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Database: PDB
Entry: 4GRY
LinkDB: 4GRY
Original site: 4GRY 
HEADER    HYDROLASE                               27-AUG-12   4GRY              
TITLE     CRYSTAL STRUCTURE OF SHP1 CATALYTIC DOMAIN WITH SO4                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 6;          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PHOSPHATASE DOMAIN UNP RESIDUES 242-528;                   
COMPND   5 SYNONYM: HEMATOPOIETIC CELL PROTEIN-TYROSINE PHOSPHATASE, PROTEIN-   
COMPND   6 TYROSINE PHOSPHATASE 1C, PTP-1C, PROTEIN-TYROSINE PHOSPHATASE SHP-1, 
COMPND   7 SH-PTP1;                                                             
COMPND   8 EC: 3.1.3.48;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HCP, PTP1C, PTPN6, SHP-1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-32                                    
KEYWDS    PHOSPHATASE DOMAIN, HYDROLASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.L.ALICEA-VELAZQUEZ,J.JAKONCIC,T.J.BOGGON                            
REVDAT   5   15-NOV-17 4GRY    1       REMARK                                   
REVDAT   4   08-MAY-13 4GRY    1       TITLE                                    
REVDAT   3   06-MAR-13 4GRY    1       JRNL                                     
REVDAT   2   23-JAN-13 4GRY    1       JRNL                                     
REVDAT   1   19-DEC-12 4GRY    0                                                
JRNL        AUTH   N.L.ALICEA-VELAZQUEZ,J.JAKONCIC,T.J.BOGGON                   
JRNL        TITL   STRUCTURE-GUIDED STUDIES OF THE SHP-1/JAK1 INTERACTION       
JRNL        TITL 2 PROVIDE NEW INSIGHTS INTO PHOSPHATASE CATALYTIC DOMAIN       
JRNL        TITL 3 SUBSTRATE RECOGNITION.                                       
JRNL        REF    J.STRUCT.BIOL.                V. 181   243 2013              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   23296072                                                     
JRNL        DOI    10.1016/J.JSB.2012.12.009                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 29569                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1498                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 25.6790 -  3.7767    0.92     2775   154  0.1818 0.2057        
REMARK   3     2  3.7767 -  2.9991    0.80     2292   120  0.1759 0.1804        
REMARK   3     3  2.9991 -  2.6205    1.00     2844   154  0.1841 0.2369        
REMARK   3     4  2.6205 -  2.3810    1.00     2837   132  0.1721 0.2369        
REMARK   3     5  2.3810 -  2.2105    0.53     1501    81  0.1759 0.2270        
REMARK   3     6  2.2105 -  2.0802    0.99     2780   139  0.1795 0.2193        
REMARK   3     7  2.0802 -  1.9761    1.00     2759   153  0.1845 0.2376        
REMARK   3     8  1.9761 -  1.8901    0.77     2162   119  0.3018 0.3773        
REMARK   3     9  1.8901 -  1.8173    0.98     2706   151  0.2405 0.3065        
REMARK   3    10  1.8173 -  1.7547    0.98     2722   157  0.2097 0.3046        
REMARK   3    11  1.7547 -  1.6998    0.97     2693   138  0.2488 0.2854        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 49.22                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.260           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.51640                                             
REMARK   3    B22 (A**2) : 0.32590                                              
REMARK   3    B33 (A**2) : 4.19050                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           2290                                  
REMARK   3   ANGLE     :  0.994           3113                                  
REMARK   3   CHIRALITY :  0.073            336                                  
REMARK   3   PLANARITY :  0.004            405                                  
REMARK   3   DIHEDRAL  : 13.686            868                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 243:273)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7911   1.0499   7.5585              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2393 T22:   0.2890                                     
REMARK   3      T33:   0.2370 T12:  -0.0511                                     
REMARK   3      T13:  -0.0165 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0296 L22:   2.1622                                     
REMARK   3      L33:   4.6809 L12:  -0.2363                                     
REMARK   3      L13:  -0.3564 L23:   3.1781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0457 S12:  -0.0031 S13:  -0.0249                       
REMARK   3      S21:   0.5364 S22:  -0.0806 S23:   0.0955                       
REMARK   3      S31:   0.7385 S32:  -0.2949 S33:   0.1410                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 274:386)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.0119  15.8719  21.0220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1042 T22:   0.0697                                     
