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Database: PDB
Entry: 6HP3
LinkDB: 6HP3
Original site: 6HP3 
HEADER    DNA BINDING PROTEIN                     19-SEP-18   6HP3              
TITLE     ARBITRIUM PEPTIDE RECEPTOR FROM SPBETA PHAGE                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SPBC2 PROPHAGE-DERIVED UNCHARACTERIZED PROTEIN YOPK;       
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;     
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 GENE: YOPK, BSU20860;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693                                      
KEYWDS    ARBITRIUM PEPTIDE RECEPTOR, SPBETA PHAGE, DNA BINDING PROTEIN         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.MARINA,F.GALLEGO DEL SOL                                            
REVDAT   3   17-APR-19 6HP3    1       JRNL                                     
REVDAT   2   20-FEB-19 6HP3    1       JRNL                                     
REVDAT   1   13-FEB-19 6HP3    0                                                
JRNL        AUTH   F.GALLEGO DEL SOL,J.R.PENADES,A.MARINA                       
JRNL        TITL   DECIPHERING THE MOLECULAR MECHANISM UNDERPINNING PHAGE       
JRNL        TITL 2 ARBITRIUM COMMUNICATION SYSTEMS.                             
JRNL        REF    MOL.CELL                      V.  74    59 2019              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   30745087                                                     
JRNL        DOI    10.1016/J.MOLCEL.2019.01.025                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 125.60                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 96094                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4902                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7109                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3410                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 328                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 25464                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 211                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.69000                                              
REMARK   3    B22 (A**2) : -3.26000                                             
REMARK   3    B33 (A**2) : -0.42000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.35000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.354         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.322         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.162        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 25926 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 34881 ; 2.168 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3082 ; 5.157 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1328 ;41.776 ;25.482       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4712 ;22.128 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   104 ;31.429 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3833 ; 0.186 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19308 ; 0.010 ; 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): 12346 ; 3.519 ; 5.249       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15419 ; 5.504 ; 7.867       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13580 ; 4.486 ; 5.438       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 38681 ; 9.144 ;69.958       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 28                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    386       B     1    386   26320  0.08  0.05     
REMARK   3    2     A     1    386       C     1    386   26212  0.08  0.05     
REMARK   3    3     A     1    386       D     1    386   26204  0.08  0.05     
REMARK   3    4     A     1    386       E     1    386   26156  0.08  0.05     
REMARK   3    5     A     1    386       F     1    386   26172  0.08  0.05     
REMARK   3    6     A     1    386       G     1    386   26182  0.08  0.05     
REMARK   3    7     A     1    386       H     1    386   25952  0.09  0.05     
REMARK   3    8     B     1    386       C     1    386   26194  0.08  0.05     
REMARK   3    9     B     1    386       D     1    386   26338  0.08  0.05     
REMARK   3   10     B     1    386       E     1    386   26180  0.08  0.05     
REMARK   3   11     B     1    386       F     1    386   26170  0.08  0.05     
REMARK   3   12     B     1    386       G     1    386   26208  0.08  0.05     
REMARK   3   13     B     1    386       H     1    386   25860  0.09  0.05     
REMARK   3   14     C     1    386       D     1    386   26202  0.08  0.05     
REMARK   3   15     C     1    386       E     1    386   25944  0.08  0.05     
REMARK   3   16     C     1    386       F     1    386   26096  0.08  0.05     
REMARK   3   17     C     1    386       G     1    386   26196  0.08  0.05     
REMARK   3   18     C     1    386       H     1    386   25904  0.09  0.05     
REMARK   3   19     D     1    386       E     1    386   26262  0.07  0.05     
REMARK   3   20     D     1    386       F     1    386   26180  0.08  0.05     
REMARK   3   21     D     1    386       G     1    386   26272  0.08  0.05     
REMARK   3   22     D     1    386       H     1    386   25654  0.09  0.05     
REMARK   3   23     E     1    386       F     1    386   26184  0.07  0.05     
REMARK   3   24     E     1    386       G     1    386   26238  0.08  0.05     
REMARK   3   25     E     1    386       H     1    386   25670  0.09  0.05     
REMARK   3   26     F     1    386       G     1    386   26096  0.08  0.05     
REMARK   3   27     F     1    386       H     1    386   25828  0.09  0.05     
REMARK   3   28     G     1    386       H     1    386   25762  0.09  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
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     1        A   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.1170  36.3406 -26.7298              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1307 T22:   0.0595                                     
REMARK   3      T33:   0.0879 T12:   0.0302                                     
REMARK   3      T13:  -0.0388 T23:   0.0428                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4403 L22:   0.3654                                     
REMARK   3      L33:   0.2795 L12:  -0.0542                                     
REMARK   3      L13:   0.0760 L23:   0.2885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0330 S12:  -0.0266 S13:   0.0094                       
REMARK   3      S21:  -0.0098 S22:   0.0122 S23:   0.0437                       
REMARK   3      S31:   0.0325 S32:   0.0219 S33:   0.0208                       
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 :   B     1        B   386                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.0831  71.6666 -14.3988              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0629 T22:   0.1045                                     
REMARK   3      T33:   0.0594 T12:   0.0294                                     
REMARK   3      T13:  -0.0163 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2727 L22:   0.5940                                     
REMARK   3      L33:   0.2140 L12:  -0.5077                                     
REMARK   3      L13:  -0.2163 L23:   0.3407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1185 S12:   0.0576 S13:  -0.0898                       
REMARK   3      S21:   0.0807 S22:   0.0956 S23:   0.0429                       
REMARK   3      S31:   0.0329 S32:   0.0357 S33:   0.0229                       
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 :   C     1        C   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5692 -26.5415  -9.3689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1312 T22:   0.0285                                     
REMARK   3      T33:   0.0797 T12:  -0.0036                                     
REMARK   3      T13:   0.0056 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4487 L22:   1.0274                                     
REMARK   3      L33:   1.0999 L12:  -0.6163                                     
REMARK   3      L13:  -0.2503 L23:   0.6310                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0670 S12:   0.0217 S13:   0.0079                       
REMARK   3      S21:  -0.0395 S22:   0.0054 S23:  -0.0946                       
REMARK   3      S31:  -0.0711 S32:   0.0081 S33:  -0.0724                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.8225  10.2233 -25.0684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1180 T22:   0.0848                                     
REMARK   3      T33:   0.0652 T12:   0.0493                                     
REMARK   3      T13:   0.0149 T23:   0.0495                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3622 L22:   0.5160                                     
REMARK   3      L33:   1.0035 L12:  -0.4189                                     
REMARK   3      L13:  -0.3319 L23:   0.2894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0625 S12:   0.0506 S13:   0.0457                       
REMARK   3      S21:  -0.0241 S22:  -0.0300 S23:  -0.0537                       
REMARK   3      S31:   0.0016 S32:  -0.0434 S33:  -0.0325                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7721 -12.6969 -58.9090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1929 T22:   0.0707                                     
REMARK   3      T33:   0.0508 T12:   0.0738                                     
REMARK   3      T13:   0.0564 T23:   0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5341 L22:   0.1739                                     
REMARK   3      L33:   0.2243 L12:   0.0216                                     
REMARK   3      L13:  -0.2846 L23:   0.0112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0296 S12:  -0.0300 S13:  -0.0421                       
REMARK   3      S21:  -0.0238 S22:  -0.0708 S23:   0.0365                       
REMARK   3      S31:   0.0266 S32:   0.0509 S33:   0.0413                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   386                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1160  26.3907 -70.8180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2199 T22:   0.0127                                     
REMARK   3      T33:   0.0768 T12:   0.0450                                     
REMARK   3      T13:   0.0237 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6631 L22:   0.9239                                     
REMARK   3      L33:   0.0824 L12:  -0.0337                                     
REMARK   3      L13:   0.1919 L23:  -0.0790                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0029 S12:   0.0196 S13:   0.1059                       
REMARK   3      S21:  -0.1893 S22:  -0.0747 S23:  -0.0951                       
REMARK   3      S31:   0.0433 S32:   0.0180 S33:   0.0775                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     1        G   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9341  50.9464 -75.7946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1507 T22:   0.0806                                     
REMARK   3      T33:   0.0729 T12:   0.0281                                     
REMARK   3      T13:  -0.0349 T23:   0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2433 L22:   0.0736                                     
REMARK   3      L33:   1.5644 L12:   0.0580                                     
REMARK   3      L13:  -0.0800 L23:  -0.2481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0686 S12:   0.0623 S13:   0.0310                       
