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Database: PDB
Entry: 2MSN
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Original site: 2MSN 
HEADER    HYDROLASE                               04-AUG-14   2MSN              
TITLE     NMR STRUCTURE OF A PUTATIVE PHOSPHOGLYCOLATE PHOSPHATASE (NP_346487.1)
TITLE    2 FROM STREPTOCOCCUS PNEUMONIAE TIGR4                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYDROLASE, HALOACID DEHALOGENASE-LIKE FAMILY;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.3.18;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE TIGR4;                 
SOURCE   3 ORGANISM_TAXID: 170187;                                              
SOURCE   4 STRAIN: TIGR4;                                                       
SOURCE   5 GENE: SP_2064;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET28TEV                                   
KEYWDS    HYDROLASE, PSI-BIOLOGY, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG    
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    K.JAUDZEMS,P.SERRANO,B.PEDRINI,M.GERALT,K.WUTHRICH,JOINT CENTER FOR   
AUTHOR   2 STRUCTURAL GENOMICS (JCSG)                                           
REVDAT   2   22-APR-15 2MSN    1       JRNL   KEYWDS                            
REVDAT   1   24-SEP-14 2MSN    0                                                
JRNL        AUTH   K.JAUDZEMS,B.PEDRINI,M.GERALT,P.SERRANO,K.WUTHRICH           
JRNL        TITL   J-UNIO PROTOCOL USED FOR NMR STRUCTURE DETERMINATION OF THE  
JRNL        TITL 2 206-RESIDUE PROTEIN NP_346487.1 FROM STREPTOCOCCUS           
JRNL        TITL 3 PNEUMONIAE TIGR4.                                            
JRNL        REF    J.BIOMOL.NMR                  V.  61    65 2015              
JRNL        REFN                   ISSN 0925-2738                               
JRNL        PMID   25428766                                                     
JRNL        DOI    10.1007/S10858-014-9886-3                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CYANA 3.0, OPAL                                      
REMARK   3   AUTHORS     : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA),           
REMARK   3                 LUGINBUHL, GUNTERT, BILLETER AND WUTHRICH (OPAL)     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2MSN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB104000.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 6.5                                
REMARK 210  IONIC STRENGTH                 : 0.08                               
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1.5 MM [U-100% 13C; U-100% 15N]    
REMARK 210                                   PROTEIN, 5 % [U-100% 2H] D2O,      
REMARK 210                                   0.03 % SODIUM AZIDE, 20 MM SODIUM  
REMARK 210                                   PHOSPHATE, 50 MM SODIUM CHLORIDE,  
REMARK 210                                   95% H2O/5% D2O                     
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 5D APSY-HACACONH; 4D APSY-         
REMARK 210                                   HACANH; 4D APSY-HNCOCA; 4D APSY-   
REMARK 210                                   HNCACO; 5D APSY-CBCACONH; 3D 1H-   
REMARK 210                                   15N NOESY; 3D 1H-13C NOESY         
REMARK 210                                   ALIPHATIC; 3D 1H-13C NOESY         
REMARK 210                                   AROMATIC                           
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ; 800 MHZ                   
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CYANA 3.0, TOPSPIN 2.1, CARA       
REMARK 210                                   1.9, UNIO-MATCH, UNIO-ATNOS/       
REMARK 210                                   ASCAN, UNIO-ATNOS/CANDID           
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS,            
REMARK 210                                   SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : TARGET FUNCTION                    
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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  1 ARG A  61   N   -  CA  -  CB  ANGL. DEV. = -12.4 DEGREES          
REMARK 500  1 LEU A  68   CB  -  CG  -  CD1 ANGL. DEV. =  14.8 DEGREES          
REMARK 500  1 LEU A  76   CB  -  CA  -  C   ANGL. DEV. =  15.8 DEGREES          
REMARK 500  1 VAL A 122   CA  -  CB  -  CG2 ANGL. DEV. =  15.0 DEGREES          
REMARK 500  2 ARG A  61   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500  2 VAL A 122   CA  -  CB  -  CG2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500  4 ARG A 201   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500  5 ARG A 192   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500  6 ARG A 192   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500  7 ARG A 192   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500  8 ARG A  61   N   -  CA  -  CB  ANGL. DEV. = -11.7 DEGREES          
