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Database: PDB
Entry: 3NRV
LinkDB: 3NRV
Original site: 3NRV 
HEADER    TRANSCRIPTION REGULATOR                 30-JUN-10   3NRV              
TITLE     CRYSTAL STRUCTURE OF MARR/EMRR FAMILY TRANSCRIPTIONAL REGULATOR FROM  
TITLE    2 ACINETOBACTER SP. ADP1                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE TRANSCRIPTIONAL REGULATOR (MARR/EMRR FAMILY);     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ACINETOBACTER SP. ADP1;                         
SOURCE   3 ORGANISM_TAXID: 62977;                                               
SOURCE   4 GENE: 2878967, ACIAD1811;                                            
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PDM68                                      
KEYWDS    TRANSCRIPTIONAL REGULATOR, PSI-2, PROTEIN STRUCTURE INITIATIVE,       
KEYWDS   2 STRUCTURAL GENOMICS, MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG),  
KEYWDS   3 TRANSCRIPTION REGULATOR                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ZHANG,R.WU,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS      
AUTHOR   2 (MCSG)                                                               
REVDAT   3   27-DEC-23 3NRV    1       REMARK                                   
REVDAT   2   09-SEP-20 3NRV    1       JRNL   REMARK SEQADV LINK                
REVDAT   1   15-SEP-10 3NRV    0                                                
JRNL        AUTH   Z.RONGGUANG,W.RUIYING,J.ANDRZEJ,                             
JRNL        AUTH 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)                
JRNL        TITL   CRYSTAL STRUCTURE OF MARR/EMRR FAMILY TRANSCRIPTIONAL        
JRNL        TITL 2 REGULATOR FROM ACINETOBACTER SP. ADP1                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.58                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 53697                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2856                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 32.5886 -  4.3086    0.98     5472   282  0.1922 0.2271        
REMARK   3     2  4.3086 -  3.4211    1.00     5405   309  0.1653 0.1722        
REMARK   3     3  3.4211 -  2.9890    1.00     5372   301  0.1979 0.2445        
REMARK   3     4  2.9890 -  2.7158    1.00     5375   262  0.2025 0.2301        
REMARK   3     5  2.7158 -  2.5213    1.00     5392   275  0.2003 0.2321        
REMARK   3     6  2.5213 -  2.3727    1.00     5322   282  0.2048 0.2503        
REMARK   3     7  2.3727 -  2.2539    0.99     5358   292  0.2088 0.2634        
REMARK   3     8  2.2539 -  2.1558    1.00     5282   308  0.2107 0.2534        
REMARK   3     9  2.1558 -  2.0728    0.99     5302   284  0.2124 0.2585        
REMARK   3    10  2.0728 -  2.0013    0.98     5234   261  0.2326 0.2853        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 60.18                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.490           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.25540                                              
REMARK   3    B22 (A**2) : -4.25580                                             
REMARK   3    B33 (A**2) : -2.99960                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.22740                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4590                                  
REMARK   3   ANGLE     :  1.040           6148                                  
REMARK   3   CHIRALITY :  0.079            700                                  
REMARK   3   PLANARITY :  0.003            771                                  
REMARK   3   DIHEDRAL  : 17.065           1778                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A RESID 3:145                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8372  29.4190  78.7363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2035 T22:   0.1820                                     
REMARK   3      T33:   0.1892 T12:  -0.0310                                     
REMARK   3      T13:  -0.0764 T23:   0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8559 L22:   0.9545                                     
REMARK   3      L33:   0.7639 L12:   0.0882                                     
REMARK   3      L13:   0.5990 L23:  -0.1739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1579 S12:   0.1587 S13:   0.0427                       
REMARK   3      S21:  -0.2202 S22:   0.0821 S23:   0.1135                       
REMARK   3      S31:  -0.0458 S32:   0.0634 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B RESID 2:145                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6896  26.3160  67.8488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1990 T22:   0.1847                                     
REMARK   3      T33:   0.2000 T12:   0.0217                                     
