GenomeNet

Database: PDB
Entry: 4WXQ
LinkDB: 4WXQ
Original site: 4WXQ 
HEADER    PROTEIN BINDING                         14-NOV-14   4WXQ              
TITLE     CRYSTAL STRUCTURE OF THE MYOCILIN 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                                                      
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    S.D.ORWIG,K.C.TURNAGE,R.K.DONEGAN,R.L.LIEBERMAN                       
REVDAT   1   01-APR-15 4WXQ    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.    2.15 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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.78                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 14510                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1446                            
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 19.7793 -  4.6142    1.00     1389   152  0.2078 0.2178        
REMARK   3     2  4.6142 -  3.6701    1.00     1334   147  0.1712 0.1887        
REMARK   3     3  3.6701 -  3.2084    1.00     1308   140  0.1719 0.2223        
REMARK   3     4  3.2084 -  2.9161    1.00     1315   144  0.1960 0.2385        
REMARK   3     5  2.9161 -  2.7076    1.00     1291   147  0.1993 0.2541        
REMARK   3     6  2.7076 -  2.5483    1.00     1294   137  0.1860 0.2780        
REMARK   3     7  2.5483 -  2.4209    1.00     1301   144  0.1969 0.2409        
REMARK   3     8  2.4209 -  2.3157    1.00     1284   149  0.2092 0.2612        
REMARK   3     9  2.3157 -  2.2267    1.00     1283   144  0.2158 0.2471        
REMARK   3    10  2.2267 -  2.1500    1.00     1265   142  0.2316 0.2744        
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)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.020           
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      :  0.002           2177                                  
REMARK   3   ANGLE     :  0.625           2940                                  
REMARK   3   CHIRALITY :  0.022            320                                  
REMARK   3   PLANARITY :  0.002            364                                  
REMARK   3   DIHEDRAL  : 12.376            801                                  
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 4WXQ 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_1000204727.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-10                          
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) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
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   : 14521                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.780                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5400                            
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   (%): 41.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000 PEG 2000 MES PH 6.0, 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       34.33000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.91000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       44.22000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       34.33000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.91000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.22000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       34.33000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.91000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       44.22000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       34.33000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.91000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       44.22000            
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 731  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 740  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 743  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   NH2  ARG A   320     O    HOH A   701              1.83            
REMARK 500   O    GLN A   297     O    HOH A   826              1.87            
REMARK 500   O7   P6G A   604     O    HOH A   702              2.09            
REMARK 500   NE2  GLN A   309     O    HOH A   703              2.14            
REMARK 500   OE2  GLU A   357     O    HOH A   704              2.15            
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   OH   TYR A   365     O13  P6G A   602     8444     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     -155.70   -111.26                                   
REMARK 500    ASP A 294       77.71   -114.57                                   
REMARK 500    ARG A 296      -24.24   -142.96                                   
REMARK 500    GLN A 309      -56.61   -120.87                                   
REMARK 500    SER A 324     -155.64     58.36                                   
REMARK 500    ALA A 356      149.28   -170.16                                   
REMARK 500    TYR A 392     -162.97   -163.61                                   
REMARK 500    TYR A 473       75.80   -161.48                                   
REMARK 500    MET A 476      146.34   -172.21                                   
REMARK 500    LEU A 492       -6.25     73.84                                   
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 A 827        DISTANCE =  6.00 ANGSTROMS                       
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  602                                                       
REMARK 610     P6G A  603                                                       
REMARK 610     P6G A  604                                                       
REMARK 610     P6G A  605                                                       
REMARK 610     P6G A  606                                                       
REMARK 610     P6G A  607                                                       
REMARK 610     P6G A  608                                                       
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 609  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 326   O                                                      
REMARK 620 2 ASP A 380   OD1  96.4                                              
REMARK 620 3 LEU A 381   O    91.5  83.2                                        
REMARK 620 4 ASP A 478   OD1 164.7  89.9 103.0                                  
REMARK 620 5 ASP A 478   OD2 125.3 138.2  96.4  49.2                            
REMARK 620 6 HOH A 761   O    91.1 105.1 171.0  73.8  75.1                      
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  46.1                                              
REMARK 620 3 ASN A 428   OD1 110.5  79.2                                        
REMARK 620 4 ALA A 429   O   120.2  80.4  75.4                                  
REMARK 620 5 ILE A 477   O   154.2 157.5  80.8  84.7                            
