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Database: PDB
Entry: 2NLK
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HEADER    HYDROLASE                               20-OCT-06   2NLK              
TITLE     CRYSTAL STRUCTURE OF D1 AND D2 CATALYTIC DOMAINS OF HUMAN PROTEIN     
TITLE    2 TYROSINE PHOSPHATASE GAMMA (D1+D2 PTPRG)                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE, RECEPTOR TYPE, G VARIANT     
COMPND   3 (FRAGMENT);                                                          
COMPND   4 CHAIN: A;                                                            
COMPND   5 EC: 3.1.3.48;                                                        
COMPND   6 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: PTPRG;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA-R3;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-CH                                   
KEYWDS    PTPRG, R-PTP GAMMA, PROTEIN TYROSINE PHOSPHATASE GAMMA, D3S1249,      
KEYWDS   2 HPTPG, RPTPG, PTPG, D1-D2 CATALYTIC DOMAINS, STRUCTURAL GENOMICS,    
KEYWDS   3 STRUCTURAL GENOMICS CONSORTIUM, SGC, HYDROLASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.FILIPPAKOPOULOS,O.GILEADI,C.JOHANSSON,E.UGOCHUKWU,A.EDWARDS,        
AUTHOR   2 C.ARROWSMITH,M.SUNDSTROM,F.VON DELFT,S.KNAPP,STRUCTURAL GENOMICS     
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   5   13-JUL-11 2NLK    1       VERSN                                    
REVDAT   4   09-JUN-09 2NLK    1       REVDAT                                   
REVDAT   3   24-FEB-09 2NLK    1       VERSN                                    
REVDAT   2   03-FEB-09 2NLK    1       JRNL                                     
REVDAT   1   21-NOV-06 2NLK    0                                                
JRNL        AUTH   A.J.BARR,E.UGOCHUKWU,W.H.LEE,O.N.KING,P.FILIPPAKOPOULOS,     
JRNL        AUTH 2 I.ALFANO,P.SAVITSKY,N.A.BURGESS-BROWN,S.MULLER,S.KNAPP       
JRNL        TITL   LARGE-SCALE STRUCTURAL ANALYSIS OF THE CLASSICAL HUMAN       
JRNL        TITL 2 PROTEIN TYROSINE PHOSPHATOME.                                
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 136   352 2009              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   19167335                                                     
JRNL        DOI    10.1016/J.CELL.2008.11.038                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 37345                          
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) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1864                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2545                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 135                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4386                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 150                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.32000                                              
REMARK   3    B22 (A**2) : -0.78000                                             
REMARK   3    B33 (A**2) : -0.54000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.297         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.240         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.177         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.248        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.905                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.887                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4493 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2970 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6106 ; 1.565 ; 1.937       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7241 ; 1.060 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   547 ; 7.626 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   214 ;32.546 ;24.252       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   742 ;14.692 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;20.899 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   685 ; 0.133 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4985 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   904 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   881 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2988 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2114 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2282 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   188 ; 0.160 ; 0.200       
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):    11 ; 0.123 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    35 ; 0.196 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.103 ; 0.200       
