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Database: PDB
Entry: 4L00
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HEADER    TRANSFERASE                             30-MAY-13   4L00              
TITLE     CRYSTAL STRUCTURE OF THE APO JAK1 PSEUDOKINASE DOMAIN                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PSEUDOKINASE DOMAIN (UNP RESIDUES 561-860);                
COMPND   5 SYNONYM: JANUS KINASE 1, JAK-1;                                      
COMPND   6 EC: 2.7.10.2;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: JAK1, JAK1A, JAK1B                                             
KEYWDS    KINASE DOMAIN FOLD, REGULATORY, TRANSFERASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.V.TOMS,M.J.ECK                                                      
REVDAT   3   05-FEB-14 4L00    1       JRNL                                     
REVDAT   2   02-OCT-13 4L00    1       JRNL                                     
REVDAT   1   04-SEP-13 4L00    0                                                
JRNL        AUTH   A.V.TOMS,A.DESHPANDE,R.MCNALLY,Y.JEONG,J.M.ROGERS,C.U.KIM,   
JRNL        AUTH 2 S.M.GRUNER,S.B.FICARRO,J.A.MARTO,M.SATTLER,J.D.GRIFFIN,      
JRNL        AUTH 3 M.J.ECK                                                      
JRNL        TITL   STRUCTURE OF A PSEUDOKINASE-DOMAIN SWITCH THAT CONTROLS      
JRNL        TITL 2 ONCOGENIC ACTIVATION OF JAK KINASES.                         
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  20  1221 2013              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   24013208                                                     
JRNL        DOI    10.1038/NSMB.2673                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 28.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 48311                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2527                            
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) : 3310                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.37                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 182                          
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4481                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 376                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.44000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.47000                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.20000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.130         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.846         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4668 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6328 ; 1.569 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   582 ; 5.167 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   208 ;36.873 ;23.750       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   886 ;15.151 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;23.919 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   707 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3470 ; 0.007 ; 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  : 12                                         
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   564        A   604                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2020  42.7040  48.3820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0913 T22:   0.0429                                     
REMARK   3      T33:   0.1679 T12:   0.0053                                     
REMARK   3      T13:  -0.0217 T23:   0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8850 L22:   0.7423                                     
REMARK   3      L33:   3.4451 L12:   0.6147                                     
REMARK   3      L13:  -0.1808 L23:  -0.1279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0620 S12:   0.1624 S13:   0.4138                       
REMARK   3      S21:  -0.0136 S22:   0.0533 S23:  -0.0336                       
REMARK   3      S31:   0.1328 S32:   0.2580 S33:   0.0087                       
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   615        A   650                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9060  39.6580  50.6470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0418 T22:   0.0301                                     
REMARK   3      T33:   0.0867 T12:  -0.0237                                     
REMARK   3      T13:  -0.0264 T23:   0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6018 L22:   2.1550                                     
REMARK   3      L33:   1.4015 L12:   0.1575                                     
