.00 11.72           C  
ATOM   1103  N   GLY A1135     -24.557  16.351 -19.470  1.00 14.20           N  
ATOM   1104  CA  GLY A1135     -23.239  16.473 -20.106  1.00 14.59           C  
ATOM   1105  C   GLY A1135     -22.811  17.921 -20.146  1.00 15.06           C  
ATOM   1106  O   GLY A1135     -22.470  18.488 -19.116  1.00 15.29           O  
ATOM   1107  N   ASN A1136     -22.853  18.531 -21.327  1.00 15.46           N  
ATOM   1108  CA  ASN A1136     -22.465  19.935 -21.479  1.00 15.82           C  
ATOM   1109  C   ASN A1136     -23.302  20.887 -20.642  1.00 15.92           C  
ATOM   1110  O   ASN A1136     -22.790  21.912 -20.216  1.00 16.71           O  
ATOM   1111  CB  ASN A1136     -22.514  20.389 -22.945  1.00 15.61           C  
ATOM   1112  CG  ASN A1136     -21.341  19.870 -23.771  1.00 15.01           C  
ATOM   1113  OD1 ASN A1136     -20.289  19.531 -23.234  1.00 15.02           O  
ATOM   1114  ND2 ASN A1136     -21.529  19.796 -25.075  1.00 12.41           N  
ATOM   1115  N   LEU A1137     -24.570  20.558 -20.394  1.00 15.49           N  
ATOM   1116  CA  LEU A1137     -25.437  21.457 -19.621  1.00 15.31           C  
ATOM   1117  C   LEU A1137     -25.202  21.397 -18.109  1.00 14.83           C  
ATOM   1118  O   LEU A1137     -25.710  22.235 -17.373  1.00 14.80           O  
ATOM   1119  CB  LEU A1137     -26.909  21.216 -19.958  1.00 15.14           C  
ATOM   1120  CG  LEU A1137     -27.270  21.656 -21.379  1.00 15.30           C  
ATOM   1121  CD1 LEU A1137     -28.692  21.232 -21.770  1.00 14.39           C  
ATOM   1122  CD2 LEU A1137     -27.078  23.160 -21.583  1.00 15.47           C  
ATOM   1123  N   GLY A1138     -24.433  20.419 -17.653  1.00 14.86           N  
ATOM   1124  CA  GLY A1138     -23.944  20.390 -16.270  1.00 14.97           C  
ATOM   1125  C   GLY A1138     -24.920  19.955 -15.173  1.00 14.75           C  
ATOM   1126  O   GLY A1138     -24.632  20.153 -13.995  1.00 14.42           O  
ATOM   1127  N   PHE A1139     -26.074  19.386 -15.521  1.00 14.50           N  
ATOM   1128  CA  PHE A1139     -26.959  18.812 -14.474  1.00 14.39           C  
ATOM   1129  C   PHE A1139     -26.211  17.671 -13.782  1.00 14.05           C  
ATOM   1130  O   PHE A1139     -25.736  16.765 -14.463  1.00 13.99           O  
ATOM   1131  CB  PHE A1139     -28.273  18.252 -15.042  1.00 14.22           C  
ATOM   1132  CG  PHE A1139     -29.345  19.273 -15.235  1.00 13.85           C  
ATOM   1133  CD1 PHE A1139     -30.503  19.223 -14.485  1.00 13.87           C  
ATOM   1134  CD2 PHE A1139     -29.204  20.280 -16.168  1.00 14.09           C  
ATOM   1135  CE1 PHE A1139     -31.497  20.154 -14.660  1.00 13.37           C  
ATOM   1136  CE2 PHE A1139     -30.195  21.228 -16.339  1.00 14.06           C  
ATOM   1137  CZ  PHE A1139     -31.346  21.164 -15.586  1.00 13.85           C  
ATOM   1138  N   PRO A1140     -26.086  17.720 -12.439  1.00 13.83           N  
ATOM   1139  CA  PRO A1140     -25.548  16.583 -11.710  1.00 13.92           C  
ATOM   1140  C   PRO A1140     -26.379  15.360 -11.955  1.00 13.63           C  
ATOM   1141  O   PRO A1140     -27.597  15.438 -11.973  1.00 13.12           O  
ATOM   1142  CB  PRO A1140     -25.676  17.009 -10.237  1.00 14.27           C  
ATOM   1143  CG  PRO A1140     -25.589  18.488 -10.282  1.00 13.67           C  
ATOM   1144  CD  PRO A1140     -26.372  18.843 -11.528  1.00 14.10           C  
ATOM   1145  N   LYS A1141     -25.716  14.228 -12.110  1.00 13.92           N  
ATOM   1146  CA  LYS A1141     -26.382  13.015 -12.546  1.00 14.11           C  
ATOM   1147  C   LYS A1141     -27.336  12.401 -11.508  1.00 14.54           C  
ATOM   1148  O   LYS A1141     -28.425  11.921 -11.868  1.00 14.25           O  
ATOM   1149  CB  LYS A1141     -25.336  12.030 -13.041  1.00 14.46           C  
ATOM   1150  CG  LYS A1141     -24.708  12.516 -14.333  1.00 14.07           C  
ATOM   1151  CD  LYS A1141     -23.470  11.750 -14.722  1.00 13.72           C  
ATOM   1152  CE  LYS A1141     -22.959  12.242 -16.081  1.00 13.59           C  
ATOM   1153  NZ  LYS A1141     -21.800  11.464 -16.602  1.00 13.18           N  
ATOM   1154  N   ASN A1142     -26.950  12.421 -10.235  1.00 14.65           N  
ATOM   1155  CA  ASN A1142     -27.861  11.976  -9.167  1.00 15.41           C  
ATOM   1156  C   ASN A1142     -29.127  12.851  -9.080  1.00 14.59           C  
ATOM   1157  O   ASN A1142     -30.222  12.359  -8.835  1.00 14.28           O  
ATOM   1158  CB  ASN A1142     -27.153  11.988  -7.810  1.00 15.97           C  
ATOM   1159  CG  ASN A1142     -26.650  13.368  -7.436  1.00 19.21           C  
ATOM   1160  OD1 ASN A1142     -26.136  14.099  -8.285  1.00 23.30           O  
ATOM   1161  ND2 ASN A1142     -26.813  13.744  -6.173  1.00 25.45           N  
ATOM   1162  N   ILE A1143     -28.966  14.151  -9.285  1.00 13.83           N  
ATOM   1163  CA  ILE A1143     -30.090  15.049  -9.195  1.00 13.62           C  
ATOM   1164  C   ILE A1143     -30.953  14.877 -10.440  1.00 12.97           C  
ATOM   1165  O   ILE A1143     -32.160  14.831 -10.340  1.00 12.96           O  
ATOM   1166  CB  ILE A1143     -29.637  16.493  -8.978  1.00 14.00           C  
ATOM   1167  CG1 ILE A1143     -28.964  16.606  -7.602  1.00 14.55           C  
ATOM   1168  CG2 ILE A1143     -30.809  17.450  -9.068  1.00 14.10           C  
ATOM   1169  CD1 ILE A1143     -28.351  17.950  -7.356  1.00 15.49           C  
ATOM   1170  N   PHE A1144     -30.339  14.718 -11.606  1.00 12.32           N  
ATOM   1171  CA  PHE A1144     -31.136  14.475 -12.804  1.00 11.54           C  
ATOM   1172  C   PHE A1144     -31.949  13.174 -12.720  1.00 10.85           C  
ATOM   1173  O   PHE A1144     -33.127  13.146 -13.095  1.00 10.90           O  
ATOM   1174  CB  PHE A1144     -30.310  14.485 -14.090  1.00 11.11           C  
ATOM   1175  CG  PHE A1144     -31.167  14.328 -15.309  1.00 10.23           C  
ATOM   1176  CD1 PHE A1144     -31.344  13.080 -15.896  1.00  8.01           C  
ATOM   1177  CD2 PHE A1144     -31.874  15.414 -15.808  1.00  9.11           C  
ATOM   1178  CE1 PHE A1144     -32.167  12.930 -16.990  1.00  9.32           C  
ATOM   1179  CE2 PHE A1144     -32.714  15.266 -16.901  1.00  9.17           C  
ATOM   1180  CZ  PHE A1144     -32.854  14.022 -17.497  1.00  8.75           C  
ATOM   1181  N   ALA A1145     -31.325  12.112 -12.230  1.00 10.05           N  
ATOM   1182  CA  ALA A1145     -32.005  10.817 -12.097  1.00  9.97           C  
ATOM   1183  C   ALA A1145     -33.293  10.922 -11.295  1.00  9.82           C  
ATOM   1184  O   ALA A1145     -34.343  10.465 -11.739  1.00  9.53           O  
ATOM   1185  CB  ALA A1145     -31.083   9.798 -11.477  1.00  9.56           C  
ATOM   1186  N   GLU A1146     -33.221  11.526 -10.110  1.00 10.06           N  
ATOM   1187  CA  GLU A1146     -34.417  11.644  -9.277  1.00 10.44           C  
ATOM   1188  C   GLU A1146     -35.438  12.627  -9.904  1.00 10.00           C  
ATOM   1189  O   GLU A1146     -36.644  12.391  -9.841  1.00  9.88           O  
ATOM   1190  CB  GLU A1146     -34.056  11.989  -7.812  1.00 10.52           C  
ATOM   1191  CG  GLU A1146     -33.549  13.410  -7.584  1.00 12.78           C  
ATOM   1192  CD  GLU A1146     -32.948  13.634  -6.190  1.00 13.18           C  
ATOM   1193  OE1 GLU A1146     -32.304  14.691  -5.994  1.00 12.39           O  
ATOM   1194  OE2 GLU A1146     -33.098  12.761  -5.309  1.00 11.38           O  
ATOM   1195  N   LEU A1147     -34.941  13.681 -10.557  1.00  9.86           N  
ATOM   1196  CA  LEU A1147     -35.798  14.657 -11.258  1.00 10.08           C  
ATOM   1197  C   LEU A1147     -36.675  13.994 -12.325  1.00  9.88           C  
ATOM   1198  O   LEU A1147     -37.885  14.170 -12.333  1.00 10.10           O  
ATOM   1199  CB  LEU A1147     -34.942  15.773 -11.891  1.00  9.73           C  
ATOM   1200  CG  LEU A1147     -35.619  16.951 -12.607  1.00  9.66           C  
ATOM   1201  CD1 LEU A1147     -34.611  18.115 -12.755  1.00 10.01           C  
ATOM   1202  CD2 LEU A1147     -36.201  16.570 -13.989  1.00  8.01           C  
ATOM   1203  N   ILE A1148     -36.070  13.218 -13.217  1.00  9.87           N  
ATOM   1204  CA  ILE A1148     -36.837  12.631 -14.324  1.00  9.54           C  
ATOM   1205  C   ILE A1148     -37.750  11.525 -13.817  1.00  9.02           C  
ATOM   1206  O   ILE A1148     -38.912  11.435 -14.226  1.00  9.00           O  
ATOM   1207  CB  ILE A1148     -35.938  12.147 -15.495  1.00  9.52           C  
ATOM   1208  CG1 ILE A1148     -36.792  11.737 -16.697  1.00  9.14           C  
ATOM   1209  CG2 ILE A1148     -34.995  11.002 -15.050  1.00  9.81           C  
ATOM   1210  CD1 ILE A1148     -35.983  11.625 -18.030  1.00  8.45           C  
ATOM   1211  N   ILE A1149     -37.248  10.701 -12.912  1.00  8.87           N  
ATOM   1212  CA  ILE A1149     -38.060   9.608 -12.399  1.00  9.06           C  
ATOM   1213  C   ILE A1149     -39.264  10.168 -11.643  1.00  9.41           C  
ATOM   1214  O   ILE A1149     -40.373   9.707 -11.848  1.00  8.90           O  
ATOM   1215  CB  ILE A1149     -37.248   8.619 -11.537  1.00  9.00           C  
ATOM   1216  CG1 ILE A1149     -36.181   7.928 -12.405  1.00  8.73           C  
ATOM   1217  CG2 ILE A1149     -38.171   7.574 -10.900  1.00  8.99           C  
ATOM   1218  CD1 ILE A1149     -35.084   7.215 -11.648  1.00  7.19           C  
ATOM   1219  N   SER A1150     -39.059  11.191 -10.814  1.00 10.42           N  
ATOM   1220  CA  SER A1150     -40.184  11.790 -10.088  1.00 11.26           C  
ATOM   1221  C   SER A1150     -41.202  12.401 -11.048  1.00 11.31           C  
ATOM   1222  O   SER A1150     -42.400  12.314 -10.802  1.00 11.17           O  
ATOM   1223  CB  SER A1150     -39.715  12.857  -9.096  1.00 11.67           C  
ATOM   1224  OG  SER A1150     -38.945  12.275  -8.061  1.00 12.91           O  
ATOM   1225  N   GLU A1151     -40.731  13.013 -12.141  1.00 11.70           N  
ATOM   1226  CA  GLU A1151     -41.642  13.600 -13.124  1.00 11.89           C  
ATOM   1227  C   GLU A1151     -42.469  12.526 -13.824  1.00 11.45           C  
ATOM   1228  O   GLU A1151     -43.651  12.730 -14.099  1.00 10.99           O  
ATOM   1229  CB  GLU A1151     -40.890  14.463 -14.153  1.00 12.30           C  
ATOM   1230  CG  GLU A1151     -41.787  15.079 -15.250  1.00 13.83           C  
ATOM   1231  CD  GLU A1151     -43.002  15.825 -14.676  1.00 16.31           C  
ATOM   1232  OE1 GLU A1151     -44.120  15.711 -15.227  1.00 19.33           O  
ATOM   1233  OE2 GLU A1151     -42.832  16.507 -13.654  1.00 17.59           O  
ATOM   1234  N   VAL A1152     -41.858  11.381 -14.113  1.00 11.85           N  
ATOM   1235  CA  VAL A1152     -42.582  10.298 -14.790  1.00 11.74           C  
ATOM   1236  C   VAL A1152     -43.697   9.779 -13.889  1.00 12.55           C  
ATOM   1237  O   VAL A1152     -44.828   9.571 -14.361  1.00 11.01           O  
ATOM   1238  CB  VAL A1152     -41.660   9.154 -15.234  1.00 11.90           C  
ATOM   1239  CG1 VAL A1152     -42.476   7.998 -15.770  1.00 10.33           C  
ATOM   1240  CG2 VAL A1152     -40.655   9.649 -16.298  1.00 10.60           C  
ATOM   1241  N   PHE A1153     -43.385   9.606 -12.598  1.00 13.61           N  
ATOM   1242  CA  PHE A1153     -44.397   9.224 -11.603  1.00 15.04           C  
ATOM   1243  C   PHE A1153     -45.501  10.264 -11.529  1.00 15.43           C  
ATOM   1244  O   PHE A1153     -46.673   9.927 -11.568  1.00 15.68           O  
ATOM   1245  CB  PHE A1153     -43.788   9.014 -10.206  1.00 15.24           C  
ATOM   1246  CG  PHE A1153     -43.244   7.614  -9.984  1.00 17.89           C  
ATOM   1247  CD1 PHE A1153     -44.096   6.576  -9.602  1.00 19.61           C  
ATOM   1248  CD2 PHE A1153     -41.892   7.335 -10.164  1.00 18.60           C  
ATOM   1249  CE1 PHE A1153     -43.602   5.278  -9.402  1.00 20.71           C  
ATOM   1250  CE2 PHE A1153     -41.391   6.049  -9.980  1.00 19.53           C  
ATOM   1251  CZ  PHE A1153     -42.242   5.018  -9.592  1.00 20.86           C  
ATOM   1252  N   LYS A1154     -45.114  11.531 -11.444  1.00 16.35           N  
ATOM   1253  CA  LYS A1154     -46.072  12.619 -11.323  1.00 16.97           C  
ATOM   1254  C   LYS A1154     -47.005  12.651 -12.534  1.00 16.93           C  
ATOM   1255  O   LYS A1154     -48.227  12.700 -12.390  1.00 17.16           O  
ATOM   1256  CB  LYS A1154     -45.329  13.946 -11.152  1.00 17.23           C  
ATOM   1257  CG  LYS A1154     -46.226  15.173 -10.999  1.00 19.45           C  
ATOM   1258  CD  LYS A1154     -45.404  16.418 -10.611  1.00 22.42           C  
ATOM   1259  CE  LYS A1154     -46.286  17.501  -9.977  1.00 25.40           C  
ATOM   1260  NZ  LYS A1154     -45.491  18.619  -9.349  1.00 27.73           N  
ATOM   1261  N   PHE A1155     -46.425  12.610 -13.725  1.00 16.99           N  
ATOM   1262  CA  PHE A1155     -47.201  12.607 -14.966  1.00 17.01           C  
ATOM   1263  C   PHE A1155     -48.189  11.454 -14.984  1.00 17.42           C  
ATOM   1264  O   PHE A1155     -49.331  11.609 -15.397  1.00 16.78           O  
ATOM   1265  CB  PHE A1155     -46.256  12.489 -16.161  1.00 16.86           C  
ATOM   1266  CG  PHE A1155     -46.944  12.446 -17.482  1.00 15.60           C  
ATOM   1267  CD1 PHE A1155     -47.371  13.618 -18.091  1.00 15.51           C  
ATOM   1268  CD2 PHE A1155     -47.146  11.243 -18.130  1.00 13.85           C  
ATOM   1269  CE1 PHE A1155     -48.014  13.590 -19.325  1.00 14.08           C  
ATOM   1270  CE2 PHE A1155     -47.786  11.200 -19.360  1.00 15.22           C  
ATOM   1271  CZ  PHE A1155     -48.220  12.376 -19.963  1.00 14.07           C  
ATOM   1272  N   SER A1156     -47.737  10.285 -14.555  1.00 18.48           N  
ATOM   1273  CA  SER A1156     -48.595   9.105 -14.565  1.00 19.37           C  
ATOM   1274  C   SER A1156     -49.751   9.260 -13.591  1.00 20.12           C  
ATOM   1275  O   SER A1156     -50.859   8.830 -13.888  1.00 20.23           O  
ATOM   1276  CB  SER A1156     -47.823   7.844 -14.210  1.00 19.29           C  
ATOM   1277  OG  SER A1156     -48.717   6.750 -14.118  1.00 19.23           O  
ATOM   1278  N   SER A1157     -49.488   9.875 -12.436  1.00 21.23           N  
ATOM   1279  CA  SER A1157     -50.513  10.026 -11.400  1.00 22.21           C  
ATOM   1280  C   SER A1157     -51.607  10.991 -11.848  1.00 22.98           C  
ATOM   1281  O   SER A1157     -52.764  10.807 -11.501  1.00 23.02           O  
ATOM   1282  CB  SER A1157     -49.903  10.482 -10.074  1.00 22.10           C  
ATOM   1283  OG  SER A1157     -49.619  11.875 -10.069  1.00 24.27           O  
ATOM   1284  N   LYS A1158     -51.236  11.998 -12.638  1.00 23.79           N  
ATOM   1285  CA  LYS A1158     -52.163  13.044 -13.057  1.00 24.57           C  
ATOM   1286  C   LYS A1158     -52.865  12.777 -14.381  1.00 24.99           C  
ATOM   1287  O   LYS A1158     -53.684  13.593 -14.812  1.00 25.40           O  
ATOM   1288  CB  LYS A1158     -51.426  14.375 -13.158  1.00 24.74           C  
ATOM   1289  CG  LYS A1158     -50.853  14.830 -11.828  1.00 26.14           C  
ATOM   1290  CD  LYS A1158     -50.341  16.271 -11.868  1.00 28.52           C  
ATOM   1291  CE  LYS A1158     -50.665  16.999 -10.552  1.00 30.07           C  
ATOM   1292  NZ  LYS A1158     -50.279  18.422 -10.587  1.00 30.61           N  
ATOM   1293  N   ASN A1159     -52.564  11.660 -15.034  1.00 25.08           N  
ATOM   1294  CA  ASN A1159     -53.091  11.414 -16.378  1.00 25.35           C  
ATOM   1295  C   ASN A1159     -53.560   9.988 -16.563  1.00 25.81           C  
ATOM   1296  O   ASN A1159     -52.922   9.051 -16.082  1.00 26.26           O  
ATOM   1297  CB  ASN A1159     -52.024  11.749 -17.434  1.00 25.34           C  
ATOM   1298  CG  ASN A1159     -51.680  13.234 -17.470  1.00 24.58           C  
ATOM   1299  OD1 ASN A1159     -52.400  14.021 -18.066  1.00 24.57           O  
ATOM   1300  ND2 ASN A1159     -50.583  13.617 -16.827  1.00 22.93           N  
ATOM   1301  N   GLN A1160     -54.691   9.834 -17.245  1.00 26.28           N  
ATOM   1302  CA  GLN A1160     -55.133   8.534 -17.739  1.00 26.90           C  
ATOM   1303  C   GLN A1160     -54.609   8.410 -19.159  1.00 26.02           C  
ATOM   1304  O   GLN A1160     -54.949   9.209 -20.019  1.00 26.41           O  
ATOM   1305  CB  GLN A1160     -56.661   8.425 -17.709  1.00 27.57           C  
ATOM   1306  CG  GLN A1160     -57.236   8.459 -16.287  1.00 31.04           C  
ATOM   1307  CD  GLN A1160     -58.750   8.510 -16.258  1.00 35.14           C  
ATOM   1308  OE1 GLN A1160     -59.341   9.392 -15.623  1.00 37.80           O  
ATOM   1309  NE2 GLN A1160     -59.393   7.564 -16.950  1.00 37.57           N  
ATOM   1310  N   LEU A1161     -53.776   7.410 -19.394  1.00 25.26           N  
ATOM   1311  CA  LEU A1161     -53.059   7.276 -20.644  1.00 24.51           C  
ATOM   1312  C   LEU A1161     -53.701   6.186 -21.479  1.00 24.15           C  
ATOM   1313  O   LEU A1161     -54.033   5.122 -20.972  1.00 24.40           O  
ATOM   1314  CB  LEU A1161     -51.587   6.962 -20.356  1.00 24.36           C  
ATOM   1315  CG  LEU A1161     -50.836   8.069 -19.599  1.00 23.55           C  
ATOM   1316  CD1 LEU A1161     -49.433   7.633 -19.197  1.00 21.12           C  
ATOM   1317  CD2 LEU A1161     -50.793   9.358 -20.439  1.00 23.19           C  
ATOM   1318  N   LYS A1162     -53.882   6.465 -22.764  1.00 23.85           N  
ATOM   1319  CA  LYS A1162     -54.516   5.531 -23.690  1.00 23.66           C  
ATOM   1320  C   LYS A1162     -53.494   4.688 -24.443  1.00 22.40           C  
ATOM   1321  O   LYS A1162     -53.762   3.525 -24.715  1.00 22.44           O  
ATOM   1322  CB  LYS A1162     -55.401   6.285 -24.684  1.00 24.25           C  
ATOM   1323  CG  LYS A1162     -56.370   7.292 -24.026  1.00 26.89           C  
ATOM   1324  CD  LYS A1162     -57.258   7.982 -25.084  1.00 30.31           C  
ATOM   1325  CE  LYS A1162     -58.352   8.853 -24.452  1.00 31.95           C  
ATOM   1326  NZ  LYS A1162     -59.676   8.661 -25.134  1.00 32.61           N  
ATOM   1327  N   THR A1163     -52.335   5.259 -24.788  1.00 20.90           N  
ATOM   1328  CA  THR A1163     -51.305   4.502 -25.514  1.00 19.82           C  
ATOM   1329  C   THR A1163     -49.903   4.496 -24.871  1.00 18.85           C  
ATOM   1330  O   THR A1163     -49.215   3.481 -24.948  1.00 19.20           O  
ATOM   1331  CB  THR A1163     -51.182   4.949 -26.992  1.00 19.75           C  
ATOM   1332  OG1 THR A1163     -50.780   6.318 -27.046  1.00 19.68           O  
ATOM   1333  CG2 THR A1163     -52.510   4.766 -27.747  1.00 20.32           C  
ATOM   1334  N   LEU A1164     -49.466   5.600 -24.269  1.00 17.70           N  
ATOM   1335  CA  LEU A1164     -48.123   5.654 -23.673  1.00 17.22           C  
ATOM   1336  C   LEU A1164     -48.025   4.659 -22.529  1.00 17.06           C  
ATOM   1337  O   LEU A1164     -48.715   4.806 -21.527  1.00 16.75           O  
ATOM   1338  CB  LEU A1164     -47.774   7.060 -23.167  1.00 16.65           C  
ATOM   1339  CG  LEU A1164     -46.419   7.241 -22.477  1.00 16.30           C  
ATOM   1340  CD1 LEU A1164     -45.278   6.833 -23.404  1.00 15.36           C  
ATOM   1341  CD2 LEU A1164     -46.232   8.688 -22.025  1.00 15.58           C  
ATOM   1342  N   GLN A1165     -47.155   3.666 -22.696  1.00 17.20           N  
ATOM   1343  CA  GLN A1165     -46.975   2.576 -21.737  1.00 17.66           C  
ATOM   1344  C   GLN A1165     -45.556   2.437 -21.182  1.00 16.81           C  
ATOM   1345  O   GLN A1165     -45.370   1.891 -20.087  1.00 16.17           O  
ATOM   1346  CB  GLN A1165     -47.352   1.253 -22.409  1.00 18.42           C  
ATOM   1347  CG  GLN A1165     -48.849   1.087 -22.626  1.00 21.03           C  
ATOM   1348  CD  GLN A1165     -49.225  -0.181 -23.401  1.00 24.67           C  
ATOM   1349  OE1 GLN A1165     -48.367  -0.873 -23.963  1.00 26.32           O  
ATOM   1350  NE2 GLN A1165     -50.525  -0.473 -23.443  1.00 25.79           N  
ATOM   1351  N   GLU A1166     -44.556   2.914 -21.924  1.00 16.05           N  
ATOM   1352  CA  GLU A1166     -43.161   2.693 -21.544  1.00 15.45           C  
ATOM   1353  C   GLU A1166     -42.310   3.932 -21.676  1.00 14.02           C  
ATOM   1354  O   GLU A1166     -42.320   4.578 -22.718  1.00 13.20           O  
ATOM   1355  CB  GLU A1166     -42.532   1.643 -22.448  1.00 15.70           C  
ATOM   1356  CG  GLU A1166     -43.172   0.301 -22.419  1.00 18.00           C  
ATOM   1357  CD  GLU A1166     -42.641  -0.580 -23.527  1.00 20.87           C  
ATOM   1358  OE1 GLU A1166     -41.418  -0.555 -23.784  1.00 21.89           O  
ATOM   1359  OE2 GLU A1166     -43.459  -1.275 -24.157  1.00 25.22           O  
ATOM   1360  N   VAL A1167     -41.544   4.220 -20.629  1.00 12.69           N  
ATOM   1361  CA  VAL A1167     -40.508   5.246 -20.650  1.00 11.85           C  
ATOM   1362  C   VAL A1167     -39.185   4.542 -20.414  1.00 11.58           C  
ATOM   1363  O   VAL A1167     -39.003   3.915 -19.368  1.00 11.71           O  
ATOM   1364  CB  VAL A1167     -40.720   6.292 -19.560  1.00 11.39           C  
ATOM   1365  CG1 VAL A1167     -39.656   7.396 -19.643  1.00 10.45           C  
ATOM   1366  CG2 VAL A1167     -42.120   6.869 -19.672  1.00 11.87           C  
ATOM   1367  N   HIS A1168     -38.282   4.608 -21.389  1.00 11.00           N  
ATOM   1368  CA  HIS A1168     -36.980   3.964 -21.275  1.00 11.16           C  
ATOM   1369  C   HIS A1168     -35.950   5.015 -20.944  1.00 11.73           C  
ATOM   1370  O   HIS A1168     -35.901   6.060 -21.600  1.00 11.98           O  
ATOM   1371  CB  HIS A1168     -36.557   3.328 -22.594  1.00 11.38           C  
ATOM   1372  CG  HIS A1168     -37.432   2.211 -23.059  1.00 11.40           C  
ATOM   1373  ND1 HIS A1168     -36.948   1.166 -23.814  1.00 13.11           N  
ATOM   1374  CD2 HIS A1168     -38.759   1.985 -22.909  1.00 13.06           C  
ATOM   1375  CE1 HIS A1168     -37.940   0.343 -24.108  1.00 13.24           C  
ATOM   1376  NE2 HIS A1168     -39.050   0.816 -23.571  1.00 12.59           N  
ATOM   1377  N   PHE A1169     -35.100   4.747 -19.957  1.00 12.14           N  
ATOM   1378  CA  PHE A1169     -33.978   5.634 -19.676  1.00 12.48           C  
ATOM   1379  C   PHE A1169     -32.739   5.015 -20.326  1.00 13.45           C  
ATOM   1380  O   PHE A1169     -32.274   3.958 -19.908  1.00 12.75           O  
ATOM   1381  CB  PHE A1169     -33.783   5.823 -18.165  1.00 12.51           C  
ATOM   1382  CG  PHE A1169     -34.999   6.353 -17.459  1.00 11.69           C  
ATOM   1383  CD1 PHE A1169     -35.570   7.554 -17.845  1.00 12.02           C  
ATOM   1384  CD2 PHE A1169     -35.557   5.674 -16.402  1.00 12.38           C  
ATOM   1385  CE1 PHE A1169     -36.699   8.060 -17.203  1.00 12.79           C  
ATOM   1386  CE2 PHE A1169     -36.684   6.188 -15.737  1.00 13.65           C  
ATOM   1387  CZ  PHE A1169     -37.254   7.382 -16.154  1.00 11.97           C  
ATOM   1388  N   LEU A1170     -32.220   5.681 -21.356  1.00 14.52           N  
ATOM   1389  CA  LEU A1170     -31.070   5.183 -22.109  1.00 14.89           C  
ATOM   1390  C   LEU A1170     -29.779   5.739 -21.567  1.00 15.07           C  
ATOM   1391  O   LEU A1170     -29.500   6.938 -21.674  1.00 15.14           O  
ATOM   1392  CB  LEU A1170     -31.185   5.533 -23.595  1.00 15.26           C  
ATOM   1393  CG  LEU A1170     -31.833   4.470 -24.476  1.00 16.58           C  
ATOM   1394  CD1 LEU A1170     -33.143   3.989 -23.859  1.00 18.34           C  
ATOM   1395  CD2 LEU A1170     -32.058   5.021 -25.892  1.00 17.46           C  
ATOM   1396  N   LEU A1171     -28.974   4.846 -21.013  1.00 15.39           N  
ATOM   1397  CA  LEU A1171     -27.707   5.202 -20.422  1.00 15.97           C  
ATOM   1398  C   LEU A1171     -26.556   4.649 -21.283  1.00 16.56           C  
ATOM   1399  O   LEU A1171     -26.535   3.468 -21.593  1.00 16.02           O  
ATOM   1400  CB  LEU A1171     -27.643   4.661 -18.990  1.00 15.81           C  
ATOM   1401  CG  LEU A1171     -28.883   5.022 -18.160  1.00 15.93           C  
ATOM   1402  CD1 LEU A1171     -28.919   4.253 -16.863  1.00 16.59           C  
ATOM   1403  CD2 LEU A1171     -28.930   6.515 -17.901  1.00 16.85           C  
ATOM   1404  N   HIS A1172     -25.620   5.510 -21.678  1.00 17.40           N  
ATOM   1405  CA  HIS A1172     -24.470   5.076 -22.482  1.00 19.01           C  
ATOM   1406  C   HIS A1172     -23.633   4.067 -21.666  1.00 19.07           C  
ATOM   1407  O   HIS A1172     -23.394   4.298 -20.487  1.00 18.95           O  
ATOM   1408  CB  HIS A1172     -23.611   6.284 -22.918  1.00 19.44           C  
ATOM   1409  CG  HIS A1172     -22.587   5.959 -23.969  1.00 22.65           C  
ATOM   1410  ND1 HIS A1172     -21.434   5.249 -23.697  1.00 26.37           N  
ATOM   1411  CD2 HIS A1172     -22.542   6.253 -25.289  1.00 24.46           C  
ATOM   1412  CE1 HIS A1172     -20.731   5.108 -24.807  1.00 27.61           C  
ATOM   1413  NE2 HIS A1172     -21.380   5.717 -25.787  1.00 27.32           N  
ATOM   1414  N   PRO A1173     -23.211   2.943 -22.284  1.00 19.58           N  
ATOM   1415  CA  PRO A1173     -22.479   1.888 -21.570  1.00 20.31           C  
ATOM   1416  C   PRO A1173     -21.282   2.344 -20.769  1.00 20.83           C  
ATOM   1417  O   PRO A1173     -21.005   1.758 -19.736  1.00 21.31           O  
ATOM   1418  CB  PRO A1173     -22.024   0.955 -22.696  1.00 20.30           C  
ATOM   1419  CG  PRO A1173     -23.126   1.057 -23.672  1.00 20.34           C  
ATOM   1420  CD  PRO A1173     -23.532   2.518 -23.658  1.00 19.61           C  
ATOM   1421  N   SER A1174     -20.580   3.375 -21.240  1.00 21.42           N  
ATOM   1422  CA  SER A1174     -19.420   3.899 -20.529  1.00 21.83           C  
ATOM   1423  C   SER A1174     -19.771   4.977 -19.506  1.00 21.75           C  
ATOM   1424  O   SER A1174     -18.902   5.424 -18.762  1.00 22.08           O  
ATOM   1425  CB  SER A1174     -18.401   4.452 -21.524  1.00 22.06           C  
ATOM   1426  OG  SER A1174     -18.961   5.519 -22.262  1.00 24.00           O  
ATOM   1427  N   ASP A1175     -21.029   5.404 -19.453  1.00 21.53           N  
ATOM   1428  CA  ASP A1175     -21.425   6.469 -18.531  1.00 21.52           C  
ATOM   1429  C   ASP A1175     -21.750   5.846 -17.171  1.00 21.59           C  
ATOM   1430  O   ASP A1175     -22.902   5.799 -16.750  1.00 21.41           O  
ATOM   1431  CB  ASP A1175     -22.608   7.269 -19.092  1.00 21.17           C  
ATOM   1432  CG  ASP A1175     -22.827   8.600 -18.377  1.00 21.25           C  
ATOM   1433  OD1 ASP A1175     -23.479   9.477 -18.985  1.00 22.01           O  
ATOM   1434  OD2 ASP A1175     -22.372   8.786 -17.221  1.00 20.34           O  
ATOM   1435  N   HIS A1176     -20.702   5.400 -16.483  1.00 21.91           N  
ATOM   1436  CA  HIS A1176     -20.832   4.693 -15.211  1.00 22.20           C  
ATOM   1437  C   HIS A1176     -21.507   5.555 -14.145  1.00 21.41           C  
ATOM   1438  O   HIS A1176     -22.271   5.046 -13.340  1.00 21.08           O  
ATOM   1439  CB  HIS A1176     -19.458   4.203 -14.713  1.00 22.65           C  
ATOM   1440  CG  HIS A1176     -18.775   3.243 -15.652  1.00 26.26           C  
ATOM   1441  ND1 HIS A1176     -19.411   2.137 -16.191  1.00 29.57           N  
ATOM   1442  CD2 HIS A1176     -17.508   3.222 -16.140  1.00 28.05           C  
ATOM   1443  CE1 HIS A1176     -18.565   1.482 -16.974  1.00 29.11           C  
ATOM   1444  NE2 HIS A1176     -17.404   2.119 -16.959  1.00 28.83           N  
ATOM   1445  N   GLU A1177     -21.229   6.856 -14.139  1.00 21.07           N  
ATOM   1446  CA  GLU A1177     -21.905   7.781 -13.201  1.00 20.93           C  
ATOM   1447  C   GLU A1177     -23.432   7.772 -13.340  1.00 19.32           C  
ATOM   1448  O   GLU A1177     -24.144   7.659 -12.344  1.00 19.23           O  
ATOM   1449  CB  GLU A1177     -21.407   9.219 -13.381  1.00 21.43           C  
ATOM   1450  CG  GLU A1177     -20.068   9.523 -12.714  1.00 25.34           C  
ATOM   1451  CD  GLU A1177     -19.308  10.708 -13.359  1.00 29.55           C  
ATOM   1452  OE1 GLU A1177     -19.836  11.385 -14.292  1.00 31.13           O  
ATOM   1453  OE2 GLU A1177     -18.164  10.956 -12.907  1.00 32.85           O  
ATOM   1454  N   ASN A1178     -23.929   7.926 -14.568  1.00 17.75           N  
ATOM   1455  CA  ASN A1178     -25.369   7.885 -14.796  1.00 16.54           C  
ATOM   1456  C   ASN A1178     -25.960   6.527 -14.477  1.00 15.76           C  
ATOM   1457  O   ASN A1178     -27.003   6.444 -13.846  1.00 14.85           O  
ATOM   1458  CB  ASN A1178     -25.741   8.302 -16.227  1.00 16.13           C  
ATOM   1459  CG  ASN A1178     -26.209   9.742 -16.308  1.00 15.63           C  
ATOM   1460  OD1 ASN A1178     -27.010  10.196 -15.483  1.00 13.25           O  
ATOM   1461  ND2 ASN A1178     -25.715  10.468 -17.301  1.00 14.92           N  
ATOM   1462  N   ILE A1179     -25.288   5.465 -14.901  1.00 15.61           N  
ATOM   1463  CA  ILE A1179     -25.758   4.108 -14.584  1.00 15.38           C  
ATOM   1464  C   ILE A1179     -25.956   3.946 -13.069  1.00 15.39           C  
ATOM   1465  O   ILE A1179     -26.985   3.434 -12.627  1.00 15.02           O  
ATOM   1466  CB  ILE A1179     -24.810   3.010 -15.134  1.00 15.12           C  
ATOM   1467  CG1 ILE A1179     -24.789   3.064 -16.670  1.00 14.61           C  
ATOM   1468  CG2 ILE A1179     -25.241   1.617 -14.629  1.00 14.14           C  
ATOM   1469  CD1 ILE A1179     -23.949   2.000 -17.343  1.00 12.70           C  
ATOM   1470  N   GLN A1180     -24.993   4.424 -12.284  1.00 15.81           N  
ATOM   1471  CA  GLN A1180     -25.084   4.346 -10.813  1.00 16.69           C  
ATOM   1472  C   GLN A1180     -26.251   5.172 -10.294  1.00 16.24           C  
ATOM   1473  O   GLN A1180     -27.067   4.681  -9.509  1.00 16.51           O  
ATOM   1474  CB  GLN A1180     -23.793   4.839 -10.137  1.00 17.04           C  
ATOM   1475  CG  GLN A1180     -23.734   4.585  -8.619  1.00 18.64           C  
ATOM   1476  CD  GLN A1180     -23.631   3.103  -8.313  1.00 21.53           C  
ATOM   1477  OE1 GLN A1180     -22.742   2.421  -8.829  1.00 21.67           O  
ATOM   1478  NE2 GLN A1180     -24.555   2.588  -7.499  1.00 21.15           N  
ATOM   1479  N   ALA A1181     -26.328   6.422 -10.740  1.00 15.92           N  
ATOM   1480  CA  ALA A1181     -27.372   7.344 -10.276  1.00 15.67           C  
ATOM   1481  C   ALA A1181     -28.756   6.764 -10.545  1.00 15.52           C  
ATOM   1482  O   ALA A1181     -29.632   6.749  -9.668  1.00 15.86           O  
ATOM   1483  CB  ALA A1181     -27.225   8.704 -10.957  1.00 15.28           C  
ATOM   1484  N   PHE A1182     -28.957   6.270 -11.755  1.00 15.05           N  
ATOM   1485  CA  PHE A1182     -30.273   5.783 -12.117  1.00 15.07           C  
ATOM   1486  C   PHE A1182     -30.586   4.497 -11.352  1.00 15.35           C  
ATOM   1487  O   PHE A1182     -31.712   4.309 -10.892  1.00 15.15           O  
ATOM   1488  CB  PHE A1182     -30.404   5.596 -13.632  1.00 14.98           C  
ATOM   1489  CG  PHE A1182     -30.849   6.844 -14.368  1.00 13.41           C  
ATOM   1490  CD1 PHE A1182     -32.171   7.013 -14.738  1.00 12.03           C  
ATOM   1491  CD2 PHE A1182     -29.943   7.835 -14.701  1.00 12.94           C  
ATOM   1492  CE1 PHE A1182     -32.577   8.142 -15.407  1.00 10.74           C  
ATOM   1493  CE2 PHE A1182     -30.352   8.970 -15.376  1.00 11.91           C  
ATOM   1494  CZ  PHE A1182     -31.668   9.121 -15.726  1.00 10.62           C  
ATOM   1495  N   SER A1183     -29.590   3.626 -11.210  1.00 15.63           N  
ATOM   1496  CA  SER A1183     -29.764   2.372 -10.469  1.00 15.93           C  
ATOM   1497  C   SER A1183     -30.110   2.654  -9.000  1.00 15.78           C  
ATOM   1498  O   SER A1183     -31.064   2.098  -8.463  1.00 15.72           O  
ATOM   1499  CB  SER A1183     -28.496   1.506 -10.577  1.00 16.27           C  
ATOM   1500  OG  SER A1183     -28.236   1.139 -11.929  1.00 16.47           O  
ATOM   1501  N   ASP A1184     -29.345   3.539  -8.372  1.00 15.68           N  
ATOM   1502  CA  ASP A1184     -29.598   3.934  -6.988  1.00 15.85           C  
ATOM   1503  C   ASP A1184     -31.029   4.442  -6.798  1.00 15.97           C  
ATOM   1504  O   ASP A1184     -31.670   4.148  -5.791  1.00 15.80           O  
ATOM   1505  CB  ASP A1184     -28.610   5.031  -6.553  1.00 15.77           C  
ATOM   1506  CG  ASP A1184     -27.193   4.505  -6.300  1.00 15.95           C  
ATOM   1507  OD1 ASP A1184     -26.956   3.290  -6.313  1.00 15.72           O  
ATOM   1508  OD2 ASP A1184     -26.295   5.328  -6.080  1.00 18.62           O  
ATOM   1509  N   GLU A1185     -31.535   5.212  -7.757  1.00 15.96           N  
ATOM   1510  CA  GLU A1185     -32.870   5.784  -7.615  1.00 15.92           C  
ATOM   1511  C   GLU A1185     -33.959   4.718  -7.807  1.00 15.81           C  
ATOM   1512  O   GLU A1185     -34.977   4.744  -7.110  1.00 15.38           O  
ATOM   1513  CB  GLU A1185     -33.054   6.955  -8.578  1.00 15.89           C  
ATOM   1514  CG  GLU A1185     -34.355   7.706  -8.410  1.00 17.07           C  
ATOM   1515  CD  GLU A1185     -34.476   8.421  -7.074  1.00 17.51           C  
ATOM   1516  OE1 GLU A1185     -33.453   8.722  -6.440  1.00 17.13           O  
ATOM   1517  OE2 GLU A1185     -35.616   8.677  -6.664  1.00 20.63           O  
ATOM   1518  N   PHE A1186     -33.758   3.789  -8.747  1.00 15.75           N  
ATOM   1519  CA  PHE A1186     -34.672   2.645  -8.888  1.00 16.38           C  
ATOM   1520  C   PHE A1186     -34.725   1.843  -7.591  1.00 17.09           C  
ATOM   1521  O   PHE A1186     -35.809   1.485  -7.142  1.00 17.37           O  
ATOM   1522  CB  PHE A1186     -34.279   1.705 -10.048  1.00 16.48           C  
ATOM   1523  CG  PHE A1186     -34.921   2.050 -11.360  1.00 16.22           C  
ATOM   1524  CD1 PHE A1186     -35.688   1.111 -12.041  1.00 15.86           C  
ATOM   1525  CD2 PHE A1186     -34.750   3.315 -11.930  1.00 15.25           C  
ATOM   1526  CE1 PHE A1186     -36.278   1.410 -13.258  1.00 14.90           C  
ATOM   1527  CE2 PHE A1186     -35.354   3.629 -13.144  1.00 15.57           C  
ATOM   1528  CZ  PHE A1186     -36.115   2.670 -13.813  1.00 14.73           C  
ATOM   1529  N   ALA A1187     -33.563   1.571  -6.995  1.00 18.14           N  
ATOM   1530  CA  ALA A1187     -33.496   0.849  -5.706  1.00 19.52           C  
ATOM   1531  C   ALA A1187     -34.358   1.534  -4.640  1.00 20.65           C  
ATOM   1532  O   ALA A1187     -35.166   0.889  -3.971  1.00 20.89           O  
ATOM   1533  CB  ALA A1187     -32.053   0.745  -5.228  1.00 19.02           C  
ATOM   1534  N   ARG A1188     -34.174   2.845  -4.495  1.00 22.12           N  
ATOM   1535  CA  ARG A1188     -34.961   3.647  -3.557  1.00 23.44           C  
ATOM   1536  C   ARG A1188     -36.464   3.557  -3.785  1.00 23.38           C  
ATOM   1537  O   ARG A1188     -37.218   3.369  -2.847  1.00 23.15           O  
ATOM   1538  CB  ARG A1188     -34.557   5.112  -3.635  1.00 24.03           C  
ATOM   1539  CG  ARG A1188     -33.276   5.430  -2.924  1.00 27.99           C  
ATOM   1540  CD  ARG A1188     -33.273   6.888  -2.447  1.00 33.33           C  
ATOM   1541  NE  ARG A1188     -31.980   7.260  -1.871  1.00 37.72           N  
ATOM   1542  CZ  ARG A1188     -30.886   7.564  -2.577  1.00 41.25           C  
ATOM   1543  NH1 ARG A1188     -30.891   7.545  -3.914  1.00 41.20           N  
ATOM   1544  NH2 ARG A1188     -29.770   7.892  -1.933  1.00 42.71           N  
ATOM   1545  N   ARG A1189     -36.892   3.725  -5.031  1.00 23.82           N  
ATOM   1546  CA  ARG A1189     -38.305   3.646  -5.373  1.00 24.02           C  
ATOM   1547  C   ARG A1189     -38.906   2.272  -5.073  1.00 24.71           C  
ATOM   1548  O   ARG A1189     -40.010   2.184  -4.547  1.00 24.92           O  
ATOM   1549  CB  ARG A1189     -38.508   3.986  -6.853  1.00 24.10           C  
ATOM   1550  CG  ARG A1189     -38.333   5.453  -7.179  1.00 24.07           C  
ATOM   1551  CD  ARG A1189     -39.518   6.249  -6.673  1.00 24.73           C  
ATOM   1552  NE  ARG A1189     -39.426   7.671  -6.981  1.00 25.07           N  
ATOM   1553  CZ  ARG A1189     -40.437   8.525  -6.859  1.00 24.58           C  
ATOM   1554  NH1 ARG A1189     -41.632   8.116  -6.442  1.00 24.48           N  
ATOM   1555  NH2 ARG A1189     -40.254   9.796  -7.165  1.00 26.32           N  
ATOM   1556  N   ALA A1190     -38.175   1.210  -5.408  1.00 25.09           N  
ATOM   1557  CA  ALA A1190     -38.643  -0.163  -5.215  1.00 25.68           C  
ATOM   1558  C   ALA A1190     -38.802  -0.552  -3.738  1.00 26.45           C  
ATOM   1559  O   ALA A1190     -39.652  -1.359  -3.399  1.00 26.54           O  
ATOM   1560  CB  ALA A1190     -37.684  -1.144  -5.906  1.00 25.20           C  
ATOM   1561  N   ASN A1191     -37.970   0.024  -2.874  1.00 27.63           N  
ATOM   1562  CA  ASN A1191     -37.916  -0.345  -1.454  1.00 28.47           C  
ATOM   1563  C   ASN A1191     -39.202  -0.034  -0.680  1.00 28.33           C  
ATOM   1564  O   ASN A1191     -39.895   0.931  -0.987  1.00 29.14           O  
ATOM   1565  CB  ASN A1191     -36.726   0.365  -0.802  1.00 28.77           C  
ATOM   1566  CG  ASN A1191     -36.491  -0.069   0.632  1.00 30.25           C  
ATOM   1567  OD1 ASN A1191     -36.480   0.760   1.538  1.00 32.77           O  
ATOM   1568  ND2 ASN A1191     -36.301  -1.364   0.844  1.00 30.54           N  
TER    1569      ASN A1191                                                      
HETATM 1570  N1  AR6 A 800     -26.141   7.481 -26.101  1.00 17.20           N  
HETATM 1571  C2  AR6 A 800     -26.672   7.710 -24.900  1.00 18.29           C  
HETATM 1572  N3  AR6 A 800     -26.209   8.654 -24.075  1.00 16.53           N  
HETATM 1573  C4  AR6 A 800     -25.156   9.403 -24.457  1.00 16.71           C  
HETATM 1574  C5  AR6 A 800     -24.576   9.187 -25.693  1.00 17.07           C  
HETATM 1575  C6  AR6 A 800     -25.091   8.207 -26.525  1.00 17.02           C  
HETATM 1576  N6  AR6 A 800     -24.525   8.009 -27.707  1.00 15.90           N  
HETATM 1577  N7  AR6 A 800     -23.571  10.048 -25.824  1.00 19.14           N  
HETATM 1578  C8  AR6 A 800     -23.505  10.784 -24.717  1.00 17.49           C  
HETATM 1579  N9  AR6 A 800     -24.468  10.382 -23.879  1.00 16.00           N  
HETATM 1580  PA  AR6 A 800     -24.615  16.148 -24.010  1.00 17.23           P  
HETATM 1581  PB  AR6 A 800     -26.494  17.973 -22.760  1.00 18.73           P  
HETATM 1582  C1' AR6 A 800     -24.770  10.958 -22.588  1.00 15.17           C  
HETATM 1583  O1A AR6 A 800     -24.530  15.670 -25.394  1.00 19.11           O  
HETATM 1584  O1B AR6 A 800     -27.987  17.913 -22.776  1.00 16.67           O  
HETATM 1585  C1D AR6 A 800     -26.079  22.247 -25.492  1.00 35.30           C  
HETATM 1586  O1D AR6 A 800     -26.945  22.973 -26.274  1.00 34.82           O  
HETATM 1587  C2' AR6 A 800     -23.644  11.720 -21.937  1.00 15.03           C  
HETATM 1588  O2' AR6 A 800     -22.966  10.841 -21.060  1.00 15.72           O  
HETATM 1589  O2A AR6 A 800     -23.530  17.007 -23.492  1.00 17.51           O  
HETATM 1590  O2B AR6 A 800     -25.760  17.820 -21.487  1.00 15.99           O  
HETATM 1591  C2D AR6 A 800     -24.713  22.069 -26.157  1.00 35.85           C  
HETATM 1592  O2D AR6 A 800     -24.606  22.935 -27.275  1.00 33.96           O  
HETATM 1593  C3' AR6 A 800     -24.418  12.760 -21.138  1.00 16.81           C  
HETATM 1594  O3' AR6 A 800     -24.726  12.214 -19.858  1.00 16.23           O  
HETATM 1595  O3A AR6 A 800     -26.041  16.845 -23.840  1.00 18.37           O  
HETATM 1596  C3D AR6 A 800     -24.736  20.648 -26.649  1.00 35.20           C  
HETATM 1597  O3D AR6 A 800     -25.279  20.644 -27.968  1.00 37.81           O  
HETATM 1598  C4' AR6 A 800     -25.733  12.942 -21.919  1.00 15.20           C  
HETATM 1599  O4' AR6 A 800     -25.630  12.037 -23.031  1.00 14.80           O  
HETATM 1600  C4D AR6 A 800     -25.787  20.003 -25.771  1.00 33.57           C  
HETATM 1601  O4D AR6 A 800     -26.755  21.003 -25.548  1.00 36.13           O  
HETATM 1602  C5' AR6 A 800     -25.882  14.394 -22.416  1.00 16.25           C  
HETATM 1603  O5' AR6 A 800     -24.681  14.843 -23.066  1.00 17.89           O  
HETATM 1604  C5D AR6 A 800     -25.233  19.519 -24.480  1.00 31.22           C  
HETATM 1605  O5D AR6 A 800     -26.244  19.366 -23.499  1.00 22.69           O  
HETATM 1606  O   HOH A   1     -49.665   6.356 -11.492  1.00 12.11           O  
HETATM 1607  O   HOH A   2     -49.303  16.405 -16.496  1.00 19.65           O  
HETATM 1608  O   HOH A   3     -46.670  16.257 -14.501  1.00 15.21           O  
HETATM 1609  O   HOH A   4     -25.582  -0.091 -27.618  1.00 34.46           O  
HETATM 1610  O   HOH A   5     -34.836   1.130 -26.306  1.00 24.23           O  
HETATM 1611  O   HOH A   6     -40.337  27.305 -25.891  1.00 14.33           O  
HETATM 1612  O   HOH A   7     -24.428  25.645 -27.833  1.00 21.77           O  
HETATM 1613  O   HOH A   8     -39.041  16.072 -10.784  1.00 12.80           O  
HETATM 1614  O   HOH A   9     -28.846  -0.252  -4.233  1.00 22.09           O  
HETATM 1615  O   HOH A  10     -27.188  -4.853 -14.549  1.00 15.75           O  
HETATM 1616  O   HOH A  11     -27.548  27.061 -27.198  1.00 26.23           O  
