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Database: PDB
Entry: 2MSX
LinkDB: 2MSX
Original site: 2MSX 
HEADER    HYDROLASE INHIBITOR                     09-AUG-14   2MSX              
TITLE     THE SOLUTION STRUCTURE OF THE MANEC-TYPE DOMAIN FROM HEPATOCYTE GROWTH
TITLE    2 FACTOR INHIBITOR 1 REVEALS AN UNEXPECTED PAN/APPLE DOMAIN-TYPE FOLD  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KUNITZ-TYPE PROTEASE INHIBITOR 1;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 47-152;                                       
COMPND   5 SYNONYM: HEPATOCYTE GROWTH FACTOR ACTIVATOR INHIBITOR TYPE 1, HAI-1; 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SPINT1, HAI1, UNQ223/PRO256;                                   
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PPICZ A                                    
KEYWDS    MANEC, HYDROLASE INHIBITOR                                            
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    Z.HONG,M.E.NOWAKOWSKI,C.SPRONK,S.V.PETERSEN,J.S.PETERSEN,W.KOZMINSKI, 
AUTHOR   2 F.MULDER,J.K.JENSEN                                                  
REVDAT   2   04-MAR-15 2MSX    1       JRNL                                     
REVDAT   1   31-DEC-14 2MSX    0                                                
JRNL        AUTH   Z.HONG,M.NOWAKOWSKI,C.SPRONK,S.V.PETERSEN,P.A.ANDREASEN,     
JRNL        AUTH 2 W.KOZMINSKI,F.A.MULDER,J.K.JENSEN                            
JRNL        TITL   THE SOLUTION STRUCTURE OF THE MANEC-TYPE DOMAIN FROM         
JRNL        TITL 2 HEPATOCYTE GROWTH FACTOR ACTIVATOR INHIBITOR-1 REVEALS AN    
JRNL        TITL 3 UNEXPECTED PAN/APPLE DOMAIN-TYPE FOLD.                       
JRNL        REF    BIOCHEM.J.                    V. 466   299 2015              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   25510835                                                     
JRNL        DOI    10.1042/BJ20141236                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : YASARA2                                              
REMARK   3   AUTHORS     : YASARA2-KRIEGER                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2MSX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-AUG-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB104007.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 310; 298                           
REMARK 210  PH                             : 6.5; 6.5                           
REMARK 210  IONIC STRENGTH                 : 100; 100                           
REMARK 210  PRESSURE                       : AMBIENT; AMBIENT                   
REMARK 210  SAMPLE CONTENTS                : 1 MM [U-99% 13C; U-99% 15N]        
REMARK 210                                   PROTEIN_1, 93% H2O/7% D2O          
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 2D 1H-13C HSQC;    
REMARK 210                                   3D CBCA(CO)NH; 3D HNCACB; 3D       
REMARK 210                                   HNCO; 4D HABCAB(CO)NH; 4D HCCH-    
REMARK 210                                   TOCSY; 2D (HB)CB(CGCD)HD; 2D (HB)  
REMARK 210                                   CB(CGCDCE)HE; 3D HBCB(CGCD)HD; 3D  
REMARK 210                                   HBCB(CGCDCE)HE; 3D 13C-EDITED      
REMARK 210                                   NOESY HSQC; 4D 13CALI,13CARO-      
REMARK 210                                   EDITED HMQC-NOESY-HSQC; 4D         
REMARK 210                                   13CALI,13CALI-EDITED HMQC-NOESY-   
REMARK 210                                   HMQC; 4D 15N,13C EDITED HMQC-      
REMARK 210                                   NOESY-HSQC; 3D 1H-15N NOESY        
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 MHZ; 600 MHZ; 800 MHZ          
REMARK 210  SPECTROMETER MODEL             : PLUS; DDR2                         
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER; AGILENT                    
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CYANA, SPARKY, NMRPIPE, SSA_       
REMARK 210                                   SOFTWARE_PACKAGE                   
REMARK 210   METHOD USED                   : DGSA-DISTANCE GEOMETRY SIMULATED   
REMARK 210                                   ANNEALING                          
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 80                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : ALL CALCULATED STRUCTURES          
REMARK 210                                   SUBMITTED                          
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 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  4 ARG A 134   CZ    ARG A 134   NH2    -0.078                       
REMARK 500  7 ARG A 150   CZ    ARG A 150   NH2    -0.081                       
REMARK 500  9 ARG A 150   CZ    ARG A 150   NH2    -0.087                       
REMARK 500 10 ARG A 150   CZ    ARG A 150   NH2    -0.080                       
REMARK 500 11 ARG A 150   CZ    ARG A 150   NH2    -0.083                       
REMARK 500 13 ARG A  83   CZ    ARG A  83   NH2    -0.082                       
REMARK 500 13 ARG A 108   CZ    ARG A 108   NH2    -0.090                       
REMARK 500 14 ARG A 150   CZ    ARG A 150   NH2    -0.085                       
REMARK 500 16 ARG A 108   CZ    ARG A 108   NH2    -0.091                       
REMARK 500 16 ARG A 147   CZ    ARG A 147   NH2    -0.081                       
REMARK 500 16 ARG A 150   CZ    ARG A 150   NH2    -0.094                       
REMARK 500 19 ARG A 150   CZ    ARG A 150   NH2    -0.081                       
REMARK 500 20 ARG A 108   CZ    ARG A 108   NH2    -0.082                       
REMARK 500 20 ARG A 150   CZ    ARG A 150   NH2    -0.080                       