REMARK   3      L13:  -0.0684 L23:  -0.0764                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0658 S12:   0.0482 S13:   0.3082                       
REMARK   3      S21:   0.0805 S22:   0.0292 S23:  -0.0115                       
REMARK   3      S31:  -0.1255 S32:   0.1034 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   651        A   700                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0100  29.4700  40.8220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0830 T22:   0.1088                                     
REMARK   3      T33:   0.0364 T12:  -0.0474                                     
REMARK   3      T13:   0.0187 T23:   0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0203 L22:   2.1815                                     
REMARK   3      L33:   1.4276 L12:   0.9812                                     
REMARK   3      L13:   0.2680 L23:   0.0970                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2157 S12:   0.4068 S13:   0.0406                       
REMARK   3      S21:  -0.3145 S22:   0.1969 S23:  -0.0835                       
REMARK   3      S31:   0.0135 S32:   0.1125 S33:   0.0189                       
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   701        A   750                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2750  28.0800  47.8690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0537 T22:   0.0246                                     
REMARK   3      T33:   0.0354 T12:  -0.0192                                     
REMARK   3      T13:  -0.0010 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1565 L22:   1.6583                                     
REMARK   3      L33:   1.2735 L12:   0.1836                                     
REMARK   3      L13:  -0.0373 L23:  -0.0149                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0595 S12:   0.1187 S13:  -0.0071                       
REMARK   3      S21:  -0.0908 S22:   0.0559 S23:  -0.1198                       
REMARK   3      S31:   0.1071 S32:   0.0286 S33:   0.0036                       
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 :   A   751        A   800                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.3240  29.5340  48.8110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0401 T22:   0.0463                                     
REMARK   3      T33:   0.0611 T12:  -0.0211                                     
REMARK   3      T13:   0.0004 T23:   0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4723 L22:   1.7747                                     
REMARK   3      L33:   1.0785 L12:  -0.1619                                     
REMARK   3      L13:  -0.1019 L23:   0.2600                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0451 S12:   0.1659 S13:   0.1632                       
REMARK   3      S21:  -0.0159 S22:   0.0049 S23:   0.1509                       
REMARK   3      S31:   0.0215 S32:  -0.1375 S33:   0.0402                       
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 :   A   801        A   850                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.8510  18.1860  51.6650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0626 T22:   0.0524                                     
REMARK   3      T33:   0.0624 T12:  -0.0228                                     
REMARK   3      T13:   0.0159 T23:  -0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8898 L22:   2.0024                                     
REMARK   3      L33:   1.5032 L12:   0.1471                                     
REMARK   3      L13:   0.5691 L23:  -0.7208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0302 S12:   0.1393 S13:  -0.1796                       
REMARK   3      S21:  -0.0410 S22:   0.0682 S23:   0.0170                       
REMARK   3      S31:   0.1741 S32:  -0.0324 S33:  -0.0380                       
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   565        B   605                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.7520  53.1280  73.4710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1589 T22:   0.0874                                     
REMARK   3      T33:   0.0817 T12:   0.0063                                     
REMARK   3      T13:  -0.0134 T23:   0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1247 L22:   3.5403                                     
REMARK   3      L33:   3.2178 L12:   0.0405                                     
REMARK   3      L13:  -0.1282 L23:   3.3087                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0146 S12:   0.0512 S13:   0.1459                       
REMARK   3      S21:  -0.2531 S22:  -0.1977 S23:   0.2379                       
REMARK   3      S31:  -0.1662 S32:  -0.1672 S33:   0.1831                       