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):  2853 ; 0.641 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1103 ; 0.132 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4479 ; 1.066 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1898 ; 1.651 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1627 ; 2.469 ; 4.500       
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  : 10                                         
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   827        A   852                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5389  12.3228  40.5983              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0081 T22:   0.1720                                     
REMARK   3      T33:   0.0312 T12:   0.0286                                     
REMARK   3      T13:  -0.0709 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9655 L22:   4.2785                                     
REMARK   3      L33:   4.6384 L12:  -1.2886                                     
REMARK   3      L13:  -1.8154 L23:   0.6530                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1218 S12:   0.1914 S13:  -0.1129                       
REMARK   3      S21:  -0.6228 S22:  -0.0649 S23:   0.4043                       
REMARK   3      S31:  -0.0405 S32:  -1.0530 S33:  -0.0569                       
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   853        A   932                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.3011  23.2213  65.1063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0973 T22:   0.0246                                     
REMARK   3      T33:   0.0768 T12:   0.0225                                     
REMARK   3      T13:   0.0036 T23:  -0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4259 L22:   1.7426                                     
REMARK   3      L33:   1.8868 L12:  -0.1039                                     
REMARK   3      L13:   0.1241 L23:   0.3067                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0299 S12:  -0.0486 S13:   0.1152                       
REMARK   3      S21:   0.1716 S22:  -0.0307 S23:  -0.1072                       
REMARK   3      S31:  -0.2875 S32:  -0.0377 S33:   0.0007                       
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   933        A  1015                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4749   5.5455  75.2521              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1205 T22:   0.0311                                     
REMARK   3      T33:   0.0686 T12:   0.0202                                     
REMARK   3      T13:  -0.0306 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7457 L22:   1.1835                                     
REMARK   3      L33:   2.3689 L12:  -0.1012                                     
REMARK   3      L13:  -0.4740 L23:   0.2943                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0160 S12:  -0.1692 S13:  -0.0236                       
REMARK   3      S21:   0.2302 S22:  -0.0380 S23:  -0.0626                       
REMARK   3      S31:   0.1251 S32:   0.0688 S33:   0.0220                       
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  1016        A  1117                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1541   8.5851  57.3829              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0619 T22:   0.0546                                     
REMARK   3      T33:   0.0618 T12:  -0.0104                                     
REMARK   3      T13:   0.0154 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9478 L22:   1.5556                                     
REMARK   3      L33:   1.6473 L12:  -0.1078                                     
REMARK   3      L13:   0.0437 L23:  -0.3136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0026 S12:   0.0666 S13:  -0.0763                       
REMARK   3      S21:  -0.0043 S22:   0.0001 S23:   0.1125                       
REMARK   3      S31:   0.1322 S32:  -0.2967 S33:  -0.0026                       
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  1118        A  1153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.2529 -14.2696  53.2014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1080 T22:   0.0784                                     
REMARK   3      T33:   0.1722 T12:  -0.0172                                     
REMARK   3      T13:   0.0342 T23:  -0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5116 L22:   7.7992                                     
REMARK   3      L33:   6.3172 L12:   0.4637                                     
REMARK   3      L13:   0.8589 L23:  -2.7616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0460 S12:   0.0798 S13:  -0.1984                       
REMARK   3      S21:  -0.0326 S22:   0.1395 S23:   0.7058                       
REMARK   3      S31:  -0.0792 S32:  -0.3538 S33:  -0.0934                       