HETATM 1617  O   HOH A  12     -24.972  12.469 -40.290  1.00 15.86           O  
HETATM 1618  O   HOH A  13     -20.969  16.233 -22.921  1.00 19.30           O  
HETATM 1619  O   HOH A  14     -42.984  30.776 -32.662  1.00 20.72           O  
HETATM 1620  O   HOH A  15     -32.434  28.392 -16.388  1.00 31.30           O  
HETATM 1621  O   HOH A  16     -27.416  -1.033 -12.950  1.00 14.46           O  
HETATM 1622  O   HOH A  17     -30.089  28.176 -20.024  1.00 23.55           O  
HETATM 1623  O   HOH A  18     -24.383  25.364 -16.313  1.00 24.18           O  
HETATM 1624  O   HOH A  19     -39.943  23.737 -20.338  1.00 11.69           O  
HETATM 1625  O   HOH A  20     -30.795  31.667 -11.898  1.00 38.40           O  
HETATM 1626  O   HOH A  21     -34.505  -1.706  -3.135  1.00 15.55           O  
HETATM 1627  O   HOH A  22     -25.285  19.648 -30.864  1.00 15.79           O  
HETATM 1628  O   HOH A  23     -29.042  24.381 -37.407  1.00 14.88           O  
HETATM 1629  O   HOH A  24     -24.187  14.963 -40.730  1.00 16.21           O  
HETATM 1630  O   HOH A  25     -36.384  29.962 -36.009  1.00 24.09           O  
HETATM 1631  O   HOH A  26     -27.339  -0.945  -8.471  1.00 20.97           O  
HETATM 1632  O   HOH A  27     -25.871  16.671 -27.328  1.00 24.31           O  
HETATM 1633  O   HOH A  28     -20.413   9.746 -32.273  1.00 21.89           O  
HETATM 1634  O   HOH A  29     -23.238  16.270 -15.094  1.00 19.78           O  
HETATM 1635  O   HOH A  30     -53.628   7.328 -13.517  1.00 36.96           O  
HETATM 1636  O   HOH A  31     -23.633  25.508 -13.302  1.00 26.51           O  
HETATM 1637  O   HOH A  32     -30.248  21.637 -25.044  1.00 13.39           O  
HETATM 1638  O   HOH A  33     -40.139   8.361 -39.207  1.00 28.67           O  
HETATM 1639  O   HOH A  34     -37.577  -6.120 -11.122  1.00 24.81           O  
HETATM 1640  O   HOH A  35     -29.138   8.459  -7.585  1.00 16.18           O  
HETATM 1641  O   HOH A  36     -19.270   8.236 -15.930  1.00 23.29           O  
HETATM 1642  O   HOH A  37     -37.779   9.727  -7.791  1.00 22.62           O  
HETATM 1643  O   HOH A  38     -53.114   8.140 -26.966  1.00 27.35           O  
HETATM 1644  O   HOH A  39     -37.930  -5.514 -18.312  1.00 39.95           O  
HETATM 1645  O   HOH A  40     -41.345  14.154 -41.190  1.00 22.71           O  
HETATM 1646  O   HOH A  41     -20.814   8.886 -22.088  1.00 34.87           O  
HETATM 1647  O   HOH A  42     -22.837  14.215 -11.940  1.00 25.11           O  
HETATM 1648  O   HOH A  43     -32.796  26.417 -38.603  1.00 28.80           O  
HETATM 1649  O   HOH A  44     -20.338   6.088 -28.594  1.00 30.55           O  
HETATM 1650  O   HOH A  45     -37.264  31.866 -38.307  1.00 42.26           O  
HETATM 1651  O   HOH A  46     -46.879   2.424 -31.212  1.00 23.74           O  
HETATM 1652  O   HOH A  47     -32.579  30.159  -8.648  1.00 28.98           O  
HETATM 1653  O   HOH A  48     -30.341  -6.788   4.260  1.00 30.25           O  
HETATM 1654  O   HOH A  49     -43.037   0.685 -28.425  1.00 29.61           O  
HETATM 1655  O   HOH A  50     -32.796  28.838 -34.235  1.00 28.54           O  
HETATM 1656  O   HOH A  51     -33.939  30.674 -10.916  1.00 27.02           O  
HETATM 1657  O   HOH A  52     -37.009  14.319  -6.981  1.00 25.14           O  
HETATM 1658  O   HOH A  53     -20.446  12.055 -23.520  1.00 24.63           O  
HETATM 1659  O   HOH A  54     -21.359  17.629 -16.859  1.00 21.90           O  
HETATM 1660  O   HOH A  55     -23.649   8.414  -9.702  1.00 33.17           O  
HETATM 1661  O   HOH A  56     -30.135   8.805 -43.642  1.00 27.06           O  
HETATM 1662  O   HOH A  57     -48.411   9.166 -34.730  1.00 27.59           O  
HETATM 1663  O   HOH A  58     -43.047  -1.447  -9.852  1.00 32.99           O  
HETATM 1664  O   HOH A  59     -21.407   9.839 -27.427  1.00 24.63           O  
HETATM 1665  O   HOH A  60     -46.793  -0.424 -31.068  1.00 26.53           O  
HETATM 1666  O   HOH A  61     -38.707  29.988 -23.372  1.00 25.81           O  
HETATM 1667  O   HOH A  62     -21.606  13.320 -18.592  1.00 32.97           O  
HETATM 1668  O   HOH A  63     -34.965  31.298 -25.228  1.00 26.96           O  
HETATM 1669  O   HOH A  64     -52.699  10.575 -32.151  1.00 25.51           O  
HETATM 1670  O   HOH A  65     -18.578  17.022 -24.455  1.00 32.98           O  
HETATM 1671  O   HOH A  66     -30.219   3.814  -3.344  1.00 29.46           O  
HETATM 1672  O   HOH A  67     -24.698  22.196  -8.357  1.00 29.67           O  
HETATM 1673  O   HOH A  68     -41.033  17.125 -38.733  1.00 29.10           O  
HETATM 1674  O   HOH A  69     -31.741  -7.710  -0.810  1.00 33.73           O  
HETATM 1675  O   HOH A  70     -19.436  19.010 -26.892  1.00 26.62           O  
HETATM 1676  O   HOH A  71     -37.369   3.692  -0.286  1.00 28.47           O  
HETATM 1677  O   HOH A  72     -49.622   3.813 -19.278  1.00 32.52           O  
HETATM 1678  O   HOH A  73     -19.382   9.705 -17.876  1.00 32.93           O  
HETATM 1679  O   HOH A  74     -27.219  28.325 -30.046  1.00 26.52           O  
HETATM 1680  O   HOH A  75     -26.607  -2.466 -25.856  1.00 33.40           O  
HETATM 1681  O   HOH A  76     -41.920  16.525 -11.263  1.00 29.96           O  
HETATM 1682  O   HOH A  77     -42.191  14.700 -37.904  1.00 26.88           O  
HETATM 1683  O   HOH A  78     -41.976  -3.998 -21.543  1.00 39.46           O  
HETATM 1684  O   HOH A  79     -27.511  23.527 -39.704  1.00 21.17           O  
HETATM 1685  O   HOH A  80     -23.794   7.199 -33.740  1.00 31.83           O  
HETATM 1686  O   HOH A  81     -21.476   0.806 -14.951  1.00 37.19           O  
HETATM 1687  O   HOH A  82     -54.308   5.339 -15.077  1.00 32.28           O  
HETATM 1688  O   HOH A  83     -49.375  17.180 -27.097  1.00 30.99           O  
HETATM 1689  O   HOH A  84     -32.295  30.991 -23.896  1.00 34.42           O  
HETATM 1690  O   HOH A  85     -24.138  12.097  -9.539  1.00 34.07           O  
HETATM 1691  O   HOH A  86     -51.351  13.936 -24.675  1.00 30.41           O  
HETATM 1692  O   HOH A  87     -27.746   8.867 -21.627  1.00  9.45           O  
HETATM 1693  O   HOH A  88     -25.804   7.926 -20.264  1.00 11.84           O  
CONECT 1570 1571 1575                                                           
CONECT 1571 1570 1572                                                           
CONECT 1572 1571 1573                                                           
CONECT 1573 1572 1574 1579                                                      
CONECT 1574 1573 1575 1577                                                      
CONECT 1575 1570 1574 1576                                                      
CONECT 1576 1575                                                                
CONECT 1577 1574 1578                                                           
CONECT 1578 1577 1579                                                           
CONECT 1579 1573 1578 1582                                                      
CONECT 1580 1583 1589 1595 1603                                                 
CONECT 1581 1584 1590 1595 1605                                                 
CONECT 1582 1579 1587 1599                                                      
CONECT 1583 1580                                                                
CONECT 1584 1581                                                                
CONECT 1585 1586 1591 1601                                                      
CONECT 1586 1585                                                                
CONECT 1587 1582 1588 1593                                                      
CONECT 1588 1587                                                                
CONECT 1589 1580                                                                
CONECT 1590 1581                                                                
CONECT 1591 1585 1592 1596                                                      
CONECT 1592 1591                                                                
CONECT 1593 1587 1594 1598                                                      
CONECT 1594 1593                                                                
CONECT 1595 1580 1581                                                           
CONECT 1596 1591 1597 1600                                                      
CONECT 1597 1596                                                                
CONECT 1598 1593 1599 1602                                                      
CONECT 1599 1582 1598                                                           
CONECT 1600 1596 1601 1604                                                      
CONECT 1601 1585 1600                                                           
CONECT 1602 1598 1603                                                           
CONECT 1603 1580 1602                                                           
CONECT 1604 1600 1605                                                           
CONECT 1605 1581 1604                                                           
MASTER      294    0    1    6    9    0    7    6 1692    1   36   17          
END                                                                             


A second structure was input as follows:


HEADER    ADP-RIBOSE-BINDING-PROTEIN              20-MAY-17   5O2D              
TITLE     PARP14 MACRODOMAIN 2 WITH INHIBITOR                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 14;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PARP-14,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 8,     
COMPND   5 ARTD8,B AGGRESSIVE LYMPHOMA PROTEIN 2;                               
COMPND   6 EC: 2.4.2.30;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PARP14, BAL2, KIAA1268;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    PARP, ADP-RIBOSE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS            
KEYWDS   2 CONSORTIUM, SGC, ADP-RIBOSE-BINDING-PROTEIN                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.UTH,M.SCHULLER,C.SIEG,J.WANG,T.KROJER,S.KNAPP,K.RIEDELS,F.BRACHER,  
AUTHOR   2 A.M.EDWARDS,C.ARROWSMITH,C.BOUNTRA,J.M.ELKINS,STRUCTURAL GENOMICS    
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   4   19-SEP-18 5O2D    1       JRNL   REMARK                            
REVDAT   3   21-FEB-18 5O2D    1       AUTHOR                                   
REVDAT   2   29-NOV-17 5O2D    1       JRNL                                     
REVDAT   1   08-NOV-17 5O2D    0                                                
JRNL        AUTH   M.SCHULLER,K.RIEDEL,I.GIBBS-SEYMOUR,K.UTH,C.SIEG,            
JRNL        AUTH 2 A.P.GEHRING,I.AHEL,F.BRACHER,B.M.KESSLER,J.M.ELKINS,S.KNAPP  
JRNL        TITL   DISCOVERY OF A SELECTIVE ALLOSTERIC INHIBITOR TARGETING      
JRNL        TITL 2 MACRODOMAIN 2 OF POLYADENOSINE-DIPHOSPHATE-RIBOSE POLYMERASE 
JRNL        TITL 3 14.                                                          
JRNL        REF    ACS CHEM. BIOL.               V.  12  2866 2017              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   28991428                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.7B00445                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 21619                          
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) : 0.132                           
REMARK   3   R VALUE            (WORKING SET) : 0.130                           
REMARK   3   FREE R VALUE                     : 0.174                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1087                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1482                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 59                           
REMARK   3   BIN FREE R VALUE                    : 0.2060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1436                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.13000                                              
REMARK   3    B22 (A**2) : -0.60000                                             
REMARK   3    B33 (A**2) : 0.39000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.43000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.105         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.079         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.050         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.135         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1564 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1462 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2145 ; 1.480 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3403 ; 0.956 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   210 ; 5.477 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    62 ;32.727 ;24.839       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   268 ;11.765 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;23.880 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   252 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1898 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   310 ; 0.001 ; 0.020       
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):   789 ; 2.110 ; 1.567       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   788 ; 2.045 ; 1.563       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   995 ; 2.641 ; 2.362       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   996 ; 2.644 ; 2.364       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   775 ; 2.492 ; 1.837       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   776 ; 2.491 ; 1.837       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1144 ; 3.130 ; 2.640       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1713 ; 4.693 ;20.130       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1684 ; 4.253 ;19.720       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3026 ; 1.863 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    78 ;29.757 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3038 ; 9.723 ; 5.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5O2D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200005064.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CS-PAD XPP                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22712                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.650                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.2000                            
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) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.600                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M SODIUM PHOSPHATE MONOBASIC, 0.8M    
REMARK 280  POTASSIUM PHOSPHATE DIBASIC, 0.1M HEPES PH 7.5, VAPOR DIFFUSION,    
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       65.70400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       17.87000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       65.70400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       17.87000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 8960 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1344  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1421  LIES ON A SPECIAL POSITION.                          
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     SER A   992                                                      
REMARK 465     MET A   993                                                      
REMARK 465     ALA A   994                                                      
REMARK 465     ALA A   995                                                      
REMARK 465     ALA A   996                                                      
REMARK 465     GLY A   997                                                      
REMARK 465     PRO A   998                                                      
REMARK 465     GLY A   999                                                      
REMARK 465     LYS A  1000                                                      
REMARK 465     THR A  1001                                                      
REMARK 465     ASN A  1191                                                      
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     LYS A1106    CD   CE   NZ                                        
REMARK 470     LYS A1125    CE   NZ                                             
REMARK 470     SER A1158    OG                                                  
REMARK 470     GLN A1160    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1309     O    HOH A  1399              2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1305     O    HOH A  1314     4544     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A1020       51.11   -106.87                                   
REMARK 500    ALA A1026      129.61    -37.67                                   
REMARK 500    TRP A1082     -120.69     55.65                                   
REMARK 500    ASP A1085       41.81    -93.63                                   
REMARK 500    SER A1101      -70.56    -67.91                                   
REMARK 500    THR A1134       45.82    -97.50                                   
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 9HH A 1201                
DBREF  5O2D A  994  1191  UNP    Q460N5   PAR14_HUMAN    994   1191             
SEQADV 5O2D SER A  992  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 5O2D MET A  993  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 5O2D SER A 1048  UNP  Q460N5    LYS  1048 ENGINEERED MUTATION            
SEQADV 5O2D SER A 1154  UNP  Q460N5    LYS  1154 ENGINEERED MUTATION            
SEQADV 5O2D SER A 1158  UNP  Q460N5    LYS  1158 ENGINEERED MUTATION            
SEQADV 5O2D SER A 1162  UNP  Q460N5    LYS  1162 ENGINEERED MUTATION            
SEQRES   1 A  200  SER MET ALA ALA ALA GLY PRO GLY LYS THR SER TRP GLU          
SEQRES   2 A  200  LYS GLY SER LEU VAL SER PRO GLY GLY LEU GLN MET LEU          
SEQRES   3 A  200  LEU VAL LYS GLU GLY VAL GLN ASN ALA LYS THR ASP VAL          
SEQRES   4 A  200  VAL VAL ASN SER VAL PRO LEU ASP LEU VAL LEU SER ARG          
SEQRES   5 A  200  GLY PRO LEU SER SER SER LEU LEU GLU LYS ALA GLY PRO          
SEQRES   6 A  200  GLU LEU GLN GLU GLU LEU ASP THR VAL GLY GLN GLY VAL          
SEQRES   7 A  200  ALA VAL SER MET GLY THR VAL LEU LYS THR SER SER TRP          
SEQRES   8 A  200  ASN LEU ASP CYS ARG TYR VAL LEU HIS VAL VAL ALA PRO          
SEQRES   9 A  200  GLU TRP ARG ASN GLY SER THR SER SER LEU LYS ILE MET          
SEQRES  10 A  200  GLU ASP ILE ILE ARG GLU CYS MET GLU ILE THR GLU SER          
SEQRES  11 A  200  LEU SER LEU LYS SER ILE ALA PHE PRO ALA ILE GLY THR          
SEQRES  12 A  200  GLY ASN LEU GLY PHE PRO LYS ASN ILE PHE ALA GLU LEU          
SEQRES  13 A  200  ILE ILE SER GLU VAL PHE SER PHE SER SER SER ASN GLN          
SEQRES  14 A  200  LEU SER THR LEU GLN GLU VAL HIS PHE LEU LEU HIS PRO          
SEQRES  15 A  200  SER ASP HIS GLU ASN ILE GLN ALA PHE SER ASP GLU PHE          
SEQRES  16 A  200  ALA ARG ARG ALA ASN                                          
HET    9HH  A1201      24                                                       
HETNAM     9HH ~{N}-[2-(9~{H}-CARBAZOL-1-YL)PHENYL]METHANESULFONAMIDE           
FORMUL   2  9HH    C19 H16 N2 O2 S                                              
FORMUL   3  HOH   *130(H2 O)                                                    
HELIX    1 AA1 GLY A 1044  GLY A 1055  1                                  12    
HELIX    2 AA2 PRO A 1056  GLN A 1067  1                                  12    
HELIX    3 AA3 GLU A 1096  ASN A 1099  5                                   4    
HELIX    4 AA4 GLY A 1100  LEU A 1122  1                                  23    
HELIX    5 AA5 PRO A 1140  ASN A 1159  1                                  20    
HELIX    6 AA6 ASP A 1175  ALA A 1190  1                                  16    
SHEET    1 AA1 7 GLY A1006  VAL A1009  0                                        
SHEET    2 AA1 7 GLN A1015  VAL A1019 -1  O  MET A1016   N  LEU A1008           
SHEET    3 AA1 7 GLU A1166  LEU A1170  1  O  PHE A1169   N  LEU A1017           
SHEET    4 AA1 7 SER A1126  PRO A1130  1  N  PHE A1129   O  HIS A1168           
SHEET    5 AA1 7 VAL A1030  SER A1034  1  N  VAL A1032   O  ALA A1128           
SHEET    6 AA1 7 TYR A1088  VAL A1092  1  O  VAL A1092   N  ASN A1033           
SHEET    7 AA1 7 VAL A1076  SER A1080 -1  N  LEU A1077   O  HIS A1091           
SITE     1 AC1 12 VAL A1032  VAL A1092  PHE A1129  PRO A1130                    
SITE     2 AC1 12 ALA A1131  ILE A1132  GLY A1133  PHE A1144                    
SITE     3 AC1 12 LEU A1171  ASN A1178  PHE A1182  HOH A1315                    
CRYST1  131.408   35.740   37.150  90.00  94.83  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007610  0.000000  0.000643        0.00000                         
SCALE2      0.000000  0.027980  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027014        0.00000                         
ATOM      1  N   SER A1002      19.197 -26.351  -3.009  1.00 34.36           N  
ANISOU    1  N   SER A1002     4433   4106   4514    -60   -353     16       N  
ATOM      2  CA  SER A1002      19.704 -27.577  -3.720  1.00 34.35           C  
ANISOU    2  CA  SER A1002     4757   4301   3990    257   -561    -12       C  
ATOM      3  C   SER A1002      18.606 -28.622  -3.985  1.00 37.80           C  
ANISOU    3  C   SER A1002     5245   5044   4070   -437   -181   -157       C  
ATOM      4  O   SER A1002      18.581 -29.257  -5.050  1.00 41.34           O  
ANISOU    4  O   SER A1002     5165   5697   4844   -671   -292  -1097       O  
ATOM      5  CB  SER A1002      20.818 -28.244  -2.891  1.00 31.39           C  
ANISOU    5  CB  SER A1002     3654   4110   4162     52   -596   -679       C  
ATOM      6  OG  SER A1002      20.258 -28.744  -1.699  1.00 33.83           O  
ANISOU    6  OG  SER A1002     5734   4052   3067    346  -1681    386       O  
ATOM      7  N   TRP A1003      17.705 -28.784  -3.016  1.00 37.93           N  
ANISOU    7  N   TRP A1003     4670   4922   4820   -425    107   -544       N  
ATOM      8  CA  TRP A1003      16.775 -29.918  -2.975  1.00 34.84           C  
ANISOU    8  CA  TRP A1003     4529   4642   4066   -150   -235   -106       C  
ATOM      9  C   TRP A1003      15.629 -29.819  -3.994  1.00 36.08           C  
ANISOU    9  C   TRP A1003     5363   3767   4576   -698  -1089   -246       C  
ATOM     10  O   TRP A1003      15.056 -30.849  -4.391  1.00 38.41           O  
ANISOU   10  O   TRP A1003     6149   3620   4824   -823  -1147   -642       O  
ATOM     11  CB  TRP A1003      16.206 -30.036  -1.560  1.00 35.09           C  
ANISOU   11  CB  TRP A1003     5079   3975   4276   -414    -10    126       C  
ATOM     12  CG  TRP A1003      15.768 -31.397  -1.180  1.00 35.20           C  
ANISOU   12  CG  TRP A1003     4678   3974   4722   -352   -460    522       C  
ATOM     13  CD1 TRP A1003      14.541 -31.967  -1.410  1.00 38.91           C  
ANISOU   13  CD1 TRP A1003     3823   5074   5884     -4      1    707       C  
ATOM     14  CD2 TRP A1003      16.555 -32.384  -0.489  1.00 34.47           C  
ANISOU   14  CD2 TRP A1003     3792   4647   4654   -136   -937    158       C  
ATOM     15  NE1 TRP A1003      14.518 -33.255  -0.892  1.00 39.80           N  
ANISOU   15  NE1 TRP A1003     4199   4938   5985   -294   -416    511       N  
ATOM     16  CE2 TRP A1003      15.737 -33.530  -0.318  1.00 36.89           C  
ANISOU   16  CE2 TRP A1003     4363   4184   5469    124   -432    408       C  
ATOM     17  CE3 TRP A1003      17.867 -32.402   0.023  1.00 34.14           C  
ANISOU   17  CE3 TRP A1003     3566   4057   5348    191   -678     -1       C  
ATOM     18  CZ2 TRP A1003      16.198 -34.697   0.334  1.00 34.38           C  
ANISOU   18  CZ2 TRP A1003     3675   4440   4944     45   -651    335       C  
ATOM     19  CZ3 TRP A1003      18.327 -33.568   0.672  1.00 32.88           C  
ANISOU   19  CZ3 TRP A1003     4065   3694   4731    -27   -864   -149       C  
ATOM     20  CH2 TRP A1003      17.489 -34.693   0.818  1.00 32.16           C  
ANISOU   20  CH2 TRP A1003     3571   4014   4634     87   -605    354       C  
ATOM     21  N   GLU A1004      15.300 -28.584  -4.399  1.00 41.13           N  
ANISOU   21  N   GLU A1004     5832   4942   4853    541  -1476    448       N  
ATOM     22  CA  GLU A1004      14.265 -28.322  -5.413  1.00 36.49           C  
ANISOU   22  CA  GLU A1004     4412   5497   3953    363   -412    291       C  
ATOM     23  C   GLU A1004      14.821 -27.914  -6.792  1.00 39.81           C  
ANISOU   23  C   GLU A1004     4993   6323   3809   -463   -456    163       C  
ATOM     24  O   GLU A1004      15.930 -27.373  -6.913  1.00 38.43           O  
ANISOU   24  O   GLU A1004     5594   6103   2903   -762    -53    -79       O  
ATOM     25  CB  GLU A1004      13.346 -27.172  -4.977  1.00 38.28           C  
ANISOU   25  CB  GLU A1004     5051   5167   4324    121    229    166       C  
ATOM     26  CG  GLU A1004      12.739 -27.218  -3.576  1.00 36.72           C  
ANISOU   26  CG  GLU A1004     4896   4717   4337    217    351    489       C  
ATOM     27  CD  GLU A1004      11.686 -26.118  -3.402  1.00 38.19           C  
ANISOU   27  CD  GLU A1004     4694   5095   4719    239    897    748       C  
ATOM     28  OE1 GLU A1004      11.633 -25.174  -4.230  1.00 35.38           O  
ANISOU   28  OE1 GLU A1004     3131   4757   5552    684  -1092   1023       O  
ATOM     29  OE2 GLU A1004      10.896 -26.187  -2.436  1.00 45.20           O  
ANISOU   29  OE2 GLU A1004     4707   7878   4587   -800    978   -221       O  
ATOM     30  N   LYS A1005      14.012 -28.177  -7.818  1.00 33.25           N  
ANISOU   30  N   LYS A1005     3615   5486   3532   -291     47    760       N  
ATOM     31  CA  LYS A1005      14.143 -27.566  -9.133  1.00 30.56           C  
ANISOU   31  CA  LYS A1005     4202   3750   3659   -161     -7    524       C  
ATOM     32  C   LYS A1005      13.009 -26.536  -9.237  1.00 31.46           C  
ANISOU   32  C   LYS A1005     3831   4061   4062   -132   -169   1074       C  
ATOM     33  O   LYS A1005      11.928 -26.758  -8.675  1.00 36.57           O  
ANISOU   33  O   LYS A1005     4597   5764   3531   -272    340   1382       O  
ATOM     34  CB  LYS A1005      13.998 -28.628 -10.234  1.00 33.54           C  
ANISOU   34  CB  LYS A1005     4399   4436   3909    328    301    -95       C  
ATOM     35  CG  LYS A1005      15.022 -29.764 -10.168  1.00 32.29           C  
ANISOU   35  CG  LYS A1005     4248   4122   3896     82    360     47       C  
ATOM     36  CD  LYS A1005      14.661 -30.888 -11.132  1.00 32.87           C  
ANISOU   36  CD  LYS A1005     4305   4309   3872   -145    405     58       C  
ATOM     37  CE  LYS A1005      15.765 -31.926 -11.228  1.00 36.13           C  
ANISOU   37  CE  LYS A1005     4754   4488   4486     88     98   -201       C  
ATOM     38  NZ  LYS A1005      15.640 -32.737 -12.465  1.00 39.62           N  
ANISOU   38  NZ  LYS A1005     5091   5450   4513    -58   -448   -344       N  
ATOM     39  N   GLY A1006      13.267 -25.395  -9.899  1.00 25.08           N  
ANISOU   39  N   GLY A1006     3021   4020   2487     68    167    563       N  
ATOM     40  CA  GLY A1006      12.223 -24.334 -10.150  1.00 21.11           C  
ANISOU   40  CA  GLY A1006     1717   3928   2377   -471   -211    258       C  
ATOM     41  C   GLY A1006      11.433 -24.797 -11.335  1.00 17.66           C  
ANISOU   41  C   GLY A1006     1378   3655   1674    322    150    275       C  
ATOM     42  O   GLY A1006      11.993 -25.450 -12.196  1.00 21.31           O  
ANISOU   42  O   GLY A1006     1613   4902   1580    364    118   -192       O  
ATOM     43  N   SER A1007      10.131 -24.506 -11.379  1.00 14.73           N  
ANISOU   43  N   SER A1007     1278   2997   1321     23    -15     68       N  
ATOM     44  CA  SER A1007       9.282 -25.064 -12.442  1.00 13.26           C  
ANISOU   44  CA  SER A1007     1338   2326   1372     92     27    -15       C  
ATOM     45  C   SER A1007       8.378 -24.011 -13.047  1.00 13.88           C  
ANISOU   45  C   SER A1007     1388   2390   1494    110    -68    -37       C  
ATOM     46  O   SER A1007       7.778 -23.213 -12.322  1.00 16.34           O  
ANISOU   46  O   SER A1007     1598   2905   1704    365    -30   -198       O  
ATOM     47  CB  SER A1007       8.443 -26.234 -11.927  1.00 14.36           C  
ANISOU   47  CB  SER A1007     1606   2343   1504     35    -15     98       C  
ATOM     48  OG  SER A1007       7.548 -26.718 -12.927  1.00 18.02           O  
ANISOU   48  OG  SER A1007     1815   2987   2043   -376   -192     11       O  
ATOM     49  N   LEU A1008       8.283 -24.013 -14.375  1.00 12.82           N  
ANISOU   49  N   LEU A1008     1198   2191   1482    195    -66   -233       N  
ATOM     50  CA  LEU A1008       7.416 -23.071 -15.087  1.00 12.62           C  
ANISOU   50  CA  LEU A1008     1240   2061   1494    280    110   -277       C  
ATOM     51  C   LEU A1008       6.894 -23.787 -16.309  1.00 12.84           C  
ANISOU   51  C   LEU A1008     1238   2117   1522    243     81   -299       C  
ATOM     52  O   LEU A1008       7.682 -24.222 -17.142  1.00 12.92           O  
ANISOU   52  O   LEU A1008      974   2388   1547    387    -41   -121       O  
ATOM     53  CB  LEU A1008       8.211 -21.826 -15.516  1.00 13.99           C  
ANISOU   53  CB  LEU A1008     1561   2008   1744    217     81   -269       C  
ATOM     54  CG  LEU A1008       7.536 -20.807 -16.432  1.00 15.55           C  
ANISOU   54  CG  LEU A1008     1608   2212   2086    264    232    -24       C  
ATOM     55  CD1 LEU A1008       6.318 -20.199 -15.755  1.00 16.53           C  
ANISOU   55  CD1 LEU A1008     1573   2338   2368    245    283   -178       C  
ATOM     56  CD2 LEU A1008       8.530 -19.730 -16.828  1.00 18.06           C  
ANISOU   56  CD2 LEU A1008     2166   2066   2629    -83     26    -90       C  
ATOM     57  N   VAL A1009       5.569 -23.951 -16.397  1.00 13.56           N  
ANISOU   57  N   VAL A1009     1199   2940   1013    -50    838   -736       N  
ATOM     58  CA  VAL A1009       4.964 -24.552 -17.589  1.00  9.45           C  
ANISOU   58  CA  VAL A1009      841   1585   1161    575    489   -399       C  
ATOM     59  C   VAL A1009       4.433 -23.445 -18.510  1.00 11.52           C  
ANISOU   59  C   VAL A1009      915   2067   1394    198     85    -79       C  
ATOM     60  O   VAL A1009       3.793 -22.484 -18.060  1.00 13.40           O  
ANISOU   60  O   VAL A1009      930   2356   1802    236    132   -223       O  
ATOM     61  CB  VAL A1009       3.851 -25.550 -17.218  1.00 12.19           C  
ANISOU   61  CB  VAL A1009      651   1932   2049    577    592   -458       C  
ATOM     62  CG1 VAL A1009       3.384 -26.297 -18.463  1.00 13.87           C  
ANISOU   62  CG1 VAL A1009     1370   1830   2068    133     29   -165       C  
ATOM     63  CG2 VAL A1009       4.391 -26.562 -16.233  1.00 10.63           C  
ANISOU   63  CG2 VAL A1009      782   1756   1501    330    728   -415       C  
ATOM     64  N   SER A1010       4.744 -23.564 -19.796  1.00 12.76           N  
ANISOU   64  N   SER A1010     1227   2161   1459    218    212    -69       N  
ATOM     65  CA  SER A1010       4.282 -22.607 -20.768  1.00 13.34           C  
ANISOU   65  CA  SER A1010     1173   2119   1775    -45     77     94       C  
ATOM     66  C   SER A1010       2.774 -22.788 -21.031  1.00 13.65           C  
ANISOU   66  C   SER A1010     1020   2254   1909    101    310    154       C  
ATOM     67  O   SER A1010       2.243 -23.871 -20.826  1.00 13.19           O  
ANISOU   67  O   SER A1010     1084   2289   1639    -15     13    -61       O  
ATOM     68  CB  SER A1010       5.049 -22.789 -22.080  1.00 15.13           C  
ANISOU   68  CB  SER A1010     1668   2317   1762     62    206    112       C  
ATOM     69  OG  SER A1010       4.686 -23.974 -22.739  1.00 13.65           O  
ANISOU   69  OG  SER A1010     1295   2202   1687    154    194    229       O  
ATOM     70  N   PRO A1011       2.116 -21.752 -21.560  1.00 15.07           N  
ANISOU   70  N   PRO A1011     1111   2400   2212     33   -259    154       N  
ATOM     71  CA  PRO A1011       0.710 -21.916 -21.992  1.00 14.30           C  
ANISOU   71  CA  PRO A1011     1013   2629   1790    -81    -37    470       C  
ATOM     72  C   PRO A1011       0.466 -23.090 -22.930  1.00 15.62           C  
ANISOU   72  C   PRO A1011     1098   2836   2001    -40    -35    285       C  
ATOM     73  O   PRO A1011      -0.623 -23.717 -22.893  1.00 15.39           O  
ANISOU   73  O   PRO A1011      907   3207   1734     -5   -157    415       O  
ATOM     74  CB  PRO A1011       0.400 -20.590 -22.668  1.00 17.75           C  
ANISOU   74  CB  PRO A1011     1943   2744   2056    198   -163    506       C  
ATOM     75  CG  PRO A1011       1.261 -19.602 -21.981  1.00 17.54           C  
ANISOU   75  CG  PRO A1011     1945   2334   2383    348   -106    485       C  
ATOM     76  CD  PRO A1011       2.554 -20.350 -21.682  1.00 16.89           C  
ANISOU   76  CD  PRO A1011     1325   2532   2557    -23     71    417       C  
ATOM     77  N   GLY A1012       1.447 -23.394 -23.770  1.00 15.62           N  
ANISOU   77  N   GLY A1012     1006   2943   1983     67   -165    258       N  
ATOM     78  CA  GLY A1012       1.363 -24.522 -24.668  1.00 16.71           C  
ANISOU   78  CA  GLY A1012     1488   2999   1860     95     22    201       C  
ATOM     79  C   GLY A1012       1.678 -25.876 -24.054  1.00 17.61           C  
ANISOU   79  C   GLY A1012     1563   2997   2130     91   -154    140       C  
ATOM     80  O   GLY A1012       1.637 -26.877 -24.761  1.00 20.64           O  
ANISOU   80  O   GLY A1012     2165   3830   1848     85   -359   -315       O  
ATOM     81  N   GLY A1013       2.046 -25.913 -22.765  1.00 17.27           N  
ANISOU   81  N   GLY A1013     1396   3097   2068     39    -16   -198       N  
ATOM     82  CA  GLY A1013       2.176 -27.169 -22.023  1.00 17.89           C  
ANISOU   82  CA  GLY A1013     1656   2764   2375    -47      4   -310       C  
ATOM     83  C   GLY A1013       3.576 -27.742 -21.884  1.00 17.34           C  
ANISOU   83  C   GLY A1013     1725   2401   2461    -38     44   -323       C  
ATOM     84  O   GLY A1013       3.747 -28.869 -21.453  1.00 19.95           O  
ANISOU   84  O   GLY A1013     1830   2570   3180   -165    -99    159       O  
ATOM     85  N   LEU A1014       4.589 -26.971 -22.237  1.00 16.06           N  
ANISOU   85  N   LEU A1014     1694   2332   2076    130    117    -64       N  
ATOM     86  CA  LEU A1014       5.963 -27.467 -22.134  1.00 15.27           C  
ANISOU   86  CA  LEU A1014     1516   2238   2048   -117    -36   -141       C  
ATOM     87  C   LEU A1014       6.500 -27.043 -20.776  1.00 13.04           C  
ANISOU   87  C   LEU A1014     1017   1918   2019   -155     19    -84       C  
ATOM     88  O   LEU A1014       6.493 -25.864 -20.461  1.00 13.97           O  
ANISOU   88  O   LEU A1014     1089   1938   2278    461   -189    -69       O  
ATOM     89  CB  LEU A1014       6.786 -26.871 -23.277  1.00 19.53           C  
ANISOU   89  CB  LEU A1014     2240   2580   2598   -265    214    240       C  
ATOM     90  CG  LEU A1014       8.125 -27.421 -23.679  1.00 21.94           C  
ANISOU   90  CG  LEU A1014     2484   2934   2918    -60    373    104       C  
ATOM     91  CD1 LEU A1014       8.187 -28.935 -23.667  1.00 24.07           C  
ANISOU   91  CD1 LEU A1014     2965   2958   3221   -297    736      5       C  
ATOM     92  CD2 LEU A1014       8.467 -26.907 -25.077  1.00 17.61           C  
ANISOU   92  CD2 LEU A1014     2262   2062   2367   -137    320   -554       C  
ATOM     93  N   GLN A1015       6.982 -28.006 -19.988  1.00 12.70           N  
ANISOU   93  N   GLN A1015     1207   1826   1791   -189      8   -211       N  
ATOM     94  CA  GLN A1015       7.484 -27.744 -18.640  1.00 12.10           C  
ANISOU   94  CA  GLN A1015      991   1941   1664     30     88   -119       C  
ATOM     95  C   GLN A1015       8.945 -27.361 -18.680  1.00 12.67           C  
ANISOU   95  C   GLN A1015      979   2006   1829     86    117   -117       C  
ATOM     96  O   GLN A1015       9.734 -28.111 -19.223  1.00 15.93           O  
ANISOU   96  O   GLN A1015     1035   2264   2752     -2    580   -351       O  
ATOM     97  CB  GLN A1015       7.320 -28.968 -17.754  1.00 13.90           C  
ANISOU   97  CB  GLN A1015     1295   2180   1803    -86    169     59       C  
ATOM     98  CG  GLN A1015       7.815 -28.713 -16.320  1.00 15.84           C  
ANISOU   98  CG  GLN A1015     1778   2386   1854   -152     20    126       C  
ATOM     99  CD  GLN A1015       7.574 -29.844 -15.371  1.00 20.30           C  
ANISOU   99  CD  GLN A1015     2850   2522   2339   -507     52    301       C  
ATOM    100  OE1 GLN A1015       7.459 -30.984 -15.788  1.00 27.14           O  
ANISOU  100  OE1 GLN A1015     4036   2623   3653   -217     27     11       O  
ATOM    101  NE2 GLN A1015       7.519 -29.538 -14.069  1.00 21.53           N  
ANISOU  101  NE2 GLN A1015     2680   3246   2252   -265    156    394       N  
ATOM    102  N   MET A1016       9.290 -26.204 -18.123  1.00 11.61           N  
ANISOU  102  N   MET A1016      922   1954   1535    172    160    -46       N  
ATOM    103  CA  MET A1016      10.685 -25.788 -17.943  1.00 11.06           C  
ANISOU  103  CA  MET A1016     1067   1887   1249     87     41   -127       C  
ATOM    104  C   MET A1016      11.095 -26.002 -16.497  1.00 11.23           C  
ANISOU  104  C   MET A1016     1057   2010   1197    219    110    -86       C  
ATOM    105  O   MET A1016      10.361 -25.631 -15.563  1.00 11.49           O  
ANISOU  105  O   MET A1016      979   2364   1021    339     21     63       O  
ATOM    106  CB  MET A1016      10.879 -24.312 -18.297  1.00 12.84           C  
ANISOU  106  CB  MET A1016     1437   2050   1391   -184    285     75       C  
ATOM    107  CG  MET A1016      10.930 -24.055 -19.788  1.00 14.97           C  
ANISOU  107  CG  MET A1016     2014   2197   1477    -55     75    311       C  
ATOM    108  SD  MET A1016      10.493 -22.358 -20.200  1.00 16.70           S  
ANISOU  108  SD  MET A1016     2257   2307   1782    147   -194    231       S  
ATOM    109  CE  MET A1016       8.725 -22.613 -20.175  1.00 18.98           C  
ANISOU  109  CE  MET A1016     2199   2787   2226    298   -306    151       C  
ATOM    110  N   LEU A1017      12.294 -26.539 -16.314  1.00 11.07           N  
ANISOU  110  N   LEU A1017     1056   1961   1189    236    173   -215       N  
ATOM    111  CA  LEU A1017      12.861 -26.720 -14.981  1.00 11.95           C  
ANISOU  111  CA  LEU A1017     1126   2144   1269     12    131    -78       C  
ATOM    112  C   LEU A1017      14.176 -25.983 -14.864  1.00 11.82           C  
ANISOU  112  C   LEU A1017     1091   2128   1270     38    227    -20       C  
ATOM    113  O   LEU A1017      15.030 -26.083 -15.743  1.00 14.11           O  
ANISOU  113  O   LEU A1017     1088   2766   1506     43    354    -59       O  
ATOM    114  CB  LEU A1017      13.066 -28.180 -14.683  1.00 13.66           C  
ANISOU  114  CB  LEU A1017     1363   2216   1610    -41     77    290       C  
ATOM    115  CG  LEU A1017      11.857 -29.123 -14.707  1.00 17.61           C  
ANISOU  115  CG  LEU A1017     1782   2431   2478   -322    -79     36       C  
ATOM    116  CD1 LEU A1017      12.374 -30.522 -14.471  1.00 21.35           C  
ANISOU  116  CD1 LEU A1017     2425   2557   3129   -197    289    318       C  
ATOM    117  CD2 LEU A1017      10.891 -28.753 -13.597  1.00 18.83           C  
ANISOU  117  CD2 LEU A1017     1781   2746   2625   -194      4    167       C  
ATOM    118  N   LEU A1018      14.334 -25.263 -13.767  1.00 12.84           N  
ANISOU  118  N   LEU A1018     1267   2440   1169     -4     88     32       N  
ATOM    119  CA  LEU A1018      15.564 -24.602 -13.441  1.00 12.88           C  
ANISOU  119  CA  LEU A1018     1454   2182   1256    -67    -65    180       C  
ATOM    120  C   LEU A1018      16.314 -25.540 -12.502  1.00 11.24           C  
ANISOU  120  C   LEU A1018     1093   2063   1113   -245    -50    136       C  
ATOM    121  O   LEU A1018      15.929 -25.730 -11.352  1.00 13.95           O  
ANISOU  121  O   LEU A1018     1569   2393   1337   -100    305    403       O  
ATOM    122  CB  LEU A1018      15.251 -23.260 -12.786  1.00 15.41           C  
ANISOU  122  CB  LEU A1018     2051   2361   1442    122     89     48       C  
ATOM    123  CG  LEU A1018      16.408 -22.347 -12.451  1.00 19.57           C  
ANISOU  123  CG  LEU A1018     2680   2577   2177   -208    157   -103       C  
ATOM    124  CD1 LEU A1018      17.310 -22.146 -13.653  1.00 20.40           C  
ANISOU  124  CD1 LEU A1018     2507   2729   2512    -24    231    145       C  
ATOM    125  CD2 LEU A1018      15.818 -21.031 -11.950  1.00 21.91           C  
ANISOU  125  CD2 LEU A1018     3229   2514   2581     89     81    124       C  
ATOM    126  N   VAL A1019      17.362 -26.164 -13.013  1.00 11.24           N  
ANISOU  126  N   VAL A1019     1154   1980   1137    -88   -199    242       N  