REMARK   3      T13:   0.0760 T23:   0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2391 L22:   1.0511                                     
REMARK   3      L33:   0.9522 L12:  -0.3502                                     
REMARK   3      L13:  -0.4209 L23:  -0.0353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1570 S12:  -0.1693 S13:  -0.0574                       
REMARK   3      S21:   0.2062 S22:   0.1120 S23:   0.1613                       
REMARK   3      S31:   0.0272 S32:  -0.0032 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C RESID 4:145                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4050  28.7512  90.2053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1927 T22:   0.1750                                     
REMARK   3      T33:   0.1618 T12:   0.0322                                     
REMARK   3      T13:   0.0057 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8358 L22:   1.3402                                     
REMARK   3      L33:   1.1498 L12:   0.3980                                     
REMARK   3      L13:  -0.1437 L23:  -0.1966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1022 S12:  -0.0206 S13:   0.0360                       
REMARK   3      S21:  -0.0853 S22:   0.1046 S23:   0.0344                       
REMARK   3      S31:   0.0678 S32:   0.0628 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D RESID 4:145                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9131  27.1178  56.4163              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1751 T22:   0.1639                                     
REMARK   3      T33:   0.1470 T12:  -0.0346                                     
REMARK   3      T13:   0.0002 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8062 L22:   1.4005                                     
REMARK   3      L33:   1.2723 L12:  -0.3841                                     
REMARK   3      L13:   0.1718 L23:  -0.0638                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0963 S12:   0.0449 S13:  -0.0663                       
REMARK   3      S21:   0.0738 S22:   0.0959 S23:   0.0336                       
REMARK   3      S31:  -0.0537 S32:   0.0664 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3NRV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060202.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97926                            
REMARK 200  MONOCHROMATOR                  : SI 111, CHANNEL                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-2                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53697                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 39.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5; 2M NH4SO4, VAPOR   
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.78650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     SER A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     THR A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     ASN A    84                                                      
REMARK 465     GLY A    85                                                      
REMARK 465     HIS A    86                                                      
REMARK 465     SER A    87                                                      
REMARK 465     GLU A    88                                                      
REMARK 465     ASP A    89                                                      
REMARK 465     LYS A    90                                                      
REMARK 465     ARG A    91                                                      
REMARK 465     THR A    92                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     LYS B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     SER B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     ASN B    84                                                      
REMARK 465     GLY B    85                                                      
REMARK 465     HIS B    86                                                      
REMARK 465     SER B    87                                                      
REMARK 465     GLU B    88                                                      
REMARK 465     ASP B    89                                                      
REMARK 465     LYS B    90                                                      
REMARK 465     ARG B    91                                                      
REMARK 465     THR B    92                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     ASN C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     ASN D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN B   2    CG   CD   OE1  NE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   99   OE2                                                 
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 B   399     O    HOH B   400              2.13            
