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Database: PDB
Entry: 4AIM
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Original site: 4AIM 
HEADER    TRANSFERASE/PEPTIDE                     10-FEB-12   4AIM              
TITLE     CRYSTAL STRUCTURE OF C. CRESCENTUS PNPASE BOUND TO RNASE E RECOGNITION
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: POLYNUCLEOTIDE PHOSPHORYLASE, PNPASE;                       
COMPND   5 EC: 2.7.7.8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RIBONUCLEASE, RNE/RNG FAMILY PROTEIN;                      
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: PNPASE BINDING PEPTIDE - GWW, RESIDUES 885-898;            
COMPND  11 SYNONYM: RNASE E;                                                    
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAULOBACTER VIBRIOIDES;                         
SOURCE   3 ORGANISM_TAXID: 190650;                                              
SOURCE   4 STRAIN: CB15;                                                        
SOURCE   5 ATCC: 19089;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: CAULOBACTER VIBRIOIDES;                         
SOURCE  12 ORGANISM_COMMON: CAULOBACTER CRESCENTUS;                             
SOURCE  13 ORGANISM_TAXID: 155892                                               
KEYWDS    TRANSFERASE-PEPTIDE COMPLEX, KH DOMAIN, S1 DOMAIN, GWW PEPTIDE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.W.HARDWICK,T.GUBBEY,I.HUG,U.JENAL,B.F.LUISI                         
REVDAT   4   20-DEC-23 4AIM    1       REMARK                                   
REVDAT   3   05-FEB-14 4AIM    1       SOURCE JRNL                              
REVDAT   2   04-JUL-12 4AIM    1       JRNL                                     
REVDAT   1   18-APR-12 4AIM    0                                                
JRNL        AUTH   S.W.HARDWICK,T.GUBBEY,I.HUG,U.JENAL,B.F.LUISI                
JRNL        TITL   CRYSTAL STRUCTURE OF CAULOBACTER CRESCENTUS POLYNUCLEOTIDE   
JRNL        TITL 2 PHOSPHORYLASE REVEALS A MECHANISM OF RNA SUBSTRATE           
JRNL        TITL 3 CHANNELLING AND RNA DEGRADOSOME ASSEMBLY.                    
JRNL        REF    OPEN BIOL.                    V.   2 20028 2012              
JRNL        REFN                   ESSN 2046-2441                               
JRNL        PMID   22724061                                                     
JRNL        DOI    10.1098/RSOB.120028                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 14616                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 771                             
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) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1038                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 64                           
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4950                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 2                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 96.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.04000                                              
REMARK   3    B12 (A**2) : -0.01000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.510         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.420         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.049        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5038 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6874 ; 1.703 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   704 ; 7.095 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   180 ;36.982 ;24.611       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   701 ;19.755 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;19.221 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   814 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3850 ; 0.007 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : 1                                          
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   623        A   697                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.4778  -6.7915 100.0420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1232 T22:   0.7689                                     
REMARK   3      T33:   0.2034 T12:   0.0126                                     
REMARK   3      T13:  -0.0258 T23:  -0.2520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0218 L22:  21.9036                                     
REMARK   3      L33:   9.0839 L12:   7.5120                                     
REMARK   3      L13:  -4.7778 L23: -14.1048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0108 S12:  -0.0410 S13:  -0.3593                       