ATOM    127  CA  VAL A1019      18.070 -27.211 -12.288  1.00 11.66           C  
ANISOU  127  CA  VAL A1019     1163   1820   1447   -143   -247    304       C  
ATOM    128  C   VAL A1019      19.431 -26.669 -11.907  1.00 12.89           C  
ANISOU  128  C   VAL A1019     1332   2136   1429   -367   -291    391       C  
ATOM    129  O   VAL A1019      20.205 -26.287 -12.769  1.00 15.79           O  
ANISOU  129  O   VAL A1019     1349   3301   1349   -533   -322    508       O  
ATOM    130  CB  VAL A1019      18.221 -28.491 -13.148  1.00 13.26           C  
ANISOU  130  CB  VAL A1019     1354   2028   1654   -140   -128    116       C  
ATOM    131  CG1 VAL A1019      18.821 -29.617 -12.326  1.00 17.00           C  
ANISOU  131  CG1 VAL A1019     2242   1857   2358     74   -194    179       C  
ATOM    132  CG2 VAL A1019      16.881 -28.936 -13.722  1.00 13.79           C  
ANISOU  132  CG2 VAL A1019     1628   1830   1781   -257   -328    151       C  
ATOM    133  N   LYS A1020      19.729 -26.669 -10.616  1.00 13.93           N  
ANISOU  133  N   LYS A1020     1537   2378   1378   -308   -304    218       N  
ATOM    134  CA  LYS A1020      20.944 -26.011 -10.086  1.00 15.26           C  
ANISOU  134  CA  LYS A1020     1776   2449   1572   -385   -287    -68       C  
ATOM    135  C   LYS A1020      21.999 -27.020  -9.663  1.00 18.56           C  
ANISOU  135  C   LYS A1020     2329   2651   2068    -31   -337    147       C  
ATOM    136  O   LYS A1020      22.532 -26.947  -8.551  1.00 21.97           O  
ANISOU  136  O   LYS A1020     2707   3490   2149    440   -494     61       O  
ATOM    137  CB  LYS A1020      20.552 -25.144  -8.895  1.00 18.26           C  
ANISOU  137  CB  LYS A1020     2161   2740   2035   -375   -144   -487       C  
ATOM    138  CG  LYS A1020      19.574 -24.042  -9.213  1.00 23.57           C  
ANISOU  138  CG  LYS A1020     2951   2906   3097    -57    -77   -488       C  
ATOM    139  CD  LYS A1020      19.225 -23.344  -7.897  1.00 28.56           C  
ANISOU  139  CD  LYS A1020     4020   3453   3375    249    380   -617       C  
ATOM    140  CE  LYS A1020      18.265 -22.193  -8.076  1.00 36.94           C  
ANISOU  140  CE  LYS A1020     4691   4312   5032    801    521     -9       C  
ATOM    141  NZ  LYS A1020      18.107 -21.469  -6.783  1.00 40.67           N  
ANISOU  141  NZ  LYS A1020     5424   5173   4854    -71    610   -148       N  
ATOM    142  N   GLU A1021      22.325 -27.953 -10.546  1.00 18.79           N  
ANISOU  142  N   GLU A1021     2776   2405   1956   -100   -761    166       N  
ATOM    143  CA  GLU A1021      23.162 -29.109 -10.169  1.00 23.82           C  
ANISOU  143  CA  GLU A1021     3158   2407   3483    217   -734   -130       C  
ATOM    144  C   GLU A1021      24.430 -29.224 -10.963  1.00 25.73           C  
ANISOU  144  C   GLU A1021     3305   2793   3677     88   -614    286       C  
ATOM    145  O   GLU A1021      25.118 -30.244 -10.868  1.00 33.52           O  
ANISOU  145  O   GLU A1021     3922   4130   4681   1231  -1110    816       O  
ATOM    146  CB  GLU A1021      22.387 -30.418 -10.364  1.00 27.00           C  
ANISOU  146  CB  GLU A1021     3211   2936   4109   -351   -869    378       C  
ATOM    147  CG  GLU A1021      21.139 -30.519  -9.524  1.00 32.51           C  
ANISOU  147  CG  GLU A1021     4196   3811   4346   -786   -288    789       C  
ATOM    148  CD  GLU A1021      20.434 -31.858  -9.685  1.00 40.14           C  
ANISOU  148  CD  GLU A1021     6336   3515   5398  -1222    554    768       C  
ATOM    149  OE1 GLU A1021      20.767 -32.614 -10.631  1.00 49.76           O  
ANISOU  149  OE1 GLU A1021     8875   3764   6265   -541   1555    536       O  
ATOM    150  OE2 GLU A1021      19.540 -32.147  -8.867  1.00 53.30           O  
ANISOU  150  OE2 GLU A1021     7694   7033   5524  -1797   1315   1286       O  
ATOM    151  N   GLY A1022      24.752 -28.215 -11.764  1.00 23.46           N  
ANISOU  151  N   GLY A1022     3101   2515   3297   -117  -1027    143       N  
ATOM    152  CA  GLY A1022      25.865 -28.321 -12.667  1.00 26.23           C  
ANISOU  152  CA  GLY A1022     3624   3138   3202   -294   -735   -157       C  
ATOM    153  C   GLY A1022      25.414 -29.034 -13.909  1.00 27.70           C  
ANISOU  153  C   GLY A1022     2958   4401   3163  -1004   -827     25       C  
ATOM    154  O   GLY A1022      24.288 -29.527 -14.006  1.00 37.39           O  
ANISOU  154  O   GLY A1022     4314   6770   3121  -3141   -681     70       O  
ATOM    155  N  AVAL A1023      26.292 -29.097 -14.889  0.50 30.40           N  
ANISOU  155  N  AVAL A1023     3499   4544   3507   -374   -467   -186       N  
ATOM    156  N  BVAL A1023      26.314 -29.105 -14.870  0.50 30.44           N  
ANISOU  156  N  BVAL A1023     3512   4537   3515   -405   -465   -159       N  
ATOM    157  CA AVAL A1023      25.917 -29.650 -16.177  0.50 35.01           C  
ANISOU  157  CA AVAL A1023     4135   5418   3749   -694   -729   -458       C  
ATOM    158  CA BVAL A1023      25.998 -29.604 -16.198  0.50 35.04           C  
ANISOU  158  CA BVAL A1023     4124   5421   3767   -710   -776   -436       C  
ATOM    159  C  AVAL A1023      26.209 -31.135 -16.363  0.50 34.99           C  
ANISOU  159  C  AVAL A1023     3770   5599   3923   -815   -328  -1090       C  
ATOM    160  C  BVAL A1023      26.254 -31.104 -16.386  0.50 34.94           C  
ANISOU  160  C  BVAL A1023     3764   5597   3912   -834   -366  -1082       C  
ATOM    161  O  AVAL A1023      25.703 -31.755 -17.303  0.50 41.19           O  
ANISOU  161  O  AVAL A1023     3818   8589   3241  -1760    229  -1563       O  
ATOM    162  O  BVAL A1023      25.764 -31.702 -17.347  0.50 40.90           O  
ANISOU  162  O  BVAL A1023     3538   8652   3350  -1777    183  -1549       O  
ATOM    163  CB AVAL A1023      26.596 -28.878 -17.290  0.50 39.67           C  
ANISOU  163  CB AVAL A1023     4994   5709   4367   -395   -445    192       C  
ATOM    164  CB BVAL A1023      26.800 -28.792 -17.212  0.50 39.84           C  
ANISOU  164  CB BVAL A1023     4839   5657   4638   -418   -484    359       C  
ATOM    165  CG1AVAL A1023      26.148 -29.481 -18.609  0.50 38.70           C  
ANISOU  165  CG1AVAL A1023     5188   5230   4285    102     20   -245       C  
ATOM    166  CG1BVAL A1023      26.429 -27.321 -17.048  0.50 41.83           C  
ANISOU  166  CG1BVAL A1023     5332   5845   4716   -283   -468    169       C  
ATOM    167  CG2AVAL A1023      26.244 -27.399 -17.131  0.50 40.66           C  
ANISOU  167  CG2AVAL A1023     5075   5883   4490   -320   -570     10       C  
ATOM    168  CG2BVAL A1023      28.292 -29.007 -16.995  0.50 39.29           C  
ANISOU  168  CG2BVAL A1023     4749   5487   4690   -302   -272    191       C  
ATOM    169  N   GLN A1024      26.995 -31.712 -15.466  1.00 36.39           N  
ANISOU  169  N   GLN A1024     4543   4852   4432   -271   -401  -1083       N  
ATOM    170  CA  GLN A1024      27.420 -33.105 -15.600  1.00 38.35           C  
ANISOU  170  CA  GLN A1024     4875   4707   4986   -333    282  -1266       C  
ATOM    171  C   GLN A1024      26.367 -34.114 -15.168  1.00 42.22           C  
ANISOU  171  C   GLN A1024     4790   4558   6692   -158   1137  -1789       C  
ATOM    172  O   GLN A1024      26.459 -35.293 -15.542  1.00 40.07           O  
ANISOU  172  O   GLN A1024     3668   4665   6889   -982   1263  -2559       O  
ATOM    173  CB  GLN A1024      28.684 -33.320 -14.791  1.00 32.59           C  
ANISOU  173  CB  GLN A1024     4304   3851   4226    173    736  -1609       C  
ATOM    174  CG  GLN A1024      29.834 -32.470 -15.291  1.00 33.24           C  
ANISOU  174  CG  GLN A1024     4752   3633   4242   -249    129  -1131       C  
ATOM    175  CD  GLN A1024      31.057 -32.561 -14.414  1.00 43.11           C  
ANISOU  175  CD  GLN A1024     5746   5776   4856     31   -657   -424       C  
ATOM    176  OE1 GLN A1024      30.939 -32.695 -13.190  1.00 46.49           O  
ANISOU  176  OE1 GLN A1024     3723   8665   5273    146    788   -458       O  
ATOM    177  NE2 GLN A1024      32.255 -32.483 -15.032  1.00 30.64           N  
ANISOU  177  NE2 GLN A1024     5907   3067   2667    771  -1285    169       N  
ATOM    178  N   ASN A1025      25.395 -33.649 -14.378  1.00 45.36           N  
ANISOU  178  N   ASN A1025     5375   5611   6246    522   1452  -1164       N  
ATOM    179  CA  ASN A1025      24.348 -34.487 -13.795  1.00 43.44           C  
ANISOU  179  CA  ASN A1025     5096   5728   5678    476    344   -432       C  
ATOM    180  C   ASN A1025      23.065 -34.555 -14.633  1.00 43.05           C  
ANISOU  180  C   ASN A1025     5268   6278   4811    466    508   -178       C  
ATOM    181  O   ASN A1025      22.130 -35.238 -14.238  1.00 42.69           O  
ANISOU  181  O   ASN A1025     3995   7290   4933   1427    664    433       O  
ATOM    182  CB  ASN A1025      24.025 -33.985 -12.375  1.00 38.42           C  
ANISOU  182  CB  ASN A1025     4669   4714   5215    195   -262    160       C  
ATOM    183  CG  ASN A1025      25.232 -34.064 -11.439  1.00 40.96           C  
ANISOU  183  CG  ASN A1025     5180   4125   6255     74   -898    234       C  
ATOM    184  OD1 ASN A1025      25.648 -35.149 -11.036  1.00 47.10           O  
ANISOU  184  OD1 ASN A1025     6065   4777   7053    705   -146   1115       O  
ATOM    185  ND2 ASN A1025      25.801 -32.912 -11.101  1.00 51.80           N  
ANISOU  185  ND2 ASN A1025     6443   4861   8377   -416   -975   -870       N  
ATOM    186  N   ALA A1026      23.028 -33.873 -15.785  1.00 42.37           N  
ANISOU  186  N   ALA A1026     5330   4911   5855    782    -45    131       N  
ATOM    187  CA  ALA A1026      21.898 -33.942 -16.731  1.00 36.93           C  
ANISOU  187  CA  ALA A1026     5879   4187   3962    349    412     13       C  
ATOM    188  C   ALA A1026      21.317 -35.346 -16.819  1.00 28.61           C  
ANISOU  188  C   ALA A1026     4129   3963   2778    448    290   1348       C  
ATOM    189  O   ALA A1026      22.066 -36.293 -17.010  1.00 35.73           O  
ANISOU  189  O   ALA A1026     5366   3485   4722    286   1292    984       O  
ATOM    190  CB  ALA A1026      22.339 -33.492 -18.123  1.00 38.72           C  
ANISOU  190  CB  ALA A1026     7236   3133   4341    352    119    833       C  
ATOM    191  N   LYS A1027      19.999 -35.466 -16.681  1.00 29.83           N  
ANISOU  191  N   LYS A1027     4074   4132   3126    554    866    543       N  
ATOM    192  CA  LYS A1027      19.273 -36.741 -16.766  1.00 26.39           C  
ANISOU  192  CA  LYS A1027     3480   3436   3108    792    233    763       C  
ATOM    193  C   LYS A1027      18.089 -36.662 -17.743  1.00 24.62           C  
ANISOU  193  C   LYS A1027     2956   3307   3090   -401    587   1319       C  
ATOM    194  O   LYS A1027      17.047 -37.239 -17.527  1.00 36.42           O  
ANISOU  194  O   LYS A1027     3106   5306   5423  -1325     70   1235       O  
ATOM    195  CB  LYS A1027      18.781 -37.171 -15.382  1.00 30.02           C  
ANISOU  195  CB  LYS A1027     4136   3976   3291    502    589    474       C  
ATOM    196  CG  LYS A1027      19.910 -37.510 -14.425  1.00 33.83           C  
ANISOU  196  CG  LYS A1027     4263   4643   3948    106      0    -48       C  
ATOM    197  CD  LYS A1027      19.642 -38.771 -13.592  1.00 36.82           C  
ANISOU  197  CD  LYS A1027     4552   4508   4927    194     54    110       C  
ATOM    198  CE  LYS A1027      20.881 -39.249 -12.825  1.00 37.02           C  
ANISOU  198  CE  LYS A1027     4941   4821   4302    -16   -227    129       C  
ATOM    199  NZ  LYS A1027      21.864 -38.172 -12.451  1.00 40.61           N  
ANISOU  199  NZ  LYS A1027     4906   5581   4941   -131   -503     25       N  
ATOM    200  N   THR A1028      18.293 -35.960 -18.830  1.00 18.06           N  
ANISOU  200  N   THR A1028     2307   2548   2006    -41     45    497       N  
ATOM    201  CA  THR A1028      17.285 -35.745 -19.855  1.00 14.93           C  
ANISOU  201  CA  THR A1028     1637   1739   2295   -358     44    135       C  
ATOM    202  C   THR A1028      17.624 -36.670 -21.011  1.00 14.21           C  
ANISOU  202  C   THR A1028     1641   1556   2202    -16   -111    288       C  
ATOM    203  O   THR A1028      18.697 -37.269 -21.024  1.00 17.33           O  
ANISOU  203  O   THR A1028     1870   1988   2724    296   -396    164       O  
ATOM    204  CB  THR A1028      17.344 -34.295 -20.359  1.00 15.32           C  
ANISOU  204  CB  THR A1028     1813   1755   2250   -364    128     74       C  
ATOM    205  OG1 THR A1028      18.710 -33.963 -20.610  1.00 14.90           O  
ANISOU  205  OG1 THR A1028     1654   2047   1960   -283    -33    172       O  
ATOM    206  CG2 THR A1028      16.798 -33.342 -19.313  1.00 16.80           C  
ANISOU  206  CG2 THR A1028     1947   2076   2359   -367     94   -144       C  
ATOM    207  N   ASP A1029      16.730 -36.790 -21.985  1.00 13.15           N  
ANISOU  207  N   ASP A1029     1408   1386   2202     33      2    171       N  
ATOM    208  CA  ASP A1029      17.021 -37.573 -23.183  1.00 12.11           C  
ANISOU  208  CA  ASP A1029     1351   1316   1933    -21   -191    275       C  
ATOM    209  C   ASP A1029      18.117 -36.935 -24.023  1.00 11.93           C  
ANISOU  209  C   ASP A1029     1278   1214   2040    119     52    -23       C  
ATOM    210  O   ASP A1029      18.984 -37.635 -24.526  1.00 14.06           O  
ANISOU  210  O   ASP A1029     1393   1347   2599    365    123     19       O  
ATOM    211  CB  ASP A1029      15.784 -37.771 -24.040  1.00 13.53           C  
ANISOU  211  CB  ASP A1029     1208   1706   2224      6   -177    101       C  
ATOM    212  CG  ASP A1029      14.705 -38.555 -23.327  1.00 16.00           C  
ANISOU  212  CG  ASP A1029     1516   1912   2652   -330   -236    289       C  
ATOM    213  OD1 ASP A1029      15.035 -39.529 -22.641  1.00 21.98           O  
ANISOU  213  OD1 ASP A1029     2226   2257   3865   -499   -113   1032       O  
ATOM    214  OD2 ASP A1029      13.512 -38.200 -23.466  1.00 20.87           O  
ANISOU  214  OD2 ASP A1029     1569   2507   3851   -305   -437    826       O  
ATOM    215  N   VAL A1030      18.092 -35.604 -24.139  1.00 10.42           N  
ANISOU  215  N   VAL A1030     1183   1188   1588     10     36    -51       N  
ATOM    216  CA  VAL A1030      19.050 -34.876 -24.946  1.00 10.30           C  
ANISOU  216  CA  VAL A1030     1398    967   1546    -65     58   -159       C  
ATOM    217  C   VAL A1030      19.715 -33.807 -24.081  1.00  9.11           C  
ANISOU  217  C   VAL A1030     1058   1233   1170    -47    -64    -40       C  
ATOM    218  O   VAL A1030      19.050 -33.158 -23.304  1.00  9.51           O  
ANISOU  218  O   VAL A1030     1077   1109   1427   -104    -66   -226       O  
ATOM    219  CB  VAL A1030      18.327 -34.220 -26.134  1.00 12.11           C  
ANISOU  219  CB  VAL A1030     1486   1551   1561   -119   -108   -196       C  
ATOM    220  CG1 VAL A1030      19.257 -33.329 -26.950  1.00 12.24           C  
ANISOU  220  CG1 VAL A1030     1379   1835   1435    -65    -19   -175       C  
ATOM    221  CG2 VAL A1030      17.657 -35.305 -27.003  1.00 14.02           C  
ANISOU  221  CG2 VAL A1030     1647   1797   1883   -116   -303   -391       C  
ATOM    222  N  AVAL A1031      21.019 -33.625 -24.256  0.70  9.29           N  
ANISOU  222  N  AVAL A1031     1078   1164   1289    -54     76   -134       N  
ATOM    223  N  BVAL A1031      21.022 -33.622 -24.249  0.30  9.44           N  
ANISOU  223  N  BVAL A1031     1092   1196   1298    -59     53    -99       N  
ATOM    224  CA AVAL A1031      21.728 -32.451 -23.714  0.70  9.52           C  
ANISOU  224  CA AVAL A1031     1067   1162   1388   -100     42    -47       C  
ATOM    225  CA BVAL A1031      21.720 -32.452 -23.699  0.30  9.82           C  
ANISOU  225  CA BVAL A1031     1169   1184   1377   -102     44    -58       C  
ATOM    226  C  AVAL A1031      22.370 -31.710 -24.870  0.70  8.67           C  
ANISOU  226  C  AVAL A1031     1089   1098   1108     -7      5   -171       C  
ATOM    227  C  BVAL A1031      22.402 -31.709 -24.844  0.30  8.93           C  
ANISOU  227  C  BVAL A1031     1128   1104   1158      3     22   -162       C  
ATOM    228  O  AVAL A1031      22.903 -32.334 -25.784  0.70  8.77           O  
ANISOU  228  O  AVAL A1031     1149    824   1357     72     65   -202       O  
ATOM    229  O  BVAL A1031      22.974 -32.334 -25.733  0.30  8.99           O  
ANISOU  229  O  BVAL A1031     1141    941   1334     52     59   -182       O  
ATOM    230  CB AVAL A1031      22.792 -32.863 -22.694  0.70 10.24           C  
ANISOU  230  CB AVAL A1031     1281   1236   1371   -185    -67     14       C  
ATOM    231  CB BVAL A1031      22.746 -32.855 -22.629  0.30 11.13           C  
ANISOU  231  CB BVAL A1031     1405   1394   1427   -157    -54     98       C  
ATOM    232  CG1AVAL A1031      23.568 -31.653 -22.179  0.70 12.19           C  
ANISOU  232  CG1AVAL A1031     1579   1315   1734   -318   -151     -8       C  
ATOM    233  CG1BVAL A1031      23.783 -33.790 -23.206  0.30 11.38           C  
ANISOU  233  CG1BVAL A1031     1551   1175   1595   -265    -61    -58       C  
ATOM    234  CG2AVAL A1031      22.111 -33.501 -21.510  0.70 12.81           C  
ANISOU  234  CG2AVAL A1031     1785   1451   1631    -65    278     89       C  
ATOM    235  CG2BVAL A1031      23.400 -31.622 -22.021  0.30 12.48           C  
ANISOU  235  CG2BVAL A1031     1628   1400   1713   -211     33     16       C  
ATOM    236  N   VAL A1032      22.327 -30.378 -24.826  1.00  8.71           N  
ANISOU  236  N   VAL A1032     1093   1100   1113      7     77   -238       N  
ATOM    237  CA  VAL A1032      22.896 -29.538 -25.882  1.00  8.90           C  
ANISOU  237  CA  VAL A1032     1061   1194   1125     19     24   -184       C  
ATOM    238  C   VAL A1032      24.257 -29.039 -25.414  1.00  9.09           C  
ANISOU  238  C   VAL A1032     1045   1097   1311    -54    111   -217       C  
ATOM    239  O   VAL A1032      24.395 -28.584 -24.294  1.00 10.83           O  
ANISOU  239  O   VAL A1032      922   1841   1350    -11    226   -433       O  
ATOM    240  CB  VAL A1032      21.966 -28.369 -26.247  1.00  9.45           C  
ANISOU  240  CB  VAL A1032     1095   1291   1201     35    -90    -99       C  
ATOM    241  CG1 VAL A1032      22.466 -27.626 -27.473  1.00 10.55           C  
ANISOU  241  CG1 VAL A1032     1300   1249   1457    -16     -8    -17       C  
ATOM    242  CG2 VAL A1032      20.572 -28.906 -26.521  1.00  9.54           C  
ANISOU  242  CG2 VAL A1032     1018   1219   1384     37     89    -60       C  
ATOM    243  N   ASN A1033      25.264 -29.183 -26.264  1.00  8.48           N  
ANISOU  243  N   ASN A1033      965   1233   1023   -133    -38   -306       N  
ATOM    244  CA  ASN A1033      26.602 -28.709 -25.995  1.00  8.33           C  
ANISOU  244  CA  ASN A1033      883   1214   1068   -102     80   -116       C  
ATOM    245  C   ASN A1033      26.930 -27.579 -26.975  1.00  9.02           C  
ANISOU  245  C   ASN A1033     1042   1226   1159   -100    -64    -12       C  
ATOM    246  O   ASN A1033      26.387 -27.527 -28.087  1.00 12.01           O  
ANISOU  246  O   ASN A1033     1516   1780   1264   -452   -269    243       O  
ATOM    247  CB  ASN A1033      27.565 -29.889 -26.153  1.00  7.84           C  
ANISOU  247  CB  ASN A1033      904   1062   1010   -126    -46    -90       C  
ATOM    248  CG  ASN A1033      28.984 -29.566 -25.735  1.00  7.85           C  
ANISOU  248  CG  ASN A1033      841   1113   1027    -46     11    -84       C  
ATOM    249  OD1 ASN A1033      29.206 -28.686 -24.893  1.00  9.59           O  
ANISOU  249  OD1 ASN A1033     1204   1237   1201    172   -232   -228       O  
ATOM    250  ND2 ASN A1033      29.943 -30.330 -26.261  1.00  9.02           N  
ANISOU  250  ND2 ASN A1033     1013   1383   1031    122     25   -171       N  
ATOM    251  N   SER A1034      27.827 -26.688 -26.577  1.00  8.69           N  
ANISOU  251  N   SER A1034     1042   1381    877   -201    113    -61       N  
ATOM    252  CA  SER A1034      28.318 -25.628 -27.444  1.00  8.93           C  
ANISOU  252  CA  SER A1034     1148   1166   1078    -12     67     19       C  
ATOM    253  C   SER A1034      29.754 -25.924 -27.796  1.00  8.16           C  
ANISOU  253  C   SER A1034     1066   1179    852   -129     53     48       C  
ATOM    254  O   SER A1034      30.582 -26.077 -26.892  1.00  9.57           O  
ANISOU  254  O   SER A1034     1096   1661    879     44     63    -89       O  
ATOM    255  CB  SER A1034      28.267 -24.309 -26.724  1.00  9.64           C  
ANISOU  255  CB  SER A1034     1384   1158   1120     72    128     15       C  
ATOM    256  OG  SER A1034      28.789 -23.271 -27.523  1.00 12.66           O  
ANISOU  256  OG  SER A1034     1643   1388   1780    -88    486    166       O  
ATOM    257  N   VAL A1035      30.043 -26.039 -29.098  1.00  8.06           N  
ANISOU  257  N   VAL A1035      901   1299    859     53     59     87       N  
ATOM    258  CA  VAL A1035      31.370 -26.457 -29.530  1.00  8.02           C  
ANISOU  258  CA  VAL A1035      952   1203    890      0    102      2       C  
ATOM    259  C   VAL A1035      31.987 -25.467 -30.506  1.00  8.82           C  
ANISOU  259  C   VAL A1035     1175   1303    872     47    114     95       C  
ATOM    260  O   VAL A1035      31.264 -24.708 -31.151  1.00  9.41           O  
ANISOU  260  O   VAL A1035     1267   1405    900     59    110    178       O  
ATOM    261  CB  VAL A1035      31.332 -27.877 -30.153  1.00  9.34           C  
ANISOU  261  CB  VAL A1035     1175   1231   1140     67    -20    -79       C  
ATOM    262  CG1 VAL A1035      30.764 -28.880 -29.160  1.00 11.53           C  
ANISOU  262  CG1 VAL A1035     1580   1358   1440   -169    -54    -21       C  
ATOM    263  CG2 VAL A1035      30.554 -27.886 -31.473  1.00  9.18           C  
ANISOU  263  CG2 VAL A1035     1177   1080   1230   -258    -95    -41       C  
ATOM    264  N   PRO A1036      33.332 -25.468 -30.603  1.00  8.44           N  
ANISOU  264  N   PRO A1036     1159   1109    939   -191      4     37       N  
ATOM    265  CA  PRO A1036      33.959 -24.598 -31.566  1.00  8.85           C  
ANISOU  265  CA  PRO A1036     1290   1269    803    -88     93     55       C  
ATOM    266  C   PRO A1036      33.866 -25.160 -32.961  1.00  8.34           C  
ANISOU  266  C   PRO A1036     1299   1025    845   -178     41     57       C  
ATOM    267  O   PRO A1036      33.525 -26.328 -33.143  1.00  9.18           O  
ANISOU  267  O   PRO A1036     1473   1045    968   -210     95      3       O  
ATOM    268  CB  PRO A1036      35.413 -24.531 -31.131  1.00 10.34           C  
ANISOU  268  CB  PRO A1036     1308   1501   1119   -233     40   -137       C  
ATOM    269  CG  PRO A1036      35.578 -25.460 -30.009  1.00 11.18           C  
ANISOU  269  CG  PRO A1036     1360   1344   1543    -50      6    -10       C  
ATOM    270  CD  PRO A1036      34.307 -26.201 -29.781  1.00 10.33           C  
ANISOU  270  CD  PRO A1036     1303   1399   1223    -26    -42    116       C  
ATOM    271  N   LEU A1037      34.215 -24.323 -33.937  1.00  9.08           N  
ANISOU  271  N   LEU A1037     1549   1102    796   -165     -8    125       N  
ATOM    272  CA  LEU A1037      34.229 -24.753 -35.355  1.00  9.59           C  
ANISOU  272  CA  LEU A1037     1557   1269    814   -228    -24    100       C  
ATOM    273  C   LEU A1037      35.167 -25.934 -35.615  1.00 10.37           C  
ANISOU  273  C   LEU A1037     1606   1370    964   -201    -71    -32       C  
ATOM    274  O   LEU A1037      34.971 -26.693 -36.563  1.00 12.58           O  
ANISOU  274  O   LEU A1037     1908   1582   1288   -302   -355   -239       O  
ATOM    275  CB  LEU A1037      34.668 -23.552 -36.207  1.00 10.21           C  
ANISOU  275  CB  LEU A1037     1528   1445    905   -103     25    305       C  
ATOM    276  CG  LEU A1037      33.589 -22.469 -36.337  1.00 12.08           C  
ANISOU  276  CG  LEU A1037     1657   1607   1326     27     96    141       C  
ATOM    277  CD1 LEU A1037      34.161 -21.173 -36.839  1.00 11.96           C  
ANISOU  277  CD1 LEU A1037     1360   1697   1486     56     -2    281       C  
ATOM    278  CD2 LEU A1037      32.500 -22.944 -37.252  1.00 12.85           C  
ANISOU  278  CD2 LEU A1037     1671   1732   1479     38    -55    307       C  
ATOM    279  N   ASP A1038      36.210 -26.090 -34.805  1.00 10.24           N  
ANISOU  279  N   ASP A1038     1381   1527    981   -287     44     63       N  
ATOM    280  CA  ASP A1038      37.122 -27.242 -34.974  1.00 12.02           C  
ANISOU  280  CA  ASP A1038     1693   1522   1352   -152    -49    101       C  
ATOM    281  C   ASP A1038      36.709 -28.514 -34.218  1.00 10.57           C  
ANISOU  281  C   ASP A1038     1447   1296   1271     -9     37    -29       C  
ATOM    282  O   ASP A1038      37.422 -29.539 -34.298  1.00 11.74           O  
ANISOU  282  O   ASP A1038     1567   1593   1300    240     98    -38       O  
ATOM    283  CB  ASP A1038      38.590 -26.885 -34.693  1.00 13.05           C  
ANISOU  283  CB  ASP A1038     1545   1745   1666   -201    264    216       C  
ATOM    284  CG  ASP A1038      38.871 -26.592 -33.256  1.00 15.79           C  
ANISOU  284  CG  ASP A1038     1881   2288   1830   -285    113      9       C  
ATOM    285  OD1 ASP A1038      37.926 -26.577 -32.451  1.00 15.67           O  
ANISOU  285  OD1 ASP A1038     2011   2479   1461   -628     95     83       O  
ATOM    286  OD2 ASP A1038      40.063 -26.351 -32.923  1.00 20.07           O  
ANISOU  286  OD2 ASP A1038     2124   3271   2231   -735   -165    367       O  
ATOM    287  N   LEU A1039      35.558 -28.454 -33.543  1.00 10.36           N  
ANISOU  287  N   LEU A1039     1465   1248   1222      7     -2    -94       N  
ATOM    288  CA  LEU A1039      34.961 -29.592 -32.848  1.00 10.91           C  
ANISOU  288  CA  LEU A1039     1501   1228   1416    -22     16   -104       C  
ATOM    289  C   LEU A1039      35.782 -30.103 -31.649  1.00 12.29           C  
ANISOU  289  C   LEU A1039     1520   1402   1747     27    -63    155       C  
ATOM    290  O   LEU A1039      35.485 -31.160 -31.117  1.00 14.07           O  
ANISOU  290  O   LEU A1039     1461   1705   2180    -88   -359    575       O  
ATOM    291  CB  LEU A1039      34.636 -30.734 -33.836  1.00 11.83           C  
ANISOU  291  CB  LEU A1039     1651   1492   1349    -78    108   -235       C  
ATOM    292  CG  LEU A1039      33.723 -30.345 -35.006  1.00 13.08           C  
ANISOU  292  CG  LEU A1039     1836   1646   1486   -202    -84   -253       C  
ATOM    293  CD1 LEU A1039      33.475 -31.598 -35.850  1.00 15.40           C  
ANISOU  293  CD1 LEU A1039     2259   2051   1541   -282    -38   -562       C  
ATOM    294  CD2 LEU A1039      32.399 -29.709 -34.602  1.00 13.33           C  
ANISOU  294  CD2 LEU A1039     1990   1989   1084   -124      2   -273       C  
ATOM    295  N   VAL A1040      36.775 -29.330 -31.200  1.00 10.22           N  
ANISOU  295  N   VAL A1040     1400   1271   1211    107    186     92       N  
ATOM    296  CA  VAL A1040      37.557 -29.695 -30.033  1.00 11.35           C  
ANISOU  296  CA  VAL A1040     1551   1520   1240     72    135    135       C  
ATOM    297  C   VAL A1040      36.731 -29.390 -28.780  1.00 11.36           C  
ANISOU  297  C   VAL A1040     1525   1298   1490     -6    289     20       C  
ATOM    298  O   VAL A1040      36.346 -28.260 -28.538  1.00 12.53           O  
ANISOU  298  O   VAL A1040     1963   1102   1694   -140    467    184       O  
ATOM    299  CB  VAL A1040      38.891 -28.973 -30.016  1.00 11.91           C  
ANISOU  299  CB  VAL A1040     1577   1618   1330    -27     64    182       C  
ATOM    300  CG1 VAL A1040      39.659 -29.261 -28.736  1.00 14.27           C  
ANISOU  300  CG1 VAL A1040     1614   2246   1561    -63    -88    201       C  
ATOM    301  CG2 VAL A1040      39.727 -29.430 -31.208  1.00 12.49           C  
ANISOU  301  CG2 VAL A1040     1442   1741   1560    -24    123     67       C  
ATOM    302  N   LEU A1041      36.484 -30.413 -27.981  1.00  9.34           N  
ANISOU  302  N   LEU A1041     1189   1171   1186    201     26    -55       N  
ATOM    303  CA  LEU A1041      35.563 -30.339 -26.874  1.00  9.08           C  
ANISOU  303  CA  LEU A1041     1013   1324   1112    108    -39    -16       C  
ATOM    304  C   LEU A1041      36.180 -29.823 -25.580  1.00  9.15           C  
ANISOU  304  C   LEU A1041     1158   1278   1040    116     93    -84       C  
ATOM    305  O   LEU A1041      35.478 -29.647 -24.585  1.00 10.36           O  
ANISOU  305  O   LEU A1041     1298   1700    936    250    111     45       O  
ATOM    306  CB  LEU A1041      34.950 -31.725 -26.622  1.00  9.71           C  
ANISOU  306  CB  LEU A1041     1112   1344   1233    101    187    -60       C  
ATOM    307  CG  LEU A1041      34.037 -32.247 -27.701  1.00 10.76           C  
ANISOU  307  CG  LEU A1041     1270   1459   1358    -28    110    -35       C  
ATOM    308  CD1 LEU A1041      33.509 -33.627 -27.340  1.00 12.16           C  
ANISOU  308  CD1 LEU A1041     1420   1545   1652   -191    136    -85       C  
ATOM    309  CD2 LEU A1041      32.876 -31.296 -27.949  1.00 12.20           C  
ANISOU  309  CD2 LEU A1041     1514   1405   1715     28    -52    -55       C  
ATOM    310  N   SER A1042      37.490 -29.604 -25.590  1.00  9.74           N  
ANISOU  310  N   SER A1042     1198   1409   1092    -72    -55     99       N  
ATOM    311  CA  SER A1042      38.221 -29.190 -24.412  1.00 10.43           C  
ANISOU  311  CA  SER A1042     1373   1501   1087     15   -206    205       C  
ATOM    312  C   SER A1042      38.547 -27.707 -24.355  1.00 11.29           C  
ANISOU  312  C   SER A1042     1417   1613   1257   -142   -209     32       C  
ATOM    313  O   SER A1042      39.355 -27.287 -23.524  1.00 15.95           O  
ANISOU  313  O   SER A1042     1961   2134   1966   -489   -672    -87       O  
ATOM    314  CB  SER A1042      39.502 -30.018 -24.335  1.00 12.18           C  
ANISOU  314  CB  SER A1042     1479   1634   1512    112   -171    160       C  
ATOM    315  OG  SER A1042      40.188 -29.963 -25.534  1.00 14.93           O  
ANISOU  315  OG  SER A1042     1461   2590   1622    277     -7     92       O  
ATOM    316  N   ARG A1043      37.930 -26.891 -25.206  1.00 10.46           N  
ANISOU  316  N   ARG A1043     1310   1510   1154   -112    -85      4       N  
ATOM    317  CA AARG A1043      38.316 -25.479 -25.257  0.70 12.09           C  
ANISOU  317  CA AARG A1043     1656   1511   1423   -145   -171    -36       C  
ATOM    318  CA BARG A1043      38.295 -25.467 -25.285  0.30 11.95           C  
ANISOU  318  CA BARG A1043     1577   1535   1428   -160   -121    -17       C  
ATOM    319  C   ARG A1043      37.488 -24.651 -24.276  1.00 13.10           C  
ANISOU  319  C   ARG A1043     1708   1806   1463    -45   -139    -98       C  
ATOM    320  O   ARG A1043      38.029 -24.119 -23.312  1.00 18.31           O  
ANISOU  320  O   ARG A1043     2527   2639   1790   -437    123   -856       O  
ATOM    321  CB AARG A1043      38.286 -24.968 -26.693  0.70 14.09           C  
ANISOU  321  CB AARG A1043     1955   1867   1529   -137   -172     97       C  
ATOM    322  CB BARG A1043      38.115 -24.924 -26.709  0.30 12.53           C  
ANISOU  322  CB BARG A1043     1634   1674   1450    -82    -59     16       C  
ATOM    323  CG AARG A1043      39.416 -25.571 -27.510  0.70 16.39           C  
ANISOU  323  CG AARG A1043     2275   2070   1879     67     -9     75       C  
ATOM    324  CG BARG A1043      38.925 -25.657 -27.765  0.30 13.16           C  
ANISOU  324  CG BARG A1043     1653   1782   1564    -10     20     31       C  
ATOM    325  CD AARG A1043      39.329 -25.227 -28.987  0.70 18.28           C  
ANISOU  325  CD AARG A1043     2675   2186   2083    -71   -219    340       C  
ATOM    326  CD BARG A1043      39.469 -24.696 -28.819  0.30 14.26           C  
ANISOU  326  CD BARG A1043     1907   1831   1679     20     24    151       C  
ATOM    327  NE AARG A1043      39.499 -23.795 -29.212  0.70 21.02           N  
ANISOU  327  NE AARG A1043     3103   2347   2536   -216     30    747       N  
ATOM    328  NE BARG A1043      40.121 -25.385 -29.933  0.30 13.70           N  
ANISOU  328  NE BARG A1043     1708   1928   1567    -50     -7    166       N  
ATOM    329  CZ AARG A1043      39.233 -23.186 -30.369  0.70 20.43           C  
ANISOU  329  CZ AARG A1043     3188   2904   1667    -43    -59     -5       C  
ATOM    330  CZ BARG A1043      41.371 -25.838 -29.904  0.30 14.85           C  
ANISOU  330  CZ BARG A1043     1796   2082   1763     72     85     43       C  
ATOM    331  NH1AARG A1043      38.786 -23.871 -31.407  0.70 19.03           N  
ANISOU  331  NH1AARG A1043     2275   2655   2299    203   -186   -354       N  
ATOM    332  NH1BARG A1043      42.107 -25.694 -28.805  0.30 17.28           N  
ANISOU  332  NH1BARG A1043     1868   2722   1972   -256      4   -116       N  
ATOM    333  NH2AARG A1043      39.397 -21.877 -30.480  0.70 25.62           N  
ANISOU  333  NH2AARG A1043     4016   3075   2641   -493    337    253       N  
ATOM    334  NH2BARG A1043      41.881 -26.445 -30.966  0.30 12.64           N  
ANISOU  334  NH2BARG A1043     1570   1704   1527    -29   -117    127       N  
ATOM    335  N   GLY A1044      36.193 -24.593 -24.474  1.00 12.72           N  
ANISOU  335  N   GLY A1044     1742   1726   1363   -231   -128    -24       N  
ATOM    336  CA  GLY A1044      35.309 -23.818 -23.633  1.00 12.55           C  
ANISOU  336  CA  GLY A1044     1747   1651   1370   -169    -86     67       C  
ATOM    337  C   GLY A1044      34.944 -24.525 -22.345  1.00 10.62           C  
ANISOU  337  C   GLY A1044     1673   1160   1200    -88   -161   -141       C  
ATOM    338  O   GLY A1044      35.064 -25.737 -22.252  1.00  9.89           O  
ANISOU  338  O   GLY A1044     1363   1141   1251   -141    -20    -80       O  
ATOM    339  N   PRO A1045      34.517 -23.760 -21.328  1.00 10.45           N  
ANISOU  339  N   PRO A1045     1497   1100   1372    -25    -83   -159       N  
ATOM    340  CA  PRO A1045      34.315 -24.372 -20.040  1.00 10.15           C  
ANISOU  340  CA  PRO A1045     1483   1039   1332     21    -25   -221       C  
ATOM    341  C   PRO A1045      33.117 -25.343 -19.994  1.00  9.89           C  
ANISOU  341  C   PRO A1045     1504   1172   1078     -5     -6     25       C  
ATOM    342  O   PRO A1045      33.228 -26.377 -19.321  1.00 10.70           O  
ANISOU  342  O   PRO A1045     1791   1137   1136    -22    -48     57       O  
ATOM    343  CB  PRO A1045      34.156 -23.176 -19.097  1.00 11.57           C  
ANISOU  343  CB  PRO A1045     1790   1257   1346    -64     -3   -368       C  
ATOM    344  CG  PRO A1045      33.663 -22.086 -19.972  1.00 12.81           C  
ANISOU  344  CG  PRO A1045     2255    580   2029   -127    -93   -543       C  
ATOM    345  CD  PRO A1045      34.354 -22.300 -21.276  1.00 12.29           C  
ANISOU  345  CD  PRO A1045     1853   1110   1707    -92   -253   -128       C  
ATOM    346  N   LEU A1046      32.015 -25.058 -20.688  1.00  9.91           N  
ANISOU  346  N   LEU A1046     1452   1033   1278    122    -27   -132       N  
ATOM    347  CA ALEU A1046      30.891 -25.976 -20.638  0.70 10.57           C  
ANISOU  347  CA ALEU A1046     1394   1247   1372    103   -134    -20       C  
ATOM    348  CA BLEU A1046      30.866 -25.992 -20.665  0.30 10.72           C  
ANISOU  348  CA BLEU A1046     1433   1256   1383     65    -73    -39       C  
ATOM    349  C   LEU A1046      31.253 -27.307 -21.312  1.00  9.33           C  
ANISOU  349  C   LEU A1046     1166   1224   1155    -23   -170    -33       C  
ATOM    350  O   LEU A1046      31.087 -28.389 -20.734  1.00  9.92           O  
ANISOU  350  O   LEU A1046     1259   1179   1330    232     65     -7       O  
ATOM    351  CB ALEU A1046      29.642 -25.338 -21.248  0.70 12.63           C  
ANISOU  351  CB ALEU A1046     1496   1436   1864    312   -223    -60       C  
ATOM    352  CB BLEU A1046      29.617 -25.463 -21.387  0.30 13.06           C  
ANISOU  352  CB BLEU A1046     1569   1601   1791    291   -154      2       C  
ATOM    353  CG ALEU A1046      28.382 -26.200 -21.220  0.70 12.20           C  
ANISOU  353  CG ALEU A1046      869   1412   2351    759   -454    212       C  
ATOM    354  CG BLEU A1046      28.556 -26.587 -21.513  0.30 15.86           C  
ANISOU  354  CG BLEU A1046     1776   1885   2362     90   -132     48       C  
ATOM    355  CD1ALEU A1046      28.332 -27.193 -22.361  0.70 16.39           C  
ANISOU  355  CD1ALEU A1046     1943   2149   2133    307   -460     19       C  
ATOM    356  CD1BLEU A1046      27.885 -26.796 -20.172  0.30 18.48           C  
ANISOU  356  CD1BLEU A1046     2153   2445   2421     72    -14     75       C  
ATOM    357  CD2ALEU A1046      28.217 -26.916 -19.912  0.70 18.53           C  
ANISOU  357  CD2ALEU A1046     2113   2531   2393     67     49    229       C  
ATOM    358  CD2BLEU A1046      27.519 -26.372 -22.590  0.30 16.95           C  
ANISOU  358  CD2BLEU A1046     1985   2333   2121     24   -130    -55       C  
ATOM    359  N   SER A1047      31.721 -27.222 -22.536  1.00  7.98           N  
ANISOU  359  N   SER A1047      984    923   1125     12   -200     76       N  
ATOM    360  CA  SER A1047      32.107 -28.405 -23.240  1.00  8.46           C  
ANISOU  360  CA  SER A1047     1099    982   1133    -35   -183     10       C  
ATOM    361  C   SER A1047      33.179 -29.197 -22.467  1.00  7.90           C  
ANISOU  361  C   SER A1047      950   1023   1026    -28   -116    -61       C  
ATOM    362  O   SER A1047      33.121 -30.421 -22.406  1.00  8.72           O  
ANISOU  362  O   SER A1047     1129   1044   1139   -103    -73    -59       O  
ATOM    363  CB  SER A1047      32.605 -28.073 -24.633  1.00 10.74           C  
ANISOU  363  CB  SER A1047     1427   1469   1183     99    -64     51       C  
ATOM    364  OG  SER A1047      32.772 -29.255 -25.346  1.00 12.00           O  
ANISOU  364  OG  SER A1047     1581   1807   1171   -173    -34   -261       O  
ATOM    365  N   SER A1048      34.154 -28.501 -21.873  1.00  7.79           N  
ANISOU  365  N   SER A1048     1025    945    988    -11   -144    -87       N  
ATOM    366  CA  SER A1048      35.199 -29.194 -21.125  1.00  8.69           C  
ANISOU  366  CA  SER A1048     1003   1087   1211    140   -131   -123       C  
ATOM    367  C   SER A1048      34.592 -29.968 -19.966  1.00  8.80           C  
ANISOU  367  C   SER A1048     1022   1125   1194     68   -213   -118       C  
ATOM    368  O   SER A1048      35.022 -31.079 -19.661  1.00 10.14           O  
ANISOU  368  O   SER A1048     1427   1156   1268    118   -278   -103       O  
ATOM    369  CB  SER A1048      36.263 -28.211 -20.612  1.00 10.69           C  
ANISOU  369  CB  SER A1048     1245   1305   1512   -100   -135   -106       C  
ATOM    370  OG  SER A1048      36.950 -27.625 -21.688  1.00 12.37           O  
ANISOU  370  OG  SER A1048     1457   1801   1440   -107    154   -392       O  
ATOM    371  N   SER A1049      33.624 -29.360 -19.281  1.00  9.37           N  
ANISOU  371  N   SER A1049     1247   1094   1218      8    -32   -130       N  
ATOM    372  CA ASER A1049      32.917 -30.002 -18.184  0.50  9.82           C  
ANISOU  372  CA ASER A1049     1267   1223   1239      4    -98    -14       C  
ATOM    373  CA BSER A1049      32.944 -30.021 -18.179  0.50  9.85           C  
ANISOU  373  CA BSER A1049     1278   1218   1245     18    -99      0       C  
ATOM    374  C   SER A1049      32.146 -31.242 -18.633  1.00  9.04           C  
ANISOU  374  C   SER A1049     1250    987   1199    164    -55     19       C  
ATOM    375  O   SER A1049      32.155 -32.282 -17.964  1.00 10.82           O  
ANISOU  375  O   SER A1049     1607   1083   1421     26   -258    199       O  
ATOM    376  CB ASER A1049      31.952 -29.014 -17.521  0.50 10.31           C  
ANISOU  376  CB ASER A1049     1438   1294   1182    -51    -78   -230       C  
ATOM    377  CB BSER A1049      32.055 -29.032 -17.418  0.50 10.67           C  
ANISOU  377  CB BSER A1049     1508   1349   1196     16     17    -88       C  
ATOM    378  OG ASER A1049      31.480 -29.544 -16.303  0.50 11.75           O  
ANISOU  378  OG ASER A1049     1689   1518   1256   -229     63   -290       O  
ATOM    379  OG BSER A1049      32.871 -28.123 -16.691  0.50 12.56           O  
ANISOU  379  OG BSER A1049     1753   1768   1251      6   -202   -226       O  
ATOM    380  N   LEU A1050      31.444 -31.126 -19.741  1.00  9.11           N  
ANISOU  380  N   LEU A1050     1338   1012   1108    126     -8    115       N  
ATOM    381  CA  LEU A1050      30.720 -32.280 -20.303  1.00  9.78           C  
ANISOU  381  CA  LEU A1050     1314   1132   1269     92   -122     72       C  
ATOM    382  C   LEU A1050      31.714 -33.389 -20.680  1.00  9.04           C  
ANISOU  382  C   LEU A1050     1170   1165   1096    -41    -21    -16       C  
ATOM    383  O   LEU A1050      31.477 -34.546 -20.382  1.00 10.74           O  
ANISOU  383  O   LEU A1050     1352   1362   1367    -25    113    432       O  
