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HEADER    MEMBRANE PROTEIN                        18-JUL-08   3DVM              
TITLE     CRYSTAL STRUCTURE OF CA2+/CAM-CAV2.1 IQ DOMAIN COMPLEX                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CAM;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: VOLTAGE-DEPENDENT P/Q-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-  
COMPND   8 1A;                                                                  
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 1963-1982;                                    
COMPND  11 SYNONYM: VOLTAGE-GATED CALCIUM CHANNEL SUBUNIT ALPHA CAV2.1, CALCIUM 
COMPND  12 CHANNEL, L TYPE, ALPHA-1 POLYPEPTIDE ISOFORM 4, BRAIN CALCIUM CHANNEL
COMPND  13 I, BI;                                                               
COMPND  14 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: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,      
SOURCE   6 CAM3, CAMC, CAMIII;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PLYSS;                           
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PEGST;                                    
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE  14 ORGANISM_COMMON: RABBIT;                                             
SOURCE  15 ORGANISM_TAXID: 9986;                                                
SOURCE  16 GENE: CACNA1A, CACH4, CACN3, CACNL1A4;                               
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PLYSS;                           
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PET28B-HMT                                
KEYWDS    CALMODULIN, CALCIUM CHANNEL, IQ DOMAIN, INACTIVATION, FACILITATION,   
KEYWDS   2 CALCIUM-DEPENDENT, VOLTAGE-GATED, MEMBRANE PROTEIN                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.Y.KIM,C.H.RUMPF,Y.FUJIWARA,E.S.COOLEY,F.VAN PETEGEM,D.L.MINOR       
REVDAT   4   25-OCT-17 3DVM    1       REMARK                                   
REVDAT   3   13-JUL-11 3DVM    1       VERSN                                    
REVDAT   2   24-FEB-09 3DVM    1       VERSN                                    
REVDAT   1   04-NOV-08 3DVM    0                                                
JRNL        AUTH   E.Y.KIM,C.H.RUMPF,Y.FUJIWARA,E.S.COOLEY,F.VAN PETEGEM,       
JRNL        AUTH 2 D.L.MINOR                                                    
JRNL        TITL   STRUCTURES OF CA(V)2 CA(2+)/CAM-IQ DOMAIN COMPLEXES REVEAL   
JRNL        TITL 2 BINDING MODES THAT UNDERLIE CALCIUM-DEPENDENT INACTIVATION   
JRNL        TITL 3 AND FACILITATION.                                            
JRNL        REF    STRUCTURE                     V.  16  1455 2008              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   18940602                                                     
JRNL        DOI    10.1016/J.STR.2008.07.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 6460                           
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) : 0.278                           
REMARK   3   R VALUE            (WORKING SET) : 0.276                           
REMARK   3   FREE R VALUE                     : 0.320                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 310                             
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 297                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.13                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 20                           
REMARK   3   BIN FREE R VALUE                    : 0.4780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1174                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.28000                                              
REMARK   3    B22 (A**2) : 2.28000                                              
REMARK   3    B33 (A**2) : -3.42000                                             
REMARK   3    B12 (A**2) : 1.14000                                              
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): 0.681         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.377         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.344         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.090        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.917                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.869                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1187 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1602 ; 1.353 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   159 ; 6.658 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    54 ;31.479 ;26.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   185 ;17.079 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ;22.112 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   182 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   907 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   796 ; 2.422 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1242 ; 3.885 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   391 ; 3.028 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   360 ; 4.312 ; 5.000       
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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    11        A    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.8184  30.6776 152.6869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1003 T22:   0.5363                                     
REMARK   3      T33:  -0.1419 T12:   0.3327                                     
REMARK   3      T13:   0.1364 T23:   0.2004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3990 L22:   6.8453                                     
REMARK   3      L33:   8.4380 L12:  -2.6879                                     
REMARK   3      L13:   2.5541 L23:   2.4109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9438 S12:   0.9355 S13:   0.2327                       
REMARK   3      S21:  -1.0794 S22:  -1.0091 S23:  -0.4089                       
REMARK   3      S31:   0.4137 S32:   0.7398 S33:   0.0653                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    83        A   145                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5124   9.7598 163.4134              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1585 T22:   0.3223                                     
REMARK   3      T33:   0.0091 T12:   0.0492                                     
REMARK   3      T13:  -0.0781 T23:   0.1054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8086 L22:   6.7866                                     
REMARK   3      L33:   5.2631 L12:  -4.5247                                     
REMARK   3      L13:  -0.7760 L23:  -0.3374                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0067 S12:   0.3511 S13:   0.1511                       
REMARK   3      S21:   0.0464 S22:  -0.4292 S23:   0.1635                       
REMARK   3      S31:  -0.4708 S32:  -0.3129 S33:   0.4359                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1961        B  1982                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9148  26.2796 157.2018              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2732 T22:   0.2539                                     
REMARK   3      T33:  -0.0311 T12:   0.1306                                     
REMARK   3      T13:   0.0814 T23:   0.0486                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3775 L22:  19.5540                                     
REMARK   3      L33:   6.6452 L12:   6.0757                                     
REMARK   3      L13:   5.0973 L23:   9.8842                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0289 S12:  -0.1160 S13:   0.3556                       
REMARK   3      S21:  -0.8299 S22:  -0.0991 S23:  -0.6244                       
REMARK   3      S31:   0.3545 S32:   0.4630 S33:   0.0702                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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 3DVM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000048544.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-FEB-08; 22-FEB-08; 22-FEB-08;   
REMARK 200                                   22-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100; 100; 100                 
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y; Y                         
REMARK 200  RADIATION SOURCE               : ALS; ALS; ALS; ALS                 
REMARK 200  BEAMLINE                       : 8.3.1; 8.3.1; 8.3.1; 8.3.1         
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL; NULL             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M; M; M                         
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11587; 0.97957; 0.97969;         
REMARK 200                                   1.01987                            
REMARK 200  MONOCHROMATOR                  : NULL; NULL; NULL; NULL             
REMARK 200  OPTICS                         : NULL; NULL; NULL; NULL             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD; CCD; CCD                 
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC QUANTUM     
REMARK 200                                   315; ADSC QUANTUM 315; ADSC        
REMARK 200                                   QUANTUM 315                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6481                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 16.40                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD; MAD; MAD               
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE 2.13, RESOLVE 2.13                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 25 % PEG 3350, PH 5.5,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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      112.62333            
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      225.24667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      168.93500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      281.55833            
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       56.31167            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      112.62333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      225.24667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      281.55833            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      168.93500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       56.31167            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8680 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     MET A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
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     LEU A   4    CG   CD1  CD2                                       
REMARK 470     THR A   5    OG1  CG2                                            
REMARK 470     GLU A   6    CG   CD   OE1  OE2                                  
REMARK 470     GLU A   7    CG   CD   OE1  OE2                                  
REMARK 470     ILE A   9    CG1  CG2  CD1                                       
REMARK 470     PHE A  12    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     GLU A  45    CD   OE1  OE2                                       
REMARK 470     ARG A  74    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  75    CG   CD   CE   NZ                                   
REMARK 470     THR A  79    OG1  CG2                                            
REMARK 470     ASP A  80    CG   OD1  OD2                                       
REMARK 470     SER A  81    OG                                                  
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  84    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     ARG A 106    CZ   NH1  NH2                                       
REMARK 470     GLU A 114    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 115    CB   CG   CD   CE   NZ                              
REMARK 470     LEU A 116    CG   CD1  CD2                                       
REMARK 470     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 120    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 123    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 126    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B1976    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B1977    CG   CD   OE1  NE2                                  
REMARK 470     SER B1978    OG                                                  
REMARK 470     LYS B1981    CG   CD   CE   NZ                                   
REMARK 470     LYS B1982    CG   CD   CE   NZ                                   
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    ASP A  56       82.89    -67.35                                   
REMARK 500    ASP A  80       33.49    -92.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  72.3                                              
REMARK 620 3 ASP A  24   OD2  81.3  79.8                                        
REMARK 620 4 THR A  26   O   102.7 156.9  77.2                                  
REMARK 620 5 GLU A  31   OE1 116.3 123.5 153.2  79.2                            
REMARK 620 6 GLU A  31   OE2 105.4  74.2 149.4 128.1  49.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD2                                                    
REMARK 620 2 ASP A  58   OD1  62.4                                              
REMARK 620 3 ASN A  60   OD1  78.3  74.6                                        
REMARK 620 4 THR A  62   O    70.4 130.7  82.9                                  
REMARK 620 5 GLU A  67   OE1  84.7 112.8 155.6  74.9                            
REMARK 620 6 GLU A  67   OE2  68.2  64.4 135.5 110.9  48.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  78.8                                              
REMARK 620 3 ASN A  97   OD1  91.1  91.9                                        
REMARK 620 4 TYR A  99   O    89.8 160.7  72.6                                  
REMARK 620 5 GLU A 104   OE1  81.6  69.5 161.0 124.6                            
REMARK 620 6 GLU A 104   OE2  98.5 117.1 150.6  79.7  48.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  72.6                                              
REMARK 620 3 ASP A 133   OD1  92.1  79.8                                        
REMARK 620 4 GLN A 135   O    85.5 148.2  78.1                                  
REMARK 620 5 GLU A 140   OE1 109.7 131.0 145.8  77.7                            
REMARK 620 6 GLU A 140   OE2  83.8  79.1 158.8 122.1  53.6                      
REMARK 620 7 HOH A 513   O   170.7  98.2  87.4 103.4  75.1  93.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DVE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DVJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DVK   RELATED DB: PDB                                   