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  1154        A  1196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.3955 -11.6163  36.1636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0591 T22:   0.1134                                     
REMARK   3      T33:  -0.0208 T12:  -0.0401                                     
REMARK   3      T13:  -0.0792 T23:   0.1192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7096 L22:   0.9045                                     
REMARK   3      L33:   1.2185 L12:  -0.2141                                     
REMARK   3      L13:  -2.3100 L23:  -0.1134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3094 S12:   0.9925 S13:   0.3874                       
REMARK   3      S21:  -0.0667 S22:  -0.1329 S23:  -0.1111                       
REMARK   3      S31:  -0.3728 S32:   0.0250 S33:  -0.1765                       
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 :   A  1204        A  1248                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.4892 -16.9690  45.2705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0718 T22:   0.0277                                     
REMARK   3      T33:   0.0915 T12:  -0.0234                                     
REMARK   3      T13:  -0.0131 T23:  -0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5963 L22:   0.9323                                     
REMARK   3      L33:   0.2185 L12:  -0.0233                                     
REMARK   3      L13:   0.0616 L23:  -0.3674                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0171 S12:   0.3421 S13:   0.1647                       
REMARK   3      S21:  -0.0260 S22:   0.0169 S23:  -0.0057                       
REMARK   3      S31:  -0.0186 S32:   0.1238 S33:   0.0002                       
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 :   A  1249        A  1317                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.6819 -27.7254  48.6838              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1017 T22:  -0.0103                                     
REMARK   3      T33:   0.0865 T12:   0.0382                                     
REMARK   3      T13:  -0.0153 T23:  -0.0183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1211 L22:   2.9952                                     
REMARK   3      L33:   0.6709 L12:   2.6457                                     
REMARK   3      L13:   0.0628 L23:   0.5575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0183 S12:   0.2266 S13:  -0.5907                       
REMARK   3      S21:   0.0550 S22:   0.0652 S23:  -0.0872                       
REMARK   3      S31:   0.2371 S32:   0.0278 S33:  -0.0469                       
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 :   A  1318        A  1377                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0738 -23.8242  54.1910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1107 T22:  -0.0038                                     
REMARK   3      T33:   0.0991 T12:  -0.0266                                     
REMARK   3      T13:  -0.0218 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8389 L22:   0.4682                                     
REMARK   3      L33:   1.0956 L12:   0.3908                                     
REMARK   3      L13:  -1.3775 L23:  -0.5643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0243 S12:   0.0115 S13:   0.0105                       
REMARK   3      S21:   0.0649 S22:   0.0350 S23:  -0.0950                       
REMARK   3      S31:   0.0614 S32:  -0.0306 S33:  -0.0107                       
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 :   A  1378        A  1412                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.5478 -18.3553  48.6746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0339 T22:   0.0200                                     
REMARK   3      T33:   0.1105 T12:  -0.0179                                     
REMARK   3      T13:   0.0039 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8416 L22:   3.5521                                     
REMARK   3      L33:   3.9030 L12:  -0.5363                                     
REMARK   3      L13:   0.4964 L23:  -1.1677                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0166 S12:   0.1367 S13:   0.1596                       
REMARK   3      S21:   0.0336 S22:  -0.0044 S23:   0.3826                       
REMARK   3      S31:   0.0185 S32:  -0.2509 S33:   0.0210                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2NLK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040012.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37418                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.936                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : 0.09900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: PDB ENTRIES 2H4V, 2C7S, 1RPM, 1YF0, 1H02, 1GWZ       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 10K, 100MM IMIDAZOLE, PH 8.0,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       59.25500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.99800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.25500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.99800            
