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Database: PDB
Entry: 4X08
LinkDB: 4X08
Original site: 4X08 
HEADER    HYDROLASE                               21-NOV-14   4X08              
TITLE     STRUCTURE OF H128N/ECP MUTANT IN COMPLEX WITH SULPHATE ANIONS AT 1.34 
TITLE    2 ANGSTROMS.                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EOSINOPHIL CATIONIC PROTEIN;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ECP,RIBONUCLEASE 3,RNASE 3;                                 
COMPND   5 EC: 3.1.27.-, 3.1.27.5;                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: RESIDUE 97 CORRESPONDS TO A PROTEIN NATURAL VARIANT   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: BONE MARROW;                                                  
SOURCE   6 CELL: EOSINOPHILS;                                                   
SOURCE   7 GENE: RNASE3, ECP, RNS3;                                             
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET11                                     
KEYWDS    ACTIVE CENTRE MUTATION, SULPHATE, SULPHATE RECOGNITION SITE, ECP,     
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.BLANCO,J.M.GARCIA,V.A.SALAZAR,D.SANCHEZ,M.MOUSSAUOI,E.BOIX        
REVDAT   1   07-OCT-15 4X08    0                                                
JRNL        AUTH   J.A.BLANCO,J.M.GARCIA,V.A.SALAZAR,D.SANCHEZ,M.MOUSSAUOI,     
JRNL        AUTH 2 E.BOIX                                                       
JRNL        TITL   STRUCTURE OF H128N/ECP MUTANT IN COMPLEX WITH SULPHATE       
JRNL        TITL 2 ANIONS AT 1.34 ANGSTROMS.                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.BOIX,D.PULIDO,M.MOUSSAOUI,M.V.NOGUES,S.RUSSI               
REMARK   1  TITL   THE SULFATE-BINDING SITE STRUCTURE OF THE HUMAN EOSINOPHIL   
REMARK   1  TITL 2 CATIONIC PROTEIN AS REVEALED BY A NEW CRYSTAL FORM.          
REMARK   1  REF    J. STRUCT. BIOL.              V. 179     1 2012              
REMARK   1  REFN                   ESSN 1095-8657                               
REMARK   1  PMID   22579681                                                     
REMARK   1  DOI    10.1016/J.JSB.2012.04.023                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   G.MALLORQUI-FERNANDEZ,J.POUS,R.PERACAULA,J.AYMAMI,T.MAEDA,   
REMARK   1  AUTH 2 H.TADA,H.YAMADA,M.SENO,R.DE LLORENS,F.X.GOMIS-RUTH,M.COLL    
REMARK   1  TITL   THREE-DIMENSIONAL CRYSTAL STRUCTURE OF HUMAN EOSINOPHIL      
REMARK   1  TITL 2 CATIONIC PROTEIN (RNASE 3) AT 1.75 A RESOLUTION.             
REMARK   1  REF    J. MOL. BIOL.                 V. 300  1297 2000              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   10903870                                                     
REMARK   1  DOI    10.1006/JMBI.2000.3939                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
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) : 1.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.37                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 54029                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2629                            
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 41.3933 -  3.5739    0.98     2773   136  0.1617 0.1832        
REMARK   3     2  3.5739 -  2.8369    0.99     2719   160  0.1653 0.2114        
REMARK   3     3  2.8369 -  2.4784    0.98     2723   128  0.1834 0.2168        
REMARK   3     4  2.4784 -  2.2518    0.99     2693   150  0.1764 0.2046        
REMARK   3     5  2.2518 -  2.0904    0.99     2693   153  0.1746 0.2074        
REMARK   3     6  2.0904 -  1.9671    0.99     2723   130  0.1716 0.2080        
REMARK   3     7  1.9671 -  1.8686    0.99     2699   133  0.1805 0.2276        
REMARK   3     8  1.8686 -  1.7873    0.99     2736   136  0.1879 0.2176        
REMARK   3     9  1.7873 -  1.7185    1.00     2669   153  0.1949 0.2267        
REMARK   3    10  1.7185 -  1.6592    0.99     2701   153  0.1929 0.2260        
REMARK   3    11  1.6592 -  1.6073    0.99     2726   143  0.1977 0.2402        
REMARK   3    12  1.6073 -  1.5614    0.99     2718   122  0.2054 0.2289        
REMARK   3    13  1.5614 -  1.5202    0.99     2722   121  0.2057 0.2488        
REMARK   3    14  1.5202 -  1.4832    0.99     2706   135  0.2089 0.2678        
REMARK   3    15  1.4832 -  1.4494    0.99     2720   118  0.2225 0.2551        
REMARK   3    16  1.4494 -  1.4186    0.99     2665   150  0.2281 0.2794        
REMARK   3    17  1.4186 -  1.3902    0.99     2679   121  0.2396 0.2712        
