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Database: PDB
Entry: 4IP7
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HEADER    TRANSFERASE                             09-JAN-13   4IP7              
TITLE     STRUCTURE OF THE S12D VARIANT OF HUMAN LIVER PYRUVATE KINASE IN       
TITLE    2 COMPLEX WITH CITRATE AND FBP.                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PYRUVATE KINASE ISOZYMES L;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: LIVER ISOZYME;                                             
COMPND   5 SYNONYM: PYRUVATE KINASE 1, L-TYPE PYRUVATE KINASE, LIVER PYRUVATE   
COMPND   6 KINASE;                                                              
COMPND   7 EC: 2.7.1.40;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PK1, PKL, PKLR;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: FF50;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    KINASE, GLYCOLYSIS, ALLOSTERIC, PHOSPHORYLATION MIMIC, LIVER,         
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.HOLYOAK,A.W.FENTON                                                  
REVDAT   3   15-NOV-17 4IP7    1       REMARK                                   
REVDAT   2   06-FEB-13 4IP7    1       JRNL                                     
REVDAT   1   30-JAN-13 4IP7    0                                                
JRNL        AUTH   T.HOLYOAK,B.ZHANG,J.DENG,Q.TANG,C.B.PRASANNAN,A.W.FENTON     
JRNL        TITL   ENERGETIC COUPLING BETWEEN AN OXIDIZABLE CYSTEINE AND THE    
JRNL        TITL 2 PHOSPHORYLATABLE N-TERMINUS OF HUMAN LIVER PYRUVATE KINASE.  
JRNL        REF    BIOCHEMISTRY                  V.  52   466 2013              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   23270483                                                     
JRNL        DOI    10.1021/BI301341R                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.53                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 236781                         
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11896                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 15133                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 778                          
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15291                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 226                                     
REMARK   3   SOLVENT ATOMS            : 1324                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.04000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.115         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.115         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.671         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16097 ; 0.022 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21874 ; 2.220 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2103 ; 6.415 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   680 ;34.000 ;23.015       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2748 ;17.167 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   163 ;19.783 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2543 ; 0.171 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12045 ; 0.011 ; 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 : NULL                              
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    26        A   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.2320 -32.7100  15.7160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0339 T22:   0.0762                                     
REMARK   3      T33:   0.0811 T12:  -0.0116                                     
REMARK   3      T13:   0.0499 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0562 L22:   4.9699                                     
REMARK   3      L33:   2.1191 L12:  -1.4138                                     
REMARK   3      L13:  -0.2296 L23:   2.1035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0804 S12:  -0.0090 S13:  -0.1768                       
REMARK   3      S21:   0.2705 S22:  -0.1261 S23:   0.3637                       
REMARK   3      S31:   0.1791 S32:  -0.2513 S33:   0.2065                       
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   131        A   228                          
REMARK   3    ORIGIN FOR THE GROUP (A):  80.0830 -24.1660  18.4960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0470 T22:   0.5322                                     
REMARK   3      T33:   0.1439 T12:   0.0981                                     
REMARK   3      T13:   0.0559 T23:  -0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.2239 L22:   3.9216                                     
REMARK   3      L33:   6.6628 L12:  -2.1238                                     
REMARK   3      L13:  -7.2759 L23:   2.2620                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3719 S12:  -1.7023 S13:   0.0833                       
REMARK   3      S21:   0.0902 S22:   0.4084 S23:  -0.0262                       
REMARK   3      S31:   0.3427 S32:   0.9976 S33:  -0.0365                       
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   232        A   411                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.4380 -24.4190   9.6360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0258 T22:   0.0676                                     
REMARK   3      T33:   0.0303 T12:  -0.0123                                     
REMARK   3      T13:   0.0181 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1406 L22:   2.2053                                     
REMARK   3      L33:   2.5886 L12:   0.4482                                     
REMARK   3      L13:   0.1276 L23:   1.2399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1191 S12:   0.1149 S13:  -0.0724                       
REMARK   3      S21:  -0.1563 S22:   0.0443 S23:  -0.0772                       
REMARK   3      S31:  -0.1192 S32:   0.1402 S33:   0.0748                       
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   412        A   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4220 -30.9590  -0.7770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0444 T22:   0.0893                                     
REMARK   3      T33:   0.0623 T12:  -0.0203                                     
REMARK   3      T13:   0.0091 T23:  -0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1931 L22:   2.2396                                     
REMARK   3      L33:   3.1073 L12:  -2.4685                                     
REMARK   3      L13:   1.8765 L23:  -0.5373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0563 S12:  -0.0898 S13:  -0.2480                       
REMARK   3      S21:  -0.1352 S22:   0.0826 S23:   0.2069                       
REMARK   3      S31:   0.0859 S32:  -0.1308 S33:  -0.0263                       
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    25        B   146                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2350   2.9350 -21.3220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0663 T22:   0.1129                                     
REMARK   3      T33:   0.0412 T12:  -0.0250                                     
REMARK   3      T13:   0.0196 T23:   0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9990 L22:   2.1048                                     
REMARK   3      L33:   1.4372 L12:   2.4755                                     
REMARK   3      L13:   1.5736 L23:   0.6280                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0737 S12:   0.3255 S13:  -0.1010                       
REMARK   3      S21:  -0.1480 S22:   0.1524 S23:  -0.2176                       
REMARK   3      S31:  -0.0095 S32:  -0.0622 S33:  -0.0787                       
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   147        B   234                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.6630  27.7620  -5.3170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2468 T22:   0.6410                                     
REMARK   3      T33:   0.6665 T12:   0.1408                                     
REMARK   3      T13:   0.0887 T23:  -0.1430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.4445 L22:  11.6392                                     
REMARK   3      L33:   3.1202 L12:  -0.0401                                     
REMARK   3      L13:  -1.6383 L23:   0.6975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1205 S12:  -0.6827 S13:   1.8089                       
REMARK   3      S21:   0.4430 S22:  -0.0945 S23:   0.9931                       
REMARK   3      S31:  -0.3849 S32:  -0.5944 S33:  -0.0260                       
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   235        B   411                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.6950   5.4090  -9.9170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0349 T22:   0.1073                                     
REMARK   3      T33:   0.0203 T12:  -0.0197                                     
REMARK   3      T13:  -0.0014 T23:   0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7709 L22:   2.0773                                     
REMARK   3      L33:   1.5351 L12:   1.2649                                     
REMARK   3      L13:   0.2082 L23:   0.2457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1538 S12:  -0.1587 S13:  -0.0947                       
REMARK   3      S21:   0.1369 S22:  -0.0281 S23:  -0.0402                       
REMARK   3      S31:   0.0661 S32:  -0.2420 S33:  -0.1257                       
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   412        B   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1150 -17.6730 -14.0690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0528 T22:   0.1025                                     
REMARK   3      T33:   0.0738 T12:  -0.0292                                     
REMARK   3      T13:   0.0154 T23:   0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4161 L22:   3.2552                                     
REMARK   3      L33:   1.7968 L12:  -1.8076                                     
REMARK   3      L13:   1.5537 L23:  -1.9725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0423 S12:   0.2560 S13:  -0.1153                       
REMARK   3      S21:  -0.3068 S22:  -0.0632 S23:   0.0076                       
REMARK   3      S31:   0.1092 S32:   0.0980 S33:   0.0209                       
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    26        C   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.8020  -0.4760  31.6160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0581 T22:   0.1389                                     
