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Database: PDB
Entry: 1D1Z
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HEADER    GENE REGULATION                         22-SEP-99   1D1Z              
TITLE     CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SAP SH2 DOMAIN;                                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: SAP SH2 DOMAIN (RESIDUES 1-104);                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: T7 EXPRESSION VECTOR                       
KEYWDS    SH2 DOMAINS, GENE REGULATION                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.POY,M.B.YAFFE,J.SAYOS,K.SAXENA,M.J.ECK                              
REVDAT   7   31-JAN-18 1D1Z    1       REMARK                                   
REVDAT   6   24-JAN-18 1D1Z    1       JRNL                                     
REVDAT   5   13-JUL-11 1D1Z    1       VERSN                                    
REVDAT   4   24-FEB-09 1D1Z    1       VERSN                                    
REVDAT   3   22-MAR-05 1D1Z    1       SOURCE JRNL   REMARK DBREF               
REVDAT   3 2                   1       MASTER                                   
REVDAT   2   23-MAY-00 1D1Z    1       JRNL                                     
REVDAT   1   13-OCT-99 1D1Z    0                                                
JRNL        AUTH   F.POY,M.B.YAFFE,J.SAYOS,K.SAXENA,M.MORRA,J.SUMEGI,           
JRNL        AUTH 2 L.C.CANTLEY,C.TERHORST,M.J.ECK                               
JRNL        TITL   CRYSTAL STRUCTURES OF THE XLP PROTEIN SAP REVEAL A CLASS OF  
JRNL        TITL 2 SH2 DOMAINS WITH EXTENDED, PHOSPHOTYROSINE-INDEPENDENT       
JRNL        TITL 3 SEQUENCE RECOGNITION.                                        
JRNL        REF    MOL.CELL                      V.   4   555 1999              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   10549287                                                     
JRNL        DOI    10.1016/S1097-2765(00)80206-3                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.SAYOS,C.WU,M.MORRA,N.WANG,C.TERHORST                       
REMARK   1  TITL   THE X-LINKED LYMPHOPROLIFERATIVE-DISEASE GENE PRODUCT SAP    
REMARK   1  TITL 2 REGULATES SIGNALS INDUCED THROUGH THE CO-RECEPTOR SLAM       
REMARK   1  REF    NATURE                        V. 395   462 1998              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  DOI    10.1038/26683                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.147                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.139                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.187                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 78862                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 3160                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 35                                            
REMARK   3   SOLVENT ATOMS      : 628                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.011                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.029                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1D1Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000009724.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : PRINCETON 2K                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83110                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.64 M AMMONIUM SULFATE, 100 MM SODIUM   
REMARK 280  CITRATE, PH 5.6, AND 10 MM DTT, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 22K, TEMPERATURE 295.0K                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -147.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000       19.69245            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000      -26.69970            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000      -57.96820            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       20.06196            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       35.56920            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -57.96820            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  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  1001                                                      
