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Database: PDB
Entry: 3QJ4
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HEADER    OXIDOREDUCTASE                          28-JAN-11   3QJ4              
TITLE     CRYSTAL STRUCTURE OF HUMAN RENALASE (ISOFORM 1)                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RENALASE;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MONOAMINE OXIDASE-C, MAO-C;                                 
COMPND   5 EC: 1.4.-.-;                                                         
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: RNLS;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET SUMO                                  
KEYWDS    FAD/NAD(P)-BINDING ROSSMANN FOLD SUPERFAMILY, FLAVIN CONTAINING AMINE 
KEYWDS   2 OXIDOREDUCTASE, MONOAMINE OXIDASE, NAD, EXTRACELLULAR,               
KEYWDS   3 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MILANI,F.CIRIELLO,S.BARONI,V.PANDINI,A.ALIVERTI,G.CANEVARI,         
AUTHOR   2 M.BOLOGNESI                                                          
REVDAT   3   01-NOV-23 3QJ4    1       REMARK                                   
REVDAT   2   19-JUN-13 3QJ4    1       JRNL                                     
REVDAT   1   13-JUL-11 3QJ4    0                                                
JRNL        AUTH   M.MILANI,F.CIRIELLO,S.BARONI,V.PANDINI,G.CANEVARI,           
JRNL        AUTH 2 M.BOLOGNESI,A.ALIVERTI                                       
JRNL        TITL   FAD-BINDING SITE AND NADP REACTIVITY IN HUMAN RENALASE: A    
JRNL        TITL 2 NEW ENZYME INVOLVED IN BLOOD PRESSURE REGULATION             
JRNL        REF    J.MOL.BIOL.                   V. 411   463 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21699903                                                     
JRNL        DOI    10.1016/J.JMB.2011.06.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.2                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 24995                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.219                          
REMARK   3   R VALUE            (WORKING SET)  : 0.217                          
REMARK   3   FREE R VALUE                      : 0.260                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.140                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1284                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.60                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2876                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2250                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2739                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2230                   
REMARK   3   BIN FREE R VALUE                        : 0.2657                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.76                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 137                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5181                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 121                                     
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.16                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.32970                                             
REMARK   3    B22 (A**2) : -17.81080                                            
REMARK   3    B33 (A**2) : 7.48110                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -3.18990                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.369               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5444   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7411   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1866   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 155    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 812    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5444   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : 18     ; 0.000  ; HARMONIC            
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 708    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5632   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.14                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.53                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.59                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: A 1 - A 341, A 401                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   14.5045   -6.4689   20.8850           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0867 T22:    0.0413                                    