REMARK 290   SMTRY3   4  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: 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 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   826                                                      
REMARK 465     GLY A   898                                                      
REMARK 465     LYS A   899                                                      
REMARK 465     ASP A   900                                                      
REMARK 465     SER A   901                                                      
REMARK 465     LYS A   902                                                      
REMARK 465     GLY A  1143                                                      
REMARK 465     VAL A  1144                                                      
REMARK 465     GLY A  1145                                                      
REMARK 465     GLY A  1146                                                      
REMARK 465     LYS A  1147                                                      
REMARK 465     ASN A  1161                                                      
REMARK 465     ALA A  1162                                                      
REMARK 465     LYS A  1163                                                      
REMARK 465     TYR A  1164                                                      
REMARK 465     VAL A  1165                                                      
REMARK 465     GLU A  1166                                                      
REMARK 465     CYS A  1167                                                      
REMARK 465     LEU A  1197                                                      
REMARK 465     PRO A  1198                                                      
REMARK 465     GLY A  1199                                                      
REMARK 465     MET A  1200                                                      
REMARK 465     LYS A  1201                                                      
REMARK 465     GLY A  1202                                                      
REMARK 465     THR A  1203                                                      
REMARK 465     ASP A  1251                                                      
REMARK 465     ASN A  1252                                                      
REMARK 465     GLN A  1253                                                      
REMARK 465     SER A  1254                                                      
REMARK 465     LEU A  1255                                                      
REMARK 465     ALA A  1256                                                      
REMARK 465     GLU A  1257                                                      
REMARK 465     ASP A  1258                                                      
REMARK 465     GLU A  1259                                                      
REMARK 465     THR A  1413                                                      
REMARK 465     LYS A  1414                                                      
REMARK 465     GLU A  1415                                                      
REMARK 465     ASN A  1416                                                      
REMARK 465     GLY A  1417                                                      
REMARK 465     ASN A  1418                                                      
REMARK 465     GLY A  1419                                                      
REMARK 465     PRO A  1420                                                      
REMARK 465     MET A  1421                                                      
REMARK 465     THR A  1422                                                      
REMARK 465     VAL A  1423                                                      
REMARK 465     ASP A  1424                                                      
REMARK 465     LYS A  1425                                                      
REMARK 465     ASN A  1426                                                      
REMARK 465     GLY A  1427                                                      
REMARK 465     ALA A  1428                                                      
REMARK 465     VAL A  1429                                                      
REMARK 465     LEU A  1430                                                      
REMARK 465     ILE A  1431                                                      
REMARK 465     ALA A  1432                                                      
