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Entry: 4KQM
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HEADER    TRANSFERASE                             15-MAY-13   4KQM              
TITLE     CRYSTAL STRUCTURE OF YEAST GLYCOGEN SYNTHASE E169Q MUTANT IN COMPLEX  
TITLE    2 WITH GLUCOSE AND UDP                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GSY2P;                                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 764101;                                              
SOURCE   5 STRAIN: STRAIN ATCC 204508 / S288C;                                  
SOURCE   6 GENE: FOSTERSO_3265, GSY2 YLR258W L8479.8;                           
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    GLUCOSYLTRANSFERASE, ROSSMAN FOLD, GT-B, TRANSFERASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.M.CHIKWANA,T.D.HURLEY                                               
REVDAT   2   05-FEB-14 4KQM    1       JRNL                                     
REVDAT   1   11-DEC-13 4KQM    0                                                
JRNL        AUTH   V.M.CHIKWANA,M.KHANNA,S.BASKARAN,V.S.TAGLIABRACCI,           
JRNL        AUTH 2 C.J.CONTRERAS,A.DEPAOLI-ROACH,P.J.ROACH,T.D.HURLEY           
JRNL        TITL   STRUCTURAL BASIS FOR 2'-PHOSPHATE INCORPORATION INTO         
JRNL        TITL 2 GLYCOGEN BY GLYCOGEN SYNTHASE.                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 20976 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24324135                                                     
JRNL        DOI    10.1073/PNAS.1310106111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.41                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 102101                         
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5074                            
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) : 2.77                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6544                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 359                          
REMARK   3   BIN FREE R VALUE                    : 0.3470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20603                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 216                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.38000                                             
REMARK   3    B22 (A**2) : 9.56000                                              
REMARK   3    B33 (A**2) : -6.18000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.701         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.316         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.235         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.257        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21324 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28903 ; 1.256 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2546 ; 5.370 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1075 ;36.216 ;23.498       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3583 ;18.839 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   164 ;19.347 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3144 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16297 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A     205      4                      
REMARK   3           1     B      2       B     205      4                      
REMARK   3           1     C      2       C     205      4                      
REMARK   3           1     D      2       D     205      4                      
REMARK   3           2     A    208       A     278      4                      
REMARK   3           2     B    208       B     278      4                      
REMARK   3           2     C    208       C     278      4                      
REMARK   3           2     D    208       D     278      4                      
REMARK   3           3     A    599       A     639      4                      
REMARK   3           3     B    599       B     639      4                      
REMARK   3           3     C    599       C     639      4                      
REMARK   3           3     D    599       D     639      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2528 ; 0.430 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   2528 ; 0.380 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   2528 ; 0.450 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   2528 ; 0.380 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2528 ; 4.820 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2528 ; 8.690 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   2528 ; 5.670 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   2528 ; 8.220 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    279       A     598      4                      
REMARK   3           1     B    279       B     598      4                      
REMARK   3           1     C    279       C     598      4                      
REMARK   3           1     D    279       D     598      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   2598 ; 0.290 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   2598 ; 0.320 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):   2598 ; 0.350 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):   2598 ; 0.320 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    A (A**2):   2598 ; 2.170 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   2598 ; 2.400 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    C (A**2):   2598 ; 2.320 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    D (A**2):   2598 ; 2.080 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
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     2        A   140                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.1341  67.5167 141.6572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8328 T22:   0.2098                                     
REMARK   3      T33:   0.5239 T12:   0.0824                                     
REMARK   3      T13:   0.1340 T23:   0.2401                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4724 L22:   3.4405                                     
REMARK   3      L33:   2.6689 L12:  -0.0630                                     
REMARK   3      L13:  -0.4427 L23:   0.5289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0964 S12:   1.0331 S13:   0.9991                       
REMARK   3      S21:  -0.8933 S22:   0.0270 S23:  -0.2037                       
REMARK   3      S31:  -0.7651 S32:   0.0564 S33:  -0.1234                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   141        A   277                          
REMARK   3    ORIGIN FOR THE GROUP (A):  80.0918  50.6217 146.7869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4756 T22:   0.4005                                     
REMARK   3      T33:   0.4828 T12:   0.0891                                     
REMARK   3      T13:   0.0099 T23:   0.0700                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8708 L22:   2.0899                                     
REMARK   3      L33:   1.3413 L12:  -1.0869                                     
REMARK   3      L13:   0.2486 L23:   0.3185                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2806 S12:   0.3301 S13:   0.0071                       
REMARK   3      S21:  -0.0730 S22:  -0.0083 S23:  -0.3254                       
REMARK   3      S31:  -0.1276 S32:   0.4487 S33:  -0.2724                       
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 :   A   278        A   533                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.5578  37.4718 111.8038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5329 T22:   0.3374                                     
REMARK   3      T33:   0.6640 T12:   0.1542                                     
REMARK   3      T13:  -0.0368 T23:  -0.0678                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0687 L22:   0.3341                                     
REMARK   3      L33:   0.9067 L12:  -0.2174                                     
REMARK   3      L13:   0.7458 L23:  -0.1796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0444 S12:   0.0766 S13:  -0.2215                       
REMARK   3      S21:  -0.0323 S22:   0.0460 S23:  -0.0681                       
REMARK   3      S31:   0.1911 S32:   0.2494 S33:  -0.0904                       
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 :   A   534        A   639                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.1504  40.3775 144.2442              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5578 T22:   0.3695                                     
REMARK   3      T33:   0.6172 T12:   0.1677                                     
REMARK   3      T13:  -0.0886 T23:   0.0654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6886 L22:   0.8538                                     
REMARK   3      L33:   2.9491 L12:   0.7187                                     
REMARK   3      L13:   1.2197 L23:   1.1351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1196 S12:  -0.1647 S13:  -0.1033                       
REMARK   3      S21:   0.0712 S22:  -0.1131 S23:   0.0362                       
REMARK   3      S31:   0.1208 S32:  -0.2723 S33:  -0.0065                       
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 :   B     2        B   140                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9096 105.2138  86.2858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5232 T22:   0.0789                                     
REMARK   3      T33:   1.0040 T12:   0.0152                                     
REMARK   3      T13:  -0.4073 T23:  -0.0850                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1073 L22:   4.0499                                     
REMARK   3      L33:   2.2543 L12:  -0.2011                                     
REMARK   3      L13:   1.4472 L23:  -0.4453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4704 S12:  -0.5766 S13:   0.9378                       
REMARK   3      S21:   0.8372 S22:   0.0492 S23:  -1.1481                       
REMARK   3      S31:  -0.3402 S32:  -0.0354 S33:   0.4212                       
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 :   B   141        B   277                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9009  99.5837  72.6217              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4336 T22:   0.0653                                     
REMARK   3      T33:   0.7013 T12:   0.0047                                     
REMARK   3      T13:  -0.0397 T23:   0.1032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5272 L22:   2.4396                                     
REMARK   3      L33:   0.6640 L12:  -1.1372                                     
REMARK   3      L13:   0.3188 L23:  -0.1678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1071 S12:   0.3482 S13:   0.5771                       
REMARK   3      S21:  -0.1604 S22:  -0.0956 S23:  -0.2420                       
REMARK   3      S31:  -0.2618 S32:   0.1073 S33:   0.2027                       
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 :   B   278        B   533                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4965  58.5775  85.8175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4402 T22:   0.1706                                     
REMARK   3      T33:   0.4970 T12:   0.0254                                     
REMARK   3      T13:  -0.0021 T23:  -0.0439                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9268 L22:   0.6072                                     
REMARK   3      L33:   0.8097 L12:  -0.3693                                     
