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Database: PDB
Entry: 1WHE
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Original site: 1WHE 
HEADER    GLYCOPROTEIN                            18-JUN-96   1WHE              
TITLE     COAGULATION FACTOR, NMR, 20 STRUCTURES                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR X;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.6;                                                        
COMPND   5 OTHER_DETAILS: THE APO FORM OF THE FRAGMENT CONTAINING THE GLA AND N-
COMPND   6 TERMINAL EGF-LIKE MODULE                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913                                                 
KEYWDS    GLYCOPROTEIN, HYDROLASE, SERINE PROTEASE, PLASMA, BLOOD COAGULATION   
KEYWDS   2 FACTOR                                                               
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    M.SUNNERHAGEN,G.A.OLAH,J.STENFLO,S.FORSEN,T.DRAKENBERG,J.TREWHELLA    
REVDAT   4   29-NOV-17 1WHE    1       HELIX                                    
REVDAT   3   20-JUN-12 1WHE    1       HETNAM VERSN                             
REVDAT   2   24-FEB-09 1WHE    1       VERSN                                    
REVDAT   1   15-MAY-97 1WHE    0                                                
JRNL        AUTH   M.SUNNERHAGEN,G.A.OLAH,J.STENFLO,S.FORSEN,T.DRAKENBERG,      
JRNL        AUTH 2 J.TREWHELLA                                                  
JRNL        TITL   THE RELATIVE ORIENTATION OF GLA AND EGF DOMAINS IN           
JRNL        TITL 2 COAGULATION FACTOR X IS ALTERED BY CA2+ BINDING TO THE FIRST 
JRNL        TITL 3 EGF DOMAIN. A COMBINED NMR-SMALL ANGLE X-RAY SCATTERING      
JRNL        TITL 4 STUDY.                                                       
JRNL        REF    BIOCHEMISTRY                  V.  35 11547 1996              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8794734                                                      
JRNL        DOI    10.1021/BI960633J                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.SUNNERHAGEN,S.FORSEN,A.M.HOFFREN,T.DRAKENBERG,O.TELEMAN,   
REMARK   1  AUTH 2 J.STENFLO                                                    
REMARK   1  TITL   STRUCTURE OF THE CA(2+)-FREE GLA DOMAIN SHEDS LIGHT ON       
REMARK   1  TITL 2 MEMBRANE BINDING OF BLOOD COAGULATION PROTEINS               
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   2   504 1995              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.SELANDER-SUNNERHAGEN,M.ULLNER,E.PERSSON,O.TELEMAN,         
REMARK   1  AUTH 2 J.STENFLO,T.DRAKENBERG                                       
REMARK   1  TITL   HOW AN EPIDERMAL GROWTH FACTOR (EGF)-LIKE DOMAIN BINDS       
REMARK   1  TITL 2 CALCIUM. HIGH RESOLUTION NMR STRUCTURE OF THE CALCIUM FORM   
REMARK   1  TITL 3 OF THE NH2-TERMINAL EGF-LIKE DOMAIN IN COAGULATION FACTOR X  
REMARK   1  REF    J.BIOL.CHEM.                  V. 267 19642 1992              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.ULLNER,M.SELANDER,E.PERSSON,J.STENFLO,T.DRAKENBERG,        
REMARK   1  AUTH 2 O.TELEMAN                                                    
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE           
REMARK   1  TITL 2 N-TERMINAL EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X AS  
REMARK   1  TITL 3 DETERMINED BY NMR SPECTROSCOPY AND SIMULATED FOLDING         
REMARK   1  REF    BIOCHEMISTRY                  V.  31  5974 1992              
REMARK   1  REFN                   ISSN 0006-2960                               
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: NULL                                      
REMARK   4                                                                      
REMARK   4 1WHE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000177194.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : NULL                               
REMARK 210  PH                             : NULL                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL                               
REMARK 210  SPECTROMETER MODEL             : NULL                               
REMARK 210  SPECTROMETER MANUFACTURER      : NULL                               
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : NULL                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
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 TYR A  68   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 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 ASN A   2     -168.06     51.13                                   
REMARK 500  1 SER A   3      -39.20   -152.29                                   
REMARK 500  1 PHE A   4      -83.58    -75.15                                   
REMARK 500  1 LEU A   5      179.24    -58.05                                   
REMARK 500  1 CGU A   6      -74.07     79.12                                   
REMARK 500  1 GLN A  10      177.22    170.74                                   
REMARK 500  1 ASN A  12     -133.32   -169.66                                   
REMARK 500  1 LEU A  13      -33.02   -151.19                                   