REMARK 465     ASP A  1433                                                      
REMARK 465     GLU A  1434                                                      
REMARK 465     SER A  1435                                                      
REMARK 465     ASP A  1436                                                      
REMARK 465     PRO A  1437                                                      
REMARK 465     ALA A  1438                                                      
REMARK 465     GLU A  1439                                                      
REMARK 465     SER A  1440                                                      
REMARK 465     MET A  1441                                                      
REMARK 465     GLU A  1442                                                      
REMARK 465     SER A  1443                                                      
REMARK 465     LEU A  1444                                                      
REMARK 465     VAL A  1445                                                      
REMARK 465     ALA A  1446                                                      
REMARK 465     HIS A  1447                                                      
REMARK 465     HIS A  1448                                                      
REMARK 465     HIS A  1449                                                      
REMARK 465     HIS A  1450                                                      
REMARK 465     HIS A  1451                                                      
REMARK 465     HIS A  1452                                                      
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     LYS A 831    CG   CD   CE   NZ                                   
REMARK 470     LYS A 835    CD   CE   NZ                                        
REMARK 470     ILE A 837    CG1  CG2  CD1                                       
REMARK 470     GLU A 873    CD   OE1  OE2                                       
REMARK 470     ARG A 894    NH1  NH2                                            
REMARK 470     ASN A 916    CG   OD1                                            
REMARK 470     LYS A 981    CD   CE   NZ                                        
REMARK 470     LYS A1123    CG   CD   CE   NZ                                   
REMARK 470     ARG A1149    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A1152    CG   CD   CE   NZ                                   
REMARK 470     LYS A1155    CD   CE   NZ                                        
REMARK 470     PHE A1168    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER A1169    OG                                                  
REMARK 470     GLN A1171    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1172    CG   CD   CE   NZ                                   
REMARK 470     GLU A1173    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A1176    CG   CD   CE   NZ                                   
REMARK 470     ARG A1189    NE   CZ   NH1  NH2                                  
REMARK 470     ASP A1204    CG   OD1  OD2                                       
REMARK 470     MET A1212    CE                                                  
REMARK 470     ASN A1218    CG   OD1                                            
REMARK 470     ARG A1266    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A1267    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1268    CG   CD   OE1  OE2                                  
REMARK 470     ILE A1280    CD1                                                 
REMARK 470     LYS A1282    CG   CD   CE   NZ                                   
REMARK 470     ARG A1284    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A1287    CG   CD1  CD2                                       
REMARK 470     GLN A1292    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1318    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    CYS A  1272     O    PHE A  1275              2.10            
REMARK 500   OG   SER A   970     OG1  THR A   979              2.19            
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 A1096   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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    ILE A 950       54.96   -110.21                                   
REMARK 500    ASN A 969     -127.32     61.95                                   
REMARK 500    CYS A1060     -124.01   -135.41                                   
REMARK 500    SER A1061      -67.50    -90.97                                   
REMARK 500    VAL A1064      -50.16   -135.25                                   
REMARK 500    ASN A1087       55.99   -148.00                                   
REMARK 500    LYS A1123     -142.36     60.46                                   