REMARK   3      T33:   0.0634 T12:  -0.0045                                     
REMARK   3      T13:  -0.0001 T23:  -0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9320 L22:   1.4386                                     
REMARK   3      L33:   6.0252 L12:   0.3189                                     
REMARK   3      L13:   1.1924 L23:   2.4170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1658 S12:  -0.0325 S13:   0.1164                       
REMARK   3      S21:  -0.2185 S22:   0.1579 S23:  -0.1618                       
REMARK   3      S31:  -0.4919 S32:   0.3191 S33:   0.0079                       
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   129        C   234                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.9010 -27.8330  50.0700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7212 T22:   0.6132                                     
REMARK   3      T33:   0.1912 T12:   0.2251                                     
REMARK   3      T13:   0.3429 T23:   0.1994                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1945 L22:   8.0455                                     
REMARK   3      L33:  14.6168 L12:  -1.2233                                     
REMARK   3      L13:  -5.1486 L23:   0.8648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1031 S12:  -1.2800 S13:  -0.8651                       
REMARK   3      S21:   0.8587 S22:   0.0958 S23:   0.1911                       
REMARK   3      S31:   2.0564 S32:   0.9082 S33:   1.0072                       
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   235        C   411                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.4760  -5.2650  33.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0842 T22:   0.1433                                     
REMARK   3      T33:   0.0459 T12:   0.0739                                     
REMARK   3      T13:  -0.0461 T23:  -0.0455                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3955 L22:   2.2642                                     
REMARK   3      L33:   2.0628 L12:   0.1778                                     
REMARK   3      L13:   0.1414 L23:   1.4854                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2020 S12:  -0.2649 S13:   0.1024                       
REMARK   3      S21:  -0.0010 S22:  -0.0886 S23:   0.2130                       
REMARK   3      S31:  -0.2467 S32:  -0.1960 S33:   0.2906                       
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   412        C   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.2120  17.9490  24.6020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1657 T22:   0.1193                                     
REMARK   3      T33:   0.0618 T12:   0.0337                                     
REMARK   3      T13:  -0.0298 T23:  -0.0504                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3725 L22:   3.1868                                     
REMARK   3      L33:   4.7139 L12:  -1.3191                                     
REMARK   3      L13:   0.8165 L23:  -1.1838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0035 S12:   0.0549 S13:   0.2031                       
REMARK   3      S21:  -0.0064 S22:   0.0347 S23:  -0.1855                       
REMARK   3      S31:  -0.1361 S32:   0.2980 S33:  -0.0312                       
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    21        D   125                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8710  32.7020  -4.1500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0870 T22:   0.1057                                     
REMARK   3      T33:   0.0768 T12:  -0.0145                                     
REMARK   3      T13:   0.0461 T23:  -0.0254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4987 L22:   5.8387                                     
REMARK   3      L33:   1.0817 L12:   2.1292                                     
REMARK   3      L13:  -0.2833 L23:  -1.6360                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2027 S12:  -0.2773 S13:   0.1875                       
REMARK   3      S21:   0.4352 S22:  -0.1687 S23:   0.2037                       
REMARK   3      S31:  -0.1390 S32:  -0.0279 S33:  -0.0340                       
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   126        D   219                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.0120  24.2780 -42.4960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5052 T22:   1.6973                                     
REMARK   3      T33:   0.1078 T12:  -0.1724                                     
REMARK   3      T13:   0.2145 T23:  -0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.9077 L22:   5.8634                                     
REMARK   3      L33:   7.5945 L12:   8.0838                                     
REMARK   3      L13:   4.8655 L23:   1.4463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1803 S12:   4.0047 S13:  -0.2553                       
REMARK   3      S21:  -0.9211 S22:   1.5908 S23:  -0.1700                       
REMARK   3      S31:  -0.5348 S32:   0.3560 S33:  -0.4105                       
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   220        D   411                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3210  25.1150 -14.5590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0652 T22:   0.0645                                     
REMARK   3      T33:   0.0731 T12:  -0.0162                                     
REMARK   3      T13:   0.0553 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9480 L22:   2.4062                                     
REMARK   3      L33:   0.8291 L12:   1.0156                                     
REMARK   3      L13:   0.0997 L23:   0.3110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0344 S12:   0.0726 S13:  -0.1076                       
REMARK   3      S21:  -0.1596 S22:   0.0512 S23:  -0.3624                       
REMARK   3      S31:  -0.0714 S32:   0.0815 S33:  -0.0856                       
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   412        D   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.2690  31.1360   9.2030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1109 T22:   0.1159                                     
REMARK   3      T33:   0.0925 T12:  -0.0222                                     
REMARK   3      T13:  -0.0159 T23:  -0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3234 L22:   3.0196                                     
REMARK   3      L33:   4.5931 L12:  -0.0691                                     
REMARK   3      L13:   1.3023 L23:  -2.5297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0526 S12:  -0.1887 S13:   0.1459                       
REMARK   3      S21:   0.3748 S22:   0.1000 S23:  -0.0874                       
REMARK   3      S31:  -0.2570 S32:  -0.1162 S33:  -0.0475                       
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: U VALUES : WITH TLS ADDED HYDROGENS       
REMARK   3  HAVE BEEN USED IF PRESENT IN THE INPUT                              
REMARK   4                                                                      
REMARK   4 4IP7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000077034.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : SIDE SCATTERING BENT CUBE-ROOT I   
REMARK 200                                   -BEAM SINGLE CRYSTAL; ASYMMETRIC   
REMARK 200                                   CUT 4.965 DEGS                     
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL FOCUSING);   
REMARK 200                                   SINGLE CRYSTAL SI(111) BENT        
REMARK 200                                   MONOCHROMATOR (HORIZONTAL          
REMARK 200                                   FOCUSING)                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 237180                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69800                            
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 2VGB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM SODIUM CITRATE (PH 4.9), 26 MM     
REMARK 280  MNCL2, 3-5% PEG 6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      102.53900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 25420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     TYR A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     GLN A    18                                                      
REMARK 465     GLU A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     PHE A    24                                                      
REMARK 465     PHE A    25                                                      
REMARK 465     ALA A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     LEU A   136                                                      
REMARK 465     GLN A   137                                                      
REMARK 465     GLY A   138                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     PRO A   140                                                      
REMARK 465     GLU A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     ASP A   229                                                      
REMARK 465     LEU A   230                                                      
REMARK 465     PRO A   231                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     TYR B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     VAL B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     GLN B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     GLN B    18                                                      
REMARK 465     GLU B    19                                                      
REMARK 465     LEU B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     THR B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     PHE B    24                                                      
REMARK 465     LEU B   136                                                      
REMARK 465     GLN B   137                                                      
REMARK 465     GLY B   138                                                      
REMARK 465     GLY B   139                                                      
REMARK 465     PRO B   140                                                      
REMARK 465     GLU B   141                                                      
REMARK 465     SER B   142                                                      
REMARK 465     ARG B   161                                                      
REMARK 465     THR B   162                                                      
REMARK 465     ARG B   163                                                      
REMARK 465     GLN B   227                                                      
