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Database: PDB
Entry: 3NRT
LinkDB: 3NRT
Original site: 3NRT 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   30-JUN-10   3NRT              
TITLE     THE CRYSTAL STRUCUTRE OF PUTATIVE RYANODINE RECEPTOR FROM BACTEROIDES 
TITLE    2 THETAIOTAOMICRON VPI-5482                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE RYANODINE RECEPTOR;                               
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;                   
SOURCE   3 ORGANISM_TAXID: 226186;                                              
SOURCE   4 STRAIN: VPI-5482;                                                    
SOURCE   5 GENE: BT_2247;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDM68                                     
KEYWDS    PSI-2, PROTEIN STRUCTURE INITIATIVE, STRUCTURAL GENOMICS, MIDWEST     
KEYWDS   2 CENTER FOR STRUCTURAL GENOMICS (MCSG), UNKNOWN FUNCTION              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.WU,R.ZHANG,A.JAMES,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL       
AUTHOR   2 GENOMICS (MCSG)                                                      
REVDAT   1   15-SEP-10 3NRT    0                                                
JRNL        AUTH   W.RUIYING,Z.RONGGUANG,A.JAMES,J.ANDRZEJ,                     
JRNL        AUTH 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)                
JRNL        TITL   HE CRYSTAL STRUCUTRE OF PUTATIVE RYANODINE RECEPTOR FROM     
JRNL        TITL 2 BACTEROIDES THETAIOTAOMICRON VPI-5482                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.890                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 61648                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3128                            
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 32.4829 -  5.3300    0.94     5673   319  0.1977 0.2171        
REMARK   3     2  5.3300 -  4.2335    0.95     5785   325  0.1602 0.2057        
REMARK   3     3  4.2335 -  3.6992    0.98     5927   332  0.1653 0.2312        
REMARK   3     4  3.6992 -  3.3614    0.99     6033   337  0.1784 0.2360        
REMARK   3     5  3.3614 -  3.1207    0.99     5984   298  0.1923 0.2649        
REMARK   3     6  3.1207 -  2.9368    0.99     6108   318  0.1997 0.2743        
REMARK   3     7  2.9368 -  2.7898    0.99     5923   348  0.2441 0.2940        
REMARK   3     8  2.7898 -  2.6684    0.99     6034   271  0.2475 0.3181        
REMARK   3     9  2.6684 -  2.5657    0.98     6007   291  0.2384 0.3031        
REMARK   3    10  2.5657 -  2.4772    0.84     5046   289  0.2593 0.3017        
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              : 0.38                                          
REMARK   3   B_SOL              : 44.55                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
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) : -2.75530                                             
REMARK   3    B22 (A**2) : 7.88900                                              
REMARK   3    B33 (A**2) : -5.13370                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -3.24240                                             
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      :  0.009           4875                                  
REMARK   3   ANGLE     :  1.129           6570                                  
REMARK   3   CHIRALITY :  0.072            693                                  
REMARK   3   PLANARITY :  0.005            852                                  
REMARK   3   DIHEDRAL  : 20.146           1903                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A RESID 7:100                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9914  -1.7027  33.3547              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1193 T22:   0.1107                                     
REMARK   3      T33:   0.2001 T12:  -0.0022                                     
REMARK   3      T13:  -0.0102 T23:   0.0324                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3204 L22:   0.3631                                     
REMARK   3      L33:   1.2098 L12:  -0.4423                                     
REMARK   3      L13:  -0.0619 L23:  -0.0537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0088 S12:  -0.1505 S13:   0.0497                       
REMARK   3      S21:   0.0293 S22:  -0.0157 S23:  -0.0564                       
REMARK   3      S31:   0.0438 S32:   0.0478 S33:   0.0074                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B RESID 7:100                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3802  -4.3169  26.4335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1968 T22:   0.1339                                     
REMARK   3      T33:   0.1241 T12:   0.0276                                     
REMARK   3      T13:   0.0191 T23:   0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4484 L22:   0.1264                                     
REMARK   3      L33:   1.5533 L12:  -0.1037                                     
REMARK   3      L13:  -0.2326 L23:  -0.2146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0335 S12:   0.1751 S13:   0.0240                       