REMARK   3      S21:   1.1125 S22:  -0.3024 S23:   1.0630                       
REMARK   3      S31:  -0.7110 S32:   0.1594 S33:  -0.7085                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4AIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290051258.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-OCT-10                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9778                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH MX-300                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15391                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: PDB ENTRY 3GME                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17 % WT/V PEG 3000, 0.1 M TRI-SODIUM     
REMARK 280  CITRATE                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       95.95500            
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       95.95500            
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       95.95500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14230 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 86990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  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   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     GLU A   697                                                      
REMARK 465     THR A   698                                                      
REMARK 465     GLY A   699                                                      
REMARK 465     GLU A   700                                                      
REMARK 465     ASP A   701                                                      
REMARK 465     LEU A   702                                                      
REMARK 465     SER A   703                                                      
REMARK 465     LYS A   704                                                      
REMARK 465     LYS A   705                                                      
REMARK 465     GLU A   706                                                      
REMARK 465     ALA A   707                                                      
REMARK 465     ALA A   708                                                      
REMARK 465     ALA A   709                                                      
REMARK 465     GLU A   710                                                      
REMARK 465     GLU A   711                                                      
REMARK 465     ALA A   712                                                      
REMARK 465     THR C   885                                                      
REMARK 465     ALA C   886                                                      
REMARK 465     PRO C   887                                                      
REMARK 465     PRO C   888                                                      
REMARK 465     GLU C   889                                                      
REMARK 465     ARG C   898                                                      
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     SER A  -1    OG                                                  
REMARK 470     ARG A   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A   7    CG   CD   CE   NZ                                   
REMARK 470     LYS A  14    CG   CD   CE   NZ                                   
REMARK 470     ARG A  83    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 105    CD   CE   NZ                                        
REMARK 470     LYS A 171    CD   CE   NZ                                        
REMARK 470     GLU A 172    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 221    CG   OD1  OD2                                       
REMARK 470     LYS A 242    CG   CD   CE   NZ                                   
REMARK 470     LYS A 244    CG   CD   CE   NZ                                   
REMARK 470     MET A 245    CG   SD   CE                                        
REMARK 470     LYS A 246    CG   CD   CE   NZ                                   
REMARK 470     LEU A 248    CG   CD1  CD2                                       
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     GLN A 260    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 261    CG   CD   CE   NZ                                   
REMARK 470     LYS A 262    CG   CD   CE   NZ                                   
REMARK 470     GLN A 263    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 264    CG   OD1  OD2                                       
REMARK 470     ARG A 265    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 267    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 273    CG   CD   CE   NZ                                   