ATOM    384  CB  LEU A1050      29.865 -31.900 -21.511  1.00 12.16           C  
ANISOU  384  CB  LEU A1050     1662   1684   1272    120   -183    282       C  
ATOM    385  CG  LEU A1050      28.560 -31.161 -21.258  1.00 15.77           C  
ANISOU  385  CG  LEU A1050     1893   2089   2008    236     59    278       C  
ATOM    386  CD1 LEU A1050      27.820 -30.849 -22.563  1.00 18.11           C  
ANISOU  386  CD1 LEU A1050     2255   2586   2039    146   -128    229       C  
ATOM    387  CD2 LEU A1050      27.658 -31.996 -20.355  1.00 19.11           C  
ANISOU  387  CD2 LEU A1050     2096   2770   2392    -71     -3    591       C  
ATOM    388  N   LEU A1051      32.822 -33.020 -21.325  1.00  9.46           N  
ANISOU  388  N   LEU A1051     1114   1103   1374    -69      5     44       N  
ATOM    389  CA  LEU A1051      33.849 -33.986 -21.716  1.00  9.82           C  
ANISOU  389  CA  LEU A1051     1259   1229   1240    -39     91    -83       C  
ATOM    390  C   LEU A1051      34.442 -34.698 -20.508  1.00  9.92           C  
ANISOU  390  C   LEU A1051     1270   1187   1311     97    226      5       C  
ATOM    391  O   LEU A1051      34.672 -35.924 -20.535  1.00 10.11           O  
ANISOU  391  O   LEU A1051     1288   1145   1408     84     -9    192       O  
ATOM    392  CB  LEU A1051      34.935 -33.299 -22.546  1.00 10.36           C  
ANISOU  392  CB  LEU A1051     1215   1337   1381    -43    142    -98       C  
ATOM    393  CG  LEU A1051      36.103 -34.138 -23.039  1.00 11.19           C  
ANISOU  393  CG  LEU A1051     1335   1380   1534     64    204     11       C  
ATOM    394  CD1 LEU A1051      35.581 -35.223 -23.964  1.00 11.48           C  
ANISOU  394  CD1 LEU A1051     1487   1509   1366    124    265    -47       C  
ATOM    395  CD2 LEU A1051      37.115 -33.240 -23.726  1.00 12.88           C  
ANISOU  395  CD2 LEU A1051     1419   1542   1931    -96    192     78       C  
ATOM    396  N   GLU A1052      34.663 -33.953 -19.431  1.00 10.54           N  
ANISOU  396  N   GLU A1052     1372   1217   1414    -27   -173     81       N  
ATOM    397  CA  GLU A1052      35.256 -34.562 -18.257  1.00 12.48           C  
ANISOU  397  CA  GLU A1052     1585   1513   1642    165   -210    304       C  
ATOM    398  C   GLU A1052      34.395 -35.678 -17.652  1.00 11.42           C  
ANISOU  398  C   GLU A1052     1345   1457   1534    211   -244    226       C  
ATOM    399  O   GLU A1052      34.930 -36.682 -17.142  1.00 15.03           O  
ANISOU  399  O   GLU A1052     1787   1284   2640    232   -450    362       O  
ATOM    400  CB  GLU A1052      35.698 -33.520 -17.252  1.00 18.03           C  
ANISOU  400  CB  GLU A1052     2731   2228   1890    -36   -381    -44       C  
ATOM    401  CG  GLU A1052      36.981 -32.822 -17.717  1.00 24.92           C  
ANISOU  401  CG  GLU A1052     3126   3322   3020   -296   -120    248       C  
ATOM    402  CD  GLU A1052      38.130 -33.802 -18.046  1.00 26.88           C  
ANISOU  402  CD  GLU A1052     3171   3771   3270    298   -310   1359       C  
ATOM    403  OE1 GLU A1052      38.492 -34.527 -17.132  1.00 29.59           O  
ANISOU  403  OE1 GLU A1052     4373   3265   3605     38  -1068   1207       O  
ATOM    404  OE2 GLU A1052      38.654 -33.893 -19.201  1.00 36.15           O  
ANISOU  404  OE2 GLU A1052     2802   6401   4532   -531   1010   1166       O  
ATOM    405  N   LYS A1053      33.076 -35.521 -17.712  1.00  9.88           N  
ANISOU  405  N   LYS A1053     1300   1450   1003     24   -216     30       N  
ATOM    406  CA  LYS A1053      32.163 -36.553 -17.263  1.00 10.18           C  
ANISOU  406  CA  LYS A1053     1397   1311   1159     58    -77    -34       C  
ATOM    407  C   LYS A1053      31.962 -37.642 -18.311  1.00  9.04           C  
ANISOU  407  C   LYS A1053     1336   1244    853      4    -35    151       C  
ATOM    408  O   LYS A1053      31.894 -38.839 -17.969  1.00 10.27           O  
ANISOU  408  O   LYS A1053     1820   1247    833    -64     35    127       O  
ATOM    409  CB  LYS A1053      30.826 -35.917 -16.878  1.00 12.82           C  
ANISOU  409  CB  LYS A1053     1425   1833   1611    170    -43   -222       C  
ATOM    410  CG  LYS A1053      29.733 -36.900 -16.460  1.00 16.78           C  
ANISOU  410  CG  LYS A1053     1961   2311   2104   -156    117    -67       C  
ATOM    411  CD  LYS A1053      30.028 -37.710 -15.232  1.00 22.96           C  
ANISOU  411  CD  LYS A1053     2878   3174   2672    145    -64    341       C  
ATOM    412  CE  LYS A1053      28.791 -38.522 -14.871  1.00 30.13           C  
ANISOU  412  CE  LYS A1053     3527   4106   3814   -398    672     77       C  
ATOM    413  NZ  LYS A1053      28.974 -39.174 -13.553  1.00 37.06           N  
ANISOU  413  NZ  LYS A1053     4728   5333   4019     -2    635    290       N  
ATOM    414  N   ALA A1054      31.856 -37.243 -19.575  1.00  7.41           N  
ANISOU  414  N   ALA A1054     1016    944    852     16     54    160       N  
ATOM    415  CA  ALA A1054      31.502 -38.189 -20.621  1.00  7.50           C  
ANISOU  415  CA  ALA A1054     1098    974    776    -18     96    161       C  
ATOM    416  C   ALA A1054      32.592 -39.185 -20.928  1.00  7.89           C  
ANISOU  416  C   ALA A1054     1145    962    889    -17     75    132       C  
ATOM    417  O   ALA A1054      32.312 -40.326 -21.324  1.00  8.98           O  
ANISOU  417  O   ALA A1054     1473    959    978     12    173      6       O  
ATOM    418  CB  ALA A1054      31.102 -37.472 -21.904  1.00  7.50           C  
ANISOU  418  CB  ALA A1054     1083   1015    751     19     10     84       C  
ATOM    419  N   GLY A1055      33.819 -38.707 -20.855  1.00  7.78           N  
ANISOU  419  N   GLY A1055     1040   1107    807     79     -1     54       N  
ATOM    420  CA  GLY A1055      34.993 -39.465 -21.266  1.00  8.27           C  
ANISOU  420  CA  GLY A1055     1015   1206    921    125     51    177       C  
ATOM    421  C   GLY A1055      35.423 -39.113 -22.683  1.00  7.80           C  
ANISOU  421  C   GLY A1055      995   1175    793     68    -96     87       C  
ATOM    422  O   GLY A1055      34.645 -38.559 -23.460  1.00  7.24           O  
ANISOU  422  O   GLY A1055      999   1030    719     68     30    150       O  
ATOM    423  N   PRO A1056      36.668 -39.458 -23.046  1.00  8.43           N  
ANISOU  423  N   PRO A1056      951   1483    767     57   -137    100       N  
ATOM    424  CA  PRO A1056      37.229 -39.085 -24.347  1.00  8.06           C  
ANISOU  424  CA  PRO A1056     1108   1175    780    -17   -149    109       C  
ATOM    425  C   PRO A1056      36.503 -39.711 -25.547  1.00  8.03           C  
ANISOU  425  C   PRO A1056     1059   1187    801    -16    -51     -8       C  
ATOM    426  O   PRO A1056      36.642 -39.227 -26.675  1.00  8.29           O  
ANISOU  426  O   PRO A1056      998   1196    953    -13     99    143       O  
ATOM    427  CB  PRO A1056      38.684 -39.534 -24.244  1.00  9.85           C  
ANISOU  427  CB  PRO A1056     1108   1437   1198     -1    -40     43       C  
ATOM    428  CG  PRO A1056      38.675 -40.601 -23.210  1.00 10.83           C  
ANISOU  428  CG  PRO A1056     1275   1604   1233    157   -207    143       C  
ATOM    429  CD  PRO A1056      37.643 -40.199 -22.231  1.00 10.02           C  
ANISOU  429  CD  PRO A1056     1180   1450   1175    162   -243    215       C  
ATOM    430  N   GLU A1057      35.762 -40.784 -25.299  1.00  8.08           N  
ANISOU  430  N   GLU A1057     1013   1125    931     17   -145   -101       N  
ATOM    431  CA  GLU A1057      34.929 -41.365 -26.342  1.00  7.87           C  
ANISOU  431  CA  GLU A1057     1058    961    968     -1   -108   -155       C  
ATOM    432  C   GLU A1057      33.946 -40.364 -26.935  1.00  7.59           C  
ANISOU  432  C   GLU A1057     1065    985    833     22    -35   -120       C  
ATOM    433  O   GLU A1057      33.586 -40.488 -28.119  1.00  9.03           O  
ANISOU  433  O   GLU A1057     1052   1445    932    -16   -234    -37       O  
ATOM    434  CB  GLU A1057      34.178 -42.619 -25.843  1.00  9.54           C  
ANISOU  434  CB  GLU A1057     1253   1057   1311   -140    -90   -113       C  
ATOM    435  CG  GLU A1057      35.109 -43.748 -25.453  1.00 11.38           C  
ANISOU  435  CG  GLU A1057     1439   1294   1589     42     39     21       C  
ATOM    436  CD  GLU A1057      35.751 -43.668 -24.087  1.00 13.61           C  
ANISOU  436  CD  GLU A1057     1734   1528   1906     36   -255   -107       C  
ATOM    437  OE1 GLU A1057      36.553 -44.594 -23.841  1.00 20.38           O  
ANISOU  437  OE1 GLU A1057     2997   1743   3001    545   -635     64       O  
ATOM    438  OE2 GLU A1057      35.482 -42.756 -23.262  1.00 12.51           O  
ANISOU  438  OE2 GLU A1057     1653   1682   1418    143     26     89       O  
ATOM    439  N   LEU A1058      33.497 -39.383 -26.146  1.00  7.10           N  
ANISOU  439  N   LEU A1058      951    945    800    108      4      0       N  
ATOM    440  CA  LEU A1058      32.640 -38.338 -26.701  1.00  7.61           C  
ANISOU  440  CA  LEU A1058      868   1129    893    137   -109      3       C  
ATOM    441  C   LEU A1058      33.344 -37.564 -27.815  1.00  7.84           C  
ANISOU  441  C   LEU A1058      851   1134    993     46   -114     29       C  
ATOM    442  O   LEU A1058      32.763 -37.257 -28.887  1.00  9.05           O  
ANISOU  442  O   LEU A1058     1012   1500    926    111   -128      0       O  
ATOM    443  CB  LEU A1058      32.198 -37.379 -25.599  1.00  7.95           C  
ANISOU  443  CB  LEU A1058      979   1034   1007    115     14     43       C  
ATOM    444  CG  LEU A1058      31.187 -36.312 -26.009  1.00  8.53           C  
ANISOU  444  CG  LEU A1058      975   1045   1219     89    -10    146       C  
ATOM    445  CD1 LEU A1058      29.841 -36.954 -26.378  1.00  9.78           C  
ANISOU  445  CD1 LEU A1058     1120   1208   1385      8    -92     55       C  
ATOM    446  CD2 LEU A1058      31.021 -35.318 -24.888  1.00  8.97           C  
ANISOU  446  CD2 LEU A1058     1153   1190   1064     41    -68    169       C  
ATOM    447  N   GLN A1059      34.598 -37.223 -27.579  1.00  7.43           N  
ANISOU  447  N   GLN A1059      896   1178    746    -39    -84   -111       N  
ATOM    448  CA  GLN A1059      35.414 -36.574 -28.618  1.00  7.59           C  
ANISOU  448  CA  GLN A1059      982   1074    828     54    -47     21       C  
ATOM    449  C   GLN A1059      35.647 -37.506 -29.830  1.00  7.52           C  
ANISOU  449  C   GLN A1059      840   1164    854     -4   -124    -64       C  
ATOM    450  O   GLN A1059      35.599 -37.053 -30.985  1.00  9.57           O  
ANISOU  450  O   GLN A1059     1284   1414    937     63   -359     36       O  
ATOM    451  CB  GLN A1059      36.761 -36.151 -28.053  1.00  8.43           C  
ANISOU  451  CB  GLN A1059     1029   1106   1068    -29    -41     38       C  
ATOM    452  CG  GLN A1059      37.620 -35.389 -29.047  1.00  7.93           C  
ANISOU  452  CG  GLN A1059      835   1181    994    123    106    -70       C  
ATOM    453  CD  GLN A1059      37.129 -33.984 -29.298  1.00  7.73           C  
ANISOU  453  CD  GLN A1059     1007   1101    829     -9     54    -22       C  
ATOM    454  OE1 GLN A1059      37.347 -33.076 -28.462  1.00  9.23           O  
ANISOU  454  OE1 GLN A1059     1388   1042   1076    161   -166   -138       O  
ATOM    455  NE2 GLN A1059      36.447 -33.779 -30.435  1.00  8.35           N  
ANISOU  455  NE2 GLN A1059      923   1208   1039    127    -92     71       N  
ATOM    456  N   GLU A1060      35.929 -38.785 -29.551  1.00  7.43           N  
ANISOU  456  N   GLU A1060      868   1151    801     14   -121   -112       N  
ATOM    457  CA  GLU A1060      36.134 -39.811 -30.599  1.00  8.72           C  
ANISOU  457  CA  GLU A1060     1041   1294    977   -121    -35   -244       C  
ATOM    458  C   GLU A1060      34.938 -39.816 -31.523  1.00  8.91           C  
ANISOU  458  C   GLU A1060      967   1384   1034    -18     -7   -135       C  
ATOM    459  O   GLU A1060      35.074 -39.755 -32.750  1.00 10.31           O  
ANISOU  459  O   GLU A1060     1027   1892    995    119   -190   -182       O  
ATOM    460  CB  GLU A1060      36.323 -41.186 -29.962  1.00 10.83           C  
ANISOU  460  CB  GLU A1060     1353   1508   1253    134   -200    -86       C  
ATOM    461  CG  GLU A1060      36.645 -42.346 -30.874  1.00 14.04           C  
ANISOU  461  CG  GLU A1060     2044   1786   1503    161   -352   -366       C  
ATOM    462  CD  GLU A1060      36.820 -43.671 -30.120  1.00 17.21           C  
ANISOU  462  CD  GLU A1060     2762   1817   1958    346   -717   -313       C  
ATOM    463  OE1 GLU A1060      36.464 -43.801 -28.920  1.00 20.61           O  
ANISOU  463  OE1 GLU A1060     3126   2251   2453     76   -172   -134       O  
ATOM    464  OE2 GLU A1060      37.293 -44.615 -30.751  1.00 24.49           O  
ANISOU  464  OE2 GLU A1060     4115   2949   2239   1291   -563   -632       O  
ATOM    465  N   GLU A1061      33.752 -39.876 -30.933  1.00  7.66           N  
ANISOU  465  N   GLU A1061      872   1179    860    -56   -112   -285       N  
ATOM    466  CA  GLU A1061      32.522 -39.957 -31.746  1.00  7.41           C  
ANISOU  466  CA  GLU A1061      969   1116    728     23   -172    -85       C  
ATOM    467  C   GLU A1061      32.245 -38.651 -32.473  1.00  7.69           C  
ANISOU  467  C   GLU A1061     1020   1173    727     23   -143    -34       C  
ATOM    468  O   GLU A1061      31.884 -38.662 -33.660  1.00  8.76           O  
ANISOU  468  O   GLU A1061     1256   1259    810     26   -361   -129       O  
ATOM    469  CB  GLU A1061      31.318 -40.393 -30.938  1.00  7.21           C  
ANISOU  469  CB  GLU A1061      889    967    881     22   -218    -44       C  
ATOM    470  CG  GLU A1061      30.116 -40.704 -31.840  1.00  8.68           C  
ANISOU  470  CG  GLU A1061     1112   1035   1149    -92   -405   -156       C  
ATOM    471  CD  GLU A1061      28.872 -41.129 -31.092  1.00 11.13           C  
ANISOU  471  CD  GLU A1061     1276   1257   1696   -137   -268     18       C  
ATOM    472  OE1 GLU A1061      27.884 -41.429 -31.756  1.00 17.49           O  
ANISOU  472  OE1 GLU A1061     1621   2745   2278   -522   -643     62       O  
ATOM    473  OE2 GLU A1061      28.842 -41.185 -29.863  1.00 16.28           O  
ANISOU  473  OE2 GLU A1061     2148   2193   1845   -606    328   -142       O  
ATOM    474  N   LEU A1062      32.404 -37.524 -31.810  1.00  7.77           N  
ANISOU  474  N   LEU A1062     1008   1159    783    -61    -28    -21       N  
ATOM    475  CA  LEU A1062      32.200 -36.246 -32.511  1.00  8.26           C  
ANISOU  475  CA  LEU A1062     1032   1202    904     65    -73    -20       C  
ATOM    476  C   LEU A1062      33.141 -36.093 -33.692  1.00  8.21           C  
ANISOU  476  C   LEU A1062     1137   1305    677    -57   -190    118       C  
ATOM    477  O   LEU A1062      32.720 -35.660 -34.772  1.00  8.31           O  
ANISOU  477  O   LEU A1062     1149   1157    850     16   -331    183       O  
ATOM    478  CB  LEU A1062      32.318 -35.051 -31.580  1.00  8.57           C  
ANISOU  478  CB  LEU A1062     1051   1164   1039    -30    -23    -58       C  
ATOM    479  CG  LEU A1062      32.030 -33.700 -32.214  1.00  9.69           C  
ANISOU  479  CG  LEU A1062     1183   1271   1227    113    -39     28       C  
ATOM    480  CD1 LEU A1062      30.633 -33.635 -32.815  1.00 10.45           C  
ANISOU  480  CD1 LEU A1062     1243   1229   1497      8   -148    128       C  
ATOM    481  CD2 LEU A1062      32.216 -32.609 -31.200  1.00 10.31           C  
ANISOU  481  CD2 LEU A1062     1406   1460   1052    186   -114     21       C  
ATOM    482  N   ASP A1063      34.401 -36.482 -33.512  1.00  8.92           N  
ANISOU  482  N   ASP A1063     1088   1417    883    -45   -108     23       N  
ATOM    483  CA  ASP A1063      35.364 -36.379 -34.610  1.00  9.94           C  
ANISOU  483  CA  ASP A1063     1291   1509    976    -82      7     84       C  
ATOM    484  C   ASP A1063      34.942 -37.263 -35.787  1.00  9.98           C  
ANISOU  484  C   ASP A1063     1366   1418   1008     -8    117     10       C  
ATOM    485  O   ASP A1063      35.060 -36.868 -36.953  1.00 11.24           O  
ANISOU  485  O   ASP A1063     1769   1482   1020   -122    138     72       O  
ATOM    486  CB  ASP A1063      36.767 -36.771 -34.147  1.00 11.41           C  
ANISOU  486  CB  ASP A1063     1217   1696   1420    -91     17     13       C  
ATOM    487  CG  ASP A1063      37.416 -35.725 -33.216  1.00 14.46           C  
ANISOU  487  CG  ASP A1063     1618   2256   1618   -463    -53   -156       C  
ATOM    488  OD1 ASP A1063      36.935 -34.567 -33.145  1.00 17.22           O  
ANISOU  488  OD1 ASP A1063     1953   2662   1926   -276     98   -560       O  
ATOM    489  OD2 ASP A1063      38.439 -36.075 -32.579  1.00 18.57           O  
ANISOU  489  OD2 ASP A1063     1837   3448   1769   -553   -447   -181       O  
ATOM    490  N   THR A1064      34.409 -38.432 -35.486  1.00  9.30           N  
ANISOU  490  N   THR A1064     1348   1311    873    114    -46     97       N  
ATOM    491  CA  THR A1064      33.983 -39.364 -36.506  1.00 10.06           C  
ANISOU  491  CA  THR A1064     1441   1397    984     54     -2     -9       C  
ATOM    492  C   THR A1064      32.751 -38.842 -37.250  1.00 10.16           C  
ANISOU  492  C   THR A1064     1514   1413    934    -31   -112     57       C  
ATOM    493  O   THR A1064      32.711 -38.869 -38.507  1.00 11.96           O  
ANISOU  493  O   THR A1064     1837   1792    914   -231   -102   -138       O  
ATOM    494  CB  THR A1064      33.691 -40.734 -35.881  1.00 10.89           C  
ANISOU  494  CB  THR A1064     1574   1406   1157    102    -25     41       C  
ATOM    495  OG1 THR A1064      34.870 -41.180 -35.213  1.00 11.28           O  
ANISOU  495  OG1 THR A1064     1445   1645   1195    232    132    -26       O  
ATOM    496  CG2 THR A1064      33.314 -41.768 -36.946  1.00 12.24           C  
ANISOU  496  CG2 THR A1064     1773   1575   1301     87    -71    -78       C  
ATOM    497  N  AVAL A1065      31.753 -38.355 -36.520  0.50 10.22           N  
ANISOU  497  N  AVAL A1065     1447   1363   1073    108   -212     33       N  
ATOM    498  N  BVAL A1065      31.766 -38.350 -36.502  0.50 10.25           N  
ANISOU  498  N  BVAL A1065     1469   1356   1068     87   -196     26       N  
ATOM    499  CA AVAL A1065      30.556 -37.834 -37.184  0.50 11.96           C  
ANISOU  499  CA AVAL A1065     1517   1842   1184    102   -395      1       C  
ATOM    500  CA BVAL A1065      30.541 -37.788 -37.086  0.50 12.14           C  
ANISOU  500  CA BVAL A1065     1563   1816   1233     68   -435      0       C  
ATOM    501  C  AVAL A1065      30.848 -36.543 -37.937  0.50 11.05           C  
ANISOU  501  C  AVAL A1065     1500   1699    999    230   -405   -122       C  
ATOM    502  C  BVAL A1065      30.845 -36.551 -37.912  0.50 11.08           C  
ANISOU  502  C  BVAL A1065     1511   1690   1008    229   -399   -120       C  
ATOM    503  O  AVAL A1065      30.241 -36.285 -38.975  0.50 14.75           O  
ANISOU  503  O  AVAL A1065     2205   2336   1063    352   -521    211       O  
ATOM    504  O  BVAL A1065      30.246 -36.339 -38.963  0.50 14.49           O  
ANISOU  504  O  BVAL A1065     2196   2244   1065    368   -516    206       O  
ATOM    505  CB AVAL A1065      29.348 -37.670 -36.230  0.50 13.47           C  
ANISOU  505  CB AVAL A1065     1218   2187   1711    201   -346    181       C  
ATOM    506  CB BVAL A1065      29.490 -37.468 -35.988  0.50 14.14           C  
ANISOU  506  CB BVAL A1065     1438   2209   1725     11   -215     44       C  
ATOM    507  CG1AVAL A1065      29.071 -38.972 -35.500  0.50 14.48           C  
ANISOU  507  CG1AVAL A1065     1535   2233   1734     78   -271    158       C  
ATOM    508  CG1BVAL A1065      28.315 -36.648 -36.530  0.50 14.98           C  
ANISOU  508  CG1BVAL A1065     1725   2106   1858     56   -232    230       C  
ATOM    509  CG2AVAL A1065      29.545 -36.537 -35.253  0.50 16.27           C  
ANISOU  509  CG2AVAL A1065     1951   2312   1918     93   -110     27       C  
ATOM    510  CG2BVAL A1065      28.995 -38.764 -35.370  0.50 16.35           C  
ANISOU  510  CG2BVAL A1065     1896   2310   2006    -46   -171    177       C  
ATOM    511  N   GLY A1066      31.793 -35.743 -37.450  1.00 11.08           N  
ANISOU  511  N   GLY A1066     1784   1852    572    111   -645     73       N  
ATOM    512  CA  GLY A1066      32.128 -34.467 -38.112  1.00 12.24           C  
ANISOU  512  CA  GLY A1066     2113   1421   1116    373   -285   -110       C  
ATOM    513  C   GLY A1066      33.118 -34.561 -39.263  1.00 13.20           C  
ANISOU  513  C   GLY A1066     2348   1385   1280    274    -95     96       C  
ATOM    514  O   GLY A1066      33.303 -33.588 -40.013  1.00 15.59           O  
ANISOU  514  O   GLY A1066     3595   1201   1127    546     11     23       O  
ATOM    515  N   GLN A1067      33.758 -35.717 -39.430  1.00 14.07           N  
ANISOU  515  N   GLN A1067     2474   1509   1363    399    -18    -98       N  
ATOM    516  CA  GLN A1067      34.791 -35.841 -40.472  1.00 15.80           C  
ANISOU  516  CA  GLN A1067     2391   1726   1887    489    147    -92       C  
ATOM    517  C   GLN A1067      34.211 -35.588 -41.852  1.00 18.09           C  
ANISOU  517  C   GLN A1067     2945   2047   1879    532     12   -455       C  
ATOM    518  O   GLN A1067      33.157 -36.114 -42.191  1.00 16.86           O  
ANISOU  518  O   GLN A1067     3019   1954   1430    823   -579   -507       O  
ATOM    519  CB  GLN A1067      35.450 -37.205 -40.423  1.00 16.42           C  
ANISOU  519  CB  GLN A1067     2578   1585   2074    382     89    -76       C  
ATOM    520  CG  GLN A1067      36.658 -37.312 -41.337  1.00 19.00           C  
ANISOU  520  CG  GLN A1067     2816   2166   2236    249    295    -49       C  
ATOM    521  CD  GLN A1067      37.413 -38.610 -41.206  1.00 17.10           C  
ANISOU  521  CD  GLN A1067     2223   1889   2384   -109    314   -111       C  
ATOM    522  OE1 GLN A1067      36.849 -39.642 -40.854  1.00 12.83           O  
ANISOU  522  OE1 GLN A1067     1868   1656   1350    284    147    111       O  
ATOM    523  NE2 GLN A1067      38.709 -38.571 -41.529  1.00 25.07           N  
ANISOU  523  NE2 GLN A1067     2452   2872   4199   -245    902    178       N  
ATOM    524  N   GLY A1068      34.901 -34.731 -42.618  1.00 21.41           N  
ANISOU  524  N   GLY A1068     3498   2488   2148    634    167    -54       N  
ATOM    525  CA  GLY A1068      34.464 -34.335 -43.943  1.00 23.43           C  
ANISOU  525  CA  GLY A1068     3673   2752   2476    659   -176    212       C  
ATOM    526  C   GLY A1068      33.145 -33.576 -44.025  1.00 22.14           C  
ANISOU  526  C   GLY A1068     3743   2603   2065    811    133    -45       C  
ATOM    527  O   GLY A1068      32.574 -33.455 -45.092  1.00 32.43           O  
ANISOU  527  O   GLY A1068     5243   4714   2363   1244   -543   -405       O  
ATOM    528  N   VAL A1069      32.669 -33.064 -42.899  1.00 19.53           N  
ANISOU  528  N   VAL A1069     3550   1989   1880    889   -145     88       N  
ATOM    529  CA  VAL A1069      31.449 -32.270 -42.827  1.00 19.87           C  
ANISOU  529  CA  VAL A1069     2871   2487   2191    446   -173    179       C  
ATOM    530  C   VAL A1069      31.921 -30.848 -42.716  1.00 17.45           C  
ANISOU  530  C   VAL A1069     2860   2329   1441    654   -359    -87       C  
ATOM    531  O   VAL A1069      32.786 -30.538 -41.885  1.00 20.41           O  
ANISOU  531  O   VAL A1069     2819   2599   2335    604   -739     19       O  
ATOM    532  CB  VAL A1069      30.607 -32.655 -41.601  1.00 22.04           C  
ANISOU  532  CB  VAL A1069     3151   2651   2572    107     51    124       C  
ATOM    533  CG1 VAL A1069      29.390 -31.746 -41.465  1.00 23.05           C  
ANISOU  533  CG1 VAL A1069     3183   2863   2709    360   -392    827       C  
ATOM    534  CG2 VAL A1069      30.210 -34.117 -41.697  1.00 23.41           C  
ANISOU  534  CG2 VAL A1069     3458   2487   2947    188   -323    552       C  
ATOM    535  N   ALA A1070      31.413 -29.982 -43.587  1.00 14.58           N  
ANISOU  535  N   ALA A1070     2586   1670   1281    426   -111   -223       N  
ATOM    536  CA  ALA A1070      31.700 -28.554 -43.475  1.00 15.45           C  
ANISOU  536  CA  ALA A1070     2356   1833   1680    283    -55   -252       C  
ATOM    537  C   ALA A1070      30.899 -28.006 -42.319  1.00 18.27           C  
ANISOU  537  C   ALA A1070     2493   2648   1798    544    -37   -428       C  
ATOM    538  O   ALA A1070      29.688 -28.174 -42.268  1.00 21.24           O  
ANISOU  538  O   ALA A1070     2451   3473   2146    758    253   -388       O  
ATOM    539  CB  ALA A1070      31.328 -27.835 -44.756  1.00 17.63           C  
ANISOU  539  CB  ALA A1070     2586   2071   2041    540    116    218       C  
ATOM    540  N   VAL A1071      31.607 -27.381 -41.381  1.00 22.37           N  
ANISOU  540  N   VAL A1071     2870   3035   2593    -40    -99   -614       N  
ATOM    541  CA  VAL A1071      31.061 -26.967 -40.111  1.00 21.21           C  
ANISOU  541  CA  VAL A1071     2798   2896   2363    286   -141   -214       C  
ATOM    542  C   VAL A1071      31.115 -25.457 -40.141  1.00 20.46           C  
ANISOU  542  C   VAL A1071     2605   2903   2264    119   -116   -270       C  
ATOM    543  O   VAL A1071      32.152 -24.872 -40.492  1.00 22.40           O  
ANISOU  543  O   VAL A1071     3220   2828   2461    -76    421   -498       O  
ATOM    544  CB  VAL A1071      31.879 -27.573 -38.914  1.00 20.77           C  
ANISOU  544  CB  VAL A1071     2582   2754   2553    555    244    242       C  
ATOM    545  CG1 VAL A1071      31.544 -26.928 -37.584  1.00 22.49           C  
ANISOU  545  CG1 VAL A1071     2928   2867   2747    181   -103    -16       C  
ATOM    546  CG2 VAL A1071      31.603 -29.063 -38.817  1.00 22.82           C  
ANISOU  546  CG2 VAL A1071     3314   3006   2349     -1    537   -190       C  
ATOM    547  N   SER A1072      29.988 -24.834 -39.811  1.00 17.87           N  
ANISOU  547  N   SER A1072     2336   2594   1857    -26   -297     50       N  
ATOM    548  CA  SER A1072      29.931 -23.401 -39.637  1.00 17.48           C  
ANISOU  548  CA  SER A1072     2117   2590   1932    476    -55    225       C  
ATOM    549  C   SER A1072      29.032 -23.077 -38.457  1.00 15.96           C  
ANISOU  549  C   SER A1072     1972   2365   1725    582   -312    169       C  
ATOM    550  O   SER A1072      28.500 -23.948 -37.767  1.00 15.53           O  
ANISOU  550  O   SER A1072     2042   2181   1675    363   -288   -288       O  
ATOM    551  CB  SER A1072      29.445 -22.692 -40.908  1.00 20.22           C  
ANISOU  551  CB  SER A1072     2674   3288   1718    403    163    454       C  
ATOM    552  OG  SER A1072      29.818 -21.304 -40.848  1.00 25.77           O  
ANISOU  552  OG  SER A1072     3259   3755   2777      7    399    944       O  
ATOM    553  N   MET A1073      28.882 -21.794 -38.207  1.00 15.48           N  
ANISOU  553  N   MET A1073     2010   2204   1665    123   -350    387       N  
ATOM    554  CA  MET A1073      28.005 -21.343 -37.159  1.00 16.90           C  
ANISOU  554  CA  MET A1073     2563   2002   1854    156   -222    143       C  
ATOM    555  C   MET A1073      26.613 -21.881 -37.450  1.00 16.10           C  
ANISOU  555  C   MET A1073     2561   1925   1630    206   -371    170       C  
ATOM    556  O   MET A1073      26.175 -21.856 -38.605  1.00 16.50           O  
ANISOU  556  O   MET A1073     2385   2245   1636    -65   -326    233       O  
ATOM    557  CB  MET A1073      28.082 -19.833 -37.140  1.00 21.40           C  
ANISOU  557  CB  MET A1073     3221   2060   2849     -9    -98    311       C  
ATOM    558  CG  MET A1073      27.348 -19.192 -36.028  1.00 29.58           C  
ANISOU  558  CG  MET A1073     4412   3338   3488    178    423   -154       C  
ATOM    559  SD  MET A1073      25.624 -19.196 -36.462  1.00 34.08           S  
ANISOU  559  SD  MET A1073     4661   3343   4941   -423    562   -318       S  
ATOM    560  CE  MET A1073      25.563 -17.963 -37.779  1.00 34.11           C  
ANISOU  560  CE  MET A1073     4097   3640   5222    918    858    219       C  
ATOM    561  N   GLY A1074      25.968 -22.441 -36.424  1.00 14.91           N  
ANISOU  561  N   GLY A1074     2173   1815   1675    133   -480     51       N  
ATOM    562  CA  GLY A1074      24.651 -23.049 -36.531  1.00 16.31           C  
ANISOU  562  CA  GLY A1074     2141   1986   2068    184   -416     94       C  
ATOM    563  C   GLY A1074      24.649 -24.527 -36.886  1.00 16.45           C  
ANISOU  563  C   GLY A1074     2157   2067   2025    295   -547     53       C  
ATOM    564  O   GLY A1074      23.606 -25.158 -36.872  1.00 19.46           O  
ANISOU  564  O   GLY A1074     2255   2029   3110    292   -948    212       O  
ATOM    565  N   THR A1075      25.814 -25.103 -37.157  1.00 13.85           N  
ANISOU  565  N   THR A1075     2086   1718   1459    157   -350    499       N  
ATOM    566  CA  THR A1075      25.882 -26.547 -37.389  1.00 14.17           C  
ANISOU  566  CA  THR A1075     2354   1750   1280    119   -321    398       C  
ATOM    567  C   THR A1075      25.485 -27.312 -36.106  1.00 13.23           C  
ANISOU  567  C   THR A1075     2063   1710   1253     21   -336    309       C  
ATOM    568  O   THR A1075      25.907 -26.928 -35.022  1.00 13.40           O  
ANISOU  568  O   THR A1075     1971   1644   1475      2   -507    206       O  
ATOM    569  CB  THR A1075      27.271 -26.976 -37.864  1.00 17.04           C  
ANISOU  569  CB  THR A1075     2496   2312   1665    192   -121    239       C  
ATOM    570  OG1 THR A1075      27.553 -26.426 -39.164  1.00 19.29           O  
ANISOU  570  OG1 THR A1075     3274   2450   1606    -12    133     61       O  
ATOM    571  CG2 THR A1075      27.364 -28.478 -37.949  1.00 20.14           C  
ANISOU  571  CG2 THR A1075     3040   2347   2264     -2    325    -94       C  
ATOM    572  N   VAL A1076      24.697 -28.381 -36.266  1.00 13.46           N  
ANISOU  572  N   VAL A1076     2097   1619   1396     67   -556    329       N  
ATOM    573  CA  VAL A1076      24.277 -29.270 -35.186  1.00 12.31           C  
ANISOU  573  CA  VAL A1076     2013   1546   1116    -27   -265    -72       C  
ATOM    574  C   VAL A1076      24.665 -30.707 -35.513  1.00 12.21           C  
ANISOU  574  C   VAL A1076     1982   1480   1177    -50   -573   -103       C  
ATOM    575  O   VAL A1076      24.216 -31.253 -36.527  1.00 15.58           O  
ANISOU  575  O   VAL A1076     2563   1807   1547    208  -1067   -359       O  
ATOM    576  CB  VAL A1076      22.759 -29.214 -34.951  1.00 16.20           C  
ANISOU  576  CB  VAL A1076     2008   2097   2050     74   -405   -115       C  
ATOM    577  CG1 VAL A1076      22.331 -30.114 -33.802  1.00 18.31           C  
ANISOU  577  CG1 VAL A1076     2267   2294   2394   -209   -209    -84       C  
ATOM    578  CG2 VAL A1076      22.311 -27.785 -34.701  1.00 17.38           C  
ANISOU  578  CG2 VAL A1076     2069   2026   2506     89   -268     89       C  
ATOM    579  N   LEU A1077      25.479 -31.311 -34.657  1.00 11.35           N  
ANISOU  579  N   LEU A1077     1883   1385   1044   -147   -392      4       N  
ATOM    580  CA  LEU A1077      25.936 -32.698 -34.819  1.00 11.08           C  
ANISOU  580  CA  LEU A1077     1754   1398   1055   -109   -283     96       C  
ATOM    581  C   LEU A1077      25.514 -33.542 -33.624  1.00 10.25           C  
ANISOU  581  C   LEU A1077     1706   1326    862   -137   -213   -119       C  
ATOM    582  O   LEU A1077      25.750 -33.149 -32.486  1.00 11.79           O  
ANISOU  582  O   LEU A1077     2099   1486    893      8   -412   -172       O  
ATOM    583  CB  LEU A1077      27.448 -32.758 -34.979  1.00 12.47           C  
ANISOU  583  CB  LEU A1077     1776   1517   1444    105   -204    219       C  
ATOM    584  CG  LEU A1077      28.030 -32.030 -36.203  1.00 14.00           C  
ANISOU  584  CG  LEU A1077     1811   1832   1673     62      6    312       C  
ATOM    585  CD1 LEU A1077      29.536 -32.045 -36.190  1.00 16.15           C  
ANISOU  585  CD1 LEU A1077     1839   2100   2195     90     17    217       C  
ATOM    586  CD2 LEU A1077      27.563 -32.656 -37.520  1.00 17.82           C  
ANISOU  586  CD2 LEU A1077     2371   2524   1874     43   -164    105       C  
ATOM    587  N   LYS A1078      24.971 -34.724 -33.898  1.00 10.46           N  
ANISOU  587  N   LYS A1078     1595   1230   1149     52   -135   -308       N  
ATOM    588  CA  LYS A1078      24.454 -35.629 -32.886  1.00 10.67           C  
ANISOU  588  CA  LYS A1078     1493   1360   1199     59   -330   -118       C  
ATOM    589  C   LYS A1078      25.448 -36.740 -32.552  1.00 10.48           C  
ANISOU  589  C   LYS A1078     1430   1293   1256      5   -301   -136       C  
ATOM    590  O   LYS A1078      25.987 -37.370 -33.432  1.00 11.80           O  
ANISOU  590  O   LYS A1078     1641   1623   1219    -39   -257   -236       O  
ATOM    591  CB  LYS A1078      23.137 -36.230 -33.361  1.00 11.82           C  
ANISOU  591  CB  LYS A1078     1522   1547   1419     43   -416   -114       C  
ATOM    592  CG  LYS A1078      22.499 -37.225 -32.440  1.00 14.41           C  
ANISOU  592  CG  LYS A1078     1941   1866   1668    -65   -347    112       C  
ATOM    593  CD  LYS A1078      21.223 -37.818 -33.031  1.00 18.04           C  
ANISOU  593  CD  LYS A1078     1977   2655   2218   -224   -486    219       C  
ATOM    594  CE  LYS A1078      21.573 -38.811 -34.125  1.00 22.90           C  
ANISOU  594  CE  LYS A1078     2991   2931   2776   -115   -420   -157       C  
ATOM    595  NZ  LYS A1078      20.362 -39.499 -34.590  1.00 31.45           N  
ANISOU  595  NZ  LYS A1078     3798   3556   4593   -771   -836     29       N  
ATOM    596  N   THR A1079      25.701 -36.946 -31.260  1.00 10.24           N  
ANISOU  596  N   THR A1079     1415   1241   1233    193   -225   -136       N  
ATOM    597  CA  THR A1079      26.436 -38.132 -30.792  1.00  9.28           C  
ANISOU  597  CA  THR A1079     1304   1108   1113     71   -117   -102       C  
ATOM    598  C   THR A1079      25.637 -38.827 -29.695  1.00  8.52           C  
ANISOU  598  C   THR A1079     1092   1049   1096     55   -142   -213       C  
ATOM    599  O   THR A1079      24.689 -38.266 -29.163  1.00  9.33           O  
ANISOU  599  O   THR A1079     1062   1070   1410     12     60   -192       O  
ATOM    600  CB  THR A1079      27.829 -37.781 -30.225  1.00  9.11           C  
ANISOU  600  CB  THR A1079     1188   1060   1210     18      0     12       C  
ATOM    601  OG1 THR A1079      27.691 -37.047 -29.004  1.00  9.17           O  
ANISOU  601  OG1 THR A1079      990   1356   1138   -161   -185    -83       O  
ATOM    602  CG2 THR A1079      28.691 -37.015 -31.188  1.00  9.17           C  
ANISOU  602  CG2 THR A1079     1193    998   1293     14    150   -152       C  
ATOM    603  N   SER A1080      26.010 -40.054 -29.364  1.00  8.32           N  
ANISOU  603  N   SER A1080     1065   1074   1020     37   -232   -211       N  
ATOM    604  CA  SER A1080      25.578 -40.663 -28.118  1.00  9.41           C  
ANISOU  604  CA  SER A1080     1175   1209   1189    -57   -226      4       C  
ATOM    605  C   SER A1080      26.215 -39.952 -26.912  1.00  9.90           C  
ANISOU  605  C   SER A1080     1459   1249   1052    -58   -228     74       C  
ATOM    606  O   SER A1080      27.083 -39.081 -27.059  1.00 10.41           O  
ANISOU  606  O   SER A1080     1578   1356   1019   -147   -355    219       O  
ATOM    607  CB  SER A1080      25.897 -42.161 -28.122  1.00 11.36           C  
ANISOU  607  CB  SER A1080     1655   1166   1495   -196   -165     79       C  
ATOM    608  OG  SER A1080      27.264 -42.410 -28.048  1.00 15.81           O  
ANISOU  608  OG  SER A1080     1777   1632   2596    -85    134    -35       O  
ATOM    609  N   SER A1081      25.777 -40.364 -25.732  1.00  9.74           N  
ANISOU  609  N   SER A1081     1202   1276   1223    -45      0     77       N  
ATOM    610  CA  SER A1081      26.103 -39.698 -24.471  1.00 10.92           C  
ANISOU  610  CA  SER A1081     1582   1381   1185    276   -115     39       C  
ATOM    611  C   SER A1081      27.292 -40.240 -23.702  1.00 10.62           C  
ANISOU  611  C   SER A1081     1376   1395   1263     88   -162   -110       C  
ATOM    612  O   SER A1081      27.797 -39.562 -22.808  1.00 11.09           O  
ANISOU  612  O   SER A1081     1836   1089   1287    208   -396    -19       O  
ATOM    613  CB  SER A1081      24.875 -39.779 -23.553  1.00 13.36           C  
ANISOU  613  CB  SER A1081     1110   1960   2006    415   -131    110       C  
ATOM    614  OG  SER A1081      24.461 -41.131 -23.470  1.00 18.62           O  
ANISOU  614  OG  SER A1081     1843   2254   2978    220    625    775       O  
ATOM    615  N   TRP A1082      27.714 -41.457 -24.007  1.00 10.11           N  
ANISOU  615  N   TRP A1082     1393   1406   1042     97    -38    -52       N  
ATOM    616  CA  TRP A1082      28.846 -42.118 -23.313  1.00 10.25           C  
ANISOU  616  CA  TRP A1082     1255   1352   1285     10    -41    -66       C  
ATOM    617  C   TRP A1082      28.603 -42.167 -21.797  1.00 10.76           C  
ANISOU  617  C   TRP A1082     1286   1459   1343   -314     42    252       C  
ATOM    618  O   TRP A1082      27.584 -42.723 -21.367  1.00 15.58           O  
ANISOU  618  O   TRP A1082     1640   2391   1886   -537    406    514       O  
ATOM    619  CB  TRP A1082      30.185 -41.514 -23.779  1.00  9.92           C  
ANISOU  619  CB  TRP A1082     1346   1224   1199     -2    -26     43       C  
ATOM    620  CG  TRP A1082      30.349 -41.806 -25.231  1.00 11.16           C  
ANISOU  620  CG  TRP A1082     1545   1391   1302   -151    -30   -141       C  
ATOM    621  CD1 TRP A1082      29.964 -41.032 -26.288  1.00 11.53           C  
ANISOU  621  CD1 TRP A1082     1649   1310   1420   -157     -9    -64       C  
ATOM    622  CD2 TRP A1082      30.808 -43.029 -25.776  1.00 11.65           C  
ANISOU  622  CD2 TRP A1082     1522   1416   1488   -188     57   -211       C  
ATOM    623  NE1 TRP A1082      30.205 -41.690 -27.453  1.00 12.51           N  
ANISOU  623  NE1 TRP A1082     1872   1503   1376   -241    -24    -55       N  
ATOM    624  CE2 TRP A1082      30.716 -42.922 -27.172  1.00 12.18           C  
ANISOU  624  CE2 TRP A1082     1752   1406   1467   -184    214   -338       C  
ATOM    625  CE3 TRP A1082      31.312 -44.208 -25.217  1.00 11.96           C  
ANISOU  625  CE3 TRP A1082     1665   1321   1555   -195     56   -285       C  
ATOM    626  CZ2 TRP A1082      31.134 -43.933 -28.019  1.00 13.70           C  
ANISOU  626  CZ2 TRP A1082     2063   1244   1897    -49     -2   -490       C  
ATOM    627  CZ3 TRP A1082      31.716 -45.207 -26.065  1.00 13.64           C  
ANISOU  627  CZ3 TRP A1082     1671   1601   1908   -154    -28   -608       C  
ATOM    628  CH2 TRP A1082      31.606 -45.070 -27.438  1.00 15.51           C  
ANISOU  628  CH2 TRP A1082     3132   1018   1743    700    323   -867       C  
ATOM    629  N   ASN A1083      29.472 -41.581 -20.988  1.00  9.71           N  
ANISOU  629  N   ASN A1083      742   1144   1803   -548    371    237       N  
ATOM    630  CA  ASN A1083      29.307 -41.659 -19.539  1.00 11.73           C  
ANISOU  630  CA  ASN A1083     1432   1361   1662    -54    167    207       C  
ATOM    631  C   ASN A1083      28.429 -40.538 -18.954  1.00 11.89           C  
ANISOU  631  C   ASN A1083     1530   1675   1312     70    304    181       C  
ATOM    632  O   ASN A1083      28.257 -40.473 -17.744  1.00 14.45           O  
ANISOU  632  O   ASN A1083     1783   2392   1314    -60    427    284       O  
ATOM    633  CB  ASN A1083      30.664 -41.706 -18.861  1.00 11.94           C  
ANISOU  633  CB  ASN A1083     1520   1641   1375   -147    199    296       C  
ATOM    634  CG  ASN A1083      30.573 -42.112 -17.410  1.00 11.89           C  
ANISOU  634  CG  ASN A1083     1498   1599   1419   -248    -51    435       C  
ATOM    635  OD1 ASN A1083      30.064 -43.176 -17.097  1.00 15.81           O  
ANISOU  635  OD1 ASN A1083     2256   1815   1936   -573   -299    710       O  
ATOM    636  ND2 ASN A1083      31.094 -41.266 -16.522  1.00 12.13           N  
ANISOU  636  ND2 ASN A1083     1452   1625   1532   -432   -161    475       N  
ATOM    637  N   LEU A1084      27.843 -39.684 -19.796  1.00 11.44           N  
ANISOU  637  N   LEU A1084     1439   1636   1272    -21    111     87       N  
ATOM    638  CA  LEU A1084      26.777 -38.780 -19.348  1.00 12.67           C  
ANISOU  638  CA  LEU A1084     1506   1903   1404    127     93     39       C  
ATOM    639  C   LEU A1084      25.490 -39.567 -19.141  1.00 13.75           C  
ANISOU  639  C   LEU A1084     1779   1702   1743      8    318    -73       C  
ATOM    640  O   LEU A1084      25.285 -40.620 -19.749  1.00 18.54           O  
ANISOU  640  O   LEU A1084     2062   1909   3072   -297    592   -504       O  