REMARK 500  1 CGU A  14      -66.83   -155.54                                   
REMARK 500  1 LEU A  18       45.23   -102.97                                   
REMARK 500  1 CGU A  19     -158.32   -145.83                                   
REMARK 500  1 LEU A  24       36.02   -177.41                                   
REMARK 500  1 CGU A  25      -91.81    -80.07                                   
REMARK 500  1 VAL A  30       50.18    -90.17                                   
REMARK 500  1 PHE A  31      -57.53   -127.35                                   
REMARK 500  1 CGU A  32      -42.36     82.41                                   
REMARK 500  1 ASP A  38     -101.89    -56.34                                   
REMARK 500  1 CGU A  39      -55.42    -27.36                                   
REMARK 500  1 PHE A  40      -77.36    -39.43                                   
REMARK 500  1 TRP A  41      -95.57    -82.09                                   
REMARK 500  1 SER A  42       52.83     33.20                                   
REMARK 500  1 LYS A  43       54.21     78.86                                   
REMARK 500  1 TYR A  44       82.32    -38.86                                   
REMARK 500  1 ASP A  46     -150.63     31.08                                   
REMARK 500  1 ASP A  48       18.41     56.10                                   
REMARK 500  1 GLN A  49      101.00     23.48                                   
REMARK 500  1 CYS A  50       13.62     99.22                                   
REMARK 500  1 HIS A  53      102.78     50.77                                   
REMARK 500  1 BHD A  63      145.51     57.67                                   
REMARK 500  1 ILE A  65      113.89    -35.90                                   
REMARK 500  1 CYS A  81       27.91     46.86                                   
REMARK 500  2 ASN A   2     -179.90    167.24                                   
REMARK 500  2 SER A   3       27.84     44.53                                   
REMARK 500  2 PHE A   4       82.10    -66.98                                   
REMARK 500  2 CGU A   6      -64.30     82.37                                   
REMARK 500  2 GLN A  10      103.59     62.08                                   
REMARK 500  2 ASN A  12     -146.68   -178.86                                   
REMARK 500  2 LEU A  13     -106.92   -169.56                                   
REMARK 500  2 CGU A  14      -62.46   -105.76                                   
REMARK 500  2 LEU A  18       36.96    -90.21                                   
REMARK 500  2 CYS A  22      163.80    -43.12                                   
REMARK 500  2 LEU A  24      -65.74     82.63                                   
REMARK 500  2 VAL A  30       54.35   -103.09                                   
REMARK 500  2 PHE A  31      -49.85   -132.55                                   
REMARK 500  2 CGU A  32      -47.65     85.05                                   
REMARK 500  2 THR A  37      -29.08    -38.67                                   
REMARK 500  2 ASP A  38      -86.83    -75.20                                   
REMARK 500  2 PHE A  40      -80.68    -37.94                                   
REMARK 500  2 TRP A  41      -88.97    -81.83                                   
REMARK 500  2 SER A  42      -92.01     47.24                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     532 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1WHE A    1    86  UNP    P00743   FA10_BOVIN      41    126             
SEQADV 1WHE CGU A    6  UNP  P00743    GLU    46 MODIFIED RESIDUE               
SEQADV 1WHE CGU A    7  UNP  P00743    GLU    47 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   14  UNP  P00743    GLU    54 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   16  UNP  P00743    GLU    56 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   19  UNP  P00743    GLU    59 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   20  UNP  P00743    GLU    60 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   25  UNP  P00743    GLU    65 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   26  UNP  P00743    GLU    66 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   29  UNP  P00743    GLU    69 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   32  UNP  P00743    GLU    72 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   35  UNP  P00743    GLU    75 MODIFIED RESIDUE               
SEQADV 1WHE CGU A   39  UNP  P00743    GLU    79 MODIFIED RESIDUE               
SEQADV 1WHE BHD A   63  UNP  P00743    ASP   103 MODIFIED RESIDUE               
SEQRES   1 A   86  ALA ASN SER PHE LEU CGU CGU VAL LYS GLN GLY ASN LEU          
SEQRES   2 A   86  CGU ARG CGU CYS LEU CGU CGU ALA CYS SER LEU CGU CGU          
SEQRES   3 A   86  ALA ARG CGU VAL PHE CGU ASP ALA CGU GLN THR ASP CGU          
SEQRES   4 A   86  PHE TRP SER LYS TYR LYS ASP GLY ASP GLN CYS GLU GLY          
SEQRES   5 A   86  HIS PRO CYS LEU ASN GLN GLY HIS CYS LYS BHD GLY ILE          
SEQRES   6 A   86  GLY ASP TYR THR CYS THR CYS ALA GLU GLY PHE GLU GLY          
