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Database: PDB
Entry: 2EVR
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Original site: 2EVR 
HEADER    HYDROLASE                               31-OCT-05   2EVR              
TITLE     CRYSTAL STRUCTURE OF A PUTATIVE GAMMA-D-GLUTAMYL-L-DIAMINO ACID       
TITLE    2 ENDOPEPTIDASE (NPUN_R0659) FROM NOSTOC PUNCTIFORME PCC 73102 AT 1.60 
TITLE    3 A RESOLUTION                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COG0791: CELL WALL-ASSOCIATED HYDROLASES (INVASION-        
COMPND   3 ASSOCIATED PROTEINS);                                                
COMPND   4 CHAIN: A;                                                            
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NOSTOC PUNCTIFORME;                             
SOURCE   3 ORGANISM_TAXID: 63737;                                               
SOURCE   4 STRAIN: PCC 73102;                                                   
SOURCE   5 GENE: 53686717;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    PUTATIVE GAMMA-D-GLUTAMYL-L-DIAMINO ACID ENDOPEPTIDASE, STRUCTURAL    
KEYWDS   2 GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN        
KEYWDS   3 STRUCTURE INITIATIVE, PSI-2, HYDROLASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   6   25-JAN-23 2EVR    1       REMARK SEQADV LINK                       
REVDAT   5   13-JUL-11 2EVR    1       VERSN                                    
REVDAT   4   28-JUL-10 2EVR    1       HEADER TITLE  KEYWDS                     
REVDAT   3   10-MAR-09 2EVR    1       JRNL                                     
REVDAT   2   24-FEB-09 2EVR    1       VERSN                                    
REVDAT   1   22-NOV-05 2EVR    0                                                
JRNL        AUTH   Q.XU,S.SUDEK,D.MCMULLAN,M.D.MILLER,B.GEIERSTANGER,D.H.JONES, 
JRNL        AUTH 2 S.S.KRISHNA,G.SPRAGGON,B.BURSALAY,P.ABDUBEK,C.ACOSTA,        
JRNL        AUTH 3 E.AMBING,T.ASTAKHOVA,H.L.AXELROD,D.CARLTON,J.CARUTHERS,      
JRNL        AUTH 4 H.J.CHIU,T.CLAYTON,M.C.DELLER,L.DUAN,Y.ELIAS,M.A.ELSLIGER,   
JRNL        AUTH 5 J.FEUERHELM,S.K.GRZECHNIK,J.HALE,G.WON HAN,J.HAUGEN,         
JRNL        AUTH 6 L.JAROSZEWSKI,K.K.JIN,H.E.KLOCK,M.W.KNUTH,P.KOZBIAL,A.KUMAR, 
JRNL        AUTH 7 D.MARCIANO,A.T.MORSE,E.NIGOGHOSSIAN,L.OKACH,S.OOMMACHEN,     
JRNL        AUTH 8 J.PAULSEN,R.REYES,C.L.RIFE,C.V.TROUT,H.VAN DEN BEDEM,        
JRNL        AUTH 9 D.WEEKES,A.WHITE,G.WOLF,C.ZUBIETA,K.O.HODGSON,J.WOOLEY,      
JRNL        AUTH10 A.M.DEACON,A.GODZIK,S.A.LESLEY,I.A.WILSON                    
JRNL        TITL   STRUCTURAL BASIS OF MUREIN PEPTIDE SPECIFICITY OF A          
JRNL        TITL 2 GAMMA-D-GLUTAMYL-L-DIAMINO ACID ENDOPEPTIDASE.               