REMARK   3    18  1.3902 -  1.3640    0.99     2740   131  0.2612 0.3022        
REMARK   3    19  1.3640 -  1.3396    0.97     2595   156  0.2762 0.2868        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.780           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.007           2474                                  
REMARK   3   ANGLE     :  1.054           3379                                  
REMARK   3   CHIRALITY :  0.049            357                                  
REMARK   3   PLANARITY :  0.006            439                                  
REMARK   3   DIHEDRAL  : 12.362            938                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4X08 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204598.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54033                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 1.820                              
REMARK 200  R MERGE                    (I) : 0.03800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 4A2O                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NEEDLE-SHAPED CRYSTALS                                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS GREW FROM A CRYSTALLISATION     
REMARK 280  CONDITION BASED ON 0.2M LITHIUM SULPHATE, 0.1M TRIS BUFFER,         
REMARK 280  PH8.5 AND 15% PEG4000, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       46.43350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.55200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       46.43350            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.55200            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -170.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 S    SO4 A 204  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 395  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     MET A     0                                                      
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    ASN A    39     O    HOH A   301              1.95            
REMARK 500   O3   SO4 B   203     O    HOH B   301              1.96            
REMARK 500   O2   SO4 A   206     O    HOH A   448              2.04            
REMARK 500   OH   TYR A   122     O    HOH A   441              2.09            
REMARK 500   NH1  ARG B    36     O    HOH B   302              2.10            
REMARK 500   O    HOH B   493     O    HOH B   495              2.10            
REMARK 500   O    HOH B   315     O    HOH B   381              2.11            
REMARK 500   OD1  ASN B   128     O    HOH B   493              2.12            
REMARK 500   NH2  ARG A    66     O3   SO4 A   205              2.12            
REMARK 500   O    HOH B   499     O    HOH B   500              2.14            
REMARK 500   N    LEU A    85     O    HOH A   301              2.15            
REMARK 500   OD1  ASN A    19     OH   TYR B    33              2.16            
REMARK 500   O4   SO4 B   202     O    HOH B   303              2.17            
REMARK 500   O    HOH A   493     O    HOH B   500              2.17            
REMARK 500   O    HOH B   436     O    HOH B   443              2.18            
REMARK 500   ND1  HIS B    82     O    HOH B   450              2.19            
REMARK 500   O    HOH B   419     O    HOH B   485              2.19            
REMARK 500   O    HOH A   435     O    HOH A   472              2.19            
REMARK 500   O    HOH B   455     O    HOH B   469              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN A    32     O1   SO4 A   205     4556     2.04            
REMARK 500   O    HOH A   321     O    HOH A   413     4556     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  91      -94.77    -37.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 503        DISTANCE =  6.50 ANGSTROMS                       
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 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 209                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4A2O   RELATED DB: PDB                                   
REMARK 900 NATIVE PROTEIN COMPLEX AT 1.69 ANGSTROMS                             
REMARK 900 RELATED ID: 4OXB   RELATED DB: PDB                                   
REMARK 900 NATIVE PROTEIN COMPLEX AT 1.50 ANGSTROMS                             
DBREF  4X08 A    1   133  UNP    P12724   ECP_HUMAN       28    160             
DBREF  4X08 B    1   133  UNP    P12724   ECP_HUMAN       28    160             
SEQADV 4X08 MET A    0  UNP  P12724              INITIATING METHIONINE          
