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Database: PDB
Entry: 4WXS
LinkDB: 4WXS
Original site: 4WXS 
HEADER    PROTEIN BINDING                         14-NOV-14   4WXS              
TITLE     CRYSTAL STRUCTURE OF THE E396D SNP VARIANT OF THE MYOCILIN            
TITLE    2 OLFACTOMEDIN DOMAIN                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOCILIN;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MYOCILIN 55 KDA SUBUNIT,TRABECULAR MESHWORK-INDUCED         
COMPND   5 GLUCOCORTICOID RESPONSE PROTEIN;                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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: MYOC, GLC1A, TIGR;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BETA PROPELLER, 5 BLADED PROPELLER, OLFACTOMEDIN, PROTEIN BINDING     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.K.DONEGAN,D.M.FREEMAN,R.L.LIEBERMAN                                 
REVDAT   1   01-APR-15 4WXS    0                                                
JRNL        AUTH   R.K.DONEGAN,S.E.HILL,D.M.FREEMAN,E.NGUYEN,S.D.ORWIG,         
JRNL        AUTH 2 K.C.TURNAGE,R.L.LIEBERMAN                                    
JRNL        TITL   STRUCTURAL BASIS FOR MISFOLDING IN MYOCILIN-ASSOCIATED       
JRNL        TITL 2 GLAUCOMA.                                                    
JRNL        REF    HUM.MOL.GENET.                V.  24  2111 2015              
JRNL        REFN                   ESSN 1460-2083                               
JRNL        PMID   25524706                                                     
JRNL        DOI    10.1093/HMG/DDU730                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 39775                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.580                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3812                            
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 18.4570 -  5.1224    0.90     1811   191  0.1972 0.1961        
REMARK   3     2  5.1224 -  4.0802    0.91     1799   181  0.1330 0.1886        
REMARK   3     3  4.0802 -  3.5687    0.90     1800   196  0.1379 0.1869        
REMARK   3     4  3.5687 -  3.2443    0.91     1793   179  0.1338 0.1798        
REMARK   3     5  3.2443 -  3.0129    0.90     1795   196  0.1600 0.1864        
REMARK   3     6  3.0129 -  2.8359    0.91     1807   186  0.1584 0.1977        
REMARK   3     7  2.8359 -  2.6943    0.90     1808   196  0.1745 0.2266        
REMARK   3     8  2.6943 -  2.5774    0.91     1803   182  0.1860 0.2611        
REMARK   3     9  2.5774 -  2.4784    0.90     1797   201  0.1844 0.2444        
REMARK   3    10  2.4784 -  2.3931    0.91     1803   183  0.1842 0.2408        
REMARK   3    11  2.3931 -  2.3184    0.90     1782   190  0.1852 0.2291        
REMARK   3    12  2.3184 -  2.2522    0.90     1810   196  0.1883 0.2112        
REMARK   3    13  2.2522 -  2.1930    0.90     1790   191  0.1879 0.2495        
REMARK   3    14  2.1930 -  2.1396    0.90     1781   187  0.1947 0.2167        
REMARK   3    15  2.1396 -  2.0910    0.90     1813   192  0.1973 0.2178        
REMARK   3    16  2.0910 -  2.0466    0.91     1830   181  0.2035 0.2297        
REMARK   3    17  2.0466 -  2.0057    0.90     1771   189  0.2088 0.2129        
REMARK   3    18  2.0057 -  1.9679    0.90     1788   190  0.2100 0.2429        
REMARK   3    19  1.9679 -  1.9328    0.91     1833   186  0.2213 0.2496        
REMARK   3    20  1.9328 -  1.9001    0.90     1771   192  0.2283 0.2599        
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)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.200           
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      :  0.003           2161                                  
REMARK   3   ANGLE     :  0.766           2933                                  
REMARK   3   CHIRALITY :  0.028            321                                  
REMARK   3   PLANARITY :  0.003            366                                  
REMARK   3   DIHEDRAL  : 14.100            790                                  
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 4WXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204732.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MAR CCD 300 - NOT LISTED AS AN     
REMARK 200                                   OPTION                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 130265                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5200                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000 CAPSO PEG 400, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       34.44000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.32500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       43.72000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       34.44000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.32500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       43.72000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       34.44000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       43.32500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.72000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       34.44000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       43.32500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       43.72000            
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 819  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 826  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     LEU A   228                                                      
REMARK 465     LYS A   229                                                      
REMARK 465     GLU A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     PRO A   232                                                      