REMARK   3      S21:   0.0310 S22:   0.0625 S23:  -0.0074                       
REMARK   3      S31:   0.0701 S32:  -0.1668 S33:  -0.1310                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6305  87.2913 -62.4830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0827 T22:   0.0292                                     
REMARK   3      T33:   0.2395 T12:   0.0096                                     
REMARK   3      T13:  -0.0762 T23:   0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2940 L22:   0.8435                                     
REMARK   3      L33:   0.7510 L12:  -0.1000                                     
REMARK   3      L13:   0.0762 L23:  -0.2135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0158 S12:   0.0213 S13:   0.1617                       
REMARK   3      S21:  -0.0854 S22:  -0.0325 S23:   0.2137                       
REMARK   3      S31:   0.0894 S32:  -0.0132 S33:   0.0483                       
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 USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 6HP3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011996.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97925                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 101076                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 251.200                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3500, SODIUM CHLORIDE, HEPES,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      125.60100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 2720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 2320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 2420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 2210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    MSE H   170     CD1  ILE H   174              2.00            
REMARK 500   OE1  GLU A   251     NE2  GLN D   250              2.07            
REMARK 500   NE2  GLN A   172     OE1  GLU B   132              2.07            
REMARK 500   OD1  ASN A   307     NH2  ARG A   340              2.16            
REMARK 500   OD1  ASN G   307     NH2  ARG G   340              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN B    46     OE1  GLN H   378     1455     1.97            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A 276   CG    PHE A 276   CD1     0.105                       
REMARK 500    PHE B 276   CG    PHE B 276   CD1     0.107                       
REMARK 500    TYR C  35   CG    TYR C  35   CD1     0.113                       
REMARK 500    PHE C 276   CG    PHE C 276   CD1     0.109                       
REMARK 500    PHE D 276   CG    PHE D 276   CD1     0.103                       
REMARK 500    GLU E 184   CG    GLU E 184   CD      0.092                       
REMARK 500    PHE E 276   CG    PHE E 276   CD1     0.115                       
REMARK 500    GLU E 382   CD    GLU E 382   OE1     0.067                       
REMARK 500    GLU F  13   CD    GLU F  13   OE1     0.073                       
REMARK 500    SER F 108   CB    SER F 108   OG     -0.083                       
REMARK 500    PHE F 276   CG    PHE F 276   CD1     0.103                       
REMARK 500    GLU H  13   CD    GLU H  13   OE2     0.091                       
REMARK 500    ASN H  16   CG    ASN H  16   ND2     0.185                       
REMARK 500    CYS H 275   CB    CYS H 275   SG     -0.105                       
REMARK 500    PHE H 276   CG    PHE H 276   CD1     0.110                       
REMARK 500    LYS H 315   CE    LYS H 315   NZ      0.167                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  12   CB  -  CG  -  CD2 ANGL. DEV. =  13.4 DEGREES          
REMARK 500    LEU A 156   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG A 228   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    LYS A 255   CD  -  CE  -  NZ  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ASP A 322   CB  -  CA  -  C   ANGL. DEV. =  12.3 DEGREES          
REMARK 500    LEU A 331   CB  -  CG  -  CD1 ANGL. DEV. =  13.6 DEGREES          
REMARK 500    MSE A 333   CG  - SE   -  CE  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG A 340   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    LEU A 385   CB  -  CG  -  CD2 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    MSE B   1   CG  - SE   -  CE  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    MSE B 110   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    LEU B 156   CA  -  CB  -  CG  ANGL. DEV. =  22.7 DEGREES          
REMARK 500    ARG B 228   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    LEU B 298   CB  -  CG  -  CD1 ANGL. DEV. =  13.9 DEGREES          
REMARK 500    LEU B 323   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    ARG B 340   CG  -  CD  -  NE  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    MSE B 374   CG  - SE   -  CE  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    TYR C  35   CB  -  CG  -  CD2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TYR C  35   CB  -  CG  -  CD1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    LEU C 156   CA  -  CB  -  CG  ANGL. DEV. =  23.2 DEGREES          
REMARK 500    PHE C 167   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG C 228   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    LEU C 242   CB  -  CG  -  CD2 ANGL. DEV. = -13.9 DEGREES          
REMARK 500    LYS C 286   CD  -  CE  -  NZ  ANGL. DEV. = -17.5 DEGREES          
REMARK 500    ASP C 293   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    LEU C 321   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    LEU C 323   CA  -  CB  -  CG  ANGL. DEV. =  19.8 DEGREES          
REMARK 500    LEU C 323   CB  -  CG  -  CD2 ANGL. DEV. = -17.0 DEGREES          
REMARK 500    LEU C 363   CB  -  CG  -  CD1 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG D 123   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    LEU D 156   CA  -  CB  -  CG  ANGL. DEV. =  23.1 DEGREES          
REMARK 500    ARG D 189   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG D 195   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LYS D 320   CB  -  CA  -  C   ANGL. DEV. =  16.1 DEGREES          
REMARK 500    LYS D 320   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    LEU D 321   CA  -  CB  -  CG  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ASP D 322   CB  -  CA  -  C   ANGL. DEV. =  12.1 DEGREES          
REMARK 500    LEU D 323   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    LEU D 324   CA  -  CB  -  CG  ANGL. DEV. =  20.2 DEGREES          
REMARK 500    LEU D 331   CB  -  CG  -  CD1 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ASP E 102   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP E 102   CB  -  CG  -  OD2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    LEU E 156   CA  -  CB  -  CG  ANGL. DEV. =  22.5 DEGREES          
REMARK 500    ARG E 195   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    MSE E 296   CA  -  CB  -  CG  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    LEU E 318   CB  -  CG  -  CD1 ANGL. DEV. =  10.4 DEGREES          
REMARK 500    LEU E 321   CB  -  CG  -  CD2 ANGL. DEV. =  17.2 DEGREES          
REMARK 500    LEU E 324   CB  -  CG  -  CD2 ANGL. DEV. = -11.8 DEGREES          
REMARK 500    ASN E 327   CB  -  CA  -  C   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    LYS E 345   CD  -  CE  -  NZ  ANGL. DEV. =  15.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  15      102.45   -164.33                                   
REMARK 500    PRO A  31        1.35    -64.89                                   
REMARK 500    GLN A 343       58.27     33.62                                   
REMARK 500    PHE A 362      -74.91   -117.61                                   
REMARK 500    ASP B  15      102.18   -163.78                                   
REMARK 500    PRO B  31        1.41    -65.27                                   
REMARK 500    ASN B 309       42.74     39.94                                   
REMARK 500    GLN B 343       58.32     33.52                                   
REMARK 500    PHE B 362      -75.12   -117.63                                   
REMARK 500    ASP C  15      102.43   -164.32                                   
REMARK 500    PRO C  31        2.11    -65.16                                   
REMARK 500    GLN C 343       58.15     33.18                                   
REMARK 500    PHE C 362      -74.52   -118.03                                   
REMARK 500    ASP D  15      101.90   -163.45                                   
REMARK 500    PRO D  31        1.65    -65.17                                   
REMARK 500    GLN D 343       58.24     32.46                                   
REMARK 500    PHE D 362      -75.44   -118.11                                   
REMARK 500    ASP E  15      102.47   -163.53                                   
REMARK 500    PRO E  31        4.98    -67.63                                   
REMARK 500    GLN E 343       57.33     32.90                                   
REMARK 500    PHE E 362      -75.53   -117.63                                   
REMARK 500    ASP F  15      102.18   -163.48                                   
REMARK 500    PRO F  31        1.82    -65.02                                   
REMARK 500    GLN F 343       58.24     34.17                                   
REMARK 500    PHE F 362      -73.84   -117.40                                   
REMARK 500    ASP G  15      102.74   -163.78                                   
REMARK 500    PRO G  31        2.91    -66.39                                   
REMARK 500    GLN G 343       58.17     32.28                                   
REMARK 500    PHE G 362      -74.35   -118.18                                   
REMARK 500    ASP H  15      102.83   -163.17                                   
REMARK 500    PRO H  31        1.08    -64.91                                   
REMARK 500    GLN H 343       56.38     34.61                                   
REMARK 500    PHE H 362      -74.56   -117.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    PHE E 167         0.07    SIDE CHAIN                              
REMARK 500    ASN H  16         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6HP3 A    1   386  UNP    O31927   YOPK_BACSU       1    386             
DBREF  6HP3 B    1   386  UNP    O31927   YOPK_BACSU       1    386             
DBREF  6HP3 C    1   386  UNP    O31927   YOPK_BACSU       1    386             
DBREF  6HP3 D    1   386  UNP    O31927   YOPK_BACSU       1    386             
DBREF  6HP3 E    1   386  UNP    O31927   YOPK_BACSU       1    386             
DBREF  6HP3 F    1   386  UNP    O31927   YOPK_BACSU       1    386             
DBREF  6HP3 G    1   386  UNP    O31927   YOPK_BACSU       1    386             
DBREF  6HP3 H    1   386  UNP    O31927   YOPK_BACSU       1    386             
SEQRES   1 A  386  MSE GLU LEU ILE ARG ILE ALA MSE LYS LYS ASP LEU GLU          
SEQRES   2 A  386  ASN ASP ASN SER LEU MSE ASN LYS TRP ALA THR VAL ALA          
SEQRES   3 A  386  GLY LEU LYS ASN PRO ASN PRO LEU TYR ASP PHE LEU ASN          
SEQRES   4 A  386  HIS ASP GLY LYS THR PHE ASN GLU PHE SER SER ILE VAL          
SEQRES   5 A  386  ASN ILE VAL LYS SER GLN TYR PRO ASP ARG GLU TYR GLU          
SEQRES   6 A  386  LEU MSE LYS ASP TYR CYS LEU ASN LEU ASP VAL LYS THR          
SEQRES   7 A  386  LYS ALA ALA ARG SER ALA LEU GLU TYR ALA ASP ALA ASN          
SEQRES   8 A  386  MSE PHE PHE GLU ILE GLU ASP VAL LEU ILE ASP SER MSE          
SEQRES   9 A  386  ILE SER CYS SER ASN MSE LYS SER LYS GLU TYR GLY LYS          
SEQRES  10 A  386  VAL TYR LYS ILE HIS ARG GLU LEU SER ASN SER VAL ILE          