REMARK   3      L13:   0.3224 L23:  -0.2464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0115 S12:   0.0416 S13:  -0.0683                       
REMARK   3      S21:  -0.0718 S22:   0.0731 S23:  -0.0347                       
REMARK   3      S31:   0.1149 S32:  -0.0525 S33:  -0.0846                       
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 :   B   534        B   639                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.6151  82.2620  64.0816              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4785 T22:   0.3385                                     
REMARK   3      T33:   0.6261 T12:   0.0228                                     
REMARK   3      T13:   0.1027 T23:   0.1650                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1540 L22:   3.7998                                     
REMARK   3      L33:   0.6665 L12:  -0.5298                                     
REMARK   3      L13:   0.1669 L23:   0.0053                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0128 S12:   0.5985 S13:   0.4471                       
REMARK   3      S21:  -0.5249 S22:  -0.0573 S23:  -0.5773                       
REMARK   3      S31:  -0.0410 S32:   0.1336 S33:   0.0445                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   141                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.9979  25.2319  65.1168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4764 T22:   0.2592                                     
REMARK   3      T33:   0.6013 T12:   0.0281                                     
REMARK   3      T13:   0.0875 T23:   0.2566                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6607 L22:   3.5456                                     
REMARK   3      L33:   2.9169 L12:   0.5614                                     
REMARK   3      L13:   0.2212 L23:   0.1758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1427 S12:  -0.9300 S13:  -1.0837                       
REMARK   3      S21:   0.4656 S22:  -0.2047 S23:   0.0020                       
REMARK   3      S31:   0.7206 S32:   0.1109 S33:   0.0619                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   142        C   277                          
REMARK   3    ORIGIN FOR THE GROUP (A):  74.2892  37.3682  57.0473              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4169 T22:   0.3904                                     
REMARK   3      T33:   0.4117 T12:   0.1606                                     
REMARK   3      T13:   0.0429 T23:   0.0378                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1135 L22:   2.0256                                     
REMARK   3      L33:   1.4868 L12:   0.8111                                     
REMARK   3      L13:  -0.2486 L23:   0.4672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0024 S12:  -0.3304 S13:  -0.4481                       
REMARK   3      S21:  -0.1132 S22:   0.0883 S23:  -0.3135                       
REMARK   3      S31:   0.1659 S32:   0.4774 S33:  -0.0908                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   278        C   533                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.0932  60.4132  90.0036              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4586 T22:   0.4156                                     
REMARK   3      T33:   0.6182 T12:   0.0212                                     
REMARK   3      T13:   0.0140 T23:  -0.0928                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7502 L22:   0.1806                                     
REMARK   3      L33:   1.1481 L12:  -0.1607                                     
REMARK   3      L13:  -0.4924 L23:   0.2480                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0196 S12:  -0.0273 S13:   0.0784                       
REMARK   3      S21:   0.0316 S22:   0.0848 S23:  -0.1143                       
REMARK   3      S31:  -0.0856 S32:   0.4091 S33:  -0.0652                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   534        C   639                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.2551  55.8959  58.6306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4732 T22:   0.4515                                     
REMARK   3      T33:   0.4921 T12:   0.0250                                     
REMARK   3      T13:   0.0630 T23:  -0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5524 L22:   2.0541                                     
REMARK   3      L33:   2.4122 L12:  -0.2774                                     
REMARK   3      L13:  -0.1554 L23:   1.8254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0107 S12:   0.0826 S13:   0.1234                       
REMARK   3      S21:  -0.3036 S22:  -0.1428 S23:   0.1099                       
REMARK   3      S31:  -0.3083 S32:   0.0698 S33:   0.1322                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   141                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0112  16.5413 117.9623              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0635 T22:   0.2533                                     
REMARK   3      T33:   1.0190 T12:  -0.3673                                     
REMARK   3      T13:   0.0776 T23:  -0.0741                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6255 L22:   4.3876                                     
REMARK   3      L33:   2.2841 L12:  -0.5909                                     
REMARK   3      L13:  -0.2195 L23:   0.8440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0207 S12:   0.5033 S13:  -0.9521                       
REMARK   3      S21:  -0.6752 S22:   0.0795 S23:   0.1532                       
REMARK   3      S31:   0.3273 S32:  -0.2198 S33:  -0.0588                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   142        D   278                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7474  25.4139 132.2947              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8828 T22:   0.6282                                     
REMARK   3      T33:   1.0064 T12:  -0.3933                                     
REMARK   3      T13:   0.1374 T23:   0.1749                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0261 L22:   1.8487                                     
REMARK   3      L33:   0.9973 L12:  -0.0001                                     
REMARK   3      L13:   0.8539 L23:   0.6031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0784 S12:  -0.5477 S13:  -0.5709                       
REMARK   3      S21:   0.3749 S22:  -0.0661 S23:   0.6435                       
REMARK   3      S31:   0.5337 S32:  -0.6421 S33:   0.1445                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   279        D   533                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5672  59.7326 117.7317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4498 T22:   0.2083                                     
REMARK   3      T33:   0.4938 T12:   0.0591                                     
REMARK   3      T13:  -0.0267 T23:  -0.0254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2427 L22:   0.2597                                     
REMARK   3      L33:   1.2864 L12:   0.0241                                     
REMARK   3      L13:  -0.4118 L23:  -0.0141                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0241 S12:  -0.2000 S13:  -0.0131                       
REMARK   3      S21:   0.0204 S22:   0.0538 S23:  -0.0571                       
REMARK   3      S31:   0.0122 S32:  -0.1031 S33:  -0.0297                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   534        D   639                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7219  35.7340 139.3985              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7099 T22:   0.5480                                     
REMARK   3      T33:   0.6656 T12:  -0.0053                                     
REMARK   3      T13:   0.0160 T23:   0.2287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7391 L22:   1.9695                                     
REMARK   3      L33:   1.5767 L12:   0.7306                                     
REMARK   3      L13:  -0.1099 L23:  -0.1895                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1213 S12:  -0.5492 S13:  -0.6598                       
REMARK   3      S21:   0.4057 S22:   0.0873 S23:  -0.1960                       
REMARK   3      S31:   0.5818 S32:  -0.3190 S33:   0.0340                       
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 4KQM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079671.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 102312                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49500                            
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: PDB ENTRY 3NB0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 16% PEG 300, PH 6.2,     
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       96.35500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      102.22150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      103.16600            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       96.35500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      102.22150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      103.16600            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       96.35500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      102.22150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      103.16600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       96.35500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      102.22150            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      103.16600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 98380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     VAL A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A   640                                                      
REMARK 465     GLY A   641                                                      
REMARK 465     LYS A   642                                                      
REMARK 465     LYS A   643                                                      
REMARK 465     LEU A   644                                                      
REMARK 465     LYS A   645                                                      
REMARK 465     VAL A   646                                                      
REMARK 465     ALA A   647                                                      
REMARK 465     ARG A   648                                                      
REMARK 465     PRO A   649                                                      
REMARK 465     LEU A   650                                                      
REMARK 465     SER A   651                                                      
REMARK 465     VAL A   652                                                      
REMARK 465     PRO A   653                                                      
REMARK 465     GLY A   654                                                      
REMARK 465     SER A   655                                                      
REMARK 465     PRO A   656                                                      
REMARK 465     ARG A   657                                                      
REMARK 465     ASP A   658                                                      
REMARK 465     LEU A   659                                                      
REMARK 465     ARG A   660                                                      
REMARK 465     SER A   661                                                      
REMARK 465     ASN A   662                                                      
REMARK 465     SER A   663                                                      