REMARK 465     VAL B   228                                                      
REMARK 465     ASP B   229                                                      
REMARK 465     LEU B   230                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     TYR C     7                                                      
REMARK 465     LEU C     8                                                      
REMARK 465     ARG C     9                                                      
REMARK 465     ARG C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     ASP C    12                                                      
REMARK 465     VAL C    13                                                      
REMARK 465     ALA C    14                                                      
REMARK 465     GLN C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     THR C    17                                                      
REMARK 465     GLN C    18                                                      
REMARK 465     GLU C    19                                                      
REMARK 465     LEU C    20                                                      
REMARK 465     GLY C    21                                                      
REMARK 465     THR C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     PHE C    24                                                      
REMARK 465     PHE C    25                                                      
REMARK 465     ILE C   135                                                      
REMARK 465     LEU C   136                                                      
REMARK 465     GLN C   137                                                      
REMARK 465     GLY C   138                                                      
REMARK 465     GLY C   139                                                      
REMARK 465     PRO C   140                                                      
REMARK 465     GLU C   141                                                      
REMARK 465     SER C   142                                                      
REMARK 465     PHE C   160                                                      
REMARK 465     ARG C   161                                                      
REMARK 465     THR C   162                                                      
REMARK 465     ARG C   163                                                      
REMARK 465     GLY C   164                                                      
REMARK 465     ALA C   226                                                      
REMARK 465     GLN C   227                                                      
REMARK 465     VAL C   228                                                      
REMARK 465     ASP C   229                                                      
REMARK 465     LEU C   230                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     PRO D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     TYR D     7                                                      
REMARK 465     LEU D     8                                                      
REMARK 465     ARG D     9                                                      
REMARK 465     ARG D    10                                                      
REMARK 465     ALA D    11                                                      
REMARK 465     ASP D    12                                                      
REMARK 465     VAL D    13                                                      
REMARK 465     ALA D    14                                                      
REMARK 465     GLN D    15                                                      
REMARK 465     LEU D    16                                                      
REMARK 465     THR D    17                                                      
REMARK 465     GLN D    18                                                      
REMARK 465     GLU D    19                                                      
REMARK 465     LEU D    20                                                      
REMARK 465     ALA D   111                                                      
REMARK 465     GLY D   112                                                      
REMARK 465     LEU D   136                                                      
REMARK 465     GLN D   137                                                      
REMARK 465     GLY D   138                                                      
REMARK 465     GLY D   139                                                      
REMARK 465     PRO D   140                                                      
REMARK 465     GLU D   141                                                      
REMARK 465     SER D   142                                                      
REMARK 465     GLY D   225                                                      
REMARK 465     ALA D   226                                                      
REMARK 465     GLN D   227                                                      
REMARK 465     VAL D   228                                                      
REMARK 465     ASP D   229                                                      
REMARK 465     LEU D   230                                                      
REMARK 465     PRO D   231                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLY C 134    CA   C    O                                         
REMARK 470     ALA C 159    CA   C    O    CB                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG C    72     O    HOH C   998              1.88            
REMARK 500   O    HOH B   904     O    HOH B   917              1.88            
REMARK 500   OE2  GLU A   430     OE1  GLU B   430              1.93            
REMARK 500   O    HOH A   975     O    HOH A  1028              2.00            
REMARK 500   O    HOH D   719     O    HOH D   965              2.00            
REMARK 500   NE   ARG D   118     O    HOH D   973              2.09            
REMARK 500   O    HOH C   842     O    HOH C   879              2.11            
REMARK 500   NH1  ARG D   418     O    HOH D   954              2.11            
REMARK 500   OE1  GLU A   488     NH2  ARG A   500              2.14            
REMARK 500   OD1  ASP A   499     O    HOH A  1039              2.15            
REMARK 500   O    HOH D   909     O    HOH D   935              2.15            
REMARK 500   NH2  ARG D    68     O    TYR D    95              2.18            
REMARK 500   O    HOH A  1058     O    HOH A  1059              2.18            
REMARK 500   O    HOH D   738     O    HOH D  1006              2.18            
REMARK 500   O    HOH C   907     O    HOH C   926              2.18            
REMARK 500   O    HOH D   797     O    HOH D   898              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   994     O    HOH A  1017     1455     1.83            
REMARK 500   NZ   LYS A    74     OE1  GLU D   246     2645     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  93   CG    HIS A  93   CD2     0.059                       
REMARK 500    SER A 358   CB    SER A 358   OG     -0.104                       
REMARK 500    TRP A 494   CE2   TRP A 494   CD2     0.074                       
REMARK 500    HIS B  90   CG    HIS B  90   CD2     0.060                       
REMARK 500    HIS C  90   CG    HIS C  90   CD2     0.060                       
REMARK 500    HIS C  96   CG    HIS C  96   CD2     0.057                       
REMARK 500    ASN C 167   CG    ASN C 167   ND2     0.157                       
REMARK 500    HIS C 476   CG    HIS C 476   CD2     0.055                       
REMARK 500    HIS D  96   CG    HIS D  96   CD2     0.058                       
REMARK 500    VAL D 156   CA    VAL D 156   C       0.178                       
REMARK 500    PRO D 158   N     PRO D 158   CA      0.126                       
REMARK 500    GLY D 164   C     GLY D 164   O       0.146                       
REMARK 500    ASN D 167   C     ASN D 167   O       0.124                       
REMARK 500    PRO D 174   C     ASN D 175   N       0.215                       
REMARK 500    GLN D 198   CD    GLN D 198   NE2     0.263                       
REMARK 500    GLU D 203   CD    GLU D 203   OE1     0.240                       
REMARK 500    GLU D 203   CD    GLU D 203   OE2     0.149                       
REMARK 500    GLY D 204   C     LEU D 205   N       0.180                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A  85   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP A 237   CB  -  CG  -  OD1 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ASP A 237   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    VAL A 263   CG1 -  CB  -  CG2 ANGL. DEV. =  12.5 DEGREES          
REMARK 500    PRO A 272   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    LEU A 343   CB  -  CG  -  CD1 ANGL. DEV. =  14.4 DEGREES          
REMARK 500    ARG A 395   NE  -  CZ  -  NH1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG A 395   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    PRO A 415   C   -  N   -  CA  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    ARG A 459   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    VAL A 475   CG1 -  CB  -  CG2 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG A 528   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A 528   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    LEU A 540   CB  -  CG  -  CD2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    LEU B  73   CB  -  CG  -  CD2 ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG B 118   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    LYS B 127   CD  -  CE  -  NZ  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    ASP B 237   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    MET B 325   CA  -  CB  -  CG  ANGL. DEV. = -10.6 DEGREES          
REMARK 500    LYS B 349   CD  -  CE  -  NZ  ANGL. DEV. = -19.9 DEGREES          
REMARK 500    ARG B 354   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG C  85   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C 178   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    VAL C 475   CG1 -  CB  -  CG2 ANGL. DEV. =  12.3 DEGREES          
REMARK 500    MET C 537   CG  -  SD  -  CE  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ASP D  46   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG D  68   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG D  68   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG D  72   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG D  85   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG D  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG D 132   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG D 132   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    PRO D 158   N   -  CA  -  CB  ANGL. DEV. =  -9.5 DEGREES          