REMARK 465     ASP A  1002                                                      
REMARK 465     ALA A  1003                                                      
REMARK 465     MET B  2001                                                      
REMARK 465     ASP B  2002                                                      
REMARK 465     ALA B  2003                                                      
REMARK 465     GLN B  2058                                                      
REMARK 465     THR B  2059                                                      
REMARK 465     GLU B  2060                                                      
REMARK 465     THR B  2061                                                      
REMARK 465     GLY B  2062                                                      
REMARK 465     SER B  2063                                                      
REMARK 465     TRP B  2064                                                      
REMARK 465     MET C  3001                                                      
REMARK 465     ASP C  3002                                                      
REMARK 465     ALA C  3003                                                      
REMARK 465     MET D  4001                                                      
REMARK 465     ASP D  4002                                                      
REMARK 465     ALA D  4003                                                      
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 A1032   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B2013   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG B2055   NE  -  CZ  -  NH2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG B2075   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    TYR C3050   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG C3055   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    THR C3059   O   -  C   -  N   ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG C3075   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG D4013   NH1 -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ARG D4013   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG D4055   CD  -  NE  -  CZ  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG D4075   CD  -  NE  -  CZ  ANGL. DEV. =  -8.9 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    THR A1068     -159.21   -120.93                                   
REMARK 500    GLN A1099      -38.35   -132.78                                   
REMARK 500    LYS B2010      -33.21     76.29                                   
REMARK 500    THR B2068     -159.86   -122.68                                   
REMARK 500    THR C3068     -151.79   -114.08                                   
REMARK 500    THR D4068     -115.90   -125.87                                   
REMARK 500    GLN D4099      -36.86   -133.14                                   
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 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 5003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 5005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 5006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5007                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D4W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1D4T   RELATED DB: PDB                                   
DBREF  1D1Z A 1001  1104  UNP    O60880   SH21A_HUMAN      1    104             
DBREF  1D1Z B 2001  2104  UNP    O60880   SH21A_HUMAN      1    104             
DBREF  1D1Z C 3001  3104  UNP    O60880   SH21A_HUMAN      1    104             
DBREF  1D1Z D 4001  4104  UNP    O60880   SH21A_HUMAN      1    104             
SEQRES   1 A  104  MET ASP ALA VAL ALA VAL TYR HIS GLY LYS ILE SER ARG          
SEQRES   2 A  104  GLU THR GLY GLU LYS LEU LEU LEU ALA THR GLY LEU ASP          
SEQRES   3 A  104  GLY SER TYR LEU LEU ARG ASP SER GLU SER VAL PRO GLY          
SEQRES   4 A  104  VAL TYR CYS LEU CYS VAL LEU TYR HIS GLY TYR ILE TYR          