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   614        B   650                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1880  48.6670  74.3100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0412 T22:   0.0404                                     
REMARK   3      T33:   0.0822 T12:   0.0032                                     
REMARK   3      T13:   0.0135 T23:  -0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9572 L22:   1.5783                                     
REMARK   3      L33:   3.3334 L12:   0.3258                                     
REMARK   3      L13:  -1.0938 L23:   0.3148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0553 S12:   0.0635 S13:   0.1066                       
REMARK   3      S21:  -0.2151 S22:  -0.0556 S23:   0.0856                       
REMARK   3      S31:  -0.1137 S32:  -0.0634 S33:   0.0002                       
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 :   B   651        B   700                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9790  46.4680  87.7360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0885 T22:   0.0664                                     
REMARK   3      T33:   0.0910 T12:   0.0041                                     
REMARK   3      T13:   0.0472 T23:  -0.0569                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4721 L22:   2.1501                                     
REMARK   3      L33:   2.1500 L12:  -0.8725                                     
REMARK   3      L13:   0.1265 L23:   0.0415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0847 S12:  -0.3103 S13:   0.1674                       
REMARK   3      S21:   0.2663 S22:   0.1838 S23:   0.0267                       
REMARK   3      S31:  -0.1467 S32:  -0.0422 S33:  -0.0991                       
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 :   B   701        B   750                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.8790  40.8700  83.6190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0536 T22:   0.0273                                     
REMARK   3      T33:   0.0673 T12:   0.0172                                     
REMARK   3      T13:   0.0000 T23:  -0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2289 L22:   1.7025                                     
REMARK   3      L33:   2.9417 L12:   0.0155                                     
REMARK   3      L13:  -0.9238 L23:  -0.3016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0065 S12:  -0.1693 S13:   0.0516                       
REMARK   3      S21:   0.1863 S22:   0.1152 S23:   0.0303                       
REMARK   3      S31:   0.0178 S32:   0.0025 S33:  -0.1087                       
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 :   B   751        B   800                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.3650  41.0840  82.0900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0367 T22:   0.0787                                     
REMARK   3      T33:   0.1476 T12:   0.0193                                     
REMARK   3      T13:  -0.0175 T23:  -0.0480                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8458 L22:   1.6353                                     
REMARK   3      L33:   2.8977 L12:  -0.0280                                     
REMARK   3      L13:  -0.0769 L23:  -0.3343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1063 S12:  -0.2545 S13:   0.3040                       
REMARK   3      S21:   0.0885 S22:   0.0426 S23:  -0.2988                       
REMARK   3      S31:  -0.0304 S32:   0.3615 S33:   0.0637                       
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 :   B   801        B   850                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5740  30.6440  87.0600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1693 T22:   0.1327                                     
REMARK   3      T33:   0.1241 T12:   0.1166                                     
REMARK   3      T13:  -0.0072 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1681 L22:   4.3252                                     
REMARK   3      L33:   2.8882 L12:   1.8366                                     
REMARK   3      L13:  -0.7841 L23:  -0.6279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0853 S12:  -0.4924 S13:  -0.0914                       
REMARK   3      S21:   0.4948 S22:   0.0498 S23:  -0.2454                       
REMARK   3      S31:   0.3702 S32:   0.3538 S33:   0.0356                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4L00 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080008.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97720                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48311                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