REMARK   3     T33:    0.1412 T12:    0.0236                                    
REMARK   3     T13:    0.0003 T23:    0.0381                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.8253 L22:    0.8266                                    
REMARK   3     L33:    3.2044 L12:   -0.2547                                    
REMARK   3     L13:   -0.6286 L23:    0.6898                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0777 S12:   -0.0395 S13:   -0.0212                     
REMARK   3     S21:   -0.0661 S22:    0.0726 S23:    0.0077                     
REMARK   3     S31:   -0.1000 S32:    0.2661 S33:    0.0050                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: B 2 - B 341, B 401                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   29.5662   36.9051   26.7451           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0696 T22:    0.2633                                    
REMARK   3     T33:    0.0863 T12:    0.0071                                    
REMARK   3     T13:    0.0057 T23:    0.0940                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.0485 L22:    0.8660                                    
REMARK   3     L33:    2.7339 L12:   -0.3076                                    
REMARK   3     L13:   -0.3147 L23:    0.5092                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0627 S12:   -0.4608 S13:   -0.0713                     
REMARK   3     S21:   -0.0913 S22:    0.1420 S23:   -0.0430                     
REMARK   3     S31:   -0.1071 S32:    0.0674 S33:   -0.0793                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QJ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063709.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87260                            
REMARK 200  MONOCHROMATOR                  : HORIZONTALLY SIDE DIFFRACTING      
REMARK 200                                   SILICON 111 CRYSTAL                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29646                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3KKJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 0.2M AMMONIUM SULFATE,     
REMARK 280  PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       43.29650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     SER A    25                                                      
REMARK 465     LYS A    99                                                      
REMARK 465     GLU A   100                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     ILE A   206                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     ILE A   342                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B    99                                                      
REMARK 465     ASP B   140                                                      
REMARK 465     SER B   150                                                      
REMARK 465     GLU B   201                                                      
REMARK 465     SER B   236                                                      
REMARK 465     GLU B   237                                                      
REMARK 465     CYS B   300                                                      
REMARK 465     ILE B   342                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 148      127.84   -173.49                                   
REMARK 500    THR A 294      -81.27    -88.15                                   
REMARK 500    ALA A 297      -68.36   -141.60                                   
REMARK 500    CYS A 300       -8.35     95.94                                   
REMARK 500    THR A 320     -104.64   -126.22                                   
REMARK 500    HIS B  73       30.33    -95.87                                   
REMARK 500    ALA B 298     -127.09     55.22                                   
REMARK 500    HIS B 307      145.44   -175.95                                   
REMARK 500    THR B 320     -100.22   -125.89                                   