DBREF  3DVM A    1   148  UNP    P62158   CALM_HUMAN       2    149             
DBREF  3DVM B 1963  1982  UNP    P27884   CAC1A_RABIT   1963   1982             
SEQADV 3DVM HIS B 1961  UNP  P27884              EXPRESSION TAG                 
SEQADV 3DVM MET B 1962  UNP  P27884              EXPRESSION TAG                 
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
SEQRES   1 B   22  HIS MET GLY LYS ILE TYR ALA ALA MET MET ILE MET GLU          
SEQRES   2 B   22  TYR TYR ARG GLN SER LYS ALA LYS LYS                          
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *10(H2 O)                                                     
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  GLU A   54  1                                  11    
HELIX    4   4 PHE A   65  LYS A   75  1                                  11    
HELIX    5   5 ASP A   80  ASP A   93  1                                  14    
HELIX    6   6 SER A  101  LEU A  112  1                                  12    
HELIX    7   7 THR A  117  ASP A  129  1                                  13    
HELIX    8   8 TYR A  138  THR A  146  1                                   9    
HELIX    9   9 MET B 1962  ALA B 1980  1                                  19    
SHEET    1   A 2 THR A  26  ILE A  27  0                                        
SHEET    2   A 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1   B 2 TYR A  99  ILE A 100  0                                        
SHEET    2   B 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
LINK         OD1 ASP A  20                CA    CA A 501     1555   1555  2.50  
LINK         OD1 ASP A  22                CA    CA A 501     1555   1555  2.37  
LINK         OD2 ASP A  24                CA    CA A 501     1555   1555  2.68  
LINK         O   THR A  26                CA    CA A 501     1555   1555  2.28  
LINK         OE1 GLU A  31                CA    CA A 501     1555   1555  2.81  
LINK         OE2 GLU A  31                CA    CA A 501     1555   1555  2.45  
LINK         OD2 ASP A  56                CA    CA A 502     1555   1555  2.47  
LINK         OD1 ASP A  58                CA    CA A 502     1555   1555  2.60  
LINK         OD1 ASN A  60                CA    CA A 502     1555   1555  2.32  
LINK         O   THR A  62                CA    CA A 502     1555   1555  2.67  
LINK         OE1 GLU A  67                CA    CA A 502     1555   1555  2.32  
LINK         OE2 GLU A  67                CA    CA A 502     1555   1555  2.84  
LINK         OD1 ASP A  93                CA    CA A 503     1555   1555  2.37  
LINK         OD1 ASP A  95                CA    CA A 503     1555   1555  2.45  
LINK         OD1 ASN A  97                CA    CA A 503     1555   1555  2.59  
LINK         O   TYR A  99                CA    CA A 503     1555   1555  2.07  
LINK         OE1 GLU A 104                CA    CA A 503     1555   1555  2.67  
LINK         OE2 GLU A 104                CA    CA A 503     1555   1555  2.71  
LINK         OD1 ASP A 129                CA    CA A 504     1555   1555  2.33  
LINK         OD1 ASP A 131                CA    CA A 504     1555   1555  2.28  
LINK         OD1 ASP A 133                CA    CA A 504     1555   1555  2.43  
LINK         O   GLN A 135                CA    CA A 504     1555   1555  2.43  
LINK         OE1 GLU A 140                CA    CA A 504     1555   1555  2.40  
LINK         OE2 GLU A 140                CA    CA A 504     1555   1555  2.47  
LINK        CA    CA A 504                 O   HOH A 513     1555   1555  2.29  
SITE     1 AC1  5 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  5 GLU A  31                                                     
SITE     1 AC2  5 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  5 GLU A  67                                                     
SITE     1 AC3  5 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  5 GLU A 104                                                     
SITE     1 AC4  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 513                                          
CRYST1   43.956   43.956  337.870  90.00  90.00 120.00 P 61 2 2     12          
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      0.022750  0.013135  0.000000        0.00000                         
SCALE2      0.000000  0.026269  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002960        0.00000                         
ATOM      1  N   LEU A   4      11.453  14.476 137.287  1.00116.37           N  
ATOM      2  CA  LEU A   4      11.176  14.412 138.751  1.00116.39           C  
ATOM      3  C   LEU A   4      10.263  13.239 139.072  1.00116.51           C  
ATOM      4  O   LEU A   4       9.422  12.859 138.262  1.00115.48           O  
ATOM      5  CB  LEU A   4      10.552  15.721 139.245  1.00116.20           C  
ATOM      6  N   THR A   5      10.439  12.669 140.260  1.00117.50           N  
ATOM      7  CA  THR A   5       9.708  11.476 140.672  1.00117.43           C  
ATOM      8  C   THR A   5       8.200  11.661 140.575  1.00116.88           C  
ATOM      9  O   THR A   5       7.674  12.723 140.891  1.00114.51           O  
ATOM     10  CB  THR A   5      10.056  11.079 142.129  1.00117.34           C  
ATOM     11  N   GLU A   6       7.506  10.623 140.128  1.00118.38           N  
ATOM     12  CA  GLU A   6       6.081  10.540 140.384  1.00119.15           C  
ATOM     13  C   GLU A   6       5.866  10.831 141.872  1.00119.09           C  
ATOM     14  O   GLU A   6       4.817  11.349 142.266  1.00120.16           O  
ATOM     15  CB  GLU A   6       5.553   9.144 140.041  1.00119.63           C  
ATOM     16  N   GLU A   7       6.874  10.488 142.685  1.00117.79           N  
ATOM     17  CA  GLU A   7       6.829  10.591 144.162  1.00114.50           C  
ATOM     18  C   GLU A   7       6.978  12.005 144.764  1.00112.02           C  
ATOM     19  O   GLU A   7       6.424  12.296 145.830  1.00111.16           O  
ATOM     20  CB  GLU A   7       7.891   9.674 144.774  1.00114.85           C  
ATOM     21  N   GLN A   8       7.752  12.860 144.108  1.00109.05           N  
ATOM     22  CA  GLN A   8       7.925  14.238 144.564  1.00107.59           C  
ATOM     23  C   GLN A   8       6.701  15.081 144.235  1.00106.07           C  
ATOM     24  O   GLN A   8       6.570  16.226 144.692  1.00106.41           O  
ATOM     25  CB  GLN A   8       9.144  14.865 143.899  1.00109.27           C  
ATOM     26  CG  GLN A   8      10.454  14.250 144.268  1.00110.56           C  
ATOM     27  CD  GLN A   8      11.539  14.683 143.325  1.00111.90           C  
ATOM     28  OE1 GLN A   8      11.473  14.398 142.134  1.00112.38           O  
ATOM     29  NE2 GLN A   8      12.538  15.396 143.844  1.00113.00           N  
ATOM     30  N   ILE A   9       5.823  14.522 143.406  1.00103.68           N  
ATOM     31  CA  ILE A   9       4.601  15.201 142.992  1.00100.34           C  
ATOM     32  C   ILE A   9       3.613  15.218 144.156  1.00 97.34           C  
ATOM     33  O   ILE A   9       3.298  16.285 144.689  1.00 98.71           O  
ATOM     34  CB  ILE A   9       3.959  14.525 141.743  1.00100.13           C  
ATOM     35  N   ALA A  10       3.174  14.031 144.582  1.00 93.20           N  
ATOM     36  CA  ALA A  10       2.264  13.904 145.722  1.00 89.36           C  
ATOM     37  C   ALA A  10       2.907  14.500 146.962  1.00 86.89           C  
ATOM     38  O   ALA A  10       2.224  15.045 147.827  1.00 88.52           O  
ATOM     39  CB  ALA A  10       1.898  12.456 145.961  1.00 89.37           C  
ATOM     40  N   GLU A  11       4.231  14.431 147.014  1.00 81.71           N  
ATOM     41  CA  GLU A  11       4.983  14.988 148.120  1.00 77.40           C  
ATOM     42  C   GLU A  11       5.034  16.509 148.138  1.00 73.26           C  
ATOM     43  O   GLU A  11       4.716  17.112 149.154  1.00 76.32           O  
ATOM     44  CB  GLU A  11       6.386  14.390 148.188  1.00 79.19           C  
ATOM     45  CG  GLU A  11       6.418  12.956 148.750  1.00 81.37           C  
ATOM     46  CD  GLU A  11       7.725  12.614 149.511  1.00 83.48           C  
ATOM     47  OE1 GLU A  11       8.638  13.471 149.583  1.00 84.74           O  
ATOM     48  OE2 GLU A  11       7.837  11.480 150.045  1.00 84.12           O  
ATOM     49  N   PHE A  12       5.436  17.142 147.041  1.00 66.56           N  
ATOM     50  CA  PHE A  12       5.450  18.606 147.001  1.00 63.79           C  
ATOM     51  C   PHE A  12       4.007  19.119 147.182  1.00 63.30           C  
ATOM     52  O   PHE A  12       3.749  20.204 147.742  1.00 60.71           O  
ATOM     53  CB  PHE A  12       6.051  19.106 145.688  1.00 63.42           C  
ATOM     54  N   LYS A  13       3.076  18.276 146.761  1.00 61.57           N  
ATOM     55  CA  LYS A  13       1.660  18.550 146.879  1.00 59.27           C  
ATOM     56  C   LYS A  13       1.175  18.681 148.310  1.00 58.73           C  
ATOM     57  O   LYS A  13       0.669  19.719 148.687  1.00 59.84           O  
ATOM     58  CB  LYS A  13       0.860  17.460 146.198  1.00 59.92           C  
ATOM     59  CG  LYS A  13      -0.605  17.770 146.197  1.00 62.03           C  
ATOM     60  CD  LYS A  13      -1.412  16.695 145.510  1.00 61.48           C  
ATOM     61  CE  LYS A  13      -1.060  16.563 144.064  1.00 59.36           C  
ATOM     62  NZ  LYS A  13      -1.477  15.217 143.608  1.00 59.08           N  
ATOM     63  N   GLU A  14       1.291  17.613 149.097  1.00 59.35           N  
ATOM     64  CA  GLU A  14       0.842  17.635 150.492  1.00 58.44           C  
ATOM     65  C   GLU A  14       1.411  18.847 151.214  1.00 57.42           C  
ATOM     66  O   GLU A  14       0.693  19.549 151.932  1.00 57.68           O  
ATOM     67  CB  GLU A  14       1.253  16.365 151.219  1.00 57.39           C  
ATOM     68  CG  GLU A  14       0.390  15.174 150.929  1.00 61.28           C  
ATOM     69  CD  GLU A  14       1.114  13.854 151.206  1.00 64.89           C  
ATOM     70  OE1 GLU A  14       2.093  13.860 151.988  1.00 65.91           O  
ATOM     71  OE2 GLU A  14       0.720  12.811 150.626  1.00 66.81           O  
ATOM     72  N   ALA A  15       2.705  19.088 151.012  1.00 54.85           N  
ATOM     73  CA  ALA A  15       3.372  20.255 151.584  1.00 52.90           C  
ATOM     74  C   ALA A  15       2.527  21.517 151.381  1.00 55.09           C  
ATOM     75  O   ALA A  15       2.307  22.292 152.322  1.00 55.62           O  
ATOM     76  CB  ALA A  15       4.712  20.430 150.961  1.00 50.72           C  
ATOM     77  N   PHE A  16       2.086  21.734 150.143  1.00 53.84           N  
ATOM     78  CA  PHE A  16       1.198  22.851 149.819  1.00 55.12           C  
ATOM     79  C   PHE A  16      -0.041  22.783 150.715  1.00 55.70           C  
ATOM     80  O   PHE A  16      -0.419  23.759 151.368  1.00 55.80           O  
ATOM     81  CB  PHE A  16       0.775  22.790 148.319  1.00 53.05           C  
ATOM     82  CG  PHE A  16       0.104  24.032 147.839  1.00 50.53           C  
ATOM     83  CD1 PHE A  16       0.802  25.222 147.772  1.00 49.68           C  
ATOM     84  CD2 PHE A  16      -1.233  24.021 147.490  1.00 52.03           C  
ATOM     85  CE1 PHE A  16       0.192  26.370 147.340  1.00 52.25           C  
ATOM     86  CE2 PHE A  16      -1.862  25.171 147.053  1.00 53.03           C  
ATOM     87  CZ  PHE A  16      -1.144  26.350 146.973  1.00 53.36           C  
ATOM     88  N   SER A  17      -0.646  21.603 150.760  1.00 57.47           N  
ATOM     89  CA  SER A  17      -1.897  21.398 151.486  1.00 59.90           C  
ATOM     90  C   SER A  17      -1.782  21.707 152.991  1.00 59.51           C  
ATOM     91  O   SER A  17      -2.788  21.870 153.677  1.00 59.18           O  
ATOM     92  CB  SER A  17      -2.412  19.961 151.246  1.00 62.66           C  
ATOM     93  OG  SER A  17      -3.277  19.512 152.284  1.00 65.74           O  
ATOM     94  N   LEU A  18      -0.560  21.773 153.498  1.00 57.64           N  
ATOM     95  CA  LEU A  18      -0.360  22.128 154.874  1.00 58.39           C  
ATOM     96  C   LEU A  18      -0.772  23.573 155.067  1.00 57.73           C  
ATOM     97  O   LEU A  18      -1.300  23.957 156.113  1.00 53.80           O  
ATOM     98  CB  LEU A  18       1.106  21.935 155.270  1.00 60.94           C  
ATOM     99  CG  LEU A  18       1.482  22.523 156.627  1.00 61.47           C  
ATOM    100  CD1 LEU A  18       0.806  21.709 157.734  1.00 61.55           C  
ATOM    101  CD2 LEU A  18       2.979  22.590 156.802  1.00 62.05           C  
ATOM    102  N   PHE A  19      -0.525  24.388 154.057  1.00 59.27           N  
ATOM    103  CA  PHE A  19      -0.859  25.792 154.196  1.00 60.33           C  
ATOM    104  C   PHE A  19      -2.214  26.128 153.593  1.00 59.72           C  
ATOM    105  O   PHE A  19      -2.976  26.900 154.189  1.00 60.16           O  
ATOM    106  CB  PHE A  19       0.228  26.689 153.614  1.00 61.70           C  
ATOM    107  CG  PHE A  19       1.560  26.542 154.283  1.00 63.62           C  
ATOM    108  CD1 PHE A  19       1.950  27.417 155.305  1.00 65.64           C  
ATOM    109  CD2 PHE A  19       2.428  25.538 153.897  1.00 63.11           C  
ATOM    110  CE1 PHE A  19       3.198  27.285 155.926  1.00 65.02           C  
ATOM    111  CE2 PHE A  19       3.678  25.402 154.512  1.00 62.68           C  
ATOM    112  CZ  PHE A  19       4.058  26.271 155.520  1.00 63.13           C  
ATOM    113  N   ASP A  20      -2.520  25.551 152.425  1.00 57.53           N  
ATOM    114  CA  ASP A  20      -3.731  25.930 151.683  1.00 58.39           C  
ATOM    115  C   ASP A  20      -4.973  25.328 152.326  1.00 60.24           C  
ATOM    116  O   ASP A  20      -5.599  24.430 151.768  1.00 59.08           O  
ATOM    117  CB  ASP A  20      -3.625  25.516 150.219  1.00 59.62           C  
ATOM    118  CG  ASP A  20      -4.795  26.015 149.376  1.00 61.36           C  
ATOM    119  OD1 ASP A  20      -5.677  26.757 149.903  1.00 60.53           O  
ATOM    120  OD2 ASP A  20      -4.835  25.647 148.177  1.00 61.10           O  
ATOM    121  N   LYS A  21      -5.322  25.844 153.506  1.00 62.19           N  
ATOM    122  CA  LYS A  21      -6.297  25.201 154.383  1.00 64.45           C  
ATOM    123  C   LYS A  21      -7.700  25.143 153.764  1.00 62.96           C  
ATOM    124  O   LYS A  21      -8.371  24.123 153.841  1.00 64.26           O  
ATOM    125  CB  LYS A  21      -6.309  25.862 155.772  1.00 66.14           C  
ATOM    126  N   ASP A  22      -8.123  26.207 153.099  1.00 61.89           N  
ATOM    127  CA  ASP A  22      -9.359  26.108 152.300  1.00 59.51           C  
ATOM    128  C   ASP A  22      -9.160  25.341 150.981  1.00 59.86           C  
ATOM    129  O   ASP A  22     -10.111  24.785 150.437  1.00 60.95           O  
