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Database: PDB
Entry: 5E1B
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HEADER    TRANSFERASE                             29-SEP-15   5E1B              
TITLE     CRYSTAL STRUCTURE OF NRMT1 IN COMPLEX WITH SPKRIA PEPTIDE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-TERMINAL XAA-PRO-LYS N-METHYLTRANSFERASE 1;              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ALPHA N-TERMINAL PROTEIN METHYLTRANSFERASE 1A,              
COMPND   5 METHYLTRANSFERASE-LIKE PROTEIN 11A,N-TERMINAL RCC1 METHYLTRANSFERASE,
COMPND   6 X-PRO-LYS N-TERMINAL PROTEIN METHYLTRANSFERASE 1A,NTM1A;             
COMPND   7 EC: 2.1.1.244;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RCC1;                                                      
COMPND  11 CHAIN: D, E;                                                         
COMPND  12 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: NTMT1, C9ORF32, METTL11A, NRMT, NRMT1, AD-003;                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V3R;                             
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.DONG,W.TEMPEL,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,STRUCTURAL 
AUTHOR   2 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   4   27-SEP-23 5E1B    1       JRNL   REMARK                            
REVDAT   3   02-DEC-15 5E1B    1       JRNL                                     
REVDAT   2   18-NOV-15 5E1B    1       JRNL                                     
REVDAT   1   28-OCT-15 5E1B    0                                                
JRNL        AUTH   C.DONG,Y.MAO,W.TEMPEL,S.QIN,L.LI,P.LOPPNAU,R.HUANG,J.MIN     
JRNL        TITL   STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION BY THE HUMAN      
JRNL        TITL 2 N-TERMINAL METHYLTRANSFERASE 1.                              
JRNL        REF    GENES DEV.                    V.  29  2343 2015              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   26543161                                                     
JRNL        DOI    10.1101/GAD.270611.115                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 80997                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS (SFTOOLS)           
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.152                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.176                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3324                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5866                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 236                          
REMARK   3   BIN FREE R VALUE                    : 0.2220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3652                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 130                                     
REMARK   3   SOLVENT ATOMS            : 436                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.04000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.13000                                             
REMARK   3    B12 (A**2) : 0.02000                                              
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): 0.066         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.274         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3974 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3775 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5409 ; 1.815 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8717 ; 1.040 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   510 ; 6.182 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   182 ;36.740 ;23.187       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   693 ;11.088 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    39 ;18.522 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   606 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4487 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   907 ; 0.002 ; 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):  1925 ; 0.517 ; 0.682       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1924 ; 0.512 ; 0.680       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2412 ; 0.878 ; 1.018       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -3        A   223                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1451  31.6356 -14.4660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0433 T22:   0.0139                                     
REMARK   3      T33:   0.0043 T12:   0.0168                                     
REMARK   3      T13:   0.0075 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9712 L22:   0.8877                                     
REMARK   3      L33:   1.6274 L12:  -0.2087                                     
REMARK   3      L13:   0.0849 L23:  -0.0911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0492 S12:  -0.0271 S13:  -0.0141                       
REMARK   3      S21:   0.0731 S22:   0.0217 S23:   0.0433                       
REMARK   3      S31:  -0.0605 S32:  -0.1027 S33:   0.0275                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -2        B   223                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.8357  38.8117  14.2247              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1039 T22:   0.0531                                     
REMARK   3      T33:   0.0365 T12:   0.0277                                     
REMARK   3      T13:   0.0413 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7626 L22:   1.5069                                     
REMARK   3      L33:   1.6010 L12:  -0.9721                                     
REMARK   3      L13:  -0.7647 L23:   0.3576                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1351 S12:  -0.1070 S13:  -0.1810                       
REMARK   3      S21:   0.1707 S22:   0.0679 S23:   0.1278                       
REMARK   3      S31:   0.1855 S32:   0.0552 S33:   0.0672                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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: COOT WAS USED FOR INTERACTIVE MODEL       
REMARK   3  BUILDING. MOLPROBITY WAS USED FOR GEOMETRY VALIDATION.              
