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Database: PDB
Entry: 4NYN
LinkDB: 4NYN
Original site: 4NYN 
HEADER    HYDROLASE                               11-DEC-13   4NYN              
TITLE     CRYSTAL STRUCTURE OF RNASE H1 FROM HALOPHILIC ARCHAEON HALOBACTERIUM  
TITLE    2 SALINARUM NRC-1                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBONUCLEASE HI;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HALO-RNASE HI, RNASE HI;                                    
COMPND   5 EC: 3.1.26.4;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HALOBACTERIUM;                                  
SOURCE   3 ORGANISM_TAXID: 64091;                                               
SOURCE   4 STRAIN: NRC-1;                                                       
SOURCE   5 GENE: RNHA, VNG_0255C;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET25B                                    
KEYWDS    HYDROLASE, RNASE H1                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.YOU,C.ANGKAWIDJAJA,Y.KOGA,S.KANAYA                                
REVDAT   2   22-NOV-17 4NYN    1       REMARK                                   
REVDAT   1   12-FEB-14 4NYN    0                                                
JRNL        AUTH   D.J.YOU,C.ANGKAWIDJAJA,Y.KOGA,S.KANAYA                       
JRNL        TITL   CRYSTAL STRUCTURE OF RNASE H1 FROM HALOPHILIC ARCHAEON       
JRNL        TITL 2 HALOBACTERIUM SALINARUM NRC-1                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 48893                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2472                            
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) : 1.41                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.45                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3360                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.49                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 158                          
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1994                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 301                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.57000                                             
REMARK   3    B22 (A**2) : -0.57000                                             
REMARK   3    B33 (A**2) : 1.15000                                              
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): 0.063         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.066         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.037         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.905         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2028 ; 0.008 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2757 ; 1.026 ; 1.938       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   263 ; 6.736 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   110 ;33.920 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   294 ;13.282 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;16.037 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   296 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1638 ; 0.020 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1302 ; 1.832 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2047 ; 2.979 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   726 ; 4.226 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   710 ; 6.443 ; 4.500       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4NYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000083820.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-11                          
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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : HORIZONTAL FOCUSING MIRROR         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER SMART 6500                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48997                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.410                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.41                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, DM 6.1                                        
REMARK 200 STARTING MODEL: 2EHG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 19.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG 8000, IMIDAZOLE(PH6.5),     
REMARK 280  3%(V/V) MPD, 10MM MANGANESE(II) CHLORIDE, VAPOR DIFFUSION,          
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       57.90100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       57.90100            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       19.14100            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       57.90100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        9.57050            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       57.90100            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       28.71150            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       57.90100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.90100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       19.14100            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       57.90100            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       28.71150            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       57.90100            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000        9.57050            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     CYS A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     ILE A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     PHE A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     ASP A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     HIS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     LEU A    31                                                      