REMARK   3      S21:  -0.0730 S22:  -0.0078 S23:  -0.0015                       
REMARK   3      S31:  -0.0198 S32:  -0.1522 S33:   0.0460                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C RESID 7:100                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5263 -12.2126   1.8866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2780 T22:   0.1872                                     
REMARK   3      T33:   0.1498 T12:  -0.0526                                     
REMARK   3      T13:   0.0288 T23:  -0.0547                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2777 L22:   0.5394                                     
REMARK   3      L33:   1.8138 L12:  -0.0379                                     
REMARK   3      L13:   0.2314 L23:  -0.9816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0365 S12:   0.1308 S13:  -0.1461                       
REMARK   3      S21:  -0.0723 S22:   0.1080 S23:  -0.0641                       
REMARK   3      S31:   0.3428 S32:  -0.1453 S33:  -0.0595                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D RESID 7:100                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7014 -11.1334  -6.0981              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1400 T22:   0.2095                                     
REMARK   3      T33:   0.1809 T12:  -0.0001                                     
REMARK   3      T13:  -0.0155 T23:   0.0254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8132 L22:   0.6711                                     
REMARK   3      L33:   2.2378 L12:   0.4187                                     
REMARK   3      L13:  -0.2399 L23:  -0.8144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0549 S12:  -0.2118 S13:  -0.2386                       
REMARK   3      S21:  -0.1451 S22:  -0.1403 S23:   0.0150                       
REMARK   3      S31:   0.1252 S32:   0.1632 S33:   0.0462                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN E RESID 7:100                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1247   6.2605  42.1792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0900 T22:   0.1250                                     
REMARK   3      T33:   0.2505 T12:  -0.0500                                     
REMARK   3      T13:  -0.0302 T23:  -0.0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7526 L22:   0.2776                                     
REMARK   3      L33:   1.4461 L12:  -0.6530                                     
REMARK   3      L13:   1.0618 L23:  -0.5501                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1617 S12:  -0.0582 S13:   0.3649                       
REMARK   3      S21:   0.0051 S22:   0.0922 S23:  -0.1282                       
REMARK   3      S31:  -0.1359 S32:   0.1599 S33:   0.1001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN F RESID 7:100                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  25.6903   4.9406  47.1691              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1551 T22:   0.1777                                     
REMARK   3      T33:   0.1328 T12:  -0.0025                                     
REMARK   3      T13:  -0.0035 T23:   0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3791 L22:   0.3031                                     
REMARK   3      L33:   1.0721 L12:  -0.5117                                     
REMARK   3      L13:   0.5025 L23:   0.2315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0785 S12:   0.2084 S13:   0.1554                       
REMARK   3      S21:   0.0877 S22:  -0.1278 S23:  -0.1244                       
REMARK   3      S31:  -0.2278 S32:  -0.0762 S33:   0.0435                       
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 3NRT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060200.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAR-09                          
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-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
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   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.540                              
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     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.170                              
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   (%): 60.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 400, 0.2M MGCL, , PH 6.5,        
REMARK 280  VAPOR 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       44.63600            
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, 3                                                 
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: 4730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 4460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 4420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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     LYS A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     ASP A   100                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     ASN C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     ASN D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     ASN D     4                                                      