SEQADV 4X08 ARG A   97  UNP  P12724    THR   124 VARIANT                        
SEQADV 4X08 ASN A  128  UNP  P12724    HIS   155 ENGINEERED MUTATION            
SEQADV 4X08 MET B    0  UNP  P12724              INITIATING METHIONINE          
SEQADV 4X08 ARG B   97  UNP  P12724    THR   124 VARIANT                        
SEQADV 4X08 ASN B  128  UNP  P12724    HIS   155 ENGINEERED MUTATION            
SEQRES   1 A  134  MET ARG PRO PRO GLN PHE THR ARG ALA GLN TRP PHE ALA          
SEQRES   2 A  134  ILE GLN HIS ILE SER LEU ASN PRO PRO ARG CYS THR ILE          
SEQRES   3 A  134  ALA MET ARG ALA ILE ASN ASN TYR ARG TRP ARG CYS LYS          
SEQRES   4 A  134  ASN GLN ASN THR PHE LEU ARG THR THR PHE ALA ASN VAL          
SEQRES   5 A  134  VAL ASN VAL CYS GLY ASN GLN SER ILE ARG CYS PRO HIS          
SEQRES   6 A  134  ASN ARG THR LEU ASN ASN CYS HIS ARG SER ARG PHE ARG          
SEQRES   7 A  134  VAL PRO LEU LEU HIS CYS ASP LEU ILE ASN PRO GLY ALA          
SEQRES   8 A  134  GLN ASN ILE SER ASN CYS ARG TYR ALA ASP ARG PRO GLY          
SEQRES   9 A  134  ARG ARG PHE TYR VAL VAL ALA CYS ASP ASN ARG ASP PRO          
SEQRES  10 A  134  ARG ASP SER PRO ARG TYR PRO VAL VAL PRO VAL ASN LEU          
SEQRES  11 A  134  ASP THR THR ILE                                              
SEQRES   1 B  134  MET ARG PRO PRO GLN PHE THR ARG ALA GLN TRP PHE ALA          
SEQRES   2 B  134  ILE GLN HIS ILE SER LEU ASN PRO PRO ARG CYS THR ILE          
SEQRES   3 B  134  ALA MET ARG ALA ILE ASN ASN TYR ARG TRP ARG CYS LYS          
SEQRES   4 B  134  ASN GLN ASN THR PHE LEU ARG THR THR PHE ALA ASN VAL          
SEQRES   5 B  134  VAL ASN VAL CYS GLY ASN GLN SER ILE ARG CYS PRO HIS          
SEQRES   6 B  134  ASN ARG THR LEU ASN ASN CYS HIS ARG SER ARG PHE ARG          
SEQRES   7 B  134  VAL PRO LEU LEU HIS CYS ASP LEU ILE ASN PRO GLY ALA          
SEQRES   8 B  134  GLN ASN ILE SER ASN CYS ARG TYR ALA ASP ARG PRO GLY          
SEQRES   9 B  134  ARG ARG PHE TYR VAL VAL ALA CYS ASP ASN ARG ASP PRO          
SEQRES  10 B  134  ARG ASP SER PRO ARG TYR PRO VAL VAL PRO VAL ASN LEU          
SEQRES  11 B  134  ASP THR THR ILE                                              
HET    SO4  A 201       5                                                       
HET    SO4  A 202      10                                                       
HET    SO4  A 203       5                                                       
HET    SO4  A 204       5                                                       
HET    SO4  A 205       5                                                       
HET    SO4  A 206       5                                                       
HET    SO4  A 207       5                                                       
HET    SO4  B 201       5                                                       
HET    SO4  B 202       5                                                       
HET    SO4  B 203       5                                                       
HET    SO4  B 204       5                                                       
HET    SO4  B 205       5                                                       
HET    SO4  B 206      10                                                       
HET    SO4  B 207       5                                                       
HET    SO4  B 208       5                                                       
HET    SO4  B 209       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    16(O4 S 2-)                                                  
FORMUL  19  HOH   *422(H2 O)                                                    
HELIX    1 AA1 THR A    6  ILE A   16  1                                  11    
HELIX    2 AA2 ARG A   22  MET A   27  1                                   6    
HELIX    3 AA3 MET A   27  ASN A   32  1                                   6    
HELIX    4 AA4 THR A   47  CYS A   55  1                                   9    
HELIX    5 AA5 ASN A   92  CYS A   96  5                                   5    
HELIX    6 AA6 THR B    6  ILE B   16  1                                  11    
HELIX    7 AA7 ARG B   22  MET B   27  1                                   6    
HELIX    8 AA8 MET B   27  ASN B   32  1                                   6    
HELIX    9 AA9 THR B   47  CYS B   55  1                                   9    
HELIX   10 AB1 ASN B   92  CYS B   96  5                                   5    
SHEET    1 AA1 3 GLN A  40  LEU A  44  0                                        
SHEET    2 AA1 3 VAL A  78  LEU A  85 -1  O  LEU A  81   N  PHE A  43           
SHEET    3 AA1 3 TYR A  98  ARG A 105 -1  O  ALA A  99   N  ASP A  84           