REMARK 465     THR A   664                                                      
REMARK 465     VAL A   665                                                      
REMARK 465     TYR A   666                                                      
REMARK 465     MET A   667                                                      
REMARK 465     THR A   668                                                      
REMARK 465     PRO A   669                                                      
REMARK 465     GLY A   670                                                      
REMARK 465     ASP A   671                                                      
REMARK 465     LEU A   672                                                      
REMARK 465     GLY A   673                                                      
REMARK 465     THR A   674                                                      
REMARK 465     LEU A   675                                                      
REMARK 465     GLN A   676                                                      
REMARK 465     GLU A   677                                                      
REMARK 465     VAL A   678                                                      
REMARK 465     ASN A   679                                                      
REMARK 465     ASN A   680                                                      
REMARK 465     ALA A   681                                                      
REMARK 465     ASP A   682                                                      
REMARK 465     ASP A   683                                                      
REMARK 465     TYR A   684                                                      
REMARK 465     PHE A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     LEU A   687                                                      
REMARK 465     GLY A   688                                                      
REMARK 465     VAL A   689                                                      
REMARK 465     ASN A   690                                                      
REMARK 465     PRO A   691                                                      
REMARK 465     ALA A   692                                                      
REMARK 465     ALA A   693                                                      
REMARK 465     ASP A   694                                                      
REMARK 465     ASP A   695                                                      
REMARK 465     ASP A   696                                                      
REMARK 465     ASP A   697                                                      
REMARK 465     ASP A   698                                                      
REMARK 465     GLY A   699                                                      
REMARK 465     PRO A   700                                                      
REMARK 465     TYR A   701                                                      
REMARK 465     ALA A   702                                                      
REMARK 465     ASP A   703                                                      
REMARK 465     ASP A   704                                                      
REMARK 465     SER A   705                                                      
REMARK 465     MET B   -18                                                      
REMARK 465     GLY B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     VAL B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     ARG B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B   640                                                      
REMARK 465     GLY B   641                                                      
REMARK 465     LYS B   642                                                      
REMARK 465     LYS B   643                                                      
REMARK 465     LEU B   644                                                      
REMARK 465     LYS B   645                                                      
REMARK 465     VAL B   646                                                      
REMARK 465     ALA B   647                                                      
REMARK 465     ARG B   648                                                      
REMARK 465     PRO B   649                                                      
REMARK 465     LEU B   650                                                      
REMARK 465     SER B   651                                                      
REMARK 465     VAL B   652                                                      
REMARK 465     PRO B   653                                                      
REMARK 465     GLY B   654                                                      
REMARK 465     SER B   655                                                      
REMARK 465     PRO B   656                                                      
REMARK 465     ARG B   657                                                      
REMARK 465     ASP B   658                                                      
REMARK 465     LEU B   659                                                      
REMARK 465     ARG B   660                                                      
REMARK 465     SER B   661                                                      
REMARK 465     ASN B   662                                                      
REMARK 465     SER B   663                                                      
REMARK 465     THR B   664                                                      
REMARK 465     VAL B   665                                                      
REMARK 465     TYR B   666                                                      
REMARK 465     MET B   667                                                      
REMARK 465     THR B   668                                                      
REMARK 465     PRO B   669                                                      
REMARK 465     GLY B   670                                                      
REMARK 465     ASP B   671                                                      
REMARK 465     LEU B   672                                                      
REMARK 465     GLY B   673                                                      
REMARK 465     THR B   674                                                      
REMARK 465     LEU B   675                                                      
REMARK 465     GLN B   676                                                      
REMARK 465     GLU B   677                                                      
REMARK 465     VAL B   678                                                      
REMARK 465     ASN B   679                                                      
REMARK 465     ASN B   680                                                      
REMARK 465     ALA B   681                                                      
REMARK 465     ASP B   682                                                      
REMARK 465     ASP B   683                                                      
REMARK 465     TYR B   684                                                      
REMARK 465     PHE B   685                                                      
REMARK 465     SER B   686                                                      
REMARK 465     LEU B   687                                                      
REMARK 465     GLY B   688                                                      
REMARK 465     VAL B   689                                                      
REMARK 465     ASN B   690                                                      
REMARK 465     PRO B   691                                                      
REMARK 465     ALA B   692                                                      
REMARK 465     ALA B   693                                                      
REMARK 465     ASP B   694                                                      
REMARK 465     ASP B   695                                                      
REMARK 465     ASP B   696                                                      
REMARK 465     ASP B   697                                                      
REMARK 465     ASP B   698                                                      
REMARK 465     GLY B   699                                                      
REMARK 465     PRO B   700                                                      
REMARK 465     TYR B   701                                                      
REMARK 465     ALA B   702                                                      
REMARK 465     ASP B   703                                                      
REMARK 465     ASP B   704                                                      
REMARK 465     SER B   705                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     GLY C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     SER C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     SER C    -7                                                      
REMARK 465     GLY C    -6                                                      
REMARK 465     LEU C    -5                                                      
REMARK 465     VAL C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     ARG C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C   640                                                      
REMARK 465     GLY C   641                                                      
REMARK 465     LYS C   642                                                      
REMARK 465     LYS C   643                                                      
REMARK 465     LEU C   644                                                      
REMARK 465     LYS C   645                                                      
REMARK 465     VAL C   646                                                      
REMARK 465     ALA C   647                                                      
REMARK 465     ARG C   648                                                      
REMARK 465     PRO C   649                                                      
REMARK 465     LEU C   650                                                      
REMARK 465     SER C   651                                                      
REMARK 465     VAL C   652                                                      
REMARK 465     PRO C   653                                                      
REMARK 465     GLY C   654                                                      
REMARK 465     SER C   655                                                      
REMARK 465     PRO C   656                                                      
REMARK 465     ARG C   657                                                      
REMARK 465     ASP C   658                                                      
REMARK 465     LEU C   659                                                      
REMARK 465     ARG C   660                                                      
REMARK 465     SER C   661                                                      
REMARK 465     ASN C   662                                                      
REMARK 465     SER C   663                                                      
REMARK 465     THR C   664                                                      
REMARK 465     VAL C   665                                                      
REMARK 465     TYR C   666                                                      
REMARK 465     MET C   667                                                      
REMARK 465     THR C   668                                                      
REMARK 465     PRO C   669                                                      
REMARK 465     GLY C   670                                                      
REMARK 465     ASP C   671                                                      