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       40.32800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   557                                                      
REMARK 465     SER A   558                                                      
REMARK 465     THR A   559                                                      
REMARK 465     SER A   560                                                      
REMARK 465     ALA A   561                                                      
REMARK 465     GLN A   562                                                      
REMARK 465     GLU A   563                                                      
REMARK 465     TYR A   605                                                      
REMARK 465     LYS A   606                                                      
REMARK 465     ASP A   607                                                      
REMARK 465     ASP A   608                                                      
REMARK 465     GLU A   609                                                      
REMARK 465     GLY A   610                                                      
REMARK 465     THR A   611                                                      
REMARK 465     SER A   612                                                      
REMARK 465     GLU A   613                                                      
REMARK 465     GLU A   614                                                      
REMARK 465     GLN A   851                                                      
REMARK 465     ASN A   852                                                      
REMARK 465     PRO A   853                                                      
REMARK 465     ASP A   854                                                      
REMARK 465     ILE A   855                                                      
REMARK 465     VAL A   856                                                      
REMARK 465     SER A   857                                                      
REMARK 465     GLU A   858                                                      
REMARK 465     LYS A   859                                                      
REMARK 465     LYS A   860                                                      
REMARK 465     GLY B   557                                                      
REMARK 465     SER B   558                                                      
REMARK 465     THR B   559                                                      
REMARK 465     SER B   560                                                      
REMARK 465     ALA B   561                                                      
REMARK 465     GLN B   562                                                      
REMARK 465     GLU B   563                                                      
REMARK 465     TRP B   564                                                      
REMARK 465     LYS B   606                                                      
REMARK 465     ASP B   607                                                      
REMARK 465     ASP B   608                                                      
REMARK 465     GLU B   609                                                      
REMARK 465     GLY B   610                                                      
REMARK 465     THR B   611                                                      
REMARK 465     SER B   612                                                      
REMARK 465     GLU B   613                                                      
REMARK 465     GLN B   851                                                      
REMARK 465     ASN B   852                                                      
REMARK 465     PRO B   853                                                      
REMARK 465     ASP B   854                                                      
REMARK 465     ILE B   855                                                      
REMARK 465     VAL B   856                                                      
REMARK 465     SER B   857                                                      
REMARK 465     GLU B   858                                                      
REMARK 465     LYS B   859                                                      
REMARK 465     LYS B   860                                                      
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   OD2  ASP B   822     NH1  ARG B   826              1.95            
REMARK 500   O    HOH A  1079     O    HOH A  1112              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 660     -117.89     52.05                                   
REMARK 500    HIS A 712      -71.42    -93.36                                   