SEQRES   5 A  104  THR TYR ARG VAL SER GLN THR GLU THR GLY SER TRP SER          
SEQRES   6 A  104  ALA GLU THR ALA PRO GLY VAL HIS LYS ARG TYR PHE ARG          
SEQRES   7 A  104  LYS ILE LYS ASN LEU ILE SER ALA PHE GLN LYS PRO ASP          
SEQRES   8 A  104  GLN GLY ILE VAL ILE PRO LEU GLN TYR PRO VAL GLU LYS          
SEQRES   1 B  104  MET ASP ALA VAL ALA VAL TYR HIS GLY LYS ILE SER ARG          
SEQRES   2 B  104  GLU THR GLY GLU LYS LEU LEU LEU ALA THR GLY LEU ASP          
SEQRES   3 B  104  GLY SER TYR LEU LEU ARG ASP SER GLU SER VAL PRO GLY          
SEQRES   4 B  104  VAL TYR CYS LEU CYS VAL LEU TYR HIS GLY TYR ILE TYR          
SEQRES   5 B  104  THR TYR ARG VAL SER GLN THR GLU THR GLY SER TRP SER          
SEQRES   6 B  104  ALA GLU THR ALA PRO GLY VAL HIS LYS ARG TYR PHE ARG          
SEQRES   7 B  104  LYS ILE LYS ASN LEU ILE SER ALA PHE GLN LYS PRO ASP          
SEQRES   8 B  104  GLN GLY ILE VAL ILE PRO LEU GLN TYR PRO VAL GLU LYS          
SEQRES   1 C  104  MET ASP ALA VAL ALA VAL TYR HIS GLY LYS ILE SER ARG          
SEQRES   2 C  104  GLU THR GLY GLU LYS LEU LEU LEU ALA THR GLY LEU ASP          
SEQRES   3 C  104  GLY SER TYR LEU LEU ARG ASP SER GLU SER VAL PRO GLY          
SEQRES   4 C  104  VAL TYR CYS LEU CYS VAL LEU TYR HIS GLY TYR ILE TYR          
SEQRES   5 C  104  THR TYR ARG VAL SER GLN THR GLU THR GLY SER TRP SER          
SEQRES   6 C  104  ALA GLU THR ALA PRO GLY VAL HIS LYS ARG TYR PHE ARG          
SEQRES   7 C  104  LYS ILE LYS ASN LEU ILE SER ALA PHE GLN LYS PRO ASP          
SEQRES   8 C  104  GLN GLY ILE VAL ILE PRO LEU GLN TYR PRO VAL GLU LYS          
SEQRES   1 D  104  MET ASP ALA VAL ALA VAL TYR HIS GLY LYS ILE SER ARG          
SEQRES   2 D  104  GLU THR GLY GLU LYS LEU LEU LEU ALA THR GLY LEU ASP          
SEQRES   3 D  104  GLY SER TYR LEU LEU ARG ASP SER GLU SER VAL PRO GLY          
SEQRES   4 D  104  VAL TYR CYS LEU CYS VAL LEU TYR HIS GLY TYR ILE TYR          
SEQRES   5 D  104  THR TYR ARG VAL SER GLN THR GLU THR GLY SER TRP SER          
SEQRES   6 D  104  ALA GLU THR ALA PRO GLY VAL HIS LYS ARG TYR PHE ARG          
SEQRES   7 D  104  LYS ILE LYS ASN LEU ILE SER ALA PHE GLN LYS PRO ASP          
SEQRES   8 D  104  GLN GLY ILE VAL ILE PRO LEU GLN TYR PRO VAL GLU LYS          
HET    SO4  A5001       5                                                       
HET    SO4  B5002       5                                                       
HET    SO4  B5007       5                                                       
HET    SO4  C5003       5                                                       
HET    SO4  D5004       5                                                       
HET    SO4  D5005       5                                                       
HET    SO4  D5006       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    7(O4 S 2-)                                                   
FORMUL  12  HOH   *628(H2 O)                                                    
HELIX    1   1 SER A 1012  GLY A 1024  1                                  13    
HELIX    2   2 LYS A 1079  PHE A 1087  1                                   9    
HELIX    3   3 SER B 2012  GLY B 2024  1                                  13    
HELIX    4   4 LYS B 2079  PHE B 2087  1                                   9    
HELIX    5   5 SER C 3012  GLY C 3024  1                                  13    
HELIX    6   6 LYS C 3079  PHE C 3087  1                                   9    
HELIX    7   7 SER D 4012  GLY D 4024  1                                  13    
HELIX    8   8 LYS D 4079  PHE D 4087  1                                   9    
SHEET    1   A 5 TRP A1064  ALA A1066  0                                        
SHEET    2   A 5 TYR A1050  GLN A1058 -1  N  SER A1057   O  SER A1065           
SHEET    3   A 5 TYR A1041  TYR A1047 -1  N  TYR A1041   O  VAL A1056           
SHEET    4   A 5 SER A1028  ASP A1033 -1  O  SER A1028   N  LEU A1046           
SHEET    5   A 5 TYR A1007  HIS A1008  1  N  HIS A1008   O  LEU A1031           
SHEET    1  A1 5 TRP A1064  ALA A1066  0                                        
SHEET    2  A1 5 TYR A1050  GLN A1058 -1  N  SER A1057   O  SER A1065           