REMARK 500   O    HOH A   358     O    HOH A   359              2.18            
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    ASP D  51   N     ASP D  51   CA     -0.133                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP D  51   CB  -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR B  30      -35.52   -130.34                                   
REMARK 500    GLU C  88       31.70    -98.39                                   
REMARK 500    ASP D  51      105.01    -41.76                                   
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 SER D   50     ASP D   51                 -128.18                    
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 B 146  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B  33   O                                                      
REMARK 620 2 TYR B  80   OH  110.8                                              
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 SO4 A 146                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 147                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 148                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 149                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 146                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 147                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 148                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 146                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 147                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 148                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 146                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 147                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC88533   RELATED DB: TARGETDB                          
DBREF  3NRV A    1   145  UNP    Q6FBB7   Q6FBB7_ACIAD     1    145             
DBREF  3NRV B    1   145  UNP    Q6FBB7   Q6FBB7_ACIAD     1    145             
DBREF  3NRV C    1   145  UNP    Q6FBB7   Q6FBB7_ACIAD     1    145             
DBREF  3NRV D    1   145  UNP    Q6FBB7   Q6FBB7_ACIAD     1    145             
SEQADV 3NRV SER A   -2  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV ASN A   -1  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV ALA A    0  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV SER B   -2  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV ASN B   -1  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV ALA B    0  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV SER C   -2  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV ASN C   -1  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV ALA C    0  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV SER D   -2  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV ASN D   -1  UNP  Q6FBB7              EXPRESSION TAG                 
SEQADV 3NRV ALA D    0  UNP  Q6FBB7              EXPRESSION TAG                 
SEQRES   1 A  148  SER ASN ALA MSE GLN LYS ILE ASN ILE ASP ARG HIS ALA          
SEQRES   2 A  148  THR ALA GLN ILE ASN MSE LEU ALA ASN LYS LEU MSE LEU          
SEQRES   3 A  148  LYS SER SER THR ALA TYR THR GLN LYS PHE GLY ILE GLY          
SEQRES   4 A  148  MSE THR GLU TRP ARG ILE ILE SER VAL LEU SER SER ALA          
SEQRES   5 A  148  SER ASP CYS SER VAL GLN LYS ILE SER ASP ILE LEU GLY          
SEQRES   6 A  148  LEU ASP LYS ALA ALA VAL SER ARG THR VAL LYS LYS LEU          
SEQRES   7 A  148  GLU GLU LYS LYS TYR ILE GLU VAL ASN GLY HIS SER GLU          
SEQRES   8 A  148  ASP LYS ARG THR TYR ALA ILE ASN LEU THR GLU MSE GLY          
SEQRES   9 A  148  GLN GLU LEU TYR GLU VAL ALA SER ASP PHE ALA ILE GLU          
SEQRES  10 A  148  ARG GLU LYS GLN LEU LEU GLU GLU PHE GLU GLU ALA GLU          
SEQRES  11 A  148  LYS ASP GLN LEU PHE ILE LEU LEU LYS LYS LEU ARG ASN          
SEQRES  12 A  148  LYS VAL ASP GLN MSE                                          
SEQRES   1 B  148  SER ASN ALA MSE GLN LYS ILE ASN ILE ASP ARG HIS ALA          
SEQRES   2 B  148  THR ALA GLN ILE ASN MSE LEU ALA ASN LYS LEU MSE LEU          
SEQRES   3 B  148  LYS SER SER THR ALA TYR THR GLN LYS PHE GLY ILE GLY          
SEQRES   4 B  148  MSE THR GLU TRP ARG ILE ILE SER VAL LEU SER SER ALA          
SEQRES   5 B  148  SER ASP CYS SER VAL GLN LYS ILE SER ASP ILE LEU GLY          
SEQRES   6 B  148  LEU ASP LYS ALA ALA VAL SER ARG THR VAL LYS LYS LEU          
SEQRES   7 B  148  GLU GLU LYS LYS TYR ILE GLU VAL ASN GLY HIS SER GLU          
SEQRES   8 B  148  ASP LYS ARG THR TYR ALA ILE ASN LEU THR GLU MSE GLY          
SEQRES   9 B  148  GLN GLU LEU TYR GLU VAL ALA SER ASP PHE ALA ILE GLU          
SEQRES  10 B  148  ARG GLU LYS GLN LEU LEU GLU GLU PHE GLU GLU ALA GLU          
SEQRES  11 B  148  LYS ASP GLN LEU PHE ILE LEU LEU LYS LYS LEU ARG ASN          
SEQRES  12 B  148  LYS VAL ASP GLN MSE                                          