REMARK 500    LYS B 339      -60.66    -21.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 343                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 344                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 343                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 NATURAL VARIANT, SEE UNP DATABASE RNLS_HUMAN                         
DBREF  3QJ4 A    1   342  UNP    Q5VYX0   RNLS_HUMAN       1    342             
DBREF  3QJ4 B    1   342  UNP    Q5VYX0   RNLS_HUMAN       1    342             
SEQADV 3QJ4 ASP A   37  UNP  Q5VYX0    GLU    37 SEE REMARK 999                 
SEQADV 3QJ4 ASP B   37  UNP  Q5VYX0    GLU    37 SEE REMARK 999                 
SEQRES   1 A  342  MET ALA GLN VAL LEU ILE VAL GLY ALA GLY MET THR GLY          
SEQRES   2 A  342  SER LEU CYS ALA ALA LEU LEU ARG ARG GLN THR SER GLY          
SEQRES   3 A  342  PRO LEU TYR LEU ALA VAL TRP ASP LYS ALA ASP ASP SER          
SEQRES   4 A  342  GLY GLY ARG MET THR THR ALA CYS SER PRO HIS ASN PRO          
SEQRES   5 A  342  GLN CYS THR ALA ASP LEU GLY ALA GLN TYR ILE THR CYS          
SEQRES   6 A  342  THR PRO HIS TYR ALA LYS LYS HIS GLN ARG PHE TYR ASP          
SEQRES   7 A  342  GLU LEU LEU ALA TYR GLY VAL LEU ARG PRO LEU SER SER          
SEQRES   8 A  342  PRO ILE GLU GLY MET VAL MET LYS GLU GLY ASP CYS ASN          
SEQRES   9 A  342  PHE VAL ALA PRO GLN GLY ILE SER SER ILE ILE LYS HIS          
SEQRES  10 A  342  TYR LEU LYS GLU SER GLY ALA GLU VAL TYR PHE ARG HIS          
SEQRES  11 A  342  ARG VAL THR GLN ILE ASN LEU ARG ASP ASP LYS TRP GLU          
SEQRES  12 A  342  VAL SER LYS GLN THR GLY SER PRO GLU GLN PHE ASP LEU          
SEQRES  13 A  342  ILE VAL LEU THR MET PRO VAL PRO GLU ILE LEU GLN LEU          
SEQRES  14 A  342  GLN GLY ASP ILE THR THR LEU ILE SER GLU CYS GLN ARG          
SEQRES  15 A  342  GLN GLN LEU GLU ALA VAL SER TYR SER SER ARG TYR ALA          
SEQRES  16 A  342  LEU GLY LEU PHE TYR GLU ALA GLY THR LYS ILE ASP VAL          
SEQRES  17 A  342  PRO TRP ALA GLY GLN TYR ILE THR SER ASN PRO CYS ILE          
SEQRES  18 A  342  ARG PHE VAL SER ILE ASP ASN LYS LYS ARG ASN ILE GLU          
SEQRES  19 A  342  SER SER GLU ILE GLY PRO SER LEU VAL ILE HIS THR THR          
SEQRES  20 A  342  VAL PRO PHE GLY VAL THR TYR LEU GLU HIS SER ILE GLU          
SEQRES  21 A  342  ASP VAL GLN GLU LEU VAL PHE GLN GLN LEU GLU ASN ILE          
SEQRES  22 A  342  LEU PRO GLY LEU PRO GLN PRO ILE ALA THR LYS CYS GLN          
SEQRES  23 A  342  LYS TRP ARG HIS SER GLN VAL THR ASN ALA ALA ALA ASN          
SEQRES  24 A  342  CYS PRO GLY GLN MET THR LEU HIS HIS LYS PRO PHE LEU          
SEQRES  25 A  342  ALA CYS GLY GLY ASP GLY PHE THR GLN SER ASN PHE ASP          
SEQRES  26 A  342  GLY CYS ILE THR SER ALA LEU CYS VAL LEU GLU ALA LEU          
SEQRES  27 A  342  LYS ASN TYR ILE                                              
SEQRES   1 B  342  MET ALA GLN VAL LEU ILE VAL GLY ALA GLY MET THR GLY          
SEQRES   2 B  342  SER LEU CYS ALA ALA LEU LEU ARG ARG GLN THR SER GLY          
SEQRES   3 B  342  PRO LEU TYR LEU ALA VAL TRP ASP LYS ALA ASP ASP SER          
SEQRES   4 B  342  GLY GLY ARG MET THR THR ALA CYS SER PRO HIS ASN PRO          
SEQRES   5 B  342  GLN CYS THR ALA ASP LEU GLY ALA GLN TYR ILE THR CYS          
SEQRES   6 B  342  THR PRO HIS TYR ALA LYS LYS HIS GLN ARG PHE TYR ASP          
SEQRES   7 B  342  GLU LEU LEU ALA TYR GLY VAL LEU ARG PRO LEU SER SER          
SEQRES   8 B  342  PRO ILE GLU GLY MET VAL MET LYS GLU GLY ASP CYS ASN          
SEQRES   9 B  342  PHE VAL ALA PRO GLN GLY ILE SER SER ILE ILE LYS HIS          
SEQRES  10 B  342  TYR LEU LYS GLU SER GLY ALA GLU VAL TYR PHE ARG HIS          
SEQRES  11 B  342  ARG VAL THR GLN ILE ASN LEU ARG ASP ASP LYS TRP GLU          
SEQRES  12 B  342  VAL SER LYS GLN THR GLY SER PRO GLU GLN PHE ASP LEU          
SEQRES  13 B  342  ILE VAL LEU THR MET PRO VAL PRO GLU ILE LEU GLN LEU          
SEQRES  14 B  342  GLN GLY ASP ILE THR THR LEU ILE SER GLU CYS GLN ARG          
SEQRES  15 B  342  GLN GLN LEU GLU ALA VAL SER TYR SER SER ARG TYR ALA          
SEQRES  16 B  342  LEU GLY LEU PHE TYR GLU ALA GLY THR LYS ILE ASP VAL          
SEQRES  17 B  342  PRO TRP ALA GLY GLN TYR ILE THR SER ASN PRO CYS ILE          
SEQRES  18 B  342  ARG PHE VAL SER ILE ASP ASN LYS LYS ARG ASN ILE GLU          
SEQRES  19 B  342  SER SER GLU ILE GLY PRO SER LEU VAL ILE HIS THR THR          
SEQRES  20 B  342  VAL PRO PHE GLY VAL THR TYR LEU GLU HIS SER ILE GLU          
SEQRES  21 B  342  ASP VAL GLN GLU LEU VAL PHE GLN GLN LEU GLU ASN ILE          