REMARK   4                                                                      
REMARK   4 5E1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214137.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.12                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92380                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 21.70                              
REMARK 200  R MERGE                    (I) : 0.13400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 21.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.21300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDBID 2EX4                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG3350, 16% TACSIMATE, VAPOR        
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      136.94400            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       68.47200            
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      102.70800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       34.23600            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      171.18000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      136.94400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       68.47200            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       34.23600            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      102.70800            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      171.18000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9950 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
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     MET A   -17                                                      
REMARK 465     GLY A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     SER A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     MET B   -17                                                      
REMARK 465     GLY B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     VAL B    -3                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A  -3    CG1  CG2                                            
REMARK 470     LYS A  10    CD   CE   NZ                                        
REMARK 470     LYS A  47    CE   NZ                                             
REMARK 470     LYS A  59    NZ                                                  
REMARK 470     ARG A  85    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 101    CD   CE   NZ                                        
REMARK 470     LYS A 109    CD   CE   NZ                                        
REMARK 470     GLN A 171    OE1  NE2                                            
REMARK 470     ARG B  -1    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B   4    OE1  OE2                                            
REMARK 470     GLU B   7    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  10    CD   CE   NZ                                        
REMARK 470     LYS B  15    NZ                                                  
REMARK 470     LYS B  21    NZ                                                  
REMARK 470     ARG B  85    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 154    CE   NZ                                             
REMARK 470     ARG B 158    NH1  NH2                                            
REMARK 470     GLN B 171    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 178    OD1  OD2                                            
REMARK 470     ILE E   5    CG1  CD1                                            
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   SG   CYS A   195     UNK  UNX A   326              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A   1   CB    SER A   1   OG     -0.099                       
REMARK 500    CYS A 117   CB    CYS A 117   SG     -0.124                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A   8   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG A  46   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP A 178   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG B  54   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
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    ARG A 112      -77.78    -91.72                                   
REMARK 500    VAL A 137      -14.14   -147.23                                   
REMARK 500    SER A 181       67.79     64.94                                   
REMARK 500    ASN B  58       62.44   -110.65                                   
REMARK 500    VAL B 137      -16.27   -146.70                                   
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 SAH A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5E1D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E2A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E1M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E2B   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E1O   RELATED DB: PDB                                   
DBREF  5E1B A    2   223  UNP    Q9BV86   NTM1A_HUMAN      2    223             
DBREF  5E1B B    2   223  UNP    Q9BV86   NTM1A_HUMAN      2    223             
DBREF  5E1B D    1     6  PDB    5E1B     5E1B             1      6             
DBREF  5E1B E    1     6  PDB    5E1B     5E1B             1      6             