SEQRES  11 A  386  THR GLU PHE GLU ALA VAL LYS ARG LEU GLY LYS LEU ASN          
SEQRES  12 A  386  ILE LYS THR PRO GLU MSE ASN SER PHE SER ARG LEU LEU          
SEQRES  13 A  386  LEU LEU TYR HIS TYR LEU SER THR GLY ASN PHE SER PRO          
SEQRES  14 A  386  MSE ALA GLN LEU ILE LYS GLN ILE ASP LEU SER GLU ILE          
SEQRES  15 A  386  SER GLU ASN MSE TYR ILE ARG ASN THR TYR GLN THR ARG          
SEQRES  16 A  386  VAL HIS VAL LEU MSE SER ASN ILE LYS LEU ASN GLU ASN          
SEQRES  17 A  386  SER LEU GLU GLU CYS ARG GLU TYR SER LYS LYS ALA LEU          
SEQRES  18 A  386  GLU SER THR ASN ILE LEU ARG PHE GLN VAL PHE SER TYR          
SEQRES  19 A  386  LEU THR ILE GLY ASN SER LEU LEU PHE SER ASN TYR GLU          
SEQRES  20 A  386  LEU ALA GLN GLU ASN PHE LEU LYS GLY LEU SER ILE SER          
SEQRES  21 A  386  VAL GLN ASN GLU ASN TYR ASN MSE ILE PHE GLN GLN ALA          
SEQRES  22 A  386  LEU CYS PHE LEU ASN ASN VAL TRP ARG LYS GLU ASN LYS          
SEQRES  23 A  386  TRP ILE ASN PHE GLU SER ASP SER ILE MSE ASP LEU GLN          
SEQRES  24 A  386  GLU GLN ALA HIS CYS PHE ILE ASN PHE ASN GLU ASN SER          
SEQRES  25 A  386  LYS ALA LYS GLU VAL LEU ASP LYS LEU ASP LEU LEU VAL          
SEQRES  26 A  386  HIS ASN ASP ASN GLU LEU ALA MSE HIS TYR TYR LEU LYS          
SEQRES  27 A  386  GLY ARG LEU GLU GLN ASN LYS ALA CYS PHE TYR SER SER          
SEQRES  28 A  386  ILE GLU TYR PHE LYS LYS SER ASN ASP LYS PHE LEU ILE          
SEQRES  29 A  386  ARG LEU PRO LEU LEU GLU LEU GLN LYS MSE GLY GLU ASN          
SEQRES  30 A  386  GLN LYS LEU LEU GLU LEU LEU LEU LEU                          
SEQRES   1 B  386  MSE GLU LEU ILE ARG ILE ALA MSE LYS LYS ASP LEU GLU          
SEQRES   2 B  386  ASN ASP ASN SER LEU MSE ASN LYS TRP ALA THR VAL ALA          
SEQRES   3 B  386  GLY LEU LYS ASN PRO ASN PRO LEU TYR ASP PHE LEU ASN          
SEQRES   4 B  386  HIS ASP GLY LYS THR PHE ASN GLU PHE SER SER ILE VAL          
SEQRES   5 B  386  ASN ILE VAL LYS SER GLN TYR PRO ASP ARG GLU TYR GLU          
SEQRES   6 B  386  LEU MSE LYS ASP TYR CYS LEU ASN LEU ASP VAL LYS THR          
SEQRES   7 B  386  LYS ALA ALA ARG SER ALA LEU GLU TYR ALA ASP ALA ASN          
SEQRES   8 B  386  MSE PHE PHE GLU ILE GLU ASP VAL LEU ILE ASP SER MSE          
SEQRES   9 B  386  ILE SER CYS SER ASN MSE LYS SER LYS GLU TYR GLY LYS          
SEQRES  10 B  386  VAL TYR LYS ILE HIS ARG GLU LEU SER ASN SER VAL ILE          
SEQRES  11 B  386  THR GLU PHE GLU ALA VAL LYS ARG LEU GLY LYS LEU ASN          
SEQRES  12 B  386  ILE LYS THR PRO GLU MSE ASN SER PHE SER ARG LEU LEU          
SEQRES  13 B  386  LEU LEU TYR HIS TYR LEU SER THR GLY ASN PHE SER PRO          
SEQRES  14 B  386  MSE ALA GLN LEU ILE LYS GLN ILE ASP LEU SER GLU ILE          
SEQRES  15 B  386  SER GLU ASN MSE TYR ILE ARG ASN THR TYR GLN THR ARG          
SEQRES  16 B  386  VAL HIS VAL LEU MSE SER ASN ILE LYS LEU ASN GLU ASN          
SEQRES  17 B  386  SER LEU GLU GLU CYS ARG GLU TYR SER LYS LYS ALA LEU          
SEQRES  18 B  386  GLU SER THR ASN ILE LEU ARG PHE GLN VAL PHE SER TYR          
SEQRES  19 B  386  LEU THR ILE GLY ASN SER LEU LEU PHE SER ASN TYR GLU          
SEQRES  20 B  386  LEU ALA GLN GLU ASN PHE LEU LYS GLY LEU SER ILE SER          
SEQRES  21 B  386  VAL GLN ASN GLU ASN TYR ASN MSE ILE PHE GLN GLN ALA          
SEQRES  22 B  386  LEU CYS PHE LEU ASN ASN VAL TRP ARG LYS GLU ASN LYS          
SEQRES  23 B  386  TRP ILE ASN PHE GLU SER ASP SER ILE MSE ASP LEU GLN          
SEQRES  24 B  386  GLU GLN ALA HIS CYS PHE ILE ASN PHE ASN GLU ASN SER          
SEQRES  25 B  386  LYS ALA LYS GLU VAL LEU ASP LYS LEU ASP LEU LEU VAL          
SEQRES  26 B  386  HIS ASN ASP ASN GLU LEU ALA MSE HIS TYR TYR LEU LYS          
SEQRES  27 B  386  GLY ARG LEU GLU GLN ASN LYS ALA CYS PHE TYR SER SER          
SEQRES  28 B  386  ILE GLU TYR PHE LYS LYS SER ASN ASP LYS PHE LEU ILE          
SEQRES  29 B  386  ARG LEU PRO LEU LEU GLU LEU GLN LYS MSE GLY GLU ASN          
SEQRES  30 B  386  GLN LYS LEU LEU GLU LEU LEU LEU LEU                          
SEQRES   1 C  386  MSE GLU LEU ILE ARG ILE ALA MSE LYS LYS ASP LEU GLU          
SEQRES   2 C  386  ASN ASP ASN SER LEU MSE ASN LYS TRP ALA THR VAL ALA          
SEQRES   3 C  386  GLY LEU LYS ASN PRO ASN PRO LEU TYR ASP PHE LEU ASN          
SEQRES   4 C  386  HIS ASP GLY LYS THR PHE ASN GLU PHE SER SER ILE VAL          
SEQRES   5 C  386  ASN ILE VAL LYS SER GLN TYR PRO ASP ARG GLU TYR GLU          
SEQRES   6 C  386  LEU MSE LYS ASP TYR CYS LEU ASN LEU ASP VAL LYS THR          
SEQRES   7 C  386  LYS ALA ALA ARG SER ALA LEU GLU TYR ALA ASP ALA ASN          
SEQRES   8 C  386  MSE PHE PHE GLU ILE GLU ASP VAL LEU ILE ASP SER MSE          
SEQRES   9 C  386  ILE SER CYS SER ASN MSE LYS SER LYS GLU TYR GLY LYS          
SEQRES  10 C  386  VAL TYR LYS ILE HIS ARG GLU LEU SER ASN SER VAL ILE          
SEQRES  11 C  386  THR GLU PHE GLU ALA VAL LYS ARG LEU GLY LYS LEU ASN          
SEQRES  12 C  386  ILE LYS THR PRO GLU MSE ASN SER PHE SER ARG LEU LEU          
SEQRES  13 C  386  LEU LEU TYR HIS TYR LEU SER THR GLY ASN PHE SER PRO          
SEQRES  14 C  386  MSE ALA GLN LEU ILE LYS GLN ILE ASP LEU SER GLU ILE          
SEQRES  15 C  386  SER GLU ASN MSE TYR ILE ARG ASN THR TYR GLN THR ARG          
SEQRES  16 C  386  VAL HIS VAL LEU MSE SER ASN ILE LYS LEU ASN GLU ASN          
SEQRES  17 C  386  SER LEU GLU GLU CYS ARG GLU TYR SER LYS LYS ALA LEU          
SEQRES  18 C  386  GLU SER THR ASN ILE LEU ARG PHE GLN VAL PHE SER TYR          
SEQRES  19 C  386  LEU THR ILE GLY ASN SER LEU LEU PHE SER ASN TYR GLU          
SEQRES  20 C  386  LEU ALA GLN GLU ASN PHE LEU LYS GLY LEU SER ILE SER          
SEQRES  21 C  386  VAL GLN ASN GLU ASN TYR ASN MSE ILE PHE GLN GLN ALA          
SEQRES  22 C  386  LEU CYS PHE LEU ASN ASN VAL TRP ARG LYS GLU ASN LYS          
SEQRES  23 C  386  TRP ILE ASN PHE GLU SER ASP SER ILE MSE ASP LEU GLN          
SEQRES  24 C  386  GLU GLN ALA HIS CYS PHE ILE ASN PHE ASN GLU ASN SER          
SEQRES  25 C  386  LYS ALA LYS GLU VAL LEU ASP LYS LEU ASP LEU LEU VAL          
SEQRES  26 C  386  HIS ASN ASP ASN GLU LEU ALA MSE HIS TYR TYR LEU LYS          
SEQRES  27 C  386  GLY ARG LEU GLU GLN ASN LYS ALA CYS PHE TYR SER SER          
SEQRES  28 C  386  ILE GLU TYR PHE LYS LYS SER ASN ASP LYS PHE LEU ILE          
SEQRES  29 C  386  ARG LEU PRO LEU LEU GLU LEU GLN LYS MSE GLY GLU ASN          
SEQRES  30 C  386  GLN LYS LEU LEU GLU LEU LEU LEU LEU                          
SEQRES   1 D  386  MSE GLU LEU ILE ARG ILE ALA MSE LYS LYS ASP LEU GLU          
SEQRES   2 D  386  ASN ASP ASN SER LEU MSE ASN LYS TRP ALA THR VAL ALA          
SEQRES   3 D  386  GLY LEU LYS ASN PRO ASN PRO LEU TYR ASP PHE LEU ASN          
SEQRES   4 D  386  HIS ASP GLY LYS THR PHE ASN GLU PHE SER SER ILE VAL          
SEQRES   5 D  386  ASN ILE VAL LYS SER GLN TYR PRO ASP ARG GLU TYR GLU          
SEQRES   6 D  386  LEU MSE LYS ASP TYR CYS LEU ASN LEU ASP VAL LYS THR          
SEQRES   7 D  386  LYS ALA ALA ARG SER ALA LEU GLU TYR ALA ASP ALA ASN          
SEQRES   8 D  386  MSE PHE PHE GLU ILE GLU ASP VAL LEU ILE ASP SER MSE          
SEQRES   9 D  386  ILE SER CYS SER ASN MSE LYS SER LYS GLU TYR GLY LYS          
SEQRES  10 D  386  VAL TYR LYS ILE HIS ARG GLU LEU SER ASN SER VAL ILE          
SEQRES  11 D  386  THR GLU PHE GLU ALA VAL LYS ARG LEU GLY LYS LEU ASN          
SEQRES  12 D  386  ILE LYS THR PRO GLU MSE ASN SER PHE SER ARG LEU LEU          
SEQRES  13 D  386  LEU LEU TYR HIS TYR LEU SER THR GLY ASN PHE SER PRO          
SEQRES  14 D  386  MSE ALA GLN LEU ILE LYS GLN ILE ASP LEU SER GLU ILE          
SEQRES  15 D  386  SER GLU ASN MSE TYR ILE ARG ASN THR TYR GLN THR ARG          
SEQRES  16 D  386  VAL HIS VAL LEU MSE SER ASN ILE LYS LEU ASN GLU ASN          
SEQRES  17 D  386  SER LEU GLU GLU CYS ARG GLU TYR SER LYS LYS ALA LEU          
SEQRES  18 D  386  GLU SER THR ASN ILE LEU ARG PHE GLN VAL PHE SER TYR          
SEQRES  19 D  386  LEU THR ILE GLY ASN SER LEU LEU PHE SER ASN TYR GLU          
SEQRES  20 D  386  LEU ALA GLN GLU ASN PHE LEU LYS GLY LEU SER ILE SER          
SEQRES  21 D  386  VAL GLN ASN GLU ASN TYR ASN MSE ILE PHE GLN GLN ALA          
SEQRES  22 D  386  LEU CYS PHE LEU ASN ASN VAL TRP ARG LYS GLU ASN LYS          
SEQRES  23 D  386  TRP ILE ASN PHE GLU SER ASP SER ILE MSE ASP LEU GLN          
SEQRES  24 D  386  GLU GLN ALA HIS CYS PHE ILE ASN PHE ASN GLU ASN SER          
SEQRES  25 D  386  LYS ALA LYS GLU VAL LEU ASP LYS LEU ASP LEU LEU VAL          
SEQRES  26 D  386  HIS ASN ASP ASN GLU LEU ALA MSE HIS TYR TYR LEU LYS          
SEQRES  27 D  386  GLY ARG LEU GLU GLN ASN LYS ALA CYS PHE TYR SER SER          
SEQRES  28 D  386  ILE GLU TYR PHE LYS LYS SER ASN ASP LYS PHE LEU ILE          
SEQRES  29 D  386  ARG LEU PRO LEU LEU GLU LEU GLN LYS MSE GLY GLU ASN          
SEQRES  30 D  386  GLN LYS LEU LEU GLU LEU LEU LEU LEU                          
SEQRES   1 E  386  MSE GLU LEU ILE ARG ILE ALA MSE LYS LYS ASP LEU GLU          
SEQRES   2 E  386  ASN ASP ASN SER LEU MSE ASN LYS TRP ALA THR VAL ALA          
SEQRES   3 E  386  GLY LEU LYS ASN PRO ASN PRO LEU TYR ASP PHE LEU ASN          
SEQRES   4 E  386  HIS ASP GLY LYS THR PHE ASN GLU PHE SER SER ILE VAL          
SEQRES   5 E  386  ASN ILE VAL LYS SER GLN TYR PRO ASP ARG GLU TYR GLU          
SEQRES   6 E  386  LEU MSE LYS ASP TYR CYS LEU ASN LEU ASP VAL LYS THR          
SEQRES   7 E  386  LYS ALA ALA ARG SER ALA LEU GLU TYR ALA ASP ALA ASN          
SEQRES   8 E  386  MSE PHE PHE GLU ILE GLU ASP VAL LEU ILE ASP SER MSE          
SEQRES   9 E  386  ILE SER CYS SER ASN MSE LYS SER LYS GLU TYR GLY LYS          
SEQRES  10 E  386  VAL TYR LYS ILE HIS ARG GLU LEU SER ASN SER VAL ILE          
SEQRES  11 E  386  THR GLU PHE GLU ALA VAL LYS ARG LEU GLY LYS LEU ASN          
SEQRES  12 E  386  ILE LYS THR PRO GLU MSE ASN SER PHE SER ARG LEU LEU          
SEQRES  13 E  386  LEU LEU TYR HIS TYR LEU SER THR GLY ASN PHE SER PRO          
SEQRES  14 E  386  MSE ALA GLN LEU ILE LYS GLN ILE ASP LEU SER GLU ILE          
SEQRES  15 E  386  SER GLU ASN MSE TYR ILE ARG ASN THR TYR GLN THR ARG          
SEQRES  16 E  386  VAL HIS VAL LEU MSE SER ASN ILE LYS LEU ASN GLU ASN          
SEQRES  17 E  386  SER LEU GLU GLU CYS ARG GLU TYR SER LYS LYS ALA LEU          
SEQRES  18 E  386  GLU SER THR ASN ILE LEU ARG PHE GLN VAL PHE SER TYR          
SEQRES  19 E  386  LEU THR ILE GLY ASN SER LEU LEU PHE SER ASN TYR GLU          
SEQRES  20 E  386  LEU ALA GLN GLU ASN PHE LEU LYS GLY LEU SER ILE SER          
SEQRES  21 E  386  VAL GLN ASN GLU ASN TYR ASN MSE ILE PHE GLN GLN ALA          
SEQRES  22 E  386  LEU CYS PHE LEU ASN ASN VAL TRP ARG LYS GLU ASN LYS          
SEQRES  23 E  386  TRP ILE ASN PHE GLU SER ASP SER ILE MSE ASP LEU GLN          
SEQRES  24 E  386  GLU GLN ALA HIS CYS PHE ILE ASN PHE ASN GLU ASN SER          
SEQRES  25 E  386  LYS ALA LYS GLU VAL LEU ASP LYS LEU ASP LEU LEU VAL          
SEQRES  26 E  386  HIS ASN ASP ASN GLU LEU ALA MSE HIS TYR TYR LEU LYS          
SEQRES  27 E  386  GLY ARG LEU GLU GLN ASN LYS ALA CYS PHE TYR SER SER          
SEQRES  28 E  386  ILE GLU TYR PHE LYS LYS SER ASN ASP LYS PHE LEU ILE          
SEQRES  29 E  386  ARG LEU PRO LEU LEU GLU LEU GLN LYS MSE GLY GLU ASN          
SEQRES  30 E  386  GLN LYS LEU LEU GLU LEU LEU LEU LEU                          
SEQRES   1 F  386  MSE GLU LEU ILE ARG ILE ALA MSE LYS LYS ASP LEU GLU          
SEQRES   2 F  386  ASN ASP ASN SER LEU MSE ASN LYS TRP ALA THR VAL ALA          
SEQRES   3 F  386  GLY LEU LYS ASN PRO ASN PRO LEU TYR ASP PHE LEU ASN          
SEQRES   4 F  386  HIS ASP GLY LYS THR PHE ASN GLU PHE SER SER ILE VAL          
SEQRES   5 F  386  ASN ILE VAL LYS SER GLN TYR PRO ASP ARG GLU TYR GLU          