ATOM    641  CB  LEU A1084      26.510 -37.684 -20.394  1.00 13.01           C  
ANISOU  641  CB  LEU A1084     1651   1791   1498    187    -26      0       C  
ATOM    642  CG  LEU A1084      27.678 -36.770 -20.701  1.00 15.47           C  
ANISOU  642  CG  LEU A1084     1879   2138   1860     53    141    117       C  
ATOM    643  CD1 LEU A1084      27.484 -35.935 -21.958  1.00 16.11           C  
ANISOU  643  CD1 LEU A1084     2146   1992   1982    -42    117    171       C  
ATOM    644  CD2 LEU A1084      28.049 -35.914 -19.506  1.00 16.49           C  
ANISOU  644  CD2 LEU A1084     2156   2239   1868   -255   -160    246       C  
ATOM    645  N   ASP A1085      24.595 -39.004 -18.328  1.00 14.39           N  
ANISOU  645  N   ASP A1085     1695   2108   1662    -56    284   -197       N  
ATOM    646  CA  ASP A1085      23.350 -39.678 -17.968  1.00 15.96           C  
ANISOU  646  CA  ASP A1085     1698   2141   2223    -52    241    -16       C  
ATOM    647  C   ASP A1085      22.193 -39.285 -18.889  1.00 17.76           C  
ANISOU  647  C   ASP A1085     1820   2820   2107    -37    190    193       C  
ATOM    648  O   ASP A1085      21.084 -39.044 -18.411  1.00 27.35           O  
ANISOU  648  O   ASP A1085     1896   5714   2780    254    250    130       O  
ATOM    649  CB  ASP A1085      22.987 -39.356 -16.509  1.00 19.71           C  
ANISOU  649  CB  ASP A1085     2528   2672   2289    -10    486     52       C  
ATOM    650  CG  ASP A1085      24.044 -39.790 -15.509  1.00 29.57           C  
ANISOU  650  CG  ASP A1085     3531   4174   3529    456   -256    407       C  
ATOM    651  OD1 ASP A1085      24.693 -40.840 -15.718  1.00 39.78           O  
ANISOU  651  OD1 ASP A1085     5323   4943   4848   1350    326    352       O  
ATOM    652  OD2 ASP A1085      24.210 -39.073 -14.485  1.00 39.84           O  
ANISOU  652  OD2 ASP A1085     5143   5806   4188    655     38   -546       O  
ATOM    653  N   CYS A1086      22.454 -39.192 -20.192  1.00 14.70           N  
ANISOU  653  N   CYS A1086     1534   1972   2077    163     20     46       N  
ATOM    654  CA ACYS A1086      21.473 -38.843 -21.216  0.50 14.13           C  
ANISOU  654  CA ACYS A1086     1648   1733   1986    126     50     92       C  
ATOM    655  CA BCYS A1086      21.419 -38.879 -21.173  0.50 13.17           C  
ANISOU  655  CA BCYS A1086     1498   1562   1944     65    100    145       C  
ATOM    656  C   CYS A1086      21.508 -39.889 -22.323  1.00 13.43           C  
ANISOU  656  C   CYS A1086     1402   1661   2037     76    -47     67       C  
ATOM    657  O   CYS A1086      22.221 -40.888 -22.227  1.00 16.84           O  
ANISOU  657  O   CYS A1086     2038   1850   2508    469   -223      8       O  
ATOM    658  CB ACYS A1086      21.811 -37.467 -21.809  0.50 16.34           C  
ANISOU  658  CB ACYS A1086     1954   1832   2420    145    114    277       C  
ATOM    659  CB BCYS A1086      21.530 -37.411 -21.642  0.50 12.14           C  
ANISOU  659  CB BCYS A1086     1288   1475   1846    125     97      0       C  
ATOM    660  SG ACYS A1086      22.151 -36.247 -20.541  0.50 18.67           S  
ANISOU  660  SG ACYS A1086     2407   1943   2744    -98     82    242       S  
ATOM    661  SG BCYS A1086      23.093 -36.924 -22.361  0.50 12.02           S  
ANISOU  661  SG BCYS A1086     1338   1275   1954     59    109    131       S  
ATOM    662  N   ARG A1087      20.737 -39.672 -23.375  1.00 12.69           N  
ANISOU  662  N   ARG A1087     1518   1393   1908    137     46    223       N  
ATOM    663  CA  ARG A1087      20.763 -40.567 -24.524  1.00 13.72           C  
ANISOU  663  CA  ARG A1087     1538   1627   2047     33     31      9       C  
ATOM    664  C   ARG A1087      21.645 -39.986 -25.621  1.00 12.63           C  
ANISOU  664  C   ARG A1087     1628   1249   1921     53     17   -134       C  
ATOM    665  O   ARG A1087      22.520 -40.666 -26.142  1.00 14.10           O  
ANISOU  665  O   ARG A1087     1776   1428   2153     63    323     27       O  
ATOM    666  CB  ARG A1087      19.327 -40.834 -25.007  1.00 15.66           C  
ANISOU  666  CB  ARG A1087     1701   1929   2319   -122   -150    112       C  
ATOM    667  CG  ARG A1087      19.241 -41.817 -26.152  1.00 16.62           C  
ANISOU  667  CG  ARG A1087     2122   1887   2304      2     87    113       C  
ATOM    668  CD  ARG A1087      17.815 -41.947 -26.649  1.00 20.65           C  
ANISOU  668  CD  ARG A1087     2233   2539   3073   -136      0     33       C  
ATOM    669  NE  ARG A1087      17.030 -42.601 -25.612  1.00 21.52           N  
ANISOU  669  NE  ARG A1087     2047   2496   3630   -342     60    188       N  
ATOM    670  CZ  ARG A1087      16.388 -43.764 -25.743  1.00 27.73           C  
ANISOU  670  CZ  ARG A1087     2828   3152   4556  -1029   -199   -266       C  
ATOM    671  NH1 ARG A1087      16.324 -44.419 -26.907  1.00 31.75           N  
ANISOU  671  NH1 ARG A1087     3313   3290   5460  -1271    637   -923       N  
ATOM    672  NH2 ARG A1087      15.748 -44.250 -24.697  1.00 34.25           N  
ANISOU  672  NH2 ARG A1087     3572   4408   5033  -1303    125     91       N  
ATOM    673  N   TYR A1088      21.399 -38.723 -25.974  1.00  9.63           N  
ANISOU  673  N   TYR A1088      749   1180   1730    424    596   -426       N  
ATOM    674  CA  TYR A1088      22.136 -38.064 -27.029  1.00 10.17           C  
ANISOU  674  CA  TYR A1088     1075   1389   1400    -16    118   -219       C  
ATOM    675  C   TYR A1088      22.640 -36.715 -26.594  1.00  8.91           C  
ANISOU  675  C   TYR A1088     1139   1184   1063    148    192   -127       C  
ATOM    676  O   TYR A1088      22.049 -36.042 -25.750  1.00 10.85           O  
ANISOU  676  O   TYR A1088     1244   1131   1747     98    392   -388       O  
ATOM    677  CB  TYR A1088      21.265 -37.801 -28.260  1.00 10.54           C  
ANISOU  677  CB  TYR A1088     1279   1324   1402   -126     14    -85       C  
ATOM    678  CG  TYR A1088      20.705 -39.034 -28.949  1.00 11.75           C  
ANISOU  678  CG  TYR A1088     1409   1221   1833    -61   -270    -69       C  
ATOM    679  CD1 TYR A1088      21.532 -39.915 -29.635  1.00 13.66           C  
ANISOU  679  CD1 TYR A1088     1561   1945   1684     78   -251   -284       C  
ATOM    680  CD2 TYR A1088      19.331 -39.294 -28.950  1.00 14.83           C  
ANISOU  680  CD2 TYR A1088     1538   1781   2313   -367    -45   -321       C  
ATOM    681  CE1 TYR A1088      21.022 -41.035 -30.280  1.00 13.87           C  
ANISOU  681  CE1 TYR A1088     1245   1935   2089     19   -417   -195       C  
ATOM    682  CE2 TYR A1088      18.814 -40.422 -29.596  1.00 15.19           C  
ANISOU  682  CE2 TYR A1088     1853   1861   2057   -359   -287   -307       C  
ATOM    683  CZ  TYR A1088      19.657 -41.284 -30.257  1.00 13.99           C  
ANISOU  683  CZ  TYR A1088     1339   1829   2146   -239   -611   -210       C  
ATOM    684  OH  TYR A1088      19.180 -42.398 -30.918  1.00 17.19           O  
ANISOU  684  OH  TYR A1088     1995   1657   2876   -208   -591   -415       O  
ATOM    685  N   VAL A1089      23.747 -36.325 -27.207  1.00  8.00           N  
ANISOU  685  N   VAL A1089     1103    855   1079    342    434   -503       N  
ATOM    686  CA  VAL A1089      24.244 -34.960 -27.114  1.00  8.76           C  
ANISOU  686  CA  VAL A1089     1072   1077   1176     73     78   -206       C  
ATOM    687  C   VAL A1089      24.105 -34.305 -28.485  1.00  8.81           C  
ANISOU  687  C   VAL A1089      917   1173   1256    -64     77    -70       C  
ATOM    688  O   VAL A1089      24.508 -34.914 -29.505  1.00 10.10           O  
ANISOU  688  O   VAL A1089     1297   1172   1368    123    110   -102       O  
ATOM    689  CB  VAL A1089      25.724 -34.906 -26.666  1.00  9.24           C  
ANISOU  689  CB  VAL A1089     1077   1196   1235     84      5   -134       C  
ATOM    690  CG1 VAL A1089      26.189 -33.454 -26.475  1.00  9.88           C  
ANISOU  690  CG1 VAL A1089     1293   1308   1152    -43    -26   -187       C  
ATOM    691  CG2 VAL A1089      25.915 -35.656 -25.376  1.00 10.29           C  
ANISOU  691  CG2 VAL A1089     1227   1308   1374    207     10    -48       C  
ATOM    692  N   LEU A1090      23.515 -33.111 -28.516  1.00  9.00           N  
ANISOU  692  N   LEU A1090     1080   1205   1132     -3    234   -110       N  
ATOM    693  CA  LEU A1090      23.516 -32.266 -29.723  1.00  8.96           C  
ANISOU  693  CA  LEU A1090     1034   1160   1209    -80     -3    -46       C  
ATOM    694  C   LEU A1090      24.590 -31.206 -29.577  1.00  8.38           C  
ANISOU  694  C   LEU A1090     1031   1140   1010    -77    -15     -3       C  
ATOM    695  O   LEU A1090      24.502 -30.345 -28.720  1.00  9.96           O  
ANISOU  695  O   LEU A1090     1397   1441    944   -165     24    -99       O  
ATOM    696  CB  LEU A1090      22.167 -31.604 -29.995  1.00  9.73           C  
ANISOU  696  CB  LEU A1090     1061   1297   1338    -12     65    -21       C  
ATOM    697  CG  LEU A1090      21.020 -32.587 -30.240  1.00  9.95           C  
ANISOU  697  CG  LEU A1090     1085   1418   1278     -4   -126   -126       C  
ATOM    698  CD1 LEU A1090      19.711 -31.811 -30.385  1.00 10.74           C  
ANISOU  698  CD1 LEU A1090     1130   1392   1556     27    -49   -149       C  
ATOM    699  CD2 LEU A1090      21.238 -33.409 -31.516  1.00 11.34           C  
ANISOU  699  CD2 LEU A1090     1180   1661   1466    -55   -142   -340       C  
ATOM    700  N   HIS A1091      25.623 -31.304 -30.390  1.00  8.04           N  
ANISOU  700  N   HIS A1091     1026   1125    902     89    -83   -113       N  
ATOM    701  CA  HIS A1091      26.745 -30.378 -30.343  1.00  8.48           C  
ANISOU  701  CA  HIS A1091     1065   1214    940     58   -167    -85       C  
ATOM    702  C   HIS A1091      26.462 -29.283 -31.339  1.00  8.93           C  
ANISOU  702  C   HIS A1091     1137   1282    972     93   -134    -48       C  
ATOM    703  O   HIS A1091      26.300 -29.568 -32.536  1.00 10.61           O  
ANISOU  703  O   HIS A1091     1474   1540   1014     81   -254   -159       O  
ATOM    704  CB  HIS A1091      28.038 -31.082 -30.692  1.00  8.86           C  
ANISOU  704  CB  HIS A1091     1023   1295   1048     80   -142     55       C  
ATOM    705  CG  HIS A1091      28.350 -32.270 -29.834  1.00  8.13           C  
ANISOU  705  CG  HIS A1091     1048   1172    869     51   -167    -73       C  
ATOM    706  ND1 HIS A1091      29.133 -32.195 -28.692  1.00  7.58           N  
ANISOU  706  ND1 HIS A1091      786   1104    988     -3   -162   -162       N  
ATOM    707  CD2 HIS A1091      27.983 -33.561 -29.965  1.00  8.29           C  
ANISOU  707  CD2 HIS A1091      912   1113   1123    137    -46    -56       C  
ATOM    708  CE1 HIS A1091      29.235 -33.405 -28.168  1.00  9.00           C  
ANISOU  708  CE1 HIS A1091     1109   1233   1075     38   -199    -74       C  
ATOM    709  NE2 HIS A1091      28.554 -34.260 -28.926  1.00  8.86           N  
ANISOU  709  NE2 HIS A1091     1173   1285    908    -13    -89    -79       N  
ATOM    710  N  AVAL A1092      26.353 -28.045 -30.868  0.50  8.45           N  
ANISOU  710  N  AVAL A1092      894   1297   1019    145   -229    -77       N  
ATOM    711  N  BVAL A1092      26.377 -28.046 -30.858  0.50  8.59           N  
ANISOU  711  N  BVAL A1092      927   1309   1024    149   -215    -84       N  
ATOM    712  CA AVAL A1092      26.011 -26.939 -31.746  0.50 10.06           C  
ANISOU  712  CA AVAL A1092     1314   1295   1211    112   -142     43       C  
ATOM    713  CA BVAL A1092      26.030 -26.915 -31.697  0.50 10.39           C  
ANISOU  713  CA BVAL A1092     1360   1344   1241    104   -159     58       C  
ATOM    714  C  AVAL A1092      27.137 -25.916 -31.795  0.50  9.87           C  
ANISOU  714  C  AVAL A1092     1204   1485   1057     74   -139     81       C  
ATOM    715  C  BVAL A1092      27.172 -25.922 -31.791  0.50  9.98           C  
ANISOU  715  C  BVAL A1092     1231   1503   1057     95   -139     78       C  
ATOM    716  O  AVAL A1092      27.764 -25.635 -30.778  0.50  8.58           O  
ANISOU  716  O  AVAL A1092     1056   1303    900    149    -53    193       O  
ATOM    717  O  BVAL A1092      27.836 -25.652 -30.795  0.50  8.82           O  
ANISOU  717  O  BVAL A1092     1105   1344    901    159    -46    153       O  
ATOM    718  CB AVAL A1092      24.700 -26.266 -31.288  0.50 11.59           C  
ANISOU  718  CB AVAL A1092     1299   1514   1591    236   -206    108       C  
ATOM    719  CB BVAL A1092      24.811 -26.175 -31.119  0.50 12.24           C  
ANISOU  719  CB BVAL A1092     1375   1663   1610    309   -221    120       C  
ATOM    720  CG1AVAL A1092      23.654 -27.306 -30.959  0.50 12.89           C  
ANISOU  720  CG1AVAL A1092     1531   1598   1768    154   -105    137       C  
ATOM    721  CG1BVAL A1092      24.486 -24.978 -31.993  0.50 14.30           C  
ANISOU  721  CG1BVAL A1092     1752   1799   1880    233   -292    325       C  
ATOM    722  CG2AVAL A1092      24.936 -25.377 -30.098  0.50 12.52           C  
ANISOU  722  CG2AVAL A1092     1687   1463   1606    239   -107     86       C  
ATOM    723  CG2BVAL A1092      23.630 -27.112 -31.036  0.50 14.01           C  
ANISOU  723  CG2BVAL A1092     1710   1720   1893    133    -75    148       C  
ATOM    724  N   VAL A1093      27.389 -25.347 -32.974  1.00 11.53           N  
ANISOU  724  N   VAL A1093     1514   1814   1050   -129    -91     93       N  
ATOM    725  CA  VAL A1093      28.351 -24.246 -33.112  1.00 13.40           C  
ANISOU  725  CA  VAL A1093     1650   2211   1230   -374   -102    175       C  
ATOM    726  C   VAL A1093      27.570 -22.950 -32.910  1.00 13.70           C  
ANISOU  726  C   VAL A1093     1744   2246   1214   -415     36    197       C  
ATOM    727  O   VAL A1093      26.856 -22.496 -33.791  1.00 13.92           O  
ANISOU  727  O   VAL A1093     2229   1762   1296   -161     29    346       O  
ATOM    728  CB  VAL A1093      29.080 -24.244 -34.467  1.00 14.07           C  
ANISOU  728  CB  VAL A1093     1613   2377   1354    103     -8    278       C  
ATOM    729  CG1 VAL A1093      30.108 -23.131 -34.472  1.00 16.05           C  
ANISOU  729  CG1 VAL A1093     1961   2401   1737     22    100    557       C  
ATOM    730  CG2 VAL A1093      29.743 -25.601 -34.723  1.00 16.37           C  
ANISOU  730  CG2 VAL A1093     2098   2443   1678    214    -16    347       C  
ATOM    731  N   ALA A1094      27.696 -22.366 -31.718  1.00 14.63           N  
ANISOU  731  N   ALA A1094     1853   2549   1155   -655    -61    186       N  
ATOM    732  CA  ALA A1094      26.914 -21.214 -31.351  1.00 18.23           C  
ANISOU  732  CA  ALA A1094     2563   2622   1739   -560     44   -102       C  
ATOM    733  C   ALA A1094      27.492 -20.033 -32.127  1.00 17.79           C  
ANISOU  733  C   ALA A1094     2374   2559   1826   -918    302   -581       C  
ATOM    734  O   ALA A1094      28.670 -20.065 -32.507  1.00 20.34           O  
ANISOU  734  O   ALA A1094     2762   2730   2235  -1299   1029  -1067       O  
ATOM    735  CB  ALA A1094      27.016 -20.954 -29.848  1.00 20.15           C  
ANISOU  735  CB  ALA A1094     2617   3294   1745   -123    341   -127       C  
ATOM    736  N   PRO A1095      26.683 -18.983 -32.336  1.00 18.73           N  
ANISOU  736  N   PRO A1095     2446   3044   1624   -596    320   -420       N  
ATOM    737  CA  PRO A1095      27.173 -17.749 -32.936  1.00 20.70           C  
ANISOU  737  CA  PRO A1095     2931   2775   2157   -517    267   -438       C  
ATOM    738  C   PRO A1095      28.095 -17.010 -32.016  1.00 23.07           C  
ANISOU  738  C   PRO A1095     3084   2995   2683   -560    402  -1038       C  
ATOM    739  O   PRO A1095      28.195 -17.337 -30.834  1.00 22.47           O  
ANISOU  739  O   PRO A1095     2262   3386   2887     29   -469  -1227       O  
ATOM    740  CB  PRO A1095      25.896 -16.938 -33.153  1.00 21.58           C  
ANISOU  740  CB  PRO A1095     2961   2794   2444   -587    288   -457       C  
ATOM    741  CG  PRO A1095      24.987 -17.445 -32.096  1.00 20.43           C  
ANISOU  741  CG  PRO A1095     2548   2890   2324   -681    257   -772       C  
ATOM    742  CD  PRO A1095      25.239 -18.905 -32.085  1.00 19.92           C  
ANISOU  742  CD  PRO A1095     2339   3024   2206   -442    367   -274       C  
ATOM    743  N   GLU A1096      28.799 -16.048 -32.596  1.00 26.72           N  
ANISOU  743  N   GLU A1096     3632   3099   3418   -998    161  -1085       N  
ATOM    744  CA  GLU A1096      29.560 -15.099 -31.836  1.00 25.34           C  
ANISOU  744  CA  GLU A1096     2985   2899   3743   -745     64  -1005       C  
ATOM    745  C   GLU A1096      29.174 -13.713 -32.254  1.00 24.58           C  
ANISOU  745  C   GLU A1096     3196   2726   3415   -694   -333  -1472       C  
ATOM    746  O   GLU A1096      28.432 -13.506 -33.206  1.00 26.71           O  
ANISOU  746  O   GLU A1096     2481   3840   3826   -370    100   -745       O  
ATOM    747  CB  GLU A1096      31.069 -15.346 -31.992  1.00 29.52           C  
ANISOU  747  CB  GLU A1096     3227   3778   4212     69    286   -355       C  
ATOM    748  CG  GLU A1096      31.520 -16.502 -31.106  1.00 33.79           C  
ANISOU  748  CG  GLU A1096     3800   4778   4260   -141   -430    176       C  
ATOM    749  CD  GLU A1096      33.020 -16.819 -31.154  1.00 41.45           C  
ANISOU  749  CD  GLU A1096     4504   5501   5741   1046    770    355       C  
ATOM    750  OE1 GLU A1096      33.767 -16.280 -32.034  1.00 45.81           O  
ANISOU  750  OE1 GLU A1096     6154   6720   4531   1080   1668   -415       O  
ATOM    751  OE2 GLU A1096      33.451 -17.623 -30.273  1.00 46.36           O  
ANISOU  751  OE2 GLU A1096     5430   6540   5641   1232    138    467       O  
ATOM    752  N   TRP A1097      29.678 -12.745 -31.500  1.00 18.44           N  
ANISOU  752  N   TRP A1097     2324   2282   2399   -702   -133   -810       N  
ATOM    753  CA  TRP A1097      29.305 -11.380 -31.743  1.00 20.95           C  
ANISOU  753  CA  TRP A1097     2487   2649   2823    -30    208   -555       C  
ATOM    754  C   TRP A1097      29.591 -10.913 -33.191  1.00 21.36           C  
ANISOU  754  C   TRP A1097     3108   2279   2727    290   -300   -439       C  
ATOM    755  O   TRP A1097      28.872 -10.071 -33.702  1.00 22.90           O  
ANISOU  755  O   TRP A1097     3270   2778   2651    578   -270   -364       O  
ATOM    756  CB  TRP A1097      29.961 -10.492 -30.693  1.00 19.37           C  
ANISOU  756  CB  TRP A1097     2820   2098   2439    109     23   -160       C  
ATOM    757  CG  TRP A1097      31.395 -10.347 -30.918  1.00 17.18           C  
ANISOU  757  CG  TRP A1097     2830   1853   1841    -80   -200   -341       C  
ATOM    758  CD1 TRP A1097      32.397 -11.109 -30.410  1.00 18.57           C  
ANISOU  758  CD1 TRP A1097     2828   2348   1880   -326   -495    185       C  
ATOM    759  CD2 TRP A1097      32.003  -9.407 -31.782  1.00 18.31           C  
ANISOU  759  CD2 TRP A1097     3074   1908   1976   -112   -114   -337       C  
ATOM    760  NE1 TRP A1097      33.599 -10.696 -30.897  1.00 18.39           N  
ANISOU  760  NE1 TRP A1097     2705   2530   1750    -30   -494    175       N  
ATOM    761  CE2 TRP A1097      33.393  -9.634 -31.730  1.00 16.69           C  
ANISOU  761  CE2 TRP A1097     3025   2029   1288    -17   -790   -347       C  
ATOM    762  CE3 TRP A1097      31.507  -8.376 -32.596  1.00 17.15           C  
ANISOU  762  CE3 TRP A1097     2776   1830   1909    135   -136   -568       C  
ATOM    763  CZ2 TRP A1097      34.298  -8.875 -32.472  1.00 21.23           C  
ANISOU  763  CZ2 TRP A1097     3180   2578   2306    -85   -484    -80       C  
ATOM    764  CZ3 TRP A1097      32.406  -7.628 -33.339  1.00 19.59           C  
ANISOU  764  CZ3 TRP A1097     3237   2056   2149   -110      3   -431       C  
ATOM    765  CH2 TRP A1097      33.778  -7.873 -33.267  1.00 21.47           C  
ANISOU  765  CH2 TRP A1097     3352   2755   2051    113   -149     -1       C  
ATOM    766  N   ARG A1098      30.614 -11.466 -33.855  1.00 20.91           N  
ANISOU  766  N   ARG A1098     2878   2289   2775   -189   -169   -522       N  
ATOM    767  CA  ARG A1098      30.951 -11.065 -35.246  1.00 25.58           C  
ANISOU  767  CA  ARG A1098     3524   3187   3008   -305    336   -631       C  
ATOM    768  C   ARG A1098      29.856 -11.312 -36.285  1.00 26.65           C  
ANISOU  768  C   ARG A1098     3801   3593   2730   -879    330   -199       C  
ATOM    769  O   ARG A1098      29.841 -10.693 -37.367  1.00 27.10           O  
ANISOU  769  O   ARG A1098     3900   3744   2653     36    878   -219       O  
ATOM    770  CB  ARG A1098      32.190 -11.794 -35.726  1.00 32.31           C  
ANISOU  770  CB  ARG A1098     3845   3975   4455    193    668   -355       C  
ATOM    771  CG  ARG A1098      33.475 -11.099 -35.382  1.00 31.09           C  
ANISOU  771  CG  ARG A1098     4520   3611   3681    149     78  -1187       C  
ATOM    772  CD  ARG A1098      34.625 -11.901 -35.959  1.00 32.35           C  
ANISOU  772  CD  ARG A1098     4112   4444   3733   -185   1228     11       C  
ATOM    773  NE  ARG A1098      35.787 -11.785 -35.108  1.00 35.15           N  
ANISOU  773  NE  ARG A1098     4030   5088   4236   -329   1116    -16       N  
ATOM    774  CZ  ARG A1098      36.599 -12.780 -34.751  1.00 33.42           C  
ANISOU  774  CZ  ARG A1098     3707   4811   4177   -338   1531    -83       C  
ATOM    775  NH1 ARG A1098      36.411 -14.033 -35.156  1.00 36.09           N  
ANISOU  775  NH1 ARG A1098     3934   4871   4905   -305   1483   -205       N  
ATOM    776  NH2 ARG A1098      37.620 -12.510 -33.961  1.00 41.25           N  
ANISOU  776  NH2 ARG A1098     5599   5578   4495     94    -11   -639       N  
ATOM    777  N   ASN A1099      28.962 -12.238 -35.956  1.00 25.48           N  
ANISOU  777  N   ASN A1099     4136   2696   2849   -927   -155   -510       N  
ATOM    778  CA  ASN A1099      27.775 -12.487 -36.752  1.00 26.15           C  
ANISOU  778  CA  ASN A1099     3856   2771   3307   -630   -259   -751       C  
ATOM    779  C   ASN A1099      26.793 -11.307 -36.764  1.00 27.62           C  
ANISOU  779  C   ASN A1099     4390   2884   3220   -399   -585   -839       C  
ATOM    780  O   ASN A1099      25.931 -11.234 -37.651  1.00 36.17           O  
ANISOU  780  O   ASN A1099     5487   4118   4136     -6  -1575   -664       O  
ATOM    781  CB  ASN A1099      27.096 -13.774 -36.263  1.00 27.75           C  
ANISOU  781  CB  ASN A1099     4421   2722   3400   -636   -401   -462       C  
ATOM    782  CG  ASN A1099      27.958 -14.999 -36.501  1.00 30.80           C  
ANISOU  782  CG  ASN A1099     4885   3307   3510   -366    -78  -1030       C  
ATOM    783  OD1 ASN A1099      28.451 -15.636 -35.560  1.00 35.62           O  
ANISOU  783  OD1 ASN A1099     6186   3276   4070   -821    441     81       O  
ATOM    784  ND2 ASN A1099      28.177 -15.313 -37.767  1.00 34.96           N  
ANISOU  784  ND2 ASN A1099     6295   3806   3182   -795   -424   -900       N  
ATOM    785  N   GLY A1100      26.942 -10.382 -35.799  1.00 24.57           N  
ANISOU  785  N   GLY A1100     3766   2768   2800     35   -375   -705       N  
ATOM    786  CA  GLY A1100      26.115  -9.194 -35.704  1.00 24.18           C  
ANISOU  786  CA  GLY A1100     3678   2939   2568     58    200   -482       C  
ATOM    787  C   GLY A1100      25.316  -9.285 -34.423  1.00 24.10           C  
ANISOU  787  C   GLY A1100     3921   3210   2025    249   -132   -168       C  
ATOM    788  O   GLY A1100      25.020 -10.384 -33.965  1.00 34.87           O  
ANISOU  788  O   GLY A1100     5760   3294   4195    435     30    442       O  
ATOM    789  N   SER A1101      24.947  -8.134 -33.860  1.00 20.69           N  
ANISOU  789  N   SER A1101     3150   2712   1998   -116   -413     21       N  
ATOM    790  CA  SER A1101      24.306  -8.092 -32.536  1.00 21.87           C  
ANISOU  790  CA  SER A1101     2939   2793   2575     40     93   -106       C  
ATOM    791  C   SER A1101      22.898  -8.711 -32.557  1.00 23.10           C  
ANISOU  791  C   SER A1101     3045   2801   2930    -72   -223     60       C  
ATOM    792  O   SER A1101      22.683  -9.813 -32.014  1.00 24.33           O  
ANISOU  792  O   SER A1101     3499   2783   2959     72   -274    125       O  
ATOM    793  CB  SER A1101      24.296  -6.659 -31.969  1.00 21.35           C  
ANISOU  793  CB  SER A1101     2725   2651   2733     19    169     72       C  
ATOM    794  OG  SER A1101      23.694  -5.737 -32.859  1.00 23.88           O  
ANISOU  794  OG  SER A1101     3539   2899   2635    -17   -182     96       O  
ATOM    795  N   THR A1102      21.948  -8.027 -33.195  1.00 23.99           N  
ANISOU  795  N   THR A1102     3500   2842   2771   -391   -677    320       N  
ATOM    796  CA  THR A1102      20.575  -8.550 -33.328  1.00 25.20           C  
ANISOU  796  CA  THR A1102     3533   2698   3342   -383   -502   -108       C  
ATOM    797  C   THR A1102      20.567  -9.923 -34.023  1.00 23.47           C  
ANISOU  797  C   THR A1102     3507   2467   2942   -881    216    126       C  
ATOM    798  O   THR A1102      19.847 -10.844 -33.591  1.00 19.78           O  
ANISOU  798  O   THR A1102     3643   2260   1609   -525   -220    716       O  
ATOM    799  CB  THR A1102      19.670  -7.556 -34.099  1.00 25.44           C  
ANISOU  799  CB  THR A1102     3776   2329   3561   -215   -271   -179       C  
ATOM    800  OG1 THR A1102      19.818  -6.245 -33.528  1.00 24.40           O  
ANISOU  800  OG1 THR A1102     3937   2178   3152   -736   -972    178       O  
ATOM    801  CG2 THR A1102      18.199  -7.983 -34.033  1.00 28.58           C  
ANISOU  801  CG2 THR A1102     3662   3661   3535   -439   -848   -517       C  
ATOM    802  N   SER A1103      21.371 -10.054 -35.084  1.00 21.99           N  
ANISOU  802  N   SER A1103     2824   2690   2842   -446   -128    -58       N  
ATOM    803  CA ASER A1103      21.509 -11.314 -35.824  0.50 22.74           C  
ANISOU  803  CA ASER A1103     3162   2613   2865   -410    -10     43       C  
ATOM    804  CA BSER A1103      21.478 -11.320 -35.808  0.50 22.39           C  
ANISOU  804  CA BSER A1103     3095   2560   2849   -533    -33     80       C  
ATOM    805  C   SER A1103      21.838 -12.490 -34.901  1.00 23.59           C  
ANISOU  805  C   SER A1103     3262   2592   3108   -595   -193    165       C  
ATOM    806  O   SER A1103      21.250 -13.564 -35.021  1.00 23.20           O  
ANISOU  806  O   SER A1103     3307   2622   2884   -810    424    409       O  
ATOM    807  CB ASER A1103      22.608 -11.197 -36.885  0.50 24.01           C  
ANISOU  807  CB ASER A1103     3488   2837   2795   -134    181   -290       C  
ATOM    808  CB BSER A1103      22.491 -11.209 -36.938  0.50 22.87           C  
ANISOU  808  CB BSER A1103     3492   2634   2560   -323     -2     87       C  
ATOM    809  OG ASER A1103      22.651 -12.364 -37.691  0.50 27.22           O  
ANISOU  809  OG ASER A1103     4456   3409   2476     49     72   -573       O  
ATOM    810  OG BSER A1103      21.875 -10.551 -38.016  0.50 22.56           O  
ANISOU  810  OG BSER A1103     3774   2412   2386   -951   -163    274       O  
ATOM    811  N   SER A1104      22.800 -12.278 -33.997  1.00 22.91           N  
ANISOU  811  N   SER A1104     2983   2934   2786   -479    -17    155       N  
ATOM    812  CA  SER A1104      23.228 -13.340 -33.083  1.00 22.45           C  
ANISOU  812  CA  SER A1104     2770   2551   3209    -91    182    -36       C  
ATOM    813  C   SER A1104      22.124 -13.831 -32.130  1.00 20.74           C  
ANISOU  813  C   SER A1104     2944   1943   2990    -43    137      6       C  
ATOM    814  O   SER A1104      22.078 -15.015 -31.813  1.00 17.56           O  
ANISOU  814  O   SER A1104     1725   1705   3241    -68    286   -352       O  
ATOM    815  CB  SER A1104      24.481 -12.950 -32.309  1.00 23.86           C  
ANISOU  815  CB  SER A1104     3220   2506   3336   -242     78   -758       C  
ATOM    816  OG  SER A1104      24.247 -11.881 -31.384  1.00 26.50           O  
ANISOU  816  OG  SER A1104     3458   2874   3736    -89    830   -925       O  
ATOM    817  N   LEU A1105      21.247 -12.932 -31.683  1.00 19.47           N  
ANISOU  817  N   LEU A1105     2241   2301   2853   -118   -112     62       N  
ATOM    818  CA  LEU A1105      20.098 -13.309 -30.855  1.00 17.78           C  
ANISOU  818  CA  LEU A1105     2341   1808   2605   -189   -215     82       C  
ATOM    819  C   LEU A1105      19.122 -14.152 -31.667  1.00 16.31           C  
ANISOU  819  C   LEU A1105     2236   1901   2058   -263   -225    397       C  
ATOM    820  O   LEU A1105      18.618 -15.152 -31.180  1.00 14.33           O  
ANISOU  820  O   LEU A1105     1807   1877   1761   -202   -210    247       O  
ATOM    821  CB  LEU A1105      19.399 -12.076 -30.263  1.00 16.46           C  
ANISOU  821  CB  LEU A1105     1769   2143   2338    -45    -99    167       C  
ATOM    822  CG  LEU A1105      20.230 -11.250 -29.285  1.00 18.13           C  
ANISOU  822  CG  LEU A1105     2122   2090   2676    -80   -208     -6       C  
ATOM    823  CD1 LEU A1105      19.508  -9.985 -28.846  1.00 20.20           C  
ANISOU  823  CD1 LEU A1105     2693   2440   2539     12    171   -335       C  
ATOM    824  CD2 LEU A1105      20.666 -12.056 -28.078  1.00 19.89           C  
ANISOU  824  CD2 LEU A1105     2686   2252   2618   -343   -204     82       C  
ATOM    825  N   LYS A1106      18.890 -13.756 -32.909  1.00 16.91           N  
ANISOU  825  N   LYS A1106     2948   1097   2378  -1063   -147    887       N  
ATOM    826  CA  LYS A1106      17.986 -14.473 -33.790  1.00 15.86           C  
ANISOU  826  CA  LYS A1106     2205   1880   1939   -465    -80    592       C  
ATOM    827  C   LYS A1106      18.541 -15.852 -34.101  1.00 16.66           C  
ANISOU  827  C   LYS A1106     2502   2242   1583   -300   -153    295       C  
ATOM    828  O   LYS A1106      17.813 -16.846 -34.092  1.00 17.97           O  
ANISOU  828  O   LYS A1106     3273   1997   1554   -520   -257    545       O  
ATOM    829  CB  LYS A1106      17.769 -13.695 -35.100  1.00 18.74           C  
ANISOU  829  CB  LYS A1106     2892   2176   2052   -149   -169    697       C  
ATOM    830  CG  LYS A1106      16.766 -14.369 -36.012  1.00 24.08           C  
ANISOU  830  CG  LYS A1106     3781   2990   2377   -170   -478    185       C  
ATOM    831  N   ILE A1107      19.850 -15.920 -34.310  1.00 16.76           N  
ANISOU  831  N   ILE A1107     2527   2311   1528   -561    263    512       N  
ATOM    832  CA  ILE A1107      20.495 -17.204 -34.548  1.00 18.07           C  
ANISOU  832  CA  ILE A1107     2512   2593   1758   -283     -1    111       C  
ATOM    833  C   ILE A1107      20.365 -18.119 -33.317  1.00 15.44           C  
ANISOU  833  C   ILE A1107     2113   2055   1699   -405    110   -115       C  
ATOM    834  O   ILE A1107      20.053 -19.306 -33.437  1.00 15.12           O  
ANISOU  834  O   ILE A1107     2000   2093   1649   -481    136   -108       O  
ATOM    835  CB  ILE A1107      21.973 -17.036 -34.934  1.00 20.04           C  
ANISOU  835  CB  ILE A1107     2744   2830   2039   -581    347     74       C  
ATOM    836  CG1 ILE A1107      22.072 -16.430 -36.342  1.00 22.34           C  
ANISOU  836  CG1 ILE A1107     3356   2800   2331   -178    581    341       C  
ATOM    837  CG2 ILE A1107      22.683 -18.383 -34.908  1.00 20.12           C  
ANISOU  837  CG2 ILE A1107     2505   3131   2009   -406    251    -39       C  
ATOM    838  CD1 ILE A1107      23.397 -15.754 -36.614  1.00 25.75           C  
ANISOU  838  CD1 ILE A1107     2966   3366   3449   -137    237     50       C  
ATOM    839  N   MET A1108      20.593 -17.577 -32.125  1.00 13.91           N  
ANISOU  839  N   MET A1108     1737   1892   1655   -305     16     -9       N  
ATOM    840  CA  MET A1108      20.393 -18.403 -30.933  1.00 12.92           C  
ANISOU  840  CA  MET A1108     1593   1877   1438     29     45   -117       C  
ATOM    841  C   MET A1108      18.968 -18.934 -30.836  1.00 12.64           C  
ANISOU  841  C   MET A1108     1683   1579   1539    -55   -237    102       C  
ATOM    842  O   MET A1108      18.761 -20.092 -30.474  1.00 11.52           O  
ANISOU  842  O   MET A1108     1572   1510   1293   -125   -279    -84       O  
ATOM    843  CB  MET A1108      20.719 -17.624 -29.642  1.00 16.39           C  
ANISOU  843  CB  MET A1108     2229   2167   1832   -137    109   -538       C  
ATOM    844  CG  MET A1108      22.155 -17.664 -29.244  1.00 22.74           C  
ANISOU  844  CG  MET A1108     2813   2927   2900    480   -390   -255       C  
ATOM    845  SD  MET A1108      22.787 -19.337 -29.059  1.00 22.26           S  
ANISOU  845  SD  MET A1108     3145   3231   2079    896   -859   -177       S  
ATOM    846  CE  MET A1108      23.912 -18.982 -27.727  1.00 25.05           C  
ANISOU  846  CE  MET A1108     2728   3749   3040   -509   -943   -176       C  
ATOM    847  N   GLU A1109      17.986 -18.094 -31.152  1.00 11.21           N  
ANISOU  847  N   GLU A1109     1423   1568   1266   -166    -82    202       N  
ATOM    848  CA  GLU A1109      16.593 -18.551 -31.138  1.00 13.12           C  
ANISOU  848  CA  GLU A1109     1444   2000   1541   -195   -166    138       C  
ATOM    849  C   GLU A1109      16.397 -19.713 -32.105  1.00 12.52           C  
ANISOU  849  C   GLU A1109     1727   1753   1277   -205   -471    413       C  
ATOM    850  O   GLU A1109      15.718 -20.700 -31.791  1.00 12.36           O  
ANISOU  850  O   GLU A1109     1436   1824   1433    -93   -214    424       O  
ATOM    851  CB  GLU A1109      15.637 -17.418 -31.509  1.00 16.47           C  
ANISOU  851  CB  GLU A1109     2214   1940   2102     -6   -394    265       C  
ATOM    852  CG  GLU A1109      15.481 -16.313 -30.467  1.00 17.71           C  
ANISOU  852  CG  GLU A1109     2253   2287   2187    271   -473    224       C  
ATOM    853  CD  GLU A1109      14.573 -15.201 -30.963  1.00 24.85           C  
ANISOU  853  CD  GLU A1109     3328   3111   3003    984   -565    788       C  
ATOM    854  OE1 GLU A1109      14.393 -15.066 -32.194  1.00 31.69           O  
ANISOU  854  OE1 GLU A1109     4497   4563   2981   1591   -612    951       O  
ATOM    855  OE2 GLU A1109      14.035 -14.457 -30.115  1.00 34.03           O  
ANISOU  855  OE2 GLU A1109     4720   3907   4301   1633   -520     89       O  
ATOM    856  N   ASP A1110      16.968 -19.579 -33.304  1.00 13.00           N  
ANISOU  856  N   ASP A1110     1333   2032   1573    -67   -223    369       N  
ATOM    857  CA  ASP A1110      16.842 -20.635 -34.313  1.00 15.04           C  
ANISOU  857  CA  ASP A1110     1956   2132   1627   -116   -364    259       C  
ATOM    858  C   ASP A1110      17.502 -21.934 -33.840  1.00 13.20           C  
ANISOU  858  C   ASP A1110     1533   1958   1522   -343   -335    184       C  
ATOM    859  O   ASP A1110      16.993 -23.017 -34.082  1.00 14.66           O  
ANISOU  859  O   ASP A1110     1742   2213   1613   -766   -233    251       O  
ATOM    860  CB  ASP A1110      17.452 -20.221 -35.665  1.00 16.99           C  
ANISOU  860  CB  ASP A1110     2227   2713   1515   -247   -424    178       C  
ATOM    861  CG  ASP A1110      16.723 -19.064 -36.332  1.00 20.26           C  
ANISOU  861  CG  ASP A1110     2787   2735   2173   -164   -444    346       C  
ATOM    862  OD1 ASP A1110      15.534 -18.791 -36.034  1.00 22.25           O  
ANISOU  862  OD1 ASP A1110     2510   3281   2662    -79   -959    293       O  
ATOM    863  OD2 ASP A1110      17.369 -18.406 -37.187  1.00 25.49           O  
ANISOU  863  OD2 ASP A1110     4177   3723   1786   -159   -348    807       O  
ATOM    864  N   ILE A1111      18.645 -21.826 -33.153  1.00 12.43           N  
ANISOU  864  N   ILE A1111     1316   1945   1460   -303   -133     86       N  
ATOM    865  CA  ILE A1111      19.328 -22.997 -32.600  1.00 12.39           C  
ANISOU  865  CA  ILE A1111     1421   1805   1479   -205    -66    -79       C  
ATOM    866  C   ILE A1111      18.485 -23.704 -31.527  1.00 11.24           C  
ANISOU  866  C   ILE A1111     1339   1696   1233    -79   -189   -106       C  
ATOM    867  O   ILE A1111      18.350 -24.932 -31.517  1.00 10.33           O  
ANISOU  867  O   ILE A1111     1140   1687   1095    -52   -298   -107       O  
ATOM    868  CB  ILE A1111      20.707 -22.587 -32.044  1.00 13.27           C  
ANISOU  868  CB  ILE A1111     1324   1693   2023    -51    -93    -93       C  
ATOM    869  CG1 ILE A1111      21.671 -22.299 -33.226  1.00 14.89           C  
ANISOU  869  CG1 ILE A1111     1712   1850   2095     -1     33    -42       C  
ATOM    870  CG2 ILE A1111      21.241 -23.641 -31.082  1.00 14.49           C  
ANISOU  870  CG2 ILE A1111     1742   1984   1777    -70    -71    -49       C  
ATOM    871  CD1 ILE A1111      22.937 -21.583 -32.765  1.00 16.28           C  
ANISOU  871  CD1 ILE A1111     1440   2125   2618    -39    347    -44       C  
ATOM    872  N   ILE A1112      17.926 -22.905 -30.627  1.00  9.50           N  
ANISOU  872  N   ILE A1112     1184   1381   1044   -133   -218     82       N  
ATOM    873  CA  ILE A1112      17.062 -23.440 -29.574  1.00  9.71           C  
ANISOU  873  CA  ILE A1112     1090   1500   1096   -135   -205    106       C  
ATOM    874  C   ILE A1112      15.884 -24.208 -30.182  1.00  9.79           C  
ANISOU  874  C   ILE A1112     1187   1437   1093   -217   -153    138       C  
ATOM    875  O   ILE A1112      15.615 -25.354 -29.814  1.00 11.20           O  
ANISOU  875  O   ILE A1112     1563   1474   1217   -318   -209    217       O  
ATOM    876  CB  ILE A1112      16.598 -22.314 -28.636  1.00 10.49           C  
ANISOU  876  CB  ILE A1112     1281   1477   1224   -140   -170     41       C  
ATOM    877  CG1 ILE A1112      17.794 -21.738 -27.834  1.00 12.11           C  
ANISOU  877  CG1 ILE A1112     1509   1756   1335   -177   -263   -126       C  
ATOM    878  CG2 ILE A1112      15.491 -22.766 -27.708  1.00 11.06           C  
ANISOU  878  CG2 ILE A1112     1324   1630   1249    -63    -84     -2       C  
ATOM    879  CD1 ILE A1112      17.548 -20.323 -27.387  1.00 12.06           C  
ANISOU  879  CD1 ILE A1112     1653   1712   1216   -144   -163    -66       C  
ATOM    880  N   ARG A1113      15.241 -23.580 -31.158  1.00 10.98           N  
ANISOU  880  N   ARG A1113     1531   1515   1124   -210   -286    190       N  
ATOM    881  CA  ARG A1113      14.088 -24.176 -31.826  1.00 11.55           C  
ANISOU  881  CA  ARG A1113     1427   1737   1223   -239   -227    117       C  
ATOM    882  C   ARG A1113      14.495 -25.462 -32.529  1.00 12.42           C  
ANISOU  882  C   ARG A1113     1676   1860   1183    -64   -299    162       C  
ATOM    883  O   ARG A1113      13.820 -26.473 -32.407  1.00 13.10           O  
ANISOU  883  O   ARG A1113     1585   1795   1596    -42   -446    114       O  
ATOM    884  CB  ARG A1113      13.447 -23.189 -32.811  1.00 14.14           C  
ANISOU  884  CB  ARG A1113     2019   1703   1648   -225   -250    374       C  
ATOM    885  CG  ARG A1113      12.178 -23.695 -33.495  1.00 18.13           C  
ANISOU  885  CG  ARG A1113     2568   2412   1906   -259   -681     36       C  
ATOM    886  CD  ARG A1113      11.667 -22.715 -34.572  1.00 22.40           C  
ANISOU  886  CD  ARG A1113     2743   3342   2426     15  -1044    443       C  
ATOM    887  NE  ARG A1113      11.757 -21.331 -34.112  1.00 29.99           N  
ANISOU  887  NE  ARG A1113     3790   3599   4003     87   -703    138       N  
ATOM    888  CZ  ARG A1113      12.587 -20.374 -34.568  1.00 31.53           C  
ANISOU  888  CZ  ARG A1113     4158   3852   3968    179    126    382       C  
ATOM    889  NH1 ARG A1113      12.559 -19.179 -33.989  1.00 35.28           N  
ANISOU  889  NH1 ARG A1113     5253   3912   4237    332    433    164       N  
ATOM    890  NH2 ARG A1113      13.425 -20.565 -35.589  1.00 32.00           N  
ANISOU  890  NH2 ARG A1113     4711   4152   3293    254    -70    269       N  
ATOM    891  N   GLU A1114      15.618 -25.432 -33.231  1.00 11.89           N  
ANISOU  891  N   GLU A1114     1528   1906   1082    -92   -441    282       N  
ATOM    892  CA  GLU A1114      16.076 -26.621 -33.948  1.00 13.13           C  
ANISOU  892  CA  GLU A1114     1545   1995   1449    -29   -500    128       C  
ATOM    893  C   GLU A1114      16.300 -27.804 -33.019  1.00 12.01           C  
ANISOU  893  C   GLU A1114     1596   1810   1155   -220   -327    -38       C  
ATOM    894  O   GLU A1114      15.932 -28.933 -33.328  1.00 13.75           O  
ANISOU  894  O   GLU A1114     1822   1907   1494   -278   -289   -222       O  
ATOM    895  CB  GLU A1114      17.353 -26.307 -34.726  1.00 14.82           C  
ANISOU  895  CB  GLU A1114     1878   2103   1651    -85   -176    174       C  
ATOM    896  CG  GLU A1114      17.889 -27.445 -35.573  1.00 18.84           C  
ANISOU  896  CG  GLU A1114     2901   2395   1859    -22    -42    -94       C  
ATOM    897  CD  GLU A1114      17.045 -27.732 -36.816  1.00 27.94           C  
ANISOU  897  CD  GLU A1114     4443   3354   2818   -224  -1092   -260       C  