SEQADV 5E1B MET A  -17  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B GLY A  -16  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER A  -15  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER A  -14  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS A  -13  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS A  -12  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS A  -11  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS A  -10  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS A   -9  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS A   -8  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER A   -7  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER A   -6  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B GLY A   -5  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B LEU A   -4  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B VAL A   -3  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B PRO A   -2  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B ARG A   -1  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B GLY A    0  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER A    1  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B MET B  -17  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B GLY B  -16  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER B  -15  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER B  -14  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS B  -13  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS B  -12  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS B  -11  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS B  -10  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS B   -9  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B HIS B   -8  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER B   -7  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER B   -6  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B GLY B   -5  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B LEU B   -4  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B VAL B   -3  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B PRO B   -2  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B ARG B   -1  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B GLY B    0  UNP  Q9BV86              EXPRESSION TAG                 
SEQADV 5E1B SER B    1  UNP  Q9BV86              EXPRESSION TAG                 
SEQRES   1 A  241  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  241  LEU VAL PRO ARG GLY SER THR SER GLU VAL ILE GLU ASP          
SEQRES   3 A  241  GLU LYS GLN PHE TYR SER LYS ALA LYS THR TYR TRP LYS          
SEQRES   4 A  241  GLN ILE PRO PRO THR VAL ASP GLY MET LEU GLY GLY TYR          
SEQRES   5 A  241  GLY HIS ILE SER SER ILE ASP ILE ASN SER SER ARG LYS          
SEQRES   6 A  241  PHE LEU GLN ARG PHE LEU ARG GLU GLY PRO ASN LYS THR          
SEQRES   7 A  241  GLY THR SER CYS ALA LEU ASP CYS GLY ALA GLY ILE GLY          
SEQRES   8 A  241  ARG ILE THR LYS ARG LEU LEU LEU PRO LEU PHE ARG GLU          
SEQRES   9 A  241  VAL ASP MET VAL ASP ILE THR GLU ASP PHE LEU VAL GLN          
SEQRES  10 A  241  ALA LYS THR TYR LEU GLY GLU GLU GLY LYS ARG VAL ARG          
SEQRES  11 A  241  ASN TYR PHE CYS CYS GLY LEU GLN ASP PHE THR PRO GLU          
SEQRES  12 A  241  PRO ASP SER TYR ASP VAL ILE TRP ILE GLN TRP VAL ILE          
SEQRES  13 A  241  GLY HIS LEU THR ASP GLN HIS LEU ALA GLU PHE LEU ARG          
SEQRES  14 A  241  ARG CYS LYS GLY SER LEU ARG PRO ASN GLY ILE ILE VAL          
SEQRES  15 A  241  ILE LYS ASP ASN MET ALA GLN GLU GLY VAL ILE LEU ASP          
SEQRES  16 A  241  ASP VAL ASP SER SER VAL CYS ARG ASP LEU ASP VAL VAL          
SEQRES  17 A  241  ARG ARG ILE ILE CYS SER ALA GLY LEU SER LEU LEU ALA          
SEQRES  18 A  241  GLU GLU ARG GLN GLU ASN LEU PRO ASP GLU ILE TYR HIS          
SEQRES  19 A  241  VAL TYR SER PHE ALA LEU ARG                                  
SEQRES   1 B  241  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  241  LEU VAL PRO ARG GLY SER THR SER GLU VAL ILE GLU ASP          
SEQRES   3 B  241  GLU LYS GLN PHE TYR SER LYS ALA LYS THR TYR TRP LYS          
SEQRES   4 B  241  GLN ILE PRO PRO THR VAL ASP GLY MET LEU GLY GLY TYR          
SEQRES   5 B  241  GLY HIS ILE SER SER ILE ASP ILE ASN SER SER ARG LYS          
SEQRES   6 B  241  PHE LEU GLN ARG PHE LEU ARG GLU GLY PRO ASN LYS THR          
SEQRES   7 B  241  GLY THR SER CYS ALA LEU ASP CYS GLY ALA GLY ILE GLY          
SEQRES   8 B  241  ARG ILE THR LYS ARG LEU LEU LEU PRO LEU PHE ARG GLU          
SEQRES   9 B  241  VAL ASP MET VAL ASP ILE THR GLU ASP PHE LEU VAL GLN          
SEQRES  10 B  241  ALA LYS THR TYR LEU GLY GLU GLU GLY LYS ARG VAL ARG          
SEQRES  11 B  241  ASN TYR PHE CYS CYS GLY LEU GLN ASP PHE THR PRO GLU          
SEQRES  12 B  241  PRO ASP SER TYR ASP VAL ILE TRP ILE GLN TRP VAL ILE          
SEQRES  13 B  241  GLY HIS LEU THR ASP GLN HIS LEU ALA GLU PHE LEU ARG          
SEQRES  14 B  241  ARG CYS LYS GLY SER LEU ARG PRO ASN GLY ILE ILE VAL          
SEQRES  15 B  241  ILE LYS ASP ASN MET ALA GLN GLU GLY VAL ILE LEU ASP          
SEQRES  16 B  241  ASP VAL ASP SER SER VAL CYS ARG ASP LEU ASP VAL VAL          
SEQRES  17 B  241  ARG ARG ILE ILE CYS SER ALA GLY LEU SER LEU LEU ALA          
SEQRES  18 B  241  GLU GLU ARG GLN GLU ASN LEU PRO ASP GLU ILE TYR HIS          
SEQRES  19 B  241  VAL TYR SER PHE ALA LEU ARG                                  
SEQRES   1 D    6  SER PRO LYS ARG ILE ALA                                      
SEQRES   1 E    6  SER PRO LYS ARG ILE ALA                                      
HET    SAH  A 301      26                                                       
HET    GOL  A 302       6                                                       