REMARK 465     SER A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     TYR A   235                                                      
REMARK 465     LEU A   236                                                      
REMARK 465     ARG A   237                                                      
REMARK 465     SER A   238                                                      
REMARK 465     GLY A   239                                                      
REMARK 465     GLU A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     ASP A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     LYS A   503                                                      
REMARK 465     MET A   504                                                      
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    HOH A   770     O    HOH A   816              1.80            
REMARK 500   O    HOH A   902     O    HOH A   915              1.85            
REMARK 500   O    HOH A   979     O    HOH A   980              1.87            
REMARK 500   O    HOH A   800     O    HOH A   819              1.88            
REMARK 500   O    HOH A   998     O    HOH A  1003              1.90            
REMARK 500   O    HOH A   984     O    HOH A   985              1.91            
REMARK 500   OE2  GLU A   357     O    HOH A   701              1.93            
REMARK 500   NH1  ARG A   320     O    HOH A   701              1.95            
REMARK 500   O    HOH A   953     O    HOH A   966              1.96            
REMARK 500   O    HOH A   802     O    HOH A   815              2.00            
REMARK 500   O    HOH A   705     O    HOH A   762              2.01            
REMARK 500   O    HOH A   752     O    HOH A   792              2.02            
REMARK 500   OH   TYR A   267     O    HOH A   950              2.04            
REMARK 500   O    HOH A   818     O    HOH A   986              2.06            
REMARK 500   OE1  GLN A   415     O    HOH A   982              2.07            
REMARK 500   ND2  ASN A   469     O    HOH A   948              2.08            
REMARK 500   O    HOH A   999     O    HOH A  1000              2.09            
REMARK 500   NE2  GLN A   424     O    HOH A   702              2.12            
REMARK 500   O    VAL A   329     O3   GOL A   603              2.14            
REMARK 500   O    HOH A   975     O    HOH A   988              2.14            
REMARK 500   NE   ARG A   258     O    HOH A   923              2.14            
REMARK 500   O    HOH A   823     O    HOH A   826              2.14            
REMARK 500   O    HOH A   969     O    HOH A  1001              2.16            
REMARK 500   O    HOH A   815     O    HOH A   925              2.17            
REMARK 500   O7   P6G A   606     O    HOH A   970              2.18            
REMARK 500   O    HOH A   935     O    HOH A   940              2.18            
REMARK 500   O    HOH A   904     O    HOH A   912              2.19            
REMARK 500   O    HOH A   961     O    HOH A   991              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   O    HOH A   723     O    HOH A   737     8544     1.87            
REMARK 500   O    HOH A   776     O    HOH A   804     4555     1.94            
REMARK 500   O    HOH A   760     O    HOH A   792     8544     2.01            
REMARK 500   O    HOH A   805     O    HOH A   809     3555     2.03            
REMARK 500   O    HOH A   810     O    HOH A   812     3455     2.04            
REMARK 500   O    HOH A   703     O    HOH A   706     4555     2.08            
REMARK 500   O    HOH A   744     O    HOH A   791     8444     2.10            
REMARK 500   O    HOH A   732     O    HOH A   773     6445     2.15            
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    CYS A 245     -153.68    -91.44                                   
REMARK 500    SER A 324     -151.55     58.58                                   
REMARK 500    THR A 377       33.14    -89.67                                   
REMARK 500    TYR A 473       85.30   -164.15                                   
REMARK 500    LEU A 492      -11.44     80.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     P6G A  606                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 607  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 326   O                                                      
REMARK 620 2 ASP A 380   OD1  96.8                                              
REMARK 620 3 LEU A 381   O    90.1  80.9                                        
REMARK 620 4 ASP A 478   OD1 163.4  88.6 106.2                                  
REMARK 620 5 ASP A 478   OD2 129.8 132.7  89.7  49.7                            
REMARK 620 6 HOH A 832   O    89.9 107.0 172.0  73.5  84.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 380   OD1                                                    
REMARK 620 2 ASP A 380   OD2  46.0                                              
REMARK 620 3 ASN A 428   OD1 110.8  80.0                                        
REMARK 620 4 ALA A 429   O   121.3  85.3  83.4                                  
REMARK 620 5 ILE A 477   O   150.8 160.8  82.5  85.1                            
REMARK 620 6 ASP A 478   OD1  81.4 126.6 138.6 125.1  72.4                      
REMARK 620 7 HOH A 836   O    78.0 101.5  74.5 155.2  81.0  69.5                
REMARK 620 8 HOH A 833   O    68.2  80.3 151.1  74.1 112.7  70.3 130.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 607                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WXQ   RELATED DB: PDB                                   
REMARK 900 4WXQ IS THE WILD TYPE STRUCTURE OF THIS PROTEIN DOMAIN.              