REMARK 465     LYS D     5                                                      
REMARK 465     LEU D     6                                                      
REMARK 465     ASP D   100                                                      
REMARK 465     SER E    -2                                                      
REMARK 465     ASN E    -1                                                      
REMARK 465     ALA E     0                                                      
REMARK 465     MSE E     1                                                      
REMARK 465     LYS E     2                                                      
REMARK 465     SER F    -2                                                      
REMARK 465     ASN F    -1                                                      
REMARK 465     ALA F     0                                                      
REMARK 465     MSE F     1                                                      
REMARK 465     LYS F     2                                                      
REMARK 465     GLU F     3                                                      
REMARK 465     ASN F     4                                                      
REMARK 465     LYS F     5                                                      
REMARK 465     LEU F     6                                                      
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 C   2    CG   CD   CE   NZ                                   
REMARK 470     GLU C   3    CG   CD   OE1  OE2                                  
REMARK 470     ASN C   4    CG   OD1  ND2                                       
REMARK 470     GLU E   3    CG   CD   OE1  OE2                                  
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   11   CD                                                  
REMARK 480     ASP A   19   CG                                                  
REMARK 480     GLU A   73   CD                                                  
REMARK 480     GLU B   11   CD                                                  
REMARK 480     GLU B   73   CD                                                  
REMARK 480     GLU C   11   CD                                                  
REMARK 480     GLU C   73   CD                                                  
REMARK 480     GLU D   11   CD                                                  
REMARK 480     GLU D   73   CD                                                  
REMARK 480     GLU E   11   CD                                                  
REMARK 480     GLU E   73   CD                                                  
REMARK 480     GLU F   11   CD                                                  
REMARK 480     GLU F   73   CD                                                  
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    ASP B  55      108.95   -160.94                                   
REMARK 500    ASP C   7       60.45   -114.89                                   
REMARK 500    ASP D  45       22.53    -76.96                                   
REMARK 500    LYS D  59       73.29     45.84                                   
REMARK 500    PRO D  62        0.75    -69.76                                   
REMARK 500    ASP E   7       67.19   -116.08                                   
REMARK 500    GLU E  46       32.46    -96.41                                   
REMARK 500    LYS E  59       62.99     61.70                                   
REMARK 500    ALA F  42      -71.20    -47.40                                   
REMARK 500    ASP F  45       25.92    -71.61                                   
REMARK 500    GLU F  46       35.94   -148.43                                   
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                              MG A 102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD2                                                    
REMARK 620 2 ASP B  56   OD2 144.8                                              
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 GOL A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 101                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC81718   RELATED DB: TARGETDB                          
DBREF  3NRT A    1   100  UNP    Q8A5J2   Q8A5J2_BACTN     1    100             
DBREF  3NRT B    1   100  UNP    Q8A5J2   Q8A5J2_BACTN     1    100             
DBREF  3NRT C    1   100  UNP    Q8A5J2   Q8A5J2_BACTN     1    100             
DBREF  3NRT D    1   100  UNP    Q8A5J2   Q8A5J2_BACTN     1    100             
DBREF  3NRT E    1   100  UNP    Q8A5J2   Q8A5J2_BACTN     1    100             
DBREF  3NRT F    1   100  UNP    Q8A5J2   Q8A5J2_BACTN     1    100             