SEQRES   6 F  386  LEU MSE LYS ASP TYR CYS LEU ASN LEU ASP VAL LYS THR          
SEQRES   7 F  386  LYS ALA ALA ARG SER ALA LEU GLU TYR ALA ASP ALA ASN          
SEQRES   8 F  386  MSE PHE PHE GLU ILE GLU ASP VAL LEU ILE ASP SER MSE          
SEQRES   9 F  386  ILE SER CYS SER ASN MSE LYS SER LYS GLU TYR GLY LYS          
SEQRES  10 F  386  VAL TYR LYS ILE HIS ARG GLU LEU SER ASN SER VAL ILE          
SEQRES  11 F  386  THR GLU PHE GLU ALA VAL LYS ARG LEU GLY LYS LEU ASN          
SEQRES  12 F  386  ILE LYS THR PRO GLU MSE ASN SER PHE SER ARG LEU LEU          
SEQRES  13 F  386  LEU LEU TYR HIS TYR LEU SER THR GLY ASN PHE SER PRO          
SEQRES  14 F  386  MSE ALA GLN LEU ILE LYS GLN ILE ASP LEU SER GLU ILE          
SEQRES  15 F  386  SER GLU ASN MSE TYR ILE ARG ASN THR TYR GLN THR ARG          
SEQRES  16 F  386  VAL HIS VAL LEU MSE SER ASN ILE LYS LEU ASN GLU ASN          
SEQRES  17 F  386  SER LEU GLU GLU CYS ARG GLU TYR SER LYS LYS ALA LEU          
SEQRES  18 F  386  GLU SER THR ASN ILE LEU ARG PHE GLN VAL PHE SER TYR          
SEQRES  19 F  386  LEU THR ILE GLY ASN SER LEU LEU PHE SER ASN TYR GLU          
SEQRES  20 F  386  LEU ALA GLN GLU ASN PHE LEU LYS GLY LEU SER ILE SER          
SEQRES  21 F  386  VAL GLN ASN GLU ASN TYR ASN MSE ILE PHE GLN GLN ALA          
SEQRES  22 F  386  LEU CYS PHE LEU ASN ASN VAL TRP ARG LYS GLU ASN LYS          
SEQRES  23 F  386  TRP ILE ASN PHE GLU SER ASP SER ILE MSE ASP LEU GLN          
SEQRES  24 F  386  GLU GLN ALA HIS CYS PHE ILE ASN PHE ASN GLU ASN SER          
SEQRES  25 F  386  LYS ALA LYS GLU VAL LEU ASP LYS LEU ASP LEU LEU VAL          
SEQRES  26 F  386  HIS ASN ASP ASN GLU LEU ALA MSE HIS TYR TYR LEU LYS          
SEQRES  27 F  386  GLY ARG LEU GLU GLN ASN LYS ALA CYS PHE TYR SER SER          
SEQRES  28 F  386  ILE GLU TYR PHE LYS LYS SER ASN ASP LYS PHE LEU ILE          
SEQRES  29 F  386  ARG LEU PRO LEU LEU GLU LEU GLN LYS MSE GLY GLU ASN          
SEQRES  30 F  386  GLN LYS LEU LEU GLU LEU LEU LEU LEU                          
SEQRES   1 G  386  MSE GLU LEU ILE ARG ILE ALA MSE LYS LYS ASP LEU GLU          
SEQRES   2 G  386  ASN ASP ASN SER LEU MSE ASN LYS TRP ALA THR VAL ALA          
SEQRES   3 G  386  GLY LEU LYS ASN PRO ASN PRO LEU TYR ASP PHE LEU ASN          
SEQRES   4 G  386  HIS ASP GLY LYS THR PHE ASN GLU PHE SER SER ILE VAL          
SEQRES   5 G  386  ASN ILE VAL LYS SER GLN TYR PRO ASP ARG GLU TYR GLU          
SEQRES   6 G  386  LEU MSE LYS ASP TYR CYS LEU ASN LEU ASP VAL LYS THR          
SEQRES   7 G  386  LYS ALA ALA ARG SER ALA LEU GLU TYR ALA ASP ALA ASN          
SEQRES   8 G  386  MSE PHE PHE GLU ILE GLU ASP VAL LEU ILE ASP SER MSE          
SEQRES   9 G  386  ILE SER CYS SER ASN MSE LYS SER LYS GLU TYR GLY LYS          
SEQRES  10 G  386  VAL TYR LYS ILE HIS ARG GLU LEU SER ASN SER VAL ILE          
SEQRES  11 G  386  THR GLU PHE GLU ALA VAL LYS ARG LEU GLY LYS LEU ASN          
SEQRES  12 G  386  ILE LYS THR PRO GLU MSE ASN SER PHE SER ARG LEU LEU          
SEQRES  13 G  386  LEU LEU TYR HIS TYR LEU SER THR GLY ASN PHE SER PRO          
SEQRES  14 G  386  MSE ALA GLN LEU ILE LYS GLN ILE ASP LEU SER GLU ILE          
SEQRES  15 G  386  SER GLU ASN MSE TYR ILE ARG ASN THR TYR GLN THR ARG          
SEQRES  16 G  386  VAL HIS VAL LEU MSE SER ASN ILE LYS LEU ASN GLU ASN          
SEQRES  17 G  386  SER LEU GLU GLU CYS ARG GLU TYR SER LYS LYS ALA LEU          
SEQRES  18 G  386  GLU SER THR ASN ILE LEU ARG PHE GLN VAL PHE SER TYR          
SEQRES  19 G  386  LEU THR ILE GLY ASN SER LEU LEU PHE SER ASN TYR GLU          
SEQRES  20 G  386  LEU ALA GLN GLU ASN PHE LEU LYS GLY LEU SER ILE SER          
SEQRES  21 G  386  VAL GLN ASN GLU ASN TYR ASN MSE ILE PHE GLN GLN ALA          
SEQRES  22 G  386  LEU CYS PHE LEU ASN ASN VAL TRP ARG LYS GLU ASN LYS          
SEQRES  23 G  386  TRP ILE ASN PHE GLU SER ASP SER ILE MSE ASP LEU GLN          
SEQRES  24 G  386  GLU GLN ALA HIS CYS PHE ILE ASN PHE ASN GLU ASN SER          
SEQRES  25 G  386  LYS ALA LYS GLU VAL LEU ASP LYS LEU ASP LEU LEU VAL          
SEQRES  26 G  386  HIS ASN ASP ASN GLU LEU ALA MSE HIS TYR TYR LEU LYS          
SEQRES  27 G  386  GLY ARG LEU GLU GLN ASN LYS ALA CYS PHE TYR SER SER          
SEQRES  28 G  386  ILE GLU TYR PHE LYS LYS SER ASN ASP LYS PHE LEU ILE          
SEQRES  29 G  386  ARG LEU PRO LEU LEU GLU LEU GLN LYS MSE GLY GLU ASN          
SEQRES  30 G  386  GLN LYS LEU LEU GLU LEU LEU LEU LEU                          
SEQRES   1 H  386  MSE GLU LEU ILE ARG ILE ALA MSE LYS LYS ASP LEU GLU          
SEQRES   2 H  386  ASN ASP ASN SER LEU MSE ASN LYS TRP ALA THR VAL ALA          
SEQRES   3 H  386  GLY LEU LYS ASN PRO ASN PRO LEU TYR ASP PHE LEU ASN          
SEQRES   4 H  386  HIS ASP GLY LYS THR PHE ASN GLU PHE SER SER ILE VAL          
SEQRES   5 H  386  ASN ILE VAL LYS SER GLN TYR PRO ASP ARG GLU TYR GLU          
SEQRES   6 H  386  LEU MSE LYS ASP TYR CYS LEU ASN LEU ASP VAL LYS THR          
SEQRES   7 H  386  LYS ALA ALA ARG SER ALA LEU GLU TYR ALA ASP ALA ASN          
SEQRES   8 H  386  MSE PHE PHE GLU ILE GLU ASP VAL LEU ILE ASP SER MSE          
SEQRES   9 H  386  ILE SER CYS SER ASN MSE LYS SER LYS GLU TYR GLY LYS          
SEQRES  10 H  386  VAL TYR LYS ILE HIS ARG GLU LEU SER ASN SER VAL ILE          
SEQRES  11 H  386  THR GLU PHE GLU ALA VAL LYS ARG LEU GLY LYS LEU ASN          
SEQRES  12 H  386  ILE LYS THR PRO GLU MSE ASN SER PHE SER ARG LEU LEU          
SEQRES  13 H  386  LEU LEU TYR HIS TYR LEU SER THR GLY ASN PHE SER PRO          
SEQRES  14 H  386  MSE ALA GLN LEU ILE LYS GLN ILE ASP LEU SER GLU ILE          
SEQRES  15 H  386  SER GLU ASN MSE TYR ILE ARG ASN THR TYR GLN THR ARG          
SEQRES  16 H  386  VAL HIS VAL LEU MSE SER ASN ILE LYS LEU ASN GLU ASN          
SEQRES  17 H  386  SER LEU GLU GLU CYS ARG GLU TYR SER LYS LYS ALA LEU          
SEQRES  18 H  386  GLU SER THR ASN ILE LEU ARG PHE GLN VAL PHE SER TYR          
SEQRES  19 H  386  LEU THR ILE GLY ASN SER LEU LEU PHE SER ASN TYR GLU          
SEQRES  20 H  386  LEU ALA GLN GLU ASN PHE LEU LYS GLY LEU SER ILE SER          
SEQRES  21 H  386  VAL GLN ASN GLU ASN TYR ASN MSE ILE PHE GLN GLN ALA          
SEQRES  22 H  386  LEU CYS PHE LEU ASN ASN VAL TRP ARG LYS GLU ASN LYS          
SEQRES  23 H  386  TRP ILE ASN PHE GLU SER ASP SER ILE MSE ASP LEU GLN          
SEQRES  24 H  386  GLU GLN ALA HIS CYS PHE ILE ASN PHE ASN GLU ASN SER          
SEQRES  25 H  386  LYS ALA LYS GLU VAL LEU ASP LYS LEU ASP LEU LEU VAL          
SEQRES  26 H  386  HIS ASN ASP ASN GLU LEU ALA MSE HIS TYR TYR LEU LYS          
SEQRES  27 H  386  GLY ARG LEU GLU GLN ASN LYS ALA CYS PHE TYR SER SER          
SEQRES  28 H  386  ILE GLU TYR PHE LYS LYS SER ASN ASP LYS PHE LEU ILE          
SEQRES  29 H  386  ARG LEU PRO LEU LEU GLU LEU GLN LYS MSE GLY GLU ASN          
SEQRES  30 H  386  GLN LYS LEU LEU GLU LEU LEU LEU LEU                          
MODRES 6HP3 MSE A    1  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A    8  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A   19  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A   67  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A   92  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  104  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  110  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  149  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  170  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  186  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  200  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  268  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  296  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  333  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE A  374  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B    1  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B    8  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B   19  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B   67  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B   92  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  104  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  110  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  149  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  170  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  186  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  200  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  268  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  296  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  333  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE B  374  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C    1  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C    8  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C   19  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C   67  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C   92  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  104  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  110  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  149  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  170  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  186  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  200  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  268  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  296  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  333  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE C  374  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D    1  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D    8  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D   19  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D   67  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D   92  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  104  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  110  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  149  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  170  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  186  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  200  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  268  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  296  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  333  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE D  374  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E    1  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E    8  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E   19  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E   67  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E   92  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  104  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  110  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  149  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  170  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  186  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  200  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  268  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  296  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  333  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE E  374  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F    1  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F    8  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F   19  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F   67  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F   92  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  104  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  110  