REMARK 465     LEU C   672                                                      
REMARK 465     GLY C   673                                                      
REMARK 465     THR C   674                                                      
REMARK 465     LEU C   675                                                      
REMARK 465     GLN C   676                                                      
REMARK 465     GLU C   677                                                      
REMARK 465     VAL C   678                                                      
REMARK 465     ASN C   679                                                      
REMARK 465     ASN C   680                                                      
REMARK 465     ALA C   681                                                      
REMARK 465     ASP C   682                                                      
REMARK 465     ASP C   683                                                      
REMARK 465     TYR C   684                                                      
REMARK 465     PHE C   685                                                      
REMARK 465     SER C   686                                                      
REMARK 465     LEU C   687                                                      
REMARK 465     GLY C   688                                                      
REMARK 465     VAL C   689                                                      
REMARK 465     ASN C   690                                                      
REMARK 465     PRO C   691                                                      
REMARK 465     ALA C   692                                                      
REMARK 465     ALA C   693                                                      
REMARK 465     ASP C   694                                                      
REMARK 465     ASP C   695                                                      
REMARK 465     ASP C   696                                                      
REMARK 465     ASP C   697                                                      
REMARK 465     ASP C   698                                                      
REMARK 465     GLY C   699                                                      
REMARK 465     PRO C   700                                                      
REMARK 465     TYR C   701                                                      
REMARK 465     ALA C   702                                                      
REMARK 465     ASP C   703                                                      
REMARK 465     ASP C   704                                                      
REMARK 465     SER C   705                                                      
REMARK 465     MET D   -18                                                      
REMARK 465     GLY D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     SER D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     SER D    -7                                                      
REMARK 465     GLY D    -6                                                      
REMARK 465     LEU D    -5                                                      
REMARK 465     VAL D    -4                                                      
REMARK 465     PRO D    -3                                                      
REMARK 465     ARG D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D   206                                                      
REMARK 465     PHE D   207                                                      
REMARK 465     ASP D   208                                                      
REMARK 465     GLY D   640                                                      
REMARK 465     GLY D   641                                                      
REMARK 465     LYS D   642                                                      
REMARK 465     LYS D   643                                                      
REMARK 465     LEU D   644                                                      
REMARK 465     LYS D   645                                                      
REMARK 465     VAL D   646                                                      
REMARK 465     ALA D   647                                                      
REMARK 465     ARG D   648                                                      
REMARK 465     PRO D   649                                                      
REMARK 465     LEU D   650                                                      
REMARK 465     SER D   651                                                      
REMARK 465     VAL D   652                                                      
REMARK 465     PRO D   653                                                      
REMARK 465     GLY D   654                                                      
REMARK 465     SER D   655                                                      
REMARK 465     PRO D   656                                                      
REMARK 465     ARG D   657                                                      
REMARK 465     ASP D   658                                                      
REMARK 465     LEU D   659                                                      
REMARK 465     ARG D   660                                                      
REMARK 465     SER D   661                                                      
REMARK 465     ASN D   662                                                      
REMARK 465     SER D   663                                                      
REMARK 465     THR D   664                                                      
REMARK 465     VAL D   665                                                      
REMARK 465     TYR D   666                                                      
REMARK 465     MET D   667                                                      
REMARK 465     THR D   668                                                      
REMARK 465     PRO D   669                                                      
REMARK 465     GLY D   670                                                      
REMARK 465     ASP D   671                                                      
REMARK 465     LEU D   672                                                      
REMARK 465     GLY D   673                                                      
REMARK 465     THR D   674                                                      
REMARK 465     LEU D   675                                                      
REMARK 465     GLN D   676                                                      
REMARK 465     GLU D   677                                                      
REMARK 465     VAL D   678                                                      
REMARK 465     ASN D   679                                                      
REMARK 465     ASN D   680                                                      
REMARK 465     ALA D   681                                                      
REMARK 465     ASP D   682                                                      
REMARK 465     ASP D   683                                                      
REMARK 465     TYR D   684                                                      
REMARK 465     PHE D   685                                                      
REMARK 465     SER D   686                                                      
REMARK 465     LEU D   687                                                      
REMARK 465     GLY D   688                                                      
REMARK 465     VAL D   689                                                      
REMARK 465     ASN D   690                                                      
REMARK 465     PRO D   691                                                      
REMARK 465     ALA D   692                                                      
REMARK 465     ALA D   693                                                      
REMARK 465     ASP D   694                                                      
REMARK 465     ASP D   695                                                      
REMARK 465     ASP D   696                                                      
REMARK 465     ASP D   697                                                      
REMARK 465     ASP D   698                                                      
REMARK 465     GLY D   699                                                      
REMARK 465     PRO D   700                                                      
REMARK 465     TYR D   701                                                      
REMARK 465     ALA D   702                                                      
REMARK 465     ASP D   703                                                      
REMARK 465     ASP D   704                                                      
REMARK 465     SER D   705                                                      
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   OG   SER D    85     OG   SER D    85     2555     1.92            
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    VAL A  21      -30.68   -131.19                                   
REMARK 500    LYS A  40     -115.83     59.61                                   
REMARK 500    VAL A 111       -2.96   -155.58                                   
REMARK 500    GLN A 169      155.54     66.09                                   
REMARK 500    ARG A 183       64.19     36.16                                   
REMARK 500    ALA A 194      175.81    172.24                                   
REMARK 500    SER A 204     -145.97    -90.26                                   
REMARK 500    TYR A 228      -54.46    -26.59                                   
REMARK 500    CYS A 304       30.12   -152.28                                   
REMARK 500    ASN A 362       42.70   -105.15                                   
REMARK 500    SER A 363     -175.48     79.29                                   
REMARK 500    ALA A 483      -18.67    -48.90                                   
REMARK 500    TRP A 511      -72.89   -126.45                                   
REMARK 500    LYS B  40     -115.40     54.05                                   
REMARK 500    SER B 110        1.39    -69.65                                   
REMARK 500    SER B 130       86.71   -158.74                                   
REMARK 500    GLN B 169      157.91     68.03                                   
REMARK 500    ALA B 194      177.25    171.95                                   
REMARK 500    CYS B 304       21.50   -148.77                                   
REMARK 500    SER B 363      177.78     72.83                                   
REMARK 500    GLN B 463       35.26     72.44                                   
REMARK 500    ALA B 483       -9.14    -55.07                                   
REMARK 500    GLU B 509       87.44   -166.98                                   
REMARK 500    TRP B 511      -97.24   -108.32                                   
REMARK 500    VAL C  21      -50.14   -121.15                                   
REMARK 500    LYS C  40     -118.89     57.48                                   
REMARK 500    GLU C  57      -20.56   -143.13                                   
REMARK 500    SER C 110        8.18    -64.62                                   
REMARK 500    VAL C 126      -35.22   -136.08                                   
REMARK 500    GLN C 169      149.09     68.40                                   
REMARK 500    ALA C 194     -165.24   -178.77                                   
REMARK 500    CYS C 212       22.64   -143.14                                   
REMARK 500    CYS C 304       26.56   -148.54                                   
REMARK 500    SER C 363      178.18     76.41                                   