SEQADV 3NRT SER A   -2  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ASN A   -1  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ALA A    0  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT SER B   -2  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ASN B   -1  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ALA B    0  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT SER C   -2  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ASN C   -1  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ALA C    0  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT SER D   -2  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ASN D   -1  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ALA D    0  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT SER E   -2  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ASN E   -1  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ALA E    0  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT SER F   -2  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ASN F   -1  UNP  Q8A5J2              EXPRESSION TAG                 
SEQADV 3NRT ALA F    0  UNP  Q8A5J2              EXPRESSION TAG                 
SEQRES   1 A  103  SER ASN ALA MSE LYS GLU ASN LYS LEU ASP TYR ILE PRO          
SEQRES   2 A  103  GLU PRO MSE ASP LEU SER LEU VAL ASP LEU PRO GLU SER          
SEQRES   3 A  103  LEU ILE GLN LEU SER GLU ARG ILE ALA GLU ASN VAL HIS          
SEQRES   4 A  103  GLU VAL TRP ALA LYS ALA ARG ILE ASP GLU GLY TRP THR          
SEQRES   5 A  103  TYR GLY GLU LYS ARG ASP ASP ILE HIS LYS LYS HIS PRO          
SEQRES   6 A  103  CYS LEU VAL PRO TYR ASP GLU LEU PRO GLU GLU GLU LYS          
SEQRES   7 A  103  GLU TYR ASP ARG ASN THR ALA MSE ASN THR ILE LYS MSE          
SEQRES   8 A  103  VAL LYS LYS LEU GLY PHE ARG ILE GLU LYS GLU ASP              
SEQRES   1 B  103  SER ASN ALA MSE LYS GLU ASN LYS LEU ASP TYR ILE PRO          
SEQRES   2 B  103  GLU PRO MSE ASP LEU SER LEU VAL ASP LEU PRO GLU SER          
SEQRES   3 B  103  LEU ILE GLN LEU SER GLU ARG ILE ALA GLU ASN VAL HIS          
SEQRES   4 B  103  GLU VAL TRP ALA LYS ALA ARG ILE ASP GLU GLY TRP THR          
SEQRES   5 B  103  TYR GLY GLU LYS ARG ASP ASP ILE HIS LYS LYS HIS PRO          
SEQRES   6 B  103  CYS LEU VAL PRO TYR ASP GLU LEU PRO GLU GLU GLU LYS          
SEQRES   7 B  103  GLU TYR ASP ARG ASN THR ALA MSE ASN THR ILE LYS MSE          
SEQRES   8 B  103  VAL LYS LYS LEU GLY PHE ARG ILE GLU LYS GLU ASP              
SEQRES   1 C  103  SER ASN ALA MSE LYS GLU ASN LYS LEU ASP TYR ILE PRO          
SEQRES   2 C  103  GLU PRO MSE ASP LEU SER LEU VAL ASP LEU PRO GLU SER          
SEQRES   3 C  103  LEU ILE GLN LEU SER GLU ARG ILE ALA GLU ASN VAL HIS          
SEQRES   4 C  103  GLU VAL TRP ALA LYS ALA ARG ILE ASP GLU GLY TRP THR          
SEQRES   5 C  103  TYR GLY GLU LYS ARG ASP ASP ILE HIS LYS LYS HIS PRO          
SEQRES   6 C  103  CYS LEU VAL PRO TYR ASP GLU LEU PRO GLU GLU GLU LYS          
SEQRES   7 C  103  GLU TYR ASP ARG ASN THR ALA MSE ASN THR ILE LYS MSE          
SEQRES   8 C  103  VAL LYS LYS LEU GLY PHE ARG ILE GLU LYS GLU ASP              
SEQRES   1 D  103  SER ASN ALA MSE LYS GLU ASN LYS LEU ASP TYR ILE PRO          
SEQRES   2 D  103  GLU PRO MSE ASP LEU SER LEU VAL ASP LEU PRO GLU SER          
SEQRES   3 D  103  LEU ILE GLN LEU SER GLU ARG ILE ALA GLU ASN VAL HIS          
SEQRES   4 D  103  GLU VAL TRP ALA LYS ALA ARG ILE ASP GLU GLY TRP THR          
SEQRES   5 D  103  TYR GLY GLU LYS ARG ASP ASP ILE HIS LYS LYS HIS PRO          
SEQRES   6 D  103  CYS LEU VAL PRO TYR ASP GLU LEU PRO GLU GLU GLU LYS          
SEQRES   7 D  103  GLU TYR ASP ARG ASN THR ALA MSE ASN THR ILE LYS MSE          
SEQRES   8 D  103  VAL LYS LYS LEU GLY PHE ARG ILE GLU LYS GLU ASP              
SEQRES   1 E  103  SER ASN ALA MSE LYS GLU ASN LYS LEU ASP TYR ILE PRO          
SEQRES   2 E  103  GLU PRO MSE ASP LEU SER LEU VAL ASP LEU PRO GLU SER          
SEQRES   3 E  103  LEU ILE GLN LEU SER GLU ARG ILE ALA GLU ASN VAL HIS          
SEQRES   4 E  103  GLU VAL TRP ALA LYS ALA ARG ILE ASP GLU GLY TRP THR          
SEQRES   5 E  103  TYR GLY GLU LYS ARG ASP ASP ILE HIS LYS LYS HIS PRO          
SEQRES   6 E  103  CYS LEU VAL PRO TYR ASP GLU LEU PRO GLU GLU GLU LYS          
SEQRES   7 E  103  GLU TYR ASP ARG ASN THR ALA MSE ASN THR ILE LYS MSE          
SEQRES   8 E  103  VAL LYS LYS LEU GLY PHE ARG ILE GLU LYS GLU ASP              
SEQRES   1 F  103  SER ASN ALA MSE LYS GLU ASN LYS LEU ASP TYR ILE PRO          
SEQRES   2 F  103  GLU PRO MSE ASP LEU SER LEU VAL ASP LEU PRO GLU SER          
SEQRES   3 F  103  LEU ILE GLN LEU SER GLU ARG ILE ALA GLU ASN VAL HIS          
SEQRES   4 F  103  GLU VAL TRP ALA LYS ALA ARG ILE ASP GLU GLY TRP THR          
SEQRES   5 F  103  TYR GLY GLU LYS ARG ASP ASP ILE HIS LYS LYS HIS PRO          
SEQRES   6 F  103  CYS LEU VAL PRO TYR ASP GLU LEU PRO GLU GLU GLU LYS          
SEQRES   7 F  103  GLU TYR ASP ARG ASN THR ALA MSE ASN THR ILE LYS MSE          
SEQRES   8 F  103  VAL LYS LYS LEU GLY PHE ARG ILE GLU LYS GLU ASP              