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  149  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  170  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  186  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  200  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  268  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  296  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  333  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE F  374  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G    1  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G    8  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G   19  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G   67  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G   92  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  104  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  110  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  149  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  170  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  186  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  200  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  268  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  296  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  333  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE G  374  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H    1  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H    8  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H   19  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H   67  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H   92  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  104  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  110  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  149  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  170  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  186  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  200  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  268  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  296  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  333  MET  MODIFIED RESIDUE                                   
MODRES 6HP3 MSE H  374  MET  MODIFIED RESIDUE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A   8       8                                                       
HET    MSE  A  19       8                                                       
HET    MSE  A  67       8                                                       
HET    MSE  A  92       8                                                       
HET    MSE  A 104       8                                                       
HET    MSE  A 110       8                                                       
HET    MSE  A 149       8                                                       
HET    MSE  A 170       8                                                       
HET    MSE  A 186       8                                                       
HET    MSE  A 200       8                                                       
HET    MSE  A 268       8                                                       
HET    MSE  A 296       8                                                       
HET    MSE  A 333       8                                                       
HET    MSE  A 374       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B   8       8                                                       
HET    MSE  B  19       8                                                       
HET    MSE  B  67       8                                                       
HET    MSE  B  92       8                                                       
HET    MSE  B 104       8                                                       
HET    MSE  B 110       8                                                       
HET    MSE  B 149       8                                                       
HET    MSE  B 170       8                                                       
HET    MSE  B 186       8                                                       
HET    MSE  B 200       8                                                       
HET    MSE  B 268       8                                                       
HET    MSE  B 296       8                                                       
HET    MSE  B 333       8                                                       
HET    MSE  B 374       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C   8       8                                                       
HET    MSE  C  19       8                                                       
HET    MSE  C  67       8                                                       
HET    MSE  C  92       8                                                       
HET    MSE  C 104       8                                                       
HET    MSE  C 110       8                                                       
HET    MSE  C 149       8                                                       
HET    MSE  C 170       8                                                       
HET    MSE  C 186       8                                                       
HET    MSE  C 200       8                                                       
HET    MSE  C 268       8                                                       
HET    MSE  C 296       8                                                       
HET    MSE  C 333       8                                                       
HET    MSE  C 374       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D   8       8                                                       
HET    MSE  D  19       8                                                       
HET    MSE  D  67       8                                                       
HET    MSE  D  92       8                                                       
HET    MSE  D 104       8                                                       
HET    MSE  D 110       8                                                       
HET    MSE  D 149       8                                                       
HET    MSE  D 170       8                                                       
HET    MSE  D 186       8                                                       
HET    MSE  D 200       8                                                       
HET    MSE  D 268       8                                                       
HET    MSE  D 296       8                                                       
HET    MSE  D 333       8                                                       
HET    MSE  D 374       8                                                       
HET    MSE  E   1       8                                                       
HET    MSE  E   8       8                                                       
HET    MSE  E  19       8                                                       
HET    MSE  E  67       8                                                       
HET    MSE  E  92       8                                                       
HET    MSE  E 104       8                                                       
HET    MSE  E 110      13                                                       
HET    MSE  E 149       8                                                       
HET    MSE  E 170       8                                                       
HET    MSE  E 186       8                                                       
HET    MSE  E 200       8                                                       
HET    MSE  E 268       8                                                       
HET    MSE  E 296       8                                                       
HET    MSE  E 333       8                                                       
HET    MSE  E 374       8                                                       
HET    MSE  F   1       8                                                       
HET    MSE  F   8       8                                                       
HET    MSE  F  19       8                                                       
HET    MSE  F  67       8                                                       
HET    MSE  F  92       8                                                       
HET    MSE  F 104       8                                                       
HET    MSE  F 110       8                                                       
HET    MSE  F 149       8                                                       
HET    MSE  F 170       8                                                       
HET    MSE  F 186       8                                                       
HET    MSE  F 200       8                                                       
HET    MSE  F 268       8                                                       
HET    MSE  F 296       8                                                       
HET    MSE  F 333       8                                                       
HET    MSE  F 374       8                                                       
HET    MSE  G   1       8                                                       
HET    MSE  G   8       8                                                       
HET    MSE  G  19       8                                                       
HET    MSE  G  67       8                                                       
HET    MSE  G  92       8                                                       
HET    MSE  G 104       8                                                       
HET    MSE  G 110       8                                                       
HET    MSE  G 149       8                                                       
HET    MSE  G 170       8                                                       
HET    MSE  G 186       8                                                       
HET    MSE  G 200       8                                                       
HET    MSE  G 268       8                                                       
HET    MSE  G 296       8                                                       
HET    MSE  G 333       8                                                       
HET    MSE  G 374       8                                                       
HET    MSE  H   1       8                                                       
HET    MSE  H   8       8                                                       
HET    MSE  H  19       8                                                       
HET    MSE  H  67       8                                                       
HET    MSE  H  92       8                                                       
HET    MSE  H 104       8                                                       
HET    MSE  H 110       8                                                       
HET    MSE  H 149       8                                                       
HET    MSE  H 170       8                                                       
HET    MSE  H 186       8                                                       
HET    MSE  H 200       8                                                       
HET    MSE  H 268       8                                                       
HET    MSE  H 296       8                                                       
HET    MSE  H 333       8                                                       
HET    MSE  H 374       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    120(C5 H11 N O2 SE)                                          
FORMUL   9  HOH   *211(H2 O)                                                    