REMARK 470     LYS A 274    CG   CD   CE   NZ                                   
REMARK 470     LYS A 275    CG   CD   CE   NZ                                   
REMARK 470     ILE A 277    CG1  CG2  CD1                                       
REMARK 470     LEU A 282    CG   CD1  CD2                                       
REMARK 470     GLU A 285    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 286    CG   OD1  ND2                                       
REMARK 470     TYR A 290    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 293    CG   CD1  CD2                                       
REMARK 470     LYS A 294    CG   CD   CE   NZ                                   
REMARK 470     LEU A 295    CG   CD1  CD2                                       
REMARK 470     ILE A 298    CG1  CG2  CD1                                       
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     LYS A 324    CG   CD   CE   NZ                                   
REMARK 470     ARG A 394    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 420    CG   CD   CE   NZ                                   
REMARK 470     GLU A 421    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 459    CG   CD1  CD2                                       
REMARK 470     GLN A 474    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 489    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 496    CD   CE   NZ                                        
REMARK 470     LYS A 512    CD   CE   NZ                                        
REMARK 470     GLU A 522    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 529    CG   CD   CE   NZ                                   
REMARK 470     GLU A 530    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 552    CG   OD1  OD2                                       
REMARK 470     LYS A 556    CG   CD   CE   NZ                                   
REMARK 470     ILE A 557    CG1  CG2  CD1                                       
REMARK 470     GLU A 558    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 566    CG   CD   CE   NZ                                   
REMARK 470     ILE A 567    CG1  CG2  CD1                                       
REMARK 470     ARG A 568    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 571    CG1  CG2  CD1                                       
REMARK 470     LYS A 576    CG   CD   CE   NZ                                   
REMARK 470     ILE A 578    CG1  CG2  CD1                                       
REMARK 470     ARG A 579    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 580    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 581    CG1  CG2  CD1                                       
REMARK 470     VAL A 582    CG1  CG2                                            
REMARK 470     LYS A 588    CG   CD   CE   NZ                                   
REMARK 470     ASP A 590    CG   OD1  OD2                                       
REMARK 470     ASP A 594    CG   OD1  OD2                                       
REMARK 470     VAL A 596    CG1  CG2                                            
REMARK 470     LYS A 598    CG   CD   CE   NZ                                   
REMARK 470     VAL A 599    CG1  CG2                                            
REMARK 470     ASP A 603    CG   OD1  OD2                                       
REMARK 470     LYS A 606    CG   CD   CE   NZ                                   
REMARK 470     ILE A 607    CG1  CG2  CD1                                       
REMARK 470     LYS A 608    CG   CD   CE   NZ                                   
REMARK 470     ILE A 611    CG1  CG2  CD1                                       
REMARK 470     ILE A 614    CG1  CG2  CD1                                       
REMARK 470     LYS A 615    CG   CD   CE   NZ                                   
REMARK 470     GLU A 620    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 622    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 623    CG1  CG2  CD1                                       
REMARK 470     LYS A 625    CG   CD   CE   NZ                                   
REMARK 470     ILE A 626    CG1  CG2  CD1                                       
REMARK 470     ASP A 628    CG   OD1  OD2                                       
REMARK 470     LYS A 630    CG   CD   CE   NZ                                   
REMARK 470     LYS A 633    CG   CD   CE   NZ                                   
REMARK 470     PHE A 644    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 647    CD   CE   NZ                                        
REMARK 470     VAL A 653    CG1  CG2                                            