REMARK 500    VAL B 661      -53.71     85.58                                   
REMARK 500    HIS B 712      -72.75    -90.15                                   
REMARK 500    MET B 828       54.92    -93.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL B 661        25.0      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 838        24.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4L01   RELATED DB: PDB                                   
DBREF  4L00 A  561   860  UNP    P23458   JAK1_HUMAN     561    860             
DBREF  4L00 B  561   860  UNP    P23458   JAK1_HUMAN     561    860             
SEQADV 4L00 GLY A  557  UNP  P23458              EXPRESSION TAG                 
SEQADV 4L00 SER A  558  UNP  P23458              EXPRESSION TAG                 
SEQADV 4L00 THR A  559  UNP  P23458              EXPRESSION TAG                 
SEQADV 4L00 SER A  560  UNP  P23458              EXPRESSION TAG                 
SEQADV 4L00 GLY B  557  UNP  P23458              EXPRESSION TAG                 
SEQADV 4L00 SER B  558  UNP  P23458              EXPRESSION TAG                 
SEQADV 4L00 THR B  559  UNP  P23458              EXPRESSION TAG                 
SEQADV 4L00 SER B  560  UNP  P23458              EXPRESSION TAG                 
SEQRES   1 A  304  GLY SER THR SER ALA GLN GLU TRP GLN PRO VAL TYR PRO          
SEQRES   2 A  304  MET SER GLN LEU SER PHE ASP ARG ILE LEU LYS LYS ASP          
SEQRES   3 A  304  LEU VAL GLN GLY GLU HIS LEU GLY ARG GLY THR ARG THR          
SEQRES   4 A  304  HIS ILE TYR SER GLY THR LEU MET ASP TYR LYS ASP ASP          
SEQRES   5 A  304  GLU GLY THR SER GLU GLU LYS LYS ILE LYS VAL ILE LEU          
SEQRES   6 A  304  LYS VAL LEU ASP PRO SER HIS ARG ASP ILE SER LEU ALA          
SEQRES   7 A  304  PHE PHE GLU ALA ALA SER MET MET ARG GLN VAL SER HIS          
SEQRES   8 A  304  LYS HIS ILE VAL TYR LEU TYR GLY VAL CYS VAL ARG ASP          
SEQRES   9 A  304  VAL GLU ASN ILE MET VAL GLU GLU PHE VAL GLU GLY GLY          
SEQRES  10 A  304  PRO LEU ASP LEU PHE MET HIS ARG LYS SER ASP VAL LEU          
SEQRES  11 A  304  THR THR PRO TRP LYS PHE LYS VAL ALA LYS GLN LEU ALA          
SEQRES  12 A  304  SER ALA LEU SER TYR LEU GLU ASP LYS ASP LEU VAL HIS          
SEQRES  13 A  304  GLY ASN VAL CYS THR LYS ASN LEU LEU LEU ALA ARG GLU          
SEQRES  14 A  304  GLY ILE ASP SER GLU CYS GLY PRO PHE ILE LYS LEU SER          
SEQRES  15 A  304  ASP PRO GLY ILE PRO ILE THR VAL LEU SER ARG GLN GLU          
SEQRES  16 A  304  CYS ILE GLU ARG ILE PRO TRP ILE ALA PRO GLU CYS VAL          
SEQRES  17 A  304  GLU ASP SER LYS ASN LEU SER VAL ALA ALA ASP LYS TRP          
SEQRES  18 A  304  SER PHE GLY THR THR LEU TRP GLU ILE CYS TYR ASN GLY          
SEQRES  19 A  304  GLU ILE PRO LEU LYS ASP LYS THR LEU ILE GLU LYS GLU          
SEQRES  20 A  304  ARG PHE TYR GLU SER ARG CYS ARG PRO VAL THR PRO SER          
SEQRES  21 A  304  CYS LYS GLU LEU ALA ASP LEU MET THR ARG CYS MET ASN          
SEQRES  22 A  304  TYR ASP PRO ASN GLN ARG PRO PHE PHE ARG ALA ILE MET          
SEQRES  23 A  304  ARG ASP ILE ASN LYS LEU GLU GLU GLN ASN PRO ASP ILE          
SEQRES  24 A  304  VAL SER GLU LYS LYS                                          
SEQRES   1 B  304  GLY SER THR SER ALA GLN GLU TRP GLN PRO VAL TYR PRO          
SEQRES   2 B  304  MET SER GLN LEU SER PHE ASP ARG ILE LEU LYS LYS ASP          
SEQRES   3 B  304  LEU VAL GLN GLY GLU HIS LEU GLY ARG GLY THR ARG THR          
SEQRES   4 B  304  HIS ILE TYR SER GLY THR LEU MET ASP TYR LYS ASP ASP          
SEQRES   5 B  304  GLU GLY THR SER GLU GLU LYS LYS ILE LYS VAL ILE LEU          
SEQRES   6 B  304  LYS VAL LEU ASP PRO SER HIS ARG ASP ILE SER LEU ALA          
SEQRES   7 B  304  PHE PHE GLU ALA ALA SER MET MET ARG GLN VAL SER HIS          
SEQRES   8 B  304  LYS HIS ILE VAL TYR LEU TYR GLY VAL CYS VAL ARG ASP          
SEQRES   9 B  304  VAL GLU ASN ILE MET VAL GLU GLU PHE VAL GLU GLY GLY          
SEQRES  10 B  304  PRO LEU ASP LEU PHE MET HIS ARG LYS SER ASP VAL LEU          
SEQRES  11 B  304  THR THR PRO TRP LYS PHE LYS VAL ALA LYS GLN LEU ALA          
SEQRES  12 B  304  SER ALA LEU SER TYR LEU GLU ASP LYS ASP LEU VAL HIS          
SEQRES  13 B  304  GLY ASN VAL CYS THR LYS ASN LEU LEU LEU ALA ARG GLU          
SEQRES  14 B  304  GLY ILE ASP SER GLU CYS GLY PRO PHE ILE LYS LEU SER          
SEQRES  15 B  304  ASP PRO GLY ILE PRO ILE THR VAL LEU SER ARG GLN GLU          
SEQRES  16 B  304  CYS ILE GLU ARG ILE PRO TRP ILE ALA PRO GLU CYS VAL          
SEQRES  17 B  304  GLU ASP SER LYS ASN LEU SER VAL ALA ALA ASP LYS TRP          
SEQRES  18 B  304  SER PHE GLY THR THR LEU TRP GLU ILE CYS TYR ASN GLY          
SEQRES  19 B  304  GLU ILE PRO LEU LYS ASP LYS THR LEU ILE GLU LYS GLU          