SEQRES   1 C  148  SER ASN ALA MSE GLN LYS ILE ASN ILE ASP ARG HIS ALA          
SEQRES   2 C  148  THR ALA GLN ILE ASN MSE LEU ALA ASN LYS LEU MSE LEU          
SEQRES   3 C  148  LYS SER SER THR ALA TYR THR GLN LYS PHE GLY ILE GLY          
SEQRES   4 C  148  MSE THR GLU TRP ARG ILE ILE SER VAL LEU SER SER ALA          
SEQRES   5 C  148  SER ASP CYS SER VAL GLN LYS ILE SER ASP ILE LEU GLY          
SEQRES   6 C  148  LEU ASP LYS ALA ALA VAL SER ARG THR VAL LYS LYS LEU          
SEQRES   7 C  148  GLU GLU LYS LYS TYR ILE GLU VAL ASN GLY HIS SER GLU          
SEQRES   8 C  148  ASP LYS ARG THR TYR ALA ILE ASN LEU THR GLU MSE GLY          
SEQRES   9 C  148  GLN GLU LEU TYR GLU VAL ALA SER ASP PHE ALA ILE GLU          
SEQRES  10 C  148  ARG GLU LYS GLN LEU LEU GLU GLU PHE GLU GLU ALA GLU          
SEQRES  11 C  148  LYS ASP GLN LEU PHE ILE LEU LEU LYS LYS LEU ARG ASN          
SEQRES  12 C  148  LYS VAL ASP GLN MSE                                          
SEQRES   1 D  148  SER ASN ALA MSE GLN LYS ILE ASN ILE ASP ARG HIS ALA          
SEQRES   2 D  148  THR ALA GLN ILE ASN MSE LEU ALA ASN LYS LEU MSE LEU          
SEQRES   3 D  148  LYS SER SER THR ALA TYR THR GLN LYS PHE GLY ILE GLY          
SEQRES   4 D  148  MSE THR GLU TRP ARG ILE ILE SER VAL LEU SER SER ALA          
SEQRES   5 D  148  SER ASP CYS SER VAL GLN LYS ILE SER ASP ILE LEU GLY          
SEQRES   6 D  148  LEU ASP LYS ALA ALA VAL SER ARG THR VAL LYS LYS LEU          
SEQRES   7 D  148  GLU GLU LYS LYS TYR ILE GLU VAL ASN GLY HIS SER GLU          
SEQRES   8 D  148  ASP LYS ARG THR TYR ALA ILE ASN LEU THR GLU MSE GLY          
SEQRES   9 D  148  GLN GLU LEU TYR GLU VAL ALA SER ASP PHE ALA ILE GLU          
SEQRES  10 D  148  ARG GLU LYS GLN LEU LEU GLU GLU PHE GLU GLU ALA GLU          
SEQRES  11 D  148  LYS ASP GLN LEU PHE ILE LEU LEU LYS LYS LEU ARG ASN          
SEQRES  12 D  148  LYS VAL ASP GLN MSE                                          
MODRES 3NRV MSE A   16  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE A   22  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE A   37  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE A  100  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE A  145  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE B   16  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE B   22  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE B   37  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE B  100  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE B  145  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE C   16  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE C   22  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE C   37  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE C  100  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE C  145  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE D   16  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE D   22  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE D   37  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE D  100  MET  SELENOMETHIONINE                                   
MODRES 3NRV MSE D  145  MET  SELENOMETHIONINE                                   
HET    MSE  A  16      16                                                       
HET    MSE  A  22       8                                                       
HET    MSE  A  37       8                                                       
HET    MSE  A 100       8                                                       
HET    MSE  A 145       8                                                       
HET    MSE  B  16      16                                                       
HET    MSE  B  22       8                                                       
HET    MSE  B  37       8                                                       
HET    MSE  B 100       8                                                       
HET    MSE  B 145       8                                                       
HET    MSE  C  16       8                                                       
HET    MSE  C  22       8                                                       
HET    MSE  C  37       8                                                       
HET    MSE  C 100       8                                                       
HET    MSE  C 145       8                                                       
HET    MSE  D  16       8                                                       
HET    MSE  D  22       8                                                       
HET    MSE  D  37       8                                                       
HET    MSE  D 100       8                                                       
HET    MSE  D 145       8                                                       
HET    SO4  A 146       5                                                       