SEQRES  22 B  342  LEU PRO GLY LEU PRO GLN PRO ILE ALA THR LYS CYS GLN          
SEQRES  23 B  342  LYS TRP ARG HIS SER GLN VAL THR ASN ALA ALA ALA ASN          
SEQRES  24 B  342  CYS PRO GLY GLN MET THR LEU HIS HIS LYS PRO PHE LEU          
SEQRES  25 B  342  ALA CYS GLY GLY ASP GLY PHE THR GLN SER ASN PHE ASP          
SEQRES  26 B  342  GLY CYS ILE THR SER ALA LEU CYS VAL LEU GLU ALA LEU          
SEQRES  27 B  342  LYS ASN TYR ILE                                              
HET    FAD  A 401      53                                                       
HET    SO4  A 343       5                                                       
HET    SO4  A 344       5                                                       
HET    FAD  B 401      53                                                       
HET    SO4  B 343       5                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   8  HOH   *128(H2 O)                                                    
HELIX    1   1 GLY A   10  ARG A   22  1                                  13    
HELIX    2   2 GLY A   40  MET A   43  5                                   4    
HELIX    3   3 HIS A   68  HIS A   73  1                                   6    
HELIX    4   4 HIS A   73  TYR A   83  1                                  11    
HELIX    5   5 SER A  112  GLY A  123  1                                  12    
HELIX    6   6 PRO A  162  LEU A  167  1                                   6    
HELIX    7   7 ASP A  172  ILE A  177  1                                   6    
HELIX    8   8 SER A  178  ALA A  187  1                                  10    
HELIX    9   9 ASP A  227  ARG A  231  1                                   5    
HELIX   10  10 THR A  247  TYR A  254  1                                   8    
HELIX   11  11 SER A  258  LEU A  274  1                                  17    
HELIX   12  12 GLY A  316  THR A  320  5                                   5    
HELIX   13  13 ASN A  323  LYS A  339  1                                  17    
HELIX   14  14 GLY B   10  THR B   24  1                                  15    
HELIX   15  15 GLY B   40  MET B   43  5                                   4    
HELIX   16  16 HIS B   68  HIS B   73  1                                   6    
HELIX   17  17 HIS B   73  TYR B   83  1                                  11    
HELIX   18  18 SER B  112  SER B  122  1                                  11    
HELIX   19  19 PRO B  162  LEU B  167  1                                   6    
HELIX   20  20 ASP B  172  ILE B  177  1                                   6    
HELIX   21  21 SER B  178  ALA B  187  1                                  10    
HELIX   22  22 ASP B  227  ARG B  231  1                                   5    
HELIX   23  23 THR B  247  TYR B  254  1                                   8    
HELIX   24  24 SER B  258  LEU B  274  1                                  17    
HELIX   25  25 GLY B  316  THR B  320  5                                   5    
HELIX   26  26 ASN B  323  LYS B  339  1                                  17    
SHEET    1   A 6 GLU A 125  TYR A 127  0                                        
SHEET    2   A 6 LEU A  28  TRP A  33  1  N  VAL A  32   O  TYR A 127           
SHEET    3   A 6 ALA A   2  VAL A   7  1  N  ALA A   2   O  TYR A  29           
SHEET    4   A 6 LEU A 156  LEU A 159  1  O  VAL A 158   N  VAL A   7           
SHEET    5   A 6 PHE A 311  CYS A 314  1  O  ALA A 313   N  LEU A 159           
SHEET    6   A 6 MET A 304  HIS A 307 -1  N  LEU A 306   O  LEU A 312           
SHEET    1   B 2 THR A  45  CYS A  47  0                                        
SHEET    2   B 2 THR A  55  ASP A  57 -1  O  ALA A  56   N  ALA A  46           
SHEET    1   C 3 ILE A  63  CYS A  65  0                                        
SHEET    2   C 3 CYS A 103  VAL A 106 -1  O  CYS A 103   N  CYS A  65           
SHEET    3   C 3 ARG A  87  PRO A  88 -1  N  ARG A  87   O  VAL A 106           
SHEET    1   D 6 ILE A  93  GLU A  94  0                                        
SHEET    2   D 6 GLY A 212  TYR A 214  1  O  TYR A 214   N  GLU A  94           
SHEET    3   D 6 ILE A 221  ILE A 226 -1  O  VAL A 224   N  GLN A 213           
SHEET    4   D 6 SER A 241  THR A 246 -1  O  HIS A 245   N  PHE A 223           
SHEET    5   D 6 ARG A 193  PHE A 199 -1  N  LEU A 198   O  LEU A 242           
SHEET    6   D 6 ALA A 282  TRP A 288 -1  O  ALA A 282   N  PHE A 199           