REMARK 465     TRP A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     LEU A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     ALA A    39                                                      
REMARK 465     HIS A    40                                                      
REMARK 465     ALA A    41                                                      
REMARK 465     VAL A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     TYR A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     ASP A    46                                                      
REMARK 465     LYS A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     VAL A    49                                                      
REMARK 465     VAL A    50                                                      
REMARK 465     GLN A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     SER A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     ASP A    57                                                      
REMARK 465     ILE A    58                                                      
REMARK 465     THR A    59                                                      
REMARK 465     ALA A    60                                                      
REMARK 465     VAL A    61                                                      
REMARK 465     VAL A    62                                                      
REMARK 465     GLN A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     ASP A    65                                                      
REMARK 465     ARG A    66                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     CYS B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     ILE B     8                                                      
REMARK 465     GLN B     9                                                      
REMARK 465     THR B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     ASP B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     PHE B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     ASN B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     GLU B    28                                                      
REMARK 465     HIS B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     LEU B    31                                                      
REMARK 465     TRP B    32                                                      
REMARK 465     HIS B    33                                                      
REMARK 465     ALA B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     LEU B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     ASP B    38                                                      
REMARK 465     ALA B    39                                                      
REMARK 465     HIS B    40                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     VAL B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     TYR B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     ASP B    46                                                      
REMARK 465     LYS B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     VAL B    49                                                      
REMARK 465     VAL B    50                                                      
REMARK 465     GLN B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     GLY B    53                                                      
REMARK 465     SER B    54                                                      
REMARK 465     PRO B    55                                                      
REMARK 465     THR B    56                                                      
REMARK 465     ASP B    57                                                      
REMARK 465     ILE B    58                                                      
REMARK 465     THR B    59                                                      
REMARK 465     ALA B    60                                                      
REMARK 465     VAL B    61                                                      
REMARK 465     VAL B    62                                                      
REMARK 465     GLN B    63                                                      
REMARK 465     PRO B    64                                                      
REMARK 465     ASP B    65                                                      
REMARK 465     ARG B    66                                                      
REMARK 465     GLY B    67                                                      
