CONTORTROSTATIN-REPROLYSIN DOMAIN STRUCTURE
ma-c12zs

CONTORTROSTATIN-REPROLYSIN DOMAIN STRUCTURE This is a legacy model originally deposited in the PDB Archive(PDBid 2GP2). The Modelarchive now holds this entry, because since Oct 15, 2006 the wwPDB does not accept theoretical models. For more information please see the RCSB Statement concerning theoretical models.

Release Date
04/16/2006
Authors
SWAMINATHAN, R. RAMYA, T. KARTHIK, C.S.
Citations
R.SWAMINATHAN,T.RAMYA,C.S.KARTHIK
CONTORTROSTATIN-REPROLYSIN DOMAIN STRUCTURE
HEADER    HYDROLASE                               16-APR-06   2GP2              
TITLE     CONTORTROSTATIN-REPROLYSIN DOMAIN STRUCTURE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ZINC METALLOPROTEINASE CONTORTROSTATIN;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 198-483;                                          
COMPND   5 EC: 3.4.24.-                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AGKISTRODON CONTORTRIX CONTORTRIX;              
SOURCE   3 ORGANISM_COMMON: SNAKE                                               
KEYWDS    BLOOD COAGULATION, CELL ADHESION, DIRECT PROTEIN SEQUENCING,          
KEYWDS   2 HYDROLASE, METAL-BINDING, METALLOPROTEASE, PROTEASE, SIGNAL,         
KEYWDS   3 ZINC, ZYMOGEN                                                        
EXPDTA    THEORETICAL MODEL                                                     
AUTHOR    R.SWAMINATHAN,T.RAMYA,C.S.KARTHIK                                     
REVDAT   1   21-NOV-06 2GP2    0                                                
JRNL        AUTH   R.SWAMINATHAN,T.RAMYA,C.S.KARTHIK                            
JRNL        TITL   CONTORTROSTATIN-REPROLYSIN DOMAIN STRUCTURE                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.PYRKO,W.WANG,F.S.MARKLAND,S.D.SWENSON,                     
REMARK   1  AUTH 2 S.SCHMITMEIER,A.H.SCHONTHAL,T.C.CHEN                         
REMARK   1  TITL   THE ROLE OF CONTORTROSTATIN, A SNAKE VENOM                   
REMARK   1  TITL 2 DISINTEGRIN, IN THE INHIBITION OF TUMOR                      
REMARK   1  TITL 3 PROGRESSION AND PROLONGATION OF SURVIVAL IN A                
REMARK   1  TITL 4 RODENT GLIOMA MODEL                                          
REMARK   1  REF    J. NEUROSURG.                 V.  50   526 2005              
REMARK   1  REFN                US ISSN 0022-3085                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NULL                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE QUALITY OF THE PROTEIN WAS            
REMARK   3  VALIDATED USING THE SAVS SERVER.THE OVERALL QUALITY WAS 95%         
REMARK   3  AND HENCE THERE WAS NO REFINEMENT DONE.                             
REMARK   4                                                                      
REMARK   4 2GP2 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-2006.                
REMARK 100 THE RCSB ID CODE IS RCSB037384.                                      
REMARK 220                                                                      
REMARK 220 EXPERIMENTAL DETAILS                                                 
REMARK 220  EXPERIMENT TYPE                : THEORETICAL MODELLING              
REMARK 220                                                                      
REMARK 220 REMARK: NULL                                                         
REMARK 225                                                                      
REMARK 225 THEORETICAL MODEL                                                    
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.           