SHEET    1   E 3 VAL A 132  LEU A 137  0                                        
SHEET    2   E 3 TRP A 142  LYS A 146 -1  O  GLU A 143   N  ASN A 136           
SHEET    3   E 3 GLU A 152  PHE A 154 -1  O  GLU A 152   N  VAL A 144           
SHEET    1   F 6 ALA B 124  TYR B 127  0                                        
SHEET    2   F 6 TYR B  29  TRP B  33  1  N  VAL B  32   O  TYR B 127           
SHEET    3   F 6 GLN B   3  VAL B   7  1  N  VAL B   4   O  TYR B  29           
SHEET    4   F 6 LEU B 156  LEU B 159  1  O  LEU B 156   N  LEU B   5           
SHEET    5   F 6 PHE B 311  CYS B 314  1  O  ALA B 313   N  LEU B 159           
SHEET    6   F 6 MET B 304  HIS B 307 -1  N  LEU B 306   O  LEU B 312           
SHEET    1   G 2 THR B  45  CYS B  47  0                                        
SHEET    2   G 2 THR B  55  ASP B  57 -1  O  ALA B  56   N  ALA B  46           
SHEET    1   H 3 ILE B  63  CYS B  65  0                                        
SHEET    2   H 3 CYS B 103  VAL B 106 -1  O  CYS B 103   N  CYS B  65           
SHEET    3   H 3 ARG B  87  PRO B  88 -1  N  ARG B  87   O  VAL B 106           
SHEET    1   I 6 ILE B  93  GLU B  94  0                                        
SHEET    2   I 6 GLY B 212  TYR B 214  1  O  TYR B 214   N  GLU B  94           
SHEET    3   I 6 ILE B 221  ILE B 226 -1  O  VAL B 224   N  GLN B 213           
SHEET    4   I 6 SER B 241  THR B 246 -1  O  HIS B 245   N  PHE B 223           
SHEET    5   I 6 ARG B 193  PHE B 199 -1  N  LEU B 198   O  LEU B 242           
SHEET    6   I 6 ALA B 282  TRP B 288 -1  O  ALA B 282   N  PHE B 199           
SHEET    1   J 3 VAL B 132  LEU B 137  0                                        
SHEET    2   J 3 TRP B 142  LYS B 146 -1  O  GLU B 143   N  ASN B 136           
SHEET    3   J 3 GLU B 152  PHE B 154 -1  O  GLU B 152   N  VAL B 144           
SHEET    1   K 2 SER B 189  TYR B 190  0                                        
SHEET    2   K 2 VAL B 293  ASN B 295 -1  O  THR B 294   N  SER B 189           
CISPEP   1 GLY A   26    PRO A   27          0         0.63                     
CISPEP   2 ALA A   70    LYS A   71          0        12.39                     
CISPEP   3 THR A  148    GLY A  149          0         0.63                     
CISPEP   4 ALA A  297    ALA A  298          0        -3.26                     
CISPEP   5 LYS A  309    PRO A  310          0         3.55                     
CISPEP   6 LYS B  309    PRO B  310          0         0.49                     
SITE     1 AC1 30 VAL A   7  GLY A   8  MET A  11  THR A  12                    
SITE     2 AC1 30 ASP A  34  LYS A  35  GLY A  41  ARG A  42                    
SITE     3 AC1 30 GLY A  59  ALA A  60  GLN A  61  TYR A  62                    
SITE     4 AC1 30 HIS A 130  ARG A 131  VAL A 132  MET A 161                    
SITE     5 AC1 30 HIS A 245  TRP A 288  SER A 291  GLN A 292                    
SITE     6 AC1 30 ASP A 317  SER A 322  ASN A 323  PHE A 324                    
SITE     7 AC1 30 CYS A 327  HOH A 348  HOH A 392  HOH A 394                    
SITE     8 AC1 30 HOH A 404  HOH A 411                                          
SITE     1 AC2  2 LYS A 287  ARG A 289                                          
SITE     1 AC3  4 ARG A 193  ARG A 222  THR A 247  VAL A 248                    
SITE     1 AC4 30 VAL B   7  GLY B   8  MET B  11  THR B  12                    
SITE     2 AC4 30 ASP B  34  LYS B  35  GLY B  41  ARG B  42                    
SITE     3 AC4 30 GLY B  59  ALA B  60  GLN B  61  TYR B  62                    
SITE     4 AC4 30 HIS B 130  ARG B 131  VAL B 132  MET B 161                    
SITE     5 AC4 30 HIS B 245  TRP B 288  SER B 291  ASP B 317                    
SITE     6 AC4 30 SER B 322  ASN B 323  PHE B 324  CYS B 327                    
SITE     7 AC4 30 HOH B 352  HOH B 386  HOH B 388  HOH B 389                    
SITE     8 AC4 30 HOH B 390  HOH B 391                                          
SITE     1 AC5  5 ARG B 193  ARG B 222  THR B 247  VAL B 248                    
SITE     2 AC5  5 HOH B 402                                                     
CRYST1   53.837   86.593   93.180  90.00  95.30  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018575  0.000000  0.001723        0.00000                         
SCALE2      0.000000  0.011548  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010778        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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