JRNL        REF    STRUCTURE                     V.  17   303 2009              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   19217401                                                     
JRNL        DOI    10.1016/J.STR.2008.12.008                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 48970                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.176                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2624                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3466                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 212                          
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1714                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 290                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.12000                                             
REMARK   3    B22 (A**2) : -0.12000                                             
REMARK   3    B33 (A**2) : 0.24000                                              
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): 0.060         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.060         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.042         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.435         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1905 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1661 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2614 ; 1.508 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3887 ; 0.818 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   259 ; 5.766 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    93 ;35.234 ;24.839       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   298 ;11.752 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;15.317 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   281 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2222 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   402 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   336 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1691 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   957 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1192 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   214 ; 0.182 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.231 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    18 ; 0.267 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    52 ; 0.241 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.189 ; 0.200       
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):  1171 ; 1.817 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   482 ; 0.498 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1891 ; 3.153 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   765 ; 4.409 ; 7.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   706 ; 6.192 ; 7.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    13        A    90                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5811  20.4375  46.6320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0207 T22:  -0.0500                                     
REMARK   3      T33:  -0.0518 T12:   0.0229                                     
REMARK   3      T13:  -0.0212 T23:  -0.0409                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5040 L22:   0.4152                                     
REMARK   3      L33:   1.0822 L12:  -0.0337                                     
REMARK   3      L13:   0.6070 L23:   0.0957                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0533 S12:  -0.2022 S13:   0.1257                       
REMARK   3      S21:   0.2303 S22:   0.0386 S23:  -0.0724                       
REMARK   3      S31:  -0.0269 S32:  -0.0029 S33:   0.0147                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    91        A   234                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.5041  -0.2780  36.4309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0018 T22:  -0.0526                                     
REMARK   3      T33:  -0.0435 T12:   0.0081                                     
REMARK   3      T13:  -0.0304 T23:  -0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4912 L22:   1.8081                                     
REMARK   3      L33:   0.6580 L12:  -0.1298                                     
REMARK   3      L13:   0.1426 L23:   0.5367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0395 S12:  -0.0469 S13:  -0.1182                       
REMARK   3      S21:   0.2586 S22:   0.0300 S23:  -0.1091                       
REMARK   3      S31:   0.1542 S32:   0.0093 S33:  -0.0695                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR         
REMARK   3  SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE       
REMARK   3  OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.7    
REMARK   3  TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET    
REMARK   3  INCORPORATION. 3. TENTATIVE MODELS WERE BUILT FOR THE FOLLOWING     
REMARK   3  AREAS WITH POOR DENSITIES: N-TERMINAL A13; C-TERMINAL A233-234.     
REMARK   3  4. THERE ARE SOME UNUSUAL DENSITIES FEATURES NEAR A114, A116        
REMARK   3  AREA THAT WERE LEFT UNINTERPRETED.                                  
REMARK   4                                                                      
REMARK   4 2EVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000035151.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-05                          
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               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0163, 0.9797                     
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51615                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.710                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 4.310                              
REMARK 200  R MERGE                    (I) : 0.11500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.33                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.150                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXD, AUTOSHARP                                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M NACL, 10.0% PEG-6000, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, NANODROP, TEMPERATURE 277K                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+3/4                                              
REMARK 290       8555   -Y,-X,-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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.90500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       23.45250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       70.35750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
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       46.90500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.35750            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       23.45250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       46.90500            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 256  LIES ON A SPECIAL POSITION.                          
