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Database: PDB
Entry: 6RTY
LinkDB: 6RTY
Original site: 6RTY 
HEADER    MEMBRANE PROTEIN                        27-MAY-19   6RTY              
TITLE     CRYSTAL STRUCTURE OF THE PATCHED ECTODOMAIN IN COMPLEX WITH NANOBODY  
TITLE    2 NB64                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN PATCHED HOMOLOG 1;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PTC1;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: HUMAN PTCH1-ECD1 RESIDUES 139-423, CONTAINING THREE N-
COMPND   7 TERMINAL ADDITIONAL RESIDUES DERIVED FROM THE EXPRESSION VECTOR      
COMPND   8 PHLSEC, AND A C-TERMINAL HIS6-TAG FOR IMAC PURIFICATION.;            
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: LLAMA-DERIVED NANOBODY NB64;                               
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 OTHER_DETAILS: NANOBODY NB64 CONTAINING A C-TERMINAL HIS6-TAG FOR    
COMPND  14 PURIFICATION                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PTCH1, PTCH;                                                   
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHLSEC;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: LAMA GLAMA;                                     
SOURCE  12 ORGANISM_TAXID: 9844;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PMES4Y                                    
KEYWDS    ---- HEDGEHOG MORPHOGEN RECEPTOR, RECEPTOR-NANOBODY COMPLEX,          
KEYWDS   2 CHOLESTEROL, PALMITATE, LIPID-PROTEIN-MODIFICATION, MEMBRANE PROTEIN 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.F.RUDOLF,C.KOWATSCH,K.EL OMARI,T.MALINAUSKAS,M.KINNEBREW,           
AUTHOR   2 T.B.ANSELL,B.BISHOP,E.PARDON,R.A.SCHWAB,M.QIAN,R.DUMAN,D.F.COVEY,    
AUTHOR   3 J.STEYAERT,A.WAGNER,M.S.P.SANSOM,R.ROHATGI,C.SIEBOLD                 
REVDAT   3   29-JUL-20 6RTY    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE                                     
REVDAT   2   09-OCT-19 6RTY    1       JRNL                                     
REVDAT   1   02-OCT-19 6RTY    0                                                
JRNL        AUTH   A.F.RUDOLF,M.KINNEBREW,C.KOWATSCH,T.B.ANSELL,K.EL OMARI,     
JRNL        AUTH 2 B.BISHOP,E.PARDON,R.A.SCHWAB,T.MALINAUSKAS,M.QIAN,R.DUMAN,   
JRNL        AUTH 3 D.F.COVEY,J.STEYAERT,A.WAGNER,M.S.P.SANSOM,R.ROHATGI,        
JRNL        AUTH 4 C.SIEBOLD                                                    
JRNL        TITL   THE MORPHOGEN SONIC HEDGEHOG INHIBITS ITS RECEPTOR PATCHED   
JRNL        TITL 2 BY A PINCER GRASP MECHANISM.                                 