REMARK 500    GLN D 198   CG  -  CD  -  OE1 ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ARG D 328   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG D 328   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    LEU D 331   CB  -  CG  -  CD1 ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ARG D 395   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG D 395   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    MET D 537   CG  -  SD  -  CE  ANGL. DEV. = -19.0 DEGREES          
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    GLN A  28       29.44     49.11                                   
REMARK 500    PHE A  88        1.05    -69.48                                   
REMARK 500    ASP A 189       78.05     64.71                                   
REMARK 500    THR A 340      122.30     84.58                                   
REMARK 500    SER A 374      -99.10   -118.04                                   
REMARK 500    GLU A 491      150.27    -46.94                                   
REMARK 500    ASN A 535       10.97   -166.30                                   
REMARK 500    GLN B  26       13.28   -144.99                                   
REMARK 500    SER B  67       44.53   -141.23                                   
REMARK 500    ALA B 159       46.93    -72.55                                   
REMARK 500    ASN B 165     -172.34    179.13                                   
REMARK 500    ASP B 189       76.19     72.99                                   
REMARK 500    THR B 340      119.58     91.80                                   
REMARK 500    SER B 374      -97.20   -117.74                                   
REMARK 500    SER B 374      -99.52   -115.88                                   
REMARK 500    VAL B 517      125.07    -39.71                                   
REMARK 500    ASN B 535        7.77   -161.19                                   
REMARK 500    SER C  67       43.15   -140.46                                   
REMARK 500    ALA C 166      -18.22    -46.05                                   
REMARK 500    ASP C 189       83.58     64.32                                   
REMARK 500    THR C 340      117.46     95.09                                   
REMARK 500    SER C 374     -100.45   -114.56                                   
REMARK 500    SER C 374      -99.79   -115.34                                   
REMARK 500    ASN C 535        9.17   -163.07                                   
REMARK 500    PHE D  88        5.70    -68.56                                   
REMARK 500    ASP D 172       42.92    -87.95                                   
REMARK 500    VAL D 179      -23.72   -146.35                                   
REMARK 500    ASP D 189       76.54     67.57                                   
REMARK 500    GLN D 198     -108.95   -103.22                                   
REMARK 500    THR D 340      114.71     97.99                                   
REMARK 500    SER D 374      -93.72   -120.78                                   
REMARK 500    LYS D 379       -5.77   -140.58                                   
REMARK 500    GLU D 491      150.49    -47.25                                   
REMARK 500    ASN D 535       13.82   -163.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLN D 151         14.74                                           
REMARK 500    ASP D 157        -10.05                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     1PE C  605                                                       
REMARK 610     1PE C  606                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 601  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 308   OD2                                                    
REMARK 620 2 GLU D 284   OE2  97.2                                              
REMARK 620 3 FLC D 602   OHB 154.8 106.3                                        
REMARK 620 4 FLC D 602   OB1  93.4  92.0  77.1                                  
REMARK 620 5 HOH D 703   O    79.4 176.2  77.3  90.0                            
REMARK 620 6 HOH D 751   O   104.3  84.5  87.1 162.2  94.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 602  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 308   OD2                                                    
REMARK 620 2 GLU C 284   OE2  96.7                                              
REMARK 620 3 FLC C 603   OHB 157.8 103.3                                        
REMARK 620 4 FLC C 603   OB1  95.7  89.0  75.3                                  
REMARK 620 5 HOH C 752   O    82.8 178.3  77.5  92.7                            
REMARK 620 6 HOH C 716   O   107.7  84.3  84.1 156.2  94.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 601  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 308   OD2                                                    
REMARK 620 2 GLU B 284   OE2  95.9                                              
REMARK 620 3 FLC B 602   OHB 154.5 106.0                                        
REMARK 620 4 FLC B 602   OB2  92.4  86.7  76.3                                  
REMARK 620 5 HOH B 720   O    82.9 174.5  76.5  98.6                            
REMARK 620 6 HOH B 736   O   105.6  85.3  89.4 161.0  89.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 601  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 284   OE2                                                    
REMARK 620 2 ASP A 308   OD2  95.6                                              
REMARK 620 3 FLC A 602   OHB 105.2 156.9                                        
REMARK 620 4 FLC A 602   OB1  90.7  95.6  74.7                                  
REMARK 620 5 HOH A 721   O   176.6  84.0  75.8  92.8                            
REMARK 620 6 HOH A1006   O    81.5 108.1  85.1 155.6  95.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 608  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN D  87   OD1                                                    
REMARK 620 2 ASP D 125   OD1 136.5                                              
REMARK 620 3 THR D 126   O   127.3  73.1                                        
REMARK 620 4 HOH D 738   O    76.9 137.7 110.0                                  
REMARK 620 5 HOH D1005   O   118.6 104.8  65.4  48.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 607  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  87   OD1                                                    
REMARK 620 2 THR A 126   O   129.1                                              
REMARK 620 3 ASP A 125   OD1 131.9  74.5                                        
REMARK 620 4 HOH A 781   O    78.3 115.4 134.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 608  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 126   O                                                      
REMARK 620 2 ASN C  87   OD1 130.1                                              
REMARK 620 3 ASP C 125   OD1  74.7 130.4                                        
REMARK 620 4 HOH C1033   O    70.9 127.5  99.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 607  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  87   OD1                                                    
REMARK 620 2 THR B 126   O   128.6                                              
REMARK 620 3 ASP B 125   OD1 128.1  74.4                                        
REMARK 620 4 HOH B1024   O    70.6 125.8 139.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE C 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 608                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 608                  
DBREF  4IP7 A    1   543  UNP    P30613   KPYR_HUMAN       1    543             
DBREF  4IP7 B    1   543  UNP    P30613   KPYR_HUMAN       1    543             
DBREF  4IP7 C    1   543  UNP    P30613   KPYR_HUMAN       1    543             
DBREF  4IP7 D    1   543  UNP    P30613   KPYR_HUMAN       1    543             
SEQADV 4IP7 ASP A   12  UNP  P30613    SER    12 ENGINEERED MUTATION            
SEQADV 4IP7 ASP B   12  UNP  P30613    SER    12 ENGINEERED MUTATION            
SEQADV 4IP7 ASP C   12  UNP  P30613    SER    12 ENGINEERED MUTATION            
SEQADV 4IP7 ASP D   12  UNP  P30613    SER    12 ENGINEERED MUTATION            
SEQRES   1 A  543  MET GLU GLY PRO ALA GLY TYR LEU ARG ARG ALA ASP VAL          
SEQRES   2 A  543  ALA GLN LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN          
SEQRES   3 A  543  GLN GLN GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU          
SEQRES   4 A  543  GLU HIS LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL          
SEQRES   5 A  543  ALA ALA ARG SER THR SER ILE ILE ALA THR ILE GLY PRO          
SEQRES   6 A  543  ALA SER ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS          
SEQRES   7 A  543  ALA GLY MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY          
SEQRES   8 A  543  SER HIS GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG          
SEQRES   9 A  543  GLU ALA VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR          
SEQRES  10 A  543  ARG PRO VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU          
SEQRES  11 A  543  ILE ARG THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU          
SEQRES  12 A  543  VAL GLU LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL          
SEQRES  13 A  543  ASP PRO ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL          
SEQRES  14 A  543  TRP VAL ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL          
SEQRES  15 A  543  GLY GLY ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU          
SEQRES  16 A  543  VAL VAL GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN          
SEQRES  17 A  543  VAL GLU ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL          
SEQRES  18 A  543  ASN LEU PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER          
SEQRES  19 A  543  GLU GLN ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS          
SEQRES  20 A  543  GLY VAL ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA          
SEQRES  21 A  543  SER ASP VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU          
SEQRES  22 A  543  GLY HIS GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS          
SEQRES  23 A  543  GLU GLY VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER          
SEQRES  24 A  543  ASP GLY ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU          