ATOM    898  OE1 GLU A1114      16.297 -26.855 -37.299  1.00 32.45           O  
ANISOU  898  OE1 GLU A1114     3942   4139   4245   -146   -886    320       O  
ATOM    899  OE2 GLU A1114      17.137 -28.864 -37.329  1.00 41.93           O  
ANISOU  899  OE2 GLU A1114     8110   3867   3953    257   -390   -832       O  
ATOM    900  N   CYS A1115      16.945 -27.548 -31.888  1.00 11.40           N  
ANISOU  900  N   CYS A1115     1463   1624   1244   -126   -365   -111       N  
ATOM    901  CA  CYS A1115      17.276 -28.639 -30.979  1.00 11.78           C  
ANISOU  901  CA  CYS A1115     1512   1684   1278    -60   -141    -21       C  
ATOM    902  C   CYS A1115      15.999 -29.255 -30.397  1.00 11.85           C  
ANISOU  902  C   CYS A1115     1480   1585   1435   -183   -214   -179       C  
ATOM    903  O   CYS A1115      15.908 -30.466 -30.245  1.00 12.26           O  
ANISOU  903  O   CYS A1115     1360   1575   1721   -101   -539    -71       O  
ATOM    904  CB  CYS A1115      18.223 -28.167 -29.887  1.00 11.44           C  
ANISOU  904  CB  CYS A1115     1342   1809   1193      6    -20   -107       C  
ATOM    905  SG  CYS A1115      19.885 -27.765 -30.470  1.00 13.85           S  
ANISOU  905  SG  CYS A1115     1179   2217   1864   -130   -274    167       S  
ATOM    906  N   MET A1116      15.006 -28.418 -30.089  1.00 11.66           N  
ANISOU  906  N   MET A1116     1469   1473   1487   -241   -115     18       N  
ATOM    907  CA  MET A1116      13.718 -28.926 -29.619  1.00 11.44           C  
ANISOU  907  CA  MET A1116     1369   1626   1350   -276   -190    -88       C  
ATOM    908  C   MET A1116      13.042 -29.753 -30.711  1.00 10.82           C  
ANISOU  908  C   MET A1116     1237   1533   1339   -471   -148     75       C  
ATOM    909  O   MET A1116      12.465 -30.814 -30.426  1.00 12.26           O  
ANISOU  909  O   MET A1116     1552   1348   1757   -590   -458    -63       O  
ATOM    910  CB  MET A1116      12.813 -27.781 -29.128  1.00 12.42           C  
ANISOU  910  CB  MET A1116     1629   1688   1401   -207   -130   -135       C  
ATOM    911  CG  MET A1116      13.304 -27.150 -27.828  1.00 12.35           C  
ANISOU  911  CG  MET A1116     1461   1850   1382   -222   -209    -70       C  
ATOM    912  SD  MET A1116      12.161 -25.952 -27.100  1.00 16.23           S  
ANISOU  912  SD  MET A1116     2104   2165   1898    216   -360   -332       S  
ATOM    913  CE  MET A1116      12.171 -24.674 -28.312  1.00 16.70           C  
ANISOU  913  CE  MET A1116     2055   2236   2053   -210    110    -99       C  
ATOM    914  N   GLU A1117      13.096 -29.272 -31.951  1.00 12.14           N  
ANISOU  914  N   GLU A1117     1455   1825   1332   -341   -328     88       N  
ATOM    915  CA  GLU A1117      12.484 -29.985 -33.080  1.00 13.85           C  
ANISOU  915  CA  GLU A1117     1631   1828   1800   -451   -521   -109       C  
ATOM    916  C   GLU A1117      13.169 -31.333 -33.301  1.00 12.67           C  
ANISOU  916  C   GLU A1117     1379   1843   1592   -453   -550   -204       C  
ATOM    917  O   GLU A1117      12.515 -32.340 -33.567  1.00 15.76           O  
ANISOU  917  O   GLU A1117     1773   2069   2144   -629   -644   -541       O  
ATOM    918  CB  GLU A1117      12.511 -29.125 -34.359  1.00 15.67           C  
ANISOU  918  CB  GLU A1117     1929   2341   1683   -306   -427    -35       C  
ATOM    919  CG  GLU A1117      11.523 -27.966 -34.254  1.00 19.26           C  
ANISOU  919  CG  GLU A1117     2358   2503   2457    -96   -512     10       C  
ATOM    920  CD  GLU A1117      11.545 -26.976 -35.404  1.00 23.00           C  
ANISOU  920  CD  GLU A1117     2795   3605   2339   -232   -160    346       C  
ATOM    921  OE1 GLU A1117      12.489 -26.995 -36.212  1.00 26.97           O  
ANISOU  921  OE1 GLU A1117     3145   4868   2235   -276     -3   -100       O  
ATOM    922  OE2 GLU A1117      10.587 -26.163 -35.501  1.00 27.52           O  
ANISOU  922  OE2 GLU A1117     3417   4271   2767    400     94    143       O  
ATOM    923  N   ILE A1118      14.490 -31.367 -33.159  1.00 13.53           N  
ANISOU  923  N   ILE A1118     1416   1995   1729   -430   -646   -274       N  
ATOM    924  CA  ILE A1118      15.225 -32.615 -33.291  1.00 13.94           C  
ANISOU  924  CA  ILE A1118     1550   1953   1792   -401   -502   -355       C  
ATOM    925  C   ILE A1118      14.780 -33.601 -32.221  1.00 12.62           C  
ANISOU  925  C   ILE A1118     1438   1742   1613   -185   -758   -335       C  
ATOM    926  O   ILE A1118      14.529 -34.774 -32.513  1.00 17.09           O  
ANISOU  926  O   ILE A1118     2033   1937   2524   -589   -602   -567       O  
ATOM    927  CB  ILE A1118      16.746 -32.388 -33.238  1.00 14.14           C  
ANISOU  927  CB  ILE A1118     1522   1830   2020   -268   -283   -235       C  
ATOM    928  CG1 ILE A1118      17.201 -31.670 -34.518  1.00 13.65           C  
ANISOU  928  CG1 ILE A1118     1612   2047   1527   -163   -437   -410       C  
ATOM    929  CG2 ILE A1118      17.499 -33.719 -33.072  1.00 15.09           C  
ANISOU  929  CG2 ILE A1118     1954   1820   1959   -117   -195   -343       C  
ATOM    930  CD1 ILE A1118      18.595 -31.059 -34.430  1.00 14.10           C  
ANISOU  930  CD1 ILE A1118     1511   1934   1913    -14   -283   -210       C  
ATOM    931  N   THR A1119      14.677 -33.125 -30.985  1.00 12.69           N  
ANISOU  931  N   THR A1119     1436   1618   1767   -328   -320   -427       N  
ATOM    932  CA  THR A1119      14.249 -33.966 -29.871  1.00 13.34           C  
ANISOU  932  CA  THR A1119     1416   1668   1982   -206   -585   -119       C  
ATOM    933  C   THR A1119      12.850 -34.594 -30.145  1.00 14.50           C  
ANISOU  933  C   THR A1119     1553   1703   2252   -388   -546   -228       C  
ATOM    934  O   THR A1119      12.656 -35.803 -30.007  1.00 15.21           O  
ANISOU  934  O   THR A1119     1609   1681   2489   -367   -756   -266       O  
ATOM    935  CB  THR A1119      14.309 -33.163 -28.571  1.00 13.43           C  
ANISOU  935  CB  THR A1119     1507   1656   1937    -83   -343    -80       C  
ATOM    936  OG1 THR A1119      15.647 -32.657 -28.392  1.00 13.94           O  
ANISOU  936  OG1 THR A1119     1513   1677   2106    -95   -550      7       O  
ATOM    937  CG2 THR A1119      13.938 -33.999 -27.350  1.00 14.22           C  
ANISOU  937  CG2 THR A1119     1815   1579   2008    -54   -304    -42       C  
ATOM    938  N   GLU A1120      11.901 -33.759 -30.544  1.00 13.76           N  
ANISOU  938  N   GLU A1120     1562   1684   1981   -360   -429   -278       N  
ATOM    939  CA  GLU A1120      10.554 -34.209 -30.927  1.00 16.77           C  
ANISOU  939  CA  GLU A1120     1625   2129   2616   -463   -527   -195       C  
ATOM    940  C   GLU A1120      10.605 -35.194 -32.113  1.00 17.01           C  
ANISOU  940  C   GLU A1120     1805   2252   2407   -621   -657   -110       C  
ATOM    941  O   GLU A1120       9.918 -36.200 -32.096  1.00 20.37           O  
ANISOU  941  O   GLU A1120     2383   1896   3460   -557   -894   -104       O  
ATOM    942  CB  GLU A1120       9.668 -32.977 -31.209  1.00 18.51           C  
ANISOU  942  CB  GLU A1120     1986   2398   2647   -208   -469    100       C  
ATOM    943  CG  GLU A1120       8.281 -33.215 -31.806  1.00 22.12           C  
ANISOU  943  CG  GLU A1120     2452   3116   2836   -459   -820   -160       C  
ATOM    944  CD  GLU A1120       7.238 -33.831 -30.868  1.00 25.59           C  
ANISOU  944  CD  GLU A1120     2921   3670   3130   -629   -385   -437       C  
ATOM    945  OE1 GLU A1120       6.167 -34.220 -31.409  1.00 29.40           O  
ANISOU  945  OE1 GLU A1120     3197   4606   3366  -1116   -620   -153       O  
ATOM    946  OE2 GLU A1120       7.440 -33.938 -29.621  1.00 24.65           O  
ANISOU  946  OE2 GLU A1120     2725   3603   3038   -595    -37    -32       O  
ATOM    947  N   SER A1121      11.466 -34.941 -33.099  1.00 15.44           N  
ANISOU  947  N   SER A1121     2030   1560   2273   -970   -662   -166       N  
ATOM    948  CA  SER A1121      11.568 -35.834 -34.258  1.00 18.77           C  
ANISOU  948  CA  SER A1121     2323   2227   2580   -553   -720   -624       C  
ATOM    949  C   SER A1121      12.118 -37.240 -33.929  1.00 19.88           C  
ANISOU  949  C   SER A1121     2741   2175   2637   -678   -712   -654       C  
ATOM    950  O   SER A1121      11.805 -38.235 -34.611  1.00 24.26           O  
ANISOU  950  O   SER A1121     3349   2366   3501   -574  -1021  -1046       O  
ATOM    951  CB  SER A1121      12.391 -35.176 -35.363  1.00 21.03           C  
ANISOU  951  CB  SER A1121     2872   2630   2488   -698   -425   -824       C  
ATOM    952  OG  SER A1121      13.777 -35.344 -35.135  1.00 25.01           O  
ANISOU  952  OG  SER A1121     2953   3470   3080   -503   -237  -1432       O  
ATOM    953  N   LEU A1122      12.928 -37.301 -32.879  1.00 18.84           N  
ANISOU  953  N   LEU A1122     2841   1574   2742   -693   -868  -1114       N  
ATOM    954  CA  LEU A1122      13.434 -38.545 -32.327  1.00 19.00           C  
ANISOU  954  CA  LEU A1122     2624   1832   2759   -672   -531   -617       C  
ATOM    955  C   LEU A1122      12.485 -39.202 -31.319  1.00 18.85           C  
ANISOU  955  C   LEU A1122     2129   2203   2830   -239   -389   -638       C  
ATOM    956  O   LEU A1122      12.851 -40.237 -30.713  1.00 18.94           O  
ANISOU  956  O   LEU A1122     2102   2058   3035   -104   -411   -727       O  
ATOM    957  CB  LEU A1122      14.789 -38.316 -31.667  1.00 18.19           C  
ANISOU  957  CB  LEU A1122     2371   2001   2537   -332   -426   -318       C  
ATOM    958  CG  LEU A1122      15.932 -37.932 -32.602  1.00 20.86           C  
ANISOU  958  CG  LEU A1122     2784   2592   2550   -232   -183   -301       C  
ATOM    959  CD1 LEU A1122      17.085 -37.338 -31.815  1.00 20.67           C  
ANISOU  959  CD1 LEU A1122     2247   2674   2929   -112   -164    -76       C  
ATOM    960  CD2 LEU A1122      16.406 -39.128 -33.413  1.00 25.68           C  
ANISOU  960  CD2 LEU A1122     3319   2886   3551   -366    246   -754       C  
ATOM    961  N   SER A1123      11.274 -38.646 -31.174  1.00 16.98           N  
ANISOU  961  N   SER A1123     1935   1748   2768   -372   -557   -410       N  
ATOM    962  CA  SER A1123      10.252 -39.168 -30.256  1.00 18.28           C  
ANISOU  962  CA  SER A1123     2218   1902   2825   -198   -328   -303       C  
ATOM    963  C   SER A1123      10.724 -39.181 -28.811  1.00 16.63           C  
ANISOU  963  C   SER A1123     1787   1705   2824   -200   -297     95       C  
ATOM    964  O   SER A1123      10.396 -40.078 -28.058  1.00 19.66           O  
ANISOU  964  O   SER A1123     1992   2291   3186   -812    -70    221       O  
ATOM    965  CB  SER A1123       9.766 -40.572 -30.678  1.00 18.93           C  
ANISOU  965  CB  SER A1123     2413   1911   2867   -298   -415   -217       C  
ATOM    966  OG  SER A1123       9.261 -40.562 -31.992  1.00 25.01           O  
ANISOU  966  OG  SER A1123     3176   2960   3365   -738  -1055   -758       O  
ATOM    967  N   LEU A1124      11.515 -38.185 -28.431  1.00 15.18           N  
ANISOU  967  N   LEU A1124     1563   1844   2358   -149   -211     -4       N  
ATOM    968  CA  LEU A1124      12.045 -38.097 -27.081  1.00 14.96           C  
ANISOU  968  CA  LEU A1124     1450   1916   2318   -238   -103    -75       C  
ATOM    969  C   LEU A1124      11.265 -37.076 -26.251  1.00 14.58           C  
ANISOU  969  C   LEU A1124     1553   1610   2377    -94   -395    -39       C  
ATOM    970  O   LEU A1124      10.484 -36.288 -26.788  1.00 14.91           O  
ANISOU  970  O   LEU A1124     1505   1539   2620     13   -196     83       O  
ATOM    971  CB  LEU A1124      13.552 -37.804 -27.128  1.00 13.39           C  
ANISOU  971  CB  LEU A1124     1483   1595   2006   -338   -125   -165       C  
ATOM    972  CG  LEU A1124      14.401 -38.868 -27.821  1.00 16.17           C  
ANISOU  972  CG  LEU A1124     1839   2048   2254   -109    -13   -322       C  
ATOM    973  CD1 LEU A1124      15.843 -38.421 -27.994  1.00 15.58           C  
ANISOU  973  CD1 LEU A1124     1753   1790   2374     86    141   -597       C  
ATOM    974  CD2 LEU A1124      14.349 -40.195 -27.070  1.00 18.25           C  
ANISOU  974  CD2 LEU A1124     2053   2084   2796   -188   -104   -197       C  
ATOM    975  N   LYS A1125      11.473 -37.131 -24.935  1.00 13.75           N  
ANISOU  975  N   LYS A1125     1409   1543   2269   -259   -398   -100       N  
ATOM    976  CA  LYS A1125      10.639 -36.424 -23.956  1.00 15.80           C  
ANISOU  976  CA  LYS A1125     1748   1637   2615   -220   -246   -293       C  
ATOM    977  C   LYS A1125      11.267 -35.162 -23.372  1.00 13.32           C  
ANISOU  977  C   LYS A1125     1279   1520   2259    131   -155   -398       C  
ATOM    978  O   LYS A1125      10.545 -34.202 -23.053  1.00 14.79           O  
ANISOU  978  O   LYS A1125      772   2115   2730    273     57   -527       O  
ATOM    979  CB  LYS A1125      10.292 -37.372 -22.804  1.00 20.98           C  
ANISOU  979  CB  LYS A1125     2573   2258   3137   -625    -63    106       C  
ATOM    980  CG  LYS A1125       9.427 -36.797 -21.691  1.00 25.46           C  
ANISOU  980  CG  LYS A1125     3258   2764   3650   -173    143    116       C  
ATOM    981  CD  LYS A1125       9.002 -37.861 -20.669  1.00 33.24           C  
ANISOU  981  CD  LYS A1125     4265   3871   4492   -492     79   1154       C  
ATOM    982  N   SER A1126      12.596 -35.151 -23.231  1.00 14.16           N  
ANISOU  982  N   SER A1126     1235   1667   2478   -195     66   -305       N  
ATOM    983  CA  SER A1126      13.237 -34.082 -22.501  1.00 12.33           C  
ANISOU  983  CA  SER A1126     1140   1542   2002    -97    150   -148       C  
ATOM    984  C   SER A1126      14.530 -33.657 -23.147  1.00 11.22           C  
ANISOU  984  C   SER A1126     1221   1395   1646   -245     22    -74       C  
ATOM    985  O   SER A1126      15.258 -34.469 -23.714  1.00 12.07           O  
ANISOU  985  O   SER A1126     1258   1294   2033   -230     67    -61       O  
ATOM    986  CB  SER A1126      13.484 -34.464 -21.048  1.00 13.96           C  
ANISOU  986  CB  SER A1126     1608   1647   2049   -241    106    -68       C  
ATOM    987  OG  SER A1126      14.240 -35.630 -20.957  1.00 15.32           O  
ANISOU  987  OG  SER A1126     1406   1959   2455   -137    130    376       O  
ATOM    988  N   ILE A1127      14.807 -32.373 -23.008  1.00  8.85           N  
ANISOU  988  N   ILE A1127      735   1318   1310    -74     20    -91       N  
ATOM    989  CA  ILE A1127      16.042 -31.770 -23.521  1.00  8.75           C  
ANISOU  989  CA  ILE A1127      872   1171   1279   -168     41    -75       C  
ATOM    990  C   ILE A1127      16.567 -30.815 -22.470  1.00  8.66           C  
ANISOU  990  C   ILE A1127      854   1362   1071   -103    127   -116       C  
ATOM    991  O   ILE A1127      15.794 -30.105 -21.838  1.00 10.08           O  
ANISOU  991  O   ILE A1127      990   1426   1411    -51     63   -411       O  
ATOM    992  CB  ILE A1127      15.827 -31.025 -24.860  1.00 10.19           C  
ANISOU  992  CB  ILE A1127     1208   1303   1359   -214     43     10       C  
ATOM    993  CG1 ILE A1127      17.143 -30.416 -25.375  1.00 10.15           C  
ANISOU  993  CG1 ILE A1127     1212   1350   1295   -199     38     47       C  
ATOM    994  CG2 ILE A1127      14.753 -29.934 -24.740  1.00 10.49           C  
ANISOU  994  CG2 ILE A1127     1180   1468   1334   -123    -73     94       C  
ATOM    995  CD1 ILE A1127      17.064 -29.959 -26.818  1.00 10.90           C  
ANISOU  995  CD1 ILE A1127     1360   1438   1341   -236    -63    106       C  
ATOM    996  N   ALA A1128      17.886 -30.809 -22.285  1.00  7.77           N  
ANISOU  996  N   ALA A1128      829   1127    996    -40    157   -176       N  
ATOM    997  CA  ALA A1128      18.555 -29.877 -21.378  1.00  8.08           C  
ANISOU  997  CA  ALA A1128      983   1090    994    -71    -33    -62       C  
ATOM    998  C   ALA A1128      19.437 -28.911 -22.151  1.00  7.71           C  
ANISOU  998  C   ALA A1128      982    947    998    -32    -96    -38       C  
ATOM    999  O   ALA A1128      20.282 -29.321 -22.969  1.00  8.66           O  
ANISOU  999  O   ALA A1128      927   1099   1265   -131      0    -83       O  
ATOM   1000  CB  ALA A1128      19.422 -30.627 -20.385  1.00  8.76           C  
ANISOU 1000  CB  ALA A1128     1115   1043   1169     67    -50    -74       C  
ATOM   1001  N   PHE A1129      19.284 -27.634 -21.823  1.00  7.44           N  
ANISOU 1001  N   PHE A1129      838    934   1054     47     66      3       N  
ATOM   1002  CA  PHE A1129      20.187 -26.566 -22.269  1.00  7.74           C  
ANISOU 1002  CA  PHE A1129      901    969   1070    -37    -20    -22       C  
ATOM   1003  C   PHE A1129      20.997 -26.115 -21.073  1.00  7.76           C  
ANISOU 1003  C   PHE A1129      968    972   1009      0     44   -117       C  
ATOM   1004  O   PHE A1129      20.466 -25.522 -20.154  1.00  8.25           O  
ANISOU 1004  O   PHE A1129      816   1250   1069    -43     70   -238       O  
ATOM   1005  CB  PHE A1129      19.415 -25.367 -22.826  1.00  8.34           C  
ANISOU 1005  CB  PHE A1129      961   1007   1197     -5    -88     -9       C  
ATOM   1006  CG  PHE A1129      18.696 -25.645 -24.118  1.00  9.19           C  
ANISOU 1006  CG  PHE A1129     1051   1269   1170     37    -72    -94       C  
ATOM   1007  CD1 PHE A1129      19.327 -25.487 -25.331  1.00  9.22           C  
ANISOU 1007  CD1 PHE A1129     1026   1329   1148     89   -160     37       C  
ATOM   1008  CD2 PHE A1129      17.388 -26.088 -24.102  1.00  9.95           C  
ANISOU 1008  CD2 PHE A1129     1033   1632   1115     -1   -129    -21       C  
ATOM   1009  CE1 PHE A1129      18.666 -25.729 -26.525  1.00 10.35           C  
ANISOU 1009  CE1 PHE A1129     1127   1616   1188   -111   -118   -112       C  
ATOM   1010  CE2 PHE A1129      16.719 -26.344 -25.291  1.00 11.05           C  
ANISOU 1010  CE2 PHE A1129     1283   1663   1250    -52   -266   -100       C  
ATOM   1011  CZ  PHE A1129      17.359 -26.153 -26.495  1.00 10.09           C  
ANISOU 1011  CZ  PHE A1129     1001   1514   1319     61   -251    -82       C  
ATOM   1012  N   PRO A1130      22.286 -26.444 -21.065  1.00  8.27           N  
ANISOU 1012  N   PRO A1130      940   1239    963      7    -14   -151       N  
ATOM   1013  CA  PRO A1130      23.134 -25.961 -19.991  1.00  8.48           C  
ANISOU 1013  CA  PRO A1130      957   1135   1127     25    -71   -255       C  
ATOM   1014  C   PRO A1130      23.608 -24.534 -20.255  1.00  8.46           C  
ANISOU 1014  C   PRO A1130     1002   1132   1081     95    -51    -94       C  
ATOM   1015  O   PRO A1130      23.615 -24.066 -21.399  1.00  8.81           O  
ANISOU 1015  O   PRO A1130     1021   1364    962     68    -29   -197       O  
ATOM   1016  CB  PRO A1130      24.339 -26.903 -20.022  1.00  9.53           C  
ANISOU 1016  CB  PRO A1130     1117   1304   1199    157    -59   -229       C  
ATOM   1017  CG  PRO A1130      24.378 -27.444 -21.383  1.00 10.48           C  
ANISOU 1017  CG  PRO A1130     1180   1610   1190    235   -231   -282       C  
ATOM   1018  CD  PRO A1130      23.011 -27.325 -22.003  1.00  9.13           C  
ANISOU 1018  CD  PRO A1130      963   1247   1259     77    -60   -266       C  
ATOM   1019  N   ALA A1131      24.025 -23.857 -19.186  1.00  8.97           N  
ANISOU 1019  N   ALA A1131     1111   1223   1074     16    -42   -106       N  
ATOM   1020  CA  ALA A1131      24.597 -22.526 -19.316  1.00  9.47           C  
ANISOU 1020  CA  ALA A1131     1198   1118   1280    146   -148    -21       C  
ATOM   1021  C   ALA A1131      25.936 -22.678 -20.024  1.00 11.05           C  
ANISOU 1021  C   ALA A1131     1292   1405   1499     87      5    100       C  
ATOM   1022  O   ALA A1131      26.787 -23.461 -19.600  1.00 13.39           O  
ANISOU 1022  O   ALA A1131     1274   1938   1874    411      4    -35       O  
ATOM   1023  CB  ALA A1131      24.770 -21.899 -17.946  1.00 11.35           C  
ANISOU 1023  CB  ALA A1131     1449   1391   1472    -98   -141   -267       C  
ATOM   1024  N   ILE A1132      26.107 -21.948 -21.112  1.00 11.24           N  
ANISOU 1024  N   ILE A1132     1208   1694   1367    118     -5     67       N  
ATOM   1025  CA  ILE A1132      27.365 -21.946 -21.841  1.00 14.56           C  
ANISOU 1025  CA  ILE A1132     1368   2054   2107    190    312    150       C  
ATOM   1026  C   ILE A1132      28.234 -20.761 -21.454  1.00 16.96           C  
ANISOU 1026  C   ILE A1132     1791   2067   2585    -13    465    189       C  
ATOM   1027  O   ILE A1132      29.456 -20.788 -21.692  1.00 24.85           O  
ANISOU 1027  O   ILE A1132     1716   2687   5036    456    286    141       O  
ATOM   1028  CB  ILE A1132      27.123 -22.165 -23.352  1.00 20.49           C  
ANISOU 1028  CB  ILE A1132     2361   3232   2193     25    471    218       C  
ATOM   1029  CG1 ILE A1132      26.156 -21.187 -23.931  1.00 19.80           C  
ANISOU 1029  CG1 ILE A1132     2446   2928   2146     60    458    183       C  
ATOM   1030  CG2 ILE A1132      26.547 -23.552 -23.553  1.00 22.00           C  
ANISOU 1030  CG2 ILE A1132     2460   3332   2564    204    352   -244       C  
ATOM   1031  CD1 ILE A1132      26.007 -21.297 -25.425  1.00 18.96           C  
ANISOU 1031  CD1 ILE A1132     2428   2619   2155    121     90   -206       C  
ATOM   1032  N   GLY A1133      27.618 -19.767 -20.809  1.00 17.22           N  
ANISOU 1032  N   GLY A1133     1321   1678   3544    241   -339     56       N  
ATOM   1033  CA  GLY A1133      28.260 -18.538 -20.398  1.00 20.48           C  
ANISOU 1033  CA  GLY A1133     2462   1660   3656    110   -222     66       C  
ATOM   1034  C   GLY A1133      27.948 -17.553 -21.515  1.00 28.38           C  
ANISOU 1034  C   GLY A1133     3522   2407   4853    116   -483   1196       C  
ATOM   1035  O   GLY A1133      27.283 -17.919 -22.481  1.00 34.99           O  
ANISOU 1035  O   GLY A1133     3721   3929   5644   -438   -493    488       O  
ATOM   1036  N   THR A1134      28.441 -16.320 -21.401  1.00 36.32           N  
ANISOU 1036  N   THR A1134     4153   3451   6197   -861   -917    445       N  
ATOM   1037  CA  THR A1134      28.289 -15.304 -22.462  1.00 32.54           C  
ANISOU 1037  CA  THR A1134     3174   2868   6320  -2189   -245    786       C  
ATOM   1038  C   THR A1134      29.561 -15.292 -23.287  1.00 33.97           C  
ANISOU 1038  C   THR A1134     5150   3346   4409   -195    619   -596       C  
ATOM   1039  O   THR A1134      30.135 -14.213 -23.653  1.00 28.97           O  
ANISOU 1039  O   THR A1134     1952   4065   4988   -495     48   -947       O  
ATOM   1040  CB  THR A1134      27.905 -13.920 -21.887  1.00 41.95           C  
ANISOU 1040  CB  THR A1134     5550   4757   5629  -1315   -210   -425       C  
ATOM   1041  OG1 THR A1134      27.883 -12.929 -22.938  1.00 54.62           O  
ANISOU 1041  OG1 THR A1134     6252   7206   7292   -747   -468   1463       O  
ATOM   1042  CG2 THR A1134      28.866 -13.467 -20.745  1.00 41.85           C  
ANISOU 1042  CG2 THR A1134     5454   4343   6100  -2780   -248     10       C  
ATOM   1043  N   GLY A1135      30.009 -16.500 -23.627  1.00 31.18           N  
ANISOU 1043  N   GLY A1135     2868   3400   5578    686   -338    383       N  
ATOM   1044  CA  GLY A1135      31.341 -16.642 -24.219  1.00 36.86           C  
ANISOU 1044  CA  GLY A1135     4236   5223   4546    584    755    670       C  
ATOM   1045  C   GLY A1135      31.314 -16.091 -25.626  1.00 29.93           C  
ANISOU 1045  C   GLY A1135     3429   3367   4575  -1490   -352    687       C  
ATOM   1046  O   GLY A1135      30.589 -16.642 -26.490  1.00 28.49           O  
ANISOU 1046  O   GLY A1135     3237   4164   3420   -531     97     44       O  
ATOM   1047  N   ASN A1136      32.043 -14.982 -25.839  1.00 21.71           N  
ANISOU 1047  N   ASN A1136     3064   3139   2045  -1818  -1517   -424       N  
ATOM   1048  CA  ASN A1136      32.200 -14.379 -27.158  1.00 22.74           C  
ANISOU 1048  CA  ASN A1136     2438   2876   3325    -73   -784    695       C  
ATOM   1049  C   ASN A1136      30.849 -13.812 -27.691  1.00 21.80           C  
ANISOU 1049  C   ASN A1136     2010   2662   3608   -479  -1206   -328       C  
ATOM   1050  O   ASN A1136      30.715 -13.555 -28.860  1.00 24.98           O  
ANISOU 1050  O   ASN A1136     2472   2779   4238   -329   -781    362       O  
ATOM   1051  CB  ASN A1136      32.782 -15.381 -28.185  1.00 27.12           C  
ANISOU 1051  CB  ASN A1136     3187   2920   4197   -333   -312    452       C  
ATOM   1052  CG  ASN A1136      34.255 -15.686 -27.963  1.00 27.09           C  
ANISOU 1052  CG  ASN A1136     2871   3493   3927    -15   1118    -44       C  
ATOM   1053  OD1 ASN A1136      35.090 -14.789 -27.984  1.00 38.10           O  
ANISOU 1053  OD1 ASN A1136     4592   4938   4944  -1583    633   -460       O  
ATOM   1054  ND2 ASN A1136      34.574 -16.955 -27.781  1.00 37.24           N  
ANISOU 1054  ND2 ASN A1136     4647   4071   5430    845   1031    384       N  
ATOM   1055  N   LEU A1137      29.852 -13.649 -26.832  1.00 21.04           N  
ANISOU 1055  N   LEU A1137     2785   2292   2915    412  -1174    132       N  
ATOM   1056  CA  LEU A1137      28.606 -13.037 -27.251  1.00 20.34           C  
ANISOU 1056  CA  LEU A1137     2589   2427   2711    761   -346   -257       C  
ATOM   1057  C   LEU A1137      28.581 -11.750 -26.443  1.00 23.20           C  
ANISOU 1057  C   LEU A1137     3626   1504   3684   -207    313    116       C  
ATOM   1058  O   LEU A1137      29.138 -11.666 -25.344  1.00 31.78           O  
ANISOU 1058  O   LEU A1137     4795   2512   4767   -695   -436   -302       O  
ATOM   1059  CB  LEU A1137      27.411 -13.935 -26.983  1.00 23.80           C  
ANISOU 1059  CB  LEU A1137     3640   1517   3884    463   -186   -348       C  
ATOM   1060  CG  LEU A1137      27.289 -15.047 -28.040  1.00 28.71           C  
ANISOU 1060  CG  LEU A1137     3995   2982   3930    168    -86   -833       C  
ATOM   1061  CD1 LEU A1137      26.436 -16.163 -27.490  1.00 31.75           C  
ANISOU 1061  CD1 LEU A1137     4478   2957   4628    472    405    151       C  
ATOM   1062  CD2 LEU A1137      26.723 -14.570 -29.388  1.00 32.85           C  
ANISOU 1062  CD2 LEU A1137     4478   3881   4119    389     33   -305       C  
ATOM   1063  N   GLY A1138      27.956 -10.753 -26.998  1.00 18.79           N  
ANISOU 1063  N   GLY A1138     1549   3024   2564    -30     74    -88       N  
ATOM   1064  CA  GLY A1138      28.023  -9.430 -26.490  1.00 17.55           C  
ANISOU 1064  CA  GLY A1138     1853   2724   2089     11     43    155       C  
ATOM   1065  C   GLY A1138      26.841  -8.995 -25.674  1.00 13.84           C  
ANISOU 1065  C   GLY A1138     1370   1824   2065   -375    -66    375       C  
ATOM   1066  O   GLY A1138      26.668  -7.808 -25.503  1.00 17.03           O  
ANISOU 1066  O   GLY A1138     2227   1738   2505   -740   -514     24       O  
ATOM   1067  N   PHE A1139      26.038  -9.933 -25.163  1.00 15.71           N  
ANISOU 1067  N   PHE A1139     1892   1606   2470   -458    250    243       N  
ATOM   1068  CA  PHE A1139      24.876  -9.579 -24.375  1.00 15.19           C  
ANISOU 1068  CA  PHE A1139     1965   1641   2162   -151     89    147       C  
ATOM   1069  C   PHE A1139      24.991 -10.184 -22.981  1.00 16.80           C  
ANISOU 1069  C   PHE A1139     2428   1590   2363   -143    125    307       C  
ATOM   1070  O   PHE A1139      25.578 -11.265 -22.799  1.00 19.58           O  
ANISOU 1070  O   PHE A1139     2695   1682   3062    119    191    180       O  
ATOM   1071  CB  PHE A1139      23.581 -10.051 -25.010  1.00 15.88           C  
ANISOU 1071  CB  PHE A1139     1904   1792   2335    -93    193   -127       C  
ATOM   1072  CG  PHE A1139      23.322  -9.470 -26.348  1.00 13.67           C  
ANISOU 1072  CG  PHE A1139     1322   1728   2144     41    108   -375       C  
ATOM   1073  CD1 PHE A1139      22.701  -8.229 -26.480  1.00 15.35           C  
ANISOU 1073  CD1 PHE A1139     1965   1643   2222     15      8   -125       C  
ATOM   1074  CD2 PHE A1139      23.709 -10.145 -27.499  1.00 14.82           C  
ANISOU 1074  CD2 PHE A1139     1710   1695   2226    -37    111   -468       C  
ATOM   1075  CE1 PHE A1139      22.465  -7.684 -27.731  1.00 14.84           C  
ANISOU 1075  CE1 PHE A1139     1747   1866   2023   -127    -55   -271       C  
ATOM   1076  CE2 PHE A1139      23.461  -9.611 -28.733  1.00 16.08           C  
ANISOU 1076  CE2 PHE A1139     1633   2291   2185     -7     72   -389       C  
ATOM   1077  CZ  PHE A1139      22.845  -8.388 -28.855  1.00 15.98           C  
ANISOU 1077  CZ  PHE A1139     1969   2125   1975   -152    216   -151       C  
ATOM   1078  N   PRO A1140      24.429  -9.499 -21.996  1.00 15.78           N  
ANISOU 1078  N   PRO A1140     2520   1464   2011   -138    -13    346       N  
ATOM   1079  CA  PRO A1140      24.369 -10.023 -20.634  1.00 17.68           C  
ANISOU 1079  CA  PRO A1140     2781   1685   2250   -288   -131    640       C  
ATOM   1080  C   PRO A1140      23.517 -11.262 -20.495  1.00 16.37           C  
ANISOU 1080  C   PRO A1140     2399   1771   2049   -272   -288    511       C  
ATOM   1081  O   PRO A1140      22.602 -11.503 -21.270  1.00 15.31           O  
ANISOU 1081  O   PRO A1140     2301   1779   1734     57   -202    314       O  
ATOM   1082  CB  PRO A1140      23.721  -8.891 -19.856  1.00 19.64           C  
ANISOU 1082  CB  PRO A1140     2881   2229   2349   -236    115    341       C  
ATOM   1083  CG  PRO A1140      24.084  -7.661 -20.619  1.00 19.27           C  
ANISOU 1083  CG  PRO A1140     2926   2093   2300   -122     58    272       C  
ATOM   1084  CD  PRO A1140      24.099  -8.063 -22.043  1.00 16.94           C  
ANISOU 1084  CD  PRO A1140     2619   1537   2280     14      6    351       C  
ATOM   1085  N   LYS A1141      23.802 -12.029 -19.463  1.00 15.54           N  
ANISOU 1085  N   LYS A1141     2212   1591   2099   -115   -480    357       N  
ATOM   1086  CA  LYS A1141      23.049 -13.242 -19.194  1.00 15.43           C  
ANISOU 1086  CA  LYS A1141     2351   1573   1938   -104   -289    394       C  
ATOM   1087  C   LYS A1141      21.516 -13.023 -19.103  1.00 13.73           C  
ANISOU 1087  C   LYS A1141     2361   1127   1726   -190   -403    336       C  
ATOM   1088  O   LYS A1141      20.760 -13.880 -19.516  1.00 13.80           O  
ANISOU 1088  O   LYS A1141     2186   1247   1809    -76   -421     52       O  
ATOM   1089  CB  LYS A1141      23.643 -13.919 -17.927  1.00 15.60           C  
ANISOU 1089  CB  LYS A1141     2662   1503   1762     36   -218    269       C  
ATOM   1090  CG  LYS A1141      24.990 -14.596 -18.233  1.00 17.08           C  
ANISOU 1090  CG  LYS A1141     2083   1959   2445   -284   -410    329       C  
ATOM   1091  CD  LYS A1141      25.704 -15.124 -17.001  1.00 20.02           C  
ANISOU 1091  CD  LYS A1141     2578   2549   2480    -49   -580    136       C  
ATOM   1092  CE  LYS A1141      26.840 -16.088 -17.353  1.00 22.50           C  
ANISOU 1092  CE  LYS A1141     2510   3055   2984     73   -284    179       C  
ATOM   1093  NZ  LYS A1141      27.552 -16.642 -16.134  1.00 22.91           N  
ANISOU 1093  NZ  LYS A1141     2571   3523   2607   -298   -328     84       N  
ATOM   1094  N   ASN A1142      21.045 -11.891 -18.574  1.00 15.53           N  
ANISOU 1094  N   ASN A1142     2625   1595   1679     13   -296     59       N  
ATOM   1095  CA  ASN A1142      19.599 -11.706 -18.435  1.00 16.23           C  
ANISOU 1095  CA  ASN A1142     2674   1721   1770    -61   -140     99       C  
ATOM   1096  C   ASN A1142      18.905 -11.627 -19.813  1.00 14.30           C  
ANISOU 1096  C   ASN A1142     2153   1438   1840    -45   -160     70       C  
ATOM   1097  O   ASN A1142      17.758 -12.058 -19.952  1.00 14.85           O  
ANISOU 1097  O   ASN A1142     2115   1473   2053     13    134    -29       O  
ATOM   1098  CB  ASN A1142      19.214 -10.534 -17.505  1.00 18.99           C  
ANISOU 1098  CB  ASN A1142     2822   1950   2441   -147    201   -212       C  
ATOM   1099  CG  ASN A1142      19.745  -9.183 -17.949  1.00 22.05           C  
ANISOU 1099  CG  ASN A1142     3809   1645   2923    -77     98   -331       C  
ATOM   1100  OD1 ASN A1142      20.441  -9.035 -18.927  1.00 23.81           O  
ANISOU 1100  OD1 ASN A1142     4047   1733   3264   -400     97     26       O  
ATOM   1101  ND2 ASN A1142      19.459  -8.187 -17.143  1.00 31.68           N  
ANISOU 1101  ND2 ASN A1142     4588   2362   5084     95   1370  -1211       N  
ATOM   1102  N   ILE A1143      19.623 -11.127 -20.823  1.00 12.84           N  
ANISOU 1102  N   ILE A1143     1986   1123   1768    -69   -387    186       N  
ATOM   1103  CA  ILE A1143      19.106 -11.098 -22.196  1.00 13.26           C  
ANISOU 1103  CA  ILE A1143     1884   1500   1654    153   -199     55       C  
ATOM   1104  C   ILE A1143      18.879 -12.544 -22.681  1.00 11.87           C  
ANISOU 1104  C   ILE A1143     1472   1523   1515     29   -214     99       C  
ATOM   1105  O   ILE A1143      17.834 -12.877 -23.270  1.00 12.37           O  
ANISOU 1105  O   ILE A1143     1425   1424   1849    230   -369    112       O  
ATOM   1106  CB  ILE A1143      20.076 -10.363 -23.186  1.00 15.28           C  
ANISOU 1106  CB  ILE A1143     2184   1464   2156     26   -166    337       C  
ATOM   1107  CG1 ILE A1143      20.393  -8.894 -22.782  1.00 18.23           C  
ANISOU 1107  CG1 ILE A1143     2732   1802   2391    -58   -346    -28       C  
ATOM   1108  CG2 ILE A1143      19.525 -10.423 -24.597  1.00 16.32           C  
ANISOU 1108  CG2 ILE A1143     2367   1701   2131     35   -173    276       C  
ATOM   1109  CD1 ILE A1143      19.196  -8.061 -22.407  1.00 20.79           C  
ANISOU 1109  CD1 ILE A1143     2919   2270   2708    219   -258    -13       C  
ATOM   1110  N   PHE A1144      19.871 -13.405 -22.454  1.00 12.18           N  
ANISOU 1110  N   PHE A1144     1584   1306   1737    -25   -333     56       N  
ATOM   1111  CA  PHE A1144      19.785 -14.805 -22.888  1.00 10.70           C  
ANISOU 1111  CA  PHE A1144     1348   1367   1349     51    -46    -69       C  
ATOM   1112  C   PHE A1144      18.754 -15.629 -22.116  1.00  9.96           C  
ANISOU 1112  C   PHE A1144     1411   1106   1266    160   -174    170       C  
ATOM   1113  O   PHE A1144      18.114 -16.508 -22.694  1.00 10.36           O  
ANISOU 1113  O   PHE A1144     1373   1233   1331    196   -279    138       O  
ATOM   1114  CB  PHE A1144      21.144 -15.478 -22.866  1.00 11.54           C  
ANISOU 1114  CB  PHE A1144     1313   1357   1712      8   -117    -12       C  
ATOM   1115  CG  PHE A1144      22.031 -15.005 -23.972  1.00 13.84           C  
ANISOU 1115  CG  PHE A1144     1469   1739   2050    111    195     16       C  
ATOM   1116  CD1 PHE A1144      21.710 -15.295 -25.300  1.00 14.77           C  
ANISOU 1116  CD1 PHE A1144     1852   1766   1993    218    359    117       C  
ATOM   1117  CD2 PHE A1144      23.149 -14.225 -23.703  1.00 15.27           C  
ANISOU 1117  CD2 PHE A1144     1965   1527   2308   -105    298   -187       C  
ATOM   1118  CE1 PHE A1144      22.490 -14.808 -26.339  1.00 17.45           C  
ANISOU 1118  CE1 PHE A1144     2164   2321   2144    147    714    -93       C  
ATOM   1119  CE2 PHE A1144      23.945 -13.752 -24.746  1.00 16.67           C  
ANISOU 1119  CE2 PHE A1144     2064   1574   2696   -385    478    -75       C  
ATOM   1120  CZ  PHE A1144      23.615 -14.053 -26.051  1.00 18.04           C  
ANISOU 1120  CZ  PHE A1144     2603   1717   2532    -77    569    245       C  
ATOM   1121  N   ALA A1145      18.559 -15.315 -20.840  1.00 10.41           N  
ANISOU 1121  N   ALA A1145     1317   1322   1316     33   -222     46       N  
ATOM   1122  CA  ALA A1145      17.544 -16.004 -20.028  1.00 11.29           C  
ANISOU 1122  CA  ALA A1145     1664   1333   1291     68     70      6       C  
ATOM   1123  C   ALA A1145      16.152 -15.700 -20.591  1.00 12.00           C  
ANISOU 1123  C   ALA A1145     1784   1369   1403    142    -11   -126       C  
ATOM   1124  O   ALA A1145      15.345 -16.613 -20.832  1.00 12.22           O  
ANISOU 1124  O   ALA A1145     1795   1321   1524    114    132   -179       O  
ATOM   1125  CB  ALA A1145      17.643 -15.574 -18.581  1.00 12.21           C  
ANISOU 1125  CB  ALA A1145     1720   1581   1337   -137     -5    -26       C  
ATOM   1126  N   GLU A1146      15.873 -14.417 -20.826  1.00 12.98           N  
ANISOU 1126  N   GLU A1146     1889   1365   1678    174   -183    -32       N  
ATOM   1127  CA AGLU A1146      14.588 -14.031 -21.442  0.70 14.19           C  
ANISOU 1127  CA AGLU A1146     1730   1708   1951     79    -83     50       C  
ATOM   1128  CA BGLU A1146      14.601 -14.019 -21.442  0.30 14.03           C  
ANISOU 1128  CA BGLU A1146     1739   1703   1888    132    -72     64       C  
ATOM   1129  C   GLU A1146      14.456 -14.679 -22.805  1.00 13.18           C  
ANISOU 1129  C   GLU A1146     1617   1553   1838    146     35    127       C  
ATOM   1130  O   GLU A1146      13.392 -15.182 -23.152  1.00 13.58           O  
ANISOU 1130  O   GLU A1146     1614   1614   1929    160    -44     99       O  
ATOM   1131  CB AGLU A1146      14.465 -12.516 -21.587  0.70 16.57           C  
ANISOU 1131  CB AGLU A1146     2352   1704   2239    233     32    -56       C  
ATOM   1132  CB BGLU A1146      14.515 -12.501 -21.604  0.30 15.66           C  
ANISOU 1132  CB BGLU A1146     2167   1702   2079    199      1      0       C  
ATOM   1133  CG AGLU A1146      13.061 -12.029 -21.935  0.70 20.97           C  
ANISOU 1133  CG AGLU A1146     2623   2168   3177    634      0    155       C  
ATOM   1134  CG BGLU A1146      13.193 -12.026 -22.186  0.30 17.80           C  
ANISOU 1134  CG BGLU A1146     2370   2044   2349    415   -139    -31       C  
ATOM   1135  CD AGLU A1146      12.700 -12.096 -23.417  0.70 24.07           C  
ANISOU 1135  CD AGLU A1146     3276   2475   3392    823    -82    243       C  
ATOM   1136  CD BGLU A1146      13.160 -10.543 -22.473  0.30 21.40           C  
ANISOU 1136  CD BGLU A1146     3083   2143   2901    458   -155    224       C  
ATOM   1137  OE1AGLU A1146      13.595 -12.112 -24.278  0.70 28.21           O  
ANISOU 1137  OE1AGLU A1146     3988   2430   4298   1530    672    319       O  
ATOM   1138  OE1BGLU A1146      14.146  -9.846 -22.188  0.30 24.44           O  
ANISOU 1138  OE1BGLU A1146     3463   2280   3541    455   -642    -23       O  
ATOM   1139  OE2AGLU A1146      11.495 -12.120 -23.736  0.70 29.83           O  
ANISOU 1139  OE2AGLU A1146     2890   2760   5684    766    362   -111       O  
ATOM   1140  OE2BGLU A1146      12.133 -10.082 -22.999  0.30 24.43           O  
ANISOU 1140  OE2BGLU A1146     3155   2269   3858    984    -95    -67       O  
ATOM   1141  N   LEU A1147      15.539 -14.659 -23.581  1.00 11.58           N  
ANISOU 1141  N   LEU A1147     1496   1335   1567    144   -101    173       N  
ATOM   1142  CA  LEU A1147      15.485 -15.203 -24.944  1.00 10.22           C  
ANISOU 1142  CA  LEU A1147     1086   1351   1445    749   -531    342       C  
ATOM   1143  C   LEU A1147      15.068 -16.672 -24.945  1.00  9.26           C  
ANISOU 1143  C   LEU A1147     1055   1347   1114    360   -173     91       C  
ATOM   1144  O   LEU A1147      14.196 -17.091 -25.711  1.00 10.52           O  
ANISOU 1144  O   LEU A1147     1283   1485   1228    202   -271     67       O  
ATOM   1145  CB  LEU A1147      16.844 -15.029 -25.629  1.00  9.48           C  
ANISOU 1145  CB  LEU A1147     1101   1158   1341    735   -443    329       C  
ATOM   1146  CG  LEU A1147      16.954 -15.439 -27.104  1.00 13.39           C  
ANISOU 1146  CG  LEU A1147     1662   1910   1516    123   -183     92       C  
ATOM   1147  CD1 LEU A1147      18.068 -14.665 -27.772  1.00 18.97           C  
ANISOU 1147  CD1 LEU A1147     2172   2768   2267   -316    123    155       C  
ATOM   1148  CD2 LEU A1147      17.219 -16.924 -27.304  1.00 19.42           C  
ANISOU 1148  CD2 LEU A1147     2576   2072   2729    175   -345    -82       C  
ATOM   1149  N   ILE A1148      15.727 -17.476 -24.132  1.00  8.82           N  
ANISOU 1149  N   ILE A1148     1018   1217   1116    175   -200    119       N  
ATOM   1150  CA  ILE A1148      15.460 -18.921 -24.205  1.00  9.60           C  
ANISOU 1150  CA  ILE A1148     1058   1222   1365    181    -31     68       C  
ATOM   1151  C   ILE A1148      14.055 -19.282 -23.669  1.00  9.68           C  
ANISOU 1151  C   ILE A1148     1115   1233   1330    174     50     98       C  
ATOM   1152  O   ILE A1148      13.340 -20.122 -24.246  1.00 10.08           O  
ANISOU 1152  O   ILE A1148     1151   1285   1391    115     38    105       O  
ATOM   1153  CB  ILE A1148      16.597 -19.778 -23.582  1.00  9.35           C  
ANISOU 1153  CB  ILE A1148     1026   1285   1242    123    -42    174       C  
ATOM   1154  CG1 ILE A1148      16.404 -21.260 -23.937  1.00  9.65           C  
ANISOU 1154  CG1 ILE A1148      994   1427   1244      4   -220      5       C  