HELIX    1 AA1 GLU A    2  ASN A   14  1                                  13    
HELIX    2 AA2 SER A   17  ALA A   26  1                                  10    
HELIX    3 AA3 PRO A   31  HIS A   40  1                                  10    
HELIX    4 AA4 PHE A   48  TYR A   59  1                                  12    
HELIX    5 AA5 ARG A   62  ASN A   73  1                                  12    
HELIX    6 AA6 THR A   78  MSE A   92  1                                  15    
HELIX    7 AA7 PHE A   93  SER A  106  1                                  14    
HELIX    8 AA8 ASN A  109  ASN A  127  1                                  19    
HELIX    9 AA9 THR A  131  LEU A  142  1                                  12    
HELIX   10 AB1 THR A  146  THR A  164  1                                  19    
HELIX   11 AB2 PRO A  169  GLN A  176  1                                   8    
HELIX   12 AB3 ILE A  177  ILE A  182  5                                   6    
HELIX   13 AB4 ASN A  185  GLU A  207  1                                  23    
HELIX   14 AB5 SER A  209  SER A  223  1                                  15    
HELIX   15 AB6 ILE A  226  LEU A  242  1                                  17    
HELIX   16 AB7 ASN A  245  VAL A  261  1                                  17    
HELIX   17 AB8 ASN A  263  TRP A  281  1                                  19    
HELIX   18 AB9 SER A  294  PHE A  308  1                                  15    
HELIX   19 AC1 GLU A  310  LEU A  323  1                                  14    
HELIX   20 AC2 ASN A  327  GLN A  343  1                                  17    
HELIX   21 AC3 ASN A  344  SER A  358  1                                  15    
HELIX   22 AC4 ILE A  364  MSE A  374  1                                  11    
HELIX   23 AC5 ASN A  377  LEU A  384  1                                   8    
HELIX   24 AC6 GLU B    2  ASN B   14  1                                  13    
HELIX   25 AC7 SER B   17  ALA B   26  1                                  10    
HELIX   26 AC8 PRO B   31  HIS B   40  1                                  10    
HELIX   27 AC9 PHE B   48  TYR B   59  1                                  12    
HELIX   28 AD1 ARG B   62  ASN B   73  1                                  12    
HELIX   29 AD2 THR B   78  MSE B   92  1                                  15    
HELIX   30 AD3 PHE B   93  SER B  106  1                                  14    
HELIX   31 AD4 ASN B  109  ASN B  127  1                                  19    
HELIX   32 AD5 THR B  131  LYS B  141  1                                  11    
HELIX   33 AD6 THR B  146  THR B  164  1                                  19    
HELIX   34 AD7 PRO B  169  GLN B  176  1                                   8    
HELIX   35 AD8 ILE B  177  ILE B  182  5                                   6    
HELIX   36 AD9 ASN B  185  GLU B  207  1                                  23    
HELIX   37 AE1 SER B  209  SER B  223  1                                  15    
HELIX   38 AE2 ILE B  226  LEU B  242  1                                  17    
HELIX   39 AE3 ASN B  245  VAL B  261  1                                  17    
HELIX   40 AE4 ASN B  263  TRP B  281  1                                  19    
HELIX   41 AE5 SER B  294  PHE B  308  1                                  15    
HELIX   42 AE6 GLU B  310  LEU B  323  1                                  14    
HELIX   43 AE7 ASN B  327  GLN B  343  1                                  17    
HELIX   44 AE8 ASN B  344  SER B  358  1                                  15    
HELIX   45 AE9 ILE B  364  MSE B  374  1                                  11    
HELIX   46 AF1 ASN B  377  LEU B  384  1                                   8    
HELIX   47 AF2 GLU C    2  ASN C   14  1                                  13    
HELIX   48 AF3 SER C   17  ALA C   26  1                                  10    
HELIX   49 AF4 PRO C   31  HIS C   40  1                                  10    
HELIX   50 AF5 PHE C   48  TYR C   59  1                                  12    
HELIX   51 AF6 ARG C   62  ASN C   73  1                                  12    
HELIX   52 AF7 THR C   78  MSE C   92  1                                  15    
HELIX   53 AF8 PHE C   93  SER C  106  1                                  14    
HELIX   54 AF9 ASN C  109  ASN C  127  1                                  19    
HELIX   55 AG1 THR C  131  LYS C  141  1                                  11    
HELIX   56 AG2 THR C  146  THR C  164  1                                  19    
HELIX   57 AG3 PRO C  169  GLN C  176  1                                   8    
HELIX   58 AG4 ILE C  177  ILE C  182  5                                   6    
HELIX   59 AG5 ASN C  185  GLU C  207  1                                  23    
HELIX   60 AG6 SER C  209  SER C  223  1                                  15    
HELIX   61 AG7 ILE C  226  LEU C  242  1                                  17    
HELIX   62 AG8 ASN C  245  VAL C  261  1                                  17    
HELIX   63 AG9 ASN C  263  TRP C  281  1                                  19    
HELIX   64 AH1 SER C  294  PHE C  308  1                                  15    
HELIX   65 AH2 GLU C  310  LEU C  323  1                                  14    
HELIX   66 AH3 ASN C  327  GLN C  343  1                                  17    
HELIX   67 AH4 ASN C  344  SER C  358  1                                  15    
HELIX   68 AH5 ILE C  364  MSE C  374  1                                  11    
HELIX   69 AH6 ASN C  377  LEU C  384  1                                   8    
HELIX   70 AH7 GLU D    2  ASN D   14  1                                  13    
HELIX   71 AH8 SER D   17  ALA D   26  1                                  10    
HELIX   72 AH9 PRO D   31  HIS D   40  1                                  10    
HELIX   73 AI1 PHE D   48  TYR D   59  1                                  12    
HELIX   74 AI2 ARG D   62  ASN D   73  1                                  12    
HELIX   75 AI3 THR D   78  MSE D   92  1                                  15    
HELIX   76 AI4 PHE D   93  SER D  106  1                                  14    
HELIX   77 AI5 ASN D  109  ASN D  127  1                                  19    
HELIX   78 AI6 THR D  131  LYS D  141  1                                  11    
HELIX   79 AI7 THR D  146  THR D  164  1                                  19    
HELIX   80 AI8 PRO D  169  GLN D  176  1                                   8    
HELIX   81 AI9 ILE D  177  ILE D  182  5                                   6    
HELIX   82 AJ1 ASN D  185  GLU D  207  1                                  23    
HELIX   83 AJ2 SER D  209  SER D  223  1                                  15    
HELIX   84 AJ3 ILE D  226  LEU D  242  1                                  17    
HELIX   85 AJ4 ASN D  245  VAL D  261  1                                  17    
HELIX   86 AJ5 ASN D  263  TRP D  281  1                                  19    
HELIX   87 AJ6 SER D  294  PHE D  308  1                                  15    
HELIX   88 AJ7 GLU D  310  LEU D  323  1                                  14    
HELIX   89 AJ8 ASN D  327  GLN D  343  1                                  17    
HELIX   90 AJ9 ASN D  344  SER D  358  1                                  15    
HELIX   91 AK1 ILE D  364  MSE D  374  1                                  11    
HELIX   92 AK2 ASN D  377  LEU D  384  1                                   8    
HELIX   93 AK3 GLU E    2  ASN E   14  1                                  13    
HELIX   94 AK4 SER E   17  ALA E   26  1                                  10    
HELIX   95 AK5 PRO E   31  HIS E   40  1                                  10    
HELIX   96 AK6 PHE E   48  TYR E   59  1                                  12    
HELIX   97 AK7 ARG E   62  ASN E   73  1                                  12    
HELIX   98 AK8 THR E   78  MSE E   92  1                                  15    
HELIX   99 AK9 PHE E   93  SER E  106  1                                  14    
HELIX  100 AL1 ASN E  109  ASN E  127  1                                  19    
HELIX  101 AL2 THR E  131  LYS E  141  1                                  11    
HELIX  102 AL3 THR E  146  THR E  164  1                                  19    
HELIX  103 AL4 PRO E  169  GLN E  176  1                                   8    
HELIX  104 AL5 ILE E  177  ILE E  182  5                                   6    
HELIX  105 AL6 ASN E  185  GLU E  207  1                                  23    
HELIX  106 AL7 SER E  209  SER E  223  1                                  15    
HELIX  107 AL8 ILE E  226  LEU E  242  1                                  17    
HELIX  108 AL9 ASN E  245  VAL E  261  1                                  17    
HELIX  109 AM1 ASN E  263  TRP E  281  1                                  19    
HELIX  110 AM2 SER E  294  PHE E  308  1                                  15    
HELIX  111 AM3 GLU E  310  LEU E  323  1                                  14    
HELIX  112 AM4 ASN E  327  GLN E  343  1                                  17    
HELIX  113 AM5 ASN E  344  SER E  358  1                                  15    
HELIX  114 AM6 ILE E  364  MSE E  374  1                                  11    
HELIX  115 AM7 ASN E  377  LEU E  384  1                                   8    
HELIX  116 AM8 GLU F    2  ASN F   14  1                                  13    
HELIX  117 AM9 SER F   17  ALA F   26  1                                  10    
HELIX  118 AN1 PRO F   31  HIS F   40  1                                  10    
HELIX  119 AN2 PHE F   48  TYR F   59  1                                  12    
HELIX  120 AN3 ARG F   62  ASN F   73  1                                  12    
HELIX  121 AN4 THR F   78  ASN F   91  1                                  14    
HELIX  122 AN5 PHE F   93  SER F  106  1                                  14    
HELIX  123 AN6 ASN F  109  ASN F  127  1                                  19    
HELIX  124 AN7 THR F  131  LYS F  141  1                                  11    
HELIX  125 AN8 THR F  146  THR F  164  1                                  19    
HELIX  126 AN9 PRO F  169  GLN F  176  1                                   8    
HELIX  127 AO1 ILE F  177  ILE F  182  5                                   6    
HELIX  128 AO2 ASN F  185  GLU F  207  1                                  23    
HELIX  129 AO3 SER F  209  SER F  223  1                                  15    
HELIX  130 AO4 ILE F  226  LEU F  242  1                                  17    
HELIX  131 AO5 ASN F  245  VAL F  261  1                                  17    
HELIX  132 AO6 ASN F  263  TRP F  281  1                                  19    
HELIX  133 AO7 SER F  294  PHE F  308  1                                  15    
HELIX  134 AO8 GLU F  310  LEU F  323  1                                  14    
HELIX  135 AO9 ASN F  327  GLN F  343  1                                  17    
HELIX  136 AP1 ASN F  344  SER F  358  1                                  15    
HELIX  137 AP2 ILE F  364  MSE F  374  1                                  11    
HELIX  138 AP3 ASN F  377  LEU F  384  1                                   8    
HELIX  139 AP4 GLU G    2  ASN G   14  1                                  13    
HELIX  140 AP5 SER G   17  ALA G   26  1                                  10    
HELIX  141 AP6 PRO G   31  HIS G   40  1                                  10    
HELIX  142 AP7 PHE G   48  TYR G   59  1                                  12    
HELIX  143 AP8 ARG G   62  ASN G   73  1                                  12    
HELIX  144 AP9 THR G   78  MSE G   92  1                                  15    
HELIX  145 AQ1 PHE G   93  SER G  106  1                                  14    