HET    SO4  A 147       5                                                       
HET    GOL  A 148       6                                                       
HET    GOL  A 149       6                                                       
HET     NA  B 146       1                                                       
HET    GOL  B 147       6                                                       
HET    GOL  B 148       6                                                       
HET    SO4  C 146       5                                                       
HET    SO4  C 147       5                                                       
HET    SO4  C 148       5                                                       
HET    SO4  D 146       5                                                       
HET    SO4  D 147       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      NA SODIUM ION                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    20(C5 H11 N O2 SE)                                           
FORMUL   5  SO4    7(O4 S 2-)                                                   
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL   9   NA    NA 1+                                                        
FORMUL  17  HOH   *302(H2 O)                                                    
HELIX    1   1 ASN A    5  ARG A    8  5                                   4    
HELIX    2   2 HIS A    9  LYS A   24  1                                  16    
HELIX    3   3 THR A   30  GLY A   34  5                                   5    
HELIX    4   4 GLY A   36  ALA A   49  1                                  14    
HELIX    5   5 SER A   53  GLY A   62  1                                  10    
HELIX    6   6 ASP A   64  LYS A   78  1                                  15    
HELIX    7   7 THR A   98  ALA A  112  1                                  15    
HELIX    8   8 ALA A  112  LEU A  120  1                                   9    
HELIX    9   9 GLU A  124  MSE A  145  1                                  22    
HELIX   10  10 ASN B    5  ARG B    8  5                                   4    
HELIX   11  11 HIS B    9  LEU B   23  1                                  15    
HELIX   12  12 THR B   30  GLY B   34  5                                   5    
HELIX   13  13 GLY B   36  ALA B   49  1                                  14    
HELIX   14  14 SER B   53  GLY B   62  1                                  10    
HELIX   15  15 ASP B   64  LYS B   78  1                                  15    
HELIX   16  16 THR B   98  ALA B  112  1                                  15    
HELIX   17  17 ALA B  112  LEU B  120  1                                   9    
HELIX   18  18 GLU B  124  MSE B  145  1                                  22    
HELIX   19  19 HIS C    9  GLY C   34  1                                  26    
HELIX   20  20 GLY C   36  ALA C   49  1                                  14    
HELIX   21  21 SER C   53  GLY C   62  1                                  10    
HELIX   22  22 ASP C   64  LYS C   78  1                                  15    
HELIX   23  23 THR C   98  LEU C  120  1                                  23    
HELIX   24  24 GLU C  124  GLN C  144  1                                  21    
HELIX   25  25 HIS D    9  GLY D   34  1                                  26    
HELIX   26  26 GLY D   36  ALA D   49  1                                  14    
HELIX   27  27 SER D   53  GLY D   62  1                                  10    
HELIX   28  28 ASP D   64  LYS D   78  1                                  15    
HELIX   29  29 THR D   98  LEU D  120  1                                  23    
HELIX   30  30 GLU D  124  MSE D  145  1                                  22    
SHEET    1   A 2 ILE A  81  GLU A  82  0                                        
SHEET    2   A 2 ASN A  96  LEU A  97 -1  O  ASN A  96   N  GLU A  82           
SHEET    1   B 2 ILE B  81  GLU B  82  0                                        
SHEET    2   B 2 ASN B  96  LEU B  97 -1  O  ASN B  96   N  GLU B  82           
SHEET    1   C 2 ILE C  81  ASN C  84  0                                        
SHEET    2   C 2 ALA C  94  LEU C  97 -1  O  ALA C  94   N  ASN C  84           
SHEET    1   D 2 ILE D  81  ASN D  84  0                                        
SHEET    2   D 2 ALA D  94  LEU D  97 -1  O  ALA D  94   N  ASN D  84           
LINK         C   ASN A  15                 N  AMSE A  16     1555   1555  1.32  
LINK         C   ASN A  15                 N  BMSE A  16     1555   1555  1.34  
LINK         C  AMSE A  16                 N   LEU A  17     1555   1555  1.33  
LINK         C  BMSE A  16                 N   LEU A  17     1555   1555  1.33  
LINK         C   LEU A  21                 N   MSE A  22     1555   1555  1.33  
LINK         C   MSE A  22                 N   LEU A  23     1555   1555  1.33  
LINK         C   GLY A  36                 N   MSE A  37     1555   1555  1.33  