REMARK 500    GLN A1171       -9.58    -54.01                                   
REMARK 500    CYS A1174       44.76    -84.37                                   
REMARK 500    ASN A1175       10.02   -144.35                                   
REMARK 500    ASP A1283     -176.21   -170.12                                   
REMARK 500    ASN A1289       41.22    -96.31                                   
REMARK 500    PRO A1317     -176.18    -65.11                                   
REMARK 500    ASP A1351     -137.48   -115.26                                   
REMARK 500    ALA A1355     -135.43   -112.31                                   
REMARK 500    ARG A1390       89.90   -155.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR A 1101     LEU A 1102                  148.90                    
REMARK 500 LEU A 1102     VAL A 1103                  -70.78                    
REMARK 500 VAL A 1103     GLN A 1104                 -144.38                    
REMARK 500 GLN A 1171     LYS A 1172                 -132.01                    
REMARK 500 LYS A 1172     GLU A 1173                  -83.59                    
REMARK 500 GLU A 1173     CYS A 1174                  135.44                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2NLK A  827  1445  UNP    Q59EE0   Q59EE0_HUMAN   912   1530             
SEQADV 2NLK MET A  826  UNP  Q59EE0              INITIATING METHIONINE          
SEQADV 2NLK ALA A 1446  UNP  Q59EE0              CLONING ARTIFACT               
SEQADV 2NLK HIS A 1447  UNP  Q59EE0              EXPRESSION TAG                 
SEQADV 2NLK HIS A 1448  UNP  Q59EE0              EXPRESSION TAG                 
SEQADV 2NLK HIS A 1449  UNP  Q59EE0              EXPRESSION TAG                 
SEQADV 2NLK HIS A 1450  UNP  Q59EE0              EXPRESSION TAG                 
SEQADV 2NLK HIS A 1451  UNP  Q59EE0              EXPRESSION TAG                 
SEQADV 2NLK HIS A 1452  UNP  Q59EE0              EXPRESSION TAG                 
SEQRES   1 A  627  MET ALA ILE PRO VAL LYS GLN PHE VAL LYS HIS ILE GLY          
SEQRES   2 A  627  GLU LEU TYR SER ASN ASN GLN HIS GLY PHE SER GLU ASP          
SEQRES   3 A  627  PHE GLU GLU VAL GLN ARG CYS THR ALA ASP MET ASN ILE          
SEQRES   4 A  627  THR ALA GLU HIS SER ASN HIS PRO GLU ASN LYS HIS LYS          
SEQRES   5 A  627  ASN ARG TYR ILE ASN ILE LEU ALA TYR ASP HIS SER ARG          
SEQRES   6 A  627  VAL LYS LEU ARG PRO LEU PRO GLY LYS ASP SER LYS HIS          
SEQRES   7 A  627  SER ASP TYR ILE ASN ALA ASN TYR VAL ASP GLY TYR ASN          
SEQRES   8 A  627  LYS ALA LYS ALA TYR ILE ALA THR GLN GLY PRO LEU LYS          
SEQRES   9 A  627  SER THR PHE GLU ASP PHE TRP ARG MET ILE TRP GLU GLN          
SEQRES  10 A  627  ASN THR GLY ILE ILE VAL MET ILE THR ASN LEU VAL GLU          
SEQRES  11 A  627  LYS GLY ARG ARG LYS CYS ASP GLN TYR TRP PRO THR GLU          
SEQRES  12 A  627  ASN SER GLU GLU TYR GLY ASN ILE ILE VAL THR LEU LYS          
SEQRES  13 A  627  SER THR LYS ILE HIS ALA CYS TYR THR VAL ARG ARG PHE          
SEQRES  14 A  627  SER ILE ARG ASN THR LYS VAL LYS LYS GLY GLN LYS GLY          
SEQRES  15 A  627  ASN PRO LYS GLY ARG GLN ASN GLU ARG VAL VAL ILE GLN          
SEQRES  16 A  627  TYR HIS TYR THR GLN TRP PRO ASP MET GLY VAL PRO GLU          
SEQRES  17 A  627  TYR ALA LEU PRO VAL LEU THR PHE VAL ARG ARG SER SER          
SEQRES  18 A  627  ALA ALA ARG MET PRO GLU THR GLY PRO VAL LEU VAL HIS          
SEQRES  19 A  627  CYS SER ALA GLY VAL GLY ARG THR GLY THR TYR ILE VAL          
SEQRES  20 A  627  ILE ASP SER MET LEU GLN GLN ILE LYS ASP LYS SER THR          
SEQRES  21 A  627  VAL ASN VAL LEU GLY PHE LEU LYS HIS ILE ARG THR GLN          
SEQRES  22 A  627  ARG ASN TYR LEU VAL GLN THR GLU GLU GLN TYR ILE PHE          
SEQRES  23 A  627  ILE HIS ASP ALA LEU LEU GLU ALA ILE LEU GLY LYS GLU          
SEQRES  24 A  627  THR GLU VAL SER SER ASN GLN LEU HIS SER TYR VAL ASN          
SEQRES  25 A  627  SER ILE LEU ILE PRO GLY VAL GLY GLY LYS THR ARG LEU          
SEQRES  26 A  627  GLU LYS GLN PHE LYS LEU VAL THR GLN CYS ASN ALA LYS          
SEQRES  27 A  627  TYR VAL GLU CYS PHE SER ALA GLN LYS GLU CYS ASN LYS          
SEQRES  28 A  627  GLU LYS ASN ARG ASN SER SER VAL VAL PRO SER GLU ARG          
SEQRES  29 A  627  ALA ARG VAL GLY LEU ALA PRO LEU PRO GLY MET LYS GLY          
SEQRES  30 A  627  THR ASP TYR ILE ASN ALA SER TYR ILE MET GLY TYR TYR          
SEQRES  31 A  627  ARG SER ASN GLU PHE ILE ILE THR GLN HIS PRO LEU PRO          
SEQRES  32 A  627  HIS THR THR LYS ASP PHE TRP ARG MET ILE TRP ASP HIS          
SEQRES  33 A  627  ASN ALA GLN ILE ILE VAL MET LEU PRO ASP ASN GLN SER          
SEQRES  34 A  627  LEU ALA GLU ASP GLU PHE VAL TYR TRP PRO SER ARG GLU          
SEQRES  35 A  627  GLU SER MET ASN CYS GLU ALA PHE THR VAL THR LEU ILE          
SEQRES  36 A  627  SER LYS ASP ARG LEU CYS LEU SER ASN GLU GLU GLN ILE          