REMARK 500  8 ARG A 138   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500  9 LEU A  93   CB  -  CG  -  CD1 ANGL. DEV. =  15.1 DEGREES          
REMARK 500  9 VAL A 122   CA  -  CB  -  CG2 ANGL. DEV. =  10.4 DEGREES          
REMARK 500 10 ASP A  60   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500 10 LEU A  93   CB  -  CG  -  CD1 ANGL. DEV. =  10.2 DEGREES          
REMARK 500 12 LEU A  93   CB  -  CG  -  CD1 ANGL. DEV. =  10.5 DEGREES          
REMARK 500 13 LEU A  68   CB  -  CG  -  CD1 ANGL. DEV. =  12.2 DEGREES          
REMARK 500 13 ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500 14 LEU A  93   CB  -  CG  -  CD1 ANGL. DEV. =  10.3 DEGREES          
REMARK 500 15 LEU A  68   CB  -  CG  -  CD1 ANGL. DEV. =  11.0 DEGREES          
REMARK 500 16 VAL A  65   CG1 -  CB  -  CG2 ANGL. DEV. =  16.0 DEGREES          
REMARK 500 17 ARG A  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500 17 LEU A  93   CB  -  CG  -  CD1 ANGL. DEV. =  11.0 DEGREES          
REMARK 500 17 VAL A 122   CG1 -  CB  -  CG2 ANGL. DEV. = -11.7 DEGREES          
REMARK 500 18 ASP A   9   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500 18 LEU A  93   CB  -  CG  -  CD1 ANGL. DEV. =  14.4 DEGREES          
REMARK 500 18 TYR A 125   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500 20 ARG A  42   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 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  1 HIS A  -1      -85.23     59.70                                   
REMARK 500  1 MET A   1       86.37     47.88                                   
REMARK 500  1 GLN A   2      175.72    -56.34                                   
REMARK 500  1 LYS A   3      105.87    -49.78                                   
REMARK 500  1 ASP A  11      -75.37    -87.07                                   
REMARK 500  1 LEU A  63     -162.10   -105.13                                   
REMARK 500  1 ASN A  80       39.69    -84.35                                   
REMARK 500  1 LEU A  85       42.26    -99.36                                   
REMARK 500  1 MET A  86       78.90     43.25                                   
REMARK 500  1 PRO A  87       95.25    -64.53                                   
REMARK 500  1 GLU A  91      -70.12    -52.13                                   
REMARK 500  1 VAL A 122       24.49   -140.09                                   
REMARK 500  1 ARG A 138      -85.63    -73.09                                   
REMARK 500  1 LEU A 167        3.14    -67.83                                   
REMARK 500  1 GLU A 170      -73.05    -57.83                                   
REMARK 500  1 THR A 186       48.58    -86.05                                   
REMARK 500  1 ALA A 195     -153.99   -127.74                                   
REMARK 500  1 THR A 205       63.02     65.33                                   
REMARK 500  2 GLN A   2     -178.25    -60.44                                   
REMARK 500  2 LYS A   3       97.76    -48.68                                   
REMARK 500  2 THR A  13      -34.13   -131.30                                   
REMARK 500  2 ASP A  16       45.41   -100.21                                   
REMARK 500  2 GLN A  74       41.35    -80.50                                   
REMARK 500  2 ALA A  81     -164.21   -124.34                                   
REMARK 500  2 MET A  86       83.73     45.08                                   
REMARK 500  2 VAL A 122       54.01   -150.17                                   
REMARK 500  2 ASP A 164       31.28   -148.35                                   
REMARK 500  2 THR A 205       28.24   -145.58                                   
REMARK 500  3 HIS A  -1       65.87     61.38                                   
REMARK 500  3 GLN A   2     -174.52    -62.99                                   
REMARK 500  3 LYS A   3       88.29    -51.79                                   
REMARK 500  3 LEU A  10        7.87     55.43                                   
REMARK 500  3 GLU A  39      -72.26    -66.97                                   
REMARK 500  3 ARG A  61     -163.89   -105.93                                   
REMARK 500  3 MET A  86       74.08     42.20                                   
REMARK 500  3 VAL A 122       42.63   -165.59                                   
REMARK 500  3 LEU A 149      -71.48    -68.34                                   
REMARK 500  3 GLN A 194       -2.96   -147.99                                   
REMARK 500  3 ALA A 195     -155.56   -148.86                                   
REMARK 500  3 THR A 205       30.68   -159.59                                   