REMARK   3      T33:   0.0659 T12:   0.0045                                     
REMARK   3      T13:  -0.0081 T23:  -0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2608 L22:   1.4485                                     
REMARK   3      L33:   1.3410 L12:  -0.0192                                     
REMARK   3      L13:   0.0055 L23:   0.3957                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0180 S12:   0.0841 S13:   0.0958                       
REMARK   3      S21:   0.0288 S22:   0.0321 S23:  -0.0041                       
REMARK   3      S31:  -0.0220 S32:   0.0002 S33:  -0.0043                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 387:457)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4946  12.3131  20.1190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0751 T22:   0.0979                                     
REMARK   3      T33:   0.1402 T12:  -0.0027                                     
REMARK   3      T13:  -0.0330 T23:  -0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6753 L22:   2.2978                                     
REMARK   3      L33:   1.9675 L12:  -0.4610                                     
REMARK   3      L13:  -0.0104 L23:   0.4807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0233 S12:   0.0861 S13:   0.0580                       
REMARK   3      S21:   0.0420 S22:   0.1919 S23:  -0.2107                       
REMARK   3      S31:  -0.0602 S32:   0.2183 S33:  -0.1530                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 458:525)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7511  -4.0665  11.6888              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1912 T22:   0.1681                                     
REMARK   3      T33:   0.1254 T12:   0.0044                                     
REMARK   3      T13:  -0.0257 T23:  -0.0616                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8232 L22:   1.0963                                     
REMARK   3      L33:   1.3712 L12:  -0.2524                                     
REMARK   3      L13:   0.3515 L23:  -0.2059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0402 S12:   0.2883 S13:  -0.3244                       
REMARK   3      S21:  -0.0560 S22:  -0.0190 S23:  -0.0944                       
REMARK   3      S31:   0.2392 S32:   0.1222 S33:  -0.0405                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4GRY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000074561.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9801                             
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL CUT                
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29703                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.5450                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.40000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.530                              
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 ENTRY 1FPR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.5 M AMMONIUM         
REMARK 280  SULFATE, 3% PEG400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
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,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       22.82200            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.43850            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       22.82200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       55.43850            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 898  LIES ON A SPECIAL POSITION.                          
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   241                                                      
REMARK 465     SER A   242                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     PRO A   314                                                      
REMARK 465     ASP A   315                                                      
REMARK 465     GLU A   316                                                      
REMARK 465     VAL A   354                                                      
REMARK 465     GLU A   355                                                      
REMARK 465     LYS A   356                                                      
REMARK 465     GLY A   357                                                      
REMARK 465     ARG A   358                                                      
REMARK 465     ASN A   359                                                      
REMARK 465     LYS A   360                                                      
REMARK 465     CYS A   361                                                      
REMARK 465     LEU A   526                                                      
REMARK 465     GLN A   527                                                      
REMARK 465     SER A   528                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  249   CD                                                  