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  1 ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500  1 ARG A  83   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  1 ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500  1 ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500  1 ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500  1 ARG A 143   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500  1 ARG A 147   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500  1 ARG A 150   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500  2 ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  2 ARG A  83   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500  2 ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500  2 ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500  2 ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  2 ARG A 143   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500  2 ARG A 147   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500  2 ARG A 150   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500  3 ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  3 ARG A  83   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500  3 ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500  3 ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500  3 ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500  3 ARG A 143   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  3 ARG A 147   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500  3 ARG A 150   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500  4 ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500  4 ARG A  83   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500  4 ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500  4 ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500  4 ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500  4 ARG A 143   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  4 ARG A 147   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500  4 ARG A 150   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500  5 ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500  5 ARG A  83   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500  5 ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500  5 ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500  5 ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500  5 ARG A 143   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500  5 ARG A 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500  5 ARG A 147   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500  5 ARG A 150   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  6 ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500  6 ARG A  83   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500  6 ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500  6 ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500  6 ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500  6 ARG A 143   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500  6 ARG A 147   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500  6 ARG A 150   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500  7 ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     163 ANGLE DEVIATIONS.                             
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 THR A  65      -60.47     56.35                                   
REMARK 500  1 ASP A 107      -43.59   -150.14                                   
REMARK 500  1 CYS A 121       13.80     57.20                                   
REMARK 500  2 LEU A  51      -36.54     64.52                                   
REMARK 500  2 THR A  65      -58.35     56.85                                   
REMARK 500  2 ASP A 107      -41.60   -167.56                                   
REMARK 500  2 CYS A 121       10.89     59.94                                   
REMARK 500  3 THR A  65      -61.91     54.15                                   
REMARK 500  3 ASP A 107      -32.41   -168.30                                   
REMARK 500  3 CYS A 121       12.46     52.61                                   
REMARK 500  4 ALA A  48       38.31    -80.87                                   
REMARK 500  4 ASN A  52       30.06    -89.12                                   
REMARK 500  4 THR A  65      -69.89     45.47                                   
REMARK 500  4 ASP A 107      -32.79   -152.64                                   
REMARK 500  4 CYS A 121       15.79     52.93                                   
REMARK 500  4 HIS A 157       40.96    -73.89                                   
REMARK 500  5 ALA A  48       49.65    -78.23                                   
REMARK 500  5 LEU A  51      -33.05     69.32                                   
REMARK 500  5 ASP A 107      -43.00   -166.11                                   
REMARK 500  5 CYS A 121       -0.18     63.62                                   
REMARK 500  6 ALA A  48       40.90    -80.44                                   
REMARK 500  6 LEU A  51      -39.12     68.07                                   
REMARK 500  6 THR A  65      -67.44     55.39                                   
REMARK 500  6 THR A  80       30.50    -91.45                                   
REMARK 500  6 ASP A 107      -34.26   -172.06                                   
REMARK 500  6 CYS A 121       21.49     42.46                                   
REMARK 500  6 PHE A 137      152.26    -39.91                                   
REMARK 500  7 ASP A  49       49.29    -70.92                                   
REMARK 500  7 LEU A  51      -39.70     65.97                                   
REMARK 500  7 VAL A  58      148.77     51.93                                   
REMARK 500  7 ASP A 107      -36.85   -172.33                                   
REMARK 500  7 CYS A 121        9.29     58.76                                   
REMARK 500  8 ALA A  48       19.34     59.42                                   
REMARK 500  8 LEU A  51      -31.53     66.80                                   
REMARK 500  8 ASP A 107      -49.56   -170.35                                   
REMARK 500  8 CYS A 121       10.46     58.08                                   
REMARK 500  9 ASP A 107      -30.49   -152.60                                   
REMARK 500  9 CYS A 121       12.40     57.45                                   
REMARK 500 10 ASP A  49     -169.76   -117.32                                   
REMARK 500 10 THR A  65      -61.39     56.40                                   
REMARK 500 10 ASP A 107      -40.55   -159.26                                   
REMARK 500 10 CYS A 121       13.92     54.32                                   
REMARK 500 11 ASN A  52      -55.57   -136.05                                   
REMARK 500 11 SER A  53       35.62   -154.36                                   
REMARK 500 11 THR A  65      -68.31     54.83                                   
REMARK 500 11 ASP A 107      -43.79   -163.09                                   
REMARK 500 12 ALA A  56        4.72    -60.26                                   
REMARK 500 12 VAL A  58      136.26     52.02                                   
REMARK 500 12 THR A  65      -57.01     56.84                                   
REMARK 500 12 ASP A 107      -38.98   -158.48                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      84 RAMACHANDRAN OUTLIERS.                        