REMARK 500    PRO C 401       40.88   -103.55                                   
REMARK 500    ASP C 449       65.54   -119.57                                   
REMARK 500    TRP C 511      -80.64   -137.74                                   
REMARK 500    THR C 527     -166.93   -125.75                                   
REMARK 500    LYS D  40     -107.32     59.73                                   
REMARK 500    SER D 110       41.46    -92.50                                   
REMARK 500    VAL D 111       -4.28   -162.67                                   
REMARK 500    SER D 115      -67.60    -26.81                                   
REMARK 500    ASN D 133        0.93    -67.88                                   
REMARK 500    GLN D 169      162.75     63.12                                   
REMARK 500    ALA D 194      170.75    176.05                                   
REMARK 500    ALA D 203       29.17    -73.52                                   
REMARK 500    SER D 204     -113.54   -132.89                                   
REMARK 500    SER D 363     -173.66     75.09                                   
REMARK 500    PRO D 478       49.22    -73.47                                   
REMARK 500    GLU D 479      136.45   -170.95                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS C 220        22.0      L          L   OUTSIDE RANGE           
REMARK 500    THR C 543        24.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC C 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP C 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P C 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP D 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G6P D 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 803                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KQ1   RELATED DB: PDB                                   
REMARK 900 ACTIVATED STATE OF YEAST GLYCOGEN SYNTHASE (GSY2P) UMP               
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 4KQ2   RELATED DB: PDB                                   
REMARK 900 GLUCOSE1,2CYCLIC PHOSPHATE BOUND ACTIVATED STATE OF YEAST            
REMARK 900 GLYCOGEN SYNTHASE'                                                   
DBREF  4KQM A    1   705  UNP    E7NKU1   E7NKU1_YEASO     1    705             
DBREF  4KQM B    1   705  UNP    E7NKU1   E7NKU1_YEASO     1    705             
DBREF  4KQM C    1   705  UNP    E7NKU1   E7NKU1_YEASO     1    705             
DBREF  4KQM D    1   705  UNP    E7NKU1   E7NKU1_YEASO     1    705             
SEQADV 4KQM MET A  -18  UNP  E7NKU1              INITIATING METHIONINE          
SEQADV 4KQM GLY A  -17  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER A  -16  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER A  -15  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS A  -14  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS A  -13  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS A  -12  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS A  -11  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS A  -10  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS A   -9  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER A   -8  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER A   -7  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLY A   -6  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM LEU A   -5  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM VAL A   -4  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM PRO A   -3  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM ARG A   -2  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLY A   -1  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER A    0  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLN A  169  UNP  E7NKU1    GLU   169 ENGINEERED MUTATION            
SEQADV 4KQM MET B  -18  UNP  E7NKU1              INITIATING METHIONINE          
SEQADV 4KQM GLY B  -17  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER B  -16  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER B  -15  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS B  -14  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS B  -13  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS B  -12  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS B  -11  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS B  -10  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS B   -9  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER B   -8  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER B   -7  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLY B   -6  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM LEU B   -5  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM VAL B   -4  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM PRO B   -3  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM ARG B   -2  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLY B   -1  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER B    0  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLN B  169  UNP  E7NKU1    GLU   169 ENGINEERED MUTATION            
SEQADV 4KQM MET C  -18  UNP  E7NKU1              INITIATING METHIONINE          
SEQADV 4KQM GLY C  -17  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER C  -16  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER C  -15  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS C  -14  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS C  -13  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS C  -12  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS C  -11  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS C  -10  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS C   -9  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER C   -8  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER C   -7  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLY C   -6  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM LEU C   -5  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM VAL C   -4  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM PRO C   -3  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM ARG C   -2  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLY C   -1  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER C    0  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLN C  169  UNP  E7NKU1    GLU   169 ENGINEERED MUTATION            
SEQADV 4KQM MET D  -18  UNP  E7NKU1              INITIATING METHIONINE          
SEQADV 4KQM GLY D  -17  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER D  -16  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER D  -15  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS D  -14  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS D  -13  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS D  -12  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS D  -11  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS D  -10  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM HIS D   -9  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER D   -8  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER D   -7  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLY D   -6  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM LEU D   -5  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM VAL D   -4  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM PRO D   -3  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM ARG D   -2  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLY D   -1  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM SER D    0  UNP  E7NKU1              EXPRESSION TAG                 
SEQADV 4KQM GLN D  169  UNP  E7NKU1    GLU   169 ENGINEERED MUTATION            
SEQRES   1 A  724  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  724  LEU VAL PRO ARG GLY SER MET SER ARG ASP LEU GLN ASN          
SEQRES   3 A  724  HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN ARG          
SEQRES   4 A  724  VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA PRO          
SEQRES   5 A  724  ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU ILE          
SEQRES   6 A  724  GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL ASP          
SEQRES   7 A  724  ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP GLU          
SEQRES   8 A  724  MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU SER          
SEQRES   9 A  724  ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE GLU          
SEQRES  10 A  724  GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER VAL          
SEQRES  11 A  724  ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP SER          
SEQRES  12 A  724  LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU THR          
SEQRES  13 A  724  ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP PHE          
SEQRES  14 A  724  LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA ILE          
SEQRES  15 A  724  VAL ALA HIS PHE HIS GLN TRP LEU ALA GLY VAL ALA LEU          
SEQRES  16 A  724  PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR ILE          
SEQRES  17 A  724  PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU CYS          
SEQRES  18 A  724  ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU SER          
SEQRES  19 A  724  VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE TYR          
SEQRES  20 A  724  HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER ALA          
SEQRES  21 A  724  ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE GLU          
SEQRES  22 A  724  ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE LEU          
SEQRES  23 A  724  PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE HIS          
SEQRES  24 A  724  GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS ILE          
SEQRES  25 A  724  ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE ASP          
SEQRES  26 A  724  PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA GLY          
SEQRES  27 A  724  ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE ILE          
SEQRES  28 A  724  GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL SER          
SEQRES  29 A  724  GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET PRO          
SEQRES  30 A  724  ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS GLY          
SEQRES  31 A  724  GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS GLU          
SEQRES  32 A  724  VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS ALA          
SEQRES  33 A  724  ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU PRO          
SEQRES  34 A  724  THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS VAL          
SEQRES  35 A  724  MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO GLU          
SEQRES  36 A  724  GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL ASP          
SEQRES  37 A  724  ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN VAL          
SEQRES  38 A  724  GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET ILE          
SEQRES  39 A  724  PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE LEU          
SEQRES  40 A  724  GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS LEU          
SEQRES  41 A  724  GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR THR          
SEQRES  42 A  724  PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE THR          
SEQRES  43 A  724  THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP LEU          
SEQRES  44 A  724  ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR ILE          
SEQRES  45 A  724  VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL GLU          
SEQRES  46 A  724  GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS THR          
SEQRES  47 A  724  ARG ARG GLN ARG ILE ASN GLN ARG ASN ARG THR GLU ARG          