REMARK 480     GLU A  329   CD                                                  
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    TYR A 364       26.60   -140.39                                   
REMARK 500    ILE A 457      -37.33   -135.97                                   
REMARK 500    VAL A 499       88.44     64.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602                 
DBREF  4GRY A  243   528  UNP    P29350   PTN6_HUMAN     243    528             
SEQADV 4GRY GLY A  241  UNP  P29350              EXPRESSION TAG                 
SEQADV 4GRY SER A  242  UNP  P29350              EXPRESSION TAG                 
SEQADV 4GRY SER A  453  UNP  P29350    CYS   453 ENGINEERED MUTATION            
SEQRES   1 A  288  GLY SER GLY PHE TRP GLU GLU PHE GLU SER LEU GLN LYS          
SEQRES   2 A  288  GLN GLU VAL LYS ASN LEU HIS GLN ARG LEU GLU GLY GLN          
SEQRES   3 A  288  ARG PRO GLU ASN LYS GLY LYS ASN ARG TYR LYS ASN ILE          
SEQRES   4 A  288  LEU PRO PHE ASP HIS SER ARG VAL ILE LEU GLN GLY ARG          
SEQRES   5 A  288  ASP SER ASN ILE PRO GLY SER ASP TYR ILE ASN ALA ASN          
SEQRES   6 A  288  TYR ILE LYS ASN GLN LEU LEU GLY PRO ASP GLU ASN ALA          
SEQRES   7 A  288  LYS THR TYR ILE ALA SER GLN GLY CYS LEU GLU ALA THR          
SEQRES   8 A  288  VAL ASN ASP PHE TRP GLN MET ALA TRP GLN GLU ASN SER          
SEQRES   9 A  288  ARG VAL ILE VAL MET THR THR ARG GLU VAL GLU LYS GLY          
SEQRES  10 A  288  ARG ASN LYS CYS VAL PRO TYR TRP PRO GLU VAL GLY MET          
SEQRES  11 A  288  GLN ARG ALA TYR GLY PRO TYR SER VAL THR ASN CYS GLY          
SEQRES  12 A  288  GLU HIS ASP THR THR GLU TYR LYS LEU ARG THR LEU GLN          
SEQRES  13 A  288  VAL SER PRO LEU ASP ASN GLY ASP LEU ILE ARG GLU ILE          
SEQRES  14 A  288  TRP HIS TYR GLN TYR LEU SER TRP PRO ASP HIS GLY VAL          
SEQRES  15 A  288  PRO SER GLU PRO GLY GLY VAL LEU SER PHE LEU ASP GLN          
SEQRES  16 A  288  ILE ASN GLN ARG GLN GLU SER LEU PRO HIS ALA GLY PRO          
SEQRES  17 A  288  ILE ILE VAL HIS SER SER ALA GLY ILE GLY ARG THR GLY          
SEQRES  18 A  288  THR ILE ILE VAL ILE ASP MET LEU MET GLU ASN ILE SER          
SEQRES  19 A  288  THR LYS GLY LEU ASP CYS ASP ILE ASP ILE GLN LYS THR          
SEQRES  20 A  288  ILE GLN MET VAL ARG ALA GLN ARG SER GLY MET VAL GLN          
SEQRES  21 A  288  THR GLU ALA GLN TYR LYS PHE ILE TYR VAL ALA ILE ALA          
SEQRES  22 A  288  GLN PHE ILE GLU THR THR LYS LYS LYS LEU GLU VAL LEU          
SEQRES  23 A  288  GLN SER                                                      
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  HOH   *228(H2 O)                                                    
HELIX    1   1 GLY A  243  GLN A  254  1                                  12    
HELIX    2   2 ARG A  262  ARG A  267  1                                   6    
HELIX    3   3 PRO A  268  ASN A  274  5                                   7    
HELIX    4   4 PHE A  282  HIS A  284  5                                   3    
HELIX    5   5 LEU A  328  ALA A  330  5                                   3    
HELIX    6   6 THR A  331  GLU A  342  1                                  12    
HELIX    7   7 PRO A  426  SER A  442  1                                  17    
HELIX    8   8 ILE A  457  GLY A  477  1                                  21    
HELIX    9   9 ASP A  483  ALA A  493  1                                  11    
HELIX   10  10 THR A  501  GLU A  524  1                                  24    
SHEET    1   A 9 ARG A 286  ILE A 288  0                                        
SHEET    2   A 9 TYR A 301  ILE A 307 -1  O  ALA A 304   N  VAL A 287           
SHEET    3   A 9 TYR A 321  GLN A 325 -1  O  ALA A 323   N  ASN A 305           
SHEET    4   A 9 ILE A 449  SER A 453  1  O  VAL A 451   N  ILE A 322           
SHEET    5   A 9 VAL A 346  MET A 349  1  N  VAL A 348   O  ILE A 450           
SHEET    6   A 9 ARG A 407  TYR A 414  1  O  TYR A 412   N  MET A 349           
SHEET    7   A 9 TYR A 390  PRO A 399 -1  N  LEU A 395   O  ILE A 409           
SHEET    8   A 9 TYR A 377  ASP A 386 -1  N  CYS A 382   O  THR A 394           
SHEET    9   A 9 GLN A 371  TYR A 374 -1  N  TYR A 374   O  TYR A 377           
SITE     1 AC1 11 SER A 453  SER A 454  ALA A 455  GLY A 456                    
SITE     2 AC1 11 ILE A 457  GLY A 458  ARG A 459  SO4 A 602                    
SITE     3 AC1 11 HOH A 751  HOH A 782  HOH A 828                               
SITE     1 AC2  5 PRO A 418  HIS A 420  GLY A 421  ARG A 459                    
SITE     2 AC2  5 SO4 A 601                                                     
CRYST1   45.644   57.281  110.877  90.00  90.00  90.00 P 21 2 21     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      0.021909  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017458  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009019        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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