REMARK 470     GLN A 655    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 659    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 660    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 663    CG   CD   CE   NZ                                   
REMARK 470     ASP A 666    CG   OD1  OD2                                       
REMARK 470     VAL A 667    CG1  CG2                                            
REMARK 470     LEU A 668    CG   CD1  CD2                                       
REMARK 470     LYS A 669    CG   CD   CE   NZ                                   
REMARK 470     GLU A 670    CG   CD   OE1  OE2                                  
REMARK 470     MET A 673    CG   SD   CE                                        
REMARK 470     LYS A 675    CG   CD   CE   NZ                                   
REMARK 470     LYS A 677    CG   CD   CE   NZ                                   
REMARK 470     LEU A 679    CG   CD1  CD2                                       
REMARK 470     ASP A 682    CG   OD1  OD2                                       
REMARK 470     ASP A 683    CG   OD1  OD2                                       
REMARK 470     ARG A 684    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 686    CG   CD   CE   NZ                                   
REMARK 470     LYS A 688    CG   CD   CE   NZ                                   
REMARK 470     LYS A 692    CD   CE   NZ                                        
REMARK 470     LYS C 890    CG   CD   CE   NZ                                   
REMARK 470     ARG C 897    O    CG   CD   NE   CZ   NH1  NH2                   
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   O    ASN A   206     OE1  GLN A   210              2.05            
REMARK 500   O    ILE A   656     CE   MET A   691              2.07            
REMARK 500   O    VAL A   635     N    PHE A   637              2.09            
REMARK 500   O    ALA A   646     N    ASP A   648              2.11            
REMARK 500   O    GLY A   281     N    SER A   283              2.13            
REMARK 500   O    ALA A   639     CD1  LEU A   650              2.13            
REMARK 500   O    LYS A   556     O    ALA A   601              2.14            
REMARK 500   O    LYS A   246     N    GLY A   250              2.15            
REMARK 500   OH   TYR A   161     O    ILE A   200              2.15            
REMARK 500   O    VAL A   635     N    GLY A   638              2.15            
REMARK 500   OD1  ASP A   368     CG2  THR A   373              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE2  GLN A   119     O    PRO A   337     3555     1.99            
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    MET A   1      122.17     67.31                                   
REMARK 500    ILE A   4      113.94    101.26                                   
REMARK 500    LYS A   5      117.79    164.59                                   
REMARK 500    THR A   8      167.82    -44.57                                   
REMARK 500    ILE A   9       90.17     87.14                                   
REMARK 500    THR A  20     -158.61   -129.40                                   
REMARK 500    ALA A  30       86.09   -152.17                                   
REMARK 500    PRO A  52      -87.37    -42.54                                   
REMARK 500    LYS A  79        9.02     50.00                                   
REMARK 500    VAL A 104      127.40    -28.73                                   
REMARK 500    LEU A 122       14.83     52.17                                   
REMARK 500    GLU A 123      -60.76   -127.99                                   
REMARK 500    ASP A 158      -60.61     62.76                                   
REMARK 500    THR A 166      172.42    -57.81                                   
REMARK 500    THR A 182     -168.63   -102.79                                   
REMARK 500    ALA A 226      -36.59    172.83                                   
REMARK 500    PRO A 235      102.42    -50.01                                   
REMARK 500    ASP A 239      -58.78    -28.10                                   
REMARK 500    ALA A 255       46.25   -109.13                                   
REMARK 500    ALA A 256      -59.91   -137.56                                   
REMARK 500    ILE A 259      100.80    -55.59                                   
REMARK 500    GLN A 263     -106.79    -55.74                                   
REMARK 500    VAL A 269      -79.46    -49.43                                   
REMARK 500    ALA A 271      -85.71    -50.83                                   
REMARK 500    ALA A 272      -69.53    -21.19                                   
REMARK 500    LYS A 273      -92.18    -27.80                                   