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 B  79       77.50   -102.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP B   95     GLY B   96                  141.50                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 202  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 189   OD1                                                    
REMARK 620 2 ASP A 198   OD1  92.7                                              
REMARK 620 3 ASP B  75   OD2  93.5 173.8                                        
REMARK 620 4 HOH B 428   O    91.2  90.4  88.6                                  
REMARK 620 5 HOH B 426   O   108.3  83.4  95.5 159.8                            
REMARK 620 6 HOH A 421   O   174.4  86.1  87.7  83.4  77.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 301  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  75   OD1                                                    
REMARK 620 2 ASP A 139   OD1  96.7                                              
REMARK 620 3 GLU A 115   OE2 102.7 108.9                                        
REMARK 620 4 HOH A 530   O    84.4 159.3  90.9                                  
REMARK 620 5 HOH A 540   O    80.7  87.0 162.9  72.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 201  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  75   OD1                                                    
REMARK 620 2 GLU B 115   OE1  90.2                                              
REMARK 620 3 ASP B 139   OD1  95.7  95.5                                        
REMARK 620 4 HOH B 429   O   172.2  89.0  92.1                                  
REMARK 620 5 HOH A 421   O    85.4 109.2 155.3  87.5                            
REMARK 620 6 HOH B 426   O    87.7 176.1  81.4  93.5  73.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 302  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 189   OD1                                                    
REMARK 620 2 ASP A  75   OD2  95.0                                              
REMARK 620 3 HOH A 540   O   111.9  91.3                                        
REMARK 620 4 HOH A 528   O    90.0  91.2 157.7                                  
REMARK 620 5 HOH A 530   O   167.1  92.5  78.3  79.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 203  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 103   O                                                      
REMARK 620 2 HOH B 444   O    88.5                                              
REMARK 620 3 HOH B 443   O    95.9  90.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 203                  
DBREF  4NYN A    1   199  UNP    Q9HSF6   RNH_HALSA        1    199             
DBREF  4NYN B    1   199  UNP    Q9HSF6   RNH_HALSA        1    199             
SEQRES   1 A  199  MET PRO VAL VAL GLU CYS ASP ILE GLN THR ALA ARG ALA          
SEQRES   2 A  199  ALA LEU ALA ASP ALA GLY ALA SER PHE SER ASP GLY ASN          
SEQRES   3 A  199  SER GLU HIS GLU LEU TRP HIS ALA ASP LEU GLY ASP ALA          
SEQRES   4 A  199  HIS ALA VAL ALA TYR ALA ASP LYS LEU VAL VAL GLN GLY          
SEQRES   5 A  199  GLY SER PRO THR ASP ILE THR ALA VAL VAL GLN PRO ASP          
SEQRES   6 A  199  ARG GLY GLY ARG VAL HIS ALA TYR PHE ASP GLY ALA SER          
SEQRES   7 A  199  ARG GLY ASN PRO GLY PRO ALA ALA VAL GLY TRP VAL LEU          
SEQRES   8 A  199  VAL SER GLY ASP GLY GLY ILE VAL ALA GLU GLY GLY ASP          
SEQRES   9 A  199  THR ILE GLY ARG ALA THR ASN ASN GLN ALA GLU TYR ASP          
SEQRES  10 A  199  ALA LEU ILE ALA ALA LEU GLU ALA ALA ALA ASP PHE GLY          
SEQRES  11 A  199  PHE ASP ASP ILE GLU LEU ARG GLY ASP SER GLN LEU VAL          
SEQRES  12 A  199  GLU LYS GLN LEU THR GLY ALA TRP ASP THR ASN ASP PRO          
SEQRES  13 A  199  ASP LEU ARG ARG LYS ARG VAL ARG ALA ARG GLU LEU LEU          
SEQRES  14 A  199  THR GLY PHE ASP ASP TRP SER ILE THR HIS VAL PRO ARG          
SEQRES  15 A  199  ALA THR ASN GLU ARG ALA ASP ALA LEU ALA ASN GLU ALA          
SEQRES  16 A  199  LEU ASP ASP ALA                                              
SEQRES   1 B  199  MET PRO VAL VAL GLU CYS ASP ILE GLN THR ALA ARG ALA          
SEQRES   2 B  199  ALA LEU ALA ASP ALA GLY ALA SER PHE SER ASP GLY ASN          
SEQRES   3 B  199  SER GLU HIS GLU LEU TRP HIS ALA ASP LEU GLY ASP ALA          
SEQRES   4 B  199  HIS ALA VAL ALA TYR ALA ASP LYS LEU VAL VAL GLN GLY          
SEQRES   5 B  199  GLY SER PRO THR ASP ILE THR ALA VAL VAL GLN PRO ASP          
SEQRES   6 B  199  ARG GLY GLY ARG VAL HIS ALA TYR PHE ASP GLY ALA SER          
SEQRES   7 B  199  ARG GLY ASN PRO GLY PRO ALA ALA VAL GLY TRP VAL LEU          
SEQRES   8 B  199  VAL SER GLY ASP GLY GLY ILE VAL ALA GLU GLY GLY ASP          
SEQRES   9 B  199  THR ILE GLY ARG ALA THR ASN ASN GLN ALA GLU TYR ASP          
SEQRES  10 B  199  ALA LEU ILE ALA ALA LEU GLU ALA ALA ALA ASP PHE GLY          
SEQRES  11 B  199  PHE ASP ASP ILE GLU LEU ARG GLY ASP SER GLN LEU VAL          
SEQRES  12 B  199  GLU LYS GLN LEU THR GLY ALA TRP ASP THR ASN ASP PRO          
SEQRES  13 B  199  ASP LEU ARG ARG LYS ARG VAL ARG ALA ARG GLU LEU LEU          
SEQRES  14 B  199  THR GLY PHE ASP ASP TRP SER ILE THR HIS VAL PRO ARG          
SEQRES  15 B  199  ALA THR ASN GLU ARG ALA ASP ALA LEU ALA ASN GLU ALA          
SEQRES  16 B  199  LEU ASP ASP ALA                                              
HET     MN  A 301       1                                                       