MODRES 3NRT MSE A   13  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE A   83  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE A   88  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE B   13  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE B   83  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE B   88  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE C   13  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE C   83  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE C   88  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE D   13  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE D   83  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE D   88  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE E   13  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE E   83  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE E   88  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE F   13  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE F   83  MET  SELENOMETHIONINE                                   
MODRES 3NRT MSE F   88  MET  SELENOMETHIONINE                                   
HET    MSE  A  13       8                                                       
HET    MSE  A  83       8                                                       
HET    MSE  A  88       8                                                       
HET    MSE  B  13       8                                                       
HET    MSE  B  83       8                                                       
HET    MSE  B  88       8                                                       
HET    MSE  C  13       8                                                       
HET    MSE  C  83       8                                                       
HET    MSE  C  88       8                                                       
HET    MSE  D  13       8                                                       
HET    MSE  D  83       8                                                       
HET    MSE  D  88       8                                                       
HET    MSE  E  13       8                                                       
HET    MSE  E  83       8                                                       
HET    MSE  E  88       8                                                       
HET    MSE  F  13       8                                                       
HET    MSE  F  83       8                                                       
HET    MSE  F  88       8                                                       
HET    GOL  A 101       6                                                       
HET     MG  A 102       1                                                       
HET    GOL  A 103       6                                                       
HET    GOL  B 101       6                                                       
HET    GOL  C 101       6                                                       
HET    GOL  D 101       6                                                       
HET    GOL  E 101       6                                                       
HET    GOL  F 101       6                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    18(C5 H11 N O2 SE)                                           
FORMUL   7  GOL    7(C3 H8 O3)                                                  
FORMUL   8   MG    MG 2+                                                        
FORMUL  15  HOH   *85(H2 O)                                                     
HELIX    1   1 PRO A   21  GLN A   26  1                                   6    
HELIX    2   2 LEU A   27  GLU A   46  1                                  20    
HELIX    3   3 PRO A   66  LEU A   70  5                                   5    
HELIX    4   4 PRO A   71  LEU A   92  1                                  22    
HELIX    5   5 PRO B   21  GLN B   26  1                                   6    
HELIX    6   6 LEU B   27  GLU B   46  1                                  20    
HELIX    7   7 PRO B   66  LEU B   70  5                                   5    
HELIX    8   8 PRO B   71  LEU B   92  1                                  22    
HELIX    9   9 PRO C   21  GLN C   26  1                                   6    
HELIX   10  10 LEU C   27  ASP C   45  1                                  19    
HELIX   11  11 PRO C   66  LEU C   70  5                                   5    
HELIX   12  12 PRO C   71  LEU C   92  1                                  22    
HELIX   13  13 PRO D   21  GLN D   26  1                                   6    
HELIX   14  14 LEU D   27  ASP D   45  1                                  19    
HELIX   15  15 PRO D   66  LEU D   70  5                                   5    
HELIX   16  16 PRO D   71  LEU D   92  1                                  22    
HELIX   17  17 PRO E   21  GLN E   26  1                                   6    
HELIX   18  18 LEU E   27  ASP E   45  1                                  19    
HELIX   19  19 PRO E   66  LEU E   70  5                                   5    
HELIX   20  20 PRO E   71  LEU E   92  1                                  22    
HELIX   21  21 PRO F   21  GLN F   26  1                                   6    
HELIX   22  22 LEU F   27  ASP F   45  1                                  19    
HELIX   23  23 PRO F   66  LEU F   70  5                                   5    
HELIX   24  24 PRO F   71  LEU F   92  1                                  22    
SHEET    1   A 2 THR A  49  TYR A  50  0                                        
SHEET    2   A 2 LYS A  60  HIS A  61  1  O  HIS A  61   N  THR A  49           
SHEET    1   B 2 PHE A  94  LYS A  98  0                                        