ATOM    130  CB  ASP A  22     -10.014  27.487 152.049  1.00 55.15           C  
ATOM    131  CG  ASP A  22      -9.040  28.517 151.489  1.00 54.07           C  
ATOM    132  OD1 ASP A  22      -8.012  28.121 150.885  1.00 55.54           O  
ATOM    133  OD2 ASP A  22      -9.304  29.723 151.649  1.00 50.40           O  
ATOM    134  N   GLY A  23      -7.935  25.304 150.458  1.00 59.31           N  
ATOM    135  CA  GLY A  23      -7.718  24.671 149.159  1.00 55.73           C  
ATOM    136  C   GLY A  23      -8.389  25.435 148.028  1.00 56.40           C  
ATOM    137  O   GLY A  23      -8.903  24.840 147.079  1.00 56.04           O  
ATOM    138  N   ASP A  24      -8.400  26.760 148.127  1.00 54.81           N  
ATOM    139  CA  ASP A  24      -8.842  27.569 147.005  1.00 55.28           C  
ATOM    140  C   ASP A  24      -7.703  27.641 145.979  1.00 54.24           C  
ATOM    141  O   ASP A  24      -7.894  28.074 144.846  1.00 57.41           O  
ATOM    142  CB  ASP A  24      -9.263  28.974 147.461  1.00 54.59           C  
ATOM    143  CG  ASP A  24      -8.097  29.786 147.954  1.00 54.59           C  
ATOM    144  OD1 ASP A  24      -8.276  30.971 148.287  1.00 55.59           O  
ATOM    145  OD2 ASP A  24      -6.986  29.229 148.006  1.00 55.35           O  
ATOM    146  N   GLY A  25      -6.514  27.234 146.387  1.00 51.46           N  
ATOM    147  CA  GLY A  25      -5.408  27.168 145.462  1.00 53.31           C  
ATOM    148  C   GLY A  25      -4.295  28.161 145.738  1.00 53.01           C  
ATOM    149  O   GLY A  25      -3.216  28.060 145.161  1.00 53.74           O  
ATOM    150  N   THR A  26      -4.542  29.126 146.612  1.00 51.65           N  
ATOM    151  CA  THR A  26      -3.515  30.111 146.922  1.00 52.21           C  
ATOM    152  C   THR A  26      -3.326  30.300 148.444  1.00 53.39           C  
ATOM    153  O   THR A  26      -4.282  30.155 149.233  1.00 50.97           O  
ATOM    154  CB  THR A  26      -3.810  31.465 146.263  1.00 52.92           C  
ATOM    155  OG1 THR A  26      -4.650  32.221 147.134  1.00 56.16           O  
ATOM    156  CG2 THR A  26      -4.525  31.274 144.903  1.00 49.91           C  
ATOM    157  N   ILE A  27      -2.083  30.599 148.844  1.00 50.68           N  
ATOM    158  CA  ILE A  27      -1.731  30.767 150.251  1.00 47.22           C  
ATOM    159  C   ILE A  27      -1.698  32.248 150.722  1.00 51.01           C  
ATOM    160  O   ILE A  27      -1.046  33.120 150.104  1.00 50.87           O  
ATOM    161  CB  ILE A  27      -0.436  30.068 150.541  1.00 43.23           C  
ATOM    162  CG1 ILE A  27      -0.610  28.560 150.237  1.00 42.43           C  
ATOM    163  CG2 ILE A  27      -0.017  30.318 151.979  1.00 44.83           C  
ATOM    164  CD1 ILE A  27       0.664  27.743 150.268  1.00 34.69           C  
ATOM    165  N   THR A  28      -2.442  32.531 151.789  1.00 50.52           N  
ATOM    166  CA  THR A  28      -2.550  33.880 152.310  1.00 52.88           C  
ATOM    167  C   THR A  28      -1.782  34.051 153.616  1.00 54.68           C  
ATOM    168  O   THR A  28      -1.428  33.070 154.294  1.00 56.15           O  
ATOM    169  CB  THR A  28      -4.002  34.224 152.655  1.00 54.49           C  
ATOM    170  OG1 THR A  28      -4.524  33.212 153.519  1.00 58.43           O  
ATOM    171  CG2 THR A  28      -4.883  34.333 151.411  1.00 53.41           C  
ATOM    172  N   THR A  29      -1.565  35.311 153.985  1.00 53.75           N  
ATOM    173  CA  THR A  29      -1.054  35.659 155.311  1.00 53.73           C  
ATOM    174  C   THR A  29      -1.822  34.969 156.428  1.00 54.77           C  
ATOM    175  O   THR A  29      -1.217  34.346 157.284  1.00 55.40           O  
ATOM    176  CB  THR A  29      -1.129  37.149 155.569  1.00 53.40           C  
ATOM    177  OG1 THR A  29      -2.497  37.591 155.414  1.00 54.46           O  
ATOM    178  CG2 THR A  29      -0.190  37.894 154.605  1.00 52.38           C  
ATOM    179  N   LYS A  30      -3.150  35.097 156.432  1.00 54.01           N  
ATOM    180  CA  LYS A  30      -3.977  34.353 157.381  1.00 50.13           C  
ATOM    181  C   LYS A  30      -3.564  32.872 157.476  1.00 52.16           C  
ATOM    182  O   LYS A  30      -3.265  32.391 158.557  1.00 56.22           O  
ATOM    183  CB  LYS A  30      -5.452  34.449 157.005  1.00 47.74           C  
ATOM    184  CG  LYS A  30      -6.033  35.834 157.115  1.00 46.01           C  
ATOM    185  CD  LYS A  30      -7.355  35.909 156.371  1.00 45.13           C  
ATOM    186  CE  LYS A  30      -7.533  37.272 155.721  1.00 43.63           C  
ATOM    187  NZ  LYS A  30      -8.319  38.076 156.646  1.00 41.64           N  
ATOM    188  N   GLU A  31      -3.536  32.152 156.352  1.00 52.40           N  
ATOM    189  CA  GLU A  31      -3.215  30.701 156.377  1.00 52.61           C  
ATOM    190  C   GLU A  31      -1.808  30.426 156.882  1.00 52.57           C  
ATOM    191  O   GLU A  31      -1.594  29.703 157.854  1.00 51.23           O  
ATOM    192  CB  GLU A  31      -3.378  30.093 154.993  1.00 51.52           C  
ATOM    193  CG  GLU A  31      -4.756  29.567 154.721  1.00 51.03           C  
ATOM    194  CD  GLU A  31      -5.107  29.657 153.273  1.00 50.72           C  
ATOM    195  OE1 GLU A  31      -4.258  30.162 152.499  1.00 51.74           O  
ATOM    196  OE2 GLU A  31      -6.238  29.251 152.894  1.00 52.52           O  
ATOM    197  N   LEU A  32      -0.840  31.014 156.218  1.00 54.55           N  
ATOM    198  CA  LEU A  32       0.497  30.991 156.733  1.00 56.48           C  
ATOM    199  C   LEU A  32       0.473  31.224 158.256  1.00 57.51           C  
ATOM    200  O   LEU A  32       1.083  30.477 159.033  1.00 60.00           O  
ATOM    201  CB  LEU A  32       1.310  32.072 156.037  1.00 55.06           C  
ATOM    202  CG  LEU A  32       2.781  31.950 156.284  1.00 52.47           C  
ATOM    203  CD1 LEU A  32       3.169  30.508 155.996  1.00 52.42           C  
ATOM    204  CD2 LEU A  32       3.442  32.918 155.387  1.00 55.02           C  
ATOM    205  N   GLY A  33      -0.253  32.254 158.676  1.00 59.88           N  
ATOM    206  CA  GLY A  33      -0.286  32.669 160.090  1.00 57.78           C  
ATOM    207  C   GLY A  33      -0.809  31.590 160.980  1.00 54.48           C  
ATOM    208  O   GLY A  33      -0.244  31.292 162.038  1.00 58.12           O  
ATOM    209  N   THR A  34      -1.893  30.986 160.564  1.00 50.84           N  
ATOM    210  CA  THR A  34      -2.436  29.930 161.357  1.00 51.08           C  
ATOM    211  C   THR A  34      -1.449  28.775 161.413  1.00 49.74           C  
ATOM    212  O   THR A  34      -1.326  28.091 162.446  1.00 51.41           O  
ATOM    213  CB  THR A  34      -3.864  29.486 160.911  1.00 51.88           C  
ATOM    214  OG1 THR A  34      -4.411  28.635 161.912  1.00 58.48           O  
ATOM    215  CG2 THR A  34      -3.858  28.732 159.615  1.00 53.07           C  
ATOM    216  N   VAL A  35      -0.692  28.583 160.340  1.00 47.32           N  
ATOM    217  CA  VAL A  35       0.259  27.473 160.330  1.00 45.88           C  
ATOM    218  C   VAL A  35       1.377  27.732 161.310  1.00 46.77           C  
ATOM    219  O   VAL A  35       1.769  26.842 162.081  1.00 47.80           O  
ATOM    220  CB  VAL A  35       0.845  27.233 158.971  1.00 46.73           C  
ATOM    221  CG1 VAL A  35       1.929  26.180 159.066  1.00 44.25           C  
ATOM    222  CG2 VAL A  35      -0.287  26.825 157.969  1.00 46.56           C  
ATOM    223  N   MET A  36       1.858  28.968 161.326  1.00 44.93           N  
ATOM    224  CA  MET A  36       2.956  29.315 162.219  1.00 42.48           C  
ATOM    225  C   MET A  36       2.509  29.235 163.674  1.00 43.97           C  
ATOM    226  O   MET A  36       3.317  28.973 164.580  1.00 48.34           O  
ATOM    227  CB  MET A  36       3.521  30.719 161.916  1.00 43.30           C  
ATOM    228  CG  MET A  36       4.127  30.949 160.507  1.00 33.65           C  
ATOM    229  SD  MET A  36       5.603  30.030 160.214  1.00 32.54           S  
ATOM    230  CE  MET A  36       6.474  30.548 161.669  1.00 34.66           C  
ATOM    231  N   ARG A  37       1.228  29.449 163.932  1.00 44.96           N  
ATOM    232  CA  ARG A  37       0.803  29.412 165.323  1.00 42.45           C  
ATOM    233  C   ARG A  37       0.726  27.979 165.742  1.00 42.05           C  
ATOM    234  O   ARG A  37       1.133  27.645 166.845  1.00 44.78           O  
ATOM    235  CB  ARG A  37      -0.502  30.180 165.557  1.00 40.85           C  
ATOM    236  CG  ARG A  37      -0.363  31.680 165.218  1.00 43.00           C  
ATOM    237  CD  ARG A  37      -1.527  32.507 165.747  1.00 42.11           C  
ATOM    238  NE  ARG A  37      -2.682  32.330 164.882  1.00 47.09           N  
ATOM    239  CZ  ARG A  37      -2.800  32.889 163.681  1.00 47.66           C  
ATOM    240  NH1 ARG A  37      -1.837  33.690 163.236  1.00 48.72           N  
ATOM    241  NH2 ARG A  37      -3.864  32.634 162.931  1.00 44.16           N  
ATOM    242  N   SER A  38       0.286  27.110 164.835  1.00 38.42           N  
ATOM    243  CA  SER A  38       0.356  25.677 165.109  1.00 38.54           C  
ATOM    244  C   SER A  38       1.793  25.280 165.483  1.00 41.17           C  
ATOM    245  O   SER A  38       2.006  24.429 166.329  1.00 45.86           O  
ATOM    246  CB  SER A  38      -0.108  24.860 163.910  1.00 40.42           C  
ATOM    247  OG  SER A  38       0.933  24.771 162.938  1.00 42.13           O  
ATOM    248  N   LEU A  39       2.789  25.914 164.881  1.00 42.62           N  
ATOM    249  CA  LEU A  39       4.169  25.519 165.158  1.00 40.29           C  
ATOM    250  C   LEU A  39       4.753  26.183 166.384  1.00 41.45           C  
ATOM    251  O   LEU A  39       5.947  26.134 166.619  1.00 42.53           O  
ATOM    252  CB  LEU A  39       5.032  25.806 163.953  1.00 39.90           C  
ATOM    253  CG  LEU A  39       4.570  24.880 162.831  1.00 42.43           C  
ATOM    254  CD1 LEU A  39       5.022  25.361 161.468  1.00 38.30           C  
ATOM    255  CD2 LEU A  39       5.038  23.435 163.142  1.00 41.77           C  
ATOM    256  N   GLY A  40       3.924  26.841 167.163  1.00 45.18           N  
ATOM    257  CA  GLY A  40       4.435  27.467 168.379  1.00 45.03           C  
ATOM    258  C   GLY A  40       5.095  28.820 168.181  1.00 48.80           C  
ATOM    259  O   GLY A  40       5.719  29.337 169.102  1.00 51.99           O  
ATOM    260  N   GLN A  41       4.941  29.415 166.993  1.00 52.36           N  
ATOM    261  CA  GLN A  41       5.420  30.785 166.733  1.00 52.71           C  
ATOM    262  C   GLN A  41       4.266  31.757 166.688  1.00 52.77           C  
ATOM    263  O   GLN A  41       3.120  31.337 166.604  1.00 55.77           O  
ATOM    264  CB  GLN A  41       6.203  30.835 165.428  1.00 53.76           C  
ATOM    265  CG  GLN A  41       7.650  30.448 165.645  1.00 60.11           C  
ATOM    266  CD  GLN A  41       8.184  30.975 166.981  1.00 60.35           C  
ATOM    267  OE1 GLN A  41       7.996  32.153 167.323  1.00 62.69           O  
ATOM    268  NE2 GLN A  41       8.820  30.104 167.743  1.00 59.50           N  
ATOM    269  N   ASN A  42       4.556  33.050 166.769  1.00 53.65           N  
ATOM    270  CA  ASN A  42       3.503  34.072 166.663  1.00 56.69           C  
ATOM    271  C   ASN A  42       3.942  35.311 165.882  1.00 54.13           C  
ATOM    272  O   ASN A  42       4.220  36.366 166.478  1.00 57.62           O  
ATOM    273  CB  ASN A  42       2.991  34.496 168.056  1.00 61.19           C  
ATOM    274  CG  ASN A  42       1.814  35.537 167.980  1.00 66.03           C  
ATOM    275  OD1 ASN A  42       1.076  35.614 166.974  1.00 64.44           O  
ATOM    276  ND2 ASN A  42       1.663  36.339 169.049  1.00 68.97           N  
ATOM    277  N   PRO A  43       3.968  35.202 164.553  1.00 48.32           N  
ATOM    278  CA  PRO A  43       4.546  36.229 163.686  1.00 45.57           C  
ATOM    279  C   PRO A  43       3.676  37.464 163.532  1.00 42.64           C  
ATOM    280  O   PRO A  43       2.504  37.332 163.380  1.00 52.15           O  
ATOM    281  CB  PRO A  43       4.696  35.510 162.358  1.00 42.85           C  
ATOM    282  CG  PRO A  43       3.697  34.411 162.394  1.00 42.42           C  
ATOM    283  CD  PRO A  43       3.565  33.994 163.819  1.00 45.12           C  
ATOM    284  N   THR A  44       4.245  38.662 163.559  1.00 45.49           N  
ATOM    285  CA  THR A  44       3.456  39.868 163.295  1.00 47.42           C  
ATOM    286  C   THR A  44       2.852  39.858 161.882  1.00 52.14           C  
ATOM    287  O   THR A  44       3.316  39.141 160.995  1.00 59.54           O  
ATOM    288  CB  THR A  44       4.289  41.139 163.418  1.00 46.63           C  
ATOM    289  OG1 THR A  44       5.334  41.110 162.440  1.00 46.11           O  
ATOM    290  CG2 THR A  44       4.873  41.255 164.823  1.00 47.72           C  
ATOM    291  N   GLU A  45       1.822  40.676 161.681  1.00 52.74           N  
ATOM    292  CA  GLU A  45       1.217  40.886 160.381  1.00 47.48           C  
ATOM    293  C   GLU A  45       2.295  41.196 159.318  1.00 51.56           C  
ATOM    294  O   GLU A  45       2.234  40.680 158.180  1.00 49.17           O  
ATOM    295  CB  GLU A  45       0.215  42.048 160.477  1.00 46.94           C  
ATOM    296  CG  GLU A  45       0.847  43.376 160.930  1.00 45.43           C  
ATOM    297  N   ALA A  46       3.287  42.016 159.699  1.00 50.55           N  
ATOM    298  CA  ALA A  46       4.316  42.510 158.758  1.00 50.17           C  
ATOM    299  C   ALA A  46       5.253  41.397 158.356  1.00 52.21           C  
ATOM    300  O   ALA A  46       5.763  41.363 157.221  1.00 53.48           O  
ATOM    301  CB  ALA A  46       5.113  43.669 159.375  1.00 46.81           C  
ATOM    302  N   GLU A  47       5.483  40.483 159.293  1.00 52.95           N  
ATOM    303  CA  GLU A  47       6.357  39.355 159.048  1.00 53.90           C  
ATOM    304  C   GLU A  47       5.707  38.399 158.058  1.00 53.73           C  
ATOM    305  O   GLU A  47       6.365  37.921 157.130  1.00 51.42           O  
ATOM    306  CB  GLU A  47       6.708  38.651 160.359  1.00 54.59           C  
ATOM    307  CG  GLU A  47       7.854  39.319 161.063  1.00 56.09           C  
ATOM    308  CD  GLU A  47       7.812  39.124 162.550  1.00 60.29           C  
ATOM    309  OE1 GLU A  47       7.070  38.226 163.010  1.00 61.76           O  
ATOM    310  OE2 GLU A  47       8.503  39.887 163.265  1.00 61.19           O  
ATOM    311  N   LEU A  48       4.410  38.152 158.226  1.00 49.24           N  
ATOM    312  CA  LEU A  48       3.707  37.265 157.302  1.00 49.37           C  
ATOM    313  C   LEU A  48       3.743  37.832 155.862  1.00 48.97           C  