SEQRES  25 A  543  ILE PRO ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET          
SEQRES  26 A  543  ILE GLY ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS          
SEQRES  27 A  543  ALA THR GLN MET LEU GLU SER MET ILE THR LYS PRO ARG          
SEQRES  28 A  543  PRO THR ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL          
SEQRES  29 A  543  LEU ASP GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR          
SEQRES  30 A  543  ALA LYS GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN          
SEQRES  31 A  543  HIS ALA ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS          
SEQRES  32 A  543  ARG GLN LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU          
SEQRES  33 A  543  SER ARG ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL          
SEQRES  34 A  543  GLU ALA ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL          
SEQRES  35 A  543  LEU THR THR THR GLY ARG SER ALA GLN LEU LEU SER ARG          
SEQRES  36 A  543  TYR ARG PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER          
SEQRES  37 A  543  ALA GLN ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL          
SEQRES  38 A  543  PHE PRO LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP          
SEQRES  39 A  543  ALA ASP ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU          
SEQRES  40 A  543  SER GLY LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU          
SEQRES  41 A  543  VAL ILE VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR          
SEQRES  42 A  543  THR ASN ILE MET ARG VAL LEU SER ILE SER                      
SEQRES   1 B  543  MET GLU GLY PRO ALA GLY TYR LEU ARG ARG ALA ASP VAL          
SEQRES   2 B  543  ALA GLN LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN          
SEQRES   3 B  543  GLN GLN GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU          
SEQRES   4 B  543  GLU HIS LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL          
SEQRES   5 B  543  ALA ALA ARG SER THR SER ILE ILE ALA THR ILE GLY PRO          
SEQRES   6 B  543  ALA SER ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS          
SEQRES   7 B  543  ALA GLY MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY          
SEQRES   8 B  543  SER HIS GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG          
SEQRES   9 B  543  GLU ALA VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR          
SEQRES  10 B  543  ARG PRO VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU          
SEQRES  11 B  543  ILE ARG THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU          
SEQRES  12 B  543  VAL GLU LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL          
SEQRES  13 B  543  ASP PRO ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL          
SEQRES  14 B  543  TRP VAL ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL          
SEQRES  15 B  543  GLY GLY ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU          
SEQRES  16 B  543  VAL VAL GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN          
SEQRES  17 B  543  VAL GLU ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL          
SEQRES  18 B  543  ASN LEU PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER          
SEQRES  19 B  543  GLU GLN ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS          
SEQRES  20 B  543  GLY VAL ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA          
SEQRES  21 B  543  SER ASP VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU          
SEQRES  22 B  543  GLY HIS GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS          
SEQRES  23 B  543  GLU GLY VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER          
SEQRES  24 B  543  ASP GLY ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU          
SEQRES  25 B  543  ILE PRO ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET          
SEQRES  26 B  543  ILE GLY ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS          
SEQRES  27 B  543  ALA THR GLN MET LEU GLU SER MET ILE THR LYS PRO ARG          
SEQRES  28 B  543  PRO THR ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL          
SEQRES  29 B  543  LEU ASP GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR          
SEQRES  30 B  543  ALA LYS GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN          
SEQRES  31 B  543  HIS ALA ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS          
SEQRES  32 B  543  ARG GLN LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU          
SEQRES  33 B  543  SER ARG ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL          
SEQRES  34 B  543  GLU ALA ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL          
SEQRES  35 B  543  LEU THR THR THR GLY ARG SER ALA GLN LEU LEU SER ARG          
SEQRES  36 B  543  TYR ARG PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER          
SEQRES  37 B  543  ALA GLN ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL          
SEQRES  38 B  543  PHE PRO LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP          
SEQRES  39 B  543  ALA ASP ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU          
SEQRES  40 B  543  SER GLY LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU          
SEQRES  41 B  543  VAL ILE VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR          
SEQRES  42 B  543  THR ASN ILE MET ARG VAL LEU SER ILE SER                      
SEQRES   1 C  543  MET GLU GLY PRO ALA GLY TYR LEU ARG ARG ALA ASP VAL          
SEQRES   2 C  543  ALA GLN LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN          
SEQRES   3 C  543  GLN GLN GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU          
SEQRES   4 C  543  GLU HIS LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL          
SEQRES   5 C  543  ALA ALA ARG SER THR SER ILE ILE ALA THR ILE GLY PRO          
SEQRES   6 C  543  ALA SER ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS          
SEQRES   7 C  543  ALA GLY MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY          
SEQRES   8 C  543  SER HIS GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG          
SEQRES   9 C  543  GLU ALA VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR          
SEQRES  10 C  543  ARG PRO VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU          
SEQRES  11 C  543  ILE ARG THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU          
SEQRES  12 C  543  VAL GLU LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL          
SEQRES  13 C  543  ASP PRO ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL          
SEQRES  14 C  543  TRP VAL ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL          
SEQRES  15 C  543  GLY GLY ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU          
SEQRES  16 C  543  VAL VAL GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN          
SEQRES  17 C  543  VAL GLU ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL          
SEQRES  18 C  543  ASN LEU PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER          
SEQRES  19 C  543  GLU GLN ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS          
SEQRES  20 C  543  GLY VAL ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA          
SEQRES  21 C  543  SER ASP VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU          
SEQRES  22 C  543  GLY HIS GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS          
SEQRES  23 C  543  GLU GLY VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER          
SEQRES  24 C  543  ASP GLY ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU          
SEQRES  25 C  543  ILE PRO ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET          
SEQRES  26 C  543  ILE GLY ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS          
SEQRES  27 C  543  ALA THR GLN MET LEU GLU SER MET ILE THR LYS PRO ARG          
SEQRES  28 C  543  PRO THR ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL          
SEQRES  29 C  543  LEU ASP GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR          
SEQRES  30 C  543  ALA LYS GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN          
SEQRES  31 C  543  HIS ALA ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS          
SEQRES  32 C  543  ARG GLN LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU          
SEQRES  33 C  543  SER ARG ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL          
SEQRES  34 C  543  GLU ALA ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL          
SEQRES  35 C  543  LEU THR THR THR GLY ARG SER ALA GLN LEU LEU SER ARG          
SEQRES  36 C  543  TYR ARG PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER          
SEQRES  37 C  543  ALA GLN ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL          
SEQRES  38 C  543  PHE PRO LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP          
SEQRES  39 C  543  ALA ASP ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU          
SEQRES  40 C  543  SER GLY LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU          
SEQRES  41 C  543  VAL ILE VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR          
SEQRES  42 C  543  THR ASN ILE MET ARG VAL LEU SER ILE SER                      
SEQRES   1 D  543  MET GLU GLY PRO ALA GLY TYR LEU ARG ARG ALA ASP VAL          
SEQRES   2 D  543  ALA GLN LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN          
SEQRES   3 D  543  GLN GLN GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU          
SEQRES   4 D  543  GLU HIS LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL          
SEQRES   5 D  543  ALA ALA ARG SER THR SER ILE ILE ALA THR ILE GLY PRO          
SEQRES   6 D  543  ALA SER ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS          
SEQRES   7 D  543  ALA GLY MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY          
SEQRES   8 D  543  SER HIS GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG          
SEQRES   9 D  543  GLU ALA VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR          
SEQRES  10 D  543  ARG PRO VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU          
SEQRES  11 D  543  ILE ARG THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU          
SEQRES  12 D  543  VAL GLU LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL          
SEQRES  13 D  543  ASP PRO ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL          
SEQRES  14 D  543  TRP VAL ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL          
SEQRES  15 D  543  GLY GLY ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU          
SEQRES  16 D  543  VAL VAL GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN          
SEQRES  17 D  543  VAL GLU ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL          