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND                
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE                   
REMARK 225 RECORDS ARE MEANINGLESS.                                             
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     LEU A   198                                                      
REMARK 465     ARG A   199                                                      
REMARK 465     THR A   200                                                      
REMARK 465     ASP A   201                                                      
REMARK 465     ILE A   202                                                      
REMARK 465     VAL A   203                                                      
REMARK 465     SER A   204                                                      
REMARK 465     THR A   205                                                      
REMARK 465     PRO A   206                                                      
REMARK 465     VAL A   207                                                      
REMARK 465     SER A   208                                                      
REMARK 465     GLY A   209                                                      
REMARK 465     ASN A   210                                                      
REMARK 465     GLU A   211                                                      
REMARK 465     LEU A   212                                                      
REMARK 465     LEU A   213                                                      
REMARK 465     GLU A   214                                                      
REMARK 465     THR A   215                                                      
REMARK 465     GLY A   216                                                      
REMARK 465     GLU A   217                                                      
REMARK 465     GLU A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     ASP A   220                                                      
REMARK 465     PHE A   221                                                      
REMARK 465     ASP A   222                                                      
REMARK 465     ALA A   223                                                      
REMARK 465     PRO A   224                                                      
REMARK 465     ALA A   225                                                      
REMARK 465     ASN A   226                                                      
REMARK 465     PRO A   227                                                      
REMARK 465     CYS A   228                                                      
REMARK 465     CYS A   229                                                      
REMARK 465     ASP A   230                                                      
REMARK 465     ALA A   231                                                      
REMARK 465     ALA A   232                                                      
REMARK 465     THR A   233                                                      
REMARK 465     CYS A   234                                                      
REMARK 465     LYS A   235                                                      
REMARK 465     LEU A   236                                                      
REMARK 465     THR A   237                                                      
REMARK 465     THR A   238                                                      
REMARK 465     GLY A   239                                                      
REMARK 465     SER A   240                                                      
REMARK 465     GLN A   241                                                      
REMARK 465     CYS A   242                                                      
REMARK 465     ALA A   243                                                      
REMARK 465     ASP A   244                                                      
REMARK 465     GLY A   245                                                      
REMARK 465     LEU A   246                                                      
REMARK 465     CYS A   247                                                      
REMARK 465     CYS A   248                                                      
REMARK 465     ASP A   249                                                      
REMARK 465     GLN A   250                                                      
REMARK 465     CYS A   251                                                      
REMARK 465     LYS A   252                                                      
REMARK 465     PHE A   253                                                      
REMARK 465     MET A   254                                                      
REMARK 465     LYS A   255                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     THR A   258                                                      
REMARK 465     VAL A   259                                                      
REMARK 465     CYS A   260                                                      
REMARK 465     ARG A   261                                                      
REMARK 465     ARG A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     ARG A   264                                                      
REMARK 465     GLY A   265                                                      
REMARK 465     ASP A   266                                                      
REMARK 465     ASP A   267                                                      