REMARK 500  4 MET A   1       47.67    -79.33                                   
REMARK 500  4 TRP A   8     -167.41   -124.10                                   
REMARK 500  4 LEU A  14      -22.34   -144.25                                   
REMARK 500  4 ASP A  16       58.32   -103.03                                   
REMARK 500  4 ARG A  61     -164.34   -114.58                                   
REMARK 500  4 GLN A  74       78.34   -115.28                                   
REMARK 500  4 MET A  86       85.84     58.78                                   
REMARK 500  4 ARG A 138       34.73    -99.84                                   
REMARK 500  4 LYS A 139      145.98     63.58                                   
REMARK 500  4 ASP A 164       20.70   -146.18                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     203 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A   -2     HIS A   -1          8      -147.89                    
REMARK 500 ASP A   60     ARG A   61          8      -146.57                    
REMARK 500 LYS A  139     PRO A  140         17       -31.77                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500  1 TYR A  48         0.07    SIDE CHAIN                              
REMARK 500  1 TYR A 147         0.09    SIDE CHAIN                              
REMARK 500  1 ARG A 165         0.12    SIDE CHAIN                              
REMARK 500  2 TYR A 125         0.08    SIDE CHAIN                              
REMARK 500  3 ARG A  56         0.10    SIDE CHAIN                              
REMARK 500  3 ARG A  90         0.08    SIDE CHAIN                              
REMARK 500  3 TYR A 125         0.11    SIDE CHAIN                              
REMARK 500  3 ARG A 201         0.10    SIDE CHAIN                              
REMARK 500  4 TYR A  18         0.10    SIDE CHAIN                              
REMARK 500  5 TYR A 106         0.06    SIDE CHAIN                              
REMARK 500  6 ARG A  72         0.09    SIDE CHAIN                              
REMARK 500  8 TYR A  18         0.07    SIDE CHAIN                              
REMARK 500  8 TYR A  36         0.07    SIDE CHAIN                              
REMARK 500  8 ARG A  42         0.09    SIDE CHAIN                              
REMARK 500  8 ARG A  72         0.11    SIDE CHAIN                              
REMARK 500  8 TYR A 125         0.11    SIDE CHAIN                              
REMARK 500  8 TYR A 187         0.07    SIDE CHAIN                              
REMARK 500  9 ARG A  56         0.08    SIDE CHAIN                              
REMARK 500  9 ARG A  61         0.08    SIDE CHAIN                              
REMARK 500  9 ARG A  90         0.10    SIDE CHAIN                              
REMARK 500 10 ARG A 165         0.14    SIDE CHAIN                              
REMARK 500 10 TYR A 187         0.08    SIDE CHAIN                              
REMARK 500 11 ARG A  56         0.08    SIDE CHAIN                              
REMARK 500 11 TYR A 161         0.07    SIDE CHAIN                              
REMARK 500 12 TYR A  36         0.07    SIDE CHAIN                              
REMARK 500 12 ARG A  56         0.08    SIDE CHAIN                              
REMARK 500 13 ARG A  72         0.09    SIDE CHAIN                              
REMARK 500 13 TYR A 125         0.07    SIDE CHAIN                              
REMARK 500 14 ARG A  42         0.08    SIDE CHAIN                              
REMARK 500 14 TYR A 187         0.07    SIDE CHAIN                              
REMARK 500 15 ARG A  42         0.09    SIDE CHAIN                              
REMARK 500 15 ARG A  61         0.12    SIDE CHAIN                              
REMARK 500 15 ARG A  90         0.09    SIDE CHAIN                              
REMARK 500 15 TYR A 161         0.07    SIDE CHAIN                              
REMARK 500 16 TYR A  18         0.07    SIDE CHAIN                              
REMARK 500 16 TYR A  36         0.07    SIDE CHAIN                              
REMARK 500 17 TYR A  18         0.07    SIDE CHAIN                              
REMARK 500 17 ARG A  56         0.08    SIDE CHAIN                              
REMARK 500 17 TYR A 161         0.06    SIDE CHAIN                              
REMARK 500 17 ARG A 165         0.08    SIDE CHAIN                              
REMARK 500 18 TYR A 125         0.14    SIDE CHAIN                              
REMARK 500 18 ARG A 138         0.08    SIDE CHAIN                              
REMARK 500 18 TYR A 147         0.10    SIDE CHAIN                              
REMARK 500 20 TYR A  36         0.07    SIDE CHAIN                              
REMARK 500 20 ARG A  56         0.09    SIDE CHAIN                              