SHEET    2   B 2 PHE B  94  LYS B  98 -1  O  ARG B  95   N  GLU A  97           
SHEET    1   C 2 THR B  49  TYR B  50  0                                        
SHEET    2   C 2 LYS B  60  HIS B  61  1  O  HIS B  61   N  THR B  49           
SHEET    1   D 2 PHE C  94  LYS C  98  0                                        
SHEET    2   D 2 PHE D  94  LYS D  98 -1  O  ARG D  95   N  GLU C  97           
SHEET    1   E 2 THR D  49  TYR D  50  0                                        
SHEET    2   E 2 LYS D  60  HIS D  61  1  O  HIS D  61   N  THR D  49           
SHEET    1   F 2 THR E  49  TYR E  50  0                                        
SHEET    2   F 2 LYS E  60  HIS E  61  1  O  HIS E  61   N  THR E  49           
SHEET    1   G 2 PHE E  94  LYS E  98  0                                        
SHEET    2   G 2 PHE F  94  LYS F  98 -1  O  ARG F  95   N  GLU E  97           
LINK         C   PRO A  12                 N   MSE A  13     1555   1555  1.33  
LINK         C   MSE A  13                 N   ASP A  14     1555   1555  1.33  
LINK         C   ALA A  82                 N   MSE A  83     1555   1555  1.34  
LINK         C   MSE A  83                 N   ASN A  84     1555   1555  1.33  
LINK         C   LYS A  87                 N   MSE A  88     1555   1555  1.32  
LINK         C   MSE A  88                 N   VAL A  89     1555   1555  1.34  
LINK         C   PRO B  12                 N   MSE B  13     1555   1555  1.33  
LINK         C   MSE B  13                 N   ASP B  14     1555   1555  1.33  
LINK         C   ALA B  82                 N   MSE B  83     1555   1555  1.34  
LINK         C   MSE B  83                 N   ASN B  84     1555   1555  1.33  
LINK         C   LYS B  87                 N   MSE B  88     1555   1555  1.32  
LINK         C   MSE B  88                 N   VAL B  89     1555   1555  1.33  
LINK         C   PRO C  12                 N   MSE C  13     1555   1555  1.33  
LINK         C   MSE C  13                 N   ASP C  14     1555   1555  1.32  
LINK         C   ALA C  82                 N   MSE C  83     1555   1555  1.33  
LINK         C   MSE C  83                 N   ASN C  84     1555   1555  1.34  
LINK         C   LYS C  87                 N   MSE C  88     1555   1555  1.33  
LINK         C   MSE C  88                 N   VAL C  89     1555   1555  1.34  
LINK         C   PRO D  12                 N   MSE D  13     1555   1555  1.32  
LINK         C   MSE D  13                 N   ASP D  14     1555   1555  1.33  
LINK         C   ALA D  82                 N   MSE D  83     1555   1555  1.33  
LINK         C   MSE D  83                 N   ASN D  84     1555   1555  1.33  
LINK         C   LYS D  87                 N   MSE D  88     1555   1555  1.33  
LINK         C   MSE D  88                 N   VAL D  89     1555   1555  1.34  
LINK         C   PRO E  12                 N   MSE E  13     1555   1555  1.33  
LINK         C   MSE E  13                 N   ASP E  14     1555   1555  1.32  
LINK         C   ALA E  82                 N   MSE E  83     1555   1555  1.33  
LINK         C   MSE E  83                 N   ASN E  84     1555   1555  1.34  
LINK         C   LYS E  87                 N   MSE E  88     1555   1555  1.33  
LINK         C   MSE E  88                 N   VAL E  89     1555   1555  1.34  
LINK         C   PRO F  12                 N   MSE F  13     1555   1555  1.32  
LINK         C   MSE F  13                 N   ASP F  14     1555   1555  1.33  
LINK         C   ALA F  82                 N   MSE F  83     1555   1555  1.33  
LINK         C   MSE F  83                 N   ASN F  84     1555   1555  1.33  
LINK         C   LYS F  87                 N   MSE F  88     1555   1555  1.34  
LINK         C   MSE F  88                 N   VAL F  89     1555   1555  1.33  
LINK         OD2 ASP A  56                MG    MG A 102     1555   1555  2.57  
LINK         OD2 ASP B  56                MG    MG A 102     1555   1555  2.69  
CISPEP   1 GLU C    3    ASN C    4          0         1.98                     
CISPEP   2 GLU E    3    ASN E    4          0         7.00                     
SITE     1 AC1  7 TRP A  39  ARG A  43  ARG A  54  HIS A  61                    
SITE     2 AC1  7 ARG B  43  ARG B  54  HIS B  61                               
SITE     1 AC2  2 ASP A  56  ASP B  56                                          
SITE     1 AC3  4 PRO A  21  GLU A  22  SER A  23  HOH A 156                    
SITE     1 AC4  3 PRO B  21  GLU B  22  SER B  23                               
SITE     1 AC5  4 PRO C  21  GLU C  22  SER C  23  HOH C 119                    
SITE     1 AC6  3 PRO D  21  GLU D  22  SER D  23                               
SITE     1 AC7  3 PRO E  21  GLU E  22  SER E  23                               
SITE     1 AC8  4 PRO F  21  GLU F  22  SER F  23  HOH F 147                    
CRYST1   74.642   89.272   74.697  90.00 110.99  90.00 P 1 21 1     12          
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      0.013397  0.000000  0.005140        0.00000                         
SCALE2      0.000000  0.011202  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014339        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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