REMARK 500    LYS A 274      -75.22    -34.52                                   
REMARK 500    LYS A 275      -73.34    -29.08                                   
REMARK 500    ILE A 277      -49.99    -28.87                                   
REMARK 500    ALA A 278     -101.06    -58.27                                   
REMARK 500    ALA A 279       93.92    -31.91                                   
REMARK 500    LEU A 280      130.09     75.10                                   
REMARK 500    LEU A 282      -44.04     57.43                                   
REMARK 500    SER A 283      161.95     71.91                                   
REMARK 500    ASP A 284       79.51     38.72                                   
REMARK 500    GLU A 285      -76.36    -65.39                                   
REMARK 500    ASN A 286       47.76    160.72                                   
REMARK 500    PRO A 287      -80.50     -2.21                                   
REMARK 500    LEU A 293      -79.04    -66.53                                   
REMARK 500    ALA A 297      -52.11    -27.32                                   
REMARK 500    THR A 314      115.94     71.86                                   
REMARK 500    VAL A 323      -27.46    -35.65                                   
REMARK 500    GLU A 332      119.22   -177.01                                   
REMARK 500    LEU A 336       89.11     57.64                                   
REMARK 500    PRO A 337     -161.88    -72.19                                   
REMARK 500    ARG A 338      -39.30     71.70                                   
REMARK 500    HIS A 340      -29.83    -37.45                                   
REMARK 500    ILE A 367       75.55   -113.42                                   
REMARK 500    ASP A 368       80.09    -58.74                                   
REMARK 500    LEU A 379       76.99   -115.65                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     111 RAMACHANDRAN OUTLIERS.                        
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 ILE A    9     GLU A   10                  147.33                    
REMARK 500 ALA A  554     PRO A  555                 -148.47                    
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 PO4 A 1697                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4AID   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF C. CRESCENTUS PNPASE BOUND TO RNASE E           
REMARK 900 RECOGNITION PEPTIDE                                                  
DBREF  4AIM A    1   712  UNP    Q9AC32   PNP_CAUCR        1    712             
DBREF  4AIM C  885   898  UNP    Q9A749   Q9A749_CAUCR   885    898             
SEQADV 4AIM MET A  -13  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM GLY A  -12  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM SER A  -11  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM SER A  -10  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM HIS A   -9  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM HIS A   -8  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM HIS A   -7  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM HIS A   -6  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM HIS A   -5  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM HIS A   -4  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM SER A   -3  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM GLN A   -2  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM SER A   -1  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM PRO A    0  UNP  Q9AC32              EXPRESSION TAG                 
SEQADV 4AIM ILE A  623  UNP  Q9AC32    VAL   623 CONFLICT                       
SEQRES   1 A  726  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN SER          
SEQRES   2 A  726  PRO MET PHE ASP ILE LYS ARG LYS THR ILE GLU TRP GLY          
SEQRES   3 A  726  GLY LYS THR LEU VAL LEU GLU THR GLY ARG ILE ALA ARG          
SEQRES   4 A  726  GLN ALA ASP GLY ALA VAL LEU ALA THR MET GLY GLU THR          
SEQRES   5 A  726  VAL VAL LEU ALA THR ALA VAL PHE ALA LYS SER GLN LYS          
SEQRES   6 A  726  PRO GLY GLN ASP PHE PHE PRO LEU THR VAL ASN TYR GLN          
SEQRES   7 A  726  GLU LYS THR PHE ALA ALA GLY LYS ILE PRO GLY GLY PHE          
SEQRES   8 A  726  PHE LYS ARG GLU GLY ARG PRO SER GLU LYS GLU THR LEU          
SEQRES   9 A  726  VAL SER ARG LEU ILE ASP ARG PRO ILE ARG PRO LEU PHE          
SEQRES  10 A  726  VAL LYS GLY PHE LYS ASN GLU VAL GLN VAL VAL VAL THR          
SEQRES  11 A  726  VAL LEU GLN HIS ASP LEU GLU ASN ASP PRO ASP ILE LEU          
SEQRES  12 A  726  GLY MET VAL ALA ALA SER ALA ALA LEU CYS LEU SER GLY          
