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Database: PDB
Entry: 2M1K
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Original site: 2M1K 
HEADER    PROTEIN BINDING                         29-NOV-12   2M1K              
TITLE     INTERACTION OF HUMAN S100A6 (C3S) WITH V DOMAIN OF RECEPTOR FOR       
TITLE    2 ADVANCED GLYCATION END PRODUCTS (RAGE)                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN S100-A6;                                           
COMPND   3 CHAIN: B, D;                                                         
COMPND   4 SYNONYM: CALCYCLIN, GROWTH FACTOR-INDUCIBLE PROTEIN 2A9, MLN 4,      
COMPND   5 PROLACTIN RECEPTOR-ASSOCIATED PROTEIN, PRA, S100 CALCIUM-BINDING     
COMPND   6 PROTEIN A6;                                                          
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ADVANCED GLYCOSYLATION END PRODUCT-SPECIFIC RECEPTOR;      
COMPND  11 CHAIN: A, C;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 23-121;                                       
COMPND  13 SYNONYM: RECEPTOR FOR ADVANCED GLYCOSYLATION END PRODUCTS;           
COMPND  14 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: CACY, S100A6;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET(20B)+;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: AGER, RAGE;                                                    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET(15B)+                                 
KEYWDS    S100A6 C3S, RAGE V, HETEROTETRAMERIC, HADDOCK MODEL, PROTEIN BINDING  
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    A.A.GUPTA,C.YU                                                        
REVDAT   1   25-MAR-15 2M1K    0                                                
JRNL        AUTH   S.K.MOHAN,A.A.GUPTA,C.YU                                     
JRNL        TITL   INTERACTION OF THE S100A6 MUTANT (C3S) WITH THE V DOMAIN OF  
JRNL        TITL 2 THE RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS (RAGE).     
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 434   328 2013              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   23537648                                                     
JRNL        DOI    10.1016/J.BBRC.2013.03.049                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : HADDOCK                                              
REMARK   3   AUTHORS     : ALEXANDRE BONVIN                                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HADDOCK STARTING STRUCTURES ARE PDB       
REMARK   3  ENTRIES 1K9K AND 2E5E. MODELS 1-10 ARE SUPERIMPOSED, WHILE MODELS   
REMARK   3  11-20 ARE SUPERIMPOSED IN A DIFFERENT ORIENTATION.                  
REMARK   4                                                                      
REMARK   4 2M1K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB103092.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : 0                                  
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1.0 MM [U-100% 13C; U-100% 15N]    
REMARK 210                                   S100A6 C3S, 20 MM TRIS, 10 MM      
REMARK 210                                   CALCIUM CHLORIDE, 0.01 % SODIUM    
REMARK 210                                   AZIDE, 90% H2O/10% D2O             
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 3D HNCA; 3D        
REMARK 210                                   HN(CO)CA; 3D HNCACB; 3D CBCA(CO)   
REMARK 210                                   NH; 3D HNCO; 3D HCACO              
REMARK 210  SPECTROMETER FIELD STRENGTH    : 700 MHZ                            
REMARK 210  SPECTROMETER MODEL             : INOVA                              
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : VNMRJ 2.3, SPARKY, HADDOCK         
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 200                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST ENERGY  
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, A, C                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-20                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     MET B     1                                                      
REMARK 465     MET D     1                                                      
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 LYS D  64       70.92     59.62                                   
REMARK 500  1 LYS A  39     -176.16    -65.39                                   
REMARK 500  1 PRO A  42     -173.56    -61.38                                   
REMARK 500  1 PRO A  46      105.67    -55.35                                   
REMARK 500  1 THR A  58      104.85     62.10                                   
REMARK 500  1 GLU A  59       16.70   -140.91                                   