JRNL        REF    NAT.CHEM.BIOL.                V.  15   975 2019              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   31548691                                                     
JRNL        DOI    10.1038/S41589-019-0370-Y                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0232                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 25995                          
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) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1372                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1423                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.3770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3127                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 79                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40000                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.39000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.235         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.196         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.149         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.902         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3278 ; 0.007 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  2930 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4459 ; 1.453 ; 1.662       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6836 ; 1.245 ; 1.586       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   397 ; 6.781 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   163 ;30.875 ;23.374       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   545 ;15.088 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;19.658 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   421 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3647 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   661 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1591 ; 5.338 ; 7.284       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1590 ; 5.330 ; 7.282       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1987 ; 7.357 ;10.894       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1988 ; 7.356 ;10.896       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1687 ; 5.366 ; 7.724       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1688 ; 5.364 ; 7.727       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2473 ; 7.899 ;11.414       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 12876 ;11.577 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 12840 ;11.586 ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6RTY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102576.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-16                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27821                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 150.540                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 11.80                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES/IMIDAZOLE PH 6.5, 0.02M OF     
REMARK 280  EACH AMINO ACID (L-GLUTAMATE, ALANINE, GLYCINE, LYSINE, SERINE),    
REMARK 280  12.5% (V/V) MPD, 12.5% (W/V) PEG 1000, 12.5% (W/V) PEG 3350,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.85900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.26900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.93650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.26900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.85900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.93650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLU A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     GLY A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     LEU A   140                                                      
REMARK 465     ASN A   141                                                      
REMARK 465     TYR A   142                                                      
REMARK 465     THR A   143                                                      
REMARK 465     ARG A   144                                                      
REMARK 465     GLN A   145                                                      
REMARK 465     LYS A   146                                                      
REMARK 465     ILE A   147                                                      
REMARK 465     GLY A   148                                                      
REMARK 465     LYS A   426                                                      
REMARK 465     HIS A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     HIS A   429                                                      
REMARK 465     HIS A   430                                                      