SEQRES  13 A  726  ALA PRO PHE MET GLY PRO ILE GLY ALA ALA ARG VAL GLY          
SEQRES  14 A  726  TRP VAL ASP GLY ALA TYR VAL LEU ASN PRO THR LEU ASP          
SEQRES  15 A  726  GLU MET LYS GLU SER LYS MET ASP LEU VAL VAL ALA GLY          
SEQRES  16 A  726  THR ALA ASP ALA VAL MET MET VAL GLU SER GLU ILE GLN          
SEQRES  17 A  726  GLU LEU SER GLU GLU ILE VAL LEU GLY GLY VAL ASN PHE          
SEQRES  18 A  726  ALA HIS GLN GLN MET GLN ALA VAL ILE ASP ALA ILE ILE          
SEQRES  19 A  726  ASP LEU ALA GLU HIS ALA ALA LYS GLU PRO PHE ALA PHE          
SEQRES  20 A  726  GLU PRO GLU ASP THR ASP ALA ILE LYS ALA LYS MET LYS          
SEQRES  21 A  726  ASP LEU VAL GLY ALA ASP ILE ALA ALA ALA TYR LYS ILE          
SEQRES  22 A  726  GLN LYS LYS GLN ASP ARG TYR GLU ALA VAL GLY ALA ALA          
SEQRES  23 A  726  LYS LYS LYS ALA ILE ALA ALA LEU GLY LEU SER ASP GLU          
SEQRES  24 A  726  ASN PRO THR GLY TYR ASP PRO LEU LYS LEU GLY ALA ILE          
SEQRES  25 A  726  PHE LYS GLU LEU GLU ALA ASP VAL VAL ARG ARG GLY ILE          
SEQRES  26 A  726  LEU ASP THR GLY LEU ARG ILE ASP GLY ARG ASP VAL LYS          
SEQRES  27 A  726  THR VAL ARG PRO ILE LEU GLY GLU VAL GLY ILE LEU PRO          
SEQRES  28 A  726  ARG THR HIS GLY SER ALA LEU PHE THR ARG GLY GLU THR          
SEQRES  29 A  726  GLN ALA ILE VAL VAL ALA THR LEU GLY THR GLY ASP ASP          
SEQRES  30 A  726  GLU GLN PHE ILE ASP ALA LEU GLU GLY THR TYR LYS GLU          
SEQRES  31 A  726  SER PHE LEU LEU HIS TYR ASN PHE PRO PRO TYR SER VAL          
SEQRES  32 A  726  GLY GLU THR GLY ARG MET GLY SER PRO GLY ARG ARG GLU          
SEQRES  33 A  726  ILE GLY HIS GLY LYS LEU ALA TRP ARG ALA LEU ARG PRO          
SEQRES  34 A  726  MET LEU PRO THR LYS GLU ASP PHE PRO TYR THR ILE ARG          
SEQRES  35 A  726  LEU VAL SER GLU ILE THR GLU SER ASN GLY SER SER SER          
SEQRES  36 A  726  MET ALA THR VAL CYS GLY SER SER LEU ALA MET MET ASP          
SEQRES  37 A  726  ALA GLY VAL PRO LEU VAL ARG PRO VAL SER GLY ILE ALA          
SEQRES  38 A  726  MET GLY LEU ILE LEU GLU GLN ASP GLY PHE ALA VAL LEU          
SEQRES  39 A  726  SER ASP ILE LEU GLY ASP GLU ASP HIS LEU GLY ASP MET          
SEQRES  40 A  726  ASP PHE LYS VAL ALA GLY THR SER GLU GLY LEU THR SER          
SEQRES  41 A  726  LEU GLN MET ASP ILE LYS ILE ALA GLY ILE THR PRO ALA          
SEQRES  42 A  726  ILE MET GLU GLN ALA LEU ALA GLN ALA LYS GLU GLY ARG          
SEQRES  43 A  726  ALA HIS ILE LEU GLY GLU MET ASN LYS ALA MET ASP ALA          
SEQRES  44 A  726  PRO ARG ALA ASP VAL GLY ASP PHE ALA PRO LYS ILE GLU          
SEQRES  45 A  726  THR ILE ASN ILE PRO THR ASP LYS ILE ARG GLU VAL ILE          
SEQRES  46 A  726  GLY SER GLY GLY LYS VAL ILE ARG GLU ILE VAL ALA THR          
SEQRES  47 A  726  THR GLY ALA LYS VAL ASP ILE ASN ASP ASP GLY VAL VAL          
SEQRES  48 A  726  LYS VAL SER ALA SER ASP GLY ALA LYS ILE LYS ALA ALA          
SEQRES  49 A  726  ILE ASP TRP ILE LYS SER ILE THR ASP GLU ALA GLU ILE          
SEQRES  50 A  726  GLY LYS ILE TYR ASP GLY LYS VAL VAL LYS VAL VAL ASP          
SEQRES  51 A  726  PHE GLY ALA PHE VAL ASN PHE PHE GLY ALA LYS ASP GLY          
SEQRES  52 A  726  LEU VAL HIS VAL SER GLN ILE SER ASN GLU ARG VAL ALA          
SEQRES  53 A  726  LYS PRO SER ASP VAL LEU LYS GLU GLY GLN MET VAL LYS          
SEQRES  54 A  726  VAL LYS LEU LEU GLY PHE ASP ASP ARG GLY LYS THR LYS          
SEQRES  55 A  726  LEU SER MET LYS VAL VAL ASP GLN GLU THR GLY GLU ASP          
SEQRES  56 A  726  LEU SER LYS LYS GLU ALA ALA ALA GLU GLU ALA                  
SEQRES   1 C   14  THR ALA PRO PRO GLU LYS PRO ARG ARG GLY TRP TRP ARG          
SEQRES   2 C   14  ARG                                                          
HET    PO4  A1697       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  HOH   *2(H2 O)                                                      
HELIX    1   1 THR A   67  GLY A   71  5                                   5    
HELIX    2   2 SER A   85  ARG A  100  1                                  16    
HELIX    3   3 ASP A  125  GLY A  142  1                                  18    
HELIX    4   4 THR A  166  GLU A  172  1                                   7    
HELIX    5   5 SER A  197  HIS A  225  1                                  29    
HELIX    6   6 THR A  238  GLY A  250  1                                  13    
HELIX    7   7 LYS A  261  ALA A  279  1                                  19    
HELIX    8   8 LYS A  294  ASP A  313  1                                  20    
HELIX    9   9 PRO A  385  GLY A  390  5                                   6    
HELIX   10  10 GLY A  399  ARG A  411  1                                  13    
HELIX   11  11 SER A  439  GLY A  456  1                                  18    