SEQRES  18 D  543  ASN LEU PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER          
SEQRES  19 D  543  GLU GLN ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS          
SEQRES  20 D  543  GLY VAL ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA          
SEQRES  21 D  543  SER ASP VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU          
SEQRES  22 D  543  GLY HIS GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS          
SEQRES  23 D  543  GLU GLY VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER          
SEQRES  24 D  543  ASP GLY ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU          
SEQRES  25 D  543  ILE PRO ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET          
SEQRES  26 D  543  ILE GLY ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS          
SEQRES  27 D  543  ALA THR GLN MET LEU GLU SER MET ILE THR LYS PRO ARG          
SEQRES  28 D  543  PRO THR ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL          
SEQRES  29 D  543  LEU ASP GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR          
SEQRES  30 D  543  ALA LYS GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN          
SEQRES  31 D  543  HIS ALA ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS          
SEQRES  32 D  543  ARG GLN LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU          
SEQRES  33 D  543  SER ARG ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL          
SEQRES  34 D  543  GLU ALA ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL          
SEQRES  35 D  543  LEU THR THR THR GLY ARG SER ALA GLN LEU LEU SER ARG          
SEQRES  36 D  543  TYR ARG PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER          
SEQRES  37 D  543  ALA GLN ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL          
SEQRES  38 D  543  PHE PRO LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP          
SEQRES  39 D  543  ALA ASP ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU          
SEQRES  40 D  543  SER GLY LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU          
SEQRES  41 D  543  VAL ILE VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR          
SEQRES  42 D  543  THR ASN ILE MET ARG VAL LEU SER ILE SER                      
HET     MN  A 601       1                                                       
HET    FLC  A 602      13                                                       
HET    FBP  A 603      20                                                       
HET    EDO  A 604       4                                                       
HET    EDO  A 605       4                                                       
HET    PEG  A 606       7                                                       
HET     NA  A 607       1                                                       
HET     MN  B 601       1                                                       
HET    FLC  B 602      13                                                       
HET    FBP  B 603      20                                                       
HET    EDO  B 604       4                                                       
HET    PEG  B 605       7                                                       
HET    EDO  B 606       4                                                       
HET     NA  B 607       1                                                       
HET    EDO  C 601       4                                                       
HET     MN  C 602       1                                                       
HET    FLC  C 603      13                                                       
HET    FBP  C 604      20                                                       
HET    1PE  C 605      10                                                       
HET    1PE  C 606       7                                                       
HET    EDO  C 607       4                                                       
HET     NA  C 608       1                                                       
HET     MN  D 601       1                                                       
HET    FLC  D 602      13                                                       
HET    FBP  D 603      20                                                       
HET    ADN  D 604      38                                                       
HET    EDO  D 605       4                                                       
HET    EDO  D 606       4                                                       
HET    EDO  D 607       4                                                       
HET     NA  D 608       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     FLC CITRATE ANION                                                    
HETNAM     FBP BETA-FRUCTOSE-1,6-DIPHOSPHATE                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      NA SODIUM ION                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     ADN ADENOSINE                                                        
HETSYN     FBP FRUCTOSE-1,6-BISPHOSPHATE                                        
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     1PE PEG400                                                           
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   6  FLC    4(C6 H5 O7 3-)                                               
FORMUL   7  FBP    4(C6 H14 O12 P2)                                             
FORMUL   8  EDO    9(C2 H6 O2)                                                  
FORMUL  10  PEG    2(C4 H10 O3)                                                 
FORMUL  11   NA    4(NA 1+)                                                     
FORMUL  23  1PE    2(C10 H22 O6)                                                
FORMUL  30  ADN    C10 H13 N5 O4                                                
FORMUL  35  HOH   *1324(H2 O)                                                   
HELIX    1   1 GLN A   29  MET A   34  1                                   6    
HELIX    2   2 THR A   37  LEU A   44  1                                   8    
HELIX    3   3 SER A   69  GLY A   80  1                                  12    
HELIX    4   4 SER A   92  SER A  109  1                                  18    
HELIX    5   5 SER A  113  TYR A  117  5                                   5    
HELIX    6   6 ASP A  157  ARG A  161  5                                   5    
HELIX    7   7 ASN A  175  VAL A  180  1                                   6    
HELIX    8   8 SER A  234  HIS A  247  1                                  14    
HELIX    9   9 LYS A  259  GLY A  271  1                                  13    
HELIX   10  10 PRO A  272  HIS A  275  5                                   4    
HELIX   11  11 ASN A  285  ARG A  291  1                                   7    
HELIX   12  12 ARG A  291  SER A  299  1                                   9    
HELIX   13  13 ARG A  306  ILE A  313  1                                   8    
HELIX   14  14 PRO A  314  GLU A  316  5                                   3    
HELIX   15  15 LYS A  317  GLY A  333  1                                  17    
HELIX   16  16 LEU A  343  THR A  348  5                                   6    
HELIX   17  17 THR A  353  GLY A  367  1                                  15    
HELIX   18  18 SER A  374  LYS A  379  1                                   6    
HELIX   19  19 PHE A  382  ALA A  400  1                                  19    
HELIX   20  20 TYR A  402  ARG A  412  1                                  11    
HELIX   21  21 ASP A  419  CYS A  436  1                                  18    
HELIX   22  22 GLY A  447  ARG A  455  1                                   9    
HELIX   23  23 SER A  468  VAL A  475  1                                   8    
HELIX   24  24 HIS A  476  CYS A  478  5                                   3    
HELIX   25  25 ILE A  493  ARG A  512  1                                  20    
HELIX   26  26 GLN B   29  MET B   34  1                                   6    
HELIX   27  27 THR B   37  LEU B   45  1                                   9    
HELIX   28  28 GLY B   64  ARG B   68  5                                   5    
HELIX   29  29 SER B   69  GLY B   80  1                                  12    
HELIX   30  30 SER B   92  SER B  109  1                                  18    
HELIX   31  31 ASN B  175  VAL B  180  1                                   6    
HELIX   32  32 SER B  234  HIS B  247  1                                  14    
HELIX   33  33 LYS B  259  GLY B  271  1                                  13    
HELIX   34  34 PRO B  272  HIS B  275  5                                   4    
HELIX   35  35 ASN B  285  ARG B  291  1                                   7    
HELIX   36  36 ARG B  291  SER B  299  1                                   9    
HELIX   37  37 ARG B  306  ILE B  313  1                                   8    
HELIX   38  38 PRO B  314  GLU B  316  5                                   3    
HELIX   39  39 LYS B  317  GLY B  333  1                                  17    
HELIX   40  40 LEU B  343  THR B  348  5                                   6    
HELIX   41  41 THR B  353  GLY B  367  1                                  15    
HELIX   42  42 SER B  374  LYS B  379  1                                   6    
HELIX   43  43 PHE B  382  ALA B  400  1                                  19    
HELIX   44  44 TYR B  402  ALA B  414  1                                  13    
HELIX   45  45 ASP B  419  CYS B  436  1                                  18    
HELIX   46  46 GLY B  447  ARG B  455  1                                   9    
HELIX   47  47 SER B  468  VAL B  475  1                                   8    
HELIX   48  48 HIS B  476  CYS B  478  5                                   3    
HELIX   49  49 ILE B  493  ARG B  512  1                                  20    
HELIX   50  50 GLN C   29  MET C   34  1                                   6    
HELIX   51  51 THR C   37  LEU C   45  1                                   9    
HELIX   52  52 SER C   69  GLY C   80  1                                  12    
HELIX   53  53 SER C   92  SER C  109  1                                  18    
HELIX   54  54 TYR C  173  VAL C  179  5                                   7    
HELIX   55  55 SER C  234  HIS C  247  1                                  14    
HELIX   56  56 LYS C  259  GLY C  271  1                                  13    
HELIX   57  57 PRO C  272  HIS C  275  5                                   4    
HELIX   58  58 ASN C  285  ARG C  291  1                                   7    
HELIX   59  59 ARG C  291  SER C  299  1                                   9    