REMARK 500  1 ALA A  88      105.45   -167.55                                   
REMARK 500  1 GLU A  94      178.17    -50.86                                   
REMARK 500  1 ASN A 103     -161.19   -100.81                                   
REMARK 500  1 ASN A 105      -76.38   -107.44                                   
REMARK 500  1 TYR A 118      -78.05    -52.94                                   
REMARK 500  1 LYS C  39     -176.19    -65.20                                   
REMARK 500  1 PRO C  42     -174.84    -61.62                                   
REMARK 500  1 PRO C  46      105.51    -55.33                                   
REMARK 500  1 THR C  58      104.87     62.07                                   
REMARK 500  1 GLU C  59       16.61   -140.97                                   
REMARK 500  1 ALA C  88      105.58   -167.48                                   
REMARK 500  1 GLU C  94      178.06    -50.83                                   
REMARK 500  1 ASN C 103     -161.90   -101.51                                   
REMARK 500  1 ASN C 105      -73.22   -102.09                                   
REMARK 500  1 TYR C 118      -77.95    -52.96                                   
REMARK 500  2 LYS B  64       73.91     61.52                                   
REMARK 500  2 LYS D  64       80.41     60.15                                   
REMARK 500  2 LYS A  39     -176.18    -65.28                                   
REMARK 500  2 PRO A  42     -172.20    -62.94                                   
REMARK 500  2 PRO A  46      105.71    -55.34                                   
REMARK 500  2 THR A  58      104.91     62.13                                   
REMARK 500  2 GLU A  59       16.65   -141.00                                   
REMARK 500  2 ALA A  88      105.51   -167.49                                   
REMARK 500  2 GLU A  94      178.13    -50.90                                   
REMARK 500  2 TYR A 118      -77.97    -53.03                                   
REMARK 500  2 LYS C  39     -176.09    -65.39                                   
REMARK 500  2 PRO C  42     -172.04    -62.85                                   
REMARK 500  2 PRO C  46      105.51    -55.16                                   
REMARK 500  2 THR C  58      104.84     62.05                                   
REMARK 500  2 GLU C  59       16.74   -140.96                                   
REMARK 500  2 ALA C  88      105.54   -167.53                                   
REMARK 500  2 GLU C  94      178.18    -51.04                                   
REMARK 500  2 TYR C 118      -78.00    -53.00                                   
REMARK 500  3 LYS B  64       73.85     65.50                                   
REMARK 500  3 LYS D  64       77.91     60.80                                   
REMARK 500  3 PRO A  42     -173.81    -61.61                                   
REMARK 500  3 PRO A  46      105.65    -55.39                                   
REMARK 500  3 THR A  58      104.84     62.21                                   
REMARK 500  3 GLU A  59       16.61   -140.94                                   
REMARK 500  3 ALA A  88      105.49   -167.49                                   
REMARK 500  3 GLU A  94      178.13    -50.80                                   
REMARK 500  3 TYR A 118      -78.07    -52.96                                   
REMARK 500  3 LYS C  39     -176.10    -65.29                                   
REMARK 500  3 PRO C  42     -173.02    -60.99                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     311 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 18868   RELATED DB: BMRB                                 
REMARK 900 RELATED ID: 1K9K   RELATED DB: PDB                                   
REMARK 900 HADDOCK STARTING STRUCTURE                                           
REMARK 900 RELATED ID: 2E5E   RELATED DB: PDB                                   
REMARK 900 HADDOCK STARTING STRUCTURE                                           
DBREF  2M1K B    1    90  UNP    P06703   S10A6_HUMAN      1     90             
DBREF  2M1K D    1    90  UNP    P06703   S10A6_HUMAN      1     90             
DBREF  2M1K A   23   121  UNP    Q15109   RAGE_HUMAN      23    121             
DBREF  2M1K C   23   121  UNP    Q15109   RAGE_HUMAN      23    121             
SEQADV 2M1K SER B    3  UNP  P06703    CYS     3 ENGINEERED MUTATION            
SEQADV 2M1K SER D    3  UNP  P06703    CYS     3 ENGINEERED MUTATION            
SEQADV 2M1K ALA A   21  UNP  Q15109              EXPRESSION TAG                 
SEQADV 2M1K MET A   22  UNP  Q15109              EXPRESSION TAG                 
SEQADV 2M1K ALA C   21  UNP  Q15109              EXPRESSION TAG                 