ATOM   1155  CG2 ILE A1148      16.719 -19.595 -22.088  1.00  9.54           C  
ANISOU 1155  CG2 ILE A1148     1117   1219   1288    -58    -48    -60       C  
ATOM   1156  CD1 ILE A1148      17.620 -22.130 -23.697  1.00 10.37           C  
ANISOU 1156  CD1 ILE A1148     1059   1384   1495    101     51     -9       C  
ATOM   1157  N   ILE A1149      13.667 -18.628 -22.588  1.00  9.97           N  
ANISOU 1157  N   ILE A1149     1085   1342   1362     12    110     -6       N  
ATOM   1158  CA  ILE A1149      12.345 -18.874 -22.010  1.00 11.68           C  
ANISOU 1158  CA  ILE A1149     1151   1607   1680     86    303     25       C  
ATOM   1159  C   ILE A1149      11.271 -18.443 -22.993  1.00 12.28           C  
ANISOU 1159  C   ILE A1149     1378   1722   1563    102    235     -8       C  
ATOM   1160  O   ILE A1149      10.289 -19.164 -23.196  1.00 13.06           O  
ANISOU 1160  O   ILE A1149     1246   1685   2031    121    198    247       O  
ATOM   1161  CB  ILE A1149      12.171 -18.209 -20.633  1.00 12.87           C  
ANISOU 1161  CB  ILE A1149     1530   1662   1697     -9    327      7       C  
ATOM   1162  CG1 ILE A1149      13.169 -18.832 -19.638  1.00 12.87           C  
ANISOU 1162  CG1 ILE A1149     1653   1615   1622    120    360     23       C  
ATOM   1163  CG2 ILE A1149      10.727 -18.375 -20.147  1.00 14.27           C  
ANISOU 1163  CG2 ILE A1149     1484   1970   1967    300    384    -80       C  
ATOM   1164  CD1 ILE A1149      13.328 -18.087 -18.331  1.00 13.97           C  
ANISOU 1164  CD1 ILE A1149     1823   1798   1687     62     87     26       C  
ATOM   1165  N   SER A1150      11.442 -17.281 -23.600  1.00 13.22           N  
ANISOU 1165  N   SER A1150     1301   1920   1799    188     94    266       N  
ATOM   1166  CA  SER A1150      10.464 -16.819 -24.588  1.00 14.42           C  
ANISOU 1166  CA  SER A1150     1567   1860   2051     34   -279    177       C  
ATOM   1167  C   SER A1150      10.370 -17.758 -25.788  1.00 12.93           C  
ANISOU 1167  C   SER A1150     1437   1582   1892    125     32    366       C  
ATOM   1168  O   SER A1150       9.286 -17.993 -26.306  1.00 17.08           O  
ANISOU 1168  O   SER A1150     1540   2126   2822    203   -413    406       O  
ATOM   1169  CB  SER A1150      10.772 -15.399 -25.049  1.00 17.92           C  
ANISOU 1169  CB  SER A1150     2192   1966   2651   -151   -243    328       C  
ATOM   1170  OG  SER A1150      10.507 -14.485 -23.983  1.00 21.71           O  
ANISOU 1170  OG  SER A1150     2635   2225   3386    248   -242    -10       O  
ATOM   1171  N   GLU A1151      11.499 -18.296 -26.225  1.00 13.65           N  
ANISOU 1171  N   GLU A1151     1377   1860   1948    150    -18    305       N  
ATOM   1172  CA  GLU A1151      11.487 -19.212 -27.336  1.00 13.26           C  
ANISOU 1172  CA  GLU A1151     1549   1565   1924    132     46    339       C  
ATOM   1173  C   GLU A1151      10.775 -20.525 -26.961  1.00 12.22           C  
ANISOU 1173  C   GLU A1151     1143   1868   1630    -16    147    305       C  
ATOM   1174  O   GLU A1151      10.045 -21.092 -27.770  1.00 14.65           O  
ANISOU 1174  O   GLU A1151     1681   2244   1639   -137   -287    507       O  
ATOM   1175  CB  GLU A1151      12.912 -19.472 -27.868  1.00 14.48           C  
ANISOU 1175  CB  GLU A1151     1449   2134   1917    116   -103    232       C  
ATOM   1176  CG  GLU A1151      12.968 -20.413 -29.067  1.00 16.38           C  
ANISOU 1176  CG  GLU A1151     2113   2369   1740     50   -138    333       C  
ATOM   1177  CD  GLU A1151      12.089 -19.954 -30.225  1.00 22.07           C  
ANISOU 1177  CD  GLU A1151     2530   3288   2566    525   -727    304       C  
ATOM   1178  OE1 GLU A1151      11.488 -20.828 -30.884  1.00 29.02           O  
ANISOU 1178  OE1 GLU A1151     3081   5389   2554    357  -1315   -584       O  
ATOM   1179  OE2 GLU A1151      12.018 -18.737 -30.480  1.00 23.42           O  
ANISOU 1179  OE2 GLU A1151     3215   3654   2027    455    -44   1012       O  
ATOM   1180  N   VAL A1152      10.983 -21.018 -25.750  1.00 11.16           N  
ANISOU 1180  N   VAL A1152     1128   1491   1617     58   -119    121       N  
ATOM   1181  CA  VAL A1152      10.239 -22.205 -25.312  1.00 11.95           C  
ANISOU 1181  CA  VAL A1152     1249   1625   1664    -54    -71    135       C  
ATOM   1182  C   VAL A1152       8.719 -21.929 -25.316  1.00 13.81           C  
ANISOU 1182  C   VAL A1152     1266   2134   1845    -43   -113    137       C  
ATOM   1183  O   VAL A1152       7.931 -22.762 -25.787  1.00 16.43           O  
ANISOU 1183  O   VAL A1152     1885   2148   2209   -266   -157      1       O  
ATOM   1184  CB  VAL A1152      10.730 -22.712 -23.945  1.00 13.88           C  
ANISOU 1184  CB  VAL A1152     1892   1943   1438     39   -123    -85       C  
ATOM   1185  CG1 VAL A1152       9.926 -23.908 -23.474  1.00 16.85           C  
ANISOU 1185  CG1 VAL A1152     2132   2274   1993    -80     87     34       C  
ATOM   1186  CG2 VAL A1152      12.189 -23.138 -24.053  1.00 13.34           C  
ANISOU 1186  CG2 VAL A1152     1963   1623   1481    199   -438    159       C  
ATOM   1187  N   PHE A1153       8.326 -20.760 -24.823  1.00 15.49           N  
ANISOU 1187  N   PHE A1153     1486   2143   2256    -56   -235     26       N  
ATOM   1188  CA  PHE A1153       6.920 -20.329 -24.863  1.00 17.03           C  
ANISOU 1188  CA  PHE A1153     1456   2352   2659    -62   -290      3       C  
ATOM   1189  C   PHE A1153       6.400 -20.283 -26.299  1.00 16.14           C  
ANISOU 1189  C   PHE A1153     1623   2151   2358    192    100     58       C  
ATOM   1190  O   PHE A1153       5.320 -20.804 -26.609  1.00 19.10           O  
ANISOU 1190  O   PHE A1153     1842   2920   2492    -71   -337    229       O  
ATOM   1191  CB  PHE A1153       6.749 -18.936 -24.257  1.00 18.05           C  
ANISOU 1191  CB  PHE A1153     1655   2574   2628     22     17   -190       C  
ATOM   1192  CG  PHE A1153       6.467 -18.913 -22.785  1.00 18.67           C  
ANISOU 1192  CG  PHE A1153     1978   2500   2615   -182   -104    119       C  
ATOM   1193  CD1 PHE A1153       7.273 -19.576 -21.884  1.00 19.61           C  
ANISOU 1193  CD1 PHE A1153     2250   2894   2306     70   -116    -52       C  
ATOM   1194  CD2 PHE A1153       5.382 -18.176 -22.297  1.00 19.70           C  
ANISOU 1194  CD2 PHE A1153     1957   2740   2789   -250    -85   -129       C  
ATOM   1195  CE1 PHE A1153       6.982 -19.535 -20.526  1.00 20.70           C  
ANISOU 1195  CE1 PHE A1153     2708   2817   2339    -27    -77   -314       C  
ATOM   1196  CE2 PHE A1153       5.101 -18.125 -20.951  1.00 21.46           C  
ANISOU 1196  CE2 PHE A1153     2496   2871   2784     -9   -103   -455       C  
ATOM   1197  CZ  PHE A1153       5.910 -18.799 -20.059  1.00 21.45           C  
ANISOU 1197  CZ  PHE A1153     2450   3211   2487    -14   -140   -467       C  
ATOM   1198  N   SER A1154       7.157 -19.643 -27.169  1.00 17.94           N  
ANISOU 1198  N   SER A1154     1643   2607   2567    -90   -182    445       N  
ATOM   1199  CA  SER A1154       6.759 -19.480 -28.562  1.00 20.83           C  
ANISOU 1199  CA  SER A1154     2281   2942   2689   -135   -423    536       C  
ATOM   1200  C   SER A1154       6.561 -20.819 -29.267  1.00 17.43           C  
ANISOU 1200  C   SER A1154     1755   2892   1973    -30   -515    704       C  
ATOM   1201  O   SER A1154       5.531 -21.079 -29.891  1.00 20.40           O  
ANISOU 1201  O   SER A1154     1610   3385   2755    -72   -568    206       O  
ATOM   1202  CB  SER A1154       7.807 -18.663 -29.317  1.00 21.94           C  
ANISOU 1202  CB  SER A1154     2863   3046   2425   -143    -83    626       C  
ATOM   1203  OG  SER A1154       7.335 -18.441 -30.622  1.00 28.58           O  
ANISOU 1203  OG  SER A1154     3503   4403   2951    101   -361   1194       O  
ATOM   1204  N   PHE A1155       7.560 -21.671 -29.133  1.00 17.46           N  
ANISOU 1204  N   PHE A1155     1364   3026   2241    -99   -293    288       N  
ATOM   1205  CA  PHE A1155       7.577 -22.951 -29.790  1.00 17.54           C  
ANISOU 1205  CA  PHE A1155     1706   2823   2134   -152   -394    483       C  
ATOM   1206  C   PHE A1155       6.388 -23.820 -29.378  1.00 16.76           C  
ANISOU 1206  C   PHE A1155     1831   2755   1782   -269   -453    209       C  
ATOM   1207  O   PHE A1155       5.679 -24.369 -30.217  1.00 19.21           O  
ANISOU 1207  O   PHE A1155     1689   3376   2231   -624   -503      0       O  
ATOM   1208  CB  PHE A1155       8.912 -23.650 -29.496  1.00 18.85           C  
ANISOU 1208  CB  PHE A1155     1800   2941   2418    -22   -408    249       C  
ATOM   1209  CG  PHE A1155       9.033 -24.993 -30.139  1.00 18.82           C  
ANISOU 1209  CG  PHE A1155     1713   2998   2438    -78   -174     19       C  
ATOM   1210  CD1 PHE A1155       9.157 -25.095 -31.514  1.00 20.64           C  
ANISOU 1210  CD1 PHE A1155     2442   2849   2549   -377    325     34       C  
ATOM   1211  CD2 PHE A1155       8.968 -26.152 -29.387  1.00 18.14           C  
ANISOU 1211  CD2 PHE A1155     1447   3073   2372    -73    -49     66       C  
ATOM   1212  CE1 PHE A1155       9.245 -26.345 -32.119  1.00 22.69           C  
ANISOU 1212  CE1 PHE A1155     2763   2948   2908   -220    -24   -168       C  
ATOM   1213  CE2 PHE A1155       9.067 -27.393 -29.987  1.00 21.09           C  
ANISOU 1213  CE2 PHE A1155     2343   3125   2543    -12   -283    -15       C  
ATOM   1214  CZ  PHE A1155       9.217 -27.487 -31.349  1.00 21.50           C  
ANISOU 1214  CZ  PHE A1155     2518   2958   2693   -285    153   -196       C  
ATOM   1215  N   SER A1156       6.159 -23.894 -28.080  1.00 17.38           N  
ANISOU 1215  N   SER A1156     1783   3050   1771    127   -294    122       N  
ATOM   1216  CA  SER A1156       5.089 -24.716 -27.531  1.00 18.93           C  
ANISOU 1216  CA  SER A1156     1863   2779   2549     63   -227     47       C  
ATOM   1217  C   SER A1156       3.693 -24.151 -27.801  1.00 19.33           C  
ANISOU 1217  C   SER A1156     1693   3052   2598     -7   -217   -175       C  
ATOM   1218  O   SER A1156       2.739 -24.902 -27.801  1.00 21.48           O  
ANISOU 1218  O   SER A1156     1735   4047   2378   -411    145   -259       O  
ATOM   1219  CB  SER A1156       5.286 -24.952 -26.023  1.00 20.22           C  
ANISOU 1219  CB  SER A1156     2260   2834   2585    187   -113    334       C  
ATOM   1220  OG  SER A1156       5.352 -23.748 -25.297  1.00 20.17           O  
ANISOU 1220  OG  SER A1156     2535   3372   1753   -527    -60    270       O  
ATOM   1221  N   SER A1157       3.561 -22.844 -28.016  1.00 21.77           N  
ANISOU 1221  N   SER A1157     1725   3357   3188    341    -70    120       N  
ATOM   1222  CA  SER A1157       2.238 -22.279 -28.329  1.00 23.87           C  
ANISOU 1222  CA  SER A1157     1550   3991   3527    177   -423   -170       C  
ATOM   1223  C   SER A1157       1.860 -22.522 -29.781  1.00 27.13           C  
ANISOU 1223  C   SER A1157     2134   4568   3604    -72   -785   -151       C  
ATOM   1224  O   SER A1157       0.681 -22.629 -30.077  1.00 33.68           O  
ANISOU 1224  O   SER A1157     1716   5830   5249    532   -451   -699       O  
ATOM   1225  CB  SER A1157       2.122 -20.783 -27.989  1.00 32.07           C  
ANISOU 1225  CB  SER A1157     3430   3916   4838   -262   -745   -303       C  
ATOM   1226  OG  SER A1157       2.959 -19.995 -28.807  1.00 38.27           O  
ANISOU 1226  OG  SER A1157     3692   4852   5995    310   -430    747       O  
ATOM   1227  N   SER A1158       2.847 -22.621 -30.673  1.00 25.58           N  
ANISOU 1227  N   SER A1158     2765   4386   2566    -58   -788   -293       N  
ATOM   1228  CA  SER A1158       2.612 -22.704 -32.128  1.00 28.73           C  
ANISOU 1228  CA  SER A1158     4031   4280   2603   -309   -894     38       C  
ATOM   1229  C   SER A1158       2.693 -24.146 -32.688  1.00 28.88           C  
ANISOU 1229  C   SER A1158     3855   4258   2858   -359  -1213    -25       C  
ATOM   1230  O   SER A1158       2.467 -24.356 -33.888  1.00 34.44           O  
ANISOU 1230  O   SER A1158     4802   5177   3104   -103  -1749   -319       O  
ATOM   1231  CB  SER A1158       3.611 -21.780 -32.853  1.00 29.02           C  
ANISOU 1231  CB  SER A1158     4164   4445   2418   -492   -634    -94       C  
ATOM   1232  N   ASN A1159       2.995 -25.125 -31.821  1.00 28.52           N  
ANISOU 1232  N   ASN A1159     3085   4030   3720   -439  -1338    298       N  
ATOM   1233  CA  ASN A1159       3.195 -26.536 -32.205  1.00 29.53           C  
ANISOU 1233  CA  ASN A1159     3138   4235   3845   -335   -793   -187       C  
ATOM   1234  C   ASN A1159       2.486 -27.512 -31.269  1.00 30.92           C  
ANISOU 1234  C   ASN A1159     4203   3730   3814    -13  -1171    295       C  
ATOM   1235  O   ASN A1159       2.512 -27.335 -30.041  1.00 37.98           O  
ANISOU 1235  O   ASN A1159     6169   4279   3983   -678  -1636   -352       O  
ATOM   1236  CB  ASN A1159       4.678 -26.891 -32.200  1.00 28.73           C  
ANISOU 1236  CB  ASN A1159     3389   4061   3465     59   -736   -113       C  
ATOM   1237  CG  ASN A1159       5.433 -26.163 -33.271  1.00 29.69           C  
ANISOU 1237  CG  ASN A1159     3476   4578   3224   -422   -291  -1055       C  
ATOM   1238  OD1 ASN A1159       5.528 -26.647 -34.397  1.00 34.70           O  
ANISOU 1238  OD1 ASN A1159     4016   5739   3427    630    307  -1491       O  
ATOM   1239  ND2 ASN A1159       5.918 -24.968 -32.956  1.00 32.65           N  
ANISOU 1239  ND2 ASN A1159     3586   5016   3801   -884   -763  -1343       N  
ATOM   1240  N   GLN A1160       1.873 -28.542 -31.860  1.00 29.40           N  
ANISOU 1240  N   GLN A1160     3424   3969   3775    -14  -1323    272       N  
ATOM   1241  CA  GLN A1160       1.393 -29.702 -31.115  1.00 28.64           C  
ANISOU 1241  CA  GLN A1160     3661   3763   3457    142   -958    -63       C  
ATOM   1242  C   GLN A1160       2.586 -30.652 -30.999  1.00 30.11           C  
ANISOU 1242  C   GLN A1160     4056   4094   3289    468   -736   -134       C  
ATOM   1243  O   GLN A1160       3.215 -30.995 -32.005  1.00 36.19           O  
ANISOU 1243  O   GLN A1160     5486   4834   3430    324   -276   -361       O  
ATOM   1244  CB  GLN A1160       0.218 -30.374 -31.828  1.00 30.04           C  
ANISOU 1244  CB  GLN A1160     3228   4086   4098     30   -424   -772       C  
ATOM   1245  N   LEU A1161       2.917 -31.028 -29.765  1.00 25.64           N  
ANISOU 1245  N   LEU A1161     3010   3616   3113   -546   -135    236       N  
ATOM   1246  CA  LEU A1161       4.071 -31.873 -29.463  1.00 25.91           C  
ANISOU 1246  CA  LEU A1161     2939   3605   3298   -566   -284   -141       C  
ATOM   1247  C   LEU A1161       3.596 -33.235 -29.016  1.00 28.08           C  
ANISOU 1247  C   LEU A1161     3761   3330   3575   -662   -532   -375       C  
ATOM   1248  O   LEU A1161       2.835 -33.330 -28.045  1.00 32.01           O  
ANISOU 1248  O   LEU A1161     4268   3743   4150  -1337     14   -515       O  
ATOM   1249  CB  LEU A1161       4.935 -31.211 -28.365  1.00 25.40           C  
ANISOU 1249  CB  LEU A1161     2646   3586   3416   -442   -260   -232       C  
ATOM   1250  CG  LEU A1161       5.513 -29.868 -28.830  1.00 25.78           C  
ANISOU 1250  CG  LEU A1161     2816   3622   3357   -652   -376   -459       C  
ATOM   1251  CD1 LEU A1161       6.248 -29.164 -27.699  1.00 25.20           C  
ANISOU 1251  CD1 LEU A1161     2553   3634   3386   -702   -365   -457       C  
ATOM   1252  CD2 LEU A1161       6.437 -30.050 -30.032  1.00 29.08           C  
ANISOU 1252  CD2 LEU A1161     3476   4129   3443   -373    -54     -9       C  
ATOM   1253  N   SER A1162       4.014 -34.278 -29.740  1.00 27.84           N  
ANISOU 1253  N   SER A1162     3602   3872   3103   -326   -119   -392       N  
ATOM   1254  CA  SER A1162       3.643 -35.669 -29.413  1.00 28.95           C  
ANISOU 1254  CA  SER A1162     3414   3847   3739   -247   -260     17       C  
ATOM   1255  C   SER A1162       4.419 -36.215 -28.223  1.00 26.52           C  
ANISOU 1255  C   SER A1162     2288   4288   3499   -551    -39   -167       C  
ATOM   1256  O   SER A1162       3.857 -36.951 -27.402  1.00 26.97           O  
ANISOU 1256  O   SER A1162     1677   4219   4350   -639   -244    144       O  
ATOM   1257  CB  SER A1162       3.889 -36.615 -30.601  1.00 29.36           C  
ANISOU 1257  CB  SER A1162     3594   4097   3463  -1175   -654   -235       C  
ATOM   1258  OG  SER A1162       3.130 -36.238 -31.718  1.00 37.33           O  
ANISOU 1258  OG  SER A1162     4319   5406   4455   -609   -727    617       O  
ATOM   1259  N   THR A1163       5.719 -35.911 -28.161  1.00 22.29           N  
ANISOU 1259  N   THR A1163     2290   2776   3403   -455   -195   -255       N  
ATOM   1260  CA  THR A1163       6.576 -36.483 -27.121  1.00 18.81           C  
ANISOU 1260  CA  THR A1163     2063   2127   2957   -495   -122   -618       C  
ATOM   1261  C   THR A1163       7.329 -35.486 -26.235  1.00 17.17           C  
ANISOU 1261  C   THR A1163     1692   2044   2788   -512   -153   -379       C  
ATOM   1262  O   THR A1163       7.504 -35.732 -25.044  1.00 18.28           O  
ANISOU 1262  O   THR A1163     1300   2613   3030   -509   -284   -194       O  
ATOM   1263  CB  THR A1163       7.578 -37.522 -27.702  1.00 19.06           C  
ANISOU 1263  CB  THR A1163     2125   2099   3015   -297   -209   -498       C  
ATOM   1264  OG1 THR A1163       8.494 -36.892 -28.608  1.00 19.57           O  
ANISOU 1264  OG1 THR A1163     2154   2547   2735   -295   -162   -563       O  
ATOM   1265  CG2 THR A1163       6.810 -38.637 -28.430  1.00 19.46           C  
ANISOU 1265  CG2 THR A1163     2085   2177   3131   -328   -277   -488       C  
ATOM   1266  N   LEU A1164       7.768 -34.366 -26.789  1.00 15.21           N  
ANISOU 1266  N   LEU A1164     1596   1839   2343   -205   -314   -399       N  
ATOM   1267  CA  LEU A1164       8.545 -33.414 -26.002  1.00 14.57           C  
ANISOU 1267  CA  LEU A1164     1686   1858   1990   -186   -211   -368       C  
ATOM   1268  C   LEU A1164       7.685 -32.774 -24.919  1.00 13.63           C  
ANISOU 1268  C   LEU A1164     1208   1796   2172    -99   -116    -90       C  
ATOM   1269  O   LEU A1164       6.659 -32.162 -25.219  1.00 16.13           O  
ANISOU 1269  O   LEU A1164     1214   2601   2311    197   -315   -381       O  
ATOM   1270  CB  LEU A1164       9.172 -32.367 -26.922  1.00 15.40           C  
ANISOU 1270  CB  LEU A1164     1766   1816   2268   -156   -128   -209       C  
ATOM   1271  CG  LEU A1164       9.995 -31.288 -26.238  1.00 14.59           C  
ANISOU 1271  CG  LEU A1164     1786   1680   2074   -256    -38    -94       C  
ATOM   1272  CD1 LEU A1164      11.273 -31.826 -25.646  1.00 16.15           C  
ANISOU 1272  CD1 LEU A1164     1896   2036   2204   -271   -208    -43       C  
ATOM   1273  CD2 LEU A1164      10.305 -30.164 -27.211  1.00 11.63           C  
ANISOU 1273  CD2 LEU A1164     1493   1119   1804   -816   -497   -506       C  
ATOM   1274  N   GLN A1165       8.111 -32.962 -23.665  1.00 13.29           N  
ANISOU 1274  N   GLN A1165     1094   1992   1964     44     59   -493       N  
ATOM   1275  CA  GLN A1165       7.395 -32.498 -22.481  1.00 14.00           C  
ANISOU 1275  CA  GLN A1165     1479   1972   1865   -155     95   -485       C  
ATOM   1276  C   GLN A1165       8.189 -31.586 -21.559  1.00 13.77           C  
ANISOU 1276  C   GLN A1165     1311   2009   1913   -185    -20   -330       C  
ATOM   1277  O   GLN A1165       7.580 -30.823 -20.833  1.00 16.34           O  
ANISOU 1277  O   GLN A1165     1467   2147   2593     14    154   -432       O  
ATOM   1278  CB  GLN A1165       6.964 -33.702 -21.671  1.00 18.65           C  
ANISOU 1278  CB  GLN A1165     1883   2712   2490   -408    640    -14       C  
ATOM   1279  CG  GLN A1165       5.904 -34.521 -22.366  1.00 24.03           C  
ANISOU 1279  CG  GLN A1165     2999   3287   2842   -663   -212    162       C  
ATOM   1280  CD  GLN A1165       5.387 -35.673 -21.535  1.00 31.65           C  
ANISOU 1280  CD  GLN A1165     3812   4223   3989  -1396     40    874       C  
ATOM   1281  OE1 GLN A1165       6.043 -36.145 -20.606  1.00 38.76           O  
ANISOU 1281  OE1 GLN A1165     4589   4760   5376  -1066   -590   1410       O  
ATOM   1282  NE2 GLN A1165       4.214 -36.153 -21.894  1.00 37.23           N  
ANISOU 1282  NE2 GLN A1165     5028   4713   4404  -2424   -512    685       N  
ATOM   1283  N   GLU A1166       9.520 -31.690 -21.555  1.00 12.84           N  
ANISOU 1283  N   GLU A1166     1289   1583   2006   -113    271   -176       N  
ATOM   1284  CA  GLU A1166      10.333 -30.985 -20.560  1.00 12.62           C  
ANISOU 1284  CA  GLU A1166     1173   1725   1896   -130    200    -96       C  
ATOM   1285  C   GLU A1166      11.573 -30.381 -21.200  1.00 10.92           C  
ANISOU 1285  C   GLU A1166      996   1500   1650      2    111   -255       C  
ATOM   1286  O   GLU A1166      12.228 -31.000 -22.023  1.00 13.37           O  
ANISOU 1286  O   GLU A1166     1100   1844   2134    -41    435   -332       O  
ATOM   1287  CB  GLU A1166      10.801 -31.924 -19.443  1.00 15.20           C  
ANISOU 1287  CB  GLU A1166     1579   2377   1818    -92     81     36       C  
ATOM   1288  CG  GLU A1166       9.723 -32.699 -18.725  1.00 18.66           C  
ANISOU 1288  CG  GLU A1166     1928   2590   2571   -369    217    103       C  
ATOM   1289  CD  GLU A1166      10.274 -33.642 -17.653  1.00 22.86           C  
ANISOU 1289  CD  GLU A1166     2037   3753   2893   -661    133    895       C  
ATOM   1290  OE1 GLU A1166      11.503 -33.673 -17.379  1.00 25.42           O  
ANISOU 1290  OE1 GLU A1166     1984   4070   3602   -722      9    948       O  
ATOM   1291  OE2 GLU A1166       9.454 -34.372 -17.071  1.00 30.38           O  
ANISOU 1291  OE2 GLU A1166     3298   4104   4140  -1470    297   1295       O  
ATOM   1292  N   VAL A1167      11.865 -29.164 -20.780  1.00  9.55           N  
ANISOU 1292  N   VAL A1167      820   1542   1266    124    698   -595       N  
ATOM   1293  CA  VAL A1167      13.091 -28.457 -21.111  1.00 10.11           C  
ANISOU 1293  CA  VAL A1167      844   1571   1424    -63    119   -127       C  
ATOM   1294  C   VAL A1167      13.763 -28.074 -19.789  1.00 11.42           C  
ANISOU 1294  C   VAL A1167     1167   1725   1446    161    104   -296       C  
ATOM   1295  O   VAL A1167      13.193 -27.357 -18.981  1.00 11.93           O  
ANISOU 1295  O   VAL A1167      954   2332   1246     96     26   -485       O  
ATOM   1296  CB  VAL A1167      12.821 -27.205 -21.937  1.00 10.96           C  
ANISOU 1296  CB  VAL A1167     1169   1564   1432   -113    148   -138       C  
ATOM   1297  CG1 VAL A1167      14.126 -26.475 -22.221  1.00 11.39           C  
ANISOU 1297  CG1 VAL A1167     1310   1568   1446   -190    186    -30       C  
ATOM   1298  CG2 VAL A1167      12.085 -27.571 -23.212  1.00 11.45           C  
ANISOU 1298  CG2 VAL A1167     1226   1689   1434    -98     33     89       C  
ATOM   1299  N   HIS A1168      14.984 -28.573 -19.582  1.00  8.76           N  
ANISOU 1299  N   HIS A1168     1233   1121    972    446    328   -626       N  
ATOM   1300  CA  HIS A1168      15.718 -28.290 -18.362  1.00 10.65           C  
ANISOU 1300  CA  HIS A1168     1365   1497   1184   -125    143   -227       C  
ATOM   1301  C   HIS A1168      16.789 -27.244 -18.654  1.00  9.67           C  
ANISOU 1301  C   HIS A1168     1229   1386   1057    -73     25   -226       C  
ATOM   1302  O   HIS A1168      17.527 -27.352 -19.642  1.00 12.15           O  
ANISOU 1302  O   HIS A1168     1365   1945   1304   -478    240   -450       O  
ATOM   1303  CB  HIS A1168      16.408 -29.542 -17.808  1.00 11.60           C  
ANISOU 1303  CB  HIS A1168     1436   1603   1369    -55     96   -124       C  
ATOM   1304  CG  HIS A1168      15.484 -30.665 -17.447  1.00 13.59           C  
ANISOU 1304  CG  HIS A1168     1837   1775   1549   -286     72      5       C  
ATOM   1305  ND1 HIS A1168      15.802 -31.595 -16.476  1.00 16.03           N  
ANISOU 1305  ND1 HIS A1168     2170   2146   1775   -125    133    205       N  
ATOM   1306  CD2 HIS A1168      14.284 -31.047 -17.957  1.00 16.26           C  
ANISOU 1306  CD2 HIS A1168     1667   2216   2293   -344     27    459       C  
ATOM   1307  CE1 HIS A1168      14.826 -32.482 -16.389  1.00 17.43           C  
ANISOU 1307  CE1 HIS A1168     2430   2267   1925   -348    186    344       C  
ATOM   1308  NE2 HIS A1168      13.895 -32.176 -17.280  1.00 17.57           N  
ANISOU 1308  NE2 HIS A1168     2061   2199   2416   -268    257    473       N  
ATOM   1309  N   PHE A1169      16.877 -26.240 -17.796  1.00  8.42           N  
ANISOU 1309  N   PHE A1169     1000   1234    963    -99    104   -125       N  
ATOM   1310  CA  PHE A1169      17.983 -25.268 -17.847  1.00  8.68           C  
ANISOU 1310  CA  PHE A1169      892   1419    986   -119    -68     22       C  
ATOM   1311  C   PHE A1169      18.970 -25.661 -16.759  1.00  8.49           C  
ANISOU 1311  C   PHE A1169      808   1441    977    -51     -5     32       C  
ATOM   1312  O   PHE A1169      18.622 -25.648 -15.573  1.00 10.44           O  
ANISOU 1312  O   PHE A1169      789   2103   1074     -5    136    251       O  
ATOM   1313  CB  PHE A1169      17.460 -23.869 -17.619  1.00  9.78           C  
ANISOU 1313  CB  PHE A1169     1002   1545   1168    -31     13   -124       C  
ATOM   1314  CG  PHE A1169      16.387 -23.468 -18.590  1.00  9.54           C  
ANISOU 1314  CG  PHE A1169     1089   1401   1132    123     38   -134       C  
ATOM   1315  CD1 PHE A1169      16.592 -23.594 -19.978  1.00  9.45           C  
ANISOU 1315  CD1 PHE A1169     1081   1426   1082     54     15    -60       C  
ATOM   1316  CD2 PHE A1169      15.157 -22.959 -18.149  1.00  9.41           C  
ANISOU 1316  CD2 PHE A1169      918   1472   1183    -12     65     19       C  
ATOM   1317  CE1 PHE A1169      15.611 -23.203 -20.888  1.00  9.93           C  
ANISOU 1317  CE1 PHE A1169     1296   1217   1260    177    -49     27       C  
ATOM   1318  CE2 PHE A1169      14.185 -22.563 -19.063  1.00 11.02           C  
ANISOU 1318  CE2 PHE A1169      425   2122   1639    404    143   -142       C  
ATOM   1319  CZ  PHE A1169      14.413 -22.690 -20.430  1.00 10.60           C  
ANISOU 1319  CZ  PHE A1169     1158   1426   1443     91     27    259       C  
ATOM   1320  N   LEU A1170      20.176 -26.059 -17.157  1.00  7.80           N  
ANISOU 1320  N   LEU A1170      797   1295    868    -54      3    172       N  
ATOM   1321  CA  LEU A1170      21.160 -26.595 -16.223  1.00  8.51           C  
ANISOU 1321  CA  LEU A1170      977   1420    837   -102   -157    114       C  
ATOM   1322  C   LEU A1170      22.171 -25.516 -15.849  1.00  9.36           C  
ANISOU 1322  C   LEU A1170      937   1445   1171   -153   -155    219       C  
ATOM   1323  O   LEU A1170      22.915 -25.003 -16.696  1.00 11.41           O  
ANISOU 1323  O   LEU A1170     1160   1966   1206   -424   -142    260       O  
ATOM   1324  CB  LEU A1170      21.907 -27.778 -16.813  1.00 10.94           C  
ANISOU 1324  CB  LEU A1170     1258   1504   1395     97    -79    113       C  
ATOM   1325  CG  LEU A1170      21.083 -28.918 -17.408  1.00 14.04           C  
ANISOU 1325  CG  LEU A1170     1732   1777   1826     47   -136   -243       C  
ATOM   1326  CD1 LEU A1170      22.019 -30.021 -17.848  1.00 15.41           C  
ANISOU 1326  CD1 LEU A1170     1697   1905   2251    211   -138   -146       C  
ATOM   1327  CD2 LEU A1170      20.000 -29.447 -16.482  1.00 15.11           C  
ANISOU 1327  CD2 LEU A1170     1891   1897   1950    -44   -110    -47       C  
ATOM   1328  N   LEU A1171      22.154 -25.156 -14.580  1.00 10.33           N  
ANISOU 1328  N   LEU A1171     1230   1499   1193   -251   -198    125       N  
ATOM   1329  CA  LEU A1171      23.030 -24.116 -14.032  1.00 10.35           C  
ANISOU 1329  CA  LEU A1171     1233   1472   1225   -185   -397    229       C  
ATOM   1330  C   LEU A1171      23.889 -24.692 -12.927  1.00 10.73           C  
ANISOU 1330  C   LEU A1171     1275   1597   1205   -266   -383    321       C  
ATOM   1331  O   LEU A1171      23.428 -25.473 -12.116  1.00 12.63           O  
ANISOU 1331  O   LEU A1171     1360   1947   1492   -361   -285    479       O  
ATOM   1332  CB  LEU A1171      22.205 -22.957 -13.461  1.00 12.40           C  
ANISOU 1332  CB  LEU A1171     1688   1628   1392   -170   -267   -108       C  
ATOM   1333  CG  LEU A1171      21.467 -22.007 -14.408  1.00 14.03           C  
ANISOU 1333  CG  LEU A1171     1955   1694   1678      9   -295   -111       C  
ATOM   1334  CD1 LEU A1171      20.442 -22.683 -15.279  1.00 14.69           C  
ANISOU 1334  CD1 LEU A1171     1727   1824   2028   -173   -192   -116       C  
ATOM   1335  CD2 LEU A1171      20.770 -20.920 -13.601  1.00 15.21           C  
ANISOU 1335  CD2 LEU A1171     1894   1599   2285    181    -40     -8       C  
ATOM   1336  N   HIS A1172      25.148 -24.277 -12.918  1.00  9.12           N  
ANISOU 1336  N   HIS A1172     1294   1581    588   -402    117    677       N  
ATOM   1337  CA  HIS A1172      26.000 -24.535 -11.764  1.00  9.86           C  
ANISOU 1337  CA  HIS A1172     1214   1447   1084   -171   -225    296       C  
ATOM   1338  C   HIS A1172      25.506 -23.644 -10.594  1.00 10.46           C  
ANISOU 1338  C   HIS A1172     1116   1593   1263   -292    -80    137       C  
ATOM   1339  O   HIS A1172      25.202 -22.486 -10.784  1.00 10.30           O  
ANISOU 1339  O   HIS A1172      934   1798   1180   -184   -246    222       O  
ATOM   1340  CB  HIS A1172      27.442 -24.201 -12.116  1.00 10.33           C  
ANISOU 1340  CB  HIS A1172     1396   1390   1139   -245    173     16       C  
ATOM   1341  CG  HIS A1172      28.431 -24.668 -11.117  1.00 11.78           C  
ANISOU 1341  CG  HIS A1172     1293   1625   1557   -136     77     26       C  
ATOM   1342  ND1 HIS A1172      28.572 -24.054  -9.903  1.00 12.56           N  
ANISOU 1342  ND1 HIS A1172     1475   1811   1486    106    124    -50       N  
ATOM   1343  CD2 HIS A1172      29.357 -25.657 -11.153  1.00 14.83           C  
ANISOU 1343  CD2 HIS A1172     1851   1929   1853    279     81    -77       C  
ATOM   1344  CE1 HIS A1172      29.532 -24.655  -9.215  1.00 13.09           C  
ANISOU 1344  CE1 HIS A1172     1545   1766   1659   -114   -197    -28       C  
ATOM   1345  NE2 HIS A1172      30.033 -25.627  -9.953  1.00 14.82           N  
ANISOU 1345  NE2 HIS A1172     1645   2228   1758    173    236     47       N  
ATOM   1346  N   PRO A1173      25.430 -24.184  -9.366  1.00 10.90           N  
ANISOU 1346  N   PRO A1173     1240   1633   1265   -299   -270    132       N  
ATOM   1347  CA  PRO A1173      24.883 -23.360  -8.262  1.00 12.35           C  
ANISOU 1347  CA  PRO A1173     1473   1840   1377   -182   -287    -13       C  
ATOM   1348  C   PRO A1173      25.700 -22.143  -7.870  1.00 11.92           C  
ANISOU 1348  C   PRO A1173     1262   1797   1466   -111   -113    -82       C  
ATOM   1349  O   PRO A1173      25.159 -21.239  -7.238  1.00 15.67           O  
ANISOU 1349  O   PRO A1173     1621   2701   1632    -36    107   -586       O  
ATOM   1350  CB  PRO A1173      24.771 -24.346  -7.097  1.00 15.14           C  
ANISOU 1350  CB  PRO A1173     2106   1876   1768   -286    -40    138       C  
ATOM   1351  CG  PRO A1173      25.665 -25.443  -7.417  1.00 13.79           C  
ANISOU 1351  CG  PRO A1173     1623   2169   1445   -100    -88    296       C  
ATOM   1352  CD  PRO A1173      25.707 -25.557  -8.932  1.00 12.14           C  
ANISOU 1352  CD  PRO A1173     1489   1656   1467   -174   -408    119       C  
ATOM   1353  N   SER A1174      26.971 -22.090  -8.282  1.00 10.38           N  
ANISOU 1353  N   SER A1174     1230   1455   1256    -60   -157    -40       N  
ATOM   1354  CA  SER A1174      27.793 -20.894  -8.106  1.00 11.71           C  
ANISOU 1354  CA  SER A1174     1221   1686   1543   -191   -154   -130       C  
ATOM   1355  C   SER A1174      27.737 -19.914  -9.272  1.00 11.70           C  
ANISOU 1355  C   SER A1174     1210   1641   1594    -27   -266    -98       C  
ATOM   1356  O   SER A1174      28.431 -18.895  -9.250  1.00 13.58           O  
ANISOU 1356  O   SER A1174     1464   1621   2073    -54   -565    -61       O  
ATOM   1357  CB  SER A1174      29.241 -21.276  -7.820  1.00 11.59           C  
ANISOU 1357  CB  SER A1174     1270   1743   1387   -171   -220     -1       C  
ATOM   1358  OG  SER A1174      29.315 -22.117  -6.700  1.00 14.80           O  
ANISOU 1358  OG  SER A1174     1969   2132   1522   -506    -89    237       O  
ATOM   1359  N   ASP A1175      26.922 -20.191 -10.292  1.00 11.08           N  
ANISOU 1359  N   ASP A1175     1535   1429   1244   -226    -96   -166       N  
ATOM   1360  CA  ASP A1175      26.742 -19.266 -11.425  1.00 11.82           C  
ANISOU 1360  CA  ASP A1175     1633   1448   1409    -95   -109    -63       C  
ATOM   1361  C   ASP A1175      25.727 -18.221 -10.986  1.00 12.59           C  
ANISOU 1361  C   ASP A1175     1643   1732   1407    -40   -104   -197       C  
ATOM   1362  O   ASP A1175      24.568 -18.242 -11.419  1.00 12.41           O  
ANISOU 1362  O   ASP A1175     1741   1606   1366     36   -222      8       O  
ATOM   1363  CB  ASP A1175      26.296 -20.050 -12.665  1.00 11.76           C  
ANISOU 1363  CB  ASP A1175     1710   1338   1419   -156    -50    -23       C  
ATOM   1364  CG  ASP A1175      26.263 -19.223 -13.936  1.00 13.44           C  
ANISOU 1364  CG  ASP A1175     2137   1409   1559   -178    170     80       C  
ATOM   1365  OD1 ASP A1175      26.375 -17.952 -13.892  1.00 16.37           O  
ANISOU 1365  OD1 ASP A1175     2643   1450   2124   -346    -30      7       O  
ATOM   1366  OD2 ASP A1175      26.015 -19.864 -14.992  1.00 14.31           O  
ANISOU 1366  OD2 ASP A1175     2337   1586   1512     62     20     99       O  
ATOM   1367  N   HIS A1176      26.171 -17.319 -10.108  1.00 11.34           N  
ANISOU 1367  N   HIS A1176     1542   1402   1363    -46   -144     35       N  
ATOM   1368  CA  HIS A1176      25.280 -16.386  -9.444  1.00 12.93           C  
ANISOU 1368  CA  HIS A1176     1788   1755   1370     43     32    -76       C  
ATOM   1369  C   HIS A1176      24.450 -15.537 -10.420  1.00 12.85           C  
ANISOU 1369  C   HIS A1176     1718   1762   1402     67    -77   -214       C  
ATOM   1370  O   HIS A1176      23.257 -15.324 -10.214  1.00 13.29           O  
ANISOU 1370  O   HIS A1176     1747   1686   1617     -1    -76   -192       O  
ATOM   1371  CB  HIS A1176      26.072 -15.487  -8.478  1.00 13.27           C  
ANISOU 1371  CB  HIS A1176     1735   1919   1386    152     81   -275       C  
ATOM   1372  CG  HIS A1176      26.825 -16.257  -7.428  1.00 16.44           C  
ANISOU 1372  CG  HIS A1176     2244   2494   1507    278   -250   -272       C  
ATOM   1373  ND1 HIS A1176      26.251 -17.292  -6.732  1.00 16.46           N  
ANISOU 1373  ND1 HIS A1176     2226   2427   1599    286   -285   -328       N  
ATOM   1374  CD2 HIS A1176      28.101 -16.155  -6.976  1.00 17.03           C  
ANISOU 1374  CD2 HIS A1176     2265   2574   1630    119   -137   -459       C  
ATOM   1375  CE1 HIS A1176      27.131 -17.787  -5.875  1.00 19.53           C  
ANISOU 1375  CE1 HIS A1176     2198   3097   2123    227   -350     79       C  
ATOM   1376  NE2 HIS A1176      28.265 -17.113  -6.000  1.00 19.19           N  
ANISOU 1376  NE2 HIS A1176     2378   3267   1645     91    219    -94       N  
ATOM   1377  N   GLU A1177      25.079 -15.070 -11.485  1.00 13.00           N  
ANISOU 1377  N   GLU A1177     1629   1739   1569    153    -47    -68       N  
ATOM   1378  CA  GLU A1177      24.415 -14.196 -12.426  1.00 12.69           C  
ANISOU 1378  CA  GLU A1177     1813   1547   1460    112    -59   -137       C  
ATOM   1379  C   GLU A1177      23.286 -14.929 -13.170  1.00 12.15           C  
ANISOU 1379  C   GLU A1177     1825   1374   1416     31     78   -152       C  
ATOM   1380  O   GLU A1177      22.181 -14.397 -13.311  1.00 12.65           O  
ANISOU 1380  O   GLU A1177     1815   1433   1557     32     69    -39       O  
ATOM   1381  CB  GLU A1177      25.407 -13.599 -13.415  1.00 15.90           C  
ANISOU 1381  CB  GLU A1177     1983   1976   2081   -350    -19     51       C  
ATOM   1382  CG  GLU A1177      24.834 -12.435 -14.204  1.00 17.73           C  
ANISOU 1382  CG  GLU A1177     2412   2064   2259   -117   -169    -20       C  
ATOM   1383  CD  GLU A1177      25.794 -11.848 -15.223  1.00 21.65           C  
ANISOU 1383  CD  GLU A1177     2813   2583   2827   -329     67    220       C  
ATOM   1384  OE1 GLU A1177      26.988 -12.260 -15.299  1.00 19.59           O  
ANISOU 1384  OE1 GLU A1177     2629   2282   2530   -622   -839     20       O  
ATOM   1385  OE2 GLU A1177      25.333 -10.957 -15.976  1.00 25.19           O  
ANISOU 1385  OE2 GLU A1177     3250   2462   3859   -368    -95    520       O  
ATOM   1386  N   ASN A1178      23.550 -16.153 -13.614  1.00 11.19           N  
ANISOU 1386  N   ASN A1178     1424   1316   1509     13     25   -124       N  
ATOM   1387  CA  ASN A1178      22.487 -16.928 -14.259  1.00 10.26           C  
ANISOU 1387  CA  ASN A1178     1472   1238   1186     43     29   -117       C  
ATOM   1388  C   ASN A1178      21.395 -17.371 -13.284  1.00  9.77           C  
ANISOU 1388  C   ASN A1178     1371   1142   1198     66     -4   -118       C  
ATOM   1389  O   ASN A1178      20.233 -17.367 -13.624  1.00 11.11           O  
ANISOU 1389  O   ASN A1178     1439   1664   1117     58   -126   -244       O  
ATOM   1390  CB  ASN A1178      23.035 -18.141 -15.013  1.00 11.29           C  
ANISOU 1390  CB  ASN A1178     1623   1324   1342     18    135   -211       C  
ATOM   1391  CG  ASN A1178      23.411 -17.814 -16.445  1.00 12.21           C  
ANISOU 1391  CG  ASN A1178     1972   1230   1435   -178     18    112       C  
ATOM   1392  OD1 ASN A1178      22.724 -17.039 -17.115  1.00 14.26           O  
ANISOU 1392  OD1 ASN A1178     2374   1728   1315     67    -53    133       O  
ATOM   1393  ND2 ASN A1178      24.486 -18.428 -16.929  1.00 12.65           N  
ANISOU 1393  ND2 ASN A1178     1972   1485   1346   -285    115    -79       N  
ATOM   1394  N   ILE A1179      21.765 -17.741 -12.069  1.00 11.10           N  
ANISOU 1394  N   ILE A1179     1408   1647   1159    -75    -19    -87       N  
ATOM   1395  CA  ILE A1179      20.779 -18.152 -11.076  1.00 12.38           C  
ANISOU 1395  CA  ILE A1179     1533   1832   1339    -52    175   -101       C  
ATOM   1396  C   ILE A1179      19.838 -16.954 -10.846  1.00 12.96           C  
ANISOU 1396  C   ILE A1179     1828   1825   1270     33     68   -112       C  
ATOM   1397  O   ILE A1179      18.615 -17.099 -10.804  1.00 15.17           O  
ANISOU 1397  O   ILE A1179     1894   2258   1611    -21    300   -261       O  
ATOM   1398  CB  ILE A1179      21.457 -18.617  -9.748  1.00 14.97           C  
ANISOU 1398  CB  ILE A1179     1773   2335   1577     -7    143    245       C  
ATOM   1399  CG1 ILE A1179      22.301 -19.898  -9.915  1.00 19.10           C  
ANISOU 1399  CG1 ILE A1179     2033   2698   2524    164    357    -70       C  
ATOM   1400  CG2 ILE A1179      20.423 -18.788  -8.652  1.00 16.42           C  
ANISOU 1400  CG2 ILE A1179     2087   2461   1690     40    375    236       C  
ATOM   1401  CD1 ILE A1179      21.569 -21.202 -10.011  1.00 23.98           C  
ANISOU 1401  CD1 ILE A1179     2700   2954   3457     78    335   -330       C  
ATOM   1402  N   GLN A1180      20.402 -15.757 -10.717  1.00 12.61           N  
ANISOU 1402  N   GLN A1180     1686   1778   1326    163     26   -311       N  
ATOM   1403  CA  GLN A1180      19.554 -14.575 -10.506  1.00 14.29           C  
ANISOU 1403  CA  GLN A1180     1600   2245   1582    477     62   -452       C  
ATOM   1404  C   GLN A1180      18.668 -14.314 -11.725  1.00 13.03           C  
ANISOU 1404  C   GLN A1180     1588   1812   1550    646    134   -366       C  
ATOM   1405  O   GLN A1180      17.462 -14.066 -11.592  1.00 15.04           O  
ANISOU 1405  O   GLN A1180     1473   2183   2057    346    327   -372       O  
ATOM   1406  CB  GLN A1180      20.377 -13.351 -10.180  1.00 17.35           C  
ANISOU 1406  CB  GLN A1180     2148   2330   2113    296    -54   -420       C  
ATOM   1407  CG  GLN A1180      19.545 -12.118  -9.849  1.00 21.67           C  
ANISOU 1407  CG  GLN A1180     2549   2836   2848    622   -119   -940       C  
ATOM   1408  CD  GLN A1180      18.854 -12.223  -8.488  1.00 27.29           C  
ANISOU 1408  CD  GLN A1180     3295   4231   2839    661   -200   -652       C  
ATOM   1409  OE1 GLN A1180      19.519 -12.261  -7.456  1.00 40.82           O  
ANISOU 1409  OE1 GLN A1180     5263   6084   4160   1037  -1888  -1292       O  
ATOM   1410  NE2 GLN A1180      17.513 -12.266  -8.480  1.00 34.31           N  
ANISOU 1410  NE2 GLN A1180     3307   5821   3907    633   -326  -1725       N  
ATOM   1411  N   ALA A1181      19.239 -14.434 -12.923  1.00 11.74           N  
ANISOU 1411  N   ALA A1181     1685   1453   1319    172    -66   -433       N  