LINK         C   MSE A  37                 N   THR A  38     1555   1555  1.33  
LINK         C   GLU A  99                 N   MSE A 100     1555   1555  1.33  
LINK         C   MSE A 100                 N   GLY A 101     1555   1555  1.33  
LINK         C   GLN A 144                 N   MSE A 145     1555   1555  1.33  
LINK         C   ASN B  15                 N  AMSE B  16     1555   1555  1.34  
LINK         C   ASN B  15                 N  BMSE B  16     1555   1555  1.32  
LINK         C  AMSE B  16                 N   LEU B  17     1555   1555  1.33  
LINK         C  BMSE B  16                 N   LEU B  17     1555   1555  1.33  
LINK         C   LEU B  21                 N   MSE B  22     1555   1555  1.33  
LINK         C   MSE B  22                 N   LEU B  23     1555   1555  1.33  
LINK         C   GLY B  36                 N   MSE B  37     1555   1555  1.33  
LINK         C   MSE B  37                 N   THR B  38     1555   1555  1.33  
LINK         C   GLU B  99                 N   MSE B 100     1555   1555  1.32  
LINK         C   MSE B 100                 N   GLY B 101     1555   1555  1.32  
LINK         C   GLN B 144                 N   MSE B 145     1555   1555  1.34  
LINK         C   ASN C  15                 N   MSE C  16     1555   1555  1.33  
LINK         C   MSE C  16                 N   LEU C  17     1555   1555  1.33  
LINK         C   LEU C  21                 N   MSE C  22     1555   1555  1.33  
LINK         C   MSE C  22                 N   LEU C  23     1555   1555  1.34  
LINK         C   GLY C  36                 N   MSE C  37     1555   1555  1.33  
LINK         C   MSE C  37                 N   THR C  38     1555   1555  1.32  
LINK         C   GLU C  99                 N   MSE C 100     1555   1555  1.33  
LINK         C   MSE C 100                 N   GLY C 101     1555   1555  1.33  
LINK         C   GLN C 144                 N   MSE C 145     1555   1555  1.33  
LINK         C   ASN D  15                 N   MSE D  16     1555   1555  1.33  
LINK         C   MSE D  16                 N   LEU D  17     1555   1555  1.33  
LINK         C   LEU D  21                 N   MSE D  22     1555   1555  1.33  
LINK         C   MSE D  22                 N   LEU D  23     1555   1555  1.34  
LINK         C   GLY D  36                 N   MSE D  37     1555   1555  1.33  
LINK         C   MSE D  37                 N   THR D  38     1555   1555  1.32  
LINK         C   GLU D  99                 N   MSE D 100     1555   1555  1.33  
LINK         C   MSE D 100                 N   GLY D 101     1555   1555  1.33  
LINK         C   GLN D 144                 N   MSE D 145     1555   1555  1.33  
LINK         O   PHE B  33                NA    NA B 146     1555   1555  2.73  
LINK         OH  TYR B  80                NA    NA B 146     1555   1555  2.77  
SITE     1 AC1  5 ALA A  49  SER A  50  HOH A 396  LYS C  20                    
SITE     2 AC1  5 HOH C 165                                                     
SITE     1 AC2  4 LYS A  24  TYR A  29  MSE A  37  GOL A 149                    
SITE     1 AC3 10 MSE A  22  ARG A  41  SER A  44  LEU A  61                    
SITE     2 AC3 10 HOH A 161  HOH A 483  HOH A 494  ASN C  15                    
SITE     3 AC3 10 ASN C  19  MSE C  22                                          
SITE     1 AC4  7 THR A  30  TRP A  40  ALA A 112  SO4 A 147                    
SITE     2 AC4  7 HOH A 156  HOH A 171  HIS C   9                               
SITE     1 AC5  5 PHE B  33  TYR B  80  GLY C  85  TYR C  93                    
SITE     2 AC5  5 HOH C 393                                                     
SITE     1 AC6  9 MSE B  22  ARG B  41  SER B  44  LEU B  61                    
SITE     2 AC6  9 HOH B 157  HOH B 445  ASN D  15  ASN D  19                    
SITE     3 AC6  9 MSE D  22                                                     
SITE     1 AC7  5 THR B  38  ARG B  41  HOH B 482  ASP D  64                    
SITE     2 AC7  5 HOH D 176                                                     
SITE     1 AC8  4 ASP A  64  LYS A  65  ARG C  70  LYS C  74                    
SITE     1 AC9  3 GLU A 125  LYS A 128  ARG C   8                               
SITE     1 BC1  7 SER C  50  ASP C  51  HIS C  86  ARG C  91                    
SITE     2 BC1  7 ALA C  94  ASN C  96  HOH C 170                               
SITE     1 BC2  3 ALA B  49  SER B  50  LYS D  20                               
SITE     1 BC3  4 ASP B  64  LYS B  65  ARG D  70  LYS D  74                    
CRYST1   72.809   59.573   97.753  90.00  89.99  90.00 P 1 21 1      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      0.013735  0.000000 -0.000002        0.00000                         
SCALE2      0.000000  0.016786  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010230        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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