ATOM    314  O   LEU A  48       4.156  37.165 154.913  1.00 44.88           O  
ATOM    315  CB  LEU A  48       2.272  37.009 157.777  1.00 49.49           C  
ATOM    316  CG  LEU A  48       2.095  36.288 159.142  1.00 51.71           C  
ATOM    317  CD1 LEU A  48       0.628  36.198 159.510  1.00 52.61           C  
ATOM    318  CD2 LEU A  48       2.709  34.886 159.139  1.00 51.49           C  
ATOM    319  N   GLN A  49       3.328  39.075 155.713  1.00 50.53           N  
ATOM    320  CA  GLN A  49       3.411  39.718 154.421  1.00 51.38           C  
ATOM    321  C   GLN A  49       4.829  39.574 153.897  1.00 51.13           C  
ATOM    322  O   GLN A  49       5.063  38.967 152.847  1.00 47.51           O  
ATOM    323  CB  GLN A  49       3.001  41.191 154.526  1.00 49.63           C  
ATOM    324  CG  GLN A  49       1.655  41.366 155.181  1.00 47.21           C  
ATOM    325  CD  GLN A  49       0.916  42.597 154.711  1.00 46.71           C  
ATOM    326  OE1 GLN A  49      -0.125  42.499 154.046  1.00 46.11           O  
ATOM    327  NE2 GLN A  49       1.425  43.765 155.075  1.00 44.11           N  
ATOM    328  N   ASP A  50       5.767  40.114 154.663  1.00 54.60           N  
ATOM    329  CA  ASP A  50       7.203  40.007 154.374  1.00 57.58           C  
ATOM    330  C   ASP A  50       7.646  38.581 153.944  1.00 55.65           C  
ATOM    331  O   ASP A  50       8.341  38.433 152.949  1.00 57.37           O  
ATOM    332  CB  ASP A  50       7.990  40.500 155.590  1.00 62.42           C  
ATOM    333  CG  ASP A  50       9.480  40.473 155.375  1.00 68.23           C  
ATOM    334  OD1 ASP A  50       9.962  39.676 154.543  1.00 71.54           O  
ATOM    335  OD2 ASP A  50      10.186  41.258 156.049  1.00 72.91           O  
ATOM    336  N   MET A  51       7.250  37.542 154.685  1.00 54.45           N  
ATOM    337  CA  MET A  51       7.564  36.164 154.268  1.00 48.55           C  
ATOM    338  C   MET A  51       6.998  35.881 152.849  1.00 50.19           C  
ATOM    339  O   MET A  51       7.686  35.329 152.002  1.00 52.38           O  
ATOM    340  CB  MET A  51       7.064  35.125 155.285  1.00 41.92           C  
ATOM    341  CG  MET A  51       7.672  35.229 156.728  1.00 40.50           C  
ATOM    342  SD  MET A  51       6.786  34.266 157.988  1.00 34.19           S  
ATOM    343  CE  MET A  51       6.833  32.700 157.132  1.00 34.40           C  
ATOM    344  N   ILE A  52       5.761  36.294 152.600  1.00 49.78           N  
ATOM    345  CA  ILE A  52       5.103  36.043 151.314  1.00 49.41           C  
ATOM    346  C   ILE A  52       5.753  36.797 150.112  1.00 51.75           C  
ATOM    347  O   ILE A  52       5.737  36.343 148.922  1.00 45.77           O  
ATOM    348  CB  ILE A  52       3.603  36.403 151.417  1.00 50.83           C  
ATOM    349  CG1 ILE A  52       2.869  35.393 152.321  1.00 50.16           C  
ATOM    350  CG2 ILE A  52       2.941  36.464 150.031  1.00 52.92           C  
ATOM    351  CD1 ILE A  52       1.377  35.530 152.280  1.00 50.53           C  
ATOM    352  N   ASN A  53       6.315  37.955 150.429  1.00 52.65           N  
ATOM    353  CA  ASN A  53       6.781  38.908 149.457  1.00 54.12           C  
ATOM    354  C   ASN A  53       8.018  38.394 148.743  1.00 56.35           C  
ATOM    355  O   ASN A  53       8.203  38.593 147.545  1.00 55.52           O  
ATOM    356  CB  ASN A  53       7.093  40.218 150.182  1.00 57.03           C  
ATOM    357  CG  ASN A  53       7.102  41.410 149.260  1.00 60.30           C  
ATOM    358  OD1 ASN A  53       8.169  41.871 148.827  1.00 58.64           O  
ATOM    359  ND2 ASN A  53       5.908  41.943 148.963  1.00 62.14           N  
ATOM    360  N   GLU A  54       8.848  37.698 149.486  1.00 56.28           N  
ATOM    361  CA  GLU A  54      10.047  37.188 148.926  1.00 58.11           C  
ATOM    362  C   GLU A  54       9.802  36.164 147.819  1.00 56.93           C  
ATOM    363  O   GLU A  54      10.627  36.014 146.932  1.00 62.84           O  
ATOM    364  CB  GLU A  54      10.936  36.639 150.033  1.00 61.06           C  
ATOM    365  CG  GLU A  54      11.459  37.742 150.937  1.00 64.02           C  
ATOM    366  CD  GLU A  54      12.324  37.219 152.045  1.00 65.45           C  
ATOM    367  OE1 GLU A  54      11.772  36.555 152.952  1.00 67.00           O  
ATOM    368  OE2 GLU A  54      13.555  37.470 152.008  1.00 67.24           O  
ATOM    369  N   VAL A  55       8.675  35.472 147.848  1.00 55.32           N  
ATOM    370  CA  VAL A  55       8.403  34.431 146.838  1.00 53.01           C  
ATOM    371  C   VAL A  55       7.350  34.824 145.770  1.00 51.99           C  
ATOM    372  O   VAL A  55       7.239  34.154 144.714  1.00 52.56           O  
ATOM    373  CB  VAL A  55       7.975  33.089 147.501  1.00 53.85           C  
ATOM    374  CG1 VAL A  55       9.122  32.476 148.296  1.00 54.60           C  
ATOM    375  CG2 VAL A  55       6.757  33.303 148.383  1.00 51.71           C  
ATOM    376  N   ASP A  56       6.583  35.879 146.077  1.00 50.44           N  
ATOM    377  CA  ASP A  56       5.462  36.353 145.252  1.00 48.56           C  
ATOM    378  C   ASP A  56       5.961  36.914 143.926  1.00 51.35           C  
ATOM    379  O   ASP A  56       6.110  38.127 143.769  1.00 50.22           O  
ATOM    380  CB  ASP A  56       4.662  37.410 145.994  1.00 42.73           C  
ATOM    381  CG  ASP A  56       3.301  37.704 145.323  1.00 41.14           C  
ATOM    382  OD1 ASP A  56       2.694  38.690 145.740  1.00 43.61           O  
ATOM    383  OD2 ASP A  56       2.799  36.838 144.525  1.00 31.47           O  
ATOM    384  N   ALA A  57       6.195  36.016 142.973  1.00 53.46           N  
ATOM    385  CA  ALA A  57       6.718  36.394 141.665  1.00 56.81           C  
ATOM    386  C   ALA A  57       5.836  37.430 140.971  1.00 59.22           C  
ATOM    387  O   ALA A  57       6.349  38.344 140.296  1.00 58.01           O  
ATOM    388  CB  ALA A  57       6.899  35.156 140.774  1.00 54.45           C  
ATOM    389  N   ASP A  58       4.515  37.278 141.107  1.00 61.15           N  
ATOM    390  CA  ASP A  58       3.565  38.084 140.326  1.00 61.86           C  
ATOM    391  C   ASP A  58       2.935  39.252 141.105  1.00 60.79           C  
ATOM    392  O   ASP A  58       2.049  39.932 140.588  1.00 61.83           O  
ATOM    393  CB  ASP A  58       2.476  37.185 139.757  1.00 64.11           C  
ATOM    394  CG  ASP A  58       1.771  36.414 140.828  1.00 67.36           C  
ATOM    395  OD1 ASP A  58       1.996  36.727 142.029  1.00 72.09           O  
ATOM    396  OD2 ASP A  58       1.006  35.492 140.489  1.00 68.63           O  
ATOM    397  N   GLY A  59       3.403  39.476 142.335  1.00 60.54           N  
ATOM    398  CA  GLY A  59       3.077  40.680 143.111  1.00 61.07           C  
ATOM    399  C   GLY A  59       1.620  40.801 143.577  1.00 63.48           C  
ATOM    400  O   GLY A  59       1.151  41.919 143.948  1.00 63.16           O  
ATOM    401  N   ASN A  60       0.905  39.671 143.559  1.00 63.98           N  
ATOM    402  CA  ASN A  60      -0.518  39.632 143.947  1.00 61.35           C  
ATOM    403  C   ASN A  60      -0.788  39.272 145.437  1.00 59.17           C  
ATOM    404  O   ASN A  60      -1.882  38.829 145.783  1.00 56.12           O  
ATOM    405  CB  ASN A  60      -1.296  38.712 143.009  1.00 59.75           C  
ATOM    406  CG  ASN A  60      -1.158  37.256 143.387  1.00 61.51           C  
ATOM    407  OD1 ASN A  60      -0.189  36.844 144.060  1.00 58.33           O  
ATOM    408  ND2 ASN A  60      -2.126  36.453 142.962  1.00 61.00           N  
ATOM    409  N   GLY A  61       0.213  39.511 146.279  1.00 57.18           N  
ATOM    410  CA  GLY A  61       0.074  39.433 147.728  1.00 59.12           C  
ATOM    411  C   GLY A  61      -0.225  38.061 148.308  1.00 58.99           C  
ATOM    412  O   GLY A  61      -0.206  37.871 149.528  1.00 59.87           O  
ATOM    413  N   THR A  62      -0.501  37.105 147.431  1.00 60.11           N  
ATOM    414  CA  THR A  62      -0.726  35.683 147.809  1.00 64.14           C  
ATOM    415  C   THR A  62       0.359  34.748 147.193  1.00 63.10           C  
ATOM    416  O   THR A  62       1.319  35.216 146.516  1.00 66.40           O  
ATOM    417  CB  THR A  62      -2.114  35.228 147.319  1.00 64.91           C  
ATOM    418  OG1 THR A  62      -2.298  33.835 147.603  1.00 68.46           O  
ATOM    419  CG2 THR A  62      -2.224  35.436 145.816  1.00 67.78           C  
ATOM    420  N   ILE A  63       0.240  33.442 147.453  1.00 62.49           N  
ATOM    421  CA  ILE A  63       1.212  32.450 146.967  1.00 62.28           C  
ATOM    422  C   ILE A  63       0.501  31.261 146.299  1.00 64.15           C  
ATOM    423  O   ILE A  63      -0.256  30.517 146.955  1.00 65.32           O  
ATOM    424  CB  ILE A  63       2.136  31.922 148.119  1.00 61.17           C  
ATOM    425  CG1 ILE A  63       3.036  33.037 148.646  1.00 61.29           C  
ATOM    426  CG2 ILE A  63       2.991  30.728 147.657  1.00 60.75           C  
ATOM    427  CD1 ILE A  63       3.623  32.757 150.032  1.00 63.21           C  
ATOM    428  N   ASP A  64       0.736  31.091 144.996  1.00 64.39           N  
ATOM    429  CA  ASP A  64       0.215  29.928 144.258  1.00 65.67           C  
ATOM    430  C   ASP A  64       1.197  28.775 144.274  1.00 67.48           C  
ATOM    431  O   ASP A  64       2.352  28.936 144.688  1.00 66.66           O  
ATOM    432  CB  ASP A  64      -0.104  30.289 142.814  1.00 65.41           C  
ATOM    433  CG  ASP A  64       1.056  30.947 142.115  1.00 66.10           C  
ATOM    434  OD1 ASP A  64       2.211  30.551 142.375  1.00 65.28           O  
ATOM    435  OD2 ASP A  64       0.811  31.872 141.311  1.00 68.06           O  
ATOM    436  N   PHE A  65       0.739  27.623 143.781  1.00 70.41           N  
ATOM    437  CA  PHE A  65       1.522  26.376 143.812  1.00 72.19           C  
ATOM    438  C   PHE A  65       2.969  26.526 143.327  1.00 71.48           C  
ATOM    439  O   PHE A  65       3.892  26.163 144.057  1.00 71.65           O  
ATOM    440  CB  PHE A  65       0.808  25.254 143.033  1.00 72.88           C  
ATOM    441  CG  PHE A  65       1.256  23.852 143.416  1.00 73.50           C  
ATOM    442  CD1 PHE A  65       0.559  23.110 144.370  1.00 74.15           C  
ATOM    443  CD2 PHE A  65       2.371  23.280 142.818  1.00 73.99           C  
ATOM    444  CE1 PHE A  65       0.979  21.822 144.730  1.00 74.41           C  
ATOM    445  CE2 PHE A  65       2.794  21.984 143.159  1.00 73.30           C  
ATOM    446  CZ  PHE A  65       2.093  21.254 144.107  1.00 73.85           C  
ATOM    447  N   PRO A  66       3.174  27.090 142.120  1.00 70.33           N  
ATOM    448  CA  PRO A  66       4.561  27.237 141.643  1.00 69.41           C  
ATOM    449  C   PRO A  66       5.409  28.215 142.480  1.00 68.46           C  
ATOM    450  O   PRO A  66       6.623  28.019 142.585  1.00 68.56           O  
ATOM    451  CB  PRO A  66       4.407  27.731 140.195  1.00 69.35           C  
ATOM    452  CG  PRO A  66       2.993  28.180 140.065  1.00 70.98           C  
ATOM    453  CD  PRO A  66       2.181  27.449 141.091  1.00 71.28           C  
ATOM    454  N   GLU A  67       4.794  29.259 143.047  1.00 65.19           N  
ATOM    455  CA  GLU A  67       5.527  30.165 143.954  1.00 64.19           C  
ATOM    456  C   GLU A  67       5.936  29.435 145.228  1.00 64.08           C  
ATOM    457  O   GLU A  67       6.917  29.858 145.933  1.00 64.50           O  
ATOM    458  CB  GLU A  67       4.704  31.368 144.324  1.00 64.07           C  
ATOM    459  CG  GLU A  67       4.613  32.424 143.199  1.00 63.92           C  
ATOM    460  CD  GLU A  67       3.758  33.639 143.537  1.00 64.95           C  
ATOM    461  OE1 GLU A  67       2.964  33.616 144.514  1.00 65.02           O  
ATOM    462  OE2 GLU A  67       3.857  34.638 142.800  1.00 65.86           O  
ATOM    463  N   PHE A  68       5.133  28.439 145.612  1.00 61.68           N  
ATOM    464  CA  PHE A  68       5.401  27.608 146.798  1.00 60.29           C  
ATOM    465  C   PHE A  68       6.557  26.660 146.470  1.00 59.93           C  
ATOM    466  O   PHE A  68       7.243  26.133 147.342  1.00 59.91           O  
ATOM    467  CB  PHE A  68       4.158  26.826 147.214  1.00 57.74           C  
ATOM    468  CG  PHE A  68       4.386  25.976 148.415  1.00 57.55           C  
ATOM    469  CD1 PHE A  68       4.419  26.538 149.696  1.00 55.54           C  
ATOM    470  CD2 PHE A  68       4.660  24.623 148.273  1.00 57.36           C  
ATOM    471  CE1 PHE A  68       4.680  25.765 150.780  1.00 54.52           C  
ATOM    472  CE2 PHE A  68       4.934  23.831 149.384  1.00 55.25           C  
ATOM    473  CZ  PHE A  68       4.942  24.400 150.630  1.00 54.89           C  
ATOM    474  N   LEU A  69       6.784  26.463 145.184  1.00 59.89           N  
ATOM    475  CA  LEU A  69       7.969  25.724 144.766  1.00 56.07           C  
ATOM    476  C   LEU A  69       9.213  26.626 144.851  1.00 57.40           C  
ATOM    477  O   LEU A  69      10.290  26.154 145.262  1.00 58.81           O  
ATOM    478  CB  LEU A  69       7.762  25.133 143.384  1.00 54.64           C  
ATOM    479  CG  LEU A  69       6.584  24.141 143.270  1.00 53.07           C  
ATOM    480  CD1 LEU A  69       6.553  23.410 141.918  1.00 53.52           C  
ATOM    481  CD2 LEU A  69       6.565  23.139 144.433  1.00 53.24           C  
ATOM    482  N   THR A  70       9.055  27.914 144.485  1.00 59.71           N  
ATOM    483  CA  THR A  70      10.073  28.969 144.783  1.00 64.79           C  
ATOM    484  C   THR A  70      10.509  29.031 146.272  1.00 65.85           C  
ATOM    485  O   THR A  70      11.697  29.221 146.564  1.00 67.42           O  
ATOM    486  CB  THR A  70       9.672  30.450 144.341  1.00 64.91           C  
ATOM    487  OG1 THR A  70       9.238  30.453 143.043  1.00 69.64           O  
ATOM    488  CG2 THR A  70      10.902  31.392 144.261  1.00 67.27           C  
ATOM    489  N   MET A  71       9.535  28.888 147.185  1.00 69.19           N  
ATOM    490  CA  MET A  71       9.734  28.716 148.641  1.00 69.84           C  
ATOM    491  C   MET A  71      10.618  27.514 148.994  1.00 72.97           C  
ATOM    492  O   MET A  71      11.677  27.662 149.628  1.00 72.28           O  
ATOM    493  CB  MET A  71       8.391  28.487 149.367  1.00 65.81           C  
ATOM    494  CG  MET A  71       7.384  29.649 149.421  1.00 59.47           C  
ATOM    495  SD  MET A  71       6.619  29.453 151.034  1.00 45.17           S  
ATOM    496  CE  MET A  71       7.403  30.941 151.716  1.00 24.07           C  
ATOM    497  N   MET A  72      10.160  26.329 148.612  1.00 73.80           N  