REMARK 465     LEU A   268                                                      
REMARK 465     ASP A   269                                                      
REMARK 465     ASP A   270                                                      
REMARK 465     TYR A   271                                                      
REMARK 465     CYS A   272                                                      
REMARK 465     ASN A   273                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     ILE A   275                                                      
REMARK 465     SER A   276                                                      
REMARK 465     ALA A   277                                                      
REMARK 465     GLY A   278                                                      
REMARK 465     CYS A   279                                                      
REMARK 465     PRO A   280                                                      
REMARK 465     ARG A   281                                                      
REMARK 465     ASN A   282                                                      
REMARK 465     PRO A   283                                                      
REMARK 465     PHE A   284                                                      
REMARK 465     HIS A   285                                                      
REMARK 465     ALA A   286                                                      
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  31   CB  -  CG  -  CD1 ANGL. DEV. =-12.7 DEGREES           
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 GLU A  196    PRO A  197                   98.11                     
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ND1   RELATED DB: PDB                                   
REMARK 900 AMINO ACID SEQUENCE AND CRYSTAL STRUCTURE OF BAP1, A                 
REMARK 900 METALLOPROTEINASE FROM BOTHROPS ASPER SNAKE VENOM THAT               
REMARK 900 EXERTS MULTIPLE TISSUE-DAMAGING ACTIVITIES                           
REMARK 900 RELATED ID: 1FVL   RELATED DB: PDB                                   
REMARK 900 THE NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF                 
REMARK 900 FLAVORIDIN, AN ANTAGONIST OF THE PLATELET GP IIB-IIIA                
REMARK 900 RECEPTOR                                                             
DBREF  2GP2 A    1   286  UNP    Q9IAB0   DISI_AGKCO     198    483             
SEQRES   1 A  286  ARG TYR ILE GLU LEU VAL VAL VAL ALA ASP HIS ARG MET          
SEQRES   2 A  286  PHE THR LYS TYR ASN GLY ASN LEU ASN THR ILE ARG ILE          
SEQRES   3 A  286  TRP VAL HIS GLU LEU VAL ASN THR MET ASN VAL PHE TYR          
SEQRES   4 A  286  ARG PRO LEU ASN ILE ARG VAL SER LEU THR ASP LEU GLU          
SEQRES   5 A  286  VAL TRP SER ASP GLN ASP LEU ILE ASN VAL GLN PRO ALA          
SEQRES   6 A  286  ALA ALA ASP THR LEU GLU ALA PHE GLY ASP TRP ARG GLU          
SEQRES   7 A  286  THR VAL LEU LEU ASN ARG ILE SER HIS ASP ASN ALA GLN          
SEQRES   8 A  286  LEU LEU THR ALA ILE GLU LEU ASP GLY GLU THR ILE GLY          
SEQRES   9 A  286  LEU ALA ASN ARG GLY THR MET CYS ASP PRO LYS LEU SER          
SEQRES  10 A  286  THR GLY ILE VAL GLN ASP HIS SER ALA ILE ASN LEU TRP          
SEQRES  11 A  286  VAL ALA VAL THR MET ALA HIS GLU MET GLY HIS ASN LEU          
SEQRES  12 A  286  GLY ILE SER HIS ASP GLY ASN GLN CYS HIS CYS ASP ALA          
SEQRES  13 A  286  ASN SER CYS ILE MET SER GLU GLU LEU ARG GLU GLN LEU          
SEQRES  14 A  286  SER PHE GLU PHE SER ASP CYS SER GLN ASN GLN TYR GLN          
SEQRES  15 A  286  THR TYR LEU THR ASP HIS ASN PRO GLN CYS MET LEU ASN          
SEQRES  16 A  286  GLU PRO LEU ARG THR ASP ILE VAL SER THR PRO VAL SER          
SEQRES  17 A  286  GLY ASN GLU LEU LEU GLU THR GLY GLU GLU SER ASP PHE          
SEQRES  18 A  286  ASP ALA PRO ALA ASN PRO CYS CYS ASP ALA ALA THR CYS          
SEQRES  19 A  286  LYS LEU THR THR GLY SER GLN CYS ALA ASP GLY LEU CYS          
SEQRES  20 A  286  CYS ASP GLN CYS LYS PHE MET LYS GLU GLY THR VAL CYS          
SEQRES  21 A  286  ARG ARG ALA ARG GLY ASP ASP LEU ASP ASP TYR CYS ASN          
SEQRES  22 A  286  GLY ILE SER ALA GLY CYS PRO ARG ASN PRO PHE HIS ALA          
HELIX    1   1 ASP A   10  TYR A   17  1                                   8    
HELIX    2   2 ASN A   20  ARG A   40  1                                  21    
HELIX    3   3 PRO A   41  ASN A   43  5                                   3    
HELIX    4   4 ALA A   65  VAL A   80  1                                  16    
HELIX    5   5 VAL A   80  ILE A   85  1                                   6    
HELIX    6   6 ILE A  127  LEU A  143  1                                  17    
HELIX    7   7 SER A  174  ASN A  189  1                                  16    
HELIX    8   8 PRO A  190  LEU A  194  5                                   5    
SHEET    1   A 5 LEU A  48  VAL A  53  0                                        
SHEET    2   A 5 LEU A   5  ALA A   9  1  N  LEU A   5   O  THR A  49           
SHEET    3   A 5 ASN A  89  THR A  94  1  O  LEU A  93   N  VAL A   8           
SHEET    4   A 5 THR A 118  GLN A 122  1  O  VAL A 121   N  LEU A  92           
SHEET    5   A 5 GLY A 104  ALA A 106 -1  N  LEU A 105   O  ILE A 120           
SHEET    1   B 2 SER A 158  CYS A 159  0                                        
SHEET    2   B 2 PHE A 171  GLU A 172  1  O  GLU A 172   N  SER A 158           
SSBOND   1 CYS A  112    CYS A  192                                             
SSBOND   2 CYS A  152    CYS A  176                                             
SSBOND   3 CYS A  154    CYS A  159