HELIX   60  60 ARG C  306  ILE C  313  1                                   8    
HELIX   61  61 PRO C  314  GLU C  316  5                                   3    
HELIX   62  62 LYS C  317  GLY C  333  1                                  17    
HELIX   63  63 LEU C  343  THR C  348  5                                   6    
HELIX   64  64 THR C  353  GLY C  367  1                                  15    
HELIX   65  65 SER C  374  LYS C  379  1                                   6    
HELIX   66  66 PHE C  382  ALA C  400  1                                  19    
HELIX   67  67 TYR C  402  ALA C  414  1                                  13    
HELIX   68  68 ASP C  419  CYS C  436  1                                  18    
HELIX   69  69 GLY C  447  ARG C  455  1                                   9    
HELIX   70  70 SER C  468  VAL C  475  1                                   8    
HELIX   71  71 HIS C  476  CYS C  478  5                                   3    
HELIX   72  72 ILE C  493  ARG C  512  1                                  20    
HELIX   73  73 ALA D   23  GLN D   27  5                                   5    
HELIX   74  74 GLN D   29  MET D   34  1                                   6    
HELIX   75  75 THR D   37  LEU D   45  1                                   9    
HELIX   76  76 SER D   69  GLY D   80  1                                  12    
HELIX   77  77 SER D   92  SER D  109  1                                  18    
HELIX   78  78 ASP D  157  ARG D  161  5                                   5    
HELIX   79  79 TYR D  173  VAL D  179  5                                   7    
HELIX   80  80 SER D  234  HIS D  247  1                                  14    
HELIX   81  81 LYS D  259  GLY D  271  1                                  13    
HELIX   82  82 PRO D  272  HIS D  275  5                                   4    
HELIX   83  83 ASN D  285  ARG D  291  1                                   7    
HELIX   84  84 ARG D  291  SER D  299  1                                   9    
HELIX   85  85 ARG D  306  ILE D  313  1                                   8    
HELIX   86  86 PRO D  314  GLU D  316  5                                   3    
HELIX   87  87 LYS D  317  GLY D  333  1                                  17    
HELIX   88  88 LEU D  343  THR D  348  5                                   6    
HELIX   89  89 THR D  353  GLY D  367  1                                  15    
HELIX   90  90 SER D  374  LYS D  379  1                                   6    
HELIX   91  91 PHE D  382  ALA D  400  1                                  19    
HELIX   92  92 TYR D  402  ARG D  412  1                                  11    
HELIX   93  93 ASP D  419  CYS D  436  1                                  18    
HELIX   94  94 GLY D  447  ARG D  455  1                                   9    
HELIX   95  95 SER D  468  VAL D  475  1                                   8    
HELIX   96  96 HIS D  476  CYS D  478  5                                   3    
HELIX   97  97 ILE D  493  ARG D  512  1                                  20    
SHEET    1   A 9 SER A  58  THR A  62  0                                        
SHEET    2   A 9 MET A  81  ASN A  87  1  O  ARG A  85   N  ALA A  61           
SHEET    3   A 9 ALA A 121  ASP A 125  1  O  ASP A 125   N  LEU A  86           
SHEET    4   A 9 ILE A 251  ALA A 254  1  O  PHE A 253   N  LEU A 124           
SHEET    5   A 9 LYS A 278  ILE A 283  1  O  LYS A 282   N  ALA A 254           
SHEET    6   A 9 GLY A 301  ALA A 305  1  O  MET A 303   N  ILE A 283           
SHEET    7   A 9 VAL A 336  ALA A 339  1  O  VAL A 337   N  VAL A 304           
SHEET    8   A 9 CYS A 370  LEU A 373  1  O  CYS A 370   N  CYS A 338           
SHEET    9   A 9 SER A  58  THR A  62  1  N  SER A  58   O  ILE A 371           
SHEET    1   B 7 ILE A 131  ARG A 132  0                                        
SHEET    2   B 7 GLY A 220  ASN A 222 -1  O  VAL A 221   N  ILE A 131           
SHEET    3   B 7 ARG A 185  ILE A 188 -1  N  TYR A 187   O  ASN A 222           
SHEET    4   B 7 ILE A 193  GLY A 201 -1  O  LEU A 195   N  ILE A 186           
SHEET    5   B 7 GLY A 204  ASN A 211 -1  O  VAL A 206   N  GLN A 198           
SHEET    6   B 7 GLN A 151  THR A 155 -1  N  VAL A 154   O  LEU A 205           
SHEET    7   B 7 THR A 168  TRP A 170  1  O  VAL A 169   N  LEU A 153           
SHEET    1   C 2 VAL A 144  LEU A 146  0                                        
SHEET    2   C 2 GLY A 213  LEU A 215 -1  O  LEU A 215   N  VAL A 144           
SHEET    1   D10 VAL A 481  LEU A 485  0                                        
SHEET    2   D10 ALA A 461  THR A 466  1  N  ALA A 464   O  LEU A 484           
SHEET    3   D10 ALA A 439  LEU A 443  1  N  ILE A 440   O  ALA A 461           
SHEET    4   D10 LEU A 520  GLY A 526  1  O  VAL A 524   N  ILE A 441           
SHEET    5   D10 THR A 534  SER A 541 -1  O  ARG A 538   N  VAL A 523           
SHEET    6   D10 THR B 534  SER B 541 -1  O  MET B 537   N  MET A 537           
SHEET    7   D10 LEU B 520  GLY B 526 -1  N  VAL B 523   O  ARG B 538           
SHEET    8   D10 ALA B 439  LEU B 443  1  N  ILE B 441   O  VAL B 524           
SHEET    9   D10 ALA B 461  THR B 466  1  O  ILE B 463   N  VAL B 442           
SHEET   10   D10 VAL B 481  LEU B 485  1  O  LEU B 484   N  ALA B 464           
SHEET    1   E 9 SER B  58  THR B  62  0                                        
SHEET    2   E 9 ILE B  83  ASN B  87  1  O  ARG B  85   N  ALA B  61           
SHEET    3   E 9 ALA B 121  ASP B 125  1  O  ASP B 125   N  LEU B  86           
SHEET    4   E 9 ILE B 251  ALA B 254  1  O  ILE B 251   N  LEU B 124           
SHEET    5   E 9 LYS B 278  ILE B 283  1  O  ILE B 280   N  VAL B 252           
SHEET    6   E 9 GLY B 301  ALA B 305  1  O  MET B 303   N  SER B 281           
SHEET    7   E 9 VAL B 336  ALA B 339  1  O  VAL B 337   N  VAL B 304           
SHEET    8   E 9 CYS B 370  LEU B 373  1  O  CYS B 370   N  CYS B 338           
SHEET    9   E 9 SER B  58  THR B  62  1  N  ILE B  60   O  ILE B 371           
SHEET    1   F 7 ILE B 131  ARG B 132  0                                        
SHEET    2   F 7 GLY B 220  ASN B 222 -1  O  VAL B 221   N  ILE B 131           
SHEET    3   F 7 GLY B 183  ILE B 188 -1  N  TYR B 187   O  ASN B 222           
SHEET    4   F 7 ILE B 193  GLY B 201 -1  O  LEU B 195   N  ILE B 186           
SHEET    5   F 7 GLY B 204  ASN B 211 -1  O  GLU B 210   N  SER B 194           
SHEET    6   F 7 GLN B 151  THR B 155 -1  N  VAL B 154   O  LEU B 205           
SHEET    7   F 7 THR B 168  TRP B 170  1  O  VAL B 169   N  LEU B 153           
SHEET    1   G 2 GLU B 145  LEU B 146  0                                        
SHEET    2   G 2 GLY B 213  VAL B 214 -1  O  GLY B 213   N  LEU B 146           
SHEET    1   H 9 SER C  58  THR C  62  0                                        
SHEET    2   H 9 MET C  81  ASN C  87  1  O  ASN C  82   N  ILE C  59           
SHEET    3   H 9 ALA C 121  ASP C 125  1  O  ALA C 121   N  ALA C  84           
SHEET    4   H 9 ILE C 251  ALA C 254  1  O  ILE C 251   N  LEU C 124           
SHEET    5   H 9 LYS C 278  ILE C 283  1  O  ILE C 280   N  VAL C 252           
SHEET    6   H 9 GLY C 301  ALA C 305  1  O  MET C 303   N  ILE C 283           
SHEET    7   H 9 VAL C 336  ALA C 339  1  O  VAL C 337   N  VAL C 304           
SHEET    8   H 9 CYS C 370  LEU C 373  1  O  CYS C 370   N  CYS C 338           
SHEET    9   H 9 SER C  58  THR C  62  1  N  ILE C  60   O  ILE C 371           
SHEET    1   I 7 ILE C 131  ARG C 132  0                                        
SHEET    2   I 7 GLY C 220  ASN C 222 -1  O  VAL C 221   N  ILE C 131           
SHEET    3   I 7 ARG C 185  ILE C 188 -1  N  TYR C 187   O  ASN C 222           
SHEET    4   I 7 ILE C 193  GLY C 201 -1  O  ILE C 193   N  ILE C 188           
SHEET    5   I 7 GLY C 204  ASN C 211 -1  O  VAL C 206   N  GLN C 198           
SHEET    6   I 7 GLN C 151  THR C 155 -1  N  VAL C 154   O  LEU C 205           
SHEET    7   I 7 THR C 168  TRP C 170  1  O  VAL C 169   N  LEU C 153           
SHEET    1   J 2 VAL C 144  LEU C 146  0                                        
SHEET    2   J 2 GLY C 213  LEU C 215 -1  O  LEU C 215   N  VAL C 144           
SHEET    1   K10 VAL C 481  LEU C 485  0                                        
SHEET    2   K10 ALA C 461  THR C 466  1  N  VAL C 462   O  PHE C 482           
SHEET    3   K10 ALA C 439  LEU C 443  1  N  ILE C 440   O  ILE C 463           
SHEET    4   K10 LEU C 520  GLY C 526  1  O  VAL C 524   N  ILE C 441           
SHEET    5   K10 THR C 534  SER C 541 -1  O  LEU C 540   N  VAL C 521           
SHEET    6   K10 THR D 534  SER D 541 -1  O  MET D 537   N  MET C 537           
SHEET    7   K10 LEU D 520  GLY D 526 -1  N  VAL D 523   O  ARG D 538           
SHEET    8   K10 ALA D 439  LEU D 443  1  N  ILE D 441   O  VAL D 524           
SHEET    9   K10 ALA D 461  THR D 466  1  O  VAL D 465   N  VAL D 442           
SHEET   10   K10 VAL D 481  LEU D 485  1  O  PHE D 482   N  VAL D 462           
SHEET    1   L 9 SER D  58  THR D  62  0                                        
SHEET    2   L 9 MET D  81  ASN D  87  1  O  ARG D  85   N  ALA D  61           
SHEET    3   L 9 ALA D 121  ASP D 125  1  O  ALA D 121   N  ALA D  84           
SHEET    4   L 9 ILE D 251  ALA D 254  1  O  PHE D 253   N  LEU D 124           
SHEET    5   L 9 LYS D 278  ILE D 283  1  O  ILE D 280   N  VAL D 252           
SHEET    6   L 9 GLY D 301  ALA D 305  1  O  MET D 303   N  SER D 281           
SHEET    7   L 9 VAL D 336  ALA D 339  1  O  VAL D 337   N  VAL D 304           
SHEET    8   L 9 CYS D 370  LEU D 373  1  O  CYS D 370   N  CYS D 338           
SHEET    9   L 9 SER D  58  THR D  62  1  N  ILE D  60   O  ILE D 371           
SHEET    1   M 2 VAL D 144  LEU D 146  0                                        
SHEET    2   M 2 GLY D 213  LEU D 215 -1  O  GLY D 213   N  LEU D 146           
SHEET    1   N 6 THR D 168  TRP D 170  0                                        
SHEET    2   N 6 GLN D 151  THR D 155  1  N  LEU D 153   O  VAL D 169           
SHEET    3   N 6 GLY D 204  VAL D 209 -1  O  LEU D 205   N  VAL D 154           
SHEET    4   N 6 ILE D 193  GLY D 201 -1  N  GLN D 198   O  VAL D 206           
SHEET    5   N 6 GLY D 183  ILE D 188 -1  N  ILE D 186   O  LEU D 195           
SHEET    6   N 6 VAL D 221  ASN D 222 -1  O  ASN D 222   N  TYR D 187           
LINK         OD2 ASP D 308                MN    MN D 601     1555   1555  1.98  
LINK         OD2 ASP C 308                MN    MN C 602     1555   1555  2.00  
LINK         OD2 ASP B 308                MN    MN B 601     1555   1555  2.00  
LINK         OE2 GLU A 284                MN    MN A 601     1555   1555  2.04  
LINK         OE2 GLU D 284                MN    MN D 601     1555   1555  2.04  