REMARK 900 RELATED ID: 4WXU   RELATED DB: PDB                                   
DBREF  4WXS A  228   504  UNP    Q99972   MYOC_HUMAN     228    504             
SEQADV 4WXS ASP A  396  UNP  Q99972    GLU   396 ENGINEERED MUTATION            
SEQRES   1 A  277  LEU LYS GLU SER PRO SER GLY TYR LEU ARG SER GLY GLU          
SEQRES   2 A  277  GLY ASP THR GLY CYS GLY GLU LEU VAL TRP VAL GLY GLU          
SEQRES   3 A  277  PRO LEU THR LEU ARG THR ALA GLU THR ILE THR GLY LYS          
SEQRES   4 A  277  TYR GLY VAL TRP MET ARG ASP PRO LYS PRO THR TYR PRO          
SEQRES   5 A  277  TYR THR GLN GLU THR THR TRP ARG ILE ASP THR VAL GLY          
SEQRES   6 A  277  THR ASP VAL ARG GLN VAL PHE GLU TYR ASP LEU ILE SER          
SEQRES   7 A  277  GLN PHE MET GLN GLY TYR PRO SER LYS VAL HIS ILE LEU          
SEQRES   8 A  277  PRO ARG PRO LEU GLU SER THR GLY ALA VAL VAL TYR SER          
SEQRES   9 A  277  GLY SER LEU TYR PHE GLN GLY ALA GLU SER ARG THR VAL          
SEQRES  10 A  277  ILE ARG TYR GLU LEU ASN THR GLU THR VAL LYS ALA GLU          
SEQRES  11 A  277  LYS GLU ILE PRO GLY ALA GLY TYR HIS GLY GLN PHE PRO          
SEQRES  12 A  277  TYR SER TRP GLY GLY TYR THR ASP ILE ASP LEU ALA VAL          
SEQRES  13 A  277  ASP GLU ALA GLY LEU TRP VAL ILE TYR SER THR ASP ASP          
SEQRES  14 A  277  ALA LYS GLY ALA ILE VAL LEU SER LYS LEU ASN PRO GLU          
SEQRES  15 A  277  ASN LEU GLU LEU GLU GLN THR TRP GLU THR ASN ILE ARG          
SEQRES  16 A  277  LYS GLN SER VAL ALA ASN ALA PHE ILE ILE CYS GLY THR          
SEQRES  17 A  277  LEU TYR THR VAL SER SER TYR THR SER ALA ASP ALA THR          
SEQRES  18 A  277  VAL ASN PHE ALA TYR ASP THR GLY THR GLY ILE SER LYS          
SEQRES  19 A  277  THR LEU THR ILE PRO PHE LYS ASN ARG TYR LYS TYR SER          
SEQRES  20 A  277  SER MET ILE ASP TYR ASN PRO LEU GLU LYS LYS LEU PHE          
SEQRES  21 A  277  ALA TRP ASP ASN LEU ASN MET VAL THR TYR ASP ILE LYS          
SEQRES  22 A  277  LEU SER LYS MET                                              
HET     CA  A 601       1                                                       
HET    GOL  A 602      14                                                       
HET    GOL  A 603      14                                                       
HET    GOL  A 604      14                                                       
HET    PG4  A 605      31                                                       
HET    P6G  A 606      16                                                       
HET     NA  A 607       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM      NA SODIUM ION                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  GOL    3(C3 H8 O3)                                                  
FORMUL   6  PG4    C8 H18 O5                                                    
FORMUL   7  P6G    C12 H26 O7                                                   
FORMUL   8   NA    NA 1+                                                        
FORMUL   9  HOH   *304(H2 O)                                                    
HELIX    1 AA1 THR A  262  LYS A  266  5                                   5    
HELIX    2 AA2 LEU A  303  GLY A  310  1                                   8    
HELIX    3 AA3 GLN A  424  VAL A  426  5                                   3    
SHEET    1 AA1 2 LEU A 248  VAL A 251  0                                        
SHEET    2 AA1 2 ILE A 499  LEU A 501 -1  O  LYS A 500   N  VAL A 249           
SHEET    1 AA2 4 LEU A 255  THR A 259  0                                        
SHEET    2 AA2 4 ASN A 493  TYR A 497 -1  O  MET A 494   N  ARG A 258           
SHEET    3 AA2 4 LYS A 485  ASP A 490 -1  N  ASP A 490   O  ASN A 493           
SHEET    4 AA2 4 SER A 474  ASN A 480 -1  N  ASP A 478   O  PHE A 487           
SHEET    1 AA3 4 GLY A 268  ARG A 272  0                                        
SHEET    2 AA3 4 THR A 285  ASP A 289 -1  O  TRP A 286   N  MET A 271           
SHEET    3 AA3 4 VAL A 295  TYR A 301 -1  O  PHE A 299   N  ARG A 287           