HELIX  146 AQ2 ASN G  109  ASN G  127  1                                  19    
HELIX  147 AQ3 THR G  131  LYS G  141  1                                  11    
HELIX  148 AQ4 THR G  146  THR G  164  1                                  19    
HELIX  149 AQ5 PRO G  169  GLN G  176  1                                   8    
HELIX  150 AQ6 ILE G  177  ILE G  182  5                                   6    
HELIX  151 AQ7 ASN G  185  GLU G  207  1                                  23    
HELIX  152 AQ8 SER G  209  SER G  223  1                                  15    
HELIX  153 AQ9 ILE G  226  LEU G  242  1                                  17    
HELIX  154 AR1 ASN G  245  VAL G  261  1                                  17    
HELIX  155 AR2 ASN G  263  TRP G  281  1                                  19    
HELIX  156 AR3 SER G  294  PHE G  308  1                                  15    
HELIX  157 AR4 GLU G  310  LEU G  323  1                                  14    
HELIX  158 AR5 ASN G  327  GLN G  343  1                                  17    
HELIX  159 AR6 ASN G  344  SER G  358  1                                  15    
HELIX  160 AR7 ILE G  364  MSE G  374  1                                  11    
HELIX  161 AR8 ASN G  377  LEU G  384  1                                   8    
HELIX  162 AR9 GLU H    2  GLU H   13  1                                  12    
HELIX  163 AS1 SER H   17  ALA H   26  1                                  10    
HELIX  164 AS2 PRO H   31  HIS H   40  1                                  10    
HELIX  165 AS3 PHE H   48  TYR H   59  1                                  12    
HELIX  166 AS4 ARG H   62  ASN H   73  1                                  12    
HELIX  167 AS5 THR H   78  MSE H   92  1                                  15    
HELIX  168 AS6 PHE H   93  SER H  106  1                                  14    
HELIX  169 AS7 ASN H  109  ASN H  127  1                                  19    
HELIX  170 AS8 THR H  131  LYS H  141  1                                  11    
HELIX  171 AS9 THR H  146  THR H  164  1                                  19    
HELIX  172 AT1 PRO H  169  GLN H  176  1                                   8    
HELIX  173 AT2 ILE H  177  ILE H  182  5                                   6    
HELIX  174 AT3 ASN H  185  GLU H  207  1                                  23    
HELIX  175 AT4 SER H  209  SER H  223  1                                  15    
HELIX  176 AT5 ILE H  226  LEU H  242  1                                  17    
HELIX  177 AT6 ASN H  245  VAL H  261  1                                  17    
HELIX  178 AT7 ASN H  263  TRP H  281  1                                  19    
HELIX  179 AT8 SER H  294  PHE H  308  1                                  15    
HELIX  180 AT9 GLU H  310  LEU H  323  1                                  14    
HELIX  181 AU1 ASN H  327  GLN H  343  1                                  17    
HELIX  182 AU2 ASN H  344  SER H  358  1                                  15    
HELIX  183 AU3 ILE H  364  MSE H  374  1                                  11    
HELIX  184 AU4 ASN H  377  LEU H  384  1                                   8    
LINK         C   MSE A   1                 N   GLU A   2     1555   1555  1.33  
LINK         C   ALA A   7                 N   MSE A   8     1555   1555  1.34  
LINK         C   MSE A   8                 N   LYS A   9     1555   1555  1.34  
LINK         C   LEU A  18                 N   MSE A  19     1555   1555  1.33  
LINK         C   MSE A  19                 N   ASN A  20     1555   1555  1.35  
LINK         C   LEU A  66                 N   MSE A  67     1555   1555  1.34  
LINK         C   MSE A  67                 N   LYS A  68     1555   1555  1.34  
LINK         C   ASN A  91                 N   MSE A  92     1555   1555  1.33  
LINK         C   MSE A  92                 N   PHE A  93     1555   1555  1.33  
LINK         C   SER A 103                 N   MSE A 104     1555   1555  1.33  
LINK         C   MSE A 104                 N   ILE A 105     1555   1555  1.35  
LINK         C   ASN A 109                 N   MSE A 110     1555   1555  1.32  
LINK         C   MSE A 110                 N   LYS A 111     1555   1555  1.35  
LINK         C   GLU A 148                 N   MSE A 149     1555   1555  1.35  
LINK         C   MSE A 149                 N   ASN A 150     1555   1555  1.33  
LINK         C   PRO A 169                 N   MSE A 170     1555   1555  1.33  
LINK         C   MSE A 170                 N   ALA A 171     1555   1555  1.34  
LINK         C   ASN A 185                 N   MSE A 186     1555   1555  1.33  
LINK         C   MSE A 186                 N   TYR A 187     1555   1555  1.34  
LINK         C   LEU A 199                 N   MSE A 200     1555   1555  1.34  
LINK         C   MSE A 200                 N   SER A 201     1555   1555  1.35  
LINK         C   ASN A 267                 N   MSE A 268     1555   1555  1.32  
LINK         C   MSE A 268                 N   ILE A 269     1555   1555  1.34  
LINK         C   ILE A 295                 N   MSE A 296     1555   1555  1.34  
LINK         C   MSE A 296                 N   ASP A 297     1555   1555  1.34  
LINK         C   ALA A 332                 N   MSE A 333     1555   1555  1.34  
LINK         C   MSE A 333                 N   HIS A 334     1555   1555  1.33  
LINK         C   LYS A 373                 N   MSE A 374     1555   1555  1.32  
LINK         C   MSE A 374                 N   GLY A 375     1555   1555  1.34  
LINK         C   MSE B   1                 N   GLU B   2     1555   1555  1.33  
LINK         C   ALA B   7                 N   MSE B   8     1555   1555  1.34  
LINK         C   MSE B   8                 N   LYS B   9     1555   1555  1.34  
LINK         C   LEU B  18                 N   MSE B  19     1555   1555  1.34  
LINK         C   MSE B  19                 N   ASN B  20     1555   1555  1.35  
LINK         C   LEU B  66                 N   MSE B  67     1555   1555  1.33  
LINK         C   MSE B  67                 N   LYS B  68     1555   1555  1.34  
LINK         C   ASN B  91                 N   MSE B  92     1555   1555  1.33  
LINK         C   MSE B  92                 N   PHE B  93     1555   1555  1.34  
LINK         C   SER B 103                 N   MSE B 104     1555   1555  1.33  
LINK         C   MSE B 104                 N   ILE B 105     1555   1555  1.35  
LINK         C   ASN B 109                 N   MSE B 110     1555   1555  1.34  
LINK         C   MSE B 110                 N   LYS B 111     1555   1555  1.34  
LINK         C   GLU B 148                 N   MSE B 149     1555   1555  1.34  
LINK         C   MSE B 149                 N   ASN B 150     1555   1555  1.33  
LINK         C   PRO B 169                 N   MSE B 170     1555   1555  1.34  
LINK         C   MSE B 170                 N   ALA B 171     1555   1555  1.35  
LINK         C   ASN B 185                 N   MSE B 186     1555   1555  1.33  
LINK         C   MSE B 186                 N   TYR B 187     1555   1555  1.33  
LINK         C   LEU B 199                 N   MSE B 200     1555   1555  1.36  
LINK         C   MSE B 200                 N   SER B 201     1555   1555  1.34  
LINK         C   ASN B 267                 N   MSE B 268     1555   1555  1.34  
LINK         C   MSE B 268                 N   ILE B 269     1555   1555  1.33  
LINK         C   ILE B 295                 N   MSE B 296     1555   1555  1.34  
LINK         C   MSE B 296                 N   ASP B 297     1555   1555  1.33  
LINK         C   ALA B 332                 N   MSE B 333     1555   1555  1.35  
LINK         C   MSE B 333                 N   HIS B 334     1555   1555  1.34  
LINK         C   LYS B 373                 N   MSE B 374     1555   1555  1.32  
LINK         C   MSE B 374                 N   GLY B 375     1555   1555  1.33  
LINK         C   MSE C   1                 N   GLU C   2     1555   1555  1.34  
LINK         C   ALA C   7                 N   MSE C   8     1555   1555  1.33  
LINK         C   MSE C   8                 N   LYS C   9     1555   1555  1.34  
LINK         C   LEU C  18                 N   MSE C  19     1555   1555  1.34  
LINK         C   MSE C  19                 N   ASN C  20     1555   1555  1.35  
LINK         C   LEU C  66                 N   MSE C  67     1555   1555  1.33  
LINK         C   MSE C  67                 N   LYS C  68     1555   1555  1.33  
LINK         C   ASN C  91                 N   MSE C  92     1555   1555  1.32  
LINK         C   MSE C  92                 N   PHE C  93     1555   1555  1.33  
LINK         C   SER C 103                 N   MSE C 104     1555   1555  1.33  
LINK         C   MSE C 104                 N   ILE C 105     1555   1555  1.34  
LINK         C   ASN C 109                 N   MSE C 110     1555   1555  1.34  
LINK         C   MSE C 110                 N   LYS C 111     1555   1555  1.34  
LINK         C   GLU C 148                 N   MSE C 149     1555   1555  1.34  
LINK         C   MSE C 149                 N   ASN C 150     1555   1555  1.33  
LINK         C   PRO C 169                 N   MSE C 170     1555   1555  1.34  
LINK         C   MSE C 170                 N   ALA C 171     1555   1555  1.34  
LINK         C   ASN C 185                 N   MSE C 186     1555   1555  1.32  
LINK         C   MSE C 186                 N   TYR C 187     1555   1555  1.34  
LINK         C   LEU C 199                 N   MSE C 200     1555   1555  1.35  
LINK         C   MSE C 200                 N   SER C 201     1555   1555  1.33  
LINK         C   ASN C 267                 N   MSE C 268     1555   1555  1.32  
LINK         C   MSE C 268                 N   ILE C 269     1555   1555  1.32  
LINK         C   ILE C 295                 N   MSE C 296     1555   1555  1.33  
LINK         C   MSE C 296                 N   ASP C 297     1555   1555  1.33  
LINK         C   ALA C 332                 N   MSE C 333     1555   1555  1.33  
LINK         C   MSE C 333                 N   HIS C 334     1555   1555  1.33  
LINK         C   LYS C 373                 N   MSE C 374     1555   1555  1.32  
LINK         C   MSE C 374                 N   GLY C 375     1555   1555  1.33  
LINK         C   MSE D   1                 N   GLU D   2     1555   1555  1.37  
LINK         C   ALA D   7                 N   MSE D   8     1555   1555  1.34  
LINK         C   MSE D   8                 N   LYS D   9     1555   1555  1.34  
LINK         C   LEU D  18                 N   MSE D  19     1555   1555  1.35  
LINK         C   MSE D  19                 N   ASN D  20     1555   1555  1.34  
LINK         C   LEU D  66                 N   MSE D  67     1555   1555  1.34  
LINK         C   MSE D  67                 N   LYS D  68     1555   1555  1.34  
LINK         C   ASN D  91                 N   MSE D  92     1555   1555  1.33  
LINK         C   MSE D  92                 N   PHE D  93     1555   1555  1.33  
LINK         C   SER D 103                 N   MSE D 104     1555   1555  1.33  
LINK         C   MSE D 104                 N   ILE D 105     1555   1555  1.34  
LINK         C   ASN D 109                 N   MSE D 110     1555   1555  1.33  
LINK         C   MSE D 110                 N   LYS D 111     1555   1555  1.34  
LINK         C   GLU D 148                 N   MSE D 149     1555   1555  1.34  
LINK         C   MSE D 149                 N   ASN D 150     1555   1555  1.33  
LINK         C   PRO D 169                 N   MSE D 170     1555   1555  1.33  
LINK         C   MSE D 170                 N   ALA D 171     1555   1555  1.34  
LINK         C   ASN D 185                 N   MSE D 186     1555   1555  1.32  
LINK         C   MSE D 186                 N   TYR D 187     1555   1555  1.34  
LINK         C   LEU D 199                 N   MSE D 200     1555   1555  1.35  