LINK         OE2 GLU C 284                MN    MN C 602     1555   1555  2.05  
LINK        MN    MN C 602                 OHB FLC C 603     1555   1555  2.07  
LINK         OE2 GLU B 284                MN    MN B 601     1555   1555  2.12  
LINK         OD2 ASP A 308                MN    MN A 601     1555   1555  2.14  
LINK        MN    MN D 601                 OHB FLC D 602     1555   1555  2.16  
LINK        MN    MN D 601                 OB1 FLC D 602     1555   1555  2.19  
LINK        MN    MN B 601                 OHB FLC B 602     1555   1555  2.19  
LINK        MN    MN B 601                 OB2 FLC B 602     1555   1555  2.21  
LINK        MN    MN C 602                 OB1 FLC C 603     1555   1555  2.30  
LINK        MN    MN A 601                 OHB FLC A 602     1555   1555  2.30  
LINK        MN    MN A 601                 OB1 FLC A 602     1555   1555  2.34  
LINK         OD1 ASN D  87                NA    NA D 608     1555   1555  2.71  
LINK         OD1 ASN A  87                NA    NA A 607     1555   1555  2.81  
LINK         O   THR C 126                NA    NA C 608     1555   1555  2.83  
LINK         OD1 ASN B  87                NA    NA B 607     1555   1555  2.86  
LINK         OD1 ASN C  87                NA    NA C 608     1555   1555  2.89  
LINK         O   THR A 126                NA    NA A 607     1555   1555  2.95  
LINK         OD1 ASP D 125                NA    NA D 608     1555   1555  2.98  
LINK         O   THR B 126                NA    NA B 607     1555   1555  3.01  
LINK         OD1 ASP C 125                NA    NA C 608     1555   1555  3.01  
LINK         O   THR D 126                NA    NA D 608     1555   1555  3.06  
LINK         OD1 ASP B 125                NA    NA B 607     1555   1555  3.12  
LINK         OD1 ASP A 125                NA    NA A 607     1555   1555  3.14  
LINK        MN    MN D 601                 O   HOH D 703     1555   1555  2.12  
LINK        MN    MN A 601                 O   HOH A 721     1555   1555  2.14  
LINK        MN    MN C 602                 O   HOH C 752     1555   1555  2.20  
LINK        MN    MN D 601                 O   HOH D 751     1555   1555  2.21  
LINK        MN    MN C 602                 O   HOH C 716     1555   1555  2.23  
LINK        MN    MN A 601                 O   HOH A1006     1555   1555  2.23  
LINK        MN    MN B 601                 O   HOH B 720     1555   1555  2.28  
LINK        MN    MN B 601                 O   HOH B 736     1555   1555  2.28  
LINK        NA    NA A 607                 O   HOH A 781     1555   1555  2.41  
LINK        NA    NA B 607                 O   HOH B1024     1555   1555  2.50  
LINK        NA    NA D 608                 O   HOH D 738     1555   1555  2.50  
LINK        NA    NA C 608                 O   HOH C1033     1555   1555  2.65  
LINK        NA    NA D 608                 O   HOH D1005     1555   1555  2.94  
CISPEP   1 VAL B  182    GLY B  183          0        -8.30                     
CISPEP   2 VAL C  182    GLY C  183          0       -25.10                     
SITE     1 AC1  5 GLU A 284  ASP A 308  FLC A 602  HOH A 721                    
SITE     2 AC1  5 HOH A1006                                                     
SITE     1 AC2 19 ARG A  85  ASP A 125  LYS A 282  GLU A 284                    
SITE     2 AC2 19 MET A 303  ALA A 305  ARG A 306  GLY A 307                    
SITE     3 AC2 19 ASP A 308  THR A 340  MET A 372   MN A 601                    
SITE     4 AC2 19  NA A 607  HOH A 721  HOH A 729  HOH A 781                    
SITE     5 AC2 19 HOH A 912  HOH A1005  HOH A1006                               
SITE     1 AC3 24 LEU A 443  THR A 444  THR A 445  THR A 446                    
SITE     2 AC3 24 SER A 449  TRP A 494  ARG A 501  GLY A 526                    
SITE     3 AC3 24 ARG A 528  PRO A 529  GLY A 530  SER A 531                    
SITE     4 AC3 24 GLY A 532  TYR A 533  THR A 534  HOH A 705                    
SITE     5 AC3 24 HOH A 707  HOH A 719  HOH A 728  HOH A 759                    
SITE     6 AC3 24 HOH A 764  HOH A 770  HOH A 784  HOH A 933                    
SITE     1 AC4 10 GLY A 333  LYS A 334  PRO A 335  ASP A 369                    
SITE     2 AC4 10 GLN A 451  SER A 454  ARG A 455  ARG A 457                    
SITE     3 AC4 10 CYS A 478  HOH A 730                                          
SITE     1 AC5  6 LYS A 278  GLN A 451  GLN A 474  HOH A 717                    
SITE     2 AC5  6 HOH A 757  HOH A 762                                          
SITE     1 AC6  8 ARG A 411  HIS B 403  ARG B 404  PHE B 407                    
SITE     2 AC6  8 PHE B 433  ARG B 459  HOH B 748  HOH B 910                    
SITE     1 AC7  7 ARG A  85  ASN A  87  SER A  89  ASP A 125                    
SITE     2 AC7  7 THR A 126  FLC A 602  HOH A 781                               
SITE     1 AC8  5 GLU B 284  ASP B 308  FLC B 602  HOH B 720                    
SITE     2 AC8  5 HOH B 736                                                     
SITE     1 AC9 18 ARG B  85  ASP B 125  LYS B 282  GLU B 284                    
SITE     2 AC9 18 MET B 303  ALA B 305  ARG B 306  GLY B 307                    
SITE     3 AC9 18 ASP B 308  THR B 340  MET B 372  SER B 374                    
SITE     4 AC9 18  MN B 601   NA B 607  HOH B 720  HOH B 837                    
SITE     5 AC9 18 HOH B 972  HOH B1024                                          
SITE     1 BC1 24 LEU B 443  THR B 444  THR B 445  THR B 446                    
SITE     2 BC1 24 SER B 449  TRP B 494  ARG B 501  GLY B 526                    
SITE     3 BC1 24 ARG B 528  PRO B 529  GLY B 530  SER B 531                    
SITE     4 BC1 24 GLY B 532  TYR B 533  THR B 534  HOH B 710                    
SITE     5 BC1 24 HOH B 732  HOH B 742  HOH B 745  HOH B 784                    
SITE     6 BC1 24 HOH B 792  HOH B 797  HOH B 800  HOH B 821                    
SITE     1 BC2 10 GLY B 333  LYS B 334  PRO B 335  ASP B 369                    
SITE     2 BC2 10 GLN B 451  SER B 454  ARG B 455  ARG B 457                    
SITE     3 BC2 10 CYS B 478  HOH B 714                                          
SITE     1 BC3  4 HIS B  93  HOH B 750  HOH B 947  EDO C 607                    
SITE     1 BC4  9 SER B  56  THR B  57  SER B  58  HIS B 476                    
SITE     2 BC4  9 VAL B 481  PHE B 482  HOH B 739  HOH B 971                    
SITE     3 BC4  9 HOH B1014                                                     
SITE     1 BC5  8 ARG B  85  ASN B  87  SER B  89  ASP B 125                    
SITE     2 BC5  8 THR B 126  LYS B 282  FLC B 602  HOH B1024                    
SITE     1 BC6  6 ASP A 190  GLN A 341  ARG C 351  PRO C 352                    
SITE     2 BC6  6 ARG C 354  HOH C 966                                          
SITE     1 BC7  5 GLU C 284  ASP C 308  FLC C 603  HOH C 716                    
SITE     2 BC7  5 HOH C 752                                                     
SITE     1 BC8 18 ARG C  85  ASP C 125  LYS C 282  GLU C 284                    
SITE     2 BC8 18 MET C 303  ALA C 305  ARG C 306  GLY C 307                    
SITE     3 BC8 18 ASP C 308  THR C 340  MET C 372  SER C 374                    
SITE     4 BC8 18  MN C 602   NA C 608  HOH C 716  HOH C 752                    
SITE     5 BC8 18 HOH C 815  HOH C 837                                          
SITE     1 BC9 24 LEU C 443  THR C 444  THR C 445  THR C 446                    
SITE     2 BC9 24 SER C 449  TRP C 494  ARG C 501  GLY C 526                    
SITE     3 BC9 24 ARG C 528  PRO C 529  GLY C 530  SER C 531                    
SITE     4 BC9 24 GLY C 532  TYR C 533  THR C 534  HOH C 708                    
SITE     5 BC9 24 HOH C 713  HOH C 722  HOH C 828  HOH C 855                    
SITE     6 BC9 24 HOH C 861  HOH C 864  HOH C 883  HOH C 983                    
SITE     1 CC1  1 GLY C  91                                                     
SITE     1 CC2 14 SER C  56  THR C  57  SER C  58  ASN C  82                    
SITE     2 CC2 14 ASP C 369  HIS C 476  LEU C 477  CYS C 478                    
SITE     3 CC2 14 ARG C 479  GLY C 480  VAL C 481  PHE C 482                    
SITE     4 CC2 14 HOH C 734  HOH C 881                                          
SITE     1 CC3  2 PEG B 605  HIS C  93                                          
SITE     1 CC4  7 ARG C  85  ASN C  87  SER C  89  ASP C 125                    
SITE     2 CC4  7 THR C 126  FLC C 603  HOH C1033                               
SITE     1 CC5  5 GLU D 284  ASP D 308  FLC D 602  HOH D 703                    
SITE     2 CC5  5 HOH D 751                                                     
SITE     1 CC6 17 ARG D  85  ASP D 125  LYS D 282  GLU D 284                    
SITE     2 CC6 17 MET D 303  ALA D 305  ARG D 306  GLY D 307                    
SITE     3 CC6 17 ASP D 308  THR D 340  MET D 372   MN D 601                    
SITE     4 CC6 17  NA D 608  HOH D 703  HOH D 738  HOH D 741                    
SITE     5 CC6 17 HOH D 751                                                     
SITE     1 CC7 24 LEU D 443  THR D 444  THR D 445  THR D 446                    
SITE     2 CC7 24 SER D 449  TRP D 494  ARG D 501  GLY D 526                    
SITE     3 CC7 24 ARG D 528  PRO D 529  GLY D 530  SER D 531                    
SITE     4 CC7 24 GLY D 532  TYR D 533  THR D 534  HOH D 705                    
SITE     5 CC7 24 HOH D 709  HOH D 723  HOH D 767  HOH D 769                    
SITE     6 CC7 24 HOH D 777  HOH D 807  HOH D 826  HOH D 889                    
SITE     1 CC8  4 ARG D  68  GLU D  98  ASN D 102  HOH D 756                    
SITE     1 CC9 10 GLY D 333  LYS D 334  PRO D 335  ASP D 369                    
SITE     2 CC9 10 GLN D 451  SER D 454  ARG D 455  ARG D 457                    
SITE     3 CC9 10 CYS D 478  HOH D 808                                          
SITE     1 DC1  5 ARG D 267  GLU D 297  SER D 299  ASP D 300                    
SITE     2 DC1  5 LYS D 334                                                     
SITE     1 DC2  6 LYS D 278  GLN D 451  GLN D 474  HOH D 728                    
SITE     2 DC2  6 HOH D 783  HOH D 799                                          
SITE     1 DC3  8 ARG D  85  ASN D  87  SER D  89  ASP D 125                    
SITE     2 DC3  8 THR D 126  FLC D 602  HOH D 738  HOH D1005                    
CRYST1   78.140  205.078   83.910  90.00  92.15  90.00 P 1 21 1      8          
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      0.012798  0.000000  0.000480        0.00000                         
SCALE2      0.000000  0.004876  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011926        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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