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     MSE A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     LYS A    -7                                                      
REMARK 465     ILE A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     ASN A    11                                                      
REMARK 465     PRO A    12                                                      
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     LYS A  13    CG   CD   CE   NZ                                   
REMARK 470     ASP A  74    OD1  OD2                                            
REMARK 470     LYS A 106    CE   NZ                                             
REMARK 470     LYS A 192    CE   NZ                                             
REMARK 470     GLU A 206    CD   OE1  OE2                                       
REMARK 470     GLN A 232    CD   OE1  NE2                                       
REMARK 470     ARG A 233    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    HOH A   310     O    HOH A   370              2.17            
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   O    HOH A   362     O    HOH A   470     7555     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A  19   CB    CYS A  19   SG     -0.106                       
REMARK 500    TRP A 116   CB    TRP A 116   CG     -0.114                       
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    LEU A  14      126.06   -175.56                                   
REMARK 500    LEU A  14      127.82   -176.85                                   
REMARK 500    ASN A  52     -112.75     51.71                                   
REMARK 500    LEU A 181      -82.82   -112.65                                   
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                              NA A 236  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  99   OE1                                                    
REMARK 620 2 GLU A  99   OE2  48.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 235                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 236                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 237                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 238                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 239                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 240                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 241                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 359701   RELATED DB: TARGETDB                            
DBREF  2EVR A    1   234  UNP    B2J9B4   B2J9B4_NOSP7     1    234             
SEQADV 2EVR MSE A  -11  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR GLY A  -10  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR SER A   -9  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR ASP A   -8  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR LYS A   -7  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR ILE A   -6  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR HIS A   -5  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR HIS A   -4  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR HIS A   -3  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR HIS A   -2  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR HIS A   -1  UNP  B2J9B4              EXPRESSION TAG                 
SEQADV 2EVR HIS A    0  UNP  B2J9B4              EXPRESSION TAG                 
SEQRES   1 A  246  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 A  246  VAL ARG LEU SER GLU ALA GLU VAL GLN ASN PRO LYS LEU          
SEQRES   3 A  246  GLY GLU TYR GLN CYS LEU ALA ASP LEU ASN LEU PHE ASP          
SEQRES   4 A  246  SER PRO GLU CYS THR ARG LEU ALA THR GLN SER ALA SER          
SEQRES   5 A  246  GLY ARG HIS LEU TRP VAL THR SER ASN HIS GLN ASN LEU          
SEQRES   6 A  246  ALA VAL GLU VAL TYR LEU CYS GLU ASP ASP TYR PRO GLY          
SEQRES   7 A  246  TRP LEU SER LEU SER ASP PHE ASP SER LEU GLN PRO ALA          
SEQRES   8 A  246  THR VAL PRO TYR GLN ALA ALA THR PHE SER GLU SER GLU          
SEQRES   9 A  246  ILE LYS LYS LEU LEU ALA GLU VAL ILE ALA PHE THR GLN          
SEQRES  10 A  246  LYS ALA MSE GLN GLN SER ASN TYR TYR LEU TRP GLY GLY          
SEQRES  11 A  246  THR VAL GLY PRO ASN TYR ASP CYS SER GLY LEU MSE GLN          
SEQRES  12 A  246  ALA ALA PHE ALA SER VAL GLY ILE TRP LEU PRO ARG ASP          
SEQRES  13 A  246  ALA TYR GLN GLN GLU GLY PHE THR GLN PRO ILE THR ILE          
SEQRES  14 A  246  ALA GLU LEU VAL ALA GLY ASP LEU VAL PHE PHE GLY THR          
SEQRES  15 A  246  SER GLN LYS ALA THR HIS VAL GLY LEU TYR LEU ALA ASP          
SEQRES  16 A  246  GLY TYR TYR ILE HIS SER SER GLY LYS ASP GLN GLY ARG          
SEQRES  17 A  246  ASP GLY ILE GLY ILE ASP ILE LEU SER GLU GLN GLY ASP          
SEQRES  18 A  246  ALA VAL SER LEU SER TYR TYR GLN GLN LEU ARG GLY ALA          
SEQRES  19 A  246  GLY ARG VAL PHE LYS SER TYR GLU PRO GLN ARG ARG              