SEQADV 2M1K MET C   22  UNP  Q15109              EXPRESSION TAG                 
SEQRES   1 B   90  MET ALA SER PRO LEU ASP GLN ALA ILE GLY LEU LEU VAL          
SEQRES   2 B   90  ALA ILE PHE HIS LYS TYR SER GLY ARG GLU GLY ASP LYS          
SEQRES   3 B   90  HIS THR LEU SER LYS LYS GLU LEU LYS GLU LEU ILE GLN          
SEQRES   4 B   90  LYS GLU LEU THR ILE GLY SER LYS LEU GLN ASP ALA GLU          
SEQRES   5 B   90  ILE ALA ARG LEU MET GLU ASP LEU ASP ARG ASN LYS ASP          
SEQRES   6 B   90  GLN GLU VAL ASN PHE GLN GLU TYR VAL THR PHE LEU GLY          
SEQRES   7 B   90  ALA LEU ALA LEU ILE TYR ASN GLU ALA LEU LYS GLY              
SEQRES   1 D   90  MET ALA SER PRO LEU ASP GLN ALA ILE GLY LEU LEU VAL          
SEQRES   2 D   90  ALA ILE PHE HIS LYS TYR SER GLY ARG GLU GLY ASP LYS          
SEQRES   3 D   90  HIS THR LEU SER LYS LYS GLU LEU LYS GLU LEU ILE GLN          
SEQRES   4 D   90  LYS GLU LEU THR ILE GLY SER LYS LEU GLN ASP ALA GLU          
SEQRES   5 D   90  ILE ALA ARG LEU MET GLU ASP LEU ASP ARG ASN LYS ASP          
SEQRES   6 D   90  GLN GLU VAL ASN PHE GLN GLU TYR VAL THR PHE LEU GLY          
SEQRES   7 D   90  ALA LEU ALA LEU ILE TYR ASN GLU ALA LEU LYS GLY              
SEQRES   1 A  101  ALA MET ALA GLN ASN ILE THR ALA ARG ILE GLY GLU PRO          
SEQRES   2 A  101  LEU VAL LEU LYS CYS LYS GLY ALA PRO LYS LYS PRO PRO          
SEQRES   3 A  101  GLN ARG LEU GLU TRP LYS LEU ASN THR GLY ARG THR GLU          
SEQRES   4 A  101  ALA TRP LYS VAL LEU SER PRO GLN GLY GLY GLY PRO TRP          
SEQRES   5 A  101  ASP SER VAL ALA ARG VAL LEU PRO ASN GLY SER LEU PHE          
SEQRES   6 A  101  LEU PRO ALA VAL GLY ILE GLN ASP GLU GLY ILE PHE ARG          
SEQRES   7 A  101  CYS GLN ALA MET ASN ARG ASN GLY LYS GLU THR LYS SER          
SEQRES   8 A  101  ASN TYR ARG VAL ARG VAL TYR GLN ILE PRO                      
SEQRES   1 C  101  ALA MET ALA GLN ASN ILE THR ALA ARG ILE GLY GLU PRO          
SEQRES   2 C  101  LEU VAL LEU LYS CYS LYS GLY ALA PRO LYS LYS PRO PRO          
SEQRES   3 C  101  GLN ARG LEU GLU TRP LYS LEU ASN THR GLY ARG THR GLU          
SEQRES   4 C  101  ALA TRP LYS VAL LEU SER PRO GLN GLY GLY GLY PRO TRP          
SEQRES   5 C  101  ASP SER VAL ALA ARG VAL LEU PRO ASN GLY SER LEU PHE          
SEQRES   6 C  101  LEU PRO ALA VAL GLY ILE GLN ASP GLU GLY ILE PHE ARG          
SEQRES   7 C  101  CYS GLN ALA MET ASN ARG ASN GLY LYS GLU THR LYS SER          
SEQRES   8 C  101  ASN TYR ARG VAL ARG VAL TYR GLN ILE PRO                      
HELIX    1   1 SER B    3  GLY B   21  1                                  19    
HELIX    2   2 SER B   30  LEU B   42  1                                  13    
HELIX    3   3 ILE B   44  LEU B   48  5                                   5    
HELIX    4   4 GLN B   49  ASP B   61  1                                  13    
HELIX    5   5 ASN B   69  GLY B   90  1                                  22    
HELIX    6   6 SER D    3  GLY D   21  1                                  19    
HELIX    7   7 SER D   30  LEU D   42  1                                  13    
HELIX    8   8 ILE D   44  LEU D   48  5                                   5    
HELIX    9   9 GLN D   49  ASP D   61  1                                  13    
HELIX   10  10 ASN D   69  GLY D   90  1                                  22    
HELIX   11  11 PRO A   71  ALA A   76  1                                   6    
HELIX   12  12 PRO C   71  ALA C   76  1                                   6    
SHEET    1   A 4 GLN A  24  ALA A  28  0                                        
SHEET    2   A 4 ASN A 112  VAL A 117  1  O  ARG A 114   N  ILE A  26           
SHEET    3   A 4 GLY A  95  MET A 102 -1  N  GLY A  95   O  VAL A 115           
SHEET    4   A 4 ARG A  48  ASN A  54 -1  N  GLU A  50   O  GLN A 100           
SHEET    1   B 2 GLU A  32  LYS A  37  0                                        
SHEET    2   B 2 SER A  83  VAL A  89 -1  O  LEU A  84   N  LEU A  36           
SHEET    1   C 4 GLN C  24  ALA C  28  0                                        
SHEET    2   C 4 ASN C 112  VAL C 117  1  O  ARG C 114   N  ILE C  26           
SHEET    3   C 4 GLY C  95  MET C 102 -1  N  GLY C  95   O  VAL C 115           
SHEET    4   C 4 ARG C  48  ASN C  54 -1  N  GLU C  50   O  GLN C 100           
SHEET    1   D 2 GLU C  32  LYS C  37  0                                        
SHEET    2   D 2 SER C  83  VAL C  89 -1  O  LEU C  84   N  LEU C  36           
SSBOND   1 CYS A   38    CYS A   99                          1555   1555  2.03  
SSBOND   2 CYS C   38    CYS C   99                          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                                                                             
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