SHEET    3  A1 5 TYR A1041  TYR A1047 -1  N  TYR A1041   O  VAL A1056           
SHEET    4  A1 5 SER A1028  ASP A1033 -1  O  SER A1028   N  LEU A1046           
SHEET    5  A1 5 TYR A1100  PRO A1101  1  O  TYR A1100   N  TYR A1029           
SHEET    1   B 4 TYR B2050  VAL B2056  0                                        
SHEET    2   B 4 TYR B2041  TYR B2047 -1  N  TYR B2041   O  VAL B2056           
SHEET    3   B 4 SER B2028  ASP B2033 -1  O  SER B2028   N  LEU B2046           
SHEET    4   B 4 TYR B2007  HIS B2008  1  N  HIS B2008   O  LEU B2031           
SHEET    1  B1 4 TYR B2050  VAL B2056  0                                        
SHEET    2  B1 4 TYR B2041  TYR B2047 -1  N  TYR B2041   O  VAL B2056           
SHEET    3  B1 4 SER B2028  ASP B2033 -1  O  SER B2028   N  LEU B2046           
SHEET    4  B1 4 TYR B2100  PRO B2101  1  O  TYR B2100   N  TYR B2029           
SHEET    1   C 5 TRP C3064  ALA C3066  0                                        
SHEET    2   C 5 TYR C3050  GLN C3058 -1  N  SER C3057   O  SER C3065           
SHEET    3   C 5 TYR C3041  TYR C3047 -1  N  TYR C3041   O  VAL C3056           
SHEET    4   C 5 SER C3028  ASP C3033 -1  O  SER C3028   N  LEU C3046           
SHEET    5   C 5 TYR C3007  HIS C3008  1  N  HIS C3008   O  LEU C3031           
SHEET    1  C1 5 TRP C3064  ALA C3066  0                                        
SHEET    2  C1 5 TYR C3050  GLN C3058 -1  N  SER C3057   O  SER C3065           
SHEET    3  C1 5 TYR C3041  TYR C3047 -1  N  TYR C3041   O  VAL C3056           
SHEET    4  C1 5 SER C3028  ASP C3033 -1  O  SER C3028   N  LEU C3046           
SHEET    5  C1 5 TYR C3100  PRO C3101  1  O  TYR C3100   N  TYR C3029           
SHEET    1   D 5 TRP D4064  ALA D4066  0                                        
SHEET    2   D 5 TYR D4050  GLN D4058 -1  N  SER D4057   O  SER D4065           
SHEET    3   D 5 TYR D4041  TYR D4047 -1  N  TYR D4041   O  VAL D4056           
SHEET    4   D 5 SER D4028  ASP D4033 -1  O  SER D4028   N  LEU D4046           
SHEET    5   D 5 TYR D4007  HIS D4008  1  N  HIS D4008   O  LEU D4031           
SHEET    1  D1 5 TRP D4064  ALA D4066  0                                        
SHEET    2  D1 5 TYR D4050  GLN D4058 -1  N  SER D4057   O  SER D4065           
SHEET    3  D1 5 TYR D4041  TYR D4047 -1  N  TYR D4041   O  VAL D4056           
SHEET    4  D1 5 SER D4028  ASP D4033 -1  O  SER D4028   N  LEU D4046           
SHEET    5  D1 5 TYR D4100  PRO D4101  1  O  TYR D4100   N  TYR D4029           
SITE     1 AC1  7 ARG A1032  SER A1034  GLU A1035  SER A1036                    
SITE     2 AC1  7 HOH A6114  HOH A6125  HOH A6300                               
SITE     1 AC2  8 ARG B2032  SER B2034  GLU B2035  SER B2036                    
SITE     2 AC2  8 CYS B2042  ARG B2055  HOH B6374  ARG D4013                    
SITE     1 AC3  9 ARG C3032  SER C3034  GLU C3035  SER C3036                    
SITE     2 AC3  9 CYS C3042  ARG C3055  HOH C6138  HOH C6194                    
SITE     3 AC3  9 HOH C6280                                                     
SITE     1 AC4  8 ARG D4013  ARG D4032  SER D4034  GLU D4035                    
SITE     2 AC4  8 SER D4036  CYS D4042  ARG D4055  HOH D6176                    
SITE     1 AC5  9 PHE A1077  ARG A1078  LYS A1079  ASN A1082                    
SITE     2 AC5  9 HOH A6266  THR D4061  SER D4063  HOH D6018                    
SITE     3 AC5  9 HOH D6475                                                     
SITE     1 AC6  8 HIS A1073  ARG A1075  HOH A6196  THR D4059                    
SITE     2 AC6  8 GLU D4060  HOH D6006  HOH D6462  HOH D6611                    
SITE     1 AC7  5 PHE B2077  ARG B2078  LYS B2079  ASN B2082                    
SITE     2 AC7  5 HOH B6627                                                     
CRYST1   32.480   62.270   65.090  65.71  78.67  89.66 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.030788 -0.000183 -0.006708        0.00000                         
SCALE2      0.000000  0.016059 -0.007397        0.00000                         
SCALE3      0.000000  0.000000  0.017251        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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