ATOM   1412  CA  ALA A1181      18.483 -14.113 -14.146  1.00 13.40           C  
ANISOU 1412  CA  ALA A1181     1691   1765   1634    209   -194   -183       C  
ATOM   1413  C   ALA A1181      17.298 -15.042 -14.361  1.00 12.36           C  
ANISOU 1413  C   ALA A1181     1835   1413   1446    240    -47   -147       C  
ATOM   1414  O   ALA A1181      16.187 -14.593 -14.645  1.00 14.90           O  
ANISOU 1414  O   ALA A1181     1886   1889   1882    312   -237   -312       O  
ATOM   1415  CB  ALA A1181      19.403 -14.171 -15.349  1.00 14.26           C  
ANISOU 1415  CB  ALA A1181     1901   1867   1649     -9   -107   -107       C  
ATOM   1416  N   PHE A1182      17.542 -16.340 -14.237  1.00 11.83           N  
ANISOU 1416  N   PHE A1182     1702   1387   1405    193     23   -126       N  
ATOM   1417  CA  PHE A1182      16.491 -17.330 -14.409  1.00 12.29           C  
ANISOU 1417  CA  PHE A1182     1453   1689   1526    154    229    -62       C  
ATOM   1418  C   PHE A1182      15.472 -17.277 -13.270  1.00 13.25           C  
ANISOU 1418  C   PHE A1182     1677   2003   1354    159    218   -383       C  
ATOM   1419  O   PHE A1182      14.290 -17.400 -13.511  1.00 16.79           O  
ANISOU 1419  O   PHE A1182     1651   2484   2244    240    184   -443       O  
ATOM   1420  CB  PHE A1182      17.074 -18.732 -14.607  1.00 10.90           C  
ANISOU 1420  CB  PHE A1182     1343   1503   1294    -41    137    -44       C  
ATOM   1421  CG  PHE A1182      17.532 -18.987 -16.018  1.00  9.91           C  
ANISOU 1421  CG  PHE A1182     1276   1320   1170    -57     51     99       C  
ATOM   1422  CD1 PHE A1182      18.745 -18.480 -16.465  1.00  9.76           C  
ANISOU 1422  CD1 PHE A1182     1107   1425   1174    -20   -116     44       C  
ATOM   1423  CD2 PHE A1182      16.752 -19.711 -16.914  1.00 11.21           C  
ANISOU 1423  CD2 PHE A1182     1201   1642   1415    -51    109   -120       C  
ATOM   1424  CE1 PHE A1182      19.161 -18.676 -17.748  1.00 10.44           C  
ANISOU 1424  CE1 PHE A1182     1218   1474   1274    125    -30     -6       C  
ATOM   1425  CE2 PHE A1182      17.159 -19.891 -18.225  1.00 11.01           C  
ANISOU 1425  CE2 PHE A1182     1562   1345   1275   -161     47     93       C  
ATOM   1426  CZ  PHE A1182      18.375 -19.385 -18.629  1.00 10.67           C  
ANISOU 1426  CZ  PHE A1182     1395   1364   1293    -33     11      4       C  
ATOM   1427  N   SER A1183      15.942 -17.099 -12.043  1.00 14.05           N  
ANISOU 1427  N   SER A1183     1662   2273   1402    157    145   -454       N  
ATOM   1428  CA  SER A1183      15.044 -16.999 -10.894  1.00 16.23           C  
ANISOU 1428  CA  SER A1183     1865   2674   1628   -111    396   -282       C  
ATOM   1429  C   SER A1183      14.067 -15.832 -11.074  1.00 16.90           C  
ANISOU 1429  C   SER A1183     1724   3017   1677     77    459   -557       C  
ATOM   1430  O   SER A1183      12.850 -15.971 -10.817  1.00 20.11           O  
ANISOU 1430  O   SER A1183     1613   3625   2404     26    466   -936       O  
ATOM   1431  CB  SER A1183      15.848 -16.858  -9.597  1.00 19.35           C  
ANISOU 1431  CB  SER A1183     2659   3124   1567     29    136     77       C  
ATOM   1432  OG  SER A1183      16.569 -18.062  -9.351  1.00 22.62           O  
ANISOU 1432  OG  SER A1183     3282   2952   2360     19     87   -215       O  
ATOM   1433  N   ASP A1184      14.598 -14.688 -11.520  1.00 17.82           N  
ANISOU 1433  N   ASP A1184     1979   2713   2076    -81     82   -742       N  
ATOM   1434  CA  ASP A1184      13.781 -13.499 -11.783  1.00 20.32           C  
ANISOU 1434  CA  ASP A1184     1924   3019   2778    234   -108   -826       C  
ATOM   1435  C   ASP A1184      12.778 -13.728 -12.909  1.00 20.71           C  
ANISOU 1435  C   ASP A1184     2288   3057   2521    323     12  -1309       C  
ATOM   1436  O   ASP A1184      11.624 -13.313 -12.793  1.00 24.47           O  
ANISOU 1436  O   ASP A1184     2205   3236   3853    293    271  -1640       O  
ATOM   1437  CB  ASP A1184      14.632 -12.281 -12.127  1.00 20.66           C  
ANISOU 1437  CB  ASP A1184     2408   2471   2968    443     88   -817       C  
ATOM   1438  CG  ASP A1184      15.429 -11.748 -10.949  1.00 24.66           C  
ANISOU 1438  CG  ASP A1184     2919   3082   3367    -66    -76   -804       C  
ATOM   1439  OD1 ASP A1184      15.175 -12.130  -9.782  1.00 29.96           O  
ANISOU 1439  OD1 ASP A1184     3877   4158   3347    388    814  -1447       O  
ATOM   1440  OD2 ASP A1184      16.332 -10.914 -11.207  1.00 28.28           O  
ANISOU 1440  OD2 ASP A1184     3045   2495   5205   -170   -473  -1092       O  
ATOM   1441  N   GLU A1185      13.223 -14.350 -14.002  1.00 17.48           N  
ANISOU 1441  N   GLU A1185     1917   2475   2246    -81    270   -870       N  
ATOM   1442  CA  GLU A1185      12.321 -14.677 -15.091  1.00 18.97           C  
ANISOU 1442  CA  GLU A1185     1958   2795   2452    238      0   -808       C  
ATOM   1443  C   GLU A1185      11.208 -15.631 -14.687  1.00 19.77           C  
ANISOU 1443  C   GLU A1185     2014   2952   2543    170    370  -1083       C  
ATOM   1444  O   GLU A1185      10.051 -15.443 -15.087  1.00 23.31           O  
ANISOU 1444  O   GLU A1185     1927   3352   3576     40    163  -1247       O  
ATOM   1445  CB  GLU A1185      13.067 -15.305 -16.244  1.00 19.31           C  
ANISOU 1445  CB  GLU A1185     2291   3156   1887    141     62   -462       C  
ATOM   1446  CG  GLU A1185      13.614 -14.291 -17.204  1.00 14.33           C  
ANISOU 1446  CG  GLU A1185     2089   2261   1095   1426    458   -603       C  
ATOM   1447  CD  GLU A1185      12.543 -13.502 -17.929  1.00 22.44           C  
ANISOU 1447  CD  GLU A1185     2852   3636   2036   1169   -827   -223       C  
ATOM   1448  OE1 GLU A1185      11.704 -14.080 -18.634  1.00 34.98           O  
ANISOU 1448  OE1 GLU A1185     4332   4898   4058   -841     12  -1971       O  
ATOM   1449  OE2 GLU A1185      12.502 -12.264 -17.773  1.00 35.41           O  
ANISOU 1449  OE2 GLU A1185     5435   3499   4518   1115  -1025    702       O  
ATOM   1450  N   PHE A1186      11.574 -16.672 -13.947  1.00 18.98           N  
ANISOU 1450  N   PHE A1186     1736   3234   2239    178    357  -1022       N  
ATOM   1451  CA  PHE A1186      10.611 -17.678 -13.496  1.00 20.82           C  
ANISOU 1451  CA  PHE A1186     2084   3243   2582    -19    187   -838       C  
ATOM   1452  C   PHE A1186       9.612 -17.067 -12.536  1.00 25.31           C  
ANISOU 1452  C   PHE A1186     2184   4478   2953   -165    413  -1379       C  
ATOM   1453  O   PHE A1186       8.407 -17.336 -12.636  1.00 30.36           O  
ANISOU 1453  O   PHE A1186     2141   4848   4543   -225    466  -2254       O  
ATOM   1454  CB  PHE A1186      11.287 -18.866 -12.815  1.00 19.11           C  
ANISOU 1454  CB  PHE A1186     1945   3111   2204   -243    198   -676       C  
ATOM   1455  CG  PHE A1186      11.652 -19.994 -13.739  1.00 15.09           C  
ANISOU 1455  CG  PHE A1186     1428   2612   1690   -291    -50   -299       C  
ATOM   1456  CD1 PHE A1186      12.300 -19.763 -14.952  1.00 16.71           C  
ANISOU 1456  CD1 PHE A1186     2319   2123   1905   -277    321   -152       C  
ATOM   1457  CD2 PHE A1186      11.368 -21.313 -13.388  1.00 14.18           C  
ANISOU 1457  CD2 PHE A1186     1499   2498   1390   -173    172   -315       C  
ATOM   1458  CE1 PHE A1186      12.647 -20.828 -15.784  1.00 16.63           C  
ANISOU 1458  CE1 PHE A1186     2270   2259   1786    -13    148   -162       C  
ATOM   1459  CE2 PHE A1186      11.695 -22.383 -14.225  1.00 13.24           C  
ANISOU 1459  CE2 PHE A1186     1457   2188   1386    -98     11   -115       C  
ATOM   1460  CZ  PHE A1186      12.353 -22.130 -15.422  1.00 14.08           C  
ANISOU 1460  CZ  PHE A1186     1729   2270   1349     66    102   -115       C  
ATOM   1461  N   ALA A1187      10.110 -16.280 -11.590  1.00 27.44           N  
ANISOU 1461  N   ALA A1187     2737   4102   3585   -165    764  -1856       N  
ATOM   1462  CA  ALA A1187       9.238 -15.598 -10.627  1.00 22.05           C  
ANISOU 1462  CA  ALA A1187     2132   3917   2329    181     38  -1242       C  
ATOM   1463  C   ALA A1187       8.278 -14.687 -11.351  1.00 23.10           C  
ANISOU 1463  C   ALA A1187     2220   3783   2774    612    658  -1018       C  
ATOM   1464  O   ALA A1187       7.092 -14.666 -11.032  1.00 30.66           O  
ANISOU 1464  O   ALA A1187     1951   5346   4349    338    517  -2162       O  
ATOM   1465  CB  ALA A1187      10.034 -14.811  -9.615  1.00 14.86           C  
ANISOU 1465  CB  ALA A1187     1059   3758    829   1418     45   -818       C  
ATOM   1466  N   ARG A1188       8.780 -13.954 -12.339  1.00 19.77           N  
ANISOU 1466  N   ARG A1188     2044   2424   3043   1091   -110   -382       N  
ATOM   1467  CA  ARG A1188       7.990 -13.006 -13.090  1.00 15.15           C  
ANISOU 1467  CA  ARG A1188     2367   2144   1242   1580     -4   -984       C  
ATOM   1468  C   ARG A1188       6.889 -13.674 -13.904  1.00 25.08           C  
ANISOU 1468  C   ARG A1188     2682   3210   3635    717   -456  -1406       C  
ATOM   1469  O   ARG A1188       5.779 -13.121 -14.020  1.00 34.73           O  
ANISOU 1469  O   ARG A1188     2878   4296   6022   1386   -511  -2613       O  
ATOM   1470  CB  ARG A1188       8.880 -12.179 -14.028  1.00 25.49           C  
ANISOU 1470  CB  ARG A1188     3264   3223   3197    357    296   -566       C  
ATOM   1471  CG  ARG A1188       8.168 -11.248 -14.983  1.00 33.53           C  
ANISOU 1471  CG  ARG A1188     4077   4229   4432    703   -477   -450       C  
ATOM   1472  CD  ARG A1188       9.138 -10.392 -15.790  1.00 38.25           C  
ANISOU 1472  CD  ARG A1188     4475   4881   5174    -23   -108   -692       C  
ATOM   1473  NE  ARG A1188       9.649 -11.077 -16.985  1.00 44.77           N  
ANISOU 1473  NE  ARG A1188     5414   5865   5732    538     78  -1008       N  
ATOM   1474  CZ  ARG A1188       9.045 -11.140 -18.181  1.00 44.46           C  
ANISOU 1474  CZ  ARG A1188     5860   5431   5599    536     73   -678       C  
ATOM   1475  NH1 ARG A1188       7.863 -10.570 -18.400  1.00 49.04           N  
ANISOU 1475  NH1 ARG A1188     5905   6916   5810   1023    212   -775       N  
ATOM   1476  NH2 ARG A1188       9.634 -11.791 -19.183  1.00 42.32           N  
ANISOU 1476  NH2 ARG A1188     5864   4623   5591   -164     28   -912       N  
ATOM   1477  N   ARG A1189       7.179 -14.840 -14.474  1.00 23.76           N  
ANISOU 1477  N   ARG A1189     2360   3133   3534    390     22  -1316       N  
ATOM   1478  CA AARG A1189       6.206 -15.545 -15.318  0.60 24.72           C  
ANISOU 1478  CA AARG A1189     2659   3240   3492    275   -341   -943       C  
ATOM   1479  CA BARG A1189       6.190 -15.530 -15.314  0.40 25.98           C  
ANISOU 1479  CA BARG A1189     2747   3452   3671    137   -425   -876       C  
ATOM   1480  C   ARG A1189       5.244 -16.457 -14.530  1.00 25.34           C  
ANISOU 1480  C   ARG A1189     1931   3998   3699    272   -367   -923       C  
ATOM   1481  O   ARG A1189       4.241 -16.909 -15.062  1.00 30.42           O  
ANISOU 1481  O   ARG A1189     1843   5284   4428    265   -760   -828       O  
ATOM   1482  CB AARG A1189       6.957 -16.323 -16.400  0.60 23.11           C  
ANISOU 1482  CB AARG A1189     2718   2914   3146     60   -123   -580       C  
ATOM   1483  CB BARG A1189       6.889 -16.244 -16.477  0.40 26.79           C  
ANISOU 1483  CB BARG A1189     3233   3422   3523     26   -159   -671       C  
ATOM   1484  CG AARG A1189       7.677 -15.420 -17.392  0.60 22.67           C  
ANISOU 1484  CG AARG A1189     2467   2919   3226    261    -93   -412       C  
ATOM   1485  CG BARG A1189       7.070 -15.315 -17.669  0.40 29.39           C  
ANISOU 1485  CG BARG A1189     3524   3560   4081    -79    -32   -295       C  
ATOM   1486  CD AARG A1189       8.680 -16.198 -18.221  0.60 24.05           C  
ANISOU 1486  CD AARG A1189     3355   2739   3044    100    494   -338       C  
ATOM   1487  CD BARG A1189       8.089 -15.810 -18.676  0.40 29.78           C  
ANISOU 1487  CD BARG A1189     3865   3607   3841     -8    -10   -345       C  
ATOM   1488  NE AARG A1189       9.365 -15.386 -19.238  0.60 25.25           N  
ANISOU 1488  NE AARG A1189     3345   2547   3702   -236    759   -361       N  
ATOM   1489  NE BARG A1189       7.691 -15.486 -20.044  0.40 29.07           N  
ANISOU 1489  NE BARG A1189     3597   3220   4228    149   -142    138       N  
ATOM   1490  CZ AARG A1189       8.887 -15.064 -20.448  0.60 30.29           C  
ANISOU 1490  CZ AARG A1189     4394   3001   4114   -151    601    398       C  
ATOM   1491  CZ BARG A1189       8.536 -15.206 -21.034  0.40 27.08           C  
ANISOU 1491  CZ BARG A1189     3620   2844   3824    289   -220     73       C  
ATOM   1492  NH1AARG A1189       7.670 -15.442 -20.858  0.60 31.94           N  
ANISOU 1492  NH1AARG A1189     4893   3241   4001   -551    139    525       N  
ATOM   1493  NH1BARG A1189       9.853 -15.173 -20.820  0.40 24.53           N  
ANISOU 1493  NH1BARG A1189     3669   2419   3232    774   -382    252       N  
ATOM   1494  NH2AARG A1189       9.652 -14.338 -21.269  0.60 33.70           N  
ANISOU 1494  NH2AARG A1189     5383   3067   4353   -649    504    616       N  
ATOM   1495  NH2BARG A1189       8.059 -14.932 -22.241  0.40 24.89           N  
ANISOU 1495  NH2BARG A1189     3003   2698   3753    336    -72   -120       N  
ATOM   1496  N   ALA A1190       5.537 -16.720 -13.256  1.00 29.31           N  
ANISOU 1496  N   ALA A1190     2400   4813   3919    285     -1   -655       N  
ATOM   1497  CA  ALA A1190       4.680 -17.563 -12.425  1.00 29.40           C  
ANISOU 1497  CA  ALA A1190     2137   4784   4247    523    819  -1102       C  
ATOM   1498  C   ALA A1190       3.662 -16.706 -11.677  1.00 39.48           C  
ANISOU 1498  C   ALA A1190     2144   8098   4758   1471   1494  -1268       C  
ATOM   1499  O   ALA A1190       2.904 -17.229 -10.869  1.00 53.37           O  
ANISOU 1499  O   ALA A1190     3297  10084   6897    924   1353    642       O  
ATOM   1500  CB  ALA A1190       5.508 -18.376 -11.443  1.00 36.13           C  
ANISOU 1500  CB  ALA A1190     3346   4929   5450   -284    262    -67       C  
TER    1501      ALA A1190                                                      
HETATM 1502  OAX 9HH A1201      24.251 -19.986 -21.747  1.00 20.10           O  
ANISOU 1502  OAX 9HH A1201     1535   2240   3861    -22    727   -189       O  
HETATM 1503  SAB 9HH A1201      23.864 -18.667 -21.358  1.00 15.06           S  
ANISOU 1503  SAB 9HH A1201     1247   2027   2446   -429    488   -279       S  
HETATM 1504  OAW 9HH A1201      24.582 -18.024 -20.307  1.00 29.45           O  
ANISOU 1504  OAW 9HH A1201     1959   5690   3539   -874    613  -1931       O  
HETATM 1505  CAA 9HH A1201      23.944 -17.655 -22.774  1.00 22.44           C  
ANISOU 1505  CAA 9HH A1201     1696   3408   3421   -162   1005    797       C  
HETATM 1506  NAC 9HH A1201      22.303 -18.700 -20.934  1.00 11.01           N  
ANISOU 1506  NAC 9HH A1201     1175   1222   1783    -58    305     31       N  
HETATM 1507  CAD 9HH A1201      21.701 -19.885 -20.434  1.00 10.15           C  
ANISOU 1507  CAD 9HH A1201     1186   1143   1525     38    127    107       C  
HETATM 1508  CAI 9HH A1201      21.118 -20.807 -21.317  1.00 10.11           C  
ANISOU 1508  CAI 9HH A1201     1134   1321   1384    164    215    -15       C  
HETATM 1509  CAH 9HH A1201      20.650 -22.025 -20.804  1.00  9.20           C  
ANISOU 1509  CAH 9HH A1201     1225   1000   1270    286    147   -224       C  
HETATM 1510  CAG 9HH A1201      20.759 -22.298 -19.451  1.00 10.93           C  
ANISOU 1510  CAG 9HH A1201     1285   1453   1414    205    190     31       C  
HETATM 1511  CAF 9HH A1201      21.319 -21.374 -18.594  1.00 10.98           C  
ANISOU 1511  CAF 9HH A1201     1432   1348   1390    301     33     59       C  
HETATM 1512  CAE 9HH A1201      21.801 -20.176 -19.074  1.00 10.79           C  
ANISOU 1512  CAE 9HH A1201     1477   1236   1385    297    226   -176       C  
HETATM 1513  CAJ 9HH A1201      21.036 -20.572 -22.787  1.00 10.24           C  
ANISOU 1513  CAJ 9HH A1201     1242   1228   1420    -37    -88      3       C  
HETATM 1514  CAK 9HH A1201      20.360 -19.455 -23.284  1.00 11.17           C  
ANISOU 1514  CAK 9HH A1201     1452   1212   1576   -110   -169     23       C  
HETATM 1515  CAL 9HH A1201      20.231 -19.270 -24.653  1.00 11.74           C  
ANISOU 1515  CAL 9HH A1201     1483   1381   1597   -135   -158    292       C  
HETATM 1516  CAM 9HH A1201      20.766 -20.187 -25.551  1.00 11.74           C  
ANISOU 1516  CAM 9HH A1201     1501   1570   1389   -155   -406    103       C  
HETATM 1517  CAN 9HH A1201      21.457 -21.305 -25.085  1.00 11.33           C  
ANISOU 1517  CAN 9HH A1201     1522   1400   1380   -199   -238    -21       C  
HETATM 1518  CAV 9HH A1201      21.589 -21.485 -23.700  1.00  9.62           C  
ANISOU 1518  CAV 9HH A1201     1109   1248   1296   -216    -91      5       C  
HETATM 1519  CAO 9HH A1201      22.130 -22.427 -25.705  1.00 12.23           C  
ANISOU 1519  CAO 9HH A1201     1767   1735   1145   -131   -104   -213       C  
HETATM 1520  CAT 9HH A1201      22.646 -23.211 -24.656  1.00 10.80           C  
ANISOU 1520  CAT 9HH A1201     1512   1419   1169   -207   -152   -303       C  
HETATM 1521  NAU 9HH A1201      22.298 -22.642 -23.452  1.00  9.17           N  
ANISOU 1521  NAU 9HH A1201     1269   1103   1111   -236   -102   -122       N  
HETATM 1522  CAP 9HH A1201      22.394 -22.805 -27.021  1.00 14.26           C  
ANISOU 1522  CAP 9HH A1201     2250   1941   1225   -159   -272   -514       C  
HETATM 1523  CAQ 9HH A1201      23.178 -23.920 -27.264  1.00 16.16           C  
ANISOU 1523  CAQ 9HH A1201     2371   2123   1644    121   -391   -296       C  
HETATM 1524  CAR 9HH A1201      23.698 -24.675 -26.216  1.00 14.83           C  
ANISOU 1524  CAR 9HH A1201     2242   1662   1730     88    -41   -247       C  
HETATM 1525  CAS 9HH A1201      23.425 -24.341 -24.903  1.00 13.97           C  
ANISOU 1525  CAS 9HH A1201     2039   1554   1714     -5   -308   -364       C  
HETATM 1526  O   HOH A1301       7.338 -14.911 -23.922  0.50 22.96           O  
ANISOU 1526  O   HOH A1301     2392   3102   3230   1216    199   -911       O  
HETATM 1527  O   HOH A1302      19.988 -28.886  -6.888  1.00 45.09           O  
ANISOU 1527  O   HOH A1302     7479   4821   4832  -1135    620   1480       O  
HETATM 1528  O   HOH A1303      30.188 -11.393 -23.260  1.00 25.42           O  
ANISOU 1528  O   HOH A1303     5334   2020   2302     70   -937    413       O  
HETATM 1529  O   HOH A1304      14.325 -25.500 -37.142  1.00 38.80           O  
ANISOU 1529  O   HOH A1304     5744   6733   2264  -2166    472   -704       O  
HETATM 1530  O   HOH A1305      39.482 -27.101 -21.122  1.00 19.89           O  
ANISOU 1530  O   HOH A1305     1320   3821   2416   -210   -455  -2148       O  
HETATM 1531  O   HOH A1306      15.867 -11.347 -24.761  1.00 28.82           O  
ANISOU 1531  O   HOH A1306     2720   3188   5039    722    -84   1400       O  
HETATM 1532  O   HOH A1307      24.981 -36.747 -16.872  1.00 67.26           O  
ANISOU 1532  O   HOH A1307     8546   6969  10039  -5253   6682  -8223       O  
HETATM 1533  O   HOH A1308      26.266 -11.277 -18.253  1.00 32.81           O  
ANISOU 1533  O   HOH A1308     4186   3881   4398  -1666  -2330   1505       O  
HETATM 1534  O   HOH A1309      26.367 -11.781 -28.615  1.00 42.26           O  
ANISOU 1534  O   HOH A1309     4664   4956   6436    508   1988    244       O  
HETATM 1535  O   HOH A1310      13.985 -13.743  -8.182  1.00 42.78           O  
ANISOU 1535  O   HOH A1310     8609   4264   3380   -682   -444  -1445       O  
HETATM 1536  O   HOH A1311       1.368 -27.064 -27.622  1.00 24.43           O  
ANISOU 1536  O   HOH A1311     3269   3370   2640  -1962   1021  -1002       O  
HETATM 1537  O   HOH A1312       6.036 -34.013 -33.966  1.00 42.20           O  
ANISOU 1537  O   HOH A1312     5895   6150   3989   -415   -218    514       O  
HETATM 1538  O   HOH A1313      42.045 -28.186 -25.675  1.00 35.25           O  
ANISOU 1538  O   HOH A1313     3889   4775   4726   -597   -555    704       O  
HETATM 1539  O   HOH A1314      29.078 -11.207 -16.391  1.00 29.30           O  
ANISOU 1539  O   HOH A1314     3237   4694   3200  -1649   -764   1656       O  
HETATM 1540  O   HOH A1315      21.581 -16.485 -19.366  1.00 12.97           O  
ANISOU 1540  O   HOH A1315     1364   1274   2288   -115   -689   -150       O  
HETATM 1541  O   HOH A1316      17.574 -30.520  -8.412  1.00 49.93           O  
ANISOU 1541  O   HOH A1316     7988   5163   5818   1771   1007   1435       O  
HETATM 1542  O   HOH A1317      29.653 -22.803 -29.926  1.00 20.22           O  
ANISOU 1542  O   HOH A1317     2059   3178   2445   -241   -314   -392       O  
HETATM 1543  O   HOH A1318      29.854 -21.214 -26.349  1.00 31.48           O  
ANISOU 1543  O   HOH A1318     2662   3107   6189   -184   -735  -1502       O  
HETATM 1544  O   HOH A1319      31.289 -18.949 -21.640  1.00 34.94           O  
ANISOU 1544  O   HOH A1319     3729   5269   4274   1667    790   2188       O  
HETATM 1545  O   HOH A1320      22.858 -21.372  -6.022  1.00 46.53           O  
ANISOU 1545  O   HOH A1320     1953  14245   1480   2210    377    289       O  
HETATM 1546  O   HOH A1321      11.587 -17.673  -9.279  1.00 39.03           O  
ANISOU 1546  O   HOH A1321     5609   6620   2600   -679    429    134       O  
HETATM 1547  O   HOH A1322       5.141 -25.704 -12.653  1.00 21.16           O  
ANISOU 1547  O   HOH A1322     1710   3978   2351    412   -378     10       O  
HETATM 1548  O   HOH A1323       4.832 -30.970 -20.276  1.00 36.88           O  
ANISOU 1548  O   HOH A1323     2590   5896   5525    871    281  -1215       O  
HETATM 1549  O   HOH A1324      28.499 -14.510 -14.880  1.00 21.11           O  
ANISOU 1549  O   HOH A1324     2811   2678   2529   -359   -892    407       O  
HETATM 1550  O   HOH A1325      22.150 -27.024  -5.925  1.00 36.00           O  
ANISOU 1550  O   HOH A1325     4805   6860   2012   -368    608    382       O  
HETATM 1551  O   HOH A1326      27.921 -36.866 -40.139  1.00 36.30           O  
ANISOU 1551  O   HOH A1326     4182   5739   3869  -1471  -2023      6       O  
HETATM 1552  O   HOH A1327       6.206 -37.615 -23.676  1.00 42.45           O  
ANISOU 1552  O   HOH A1327     4899   5396   5831  -3717   -661   1325       O  
HETATM 1553  O   HOH A1328      20.947  -6.491 -19.609  1.00 41.10           O  
ANISOU 1553  O   HOH A1328     8312   1708   5594  -1311   1931   -195       O  
HETATM 1554  O   HOH A1329      12.801 -37.640 -19.905  1.00 36.10           O  
ANISOU 1554  O   HOH A1329     3581   3041   7094    -67    386   2500       O  
HETATM 1555  O   HOH A1330       7.477 -36.909 -31.220  1.00 33.29           O  
ANISOU 1555  O   HOH A1330     3182   5294   4170    150   -840  -1180       O  
HETATM 1556  O   HOH A1331      27.866 -19.742 -16.940  1.00 32.97           O  
ANISOU 1556  O   HOH A1331     3008   4148   5368  -1135   1371  -1104       O  
HETATM 1557  O   HOH A1332      35.298 -26.902 -26.465  1.00 16.26           O  
ANISOU 1557  O   HOH A1332     2014   2501   1663   -562   -317    179       O  
HETATM 1558  O   HOH A1333      25.452  -4.177 -34.179  1.00 33.53           O  
ANISOU 1558  O   HOH A1333     3600   3799   5338   -986   1579  -2498       O  
HETATM 1559  O   HOH A1334      29.460 -17.986 -28.543  1.00 45.11           O  
ANISOU 1559  O   HOH A1334     5367   4499   7271   1898  -3098  -3190       O  
HETATM 1560  O   HOH A1335      37.470  -9.956 -33.104  1.00 44.95           O  
ANISOU 1560  O   HOH A1335     2370  10221   4485   1407   1470   3005       O  
HETATM 1561  O   HOH A1336      28.834 -24.691  -6.013  1.00 31.99           O  
ANISOU 1561  O   HOH A1336     3461   3679   5014   -642   -196    481       O  
HETATM 1562  O   HOH A1337       6.964 -11.945 -20.555  1.00 45.85           O  
ANISOU 1562  O   HOH A1337     7062   4354   6005    897   1945    358       O  
HETATM 1563  O   HOH A1338      22.754 -10.295 -16.497  1.00 19.88           O  
ANISOU 1563  O   HOH A1338     3342   1587   2621    178   -332   -131       O  
HETATM 1564  O   HOH A1339      11.042 -40.843 -34.024  1.00 36.85           O  
ANISOU 1564  O   HOH A1339     4915   3768   5316   -190  -1756     56       O  
HETATM 1565  O   HOH A1340      10.455 -24.271 -37.451  1.00 43.69           O  
ANISOU 1565  O   HOH A1340     6720   5669   4210   2265  -2538  -1352       O  
HETATM 1566  O   HOH A1341       3.389 -21.425 -24.796  1.00 22.72           O  
ANISOU 1566  O   HOH A1341      869   3913   3850   -440     -2   1490       O  
HETATM 1567  O   HOH A1342      23.630 -18.018  -6.653  1.00 34.53           O  
ANISOU 1567  O   HOH A1342     5771   4537   2811  -2335  -1515   1847       O  
HETATM 1568  O   HOH A1343       6.998 -34.805 -18.164  1.00 40.04           O  
ANISOU 1568  O   HOH A1343     2748   4502   7963   -934    572    755       O  
HETATM 1569  O   HOH A1344       1.564 -20.978 -18.509  0.50 17.19           O  
ANISOU 1569  O   HOH A1344     1111   2445   2973     44   -151    -15       O  
HETATM 1570  O   HOH A1345      21.174  -6.093 -16.798  1.00 41.27           O  
ANISOU 1570  O   HOH A1345     4064   6720   4895    554   1398   2772       O  
HETATM 1571  O   HOH A1346      18.038 -27.837  -8.599  1.00 24.46           O  
ANISOU 1571  O   HOH A1346     2639   4604   2050  -1472   -334    496       O  
HETATM 1572  O   HOH A1347      32.991 -34.854 -13.845  1.00 36.31           O  
ANISOU 1572  O   HOH A1347     4418   5804   3572  -1356    487    807       O  
HETATM 1573  O   HOH A1348      13.017 -15.407 -27.739  1.00 18.91           O  
ANISOU 1573  O   HOH A1348     1770   2709   2705    429    -64    911       O  
HETATM 1574  O   HOH A1349      14.371 -16.648 -34.458  1.00 47.31           O  
ANISOU 1574  O   HOH A1349     7568   5594   4813   -137  -1818   2123       O  
HETATM 1575  O   HOH A1350       4.528 -30.721 -24.208  1.00 30.80           O  
ANISOU 1575  O   HOH A1350     3227   5110   3362    673    709     80       O  
HETATM 1576  O   HOH A1351      39.501 -32.621 -26.787  1.00 23.89           O  
ANISOU 1576  O   HOH A1351     2283   4569   2223   -203   -242   -502       O  
HETATM 1577  O   HOH A1352      17.576  -9.033  -9.601  1.00 49.60           O  
ANISOU 1577  O   HOH A1352     7201   7526   4117    768    468  -1377       O  
HETATM 1578  O   HOH A1353       9.196 -20.879 -32.437  1.00 41.61           O  
ANISOU 1578  O   HOH A1353     4412   6672   4725   -923    570   1310       O  
HETATM 1579  O   HOH A1354      26.335 -22.613 -14.872  1.00 12.76           O  
ANISOU 1579  O   HOH A1354     1935   1472   1438   -328   -116    280       O  
HETATM 1580  O   HOH A1355      15.716 -24.255  -9.013  1.00 35.66           O  
ANISOU 1580  O   HOH A1355     3382   6125   4039   -362    -44    107       O  
HETATM 1581  O   HOH A1356      16.167 -11.971 -15.559  1.00 23.67           O  
ANISOU 1581  O   HOH A1356     3446   1924   3620     50   -383     87       O  
HETATM 1582  O   HOH A1357       9.671 -38.239 -36.392  1.00 49.28           O  
ANISOU 1582  O   HOH A1357     8366   4568   5787  -1277  -1973  -1645       O  
HETATM 1583  O   HOH A1358      13.176 -10.994 -15.391  1.00 33.87           O  
ANISOU 1583  O   HOH A1358     4899   3863   4105   1170   -396  -1034       O  
HETATM 1584  O   HOH A1359      15.823 -11.617 -17.999  1.00 38.23           O  
ANISOU 1584  O   HOH A1359     3678   6827   4020  -1077   -293  -2023       O  
HETATM 1585  O   HOH A1360      11.020 -11.097 -11.208  1.00 41.62           O  
ANISOU 1585  O   HOH A1360     5948   4582   5283   1214   1065  -1872       O  
HETATM 1586  O   HOH A1361      38.505 -32.318 -32.606  1.00 25.69           O  
ANISOU 1586  O   HOH A1361     2708   3437   3615   -943    942   -778       O  
HETATM 1587  O   HOH A1362      40.604 -25.132 -22.218  1.00 28.83           O  
ANISOU 1587  O   HOH A1362     1776   6815   2362  -1056    458  -1796       O  
HETATM 1588  O   HOH A1363      38.044 -31.487 -20.526  1.00 32.91           O  
ANISOU 1588  O   HOH A1363     3253   3083   6167   1128  -1605  -1984       O  
HETATM 1589  O   HOH A1364      36.407 -34.478 -37.602  1.00 31.76           O  
ANISOU 1589  O   HOH A1364     4941   5155   1971  -2613   -209    613       O  
HETATM 1590  O   HOH A1365      29.327 -20.651  -4.268  1.00 21.14           O  
ANISOU 1590  O   HOH A1365     2468   3944   1617   -741   -137   -415       O  
HETATM 1591  O   HOH A1366      27.269 -20.036 -40.870  1.00 36.39           O  
ANISOU 1591  O   HOH A1366     4896   4793   4136    524   -894   -112       O  
HETATM 1592  O   HOH A1367       7.221 -16.027 -26.404  1.00 33.00           O  
ANISOU 1592  O   HOH A1367     3378   2828   6331    804   -825    588       O  
HETATM 1593  O   HOH A1368      11.988 -40.577 -23.909  1.00 40.69           O  
ANISOU 1593  O   HOH A1368     4510   4907   6042  -1518  -1101   -145       O  
HETATM 1594  O   HOH A1369      28.032 -23.446 -17.027  1.00 25.86           O  
ANISOU 1594  O   HOH A1369     2273   4826   2724    977   -796  -1162       O  
HETATM 1595  O   HOH A1370      21.571 -28.907 -13.357  1.00 39.06           O  
ANISOU 1595  O   HOH A1370     4188   4299   6353    746   -531    529       O  
HETATM 1596  O   HOH A1371      30.001  -7.840 -37.139  1.00 44.94           O  
ANISOU 1596  O   HOH A1371     5150   7289   4634  -2245   -319   1228       O  
HETATM 1597  O   HOH A1372      22.173 -15.486  -7.549  1.00 32.49           O  
ANISOU 1597  O   HOH A1372     4693   3619   4033    330    -79   -813       O  
HETATM 1598  O   HOH A1373      32.510 -25.277 -16.383  1.00 23.71           O  
ANISOU 1598  O   HOH A1373     4280   3054   1674    555    200   -311       O  
HETATM 1599  O   HOH A1374      35.438 -26.650 -17.478  1.00 18.25           O  
ANISOU 1599  O   HOH A1374     3225   2151   1556   -488    172   -649       O  
HETATM 1600  O   HOH A1375      18.339 -32.613 -15.534  1.00 32.32           O  
ANISOU 1600  O   HOH A1375     3249   3586   5442   -697  -1799   1842       O  
HETATM 1601  O   HOH A1376      25.849 -30.782  -8.113  1.00 34.76           O  
ANISOU 1601  O   HOH A1376     4281   4933   3992    513  -1860   1947       O  
HETATM 1602  O   HOH A1377      10.034 -31.981 -35.033  1.00 28.34           O  
ANISOU 1602  O   HOH A1377     3084   3865   3816   -971  -1090    604       O  
HETATM 1603  O   HOH A1378      31.386 -22.668 -22.776  1.00 18.68           O  
ANISOU 1603  O   HOH A1378     1260   2193   3644     82   -392    727       O  
HETATM 1604  O   HOH A1379      37.492 -22.897 -33.833  1.00 15.57           O  
ANISOU 1604  O   HOH A1379     2567   2415    935     49    285    178       O  
HETATM 1605  O   HOH A1380      31.032 -21.346 -31.361  1.00 48.69           O  
ANISOU 1605  O   HOH A1380     4636   9978   3886  -4067   -791   2995       O  
HETATM 1606  O   HOH A1381       4.145 -33.790 -25.470  1.00 44.88           O  
ANISOU 1606  O   HOH A1381     2346   5321   9382   -883   -837    997       O  
HETATM 1607  O   HOH A1382      12.329 -12.850 -26.813  1.00 34.98           O  
ANISOU 1607  O   HOH A1382     4189   2771   6328    220   1501   1135       O  
HETATM 1608  O   HOH A1383      17.443 -10.300 -13.848  1.00 42.14           O  
ANISOU 1608  O   HOH A1383     2914   5634   7459   -267   -235  -3384       O  
HETATM 1609  O   HOH A1384      40.094 -20.380 -32.905  1.00 26.48           O  
ANISOU 1609  O   HOH A1384     4656   3239   2163   -698  -1183    731       O  
HETATM 1610  O   HOH A1385      24.698 -35.534 -36.706  1.00 19.47           O  
ANISOU 1610  O   HOH A1385     3262   2627   1509   -465   -635    130       O  
HETATM 1611  O   HOH A1386      26.520 -24.026 -40.561  1.00 37.77           O  
ANISOU 1611  O   HOH A1386     6713   5065   2572    211  -1022   -371       O  
HETATM 1612  O   HOH A1387      31.874 -24.938 -24.390  1.00 21.84           O  
ANISOU 1612  O   HOH A1387     2986   2285   3024    -12     55   1283       O  
HETATM 1613  O   HOH A1388      16.097  -9.126 -20.096  1.00 40.86           O  
ANISOU 1613  O   HOH A1388     5718   3722   6082    416   1946    274       O  
HETATM 1614  O   HOH A1389      15.090 -23.152 -36.376  1.00 31.22           O  
ANISOU 1614  O   HOH A1389     4350   4899   2613   -387   -171   -414       O  
HETATM 1615  O   HOH A1390      31.755 -27.988  -9.283  1.00 47.55           O  
ANISOU 1615  O   HOH A1390     5152   5233   7681  -1909   2870     46       O  
HETATM 1616  O   HOH A1391      36.317 -11.559 -29.947  1.00 43.28           O  
ANISOU 1616  O   HOH A1391     4467   3787   8190    301   1710   1230       O  
HETATM 1617  O   HOH A1392      37.737 -40.631 -33.835  1.00 21.24           O  
ANISOU 1617  O   HOH A1392     2915   2935   2218     86   -146    -22       O  
HETATM 1618  O   HOH A1393      30.396 -27.095 -14.912  1.00 37.46           O  
ANISOU 1618  O   HOH A1393     5671   5042   3518    270  -1222  -1788       O  
HETATM 1619  O   HOH A1394      27.952 -15.643 -12.312  1.00 23.02           O  
ANISOU 1619  O   HOH A1394     1836   3884   3026  -1307   -524   1616       O  
HETATM 1620  O   HOH A1395      30.885 -19.133 -34.383  1.00 42.64           O  
ANISOU 1620  O   HOH A1395     5515   4517   6168    388   1346    976       O  
HETATM 1621  O   HOH A1396      37.301 -32.929 -35.720  1.00 44.56           O  
ANISOU 1621  O   HOH A1396     4834   4589   7507   1456    327    483       O  
HETATM 1622  O   HOH A1397      21.300 -11.520 -13.958  1.00 41.44           O  
ANISOU 1622  O   HOH A1397     4374   3252   8117   -950   -783   -588       O  
HETATM 1623  O   HOH A1398      42.142 -26.093 -24.477  1.00 35.51           O  
ANISOU 1623  O   HOH A1398     2295   7282   3916   -578    233    720       O  
HETATM 1624  O   HOH A1399      26.578 -10.282 -29.919  1.00 33.79           O  
ANISOU 1624  O   HOH A1399     2830   7671   2338   -671    594    615       O  
HETATM 1625  O   HOH A1400      10.776 -16.190 -28.947  1.00 41.56           O  
ANISOU 1625  O   HOH A1400     7609   3890   4290   -622   -803   1789       O  
HETATM 1626  O   HOH A1401      28.492  -9.885 -21.905  1.00 44.41           O  
ANISOU 1626  O   HOH A1401     7082   1873   7919    375   -127   2220       O  
HETATM 1627  O   HOH A1402      33.642 -24.823 -26.530  1.00 26.99           O  
ANISOU 1627  O   HOH A1402     4078   4284   1893   1974   -337   -783       O  
HETATM 1628  O   HOH A1403      22.815  -7.456 -36.561  1.00 37.36           O  
ANISOU 1628  O   HOH A1403     3444   7770   2981  -1522    255   -341       O  
HETATM 1629  O   HOH A1404      21.156 -24.614  -5.073  1.00 43.70           O  
ANISOU 1629  O   HOH A1404     5512   5447   5643   1447    332   -198       O  
HETATM 1630  O   HOH A1405      29.676 -18.594 -14.397  1.00 43.56           O  
ANISOU 1630  O   HOH A1405     1765   5884   8899   -769    142     72       O  
HETATM 1631  O   HOH A1406       4.576 -17.233 -26.801  1.00 31.26           O  
ANISOU 1631  O   HOH A1406     3713   3611   4552    849   -297    903       O  
HETATM 1632  O   HOH A1407       2.873 -18.663 -25.159  1.00 34.07           O  
ANISOU 1632  O   HOH A1407     2975   4774   5193    872    961   1446       O  
HETATM 1633  O   HOH A1408      30.613 -20.843 -18.241  1.00 42.93           O  
ANISOU 1633  O   HOH A1408     8687   5772   1853   4305   -783    337       O  
HETATM 1634  O   HOH A1409      -0.814 -26.100 -29.146  1.00 51.25           O  
ANISOU 1634  O   HOH A1409     6703   6822   5947    706  -1419   -280       O  
HETATM 1635  O   HOH A1410      14.436 -15.442 -37.079  1.00 63.00           O  
ANISOU 1635  O   HOH A1410    10643   8735   4555   1457  -4550  -1944       O  
HETATM 1636  O   HOH A1411      14.205 -22.093  -8.496  1.00 32.99           O  
ANISOU 1636  O   HOH A1411     3844   5062   3629   1210    408   1603       O  
HETATM 1637  O   HOH A1412      36.544  -8.153 -34.874  1.00 38.33           O  
ANISOU 1637  O   HOH A1412     6414   5617   2529   1424   1945    281       O  
HETATM 1638  O   HOH A1413      27.219  -8.296 -30.851  1.00 33.93           O  
ANISOU 1638  O   HOH A1413     3066   3134   6692    217   -473    231       O  
HETATM 1639  O   HOH A1414      23.236  -7.514 -16.805  1.00 35.50           O  
ANISOU 1639  O   HOH A1414     6283   2829   4373   -102   1085  -1066       O  
HETATM 1640  O   HOH A1415       8.334 -34.234 -35.185  1.00 34.18           O  
ANISOU 1640  O   HOH A1415     4109   4788   4088  -1450   -565  -1748       O  
HETATM 1641  O   HOH A1416      38.542 -27.421 -18.038  1.00 31.28           O  
ANISOU 1641  O   HOH A1416     6039   1565   4277   -540  -2480    -53       O  
HETATM 1642  O   HOH A1417      33.481 -22.556 -27.834  1.00 44.11           O  
ANISOU 1642  O   HOH A1417     6487   4494   5779   2144    290    -33       O  
HETATM 1643  O   HOH A1418      33.808 -18.316 -22.986  1.00 56.85           O  
ANISOU 1643  O   HOH A1418    10678   8707   2212  -5796    578   -330       O  
HETATM 1644  O   HOH A1419      35.688 -24.965 -15.236  1.00 15.76           O  
ANISOU 1644  O   HOH A1419     2421   1437   2129   -233    451    245       O  
HETATM 1645  O   HOH A1420      24.154 -27.853  -4.463  1.00 36.67           O  
ANISOU 1645  O   HOH A1420     4119   5585   4228  -2042    374   -413       O  
HETATM 1646  O   HOH A1421       1.564 -18.148 -18.509  0.50 24.04           O  
ANISOU 1646  O   HOH A1421     2571   2710   3851      0   -940      0       O  
HETATM 1647  O   HOH A1422       8.449 -30.129 -33.805  1.00 39.12           O  
ANISOU 1647  O   HOH A1422     5730   4892   4242  -2198  -1029   -690       O  
HETATM 1648  O   HOH A1423      18.201  -4.943 -20.135  1.00 39.23           O  
ANISOU 1648  O   HOH A1423     4245   3494   7166  -1383   1139    902       O  
HETATM 1649  O   HOH A1424      16.526  -5.955 -23.084  1.00 28.84           O  
ANISOU 1649  O   HOH A1424     2740   3209   5008     55   2009    656       O  
HETATM 1650  O   HOH A1425      26.576  -6.499 -16.639  1.00 48.31           O  
ANISOU 1650  O   HOH A1425     8271   3254   6829   3252   5821   3129       O  
HETATM 1651  O   HOH A1426      16.809  -7.493 -30.165  1.00 27.39           O  
ANISOU 1651  O   HOH A1426     3473   2230   4701  -1162    109   -615       O  
HETATM 1652  O   HOH A1427      31.595 -19.149 -16.592  1.00 72.54           O  
ANISOU 1652  O   HOH A1427     6143   7547  13871  -5119  -9060   7152       O  
HETATM 1653  O   HOH A1428      15.235  -6.354 -31.514  1.00 39.06           O  
ANISOU 1653  O   HOH A1428     5296   4984   4559   1228  -1267  -1553       O  
HETATM 1654  O   HOH A1429      10.743  -5.408 -21.038  1.00 49.31           O  
ANISOU 1654  O   HOH A1429     7038   3281   8415   1385    333    977       O  
HETATM 1655  O   HOH A1430      12.908  -4.462 -21.067  1.00 47.81           O  
ANISOU 1655  O   HOH A1430     5271   6628   6265   -295   3214   1340       O  
CONECT 1502 1503                                                                
CONECT 1503 1502 1504 1505 1506                                                 
CONECT 1504 1503                                                                
CONECT 1505 1503                                                                
CONECT 1506 1503 1507                                                           
CONECT 1507 1506 1508 1512                                                      
CONECT 1508 1507 1509 1513                                                      
CONECT 1509 1508 1510                                                           
CONECT 1510 1509 1511                                                           
CONECT 1511 1510 1512                                                           
CONECT 1512 1507 1511                                                           
CONECT 1513 1508 1514 1518                                                      
CONECT 1514 1513 1515                                                           
CONECT 1515 1514 1516                                                           
CONECT 1516 1515 1517                                                           
CONECT 1517 1516 1518 1519                                                      
CONECT 1518 1513 1517 1521                                                      
CONECT 1519 1517 1520 1522                                                      
CONECT 1520 1519 1521 1525                                                      
CONECT 1521 1518 1520                                                           
CONECT 1522 1519 1523                                                           
CONECT 1523 1522 1524                                                           
CONECT 1524 1523 1525                                                           
CONECT 1525 1520 1524                                                           
MASTER      334    0    1    6    7    0    3    6 1590    1   24   16          
END                                                                             



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