SEQRES   7 A   86  LYS ASN CYS GLU PHE SER THR ARG                              
MODRES 1WHE CGU A    6  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A    7  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   14  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   16  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   19  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   20  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   25  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   26  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   29  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   32  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   35  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE CGU A   39  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 1WHE BHD A   63  ASP  (3S)-3-HYDROXY-L-ASPARTIC ACID                     
HET    CGU  A   6      17                                                       
HET    CGU  A   7      17                                                       
HET    CGU  A  14      17                                                       
HET    CGU  A  16      17                                                       
HET    CGU  A  19      17                                                       
HET    CGU  A  20      17                                                       
HET    CGU  A  25      17                                                       
HET    CGU  A  26      17                                                       
HET    CGU  A  29      17                                                       
HET    CGU  A  32      17                                                       
HET    CGU  A  35      17                                                       
HET    CGU  A  39      17                                                       
HET    BHD  A  63      13                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM     BHD (3S)-3-HYDROXY-L-ASPARTIC ACID                                   
HETSYN     BHD BETA-HYDROXYASPARTIC ACID                                        
FORMUL   1  CGU    12(C6 H9 N O6)                                               
FORMUL   1  BHD    C4 H7 N O5                                                   
HELIX    1  A1 LEU A   13  LEU A   18  1                                   6    
HELIX    2  A2 CGU A   20  VAL A   30  1                                  11    
HELIX    3  A3 ALA A   34  TRP A   41  1                                   8    
SHEET    1  S1 2 GLY A  59  BHD A  63  0                                        
SHEET    2  S1 2 TYR A  68  CYS A  72 -1                                        
SHEET    1  S2 2 PHE A  76  GLU A  77  0                                        
SHEET    2  S2 2 PHE A  83  SER A  84 -1                                        
SSBOND   1 CYS A   17    CYS A   22                          1555   1555  2.02  
SSBOND   2 CYS A   50    CYS A   61                          1555   1555  2.02  
SSBOND   3 CYS A   55    CYS A   70                          1555   1555  2.02  
SSBOND   4 CYS A   72    CYS A   81                          1555   1555  2.02  
LINK         N   CGU A   6                 C   LEU A   5     1555   1555  1.31  
LINK         C   CGU A   6                 N   CGU A   7     1555   1555  1.31  
LINK         C   CGU A   7                 N   VAL A   8     1555   1555  1.29  
LINK         N   CGU A  14                 C   LEU A  13     1555   1555  1.31  
LINK         C   CGU A  14                 N   ARG A  15     1555   1555  1.30  
LINK         N   CGU A  16                 C   ARG A  15     1555   1555  1.30  
LINK         C   CGU A  16                 N   CYS A  17     1555   1555  1.30  
LINK         N   CGU A  19                 C   LEU A  18     1555   1555  1.31  
LINK         C   CGU A  19                 N   CGU A  20     1555   1555  1.31  
LINK         C   CGU A  20                 N   ALA A  21     1555   1555  1.30  
LINK         N   CGU A  25                 C   LEU A  24     1555   1555  1.31  
LINK         C   CGU A  25                 N   CGU A  26     1555   1555  1.31  
LINK         C   CGU A  26                 N   ALA A  27     1555   1555  1.30  
LINK         N   CGU A  29                 C   ARG A  28     1555   1555  1.30  
LINK         C   CGU A  29                 N   VAL A  30     1555   1555  1.31  
LINK         N   CGU A  32                 C   PHE A  31     1555   1555  1.31  
LINK         C   CGU A  32                 N   ASP A  33     1555   1555  1.31  
LINK         N   CGU A  35                 C   ALA A  34     1555   1555  1.31  
LINK         C   CGU A  35                 N   GLN A  36     1555   1555  1.31  
LINK         N   CGU A  39                 C   ASP A  38     1555   1555  1.31  
LINK         C   CGU A  39                 N   PHE A  40     1555   1555  1.30  
LINK         N   BHD A  63                 C   LYS A  62     1555   1555  1.31  
LINK         C   BHD A  63                 N   GLY A  64     1555   1555  1.30  
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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