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 12 VAL A  58        25.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 25139   RELATED DB: BMRB                                 
DBREF  2MSX A   47   152  UNP    O43278   SPIT1_HUMAN     47    152             
SEQADV 2MSX GLN A   66  UNP  O43278    ASN    66 CONFLICT                       
SEQADV 2MSX VAL A  153  UNP  O43278              EXPRESSION TAG                 
SEQADV 2MSX ASP A  154  UNP  O43278              EXPRESSION TAG                 
SEQADV 2MSX HIS A  155  UNP  O43278              EXPRESSION TAG                 
SEQADV 2MSX HIS A  156  UNP  O43278              EXPRESSION TAG                 
SEQADV 2MSX HIS A  157  UNP  O43278              EXPRESSION TAG                 
SEQADV 2MSX HIS A  158  UNP  O43278              EXPRESSION TAG                 
SEQADV 2MSX HIS A  159  UNP  O43278              EXPRESSION TAG                 
SEQADV 2MSX HIS A  160  UNP  O43278              EXPRESSION TAG                 
SEQRES   1 A  114  GLY ALA ASP CYS LEU ASN SER PHE THR ALA GLY VAL PRO          
SEQRES   2 A  114  GLY PHE VAL LEU ASP THR GLN ALA SER VAL SER ASN GLY          
SEQRES   3 A  114  ALA THR PHE LEU GLU SER PRO THR VAL ARG ARG GLY TRP          
SEQRES   4 A  114  ASP CYS VAL ARG ALA CYS CYS THR THR GLN ASN CYS ASN          
SEQRES   5 A  114  LEU ALA LEU VAL GLU LEU GLN PRO ASP ARG GLY GLU ASP          
SEQRES   6 A  114  ALA ILE ALA ALA CYS PHE LEU ILE ASN CYS LEU TYR GLU          
SEQRES   7 A  114  GLN ASN PHE VAL CYS LYS PHE ALA PRO ARG GLU GLY PHE          
SEQRES   8 A  114  ILE ASN TYR LEU THR ARG GLU VAL TYR ARG SER TYR ARG          
SEQRES   9 A  114  GLN LEU VAL ASP HIS HIS HIS HIS HIS HIS                      
HELIX    1   1 ASP A   49  ASN A   52  5                                   4    
HELIX    2   2 THR A   65  SER A   70  1                                   6    
HELIX    3   3 ARG A   83  THR A   94  1                                  12    
HELIX    4   4 VAL A  145  ARG A  150  1                                   6    
SHEET    1   A 5 PHE A  54  ALA A  56  0                                        
SHEET    2   A 5 PHE A 137  THR A 142 -1  O  LEU A 141   N  THR A  55           
SHEET    3   A 5 LEU A  99  LEU A 104 -1  N  VAL A 102   O  ILE A 138           
SHEET    4   A 5 ILE A 113  ILE A 119 -1  O  PHE A 117   N  LEU A 101           
SHEET    5   A 5 PHE A  75  GLU A  77 -1  N  GLU A  77   O  LEU A 118           
SHEET    1   B 2 PHE A  61  LEU A  63  0                                        
SHEET    2   B 2 PHE A 131  PRO A 133 -1  O  ALA A 132   N  VAL A  62           
SHEET    1   C 2 LEU A 122  TYR A 123  0                                        
SHEET    2   C 2 ASN A 126  PHE A 127 -1  O  ASN A 126   N  TYR A 123           
SSBOND   1 CYS A   50    CYS A   92                          1555   1555  2.02  
SSBOND   2 CYS A   87    CYS A  116                          1555   1555  2.02  
SSBOND   3 CYS A   91    CYS A   97                          1555   1555  2.03  
SSBOND   4 CYS A  121    CYS A  129                          1555   1555  2.03  
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                                                                             
DBGET integrated database retrieval system