SHEET    4 AA3 4 LYS A 314  LEU A 322 -1  O  LEU A 318   N  ARG A 296           
SHEET    1 AA4 4 VAL A 328  TYR A 330  0                                        
SHEET    2 AA4 4 SER A 333  GLN A 337 -1  O  TYR A 335   N  VAL A 328           
SHEET    3 AA4 4 THR A 343  GLU A 348 -1  O  ILE A 345   N  PHE A 336           
SHEET    4 AA4 4 VAL A 354  GLU A 359 -1  O  ALA A 356   N  ARG A 346           
SHEET    1 AA5 4 ASP A 380  ASP A 384  0                                        
SHEET    2 AA5 4 GLY A 387  TYR A 392 -1  O  TRP A 389   N  ALA A 382           
SHEET    3 AA5 4 ALA A 400  LEU A 406 -1  O  VAL A 402   N  TYR A 392           
SHEET    4 AA5 4 LEU A 413  ARG A 422 -1  O  GLU A 414   N  LYS A 405           
SHEET    1 AA6 4 ASN A 428  ILE A 432  0                                        
SHEET    2 AA6 4 THR A 435  SER A 441 -1  O  TYR A 437   N  PHE A 430           
SHEET    3 AA6 4 ASP A 446  ASP A 454 -1  O  TYR A 453   N  LEU A 436           
SHEET    4 AA6 4 SER A 460  LYS A 468 -1  O  ILE A 465   N  VAL A 449           
SSBOND   1 CYS A  245    CYS A  433                          1555   1555  2.03  
LINK         O   GLY A 326                NA    NA A 607     1555   1555  2.56  
LINK         OD1 ASP A 380                CA    CA A 601     1555   1555  3.02  
LINK         OD1 ASP A 380                NA    NA A 607     1555   1555  2.36  
LINK         OD2 ASP A 380                CA    CA A 601     1555   1555  2.39  
LINK         O   LEU A 381                NA    NA A 607     1555   1555  2.35  
LINK         OD1 ASN A 428                CA    CA A 601     1555   1555  2.46  
LINK         O   ALA A 429                CA    CA A 601     1555   1555  2.38  
LINK         O   ILE A 477                CA    CA A 601     1555   1555  2.50  
LINK         OD1 ASP A 478                CA    CA A 601     1555   1555  2.40  
LINK         OD1 ASP A 478                NA    NA A 607     1555   1555  2.73  
LINK         OD2 ASP A 478                NA    NA A 607     1555   1555  2.44  
LINK        CA    CA A 601                 O   HOH A 836     1555   1555  2.49  
LINK        CA    CA A 601                 O   HOH A 833     1555   1555  2.57  
LINK        NA    NA A 607                 O   HOH A 832     1555   1555  2.37  
CISPEP   1 TYR A  278    PRO A  279          0         5.04                     
SITE     1 AC1  7 ASP A 380  ASN A 428  ALA A 429  ILE A 477                    
SITE     2 AC1  7 ASP A 478  HOH A 833  HOH A 836                               
SITE     1 AC2 10 TRP A 373  SER A 441  SER A 444  ASN A 469                    
SITE     2 AC2 10 LYS A 472  TYR A 473  SER A 474  HOH A 944                    
SITE     3 AC2 10 HOH A 948  HOH A 963                                          
SITE     1 AC3 11 MET A 271  ARG A 272  PRO A 274  VAL A 328                    
SITE     2 AC3 11 VAL A 329  ASP A 478  ASN A 480  PHE A 487                    
SITE     3 AC3 11 HOH A 898  HOH A 899  HOH A 959                               
SITE     1 AC4  7 LYS A 314  VAL A 315  HIS A 316  ILE A 317                    
SITE     2 AC4  7 GLU A 352  TYR A 442  HOH A 848                               
SITE     1 AC5  7 TRP A 250  SER A 372  GLN A 424  LYS A 500                    
SITE     2 AC5  7 HOH A 733  HOH A 742  HOH A 791                               
SITE     1 AC6  7 PRO A 274  LYS A 275  TYR A 330  ASP A 384                    
SITE     2 AC6  7 GLU A 385  PRO A 481  HOH A 970                               
SITE     1 AC7  5 GLY A 326  ASP A 380  LEU A 381  ASP A 478                    
SITE     2 AC7  5 HOH A 832                                                     
CRYST1   68.880   86.650   87.440  90.00  90.00  90.00 I 2 2 2       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      0.014518  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011541  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011436        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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