REMARK 500 20 ARG A  90         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500  1 LEU A  76        24.4      L          L   OUTSIDE RANGE           
REMARK 500 15 LYS A 109        19.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 25127   RELATED DB: BMRB                                 
REMARK 900 RELATED ID: JCSG-359637   RELATED DB: TARGETTRACK                    
DBREF  2MSN A    1   206  UNP    Q97NG6   Q97NG6_STRPN     1    206             
SEQADV 2MSN GLY A   -2  UNP  Q97NG6              EXPRESSION TAG                 
SEQADV 2MSN HIS A   -1  UNP  Q97NG6              EXPRESSION TAG                 
SEQRES   1 A  208  GLY HIS MET GLN LYS THR ALA PHE ILE TRP ASP LEU ASP          
SEQRES   2 A  208  GLY THR LEU LEU ASP SER TYR GLU ALA ILE LEU SER GLY          
SEQRES   3 A  208  ILE GLU GLU THR PHE ALA GLN PHE SER ILE PRO TYR ASP          
SEQRES   4 A  208  LYS GLU LYS VAL ARG GLU PHE ILE PHE LYS TYR SER VAL          
SEQRES   5 A  208  GLN ASP LEU LEU VAL ARG VAL ALA GLU ASP ARG ASN LEU          
SEQRES   6 A  208  ASP VAL GLU VAL LEU ASN GLN VAL ARG ALA GLN SER LEU          
SEQRES   7 A  208  ALA GLU LYS ASN ALA GLN VAL VAL LEU MET PRO GLY ALA          
SEQRES   8 A  208  ARG GLU VAL LEU ALA TRP ALA ASP GLU SER GLY ILE GLN          
SEQRES   9 A  208  GLN PHE ILE TYR THR HIS LYS GLY ASN ASN ALA PHE THR          
SEQRES  10 A  208  ILE LEU LYS ASP LEU GLY VAL GLU SER TYR PHE THR GLU          
SEQRES  11 A  208  ILE LEU THR SER GLN SER GLY PHE VAL ARG LYS PRO SER          
SEQRES  12 A  208  PRO GLU ALA ALA THR TYR LEU LEU ASP LYS TYR GLN LEU          
SEQRES  13 A  208  ASN SER ASP ASN THR TYR TYR ILE GLY ASP ARG THR LEU          
SEQRES  14 A  208  ASP VAL GLU PHE ALA GLN ASN SER GLY ILE GLN SER ILE          
SEQRES  15 A  208  ASN PHE LEU GLU SER THR TYR GLU GLY ASN HIS ARG ILE          
SEQRES  16 A  208  GLN ALA LEU ALA ASP ILE SER ARG ILE PHE GLU THR LYS          
HELIX    1   1 SER A   17  PHE A   32  1                                  16    
HELIX    2   2 ASP A   37  TYR A   48  1                                  12    
HELIX    3   3 SER A   49  ASN A   62  1                                  14    
HELIX    4   4 ASP A   64  ARG A   72  1                                   9    
HELIX    5   5 ALA A   89  SER A   99  1                                  11    
HELIX    6   6 ASN A  111  GLY A  121  1                                  11    
HELIX    7   7 THR A  131  GLY A  135  5                                   5    
HELIX    8   8 PRO A  142  TYR A  152  1                                  11    
HELIX    9   9 THR A  166  GLY A  176  1                                  11    
HELIX   10  10 LEU A  196  PHE A  203  1                                   8    
SHEET    1   A 6 GLU A 128  ILE A 129  0                                        
SHEET    2   A 6 GLN A 102  ILE A 105  1  N  ILE A 105   O  GLU A 128           
SHEET    3   A 6 ALA A   5  TRP A   8  1  N  PHE A   6   O  GLN A 102           
SHEET    4   A 6 THR A 159  ILE A 162  1  O  ILE A 162   N  ILE A   7           
SHEET    5   A 6 GLN A 178  ASN A 181  1  O  GLN A 178   N  THR A 159           
SHEET    6   A 6 ASN A 190  ARG A 192  1  O  HIS A 191   N  SER A 179           
CISPEP   1 LYS A  139    PRO A  140          1       -13.95                     
CISPEP   2 LYS A  139    PRO A  140          2        -4.07                     
CISPEP   3 LYS A  139    PRO A  140          3        -6.43                     
CISPEP   4 LYS A  139    PRO A  140          4       -16.81                     
CISPEP   5 LYS A  139    PRO A  140          5       -22.13                     
CISPEP   6 LYS A  139    PRO A  140          6        -3.76                     
CISPEP   7 LYS A  139    PRO A  140          7        -2.39                     
CISPEP   8 LYS A  139    PRO A  140          8         3.97                     
CISPEP   9 LYS A  139    PRO A  140          9       -28.87                     
CISPEP  10 LYS A  139    PRO A  140         10        23.21                     
CISPEP  11 LYS A  139    PRO A  140         11       -11.20                     
CISPEP  12 LYS A  139    PRO A  140         12       -29.71                     
CISPEP  13 LYS A  139    PRO A  140         13       -27.36                     
CISPEP  14 LYS A  139    PRO A  140         14       -11.96                     
CISPEP  15 LYS A  139    PRO A  140         15        15.04                     
CISPEP  16 LYS A  139    PRO A  140         16        -4.28                     
CISPEP  17 LYS A  139    PRO A  140         18         1.29                     
CISPEP  18 LYS A  139    PRO A  140         19         3.12                     
CISPEP  19 LYS A  139    PRO A  140         20        -9.76                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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