HET    GOL  A 303       6                                                       
HET    GOL  A 304       6                                                       
HET    UNX  A 305       1                                                       
HET    UNX  A 306       1                                                       
HET    UNX  A 307       1                                                       
HET    UNX  A 308       1                                                       
HET    UNX  A 309       1                                                       
HET    UNX  A 310       1                                                       
HET    UNX  A 311       1                                                       
HET    UNX  A 312       1                                                       
HET    UNX  A 313       1                                                       
HET    UNX  A 314       1                                                       
HET    UNX  A 315       1                                                       
HET    UNX  A 316       1                                                       
HET    UNX  A 317       1                                                       
HET    UNX  A 318       1                                                       
HET    UNX  A 319       1                                                       
HET    UNX  A 320       1                                                       
HET    UNX  A 321       1                                                       
HET    UNX  A 322       1                                                       
HET    UNX  A 323       1                                                       
HET    UNX  A 324       1                                                       
HET    UNX  A 325       1                                                       
HET    UNX  A 326       1                                                       
HET    UNX  A 327       1                                                       
HET    UNX  A 328       1                                                       
HET    SAH  B 301      26                                                       
HET    GOL  B 302       6                                                       
HET    UNX  B 303       1                                                       
HET    UNX  B 304       1                                                       
HET    UNX  B 305       1                                                       
HET    UNX  B 306       1                                                       
HET    UNX  B 307       1                                                       
HET    UNX  B 308       1                                                       
HET    UNX  B 309       1                                                       
HET    UNX  B 310       1                                                       
HET    UNX  B 311       1                                                       
HET    UNX  B 312       1                                                       
HET    UNX  B 313       1                                                       
HET    UNX  B 314       1                                                       
HET    UNX  B 315       1                                                       
HET    UNX  B 316       1                                                       
HET    UNX  B 317       1                                                       
HET    UNX  B 318       1                                                       
HET    UNX  B 319       1                                                       
HET    UNX  B 320       1                                                       
HET    UNX  B 321       1                                                       
HET    UNX  B 322       1                                                       
HET    UNX  B 323       1                                                       
HET    UNX  B 324       1                                                       
HET    UNX  B 325       1                                                       
HET    UNX  B 326       1                                                       
HET    UNX  B 327       1                                                       
HET    UNX  B 328       1                                                       
HET    UNX  B 329       1                                                       
HET    UNX  D 101       1                                                       
HET    UNX  E 101       1                                                       
HET    UNX  E 102       1                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     GOL GLYCEROL                                                         
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   6  GOL    4(C3 H8 O3)                                                  
FORMUL   9  UNX    54(X)                                                        
FORMUL  65  HOH   *436(H2 O)                                                    
HELIX    1 AA1 SER A    1  VAL A    5  5                                   5    
HELIX    2 AA2 ASP A    8  GLN A   22  1                                  15    
HELIX    3 AA3 THR A   26  LEU A   31  1                                   6    
HELIX    4 AA4 TYR A   34  HIS A   36  5                                   3    
HELIX    5 AA5 ILE A   37  ARG A   51  1                                  15    
HELIX    6 AA6 PHE A   52  ARG A   54  5                                   3    