SEQRES  37 A  627  ILE ILE HIS ASP PHE ILE LEU GLU ALA THR GLN ASP ASP          
SEQRES  38 A  627  TYR VAL LEU GLU VAL ARG HIS PHE GLN CYS PRO LYS TRP          
SEQRES  39 A  627  PRO ASN PRO ASP ALA PRO ILE SER SER THR PHE GLU LEU          
SEQRES  40 A  627  ILE ASN VAL ILE LYS GLU GLU ALA LEU THR ARG ASP GLY          
SEQRES  41 A  627  PRO THR ILE VAL HIS ASP GLU TYR GLY ALA VAL SER ALA          
SEQRES  42 A  627  GLY MET LEU CYS ALA LEU THR THR LEU SER GLN GLN LEU          
SEQRES  43 A  627  GLU ASN GLU ASN ALA VAL ASP VAL PHE GLN VAL ALA LYS          
SEQRES  44 A  627  MET ILE ASN LEU MET ARG PRO GLY VAL PHE THR ASP ILE          
SEQRES  45 A  627  GLU GLN TYR GLN PHE ILE TYR LYS ALA MET LEU SER LEU          
SEQRES  46 A  627  VAL SER THR LYS GLU ASN GLY ASN GLY PRO MET THR VAL          
SEQRES  47 A  627  ASP LYS ASN GLY ALA VAL LEU ILE ALA ASP GLU SER ASP          
SEQRES  48 A  627  PRO ALA GLU SER MET GLU SER LEU VAL ALA HIS HIS HIS          
SEQRES  49 A  627  HIS HIS HIS                                                  
FORMUL   2  HOH   *150(H2 O)                                                    
HELIX    1   1 GLN A  832  CYS A  858  1                                  27    
HELIX    2   2 THR A  859  ASN A  863  5                                   5    
HELIX    3   3 HIS A  871  ASN A  878  5                                   8    
HELIX    4   4 LEU A  928  SER A  930  5                                   3    
HELIX    5   5 THR A  931  ASN A  943  1                                  13    
HELIX    6   6 ALA A 1035  ALA A 1048  1                                  14    
HELIX    7   7 VAL A 1064  SER A 1084  1                                  21    
HELIX    8   8 ASN A 1087  ARG A 1096  1                                  10    
HELIX    9   9 THR A 1105  GLY A 1122  1                                  18    
HELIX   10  10 GLN A 1131  LEU A 1140  1                                  10    
HELIX   11  11 THR A 1148  THR A 1158  1                                  11    
HELIX   12  12 LEU A 1227  HIS A 1229  5                                   3    
HELIX   13  13 THR A 1230  ASN A 1242  1                                  13    
HELIX   14  14 PRO A 1325  SER A 1327  5                                   3    
HELIX   15  15 SER A 1328  LEU A 1341  1                                  14    
HELIX   16  16 ALA A 1355  ASN A 1375  1                                  21    
HELIX   17  17 ASP A 1378  ARG A 1390  1                                  13    
HELIX   18  18 ASP A 1396  SER A 1409  1                                  14    
SHEET    1   A 2 ILE A 828  PRO A 829  0                                        
SHEET    2   A 2 THR A1085  VAL A1086 -1  O  VAL A1086   N  ILE A 828           
SHEET    1   B 9 ARG A 890  LYS A 892  0                                        
SHEET    2   B 9 TYR A 906  GLY A 914 -1  O  ALA A 909   N  VAL A 891           
SHEET    3   B 9 LYS A 917  THR A 924 -1  O  ALA A 923   N  ASN A 910           
SHEET    4   B 9 VAL A1056  HIS A1059  1  O  VAL A1058   N  ILE A 922           
SHEET    5   B 9 ILE A 946  MET A 949  1  N  VAL A 948   O  LEU A1057           
SHEET    6   B 9 GLU A1015  TYR A1023  1  O  TYR A1021   N  ILE A 947           
SHEET    7   B 9 TYR A 989  ASN A 998 -1  N  THR A 990   O  HIS A1022           
SHEET    8   B 9 ILE A 976  ILE A 985 -1  N  LYS A 984   O  VAL A 991           
SHEET    9   B 9 SER A 970  TYR A 973 -1  N  GLU A 971   O  VAL A 978           
SHEET    1   C 2 VAL A 954  GLU A 955  0                                        
SHEET    2   C 2 ARG A 958  ARG A 959 -1  O  ARG A 958   N  GLU A 955           
SHEET    1   D 2 VAL A1127  SER A1128  0                                        
SHEET    2   D 2 ALA A1376  VAL A1377 -1  O  VAL A1377   N  VAL A1127           
SHEET    1   E 8 ALA A1208  ILE A1211  0                                        
SHEET    2   E 8 PHE A1220  GLN A1224 -1  O  ILE A1222   N  SER A1209           
SHEET    3   E 8 THR A1347  ASP A1351  1  O  VAL A1349   N  ILE A1221           
SHEET    4   E 8 ILE A1245  MET A1248  1  N  VAL A1247   O  ILE A1348           
SHEET    5   E 8 VAL A1308  GLN A1315  1  O  PHE A1314   N  ILE A1246           
SHEET    6   E 8 GLN A1292  ALA A1302 -1  N  ILE A1294   O  GLN A1315           
SHEET    7   E 8 PHE A1275  CYS A1286 -1  N  ILE A1280   O  ASP A1297           
SHEET    8   E 8 MET A1270  CYS A1272 -1  N  MET A1270   O  VAL A1277           
CISPEP   1 TRP A 1319    PRO A 1320          0       -10.89                     
CRYST1  118.510  133.996   59.084  90.00  90.00  90.00 P 21 21 2     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      0.008438  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007463  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016925        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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