MODRES 2EVR MSE A  108  MET  SELENOMETHIONINE                                   
MODRES 2EVR MSE A  130  MET  SELENOMETHIONINE                                   
HET    MSE  A 108       8                                                       
HET    MSE  A 130       8                                                       
HET     CL  A 235       1                                                       
HET     NA  A 236       1                                                       
HET    EDO  A 237       4                                                       
HET    EDO  A 238       4                                                       
HET    EDO  A 239       4                                                       
HET    EDO  A 240       4                                                       
HET    EDO  A 241       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    2(C5 H11 N O2 SE)                                            
FORMUL   2   CL    CL 1-                                                        
FORMUL   3   NA    NA 1+                                                        
FORMUL   4  EDO    5(C2 H6 O2)                                                  
FORMUL   9  HOH   *290(H2 O)                                                    
HELIX    1   1 SER A   71  ASP A   74  5                                   4    
HELIX    2   2 SER A   89  GLN A  110  1                                  22    
HELIX    3   3 ASP A  125  SER A  136  1                                  12    
HELIX    4   4 ASP A  144  THR A  152  1                                   9    
HELIX    5   5 THR A  156  LEU A  160  5                                   5    
HELIX    6   6 ASP A  209  GLN A  217  1                                   9    
SHEET    1   A 5 PRO A  65  SER A  69  0                                        
SHEET    2   A 5 ALA A  54  LEU A  59 -1  N  VAL A  57   O  GLY A  66           
SHEET    3   A 5 HIS A  43  GLN A  51 -1  N  TRP A  45   O  TYR A  58           
SHEET    4   A 5 GLY A  15  CYS A  19 -1  N  TYR A  17   O  LEU A  44           
SHEET    5   A 5 LEU A  76  PRO A  78 -1  O  GLN A  77   N  GLN A  18           
SHEET    1   B 2 LEU A  23  PHE A  26  0                                        
SHEET    2   B 2 LEU A  34  SER A  38 -1  O  ALA A  35   N  LEU A  25           
SHEET    1   C 6 GLN A 153  ILE A 155  0                                        
SHEET    2   C 6 LEU A 219  ARG A 224 -1  O  ARG A 224   N  GLN A 153           
SHEET    3   C 6 LEU A 165  GLY A 169 -1  N  LEU A 165   O  GLY A 223           
SHEET    4   C 6 ALA A 174  TYR A 180 -1  O  THR A 175   N  PHE A 168           
SHEET    5   C 6 TYR A 185  SER A 190 -1  O  ILE A 187   N  LEU A 179           
SHEET    6   C 6 GLY A 198  ILE A 203 -1  O  GLY A 200   N  HIS A 188           
LINK         C   ALA A 107                 N   MSE A 108     1555   1555  1.32  
LINK         C   MSE A 108                 N   GLN A 109     1555   1555  1.34  
LINK         C   LEU A 129                 N   MSE A 130     1555   1555  1.34  
LINK         C   MSE A 130                 N   GLN A 131     1555   1555  1.33  
LINK         OE1 GLU A  99                NA    NA A 236     1555   1555  2.18  
LINK         OE2 GLU A  99                NA    NA A 236     1555   1555  2.94  
CISPEP   1 GLY A  121    PRO A  122          0         6.04                     
CISPEP   2 ARG A  233    ARG A  234          0       -12.98                     
SITE     1 AC1  5 ASP A  27  SER A  28  CYS A  31  THR A  32                    
SITE     2 AC1  5 ARG A  33                                                     
SITE     1 AC2  3 GLU A  99  ALA A 162  LEU A 181                               
SITE     1 AC3  6 THR A 119  GLN A 131  ALA A 132  TRP A 140                    
SITE     2 AC3  6 HOH A 244  HOH A 292                                          
SITE     1 AC4  9 ASN A 112  ARG A 196  ASP A 197  GLY A 198                    
SITE     2 AC4  9 ILE A 199  HOH A 276  HOH A 371  HOH A 520                    
SITE     3 AC4  9 HOH A 528                                                     
SITE     1 AC5  5 ASP A  22  LEU A  23  ASN A  24  ASP A  72                    
SITE     2 AC5  5 HOH A 434                                                     
SITE     1 AC6  8 THR A  32  GLN A  37  GLY A 121  PRO A 122                    
SITE     2 AC6  8 ASN A 123  HOH A 246  HOH A 300  HOH A 324                    
SITE     1 AC7  5 GLN A  84  ALA A  85  THR A  87  GLU A  92                    
SITE     2 AC7  5 GLU A 230                                                     
CRYST1   90.470   90.470   93.810  90.00  90.00  90.00 P 41 2 2      8          
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      0.011050  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011050  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010660        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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