ATOM    498  CA  MET A  72      10.838  25.160 149.049  1.00 79.35           C  
ATOM    499  C   MET A  72      12.277  25.056 148.505  1.00 86.89           C  
ATOM    500  O   MET A  72      13.214  24.679 149.237  1.00 89.56           O  
ATOM    501  CB  MET A  72       9.969  23.918 148.848  1.00 74.66           C  
ATOM    502  CG  MET A  72       9.041  23.777 150.042  1.00 67.93           C  
ATOM    503  SD  MET A  72       7.978  22.337 150.147  1.00 70.14           S  
ATOM    504  CE  MET A  72       9.094  20.952 150.307  1.00 67.22           C  
ATOM    505  N   ALA A  73      12.477  25.492 147.267  1.00 92.42           N  
ATOM    506  CA  ALA A  73      13.773  25.351 146.620  1.00 95.06           C  
ATOM    507  C   ALA A  73      14.851  26.335 147.130  1.00 96.62           C  
ATOM    508  O   ALA A  73      16.038  26.045 147.056  1.00 98.78           O  
ATOM    509  CB  ALA A  73      13.603  25.456 145.114  1.00 94.45           C  
ATOM    510  N   ARG A  74      14.439  27.473 147.671  1.00 98.08           N  
ATOM    511  CA  ARG A  74      15.394  28.557 147.924  1.00101.05           C  
ATOM    512  C   ARG A  74      16.206  28.356 149.209  1.00103.85           C  
ATOM    513  O   ARG A  74      17.442  28.320 149.168  1.00104.18           O  
ATOM    514  CB  ARG A  74      14.695  29.931 147.914  1.00100.72           C  
ATOM    515  N   LYS A  75      15.508  28.220 150.339  1.00105.90           N  
ATOM    516  CA  LYS A  75      16.163  27.994 151.630  1.00105.95           C  
ATOM    517  C   LYS A  75      16.547  26.514 151.803  1.00107.13           C  
ATOM    518  O   LYS A  75      17.473  26.008 151.148  1.00106.16           O  
ATOM    519  CB  LYS A  75      15.261  28.454 152.779  1.00104.32           C  
ATOM    520  N   THR A  79      20.856  26.638 154.747  1.00100.91           N  
ATOM    521  CA  THR A  79      22.213  26.096 154.811  1.00102.40           C  
ATOM    522  C   THR A  79      22.728  25.902 156.254  1.00103.30           C  
ATOM    523  O   THR A  79      23.780  25.292 156.468  1.00103.94           O  
ATOM    524  CB  THR A  79      23.212  26.963 154.016  1.00100.57           C  
ATOM    525  N   ASP A  80      21.971  26.398 157.237  1.00103.90           N  
ATOM    526  CA  ASP A  80      22.272  26.154 158.664  1.00102.28           C  
ATOM    527  C   ASP A  80      21.500  24.906 159.184  1.00100.31           C  
ATOM    528  O   ASP A  80      21.116  24.828 160.361  1.00100.71           O  
ATOM    529  CB  ASP A  80      21.957  27.411 159.499  1.00101.06           C  
ATOM    530  N   SER A  81      21.322  23.932 158.285  1.00 97.81           N  
ATOM    531  CA  SER A  81      20.363  22.815 158.430  1.00 95.62           C  
ATOM    532  C   SER A  81      20.372  22.070 159.774  1.00 94.51           C  
ATOM    533  O   SER A  81      19.304  21.754 160.333  1.00 94.97           O  
ATOM    534  CB  SER A  81      20.557  21.806 157.287  1.00 95.18           C  
ATOM    535  N   GLU A  82      21.571  21.770 160.271  1.00 91.09           N  
ATOM    536  CA  GLU A  82      21.733  20.821 161.373  1.00 87.43           C  
ATOM    537  C   GLU A  82      21.083  21.281 162.655  1.00 83.69           C  
ATOM    538  O   GLU A  82      20.463  20.483 163.371  1.00 84.15           O  
ATOM    539  CB  GLU A  82      23.212  20.521 161.651  1.00 89.84           C  
ATOM    540  CG  GLU A  82      23.405  19.266 162.502  1.00 92.62           C  
ATOM    541  CD  GLU A  82      24.674  19.307 163.344  1.00 93.11           C  
ATOM    542  OE1 GLU A  82      24.786  20.239 164.173  1.00 92.63           O  
ATOM    543  OE2 GLU A  82      25.540  18.406 163.185  1.00 91.82           O  
ATOM    544  N   GLU A  83      21.254  22.561 162.970  1.00 78.09           N  
ATOM    545  CA  GLU A  83      20.738  23.118 164.210  1.00 73.02           C  
ATOM    546  C   GLU A  83      19.212  23.054 164.231  1.00 69.98           C  
ATOM    547  O   GLU A  83      18.616  22.763 165.269  1.00 68.93           O  
ATOM    548  CB  GLU A  83      21.222  24.556 164.390  1.00 73.22           C  
ATOM    549  N   GLU A  84      18.601  23.303 163.066  1.00 65.54           N  
ATOM    550  CA  GLU A  84      17.145  23.246 162.880  1.00 59.06           C  
ATOM    551  C   GLU A  84      16.623  21.805 162.879  1.00 55.25           C  
ATOM    552  O   GLU A  84      15.485  21.527 163.299  1.00 53.65           O  
ATOM    553  CB  GLU A  84      16.762  23.937 161.569  1.00 58.60           C  
ATOM    554  N   ILE A  85      17.459  20.889 162.408  1.00 48.76           N  
ATOM    555  CA  ILE A  85      17.072  19.490 162.330  1.00 43.28           C  
ATOM    556  C   ILE A  85      17.184  18.773 163.676  1.00 43.04           C  
ATOM    557  O   ILE A  85      16.289  18.011 164.055  1.00 39.15           O  
ATOM    558  CB  ILE A  85      17.879  18.743 161.271  1.00 41.90           C  
ATOM    559  CG1 ILE A  85      17.298  19.041 159.884  1.00 42.48           C  
ATOM    560  CG2 ILE A  85      17.801  17.259 161.544  1.00 39.45           C  
ATOM    561  CD1 ILE A  85      18.298  19.190 158.780  1.00 41.38           C  
ATOM    562  N   ARG A  86      18.284  19.025 164.395  1.00 43.69           N  
ATOM    563  CA  ARG A  86      18.439  18.532 165.770  1.00 43.63           C  
ATOM    564  C   ARG A  86      17.253  18.946 166.662  1.00 44.10           C  
ATOM    565  O   ARG A  86      16.833  18.192 167.530  1.00 42.89           O  
ATOM    566  CB  ARG A  86      19.774  18.992 166.375  1.00 42.65           C  
ATOM    567  N   GLU A  87      16.720  20.147 166.438  1.00 46.30           N  
ATOM    568  CA  GLU A  87      15.434  20.551 167.032  1.00 48.40           C  
ATOM    569  C   GLU A  87      14.291  19.686 166.571  1.00 48.25           C  
ATOM    570  O   GLU A  87      13.528  19.200 167.387  1.00 53.53           O  
ATOM    571  CB  GLU A  87      15.084  21.984 166.668  1.00 49.86           C  
ATOM    572  CG  GLU A  87      15.315  22.986 167.754  1.00 51.80           C  
ATOM    573  CD  GLU A  87      15.521  24.365 167.182  1.00 52.90           C  
ATOM    574  OE1 GLU A  87      14.697  24.779 166.331  1.00 52.36           O  
ATOM    575  OE2 GLU A  87      16.520  25.021 167.559  1.00 53.24           O  
ATOM    576  N   ALA A  88      14.122  19.554 165.258  1.00 46.66           N  
ATOM    577  CA  ALA A  88      13.039  18.728 164.730  1.00 43.83           C  
ATOM    578  C   ALA A  88      13.110  17.354 165.405  1.00 43.61           C  
ATOM    579  O   ALA A  88      12.111  16.869 165.947  1.00 40.36           O  
ATOM    580  CB  ALA A  88      13.139  18.598 163.219  1.00 39.91           C  
ATOM    581  N   PHE A  89      14.292  16.740 165.404  1.00 40.52           N  
ATOM    582  CA  PHE A  89      14.412  15.453 166.058  1.00 43.42           C  
ATOM    583  C   PHE A  89      13.841  15.552 167.483  1.00 47.23           C  
ATOM    584  O   PHE A  89      12.949  14.776 167.870  1.00 48.41           O  
ATOM    585  CB  PHE A  89      15.866  14.911 166.085  1.00 37.06           C  
ATOM    586  CG  PHE A  89      15.954  13.487 166.574  1.00 35.41           C  
ATOM    587  CD1 PHE A  89      15.756  12.440 165.708  1.00 36.25           C  
ATOM    588  CD2 PHE A  89      16.167  13.198 167.914  1.00 36.23           C  
ATOM    589  CE1 PHE A  89      15.770  11.134 166.153  1.00 35.06           C  
ATOM    590  CE2 PHE A  89      16.230  11.884 168.365  1.00 32.89           C  
ATOM    591  CZ  PHE A  89      16.045  10.857 167.490  1.00 33.16           C  
ATOM    592  N   ARG A  90      14.367  16.499 168.256  1.00 49.07           N  
ATOM    593  CA  ARG A  90      13.952  16.686 169.631  1.00 52.65           C  
ATOM    594  C   ARG A  90      12.422  16.786 169.708  1.00 55.05           C  
ATOM    595  O   ARG A  90      11.787  16.157 170.565  1.00 57.64           O  
ATOM    596  CB  ARG A  90      14.592  17.960 170.186  1.00 54.77           C  
ATOM    597  CG  ARG A  90      15.249  17.797 171.543  1.00 57.35           C  
ATOM    598  CD  ARG A  90      15.941  19.090 171.985  1.00 57.98           C  
ATOM    599  NE  ARG A  90      17.363  19.121 171.636  1.00 57.83           N  
ATOM    600  CZ  ARG A  90      17.923  20.003 170.808  1.00 56.84           C  
ATOM    601  NH1 ARG A  90      17.189  20.946 170.224  1.00 55.02           N  
ATOM    602  NH2 ARG A  90      19.226  19.943 170.571  1.00 56.83           N  
ATOM    603  N   VAL A  91      11.833  17.576 168.804  1.00 54.34           N  
ATOM    604  CA  VAL A  91      10.375  17.770 168.758  1.00 50.51           C  
ATOM    605  C   VAL A  91       9.623  16.458 168.537  1.00 49.75           C  
ATOM    606  O   VAL A  91       8.577  16.256 169.110  1.00 52.71           O  
ATOM    607  CB  VAL A  91       9.948  18.767 167.640  1.00 50.26           C  
ATOM    608  CG1 VAL A  91       8.445  18.946 167.663  1.00 47.45           C  
ATOM    609  CG2 VAL A  91      10.671  20.128 167.782  1.00 47.59           C  
ATOM    610  N   PHE A  92      10.158  15.588 167.679  1.00 50.02           N  
ATOM    611  CA  PHE A  92       9.563  14.274 167.381  1.00 48.43           C  
ATOM    612  C   PHE A  92       9.752  13.299 168.503  1.00 46.36           C  
ATOM    613  O   PHE A  92       8.862  12.514 168.808  1.00 47.60           O  
ATOM    614  CB  PHE A  92      10.232  13.653 166.156  1.00 51.83           C  
ATOM    615  CG  PHE A  92       9.795  14.247 164.886  1.00 55.23           C  
ATOM    616  CD1 PHE A  92       9.917  15.618 164.675  1.00 57.64           C  
ATOM    617  CD2 PHE A  92       9.231  13.454 163.890  1.00 57.28           C  
ATOM    618  CE1 PHE A  92       9.482  16.202 163.466  1.00 57.93           C  
ATOM    619  CE2 PHE A  92       8.801  14.015 162.681  1.00 58.00           C  
ATOM    620  CZ  PHE A  92       8.928  15.397 162.471  1.00 58.58           C  
ATOM    621  N   ASP A  93      10.945  13.290 169.078  1.00 40.94           N  
ATOM    622  CA  ASP A  93      11.268  12.270 170.027  1.00 38.49           C  
ATOM    623  C   ASP A  93      10.657  12.635 171.346  1.00 40.13           C  
ATOM    624  O   ASP A  93      11.367  12.950 172.286  1.00 36.78           O  
ATOM    625  CB  ASP A  93      12.762  12.125 170.181  1.00 35.14           C  
ATOM    626  CG  ASP A  93      13.131  10.942 171.041  1.00 36.75           C  
ATOM    627  OD1 ASP A  93      12.211  10.205 171.453  1.00 32.15           O  
ATOM    628  OD2 ASP A  93      14.345  10.752 171.320  1.00 40.60           O  
ATOM    629  N   LYS A  94       9.326  12.617 171.406  1.00 40.52           N  
ATOM    630  CA  LYS A  94       8.617  13.123 172.566  1.00 39.88           C  
ATOM    631  C   LYS A  94       9.313  12.719 173.880  1.00 39.82           C  
ATOM    632  O   LYS A  94       9.585  13.562 174.733  1.00 42.56           O  
ATOM    633  CB  LYS A  94       7.136  12.686 172.545  1.00 38.19           C  
ATOM    634  N   ASP A  95       9.622  11.443 174.051  1.00 36.56           N  
ATOM    635  CA  ASP A  95      10.149  11.014 175.338  1.00 33.48           C  
ATOM    636  C   ASP A  95      11.663  10.962 175.292  1.00 35.57           C  
ATOM    637  O   ASP A  95      12.319  10.487 176.215  1.00 38.33           O  
ATOM    638  CB  ASP A  95       9.590   9.652 175.717  1.00 32.10           C  
ATOM    639  CG  ASP A  95      10.005   8.568 174.753  1.00 34.35           C  
ATOM    640  OD1 ASP A  95      10.692   8.879 173.755  1.00 37.80           O  
ATOM    641  OD2 ASP A  95       9.653   7.395 174.989  1.00 33.12           O  
ATOM    642  N   GLY A  96      12.209  11.422 174.187  1.00 37.13           N  
ATOM    643  CA  GLY A  96      13.629  11.609 174.057  1.00 38.17           C  
ATOM    644  C   GLY A  96      14.455  10.457 174.549  1.00 38.83           C  
ATOM    645  O   GLY A  96      15.385  10.677 175.334  1.00 35.47           O  
ATOM    646  N   ASN A  97      14.106   9.224 174.128  1.00 37.16           N  
ATOM    647  CA  ASN A  97      14.987   8.040 174.418  1.00 34.05           C  
ATOM    648  C   ASN A  97      16.005   7.852 173.300  1.00 34.12           C  
ATOM    649  O   ASN A  97      16.735   6.874 173.278  1.00 36.50           O  
ATOM    650  CB  ASN A  97      14.194   6.730 174.599  1.00 27.95           C  
ATOM    651  CG  ASN A  97      13.593   6.238 173.291  1.00 27.50           C  
ATOM    652  OD1 ASN A  97      13.473   7.020 172.351  1.00 29.21           O  
ATOM    653  ND2 ASN A  97      13.229   4.934 173.210  1.00 20.08           N  
ATOM    654  N   GLY A  98      16.022   8.777 172.355  1.00 33.73           N  
ATOM    655  CA  GLY A  98      16.946   8.698 171.242  1.00 35.21           C  
ATOM    656  C   GLY A  98      16.363   8.082 169.992  1.00 41.01           C  
ATOM    657  O   GLY A  98      16.990   8.126 168.937  1.00 43.92           O  
ATOM    658  N   TYR A  99      15.153   7.520 170.095  1.00 42.40           N  
ATOM    659  CA  TYR A  99      14.493   6.906 168.939  1.00 40.74           C  
ATOM    660  C   TYR A  99      13.062   7.398 168.833  1.00 41.50           C  
ATOM    661  O   TYR A  99      12.347   7.514 169.849  1.00 37.06           O  
ATOM    662  CB  TYR A  99      14.444   5.371 169.038  1.00 43.52           C  
ATOM    663  CG  TYR A  99      15.766   4.680 169.246  1.00 45.74           C  
ATOM    664  CD1 TYR A  99      16.424   4.062 168.182  1.00 44.50           C  
ATOM    665  CD2 TYR A  99      16.343   4.593 170.528  1.00 45.57           C  
ATOM    666  CE1 TYR A  99      17.644   3.404 168.377  1.00 43.99           C  
ATOM    667  CE2 TYR A  99      17.566   3.943 170.723  1.00 43.33           C  
ATOM    668  CZ  TYR A  99      18.210   3.364 169.640  1.00 41.94           C  
ATOM    669  OH  TYR A  99      19.394   2.719 169.816  1.00 42.79           O  
ATOM    670  N   ILE A 100      12.652   7.658 167.587  1.00 37.45           N  
ATOM    671  CA  ILE A 100      11.311   8.026 167.236  1.00 34.59           C  
ATOM    672  C   ILE A 100      10.510   6.771 166.888  1.00 35.64           C  
ATOM    673  O   ILE A 100      10.895   6.017 165.988  1.00 32.69           O  
ATOM    674  CB  ILE A 100      11.328   8.851 165.967  1.00 36.15           C  
ATOM    675  CG1 ILE A 100      12.171  10.122 166.160  1.00 37.23           C  
ATOM    676  CG2 ILE A 100       9.888   9.121 165.513  1.00 31.32           C  
ATOM    677  CD1 ILE A 100      12.246  11.001 164.900  1.00 39.97           C  
ATOM    678  N   SER A 101       9.405   6.542 167.589  1.00 33.29           N  
ATOM    679  CA  SER A 101       8.591   5.377 167.315  1.00 36.21           C  
ATOM    680  C   SER A 101       7.520   5.718 166.276  1.00 37.39           C  
ATOM    681  O   SER A 101       7.230   6.894 166.035  1.00 40.28           O  