SEQRES  20 B  304  ARG PHE TYR GLU SER ARG CYS ARG PRO VAL THR PRO SER          
SEQRES  21 B  304  CYS LYS GLU LEU ALA ASP LEU MET THR ARG CYS MET ASN          
SEQRES  22 B  304  TYR ASP PRO ASN GLN ARG PRO PHE PHE ARG ALA ILE MET          
SEQRES  23 B  304  ARG ASP ILE ASN LYS LEU GLU GLU GLN ASN PRO ASP ILE          
SEQRES  24 B  304  VAL SER GLU LYS LYS                                          
FORMUL   3  HOH   *376(H2 O)                                                    
HELIX    1   1 TYR A  568  LEU A  573  1                                   6    
HELIX    2   2 LEU A  579  LYS A  581  5                                   3    
HELIX    3   3 HIS A  628  VAL A  645  1                                  18    
HELIX    4   4 PRO A  674  SER A  683  1                                  10    
HELIX    5   5 THR A  687  LYS A  708  1                                  22    
HELIX    6   6 CYS A  716  LYS A  718  5                                   3    
HELIX    7   7 PRO A  743  LEU A  747  5                                   5    
HELIX    8   8 SER A  748  ARG A  755  1                                   8    
HELIX    9   9 ALA A  760  ASP A  766  1                                   7    
HELIX   10  10 SER A  767  LEU A  770  5                                   4    
HELIX   11  11 SER A  771  VAL A  772  5                                   2    
HELIX   12  12 ALA A  773  TYR A  788  1                                  16    
HELIX   13  13 THR A  798  SER A  808  1                                  11    
HELIX   14  14 CYS A  817  MET A  828  1                                  12    
HELIX   15  15 ASP A  831  ARG A  835  5                                   5    
HELIX   16  16 PHE A  837  GLU A  849  1                                  13    
HELIX   17  17 TYR B  568  SER B  574  1                                   7    
HELIX   18  18 LEU B  579  LYS B  581  5                                   3    
HELIX   19  19 PRO B  626  ASP B  630  5                                   5    
HELIX   20  20 ILE B  631  VAL B  645  1                                  15    
HELIX   21  21 PRO B  674  SER B  683  1                                  10    
HELIX   22  22 THR B  687  LYS B  708  1                                  22    
HELIX   23  23 CYS B  716  LYS B  718  5                                   3    
HELIX   24  24 PRO B  743  LEU B  747  5                                   5    
HELIX   25  25 SER B  748  ARG B  755  1                                   8    
HELIX   26  26 ALA B  760  ASP B  766  1                                   7    
HELIX   27  27 SER B  767  SER B  771  5                                   5    
HELIX   28  28 VAL B  772  TYR B  788  1                                  17    
HELIX   29  29 THR B  798  SER B  808  1                                  11    
HELIX   30  30 CYS B  817  MET B  828  1                                  12    
HELIX   31  31 ASP B  831  ARG B  835  5                                   5    
HELIX   32  32 PHE B  837  GLU B  850  1                                  14    
SHEET    1   A 5 LEU A 583  GLY A 592  0                                        
SHEET    2   A 5 THR A 595  LEU A 602 -1  O  ILE A 597   N  LEU A 589           
SHEET    3   A 5 ILE A 617  LEU A 624 -1  O  VAL A 623   N  HIS A 596           
SHEET    4   A 5 GLU A 662  GLU A 668 -1  O  ASN A 663   N  LEU A 624           
SHEET    5   A 5 LEU A 653  ARG A 659 -1  N  ARG A 659   O  GLU A 662           
SHEET    1   B 2 LEU A 720  ARG A 724  0                                        
SHEET    2   B 2 PHE A 734  LEU A 737 -1  O  LYS A 736   N  LEU A 721           
SHEET    1   C 6 ARG B 577  ILE B 578  0                                        
SHEET    2   C 6 LEU B 653  VAL B 658  1  O  VAL B 656   N  ILE B 578           
SHEET    3   C 6 ASN B 663  GLU B 668 -1  O  VAL B 666   N  GLY B 655           
SHEET    4   C 6 LYS B 616  LEU B 624 -1  N  ILE B 620   O  GLU B 667           
SHEET    5   C 6 THR B 595  MET B 603 -1  N  LEU B 602   O  ILE B 617           
SHEET    6   C 6 LEU B 583  GLY B 592 -1  N  LEU B 589   O  ILE B 597           
SHEET    1   D 2 LEU B 720  ARG B 724  0                                        
SHEET    2   D 2 PHE B 734  LEU B 737 -1  O  LYS B 736   N  LEU B 721           
CISPEP   1 ILE A  756    PRO A  757          0         8.68                     
CISPEP   2 ILE B  756    PRO B  757          0         9.81                     
CRYST1   47.026   80.656   76.231  90.00  95.44  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021265  0.000000  0.002027        0.00000                         
SCALE2      0.000000  0.012398  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013177        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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