REMARK 465     HIS A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     GLY B    28                                                      
REMARK 465     ASN B    29                                                      
REMARK 465     HIS B   124                                                      
REMARK 465     HIS B   125                                                      
REMARK 465     HIS B   126                                                      
REMARK 465     GLU B   127                                                      
REMARK 465     PRO B   128                                                      
REMARK 465     GLU B   129                                                      
REMARK 465     ALA B   130                                                      
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    GLU A 212      -67.06   -125.56                                   
REMARK 500    VAL A 275       20.15   -141.08                                   
REMARK 500    PRO A 309        2.09    -68.79                                   
REMARK 500    ASN A 349     -168.31   -114.93                                   
REMARK 500    THR A 423     -168.66   -103.47                                   
REMARK 500    VAL B  48      -61.06   -106.40                                   
REMARK 500    ASN B  76       60.44     39.73                                   
REMARK 500    ALA B  91      167.81    174.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6RTY A  136   423  UNP    Q13635   PTC1_HUMAN     136    423             
DBREF  6RTY B    1   130  PDB    6RTY     6RTY             1    130             
SEQADV 6RTY GLU A  136  UNP  Q13635    VAL   136 CONFLICT                       
SEQADV 6RTY THR A  137  UNP  Q13635    SER   137 CONFLICT                       
SEQADV 6RTY GLY A  138  UNP  Q13635    ARG   138 CONFLICT                       
SEQADV 6RTY GLY A  424  UNP  Q13635              EXPRESSION TAG                 
SEQADV 6RTY THR A  425  UNP  Q13635              EXPRESSION TAG                 
SEQADV 6RTY LYS A  426  UNP  Q13635              EXPRESSION TAG                 
SEQADV 6RTY HIS A  427  UNP  Q13635              EXPRESSION TAG                 
SEQADV 6RTY HIS A  428  UNP  Q13635              EXPRESSION TAG                 
SEQADV 6RTY HIS A  429  UNP  Q13635              EXPRESSION TAG                 
SEQADV 6RTY HIS A  430  UNP  Q13635              EXPRESSION TAG                 
SEQADV 6RTY HIS A  431  UNP  Q13635              EXPRESSION TAG                 
SEQADV 6RTY HIS A  432  UNP  Q13635              EXPRESSION TAG                 
SEQRES   1 A  297  GLU THR GLY GLU LEU ASN TYR THR ARG GLN LYS ILE GLY          
SEQRES   2 A  297  GLU GLU ALA MET PHE ASN PRO GLN LEU MET ILE GLN THR          
SEQRES   3 A  297  PRO LYS GLU GLU GLY ALA ASN VAL LEU THR THR GLU ALA          
SEQRES   4 A  297  LEU LEU GLN HIS LEU ASP SER ALA LEU GLN ALA SER ARG          
SEQRES   5 A  297  VAL HIS VAL TYR MET TYR ASN ARG GLN TRP LYS LEU GLU          
SEQRES   6 A  297  HIS LEU CYS TYR LYS SER GLY GLU LEU ILE THR GLU THR          
SEQRES   7 A  297  GLY TYR MET ASP GLN ILE ILE GLU TYR LEU TYR PRO CYS          
SEQRES   8 A  297  LEU ILE ILE THR PRO LEU ASP CYS PHE TRP GLU GLY ALA          
SEQRES   9 A  297  LYS LEU GLN SER GLY THR ALA TYR LEU LEU GLY LYS PRO          
SEQRES  10 A  297  PRO LEU ARG TRP THR ASN PHE ASP PRO LEU GLU PHE LEU          
SEQRES  11 A  297  GLU GLU LEU LYS LYS ILE ASN TYR GLN VAL ASP SER TRP          
SEQRES  12 A  297  GLU GLU MET LEU ASN LYS ALA GLU VAL GLY HIS GLY TYR          
SEQRES  13 A  297  MET ASP ARG PRO CYS LEU ASN PRO ALA ASP PRO ASP CYS          
SEQRES  14 A  297  PRO ALA THR ALA PRO ASN LYS ASN SER THR LYS PRO LEU          
SEQRES  15 A  297  ASP MET ALA LEU VAL LEU ASN GLY GLY CYS HIS GLY LEU          
SEQRES  16 A  297  SER ARG LYS TYR MET HIS TRP GLN GLU GLU LEU ILE VAL          
SEQRES  17 A  297  GLY GLY THR VAL LYS ASN SER THR GLY LYS LEU VAL SER          
SEQRES  18 A  297  ALA HIS ALA LEU GLN THR MET PHE GLN LEU MET THR PRO          
SEQRES  19 A  297  LYS GLN MET TYR GLU HIS PHE LYS GLY TYR GLU TYR VAL          
SEQRES  20 A  297  SER HIS ILE ASN TRP ASN GLU ASP LYS ALA ALA ALA ILE          
SEQRES  21 A  297  LEU GLU ALA TRP GLN ARG THR TYR VAL GLU VAL VAL HIS          
SEQRES  22 A  297  GLN SER VAL ALA GLN ASN SER THR GLN LYS VAL LEU SER          
SEQRES  23 A  297  PHE THR GLY THR LYS HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  130  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 B  130  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 B  130  SER GLY ASN SER ILE ASN VAL MET GLY TRP TYR ARG GLN          
SEQRES   4 B  130  ALA PRO GLY LYS PRO ARG GLU LEU VAL ALA GLU ILE THR          
SEQRES   5 B  130  SER SER GLY THR THR ASN TYR ALA ASP SER VAL LYS GLY          