HET     MN  A 302       1                                                       
HET     MN  B 201       1                                                       
HET     MN  B 202       1                                                       
HET     MN  B 203       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    5(MN 2+)                                                     
FORMUL   8  HOH   *301(H2 O)                                                    
HELIX    1   1 THR A  110  PHE A  129  1                                  20    
HELIX    2   2 SER A  140  THR A  148  1                                   9    
HELIX    3   3 ASP A  155  GLY A  171  1                                  17    
HELIX    4   4 ASN A  185  ASP A  198  1                                  14    
HELIX    5   5 THR B  110  PHE B  129  1                                  20    
HELIX    6   6 SER B  140  THR B  148  1                                   9    
HELIX    7   7 ASP B  155  THR B  170  1                                  16    
HELIX    8   8 PRO B  181  THR B  184  5                                   4    
HELIX    9   9 ASN B  185  ALA B  199  1                                  15    
SHEET    1   A 5 ILE A  98  ALA A 109  0                                        
SHEET    2   A 5 GLY A  83  VAL A  92 -1  N  LEU A  91   O  ALA A 100           
SHEET    3   A 5 ARG A  69  SER A  78 -1  N  HIS A  71   O  VAL A  92           
SHEET    4   A 5 ASP A 133  GLY A 138  1  O  GLU A 135   N  VAL A  70           
SHEET    5   A 5 ASP A 174  HIS A 179  1  O  SER A 176   N  LEU A 136           
SHEET    1   B 5 ILE B  98  ALA B 109  0                                        
SHEET    2   B 5 GLY B  83  SER B  93 -1  N  LEU B  91   O  ALA B 100           
SHEET    3   B 5 ARG B  69  SER B  78 -1  N  HIS B  71   O  VAL B  92           
SHEET    4   B 5 ASP B 133  GLY B 138  1  O  GLU B 135   N  VAL B  70           
SHEET    5   B 5 ASP B 174  HIS B 179  1  O  SER B 176   N  LEU B 136           
LINK         OD1 ASP B 189                MN    MN B 202     1555   1555  2.08  
LINK         OD1 ASP A  75                MN    MN A 301     1555   1555  2.09  
LINK         OD1 ASP B  75                MN    MN B 201     1555   1555  2.09  
LINK         OD1 ASP A 139                MN    MN A 301     1555   1555  2.10  
LINK         OD1 ASP A 189                MN    MN A 302     1555   1555  2.11  
LINK         OE2 GLU A 115                MN    MN A 301     1555   1555  2.12  
LINK         OE1 GLU B 115                MN    MN B 201     1555   1555  2.13  
LINK         OD1 ASP A 198                MN    MN B 202     1555   1555  2.14  
LINK         OD2 ASP A  75                MN    MN A 302     1555   1555  2.15  
LINK         OD2 ASP B  75                MN    MN B 202     1555   1555  2.18  
LINK         O   GLY B 103                MN    MN B 203     1555   1555  2.19  
LINK         OD1 ASP B 139                MN    MN B 201     1555   1555  2.21  
LINK        MN    MN B 201                 O   HOH B 429     1555   1555  2.07  
LINK        MN    MN A 302                 O   HOH A 540     1555   1555  2.14  
LINK        MN    MN B 203                 O   HOH B 444     1555   1555  2.16  
LINK        MN    MN B 202                 O   HOH B 428     1555   1555  2.22  
LINK        MN    MN B 203                 O   HOH B 443     1555   1555  2.24  
LINK        MN    MN B 202                 O   HOH B 426     1555   1555  2.26  
LINK        MN    MN A 302                 O   HOH A 528     1555   1555  2.28  
LINK        MN    MN A 301                 O   HOH A 530     1555   1555  2.28  
LINK        MN    MN B 202                 O   HOH A 421     1555   1555  2.36  
LINK        MN    MN B 201                 O   HOH A 421     1555   1555  2.37  
LINK        MN    MN B 201                 O   HOH B 426     1555   1555  2.41  
LINK        MN    MN A 302                 O   HOH A 530     1555   1555  2.45  
LINK        MN    MN A 301                 O   HOH A 540     1555   1555  2.60  
CISPEP   1 ASN A   81    PRO A   82          0         4.28                     
CISPEP   2 ASN B   81    PRO B   82          0        12.97                     
SITE     1 AC1  7 ASP A  75  GLU A 115  ASP A 139  ASP A 174                    
SITE     2 AC1  7  MN A 302  HOH A 530  HOH A 540                               
SITE     1 AC2  7 ASP A  75  ASP A 173  ASP A 189   MN A 301                    
SITE     2 AC2  7 HOH A 528  HOH A 530  HOH A 540                               
SITE     1 AC3  7 HOH A 421  ASP B  75  GLU B 115  ASP B 139                    
SITE     2 AC3  7  MN B 202  HOH B 426  HOH B 429                               
SITE     1 AC4  7 ASP A 198  HOH A 421  ASP B  75  ASP B 189                    
SITE     2 AC4  7  MN B 201  HOH B 426  HOH B 428                               
SITE     1 AC5  6 GLY B 103  HOH B 325  HOH B 413  HOH B 423                    
SITE     2 AC5  6 HOH B 443  HOH B 444                                          
CRYST1  115.802  115.802   38.282  90.00  90.00  90.00 I 41         16          
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      0.008635  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008635  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026122        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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