ATOM    682  CB  SER A 101       7.924   4.913 168.606  1.00 35.77           C  
ATOM    683  OG  SER A 101       6.968   5.870 169.036  1.00 39.87           O  
ATOM    684  N   ALA A 102       6.926   4.696 165.659  1.00 38.51           N  
ATOM    685  CA  ALA A 102       5.658   4.879 164.906  1.00 37.69           C  
ATOM    686  C   ALA A 102       4.661   5.736 165.700  1.00 39.50           C  
ATOM    687  O   ALA A 102       4.136   6.730 165.182  1.00 42.69           O  
ATOM    688  CB  ALA A 102       5.019   3.529 164.549  1.00 33.53           C  
ATOM    689  N   ALA A 103       4.415   5.374 166.963  1.00 38.57           N  
ATOM    690  CA  ALA A 103       3.510   6.162 167.812  1.00 39.60           C  
ATOM    691  C   ALA A 103       3.864   7.659 167.743  1.00 40.84           C  
ATOM    692  O   ALA A 103       3.010   8.509 167.435  1.00 38.97           O  
ATOM    693  CB  ALA A 103       3.557   5.669 169.241  1.00 36.12           C  
ATOM    694  N   GLU A 104       5.138   7.965 167.976  1.00 41.88           N  
ATOM    695  CA  GLU A 104       5.584   9.355 168.056  1.00 44.37           C  
ATOM    696  C   GLU A 104       5.464  10.036 166.730  1.00 44.22           C  
ATOM    697  O   GLU A 104       5.174  11.237 166.672  1.00 45.31           O  
ATOM    698  CB  GLU A 104       7.018   9.437 168.533  1.00 45.83           C  
ATOM    699  CG  GLU A 104       7.190   9.059 170.001  1.00 47.32           C  
ATOM    700  CD  GLU A 104       8.614   8.958 170.377  1.00 48.37           C  
ATOM    701  OE1 GLU A 104       8.993   9.474 171.449  1.00 49.29           O  
ATOM    702  OE2 GLU A 104       9.379   8.381 169.574  1.00 52.00           O  
ATOM    703  N   LEU A 105       5.690   9.270 165.660  1.00 44.15           N  
ATOM    704  CA  LEU A 105       5.441   9.752 164.300  1.00 42.27           C  
ATOM    705  C   LEU A 105       3.963  10.088 164.032  1.00 40.63           C  
ATOM    706  O   LEU A 105       3.667  11.168 163.497  1.00 39.86           O  
ATOM    707  CB  LEU A 105       5.929   8.759 163.255  1.00 40.83           C  
ATOM    708  CG  LEU A 105       6.021   9.362 161.834  1.00 38.00           C  
ATOM    709  CD1 LEU A 105       6.779  10.688 161.897  1.00 37.88           C  
ATOM    710  CD2 LEU A 105       6.727   8.413 160.890  1.00 34.08           C  
ATOM    711  N   ARG A 106       3.055   9.168 164.378  1.00 36.77           N  
ATOM    712  CA  ARG A 106       1.629   9.461 164.256  1.00 41.71           C  
ATOM    713  C   ARG A 106       1.395  10.847 164.788  1.00 40.56           C  
ATOM    714  O   ARG A 106       0.913  11.724 164.072  1.00 40.69           O  
ATOM    715  CB  ARG A 106       0.748   8.452 165.025  1.00 45.28           C  
ATOM    716  CG  ARG A 106       0.909   7.002 164.571  1.00 52.19           C  
ATOM    717  CD  ARG A 106      -0.282   6.119 164.974  1.00 53.14           C  
ATOM    718  NE  ARG A 106      -0.135   4.725 164.390  1.00 54.53           N  
ATOM    719  N   HIS A 107       1.810  11.068 166.032  1.00 41.86           N  
ATOM    720  CA  HIS A 107       1.436  12.288 166.745  1.00 43.00           C  
ATOM    721  C   HIS A 107       1.834  13.495 165.935  1.00 43.81           C  
ATOM    722  O   HIS A 107       1.064  14.460 165.839  1.00 43.73           O  
ATOM    723  CB  HIS A 107       2.102  12.379 168.128  1.00 41.64           C  
ATOM    724  CG  HIS A 107       1.468  11.519 169.167  1.00 41.01           C  
ATOM    725  ND1 HIS A 107       0.111  11.495 169.385  1.00 44.24           N  
ATOM    726  CD2 HIS A 107       2.009  10.676 170.078  1.00 43.61           C  
ATOM    727  CE1 HIS A 107      -0.164  10.663 170.376  1.00 44.17           C  
ATOM    728  NE2 HIS A 107       0.972  10.153 170.814  1.00 42.82           N  
ATOM    729  N   VAL A 108       3.049  13.447 165.370  1.00 44.14           N  
ATOM    730  CA  VAL A 108       3.587  14.582 164.629  1.00 45.87           C  
ATOM    731  C   VAL A 108       2.795  14.867 163.370  1.00 45.77           C  
ATOM    732  O   VAL A 108       2.426  16.002 163.131  1.00 45.97           O  
ATOM    733  CB  VAL A 108       5.076  14.427 164.278  1.00 45.63           C  
ATOM    734  CG1 VAL A 108       5.435  15.377 163.132  1.00 45.71           C  
ATOM    735  CG2 VAL A 108       5.933  14.743 165.493  1.00 44.70           C  
ATOM    736  N   MET A 109       2.521  13.832 162.582  1.00 44.67           N  
ATOM    737  CA  MET A 109       1.766  14.006 161.358  1.00 45.36           C  
ATOM    738  C   MET A 109       0.462  14.692 161.676  1.00 45.68           C  
ATOM    739  O   MET A 109       0.072  15.639 161.007  1.00 44.69           O  
ATOM    740  CB  MET A 109       1.513  12.646 160.705  1.00 47.57           C  
ATOM    741  CG  MET A 109       2.795  11.942 160.278  1.00 44.52           C  
ATOM    742  SD  MET A 109       3.552  12.880 158.959  1.00 45.59           S  
ATOM    743  CE  MET A 109       4.684  13.946 159.812  1.00 27.16           C  
ATOM    744  N   THR A 110      -0.205  14.199 162.715  1.00 46.00           N  
ATOM    745  CA  THR A 110      -1.458  14.759 163.209  1.00 47.16           C  
ATOM    746  C   THR A 110      -1.373  16.259 163.584  1.00 47.67           C  
ATOM    747  O   THR A 110      -2.192  17.061 163.143  1.00 47.29           O  
ATOM    748  CB  THR A 110      -1.959  13.940 164.426  1.00 47.83           C  
ATOM    749  OG1 THR A 110      -2.413  12.654 163.984  1.00 46.23           O  
ATOM    750  CG2 THR A 110      -3.094  14.660 165.126  1.00 45.79           C  
ATOM    751  N   ASN A 111      -0.397  16.624 164.412  1.00 51.06           N  
ATOM    752  CA  ASN A 111      -0.156  18.037 164.738  1.00 54.64           C  
ATOM    753  C   ASN A 111      -0.106  18.889 163.475  1.00 55.34           C  
ATOM    754  O   ASN A 111      -0.389  20.080 163.506  1.00 55.82           O  
ATOM    755  CB  ASN A 111       1.144  18.209 165.540  1.00 56.76           C  
ATOM    756  CG  ASN A 111       1.023  17.701 166.991  1.00 59.79           C  
ATOM    757  OD1 ASN A 111      -0.082  17.501 167.507  1.00 58.99           O  
ATOM    758  ND2 ASN A 111       2.171  17.495 167.646  1.00 60.57           N  
ATOM    759  N   LEU A 112       0.260  18.264 162.360  1.00 57.32           N  
ATOM    760  CA  LEU A 112       0.304  18.942 161.063  1.00 58.61           C  
ATOM    761  C   LEU A 112      -1.036  18.859 160.322  1.00 61.87           C  
ATOM    762  O   LEU A 112      -1.250  19.563 159.338  1.00 65.33           O  
ATOM    763  CB  LEU A 112       1.403  18.350 160.181  1.00 52.82           C  
ATOM    764  CG  LEU A 112       2.815  18.366 160.739  1.00 49.92           C  
ATOM    765  CD1 LEU A 112       3.727  17.592 159.844  1.00 47.14           C  
ATOM    766  CD2 LEU A 112       3.324  19.786 160.921  1.00 48.86           C  
ATOM    767  N   GLY A 113      -1.919  17.976 160.774  1.00 64.67           N  
ATOM    768  CA  GLY A 113      -3.235  17.848 160.172  1.00 66.92           C  
ATOM    769  C   GLY A 113      -3.453  16.580 159.361  1.00 69.05           C  
ATOM    770  O   GLY A 113      -4.599  16.250 159.041  1.00 69.17           O  
ATOM    771  N   GLU A 114      -2.370  15.865 159.022  1.00 69.29           N  
ATOM    772  CA  GLU A 114      -2.488  14.631 158.214  1.00 69.61           C  
ATOM    773  C   GLU A 114      -2.864  13.391 159.063  1.00 69.91           C  
ATOM    774  O   GLU A 114      -2.004  12.800 159.738  1.00 72.40           O  
ATOM    775  CB  GLU A 114      -1.217  14.386 157.383  1.00 66.31           C  
ATOM    776  N   LYS A 115      -4.153  13.025 159.034  1.00 68.49           N  
ATOM    777  CA  LYS A 115      -4.683  11.873 159.785  1.00 67.68           C  
ATOM    778  C   LYS A 115      -4.505  10.594 158.969  1.00 68.28           C  
ATOM    779  O   LYS A 115      -5.344  10.256 158.138  1.00 66.97           O  
ATOM    780  N   LEU A 116      -3.415   9.876 159.260  1.00 70.38           N  
ATOM    781  CA  LEU A 116      -2.821   8.856 158.362  1.00 71.20           C  
ATOM    782  C   LEU A 116      -3.305   7.426 158.627  1.00 69.47           C  
ATOM    783  O   LEU A 116      -3.643   7.077 159.764  1.00 71.36           O  
ATOM    784  CB  LEU A 116      -1.271   8.891 158.465  1.00 68.52           C  
ATOM    785  N   THR A 117      -3.314   6.603 157.576  1.00 65.04           N  
ATOM    786  CA  THR A 117      -3.429   5.164 157.742  1.00 61.61           C  
ATOM    787  C   THR A 117      -2.247   4.718 158.579  1.00 64.14           C  
ATOM    788  O   THR A 117      -1.147   5.264 158.447  1.00 65.75           O  
ATOM    789  CB  THR A 117      -3.376   4.450 156.387  1.00 60.03           C  
ATOM    790  OG1 THR A 117      -2.272   4.944 155.626  1.00 54.21           O  
ATOM    791  CG2 THR A 117      -4.647   4.723 155.600  1.00 61.44           C  
ATOM    792  N   ASP A 118      -2.459   3.773 159.483  1.00 63.37           N  
ATOM    793  CA  ASP A 118      -1.331   3.298 160.284  1.00 59.84           C  
ATOM    794  C   ASP A 118      -0.266   2.698 159.401  1.00 55.98           C  
ATOM    795  O   ASP A 118       0.933   2.779 159.705  1.00 57.23           O  
ATOM    796  CB  ASP A 118      -1.792   2.262 161.309  1.00 61.16           C  
ATOM    797  CG  ASP A 118      -2.385   2.915 162.646  1.00 62.11           C  
ATOM    798  OD1 ASP A 118      -2.934   4.067 162.662  1.00 58.47           O  
ATOM    799  OD2 ASP A 118      -2.305   2.210 163.686  1.00 64.24           O  
ATOM    800  N   GLU A 119      -0.720   2.103 158.305  1.00 53.24           N  
ATOM    801  CA  GLU A 119       0.145   1.401 157.379  1.00 52.52           C  
ATOM    802  C   GLU A 119       1.094   2.389 156.724  1.00 51.69           C  
ATOM    803  O   GLU A 119       2.278   2.086 156.505  1.00 51.04           O  
ATOM    804  CB  GLU A 119      -0.686   0.660 156.326  1.00 52.82           C  
ATOM    805  N   GLU A 120       0.583   3.586 156.441  1.00 51.01           N  
ATOM    806  CA  GLU A 120       1.417   4.673 155.907  1.00 52.53           C  
ATOM    807  C   GLU A 120       2.463   5.093 156.929  1.00 53.49           C  
ATOM    808  O   GLU A 120       3.627   5.338 156.593  1.00 54.00           O  
ATOM    809  CB  GLU A 120       0.577   5.884 155.534  1.00 49.79           C  
ATOM    810  N   VAL A 121       2.052   5.169 158.186  1.00 50.66           N  
ATOM    811  CA  VAL A 121       2.992   5.524 159.226  1.00 48.89           C  
ATOM    812  C   VAL A 121       4.095   4.456 159.380  1.00 48.30           C  
ATOM    813  O   VAL A 121       5.279   4.771 159.586  1.00 40.84           O  
ATOM    814  CB  VAL A 121       2.303   5.761 160.586  1.00 48.40           C  
ATOM    815  CG1 VAL A 121       3.357   6.215 161.624  1.00 46.75           C  
ATOM    816  CG2 VAL A 121       1.147   6.782 160.450  1.00 46.31           C  
ATOM    817  N   ASP A 122       3.707   3.194 159.286  1.00 46.11           N  
ATOM    818  CA  ASP A 122       4.701   2.153 159.379  1.00 44.96           C  
ATOM    819  C   ASP A 122       5.624   2.173 158.164  1.00 43.09           C  
ATOM    820  O   ASP A 122       6.839   2.114 158.296  1.00 43.30           O  
ATOM    821  CB  ASP A 122       4.008   0.823 159.540  1.00 47.36           C  
ATOM    822  CG  ASP A 122       3.076   0.828 160.700  1.00 47.07           C  
ATOM    823  OD1 ASP A 122       3.555   1.060 161.832  1.00 50.83           O  
ATOM    824  OD2 ASP A 122       1.872   0.657 160.489  1.00 48.73           O  
ATOM    825  N   GLU A 123       5.049   2.270 156.974  1.00 41.39           N  
ATOM    826  CA  GLU A 123       5.868   2.437 155.785  1.00 39.34           C  
ATOM    827  C   GLU A 123       6.801   3.650 155.952  1.00 36.73           C  
ATOM    828  O   GLU A 123       7.973   3.571 155.574  1.00 39.31           O  
ATOM    829  CB  GLU A 123       5.015   2.535 154.493  1.00 38.43           C  
ATOM    830  N   MET A 124       6.307   4.751 156.538  1.00 32.23           N  
ATOM    831  CA  MET A 124       7.170   5.939 156.765  1.00 32.25           C  
ATOM    832  C   MET A 124       8.374   5.542 157.571  1.00 33.16           C  
ATOM    833  O   MET A 124       9.512   5.869 157.210  1.00 34.97           O  
ATOM    834  CB  MET A 124       6.433   7.096 157.457  1.00 29.44           C  
ATOM    835  CG  MET A 124       5.470   7.879 156.534  1.00 27.06           C  
ATOM    836  SD  MET A 124       4.611   9.226 157.369  1.00 26.39           S  
ATOM    837  CE  MET A 124       5.921  10.386 157.659  1.00 26.55           C  
ATOM    838  N   ILE A 125       8.117   4.794 158.643  1.00 35.10           N  
ATOM    839  CA  ILE A 125       9.165   4.272 159.499  1.00 35.61           C  
ATOM    840  C   ILE A 125      10.009   3.284 158.724  1.00 37.59           C  
ATOM    841  O   ILE A 125      11.259   3.377 158.726  1.00 36.40           O  
ATOM    842  CB  ILE A 125       8.583   3.547 160.739  1.00 36.29           C  
ATOM    843  CG1 ILE A 125       7.898   4.550 161.663  1.00 35.73           C  
ATOM    844  CG2 ILE A 125       9.692   2.838 161.505  1.00 34.12           C  
ATOM    845  CD1 ILE A 125       8.892   5.360 162.482  1.00 39.84           C  
ATOM    846  N   ARG A 126       9.331   2.341 158.067  1.00 34.18           N  
ATOM    847  CA  ARG A 126      10.009   1.310 157.304  1.00 36.48           C  
ATOM    848  C   ARG A 126      10.922   1.961 156.269  1.00 39.73           C  
ATOM    849  O   ARG A 126      11.946   1.407 155.927  1.00 43.09           O  
ATOM    850  CB  ARG A 126       8.993   0.375 156.629  1.00 36.84           C  
ATOM    851  CG  ARG A 126       9.580  -0.724 155.735  1.00 35.26           C  
ATOM    852  N   GLU A 127      10.569   3.148 155.785  1.00 40.20           N  
ATOM    853  CA  GLU A 127      11.360   3.765 154.708  1.00 40.65           C  
ATOM    854  C   GLU A 127      12.560   4.500 155.234  1.00 38.88           C  
ATOM    855  O   GLU A 127      13.583   4.521 154.599  1.00 44.63           O  
ATOM    856  CB  GLU A 127      10.518   4.706 153.843  1.00 44.80           C  
ATOM    857  CG  GLU A 127      10.046   4.113 152.509  1.00 48.17           C  
ATOM    858  CD  GLU A 127       8.692   4.676 152.073  1.00 53.20           C  
ATOM    859  OE1 GLU A 127       8.400   5.863 152.397  1.00 54.95           O  
ATOM    860  OE2 GLU A 127       7.905   3.928 151.423  1.00 53.38           O  
ATOM    861  N   ALA A 128      12.453   5.087 156.412  1.00 38.70           N  
ATOM    862  CA  ALA A 128      13.599   5.783 157.000  1.00 34.46           C  
ATOM    863  C   ALA A 128      14.470   4.878 157.868  1.00 33.03           C  
ATOM    864  O   ALA A 128      15.533   5.288 158.286  1.00 29.56           O  
ATOM    865  CB  ALA A 128      13.130   6.975 157.810  1.00 32.67           C  
ATOM    866  N   ASP A 129      14.007   3.664 158.153  1.00 32.83           N  