LINK         C   MSE D 200                 N   SER D 201     1555   1555  1.34  
LINK         C   ASN D 267                 N   MSE D 268     1555   1555  1.34  
LINK         C   MSE D 268                 N   ILE D 269     1555   1555  1.33  
LINK         C   ILE D 295                 N   MSE D 296     1555   1555  1.33  
LINK         C   MSE D 296                 N   ASP D 297     1555   1555  1.34  
LINK         C   ALA D 332                 N   MSE D 333     1555   1555  1.33  
LINK         C   MSE D 333                 N   HIS D 334     1555   1555  1.33  
LINK         C   LYS D 373                 N   MSE D 374     1555   1555  1.33  
LINK         C   MSE D 374                 N   GLY D 375     1555   1555  1.33  
LINK         C   MSE E   1                 N   GLU E   2     1555   1555  1.34  
LINK         C   ALA E   7                 N   MSE E   8     1555   1555  1.34  
LINK         C   MSE E   8                 N   LYS E   9     1555   1555  1.34  
LINK         C   LEU E  18                 N   MSE E  19     1555   1555  1.35  
LINK         C   MSE E  19                 N   ASN E  20     1555   1555  1.34  
LINK         C   LEU E  66                 N   MSE E  67     1555   1555  1.33  
LINK         C   MSE E  67                 N   LYS E  68     1555   1555  1.34  
LINK         C   ASN E  91                 N   MSE E  92     1555   1555  1.33  
LINK         C   MSE E  92                 N   PHE E  93     1555   1555  1.33  
LINK         C   SER E 103                 N   MSE E 104     1555   1555  1.33  
LINK         C   MSE E 104                 N   ILE E 105     1555   1555  1.34  
LINK         C   ASN E 109                 N   MSE E 110     1555   1555  1.34  
LINK         C   MSE E 110                 N   LYS E 111     1555   1555  1.33  
LINK         C   GLU E 148                 N   MSE E 149     1555   1555  1.34  
LINK         C   MSE E 149                 N   ASN E 150     1555   1555  1.33  
LINK         C   PRO E 169                 N   MSE E 170     1555   1555  1.34  
LINK         C   MSE E 170                 N   ALA E 171     1555   1555  1.33  
LINK         C   ASN E 185                 N   MSE E 186     1555   1555  1.32  
LINK         C   MSE E 186                 N   TYR E 187     1555   1555  1.32  
LINK         C   LEU E 199                 N   MSE E 200     1555   1555  1.34  
LINK         C   MSE E 200                 N   SER E 201     1555   1555  1.34  
LINK         C   ASN E 267                 N   MSE E 268     1555   1555  1.34  
LINK         C   MSE E 268                 N   ILE E 269     1555   1555  1.34  
LINK         C   ILE E 295                 N   MSE E 296     1555   1555  1.33  
LINK         C   MSE E 296                 N   ASP E 297     1555   1555  1.34  
LINK         C   ALA E 332                 N   MSE E 333     1555   1555  1.33  
LINK         C   MSE E 333                 N   HIS E 334     1555   1555  1.34  
LINK         C   LYS E 373                 N   MSE E 374     1555   1555  1.33  
LINK         C   MSE E 374                 N   GLY E 375     1555   1555  1.34  
LINK         C   MSE F   1                 N   GLU F   2     1555   1555  1.34  
LINK         C   ALA F   7                 N   MSE F   8     1555   1555  1.33  
LINK         C   MSE F   8                 N   LYS F   9     1555   1555  1.34  
LINK         C   LEU F  18                 N   MSE F  19     1555   1555  1.34  
LINK         C   MSE F  19                 N   ASN F  20     1555   1555  1.35  
LINK         C   LEU F  66                 N   MSE F  67     1555   1555  1.34  
LINK         C   MSE F  67                 N   LYS F  68     1555   1555  1.34  
LINK         C   ASN F  91                 N   MSE F  92     1555   1555  1.33  
LINK         C   MSE F  92                 N   PHE F  93     1555   1555  1.33  
LINK         C   SER F 103                 N   MSE F 104     1555   1555  1.33  
LINK         C   MSE F 104                 N   ILE F 105     1555   1555  1.34  
LINK         C   ASN F 109                 N   MSE F 110     1555   1555  1.33  
LINK         C   MSE F 110                 N   LYS F 111     1555   1555  1.34  
LINK         C   GLU F 148                 N   MSE F 149     1555   1555  1.34  
LINK         C   MSE F 149                 N   ASN F 150     1555   1555  1.33  
LINK         C   PRO F 169                 N   MSE F 170     1555   1555  1.35  
LINK         C   MSE F 170                 N   ALA F 171     1555   1555  1.33  
LINK         C   ASN F 185                 N   MSE F 186     1555   1555  1.33  
LINK         C   MSE F 186                 N   TYR F 187     1555   1555  1.34  
LINK         C   LEU F 199                 N   MSE F 200     1555   1555  1.35  
LINK         C   MSE F 200                 N   SER F 201     1555   1555  1.36  
LINK         C   ASN F 267                 N   MSE F 268     1555   1555  1.33  
LINK         C   MSE F 268                 N   ILE F 269     1555   1555  1.34  
LINK         C   ILE F 295                 N   MSE F 296     1555   1555  1.33  
LINK         C   MSE F 296                 N   ASP F 297     1555   1555  1.33  
LINK         C   ALA F 332                 N   MSE F 333     1555   1555  1.34  
LINK         C   MSE F 333                 N   HIS F 334     1555   1555  1.34  
LINK         C   LYS F 373                 N   MSE F 374     1555   1555  1.33  
LINK         C   MSE F 374                 N   GLY F 375     1555   1555  1.34  
LINK         C   MSE G   1                 N   GLU G   2     1555   1555  1.34  
LINK         C   ALA G   7                 N   MSE G   8     1555   1555  1.34  
LINK         C   MSE G   8                 N   LYS G   9     1555   1555  1.34  
LINK         C   LEU G  18                 N   MSE G  19     1555   1555  1.35  
LINK         C   MSE G  19                 N   ASN G  20     1555   1555  1.34  
LINK         C   LEU G  66                 N   MSE G  67     1555   1555  1.33  
LINK         C   MSE G  67                 N   LYS G  68     1555   1555  1.33  
LINK         C   ASN G  91                 N   MSE G  92     1555   1555  1.33  
LINK         C   MSE G  92                 N   PHE G  93     1555   1555  1.33  
LINK         C   SER G 103                 N   MSE G 104     1555   1555  1.33  
LINK         C   MSE G 104                 N   ILE G 105     1555   1555  1.34  
LINK         C   ASN G 109                 N   MSE G 110     1555   1555  1.34  
LINK         C   MSE G 110                 N   LYS G 111     1555   1555  1.34  
LINK         C   GLU G 148                 N   MSE G 149     1555   1555  1.34  
LINK         C   MSE G 149                 N   ASN G 150     1555   1555  1.33  
LINK         C   PRO G 169                 N   MSE G 170     1555   1555  1.35  
LINK         C   MSE G 170                 N   ALA G 171     1555   1555  1.33  
LINK         C   ASN G 185                 N   MSE G 186     1555   1555  1.33  
LINK         C   MSE G 186                 N   TYR G 187     1555   1555  1.33  
LINK         C   LEU G 199                 N   MSE G 200     1555   1555  1.35  
LINK         C   MSE G 200                 N   SER G 201     1555   1555  1.35  
LINK         C   ASN G 267                 N   MSE G 268     1555   1555  1.33  
LINK         C   MSE G 268                 N   ILE G 269     1555   1555  1.34  
LINK         C   ILE G 295                 N   MSE G 296     1555   1555  1.33  
LINK         C   MSE G 296                 N   ASP G 297     1555   1555  1.34  
LINK         C   ALA G 332                 N   MSE G 333     1555   1555  1.34  
LINK         C   MSE G 333                 N   HIS G 334     1555   1555  1.34  
LINK         C   LYS G 373                 N   MSE G 374     1555   1555  1.32  
LINK         C   MSE G 374                 N   GLY G 375     1555   1555  1.33  
LINK         C   MSE H   1                 N   GLU H   2     1555   1555  1.34  
LINK         C   ALA H   7                 N   MSE H   8     1555   1555  1.33  
LINK         C   MSE H   8                 N   LYS H   9     1555   1555  1.35  
LINK         C   LEU H  18                 N   MSE H  19     1555   1555  1.35  
LINK         C   MSE H  19                 N   ASN H  20     1555   1555  1.34  
LINK         C   LEU H  66                 N   MSE H  67     1555   1555  1.34  
LINK         C   MSE H  67                 N   LYS H  68     1555   1555  1.34  
LINK         C   ASN H  91                 N   MSE H  92     1555   1555  1.32  
LINK         C   MSE H  92                 N   PHE H  93     1555   1555  1.33  
LINK         C   SER H 103                 N   MSE H 104     1555   1555  1.33  
LINK         C   MSE H 104                 N   ILE H 105     1555   1555  1.34  
LINK         C   ASN H 109                 N   MSE H 110     1555   1555  1.33  
LINK         C   MSE H 110                 N   LYS H 111     1555   1555  1.33  
LINK         C   GLU H 148                 N   MSE H 149     1555   1555  1.34  
LINK         C   MSE H 149                 N   ASN H 150     1555   1555  1.32  
LINK         C   PRO H 169                 N   MSE H 170     1555   1555  1.34  
LINK         C   MSE H 170                 N   ALA H 171     1555   1555  1.33  
LINK         C   ASN H 185                 N   MSE H 186     1555   1555  1.34  
LINK         C   MSE H 186                 N   TYR H 187     1555   1555  1.34  
LINK         C   LEU H 199                 N   MSE H 200     1555   1555  1.34  
LINK         C   MSE H 200                 N   SER H 201     1555   1555  1.34  
LINK         C   ASN H 267                 N   MSE H 268     1555   1555  1.33  
LINK         C   MSE H 268                 N   ILE H 269     1555   1555  1.32  
LINK         C   ILE H 295                 N   MSE H 296     1555   1555  1.34  
LINK         C   MSE H 296                 N   ASP H 297     1555   1555  1.33  
LINK         C   ALA H 332                 N   MSE H 333     1555   1555  1.33  
LINK         C   MSE H 333                 N   HIS H 334     1555   1555  1.34  
LINK         C   LYS H 373                 N   MSE H 374     1555   1555  1.33  
LINK         C   MSE H 374                 N   GLY H 375     1555   1555  1.34  
CRYST1   78.907  251.202   95.077  90.00  90.89  90.00 P 1 21 1     16          
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      0.012673  0.000000  0.000198        0.00000                         
SCALE2      0.000000  0.003981  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010519        0.00000                         
HETATM    1  N   MSE A   1     -24.925  11.411 -44.180  1.00 68.13           N  
ANISOU    1  N   MSE A   1     8744   7809   9331    216   -489   -236       N  
HETATM    2  CA  MSE A   1     -24.468  11.217 -42.750  1.00 70.57           C  
ANISOU    2  CA  MSE A   1     9080   8090   9643    194   -445   -176       C  
HETATM    3  C   MSE A   1     -23.151  11.957 -42.504  1.00 71.74           C  
ANISOU    3  C   MSE A   1     9265   8271   9719    211   -447   -124       C  
HETATM    4  O   MSE A   1     -22.181  11.832 -43.307  1.00 72.65           O  
ANISOU    4  O   MSE A   1     9392   8410   9800    235   -470   -129       O  
HETATM    5  CB  MSE A   1     -24.340   9.729 -42.429  1.00 71.28           C  
ANISOU    5  CB  MSE A   1     9169   8125   9788    181   -422   -180       C  
HETATM    6  CG  MSE A   1     -24.400   9.453 -40.921  1.00 73.49           C  
ANISOU    6  CG  MSE A   1     9468   8366  10087    152   -374   -130       C  
HETATM    7 SE   MSE A   1     -23.846   7.539 -40.404  1.00 77.42          SE  
ANISOU    7 SE   MSE A   1     9982   8789  10642    140   -346   -115      SE  
HETATM    8  CE  MSE A   1     -25.519   6.574 -40.850  1.00 70.48           C  
ANISOU    8  CE  MSE A   1     9051   7863   9864    110   -338   -187       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system