SHEET    1 AA2 4 SER A  59  ILE A  60  0                                        
SHEET    2 AA2 4 CYS A  71  ARG A  73 -1  O  CYS A  71   N  ILE A  60           
SHEET    3 AA2 4 TYR A 107  ASN A 113 -1  O  VAL A 109   N  HIS A  72           
SHEET    4 AA2 4 VAL A 124  THR A 132 -1  O  VAL A 127   N  ALA A 110           
SHEET    1 AA3 3 GLN B  40  LEU B  44  0                                        
SHEET    2 AA3 3 VAL B  78  LEU B  85 -1  O  LEU B  81   N  PHE B  43           
SHEET    3 AA3 3 TYR B  98  ARG B 105 -1  O  ALA B  99   N  ASP B  84           
SHEET    1 AA4 4 SER B  59  ILE B  60  0                                        
SHEET    2 AA4 4 CYS B  71  ARG B  73 -1  O  CYS B  71   N  ILE B  60           
SHEET    3 AA4 4 TYR B 107  ASN B 113 -1  O  VAL B 109   N  HIS B  72           
SHEET    4 AA4 4 VAL B 124  THR B 132 -1  O  VAL B 127   N  ALA B 110           
SSBOND   1 CYS A   23    CYS A   83                          1555   1555  2.04  
SSBOND   2 CYS A   37    CYS A   96                          1555   1555  2.02  
SSBOND   3 CYS A   55    CYS A  111                          1555   1555  2.04  
SSBOND   4 CYS A   62    CYS A   71                          1555   1555  2.05  
SSBOND   5 CYS B   23    CYS B   83                          1555   1555  2.05  
SSBOND   6 CYS B   37    CYS B   96                          1555   1555  2.03  
SSBOND   7 CYS B   55    CYS B  111                          1555   1555  2.03  
SSBOND   8 CYS B   62    CYS B   71                          1555   1555  2.02  
SITE     1 AC1  4 ARG A   1  ARG A   7  ARG A 101  HOH A 439                    
SITE     1 AC2 10 ARG A  34  LYS A  38  HOH A 304  HOH A 305                    
SITE     2 AC2 10 HOH A 307  HOH A 317  HOH A 380  HOH A 434                    
SITE     3 AC2 10 ARG B 104  HOH B 356                                          
SITE     1 AC3  7 ARG A  77  ARG A 104  HOH A 324  TRP B  35                    
SITE     2 AC3  7 ARG B  36  HOH B 302  HOH B 369                               
SITE     1 AC4  6 ARG A 121  HOH A 310  HOH A 314  HOH A 319                    
SITE     2 AC4  6 HOH A 367  PRO B 123                                          
SITE     1 AC5  8 ARG A  28  ASN A  32  ARG A  61  ARG A  66                    
SITE     2 AC5  8 SO4 A 207  HOH A 312  HOH A 313  ARG B  22                    
SITE     1 AC6  9 ASN A  53  VAL A  54  ASN A  57  SER A  74                    
SITE     2 AC6  9 ARG A  75  PHE A  76  HOH A 302  HOH A 448                    
SITE     3 AC6  9 HOH A 453                                                     
SITE     1 AC7  5 ARG A  28  ARG A  61  SO4 A 205  HOH A 303                    
SITE     2 AC7  5 HOH A 494                                                     
SITE     1 AC8  4 ARG B   1  ARG B 101  HOH B 305  HOH B 330                    
SITE     1 AC9  7 ARG A 104  ARG B  34  LYS B  38  ASN B  39                    
SITE     2 AC9  7 HOH B 303  HOH B 307  HOH B 348                               
SITE     1 AD1 10 ASN A  53  ARG A  75  ASN B  87  PRO B  88                    
SITE     2 AD1 10 GLY B  89  HOH B 301  HOH B 320  HOH B 328                    
SITE     3 AD1 10 HOH B 336  HOH B 357                                          
SITE     1 AD2  6 ASN A  57  GLN A  58  ARG A  75  ASN B  87                    
SITE     2 AD2  6 ARG B  97  HOH B 351                                          
SITE     1 AD3  4 ARG A  36  ARG B  77  ARG B 104  HOH B 304                    
SITE     1 AD4  9 ASN B  57  GLN B  58  ARG B  73  ARG B  75                    
SITE     2 AD4  9 HOH B 309  HOH B 319  HOH B 378  HOH B 422                    
SITE     3 AD4  9 HOH B 431                                                     
SITE     1 AD5  6 GLN A  58  SER A  59  ARG B  97  HOH B 310                    
SITE     2 AD5  6 HOH B 349  HOH B 442                                          
SITE     1 AD6  8 ARG A  22  ARG B  28  ASN B  32  ARG B  61                    
SITE     2 AD6  8 ARG B  66  HOH B 306  HOH B 311  HOH B 379                    
SITE     1 AD7  8 GLN B  58  SER B  59  ARG B  75  HOH B 308                    
SITE     2 AD7  8 HOH B 315  HOH B 362  HOH B 381  HOH B 486                    
CRYST1   92.867   51.104   55.601  90.00 111.09  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010768  0.000000  0.004152        0.00000                         
SCALE2      0.000000  0.019568  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019276        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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