SEQRES   6 B  130  ARG PHE SER ILE SER ARG ASP ASN ALA LYS ASN THR VAL          
SEQRES   7 B  130  PRO LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 B  130  ILE TYR TYR CYS SER ALA VAL LEU VAL ARG PHE GLY GLY          
SEQRES   9 B  130  LEU ARG ARG SER TYR TRP GLY GLN GLY THR GLN VAL THR          
SEQRES  10 B  130  VAL SER SER HIS HIS HIS HIS HIS HIS GLU PRO GLU ALA          
HET    NAG  A 501      14                                                       
HET    NAG  A 502      14                                                       
HET    NAG  A 503      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   6  HOH   *79(H2 O)                                                     
HELIX    1 AA1 THR A  171  ARG A  187  1                                  17    
HELIX    2 AA2 LYS A  198  CYS A  203  1                                   6    
HELIX    3 AA3 THR A  213  TYR A  224  1                                  12    
HELIX    4 AA4 THR A  230  GLN A  242  5                                  13    
HELIX    5 AA5 ASP A  260  ILE A  271  1                                  12    
HELIX    6 AA6 VAL A  275  GLU A  286  1                                  12    
HELIX    7 AA7 ASP A  318  ASN A  324  1                                   7    
HELIX    8 AA8 GLN A  338  ILE A  342  1                                   5    
HELIX    9 AA9 THR A  368  LYS A  377  1                                  10    
HELIX   10 AB1 TYR A  379  SER A  383  5                                   5    
HELIX   11 AB2 ASN A  388  SER A  410  1                                  23    
HELIX   12 AB3 LYS B   86  THR B   90  5                                   5    
SHEET    1 AA1 3 ILE A 228  ILE A 229  0                                        
SHEET    2 AA1 3 ALA A 359  LEU A 366 -1  O  MET A 363   N  ILE A 229           
SHEET    3 AA1 3 VAL A 343  GLY A 344 -1  N  GLY A 344   O  ALA A 359           
SHEET    1 AA2 4 ILE A 228  ILE A 229  0                                        
SHEET    2 AA2 4 ALA A 359  LEU A 366 -1  O  MET A 363   N  ILE A 229           
SHEET    3 AA2 4 ASN A 154  PRO A 162 -1  N  GLN A 156   O  PHE A 364           
SHEET    4 AA2 4 GLN A 417  PHE A 422 -1  O  PHE A 422   N  LEU A 157           
SHEET    1 AA3 2 VAL A 190  MET A 192  0                                        
SHEET    2 AA3 2 ARG A 195  TRP A 197 -1  O  TRP A 197   N  VAL A 190           
SHEET    1 AA4 5 LYS A 205  ILE A 210  0                                        
SHEET    2 AA4 5 GLY B 103  TRP B 110  1  O  ARG B 106   N  LEU A 209           
SHEET    3 AA4 5 ALA B  91  ARG B 101 -1  N  ARG B 101   O  LEU B 105           
SHEET    4 AA4 5 THR B 114  VAL B 118 -1  O  THR B 114   N  TYR B  93           
SHEET    5 AA4 5 LEU B  11  VAL B  12  1  N  VAL B  12   O  THR B 117           
SHEET    1 AA5 6 LYS A 205  ILE A 210  0                                        
SHEET    2 AA5 6 GLY B 103  TRP B 110  1  O  ARG B 106   N  LEU A 209           
SHEET    3 AA5 6 ALA B  91  ARG B 101 -1  N  ARG B 101   O  LEU B 105           
SHEET    4 AA5 6 VAL B  33  GLN B  39 -1  N  TYR B  37   O  TYR B  94           
SHEET    5 AA5 6 GLU B  46  THR B  52 -1  O  ALA B  49   N  TRP B  36           
SHEET    6 AA5 6 THR B  57  TYR B  59 -1  O  ASN B  58   N  GLU B  50           
SHEET    1 AA6 2 CYS A 327  HIS A 328  0                                        
SHEET    2 AA6 2 HIS A 336  TRP A 337 -1  O  TRP A 337   N  CYS A 327           
SHEET    1 AA7 2 VAL A 347  LYS A 348  0                                        
SHEET    2 AA7 2 LEU A 354  SER A 356 -1  O  VAL A 355   N  VAL A 347           
SHEET    1 AA8 4 LEU B   4  SER B   7  0                                        
SHEET    2 AA8 4 LEU B  18  ALA B  24 -1  O  ALA B  23   N  GLN B   5           
SHEET    3 AA8 4 THR B  77  MET B  82 -1  O  LEU B  80   N  LEU B  20           
SHEET    4 AA8 4 PHE B  67  ILE B  69 -1  N  SER B  68   O  GLN B  81           
SSBOND   1 CYS A  203    CYS A  226                          1555   1555  2.13  
SSBOND   2 CYS A  234    CYS A  327                          1555   1555  2.13  
SSBOND   3 CYS A  296    CYS A  304                          1555   1555  2.12  
SSBOND   4 CYS B   22    CYS B   95                          1555   1555  2.02  
LINK         ND2 ASN A 312                 C1  NAG A 501     1555   1555  1.45  
LINK         ND2 ASN A 349                 C1  NAG A 502     1555   1555  1.44  
LINK         ND2 ASN A 414                 C1  NAG A 503     1555   1555  1.44  
CRYST1   47.718   65.873  150.538  90.00  90.00  90.00 P 21 21 21    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      0.020956  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015181  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006643        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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