HELIX    7 AA7 GLY A   73  LEU A   79  1                                   7    
HELIX    8 AA8 THR A   93  LEU A  104  1                                  12    
HELIX    9 AA9 GLY A  105  LYS A  109  5                                   5    
HELIX   10 AB1 GLY A  118  PHE A  122  5                                   5    
HELIX   11 AB2 VAL A  137  LEU A  141  5                                   5    
HELIX   12 AB3 THR A  142  SER A  156  1                                  15    
HELIX   13 AB4 LEU A  187  ALA A  197  1                                  11    
HELIX   14 AB5 SER B    1  ILE B    6  1                                   6    
HELIX   15 AB6 ASP B    8  GLN B   22  1                                  15    
HELIX   16 AB7 THR B   26  LEU B   31  1                                   6    
HELIX   17 AB8 TYR B   34  HIS B   36  5                                   3    
HELIX   18 AB9 ILE B   37  GLU B   55  1                                  19    
HELIX   19 AC1 GLY B   73  LEU B   79  1                                   7    
HELIX   20 AC2 THR B   93  LEU B  104  1                                  12    
HELIX   21 AC3 GLY B  105  LYS B  109  5                                   5    
HELIX   22 AC4 GLY B  118  PHE B  122  5                                   5    
HELIX   23 AC5 VAL B  137  LEU B  141  5                                   5    
HELIX   24 AC6 THR B  142  SER B  156  1                                  15    
HELIX   25 AC7 ASP B  186  ALA B  197  1                                  12    
SHEET    1 AA1 7 VAL A 111  CYS A 116  0                                        
SHEET    2 AA1 7 GLU A  86  ASP A  91  1  N  MET A  89   O  PHE A 115           
SHEET    3 AA1 7 CYS A  64  CYS A  68  1  N  ASP A  67   O  ASP A  88           
SHEET    4 AA1 7 TYR A 129  GLN A 135  1  O  TRP A 133   N  CYS A  68           
SHEET    5 AA1 7 LEU A 157  ALA A 170  1  O  VAL A 164   N  ILE A 132           
SHEET    6 AA1 7 SER A 182  ASP A 186  1  O  ARG A 185   N  ALA A 170           
SHEET    7 AA1 7 VAL A 174  ASP A 177 -1  N  ASP A 177   O  SER A 182           
SHEET    1 AA2 7 VAL A 111  CYS A 116  0                                        
SHEET    2 AA2 7 GLU A  86  ASP A  91  1  N  MET A  89   O  PHE A 115           
SHEET    3 AA2 7 CYS A  64  CYS A  68  1  N  ASP A  67   O  ASP A  88           
SHEET    4 AA2 7 TYR A 129  GLN A 135  1  O  TRP A 133   N  CYS A  68           
SHEET    5 AA2 7 LEU A 157  ALA A 170  1  O  VAL A 164   N  ILE A 132           
SHEET    6 AA2 7 HIS A 216  ARG A 223 -1  O  LEU A 222   N  ILE A 163           
SHEET    7 AA2 7 SER A 200  ARG A 206 -1  N  LEU A 202   O  ALA A 221           
SHEET    1 AA3 7 VAL B 111  CYS B 116  0                                        
SHEET    2 AA3 7 GLU B  86  ASP B  91  1  N  MET B  89   O  PHE B 115           
SHEET    3 AA3 7 CYS B  64  CYS B  68  1  N  ASP B  67   O  ASP B  88           
SHEET    4 AA3 7 TYR B 129  GLN B 135  1  O  TRP B 133   N  CYS B  68           
SHEET    5 AA3 7 LEU B 157  MET B 169  1  O  VAL B 164   N  ILE B 132           
SHEET    6 AA3 7 HIS B 216  ARG B 223 -1  O  LEU B 222   N  ILE B 163           
SHEET    7 AA3 7 SER B 200  ARG B 206 -1  N  LEU B 202   O  ALA B 221           
SHEET    1 AA4 2 VAL B 174  ASP B 177  0                                        
SHEET    2 AA4 2 SER B 182  ARG B 185 -1  O  SER B 182   N  ASP B 177           
CISPEP   1 GLY B   56    PRO B   57          0         0.17                     
CISPEP   2 GLY B   56    PRO B   57          0         7.27                     
SITE     1 AC1 20 TRP A  20  MET A  30  GLY A  69  GLY A  71                    
SITE     2 AC1 20 ARG A  74  ILE A  75  ASP A  91  ILE A  92                    
SITE     3 AC1 20 THR A  93  PHE A  96  GLY A 118  LEU A 119                    
SITE     4 AC1 20 GLN A 120  GLN A 135  TRP A 136  VAL A 137                    
SITE     5 AC1 20 HIS A 140  HOH A 439  HOH A 520  HOH A 525                    
SITE     1 AC2  8 TYR A  19  ASP A 177  VAL A 179  HOH A 433                    
SITE     2 AC2  8 HOH A 452  HOH A 458  LYS D   3  HOH D 202                    
SITE     1 AC3  6 GLU A  86  ARG A 112  HOH A 436  HOH A 442                    
SITE     2 AC3  6 HOH A 500  ARG B  46                                          
SITE     1 AC4 10 TRP A 136  VAL A 137  ILE A 138  GLY A 139                    
SITE     2 AC4 10 ASP A 167  ASN A 168  VAL A 183  HOH A 426                    
SITE     3 AC4 10 HOH A 444  SER D   1                                          
SITE     1 AC5 21 TRP B  20  MET B  30  GLY B  69  GLY B  71                    
SITE     2 AC5 21 ARG B  74  ILE B  75  ASP B  91  ILE B  92                    
SITE     3 AC5 21 THR B  93  PHE B  96  CYS B 117  GLY B 118                    
SITE     4 AC5 21 LEU B 119  GLN B 120  GLN B 135  TRP B 136                    
SITE     5 AC5 21 VAL B 137  HIS B 140  HOH B 444  HOH B 479                    
SITE     6 AC5 21 HOH B 486                                                     
SITE     1 AC6 11 TRP B 136  VAL B 137  ILE B 138  GLY B 139                    
SITE     2 AC6 11 ASP B 167  ASN B 168  VAL B 183  CYS B 184                    
SITE     3 AC6 11 HOH B 407  HOH B 422  SER E   1                               
CRYST1  107.259  107.259  205.416  90.00  90.00 120.00 P 65 2 2     24          
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      0.009323  0.005383  0.000000        0.00000                         
SCALE2      0.000000  0.010766  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004868        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system