REMARK 620 6 ASP A 478   OD1  83.7 128.1 142.6 128.2  74.4                      
REMARK 620 7 HOH A 760   O    76.8 101.9  77.2 151.6  83.6  72.7                
REMARK 620 8 HOH A 764   O    70.2  74.5 140.5  71.5 116.3  76.5 136.7          
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 P6G A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G 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 P6G A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 609                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WXS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4WXU   RELATED DB: PDB                                   
DBREF  4WXQ A  228   504  UNP    Q99972   MYOC_HUMAN     228    504             
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 GLU          
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    P6G  A 602      30                                                       
HET    P6G  A 603      19                                                       
HET    P6G  A 604      19                                                       
HET    P6G  A 605      19                                                       
HET    P6G  A 606      21                                                       
HET    P6G  A 607      24                                                       
HET    P6G  A 608      19                                                       
HET     NA  A 609       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM      NA SODIUM ION                                                       
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  P6G    7(C12 H26 O7)                                                
FORMUL  10   NA    NA 1+                                                        
FORMUL  11  HOH   *138(H2 O)                                                    
HELIX    1 AA1 THR A  262  LYS A  266  5                                   5    
HELIX    2 AA2 LEU A  303  GLN A  309  1                                   7    
HELIX    3 AA3 GLN A  424  VAL A  426  5                                   3    
SHEET    1 AA1 4 LEU A 248  THR A 259  0                                        
SHEET    2 AA1 4 ASN A 493  LEU A 501 -1  O  MET A 494   N  LEU A 257           
SHEET    3 AA1 4 LYS A 485  ASP A 490 -1  N  ASP A 490   O  ASN A 493           
SHEET    4 AA1 4 SER A 474  ASN A 480 -1  N  ASP A 478   O  PHE A 487           
SHEET    1 AA2 4 GLY A 268  ARG A 272  0                                        
SHEET    2 AA2 4 THR A 285  ASP A 289 -1  O  TRP A 286   N  MET A 271           
SHEET    3 AA2 4 GLN A 297  TYR A 301 -1  O  TYR A 301   N  THR A 285           
SHEET    4 AA2 4 LYS A 314  ILE A 317 -1  O  LYS A 314   N  GLU A 300           
SHEET    1 AA3 4 LEU A 322  TYR A 330  0                                        
SHEET    2 AA3 4 SER A 333  GLY A 338 -1  O  TYR A 335   N  VAL A 328           
SHEET    3 AA3 4 THR A 343  GLU A 348 -1  O  ILE A 345   N  PHE A 336           
SHEET    4 AA3 4 THR A 353  GLU A 359 -1  O  LYS A 358   N  VAL A 344           
SHEET    1 AA4 4 ASP A 380  ASP A 384  0                                        
SHEET    2 AA4 4 GLY A 387  TYR A 392 -1  O  ILE A 391   N  ASP A 380           
SHEET    3 AA4 4 ALA A 400  LEU A 406 -1  O  VAL A 402   N  TYR A 392           
SHEET    4 AA4 4 LEU A 413  ARG A 422 -1  O  GLU A 414   N  LYS A 405           
SHEET    1 AA5 4 ASN A 428  ILE A 432  0                                        
SHEET    2 AA5 4 THR A 435  SER A 441 -1  O  TYR A 437   N  PHE A 430           
SHEET    3 AA5 4 ASP A 446  ASP A 454 -1  O  TYR A 453   N  LEU A 436           
SHEET    4 AA5 4 SER A 460  LYS A 468 -1  O  LEU A 463   N  ASN A 450           
SSBOND   1 CYS A  245    CYS A  433                          1555   1555  2.03  
LINK         CB  CYS A 245                 SG  CYS A 433     1555   1555  1.96  
LINK         O   GLY A 326                NA    NA A 609     1555   1555  2.71  
LINK         OD1 ASP A 380                CA    CA A 601     1555   1555  3.00  
LINK         OD1 ASP A 380                NA    NA A 609     1555   1555  2.37  
LINK         OD2 ASP A 380                CA    CA A 601     1555   1555  2.45  
LINK         O   LEU A 381                NA    NA A 609     1555   1555  2.37  
LINK         OD1 ASN A 428                CA    CA A 601     1555   1555  2.50  
LINK         O   ALA A 429                CA    CA A 601     1555   1555  2.43  
LINK         O   ILE A 477                CA    CA A 601     1555   1555  2.64  
LINK         OD1 ASP A 478                CA    CA A 601     1555   1555  2.41  
LINK         OD1 ASP A 478                NA    NA A 609     1555   1555  2.76  
LINK         OD2 ASP A 478                NA    NA A 609     1555   1555  2.47  
LINK        CA    CA A 601                 O   HOH A 760     1555   1555  2.62  
LINK        CA    CA A 601                 O   HOH A 764     1555   1555  2.75  
LINK        NA    NA A 609                 O   HOH A 761     1555   1555  2.41  
CISPEP   1 TYR A  278    PRO A  279          0         3.60                     
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 760  HOH A 764                               
SITE     1 AC2 14 PRO A 254  ARG A 342  GLY A 362  TYR A 365                    
SITE     2 AC2 14 GLN A 368  PHE A 369  ASP A 395  TYR A 442                    
SITE     3 AC2 14 ASP A 446  ALA A 447  THR A 448  LYS A 468                    
SITE     4 AC2 14 P6G A 605  HOH A 710                                          
SITE     1 AC3  3 TYR A 330  GLU A 385  PRO A 481                               
SITE     1 AC4  8 SER A 341  ARG A 342  THR A 343  GLU A 359                    
SITE     2 AC4  8 TYR A 365  THR A 443  ASP A 446  HOH A 702                    
SITE     1 AC5 11 GLU A 253  PRO A 254  GLN A 306  GLN A 309                    
SITE     2 AC5 11 GLY A 310  PHE A 369  ASP A 395  ARG A 422                    
SITE     3 AC5 11 P6G A 602  HOH A 715  HOH A 727                               
SITE     1 AC6  6 TRP A 250  ASP A 302  GLY A 367  PRO A 370                    
SITE     2 AC6  6 ARG A 422  GLN A 424                                          
SITE     1 AC7  5 GLU A 348  THR A 353  LYS A 355  GLU A 409                    
SITE     2 AC7  5 ASN A 410                                                     
SITE     1 AC8  7 TYR A 371  TRP A 373  ALA A 427  ASN A 428                    
SITE     2 AC8  7 SER A 474  SER A 475  MET A 476                               
SITE     1 AC9  5 GLY A 326  ASP A 380  LEU A 381  ASP A 478                    
SITE     2 AC9  5 HOH A 761                                                     
CRYST1   68.660   85.820   88.440  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      0.014565  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011652  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011307        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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