SEQRES  48 A  724  LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU GLU          
SEQRES  49 A  724  TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY TYR          
SEQRES  50 A  724  PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU ASN          
SEQRES  51 A  724  ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS LEU          
SEQRES  52 A  724  LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO ARG          
SEQRES  53 A  724  ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO GLY          
SEQRES  54 A  724  ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP ASP          
SEQRES  55 A  724  TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP ASP          
SEQRES  56 A  724  ASP ASP GLY PRO TYR ALA ASP ASP SER                          
SEQRES   1 B  724  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  724  LEU VAL PRO ARG GLY SER MET SER ARG ASP LEU GLN ASN          
SEQRES   3 B  724  HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN ARG          
SEQRES   4 B  724  VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA PRO          
SEQRES   5 B  724  ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU ILE          
SEQRES   6 B  724  GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL ASP          
SEQRES   7 B  724  ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP GLU          
SEQRES   8 B  724  MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU SER          
SEQRES   9 B  724  ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE GLU          
SEQRES  10 B  724  GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER VAL          
SEQRES  11 B  724  ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP SER          
SEQRES  12 B  724  LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU THR          
SEQRES  13 B  724  ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP PHE          
SEQRES  14 B  724  LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA ILE          
SEQRES  15 B  724  VAL ALA HIS PHE HIS GLN TRP LEU ALA GLY VAL ALA LEU          
SEQRES  16 B  724  PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR ILE          
SEQRES  17 B  724  PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU CYS          
SEQRES  18 B  724  ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU SER          
SEQRES  19 B  724  VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE TYR          
SEQRES  20 B  724  HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER ALA          
SEQRES  21 B  724  ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE GLU          
SEQRES  22 B  724  ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE LEU          
SEQRES  23 B  724  PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE HIS          
SEQRES  24 B  724  GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS ILE          
SEQRES  25 B  724  ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE ASP          
SEQRES  26 B  724  PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA GLY          
SEQRES  27 B  724  ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE ILE          
SEQRES  28 B  724  GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL SER          
SEQRES  29 B  724  GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET PRO          
SEQRES  30 B  724  ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS GLY          
SEQRES  31 B  724  GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS GLU          
SEQRES  32 B  724  VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS ALA          
SEQRES  33 B  724  ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU PRO          
SEQRES  34 B  724  THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS VAL          
SEQRES  35 B  724  MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO GLU          
SEQRES  36 B  724  GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL ASP          
SEQRES  37 B  724  ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN VAL          
SEQRES  38 B  724  GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET ILE          
SEQRES  39 B  724  PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE LEU          
SEQRES  40 B  724  GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS LEU          
SEQRES  41 B  724  GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR THR          
SEQRES  42 B  724  PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE THR          
SEQRES  43 B  724  THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP LEU          
SEQRES  44 B  724  ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR ILE          
SEQRES  45 B  724  VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL GLU          
SEQRES  46 B  724  GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS THR          
SEQRES  47 B  724  ARG ARG GLN ARG ILE ASN GLN ARG ASN ARG THR GLU ARG          
SEQRES  48 B  724  LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU GLU          
SEQRES  49 B  724  TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY TYR          
SEQRES  50 B  724  PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU ASN          
SEQRES  51 B  724  ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS LEU          
SEQRES  52 B  724  LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO ARG          
SEQRES  53 B  724  ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO GLY          
SEQRES  54 B  724  ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP ASP          
SEQRES  55 B  724  TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP ASP          
SEQRES  56 B  724  ASP ASP GLY PRO TYR ALA ASP ASP SER                          
SEQRES   1 C  724  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  724  LEU VAL PRO ARG GLY SER MET SER ARG ASP LEU GLN ASN          
SEQRES   3 C  724  HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN ARG          
SEQRES   4 C  724  VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA PRO          
SEQRES   5 C  724  ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU ILE          
SEQRES   6 C  724  GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL ASP          
SEQRES   7 C  724  ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP GLU          
SEQRES   8 C  724  MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU SER          
SEQRES   9 C  724  ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE GLU          
SEQRES  10 C  724  GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER VAL          
SEQRES  11 C  724  ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP SER          
SEQRES  12 C  724  LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU THR          
SEQRES  13 C  724  ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP PHE          
SEQRES  14 C  724  LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA ILE          
SEQRES  15 C  724  VAL ALA HIS PHE HIS GLN TRP LEU ALA GLY VAL ALA LEU          
SEQRES  16 C  724  PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR ILE          
SEQRES  17 C  724  PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU CYS          
SEQRES  18 C  724  ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU SER          
SEQRES  19 C  724  VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE TYR          
SEQRES  20 C  724  HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER ALA          
SEQRES  21 C  724  ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE GLU          
SEQRES  22 C  724  ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE LEU          
SEQRES  23 C  724  PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE HIS          
SEQRES  24 C  724  GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS ILE          
SEQRES  25 C  724  ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE ASP          
SEQRES  26 C  724  PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA GLY          
SEQRES  27 C  724  ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE ILE          
SEQRES  28 C  724  GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL SER          
SEQRES  29 C  724  GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET PRO          
SEQRES  30 C  724  ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS GLY          
SEQRES  31 C  724  GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS GLU          
SEQRES  32 C  724  VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS ALA          
SEQRES  33 C  724  ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU PRO          
SEQRES  34 C  724  THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS VAL          
SEQRES  35 C  724  MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO GLU          
SEQRES  36 C  724  GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL ASP          
SEQRES  37 C  724  ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN VAL          
SEQRES  38 C  724  GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET ILE          
SEQRES  39 C  724  PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE LEU          
SEQRES  40 C  724  GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS LEU          
SEQRES  41 C  724  GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR THR          
SEQRES  42 C  724  PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE THR          
SEQRES  43 C  724  THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP LEU          
SEQRES  44 C  724  ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR ILE          
SEQRES  45 C  724  VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL GLU          
SEQRES  46 C  724  GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS THR          
SEQRES  47 C  724  ARG ARG GLN ARG ILE ASN GLN ARG ASN ARG THR GLU ARG          
SEQRES  48 C  724  LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU GLU          
SEQRES  49 C  724  TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY TYR          
SEQRES  50 C  724  PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU ASN          
SEQRES  51 C  724  ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS LEU          
SEQRES  52 C  724  LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO ARG          
SEQRES  53 C  724  ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO GLY          
SEQRES  54 C  724  ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP ASP          
SEQRES  55 C  724  TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP ASP          
SEQRES  56 C  724  ASP ASP GLY PRO TYR ALA ASP ASP SER                          
SEQRES   1 D  724  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  724  LEU VAL PRO ARG GLY SER MET SER ARG ASP LEU GLN ASN          
SEQRES   3 D  724  HIS LEU LEU PHE GLU THR ALA THR GLU VAL ALA ASN ARG          
SEQRES   4 D  724  VAL GLY GLY ILE TYR SER VAL LEU LYS SER LYS ALA PRO          
SEQRES   5 D  724  ILE THR VAL ALA GLN TYR LYS ASP HIS TYR HIS LEU ILE          
SEQRES   6 D  724  GLY PRO LEU ASN LYS ALA THR TYR GLN ASN GLU VAL ASP          
SEQRES   7 D  724  ILE LEU ASP TRP LYS LYS PRO GLU ALA PHE SER ASP GLU          
SEQRES   8 D  724  MET ARG PRO VAL GLN HIS ALA LEU GLN THR MET GLU SER          
SEQRES   9 D  724  ARG GLY VAL HIS PHE VAL TYR GLY ARG TRP LEU ILE GLU          
SEQRES  10 D  724  GLY ALA PRO LYS VAL ILE LEU PHE ASP LEU ASP SER VAL          
SEQRES  11 D  724  ARG GLY TYR SER ASN GLU TRP LYS GLY ASP LEU TRP SER          
SEQRES  12 D  724  LEU VAL GLY ILE PRO SER PRO GLU ASN ASP PHE GLU THR          
SEQRES  13 D  724  ASN ASP ALA ILE LEU LEU GLY TYR THR VAL ALA TRP PHE          
SEQRES  14 D  724  LEU GLY GLU VAL ALA HIS LEU ASP SER GLN HIS ALA ILE          
SEQRES  15 D  724  VAL ALA HIS PHE HIS GLN TRP LEU ALA GLY VAL ALA LEU          
SEQRES  16 D  724  PRO LEU CYS ARG LYS ARG ARG ILE ASP VAL VAL THR ILE          
SEQRES  17 D  724  PHE THR THR HIS ALA THR LEU LEU GLY ARG TYR LEU CYS          