ATOM    867  CA  ASP A 129      14.718   2.795 159.082  1.00 35.24           C  
ATOM    868  C   ASP A 129      15.883   2.114 158.396  1.00 37.27           C  
ATOM    869  O   ASP A 129      15.703   1.132 157.700  1.00 43.98           O  
ATOM    870  CB  ASP A 129      13.771   1.759 159.702  1.00 33.16           C  
ATOM    871  CG  ASP A 129      14.462   0.847 160.703  1.00 32.41           C  
ATOM    872  OD1 ASP A 129      15.557   1.193 161.221  1.00 32.96           O  
ATOM    873  OD2 ASP A 129      13.892  -0.225 160.987  1.00 29.62           O  
ATOM    874  N   ILE A 130      17.089   2.622 158.618  1.00 38.78           N  
ATOM    875  CA  ILE A 130      18.269   2.032 158.004  1.00 38.07           C  
ATOM    876  C   ILE A 130      18.742   0.726 158.646  1.00 37.88           C  
ATOM    877  O   ILE A 130      18.916  -0.281 157.946  1.00 38.81           O  
ATOM    878  CB  ILE A 130      19.391   3.030 157.899  1.00 37.11           C  
ATOM    879  CG1 ILE A 130      18.950   4.149 156.945  1.00 38.90           C  
ATOM    880  CG2 ILE A 130      20.578   2.374 157.323  1.00 36.30           C  
ATOM    881  CD1 ILE A 130      19.629   5.480 157.201  1.00 39.63           C  
ATOM    882  N   ASP A 131      18.911   0.727 159.967  1.00 36.17           N  
ATOM    883  CA  ASP A 131      19.419  -0.449 160.683  1.00 34.54           C  
ATOM    884  C   ASP A 131      18.343  -1.484 160.979  1.00 39.07           C  
ATOM    885  O   ASP A 131      18.633  -2.528 161.569  1.00 39.93           O  
ATOM    886  CB  ASP A 131      20.007  -0.016 161.997  1.00 33.06           C  
ATOM    887  CG  ASP A 131      18.992   0.661 162.889  1.00 38.54           C  
ATOM    888  OD1 ASP A 131      17.719   0.477 162.721  1.00 39.24           O  
ATOM    889  OD2 ASP A 131      19.460   1.366 163.799  1.00 38.30           O  
ATOM    890  N   GLY A 132      17.086  -1.160 160.656  1.00 42.18           N  
ATOM    891  CA  GLY A 132      16.014  -2.156 160.680  1.00 39.94           C  
ATOM    892  C   GLY A 132      15.469  -2.501 162.043  1.00 41.30           C  
ATOM    893  O   GLY A 132      14.881  -3.569 162.218  1.00 42.21           O  
ATOM    894  N   ASP A 133      15.627  -1.604 163.017  1.00 40.00           N  
ATOM    895  CA  ASP A 133      15.140  -1.912 164.383  1.00 37.93           C  
ATOM    896  C   ASP A 133      13.701  -1.451 164.655  1.00 40.56           C  
ATOM    897  O   ASP A 133      13.163  -1.686 165.752  1.00 47.75           O  
ATOM    898  CB  ASP A 133      16.072  -1.354 165.450  1.00 31.64           C  
ATOM    899  CG  ASP A 133      16.057   0.157 165.485  1.00 34.27           C  
ATOM    900  OD1 ASP A 133      15.384   0.770 164.616  1.00 34.43           O  
ATOM    901  OD2 ASP A 133      16.700   0.739 166.377  1.00 32.27           O  
ATOM    902  N   GLY A 134      13.060  -0.839 163.667  1.00 38.95           N  
ATOM    903  CA  GLY A 134      11.629  -0.540 163.775  1.00 32.57           C  
ATOM    904  C   GLY A 134      11.458   0.915 164.101  1.00 34.48           C  
ATOM    905  O   GLY A 134      10.361   1.462 164.060  1.00 34.12           O  
ATOM    906  N   GLN A 135      12.555   1.560 164.432  1.00 33.26           N  
ATOM    907  CA  GLN A 135      12.455   2.917 164.912  1.00 35.86           C  
ATOM    908  C   GLN A 135      13.380   3.787 164.058  1.00 38.27           C  
ATOM    909  O   GLN A 135      14.207   3.265 163.298  1.00 39.82           O  
ATOM    910  CB  GLN A 135      12.856   2.962 166.409  1.00 38.52           C  
ATOM    911  CG  GLN A 135      11.739   2.660 167.375  1.00 36.40           C  
ATOM    912  CD  GLN A 135      12.206   2.538 168.808  1.00 36.87           C  
ATOM    913  OE1 GLN A 135      13.349   2.227 169.074  1.00 42.68           O  
ATOM    914  NE2 GLN A 135      11.310   2.771 169.737  1.00 40.15           N  
ATOM    915  N   VAL A 136      13.241   5.110 164.163  1.00 39.08           N  
ATOM    916  CA  VAL A 136      14.184   6.029 163.503  1.00 36.28           C  
ATOM    917  C   VAL A 136      15.042   6.769 164.542  1.00 40.33           C  
ATOM    918  O   VAL A 136      14.535   7.514 165.409  1.00 44.39           O  
ATOM    919  CB  VAL A 136      13.450   7.044 162.693  1.00 31.80           C  
ATOM    920  CG1 VAL A 136      14.437   8.000 162.013  1.00 24.89           C  
ATOM    921  CG2 VAL A 136      12.570   6.335 161.704  1.00 28.41           C  
ATOM    922  N   ASN A 137      16.338   6.568 164.468  1.00 38.36           N  
ATOM    923  CA  ASN A 137      17.213   7.242 165.387  1.00 39.04           C  
ATOM    924  C   ASN A 137      17.723   8.524 164.738  1.00 41.17           C  
ATOM    925  O   ASN A 137      17.355   8.866 163.600  1.00 43.48           O  
ATOM    926  CB  ASN A 137      18.373   6.339 165.752  1.00 33.01           C  
ATOM    927  CG  ASN A 137      19.286   6.106 164.585  1.00 38.16           C  
ATOM    928  OD1 ASN A 137      19.159   6.764 163.529  1.00 42.85           O  
ATOM    929  ND2 ASN A 137      20.209   5.184 164.738  1.00 33.99           N  
ATOM    930  N   TYR A 138      18.599   9.224 165.444  1.00 41.98           N  
ATOM    931  CA  TYR A 138      19.005  10.542 164.995  1.00 40.61           C  
ATOM    932  C   TYR A 138      19.542  10.532 163.560  1.00 41.33           C  
ATOM    933  O   TYR A 138      19.025  11.227 162.699  1.00 38.91           O  
ATOM    934  CB  TYR A 138      20.006  11.152 165.946  1.00 42.45           C  
ATOM    935  CG  TYR A 138      20.433  12.497 165.500  1.00 44.27           C  
ATOM    936  CD1 TYR A 138      19.513  13.528 165.407  1.00 46.56           C  
ATOM    937  CD2 TYR A 138      21.748  12.746 165.136  1.00 46.63           C  
ATOM    938  CE1 TYR A 138      19.875  14.780 164.976  1.00 46.58           C  
ATOM    939  CE2 TYR A 138      22.131  14.008 164.705  1.00 49.10           C  
ATOM    940  CZ  TYR A 138      21.177  15.022 164.637  1.00 48.81           C  
ATOM    941  OH  TYR A 138      21.531  16.277 164.210  1.00 53.70           O  
ATOM    942  N   GLU A 139      20.574   9.737 163.307  1.00 42.42           N  
ATOM    943  CA  GLU A 139      21.196   9.694 161.977  1.00 43.42           C  
ATOM    944  C   GLU A 139      20.162   9.343 160.922  1.00 44.60           C  
ATOM    945  O   GLU A 139      20.102   9.968 159.848  1.00 43.28           O  
ATOM    946  CB  GLU A 139      22.330   8.682 161.948  1.00 46.15           C  
ATOM    947  CG  GLU A 139      23.583   9.143 162.712  1.00 49.60           C  
ATOM    948  CD  GLU A 139      24.241  10.370 162.071  1.00 53.71           C  
ATOM    949  OE1 GLU A 139      24.068  10.573 160.831  1.00 55.29           O  
ATOM    950  OE2 GLU A 139      24.934  11.127 162.802  1.00 53.28           O  
ATOM    951  N   GLU A 140      19.324   8.354 161.228  1.00 44.21           N  
ATOM    952  CA  GLU A 140      18.381   7.899 160.233  1.00 41.76           C  
ATOM    953  C   GLU A 140      17.472   9.086 159.960  1.00 42.37           C  
ATOM    954  O   GLU A 140      17.143   9.402 158.795  1.00 42.54           O  
ATOM    955  CB  GLU A 140      17.604   6.678 160.727  1.00 39.55           C  
ATOM    956  CG  GLU A 140      18.458   5.491 160.992  1.00 35.01           C  
ATOM    957  CD  GLU A 140      17.716   4.364 161.686  1.00 36.63           C  
ATOM    958  OE1 GLU A 140      16.793   4.628 162.507  1.00 36.14           O  
ATOM    959  OE2 GLU A 140      18.059   3.190 161.427  1.00 35.79           O  
ATOM    960  N   PHE A 141      17.136   9.803 161.032  1.00 40.08           N  
ATOM    961  CA  PHE A 141      16.281  10.977 160.910  1.00 39.16           C  
ATOM    962  C   PHE A 141      16.951  12.001 160.007  1.00 41.21           C  
ATOM    963  O   PHE A 141      16.300  12.547 159.118  1.00 42.55           O  
ATOM    964  CB  PHE A 141      16.000  11.576 162.277  1.00 38.69           C  
ATOM    965  CG  PHE A 141      15.120  12.782 162.240  1.00 39.40           C  
ATOM    966  CD1 PHE A 141      13.747  12.652 162.013  1.00 39.89           C  
ATOM    967  CD2 PHE A 141      15.652  14.059 162.453  1.00 41.23           C  
ATOM    968  CE1 PHE A 141      12.918  13.768 161.979  1.00 38.17           C  
ATOM    969  CE2 PHE A 141      14.823  15.190 162.434  1.00 41.73           C  
ATOM    970  CZ  PHE A 141      13.451  15.040 162.187  1.00 40.07           C  
ATOM    971  N   VAL A 142      18.261  12.216 160.222  1.00 40.32           N  
ATOM    972  CA  VAL A 142      19.070  13.182 159.481  1.00 40.35           C  
ATOM    973  C   VAL A 142      18.972  12.915 157.970  1.00 45.08           C  
ATOM    974  O   VAL A 142      18.830  13.857 157.161  1.00 45.53           O  
ATOM    975  CB  VAL A 142      20.571  13.146 159.932  1.00 40.34           C  
ATOM    976  CG1 VAL A 142      21.418  14.102 159.089  1.00 36.18           C  
ATOM    977  CG2 VAL A 142      20.720  13.509 161.404  1.00 36.28           C  
ATOM    978  N   GLN A 143      18.984  11.632 157.599  1.00 45.44           N  
ATOM    979  CA  GLN A 143      18.866  11.259 156.189  1.00 44.93           C  
ATOM    980  C   GLN A 143      17.427  11.277 155.681  1.00 46.06           C  
ATOM    981  O   GLN A 143      17.171  11.713 154.561  1.00 46.19           O  
ATOM    982  CB  GLN A 143      19.525   9.915 155.923  1.00 41.10           C  
ATOM    983  CG  GLN A 143      20.819   9.804 156.618  1.00 40.05           C  
ATOM    984  CD  GLN A 143      21.604   8.603 156.180  1.00 39.68           C  
ATOM    985  OE1 GLN A 143      21.382   8.065 155.087  1.00 36.50           O  
ATOM    986  NE2 GLN A 143      22.548   8.171 157.025  1.00 37.06           N  
ATOM    987  N   MET A 144      16.499  10.785 156.491  1.00 46.46           N  
ATOM    988  CA  MET A 144      15.077  10.904 156.170  1.00 47.05           C  
ATOM    989  C   MET A 144      14.747  12.363 155.827  1.00 49.95           C  
ATOM    990  O   MET A 144      13.923  12.635 154.964  1.00 54.36           O  
ATOM    991  CB  MET A 144      14.231  10.433 157.371  1.00 42.01           C  
ATOM    992  CG  MET A 144      12.716  10.425 157.167  1.00 40.46           C  
ATOM    993  SD  MET A 144      11.864  10.324 158.773  1.00 33.17           S  
ATOM    994  CE  MET A 144      11.539  12.063 159.041  1.00 39.31           C  
ATOM    995  N   MET A 145      15.407  13.300 156.503  1.00 54.90           N  
ATOM    996  CA  MET A 145      15.034  14.728 156.423  1.00 57.59           C  
ATOM    997  C   MET A 145      15.801  15.484 155.362  1.00 61.17           C  
ATOM    998  O   MET A 145      15.266  16.380 154.734  1.00 66.67           O  
ATOM    999  CB  MET A 145      15.250  15.429 157.768  1.00 54.50           C  
ATOM   1000  CG  MET A 145      14.287  14.984 158.855  1.00 51.75           C  
ATOM   1001  SD  MET A 145      12.647  15.404 158.349  1.00 42.87           S  
ATOM   1002  CE  MET A 145      12.868  17.166 158.323  1.00 44.41           C  
ATOM   1003  N   THR A 146      17.066  15.148 155.183  1.00 66.87           N  
ATOM   1004  CA  THR A 146      17.915  15.855 154.223  1.00 71.22           C  
ATOM   1005  C   THR A 146      17.651  15.416 152.779  1.00 72.55           C  
ATOM   1006  O   THR A 146      18.423  14.650 152.201  1.00 73.75           O  
ATOM   1007  CB  THR A 146      19.397  15.664 154.557  1.00 72.16           C  
ATOM   1008  OG1 THR A 146      19.643  14.282 154.838  1.00 74.49           O  
ATOM   1009  CG2 THR A 146      19.768  16.479 155.779  1.00 71.54           C  
TER    1010      THR A 146                                                      
ATOM   1011  N   HIS B1961       4.951  10.312 152.331  1.00 86.54           N  
ATOM   1012  CA  HIS B1961       4.039  11.371 152.874  1.00 86.08           C  
ATOM   1013  C   HIS B1961       4.848  12.432 153.624  1.00 85.39           C  
ATOM   1014  O   HIS B1961       4.327  13.211 154.421  1.00 86.80           O  
ATOM   1015  CB  HIS B1961       2.960  10.748 153.761  1.00 86.65           C  
ATOM   1016  CG  HIS B1961       2.014   9.845 153.018  1.00 89.02           C  
ATOM   1017  ND1 HIS B1961       1.915   8.492 153.273  1.00 90.33           N  
ATOM   1018  CD2 HIS B1961       1.138  10.100 152.016  1.00 89.53           C  
ATOM   1019  CE1 HIS B1961       1.007   7.958 152.473  1.00 90.08           C  
ATOM   1020  NE2 HIS B1961       0.524   8.911 151.697  1.00 90.40           N  
ATOM   1021  N   MET B1962       6.136  12.459 153.334  1.00 83.11           N  
ATOM   1022  CA  MET B1962       7.052  13.350 154.004  1.00 80.28           C  
ATOM   1023  C   MET B1962       6.752  14.801 153.703  1.00 77.46           C  
ATOM   1024  O   MET B1962       7.443  15.714 154.198  1.00 75.44           O  
ATOM   1025  CB  MET B1962       8.480  13.026 153.553  1.00 81.67           C  
ATOM   1026  CG  MET B1962       9.002  11.700 154.060  1.00 82.87           C  
ATOM   1027  SD  MET B1962       9.023  11.688 155.856  1.00 83.35           S  
ATOM   1028  CE  MET B1962      10.106  13.094 156.204  1.00 84.64           C  
ATOM   1029  N   GLY B1963       5.755  15.020 152.853  1.00 74.08           N  
ATOM   1030  CA  GLY B1963       5.453  16.363 152.382  1.00 71.36           C  
ATOM   1031  C   GLY B1963       5.408  17.415 153.491  1.00 71.90           C  
ATOM   1032  O   GLY B1963       6.155  18.416 153.457  1.00 67.83           O  
ATOM   1033  N   LYS B1964       4.547  17.182 154.489  1.00 71.43           N  
ATOM   1034  CA  LYS B1964       4.234  18.203 155.498  1.00 72.05           C  
ATOM   1035  C   LYS B1964       5.413  18.591 156.441  1.00 73.53           C  
ATOM   1036  O   LYS B1964       5.627  19.793 156.744  1.00 73.24           O  
ATOM   1037  CB  LYS B1964       2.979  17.804 156.278  1.00 71.10           C  
ATOM   1038  CG  LYS B1964       1.666  18.147 155.571  1.00 71.34           C  
ATOM   1039  CD  LYS B1964       0.640  17.009 155.709  1.00 73.20           C  
ATOM   1040  CE  LYS B1964      -0.766  17.450 155.258  1.00 74.48           C  
ATOM   1041  NZ  LYS B1964      -1.715  16.297 155.106  1.00 74.02           N  
ATOM   1042  N   ILE B1965       6.179  17.586 156.881  1.00 71.12           N  
ATOM   1043  CA  ILE B1965       7.387  17.835 157.668  1.00 68.29           C  
ATOM   1044  C   ILE B1965       8.303  18.800 156.944  1.00 69.19           C  
ATOM   1045  O   ILE B1965       8.775  19.793 157.524  1.00 67.51           O  
ATOM   1046  CB  ILE B1965       8.212  16.570 157.862  1.00 67.89           C  
ATOM   1047  CG1 ILE B1965       7.390  15.456 158.508  1.00 64.79           C  
ATOM   1048  CG2 ILE B1965       9.453  16.890 158.653  1.00 65.42           C  
ATOM   1049  CD1 ILE B1965       7.563  14.102 157.775  1.00 67.43           C  
ATOM   1050  N   TYR B1966       8.606  18.478 155.687  1.00 69.39           N  