HELIX   12  12 LEU A  484  HIS A  489  1                                   6    
HELIX   13  13 THR A  517  LYS A  541  1                                  25    
HELIX   14  14 PRO A  563  ASP A  565  5                                   3    
HELIX   15  15 LYS A  566  GLY A  572  1                                   7    
HELIX   16  16 GLY A  575  GLY A  586  1                                  12    
HELIX   17  17 ASP A  603  ASP A  619  1                                  17    
SHEET    1  AA 6 GLU A  10  TRP A  11  0                                        
SHEET    2  AA 6 LYS A  14  GLU A  19 -1  O  LYS A  14   N  TRP A  11           
SHEET    3  AA 6 GLY A  29  MET A  35 -1  O  LEU A  32   N  GLU A  19           
SHEET    4  AA 6 THR A  38  PHE A  46 -1  O  THR A  38   N  MET A  35           
SHEET    5  AA 6 VAL A 111  GLN A 119 -1  O  GLN A 112   N  VAL A  45           
SHEET    6  AA 6 LEU A  59  GLU A  65  1  O  THR A  60   N  VAL A 113           
SHEET    1  AB 7 ALA A 160  LEU A 163  0                                        
SHEET    2  AB 7 GLY A 150  VAL A 157 -1  O  GLY A 155   N  VAL A 162           
SHEET    3  AB 7 MET A 175  GLY A 181 -1  O  LEU A 177   N  VAL A 154           
SHEET    4  AB 7 VAL A 186  ILE A 193 -1  N  MET A 187   O  ALA A 180           
SHEET    5  AB 7 GLY A 503  ILE A 511 -1  O  THR A 505   N  ILE A 193           
SHEET    6  AB 7 MET A 493  THR A 500 -1  O  ASP A 494   N  ASP A 510           
SHEET    7  AB 7 SER A 464  GLY A 469 -1  O  SER A 464   N  GLY A 499           
SHEET    1  AC 2 ILE A 329  LEU A 330  0                                        
SHEET    2  AC 2 THR A 346  ARG A 347 -1  O  THR A 346   N  LEU A 330           
SHEET    1  AD 4 GLY A 341  ALA A 343  0                                        
SHEET    2  AD 4 ALA A 352  ALA A 356 -1  O  VAL A 354   N  ALA A 343           
SHEET    3  AD 4 VAL A 430  ILE A 433 -1  O  VAL A 430   N  VAL A 355           
SHEET    4  AD 4 HIS A 381  ASN A 383  1  O  HIS A 381   N  SER A 431           
SHEET    1  AE 2 GLN A 365  ILE A 367  0                                        
SHEET    2  AE 2 TYR A 374  GLU A 376 -1  O  TYR A 374   N  ILE A 367           
SHEET    1  AF 2 ILE A 471  LEU A 472  0                                        
SHEET    2  AF 2 PHE A 477  ALA A 478 -1  O  ALA A 478   N  ILE A 471           
SHEET    1  AG 3 LYS A 556  ASN A 561  0                                        
SHEET    2  AG 3 VAL A 596  ALA A 601 -1  O  VAL A 597   N  ILE A 560           
SHEET    3  AG 3 LYS A 588  ASP A 590 -1  O  LYS A 588   N  SER A 600           
SHEET    1  AH 5 GLY A 649  HIS A 652  0                                        
SHEET    2  AH 5 GLY A 638  ASN A 642 -1  O  ALA A 639   N  VAL A 651           
SHEET    3  AH 5 TYR A 627  VAL A 635 -1  O  LYS A 630   N  ASN A 642           
SHEET    4  AH 5 MET A 673  GLY A 680 -1  O  VAL A 674   N  GLY A 629           
SHEET    5  AH 5 LYS A 688  SER A 690 -1  O  LYS A 688   N  GLY A 680           
CISPEP   1 ASP A    3    ILE A    4          0       -12.75                     
CISPEP   2 SER A  283    ASP A  284          0        -8.63                     
CISPEP   3 ASP A  284    GLU A  285          0        -4.32                     
CISPEP   4 GLU A  285    ASN A  286          0        -4.95                     
CISPEP   5 THR A  288    GLY A  289          0         3.67                     
CISPEP   6 PHE A  553    ALA A  554          0        13.03                     
CISPEP   7 LYS A  556    ILE A  557          0        -7.83                     
CISPEP   8 ASP A  590    ILE A  591          0        -0.96                     
CISPEP   9 ALA A  621    GLU A  622          0        -5.02                     
CISPEP  10 GLU A  622    ILE A  623          0        -4.71                     
CISPEP  11 GLY A  624    LYS A  625          0        -3.23                     
CISPEP  12 ASP A  683    ARG A  684          0        -4.54                     
CISPEP  13 VAL A  693    VAL A  694          0         9.04                     
CISPEP  14 VAL A  694    ASP A  695          0        -0.73                     
CISPEP  15 ARG C  893    GLY C  894          0        13.09                     
CISPEP  16 TRP C  896    ARG C  897          0         7.24                     
SITE     1 AC1  4 ARG A 401  HIS A 405  SER A 436  GLY A 438                    
CRYST1   97.329   97.329  191.910  90.00  90.00 120.00 P 63          6          
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      0.010274  0.005932  0.000000        0.00000                         
SCALE2      0.000000  0.011864  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005211        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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