SEQRES  18 D  724  ALA SER GLY SER PHE ASP PHE TYR ASN CYS LEU GLU SER          
SEQRES  19 D  724  VAL ASP VAL ASP HIS GLU ALA GLY ARG PHE GLY ILE TYR          
SEQRES  20 D  724  HIS ARG TYR CYS ILE GLU ARG ALA ALA ALA HIS SER ALA          
SEQRES  21 D  724  ASP VAL PHE THR THR VAL SER GLN ILE THR ALA PHE GLU          
SEQRES  22 D  724  ALA GLU HIS LEU LEU LYS ARG LYS PRO ASP GLY ILE LEU          
SEQRES  23 D  724  PRO ASN GLY LEU ASN VAL ILE LYS PHE GLN ALA PHE HIS          
SEQRES  24 D  724  GLU PHE GLN ASN LEU HIS ALA LEU LYS LYS GLU LYS ILE          
SEQRES  25 D  724  ASN ASP PHE VAL ARG GLY HIS PHE HIS GLY CYS PHE ASP          
SEQRES  26 D  724  PHE ASP LEU ASP ASN THR LEU TYR PHE PHE ILE ALA GLY          
SEQRES  27 D  724  ARG TYR GLU TYR LYS ASN LYS GLY ALA ASP MET PHE ILE          
SEQRES  28 D  724  GLU ALA LEU ALA ARG LEU ASN TYR ARG LEU LYS VAL SER          
SEQRES  29 D  724  GLY SER LYS LYS THR VAL VAL ALA PHE ILE VAL MET PRO          
SEQRES  30 D  724  ALA LYS ASN ASN SER PHE THR VAL GLU ALA LEU LYS GLY          
SEQRES  31 D  724  GLN ALA GLU VAL ARG ALA LEU GLU ASN THR VAL HIS GLU          
SEQRES  32 D  724  VAL THR THR SER ILE GLY LYS ARG ILE PHE ASP HIS ALA          
SEQRES  33 D  724  ILE ARG TYR PRO HIS ASN GLY LEU THR THR GLU LEU PRO          
SEQRES  34 D  724  THR ASP LEU GLY GLU LEU LEU LYS SER SER ASP LYS VAL          
SEQRES  35 D  724  MET LEU LYS ARG ARG ILE LEU ALA LEU ARG ARG PRO GLU          
SEQRES  36 D  724  GLY GLN LEU PRO PRO ILE VAL THR HIS ASN MET VAL ASP          
SEQRES  37 D  724  ASP ALA ASN ASP LEU ILE LEU ASN LYS ILE ARG GLN VAL          
SEQRES  38 D  724  GLN LEU PHE ASN SER PRO SER ASP ARG VAL LYS MET ILE          
SEQRES  39 D  724  PHE HIS PRO GLU PHE LEU ASN ALA ASN ASN PRO ILE LEU          
SEQRES  40 D  724  GLY LEU ASP TYR ASP GLU PHE VAL ARG GLY CYS HIS LEU          
SEQRES  41 D  724  GLY VAL PHE PRO SER TYR TYR GLU PRO TRP GLY TYR THR          
SEQRES  42 D  724  PRO ALA GLU CYS THR VAL MET GLY VAL PRO SER ILE THR          
SEQRES  43 D  724  THR ASN VAL SER GLY PHE GLY SER TYR MET GLU ASP LEU          
SEQRES  44 D  724  ILE GLU THR ASN GLN ALA LYS ASP TYR GLY ILE TYR ILE          
SEQRES  45 D  724  VAL ASP ARG ARG PHE LYS ALA PRO ASP GLU SER VAL GLU          
SEQRES  46 D  724  GLN LEU VAL ASP TYR MET GLU GLU PHE VAL LYS LYS THR          
SEQRES  47 D  724  ARG ARG GLN ARG ILE ASN GLN ARG ASN ARG THR GLU ARG          
SEQRES  48 D  724  LEU SER ASP LEU LEU ASP TRP LYS ARG MET GLY LEU GLU          
SEQRES  49 D  724  TYR VAL LYS ALA ARG GLN LEU ALA LEU ARG ARG GLY TYR          
SEQRES  50 D  724  PRO ASP GLN PHE ARG GLU LEU VAL GLY GLU GLU LEU ASN          
SEQRES  51 D  724  ASP SER ASN MET ASP ALA LEU ALA GLY GLY LYS LYS LEU          
SEQRES  52 D  724  LYS VAL ALA ARG PRO LEU SER VAL PRO GLY SER PRO ARG          
SEQRES  53 D  724  ASP LEU ARG SER ASN SER THR VAL TYR MET THR PRO GLY          
SEQRES  54 D  724  ASP LEU GLY THR LEU GLN GLU VAL ASN ASN ALA ASP ASP          
SEQRES  55 D  724  TYR PHE SER LEU GLY VAL ASN PRO ALA ALA ASP ASP ASP          
SEQRES  56 D  724  ASP ASP GLY PRO TYR ALA ASP ASP SER                          
HET    UDP  A 801      25                                                       
HET    G6P  A 802      16                                                       
HET    PEG  A 803       7                                                       
HET    UDP  B 801      25                                                       
HET    G6P  B 802      16                                                       
HET    PEG  B 803       7                                                       
HET    GLC  C 801      12                                                       
HET    BGC  C 802      12                                                       
HET    UDP  C 803      25                                                       
HET    G6P  C 804      16                                                       
HET    PEG  C 805       7                                                       
HET    UDP  D 801      25                                                       
HET    G6P  D 802      16                                                       
HET    PEG  D 803       7                                                       
HETNAM     UDP URIDINE-5'-DIPHOSPHATE                                           
HETNAM     G6P ALPHA-D-GLUCOSE-6-PHOSPHATE                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     BGC BETA-D-GLUCOSE                                                   
FORMUL   5  UDP    4(C9 H14 N2 O12 P2)                                          
FORMUL   6  G6P    4(C6 H13 O9 P)                                               
FORMUL   7  PEG    4(C4 H10 O3)                                                 
FORMUL  11  GLC    C6 H12 O6                                                    
FORMUL  11  BGC    C6 H12 O6                                                    
HELIX    1   1 GLY A   23  LYS A   40  1                                  18    
HELIX    2   2 THR A   53  GLU A   57  1                                   5    
HELIX    3   3 LYS A   65  PHE A   69  5                                   5    
HELIX    4   4 SER A   70  GLU A   72  5                                   3    
HELIX    5   5 MET A   73  ARG A   86  1                                  14    
HELIX    6   6 LEU A  108  GLY A  113  5                                   6    
HELIX    7   7 TYR A  114  VAL A  126  1                                  13    
HELIX    8   8 ASP A  134  ASP A  158  1                                  25    
HELIX    9   9 TRP A  170  GLY A  173  5                                   4    
HELIX   10  10 VAL A  174  ARG A  182  1                                   9    
HELIX   11  11 THR A  195  SER A  204  1                                  10    
HELIX   12  12 ASP A  217  PHE A  225  1                                   9    
HELIX   13  13 ILE A  227  ALA A  241  1                                  15    
HELIX   14  14 SER A  248  LEU A  259  1                                  12    
HELIX   15  15 HIS A  280  PHE A  301  1                                  22    
HELIX   16  16 ASP A  308  ASP A  310  5                                   3    
HELIX   17  17 GLY A  327  GLY A  346  1                                  20    
HELIX   18  18 THR A  365  TYR A  400  1                                  36    
HELIX   19  19 ASP A  412  LEU A  416  5                                   5    
HELIX   20  20 LYS A  418  ARG A  433  1                                  16    
HELIX   21  21 ASP A  449  ASN A  452  5                                   4    
HELIX   22  22 ASP A  453  GLN A  463  1                                  11    
HELIX   23  23 ASP A  491  CYS A  499  1                                   9    
HELIX   24  24 GLY A  512  MET A  521  1                                  10    
HELIX   25  25 SER A  531  ILE A  541  1                                  11    
HELIX   26  26 GLU A  542  LYS A  547  1                                   6    
HELIX   27  27 ALA A  560  LYS A  578  1                                  19    
HELIX   28  28 THR A  579  ASP A  595  1                                  17    
HELIX   29  29 ASP A  598  TYR A  618  1                                  21    
HELIX   30  30 TYR A  618  GLY A  627  1                                  10    
HELIX   31  31 ASN A  634  ALA A  639  1                                   6    
HELIX   32  32 GLY B   23  LYS B   40  1                                  18    
HELIX   33  33 THR B   53  GLU B   57  1                                   5    
HELIX   34  34 LYS B   65  PHE B   69  5                                   5    
HELIX   35  35 SER B   70  GLU B   72  5                                   3    
HELIX   36  36 MET B   73  ARG B   86  1                                  14    
HELIX   37  37 LEU B  108  GLY B  113  5                                   6    
HELIX   38  38 TYR B  114  GLY B  127  1                                  14    
HELIX   39  39 ASP B  134  ASP B  158  1                                  25    
HELIX   40  40 TRP B  170  GLY B  173  5                                   4    
HELIX   41  41 VAL B  174  ARG B  182  1                                   9    
HELIX   42  42 THR B  195  SER B  204  1                                  10    
HELIX   43  43 ASP B  208  LEU B  213  1                                   6    
HELIX   44  44 GLU B  214  VAL B  216  5                                   3    
HELIX   45  45 ASP B  217  PHE B  225  1                                   9    
HELIX   46  46 ILE B  227  ALA B  241  1                                  15    
HELIX   47  47 SER B  248  LEU B  259  1                                  12    
HELIX   48  48 HIS B  280  PHE B  301  1                                  22    
HELIX   49  49 ASP B  308  ASP B  310  5                                   3    
HELIX   50  50 GLY B  327  GLY B  346  1                                  20    
HELIX   51  51 THR B  365  TYR B  400  1                                  36    
HELIX   52  52 ASP B  412  LEU B  417  1                                   6    
HELIX   53  53 LYS B  418  ARG B  433  1                                  16    
HELIX   54  54 ASP B  449  ASN B  452  5                                   4    
HELIX   55  55 ASP B  453  GLN B  463  1                                  11    
HELIX   56  56 ASP B  491  CYS B  499  1                                   9    
HELIX   57  57 GLY B  512  MET B  521  1                                  10    
HELIX   58  58 SER B  531  ILE B  541  1                                  11    
HELIX   59  59 GLU B  542  ASP B  548  1                                   7    
HELIX   60  60 ALA B  560  LYS B  577  1                                  18    
HELIX   61  61 THR B  579  SER B  594  1                                  16    
HELIX   62  62 ASP B  595  LEU B  597  5                                   3    
HELIX   63  63 ASP B  598  TYR B  618  1                                  21    
HELIX   64  64 TYR B  618  GLY B  627  1                                  10    
HELIX   65  65 GLY C   22  LYS C   40  1                                  19    
HELIX   66  66 THR C   53  ASN C   56  5                                   4    
HELIX   67  67 LYS C   65  PHE C   69  5                                   5    
HELIX   68  68 MET C   73  ARG C   86  1                                  14    
HELIX   69  69 LEU C  108  GLY C  113  5                                   6    
HELIX   70  70 TYR C  114  VAL C  126  1                                  13    
HELIX   71  71 ASP C  134  ASP C  158  1                                  25    
HELIX   72  72 TRP C  170  GLY C  173  5                                   4    
HELIX   73  73 VAL C  174  ARG C  182  1                                   9    
HELIX   74  74 THR C  195  GLY C  205  1                                  11    
HELIX   75  75 CYS C  212  VAL C  216  5                                   5    
HELIX   76  76 ASP C  217  PHE C  225  1                                   9    
HELIX   77  77 ILE C  227  ALA C  241  1                                  15    
HELIX   78  78 SER C  248  LYS C  260  1                                  13    
HELIX   79  79 HIS C  280  PHE C  301  1                                  22    
HELIX   80  80 ASP C  308  ASP C  310  5                                   3    
HELIX   81  81 GLY C  327  GLY C  346  1                                  20    
HELIX   82  82 THR C  365  TYR C  400  1                                  36    
HELIX   83  83 ASP C  412  LEU C  416  5                                   5    
HELIX   84  84 LYS C  418  LEU C  432  1                                  15    
HELIX   85  85 ASP C  449  ASN C  452  5                                   4    
HELIX   86  86 ASP C  453  VAL C  462  1                                  10    