ATOM   1051  CA  TYR B1966       9.476  19.344 154.887  1.00 72.37           C  
ATOM   1052  C   TYR B1966       9.007  20.799 154.972  1.00 70.82           C  
ATOM   1053  O   TYR B1966       9.824  21.720 155.175  1.00 68.75           O  
ATOM   1054  CB  TYR B1966       9.515  18.899 153.421  1.00 77.55           C  
ATOM   1055  CG  TYR B1966      10.193  17.568 153.179  1.00 82.03           C  
ATOM   1056  CD1 TYR B1966       9.453  16.446 152.785  1.00 84.07           C  
ATOM   1057  CD2 TYR B1966      11.571  17.424 153.343  1.00 82.55           C  
ATOM   1058  CE1 TYR B1966      10.081  15.213 152.548  1.00 83.43           C  
ATOM   1059  CE2 TYR B1966      12.201  16.195 153.120  1.00 83.64           C  
ATOM   1060  CZ  TYR B1966      11.448  15.093 152.724  1.00 83.90           C  
ATOM   1061  OH  TYR B1966      12.064  13.876 152.501  1.00 83.55           O  
ATOM   1062  N   ALA B1967       7.693  20.996 154.808  1.00 66.55           N  
ATOM   1063  CA  ALA B1967       7.083  22.326 154.865  1.00 63.84           C  
ATOM   1064  C   ALA B1967       7.261  23.047 156.214  1.00 63.95           C  
ATOM   1065  O   ALA B1967       7.639  24.238 156.260  1.00 63.81           O  
ATOM   1066  CB  ALA B1967       5.634  22.227 154.531  1.00 66.75           C  
ATOM   1067  N   ALA B1968       6.970  22.349 157.309  1.00 60.04           N  
ATOM   1068  CA  ALA B1968       7.132  22.954 158.641  1.00 62.89           C  
ATOM   1069  C   ALA B1968       8.555  23.432 158.835  1.00 62.83           C  
ATOM   1070  O   ALA B1968       8.810  24.524 159.383  1.00 59.52           O  
ATOM   1071  CB  ALA B1968       6.779  21.956 159.727  1.00 63.72           C  
ATOM   1072  N   MET B1969       9.474  22.569 158.410  1.00 62.82           N  
ATOM   1073  CA  MET B1969      10.891  22.846 158.380  1.00 63.01           C  
ATOM   1074  C   MET B1969      11.237  24.085 157.594  1.00 64.42           C  
ATOM   1075  O   MET B1969      11.847  25.050 158.110  1.00 60.92           O  
ATOM   1076  CB  MET B1969      11.557  21.691 157.690  1.00 67.15           C  
ATOM   1077  CG  MET B1969      11.600  20.488 158.515  1.00 69.50           C  
ATOM   1078  SD  MET B1969      12.526  20.932 159.963  1.00 77.77           S  
ATOM   1079  CE  MET B1969      14.089  21.564 159.271  1.00 74.66           C  
ATOM   1080  N   MET B1970      10.894  24.037 156.314  1.00 64.54           N  
ATOM   1081  CA  MET B1970      11.142  25.153 155.455  1.00 66.46           C  
ATOM   1082  C   MET B1970      10.616  26.400 156.140  1.00 67.20           C  
ATOM   1083  O   MET B1970      11.371  27.342 156.403  1.00 61.46           O  
ATOM   1084  CB  MET B1970      10.436  24.957 154.125  1.00 70.50           C  
ATOM   1085  CG  MET B1970      10.350  26.217 153.281  1.00 75.38           C  
ATOM   1086  SD  MET B1970       8.858  26.210 152.281  1.00 81.49           S  
ATOM   1087  CE  MET B1970       7.675  26.902 153.379  1.00 79.76           C  
ATOM   1088  N   ILE B1971       9.310  26.409 156.432  1.00 68.25           N  
ATOM   1089  CA  ILE B1971       8.649  27.672 156.765  1.00 69.54           C  
ATOM   1090  C   ILE B1971       9.231  28.250 158.043  1.00 69.50           C  
ATOM   1091  O   ILE B1971       9.418  29.471 158.172  1.00 68.41           O  
ATOM   1092  CB  ILE B1971       7.112  27.553 156.829  1.00 68.11           C  
ATOM   1093  CG1 ILE B1971       6.490  28.943 156.732  1.00 68.41           C  
ATOM   1094  CG2 ILE B1971       6.663  26.865 158.105  1.00 71.95           C  
ATOM   1095  CD1 ILE B1971       6.874  29.705 155.487  1.00 64.37           C  
ATOM   1096  N   MET B1972       9.523  27.351 158.976  1.00 70.76           N  
ATOM   1097  CA  MET B1972      10.241  27.683 160.172  1.00 74.81           C  
ATOM   1098  C   MET B1972      11.515  28.439 159.807  1.00 77.44           C  
ATOM   1099  O   MET B1972      11.732  29.580 160.268  1.00 75.54           O  
ATOM   1100  CB  MET B1972      10.588  26.403 160.895  1.00 77.30           C  
ATOM   1101  CG  MET B1972       9.412  25.783 161.552  1.00 80.30           C  
ATOM   1102  SD  MET B1972       8.889  26.862 162.908  1.00 85.16           S  
ATOM   1103  CE  MET B1972      10.252  26.654 164.065  1.00 85.72           C  
ATOM   1104  N   GLU B1973      12.363  27.806 158.990  1.00 77.70           N  
ATOM   1105  CA  GLU B1973      13.551  28.495 158.480  1.00 81.97           C  
ATOM   1106  C   GLU B1973      13.107  29.830 157.883  1.00 80.77           C  
ATOM   1107  O   GLU B1973      13.609  30.891 158.265  1.00 81.30           O  
ATOM   1108  CB  GLU B1973      14.317  27.646 157.435  1.00 84.76           C  
ATOM   1109  CG  GLU B1973      14.966  26.375 157.985  1.00 88.87           C  
ATOM   1110  CD  GLU B1973      15.561  25.493 156.876  1.00 91.79           C  
ATOM   1111  OE1 GLU B1973      15.035  25.542 155.739  1.00 92.45           O  
ATOM   1112  OE2 GLU B1973      16.549  24.755 157.142  1.00 92.12           O  
ATOM   1113  N   TYR B1974      12.128  29.767 156.981  1.00 79.22           N  
ATOM   1114  CA  TYR B1974      11.584  30.965 156.345  1.00 78.40           C  
ATOM   1115  C   TYR B1974      11.269  32.106 157.296  1.00 77.42           C  
ATOM   1116  O   TYR B1974      11.625  33.258 157.039  1.00 77.42           O  
ATOM   1117  CB  TYR B1974      10.339  30.625 155.559  1.00 80.23           C  
ATOM   1118  CG  TYR B1974      10.586  30.603 154.088  1.00 81.48           C  
ATOM   1119  CD1 TYR B1974      10.591  31.787 153.338  1.00 81.91           C  
ATOM   1120  CD2 TYR B1974      10.845  29.407 153.438  1.00 82.26           C  
ATOM   1121  CE1 TYR B1974      10.832  31.766 151.974  1.00 81.50           C  
ATOM   1122  CE2 TYR B1974      11.086  29.372 152.079  1.00 83.14           C  
ATOM   1123  CZ  TYR B1974      11.077  30.550 151.349  1.00 81.69           C  
ATOM   1124  OH  TYR B1974      11.324  30.489 150.005  1.00 80.42           O  
ATOM   1125  N   TYR B1975      10.568  31.786 158.375  1.00 73.52           N  
ATOM   1126  CA  TYR B1975      10.134  32.789 159.317  1.00 72.70           C  
ATOM   1127  C   TYR B1975      11.302  33.536 159.985  1.00 76.10           C  
ATOM   1128  O   TYR B1975      11.341  34.773 159.978  1.00 74.39           O  
ATOM   1129  CB  TYR B1975       9.225  32.135 160.351  1.00 72.77           C  
ATOM   1130  CG  TYR B1975       8.915  32.958 161.595  1.00 70.37           C  
ATOM   1131  CD1 TYR B1975       8.266  34.199 161.515  1.00 70.87           C  
ATOM   1132  CD2 TYR B1975       9.170  32.445 162.859  1.00 69.10           C  
ATOM   1133  CE1 TYR B1975       7.970  34.936 162.666  1.00 71.17           C  
ATOM   1134  CE2 TYR B1975       8.882  33.176 164.007  1.00 71.07           C  
ATOM   1135  CZ  TYR B1975       8.274  34.413 163.906  1.00 71.95           C  
ATOM   1136  OH  TYR B1975       7.970  35.125 165.055  1.00 75.26           O  
ATOM   1137  N   ARG B1976      12.266  32.786 160.533  1.00 79.96           N  
ATOM   1138  CA  ARG B1976      13.549  33.361 160.997  1.00 80.68           C  
ATOM   1139  C   ARG B1976      14.309  33.953 159.810  1.00 81.06           C  
ATOM   1140  O   ARG B1976      14.708  35.136 159.820  1.00 80.51           O  
ATOM   1141  CB  ARG B1976      14.407  32.288 161.687  1.00 79.28           C  
ATOM   1142  N   GLN B1977      14.479  33.129 158.776  1.00 81.59           N  
ATOM   1143  CA  GLN B1977      15.178  33.521 157.541  1.00 82.51           C  
ATOM   1144  C   GLN B1977      14.543  34.715 156.818  1.00 83.54           C  
ATOM   1145  O   GLN B1977      15.186  35.335 155.973  1.00 81.02           O  
ATOM   1146  CB  GLN B1977      15.288  32.324 156.580  1.00 82.76           C  
ATOM   1147  N   SER B1978      13.265  35.001 157.089  1.00 86.46           N  
ATOM   1148  CA  SER B1978      12.632  36.218 156.557  1.00 86.90           C  
ATOM   1149  C   SER B1978      12.773  37.332 157.572  1.00 87.64           C  
ATOM   1150  O   SER B1978      12.979  38.496 157.229  1.00 87.96           O  
ATOM   1151  CB  SER B1978      11.150  35.995 156.256  1.00 85.61           C  
ATOM   1152  N   LYS B1979      12.689  36.949 158.837  1.00 88.77           N  
ATOM   1153  CA  LYS B1979      12.756  37.882 159.945  1.00 89.37           C  
ATOM   1154  C   LYS B1979      14.201  38.346 160.233  1.00 89.55           C  
ATOM   1155  O   LYS B1979      14.426  39.158 161.142  1.00 92.00           O  
ATOM   1156  CB  LYS B1979      12.140  37.241 161.193  1.00 87.78           C  
ATOM   1157  CG  LYS B1979      12.621  37.793 162.514  1.00 86.50           C  
ATOM   1158  CD  LYS B1979      12.111  36.769 163.664  1.00 88.21           C  
ATOM   1159  CE  LYS B1979      12.493  37.421 164.987  1.00 88.75           C  
ATOM   1160  NZ  LYS B1979      11.707  36.961 166.089  1.00 90.80           N  
ATOM   1161  N   ALA B1980      15.165  37.840 159.469  1.00 87.49           N  
ATOM   1162  CA  ALA B1980      16.486  38.475 159.393  1.00 87.99           C  
ATOM   1163  C   ALA B1980      16.400  39.596 158.373  1.00 88.07           C  
ATOM   1164  O   ALA B1980      17.424  40.106 157.889  1.00 86.48           O  
ATOM   1165  CB  ALA B1980      17.578  37.471 158.999  1.00 86.48           C  
ATOM   1166  N   LYS B1981      15.151  39.944 158.042  1.00 87.85           N  
ATOM   1167  CA  LYS B1981      14.823  41.097 157.194  1.00 88.27           C  
ATOM   1168  C   LYS B1981      14.176  42.213 158.037  1.00 87.84           C  
ATOM   1169  O   LYS B1981      13.768  43.253 157.503  1.00 86.97           O  
ATOM   1170  CB  LYS B1981      13.901  40.680 156.039  1.00 87.54           C  
ATOM   1171  N   LYS B1982      14.081  41.962 159.354  1.00 87.92           N  
ATOM   1172  CA  LYS B1982      13.782  43.006 160.373  1.00 87.09           C  
ATOM   1173  C   LYS B1982      14.717  42.916 161.603  1.00 84.10           C  
ATOM   1174  O   LYS B1982      14.744  43.827 162.442  1.00 78.92           O  
ATOM   1175  CB  LYS B1982      12.308  42.948 160.819  1.00 85.75           C  
TER    1176      LYS B1982                                                      
HETATM 1177 CA    CA A 501      -5.928  29.180 150.470  1.00 64.75          CA  
HETATM 1178 CA    CA A 502       1.253  35.039 143.855  1.00 76.06          CA  
HETATM 1179 CA    CA A 503      11.246   8.044 171.515  1.00 50.28          CA  
HETATM 1180 CA    CA A 504      16.428   2.320 163.065  1.00 39.14          CA  
HETATM 1181  O   HOH A 505      -5.656  21.757 153.676  1.00 65.12           O  
HETATM 1182  O   HOH A 506     -10.593  28.513 143.499  1.00 51.37           O  
HETATM 1183  O   HOH A 507       6.868  43.159 162.651  1.00 61.52           O  
HETATM 1184  O   HOH A 508       5.217   3.068 167.873  1.00 56.66           O  
HETATM 1185  O   HOH A 509      14.222  10.789 178.831  1.00 41.46           O  
HETATM 1186  O   HOH A 510      10.721   3.882 172.012  1.00 43.90           O  
HETATM 1187  O   HOH A 511       6.850   4.577 171.667  1.00 41.77           O  
HETATM 1188  O   HOH A 512       8.050   2.680 166.319  1.00 45.11           O  
HETATM 1189  O   HOH A 513      17.564   3.187 164.856  1.00 38.24           O  
HETATM 1190  O   HOH A 514      16.686   7.465 157.082  1.00 45.28           O  
CONECT  119 1177                                                                
CONECT  132 1177                                                                
CONECT  145 1177                                                                
CONECT  153 1177                                                                
CONECT  195 1177                                                                
CONECT  196 1177                                                                
CONECT  383 1178                                                                
CONECT  395 1178                                                                
CONECT  407 1178                                                                
CONECT  416 1178                                                                
CONECT  461 1178                                                                
CONECT  462 1178                                                                
CONECT  627 1179                                                                
CONECT  640 1179                                                                
CONECT  652 1179                                                                
CONECT  661 1179                                                                
CONECT  701 1179                                                                
CONECT  702 1179                                                                
CONECT  872 1180                                                                
CONECT  888 1180                                                                
CONECT  900 1180                                                                
CONECT  909 1180                                                                
CONECT  958 1180                                                                
CONECT  959 1180                                                                
CONECT 1177  119  132  145  153                                                 
CONECT 1177  195  196                                                           
CONECT 1178  383  395  407  416                                                 
CONECT 1178  461  462                                                           
CONECT 1179  627  640  652  661                                                 
CONECT 1179  701  702                                                           
CONECT 1180  872  888  900  909                                                 
CONECT 1180  958  959 1189                                                      
CONECT 1189 1180                                                                
MASTER      470    0    4    9    4    0    8    6 1188    2   33   14          
END

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Related entries of code: 3dvm

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
1qur	RCSB PDB PDBbind	22-mer
1smf	RCSB PDB PDBbind	22-mer
3kj1	RCSB PDB PDBbind	22-mer
3kj2	RCSB PDB PDBbind	22-mer
3o34	RCSB PDB PDBbind	22-mer

Entry Information

PDB ID	3dvm
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	Ca2+/CaM, Calmodulin
Ligand Name	22-mer
EC.Number	E.C.-.-.-.-
Resolution	2.6(Å)
Affinity (Kd/Ki/IC50)	Kd=4.32nM
Release Year	2008
Protein/NA Sequence	Check fasta file
Primary Reference	(2008) Structure Vol. 16: pp. 1455-1467

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): P27884 P0DP23
Entrez Gene ID	NCBI Entrez Gene ID: 100009265 801 805 808
ASD	Information of known allosteric effects of PDB entries

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