HELIX   87  87 ASP C  491  CYS C  499  1                                   9    
HELIX   88  88 GLY C  512  MET C  521  1                                  10    
HELIX   89  89 SER C  531  ILE C  541  1                                  11    
HELIX   90  90 GLU C  542  TYR C  549  1                                   8    
HELIX   91  91 ALA C  560  LYS C  577  1                                  18    
HELIX   92  92 THR C  579  LEU C  593  1                                  15    
HELIX   93  93 SER C  594  LEU C  597  5                                   4    
HELIX   94  94 ASP C  598  TYR C  618  1                                  21    
HELIX   95  95 TYR C  618  GLY C  627  1                                  10    
HELIX   96  96 ASN C  634  ALA C  639  1                                   6    
HELIX   97  97 GLY D   23  LYS D   40  1                                  18    
HELIX   98  98 THR D   53  ASN D   56  5                                   4    
HELIX   99  99 MET D   73  ARG D   86  1                                  14    
HELIX  100 100 LEU D  108  GLY D  113  5                                   6    
HELIX  101 101 TYR D  114  SER D  124  1                                  11    
HELIX  102 102 ASP D  134  ASP D  158  1                                  25    
HELIX  103 103 TRP D  170  GLY D  173  5                                   4    
HELIX  104 104 VAL D  174  ARG D  182  1                                   9    
HELIX  105 105 THR D  195  ALA D  203  1                                   9    
HELIX  106 106 ASP D  217  PHE D  225  1                                   9    
HELIX  107 107 ILE D  227  ALA D  241  1                                  15    
HELIX  108 108 SER D  248  LYS D  260  1                                  13    
HELIX  109 109 HIS D  280  PHE D  301  1                                  22    
HELIX  110 110 ASP D  308  ASP D  310  5                                   3    
HELIX  111 111 GLY D  327  SER D  345  1                                  19    
HELIX  112 112 THR D  365  TYR D  400  1                                  36    
HELIX  113 113 ASP D  412  LEU D  416  5                                   5    
HELIX  114 114 LYS D  418  ARG D  433  1                                  16    
HELIX  115 115 ASP D  453  VAL D  462  1                                  10    
HELIX  116 116 ASP D  491  CYS D  499  1                                   9    
HELIX  117 117 GLY D  512  MET D  521  1                                  10    
HELIX  118 118 SER D  531  ASP D  539  1                                   9    
HELIX  119 119 ASN D  544  TYR D  549  1                                   6    
HELIX  120 120 ALA D  560  LYS D  577  1                                  18    
HELIX  121 121 THR D  579  SER D  594  1                                  16    
HELIX  122 122 ASP D  595  LEU D  597  5                                   3    
HELIX  123 123 ASP D  598  TYR D  618  1                                  21    
HELIX  124 124 TYR D  618  GLY D  627  1                                  10    
HELIX  125 125 ASN D  634  ALA D  639  1                                   6    
SHEET    1   A 9 VAL A  58  ILE A  60  0                                        
SHEET    2   A 9 PHE A  90  TRP A  95 -1  O  ARG A  94   N  ASP A  59           
SHEET    3   A 9 LYS A 102  PHE A 106 -1  O  LEU A 105   N  VAL A  91           
SHEET    4   A 9 TYR A  43  PRO A  48  1  N  LEU A  45   O  LYS A 102           
SHEET    5   A 9 ASP A   4  THR A  13  1  N  GLU A  12   O  ILE A  46           
SHEET    6   A 9 HIS A 161  HIS A 168  1  O  HIS A 166   N  THR A  13           
SHEET    7   A 9 VAL A 187  THR A 192  1  O  VAL A 187   N  ALA A 165           
SHEET    8   A 9 VAL A 243  THR A 246  1  O  THR A 245   N  PHE A 190           
SHEET    9   A 9 GLY A 265  ILE A 266  1  O  GLY A 265   N  THR A 246           
SHEET    1   B 6 VAL A 472  HIS A 477  0                                        
SHEET    2   B 6 THR A 350  VAL A 356  1  N  ILE A 355   O  HIS A 477           
SHEET    3   B 6 THR A 312  ALA A 318  1  N  LEU A 313   O  THR A 350           
SHEET    4   B 6 LEU A 501  VAL A 503  1  O  VAL A 503   N  PHE A 316           
SHEET    5   B 6 SER A 525  THR A 528  1  O  ILE A 526   N  GLY A 502           
SHEET    6   B 6 ILE A 551  VAL A 554  1  O  TYR A 552   N  THR A 527           
SHEET    1   C 2 ASN A 361  PHE A 364  0                                        
SHEET    2   C 2 HIS A 445  MET A 447 -1  O  ASN A 446   N  ASN A 362           
SHEET    1   D 9 VAL B  58  ILE B  60  0                                        
SHEET    2   D 9 PHE B  90  TRP B  95 -1  O  ARG B  94   N  ASP B  59           
SHEET    3   D 9 LYS B 102  PHE B 106 -1  O  LEU B 105   N  VAL B  91           
SHEET    4   D 9 TYR B  43  PRO B  48  1  N  LEU B  45   O  LYS B 102           
SHEET    5   D 9 ASP B   4  ALA B  14  1  N  GLU B  12   O  ILE B  46           
SHEET    6   D 9 HIS B 161  HIS B 168  1  O  HIS B 166   N  THR B  13           
SHEET    7   D 9 VAL B 187  THR B 192  1  O  ILE B 189   N  PHE B 167           
SHEET    8   D 9 VAL B 243  THR B 246  1  O  THR B 245   N  PHE B 190           
SHEET    9   D 9 GLY B 265  ILE B 266  1  O  GLY B 265   N  THR B 246           
SHEET    1   E 6 VAL B 472  HIS B 477  0                                        
SHEET    2   E 6 THR B 350  VAL B 356  1  N  VAL B 351   O  LYS B 473           
SHEET    3   E 6 THR B 312  ALA B 318  1  N  LEU B 313   O  THR B 350           
SHEET    4   E 6 LEU B 501  VAL B 503  1  O  VAL B 503   N  PHE B 316           
SHEET    5   E 6 SER B 525  THR B 528  1  O  ILE B 526   N  GLY B 502           
SHEET    6   E 6 ILE B 551  VAL B 554  1  O  TYR B 552   N  THR B 527           
SHEET    1   F 2 ASN B 361  PHE B 364  0                                        
SHEET    2   F 2 HIS B 445  MET B 447 -1  O  ASN B 446   N  ASN B 362           
SHEET    1   G 9 VAL C  58  ILE C  60  0                                        
SHEET    2   G 9 PHE C  90  TRP C  95 -1  O  ARG C  94   N  ASP C  59           
SHEET    3   G 9 LYS C 102  PHE C 106 -1  O  LEU C 105   N  VAL C  91           
SHEET    4   G 9 TYR C  43  PRO C  48  1  N  GLY C  47   O  PHE C 106           
SHEET    5   G 9 ASP C   4  THR C  13  1  N  GLU C  12   O  ILE C  46           
SHEET    6   G 9 HIS C 161  HIS C 168  1  O  HIS C 166   N  THR C  13           
SHEET    7   G 9 VAL C 187  THR C 192  1  O  VAL C 187   N  ALA C 165           
SHEET    8   G 9 VAL C 243  THR C 246  1  O  THR C 245   N  PHE C 190           
SHEET    9   G 9 GLY C 265  ILE C 266  1  O  GLY C 265   N  THR C 246           
SHEET    1   H 6 VAL C 472  HIS C 477  0                                        
SHEET    2   H 6 THR C 350  VAL C 356  1  N  VAL C 351   O  LYS C 473           
SHEET    3   H 6 THR C 312  ALA C 318  1  N  LEU C 313   O  THR C 350           
SHEET    4   H 6 LEU C 501  VAL C 503  1  O  VAL C 503   N  PHE C 316           
SHEET    5   H 6 SER C 525  THR C 528  1  O  ILE C 526   N  GLY C 502           
SHEET    6   H 6 ILE C 551  VAL C 554  1  O  VAL C 554   N  THR C 527           
SHEET    1   I 2 ASN C 361  PHE C 364  0                                        
SHEET    2   I 2 HIS C 445  MET C 447 -1  O  ASN C 446   N  ASN C 362           
SHEET    1   J 8 VAL D  58  ILE D  60  0                                        
SHEET    2   J 8 PHE D  90  TRP D  95 -1  O  ARG D  94   N  ASP D  59           
SHEET    3   J 8 LYS D 102  PHE D 106 -1  O  VAL D 103   N  GLY D  93           
SHEET    4   J 8 TYR D  43  PRO D  48  1  N  LEU D  45   O  LYS D 102           
SHEET    5   J 8 ASP D   4  ALA D  14  1  N  GLU D  12   O  ILE D  46           
SHEET    6   J 8 HIS D 161  HIS D 168  1  O  HIS D 166   N  THR D  13           
SHEET    7   J 8 VAL D 187  THR D 192  1  O  ILE D 189   N  PHE D 167           
SHEET    8   J 8 VAL D 243  THR D 246  1  O  THR D 245   N  PHE D 190           
SHEET    1   K 6 VAL D 472  HIS D 477  0                                        
SHEET    2   K 6 THR D 350  VAL D 356  1  N  VAL D 351   O  LYS D 473           
SHEET    3   K 6 THR D 312  ALA D 318  1  N  PHE D 315   O  PHE D 354           
SHEET    4   K 6 LEU D 501  VAL D 503  1  O  VAL D 503   N  PHE D 316           
SHEET    5   K 6 SER D 525  THR D 528  1  O  ILE D 526   N  GLY D 502           
SHEET    6   K 6 ILE D 551  VAL D 554  1  O  TYR D 552   N  THR D 527           
SHEET    1   L 2 ASN D 361  PHE D 364  0                                        
SHEET    2   L 2 HIS D 445  MET D 447 -1  O  ASN D 446   N  ASN D 362           
CISPEP   1 TYR A  400    PRO A  401          0         3.21                     
CISPEP   2 TYR B  400    PRO B  401          0         2.99                     
CISPEP   3 TYR C  400    PRO C  401          0        -5.01                     
CISPEP   4 TYR D  400    PRO D  401          0         1.97                     
SITE     1 AC1 12 GLY A 319  ARG A 320  LYS A 326  VAL A 356                    
SITE     2 AC1 12 PHE A 480  LEU A 481  TYR A 492  GLU A 509                    
SITE     3 AC1 12 GLY A 512  TYR A 513  THR A 514  GLU A 517                    
SITE     1 AC2  8 GLN A 283  HIS A 286  LYS A 290  HIS A 500                    
SITE     2 AC2  8 ARG A 580  ARG A 583  ARG A 587  HIS D 280                    
SITE     1 AC3  3 LYS A 391  PHE A 394  GLU B 379                               
SITE     1 AC4 12 GLY B 319  ARG B 320  LYS B 326  VAL B 356                    
SITE     2 AC4 12 PHE B 480  LEU B 481  TYR B 492  GLU B 509                    
SITE     3 AC4 12 GLY B 512  TYR B 513  THR B 514  GLU B 517                    
SITE     1 AC5  8 GLN B 283  HIS B 286  LYS B 290  HIS B 500                    
SITE     2 AC5  8 ARG B 580  ARG B 583  ARG B 587  HIS C 280                    
SITE     1 AC6  4 GLU A 291  GLU A 379  LYS B 391  PHE B 394                    
SITE     1 AC7 10 GLY C  23  HIS C 193  ARG C 199  ASN C 269                    
SITE     2 AC7 10 GLU C 509  PRO C 510  TRP C 511  GLY C 512                    
SITE     3 AC7 10 BGC C 802  UDP C 803                                          
SITE     1 AC8  9 HIS C 193  ARG C 199  ASN C 269  GLU C 509                    
SITE     2 AC8  9 PRO C 510  TRP C 511  GLY C 512  GLC C 801                    
SITE     3 AC8  9 UDP C 803                                                     
SITE     1 AC9 18 ARG C  20  GLY C  22  GLY C  23  SER C  26                    
SITE     2 AC9 18 ARG C 199  ARG C 320  LYS C 326  VAL C 356                    
SITE     3 AC9 18 PHE C 480  LEU C 481  TYR C 492  GLU C 509                    
SITE     4 AC9 18 GLY C 512  TYR C 513  THR C 514  GLU C 517                    
SITE     5 AC9 18 GLC C 801  BGC C 802                                          
SITE     1 BC1 10 HIS B 280  GLN C 283  ASN C 284  HIS C 286                    
SITE     2 BC1 10 LYS C 290  HIS C 500  ARG C 580  ARG C 583                    
SITE     3 BC1 10 ILE C 584  ARG C 587                                          
SITE     1 BC2  2 LYS C 391  GLU D 291                                          
SITE     1 BC3 11 GLY D 319  ARG D 320  LYS D 326  PHE D 480                    
SITE     2 BC3 11 LEU D 481  TYR D 492  GLU D 509  GLY D 512                    
SITE     3 BC3 11 TYR D 513  THR D 514  GLU D 517                               
SITE     1 BC4  8 HIS A 280  GLN D 283  HIS D 286  LYS D 290                    
SITE     2 BC4  8 HIS D 500  ARG D 580  ARG D 583  ARG D 587                    
SITE     1 BC5  3 GLU C 379  LYS D 391  PHE D 394                               
CRYST1  192.710  204.443  206.332  90.00  90.00  90.00 I 2 2 2      32          
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      0.005189  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004891  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004847        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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